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Database: PDB
Entry: 1P9M
LinkDB: 1P9M
Original site: 1P9M 
HEADER    SIGNALING PROTEIN/CYTOKINE              12-MAY-03   1P9M              
TITLE     CRYSTAL STRUCTURE OF THE HEXAMERIC HUMAN IL-6/IL-6 ALPHA              
TITLE    2 RECEPTOR/GP130 COMPLEX                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-6 RECEPTOR BETA CHAIN;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAINS D1 - D3;                             
COMPND   5 SYNONYM: IL-6R-BETA, INTERLEUKIN 6 SIGNAL TRANSDUCER, MEMBRANE       
COMPND   6 GLYCOPROTEIN 130, GP130, ONCOSTATIN M RECEPTOR, CDW130, CD130        
COMPND   7 ANTIGEN;                                                             
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: INTERLEUKIN-6;                                             
COMPND  11 CHAIN: B;                                                            
COMPND  12 SYNONYM: IL-6, B-CELL STIMULATORY FACTOR 2, BSF-2, INTERFERON BETA-2,
COMPND  13 HYBRIDOMA GROWTH FACTOR;                                             
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: INTERLEUKIN-6 RECEPTOR ALPHA CHAIN;                        
COMPND  17 CHAIN: C;                                                            
COMPND  18 FRAGMENT: EXTRACELLULAR DOMAINS D2 - D3;                             
COMPND  19 SYNONYM: IL-6R-ALPHA, IL-6R 1, CD126 ANTIGEN;                        
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: IL6ST;                                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PACGP67A;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: IL6 OR IFNB2;                                                  
SOURCE  16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  17 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PACGP67A;                                 
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 GENE: IL6R;                                                          
SOURCE  26 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  27 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PACGP67A                                  
KEYWDS    IG DOMAIN, FOUR HELIX BUNDLE, CYTOKINE, INTERLEUKIN-6, GP130,         
KEYWDS   2 SIGNALING PROTEIN-CYTOKINE COMPLEX                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.J.BOULANGER,D.C.CHOW,E.E.BREVNOVA,K.C.GARCIA                        
REVDAT   4   13-JUL-11 1P9M    1       VERSN                                    
REVDAT   3   24-FEB-09 1P9M    1       VERSN                                    
REVDAT   2   08-JUL-03 1P9M    1       REMARK COMPND SEQRES                     
REVDAT   1   01-JUL-03 1P9M    0                                                
JRNL        AUTH   M.J.BOULANGER,D.C.CHOW,E.E.BREVNOVA,K.C.GARCIA               
JRNL        TITL   HEXAMERIC STRUCTURE AND ASSEMBLY OF THE INTERLEUKIN-6/IL-6   
JRNL        TITL 2 ALPHA-RECEPTOR/GP130 COMPLEX                                 
JRNL        REF    SCIENCE                       V. 300  2101 2003              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   12829785                                                     
JRNL        DOI    10.1126/SCIENCE.1083901                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 15767                          
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 SET) : 0.282                           
REMARK   3   FREE R VALUE                     : 0.334                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1237                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.88                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2396                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4030                       
REMARK   3   BIN FREE R VALUE                    : 0.4870                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 185                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.036                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5322                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 117.10                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.77000                                              
REMARK   3    B22 (A**2) : 2.77000                                              
REMARK   3    B33 (A**2) : -5.55000                                             
REMARK   3    B12 (A**2) : 30.66000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.48                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.94                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.65                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 1.29                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.00                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.03                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : GROUP                                     
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.12                                                 
REMARK   3   BSOL        : 10.00                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER_REP.TOP                                  
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : &_1_TOPOLOGY_INFILE_4                          
REMARK   3  TOPOLOGY FILE  5   : &_1_TOPOLOGY_INFILE_5                          
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1P9M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAY-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019180.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-SEP-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15861                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.850                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1ALU                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM FORMATE, SODIUM ACETATE, PH       
REMARK 280  4.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000      139.90000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       80.77130            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       32.23333            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000      139.90000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       80.77130            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       32.23333            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000      139.90000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       80.77130            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       32.23333            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000      139.90000            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       80.77130            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       32.23333            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000      139.90000            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       80.77130            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       32.23333            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000      139.90000            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       80.77130            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       32.23333            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000      161.54261            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       64.46667            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000      161.54261            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       64.46667            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000      161.54261            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       64.46667            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000      161.54261            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       64.46667            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000      161.54261            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000       64.46667            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000      161.54261            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000       64.46667            
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 13030 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 65930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000     -279.80000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000      161.54261            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       64.46667            
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     GLU A     1                                                      
REMARK 465     ALA B    -1                                                      
REMARK 465     PRO B     0                                                      
REMARK 465     PRO B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     ASP B     7                                                      
REMARK 465     SER B     8                                                      
REMARK 465     LYS B     9                                                      
REMARK 465     ASP B    10                                                      
REMARK 465     VAL B    11                                                      
REMARK 465     ALA B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     PRO B    14                                                      
REMARK 465     HIS B    15                                                      
REMARK 465     ARG B    16                                                      
REMARK 465     GLN B    17                                                      
REMARK 465     PRO B    18                                                      
REMARK 465     SER B    47                                                      
REMARK 465     ASN B    48                                                      
REMARK 465     MET B    49                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     ASN C  136                                                       
REMARK 475     SER C  137                                                       
REMARK 475     PRO C  138                                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     TYR A    8   CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 480     GLN A   17   CG   CD   OE1  NE2                                  
REMARK 480     LYS A   29   CG   CD   CE   NZ                                   
REMARK 480     TYR A   35   CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 480     HIS A   49   CG   ND1  CD2  CE1  NE2                             
REMARK 480     ARG A   62   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ILE A   77   CG1  CG2  CD1                                       
REMARK 480     GLU A   90   CG   CD   OE1  OE2                                  
REMARK 480     GLN A   91   CG   CD   OE1  NE2                                  
REMARK 480     LYS A  108   CG   CD   CE   NZ                                   
REMARK 480     HIS A  145   CG   ND1  CD2  CE1  NE2                             
REMARK 480     LYS A  146   CG   CD   CE   NZ                                   
REMARK 480     LYS A  153   CG   CD   CE   NZ                                   
REMARK 480     ARG A  154   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLU A  179   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  184   CG   CD   CE   NZ                                   
REMARK 480     LYS A  199   CG   CD   CE   NZ                                   
REMARK 480     GLU A  212   CG   CD   OE1  OE2                                  
REMARK 480     GLU A  272   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  285   CG   CD   CE   NZ                                   
REMARK 480     ARG B   40   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS B   46   CG   CD   CE   NZ                                   
REMARK 480     LYS B   54   CG   CD   CE   NZ                                   
REMARK 480     GLU B   55   CG   CD   OE1  OE2                                  
REMARK 480     LEU B   57   CG   CD1  CD2                                       
REMARK 480     GLU B   59   CG   CD   OE1                                       
REMARK 480     ASN B   60   CG   OD1  ND2                                       
REMARK 480     ASN B   61   CG   OD1  ND2                                       
REMARK 480     LEU B   62   CG   CD1  CD2                                       
REMARK 480     ASN B   63   CG   OD1  ND2                                       
REMARK 480     LEU B   64   CG   CD1  CD2                                       
REMARK 480     LYS B   66   CG   CD   CE   NZ                                   
REMARK 480     GLU B   69   CB   CG   CD   OE1  OE2                             
REMARK 480     GLU B   93   CG   CD   OE1  OE2                                  
REMARK 480     PHE B  105   CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 480     GLU B  106   CG   CD   OE1  OE2                                  
REMARK 480     GLU B  109   CG   CD   OE1  OE2                                  
REMARK 480     GLU B  110   CB   CG   CD   OE1  OE2                             
REMARK 480     GLN B  111   CG   CD   OE1  NE2                                  
REMARK 480     ARG B  113   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     MET B  117   CG   SD   CE                                        
REMARK 480     LYS B  120   CG   CD   CE   NZ                                   
REMARK 480     LYS B  128   CG   CD   CE   NZ                                   
REMARK 480     LYS B  131   CG   CD   CE   NZ                                   
REMARK 480     ASN B  132   CG   OD1  ND2                                       
REMARK 480     GLN B  152   CG   CD   OE1  NE2                                  
REMARK 480     LEU B  158   CG   CD1  CD2                                       
REMARK 480     MET B  161   CG   SD                                             
REMARK 480     LYS C  244   CD   CE   NZ                                        
REMARK 480     LYS C  252   CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B  95   CD    GLU B  95   OE2     0.076                       
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    TRP C 249   CB  -  CA  -  C   ANGL. DEV. = -15.5 DEGREES          
REMARK 500    TRP C 249   CG  -  CD2 -  CE3 ANGL. DEV. =   5.4 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    CYS A   6        9.44    -63.28                                   
REMARK 500    GLU A  12      -83.57    -60.06                                   
REMARK 500    LEU A  18      -97.80    -39.70                                   
REMARK 500    HIS A  19       41.11    -70.27                                   
REMARK 500    GLU A  30      -92.54    -64.39                                   
REMARK 500    LYS A  31      -63.88    -11.88                                   
REMARK 500    PHE A  36       -8.46   -144.23                                   
REMARK 500    HIS A  37      -12.46     69.51                                   
REMARK 500    ALA A  40       -1.29    -54.31                                   
REMARK 500    ASN A  48      -48.10   -135.99                                   
REMARK 500    HIS A  49      -10.05   -162.63                                   
REMARK 500    THR A  51      109.37    -48.38                                   
REMARK 500    ILE A  60     -106.62    -85.44                                   
REMARK 500    THR A  63       10.90   -142.86                                   
REMARK 500    PHE A  86       47.20     36.58                                   
REMARK 500    GLN A  88       -4.26   -169.99                                   
REMARK 500    GLU A  90       49.29    -78.61                                   
REMARK 500    VAL A  93      -68.94   -109.07                                   
REMARK 500    ILE A 113      149.48   -175.70                                   
REMARK 500    TRP A 124     -174.10    176.97                                   
REMARK 500    ALA A 143      -87.59     11.56                                   
REMARK 500    PRO A 157      -75.05    -66.95                                   
REMARK 500    VAL A 162     -178.32    -52.58                                   
REMARK 500    PHE A 169       40.49     74.42                                   
REMARK 500    ASN A 171       81.15    -67.64                                   
REMARK 500    ASN A 180      142.42   -173.86                                   
REMARK 500    PRO A 194      -36.86    -33.71                                   
REMARK 500    SER A 211      -56.67     -7.36                                   
REMARK 500    GLU A 213       64.98    -67.91                                   
REMARK 500    SER A 216       34.90    -74.20                                   
REMARK 500    TRP A 247       97.98    -56.96                                   
REMARK 500    PRO A 251      120.62    -31.90                                   
REMARK 500    THR A 255       23.07   -153.74                                   
REMARK 500    ASP A 266       87.19     42.38                                   
REMARK 500    PRO A 269     -120.74    -25.45                                   
REMARK 500    PHE A 270       84.57    -54.40                                   
REMARK 500    GLU A 272       70.81   -106.33                                   
REMARK 500    ASP A 283       10.66    -66.75                                   
REMARK 500    ILE A 298     -151.90    -74.55                                   
REMARK 500    ARG B  24       21.63    -69.01                                   
REMARK 500    ILE B  25      -57.91   -139.53                                   
REMARK 500    ASP B  26       -8.74    -58.69                                   
REMARK 500    ARG B  40      -72.01    -72.43                                   
REMARK 500    ASN B  45      -11.55   -164.25                                   
REMARK 500    GLU B  51      -95.06    -48.08                                   
REMARK 500    GLU B  55       52.02   -100.72                                   
REMARK 500    ALA B  56      -89.60    -55.90                                   
REMARK 500    LEU B  57       73.12     67.04                                   
REMARK 500    ALA B  58     -133.87   -111.61                                   
REMARK 500    GLU B  59      -27.94   -151.15                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      99 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1P9M A    1   299  UNP    P40189   IL6RB_HUMAN     23    321             
DBREF  1P9M B    1   184  UNP    P05231   IL6_HUMAN       29    212             
DBREF  1P9M C   96   296  UNP    P08887   IL6RA_HUMAN    115    315             
SEQADV 1P9M ALA B   -1  UNP  P05231              CLONING ARTIFACT               
SEQADV 1P9M PRO B    0  UNP  P05231              CLONING ARTIFACT               
SEQRES   1 A  299  GLU LEU LEU ASP PRO CYS GLY TYR ILE SER PRO GLU SER          
SEQRES   2 A  299  PRO VAL VAL GLN LEU HIS SER ASN PHE THR ALA VAL CYS          
SEQRES   3 A  299  VAL LEU LYS GLU LYS CYS MET ASP TYR PHE HIS VAL ASN          
SEQRES   4 A  299  ALA ASN TYR ILE VAL TRP LYS THR ASN HIS PHE THR ILE          
SEQRES   5 A  299  PRO LYS GLU GLN TYR THR ILE ILE ASN ARG THR ALA SER          
SEQRES   6 A  299  SER VAL THR PHE THR ASP ILE ALA SER LEU ASN ILE GLN          
SEQRES   7 A  299  LEU THR CYS ASN ILE LEU THR PHE GLY GLN LEU GLU GLN          
SEQRES   8 A  299  ASN VAL TYR GLY ILE THR ILE ILE SER GLY LEU PRO PRO          
SEQRES   9 A  299  GLU LYS PRO LYS ASN LEU SER CYS ILE VAL ASN GLU GLY          
SEQRES  10 A  299  LYS LYS MET ARG CYS GLU TRP ASP GLY GLY ARG GLU THR          
SEQRES  11 A  299  HIS LEU GLU THR ASN PHE THR LEU LYS SER GLU TRP ALA          
SEQRES  12 A  299  THR HIS LYS PHE ALA ASP CYS LYS ALA LYS ARG ASP THR          
SEQRES  13 A  299  PRO THR SER CYS THR VAL ASP TYR SER THR VAL TYR PHE          
SEQRES  14 A  299  VAL ASN ILE GLU VAL TRP VAL GLU ALA GLU ASN ALA LEU          
SEQRES  15 A  299  GLY LYS VAL THR SER ASP HIS ILE ASN PHE ASP PRO VAL          
SEQRES  16 A  299  TYR LYS VAL LYS PRO ASN PRO PRO HIS ASN LEU SER VAL          
SEQRES  17 A  299  ILE ASN SER GLU GLU LEU SER SER ILE LEU LYS LEU THR          
SEQRES  18 A  299  TRP THR ASN PRO SER ILE LYS SER VAL ILE ILE LEU LYS          
SEQRES  19 A  299  TYR ASN ILE GLN TYR ARG THR LYS ASP ALA SER THR TRP          
SEQRES  20 A  299  SER GLN ILE PRO PRO GLU ASP THR ALA SER THR ARG SER          
SEQRES  21 A  299  SER PHE THR VAL GLN ASP LEU LYS PRO PHE THR GLU TYR          
SEQRES  22 A  299  VAL PHE ARG ILE ARG CYS MET LYS GLU ASP GLY LYS GLY          
SEQRES  23 A  299  TYR TRP SER ASP TRP SER GLU GLU ALA SER GLY ILE THR          
SEQRES   1 B  186  ALA PRO PRO VAL PRO PRO GLY GLU ASP SER LYS ASP VAL          
SEQRES   2 B  186  ALA ALA PRO HIS ARG GLN PRO LEU THR SER SER GLU ARG          
SEQRES   3 B  186  ILE ASP LYS GLN ILE ARG TYR ILE LEU ASP GLY ILE SER          
SEQRES   4 B  186  ALA LEU ARG LYS GLU THR CYS ASN LYS SER ASN MET CYS          
SEQRES   5 B  186  GLU SER SER LYS GLU ALA LEU ALA GLU ASN ASN LEU ASN          
SEQRES   6 B  186  LEU PRO LYS MET ALA GLU LYS ASP GLY CYS PHE GLN SER          
SEQRES   7 B  186  GLY PHE ASN GLU GLU THR CYS LEU VAL LYS ILE ILE THR          
SEQRES   8 B  186  GLY LEU LEU GLU PHE GLU VAL TYR LEU GLU TYR LEU GLN          
SEQRES   9 B  186  ASN ARG PHE GLU SER SER GLU GLU GLN ALA ARG ALA VAL          
SEQRES  10 B  186  GLN MET SER THR LYS VAL LEU ILE GLN PHE LEU GLN LYS          
SEQRES  11 B  186  LYS ALA LYS ASN LEU ASP ALA ILE THR THR PRO ASP PRO          
SEQRES  12 B  186  THR THR ASN ALA SER LEU LEU THR LYS LEU GLN ALA GLN          
SEQRES  13 B  186  ASN GLN TRP LEU GLN ASP MET THR THR HIS LEU ILE LEU          
SEQRES  14 B  186  ARG SER PHE LYS GLU PHE LEU GLN SER SER LEU ARG ALA          
SEQRES  15 B  186  LEU ARG GLN MET                                              
SEQRES   1 C  201  GLU GLU PRO GLN LEU SER CYS PHE ARG LYS SER PRO LEU          
SEQRES   2 C  201  SER ASN VAL VAL CYS GLU TRP GLY PRO ARG SER THR PRO          
SEQRES   3 C  201  SER LEU THR THR LYS ALA VAL LEU LEU VAL ARG LYS PHE          
SEQRES   4 C  201  GLN ASN SER PRO ALA GLU ASP PHE GLN GLU PRO CYS GLN          
SEQRES   5 C  201  TYR SER GLN GLU SER GLN LYS PHE SER CYS GLN LEU ALA          
SEQRES   6 C  201  VAL PRO GLU GLY ASP SER SER PHE TYR ILE VAL SER MET          
SEQRES   7 C  201  CYS VAL ALA SER SER VAL GLY SER LYS PHE SER LYS THR          
SEQRES   8 C  201  GLN THR PHE GLN GLY CYS GLY ILE LEU GLN PRO ASP PRO          
SEQRES   9 C  201  PRO ALA ASN ILE THR VAL THR ALA VAL ALA ARG ASN PRO          
SEQRES  10 C  201  ARG TRP LEU SER VAL THR TRP GLN ASP PRO HIS SER TRP          
SEQRES  11 C  201  ASN SER SER PHE TYR ARG LEU ARG PHE GLU LEU ARG TYR          
SEQRES  12 C  201  ARG ALA GLU ARG SER LYS THR PHE THR THR TRP MET VAL          
SEQRES  13 C  201  LYS ASP LEU GLN HIS HIS CYS VAL ILE HIS ASP ALA TRP          
SEQRES  14 C  201  SER GLY LEU ARG HIS VAL VAL GLN LEU ARG ALA GLN GLU          
SEQRES  15 C  201  GLU PHE GLY GLN GLY GLU TRP SER GLU TRP SER PRO GLU          
SEQRES  16 C  201  ALA MET GLY THR PRO TRP                                      
HELIX    1   1 LYS A   29  PHE A   36  1                                   8    
HELIX    2   2 SER B   22  LYS B   27  1                                   6    
HELIX    3   3 LYS B   27  CYS B   44  1                                  18    
HELIX    4   4 ALA B   68  GLY B   72  5                                   5    
HELIX    5   5 ASN B   79  GLN B  102  1                                  24    
HELIX    6   6 SER B  108  LYS B  129  1                                  22    
HELIX    7   7 THR B  142  GLN B  152  1                                  11    
HELIX    8   8 ASN B  155  GLN B  183  1                                  29    
SHEET    1   A 4 GLY A   7  SER A  10  0                                        
SHEET    2   A 4 VAL A  25  LEU A  28 -1  O  VAL A  27   N  TYR A   8           
SHEET    3   A 4 ALA A  64  SER A  66 -1  O  SER A  65   N  CYS A  26           
SHEET    4   A 4 THR A  58  ILE A  59 -1  N  THR A  58   O  SER A  66           
SHEET    1   B 3 VAL A  44  LYS A  46  0                                        
SHEET    2   B 3 THR A  80  ASN A  82 -1  O  ASN A  82   N  VAL A  44           
SHEET    3   B 3 ASN A  92  GLY A  95 -1  O  VAL A  93   N  CYS A  81           
SHEET    1   C 3 LYS A 108  SER A 111  0                                        
SHEET    2   C 3 ARG A 121  ASP A 125 -1  O  ASP A 125   N  LYS A 108           
SHEET    3   C 3 CYS A 160  THR A 161 -1  O  CYS A 160   N  CYS A 122           
SHEET    1   D 2 VAL A 114  ASN A 115  0                                        
SHEET    2   D 2 VAL A 198  LYS A 199  1  O  LYS A 199   N  VAL A 114           
SHEET    1   E 4 HIS A 145  LYS A 146  0                                        
SHEET    2   E 4 ASN A 135  TRP A 142 -1  N  TRP A 142   O  HIS A 145           
SHEET    3   E 4 ILE A 172  GLU A 179 -1  O  GLU A 173   N  GLU A 141           
SHEET    4   E 4 VAL A 185  THR A 186 -1  O  VAL A 185   N  ALA A 178           
SHEET    1   F 4 CYS A 150  LYS A 151  0                                        
SHEET    2   F 4 ASN A 135  TRP A 142 -1  N  LEU A 138   O  CYS A 150           
SHEET    3   F 4 ILE A 172  GLU A 179 -1  O  GLU A 173   N  GLU A 141           
SHEET    4   F 4 ILE A 190  PHE A 192 -1  O  PHE A 192   N  ILE A 172           
SHEET    1   G 3 SER A 207  ILE A 209  0                                        
SHEET    2   G 3 LEU A 218  THR A 221 -1  O  LYS A 219   N  ILE A 209           
SHEET    3   G 3 SER A 261  VAL A 264 -1  O  PHE A 262   N  LEU A 220           
SHEET    1   H 4 SER A 248  GLN A 249  0                                        
SHEET    2   H 4 LEU A 233  THR A 241 -1  N  TYR A 239   O  SER A 248           
SHEET    3   H 4 TYR A 273  LYS A 281 -1  O  VAL A 274   N  ARG A 240           
SHEET    4   H 4 ALA A 295  GLY A 297 -1  O  ALA A 295   N  PHE A 275           
SHEET    1   I 5 LYS C 154  CYS C 157  0                                        
SHEET    2   I 5 GLU C 140  SER C 149 -1  N  GLN C 147   O  SER C 156           
SHEET    3   I 5 VAL C 128  LYS C 133 -1  N  LYS C 133   O  GLU C 140           
SHEET    4   I 5 TYR C 169  ALA C 176 -1  O  SER C 172   N  LEU C 130           
SHEET    5   I 5 SER C 181  LYS C 182 -1  O  LYS C 182   N  VAL C 175           
SHEET    1   J 5 LYS C 154  CYS C 157  0                                        
SHEET    2   J 5 GLU C 140  SER C 149 -1  N  GLN C 147   O  SER C 156           
SHEET    3   J 5 VAL C 128  LYS C 133 -1  N  LYS C 133   O  GLU C 140           
SHEET    4   J 5 TYR C 169  ALA C 176 -1  O  SER C 172   N  LEU C 130           
SHEET    5   J 5 GLN C 187  PHE C 189 -1  O  GLN C 187   N  VAL C 171           
SHEET    1   K 3 ALA C 201  THR C 206  0                                        
SHEET    2   K 3 LEU C 215  GLN C 220 -1  O  SER C 216   N  THR C 206           
SHEET    3   K 3 CYS C 258  ILE C 260 -1  O  ILE C 260   N  LEU C 215           
SHEET    1   L 3 THR C 247  MET C 250  0                                        
SHEET    2   L 3 LEU C 232  ALA C 240 -1  N  TYR C 238   O  THR C 247           
SHEET    3   L 3 ALA C 275  GLU C 277 -1  O  GLN C 276   N  ARG C 233           
SHEET    1   M 4 THR C 247  MET C 250  0                                        
SHEET    2   M 4 LEU C 232  ALA C 240 -1  N  TYR C 238   O  THR C 247           
SHEET    3   M 4 HIS C 269  GLN C 272 -1  O  VAL C 270   N  ARG C 239           
SHEET    4   M 4 ALA C 291  GLY C 293 -1  O  GLY C 293   N  HIS C 269           
SSBOND   1 CYS A    6    CYS A   32                          1555   1555  2.03  
SSBOND   2 CYS A   26    CYS A   81                          1555   1555  2.03  
SSBOND   3 CYS A  112    CYS A  122                          1555   1555  2.03  
SSBOND   4 CYS A  150    CYS A  160                          1555   1555  2.03  
SSBOND   5 CYS B   44    CYS B   50                          1555   1555  2.03  
SSBOND   6 CYS B   73    CYS B   83                          1555   1555  2.03  
SSBOND   7 CYS C  102    CYS C  113                          1555   1555  2.03  
SSBOND   8 CYS C  146    CYS C  157                          1555   1555  2.03  
CISPEP   1 SER A   10    PRO A   11          0         0.04                     
CRYST1  279.800  279.800   96.700  90.00  90.00 120.00 H 3 2        18          
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      0.003574  0.002063  0.000000        0.00000                         
SCALE2      0.000000  0.004127  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010341        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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