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Database: PDB
Entry: 4GAF
LinkDB: 4GAF
Original site: 4GAF 
HEADER    SIGNALING PROTEIN                       25-JUL-12   4GAF              
TITLE     CRYSTAL STRUCTURE OF EBI-005, A CHIMERA OF HUMAN IL-1BETA AND IL-1RA, 
TITLE    2 BOUND TO HUMAN INTERLEUKIN-1 RECEPTOR TYPE 1                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EBI-005;                                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: INTERLEUKIN-1 RECEPTOR TYPE 1;                             
COMPND   7 CHAIN: B;                                                            
COMPND   8 FRAGMENT: UNP RESIDUES 18-336;                                       
COMPND   9 SYNONYM: IL-1R-1, IL-1RT-1, IL-1RT1, CD121 ANTIGEN-LIKE FAMILY MEMBER
COMPND  10 A, INTERLEUKIN-1 RECEPTOR ALPHA, IL-1R-ALPHA, INTERLEUKIN-1 RECEPTOR 
COMPND  11 TYPE I, P80, INTERLEUKIN-1 RECEPTOR TYPE 1, MEMBRANE FORM, MIL-1R1,  
COMPND  12 MIL-1RI, INTERLEUKIN-1 RECEPTOR TYPE 1, SOLUBLE FORM, SIL-1R1, SIL-  
COMPND  13 1RI;                                                                 
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 GENE: IL1R1, IL1R, IL1RA, IL1RT1;                                    
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    IL-1BETA, IL-1RA, IL-1R1, IL-1 SIGNALING, BETA-TREFOIL, SIGNALING     
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.HOU,S.A.TOWNSON,J.T.KOVALCHIN,A.MASCI,O.KINER,Y.SHU,B.KING,         
AUTHOR   2 C.THOMAS,K.C.GARCIA,E.S.FURFINE,T.M.BARNES                           
REVDAT   4   29-JUL-20 4GAF    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE                                     
REVDAT   3   15-NOV-17 4GAF    1       REMARK                                   
REVDAT   2   27-MAR-13 4GAF    1       JRNL                                     
REVDAT   1   20-FEB-13 4GAF    0                                                
JRNL        AUTH   J.HOU,S.A.TOWNSON,J.T.KOVALCHIN,A.MASCI,O.KINER,Y.SHU,       
JRNL        AUTH 2 B.M.KING,E.SCHIRMER,K.GOLDEN,C.THOMAS,K.C.GARCIA,            
JRNL        AUTH 3 G.ZARBIS-PAPASTOITSIS,E.S.FURFINE,T.M.BARNES                 
JRNL        TITL   DESIGN OF A SUPERIOR CYTOKINE ANTAGONIST FOR TOPICAL         
JRNL        TITL 2 OPHTHALMIC USE.                                              
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 110  3913 2013              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   23431173                                                     
JRNL        DOI    10.1073/PNAS.1217996110                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.86                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 31383                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1585                            
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) : 2148                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3030                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 126                          
REMARK   3   BIN FREE R VALUE                    : 0.3400                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3716                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 57                                      
REMARK   3   SOLVENT ATOMS            : 209                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.18000                                              
REMARK   3    B22 (A**2) : -0.59000                                             
REMARK   3    B33 (A**2) : 0.41000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.255         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.218         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.170         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.350        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3904 ; 0.022 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5304 ; 1.983 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   465 ; 7.479 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   186 ;37.358 ;25.161       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   688 ;18.993 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;22.557 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   583 ; 0.145 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2960 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  2314 ; 1.232 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3779 ; 2.209 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1590 ; 3.324 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1521 ; 5.356 ; 4.500       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    21                          
REMARK   3    RESIDUE RANGE :   A    22        A    53                          
REMARK   3    RESIDUE RANGE :   A    54        A   116                          
REMARK   3    RESIDUE RANGE :   A   117        A   152                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.5020 -33.2310  11.5070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1166 T22:   0.1142                                     
REMARK   3      T33:   0.0474 T12:  -0.1007                                     
REMARK   3      T13:   0.0193 T23:  -0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5823 L22:   4.1355                                     
REMARK   3      L33:   3.4976 L12:   1.2555                                     
REMARK   3      L13:  -0.4896 L23:  -1.0404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2051 S12:  -0.1420 S13:   0.1352                       
REMARK   3      S21:   0.1936 S22:  -0.1081 S23:  -0.0933                       
REMARK   3      S31:  -0.1646 S32:   0.1422 S33:  -0.0971                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     4        B    69                          
REMARK   3    RESIDUE RANGE :   B    70        B   166                          
REMARK   3    RESIDUE RANGE :   B   167        B   204                          
REMARK   3    RESIDUE RANGE :   B   205        B   313                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.8510 -39.8700  16.7530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1543 T22:   0.2238                                     
REMARK   3      T33:   0.0691 T12:  -0.0812                                     
REMARK   3      T13:  -0.0034 T23:   0.0380                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3040 L22:   3.6745                                     
REMARK   3      L33:   0.0348 L12:   0.9541                                     
REMARK   3      L13:   0.0355 L23:   0.0008                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0685 S12:   0.0839 S13:   0.0208                       
REMARK   3      S21:  -0.2749 S22:   0.0696 S23:  -0.0530                       
REMARK   3      S31:   0.0046 S32:   0.0567 S33:  -0.0011                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 U VALUES : RESIDUAL ONLY                                  
REMARK   4                                                                      
REMARK   4 4GAF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000073940.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-SEP-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9755                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31476                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.8000                            
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       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56000                            
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 100 MM TRIS, 200 MM        
REMARK 280  LITHIUM CITRATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K,   
REMARK 280  PH 7.0                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
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   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
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       63.08500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       63.08500            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       30.17500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       74.63500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       30.17500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       74.63500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       63.08500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       30.17500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       74.63500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       63.08500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       30.17500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       74.63500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A   153                                                      
REMARK 465     LEU B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ARG B    82                                                      
REMARK 465     ASN B    83                                                      
REMARK 465     SER B    84                                                      
REMARK 465     SER B    85                                                      
REMARK 465     VAL B   314                                                      
REMARK 465     THR B   315                                                      
REMARK 465     ASN B   316                                                      
REMARK 465     PHE B   317                                                      
REMARK 465     GLN B   318                                                      
REMARK 465     LYS B   319                                                      
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   NH2  ARG A    21     OE2  GLU B    11              2.15            
REMARK 500   O    SER B    93     O    HOH B   741              2.18            
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    VAL B  24   CB  -  CA  -  C   ANGL. DEV. = -14.6 DEGREES          
REMARK 500    PRO B 206   C   -  N   -  CA  ANGL. DEV. =   9.8 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    ASN A  22     -121.83     45.45                                   
REMARK 500    ASN A 118       -2.74     78.98                                   
REMARK 500    LYS B   5      119.85     84.11                                   
REMARK 500    ASN B  32      -40.52    128.98                                   
REMARK 500    LYS B  35       71.13    120.31                                   
REMARK 500    ASP B  43     -129.16     62.64                                   
REMARK 500    ASN B 102       18.63     58.15                                   
REMARK 500    ALA B 118       -0.85     78.79                                   
REMARK 500    LYS B 161     -112.83     53.68                                   
REMARK 500    VAL B 169      127.08    -37.81                                   
REMARK 500    GLU B 202      150.06    -48.70                                   
REMARK 500    ASN B 204       92.11    -65.06                                   
REMARK 500    PRO B 206       92.48    -58.31                                   
REMARK 500    PRO B 214     -178.53    -69.12                                   
REMARK 500    ALA B 215       47.13   -140.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 505  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B  18   OG                                                     
REMARK 620 2 GLU B  21   OE1  84.0                                              
REMARK 620 3 THR B 193   O   171.1  90.0                                        
REMARK 620 4 THR B 193   OG1  93.1  78.7  79.3                                  
REMARK 620 5 HOH B 627   O    84.3 167.5 101.2  97.7                            
REMARK 620 6 HOH B 642   O    92.8  85.3  93.2 162.2  99.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4GAI   RELATED DB: PDB                                   
DBREF  4GAF B    1   319  UNP    P14778   IL1R1_HUMAN     18    336             
DBREF  4GAF A    1   153  PDB    4GAF     4GAF             1    153             
SEQRES   1 A  153  ALA PRO VAL ARG SER LEU ASN CYS ARG ILE TRP ASP VAL          
SEQRES   2 A  153  ASN GLN LYS THR PHE TYR LEU ARG ASN ASN GLN LEU VAL          
SEQRES   3 A  153  ALA GLY TYR LEU GLN GLY PRO ASN VAL ASN LEU GLU GLU          
SEQRES   4 A  153  LYS PHE SER MET SER PHE VAL GLN GLY GLU GLU SER ASN          
SEQRES   5 A  153  ASP LYS ILE PRO VAL ALA LEU GLY LEU LYS GLU LYS ASN          
SEQRES   6 A  153  LEU TYR LEU SER CYS VAL LEU LYS ASP ASP LYS PRO THR          
SEQRES   7 A  153  LEU GLN LEU GLU SER VAL ASP PRO LYS ASN TYR PRO LYS          
SEQRES   8 A  153  LYS LYS MET GLU LYS ARG PHE VAL PHE ASN LYS ILE GLU          
SEQRES   9 A  153  ILE ASN ASN LYS LEU GLU PHE GLU SER ALA GLN PHE PRO          
SEQRES  10 A  153  ASN TRP PHE LEU CYS THR ALA MET GLU ALA ASP GLN PRO          
SEQRES  11 A  153  VAL SER LEU THR ASN MET PRO ASP GLU GLY VAL MET VAL          
SEQRES  12 A  153  THR LYS PHE TYR MET GLN PHE VAL SER SER                      
SEQRES   1 B  319  LEU GLU ALA ASP LYS CYS LYS GLU ARG GLU GLU LYS ILE          
SEQRES   2 B  319  ILE LEU VAL SER SER ALA ASN GLU ILE ASP VAL ARG PRO          
SEQRES   3 B  319  CYS PRO LEU ASN PRO ASN GLU HIS LYS GLY THR ILE THR          
SEQRES   4 B  319  TRP TYR LYS ASP ASP SER LYS THR PRO VAL SER THR GLU          
SEQRES   5 B  319  GLN ALA SER ARG ILE HIS GLN HIS LYS GLU LYS LEU TRP          
SEQRES   6 B  319  PHE VAL PRO ALA LYS VAL GLU ASP SER GLY HIS TYR TYR          
SEQRES   7 B  319  CYS VAL VAL ARG ASN SER SER TYR CYS LEU ARG ILE LYS          
SEQRES   8 B  319  ILE SER ALA LYS PHE VAL GLU ASN GLU PRO ASN LEU CYS          
SEQRES   9 B  319  TYR ASN ALA GLN ALA ILE PHE LYS GLN LYS LEU PRO VAL          
SEQRES  10 B  319  ALA GLY ASP GLY GLY LEU VAL CYS PRO TYR MET GLU PHE          
SEQRES  11 B  319  PHE LYS ASN GLU ASN ASN GLU LEU PRO LYS LEU GLN TRP          
SEQRES  12 B  319  TYR LYS ASP CYS LYS PRO LEU LEU LEU ASP ASN ILE HIS          
SEQRES  13 B  319  PHE SER GLY VAL LYS ASP ARG LEU ILE VAL MET ASN VAL          
SEQRES  14 B  319  ALA GLU LYS HIS ARG GLY ASN TYR THR CYS HIS ALA SER          
SEQRES  15 B  319  TYR THR TYR LEU GLY LYS GLN TYR PRO ILE THR ARG VAL          
SEQRES  16 B  319  ILE GLU PHE ILE THR LEU GLU GLU ASN LYS PRO THR ARG          
SEQRES  17 B  319  PRO VAL ILE VAL SER PRO ALA ASN GLU THR MET GLU VAL          
SEQRES  18 B  319  ASP LEU GLY SER GLN ILE GLN LEU ILE CYS ASN VAL THR          
SEQRES  19 B  319  GLY GLN LEU SER ASP ILE ALA TYR TRP LYS TRP ASN GLY          
SEQRES  20 B  319  SER VAL ILE ASP GLU ASP ASP PRO VAL LEU GLY GLU ASP          
SEQRES  21 B  319  TYR TYR SER VAL GLU ASN PRO ALA ASN LYS ARG ARG SER          
SEQRES  22 B  319  THR LEU ILE THR VAL LEU ASN ILE SER GLU ILE GLU SER          
SEQRES  23 B  319  ARG PHE TYR LYS HIS PRO PHE THR CYS PHE ALA LYS ASN          
SEQRES  24 B  319  THR HIS GLY ILE ASP ALA ALA TYR ILE GLN LEU ILE TYR          
SEQRES  25 B  319  PRO VAL THR ASN PHE GLN LYS                                  
MODRES 4GAF ASN B  216  ASN  GLYCOSYLATION SITE                                 
MODRES 4GAF ASN B  232  ASN  GLYCOSYLATION SITE                                 
MODRES 4GAF ASN B  246  ASN  GLYCOSYLATION SITE                                 
MODRES 4GAF ASN B  176  ASN  GLYCOSYLATION SITE                                 
HET    NAG  B 501      14                                                       
HET    NAG  B 502      14                                                       
HET    NAG  B 503      14                                                       
HET    NAG  B 504      14                                                       
HET     NA  B 505       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      NA SODIUM ION                                                       
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   7   NA    NA 1+                                                        
FORMUL   8  HOH   *209(H2 O)                                                    
HELIX    1   1 GLN A   31  GLU A   38  5                                   8    
HELIX    2   2 GLU A   95  PHE A   98  5                                   4    
HELIX    3   3 LYS B   70  SER B   74  5                                   5    
HELIX    4   4 ASN B  106  GLN B  108  5                                   3    
HELIX    5   5 MET B  128  LYS B  132  5                                   5    
HELIX    6   6 ALA B  170  ARG B  174  5                                   5    
HELIX    7   7 ASN B  269  ARG B  272  5                                   4    
HELIX    8   8 GLU B  285  LYS B  290  5                                   6    
SHEET    1   A 7 SER A   5  ASP A  12  0                                        
SHEET    2   A 7 PHE A  41  SER A  44 -1  O  MET A  43   N  LEU A   6           
SHEET    3   A 7 LYS A  54  LEU A  61 -1  O  GLY A  60   N  SER A  42           
SHEET    4   A 7 PHE A 100  ILE A 105 -1  O  PHE A 100   N  VAL A  57           
SHEET    5   A 7 LYS A 108  SER A 113 -1  O  GLU A 112   N  ASN A 101           
SHEET    6   A 7 PHE A 146  PHE A 150 -1  O  PHE A 146   N  LEU A 109           
SHEET    7   A 7 SER A   5  ASP A  12 -1  N  TRP A  11   O  TYR A 147           
SHEET    1   B 3 THR A  17  ARG A  21  0                                        
SHEET    2   B 3 GLN A  24  GLY A  28 -1  O  VAL A  26   N  TYR A  19           
SHEET    3   B 3 GLN A 129  PRO A 130 -1  O  GLN A 129   N  ALA A  27           
SHEET    1   C 2 LEU A  66  LYS A  73  0                                        
SHEET    2   C 2 LYS A  76  SER A  83 -1  O  THR A  78   N  VAL A  71           
SHEET    1   D 2 PHE A 120  CYS A 122  0                                        
SHEET    2   D 2 SER A 132  THR A 134 -1  O  SER A 132   N  CYS A 122           
SHEET    1   E 3 LYS B   7  GLU B  10  0                                        
SHEET    2   E 3 LEU B  88  VAL B  97  1  O  LYS B  91   N  ARG B   9           
SHEET    3   E 3 LEU B  15  SER B  18  1  N  SER B  17   O  LYS B  95           
SHEET    1   F 4 LYS B   7  GLU B  10  0                                        
SHEET    2   F 4 LEU B  88  VAL B  97  1  O  LYS B  91   N  ARG B   9           
SHEET    3   F 4 GLY B  75  VAL B  80 -1  N  TYR B  77   O  ILE B  92           
SHEET    4   F 4 THR B  39  LYS B  42 -1  N  TYR B  41   O  TYR B  78           
SHEET    1   G 3 ASP B  23  PRO B  26  0                                        
SHEET    2   G 3 LYS B  63  PHE B  66 -1  O  PHE B  66   N  ASP B  23           
SHEET    3   G 3 ILE B  57  HIS B  60 -1  N  HIS B  58   O  TRP B  65           
SHEET    1   H 5 ILE B 110  PRO B 116  0                                        
SHEET    2   H 5 LYS B 188  LEU B 201  1  O  GLU B 197   N  GLN B 113           
SHEET    3   H 5 GLY B 175  TYR B 185 -1  N  TYR B 183   O  TYR B 190           
SHEET    4   H 5 GLN B 142  LYS B 145 -1  N  GLN B 142   O  HIS B 180           
SHEET    5   H 5 LYS B 148  PRO B 149 -1  O  LYS B 148   N  LYS B 145           
SHEET    1   I 3 GLY B 121  VAL B 124  0                                        
SHEET    2   I 3 ARG B 163  VAL B 166 -1  O  VAL B 166   N  GLY B 121           
SHEET    3   I 3 PHE B 157  VAL B 160 -1  N  SER B 158   O  ILE B 165           
SHEET    1   J 4 VAL B 210  SER B 213  0                                        
SHEET    2   J 4 ILE B 227  GLY B 235 -1  O  ASN B 232   N  VAL B 212           
SHEET    3   J 4 SER B 273  ILE B 281 -1  O  LEU B 275   N  VAL B 233           
SHEET    4   J 4 LEU B 257  VAL B 264 -1  N  GLY B 258   O  ASN B 280           
SHEET    1   K 5 GLU B 217  GLU B 220  0                                        
SHEET    2   K 5 GLY B 302  ILE B 311  1  O  GLN B 309   N  GLU B 217           
SHEET    3   K 5 PHE B 293  ASN B 299 -1  N  PHE B 293   O  ILE B 308           
SHEET    4   K 5 ILE B 240  TRP B 245 -1  N  TYR B 242   O  PHE B 296           
SHEET    5   K 5 SER B 248  VAL B 249 -1  O  SER B 248   N  TRP B 245           
SSBOND   1 CYS B    6    CYS B   87                          1555   1555  2.04  
SSBOND   2 CYS B   27    CYS B   79                          1555   1555  2.05  
SSBOND   3 CYS B  104    CYS B  147                          1555   1555  2.14  
SSBOND   4 CYS B  125    CYS B  179                          1555   1555  2.09  
SSBOND   5 CYS B  231    CYS B  295                          1555   1555  1.94  
LINK         ND2 ASN B 176                 C1  NAG B 503     1555   1555  1.45  
LINK         ND2 ASN B 216                 C1  NAG B 502     1555   1555  1.43  
LINK         ND2 ASN B 232                 C1  NAG B 501     1555   1555  1.44  
LINK         ND2 ASN B 246                 C1  NAG B 504     1555   1555  1.44  
LINK         OG  SER B  18                NA    NA B 505     1555   1555  2.55  
LINK         OE1 GLU B  21                NA    NA B 505     1555   1555  2.58  
LINK         O   THR B 193                NA    NA B 505     1555   1555  2.32  
LINK         OG1 THR B 193                NA    NA B 505     1555   1555  2.56  
LINK        NA    NA B 505                 O   HOH B 627     1555   1555  2.34  
LINK        NA    NA B 505                 O   HOH B 642     1555   1555  2.33  
CISPEP   1 TYR A   89    PRO A   90          0        -0.10                     
CISPEP   2 VAL B   67    PRO B   68          0        -7.76                     
CISPEP   3 GLU B  134    ASN B  135          0        15.92                     
CISPEP   4 SER B  213    PRO B  214          0        -0.51                     
CRYST1   60.350  149.270  126.170  90.00  90.00  90.00 C 2 2 21      8          
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      0.016570  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006699  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007926        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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