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Database: PDB
Entry: 5UWC
LinkDB: 5UWC
Original site: 5UWC 
HEADER    SIGNALING PROTEIN                       21-FEB-17   5UWC              
TITLE     CYTOKINE-RECEPTOR COMPLEX                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-3 RECEPTOR SUBUNIT ALPHA;                      
COMPND   3 CHAIN: G;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 20-307;                                       
COMPND   5 SYNONYM: IL-3RA;                                                     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTERLEUKIN-3;                                             
COMPND  10 CHAIN: I;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 31-152;                                       
COMPND  12 SYNONYM: IL-3,HEMATOPOIETIC GROWTH FACTOR,MAST CELL GROWTH FACTOR,   
COMPND  13 MCGF,MULTIPOTENTIAL COLONY-STIMULATING FACTOR,P-CELL-STIMULATING     
COMPND  14 FACTOR;                                                              
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: IL3RA, IL3R;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: IL3;                                                           
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CYTOKINE, RECEPTOR, SIGNALLING, SIGNALING PROTEIN                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.E.BROUGHTON,M.W.PARKER                                              
REVDAT   3   04-OCT-23 5UWC    1       HETSYN LINK                              
REVDAT   2   29-JUL-20 5UWC    1       COMPND REMARK HETNAM LINK                
REVDAT   2 2                   1       SITE   ATOM                              
REVDAT   1   07-FEB-18 5UWC    0                                                
JRNL        AUTH   S.E.BROUGHTON,T.R.HERCUS,T.L.NERO,W.L.KAN,E.F.BARRY,         
JRNL        AUTH 2 M.DOTTORE,K.S.CHEUNG TUNG SHING,C.J.MORTON,U.DHAGAT,         
JRNL        AUTH 3 M.P.HARDY,N.J.WILSON,M.T.DOWNTON,C.SCHIEBER,T.P.HUGHES,      
JRNL        AUTH 4 A.F.LOPEZ,M.W.PARKER                                         
JRNL        TITL   A DUAL ROLE FOR THE N-TERMINAL DOMAIN OF THE IL-3 RECEPTOR   
JRNL        TITL 2 IN CELL SIGNALLING.                                          
JRNL        REF    NAT COMMUN                    V.   9   386 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   29374162                                                     
JRNL        DOI    10.1038/S41467-017-02633-7                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 92.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 23081                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1242                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1650                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.60                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 84                           
REMARK   3   BIN FREE R VALUE                    : 0.3380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2958                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 103                                     
REMARK   3   SOLVENT ATOMS            : 64                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.48000                                              
REMARK   3    B22 (A**2) : 0.48000                                              
REMARK   3    B33 (A**2) : -1.57000                                             
REMARK   3    B12 (A**2) : 0.24000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.286         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.217         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.173         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.867        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3126 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2905 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4241 ; 1.550 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6669 ; 0.995 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   362 ; 6.456 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   153 ;36.569 ;23.660       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   515 ;16.522 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;16.414 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   465 ; 0.103 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3502 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   763 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1460 ; 1.736 ; 5.727       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1459 ; 1.737 ; 5.724       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1818 ; 3.115 ; 8.570       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1819 ; 3.114 ; 8.574       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1666 ; 1.632 ; 6.013       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1664 ; 1.631 ; 6.014       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2423 ; 2.887 ; 8.941       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3295 ; 5.854 ;44.871       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3296 ; 5.853 ;44.874       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G    27        G   293                          
REMARK   3    ORIGIN FOR THE GROUP (A):  87.4046  55.1976   6.4162              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0294 T22:   0.0794                                     
REMARK   3      T33:   0.0231 T12:   0.0191                                     
REMARK   3      T13:   0.0035 T23:   0.0295                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9228 L22:   1.1998                                     
REMARK   3      L33:   1.1252 L12:   0.8075                                     
REMARK   3      L13:   0.2993 L23:   0.6958                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0832 S12:  -0.0288 S13:  -0.1037                       
REMARK   3      S21:   0.0382 S22:  -0.0828 S23:  -0.1335                       
REMARK   3      S31:   0.0844 S32:   0.1376 S33:  -0.0004                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5UWC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000226546.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-FEB-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6-5                              
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.954                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23081                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 92.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 16.10                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.39                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4JZJ, 1JLI                                           
REMARK 200                                                                      
REMARK 200 REMARK: TETRAGONAL                                                   
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 200 MM NACL AND 100 MM     
REMARK 280  CITRATE-PHOSPHATE BUFFER PH 4.8, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
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                                                                      
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       32.03867            
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       64.07733            
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       48.05800            
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       80.09667            
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       16.01933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, I, 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 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     LYS G    20                                                      
REMARK 465     GLU G    21                                                      
REMARK 465     ASP G    22                                                      
REMARK 465     PRO G    23                                                      
REMARK 465     ASN G    24                                                      
REMARK 465     PRO G    25                                                      
REMARK 465     PRO G    26                                                      
REMARK 465     ASP G    42                                                      
REMARK 465     LEU G    43                                                      
REMARK 465     ASN G    44                                                      
REMARK 465     ARG G    45                                                      
REMARK 465     ASN G    46                                                      
REMARK 465     VAL G    47                                                      
REMARK 465     THR G    48                                                      
REMARK 465     ASP G    49                                                      
REMARK 465     ILE G    50                                                      
REMARK 465     ALA G    86                                                      
REMARK 465     ASN G    87                                                      
REMARK 465     PRO G    88                                                      
REMARK 465     PRO G    89                                                      
REMARK 465     PHE G    90                                                      
REMARK 465     ASP G   294                                                      
REMARK 465     GLN G   295                                                      
REMARK 465     GLU G   296                                                      
REMARK 465     GLU G   297                                                      
REMARK 465     GLY G   298                                                      
REMARK 465     VAL G   299                                                      
REMARK 465     ASN G   300                                                      
REMARK 465     THR G   301                                                      
REMARK 465     ARG G   302                                                      
REMARK 465     ALA G   303                                                      
REMARK 465     TRP G   304                                                      
REMARK 465     ARG G   305                                                      
REMARK 465     THR G   306                                                      
REMARK 465     SER G   307                                                      
REMARK 465     GLN I   124                                                      
REMARK 465     GLN I   125                                                      
REMARK 465     THR I   126                                                      
REMARK 465     THR I   127                                                      
REMARK 465     LEU I   128                                                      
REMARK 465     SER I   129                                                      
REMARK 465     LEU I   130                                                      
REMARK 465     ALA I   131                                                      
REMARK 465     ILE I   132                                                      
REMARK 465     PHE I   133                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CZ3  TRP G    41     CG2  VAL G    83              1.73            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CD1  LEU I    32     CB   ASN I    80     3774     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN G  29       51.33   -112.96                                   
REMARK 500    ARG G  31      143.19   -173.30                                   
REMARK 500    THR G  40     -161.27   -111.19                                   
REMARK 500    SER G  66      -32.07   -136.47                                   
REMARK 500    ALA G  72       45.83   -148.09                                   
REMARK 500    SER G 100      -58.86   -135.92                                   
REMARK 500    VAL G 117      -54.72     71.49                                   
REMARK 500    ARG G 146       71.79   -118.12                                   
REMARK 500    ASN G 218      155.75    178.54                                   
REMARK 500    ASP G 256       71.23     28.16                                   
REMARK 500    ARG G 257      132.54   -171.35                                   
REMARK 500    LYS I  28       43.97   -100.56                                   
REMARK 500    LEU I  32     -115.68     61.06                                   
REMARK 500    ASN I  39       39.11    -94.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG A    1                                                       
REMARK 610     NAG G  401                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5UV8   RELATED DB: PDB                                   
DBREF  5UWC G   20   307  UNP    P26951   IL3RA_HUMAN     20    307             
DBREF  5UWC I   12   133  UNP    P08700   IL3_HUMAN       31    152             
SEQADV 5UWC GLN G  212  UNP  P26951    ASN   212 ENGINEERED MUTATION            
SEQADV 5UWC VAL G  299  UNP  P26951    ALA   299 ENGINEERED MUTATION            
SEQADV 5UWC TYR I   13  UNP  P08700    TRP    32 ENGINEERED MUTATION            
SEQADV 5UWC TRP I  116  UNP  P08700    LYS   135 ENGINEERED MUTATION            
SEQRES   1 G  288  LYS GLU ASP PRO ASN PRO PRO ILE THR ASN LEU ARG MET          
SEQRES   2 G  288  LYS ALA LYS ALA GLN GLN LEU THR TRP ASP LEU ASN ARG          
SEQRES   3 G  288  ASN VAL THR ASP ILE GLU CYS VAL LYS ASP ALA ASP TYR          
SEQRES   4 G  288  SER MET PRO ALA VAL ASN ASN SER TYR CYS GLN PHE GLY          
SEQRES   5 G  288  ALA ILE SER LEU CYS GLU VAL THR ASN TYR THR VAL ARG          
SEQRES   6 G  288  VAL ALA ASN PRO PRO PHE SER THR TRP ILE LEU PHE PRO          
SEQRES   7 G  288  GLU ASN SER GLY LYS PRO TRP ALA GLY ALA GLU ASN LEU          
SEQRES   8 G  288  THR CYS TRP ILE HIS ASP VAL ASP PHE LEU SER CYS SER          
SEQRES   9 G  288  TRP ALA VAL GLY PRO GLY ALA PRO ALA ASP VAL GLN TYR          
SEQRES  10 G  288  ASP LEU TYR LEU ASN VAL ALA ASN ARG ARG GLN GLN TYR          
SEQRES  11 G  288  GLU CYS LEU HIS TYR LYS THR ASP ALA GLN GLY THR ARG          
SEQRES  12 G  288  ILE GLY CYS ARG PHE ASP ASP ILE SER ARG LEU SER SER          
SEQRES  13 G  288  GLY SER GLN SER SER HIS ILE LEU VAL ARG GLY ARG SER          
SEQRES  14 G  288  ALA ALA PHE GLY ILE PRO CYS THR ASP LYS PHE VAL VAL          
SEQRES  15 G  288  PHE SER GLN ILE GLU ILE LEU THR PRO PRO GLN MET THR          
SEQRES  16 G  288  ALA LYS CYS ASN LYS THR HIS SER PHE MET HIS TRP LYS          
SEQRES  17 G  288  MET ARG SER HIS PHE ASN ARG LYS PHE ARG TYR GLU LEU          
SEQRES  18 G  288  GLN ILE GLN LYS ARG MET GLN PRO VAL ILE THR GLU GLN          
SEQRES  19 G  288  VAL ARG ASP ARG THR SER PHE GLN LEU LEU ASN PRO GLY          
SEQRES  20 G  288  THR TYR THR VAL GLN ILE ARG ALA ARG GLU ARG VAL TYR          
SEQRES  21 G  288  GLU PHE LEU SER ALA TRP SER THR PRO GLN ARG PHE GLU          
SEQRES  22 G  288  CYS ASP GLN GLU GLU GLY VAL ASN THR ARG ALA TRP ARG          
SEQRES  23 G  288  THR SER                                                      
SEQRES   1 I  122  SER TYR VAL ASN CYS SER ASN MET ILE ASP GLU ILE ILE          
SEQRES   2 I  122  THR HIS LEU LYS GLN PRO PRO LEU PRO LEU LEU ASP PHE          
SEQRES   3 I  122  ASN ASN LEU ASN GLY GLU ASP GLN ASP ILE LEU MET GLU          
SEQRES   4 I  122  ASN ASN LEU ARG ARG PRO ASN LEU GLU ALA PHE ASN ARG          
SEQRES   5 I  122  ALA VAL LYS SER LEU GLN ASN ALA SER ALA ILE GLU SER          
SEQRES   6 I  122  ILE LEU LYS ASN LEU LEU PRO CYS LEU PRO LEU ALA THR          
SEQRES   7 I  122  ALA ALA PRO THR ARG HIS PRO ILE HIS ILE LYS ASP GLY          
SEQRES   8 I  122  ASP TRP ASN GLU PHE ARG ARG LYS LEU THR PHE TYR LEU          
SEQRES   9 I  122  TRP THR LEU GLU ASN ALA GLN ALA GLN GLN THR THR LEU          
SEQRES  10 I  122  SER LEU ALA ILE PHE                                          
HET    NAG  A   1      14                                                       
HET    NAG  A   2      14                                                       
HET    FUL  A   3      10                                                       
HET    NAG  G 401      14                                                       
HET    CIT  G 402      13                                                       
HET    IMD  G 406       5                                                       
HET    EDT  G 407      20                                                       
HET    CIT  I 201      13                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     FUL BETA-L-FUCOPYRANOSE                                              
HETNAM     CIT CITRIC ACID                                                      
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     EDT {[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-               
HETNAM   2 EDT  AMINO}-ACETIC ACID                                              
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     FUL BETA-L-FUCOSE; 6-DEOXY-BETA-L-GALACTOPYRANOSE; L-                
HETSYN   2 FUL  FUCOSE; FUCOSE; 6-DEOXY-BETA-L-GALACTOSE                        
FORMUL   3  NAG    3(C8 H15 N O6)                                               
FORMUL   3  FUL    C6 H12 O5                                                    
FORMUL   5  CIT    2(C6 H8 O7)                                                  
FORMUL   6  IMD    C3 H5 N2 1+                                                  
FORMUL   7  EDT    C10 H16 N2 O8                                                
FORMUL   9  HOH   *64(H2 O)                                                     
HELIX    1 AA1 ASP G  169  SER G  175  1                                   7    
HELIX    2 AA2 SER G  203  ILE G  205  5                                   3    
HELIX    3 AA3 ASN I   15  LYS I   28  1                                  14    
HELIX    4 AA4 ASP I   36  LEU I   40  5                                   5    
HELIX    5 AA5 ASN I   41  GLU I   50  1                                  10    
HELIX    6 AA6 LEU I   53  LYS I   66  1                                  14    
HELIX    7 AA7 ALA I   71  LYS I   79  1                                   9    
HELIX    8 AA8 ASN I   80  LEU I   85  5                                   6    
HELIX    9 AA9 ASP I  103  GLN I  122  1                                  20    
SHEET    1 AA1 3 MET G  32  LYS G  33  0                                        
SHEET    2 AA1 3 GLN G  38  LEU G  39 -1  O  GLN G  38   N  LYS G  33           
SHEET    3 AA1 3 CYS G  68  GLN G  69 -1  O  CYS G  68   N  LEU G  39           
SHEET    1 AA2 4 TYR G  58  MET G  60  0                                        
SHEET    2 AA2 4 CYS G  52  LYS G  54 -1  N  CYS G  52   O  MET G  60           
SHEET    3 AA2 4 THR G  79  VAL G  83 -1  O  THR G  82   N  VAL G  53           
SHEET    4 AA2 4 THR G  92  PHE G  96 -1  O  ILE G  94   N  TYR G  81           
SHEET    1 AA3 4 GLU G 108  HIS G 115  0                                        
SHEET    2 AA3 4 PHE G 119  ALA G 125 -1  O  ALA G 125   N  GLU G 108           
SHEET    3 AA3 4 ARG G 162  PHE G 167 -1  O  CYS G 165   N  CYS G 122           
SHEET    4 AA3 4 HIS G 153  THR G 156 -1  N  LYS G 155   O  GLY G 164           
SHEET    1 AA4 4 GLN G 148  GLU G 150  0                                        
SHEET    2 AA4 4 GLN G 135  VAL G 142 -1  N  LEU G 140   O  TYR G 149           
SHEET    3 AA4 4 SER G 179  ARG G 187 -1  O  HIS G 181   N  ASN G 141           
SHEET    4 AA4 4 THR G 196  VAL G 201 -1  O  THR G 196   N  VAL G 184           
SHEET    1 AA5 3 GLN G 212  LYS G 216  0                                        
SHEET    2 AA5 3 HIS G 221  LYS G 227 -1  O  HIS G 225   N  THR G 214           
SHEET    3 AA5 3 SER G 259  LEU G 263 -1  O  LEU G 262   N  SER G 222           
SHEET    1 AA6 4 ILE G 250  ARG G 255  0                                        
SHEET    2 AA6 4 PHE G 236  GLN G 243 -1  N  ILE G 242   O  ILE G 250           
SHEET    3 AA6 4 THR G 267  GLU G 276 -1  O  ARG G 275   N  ARG G 237           
SHEET    4 AA6 4 GLN G 289  GLU G 292 -1  O  PHE G 291   N  TYR G 268           
SSBOND   1 CYS G   52    CYS G   68                          1555   1555  2.98  
SSBOND   2 CYS G   76    CYS G  195                          1555   1555  2.89  
SSBOND   3 CYS G  112    CYS G  122                          1555   1555  2.87  
SSBOND   4 CYS G  151    CYS G  165                          1555   1555  2.05  
LINK         O4  NAG A   1                 C1  NAG A   2     1555   1555  1.73  
LINK         O6  NAG A   1                 C1  FUL A   3     1555   1555  1.43  
CISPEP   1 ASP G   55    ALA G   56          0        -5.13                     
CISPEP   2 PHE G   96    PRO G   97          0       -10.21                     
CISPEP   3 ARG G  145    ARG G  146          0       -14.91                     
CISPEP   4 PRO I   31    LEU I   32          0       -13.28                     
CRYST1  106.461  106.461   96.116  90.00  90.00 120.00 P 61          6          
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      0.009393  0.005423  0.000000        0.00000                         
SCALE2      0.000000  0.010846  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010404        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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