GenomeNet

Database: PDB
Entry: 3S8W
LinkDB: 3S8W
Original site: 3S8W 
HEADER    SIGNALING PROTEIN RECEPTOR              31-MAY-11   3S8W              
TITLE     D2 DOMAIN OF HUMAN IFNAR2                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERFERON ALPHA/BETA RECEPTOR 2;                          
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: UNP RESIDUES 131-232;                                      
COMPND   5 SYNONYM: IFN-R-2, IFN-ALPHA BINDING PROTEIN, IFN-ALPHA/BETA RECEPTOR 
COMPND   6 2, INTERFERON ALPHA BINDING PROTEIN, TYPE I INTERFERON RECEPTOR 2;   
COMPND   7 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: IFNAR2, IFNABR, IFNARB;                                        
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111                                        
KEYWDS    HUMAN, TYPE I INTERFERONS, RECEPTOR CHAIN, IFNAR2, FIBRONECTIN TYPE   
KEYWDS   2 III MODULE, PART OF TYPE I INTERFERON RECEPTOR CHAIN, INTERFERON,    
KEYWDS   3 EXTRACELLULAR SPACE, SIGNALING PROTEIN RECEPTOR                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.THOMAS,K.C.GARCIA                                                   
REVDAT   2   21-MAR-12 3S8W    1       JRNL                                     
REVDAT   1   31-AUG-11 3S8W    0                                                
JRNL        AUTH   C.THOMAS,I.MORAGA,D.LEVIN,P.O.KRUTZIK,Y.PODOPLELOVA,A.TREJO, 
JRNL        AUTH 2 C.LEE,G.YARDEN,S.E.VLECK,J.S.GLENN,G.P.NOLAN,J.PIEHLER,      
JRNL        AUTH 3 G.SCHREIBER,K.C.GARCIA                                       
JRNL        TITL   STRUCTURAL LINKAGE BETWEEN LIGAND DISCRIMINATION AND         
JRNL        TITL 2 RECEPTOR ACTIVATION BY TYPE I INTERFERONS.                   
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 146   621 2011              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   21854986                                                     
JRNL        DOI    10.1016/J.CELL.2011.06.048                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.93                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.430                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 26342                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1329                            
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 19.9252 -  5.3766    1.00     2805   147  0.2498 0.2699        
REMARK   3     2  5.3766 -  4.2815    1.00     2778   147  0.1611 0.2076        
REMARK   3     3  4.2815 -  3.7443    1.00     2769   145  0.1928 0.2300        
REMARK   3     4  3.7443 -  3.4038    1.00     2794   153  0.1996 0.3145        
REMARK   3     5  3.4038 -  3.1609    1.00     2793   145  0.2179 0.3020        
REMARK   3     6  3.1609 -  2.9752    1.00     2783   152  0.2449 0.2590        
REMARK   3     7  2.9752 -  2.8266    0.99     2753   150  0.2657 0.3157        
REMARK   3     8  2.8266 -  2.7039    0.99     2771   143  0.2650 0.2869        
REMARK   3     9  2.7039 -  2.6000    0.99     2769   147  0.3029 0.3817        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 45.30                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.80000                                              
REMARK   3    B22 (A**2) : 8.80000                                              
REMARK   3    B33 (A**2) : -17.59000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  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      :  0.017           2001                                  
REMARK   3   ANGLE     :  1.220           2716                                  
REMARK   3   CHIRALITY :  0.084            324                                  
REMARK   3   PLANARITY :  0.007            342                                  
REMARK   3   DIHEDRAL  : 17.257            735                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: all                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  25.2747 -26.4021   0.5411              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1170 T22:   0.1367                                     
REMARK   3      T33:   0.1371 T12:  -0.0234                                     
REMARK   3      T13:   0.0032 T23:  -0.0365                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7434 L22:   0.2268                                     
REMARK   3      L33:   1.0209 L12:   0.3010                                     
REMARK   3      L13:  -0.6159 L23:  -0.0223                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0554 S12:   0.0162 S13:   0.0050                       
REMARK   3      S21:   0.0430 S22:   0.0463 S23:  -0.0223                       
REMARK   3      S31:  -0.0029 S32:  -0.0412 S33:  -0.0014                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ANOMALOUS SCATTERER GROUP USED FOR ATOM   
REMARK   3  SE WITH FP = -3.6227 AND FDP = 5.4465                               
REMARK   4                                                                      
REMARK   4 3S8W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB065908.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26344                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.925                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 9.00000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 66.40000                           
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: AUTOSHARP                                             
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 31% (W/V) PEG 4000, 200 MM LI2SO4, 100   
REMARK 280  MM TRIS PH 8.5, 5% (V/V) MPD, 10 MM NA ACETATE, 1.5% (W/V)          
REMARK 280  PEG8000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K            
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      150.22000            
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       75.11000            
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      112.66500            
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       37.55500            
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      187.77500            
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      150.22000            
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       75.11000            
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       37.55500            
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      112.66500            
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      187.77500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: MONOMERIC                         
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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     ALA A   101                                                      
REMARK 465     ASP A   102                                                      
REMARK 465     PRO A   103                                                      
REMARK 465     ASP A   104                                                      
REMARK 465     MSE A   105                                                      
REMARK 465     PRO A   128                                                      
REMARK 465     SER A   129                                                      
REMARK 465     ILE A   130                                                      
REMARK 465     VAL A   131                                                      
REMARK 465     GLU A   132                                                      
REMARK 465     GLU A   133                                                      
REMARK 465     GLU A   134                                                      
REMARK 465     LEU A   135                                                      
REMARK 465     GLN A   136                                                      
REMARK 465     PHE A   137                                                      
REMARK 465     ASP A   138                                                      
REMARK 465     LEU A   139                                                      
REMARK 465     LYS A   159                                                      
REMARK 465     GLY A   160                                                      
REMARK 465     ASN A   161                                                      
REMARK 465     MSE A   162                                                      
REMARK 465     SER A   163                                                      
REMARK 465     GLY A   164                                                      
REMARK 465     SER A   188                                                      
REMARK 465     ASP A   189                                                      
REMARK 465     GLU A   190                                                      
REMARK 465     GLN A   191                                                      
REMARK 465     ALA A   192                                                      
REMARK 465     ALA B   101                                                      
REMARK 465     ASP B   102                                                      
REMARK 465     PRO B   103                                                      
REMARK 465     ASP B   104                                                      
REMARK 465     MSE B   105                                                      
REMARK 465     SER B   106                                                      
REMARK 465     PRO B   128                                                      
REMARK 465     SER B   129                                                      
REMARK 465     ILE B   130                                                      
REMARK 465     VAL B   131                                                      
REMARK 465     GLU B   132                                                      
REMARK 465     GLU B   133                                                      
REMARK 465     GLU B   134                                                      
REMARK 465     LEU B   135                                                      
REMARK 465     GLN B   136                                                      
REMARK 465     PHE B   137                                                      
REMARK 465     ASP B   138                                                      
REMARK 465     LYS B   159                                                      
REMARK 465     GLY B   160                                                      
REMARK 465     ASN B   161                                                      
REMARK 465     MSE B   162                                                      
REMARK 465     SER B   163                                                      
REMARK 465     GLY B   164                                                      
REMARK 465     GLU B   190                                                      
REMARK 465     ALA C   101                                                      
REMARK 465     ASP C   102                                                      
REMARK 465     PRO C   103                                                      
REMARK 465     ASP C   104                                                      
REMARK 465     MSE C   105                                                      
REMARK 465     SER C   129                                                      
REMARK 465     ILE C   130                                                      
REMARK 465     VAL C   131                                                      
REMARK 465     GLU C   132                                                      
REMARK 465     GLU C   133                                                      
REMARK 465     GLU C   134                                                      
REMARK 465     LEU C   135                                                      
REMARK 465     GLN C   136                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 126    CG   CD   CE   NZ                                   
REMARK 470     PHE A 127    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER A 140    OG                                                  
REMARK 470     ILE A 158    CG1  CG2  CD1                                       
REMARK 470     HIS A 187    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 126    CG   CD   CE   NZ                                   
REMARK 470     LEU B 139    CG   CD1  CD2                                       
REMARK 470     GLU B 157    CG   CD   OE1  OE2                                  
REMARK 470     HIS B 187    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER B 188    OG                                                  
REMARK 470     ASP B 189    CG   OD1  OD2                                       
REMARK 470     GLN B 191    CG   CD   OE1  NE2                                  
REMARK 470     SER C 106    OG                                                  
REMARK 470     GLU C 113    CG   CD   OE1  OE2                                  
REMARK 470     PHE C 137    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP C 138    CG   OD1  OD2                                       
REMARK 470     GLU C 148    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 172    CG   CD   CE   NZ                                   
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    GLU A 157       99.95    -68.02                                   
REMARK 500    ASN A 176       36.44     73.54                                   
REMARK 500    ASP C 171     -169.74   -114.35                                   
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 RESIDUE CL A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3S98   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3S9D   RELATED DB: PDB                                   
DBREF  3S8W A  104   205  UNP    P48551   INAR2_HUMAN    131    232             
DBREF  3S8W B  104   205  UNP    P48551   INAR2_HUMAN    131    232             
DBREF  3S8W C  104   205  UNP    P48551   INAR2_HUMAN    131    232             
SEQADV 3S8W ALA A  101  UNP  P48551              CLONING ARTIFACT               
SEQADV 3S8W ASP A  102  UNP  P48551              CLONING ARTIFACT               
SEQADV 3S8W PRO A  103  UNP  P48551              CLONING ARTIFACT               
SEQADV 3S8W ALA B  101  UNP  P48551              CLONING ARTIFACT               
SEQADV 3S8W ASP B  102  UNP  P48551              CLONING ARTIFACT               
SEQADV 3S8W PRO B  103  UNP  P48551              CLONING ARTIFACT               
SEQADV 3S8W ALA C  101  UNP  P48551              CLONING ARTIFACT               
SEQADV 3S8W ASP C  102  UNP  P48551              CLONING ARTIFACT               
SEQADV 3S8W PRO C  103  UNP  P48551              CLONING ARTIFACT               
SEQRES   1 A  105  ALA ASP PRO ASP MSE SER PHE GLU PRO PRO GLU PHE GLU          
SEQRES   2 A  105  ILE VAL GLY PHE THR ASN HIS ILE ASN VAL MSE VAL LYS          
SEQRES   3 A  105  PHE PRO SER ILE VAL GLU GLU GLU LEU GLN PHE ASP LEU          
SEQRES   4 A  105  SER LEU VAL ILE GLU GLU GLN SER GLU GLY ILE VAL LYS          
SEQRES   5 A  105  LYS HIS LYS PRO GLU ILE LYS GLY ASN MSE SER GLY ASN          
SEQRES   6 A  105  PHE THR TYR ILE ILE ASP LYS LEU ILE PRO ASN THR ASN          
SEQRES   7 A  105  TYR CYS VAL SER VAL TYR LEU GLU HIS SER ASP GLU GLN          
SEQRES   8 A  105  ALA VAL ILE LYS SER PRO LEU LYS CYS THR LEU LEU PRO          
SEQRES   9 A  105  PRO                                                          
SEQRES   1 B  105  ALA ASP PRO ASP MSE SER PHE GLU PRO PRO GLU PHE GLU          
SEQRES   2 B  105  ILE VAL GLY PHE THR ASN HIS ILE ASN VAL MSE VAL LYS          
SEQRES   3 B  105  PHE PRO SER ILE VAL GLU GLU GLU LEU GLN PHE ASP LEU          
SEQRES   4 B  105  SER LEU VAL ILE GLU GLU GLN SER GLU GLY ILE VAL LYS          
SEQRES   5 B  105  LYS HIS LYS PRO GLU ILE LYS GLY ASN MSE SER GLY ASN          
SEQRES   6 B  105  PHE THR TYR ILE ILE ASP LYS LEU ILE PRO ASN THR ASN          
SEQRES   7 B  105  TYR CYS VAL SER VAL TYR LEU GLU HIS SER ASP GLU GLN          
SEQRES   8 B  105  ALA VAL ILE LYS SER PRO LEU LYS CYS THR LEU LEU PRO          
SEQRES   9 B  105  PRO                                                          
SEQRES   1 C  105  ALA ASP PRO ASP MSE SER PHE GLU PRO PRO GLU PHE GLU          
SEQRES   2 C  105  ILE VAL GLY PHE THR ASN HIS ILE ASN VAL MSE VAL LYS          
SEQRES   3 C  105  PHE PRO SER ILE VAL GLU GLU GLU LEU GLN PHE ASP LEU          
SEQRES   4 C  105  SER LEU VAL ILE GLU GLU GLN SER GLU GLY ILE VAL LYS          
SEQRES   5 C  105  LYS HIS LYS PRO GLU ILE LYS GLY ASN MSE SER GLY ASN          
SEQRES   6 C  105  PHE THR TYR ILE ILE ASP LYS LEU ILE PRO ASN THR ASN          
SEQRES   7 C  105  TYR CYS VAL SER VAL TYR LEU GLU HIS SER ASP GLU GLN          
SEQRES   8 C  105  ALA VAL ILE LYS SER PRO LEU LYS CYS THR LEU LEU PRO          
SEQRES   9 C  105  PRO                                                          
MODRES 3S8W MSE A  124  MET  SELENOMETHIONINE                                   
MODRES 3S8W MSE B  124  MET  SELENOMETHIONINE                                   
MODRES 3S8W MSE C  124  MET  SELENOMETHIONINE                                   
MODRES 3S8W MSE C  162  MET  SELENOMETHIONINE                                   
HET    MSE  A 124      13                                                       
HET    MSE  B 124       8                                                       
HET    MSE  C 124       8                                                       
HET    MSE  C 162       8                                                       
HET     CL  A   1       1                                                       
HET     CL  C   1       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CL CHLORIDE ION                                                     
FORMUL   1  MSE    4(C5 H11 N O2 SE)                                            
FORMUL   4   CL    2(CL 1-)                                                     
FORMUL   6  HOH   *35(H2 O)                                                     
SHEET    1   A 4 GLU A 111  GLY A 116  0                                        
SHEET    2   A 4 ILE A 121  LYS A 126 -1  O  MSE A 124   N  GLU A 113           
SHEET    3   A 4 PHE A 166  ILE A 170 -1  O  TYR A 168   N  VAL A 123           
SHEET    4   A 4 GLU C 157  ILE C 158  1  O  GLU C 157   N  ILE A 169           
SHEET    1   B 8 VAL A 151  HIS A 154  0                                        
SHEET    2   B 8 LEU A 141  GLN A 146 -1  N  GLU A 145   O  LYS A 152           
SHEET    3   B 8 ASN A 178  LEU A 185 -1  O  TYR A 184   N  VAL A 142           
SHEET    4   B 8 LYS A 199  LEU A 202 -1  O  LYS A 199   N  VAL A 181           
SHEET    5   B 8 LEU B 198  LEU B 202  1  O  CYS B 200   N  CYS A 200           
SHEET    6   B 8 ASN B 178  GLU B 186 -1  N  TYR B 179   O  THR B 201           
SHEET    7   B 8 SER B 140  SER B 147 -1  N  GLU B 144   O  SER B 182           
SHEET    8   B 8 ILE B 150  HIS B 154 -1  O  HIS B 154   N  ILE B 143           
SHEET    1   C 3 GLU B 111  GLY B 116  0                                        
SHEET    2   C 3 ILE B 121  LYS B 126 -1  O  LYS B 126   N  GLU B 111           
SHEET    3   C 3 PHE B 166  ILE B 170 -1  O  PHE B 166   N  VAL B 125           
SHEET    1   D 3 GLU C 111  GLY C 116  0                                        
SHEET    2   D 3 ILE C 121  PHE C 127 -1  O  MSE C 124   N  GLU C 113           
SHEET    3   D 3 GLY C 164  ILE C 170 -1  O  ILE C 170   N  ILE C 121           
SHEET    1   E 4 ILE C 150  HIS C 154  0                                        
SHEET    2   E 4 SER C 140  SER C 147 -1  N  GLU C 145   O  LYS C 152           
SHEET    3   E 4 ASN C 178  GLU C 186 -1  O  SER C 182   N  GLU C 144           
SHEET    4   E 4 LYS C 199  LEU C 202 -1  O  LYS C 199   N  VAL C 181           
SSBOND   1 CYS A  180    CYS A  200                          1555   1555  2.09  
SSBOND   2 CYS B  180    CYS B  200                          1555   1555  2.08  
SSBOND   3 CYS C  180    CYS C  200                          1555   1555  2.06  
LINK         C   VAL A 123                 N   MSE A 124     1555   1555  1.33  
LINK         C   MSE A 124                 N   VAL A 125     1555   1555  1.34  
LINK         C   VAL B 123                 N   MSE B 124     1555   1555  1.34  
LINK         C   MSE B 124                 N   VAL B 125     1555   1555  1.33  
LINK         C   VAL C 123                 N   MSE C 124     1555   1555  1.33  
LINK         C   MSE C 124                 N   VAL C 125     1555   1555  1.33  
LINK         C   ASN C 161                 N   MSE C 162     1555   1555  1.33  
LINK         C   MSE C 162                 N   SER C 163     1555   1555  1.33  
SITE     1 AC1  1 LYS A 172                                                     
SITE     1 AC2  1 THR A 167                                                     
CRYST1   82.660   82.660  225.330  90.00  90.00 120.00 P 65 2 2     36          
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      0.012098  0.006985  0.000000        0.00000                         
SCALE2      0.000000  0.013969  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004438        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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