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Database: PDB
Entry: 1B6U
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HEADER    KILLER CELL INHIBITORY RECEPTOR         18-JAN-99   1B6U              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN KILLER CELL INHIBITORY RECEPTOR        
TITLE    2 (KIR2DL3) SPECIFIC FOR HLA-CW3 RELATED ALLELES                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: P58 KILLER CELL INHIBITORY RECEPTOR;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EXTRACELLULAR REGION;                                      
COMPND   5 SYNONYM: KIR2DL3;                                                    
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: BL21;                                                     
SOURCE   6 CELL: NATURAL KILLER CELL;                                           
SOURCE   7 CELLULAR_LOCATION: CELL SURFACE;                                     
SOURCE   8 GENE: NKAT2;                                                         
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  11 EXPRESSION_SYSTEM_STRAIN: BL21 PLYSS;                                
SOURCE  12 EXPRESSION_SYSTEM_CELLULAR_LOCATION: MEDIA AND PERIPLASMIC SPACE;    
SOURCE  13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  14 EXPRESSION_SYSTEM_VECTOR: ESCHERICHIA COLI;                          
SOURCE  15 EXPRESSION_SYSTEM_PLASMID: PKMATHNK2;                                
SOURCE  16 EXPRESSION_SYSTEM_GENE: NKAT2;                                       
SOURCE  17 OTHER_DETAILS: CLONING BY PCR                                        
KEYWDS    KILLER CELL INHIBITORY RECEPTOR, NATURAL KILLER CELL, HLA, MAJOR      
KEYWDS   2 HISTOCOMPATIBILITY COMPLEX CLASS I (MHC CLASS I), CELL SURFACE       
KEYWDS   3 RECEPTOR, IMMUNOGLOBULIN SUPERFAMILY                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.MAENAKA,T.JUJI,D.I.STUART,E.Y.JONES                                 
REVDAT   4   13-JUN-18 1B6U    1       REMARK                                   
REVDAT   3   24-FEB-09 1B6U    1       VERSN                                    
REVDAT   2   06-APR-99 1B6U    3       ATOM   SOURCE COMPND REMARK              
REVDAT   2 2                   3       SEQRES DBREF  CISPEP SEQADV              
REVDAT   2 3                   3       KEYWDS SSBOND SHEET  TER                 
REVDAT   1   27-JAN-99 1B6U    0                                                
JRNL        AUTH   K.MAENAKA,T.JUJI,D.I.STUART,E.Y.JONES                        
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN P58 KILLER CELL INHIBITORY    
JRNL        TITL 2 RECEPTOR (KIR2DL3) SPECIFIC FOR HLA-CW3-RELATED MHC CLASS I. 
JRNL        REF    STRUCTURE FOLD.DES.           V.   7   391 1999              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   10196125                                                     
JRNL        DOI    10.1016/S0969-2126(99)80052-5                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.5                                              
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 79.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 5896                           
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) : 0.248                           
REMARK   3   FREE R VALUE                     : 0.320                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 354                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1540                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.40000                                             
REMARK   3    B22 (A**2) : -0.40000                                             
REMARK   3    B33 (A**2) : 0.81000                                              
REMARK   3    B12 (A**2) : -4.12000                                             
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.570                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.25                                                 
REMARK   3   BSOL        : 20.00                                                
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: REFINED BY X-PLOR, REFMAC AND CN          
REMARK   4                                                                      
REMARK   4 1B6U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000171504.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : OCT-96                             
REMARK 200  TEMPERATURE           (KELVIN) : 288                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : FUJI                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6281                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.9                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.19500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS 0.5                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: DATA WERE COLLECTED USING WEISSENBERG METHOD.                
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       87.20000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       43.60000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       65.40000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       21.80000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      109.00000            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       87.20000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       43.60000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       21.80000            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       65.40000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      109.00000            
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000      143.10000            
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000       82.61882            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       43.60000            
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 A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     SER A   204                                                      
REMARK 465     ASN A   205                                                      
REMARK 465     SER A   206                                                      
REMARK 465     TRP A   207                                                      
REMARK 465     PRO A   208                                                      
REMARK 465     SER A   209                                                      
REMARK 465     PRO A   210                                                      
REMARK 465     THR A   211                                                      
REMARK 465     GLU A   212                                                      
REMARK 465     PRO A   213                                                      
REMARK 465     SER A   214                                                      
REMARK 465     SER A   215                                                      
REMARK 465     GLU A   216                                                      
REMARK 465     THR A   217                                                      
REMARK 465     GLY A   218                                                      
REMARK 465     ASN A   219                                                      
REMARK 465     PRO A   220                                                      
REMARK 465     ARG A   221                                                      
REMARK 465     HIS A   222                                                      
REMARK 465     LEU A   223                                                      
REMARK 465     HIS A   224                                                      
REMARK 465     ALA A   225                                                      
REMARK 465     ALA A   226                                                      
REMARK 465     ALA A   227                                                      
REMARK 465     GLU A   228                                                      
REMARK 465     GLN A   229                                                      
REMARK 465     LYS A   230                                                      
REMARK 465     LEU A   231                                                      
REMARK 465     ILE A   232                                                      
REMARK 465     SER A   233                                                      
REMARK 465     GLU A   234                                                      
REMARK 465     GLU A   235                                                      
REMARK 465     ASP A   236                                                      
REMARK 465     LEU A   237                                                      
REMARK 465     ASN A   238                                                      
REMARK 465     LEU A   239                                                      
REMARK 465     ASP A   240                                                      
REMARK 465     LEU A   241                                                      
REMARK 465     VAL A   242                                                      
REMARK 465     PRO A   243                                                      
REMARK 465     ARG A   244                                                      
REMARK 465     GLY A   245                                                      
REMARK 465     SER A   246                                                      
REMARK 465     SER A   247                                                      
REMARK 465     SER A   248                                                      
REMARK 465     HIS A   249                                                      
REMARK 465     HIS A   250                                                      
REMARK 465     HIS A   251                                                      
REMARK 465     HIS A   252                                                      
REMARK 465     HIS A   253                                                      
REMARK 465     HIS A   254                                                      
REMARK 465     SER A   255                                                      
REMARK 465     SER A   256                                                      
REMARK 465     GLY A   257                                                      
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    PRO A 154   C   -  N   -  CA  ANGL. DEV. =   9.1 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    ARG A   6      165.49    -38.50                                   
REMARK 500    GLU A  21      -42.49     61.05                                   
REMARK 500    ARG A  33       36.74    -95.74                                   
REMARK 500    LYS A  44      -86.28    -48.13                                   
REMARK 500    LYS A  46      108.75    -48.22                                   
REMARK 500    ASP A  57      118.84    -13.71                                   
REMARK 500    PRO A  68      108.75    -32.85                                   
REMARK 500    THR A  84      -72.40     -9.30                                   
REMARK 500    HIS A  85       43.91    -72.47                                   
REMARK 500    SER A  86       51.86    155.18                                   
REMARK 500    PRO A  87        4.48    -61.71                                   
REMARK 500    GLN A 113      133.91   -175.19                                   
REMARK 500    VAL A 118      160.57    -42.58                                   
REMARK 500    SER A 133       49.95    -87.19                                   
REMARK 500    GLU A 142      101.12    -15.16                                   
REMARK 500    GLU A 144      125.74    -37.47                                   
REMARK 500    ALA A 145      -88.41      3.15                                   
REMARK 500    PHE A 150      138.19   -172.60                                   
REMARK 500    LYS A 155      123.47     56.52                                   
REMARK 500    VAL A 156      -39.10   -158.66                                   
REMARK 500    ASN A 157       29.83   -157.27                                   
REMARK 500    ALA A 169      104.07    -56.84                                   
REMARK 500    THR A 170      -90.44    -70.86                                   
REMARK 500    ASP A 183      -72.01    -22.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1B6U A    1   224  UNP    P43628   KI2L3_HUMAN     22    245             
SEQRES   1 A  257  HIS GLU GLY VAL HIS ARG LYS PRO SER LEU LEU ALA HIS          
SEQRES   2 A  257  PRO GLY PRO LEU VAL LYS SER GLU GLU THR VAL ILE LEU          
SEQRES   3 A  257  GLN CYS TRP SER ASP VAL ARG PHE GLN HIS PHE LEU LEU          
SEQRES   4 A  257  HIS ARG GLU GLY LYS PHE LYS ASP THR LEU HIS LEU ILE          
SEQRES   5 A  257  GLY GLU HIS HIS ASP GLY VAL SER LYS ALA ASN PHE SER          
SEQRES   6 A  257  ILE GLY PRO MET MET GLN ASP LEU ALA GLY THR TYR ARG          
SEQRES   7 A  257  CYS TYR GLY SER VAL THR HIS SER PRO TYR GLN LEU SER          
SEQRES   8 A  257  ALA PRO SER ASP PRO LEU ASP ILE VAL ILE THR GLY LEU          
SEQRES   9 A  257  TYR GLU LYS PRO SER LEU SER ALA GLN PRO GLY PRO THR          
SEQRES  10 A  257  VAL LEU ALA GLY GLU SER VAL THR LEU SER CYS SER SER          
SEQRES  11 A  257  ARG SER SER TYR ASP MET TYR HIS LEU SER ARG GLU GLY          
SEQRES  12 A  257  GLU ALA HIS GLU ARG ARG PHE SER ALA GLY PRO LYS VAL          
SEQRES  13 A  257  ASN GLY THR PHE GLN ALA ASP PHE PRO LEU GLY PRO ALA          
SEQRES  14 A  257  THR HIS GLY GLY THR TYR ARG CYS PHE GLY SER PHE ARG          
SEQRES  15 A  257  ASP SER PRO TYR GLU TRP SER ASN SER SER ASP PRO LEU          
SEQRES  16 A  257  LEU VAL SER VAL THR GLY ASN PRO SER ASN SER TRP PRO          
SEQRES  17 A  257  SER PRO THR GLU PRO SER SER GLU THR GLY ASN PRO ARG          
SEQRES  18 A  257  HIS LEU HIS ALA ALA ALA GLU GLN LYS LEU ILE SER GLU          
SEQRES  19 A  257  GLU ASP LEU ASN LEU ASP LEU VAL PRO ARG GLY SER SER          
SEQRES  20 A  257  SER HIS HIS HIS HIS HIS HIS SER SER GLY                      
SHEET    1   A 2 LEU A  17  LYS A  19  0                                        
SHEET    2   A 2 VAL A 100  THR A 102  1  N  VAL A 100   O  VAL A  18           
SHEET    1   B 2 VAL A  24  SER A  30  0                                        
SHEET    2   B 2 SER A  60  ILE A  66 -1  N  ILE A  66   O  VAL A  24           
SHEET    1   C 4 ASP A  47  ILE A  52  0                                        
SHEET    2   C 4 HIS A  36  GLU A  42 -1  N  ARG A  41   O  ASP A  47           
SHEET    3   C 4 GLY A  75  SER A  82 -1  N  SER A  82   O  HIS A  36           
SHEET    4   C 4 LEU A  97  ILE A  99 -1  N  ILE A  99   O  GLY A  75           
SHEET    1   D 3 SER A 109  SER A 111  0                                        
SHEET    2   D 3 SER A 123  SER A 130 -1  N  SER A 129   O  SER A 109           
SHEET    3   D 3 PHE A 160  PRO A 168 -1  N  GLY A 167   O  VAL A 124           
SHEET    1   E 3 MET A 136  ARG A 141  0                                        
SHEET    2   E 3 GLY A 173  SER A 180 -1  N  SER A 180   O  MET A 136           
SHEET    3   E 3 LEU A 195  VAL A 197 -1  N  VAL A 197   O  GLY A 173           
SSBOND   1 CYS A   28    CYS A   79                          1555   1555  2.02  
SSBOND   2 CYS A  128    CYS A  177                          1555   1555  2.03  
CISPEP   1 HIS A   13    PRO A   14          0         0.07                     
CISPEP   2 GLN A  113    PRO A  114          0         0.19                     
CRYST1   95.400   95.400  130.800  90.00  90.00 120.00 P 65 2 2     12          
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      0.010482  0.006052  0.000000        0.00000                         
SCALE2      0.000000  0.012104  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007645        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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