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Database: PDB
Entry: 1EFX
LinkDB: 1EFX
Original site: 1EFX 
HEADER    IMMUNE SYSTEM                           10-FEB-00   1EFX              
TITLE     STRUCTURE OF A COMPLEX BETWEEN THE HUMAN NATURAL KILLER               
TITLE    2 CELL RECEPTOR KIR2DL2 AND A CLASS I MHC LIGAND HLA-CW3               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA-CW3 (HEAVY CHAIN);                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EXTRACELLULAR ALPHA-1, ALPHA-2 AND ALPHA-3                 
COMPND   5 DOMAINS;                                                             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: BETA-2-MICROGLOBULIN;                                      
COMPND   9 CHAIN: B;                                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 OTHER_DETAILS: MATURE FORM;                                          
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: PEPTIDE FROM IMPORTIN ALPHA-2;                             
COMPND  14 CHAIN: C;                                                            
COMPND  15 FRAGMENT: RESIDUES 204-212;                                          
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: NATURAL KILLER CELL RECEPTOR KIR2DL2;                      
COMPND  19 CHAIN: D, E;                                                         
COMPND  20 FRAGMENT: EXTRACELLULAR D1 AND D2 DOMAINS;                           
COMPND  21 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_PLASMID: MODIFIED PET30A;                          
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET30A;                          
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED.              
SOURCE  18 THE SEQUENCE IS NATURALLY FOUND IN HOMO SAPIENS (HUMAN).;            
SOURCE  19 MOL_ID: 4;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  25 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET30A                           
KEYWDS    MHC, HLA, CLASS I, KIR, NK CELL RECEPTOR, IMMUNOGLOBULIN              
KEYWDS   2 FOLD, RECEPTOR/MHC COMPLEX, IMMUNE SYSTEM                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.C.BOYINGTON,S.A.MOTYKA,P.SCHUCK,A.G.BROOKS,P.D.SUN                  
REVDAT   3   24-FEB-09 1EFX    1       VERSN                                    
REVDAT   2   30-SEP-03 1EFX    1       JRNL   DBREF                             
REVDAT   1   14-JUN-00 1EFX    0                                                
JRNL        AUTH   J.C.BOYINGTON,S.A.MOTYKA,P.SCHUCK,A.G.BROOKS,                
JRNL        AUTH 2 P.D.SUN                                                      
JRNL        TITL   CRYSTAL STRUCTURE OF AN NK CELL                              
JRNL        TITL 2 IMMUNOGLOBULIN-LIKE RECEPTOR IN COMPLEX WITH ITS             
JRNL        TITL 3 CLASS I MHC LIGAND.                                          
JRNL        REF    NATURE                        V. 405   537 2000              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   10850706                                                     
JRNL        DOI    10.1038/35014520                                             
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.A.SNYDER,A.G.BROOKS,P.D.SUN                                
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE HLA-CW3 ALLOTYPE-SPECIFIC           
REMARK   1  TITL 2 KILLER CELL INHIBITORY RECEPTOR KIR2DL2                      
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  96  3864 1999              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1  DOI    10.1073/PNAS.96.7.3864                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2163178.140                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 22800                          
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) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.294                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1085                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
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) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2788                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3940                       
REMARK   3   BIN FREE R VALUE                    : 0.4560                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.60                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 134                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.039                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6226                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 185                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 63.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 12.60000                                             
REMARK   3    B22 (A**2) : 15.30000                                             
REMARK   3    B33 (A**2) : -27.90000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.41                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.70                            
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) : 0.52                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.83                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.95                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : GROUP                                     
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        : 0.28                                                 
REMARK   3   BSOL        : 42.05                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 1EFX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-FEB-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB010535.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JUL-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 93.0                               
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                       : X9B                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0358                             
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 : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24517                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -0.500                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.1                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6000                            
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     (%) : 75.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: KIR2DL2 (PDB ENTRY 2DL2) AND HLA-A2 (PDB ENTRY       
REMARK 200  1B0G)                                                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, CALCIUM CHLORIDE, SODIUM      
REMARK 280  CACODYLATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  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       34.27000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      103.63500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.16500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      103.63500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.27000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.16500            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS THE 1:1 COMPLEX BETWEEN           
REMARK 300 KIR2DL2 AND HLA-CW3 OBSERVED IN THE ASYMMETRIC UNIT THE              
REMARK 300 BIOLOGICAL ASSEMBLY IS THE 1:1 COMPLEX BETWEEN KIR2DL2 AND HLA-      
REMARK 300 CW3 OBSERVED IN THE ASYMMETRIC UNIT                                  
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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
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     HIS D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     HIS E     1                                                      
REMARK 465     GLU E     2                                                      
REMARK 465     GLY E     3                                                      
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     VAL D   4    CG1  CG2                                            
REMARK 470     VAL E   4    CG1  CG2                                            
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    CYS D 128   CA  -  CB  -  SG  ANGL. DEV. =   6.8 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    PRO A  15      -44.11    -20.41                                   
REMARK 500    ARG A  17       11.44    -53.42                                   
REMARK 500    ASP A  29     -149.23     70.19                                   
REMARK 500    ALA A  40      148.58    -38.35                                   
REMARK 500    PRO A  50      -74.76    -47.04                                   
REMARK 500    TRP A  51      -54.28    -29.89                                   
REMARK 500    GLU A  55      172.47    -57.23                                   
REMARK 500    LEU A  78      -72.28    -58.34                                   
REMARK 500    ARG A  79      -28.39    -39.88                                   
REMARK 500    ASN A  86       86.42     42.23                                   
REMARK 500    SER A  88      154.23    -47.97                                   
REMARK 500    SER A  92      159.94    -40.81                                   
REMARK 500    ARG A 108      137.59     62.56                                   
REMARK 500    LEU A 110      -63.62   -100.24                                   
REMARK 500    ASP A 114      114.88    171.56                                   
REMARK 500    ASP A 122      117.79    -35.60                                   
REMARK 500    TYR A 123      -89.36    -99.03                                   
REMARK 500    ARG A 131       -3.07   -142.82                                   
REMARK 500    GLU A 177        4.97    -68.03                                   
REMARK 500    THR A 178      -72.58   -126.43                                   
REMARK 500    ARG A 181     -137.80    -99.97                                   
REMARK 500    ALA A 182      -59.05   -155.45                                   
REMARK 500    GLU A 183       85.21     59.68                                   
REMARK 500    HIS A 188      167.89    177.08                                   
REMARK 500    VAL A 194      -72.98    -80.51                                   
REMARK 500    ASP A 196      101.53     -3.98                                   
REMARK 500    HIS A 197       -7.04     93.55                                   
REMARK 500    TYR A 209      139.52   -172.17                                   
REMARK 500    THR A 225      -39.12    -24.19                                   
REMARK 500    ASP A 238       31.04   -142.99                                   
REMARK 500    LYS A 243      154.83    166.35                                   
REMARK 500    SER A 251      157.17    -39.73                                   
REMARK 500    GLU A 253       16.66    -67.61                                   
REMARK 500    GLN A 255       -2.16    -49.21                                   
REMARK 500    PRO A 276       43.04    -46.97                                   
REMARK 500    SER A 277     -106.17     64.46                                   
REMARK 500    GLU B  16      115.46   -175.13                                   
REMARK 500    ASN B  17      150.70    -33.69                                   
REMARK 500    ASN B  21     -179.49   -170.09                                   
REMARK 500    HIS B  31      132.51   -177.84                                   
REMARK 500    PRO B  32     -173.68    -60.71                                   
REMARK 500    ASP B  34      118.87    -33.37                                   
REMARK 500    ARG B  45      141.69    -35.74                                   
REMARK 500    SER B  52      171.07    -59.91                                   
REMARK 500    TRP B  60       -3.29     70.79                                   
REMARK 500    TYR B  63      136.82   -179.51                                   
REMARK 500    THR B  68      132.90    169.00                                   
REMARK 500    PHE B  70      143.44   -179.65                                   
REMARK 500    ARG B  97       -6.59    -52.89                                   
REMARK 500    LEU C   6     -120.69   -108.61                                   
REMARK 500    GLU D  21      -52.33     75.65                                   
REMARK 500    LEU D  51      134.57   -174.14                                   
REMARK 500    HIS D  56      142.21    175.85                                   
REMARK 500    ASP D  57       40.42     72.25                                   
REMARK 500    ALA D  62      121.47   -173.90                                   
REMARK 500    PRO D  68      103.57    -41.68                                   
REMARK 500    GLN D  71      -72.55      1.46                                   
REMARK 500    HIS D  85     -144.61    -98.73                                   
REMARK 500    SER D  86      -76.35     16.93                                   
REMARK 500    TYR D  88      116.10     78.78                                   
REMARK 500    GLN D  89       66.46   -104.37                                   
REMARK 500    ALA D 120      163.67    -48.10                                   
REMARK 500    SER D 130      149.14   -170.18                                   
REMARK 500    SER D 133       46.41    -91.23                                   
REMARK 500    GLU D 142     -110.39     14.34                                   
REMARK 500    ARG D 149      110.82   -162.67                                   
REMARK 500    PRO D 154      174.30    -32.25                                   
REMARK 500    LYS D 155      104.09    -34.29                                   
REMARK 500    GLN D 161     -169.38   -106.35                                   
REMARK 500    ALA D 162      113.42    177.14                                   
REMARK 500    SER D 189     -168.67    -79.32                                   
REMARK 500    GLU E  21      -51.42     73.62                                   
REMARK 500    PHE E  45       50.64    -99.54                                   
REMARK 500    LEU E  51      136.12   -176.97                                   
REMARK 500    HIS E  56      147.75    152.53                                   
REMARK 500    ALA E  62      119.48   -170.31                                   
REMARK 500    PRO E  68       94.46    -40.76                                   
REMARK 500    GLN E  71      -72.86     -2.77                                   
REMARK 500    HIS E  85     -154.66   -101.71                                   
REMARK 500    SER E  86      -76.05     21.27                                   
REMARK 500    TYR E  88      129.42     53.19                                   
REMARK 500    GLN E  89       70.45   -113.88                                   
REMARK 500    ALA E 120      157.09    -46.22                                   
REMARK 500    SER E 133       55.70   -103.31                                   
REMARK 500    HIS E 146     -171.55   -173.69                                   
REMARK 500    ARG E 149      113.49   -160.41                                   
REMARK 500    PRO E 154      173.02    -37.93                                   
REMARK 500    ASN E 157       38.05     77.47                                   
REMARK 500    ALA E 162      112.89    177.91                                   
REMARK 500    THR E 170      -38.80   -133.30                                   
REMARK 500    SER E 184       75.45   -119.00                                   
REMARK 500    SER E 189     -165.40    -72.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH E 217        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH D 232        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH D 239        DISTANCE =  6.97 ANGSTROMS                       
REMARK 525    HOH A 338        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH A 341        DISTANCE =  8.81 ANGSTROMS                       
REMARK 525    HOH A 353        DISTANCE =  5.92 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2DL2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF UNBOUND KIR2DL2                                 
DBREF  1EFX A    1   278  GB     495038   AAA88088        25    302             
DBREF  1EFX B    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  1EFX C    1     9  UNP    P52292   IMA2_HUMAN     204    212             
DBREF  1EFX D    1   200  UNP    P43627   KI2L2_HUMAN     22    221             
DBREF  1EFX E    1   200  UNP    P43627   KI2L2_HUMAN     22    221             
SEQADV 1EFX MET B    0  UNP  P61769              SEE REMARK 999                 
SEQRES   1 A  278  GLY SER HIS SER MET ARG TYR PHE TYR THR ALA VAL SER          
SEQRES   2 A  278  ARG PRO GLY ARG GLY GLU PRO HIS PHE ILE ALA VAL GLY          
SEQRES   3 A  278  TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP          
SEQRES   4 A  278  ALA ALA SER PRO ARG GLY GLU PRO ARG ALA PRO TRP VAL          
SEQRES   5 A  278  GLU GLN GLU GLY PRO GLU TYR TRP ASP ARG GLU THR GLN          
SEQRES   6 A  278  LYS TYR LYS ARG GLN ALA GLN THR ASP ARG VAL SER LEU          
SEQRES   7 A  278  ARG ASN LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY          
SEQRES   8 A  278  SER HIS ILE ILE GLN ARG MET TYR GLY CYS ASP VAL GLY          
SEQRES   9 A  278  PRO ASP GLY ARG LEU LEU ARG GLY TYR ASP GLN TYR ALA          
SEQRES  10 A  278  TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP LEU          
SEQRES  11 A  278  ARG SER TRP THR ALA ALA ASP THR ALA ALA GLN ILE THR          
SEQRES  12 A  278  GLN ARG LYS TRP GLU ALA ALA ARG GLU ALA GLU GLN LEU          
SEQRES  13 A  278  ARG ALA TYR LEU GLU GLY LEU CYS VAL GLU TRP LEU ARG          
SEQRES  14 A  278  ARG TYR LEU LYS ASN GLY LYS GLU THR LEU GLN ARG ALA          
SEQRES  15 A  278  GLU HIS PRO LYS THR HIS VAL THR HIS HIS PRO VAL SER          
SEQRES  16 A  278  ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY PHE          
SEQRES  17 A  278  TYR PRO ALA GLU ILE THR LEU THR TRP GLN TRP ASP GLY          
SEQRES  18 A  278  GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG          
SEQRES  19 A  278  PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL          
SEQRES  20 A  278  VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS          
SEQRES  21 A  278  VAL GLN HIS GLU GLY LEU PRO GLU PRO LEU THR LEU ARG          
SEQRES  22 A  278  TRP GLU PRO SER SER                                          
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  GLY ALA VAL ASP PRO LEU LEU ALA LEU                          
SEQRES   1 D  200  HIS GLU GLY VAL HIS ARG LYS PRO SER LEU LEU ALA HIS          
SEQRES   2 D  200  PRO GLY ARG LEU VAL LYS SER GLU GLU THR VAL ILE LEU          
SEQRES   3 D  200  GLN CYS TRP SER ASP VAL ARG PHE GLU HIS PHE LEU LEU          
SEQRES   4 D  200  HIS ARG GLU GLY LYS PHE LYS ASP THR LEU HIS LEU ILE          
SEQRES   5 D  200  GLY GLU HIS HIS ASP GLY VAL SER LYS ALA ASN PHE SER          
SEQRES   6 D  200  ILE GLY PRO MET MET GLN ASP LEU ALA GLY THR TYR ARG          
SEQRES   7 D  200  CYS TYR GLY SER VAL THR HIS SER PRO TYR GLN LEU SER          
SEQRES   8 D  200  ALA PRO SER ASP PRO LEU ASP ILE VAL ILE THR GLY LEU          
SEQRES   9 D  200  TYR GLU LYS PRO SER LEU SER ALA GLN PRO GLY PRO THR          
SEQRES  10 D  200  VAL LEU ALA GLY GLU SER VAL THR LEU SER CYS SER SER          
SEQRES  11 D  200  ARG SER SER TYR ASP MET TYR HIS LEU SER ARG GLU GLY          
SEQRES  12 D  200  GLU ALA HIS GLU CYS ARG PHE SER ALA GLY PRO LYS VAL          
SEQRES  13 D  200  ASN GLY THR PHE GLN ALA ASP PHE PRO LEU GLY PRO ALA          
SEQRES  14 D  200  THR HIS GLY GLY THR TYR ARG CYS PHE GLY SER PHE ARG          
SEQRES  15 D  200  ASP SER PRO TYR GLU TRP SER ASN SER SER ASP PRO LEU          
SEQRES  16 D  200  LEU VAL SER VAL ILE                                          
SEQRES   1 E  200  HIS GLU GLY VAL HIS ARG LYS PRO SER LEU LEU ALA HIS          
SEQRES   2 E  200  PRO GLY ARG LEU VAL LYS SER GLU GLU THR VAL ILE LEU          
SEQRES   3 E  200  GLN CYS TRP SER ASP VAL ARG PHE GLU HIS PHE LEU LEU          
SEQRES   4 E  200  HIS ARG GLU GLY LYS PHE LYS ASP THR LEU HIS LEU ILE          
SEQRES   5 E  200  GLY GLU HIS HIS ASP GLY VAL SER LYS ALA ASN PHE SER          
SEQRES   6 E  200  ILE GLY PRO MET MET GLN ASP LEU ALA GLY THR TYR ARG          
SEQRES   7 E  200  CYS TYR GLY SER VAL THR HIS SER PRO TYR GLN LEU SER          
SEQRES   8 E  200  ALA PRO SER ASP PRO LEU ASP ILE VAL ILE THR GLY LEU          
SEQRES   9 E  200  TYR GLU LYS PRO SER LEU SER ALA GLN PRO GLY PRO THR          
SEQRES  10 E  200  VAL LEU ALA GLY GLU SER VAL THR LEU SER CYS SER SER          
SEQRES  11 E  200  ARG SER SER TYR ASP MET TYR HIS LEU SER ARG GLU GLY          
SEQRES  12 E  200  GLU ALA HIS GLU CYS ARG PHE SER ALA GLY PRO LYS VAL          
SEQRES  13 E  200  ASN GLY THR PHE GLN ALA ASP PHE PRO LEU GLY PRO ALA          
SEQRES  14 E  200  THR HIS GLY GLY THR TYR ARG CYS PHE GLY SER PHE ARG          
SEQRES  15 E  200  ASP SER PRO TYR GLU TRP SER ASN SER SER ASP PRO LEU          
SEQRES  16 E  200  LEU VAL SER VAL ILE                                          
FORMUL   6  HOH   *185(H2 O)                                                    
HELIX    1   1 ALA A   49  GLN A   54  1                                   6    
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 GLY A  252  GLN A  255  5                                   4    
HELIX    8   8 MET D   70  ALA D   74  5                                   5    
HELIX    9   9 MET E   70  ALA E   74  5                                   5    
SHEET    1   A 8 GLY A  45  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 HIS A  21  VAL A  28 -1  O  ALA A  24   N  PHE A  36           
SHEET    4   A 8 SER A   4  VAL A  12 -1  O  ARG A   6   N  TYR A  27           
SHEET    5   A 8 ILE A  94  GLY A 104 -1  N  ILE A  95   O  ALA A  11           
SHEET    6   A 8 GLY A 107  TYR A 118 -1  N  GLY A 107   O  GLY A 104           
SHEET    7   A 8 ASP A 122  LEU A 126 -1  N  TYR A 123   O  TYR A 116           
SHEET    8   A 8 TRP A 133  ALA A 135 -1  N  THR A 134   O  ALA A 125           
SHEET    1   B 4 LYS A 186  HIS A 192  0                                        
SHEET    2   B 4 GLU A 198  LEU A 206 -1  O  THR A 200   N  HIS A 192           
SHEET    3   B 4 TRP A 244  PRO A 250 -1  O  ALA A 245   N  CYS A 203           
SHEET    4   B 4 GLU A 229  LEU A 230 -1  N  GLU A 229   O  ALA A 246           
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  N  THR A 258   O  GLN A 218           
SHEET    4   C 4 LEU A 270  LEU A 272 -1  O  LEU A 270   N  VAL A 261           
SHEET    1   D 2 ARG A 234  PRO A 235  0                                        
SHEET    2   D 2 PHE A 241  GLN A 242 -1  N  GLN A 242   O  ARG A 234           
SHEET    1   E 8 GLU B  50  HIS B  51  0                                        
SHEET    2   E 8 PHE B  62  TYR B  67 -1  N  TYR B  67   O  GLU B  50           
SHEET    3   E 8 SER B  55  PHE B  56 -1  N  SER B  55   O  TYR B  63           
SHEET    4   E 8 PHE B  62  TYR B  67 -1  O  TYR B  63   N  SER B  55           
SHEET    5   E 8 ASN B  21  SER B  28 -1  O  CYS B  25   N  TYR B  66           
SHEET    6   E 8 LYS B   6  SER B  11 -1  N  LYS B   6   O  SER B  28           
SHEET    7   E 8 ASN B  21  SER B  28 -1  N  ASN B  24   O  TYR B  10           
SHEET    8   E 8 GLU B  69  PHE B  70 -1  N  PHE B  70   O  ASN B  21           
SHEET    1   F 4 GLU B  44  ARG B  45  0                                        
SHEET    2   F 4 GLU B  36  LYS B  41 -1  N  LYS B  41   O  GLU B  44           
SHEET    3   F 4 TYR B  78  ASN B  83 -1  O  ALA B  79   N  LEU B  40           
SHEET    4   F 4 LYS B  91  LYS B  94 -1  N  LYS B  91   O  VAL B  82           
SHEET    1   G 4 SER D   9  HIS D  13  0                                        
SHEET    2   G 4 VAL D  24  SER D  30 -1  O  ILE D  25   N  HIS D  13           
SHEET    3   G 4 VAL D  59  ILE D  66 -1  N  SER D  60   O  SER D  30           
SHEET    4   G 4 GLU D  54  HIS D  56 -1  N  GLU D  54   O  LYS D  61           
SHEET    1   H 5 LEU D  17  LYS D  19  0                                        
SHEET    2   H 5 LEU D  97  THR D 102  1  O  VAL D 100   N  VAL D  18           
SHEET    3   H 5 GLY D  75  SER D  82 -1  O  GLY D  75   N  ILE D  99           
SHEET    4   H 5 HIS D  36  GLU D  42 -1  O  HIS D  36   N  SER D  82           
SHEET    5   H 5 ASP D  47  ILE D  52 -1  N  ASP D  47   O  ARG D  41           
SHEET    1   I 3 SER D 109  GLN D 113  0                                        
SHEET    2   I 3 SER D 123  SER D 129 -1  O  THR D 125   N  GLN D 113           
SHEET    3   I 3 ASP D 163  PRO D 165 -1  N  PHE D 164   O  LEU D 126           
SHEET    1   J 7 THR D 117  LEU D 119  0                                        
SHEET    2   J 7 LEU D 195  ILE D 200  1  O  SER D 198   N  VAL D 118           
SHEET    3   J 7 GLY D 173  PHE D 178 -1  O  GLY D 173   N  VAL D 197           
SHEET    4   J 7 SER D 184  TRP D 188 -1  O  SER D 184   N  PHE D 178           
SHEET    5   J 7 GLY D 173  PHE D 178 -1  N  PHE D 178   O  SER D 184           
SHEET    6   J 7 MET D 136  ARG D 141 -1  O  MET D 136   N  SER D 180           
SHEET    7   J 7 CYS D 148  SER D 151 -1  N  CYS D 148   O  LEU D 139           
SHEET    1   K 2 GLY D 153  VAL D 156  0                                        
SHEET    2   K 2 THR D 159  GLN D 161 -1  O  THR D 159   N  VAL D 156           
SHEET    1   L 4 SER E   9  HIS E  13  0                                        
SHEET    2   L 4 VAL E  24  SER E  30 -1  O  ILE E  25   N  HIS E  13           
SHEET    3   L 4 VAL E  59  ILE E  66 -1  N  SER E  60   O  SER E  30           
SHEET    4   L 4 GLU E  54  HIS E  56 -1  N  GLU E  54   O  LYS E  61           
SHEET    1   M 2 VAL E  18  LYS E  19  0                                        
SHEET    2   M 2 ILE E 101  THR E 102  1  N  THR E 102   O  VAL E  18           
SHEET    1   N 4 ASP E  47  ILE E  52  0                                        
SHEET    2   N 4 HIS E  36  GLU E  42 -1  N  PHE E  34   O  LEU E  51           
SHEET    3   N 4 GLY E  75  SER E  82 -1  O  THR E  76   N  GLU E  42           
SHEET    4   N 4 LEU E  97  ILE E  99 -1  O  LEU E  97   N  TYR E  77           
SHEET    1   O 3 SER E 109  GLN E 113  0                                        
SHEET    2   O 3 SER E 123  SER E 129 -1  O  THR E 125   N  GLN E 113           
SHEET    3   O 3 ASP E 163  PRO E 165 -1  N  PHE E 164   O  LEU E 126           
SHEET    1   P 5 THR E 117  LEU E 119  0                                        
SHEET    2   P 5 LEU E 195  ILE E 200  1  O  SER E 198   N  VAL E 118           
SHEET    3   P 5 GLY E 173  SER E 180 -1  O  GLY E 173   N  VAL E 197           
SHEET    4   P 5 MET E 136  ARG E 141 -1  O  MET E 136   N  SER E 180           
SHEET    5   P 5 CYS E 148  SER E 151 -1  N  CYS E 148   O  LEU E 139           
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  2.04  
SSBOND   4 CYS D   28    CYS D   79                          1555   1555  2.03  
SSBOND   5 CYS D  128    CYS D  177                          1555   1555  2.03  
SSBOND   6 CYS E   28    CYS E   79                          1555   1555  2.02  
SSBOND   7 CYS E  128    CYS E  177                          1555   1555  2.03  
CISPEP   1 TYR A  209    PRO A  210          0        -0.22                     
CISPEP   2 HIS B   31    PRO B   32          0         1.61                     
CISPEP   3 HIS D   13    PRO D   14          0         0.47                     
CISPEP   4 GLN D  113    PRO D  114          0        -0.13                     
CISPEP   5 HIS E   13    PRO E   14          0         0.18                     
CISPEP   6 GLN E  113    PRO E  114          0         1.87                     
CRYST1   68.540   90.330  207.270  90.00  90.00  90.00 P 21 21 21    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      0.014590  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011071  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004825        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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