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Database: PDB
Entry: 5UV8
LinkDB: 5UV8
Original site: 5UV8 
HEADER    SIGNALING PROTEIN                       19-FEB-17   5UV8              
TITLE     INTERLEUKIN-3 RECEPTOR COMPLEX                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-3 RECEPTOR SUBUNIT ALPHA;                      
COMPND   3 CHAIN: A, 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: B, 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    RECEPTOR, SIGNALING PROTEIN                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.E.BROUGHTON,M.W.PARKER                                              
REVDAT   2   29-JUL-20 5UV8    1       COMPND REMARK HETNAM LINK                
REVDAT   2 2                   1       SITE   ATOM                              
REVDAT   1   07-FEB-18 5UV8    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.    2.70 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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 114.35                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 28930                          
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) : 0.244                           
REMARK   3   R VALUE            (WORKING SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1535                            
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2053                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.95                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3150                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 123                          
REMARK   3   BIN FREE R VALUE                    : 0.3670                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5964                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 197                                     
REMARK   3   SOLVENT ATOMS            : 100                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.64000                                             
REMARK   3    B22 (A**2) : -1.64000                                             
REMARK   3    B33 (A**2) : 5.33000                                              
REMARK   3    B12 (A**2) : -0.82000                                             
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): 0.844         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.365         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.311         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.381        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.899                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.849                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6325 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5891 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8588 ; 1.405 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13552 ; 1.198 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   725 ; 6.316 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   308 ;34.740 ;23.734       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1034 ;15.387 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    50 ;16.766 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   967 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6965 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1511 ; 0.004 ; 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):  2936 ; 1.549 ; 4.272       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2935 ; 1.549 ; 4.272       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3649 ; 2.763 ; 6.381       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3650 ; 2.762 ; 6.382       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3389 ; 1.455 ; 4.617       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3390 ; 1.455 ; 4.617       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4940 ; 2.560 ; 6.877       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6518 ; 4.676 ;33.038       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  6519 ; 4.676 ;33.040       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 2                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A    28    293       G    28    293   26054  0.16  0.05     
REMARK   3    2     B    15    120       I    15    120   12444  0.12  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 5UV8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000226522.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-JUL-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                  : GRAPHITE                           
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   : 30501                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 114.350                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 8.100                              
REMARK 200  R MERGE                    (I) : 0.17000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.74000                            
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: 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: 20% PEG 8000, 200 MM NACI, 100 MM        
REMARK 280  CITRATE-PHOSPHATE BUFFER PH 5, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      140.42067            
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       70.21033            
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      105.31550            
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       35.10517            
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      175.52583            
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      140.42067            
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       70.21033            
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       35.10517            
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      105.31550            
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      175.52583            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 3990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 14.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, I, E                               
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 A    20                                                      
REMARK 465     GLU A    21                                                      
REMARK 465     ASP A    22                                                      
REMARK 465     PRO A    23                                                      
REMARK 465     ASN A    24                                                      
REMARK 465     PRO A    25                                                      
REMARK 465     PRO A    26                                                      
REMARK 465     ILE A    27                                                      
REMARK 465     LEU A    43                                                      
REMARK 465     ASN A    44                                                      
REMARK 465     THR A    48                                                      
REMARK 465     ASP A    49                                                      
REMARK 465     ALA A    86                                                      
REMARK 465     ASN A    87                                                      
REMARK 465     MET A   246                                                      
REMARK 465     ASP A   294                                                      
REMARK 465     GLN A   295                                                      
REMARK 465     GLU A   296                                                      
REMARK 465     GLU A   297                                                      
REMARK 465     GLY A   298                                                      
REMARK 465     VAL A   299                                                      
REMARK 465     ASN A   300                                                      
REMARK 465     THR A   301                                                      
REMARK 465     ARG A   302                                                      
REMARK 465     ALA A   303                                                      
REMARK 465     TRP A   304                                                      
REMARK 465     ARG A   305                                                      
REMARK 465     THR A   306                                                      
REMARK 465     SER A   307                                                      
REMARK 465     SER B    12                                                      
REMARK 465     TYR B    13                                                      
REMARK 465     VAL B    14                                                      
REMARK 465     PRO B    31                                                      
REMARK 465     LEU B    32                                                      
REMARK 465     GLN B   122                                                      
REMARK 465     ALA B   123                                                      
REMARK 465     GLN B   124                                                      
REMARK 465     GLN B   125                                                      
REMARK 465     THR B   126                                                      
REMARK 465     THR B   127                                                      
REMARK 465     LEU B   128                                                      
REMARK 465     SER B   129                                                      
REMARK 465     LEU B   130                                                      
REMARK 465     ALA B   131                                                      
REMARK 465     ILE B   132                                                      
REMARK 465     PHE B   133                                                      
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     THR G    48                                                      
REMARK 465     ALA G   143                                                      
REMARK 465     ASN G   144                                                      
REMARK 465     ARG G   145                                                      
REMARK 465     ARG G   146                                                      
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     SER I    12                                                      
REMARK 465     LEU I    32                                                      
REMARK 465     GLN I   122                                                      
REMARK 465     ALA I   123                                                      
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN G  87    C    O                                              
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    ALA A  56       12.04     58.71                                   
REMARK 500    VAL A  63      -73.10    -74.48                                   
REMARK 500    ASN A  65       11.49     53.91                                   
REMARK 500    ALA A  72       47.36   -149.06                                   
REMARK 500    CYS A  76      -50.09   -138.76                                   
REMARK 500    VAL A 117      -59.23     69.41                                   
REMARK 500    THR G  28      -82.89   -126.09                                   
REMARK 500    ASN G  44      -60.57    -97.19                                   
REMARK 500    ASN G  65       11.08     57.12                                   
REMARK 500    ALA G  72       47.01   -149.19                                   
REMARK 500    CYS G  76      -48.91   -138.98                                   
REMARK 500    VAL G 117      -59.38     69.73                                   
REMARK 500    HIS G 153       76.15   -112.88                                   
REMARK 500    LEU I  34      -75.76    -62.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5UV8 A   20   307  UNP    P26951   IL3RA_HUMAN     20    307             
DBREF  5UV8 B   12   133  UNP    P08700   IL3_HUMAN       31    152             
DBREF  5UV8 G   20   307  UNP    P26951   IL3RA_HUMAN     20    307             
DBREF  5UV8 I   12   133  UNP    P08700   IL3_HUMAN       31    152             
SEQADV 5UV8 GLN A  212  UNP  P26951    ASN   212 ENGINEERED MUTATION            
SEQADV 5UV8 VAL A  299  UNP  P26951    ALA   299 ENGINEERED MUTATION            
SEQADV 5UV8 TYR B   13  UNP  P08700    TRP    32 ENGINEERED MUTATION            
SEQADV 5UV8 GLN G  212  UNP  P26951    ASN   212 ENGINEERED MUTATION            
SEQADV 5UV8 VAL G  299  UNP  P26951    ALA   299 ENGINEERED MUTATION            
SEQADV 5UV8 TYR I   13  UNP  P08700    TRP    32 ENGINEERED MUTATION            
SEQRES   1 A  288  LYS GLU ASP PRO ASN PRO PRO ILE THR ASN LEU ARG MET          
SEQRES   2 A  288  LYS ALA LYS ALA GLN GLN LEU THR TRP ASP LEU ASN ARG          
SEQRES   3 A  288  ASN VAL THR ASP ILE GLU CYS VAL LYS ASP ALA ASP TYR          
SEQRES   4 A  288  SER MET PRO ALA VAL ASN ASN SER TYR CYS GLN PHE GLY          
SEQRES   5 A  288  ALA ILE SER LEU CYS GLU VAL THR ASN TYR THR VAL ARG          
SEQRES   6 A  288  VAL ALA ASN PRO PRO PHE SER THR TRP ILE LEU PHE PRO          
SEQRES   7 A  288  GLU ASN SER GLY LYS PRO TRP ALA GLY ALA GLU ASN LEU          
SEQRES   8 A  288  THR CYS TRP ILE HIS ASP VAL ASP PHE LEU SER CYS SER          
SEQRES   9 A  288  TRP ALA VAL GLY PRO GLY ALA PRO ALA ASP VAL GLN TYR          
SEQRES  10 A  288  ASP LEU TYR LEU ASN VAL ALA ASN ARG ARG GLN GLN TYR          
SEQRES  11 A  288  GLU CYS LEU HIS TYR LYS THR ASP ALA GLN GLY THR ARG          
SEQRES  12 A  288  ILE GLY CYS ARG PHE ASP ASP ILE SER ARG LEU SER SER          
SEQRES  13 A  288  GLY SER GLN SER SER HIS ILE LEU VAL ARG GLY ARG SER          
SEQRES  14 A  288  ALA ALA PHE GLY ILE PRO CYS THR ASP LYS PHE VAL VAL          
SEQRES  15 A  288  PHE SER GLN ILE GLU ILE LEU THR PRO PRO GLN MET THR          
SEQRES  16 A  288  ALA LYS CYS ASN LYS THR HIS SER PHE MET HIS TRP LYS          
SEQRES  17 A  288  MET ARG SER HIS PHE ASN ARG LYS PHE ARG TYR GLU LEU          
SEQRES  18 A  288  GLN ILE GLN LYS ARG MET GLN PRO VAL ILE THR GLU GLN          
SEQRES  19 A  288  VAL ARG ASP ARG THR SER PHE GLN LEU LEU ASN PRO GLY          
SEQRES  20 A  288  THR TYR THR VAL GLN ILE ARG ALA ARG GLU ARG VAL TYR          
SEQRES  21 A  288  GLU PHE LEU SER ALA TRP SER THR PRO GLN ARG PHE GLU          
SEQRES  22 A  288  CYS ASP GLN GLU GLU GLY VAL ASN THR ARG ALA TRP ARG          
SEQRES  23 A  288  THR SER                                                      
SEQRES   1 B  122  SER TYR VAL ASN CYS SER ASN MET ILE ASP GLU ILE ILE          
SEQRES   2 B  122  THR HIS LEU LYS GLN PRO PRO LEU PRO LEU LEU ASP PHE          
SEQRES   3 B  122  ASN ASN LEU ASN GLY GLU ASP GLN ASP ILE LEU MET GLU          
SEQRES   4 B  122  ASN ASN LEU ARG ARG PRO ASN LEU GLU ALA PHE ASN ARG          
SEQRES   5 B  122  ALA VAL LYS SER LEU GLN ASN ALA SER ALA ILE GLU SER          
SEQRES   6 B  122  ILE LEU LYS ASN LEU LEU PRO CYS LEU PRO LEU ALA THR          
SEQRES   7 B  122  ALA ALA PRO THR ARG HIS PRO ILE HIS ILE LYS ASP GLY          
SEQRES   8 B  122  ASP TRP ASN GLU PHE ARG ARG LYS LEU THR PHE TYR LEU          
SEQRES   9 B  122  LYS THR LEU GLU ASN ALA GLN ALA GLN GLN THR THR LEU          
SEQRES  10 B  122  SER LEU ALA ILE PHE                                          
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  LYS THR LEU GLU ASN ALA GLN ALA GLN GLN THR THR LEU          
SEQRES  10 I  122  SER LEU ALA ILE PHE                                          
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    BMA  C   3      11                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    BMA  D   3      11                                                       
HET    FUC  D   4      10                                                       
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    BMA  E   3      11                                                       
HET    FUC  E   4      10                                                       
HET    NAG  A 404      14                                                       
HET    GOL  G 401       6                                                       
HET    GOL  G 402       6                                                       
HET    GOL  G 403       6                                                       
HET    NAG  G 408      14                                                       
HET    NAG  G 409      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  NAG    9(C8 H15 N O6)                                               
FORMUL   5  BMA    3(C6 H12 O6)                                                 
FORMUL   6  FUC    2(C6 H12 O5)                                                 
FORMUL   9  GOL    3(C3 H8 O3)                                                  
FORMUL  14  HOH   *100(H2 O)                                                    
HELIX    1 AA1 ASP A  169  SER A  175  1                                   7    
HELIX    2 AA2 SER A  203  GLU A  206  5                                   4    
HELIX    3 AA3 CYS B   16  LYS B   28  1                                  13    
HELIX    4 AA4 LEU B   35  LEU B   40  5                                   6    
HELIX    5 AA5 ASN B   41  GLU B   50  1                                  10    
HELIX    6 AA6 LEU B   53  SER B   67  1                                  15    
HELIX    7 AA7 ALA B   71  LYS B   79  1                                   9    
HELIX    8 AA8 ASN B   80  LEU B   85  5                                   6    
HELIX    9 AA9 ASP B  103  ALA B  121  1                                  19    
HELIX   10 AB1 ASP G  169  SER G  174  1                                   6    
HELIX   11 AB2 SER G  203  GLU G  206  5                                   4    
HELIX   12 AB3 ASN I   15  GLN I   29  1                                  15    
HELIX   13 AB4 ASP I   36  LEU I   40  5                                   5    
HELIX   14 AB5 ASN I   41  GLU I   50  1                                  10    
HELIX   15 AB6 LEU I   53  SER I   67  1                                  15    
HELIX   16 AB7 ALA I   71  LYS I   79  1                                   9    
HELIX   17 AB8 ASN I   80  LEU I   85  5                                   6    
HELIX   18 AB9 ASP I  103  ALA I  121  1                                  19    
SHEET    1 AA1 3 ARG A  31  LYS A  33  0                                        
SHEET    2 AA1 3 GLN A  38  THR A  40 -1  O  GLN A  38   N  LYS A  33           
SHEET    3 AA1 3 TYR A  67  GLN A  69 -1  O  CYS A  68   N  LEU A  39           
SHEET    1 AA2 4 TYR A  58  PRO A  61  0                                        
SHEET    2 AA2 4 GLU A  51  LYS A  54 -1  N  CYS A  52   O  MET A  60           
SHEET    3 AA2 4 THR A  79  VAL A  85 -1  O  THR A  82   N  VAL A  53           
SHEET    4 AA2 4 PHE A  90  PHE A  96 -1  O  THR A  92   N  VAL A  83           
SHEET    1 AA3 4 GLU A 108  HIS A 115  0                                        
SHEET    2 AA3 4 PHE A 119  ALA A 125 -1  O  ALA A 125   N  GLU A 108           
SHEET    3 AA3 4 ARG A 162  PHE A 167 -1  O  PHE A 167   N  LEU A 120           
SHEET    4 AA3 4 HIS A 153  THR A 156 -1  N  LYS A 155   O  ILE A 163           
SHEET    1 AA4 4 GLN A 148  GLU A 150  0                                        
SHEET    2 AA4 4 GLN A 135  VAL A 142 -1  N  LEU A 140   O  TYR A 149           
SHEET    3 AA4 4 SER A 179  ARG A 187 -1  O  HIS A 181   N  ASN A 141           
SHEET    4 AA4 4 THR A 196  VAL A 201 -1  O  THR A 196   N  VAL A 184           
SHEET    1 AA5 3 GLN A 212  CYS A 217  0                                        
SHEET    2 AA5 3 HIS A 221  LYS A 227 -1  O  PHE A 223   N  LYS A 216           
SHEET    3 AA5 3 SER A 259  LEU A 263 -1  O  PHE A 260   N  MET A 224           
SHEET    1 AA6 4 VAL A 249  ARG A 255  0                                        
SHEET    2 AA6 4 PHE A 236  LYS A 244 -1  N  LEU A 240   O  GLU A 252           
SHEET    3 AA6 4 THR A 267  GLU A 276 -1  O  ARG A 275   N  ARG A 237           
SHEET    4 AA6 4 GLN A 289  GLU A 292 -1  O  PHE A 291   N  TYR A 268           
SHEET    1 AA7 3 ARG G  31  LYS G  33  0                                        
SHEET    2 AA7 3 GLN G  38  THR G  40 -1  O  GLN G  38   N  LYS G  33           
SHEET    3 AA7 3 TYR G  67  GLN G  69 -1  O  CYS G  68   N  LEU G  39           
SHEET    1 AA8 4 SER G  59  PRO G  61  0                                        
SHEET    2 AA8 4 ILE G  50  LYS G  54 -1  N  CYS G  52   O  MET G  60           
SHEET    3 AA8 4 THR G  79  VAL G  85 -1  O  THR G  82   N  VAL G  53           
SHEET    4 AA8 4 PHE G  90  PHE G  96 -1  O  THR G  92   N  VAL G  83           
SHEET    1 AA9 4 GLU G 108  HIS G 115  0                                        
SHEET    2 AA9 4 PHE G 119  ALA G 125 -1  O  ALA G 125   N  GLU G 108           
SHEET    3 AA9 4 ARG G 162  PHE G 167 -1  O  PHE G 167   N  LEU G 120           
SHEET    4 AA9 4 LYS G 155  THR G 156 -1  N  LYS G 155   O  GLY G 164           
SHEET    1 AB1 4 TYR G 149  GLU G 150  0                                        
SHEET    2 AB1 4 GLN G 135  ASN G 141 -1  N  LEU G 140   O  TYR G 149           
SHEET    3 AB1 4 SER G 179  ARG G 187 -1  O  HIS G 181   N  ASN G 141           
SHEET    4 AB1 4 THR G 196  VAL G 201 -1  O  THR G 196   N  VAL G 184           
SHEET    1 AB2 3 GLN G 212  CYS G 217  0                                        
SHEET    2 AB2 3 HIS G 221  LYS G 227 -1  O  PHE G 223   N  LYS G 216           
SHEET    3 AB2 3 SER G 259  LEU G 263 -1  O  PHE G 260   N  MET G 224           
SHEET    1 AB3 4 ILE G 250  ARG G 255  0                                        
SHEET    2 AB3 4 PHE G 236  LYS G 244 -1  N  LEU G 240   O  GLU G 252           
SHEET    3 AB3 4 THR G 267  GLU G 276 -1  O  ARG G 275   N  ARG G 237           
SHEET    4 AB3 4 GLN G 289  GLU G 292 -1  O  PHE G 291   N  TYR G 268           
SSBOND   1 CYS A   52    CYS A   68                          1555   1555  2.03  
SSBOND   2 CYS A   76    CYS A  195                          1555   1555  2.07  
SSBOND   3 CYS A  112    CYS A  122                          1555   1555  2.08  
SSBOND   4 CYS A  151    CYS A  165                          1555   1555  2.01  
SSBOND   5 CYS A  217    CYS A  293                          1555   1555  2.05  
SSBOND   6 CYS B   16    CYS B   84                          1555   1555  2.07  
SSBOND   7 CYS G   52    CYS G   68                          1555   1555  2.04  
SSBOND   8 CYS G   76    CYS G  195                          1555   1555  2.04  
SSBOND   9 CYS G  112    CYS G  122                          1555   1555  2.07  
SSBOND  10 CYS G  151    CYS G  165                          1555   1555  2.06  
SSBOND  11 CYS G  217    CYS G  293                          1555   1555  2.02  
SSBOND  12 CYS I   16    CYS I   84                          1555   1555  2.63  
LINK         ND2 ASN A  80                 C1  NAG D   1     1555   1555  1.45  
LINK         ND2 ASN A 109                 C1  NAG A 404     1555   1555  1.46  
LINK         ND2 ASN A 218                 C1  NAG C   1     1555   1555  1.44  
LINK         ND2 ASN G  80                 C1  NAG E   1     1555   1555  1.43  
LINK         ND2 ASN G 109                 C1  NAG G 408     1555   1555  1.45  
LINK         ND2 ASN G 218                 C1  NAG G 409     1555   1555  1.44  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.47  
LINK         O4  NAG C   2                 C1  BMA C   3     1555   1555  1.46  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.45  
LINK         O6  NAG D   1                 C1  FUC D   4     1555   1555  1.45  
LINK         O4  NAG D   2                 C1  BMA D   3     1555   1555  1.47  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.44  
LINK         O6  NAG E   1                 C1  FUC E   4     1555   1555  1.44  
LINK         O3  NAG E   2                 C1  BMA E   3     1555   1555  1.45  
CISPEP   1 THR A   28    ASN A   29          0       -12.84                     
CISPEP   2 PHE A   96    PRO A   97          0       -10.24                     
CISPEP   3 PHE G   96    PRO G   97          0        -5.70                     
CRYST1  132.039  132.039  210.631  90.00  90.00 120.00 P 65 2 2     24          
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      0.007574  0.004373  0.000000        0.00000                         
SCALE2      0.000000  0.008745  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004748        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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