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Database: PDB
Entry: 3SE3
LinkDB: 3SE3
Original site: 3SE3 
HEADER    IMMUNE SYSTEM RECEPTOR                  10-JUN-11   3SE3              
TITLE     HUMAN IFNA2-IFNAR TERNARY COMPLEX                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERFERON ALPHA/BETA RECEPTOR 1;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: IFNA2(YNS) (UNP RESIDUES 28-436);                          
COMPND   5 SYNONYM: IFN-R-1, IFN-ALPHA/BETA RECEPTOR 1, CYTOKINE RECEPTOR CLASS-
COMPND   6 II MEMBER 1, CYTOKINE RECEPTOR FAMILY 2 MEMBER 1, CRF2-1, TYPE I     
COMPND   7 INTERFERON RECEPTOR 1;                                               
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: INTERFERON ALPHA 2B;                                       
COMPND  11 CHAIN: B;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES;                                                       
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: INTERFERON ALPHA/BETA RECEPTOR 2;                          
COMPND  16 CHAIN: C;                                                            
COMPND  17 FRAGMENT: UNP RESIDUES 34-232;                                       
COMPND  18 SYNONYM: IFN-R-2, IFN-ALPHA BINDING PROTEIN, IFN-ALPHA/BETA RECEPTOR 
COMPND  19 2, INTERFERON ALPHA BINDING PROTEIN, TYPE I INTERFERON RECEPTOR 2;   
COMPND  20 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: IFNAR1, IFNAR;                                                 
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 MOL_ID: 3;                                                           
SOURCE  15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  16 ORGANISM_COMMON: HUMAN;                                              
SOURCE  17 ORGANISM_TAXID: 9606;                                                
SOURCE  18 GENE: IFNAR2, IFNABR, IFNARB;                                        
SOURCE  19 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 7111                                        
KEYWDS    TYPE I INTERFERON SIGNALING COMPLEX, EXTRACELLULAR SPACE, IMMUNE      
KEYWDS   2 SYSTEM RECEPTOR                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.THOMAS,K.C.GARCIA                                                   
REVDAT   4   29-JUL-20 3SE3    1       COMPND REMARK SEQADV HETNAM              
REVDAT   4 2                   1       LINK   SITE                              
REVDAT   3   21-AUG-13 3SE3    1       COMPND                                   
REVDAT   2   21-MAR-12 3SE3    1       JRNL                                     
REVDAT   1   31-AUG-11 3SE3    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.    4.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 4.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.78                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.010                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 9530                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.251                           
REMARK   3   FREE R VALUE                     : 0.311                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 477                             
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 46.7860 -  5.7667    1.00     3177   168  0.2740 0.3049        
REMARK   3     2  5.7667 -  4.5785    1.00     2969   156  0.2178 0.3145        
REMARK   3     3  4.5785 -  4.0001    1.00     2907   153  0.2344 0.3253        
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              : 162.5                                         
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) : 137.0                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 160.4                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.21000                                             
REMARK   3    B22 (A**2) : -6.21000                                             
REMARK   3    B33 (A**2) : 12.41000                                             
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      :  0.010           4574                                  
REMARK   3   ANGLE     :  1.817           6242                                  
REMARK   3   CHIRALITY :  0.106            728                                  
REMARK   3   PLANARITY :  0.008            794                                  
REMARK   3   DIHEDRAL  : 13.821           1523                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 6:104)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  10.3368 -18.7501 -23.1307              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5594 T22:   1.1710                                     
REMARK   3      T33:   0.3810 T12:   0.1467                                     
REMARK   3      T13:  -0.7365 T23:  -0.2589                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4800 L22:   1.4268                                     
REMARK   3      L33:   0.0720 L12:   0.3832                                     
REMARK   3      L13:  -0.1108 L23:   0.1154                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0487 S12:   0.1815 S13:   0.1508                       
REMARK   3      S21:  -0.0107 S22:  -0.1718 S23:   0.5325                       
REMARK   3      S31:  -0.0706 S32:   0.0040 S33:  -0.0245                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 105:232)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  25.7498 -14.0238  10.6866              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0709 T22:   0.5259                                     
REMARK   3      T33:   1.0010 T12:  -0.1850                                     
REMARK   3      T13:  -0.4720 T23:  -0.2277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6812 L22:   0.2716                                     
REMARK   3      L33:   0.9651 L12:  -0.8219                                     
REMARK   3      L13:  -0.3734 L23:  -0.0520                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5225 S12:  -0.0094 S13:   0.2597                       
REMARK   3      S21:   0.0150 S22:   0.0695 S23:   0.1029                       
REMARK   3      S31:  -0.8310 S32:  -0.0754 S33:   0.2846                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 233:302)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  35.4643 -25.6402  18.2765              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3591 T22:   0.4341                                     
REMARK   3      T33:   0.3561 T12:   0.2099                                     
REMARK   3      T13:  -0.5278 T23:  -0.4524                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3163 L22:   0.4219                                     
REMARK   3      L33:   0.0929 L12:  -0.0416                                     
REMARK   3      L13:   0.0394 L23:  -0.0457                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0668 S12:  -0.2079 S13:   0.1171                       
REMARK   3      S21:  -0.2518 S22:   0.0089 S23:   0.2375                       
REMARK   3      S31:   0.1396 S32:  -0.0798 S33:  -0.1088                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 8:66)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  39.2725 -33.2853 -12.7755              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8369 T22:   0.6554                                     
REMARK   3      T33:   0.6450 T12:  -0.0238                                     
REMARK   3      T13:  -0.2524 T23:   0.0200                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5362 L22:   0.5419                                     
REMARK   3      L33:   0.6758 L12:   0.2810                                     
REMARK   3      L13:  -0.5270 L23:   0.0426                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5855 S12:   0.1680 S13:   0.0002                       
REMARK   3      S21:  -0.2465 S22:  -0.1721 S23:  -0.0582                       
REMARK   3      S31:  -0.2895 S32:  -0.4208 S33:  -0.0285                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 67:156)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.8903 -32.2404  -9.4076              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2907 T22:   0.8594                                     
REMARK   3      T33:   0.8321 T12:  -0.1277                                     
REMARK   3      T13:  -0.0710 T23:  -0.1537                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3585 L22:   0.6658                                     
REMARK   3      L33:   0.4713 L12:  -0.1131                                     
REMARK   3      L13:  -0.3168 L23:  -0.4883                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0899 S12:   0.0842 S13:  -0.9834                       
REMARK   3      S21:   0.2039 S22:  -0.2869 S23:   0.0704                       
REMARK   3      S31:   0.3986 S32:  -0.3399 S33:  -0.0025                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 11:29)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  59.7397 -49.2569 -13.9927              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0555 T22:   1.0641                                     
REMARK   3      T33:   1.0313 T12:   0.0473                                     
REMARK   3      T13:  -0.1176 T23:  -0.1439                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0662 L22:   0.0906                                     
REMARK   3      L33:   0.0030 L12:   0.0687                                     
REMARK   3      L13:   0.0001 L23:   0.0023                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2166 S12:  -0.4312 S13:  -0.8569                       
REMARK   3      S21:  -0.2653 S22:  -0.0172 S23:  -0.4302                       
REMARK   3      S31:   0.7156 S32:   0.7026 S33:  -0.0025                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 30:104)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.8943 -52.2719 -19.4050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3511 T22:   0.9047                                     
REMARK   3      T33:   0.9930 T12:   0.0038                                     
REMARK   3      T13:   0.1395 T23:  -0.3010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2462 L22:   1.2707                                     
REMARK   3      L33:   0.3781 L12:  -0.5841                                     
REMARK   3      L13:  -0.2865 L23:   0.6826                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0272 S12:   0.0228 S13:   0.2422                       
REMARK   3      S21:   0.0976 S22:  -0.5594 S23:  -0.3494                       
REMARK   3      S31:  -0.0843 S32:  -0.3250 S33:  -0.0062                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 105:139)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  74.6321 -32.6660 -14.5360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7513 T22:   0.8706                                     
REMARK   3      T33:   1.0213 T12:  -0.0662                                     
REMARK   3      T13:   0.0329 T23:  -0.1618                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3853 L22:   0.9049                                     
REMARK   3      L33:   0.2111 L12:   0.2498                                     
REMARK   3      L13:   0.3001 L23:   0.0604                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8576 S12:  -0.3498 S13:  -0.8505                       
REMARK   3      S21:   0.6086 S22:  -0.2914 S23:  -1.1370                       
REMARK   3      S31:  -0.1508 S32:  -0.2877 S33:   0.0065                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 140:204)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  76.0711 -28.8018  -6.6267              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1326 T22:   0.4967                                     
REMARK   3      T33:   1.1732 T12:  -0.2504                                     
REMARK   3      T13:   0.0726 T23:   0.0190                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1566 L22:   0.0649                                     
REMARK   3      L33:   1.3977 L12:  -0.0843                                     
REMARK   3      L13:  -1.0007 L23:  -0.0826                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5407 S12:   0.5734 S13:  -0.2287                       
REMARK   3      S21:  -0.1088 S22:   0.5427 S23:  -0.2612                       
REMARK   3      S31:  -0.3651 S32:  -0.6293 S33:   0.0172                       
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 3SE3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000066090.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-JUL-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9537                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 11.00                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.17200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.50                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 1.03000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
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: PDB ENTRY 3SE4, 3S9D                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% (W/V) PEG 3350, 100 MM NA            
REMARK 280  MALONATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 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+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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      133.83333            
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      267.66667            
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      200.75000            
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      334.58333            
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       66.91667            
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      133.83333            
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      267.66667            
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      334.58333            
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      200.75000            
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       66.91667            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     LEU A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     LYS A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     TRP A    22                                                      
REMARK 465     ASN A    23                                                      
REMARK 465     ARG A    24                                                      
REMARK 465     SER A    25                                                      
REMARK 465     ASP A    26                                                      
REMARK 465     GLU A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     VAL A    29                                                      
REMARK 465     GLY A    30                                                      
REMARK 465     ASN A    31                                                      
REMARK 465     HIS A   246                                                      
REMARK 465     LEU A   247                                                      
REMARK 465     ALA A   303                                                      
REMARK 465     PHE A   304                                                      
REMARK 465     LEU A   305                                                      
REMARK 465     LEU A   306                                                      
REMARK 465     PRO A   307                                                      
REMARK 465     PRO A   308                                                      
REMARK 465     VAL A   309                                                      
REMARK 465     PHE A   310                                                      
REMARK 465     ASN A   311                                                      
REMARK 465     ILE A   312                                                      
REMARK 465     ARG A   313                                                      
REMARK 465     SER A   314                                                      
REMARK 465     LEU A   315                                                      
REMARK 465     SER A   316                                                      
REMARK 465     ASP A   317                                                      
REMARK 465     SER A   318                                                      
REMARK 465     PHE A   319                                                      
REMARK 465     HIS A   320                                                      
REMARK 465     ILE A   321                                                      
REMARK 465     TYR A   322                                                      
REMARK 465     ILE A   323                                                      
REMARK 465     GLY A   324                                                      
REMARK 465     ALA A   325                                                      
REMARK 465     PRO A   326                                                      
REMARK 465     LYS A   327                                                      
REMARK 465     GLN A   328                                                      
REMARK 465     SER A   329                                                      
REMARK 465     GLY A   330                                                      
REMARK 465     ASN A   331                                                      
REMARK 465     THR A   332                                                      
REMARK 465     PRO A   333                                                      
REMARK 465     VAL A   334                                                      
REMARK 465     ILE A   335                                                      
REMARK 465     GLN A   336                                                      
REMARK 465     ASP A   337                                                      
REMARK 465     TYR A   338                                                      
REMARK 465     PRO A   339                                                      
REMARK 465     LEU A   340                                                      
REMARK 465     ILE A   341                                                      
REMARK 465     TYR A   342                                                      
REMARK 465     GLU A   343                                                      
REMARK 465     ILE A   344                                                      
REMARK 465     ILE A   345                                                      
REMARK 465     PHE A   346                                                      
REMARK 465     TRP A   347                                                      
REMARK 465     GLU A   348                                                      
REMARK 465     ASN A   349                                                      
REMARK 465     THR A   350                                                      
REMARK 465     SER A   351                                                      
REMARK 465     ASN A   352                                                      
REMARK 465     ALA A   353                                                      
REMARK 465     GLU A   354                                                      
REMARK 465     ARG A   355                                                      
REMARK 465     LYS A   356                                                      
REMARK 465     ILE A   357                                                      
REMARK 465     ILE A   358                                                      
REMARK 465     GLU A   359                                                      
REMARK 465     LYS A   360                                                      
REMARK 465     LYS A   361                                                      
REMARK 465     THR A   362                                                      
REMARK 465     ASP A   363                                                      
REMARK 465     VAL A   364                                                      
REMARK 465     THR A   365                                                      
REMARK 465     VAL A   366                                                      
REMARK 465     PRO A   367                                                      
REMARK 465     ASN A   368                                                      
REMARK 465     LEU A   369                                                      
REMARK 465     LYS A   370                                                      
REMARK 465     PRO A   371                                                      
REMARK 465     LEU A   372                                                      
REMARK 465     THR A   373                                                      
REMARK 465     VAL A   374                                                      
REMARK 465     TYR A   375                                                      
REMARK 465     CYS A   376                                                      
REMARK 465     VAL A   377                                                      
REMARK 465     LYS A   378                                                      
REMARK 465     ALA A   379                                                      
REMARK 465     ARG A   380                                                      
REMARK 465     ALA A   381                                                      
REMARK 465     HIS A   382                                                      
REMARK 465     THR A   383                                                      
REMARK 465     MET A   384                                                      
REMARK 465     ASP A   385                                                      
REMARK 465     GLU A   386                                                      
REMARK 465     LYS A   387                                                      
REMARK 465     LEU A   388                                                      
REMARK 465     ASN A   389                                                      
REMARK 465     LYS A   390                                                      
REMARK 465     SER A   391                                                      
REMARK 465     SER A   392                                                      
REMARK 465     VAL A   393                                                      
REMARK 465     PHE A   394                                                      
REMARK 465     SER A   395                                                      
REMARK 465     ASP A   396                                                      
REMARK 465     ALA A   397                                                      
REMARK 465     VAL A   398                                                      
REMARK 465     CYS A   399                                                      
REMARK 465     GLU A   400                                                      
REMARK 465     LYS A   401                                                      
REMARK 465     THR A   402                                                      
REMARK 465     LYS A   403                                                      
REMARK 465     PRO A   404                                                      
REMARK 465     GLY A   405                                                      
REMARK 465     ASN A   406                                                      
REMARK 465     THR A   407                                                      
REMARK 465     SER A   408                                                      
REMARK 465     LYS A   409                                                      
REMARK 465     MET B     0                                                      
REMARK 465     CYS B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     GLN B     5                                                      
REMARK 465     THR B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     GLY B    44                                                      
REMARK 465     ASN B    45                                                      
REMARK 465     GLN B    46                                                      
REMARK 465     PHE B    47                                                      
REMARK 465     GLN B    48                                                      
REMARK 465     LYS B    49                                                      
REMARK 465     ALA B    50                                                      
REMARK 465     ILE B   100                                                      
REMARK 465     GLN B   101                                                      
REMARK 465     GLY B   102                                                      
REMARK 465     VAL B   103                                                      
REMARK 465     GLY B   104                                                      
REMARK 465     VAL B   105                                                      
REMARK 465     THR B   106                                                      
REMARK 465     GLU B   107                                                      
REMARK 465     THR B   108                                                      
REMARK 465     PRO B   109                                                      
REMARK 465     LEU B   110                                                      
REMARK 465     MET B   111                                                      
REMARK 465     LYS B   112                                                      
REMARK 465     GLU B   113                                                      
REMARK 465     LEU B   157                                                      
REMARK 465     GLN B   158                                                      
REMARK 465     GLU B   159                                                      
REMARK 465     SER B   160                                                      
REMARK 465     LEU B   161                                                      
REMARK 465     ARG B   162                                                      
REMARK 465     SER B   163                                                      
REMARK 465     LYS B   164                                                      
REMARK 465     GLU B   165                                                      
REMARK 465     TYR C     7                                                      
REMARK 465     THR C     8                                                      
REMARK 465     ASP C     9                                                      
REMARK 465     GLU C    10                                                      
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     GLU C   157                                                      
REMARK 465     ILE C   158                                                      
REMARK 465     LYS C   159                                                      
REMARK 465     GLY C   160                                                      
REMARK 465     ASN C   161                                                      
REMARK 465     PRO C   205                                                      
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     GLN A   7    CG   CD   OE1  NE2                                  
REMARK 470     LYS A   8    CG   CD   CE   NZ                                   
REMARK 470     VAL A   9    CG1  CG2                                            
REMARK 470     ARG A  21    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A  32    CG1  CG2                                            
REMARK 470     SER A  35    OG                                                  
REMARK 470     PHE A  36    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A  39    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  40    CG   CD   CE   NZ                                   
REMARK 470     THR A  41    OG1  CG2                                            
REMARK 470     ASP A  44    CG   OD1  OD2                                       
REMARK 470     ASN A  45    CG   OD1  ND2                                       
REMARK 470     ILE A  47    CG1  CG2  CD1                                       
REMARK 470     LYS A  48    CG   CD   CE   NZ                                   
REMARK 470     LEU A  49    CG   CD1  CD2                                       
REMARK 470     SER A  50    OG                                                  
REMARK 470     THR A  56    OG1  CG2                                            
REMARK 470     SER A  57    OG                                                  
REMARK 470     LYS A  59    CG   CD   CE   NZ                                   
REMARK 470     LEU A  65    CG   CD1  CD2                                       
REMARK 470     LYS A  66    CG   CD   CE   NZ                                   
REMARK 470     LEU A  67    CG   CD1  CD2                                       
REMARK 470     VAL A  69    CG1  CG2                                            
REMARK 470     GLU A  71    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  72    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  74    CG   CD   CE   NZ                                   
REMARK 470     ARG A  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  80    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  81    CG   CD   CE   NZ                                   
REMARK 470     GLU A  82    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  83    CG   OD1  ND2                                       
REMARK 470     THR A  84    OG1  CG2                                            
REMARK 470     SER A  85    OG                                                  
REMARK 470     TRP A  87    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A  87    CZ3  CH2                                            
REMARK 470     GLU A  89    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  91    CG   OD1  OD2                                       
REMARK 470     SER A  92    OG                                                  
REMARK 470     PHE A  93    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A  97    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 100    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 112    CG   OD1  OD2                                       
REMARK 470     LYS A 113    CG   CD   CE   NZ                                   
REMARK 470     THR A 123    OG1  CG2                                            
REMARK 470     LYS A 124    CG   CD   CE   NZ                                   
REMARK 470     SER A 135    OG                                                  
REMARK 470     LYS A 144    CG   CD   CE   NZ                                   
REMARK 470     SER A 147    OG                                                  
REMARK 470     SER A 158    OG                                                  
REMARK 470     LYS A 164    CG   CD   CE   NZ                                   
REMARK 470     GLU A 168    CG   CD   OE1  OE2                                  
REMARK 470     THR A 169    OG1  CG2                                            
REMARK 470     LEU A 180    CG   CD1  CD2                                       
REMARK 470     THR A 181    OG1  CG2                                            
REMARK 470     TRP A 183    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 183    CZ3  CH2                                            
REMARK 470     LYS A 184    CG   CD   CE   NZ                                   
REMARK 470     VAL A 187    CG1  CG2                                            
REMARK 470     LYS A 195    CG   CD   CE   NZ                                   
REMARK 470     ASN A 200    CG   OD1  ND2                                       
REMARK 470     GLU A 201    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 202    CG   CD1  CD2                                       
REMARK 470     ILE A 208    CG1  CG2  CD1                                       
REMARK 470     GLN A 213    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 214    CG   OD1  ND2                                       
REMARK 470     GLN A 215    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 216    CG   OD1  ND2                                       
REMARK 470     VAL A 218    CG1  CG2                                            
REMARK 470     LEU A 219    CG   CD1  CD2                                       
REMARK 470     LYS A 220    CG   CD   CE   NZ                                   
REMARK 470     TYR A 223    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN A 227    CG   OD1  ND2                                       
REMARK 470     GLN A 231    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 239    CG   CD1  CD2                                       
REMARK 470     ASN A 242    CG   OD1  ND2                                       
REMARK 470     ASN A 245    CG   OD1  ND2                                       
REMARK 470     LYS A 249    CG   CD   CE   NZ                                   
REMARK 470     LYS A 251    CG   CD   CE   NZ                                   
REMARK 470     LYS A 260    CG   CD   CE   NZ                                   
REMARK 470     GLN A 263    CG   CD   OE1  NE2                                  
REMARK 470     PHE A 266    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A 268    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 269    CG   OD1  ND2                                       
REMARK 470     VAL A 270    CG1  CG2                                            
REMARK 470     LYS A 273    CG   CD   CE   NZ                                   
REMARK 470     SER A 283    OG                                                  
REMARK 470     ASN A 287    CG   OD1  ND2                                       
REMARK 470     THR A 288    OG1  CG2                                            
REMARK 470     LYS A 296    CG   CD   CE   NZ                                   
REMARK 470     PHE A 297    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR A 299    OG1  CG2                                            
REMARK 470     ILE A 301    CG1  CG2  CD1                                       
REMARK 470     GLN A 302    CG   CD   OE1  NE2                                  
REMARK 470     SER B   8    OG                                                  
REMARK 470     LEU B   9    CG   CD1  CD2                                       
REMARK 470     ARG B  12    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  13    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  31    CG   CD   CE   NZ                                   
REMARK 470     GLU B  51    CG   CD   OE1  OE2                                  
REMARK 470     ILE B  53    CG1  CG2  CD1                                       
REMARK 470     ASN B  65    CG   OD1  ND2                                       
REMARK 470     LEU B  81    CG   CD1  CD2                                       
REMARK 470     LYS B  83    CG   CD   CE   NZ                                   
REMARK 470     LEU B 117    CG   CD1  CD2                                       
REMARK 470     ARG B 120    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 134    CG   CD   CE   NZ                                   
REMARK 470     SER C  11    OG                                                  
REMARK 470     PHE C  21    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS C  30    CG   CD   CE   NZ                                   
REMARK 470     ILE C  34    CG1  CG2  CD1                                       
REMARK 470     LYS C  53    CG   CD   CE   NZ                                   
REMARK 470     LYS C  56    CG   CD   CE   NZ                                   
REMARK 470     ASN C  60    CG   OD1  ND2                                       
REMARK 470     ARG C  63    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 113    CG   CD   OE1  OE2                                  
REMARK 470     THR C 118    OG1  CG2                                            
REMARK 470     GLN C 136    CG   CD   OE1  NE2                                  
REMARK 470     ILE C 143    CG1  CG2  CD1                                       
REMARK 470     MET C 162    CG   SD   CE                                        
REMARK 470     LYS C 172    CG   CD   CE   NZ                                   
REMARK 470     HIS C 187    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN C 191    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    VAL A  69   N   -  CA  -  CB  ANGL. DEV. = -14.1 DEGREES          
REMARK 500    GLY A 122   N   -  CA  -  C   ANGL. DEV. = -15.4 DEGREES          
REMARK 500    PRO A 267   C   -  N   -  CA  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    PRO C  36   C   -  N   -  CA  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    GLN C 191   N   -  CA  -  CB  ANGL. DEV. =  11.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  15     -118.96     47.72                                   
REMARK 500    ASP A  44      -67.29   -130.46                                   
REMARK 500    THR A  56      -73.32    -58.58                                   
REMARK 500    GLU A  82     -124.58     63.07                                   
REMARK 500    ASP A 112      -72.61    -45.41                                   
REMARK 500    ASP A 125        8.91     87.00                                   
REMARK 500    ALA A 130     -128.54     50.24                                   
REMARK 500    THR A 181      -71.59    -71.62                                   
REMARK 500    ASN A 214     -122.53     53.65                                   
REMARK 500    PHE A 266      142.69   -176.03                                   
REMARK 500    ASN A 286      -72.52   -118.19                                   
REMARK 500    THR C  37      -61.22   -104.99                                   
REMARK 500    SER C  64       30.04    -84.16                                   
REMARK 500    PHE C  93      162.87    178.55                                   
REMARK 500    THR C 118      -70.23    -49.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3S8W   RELATED DB: PDB                                   
REMARK 900 D2 DOMAIN OF IFNAR2                                                  
REMARK 900 RELATED ID: 3S98   RELATED DB: PDB                                   
REMARK 900 IFNAR1                                                               
REMARK 900 RELATED ID: 3S9D   RELATED DB: PDB                                   
REMARK 900 IFNA2-IFNAR2 BINARY COMPLEX                                          
REMARK 900 RELATED ID: 3SE4   RELATED DB: PDB                                   
REMARK 900 IFNW-IFNAR TERNARY COMPLEX                                           
DBREF  3SE3 A    1   409  UNP    P17181   INAR1_HUMAN     28    436             
DBREF  3SE3 B    0   165  UNP    Q86UP4   Q86UP4_HUMAN     1    166             
DBREF  3SE3 C    7   205  UNP    P48551   INAR2_HUMAN     34    232             
SEQADV 3SE3 ALA A   -4  UNP  P17181              CLONING ARTIFACT               
SEQADV 3SE3 ASP A   -3  UNP  P17181              CLONING ARTIFACT               
SEQADV 3SE3 LEU A   -2  UNP  P17181              CLONING ARTIFACT               
SEQADV 3SE3 GLY A   -1  UNP  P17181              CLONING ARTIFACT               
SEQADV 3SE3 SER A    0  UNP  P17181              CLONING ARTIFACT               
SEQADV 3SE3 TYR B   57  UNP  Q86UP4    HIS    58 ENGINEERED MUTATION            
SEQADV 3SE3 ASN B   58  UNP  Q86UP4    GLU    59 ENGINEERED MUTATION            
SEQADV 3SE3 SER B   61  UNP  Q86UP4    GLN    62 ENGINEERED MUTATION            
SEQRES   1 A  414  ALA ASP LEU GLY SER LYS ASN LEU LYS SER PRO GLN LYS          
SEQRES   2 A  414  VAL GLU VAL ASP ILE ILE ASP ASP ASN PHE ILE LEU ARG          
SEQRES   3 A  414  TRP ASN ARG SER ASP GLU SER VAL GLY ASN VAL THR PHE          
SEQRES   4 A  414  SER PHE ASP TYR GLN LYS THR GLY MET ASP ASN TRP ILE          
SEQRES   5 A  414  LYS LEU SER GLY CYS GLN ASN ILE THR SER THR LYS CYS          
SEQRES   6 A  414  ASN PHE SER SER LEU LYS LEU ASN VAL TYR GLU GLU ILE          
SEQRES   7 A  414  LYS LEU ARG ILE ARG ALA GLU LYS GLU ASN THR SER SER          
SEQRES   8 A  414  TRP TYR GLU VAL ASP SER PHE THR PRO PHE ARG LYS ALA          
SEQRES   9 A  414  GLN ILE GLY PRO PRO GLU VAL HIS LEU GLU ALA GLU ASP          
SEQRES  10 A  414  LYS ALA ILE VAL ILE HIS ILE SER PRO GLY THR LYS ASP          
SEQRES  11 A  414  SER VAL MET TRP ALA LEU ASP GLY LEU SER PHE THR TYR          
SEQRES  12 A  414  SER LEU VAL ILE TRP LYS ASN SER SER GLY VAL GLU GLU          
SEQRES  13 A  414  ARG ILE GLU ASN ILE TYR SER ARG HIS LYS ILE TYR LYS          
SEQRES  14 A  414  LEU SER PRO GLU THR THR TYR CYS LEU LYS VAL LYS ALA          
SEQRES  15 A  414  ALA LEU LEU THR SER TRP LYS ILE GLY VAL TYR SER PRO          
SEQRES  16 A  414  VAL HIS CYS ILE LYS THR THR VAL GLU ASN GLU LEU PRO          
SEQRES  17 A  414  PRO PRO GLU ASN ILE GLU VAL SER VAL GLN ASN GLN ASN          
SEQRES  18 A  414  TYR VAL LEU LYS TRP ASP TYR THR TYR ALA ASN MET THR          
SEQRES  19 A  414  PHE GLN VAL GLN TRP LEU HIS ALA PHE LEU LYS ARG ASN          
SEQRES  20 A  414  PRO GLY ASN HIS LEU TYR LYS TRP LYS GLN ILE PRO ASP          
SEQRES  21 A  414  CYS GLU ASN VAL LYS THR THR GLN CYS VAL PHE PRO GLN          
SEQRES  22 A  414  ASN VAL PHE GLN LYS GLY ILE TYR LEU LEU ARG VAL GLN          
SEQRES  23 A  414  ALA SER ASP GLY ASN ASN THR SER PHE TRP SER GLU GLU          
SEQRES  24 A  414  ILE LYS PHE ASP THR GLU ILE GLN ALA PHE LEU LEU PRO          
SEQRES  25 A  414  PRO VAL PHE ASN ILE ARG SER LEU SER ASP SER PHE HIS          
SEQRES  26 A  414  ILE TYR ILE GLY ALA PRO LYS GLN SER GLY ASN THR PRO          
SEQRES  27 A  414  VAL ILE GLN ASP TYR PRO LEU ILE TYR GLU ILE ILE PHE          
SEQRES  28 A  414  TRP GLU ASN THR SER ASN ALA GLU ARG LYS ILE ILE GLU          
SEQRES  29 A  414  LYS LYS THR ASP VAL THR VAL PRO ASN LEU LYS PRO LEU          
SEQRES  30 A  414  THR VAL TYR CYS VAL LYS ALA ARG ALA HIS THR MET ASP          
SEQRES  31 A  414  GLU LYS LEU ASN LYS SER SER VAL PHE SER ASP ALA VAL          
SEQRES  32 A  414  CYS GLU LYS THR LYS PRO GLY ASN THR SER LYS                  
SEQRES   1 B  166  MET CYS ASP LEU PRO GLN THR HIS SER LEU GLY SER ARG          
SEQRES   2 B  166  ARG THR LEU MET LEU LEU ALA GLN MET ARG ARG ILE SER          
SEQRES   3 B  166  LEU PHE SER CYS LEU LYS ASP ARG HIS ASP PHE GLY PHE          
SEQRES   4 B  166  PRO GLN GLU GLU PHE GLY ASN GLN PHE GLN LYS ALA GLU          
SEQRES   5 B  166  THR ILE PRO VAL LEU TYR ASN MET ILE SER GLN ILE PHE          
SEQRES   6 B  166  ASN LEU PHE SER THR LYS ASP SER SER ALA ALA TRP ASP          
SEQRES   7 B  166  GLU THR LEU LEU ASP LYS PHE TYR THR GLU LEU TYR GLN          
SEQRES   8 B  166  GLN LEU ASN ASP LEU GLU ALA CYS VAL ILE GLN GLY VAL          
SEQRES   9 B  166  GLY VAL THR GLU THR PRO LEU MET LYS GLU ASP SER ILE          
SEQRES  10 B  166  LEU ALA VAL ARG LYS TYR PHE GLN ARG ILE THR LEU TYR          
SEQRES  11 B  166  LEU LYS GLU LYS LYS TYR SER PRO CYS ALA TRP GLU VAL          
SEQRES  12 B  166  VAL ARG ALA GLU ILE MET ARG SER PHE SER LEU SER THR          
SEQRES  13 B  166  ASN LEU GLN GLU SER LEU ARG SER LYS GLU                      
SEQRES   1 C  199  TYR THR ASP GLU SER CYS THR PHE LYS ILE SER LEU ARG          
SEQRES   2 C  199  ASN PHE ARG SER ILE LEU SER TRP GLU LEU LYS ASN HIS          
SEQRES   3 C  199  SER ILE VAL PRO THR HIS TYR THR LEU LEU TYR THR ILE          
SEQRES   4 C  199  MET SER LYS PRO GLU ASP LEU LYS VAL VAL LYS ASN CYS          
SEQRES   5 C  199  ALA ASN THR THR ARG SER PHE CYS ASP LEU THR ASP GLU          
SEQRES   6 C  199  TRP ARG SER THR HIS GLU ALA TYR VAL THR VAL LEU GLU          
SEQRES   7 C  199  GLY PHE SER GLY ASN THR THR LEU PHE SER CYS SER HIS          
SEQRES   8 C  199  ASN PHE TRP LEU ALA ILE ASP MET SER PHE GLU PRO PRO          
SEQRES   9 C  199  GLU PHE GLU ILE VAL GLY PHE THR ASN HIS ILE ASN VAL          
SEQRES  10 C  199  MET VAL LYS PHE PRO SER ILE VAL GLU GLU GLU LEU GLN          
SEQRES  11 C  199  PHE ASP LEU SER LEU VAL ILE GLU GLU GLN SER GLU GLY          
SEQRES  12 C  199  ILE VAL LYS LYS HIS LYS PRO GLU ILE LYS GLY ASN MET          
SEQRES  13 C  199  SER GLY ASN PHE THR TYR ILE ILE ASP LYS LEU ILE PRO          
SEQRES  14 C  199  ASN THR ASN TYR CYS VAL SER VAL TYR LEU GLU HIS SER          
SEQRES  15 C  199  ASP GLU GLN ALA VAL ILE LYS SER PRO LEU LYS CYS THR          
SEQRES  16 C  199  LEU LEU PRO PRO                                              
MODRES 3SE3 ASN A  145  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 410      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   4  NAG    C8 H15 N O6                                                  
HELIX    1   1 THR A   94  LYS A   98  1                                   5    
HELIX    2   2 TRP A  129  PHE A  136  5                                   8    
HELIX    3   3 PHE A  238  ASN A  242  5                                   5    
HELIX    4   4 PRO A  254  GLU A  257  5                                   4    
HELIX    5   5 PRO A  267  PHE A  271  5                                   5    
HELIX    6   6 SER B    8  MET B   21  1                                  14    
HELIX    7   7 LEU B   26  ARG B   33  5                                   8    
HELIX    8   8 PRO B   39  PHE B   43  5                                   5    
HELIX    9   9 THR B   52  PHE B   67  1                                  16    
HELIX   10  10 THR B   69  TRP B   76  1                                   8    
HELIX   11  11 ASP B   77  CYS B   98  1                                  22    
HELIX   12  12 ASP B  114  LYS B  133  1                                  20    
HELIX   13  13 SER B  136  ASN B  156  1                                  21    
HELIX   14  14 LYS C   56  ALA C   59  5                                   4    
HELIX   15  15 LEU C  101  MET C  105  1                                   5    
SHEET    1   A 3 ILE A  19  LEU A  20  0                                        
SHEET    2   A 3 VAL A  11  ILE A  14 -1  N  ASP A  12   O  ILE A  19           
SHEET    3   A 3 ALA A  99  GLN A 100  1  O  GLN A 100   N  ILE A  13           
SHEET    1   B 4 ILE A  47  LYS A  48  0                                        
SHEET    2   B 4 THR A  33  TYR A  38 -1  N  TYR A  38   O  ILE A  47           
SHEET    3   B 4 LEU A  75  LYS A  81 -1  O  GLU A  80   N  THR A  33           
SHEET    4   B 4 THR A  84  VAL A  90 -1  O  SER A  86   N  ALA A  79           
SHEET    1   C 3 GLU A 105  ALA A 110  0                                        
SHEET    2   C 3 ILE A 115  SER A 120 -1  O  SER A 120   N  GLU A 105           
SHEET    3   C 3 ARG A 159  ILE A 162 -1  O  ILE A 162   N  ILE A 115           
SHEET    1   D 4 GLU A 150  ILE A 156  0                                        
SHEET    2   D 4 THR A 137  LYS A 144 -1  N  LEU A 140   O  ILE A 153           
SHEET    3   D 4 THR A 170  ALA A 178 -1  O  CYS A 172   N  TRP A 143           
SHEET    4   D 4 ILE A 185  TYR A 188 -1  O  GLY A 186   N  ALA A 177           
SHEET    1   E 4 GLU A 150  ILE A 156  0                                        
SHEET    2   E 4 THR A 137  LYS A 144 -1  N  LEU A 140   O  ILE A 153           
SHEET    3   E 4 THR A 170  ALA A 178 -1  O  CYS A 172   N  TRP A 143           
SHEET    4   E 4 HIS A 192  LYS A 195 -1  O  HIS A 192   N  LEU A 173           
SHEET    1   F 3 GLU A 209  GLN A 213  0                                        
SHEET    2   F 3 ASN A 216  LYS A 220 -1  O  VAL A 218   N  SER A 211           
SHEET    3   F 3 GLN A 263  PHE A 266 -1  O  PHE A 266   N  TYR A 217           
SHEET    1   G 3 THR A 229  PHE A 230  0                                        
SHEET    2   G 3 GLN A 281  SER A 283 -1  O  SER A 283   N  THR A 229           
SHEET    3   G 3 THR A 288  TRP A 291 -1  O  SER A 289   N  ALA A 282           
SHEET    1   H 4 LYS A 251  GLN A 252  0                                        
SHEET    2   H 4 GLN A 233  HIS A 236 -1  N  TRP A 234   O  LYS A 251           
SHEET    3   H 4 TYR A 276  ARG A 279 -1  O  LEU A 277   N  LEU A 235           
SHEET    4   H 4 ILE A 295  PHE A 297 -1  O  ILE A 295   N  LEU A 278           
SHEET    1   I 3 CYS C  12  LEU C  18  0                                        
SHEET    2   I 3 SER C  23  LEU C  29 -1  O  SER C  26   N  LYS C  15           
SHEET    3   I 3 PHE C  65  ASP C  67 -1  O  CYS C  66   N  LEU C  25           
SHEET    1   J 4 LYS C  53  VAL C  54  0                                        
SHEET    2   J 4 HIS C  38  ILE C  45 -1  N  TYR C  43   O  LYS C  53           
SHEET    3   J 4 ALA C  78  PHE C  86 -1  O  GLU C  84   N  THR C  40           
SHEET    4   J 4 THR C  91  TRP C 100 -1  O  LEU C  92   N  GLY C  85           
SHEET    1   K 3 GLU C 111  GLY C 116  0                                        
SHEET    2   K 3 ILE C 121  LYS C 126 -1  O  ASN C 122   N  VAL C 115           
SHEET    3   K 3 PHE C 166  ILE C 170 -1  O  PHE C 166   N  VAL C 125           
SHEET    1   L 4 ILE C 150  HIS C 154  0                                        
SHEET    2   L 4 SER C 140  SER C 147 -1  N  GLU C 145   O  LYS C 152           
SHEET    3   L 4 TYR C 179  GLU C 186 -1  O  CYS C 180   N  GLN C 146           
SHEET    4   L 4 LYS C 199  THR C 201 -1  O  LYS C 199   N  VAL C 181           
SSBOND   1 CYS A   52    CYS A   60                          1555   1555  2.16  
SSBOND   2 CYS A  172    CYS A  193                          1555   1555  2.04  
SSBOND   3 CYS A  256    CYS A  264                          1555   1555  2.04  
SSBOND   4 CYS B   29    CYS B  138                          1555   1555  2.04  
SSBOND   5 CYS C   12    CYS C   95                          1555   1555  2.06  
SSBOND   6 CYS C   58    CYS C   66                          1555   1555  2.03  
SSBOND   7 CYS C  180    CYS C  200                          1555   1555  2.04  
LINK         ND2 ASN A 145                 C1  NAG A 410     1555   1555  2.08  
CRYST1   93.370   93.370  401.500  90.00  90.00 120.00 P 61 2 2     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010710  0.006183  0.000000        0.00000                         
SCALE2      0.000000  0.012367  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002491        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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