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Database: PDB
Entry: 3WYR
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Original site: 3WYR 
HEADER    IMMUNE SYSTEM                           07-SEP-14   3WYR              
TITLE     CRYSTAL STRUCTURE OF KILLER CELL IMMUNOGLOBULIN-LIKE RECEPTOR 2DL4    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KILLER CELL IMMUNOGLOBULIN-LIKE RECEPTOR 2DL4;             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN, UNP RESIDUES 24-218;                 
COMPND   5 SYNONYM: CD158 ANTIGEN-LIKE FAMILY MEMBER D, G9P, KILLER CELL        
COMPND   6 INHIBITORY RECEPTOR 103AS, KIR-103AS, MHC CLASS I NK CELL RECEPTOR   
COMPND   7 KIR103AS;                                                            
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KIR2DL4, CD158D, KIR103AS;                                     
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK 293S;                               
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PHLSEC                                    
KEYWDS    IMMUNOGLOBULIN DOMAINS, IMMUNE RECEPTOR, IMMUNE SYSTEM                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.P.VIVIAN,S.MORADI,J.ROSSJOHN                                        
REVDAT   3   29-JUL-20 3WYR    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE                                     
REVDAT   2   01-JAN-20 3WYR    1       JRNL   SEQADV LINK                       
REVDAT   1   18-MAR-15 3WYR    0                                                
JRNL        AUTH   S.MORADI,R.BERRY,P.PYMM,C.HITCHEN,S.A.BECKHAM,M.C.WILCE,     
JRNL        AUTH 2 N.G.WALPOLE,C.S.CLEMENTS,H.H.REID,M.A.PERUGINI,A.G.BROOKS,   
JRNL        AUTH 3 J.ROSSJOHN,J.P.VIVIAN                                        
JRNL        TITL   THE STRUCTURE OF THE ATYPICAL KILLER CELL                    
JRNL        TITL 2 IMMUNOGLOBULIN-LIKE RECEPTOR, KIR2DL4.                       
JRNL        REF    J.BIOL.CHEM.                  V. 290 10460 2015              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   25759384                                                     
JRNL        DOI    10.1074/JBC.M114.612291                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1690)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 67.63                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 10746                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.560                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 490                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 67.6519 -  4.4448    1.00     2703   121  0.2056 0.2234        
REMARK   3     2  4.4448 -  3.5280    1.00     2536   132  0.1822 0.2228        
REMARK   3     3  3.5280 -  3.0820    1.00     2534   115  0.2269 0.2348        
REMARK   3     4  3.0820 -  2.8002    1.00     2483   122  0.2760 0.3595        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.070           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           3089                                  
REMARK   3   ANGLE     :  0.717           4228                                  
REMARK   3   CHIRALITY :  0.031            447                                  
REMARK   3   PLANARITY :  0.004            552                                  
REMARK   3   DIHEDRAL  : 13.552           1092                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 7 THROUGH 97)                       
REMARK   3    ORIGIN FOR THE GROUP (A):  20.2056  34.7266  17.7923              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2019 T22:   0.2147                                     
REMARK   3      T33:   0.2456 T12:   0.0035                                     
REMARK   3      T13:  -0.0180 T23:  -0.0535                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9117 L22:   3.1542                                     
REMARK   3      L33:   2.5239 L12:   0.9096                                     
REMARK   3      L13:  -1.2367 L23:  -0.7522                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0040 S12:  -0.0163 S13:  -0.0511                       
REMARK   3      S21:  -0.1234 S22:   0.0850 S23:  -0.3639                       
REMARK   3      S31:   0.0986 S32:   0.3265 S33:  -0.1111                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 7 THROUGH 97)                       
REMARK   3    ORIGIN FOR THE GROUP (A):  38.6782  22.1420   4.0084              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3181 T22:   0.2670                                     
REMARK   3      T33:   0.3199 T12:   0.0712                                     
REMARK   3      T13:  -0.0134 T23:  -0.0590                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3643 L22:   1.9573                                     
REMARK   3      L33:   8.6640 L12:   0.0925                                     
REMARK   3      L13:  -2.4280 L23:  -1.1556                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0147 S12:  -0.3427 S13:  -0.1604                       
REMARK   3      S21:  -0.1299 S22:  -0.1125 S23:  -0.0745                       
REMARK   3      S31:  -0.0671 S32:   0.5618 S33:  -0.0281                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 98 THROUGH 195)                     
REMARK   3    ORIGIN FOR THE GROUP (A):   7.1150  23.9601  40.8369              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5964 T22:   0.5356                                     
REMARK   3      T33:   0.3703 T12:  -0.0852                                     
REMARK   3      T13:  -0.1454 T23:   0.0891                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9560 L22:   2.8510                                     
REMARK   3      L33:   4.2364 L12:  -0.0035                                     
REMARK   3      L13:  -1.0203 L23:  -0.4483                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2821 S12:  -0.7924 S13:   0.1158                       
REMARK   3      S21:   1.0058 S22:  -0.1809 S23:  -0.2029                       
REMARK   3      S31:   0.5311 S32:   0.2699 S33:  -0.1406                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 98 THROUGH 195)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  30.8620  15.3777  32.1958              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7245 T22:   0.5904                                     
REMARK   3      T33:   0.4095 T12:   0.1060                                     
REMARK   3      T13:   0.0066 T23:   0.0923                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8112 L22:   2.0637                                     
REMARK   3      L33:   2.0915 L12:  -0.1489                                     
REMARK   3      L13:   0.3112 L23:   0.2367                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1350 S12:  -0.4270 S13:  -0.2118                       
REMARK   3      S21:   0.7395 S22:   0.3124 S23:  -0.1159                       
REMARK   3      S31:   0.6124 S32:  -0.4752 S33:  -0.0746                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3WYR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-SEP-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000096961.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-MAY-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9546                             
REMARK 200  MONOCHROMATOR                  : SYNCHROTRON                        
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10753                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 67.632                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.8000                            
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: KIR2DS4 PDB CODE 3H8N                                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 3350, 4% TACSIMATE, PH 6.0,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z                                          
REMARK 290       4555   Y+1/2,-X+1/2,Z                                          
REMARK 290       5555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       6555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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  0.000000 -1.000000  0.000000       43.91800            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       43.91800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       43.91800            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       43.91800            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       43.91800            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       43.91800            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       43.91800            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       43.91800            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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 A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     LYS A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     ASP B    -4                                                      
REMARK 465     ASP B    -3                                                      
REMARK 465     ASP B    -2                                                      
REMARK 465     ASP B    -1                                                      
REMARK 465     LYS B     0                                                      
REMARK 465     HIS B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     GLN B     5                                                      
REMARK 465     ASP B     6                                                      
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     GLU A 168    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU B 168    CB   CG   CD   OE1  OE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLY A    98     O    HOH A   301              2.01            
REMARK 500   O    PHE A   176     O    HOH A   305              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  35       43.73    -75.48                                   
REMARK 500    ASN A  57      -79.73     63.01                                   
REMARK 500    HIS A  80       65.24   -101.15                                   
REMARK 500    GLU A  84       12.78     58.82                                   
REMARK 500    SER A  89     -177.24    -69.90                                   
REMARK 500    SER A 128       53.43    -91.04                                   
REMARK 500    ALA A 140       49.08    -79.37                                   
REMARK 500    SER A 150      135.55   -172.07                                   
REMARK 500    ASN B  35       41.47    -82.69                                   
REMARK 500    ASN B  57      -66.09     60.23                                   
REMARK 500    HIS B  80       57.63   -107.71                                   
REMARK 500    GLU B  84        7.60     58.31                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THESE RESIDUES ARE NATURAL VARIANT.                                  
DBREF  3WYR A    1   195  UNP    Q99706   KI2L4_HUMAN     24    218             
DBREF  3WYR B    1   195  UNP    Q99706   KI2L4_HUMAN     24    218             
SEQADV 3WYR HIS A  -10  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR HIS A   -9  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR HIS A   -8  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR HIS A   -7  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR HIS A   -6  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR HIS A   -5  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR ASP A   -4  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR ASP A   -3  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR ASP A   -2  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR ASP A   -1  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR LYS A    0  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR THR A  115  UNP  Q99706    ALA   138 SEE REMARK 999                 
SEQADV 3WYR ALA A  186  UNP  Q99706    PRO   209 SEE REMARK 999                 
SEQADV 3WYR HIS B  -10  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR HIS B   -9  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR HIS B   -8  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR HIS B   -7  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR HIS B   -6  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR HIS B   -5  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR ASP B   -4  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR ASP B   -3  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR ASP B   -2  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR ASP B   -1  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR LYS B    0  UNP  Q99706              EXPRESSION TAG                 
SEQADV 3WYR THR B  115  UNP  Q99706    ALA   138 SEE REMARK 999                 
SEQADV 3WYR ALA B  186  UNP  Q99706    PRO   209 SEE REMARK 999                 
SEQRES   1 A  206  HIS HIS HIS HIS HIS HIS ASP ASP ASP ASP LYS HIS VAL          
SEQRES   2 A  206  GLY GLY GLN ASP LYS PRO PHE CYS SER ALA TRP PRO SER          
SEQRES   3 A  206  ALA VAL VAL PRO GLN GLY GLY HIS VAL THR LEU ARG CYS          
SEQRES   4 A  206  HIS TYR ARG ARG GLY PHE ASN ILE PHE THR LEU TYR LYS          
SEQRES   5 A  206  LYS ASP GLY VAL PRO VAL PRO GLU LEU TYR ASN ARG ILE          
SEQRES   6 A  206  PHE TRP ASN SER PHE LEU ILE SER PRO VAL THR PRO ALA          
SEQRES   7 A  206  HIS ALA GLY THR TYR ARG CYS ARG GLY PHE HIS PRO HIS          
SEQRES   8 A  206  SER PRO THR GLU TRP SER ALA PRO SER ASN PRO LEU VAL          
SEQRES   9 A  206  ILE MET VAL THR GLY LEU TYR GLU LYS PRO SER LEU THR          
SEQRES  10 A  206  ALA ARG PRO GLY PRO THR VAL ARG THR GLY GLU ASN VAL          
SEQRES  11 A  206  THR LEU SER CYS SER SER GLN SER SER PHE ASP ILE TYR          
SEQRES  12 A  206  HIS LEU SER ARG GLU GLY GLU ALA HIS GLU LEU ARG LEU          
SEQRES  13 A  206  PRO ALA VAL PRO SER ILE ASN GLY THR PHE GLN ALA ASP          
SEQRES  14 A  206  PHE PRO LEU GLY PRO ALA THR HIS GLY GLU THR TYR ARG          
SEQRES  15 A  206  CYS PHE GLY SER PHE HIS GLY SER PRO TYR GLU TRP SER          
SEQRES  16 A  206  ASP ALA SER ASP PRO LEU PRO VAL SER VAL THR                  
SEQRES   1 B  206  HIS HIS HIS HIS HIS HIS ASP ASP ASP ASP LYS HIS VAL          
SEQRES   2 B  206  GLY GLY GLN ASP LYS PRO PHE CYS SER ALA TRP PRO SER          
SEQRES   3 B  206  ALA VAL VAL PRO GLN GLY GLY HIS VAL THR LEU ARG CYS          
SEQRES   4 B  206  HIS TYR ARG ARG GLY PHE ASN ILE PHE THR LEU TYR LYS          
SEQRES   5 B  206  LYS ASP GLY VAL PRO VAL PRO GLU LEU TYR ASN ARG ILE          
SEQRES   6 B  206  PHE TRP ASN SER PHE LEU ILE SER PRO VAL THR PRO ALA          
SEQRES   7 B  206  HIS ALA GLY THR TYR ARG CYS ARG GLY PHE HIS PRO HIS          
SEQRES   8 B  206  SER PRO THR GLU TRP SER ALA PRO SER ASN PRO LEU VAL          
SEQRES   9 B  206  ILE MET VAL THR GLY LEU TYR GLU LYS PRO SER LEU THR          
SEQRES  10 B  206  ALA ARG PRO GLY PRO THR VAL ARG THR GLY GLU ASN VAL          
SEQRES  11 B  206  THR LEU SER CYS SER SER GLN SER SER PHE ASP ILE TYR          
SEQRES  12 B  206  HIS LEU SER ARG GLU GLY GLU ALA HIS GLU LEU ARG LEU          
SEQRES  13 B  206  PRO ALA VAL PRO SER ILE ASN GLY THR PHE GLN ALA ASP          
SEQRES  14 B  206  PHE PRO LEU GLY PRO ALA THR HIS GLY GLU THR TYR ARG          
SEQRES  15 B  206  CYS PHE GLY SER PHE HIS GLY SER PRO TYR GLU TRP SER          
SEQRES  16 B  206  ASP ALA SER ASP PRO LEU PRO VAL SER VAL THR                  
MODRES 3WYR ASN B  118  ASN  GLYCOSYLATION SITE                                 
MODRES 3WYR ASN A  118  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 201      14                                                       
HET    NAG  B 201      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   5  HOH   *36(H2 O)                                                     
HELIX    1   1 VAL A   47  TYR A   51  5                                   5    
HELIX    2   2 THR A   65  ALA A   69  5                                   5    
HELIX    3   3 VAL B   47  TYR B   51  5                                   5    
HELIX    4   4 THR B   65  ALA B   69  5                                   5    
SHEET    1   A 3 PHE A   9  TRP A  13  0                                        
SHEET    2   A 3 VAL A  24  HIS A  29 -1  O  ARG A  27   N  SER A  11           
SHEET    3   A 3 SER A  58  ILE A  61 -1  O  ILE A  61   N  VAL A  24           
SHEET    1   B 5 VAL A  17  PRO A  19  0                                        
SHEET    2   B 5 LEU A  92  THR A  97  1  O  MET A  95   N  VAL A  18           
SHEET    3   B 5 GLY A  70  PHE A  77 -1  N  TYR A  72   O  LEU A  92           
SHEET    4   B 5 PHE A  34  LYS A  41 -1  N  PHE A  34   O  PHE A  77           
SHEET    5   B 5 ARG A  53  TRP A  56 -1  O  ARG A  53   N  LEU A  39           
SHEET    1   C 4 SER A 104  ARG A 108  0                                        
SHEET    2   C 4 ASN A 118  SER A 125 -1  O  SER A 124   N  SER A 104           
SHEET    3   C 4 THR A 154  PRO A 163 -1  O  PHE A 159   N  LEU A 121           
SHEET    4   C 4 VAL A 148  SER A 150 -1  N  SER A 150   O  THR A 154           
SHEET    1   D 5 THR A 112  VAL A 113  0                                        
SHEET    2   D 5 LEU A 190  VAL A 194  1  O  SER A 193   N  VAL A 113           
SHEET    3   D 5 GLU A 168  SER A 175 -1  N  TYR A 170   O  LEU A 190           
SHEET    4   D 5 ILE A 131  ARG A 136 -1  N  ILE A 131   O  SER A 175           
SHEET    5   D 5 GLU A 139  PRO A 146 -1  O  LEU A 145   N  TYR A 132           
SHEET    1   E 3 PHE B   9  TRP B  13  0                                        
SHEET    2   E 3 VAL B  24  HIS B  29 -1  O  ARG B  27   N  SER B  11           
SHEET    3   E 3 SER B  58  ILE B  61 -1  O  ILE B  61   N  VAL B  24           
SHEET    1   F 5 VAL B  17  PRO B  19  0                                        
SHEET    2   F 5 LEU B  92  THR B  97  1  O  MET B  95   N  VAL B  18           
SHEET    3   F 5 GLY B  70  PHE B  77 -1  N  GLY B  70   O  ILE B  94           
SHEET    4   F 5 PHE B  34  LYS B  41 -1  N  TYR B  40   O  ARG B  73           
SHEET    5   F 5 ILE B  54  TRP B  56 -1  O  PHE B  55   N  PHE B  37           
SHEET    1   G 4 VAL B  17  PRO B  19  0                                        
SHEET    2   G 4 LEU B  92  THR B  97  1  O  MET B  95   N  VAL B  18           
SHEET    3   G 4 GLY B  70  PHE B  77 -1  N  GLY B  70   O  ILE B  94           
SHEET    4   G 4 TRP B  85  PRO B  88 -1  O  SER B  86   N  GLY B  76           
SHEET    1   H 4 SER B 104  ARG B 108  0                                        
SHEET    2   H 4 ASN B 118  SER B 125 -1  O  THR B 120   N  ARG B 108           
SHEET    3   H 4 PHE B 155  PRO B 163 -1  O  LEU B 161   N  VAL B 119           
SHEET    4   H 4 VAL B 148  PRO B 149 -1  N  VAL B 148   O  GLN B 156           
SHEET    1   I 5 THR B 112  VAL B 113  0                                        
SHEET    2   I 5 LEU B 190  VAL B 194  1  O  SER B 193   N  VAL B 113           
SHEET    3   I 5 GLU B 168  SER B 175 -1  N  TYR B 170   O  LEU B 190           
SHEET    4   I 5 ILE B 131  ARG B 136 -1  N  SER B 135   O  ARG B 171           
SHEET    5   I 5 LEU B 143  PRO B 146 -1  O  LEU B 145   N  TYR B 132           
SSBOND   1 CYS A   10    CYS A   28                          1555   1555  2.03  
SSBOND   2 CYS A  123    CYS A  172                          1555   1555  2.03  
SSBOND   3 CYS B   10    CYS B   28                          1555   1555  2.03  
SSBOND   4 CYS B  123    CYS B  172                          1555   1555  2.03  
LINK         ND2 ASN A 118                 C1  NAG A 201     1555   1555  1.44  
LINK         ND2 ASN B 118                 C1  NAG B 201     1555   1555  1.44  
CISPEP   1 TRP A   13    PRO A   14          0         7.17                     
CISPEP   2 SER A   62    PRO A   63          0        -0.88                     
CISPEP   3 ARG A  108    PRO A  109          0         4.83                     
CISPEP   4 ILE A  151    ASN A  152          0         6.00                     
CISPEP   5 TRP B   13    PRO B   14          0         3.82                     
CISPEP   6 SER B   62    PRO B   63          0        -0.39                     
CISPEP   7 ARG B  108    PRO B  109          0         1.85                     
CRYST1   87.836   87.836  105.996  90.00  90.00  90.00 P 4 21 2     16          
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      0.011385  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011385  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009434        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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