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Database: PDB
Entry: 4DEP
LinkDB: 4DEP
Original site: 4DEP 
HEADER    IMMUNE SYSTEM                           21-JAN-12   4DEP              
TITLE     STRUCTURE OF THE IL-1B SIGNALING COMPLEX                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-1 BETA;                                        
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 117-269;                                      
COMPND   5 SYNONYM: IL-1 BETA, CATABOLIN;                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: INTERLEUKIN-1 RECEPTOR TYPE 1;                             
COMPND   9 CHAIN: B, E;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 18-336;                                       
COMPND  11 SYNONYM: IL-1R-1, IL-1RT-1, IL-1RT1, CD121 ANTIGEN-LIKE FAMILY MEMBER
COMPND  12 A, INTERLEUKIN-1 RECEPTOR ALPHA, IL-1R-ALPHA, INTERLEUKIN-1 RECEPTOR 
COMPND  13 TYPE I, P80;                                                         
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: INTERLEUKIN-1 RECEPTOR ACCESSORY PROTEIN;                  
COMPND  17 CHAIN: C, F;                                                         
COMPND  18 FRAGMENT: UNP RESIDUES 21-367;                                       
COMPND  19 SYNONYM: IL-1 RECEPTOR ACCESSORY PROTEIN, IL-1RACP, INTERLEUKIN-1    
COMPND  20 RECEPTOR 3, IL-1R-3, IL-1R3;                                         
COMPND  21 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: IL-1B, IL1B, IL1F2;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1;                                
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: IL-1RI, IL1R, IL1R1, IL1RA, IL1RT1;                            
SOURCE  14 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  16 MOL_ID: 3;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 GENE: C3ORF13, IL-1RACP, IL1R3, IL1RAP;                              
SOURCE  21 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    B-TREFOIL, IMMUNOGLOBULIN, IMMUNE SYSTEM, EXTRACELLULAR               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.THOMAS,K.C.GARCIA                                                   
REVDAT   3   29-JUL-20 4DEP    1       COMPND REMARK SEQADV HETNAM              
REVDAT   3 2                   1       LINK   SITE                              
REVDAT   2   18-APR-12 4DEP    1       JRNL                                     
REVDAT   1   21-MAR-12 4DEP    0                                                
JRNL        AUTH   C.THOMAS,J.F.BAZAN,K.C.GARCIA                                
JRNL        TITL   STRUCTURE OF THE ACTIVATING IL-1 RECEPTOR SIGNALING COMPLEX. 
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  19   455 2012              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   22426547                                                     
JRNL        DOI    10.1038/NSMB.2260                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.2_869)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.70                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 41079                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2055                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 19.7051 -  7.5113    0.94     2561   136  0.2200 0.2451        
REMARK   3     2  7.5113 -  6.0178    0.99     2626   138  0.2273 0.2548        
REMARK   3     3  6.0178 -  5.2738    0.99     2632   138  0.2052 0.2507        
REMARK   3     4  5.2738 -  4.7992    1.00     2614   138  0.1813 0.2556        
REMARK   3     5  4.7992 -  4.4595    1.00     2604   137  0.1638 0.2423        
REMARK   3     6  4.4595 -  4.1992    1.00     2612   137  0.1765 0.2169        
REMARK   3     7  4.1992 -  3.9908    1.00     2643   140  0.1927 0.2647        
REMARK   3     8  3.9908 -  3.8183    1.00     2567   135  0.2140 0.3270        
REMARK   3     9  3.8183 -  3.6723    1.00     2573   135  0.2202 0.3274        
REMARK   3    10  3.6723 -  3.5464    1.00     2631   139  0.2178 0.3141        
REMARK   3    11  3.5464 -  3.4361    1.00     2597   136  0.2234 0.2690        
REMARK   3    12  3.4361 -  3.3383    1.00     2598   137  0.2364 0.3209        
REMARK   3    13  3.3383 -  3.2508    1.00     2584   136  0.2426 0.3490        
REMARK   3    14  3.2508 -  3.1719    1.00     2591   136  0.2637 0.3258        
REMARK   3    15  3.1719 -  3.1000    1.00     2591   137  0.2911 0.3722        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.30                                          
REMARK   3   B_SOL              : 21.56                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.950            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.070           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.017          11971                                  
REMARK   3   ANGLE     :  1.523          16284                                  
REMARK   3   CHIRALITY :  0.092           1865                                  
REMARK   3   PLANARITY :  0.010           2070                                  
REMARK   3   DIHEDRAL  : 19.462           4281                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4DEP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000070235.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-SEP-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
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) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC Q315R                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41079                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 1.700                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
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   (%): 59.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 5000 MME, 100 MM MES PH 6.5,     
REMARK 280  12% 1-PROPANOL, PROTEIN AT 12 MG/ML, VAPOR DIFFUSION, HANGING       
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       32.95000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     LEU A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     SER A   152                                                      
REMARK 465     SER A   153                                                      
REMARK 465     GLU B    -1                                                      
REMARK 465     PRO B     0                                                      
REMARK 465     LEU B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     CYS B     6                                                      
REMARK 465     HIS B    34                                                      
REMARK 465     LYS B    35                                                      
REMARK 465     ASP B    44                                                      
REMARK 465     SER B    45                                                      
REMARK 465     LYS B    46                                                      
REMARK 465     THR B    47                                                      
REMARK 465     GLY B   224                                                      
REMARK 465     SER B   225                                                      
REMARK 465     ILE B   311                                                      
REMARK 465     TYR B   312                                                      
REMARK 465     PRO B   313                                                      
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 465     GLU C    -1                                                      
REMARK 465     PRO C     0                                                      
REMARK 465     SER C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     SER C   227                                                      
REMARK 465     PRO C   228                                                      
REMARK 465     ASN C   229                                                      
REMARK 465     ASP C   230                                                      
REMARK 465     HIS C   231                                                      
REMARK 465     VAL C   232                                                      
REMARK 465     VAL C   233                                                      
REMARK 465     TYR C   234                                                      
REMARK 465     GLU C   235                                                      
REMARK 465     LYS C   236                                                      
REMARK 465     GLU C   237                                                      
REMARK 465     PRO C   238                                                      
REMARK 465     GLY C   239                                                      
REMARK 465     GLU C   240                                                      
REMARK 465     GLU C   241                                                      
REMARK 465     LEU C   242                                                      
REMARK 465     LYS C   268                                                      
REMARK 465     PRO C   269                                                      
REMARK 465     ASP C   270                                                      
REMARK 465     ASP C   271                                                      
REMARK 465     ILE C   272                                                      
REMARK 465     THR C   273                                                      
REMARK 465     ILE C   274                                                      
REMARK 465     ASP C   275                                                      
REMARK 465     SER C   297                                                      
REMARK 465     ILE C   298                                                      
REMARK 465     LYS C   299                                                      
REMARK 465     LYS C   300                                                      
REMARK 465     VAL C   301                                                      
REMARK 465     THR C   302                                                      
REMARK 465     SER C   303                                                      
REMARK 465     GLU C   304                                                      
REMARK 465     ASP C   305                                                      
REMARK 465     LEU C   306                                                      
REMARK 465     LYS C   307                                                      
REMARK 465     ARG C   308                                                      
REMARK 465     SER C   309                                                      
REMARK 465     VAL C   327                                                      
REMARK 465     LYS C   328                                                      
REMARK 465     GLN C   329                                                      
REMARK 465     LYS C   330                                                      
REMARK 465     VAL C   331                                                      
REMARK 465     PRO C   332                                                      
REMARK 465     ALA C   333                                                      
REMARK 465     PRO C   334                                                      
REMARK 465     ARG C   335                                                      
REMARK 465     TYR C   336                                                      
REMARK 465     THR C   337                                                      
REMARK 465     VAL C   338                                                      
REMARK 465     GLU C   339                                                      
REMARK 465     LEU C   340                                                      
REMARK 465     ALA C   341                                                      
REMARK 465     CYS C   342                                                      
REMARK 465     GLY C   343                                                      
REMARK 465     PHE C   344                                                      
REMARK 465     GLY C   345                                                      
REMARK 465     ALA C   346                                                      
REMARK 465     THR C   347                                                      
REMARK 465     GLY D    -4                                                      
REMARK 465     PRO D    -3                                                      
REMARK 465     LEU D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D   152                                                      
REMARK 465     SER D   153                                                      
REMARK 465     GLU E    -1                                                      
REMARK 465     PRO E     0                                                      
REMARK 465     LEU E     1                                                      
REMARK 465     GLU E     2                                                      
REMARK 465     ALA E     3                                                      
REMARK 465     ASP E     4                                                      
REMARK 465     LYS E     5                                                      
REMARK 465     LYS E    35                                                      
REMARK 465     GLY E    36                                                      
REMARK 465     THR E   315                                                      
REMARK 465     ASN E   316                                                      
REMARK 465     PHE E   317                                                      
REMARK 465     GLN E   318                                                      
REMARK 465     LYS E   319                                                      
REMARK 465     GLU F    -1                                                      
REMARK 465     PRO F     0                                                      
REMARK 465     SER F     1                                                      
REMARK 465     GLU F     2                                                      
REMARK 465     ARG F     3                                                      
REMARK 465     CYS F     4                                                      
REMARK 465     GLN F    55                                                      
REMARK 465     ASP F    56                                                      
REMARK 465     ARG F    57                                                      
REMARK 465     PRO F    62                                                      
REMARK 465     ILE F    63                                                      
REMARK 465     ASN F    64                                                      
REMARK 465     PHE F    65                                                      
REMARK 465     ARG F    66                                                      
REMARK 465     GLU F   198                                                      
REMARK 465     ASN F   199                                                      
REMARK 465     LYS F   236                                                      
REMARK 465     GLU F   237                                                      
REMARK 465     PRO F   238                                                      
REMARK 465     GLY F   239                                                      
REMARK 465     GLU F   240                                                      
REMARK 465     GLU F   241                                                      
REMARK 465     LEU F   242                                                      
REMARK 465     GLY F   266                                                      
REMARK 465     LYS F   267                                                      
REMARK 465     LYS F   268                                                      
REMARK 465     PRO F   269                                                      
REMARK 465     ASP F   270                                                      
REMARK 465     ASP F   271                                                      
REMARK 465     ILE F   272                                                      
REMARK 465     THR F   273                                                      
REMARK 465     ILE F   274                                                      
REMARK 465     ASP F   275                                                      
REMARK 465     VAL F   276                                                      
REMARK 465     ILE F   298                                                      
REMARK 465     LYS F   299                                                      
REMARK 465     LYS F   300                                                      
REMARK 465     VAL F   301                                                      
REMARK 465     THR F   302                                                      
REMARK 465     SER F   303                                                      
REMARK 465     GLU F   304                                                      
REMARK 465     GLN F   329                                                      
REMARK 465     LYS F   330                                                      
REMARK 465     VAL F   331                                                      
REMARK 465     PRO F   332                                                      
REMARK 465     ALA F   333                                                      
REMARK 465     PRO F   334                                                      
REMARK 465     ARG F   335                                                      
REMARK 465     TYR F   336                                                      
REMARK 465     THR F   337                                                      
REMARK 465     VAL F   338                                                      
REMARK 465     GLU F   339                                                      
REMARK 465     LEU F   340                                                      
REMARK 465     ALA F   341                                                      
REMARK 465     CYS F   342                                                      
REMARK 465     GLY F   343                                                      
REMARK 465     PHE F   344                                                      
REMARK 465     GLY F   345                                                      
REMARK 465     ALA F   346                                                      
REMARK 465     THR F   347                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  27    CG   CD   CE   NZ                                   
REMARK 470     GLU A  37    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  50    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  76    CG   OD1  OD2                                       
REMARK 470     LYS A  88    CG   CD   CE   NZ                                   
REMARK 470     LYS A  92    CG   CD   CE   NZ                                   
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     GLU A  96    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 149    CG   CD   OE1  NE2                                  
REMARK 470     LYS B   7    CG   CD   CE   NZ                                   
REMARK 470     GLU B   8    CG   CD   OE1  OE2                                  
REMARK 470     ARG B   9    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  10    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  11    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  12    CG   CD   CE   NZ                                   
REMARK 470     SER B  17    OG                                                  
REMARK 470     GLU B  21    CG   CD   OE1  OE2                                  
REMARK 470     ASN B  30    CG   OD1  ND2                                       
REMARK 470     THR B  37    OG1  CG2                                            
REMARK 470     ILE B  38    CG1  CG2  CD1                                       
REMARK 470     LYS B  42    CG   CD   CE   NZ                                   
REMARK 470     ASP B  43    CG   OD1  OD2                                       
REMARK 470     VAL B  49    CG1  CG2                                            
REMARK 470     THR B  51    OG1  CG2                                            
REMARK 470     GLU B  52    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  61    CG   CD   CE   NZ                                   
REMARK 470     LYS B  70    CG   CD   CE   NZ                                   
REMARK 470     VAL B  71    CG1  CG2                                            
REMARK 470     SER B  74    OG                                                  
REMARK 470     HIS B  76    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL B  80    CG1  CG2                                            
REMARK 470     VAL B  81    CG1  CG2                                            
REMARK 470     ARG B  82    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B  83    CG   OD1  ND2                                       
REMARK 470     SER B  84    OG                                                  
REMARK 470     SER B  85    OG                                                  
REMARK 470     TYR B  86    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     CYS B  87    SG                                                  
REMARK 470     LEU B  88    CG   CD1  CD2                                       
REMARK 470     ARG B  89    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  91    CG   CD   CE   NZ                                   
REMARK 470     GLU B  98    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 132    CG   CD   CE   NZ                                   
REMARK 470     ASN B 133    CG   OD1  ND2                                       
REMARK 470     GLU B 134    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 135    CG   OD1  ND2                                       
REMARK 470     ASN B 136    CG   OD1  ND2                                       
REMARK 470     GLU B 137    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 140    CG   CD   CE   NZ                                   
REMARK 470     LYS B 148    CG   CD   CE   NZ                                   
REMARK 470     LEU B 151    CG   CD1  CD2                                       
REMARK 470     GLU B 171    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 172    CG   CD   CE   NZ                                   
REMARK 470     LYS B 188    CG   CD   CE   NZ                                   
REMARK 470     GLN B 189    CG   CD   OE1  NE2                                  
REMARK 470     THR B 218    OG1  CG2                                            
REMARK 470     GLU B 220    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 221    CG1  CG2                                            
REMARK 470     ASP B 222    CG   OD1  OD2                                       
REMARK 470     LEU B 223    CG   CD1  CD2                                       
REMARK 470     GLN B 228    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 244    CG   CD   CE   NZ                                   
REMARK 470     GLU B 252    CG   CD   OE1  OE2                                  
REMARK 470     TYR B 262    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B 265    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 270    CG   CD   CE   NZ                                   
REMARK 470     ARG B 271    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 274    OG1  CG2                                            
REMARK 470     ASN B 280    CG   OD1  ND2                                       
REMARK 470     ILE B 281    CG1  CG2  CD1                                       
REMARK 470     GLU B 283    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 285    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 290    CG   CD   CE   NZ                                   
REMARK 470     ILE B 308    CG1  CG2  CD1                                       
REMARK 470     ARG C   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C  14    CG   CD   OE1  NE2                                  
REMARK 470     ILE C  15    CG1  CG2  CD1                                       
REMARK 470     GLU C  31    CG   CD   OE1  OE2                                  
REMARK 470     SER C  39    OG                                                  
REMARK 470     SER C  43    OG                                                  
REMARK 470     ARG C  54    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C  56    CG   OD1  OD2                                       
REMARK 470     ASP C  58    CG   OD1  OD2                                       
REMARK 470     LEU C  59    CG   CD1  CD2                                       
REMARK 470     ASN C  70    CG   OD1  ND2                                       
REMARK 470     GLU C  75    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 152    CG   CD   CE   NZ                                   
REMARK 470     GLN C 165    CG   CD   OE1  NE2                                  
REMARK 470     ASN C 199    CG   OD1  ND2                                       
REMARK 470     ARG C 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR C 249    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP C 265    CG   OD1  OD2                                       
REMARK 470     LYS C 267    CG   CD   CE   NZ                                   
REMARK 470     LEU C 296    CG   CD1  CD2                                       
REMARK 470     TYR C 310    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS C 326    CG   CD   CE   NZ                                   
REMARK 470     SER D   0    OG                                                  
REMARK 470     ASN D  53    CG   OD1  ND2                                       
REMARK 470     GLU D  64    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  65    CG   CD   CE   NZ                                   
REMARK 470     ASP D  76    CG   OD1  OD2                                       
REMARK 470     LYS D  88    CG   CD   CE   NZ                                   
REMARK 470     LYS E   7    CG   CD   CE   NZ                                   
REMARK 470     GLU E  10    CG   CD   OE1  OE2                                  
REMARK 470     ASP E  44    CG   OD1  OD2                                       
REMARK 470     SER E  45    OG                                                  
REMARK 470     LYS E  61    CG   CD   CE   NZ                                   
REMARK 470     ASN E  83    CG   OD1  ND2                                       
REMARK 470     SER E  85    OG                                                  
REMARK 470     TYR E  86    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN E 102    CG   OD1  ND2                                       
REMARK 470     GLU E 134    CG   CD   OE1  OE2                                  
REMARK 470     ASN E 135    CG   OD1  ND2                                       
REMARK 470     ASN E 136    CG   OD1  ND2                                       
REMARK 470     GLU E 137    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 148    CG   CD   CE   NZ                                   
REMARK 470     GLU E 171    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 270    CG   CD   CE   NZ                                   
REMARK 470     LEU F   9    CG   CD1  CD2                                       
REMARK 470     MET F  12    CG   SD   CE                                        
REMARK 470     ARG F  13    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE F  15    CG1  CG2  CD1                                       
REMARK 470     LYS F  26    CG   CD   CE   NZ                                   
REMARK 470     GLU F  31    CG   CD   OE1  OE2                                  
REMARK 470     LYS F  35    CG   CD   CE   NZ                                   
REMARK 470     PHE F  36    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR F  40    OG1  CG2                                            
REMARK 470     ARG F  54    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP F  58    CG   OD1  OD2                                       
REMARK 470     LEU F  59    CG   CD1  CD2                                       
REMARK 470     GLU F  60    CG   CD   OE1  OE2                                  
REMARK 470     LEU F  67    CG   CD1  CD2                                       
REMARK 470     ASN F  70    CG   OD1  ND2                                       
REMARK 470     GLU F  75    CG   CD   OE1  OE2                                  
REMARK 470     LYS F  76    CG   CD   CE   NZ                                   
REMARK 470     ASP F  77    CG   OD1  OD2                                       
REMARK 470     PRO F  83    CG   CD                                             
REMARK 470     ASN F  87    CG   OD1  ND2                                       
REMARK 470     SER F 116    OG                                                  
REMARK 470     SER F 149    OG                                                  
REMARK 470     SER F 227    OG                                                  
REMARK 470     ARG F 257    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR F 277    OG1  CG2                                            
REMARK 470     GLU F 280    CG   CD   OE1  OE2                                  
REMARK 470     SER F 281    OG                                                  
REMARK 470     SER F 297    OG                                                  
REMARK 470     LEU F 306    CG   CD1  CD2                                       
REMARK 470     LYS F 307    CG   CD   CE   NZ                                   
REMARK 470     ARG F 308    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F 328    CG   CD   CE   NZ                                   
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   OD1  ASN C    98     O5   NAG C   401              1.81            
REMARK 500   CB   CYS C   117     SG   CYS C   161              2.00            
REMARK 500   ND2  ASN F    98     O5   NAG F   403              2.01            
REMARK 500   SG   CYS F   117     CB   CYS F   161              2.02            
REMARK 500   CG   ASN C    98     C1   NAG C   401              2.07            
REMARK 500   ND2  ASN C    37     C2   NAG C   402              2.15            
REMARK 500   CG   ASN C    98     O5   NAG C   401              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS B  79   CA  -  CB  -  SG  ANGL. DEV. =  10.1 DEGREES          
REMARK 500    PRO B 116   C   -  N   -  CD  ANGL. DEV. = -26.9 DEGREES          
REMARK 500    LYS E  61   N   -  CA  -  C   ANGL. DEV. = -16.4 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    GLU A  25      116.89   -161.93                                   
REMARK 500    ASP A  54        4.76   -150.68                                   
REMARK 500    LYS A  74      105.10   -165.59                                   
REMARK 500    ASN B  20       16.88     54.02                                   
REMARK 500    LYS B  61     -130.26     50.07                                   
REMARK 500    SER B  84      -59.30     70.70                                   
REMARK 500    CYS B  87       69.67   -160.18                                   
REMARK 500    LYS B 161     -129.93     52.10                                   
REMARK 500    ASN B 216       73.00     57.19                                   
REMARK 500    GLU B 265     -177.84    -65.76                                   
REMARK 500    ASN B 269       86.11   -154.27                                   
REMARK 500    ILE C  15       60.88   -112.92                                   
REMARK 500    GLU C  31       -4.64     74.15                                   
REMARK 500    HIS C  32      -80.95   -111.91                                   
REMARK 500    ASP C  56       61.91     62.47                                   
REMARK 500    ARG C  66       54.15   -117.74                                   
REMARK 500    LYS C  76     -129.30     57.59                                   
REMARK 500    ASN C  87        0.46    -65.70                                   
REMARK 500    ASN C  98     -160.01   -121.19                                   
REMARK 500    CYS C 102      113.96   -160.08                                   
REMARK 500    CYS C 117       54.06   -116.03                                   
REMARK 500    TYR C 133       62.21   -117.28                                   
REMARK 500    CYS C 140      107.73    -46.47                                   
REMARK 500    ILE C 181       77.09     53.97                                   
REMARK 500    LYS C 218        4.61    -69.59                                   
REMARK 500    PRO C 222      170.37    -55.97                                   
REMARK 500    ASP C 265      -33.91   -131.84                                   
REMARK 500    ALA D   1       88.48   -161.14                                   
REMARK 500    PRO D  87       30.99    -71.15                                   
REMARK 500    ARG E   9      120.27   -170.45                                   
REMARK 500    PRO E  28       67.00    -61.16                                   
REMARK 500    PRO E  31       63.42    -66.28                                   
REMARK 500    LYS E  42     -158.77    -89.95                                   
REMARK 500    LYS E  61     -135.37     52.75                                   
REMARK 500    ASN E  83       73.56   -156.52                                   
REMARK 500    SER E  84      -64.22     67.27                                   
REMARK 500    ILE E 155      -52.32   -133.73                                   
REMARK 500    LYS E 161     -131.21     54.38                                   
REMARK 500    ASN E 168       76.57     54.40                                   
REMARK 500    ARG E 272       52.71   -110.64                                   
REMARK 500    ARG F  13       68.08   -102.45                                   
REMARK 500    ALA F  23       87.93   -157.44                                   
REMARK 500    GLU F  31       -6.71     73.23                                   
REMARK 500    HIS F  32      -85.20   -106.59                                   
REMARK 500    THR F  40        4.68    -54.78                                   
REMARK 500    ALA F  41       41.67   -107.04                                   
REMARK 500    LYS F  76     -134.23     60.00                                   
REMARK 500    ARG F  82       89.48   -168.63                                   
REMARK 500    PRO F  83     -158.30    -90.03                                   
REMARK 500    ILE F 181       73.13     53.37                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      53 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 MET A   20     SER A   21                 -144.45                    
REMARK 500 ILE C   15     GLN C   16                  147.56                    
REMARK 500 ILE C  264     ASP C  265                  134.47                    
REMARK 500 PRO E  313     VAL E  314                  146.52                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4DEP A    1   153  UNP    P01584   IL1B_HUMAN     117    269             
DBREF  4DEP B    1   319  UNP    P14778   IL1R1_HUMAN     18    336             
DBREF  4DEP C    1   347  UNP    Q9NPH3   IL1AP_HUMAN     21    367             
DBREF  4DEP D    1   153  UNP    P01584   IL1B_HUMAN     117    269             
DBREF  4DEP E    1   319  UNP    P14778   IL1R1_HUMAN     18    336             
DBREF  4DEP F    1   347  UNP    Q9NPH3   IL1AP_HUMAN     21    367             
SEQADV 4DEP GLY A   -4  UNP  P01584              EXPRESSION TAG                 
SEQADV 4DEP PRO A   -3  UNP  P01584              EXPRESSION TAG                 
SEQADV 4DEP LEU A   -2  UNP  P01584              EXPRESSION TAG                 
SEQADV 4DEP GLY A   -1  UNP  P01584              EXPRESSION TAG                 
SEQADV 4DEP SER A    0  UNP  P01584              EXPRESSION TAG                 
SEQADV 4DEP GLU B   -1  UNP  P14778              EXPRESSION TAG                 
SEQADV 4DEP PRO B    0  UNP  P14778              EXPRESSION TAG                 
SEQADV 4DEP GLU C   -1  UNP  Q9NPH3              EXPRESSION TAG                 
SEQADV 4DEP PRO C    0  UNP  Q9NPH3              EXPRESSION TAG                 
SEQADV 4DEP GLY D   -4  UNP  P01584              EXPRESSION TAG                 
SEQADV 4DEP PRO D   -3  UNP  P01584              EXPRESSION TAG                 
SEQADV 4DEP LEU D   -2  UNP  P01584              EXPRESSION TAG                 
SEQADV 4DEP GLY D   -1  UNP  P01584              EXPRESSION TAG                 
SEQADV 4DEP SER D    0  UNP  P01584              EXPRESSION TAG                 
SEQADV 4DEP GLU E   -1  UNP  P14778              EXPRESSION TAG                 
SEQADV 4DEP PRO E    0  UNP  P14778              EXPRESSION TAG                 
SEQADV 4DEP GLU F   -1  UNP  Q9NPH3              EXPRESSION TAG                 
SEQADV 4DEP PRO F    0  UNP  Q9NPH3              EXPRESSION TAG                 
SEQRES   1 A  158  GLY PRO LEU GLY SER ALA PRO VAL ARG SER LEU ASN CYS          
SEQRES   2 A  158  THR LEU ARG ASP SER GLN GLN LYS SER LEU VAL MET SER          
SEQRES   3 A  158  GLY PRO TYR GLU LEU LYS ALA LEU HIS LEU GLN GLY GLN          
SEQRES   4 A  158  ASP MET GLU GLN GLN VAL VAL PHE SER MET SER PHE VAL          
SEQRES   5 A  158  GLN GLY GLU GLU SER ASN ASP LYS ILE PRO VAL ALA LEU          
SEQRES   6 A  158  GLY LEU LYS GLU LYS ASN LEU TYR LEU SER CYS VAL LEU          
SEQRES   7 A  158  LYS ASP ASP LYS PRO THR LEU GLN LEU GLU SER VAL ASP          
SEQRES   8 A  158  PRO LYS ASN TYR PRO LYS LYS LYS MET GLU LYS ARG PHE          
SEQRES   9 A  158  VAL PHE ASN LYS ILE GLU ILE ASN ASN LYS LEU GLU PHE          
SEQRES  10 A  158  GLU SER ALA GLN PHE PRO ASN TRP TYR ILE SER THR SER          
SEQRES  11 A  158  GLN ALA GLU ASN MET PRO VAL PHE LEU GLY GLY THR LYS          
SEQRES  12 A  158  GLY GLY GLN ASP ILE THR ASP PHE THR MET GLN PHE VAL          
SEQRES  13 A  158  SER SER                                                      
SEQRES   1 B  321  GLU PRO LEU GLU ALA ASP LYS CYS LYS GLU ARG GLU GLU          
SEQRES   2 B  321  LYS ILE ILE LEU VAL SER SER ALA ASN GLU ILE ASP VAL          
SEQRES   3 B  321  ARG PRO CYS PRO LEU ASN PRO ASN GLU HIS LYS GLY THR          
SEQRES   4 B  321  ILE THR TRP TYR LYS ASP ASP SER LYS THR PRO VAL SER          
SEQRES   5 B  321  THR GLU GLN ALA SER ARG ILE HIS GLN HIS LYS GLU LYS          
SEQRES   6 B  321  LEU TRP PHE VAL PRO ALA LYS VAL GLU ASP SER GLY HIS          
SEQRES   7 B  321  TYR TYR CYS VAL VAL ARG ASN SER SER TYR CYS LEU ARG          
SEQRES   8 B  321  ILE LYS ILE SER ALA LYS PHE VAL GLU ASN GLU PRO ASN          
SEQRES   9 B  321  LEU CYS TYR ASN ALA GLN ALA ILE PHE LYS GLN LYS LEU          
SEQRES  10 B  321  PRO VAL ALA GLY ASP GLY GLY LEU VAL CYS PRO TYR MET          
SEQRES  11 B  321  GLU PHE PHE LYS ASN GLU ASN ASN GLU LEU PRO LYS LEU          
SEQRES  12 B  321  GLN TRP TYR LYS ASP CYS LYS PRO LEU LEU LEU ASP ASN          
SEQRES  13 B  321  ILE HIS PHE SER GLY VAL LYS ASP ARG LEU ILE VAL MET          
SEQRES  14 B  321  ASN VAL ALA GLU LYS HIS ARG GLY ASN TYR THR CYS HIS          
SEQRES  15 B  321  ALA SER TYR THR TYR LEU GLY LYS GLN TYR PRO ILE THR          
SEQRES  16 B  321  ARG VAL ILE GLU PHE ILE THR LEU GLU GLU ASN LYS PRO          
SEQRES  17 B  321  THR ARG PRO VAL ILE VAL SER PRO ALA ASN GLU THR MET          
SEQRES  18 B  321  GLU VAL ASP LEU GLY SER GLN ILE GLN LEU ILE CYS ASN          
SEQRES  19 B  321  VAL THR GLY GLN LEU SER ASP ILE ALA TYR TRP LYS TRP          
SEQRES  20 B  321  ASN GLY SER VAL ILE ASP GLU ASP ASP PRO VAL LEU GLY          
SEQRES  21 B  321  GLU ASP TYR TYR SER VAL GLU ASN PRO ALA ASN LYS ARG          
SEQRES  22 B  321  ARG SER THR LEU ILE THR VAL LEU ASN ILE SER GLU ILE          
SEQRES  23 B  321  GLU SER ARG PHE TYR LYS HIS PRO PHE THR CYS PHE ALA          
SEQRES  24 B  321  LYS ASN THR HIS GLY ILE ASP ALA ALA TYR ILE GLN LEU          
SEQRES  25 B  321  ILE TYR PRO VAL THR ASN PHE GLN LYS                          
SEQRES   1 C  349  GLU PRO SER GLU ARG CYS ASP ASP TRP GLY LEU ASP THR          
SEQRES   2 C  349  MET ARG GLN ILE GLN VAL PHE GLU ASP GLU PRO ALA ARG          
SEQRES   3 C  349  ILE LYS CYS PRO LEU PHE GLU HIS PHE LEU LYS PHE ASN          
SEQRES   4 C  349  TYR SER THR ALA HIS SER ALA GLY LEU THR LEU ILE TRP          
SEQRES   5 C  349  TYR TRP THR ARG GLN ASP ARG ASP LEU GLU GLU PRO ILE          
SEQRES   6 C  349  ASN PHE ARG LEU PRO GLU ASN ARG ILE SER LYS GLU LYS          
SEQRES   7 C  349  ASP VAL LEU TRP PHE ARG PRO THR LEU LEU ASN ASP THR          
SEQRES   8 C  349  GLY ASN TYR THR CYS MET LEU ARG ASN THR THR TYR CYS          
SEQRES   9 C  349  SER LYS VAL ALA PHE PRO LEU GLU VAL VAL GLN LYS ASP          
SEQRES  10 C  349  SER CYS PHE ASN SER PRO MET LYS LEU PRO VAL HIS LYS          
SEQRES  11 C  349  LEU TYR ILE GLU TYR GLY ILE GLN ARG ILE THR CYS PRO          
SEQRES  12 C  349  ASN VAL ASP GLY TYR PHE PRO SER SER VAL LYS PRO THR          
SEQRES  13 C  349  ILE THR TRP TYR MET GLY CYS TYR LYS ILE GLN ASN PHE          
SEQRES  14 C  349  ASN ASN VAL ILE PRO GLU GLY MET ASN LEU SER PHE LEU          
SEQRES  15 C  349  ILE ALA LEU ILE SER ASN ASN GLY ASN TYR THR CYS VAL          
SEQRES  16 C  349  VAL THR TYR PRO GLU ASN GLY ARG THR PHE HIS LEU THR          
SEQRES  17 C  349  ARG THR LEU THR VAL LYS VAL VAL GLY SER PRO LYS ASN          
SEQRES  18 C  349  ALA VAL PRO PRO VAL ILE HIS SER PRO ASN ASP HIS VAL          
SEQRES  19 C  349  VAL TYR GLU LYS GLU PRO GLY GLU GLU LEU LEU ILE PRO          
SEQRES  20 C  349  CYS THR VAL TYR PHE SER PHE LEU MET ASP SER ARG ASN          
SEQRES  21 C  349  GLU VAL TRP TRP THR ILE ASP GLY LYS LYS PRO ASP ASP          
SEQRES  22 C  349  ILE THR ILE ASP VAL THR ILE ASN GLU SER ILE SER HIS          
SEQRES  23 C  349  SER ARG THR GLU ASP GLU THR ARG THR GLN ILE LEU SER          
SEQRES  24 C  349  ILE LYS LYS VAL THR SER GLU ASP LEU LYS ARG SER TYR          
SEQRES  25 C  349  VAL CYS HIS ALA ARG SER ALA LYS GLY GLU VAL ALA LYS          
SEQRES  26 C  349  ALA ALA LYS VAL LYS GLN LYS VAL PRO ALA PRO ARG TYR          
SEQRES  27 C  349  THR VAL GLU LEU ALA CYS GLY PHE GLY ALA THR                  
SEQRES   1 D  158  GLY PRO LEU GLY SER ALA PRO VAL ARG SER LEU ASN CYS          
SEQRES   2 D  158  THR LEU ARG ASP SER GLN GLN LYS SER LEU VAL MET SER          
SEQRES   3 D  158  GLY PRO TYR GLU LEU LYS ALA LEU HIS LEU GLN GLY GLN          
SEQRES   4 D  158  ASP MET GLU GLN GLN VAL VAL PHE SER MET SER PHE VAL          
SEQRES   5 D  158  GLN GLY GLU GLU SER ASN ASP LYS ILE PRO VAL ALA LEU          
SEQRES   6 D  158  GLY LEU LYS GLU LYS ASN LEU TYR LEU SER CYS VAL LEU          
SEQRES   7 D  158  LYS ASP ASP LYS PRO THR LEU GLN LEU GLU SER VAL ASP          
SEQRES   8 D  158  PRO LYS ASN TYR PRO LYS LYS LYS MET GLU LYS ARG PHE          
SEQRES   9 D  158  VAL PHE ASN LYS ILE GLU ILE ASN ASN LYS LEU GLU PHE          
SEQRES  10 D  158  GLU SER ALA GLN PHE PRO ASN TRP TYR ILE SER THR SER          
SEQRES  11 D  158  GLN ALA GLU ASN MET PRO VAL PHE LEU GLY GLY THR LYS          
SEQRES  12 D  158  GLY GLY GLN ASP ILE THR ASP PHE THR MET GLN PHE VAL          
SEQRES  13 D  158  SER SER                                                      
SEQRES   1 E  321  GLU PRO LEU GLU ALA ASP LYS CYS LYS GLU ARG GLU GLU          
SEQRES   2 E  321  LYS ILE ILE LEU VAL SER SER ALA ASN GLU ILE ASP VAL          
SEQRES   3 E  321  ARG PRO CYS PRO LEU ASN PRO ASN GLU HIS LYS GLY THR          
SEQRES   4 E  321  ILE THR TRP TYR LYS ASP ASP SER LYS THR PRO VAL SER          
SEQRES   5 E  321  THR GLU GLN ALA SER ARG ILE HIS GLN HIS LYS GLU LYS          
SEQRES   6 E  321  LEU TRP PHE VAL PRO ALA LYS VAL GLU ASP SER GLY HIS          
SEQRES   7 E  321  TYR TYR CYS VAL VAL ARG ASN SER SER TYR CYS LEU ARG          
SEQRES   8 E  321  ILE LYS ILE SER ALA LYS PHE VAL GLU ASN GLU PRO ASN          
SEQRES   9 E  321  LEU CYS TYR ASN ALA GLN ALA ILE PHE LYS GLN LYS LEU          
SEQRES  10 E  321  PRO VAL ALA GLY ASP GLY GLY LEU VAL CYS PRO TYR MET          
SEQRES  11 E  321  GLU PHE PHE LYS ASN GLU ASN ASN GLU LEU PRO LYS LEU          
SEQRES  12 E  321  GLN TRP TYR LYS ASP CYS LYS PRO LEU LEU LEU ASP ASN          
SEQRES  13 E  321  ILE HIS PHE SER GLY VAL LYS ASP ARG LEU ILE VAL MET          
SEQRES  14 E  321  ASN VAL ALA GLU LYS HIS ARG GLY ASN TYR THR CYS HIS          
SEQRES  15 E  321  ALA SER TYR THR TYR LEU GLY LYS GLN TYR PRO ILE THR          
SEQRES  16 E  321  ARG VAL ILE GLU PHE ILE THR LEU GLU GLU ASN LYS PRO          
SEQRES  17 E  321  THR ARG PRO VAL ILE VAL SER PRO ALA ASN GLU THR MET          
SEQRES  18 E  321  GLU VAL ASP LEU GLY SER GLN ILE GLN LEU ILE CYS ASN          
SEQRES  19 E  321  VAL THR GLY GLN LEU SER ASP ILE ALA TYR TRP LYS TRP          
SEQRES  20 E  321  ASN GLY SER VAL ILE ASP GLU ASP ASP PRO VAL LEU GLY          
SEQRES  21 E  321  GLU ASP TYR TYR SER VAL GLU ASN PRO ALA ASN LYS ARG          
SEQRES  22 E  321  ARG SER THR LEU ILE THR VAL LEU ASN ILE SER GLU ILE          
SEQRES  23 E  321  GLU SER ARG PHE TYR LYS HIS PRO PHE THR CYS PHE ALA          
SEQRES  24 E  321  LYS ASN THR HIS GLY ILE ASP ALA ALA TYR ILE GLN LEU          
SEQRES  25 E  321  ILE TYR PRO VAL THR ASN PHE GLN LYS                          
SEQRES   1 F  349  GLU PRO SER GLU ARG CYS ASP ASP TRP GLY LEU ASP THR          
SEQRES   2 F  349  MET ARG GLN ILE GLN VAL PHE GLU ASP GLU PRO ALA ARG          
SEQRES   3 F  349  ILE LYS CYS PRO LEU PHE GLU HIS PHE LEU LYS PHE ASN          
SEQRES   4 F  349  TYR SER THR ALA HIS SER ALA GLY LEU THR LEU ILE TRP          
SEQRES   5 F  349  TYR TRP THR ARG GLN ASP ARG ASP LEU GLU GLU PRO ILE          
SEQRES   6 F  349  ASN PHE ARG LEU PRO GLU ASN ARG ILE SER LYS GLU LYS          
SEQRES   7 F  349  ASP VAL LEU TRP PHE ARG PRO THR LEU LEU ASN ASP THR          
SEQRES   8 F  349  GLY ASN TYR THR CYS MET LEU ARG ASN THR THR TYR CYS          
SEQRES   9 F  349  SER LYS VAL ALA PHE PRO LEU GLU VAL VAL GLN LYS ASP          
SEQRES  10 F  349  SER CYS PHE ASN SER PRO MET LYS LEU PRO VAL HIS LYS          
SEQRES  11 F  349  LEU TYR ILE GLU TYR GLY ILE GLN ARG ILE THR CYS PRO          
SEQRES  12 F  349  ASN VAL ASP GLY TYR PHE PRO SER SER VAL LYS PRO THR          
SEQRES  13 F  349  ILE THR TRP TYR MET GLY CYS TYR LYS ILE GLN ASN PHE          
SEQRES  14 F  349  ASN ASN VAL ILE PRO GLU GLY MET ASN LEU SER PHE LEU          
SEQRES  15 F  349  ILE ALA LEU ILE SER ASN ASN GLY ASN TYR THR CYS VAL          
SEQRES  16 F  349  VAL THR TYR PRO GLU ASN GLY ARG THR PHE HIS LEU THR          
SEQRES  17 F  349  ARG THR LEU THR VAL LYS VAL VAL GLY SER PRO LYS ASN          
SEQRES  18 F  349  ALA VAL PRO PRO VAL ILE HIS SER PRO ASN ASP HIS VAL          
SEQRES  19 F  349  VAL TYR GLU LYS GLU PRO GLY GLU GLU LEU LEU ILE PRO          
SEQRES  20 F  349  CYS THR VAL TYR PHE SER PHE LEU MET ASP SER ARG ASN          
SEQRES  21 F  349  GLU VAL TRP TRP THR ILE ASP GLY LYS LYS PRO ASP ASP          
SEQRES  22 F  349  ILE THR ILE ASP VAL THR ILE ASN GLU SER ILE SER HIS          
SEQRES  23 F  349  SER ARG THR GLU ASP GLU THR ARG THR GLN ILE LEU SER          
SEQRES  24 F  349  ILE LYS LYS VAL THR SER GLU ASP LEU LYS ARG SER TYR          
SEQRES  25 F  349  VAL CYS HIS ALA ARG SER ALA LYS GLY GLU VAL ALA LYS          
SEQRES  26 F  349  ALA ALA LYS VAL LYS GLN LYS VAL PRO ALA PRO ARG TYR          
SEQRES  27 F  349  THR VAL GLU LEU ALA CYS GLY PHE GLY ALA THR                  
MODRES 4DEP ASN E  216  ASN  GLYCOSYLATION SITE                                 
MODRES 4DEP ASN F   98  ASN  GLYCOSYLATION SITE                                 
MODRES 4DEP ASN F   91  ASN  GLYCOSYLATION SITE                                 
MODRES 4DEP ASN E  246  ASN  GLYCOSYLATION SITE                                 
MODRES 4DEP ASN F  189  ASN  GLYCOSYLATION SITE                                 
MODRES 4DEP ASN E  232  ASN  GLYCOSYLATION SITE                                 
MODRES 4DEP ASN C   91  ASN  GLYCOSYLATION SITE                                 
MODRES 4DEP ASN C  189  ASN  GLYCOSYLATION SITE                                 
MODRES 4DEP ASN B  216  ASN  GLYCOSYLATION SITE                                 
MODRES 4DEP ASN E  176  ASN  GLYCOSYLATION SITE                                 
MODRES 4DEP ASN B  232  ASN  GLYCOSYLATION SITE                                 
MODRES 4DEP ASN C   98  ASN  GLYCOSYLATION SITE                                 
MODRES 4DEP ASN C   37  ASN  GLYCOSYLATION SITE                                 
MODRES 4DEP ASN B  176  ASN  GLYCOSYLATION SITE                                 
HET    NAG  B 401      14                                                       
HET    NAG  B 402      14                                                       
HET    NAG  B 403      14                                                       
HET    NAG  C 401      14                                                       
HET    NAG  C 402      14                                                       
HET    NAG  C 403      14                                                       
HET    NAG  C 404      14                                                       
HET    NAG  E 401      14                                                       
HET    NAG  E 402      14                                                       
HET    NAG  E 403      14                                                       
HET    NAG  E 404      14                                                       
HET    NAG  F 401      14                                                       
HET    NAG  F 402      14                                                       
HET    NAG  F 403      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   7  NAG    14(C8 H15 N O6)                                              
FORMUL  21  HOH   *7(H2 O)                                                      
HELIX    1   1 GLN A   32  GLN A   39  5                                   8    
HELIX    2   2 LYS B   70  SER B   74  5                                   5    
HELIX    3   3 ALA B  170  ARG B  174  5                                   5    
HELIX    4   4 GLU B  285  LYS B  290  5                                   6    
HELIX    5   5 ASN C   37  ALA C   44  1                                   8    
HELIX    6   6 LEU C   67  ASN C   70  5                                   4    
HELIX    7   7 LEU C   85  ASP C   88  5                                   4    
HELIX    8   8 LEU C  183  ASN C  187  5                                   5    
HELIX    9   9 SER C  216  ALA C  220  5                                   5    
HELIX   10  10 GLN D   32  GLN D   39  5                                   8    
HELIX   11  11 GLU D   96  ARG D   98  5                                   3    
HELIX   12  12 LYS E   70  SER E   74  5                                   5    
HELIX   13  13 ASN E  106  GLN E  108  5                                   3    
HELIX   14  14 GLU E  285  HIS E  291  5                                   7    
HELIX   15  15 LEU F   85  THR F   89  5                                   5    
HELIX   16  16 LEU F  183  ASN F  187  5                                   5    
HELIX   17  17 SER F  216  ALA F  220  5                                   5    
SHEET    1   A 7 SER A   5  ASP A  12  0                                        
SHEET    2   A 7 VAL A  41  SER A  45 -1  O  PHE A  42   N  CYS A   8           
SHEET    3   A 7 ILE A  56  LEU A  62 -1  O  GLY A  61   N  SER A  43           
SHEET    4   A 7 VAL A 100  GLU A 105 -1  O  PHE A 101   N  VAL A  58           
SHEET    5   A 7 LEU A 110  SER A 114 -1  O  GLU A 113   N  ASN A 102           
SHEET    6   A 7 PHE A 146  PHE A 150 -1  O  PHE A 146   N  LEU A 110           
SHEET    7   A 7 SER A   5  ASP A  12 -1  N  THR A   9   O  GLN A 149           
SHEET    1   B 3 SER A  17  MET A  20  0                                        
SHEET    2   B 3 LEU A  26  LEU A  29 -1  O  LEU A  29   N  SER A  17           
SHEET    3   B 3 MET A 130  PRO A 131 -1  O  MET A 130   N  ALA A  28           
SHEET    1   C 2 LEU A  67  VAL A  72  0                                        
SHEET    2   C 2 THR A  79  SER A  84 -1  O  GLN A  81   N  SER A  70           
SHEET    1   D 2 TYR A 121  SER A 123  0                                        
SHEET    2   D 2 PHE A 133  GLY A 135 -1  O  GLY A 135   N  TYR A 121           
SHEET    1   E 3 GLU B   8  GLU B  11  0                                        
SHEET    2   E 3 ARG B  89  VAL B  97  1  O  LYS B  91   N  GLU B  11           
SHEET    3   E 3 VAL B  16  SER B  18  1  N  SER B  17   O  LYS B  95           
SHEET    1   F 4 GLU B   8  GLU B  11  0                                        
SHEET    2   F 4 ARG B  89  VAL B  97  1  O  LYS B  91   N  GLU B  11           
SHEET    3   F 4 GLY B  75  VAL B  81 -1  N  GLY B  75   O  ALA B  94           
SHEET    4   F 4 ILE B  38  TYR B  41 -1  N  TYR B  41   O  TYR B  78           
SHEET    1   G 3 GLU B  21  ARG B  25  0                                        
SHEET    2   G 3 LYS B  63  ALA B  69 -1  O  LEU B  64   N  ARG B  25           
SHEET    3   G 3 ILE B  57  HIS B  60 -1  N  HIS B  58   O  TRP B  65           
SHEET    1   H 5 PHE B 111  PRO B 116  0                                        
SHEET    2   H 5 LYS B 188  LEU B 201  1  O  VAL B 195   N  PHE B 111           
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  TYR B 144   O  THR B 178           
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 GLN B 228  GLY B 235 -1  O  THR B 234   N  VAL B 210           
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  SER B 263 -1  N  TYR B 262   O  ILE B 276           
SHEET    1   K 5 GLU B 217  THR B 218  0                                        
SHEET    2   K 5 ILE B 303  GLN B 309  1  O  GLN B 309   N  GLU B 217           
SHEET    3   K 5 PHE B 293  LYS B 298 -1  N  CYS B 295   O  ALA B 306           
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           
SHEET    1   L 3 ASP C   5  LEU C   9  0                                        
SHEET    2   L 3 CYS C 102  VAL C 112  1  O  CYS C 102   N  ASP C   5           
SHEET    3   L 3 GLN C  16  PHE C  18  1  N  VAL C  17   O  GLU C 110           
SHEET    1   M 5 ASP C   5  LEU C   9  0                                        
SHEET    2   M 5 CYS C 102  VAL C 112  1  O  CYS C 102   N  ASP C   5           
SHEET    3   M 5 GLY C  90  ARG C  97 -1  N  GLY C  90   O  LEU C 109           
SHEET    4   M 5 THR C  47  ARG C  54 -1  N  TYR C  51   O  THR C  93           
SHEET    5   M 5 GLU C  60  PRO C  62 -1  O  GLU C  61   N  TRP C  52           
SHEET    1   N 3 ALA C  23  LYS C  26  0                                        
SHEET    2   N 3 VAL C  78  PHE C  81 -1  O  LEU C  79   N  ILE C  25           
SHEET    3   N 3 ILE C  72  GLU C  75 -1  N  SER C  73   O  TRP C  80           
SHEET    1   O 5 VAL C 126  TYR C 130  0                                        
SHEET    2   O 5 ARG C 201  VAL C 214  1  O  VAL C 214   N  LEU C 129           
SHEET    3   O 5 GLY C 188  GLU C 198 -1  N  TYR C 196   O  PHE C 203           
SHEET    4   O 5 THR C 154  MET C 159 -1  N  TYR C 158   O  THR C 191           
SHEET    5   O 5 TYR C 162  LYS C 163 -1  O  TYR C 162   N  MET C 159           
SHEET    1   P 3 ILE C 135  THR C 139  0                                        
SHEET    2   P 3 ASN C 176  LEU C 180 -1  O  PHE C 179   N  GLN C 136           
SHEET    3   P 3 VAL C 170  GLU C 173 -1  N  GLU C 173   O  ASN C 176           
SHEET    1   Q 4 VAL C 224  HIS C 226  0                                        
SHEET    2   Q 4 CYS C 246  PHE C 250 -1  O  THR C 247   N  HIS C 226           
SHEET    3   Q 4 GLU C 290  GLN C 294 -1  O  GLU C 290   N  PHE C 250           
SHEET    4   Q 4 GLU C 280  SER C 283 -1  N  SER C 283   O  THR C 291           
SHEET    1   R 3 GLU C 259  THR C 263  0                                        
SHEET    2   R 3 VAL C 311  ARG C 315 -1  O  VAL C 311   N  THR C 263           
SHEET    3   R 3 GLU C 320  ALA C 324 -1  O  LYS C 323   N  CYS C 312           
SHEET    1   S 9 LYS D  77  SER D  84  0                                        
SHEET    2   S 9 LEU D  67  LYS D  74 -1  N  SER D  70   O  GLN D  81           
SHEET    3   S 9 ILE D  56  LEU D  62 -1  N  LEU D  62   O  LEU D  67           
SHEET    4   S 9 VAL D 100  GLU D 105 -1  O  PHE D 101   N  VAL D  58           
SHEET    5   S 9 LEU D 110  SER D 114 -1  O  GLU D 113   N  ASN D 102           
SHEET    6   S 9 PHE D 146  PHE D 150 -1  O  PHE D 146   N  LEU D 110           
SHEET    7   S 9 SER D   5  ASP D  12 -1  N  ARG D  11   O  THR D 147           
SHEET    8   S 9 PHE D  42  PHE D  46 -1  O  PHE D  42   N  CYS D   8           
SHEET    9   S 9 ILE D  56  LEU D  62 -1  O  GLY D  61   N  SER D  43           
SHEET    1   T 3 SER D  17  GLY D  22  0                                        
SHEET    2   T 3 GLU D  25  LEU D  29 -1  O  LEU D  29   N  SER D  17           
SHEET    3   T 3 MET D 130  PRO D 131 -1  O  MET D 130   N  ALA D  28           
SHEET    1   U 2 TYR D 121  SER D 123  0                                        
SHEET    2   U 2 PHE D 133  GLY D 135 -1  O  PHE D 133   N  SER D 123           
SHEET    1   V 3 LYS E   7  GLU E  10  0                                        
SHEET    2   V 3 TYR E  86  VAL E  97  1  O  LYS E  91   N  ARG E   9           
SHEET    3   V 3 LEU E  15  SER E  18  1  N  SER E  17   O  LYS E  95           
SHEET    1   W 4 LYS E   7  GLU E  10  0                                        
SHEET    2   W 4 TYR E  86  VAL E  97  1  O  LYS E  91   N  ARG E   9           
SHEET    3   W 4 GLY E  75  ASN E  83 -1  N  VAL E  81   O  LEU E  88           
SHEET    4   W 4 ILE E  38  TYR E  41 -1  N  TYR E  41   O  TYR E  78           
SHEET    1   X 3 ASP E  23  ARG E  25  0                                        
SHEET    2   X 3 LYS E  63  PHE E  66 -1  O  LEU E  64   N  ARG E  25           
SHEET    3   X 3 ILE E  57  HIS E  60 -1  N  HIS E  60   O  LYS E  63           
SHEET    1   Y 5 ILE E 110  PRO E 116  0                                        
SHEET    2   Y 5 LYS E 188  LEU E 201  1  O  VAL E 195   N  PHE E 111           
SHEET    3   Y 5 GLY E 175  TYR E 185 -1  N  TYR E 177   O  ILE E 196           
SHEET    4   Y 5 GLN E 142  LYS E 145 -1  N  TYR E 144   O  THR E 178           
SHEET    5   Y 5 LYS E 148  PRO E 149 -1  O  LYS E 148   N  LYS E 145           
SHEET    1   Z 3 GLY E 121  VAL E 124  0                                        
SHEET    2   Z 3 ARG E 163  VAL E 166 -1  O  VAL E 166   N  GLY E 121           
SHEET    3   Z 3 PHE E 157  VAL E 160 -1  N  VAL E 160   O  ARG E 163           
SHEET    1  AA 4 VAL E 210  SER E 213  0                                        
SHEET    2  AA 4 ILE E 227  GLY E 235 -1  O  ASN E 232   N  SER E 213           
SHEET    3  AA 4 SER E 273  ILE E 281 -1  O  LEU E 275   N  VAL E 233           
SHEET    4  AA 4 LEU E 257  VAL E 264 -1  N  GLY E 258   O  ASN E 280           
SHEET    1  AB 5 GLU E 217  GLU E 220  0                                        
SHEET    2  AB 5 GLY E 302  ILE E 311  1  O  GLN E 309   N  GLU E 217           
SHEET    3  AB 5 PHE E 293  ASN E 299 -1  N  CYS E 295   O  ALA E 306           
SHEET    4  AB 5 ILE E 240  TRP E 245 -1  N  TYR E 242   O  PHE E 296           
SHEET    5  AB 5 SER E 248  VAL E 249 -1  O  SER E 248   N  TRP E 245           
SHEET    1  AC 3 ASP F   6  LEU F   9  0                                        
SHEET    2  AC 3 CYS F 102  VAL F 112  1  O  ALA F 106   N  GLY F   8           
SHEET    3  AC 3 ILE F  15  PHE F  18  1  N  VAL F  17   O  GLU F 110           
SHEET    1  AD 4 ASP F   6  LEU F   9  0                                        
SHEET    2  AD 4 CYS F 102  VAL F 112  1  O  ALA F 106   N  GLY F   8           
SHEET    3  AD 4 GLY F  90  ARG F  97 -1  N  LEU F  96   O  SER F 103           
SHEET    4  AD 4 THR F  47  TYR F  51 -1  N  ILE F  49   O  MET F  95           
SHEET    1  AE 2 ILE F  25  LYS F  26  0                                        
SHEET    2  AE 2 VAL F  78  LEU F  79 -1  O  LEU F  79   N  ILE F  25           
SHEET    1  AF 5 VAL F 126  TYR F 130  0                                        
SHEET    2  AF 5 PHE F 203  VAL F 214  1  O  THR F 210   N  HIS F 127           
SHEET    3  AF 5 GLY F 188  TYR F 196 -1  N  TYR F 190   O  LEU F 209           
SHEET    4  AF 5 THR F 154  MET F 159 -1  N  TYR F 158   O  THR F 191           
SHEET    5  AF 5 TYR F 162  LYS F 163 -1  O  TYR F 162   N  MET F 159           
SHEET    1  AG 3 ILE F 135  THR F 139  0                                        
SHEET    2  AG 3 ASN F 176  LEU F 180 -1  O  PHE F 179   N  GLN F 136           
SHEET    3  AG 3 VAL F 170  GLU F 173 -1  N  ILE F 171   O  SER F 178           
SHEET    1  AH 4 VAL F 224  SER F 227  0                                        
SHEET    2  AH 4 ILE F 244  PHE F 250 -1  O  TYR F 249   N  VAL F 224           
SHEET    3  AH 4 GLU F 290  LEU F 296 -1  O  ARG F 292   N  VAL F 248           
SHEET    4  AH 4 ASN F 279  SER F 281 -1  N  ASN F 279   O  ILE F 295           
SHEET    1  AI 2 VAL F 233  TYR F 234  0                                        
SHEET    2  AI 2 LYS F 326  VAL F 327  1  O  LYS F 326   N  TYR F 234           
SHEET    1  AJ 3 GLU F 259  ILE F 264  0                                        
SHEET    2  AJ 3 TYR F 310  SER F 316 -1  O  ARG F 315   N  GLU F 259           
SHEET    3  AJ 3 GLY F 319  ALA F 324 -1  O  GLY F 319   N  SER F 316           
SSBOND   1 CYS B   27    CYS B   79                          1555   1555  1.98  
SSBOND   2 CYS B  104    CYS B  147                          1555   1555  2.04  
SSBOND   3 CYS B  125    CYS B  179                          1555   1555  2.04  
SSBOND   4 CYS B  231    CYS B  295                          1555   1555  2.04  
SSBOND   5 CYS C    4    CYS C  102                          1555   1555  2.06  
SSBOND   6 CYS C   27    CYS C   94                          1555   1555  2.05  
SSBOND   7 CYS C  117    CYS C  161                          1555   1555  2.05  
SSBOND   8 CYS C  140    CYS C  192                          1555   1555  2.03  
SSBOND   9 CYS C  246    CYS C  312                          1555   1555  2.03  
SSBOND  10 CYS E    6    CYS E   87                          1555   1555  2.06  
SSBOND  11 CYS E   27    CYS E   79                          1555   1555  2.04  
SSBOND  12 CYS E  104    CYS E  147                          1555   1555  2.05  
SSBOND  13 CYS E  125    CYS E  179                          1555   1555  2.04  
SSBOND  14 CYS E  231    CYS E  295                          1555   1555  2.05  
SSBOND  15 CYS F   27    CYS F   94                          1555   1555  2.01  
SSBOND  16 CYS F  117    CYS F  161                          1555   1555  2.03  
SSBOND  17 CYS F  140    CYS F  192                          1555   1555  2.03  
SSBOND  18 CYS F  246    CYS F  312                          1555   1555  2.03  
LINK         ND2 ASN B 176                 C1  NAG B 401     1555   1555  1.46  
LINK         ND2 ASN B 216                 C1  NAG B 402     1555   1555  1.44  
LINK         ND2 ASN B 232                 C1  NAG B 403     1555   1555  1.63  
LINK         ND2 ASN C  37                 C1  NAG C 402     1555   1555  1.45  
LINK         ND2 ASN C  91                 C1  NAG C 403     1555   1555  1.44  
LINK         ND2 ASN C  98                 C1  NAG C 401     1555   1555  1.60  
LINK         ND2 ASN C 189                 C1  NAG C 404     1555   1555  1.44  
LINK         ND2 ASN E 176                 C1  NAG E 401     1555   1555  1.51  
LINK         ND2 ASN E 216                 C1  NAG E 402     1555   1555  1.44  
LINK         ND2 ASN E 232                 C1  NAG E 403     1555   1555  1.44  
LINK         ND2 ASN E 246                 C1  NAG E 404     1555   1555  1.44  
LINK         ND2 ASN F  91                 C1  NAG F 402     1555   1555  1.44  
LINK         ND2 ASN F  98                 C1  NAG F 403     1555   1555  1.57  
LINK         ND2 ASN F 189                 C1  NAG F 401     1555   1555  1.44  
CISPEP   1 TYR A   90    PRO A   91          0        13.67                     
CISPEP   2 VAL B   67    PRO B   68          0        -5.22                     
CISPEP   3 SER B  213    PRO B  214          0        15.94                     
CISPEP   4 ARG C   82    PRO C   83          0        -3.87                     
CISPEP   5 TYR D   90    PRO D   91          0         5.53                     
CISPEP   6 VAL E   67    PRO E   68          0        -4.20                     
CISPEP   7 SER E  213    PRO E  214          0        16.54                     
CISPEP   8 ARG F   82    PRO F   83          0        14.36                     
CISPEP   9 SER F  227    PRO F  228          0         9.10                     
CRYST1  105.990   65.900  163.400  90.00  90.35  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009435  0.000000  0.000058        0.00000                         
SCALE2      0.000000  0.015175  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006120        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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