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Database: PDB
Entry: 6DF3
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Original site: 6DF3 
HEADER    CYTOKINE                                14-MAY-18   6DF3              
TITLE     CRYSTAL STRUCTURE OF TERNARY COMPLEX OF IL-24 WITH SOLUBLE RECEPTORS  
TITLE    2 IL-22RA AND IL-20RB                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-22 RECEPTOR SUBUNIT ALPHA-1;                   
COMPND   3 CHAIN: L;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 24-228;                                       
COMPND   5 SYNONYM: IL-22RA1, CYTOKINE RECEPTOR CLASS-II MEMBER 9, CYTOKINE     
COMPND   6 RECEPTOR FAMILY 2 MEMBER 9, CRF2-9, ZCYTOR11;                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTERLEUKIN-24;                                            
COMPND  10 CHAIN: C;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 52-206;                                       
COMPND  12 SYNONYM: IL-24, MELANOMA DIFFERENTIATION-ASSOCIATED GENE 7 PROTEIN,  
COMPND  13 MDA-7, SUPPRESSION OF TUMORIGENICITY 16 PROTEIN;                     
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: YES;                                                       
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: INTERLEUKIN-20 RECEPTOR SUBUNIT BETA;                      
COMPND  18 CHAIN: H;                                                            
COMPND  19 FRAGMENT: UNP RESIDUES 35-224;                                       
COMPND  20 SYNONYM: IL-20RB, FIBRONECTIN TYPE III DOMAIN CONTAINING 6, FNDC6,   
COMPND  21 IL-20R2;                                                             
COMPND  22 ENGINEERED: YES;                                                     
COMPND  23 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: IL22RA1, IL22R;                                                
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: IL24, MDA7, ST16;                                              
SOURCE  14 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE  15 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 GENE: IL20RB, DIRS1, UNQ557/PRO1114;                                 
SOURCE  22 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE  23 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 7227                                        
KEYWDS    CYTOKINE, TERNARY COMPLEX, CELL SIGNALING, JAK-STAT PATHWAY           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LUBKOWSKI,A.WLODAWER                                                
REVDAT   3   03-OCT-18 6DF3    1       JRNL                                     
REVDAT   2   29-AUG-18 6DF3    1       JRNL                                     
REVDAT   1   15-AUG-18 6DF3    0                                                
JRNL        AUTH   J.LUBKOWSKI,C.SONMEZ,S.V.SMIRNOV,A.ANISHKIN,S.V.KOTENKO,     
JRNL        AUTH 2 A.WLODAWER                                                   
JRNL        TITL   CRYSTAL STRUCTURE OF THE LABILE COMPLEX OF IL-24 WITH THE    
JRNL        TITL 2 EXTRACELLULAR DOMAINS OF IL-22R1 AND IL-20R2.                
JRNL        REF    J. IMMUNOL.                   V. 201  2082 2018              
JRNL        REFN                   ESSN 1550-6606                               
JRNL        PMID   30111632                                                     
JRNL        DOI    10.4049/JIMMUNOL.1800726                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0189                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 37897                          
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) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1978                            
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) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2738                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.88                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2980                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 167                          
REMARK   3   BIN FREE R VALUE                    : 0.3160                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4395                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 80                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 74.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.75000                                              
REMARK   3    B22 (A**2) : 1.75000                                              
REMARK   3    B33 (A**2) : -3.49000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.191         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.170         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.155         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.072        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.953                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4563 ; 0.019 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4172 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6200 ; 2.018 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9684 ; 1.080 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   539 ; 7.899 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   207 ;33.478 ;23.575       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   769 ;17.224 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;18.073 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   701 ; 0.117 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4950 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   950 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 3                                          
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 :   L    24        L   303                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.2815   5.2394  54.6311              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4123 T22:   0.1529                                     
REMARK   3      T33:   0.0730 T12:   0.1965                                     
REMARK   3      T13:   0.0735 T23:  -0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5034 L22:   2.0997                                     
REMARK   3      L33:   1.9004 L12:   1.2500                                     
REMARK   3      L13:   2.9351 L23:   0.3930                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4345 S12:   0.3300 S13:  -0.2751                       
REMARK   3      S21:  -0.6579 S22:  -0.4019 S23:  -0.1270                       
REMARK   3      S31:   0.4571 S32:   0.2220 S33:  -0.0327                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    52        C   206                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.2312  23.3804  52.0204              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0988 T22:   0.0621                                     
REMARK   3      T33:   0.0521 T12:   0.0436                                     
REMARK   3      T13:  -0.0572 T23:  -0.0223                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5118 L22:   3.6917                                     
REMARK   3      L33:   6.7343 L12:  -0.4496                                     
REMARK   3      L13:   2.2657 L23:  -1.2297                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2419 S12:   0.3228 S13:  -0.0220                       
REMARK   3      S21:  -0.4795 S22:   0.0108 S23:   0.2320                       
REMARK   3      S31:   0.3521 S32:   0.2674 S33:  -0.2527                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H    35        H   224                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9997  26.9685  79.3283              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0995 T22:   0.2821                                     
REMARK   3      T33:   0.1617 T12:  -0.0122                                     
REMARK   3      T13:  -0.0140 T23:  -0.1528                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6190 L22:   2.6818                                     
REMARK   3      L33:   2.7858 L12:  -0.3699                                     
REMARK   3      L13:   1.3552 L23:   0.5334                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1205 S12:  -0.6762 S13:  -0.0926                       
REMARK   3      S21:   0.2361 S22:   0.3312 S23:  -0.4775                       
REMARK   3      S31:   0.0523 S32:   0.5364 S33:  -0.4518                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 6DF3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAY-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000234501.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUL-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5 - 8.0                          
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39903                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 8.000                              
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.41600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.620                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4DOH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8 MG/ML PROTEIN IN 0.2 M SODIUM          
REMARK 280  CHLORIDE, 0.05 M HEPES AGAINST 215 W/V MEPEG2000, 0.05 M TRIS,      
REMARK 280  PH 8.5, 0.05 M TRIMETHYLAMINE N-OXIDE DIHYDRATE, VAPOR DIFFUSION,   
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.39250            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       93.58875            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       31.19625            
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, C, H                               
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     GLY L    44                                                      
REMARK 465     PRO L    45                                                      
REMARK 465     GLU L    46                                                      
REMARK 465     GLY L    47                                                      
REMARK 465     GLY L   102                                                      
REMARK 465     GLY L   103                                                      
REMARK 465     ARG L   104                                                      
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     SER L 105    OG                                                  
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   OE1  GLN C   201     O2   GOL C   302              2.13            
REMARK 500   OD2  ASP L   162     OG1  THR L   207              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP C 102   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG C 168   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    LEU C 186   CA  -  CB  -  CG  ANGL. DEV. =  22.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP L 150       70.30     46.34                                   
REMARK 500    ASN L 172     -130.61     47.88                                   
REMARK 500    THR C 119      -62.05   -108.06                                   
REMARK 500    ALA H  59       63.27   -157.01                                   
REMARK 500    THR H  79       58.73   -146.63                                   
REMARK 500    PRO H  95       37.99    -84.30                                   
REMARK 500    LEU H 117       64.74   -158.77                                   
REMARK 500    GLN H 120      108.07    -59.25                                   
REMARK 500    MET H 143      130.19   -177.80                                   
REMARK 500    PRO H 174      -51.32    -29.83                                   
REMARK 500    ALA H 176      153.02    -44.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG L    
REMARK 800  301 through NAG L 302 bound to ASN L 80                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG L 303 bound   
REMARK 800  to ASN L 87                                                         
DBREF  6DF3 L   24   228  UNP    Q8N6P7   I22R1_HUMAN     24    228             
DBREF  6DF3 C   52   206  UNP    Q13007   IL24_HUMAN      52    206             
DBREF  6DF3 H   35   224  UNP    Q6UXL0   I20RB_HUMAN     35    224             
SEQADV 6DF3 GLY L  229  UNP  Q8N6P7              EXPRESSION TAG                 
SEQADV 6DF3 GLN C   85  UNP  Q13007    ASN    85 ENGINEERED MUTATION            
SEQADV 6DF3 GLN C   99  UNP  Q13007    ASN    99 ENGINEERED MUTATION            
SEQADV 6DF3 HIS C  124  UNP  Q13007    TYR   124 CONFLICT                       
SEQADV 6DF3 GLN C  126  UNP  Q13007    ASN   126 ENGINEERED MUTATION            
SEQADV 6DF3 GLN H  134  UNP  Q6UXL0    ASN   134 ENGINEERED MUTATION            
SEQADV 6DF3 GLU H  206  UNP  Q6UXL0    GLN   206 CONFLICT                       
SEQRES   1 L  206  LEU LEU GLN HIS VAL LYS PHE GLN SER SER ASN PHE GLU          
SEQRES   2 L  206  ASN ILE LEU THR TRP ASP SER GLY PRO GLU GLY THR PRO          
SEQRES   3 L  206  ASP THR VAL TYR SER ILE GLU TYR LYS THR TYR GLY GLU          
SEQRES   4 L  206  ARG ASP TRP VAL ALA LYS LYS GLY CYS GLN ARG ILE THR          
SEQRES   5 L  206  ARG LYS SER CYS ASN LEU THR VAL GLU THR GLY ASN LEU          
SEQRES   6 L  206  THR GLU LEU TYR TYR ALA ARG VAL THR ALA VAL SER ALA          
SEQRES   7 L  206  GLY GLY ARG SER ALA THR LYS MET THR ASP ARG PHE SER          
SEQRES   8 L  206  SER LEU GLN HIS THR THR LEU LYS PRO PRO ASP VAL THR          
SEQRES   9 L  206  CYS ILE SER LYS VAL ARG SER ILE GLN MET ILE VAL HIS          
SEQRES  10 L  206  PRO THR PRO THR PRO ILE ARG ALA GLY ASP GLY HIS ARG          
SEQRES  11 L  206  LEU THR LEU GLU ASP ILE PHE HIS ASP LEU PHE TYR HIS          
SEQRES  12 L  206  LEU GLU LEU GLN VAL ASN ARG THR TYR GLN MET HIS LEU          
SEQRES  13 L  206  GLY GLY LYS GLN ARG GLU TYR GLU PHE PHE GLY LEU THR          
SEQRES  14 L  206  PRO ASP THR GLU PHE LEU GLY THR ILE MET ILE CYS VAL          
SEQRES  15 L  206  PRO THR TRP ALA LYS GLU SER ALA PRO TYR MET CYS ARG          
SEQRES  16 L  206  VAL LYS THR LEU PRO ASP ARG THR TRP THR GLY                  
SEQRES   1 C  155  GLN GLU PHE HIS PHE GLY PRO CYS GLN VAL LYS GLY VAL          
SEQRES   2 C  155  VAL PRO GLN LYS LEU TRP GLU ALA PHE TRP ALA VAL LYS          
SEQRES   3 C  155  ASP THR MET GLN ALA GLN ASP GLN ILE THR SER ALA ARG          
SEQRES   4 C  155  LEU LEU GLN GLN GLU VAL LEU GLN GLN VAL SER ASP ALA          
SEQRES   5 C  155  GLU SER CYS TYR LEU VAL HIS THR LEU LEU GLU PHE TYR          
SEQRES   6 C  155  LEU LYS THR VAL PHE LYS ASN HIS HIS GLN ARG THR VAL          
SEQRES   7 C  155  GLU VAL ARG THR LEU LYS SER PHE SER THR LEU ALA ASN          
SEQRES   8 C  155  ASN PHE VAL LEU ILE VAL SER GLN LEU GLN PRO SER GLN          
SEQRES   9 C  155  GLU ASN GLU MET PHE SER ILE ARG ASP SER ALA HIS ARG          
SEQRES  10 C  155  ARG PHE LEU LEU PHE ARG ARG ALA PHE LYS GLN LEU ASP          
SEQRES  11 C  155  VAL GLU ALA ALA LEU THR LYS ALA LEU GLY GLU VAL ASP          
SEQRES  12 C  155  ILE LEU LEU THR TRP MET GLN LYS PHE TYR LYS LEU              
SEQRES   1 H  190  LEU PRO ALA PRO GLN ASN LEU SER VAL LEU SER THR ASN          
SEQRES   2 H  190  MET LYS HIS LEU LEU MET TRP SER PRO VAL ILE ALA PRO          
SEQRES   3 H  190  GLY GLU THR VAL TYR TYR SER VAL GLU TYR GLN GLY GLU          
SEQRES   4 H  190  TYR GLU SER LEU TYR THR SER HIS ILE TRP ILE PRO SER          
SEQRES   5 H  190  SER TRP CYS SER LEU THR GLU GLY PRO GLU CYS ASP VAL          
SEQRES   6 H  190  THR ASP ASP ILE THR ALA THR VAL PRO TYR ASN LEU ARG          
SEQRES   7 H  190  VAL ARG ALA THR LEU GLY SER GLN THR SER ALA TRP SER          
SEQRES   8 H  190  ILE LEU LYS HIS PRO PHE ASN ARG GLN SER THR ILE LEU          
SEQRES   9 H  190  THR ARG PRO GLY MET GLU ILE THR LYS ASP GLY PHE HIS          
SEQRES  10 H  190  LEU VAL ILE GLU LEU GLU ASP LEU GLY PRO GLN PHE GLU          
SEQRES  11 H  190  PHE LEU VAL ALA TYR TRP ARG ARG GLU PRO GLY ALA GLU          
SEQRES  12 H  190  GLU HIS VAL LYS MET VAL ARG SER GLY GLY ILE PRO VAL          
SEQRES  13 H  190  HIS LEU GLU THR MET GLU PRO GLY ALA ALA TYR CYS VAL          
SEQRES  14 H  190  LYS ALA GLU THR PHE VAL LYS ALA ILE GLY ARG TYR SER          
SEQRES  15 H  190  ALA PHE SER GLN THR GLU CYS VAL                              
HET    NAG  L 301      14                                                       
HET    NAG  L 302      14                                                       
HET    NAG  L 303      14                                                       
HET    GOL  C 301       6                                                       
HET    GOL  C 302       6                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   4  NAG    3(C8 H15 N O6)                                               
FORMUL   6  GOL    2(C3 H8 O3)                                                  
FORMUL   8  HOH   *80(H2 O)                                                     
HELIX    1 AA1 SER L  114  THR L  119  1                                   6    
HELIX    2 AA2 LEU L  156  PHE L  160  1                                   5    
HELIX    3 AA3 PRO L  206  ALA L  209  5                                   4    
HELIX    4 AA4 VAL C   65  ASP C   84  1                                  20    
HELIX    5 AA5 GLN C   93  GLN C   98  1                                   6    
HELIX    6 AA6 SER C  101  THR C  119  1                                  19    
HELIX    7 AA7 THR C  119  THR C  128  1                                  10    
HELIX    8 AA8 GLU C  130  GLN C  150  1                                  21    
HELIX    9 AA9 GLU C  156  GLU C  158  5                                   3    
HELIX   10 AB1 MET C  159  GLN C  179  1                                  21    
HELIX   11 AB2 ASP C  181  GLU C  192  1                                  12    
HELIX   12 AB3 GLU C  192  GLN C  201  1                                  10    
HELIX   13 AB4 GLY H   72  THR H   79  1                                   8    
HELIX   14 AB5 THR H  100  ILE H  103  5                                   4    
HELIX   15 AB6 GLN H  134  THR H  136  5                                   3    
SHEET    1 AA1 3 GLN L  26  SER L  33  0                                        
SHEET    2 AA1 3 GLU L  36  ASP L  42 -1  O  ASP L  42   N  GLN L  26           
SHEET    3 AA1 3 SER L  78  ASN L  80 -1  O  CYS L  79   N  LEU L  39           
SHEET    1 AA2 4 VAL L  66  ALA L  67  0                                        
SHEET    2 AA2 4 THR L  51  THR L  59 -1  N  TYR L  57   O  VAL L  66           
SHEET    3 AA2 4 TYR L  92  SER L 100 -1  O  THR L  97   N  SER L  54           
SHEET    4 AA2 4 ALA L 106  MET L 109 -1  O  ALA L 106   N  ALA L  98           
SHEET    1 AA3 3 VAL L 126  SER L 130  0                                        
SHEET    2 AA3 3 ILE L 135  VAL L 139 -1  O  GLN L 136   N  ILE L 129           
SHEET    3 AA3 3 GLU L 185  PHE L 188 -1  O  TYR L 186   N  MET L 137           
SHEET    1 AA4 2 PRO L 143  ARG L 147  0                                        
SHEET    2 AA4 2 ARG L 153  THR L 155 -1  O  LEU L 154   N  ILE L 146           
SHEET    1 AA5 4 TYR L 175  GLY L 181  0                                        
SHEET    2 AA5 4 PHE L 164  VAL L 171 -1  N  LEU L 167   O  LEU L 179           
SHEET    3 AA5 4 GLU L 196  VAL L 205 -1  O  CYS L 204   N  PHE L 164           
SHEET    4 AA5 4 LYS L 210  GLU L 211 -1  O  LYS L 210   N  VAL L 205           
SHEET    1 AA6 4 TYR L 175  GLY L 181  0                                        
SHEET    2 AA6 4 PHE L 164  VAL L 171 -1  N  LEU L 167   O  LEU L 179           
SHEET    3 AA6 4 GLU L 196  VAL L 205 -1  O  CYS L 204   N  PHE L 164           
SHEET    4 AA6 4 TYR L 215  LYS L 220 -1  O  CYS L 217   N  GLY L 199           
SHEET    1 AA7 3 CYS C  59  VAL C  61  0                                        
SHEET    2 AA7 3 GLU C  53  PHE C  56 -1  N  PHE C  54   O  VAL C  61           
SHEET    3 AA7 3 TYR C 204  LYS C 205 -1  O  LYS C 205   N  GLU C  53           
SHEET    1 AA8 3 SER H  42  THR H  46  0                                        
SHEET    2 AA8 3 LYS H  49  MET H  53 -1  O  LEU H  51   N  LEU H  44           
SHEET    3 AA8 3 GLU H  96  ASP H  98 -1  O  CYS H  97   N  LEU H  52           
SHEET    1 AA9 4 ILE H  84  PRO H  85  0                                        
SHEET    2 AA9 4 TYR H  65  GLN H  71 -1  N  TYR H  70   O  ILE H  84           
SHEET    3 AA9 4 PRO H 108  LEU H 117 -1  O  THR H 116   N  TYR H  65           
SHEET    4 AA9 4 SER H 125  ILE H 126 -1  O  SER H 125   N  VAL H 113           
SHEET    1 AB1 3 GLN H 120  THR H 121  0                                        
SHEET    2 AB1 3 PRO H 108  LEU H 117 -1  N  LEU H 117   O  GLN H 120           
SHEET    3 AB1 3 PHE H 131  ASN H 132 -1  O  PHE H 131   N  TYR H 109           
SHEET    1 AB2 3 MET H 143  ASP H 148  0                                        
SHEET    2 AB2 3 HIS H 151  LEU H 156 -1  O  VAL H 153   N  THR H 146           
SHEET    3 AB2 3 VAL H 190  THR H 194 -1  O  GLU H 193   N  LEU H 152           
SHEET    1 AB3 4 HIS H 179  VAL H 183  0                                        
SHEET    2 AB3 4 GLU H 164  ARG H 171 -1  N  TYR H 169   O  HIS H 179           
SHEET    3 AB3 4 TYR H 201  PHE H 208 -1  O  PHE H 208   N  GLU H 164           
SHEET    4 AB3 4 GLU H 222  CYS H 223 -1  O  GLU H 222   N  VAL H 203           
SSBOND   1 CYS L  128    CYS L  217                          1555   1555  2.19  
SSBOND   2 CYS C   59    CYS C  106                          1555   1555  2.71  
SSBOND   3 CYS H   89    CYS H   97                          1555   1555  2.03  
SSBOND   4 CYS H  202    CYS H  223                          1555   1555  2.06  
LINK         ND2 ASN L  80                 C1  NAG L 301     1555   1555  1.46  
LINK         ND2 ASN L  87                 C1  NAG L 303     1555   1555  1.44  
LINK         O4  NAG L 301                 C1  NAG L 302     1555   1555  1.46  
SITE     1 AC1  2 LYS C  77  GLN L 117                                          
SITE     1 AC2  7 PHE C  54  PRO C  66  LEU C  69  TRP C  70                    
SITE     2 AC2  7 LEU C 197  MET C 200  GLN C 201                               
SITE     1 AC3  6 GLU L  36  ASN L  80  THR L  82  VAL L  83                    
SITE     2 AC3  6 PRO L 145  ARG L 153                                          
SITE     1 AC4  3 ASN L  87  THR L  89  GLU L  90                               
CRYST1   77.702   77.702  124.785  90.00  90.00  90.00 P 43          4          
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      0.012870  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012870  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008014        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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