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Database: PDB
Entry: 5B38
LinkDB: 5B38
Original site: 5B38 
HEADER    IMMUNE SYSTEM                           12-FEB-16   5B38              
TITLE     KIR3DL1*005 IN COMPLEX WITH HLA-B*57:01                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, B-57 ALPHA CHAIN;  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 25-300;                                       
COMPND   5 SYNONYM: HLA-B*57:01,BW-57,MHC CLASS I ANTIGEN B*57;                 
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 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: PEPTIDE FROM IG KAPPA CHAIN C REGION;                      
COMPND  13 CHAIN: C;                                                            
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: KILLER CELL IMMUNOGLOBULIN-LIKE RECEPTOR 3DL1;             
COMPND  17 CHAIN: G;                                                            
COMPND  18 FRAGMENT: UNP RESIDUES 22-320;                                       
COMPND  19 SYNONYM: KIR3DL1*005,CD158 ANTIGEN-LIKE FAMILY MEMBER E,HLA-BW4-     
COMPND  20 SPECIFIC INHIBITORY NK CELL RECEPTOR,MHC CLASS I NK CELL RECEPTOR,   
COMPND  21 NATURAL KILLER-ASSOCIATED TRANSCRIPT 3,NKAT-3,P70 NATURAL KILLER CELL
COMPND  22 RECEPTOR CLONES CL-2/CL-11,P70 NK RECEPTOR CL-2/CL-11;               
COMPND  23 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: HLA-B, HLAB;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ENTEROBACTERIA PHAGE L1;                          
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 268588;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: B2M, CDABP0092, HDCMA22P;                                      
SOURCE  13 EXPRESSION_SYSTEM: ENTEROBACTERIA PHAGE L1;                          
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 268588;                                     
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 MOL_ID: 4;                                                           
SOURCE  21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  22 ORGANISM_COMMON: HUMAN;                                              
SOURCE  23 ORGANISM_TAXID: 9606;                                                
SOURCE  24 GENE: KIR3DL1, CD158E, NKAT3, NKB1;                                  
SOURCE  25 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  26 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 7111                                        
KEYWDS    INNATE IMMUNE RECEPTOR, KIR, NATURAL KILLER CELL, IMMUNE SYSTEM       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.P.VIVIAN,J.ROSSJOHN                                                 
REVDAT   4   18-OCT-17 5B38    1       JRNL   REMARK                            
REVDAT   3   18-MAY-16 5B38    1       JRNL                                     
REVDAT   2   20-APR-16 5B38    1       JRNL                                     
REVDAT   1   30-MAR-16 5B38    0                                                
JRNL        AUTH   P.M.SAUNDERS,P.PYMM,G.PIETRA,V.A.HUGHES,C.HITCHEN,           
JRNL        AUTH 2 G.M.O'CONNOR,F.LOIACONO,J.WIDJAJA,D.A.PRICE,M.FALCO,         
JRNL        AUTH 3 M.C.MINGARI,L.MORETTA,D.W.MCVICAR,J.ROSSJOHN,A.G.BROOKS,     
JRNL        AUTH 4 J.P.VIVIAN                                                   
JRNL        TITL   KILLER CELL IMMUNOGLOBULIN-LIKE RECEPTOR 3DL1 POLYMORPHISM   
JRNL        TITL 2 DEFINES DISTINCT HIERARCHIES OF HLA CLASS I RECOGNITION      
JRNL        REF    J.EXP.MED.                    V. 213   791 2016              
JRNL        REFN                   ESSN 1540-9538                               
JRNL        PMID   27045007                                                     
JRNL        DOI    10.1084/JEM.20152023                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.650                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 61236                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3068                            
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 35.5002 -  6.4325    0.83     2383   125  0.1727 0.2269        
REMARK   3     2  6.4325 -  5.1105    0.95     2705   156  0.1646 0.2103        
REMARK   3     3  5.1105 -  4.4659    0.80     2303   133  0.1388 0.1702        
REMARK   3     4  4.4659 -  4.0583    0.89     2599   141  0.1534 0.1925        
REMARK   3     5  4.0583 -  3.7677    0.88     2514   120  0.1812 0.2003        
REMARK   3     6  3.7677 -  3.5458    0.90     2648   125  0.2252 0.3291        
REMARK   3     7  3.5458 -  3.3684    0.93     2608   146  0.1940 0.2527        
REMARK   3     8  3.3684 -  3.2218    0.92     2623   165  0.1910 0.2404        
REMARK   3     9  3.2218 -  3.0979    0.92     2647   179  0.2051 0.2418        
REMARK   3    10  3.0979 -  2.9910    0.93     2684   140  0.1997 0.2823        
REMARK   3    11  2.9910 -  2.8976    0.93     2635   132  0.2070 0.2393        
REMARK   3    12  2.8976 -  2.8148    0.93     2703   145  0.2230 0.3497        
REMARK   3    13  2.8148 -  2.7407    0.94     2709   141  0.2265 0.2788        
REMARK   3    14  2.7407 -  2.6739    0.94     2655   138  0.2295 0.2853        
REMARK   3    15  2.6739 -  2.6131    0.95     2753   152  0.2222 0.3284        
REMARK   3    16  2.6131 -  2.5575    0.94     2660   152  0.2362 0.3058        
REMARK   3    17  2.5575 -  2.5063    0.95     2846   121  0.2322 0.3171        
REMARK   3    18  2.5063 -  2.4591    0.95     2581   122  0.2406 0.3213        
REMARK   3    19  2.4591 -  2.4152    0.93     2815   146  0.2336 0.3068        
REMARK   3    20  2.4152 -  2.3742    0.95     2671   139  0.2454 0.2984        
REMARK   3    21  2.3742 -  2.3359    0.95     2742   140  0.2414 0.3117        
REMARK   3    22  2.3359 -  2.3000    0.93     2684   110  0.2524 0.2878        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.130           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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           5468                                  
REMARK   3   ANGLE     :  0.702           7412                                  
REMARK   3   CHIRALITY :  0.030            777                                  
REMARK   3   PLANARITY :  0.003            963                                  
REMARK   3   DIHEDRAL  : 12.771           1989                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE ENTRY CONTAINS FRIEDEL PAIRS IN       
REMARK   3  F_PLUS/MINUS COLUMNS                                                
REMARK   4                                                                      
REMARK   4 5B38 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-FEB-16.                  
REMARK 100 THE DEPOSITION ID IS D_1300000450.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-FEB-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
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) : 0.954                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61910                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: 3VH8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14 TO 18% PEG 3350, 2% TACSIMATE PH      
REMARK 280  5.0, 0.1 M TRI-SODIUM CITRATE PH 5.6, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 294K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, G                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A   276                                                      
REMARK 465     HIS G     1                                                      
REMARK 465     MET G     2                                                      
REMARK 465     GLY G     3                                                      
REMARK 465     GLY G     4                                                      
REMARK 465     GLN G     5                                                      
REMARK 465     ASP G     6                                                      
REMARK 465     PRO G   209                                                      
REMARK 465     GLY G   210                                                      
REMARK 465     PRO G   211                                                      
REMARK 465     LYS G   212                                                      
REMARK 465     VAL G   213                                                      
REMARK 465     GLN G   214                                                      
REMARK 465     ALA G   215                                                      
REMARK 465     GLY G   216                                                      
REMARK 465     GLU G   217                                                      
REMARK 465     GLY G   262                                                      
REMARK 465     PRO G   263                                                      
REMARK 465     ALA G   264                                                      
REMARK 465     THR G   265                                                      
REMARK 465     HIS G   266                                                      
REMARK 465     VAL G   294                                                      
REMARK 465     THR G   295                                                      
REMARK 465     GLY G   296                                                      
REMARK 465     ASN G   297                                                      
REMARK 465     PRO G   298                                                      
REMARK 465     SER G   299                                                      
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     ASN G  35    CG   OD1  ND2                                       
REMARK 470     GLU G  42    CG   CD   OE1  OE2                                  
REMARK 470     GLU G  57    CG   CD   OE1  OE2                                  
REMARK 470     GLN G 208    CG   CD   OE1  NE2                                  
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    PRO G   286     O    HOH G   401              1.88            
REMARK 500   OD1  ASP A   114     O    HOH A   301              1.89            
REMARK 500   O    HOH G   480     O    HOH G   481              1.93            
REMARK 500   OD1  ASN B    83     O    HOH B   101              1.99            
REMARK 500   OD1  ASP B    76     O    HOH B   102              2.03            
REMARK 500   O    ALA A    40     O    HOH A   302              2.04            
REMARK 500   OH   TYR G    30     O    HOH G   402              2.05            
REMARK 500   O    HOH G   423     O    HOH G   443              2.05            
REMARK 500   O    HOH G   431     O    HOH G   483              2.06            
REMARK 500   OE1  GLU A   275     O    HOH A   303              2.07            
REMARK 500   O    HOH A   353     O    HOH A   392              2.08            
REMARK 500   NE2  HIS G    46     O    HOH G   403              2.09            
REMARK 500   O    HOH A   370     O    HOH A   391              2.11            
REMARK 500   ND2  ASN G    71     O5   NAG G   301              2.13            
REMARK 500   OE2  GLU A    76     O    HOH A   304              2.14            
REMARK 500   OD2  ASP A   227     O    HOH A   305              2.16            
REMARK 500   NE   ARG A    65     O    HOH A   306              2.16            
REMARK 500   O7   NAG G   303     O    HOH G   404              2.16            
REMARK 500   O    ASN G   252     O    HOH G   405              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   355     O    HOH G   479     1445     2.05            
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  14       71.03   -153.44                                   
REMARK 500    ASP A  29     -115.90     55.57                                   
REMARK 500    ASP A 114       92.40   -161.78                                   
REMARK 500    ASP A 227       36.80    -91.70                                   
REMARK 500    PRO B  32     -165.83    -74.27                                   
REMARK 500    GLU B  47      -71.60    -70.38                                   
REMARK 500    LYS C   7       76.78   -116.89                                   
REMARK 500    PHE G  34       57.77    -94.01                                   
REMARK 500    SER G  62      119.63   -163.15                                   
REMARK 500    SER G 140       66.51     60.38                                   
REMARK 500    HIS G 180       -1.98     76.05                                   
REMARK 500    ALA G 240      -70.16    -98.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 301 bound   
REMARK 800  to ASN G 71                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 302 bound   
REMARK 800  to ASN G 158                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 303 bound   
REMARK 800  to ASN G 252                                                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3VH8   RELATED DB: PDB                                   
REMARK 900 3VH8 CONTAINS A SIMILAR KIR3DL1 (*001) IN COMPLEX WITH THE SAME PHLA 
REMARK 900 RELATED ID: 5B39   RELATED DB: PDB                                   
DBREF  5B38 A    1   276  UNP    P18465   1B57_HUMAN      25    300             
DBREF  5B38 B    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  5B38 C    1     9  UNP    P01834   IGKC_HUMAN      93    101             
DBREF  5B38 G    1   299  UNP    P43629   KI3L1_HUMAN     22    320             
SEQADV 5B38 SER G  182  UNP  P43629    PRO   203 VARIANT                        
SEQADV 5B38 LEU G  283  UNP  P43629    TRP   304 VARIANT                        
SEQRES   1 A  276  GLY SER HIS SER MET ARG TYR PHE TYR THR ALA MET SER          
SEQRES   2 A  276  ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY          
SEQRES   3 A  276  TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP          
SEQRES   4 A  276  ALA ALA SER PRO ARG MET ALA PRO ARG ALA PRO TRP ILE          
SEQRES   5 A  276  GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG          
SEQRES   6 A  276  ASN MET LYS ALA SER ALA GLN THR TYR ARG GLU ASN LEU          
SEQRES   7 A  276  ARG ILE ALA LEU ARG TYR TYR ASN GLN SER GLU ALA GLY          
SEQRES   8 A  276  SER HIS ILE ILE GLN VAL MET TYR GLY CYS ASP VAL GLY          
SEQRES   9 A  276  PRO ASP GLY ARG LEU LEU ARG GLY HIS ASP GLN SER ALA          
SEQRES  10 A  276  TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP LEU          
SEQRES  11 A  276  SER SER TRP THR ALA ALA ASP THR ALA ALA GLN ILE THR          
SEQRES  12 A  276  GLN ARG LYS TRP GLU ALA ALA ARG VAL ALA GLU GLN LEU          
SEQRES  13 A  276  ARG ALA TYR LEU GLU GLY LEU CYS VAL GLU TRP LEU ARG          
SEQRES  14 A  276  ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG ALA          
SEQRES  15 A  276  ASP PRO PRO LYS THR HIS VAL THR HIS HIS PRO ILE SER          
SEQRES  16 A  276  ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY PHE          
SEQRES  17 A  276  TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY          
SEQRES  18 A  276  GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG          
SEQRES  19 A  276  PRO ALA GLY ASP ARG THR PHE GLN LYS TRP ALA ALA VAL          
SEQRES  20 A  276  VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS          
SEQRES  21 A  276  VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG          
SEQRES  22 A  276  TRP GLU PRO                                                  
SEQRES   1 B   99  ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS          
SEQRES   2 B   99  PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR          
SEQRES   3 B   99  VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU          
SEQRES   4 B   99  LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER          
SEQRES   5 B   99  ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU          
SEQRES   6 B   99  TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR          
SEQRES   7 B   99  ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS          
SEQRES   8 B   99  ILE VAL LYS TRP ASP ARG ASP MET                              
SEQRES   1 C    9  LEU SER SER PRO VAL THR LYS SER PHE                          
SEQRES   1 G  299  HIS MET GLY GLY GLN ASP LYS PRO PHE LEU SER ALA TRP          
SEQRES   2 G  299  PRO SER ALA VAL VAL PRO ARG GLY GLY HIS VAL THR LEU          
SEQRES   3 G  299  ARG CYS HIS TYR ARG HIS ARG PHE ASN ASN PHE MET LEU          
SEQRES   4 G  299  TYR LYS GLU ASP ARG ILE HIS ILE PRO ILE PHE HIS GLY          
SEQRES   5 G  299  ARG ILE PHE GLN GLU SER PHE ASN MET SER PRO VAL THR          
SEQRES   6 G  299  THR ALA HIS ALA GLY ASN TYR THR CYS ARG GLY SER HIS          
SEQRES   7 G  299  PRO HIS SER PRO THR GLY TRP SER ALA PRO SER ASN PRO          
SEQRES   8 G  299  VAL VAL ILE MET VAL THR GLY ASN HIS ARG LYS PRO SER          
SEQRES   9 G  299  LEU LEU ALA HIS PRO GLY PRO LEU VAL LYS SER GLY GLU          
SEQRES  10 G  299  ARG VAL ILE LEU GLN CYS TRP SER ASP ILE MET PHE GLU          
SEQRES  11 G  299  HIS PHE PHE LEU HIS LYS GLU GLY ILE SER LYS ASP PRO          
SEQRES  12 G  299  SER ARG LEU VAL GLY GLN ILE HIS ASP GLY VAL SER LYS          
SEQRES  13 G  299  ALA ASN PHE SER ILE GLY PRO MET MET LEU ALA LEU ALA          
SEQRES  14 G  299  GLY THR TYR ARG CYS TYR GLY SER VAL THR HIS THR SER          
SEQRES  15 G  299  TYR GLN LEU SER ALA PRO SER ASP PRO LEU ASP ILE VAL          
SEQRES  16 G  299  VAL THR GLY PRO TYR GLU LYS PRO SER LEU SER ALA GLN          
SEQRES  17 G  299  PRO GLY PRO LYS VAL GLN ALA GLY GLU SER VAL THR LEU          
SEQRES  18 G  299  SER CYS SER SER ARG SER SER TYR ASP MET TYR HIS LEU          
SEQRES  19 G  299  SER ARG GLU GLY GLY ALA HIS GLU ARG ARG LEU PRO ALA          
SEQRES  20 G  299  VAL ARG LYS VAL ASN ARG THR PHE GLN ALA ASP PHE PRO          
SEQRES  21 G  299  LEU GLY PRO ALA THR HIS GLY GLY THR TYR ARG CYS PHE          
SEQRES  22 G  299  GLY SER PHE ARG HIS SER PRO TYR GLU LEU SER ASP PRO          
SEQRES  23 G  299  SER ASP PRO LEU LEU VAL SER VAL THR GLY ASN PRO SER          
HET    NAG  G 301      14                                                       
HET    NAG  G 302      14                                                       
HET    NAG  G 303      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   5  NAG    3(C8 H15 N O6)                                               
FORMUL   8  HOH   *235(H2 O)                                                    
HELIX    1 AA1 ALA A   49  GLU A   53  5                                   5    
HELIX    2 AA2 GLY A   56  TYR A   85  1                                  30    
HELIX    3 AA3 ASP A  137  ALA A  150  1                                  14    
HELIX    4 AA4 ARG A  151  GLY A  162  1                                  12    
HELIX    5 AA5 GLY A  162  GLY A  175  1                                  14    
HELIX    6 AA6 GLY A  175  GLN A  180  1                                   6    
HELIX    7 AA7 GLU A  253  GLN A  255  5                                   3    
HELIX    8 AA8 PRO G   48  ARG G   53  1                                   6    
HELIX    9 AA9 THR G   65  ALA G   69  5                                   5    
HELIX   10 AB1 MET G  165  ALA G  169  5                                   5    
SHEET    1 AA1 8 ALA A  46  PRO A  47  0                                        
SHEET    2 AA1 8 THR A  31  ASP A  37 -1  N  ARG A  35   O  ALA A  46           
SHEET    3 AA1 8 ARG A  21  VAL A  28 -1  N  VAL A  28   O  THR A  31           
SHEET    4 AA1 8 HIS A   3  MET A  12 -1  N  ARG A   6   O  TYR A  27           
SHEET    5 AA1 8 ILE A  94  VAL A 103 -1  O  ILE A  95   N  ALA A  11           
SHEET    6 AA1 8 LEU A 109  TYR A 118 -1  O  LEU A 110   N  ASP A 102           
SHEET    7 AA1 8 LYS A 121  LEU A 126 -1  O  LEU A 126   N  ASP A 114           
SHEET    8 AA1 8 TRP A 133  ALA A 135 -1  O  THR A 134   N  ALA A 125           
SHEET    1 AA2 4 LYS A 186  PRO A 193  0                                        
SHEET    2 AA2 4 GLU A 198  PHE A 208 -1  O  TRP A 204   N  HIS A 188           
SHEET    3 AA2 4 PHE A 241  PRO A 250 -1  O  ALA A 245   N  CYS A 203           
SHEET    4 AA2 4 THR A 228  LEU A 230 -1  N  GLU A 229   O  ALA A 246           
SHEET    1 AA3 4 LYS A 186  PRO A 193  0                                        
SHEET    2 AA3 4 GLU A 198  PHE A 208 -1  O  TRP A 204   N  HIS A 188           
SHEET    3 AA3 4 PHE A 241  PRO A 250 -1  O  ALA A 245   N  CYS A 203           
SHEET    4 AA3 4 ARG A 234  PRO A 235 -1  N  ARG A 234   O  GLN A 242           
SHEET    1 AA4 4 GLU A 222  ASP A 223  0                                        
SHEET    2 AA4 4 THR A 214  ARG A 219 -1  N  ARG A 219   O  GLU A 222           
SHEET    3 AA4 4 TYR A 257  GLN A 262 -1  O  HIS A 260   N  THR A 216           
SHEET    4 AA4 4 LEU A 270  LEU A 272 -1  O  LEU A 270   N  VAL A 261           
SHEET    1 AA5 4 LYS B   6  SER B  11  0                                        
SHEET    2 AA5 4 ASN B  21  PHE B  30 -1  O  TYR B  26   N  GLN B   8           
SHEET    3 AA5 4 PHE B  62  PHE B  70 -1  O  THR B  68   N  LEU B  23           
SHEET    4 AA5 4 GLU B  50  HIS B  51 -1  N  GLU B  50   O  TYR B  67           
SHEET    1 AA6 4 LYS B   6  SER B  11  0                                        
SHEET    2 AA6 4 ASN B  21  PHE B  30 -1  O  TYR B  26   N  GLN B   8           
SHEET    3 AA6 4 PHE B  62  PHE B  70 -1  O  THR B  68   N  LEU B  23           
SHEET    4 AA6 4 SER B  55  PHE B  56 -1  N  SER B  55   O  TYR B  63           
SHEET    1 AA7 4 GLU B  44  ARG B  45  0                                        
SHEET    2 AA7 4 ILE B  35  LYS B  41 -1  N  LYS B  41   O  GLU B  44           
SHEET    3 AA7 4 TYR B  78  HIS B  84 -1  O  ASN B  83   N  GLU B  36           
SHEET    4 AA7 4 LYS B  91  LYS B  94 -1  O  VAL B  93   N  CYS B  80           
SHEET    1 AA8 3 PHE G   9  TRP G  13  0                                        
SHEET    2 AA8 3 VAL G  24  HIS G  29 -1  O  HIS G  29   N  PHE G   9           
SHEET    3 AA8 3 PHE G  59  MET G  61 -1  O  MET G  61   N  VAL G  24           
SHEET    1 AA9 4 VAL G  17  PRO G  19  0                                        
SHEET    2 AA9 4 VAL G  92  THR G  97  1  O  MET G  95   N  VAL G  18           
SHEET    3 AA9 4 GLY G  70  GLY G  76 -1  N  GLY G  70   O  ILE G  94           
SHEET    4 AA9 4 PHE G  37  TYR G  40 -1  N  MET G  38   O  ARG G  75           
SHEET    1 AB1 4 SER G 104  HIS G 108  0                                        
SHEET    2 AB1 4 VAL G 119  SER G 125 -1  O  TRP G 124   N  SER G 104           
SHEET    3 AB1 4 VAL G 154  ILE G 161 -1  O  PHE G 159   N  LEU G 121           
SHEET    4 AB1 4 GLN G 149  HIS G 151 -1  N  GLN G 149   O  LYS G 156           
SHEET    1 AB2 5 LEU G 112  LYS G 114  0                                        
SHEET    2 AB2 5 LEU G 192  THR G 197  1  O  VAL G 195   N  VAL G 113           
SHEET    3 AB2 5 GLY G 170  SER G 177 -1  N  TYR G 172   O  LEU G 192           
SHEET    4 AB2 5 HIS G 131  LYS G 136 -1  N  HIS G 135   O  ARG G 173           
SHEET    5 AB2 5 SER G 144  VAL G 147 -1  O  LEU G 146   N  PHE G 132           
SHEET    1 AB3 3 LEU G 112  LYS G 114  0                                        
SHEET    2 AB3 3 LEU G 192  THR G 197  1  O  VAL G 195   N  VAL G 113           
SHEET    3 AB3 3 GLU G 282  LEU G 283  1  O  LEU G 283   N  VAL G 196           
SHEET    1 AB4 4 SER G 204  ALA G 207  0                                        
SHEET    2 AB4 4 THR G 220  SER G 225 -1  O  SER G 222   N  SER G 206           
SHEET    3 AB4 4 PHE G 255  PRO G 260 -1  O  PHE G 259   N  LEU G 221           
SHEET    4 AB4 4 VAL G 248  ARG G 249 -1  N  VAL G 248   O  GLN G 256           
SHEET    1 AB5 4 ARG G 243  PRO G 246  0                                        
SHEET    2 AB5 4 MET G 231  ARG G 236 -1  N  LEU G 234   O  ARG G 243           
SHEET    3 AB5 4 GLY G 268  SER G 275 -1  O  PHE G 273   N  HIS G 233           
SHEET    4 AB5 4 LEU G 290  VAL G 292 -1  O  VAL G 292   N  GLY G 268           
SSBOND   1 CYS A  101    CYS A  164                          1555   1555  2.04  
SSBOND   2 CYS A  203    CYS A  259                          1555   1555  2.03  
SSBOND   3 CYS B   25    CYS B   80                          1555   1555  2.03  
SSBOND   4 CYS G   28    CYS G   74                          1555   1555  2.04  
SSBOND   5 CYS G  123    CYS G  174                          1555   1555  2.03  
SSBOND   6 CYS G  223    CYS G  272                          1555   1555  2.04  
LINK         ND2 ASN G  71                 C1  NAG G 301     1555   1555  1.43  
LINK         ND2 ASN G 158                 C1  NAG G 302     1555   1555  1.47  
LINK         ND2 ASN G 252                 C1  NAG G 303     1555   1555  1.45  
CISPEP   1 GLY A    1    SER A    2          0        -0.81                     
CISPEP   2 TYR A  209    PRO A  210          0         5.31                     
CISPEP   3 HIS B   31    PRO B   32          0         0.52                     
CISPEP   4 TRP G   13    PRO G   14          0         0.90                     
CISPEP   5 SER G   62    PRO G   63          0         0.18                     
CISPEP   6 HIS G  108    PRO G  109          0         0.82                     
CISPEP   7 GLY G  162    PRO G  163          0         1.68                     
CISPEP   8 GLY G  198    PRO G  199          0         3.77                     
SITE     1 AC1  1 ASN G  71                                                     
SITE     1 AC2  5 GLU A 275  ILE G 120  ASN G 158  HOH G 406                    
SITE     2 AC2  5 HOH G 441                                                     
SITE     1 AC3  5 LYS G 250  ASN G 252  THR G 254  GLN G 256                    
SITE     2 AC3  5 HOH G 404                                                     
CRYST1   51.557   61.271   66.365  95.20 100.25 108.22 P 1           1          
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      0.019396  0.006383  0.004565        0.00000                         
SCALE2      0.000000  0.017182  0.002724        0.00000                         
SCALE3      0.000000  0.000000  0.015504        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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