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Database: PDB
Entry: 3O4O
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HEADER    IMMUNE SYSTEM                           27-JUL-10   3O4O              
TITLE     CRYSTAL STRUCTURE OF AN INTERLEUKIN-1 RECEPTOR COMPLEX                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-1 BETA;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: IL-1BETA, IL-1 BETA, CATABOLIN;                             
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: INTERLEUKIN-1 RECEPTOR TYPE 2;                             
COMPND   8 CHAIN: C;                                                            
COMPND   9 FRAGMENT: IL-1RII ECTODOMAIN, RESIDUES 14-343;                       
COMPND  10 SYNONYM: IL-1RII, IL-1RT-2, IL-1RT2, IL-1R-2, INTERLEUKIN-1 RECEPTOR 
COMPND  11 TYPE II, INTERLEUKIN-1 RECEPTOR BETA, IL-1R-BETA, CD121 ANTIGEN-LIKE 
COMPND  12 FAMILY MEMBER B, CDW121B;                                            
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: INTERLEUKIN-1 RECEPTOR ACCESSORY PROTEIN;                  
COMPND  16 CHAIN: B;                                                            
COMPND  17 FRAGMENT: IL-1RACP ECTODOMAIN, RESIDUES 21-350;                      
COMPND  18 SYNONYM: IL-1RACP, IL-1 RECEPTOR ACCESSORY PROTEIN, INTERLEUKIN-1    
COMPND  19 RECEPTOR 3, IL-1R-3, IL-1R3;                                         
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1;                                
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  17 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  19 EXPRESSION_SYSTEM_VECTOR: PACGP67-A;                                 
SOURCE  20 MOL_ID: 3;                                                           
SOURCE  21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  22 ORGANISM_COMMON: HUMAN;                                              
SOURCE  23 ORGANISM_TAXID: 9606;                                                
SOURCE  24 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  25 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  26 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  27 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  28 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  29 EXPRESSION_SYSTEM_VECTOR: PACGP67-A                                  
KEYWDS    CYTOKINE-RECEPTOR COMPLEX, BETA-TREFOIL, IG-LIKE FOLD, IMMUNE SYSTEM  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.Q.WANG,D.L.WANG,S.Y.ZHANG,L.LI,X.LIU,K.R.MEI                        
REVDAT   3   20-OCT-10 3O4O    1       JRNL                                     
REVDAT   2   08-SEP-10 3O4O    1       JRNL                                     
REVDAT   1   01-SEP-10 3O4O    0                                                
JRNL        AUTH   D.L.WANG,S.Y.ZHANG,L.LI,X.LIU,K.R.MEI,X.Q.WANG               
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE ASSEMBLY AND ACTIVATION OF      
JRNL        TITL 2 IL-1BETA WITH ITS RECEPTORS                                  
JRNL        REF    NAT.IMMUNOL.                  V.  11   905 2010              
JRNL        REFN                   ISSN 1529-2908                               
JRNL        PMID   20802483                                                     
JRNL        DOI    10.1038/NI.1925                                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.59                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.400                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 21443                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.253                           
REMARK   3   R VALUE            (WORKING SET) : 0.252                           
REMARK   3   FREE R VALUE                     : 0.289                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.130                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1101                            
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 36.5869 -  6.5894    0.99     2830   160  0.2777 0.3283        
REMARK   3     2  6.5894 -  5.2351    1.00     2721   151  0.2461 0.2674        
REMARK   3     3  5.2351 -  4.5748    1.00     2664   146  0.1986 0.2489        
REMARK   3     4  4.5748 -  4.1572    1.00     2649   151  0.2058 0.2578        
REMARK   3     5  4.1572 -  3.8595    1.00     2694   126  0.2571 0.3017        
REMARK   3     6  3.8595 -  3.6322    1.00     2631   134  0.2604 0.2855        
REMARK   3     7  3.6322 -  3.4504    0.99     2563   148  0.2870 0.3273        
REMARK   3     8  3.4504 -  3.3003    0.60     1590    85  0.3147 0.3283        
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              : 0.29                                          
REMARK   3   B_SOL              : 70.26                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.020            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
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) : -20.59630                                            
REMARK   3    B22 (A**2) : -22.62510                                            
REMARK   3    B33 (A**2) : -20.51560                                            
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  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      :  0.012           6877                                  
REMARK   3   ANGLE     :  1.120           9262                                  
REMARK   3   CHIRALITY :  0.069           1022                                  
REMARK   3   PLANARITY :  0.006           1146                                  
REMARK   3   DIHEDRAL  : 26.335           4061                                  
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 3O4O COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-AUG-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB060660.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22655                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.400                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2I1B                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG 10000, 0.1M BIS-TRIS, PH 5.5,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       22.41500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       90.33000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       88.73500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       90.33000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.41500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       88.73500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: AUTHOR STATES THAT THE BIOLOGICAL ASSEMBLY IS UNKNOWN.       
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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   153                                                      
REMARK 465     ALA C    -2                                                      
REMARK 465     ASP C    -1                                                      
REMARK 465     PRO C     0                                                      
REMARK 465     PHE C     1                                                      
REMARK 465     THR C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 465     GLN C     4                                                      
REMARK 465     PRO C     5                                                      
REMARK 465     ALA C     6                                                      
REMARK 465     ALA C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     THR C     9                                                      
REMARK 465     GLY C    10                                                      
REMARK 465     ALA C    11                                                      
REMARK 465     ALA C    12                                                      
REMARK 465     ARG C    13                                                      
REMARK 465     SER C    14                                                      
REMARK 465     HIS C   331                                                      
REMARK 465     HIS C   332                                                      
REMARK 465     HIS C   333                                                      
REMARK 465     HIS C   334                                                      
REMARK 465     HIS C   335                                                      
REMARK 465     HIS C   336                                                      
REMARK 465     ALA B    -2                                                      
REMARK 465     ASP B    -1                                                      
REMARK 465     PRO B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     VAL B   327                                                      
REMARK 465     LYS B   328                                                      
REMARK 465     GLN B   329                                                      
REMARK 465     LYS B   330                                                      
REMARK 465     HIS B   331                                                      
REMARK 465     HIS B   332                                                      
REMARK 465     HIS B   333                                                      
REMARK 465     HIS B   334                                                      
REMARK 465     HIS B   335                                                      
REMARK 465     HIS B   336                                                      
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   SG   CYS C   139     CB   CYS C   194              1.69            
REMARK 500   O    ASN C    99     N    TYR C   102              1.99            
REMARK 500   CB   CYS C   139     SG   CYS C   194              2.04            
REMARK 500   ND2  ASN C   206     C2   NAG C   338              2.09            
REMARK 500   ND2  ASN C    99     O5   NAG C   337              2.10            
REMARK 500   SG   CYS C    15     CB   CYS C   103              2.11            
REMARK 500   ND2  ASN B    87     C2   NAG B   337              2.16            
REMARK 500   O    TYR B   234     O    ALA B   325              2.17            
REMARK 500   SG   CYS C    37     CB   CYS C    95              2.19            
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    PRO A   2      -78.01    -87.56                                   
REMARK 500    GLN A  14       30.42    -98.63                                   
REMARK 500    GLN A  15       -7.71     72.63                                   
REMARK 500    SER A  21       64.73   -164.25                                   
REMARK 500    PRO A  23       32.32    -76.23                                   
REMARK 500    GLU A  37       29.64    -78.15                                   
REMARK 500    SER A  52      142.43   -179.06                                   
REMARK 500    GLU A  64       15.43     52.89                                   
REMARK 500    ASP A  75       49.77     70.59                                   
REMARK 500    ASN A 108       -1.82     62.45                                   
REMARK 500    GLN C  39        7.40     49.80                                   
REMARK 500    TRP C  43       -0.96     67.22                                   
REMARK 500    LEU C  44       87.49    -69.50                                   
REMARK 500    VAL C  48      -23.86   -145.31                                   
REMARK 500    SER C  49      155.73    -46.11                                   
REMARK 500    PRO C  50       82.52     16.71                                   
REMARK 500    GLU C  70     -118.04    -94.35                                   
REMARK 500    ASP C  77       90.81    -59.43                                   
REMARK 500    GLU C  88      -23.74    101.80                                   
REMARK 500    ALA C 100      -32.51    -37.65                                   
REMARK 500    CYS C 103      138.82   -172.72                                   
REMARK 500    ASN C 115       45.60    -74.44                                   
REMARK 500    ASP C 141       80.01     45.98                                   
REMARK 500    LEU C 142       -0.29   -148.36                                   
REMARK 500    THR C 150       88.36    -61.97                                   
REMARK 500    ASP C 151       94.25    -56.50                                   
REMARK 500    VAL C 152       88.27     42.64                                   
REMARK 500    ALA C 199       83.95   -151.58                                   
REMARK 500    GLU C 201       13.71     57.08                                   
REMARK 500    GLU C 221      101.83   -160.74                                   
REMARK 500    ILE C 227       24.35   -141.58                                   
REMARK 500    THR C 232       96.26    -39.40                                   
REMARK 500    ALA C 235      166.48    161.64                                   
REMARK 500    SER C 236       -9.63    173.72                                   
REMARK 500    LEU C 237       26.25     85.22                                   
REMARK 500    SER C 239      -19.27     75.06                                   
REMARK 500    THR C 253       53.06   -148.10                                   
REMARK 500    PRO C 254       40.60    -72.76                                   
REMARK 500    LEU C 255      -99.52    -76.56                                   
REMARK 500    ASN C 264      -48.63    160.55                                   
REMARK 500    HIS C 267       -7.17     87.80                                   
REMARK 500    ILE C 268       -4.12     68.55                                   
REMARK 500    SER C 270       39.33     39.14                                   
REMARK 500    ALA C 271      -56.08   -169.74                                   
REMARK 500    PRO C 281     -177.19    -61.69                                   
REMARK 500    SER C 286      -50.73     72.96                                   
REMARK 500    GLU C 287     -129.32     42.81                                   
REMARK 500    ASN C 289      -72.25    -39.58                                   
REMARK 500    MET C 309      139.12   -176.95                                   
REMARK 500    LYS C 329     -172.19    103.82                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      82 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 337                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 338                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 339                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 340                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 341                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 342                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 337                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 338                 
DBREF  3O4O A    1   153  UNP    P01584   IL1B_HUMAN     117    269             
DBREF  3O4O C    1   330  UNP    P27930   IL1R2_HUMAN     14    343             
DBREF  3O4O B    1   330  UNP    Q9NPH3   IL1AP_HUMAN     21    350             
SEQADV 3O4O GLY A   -4  UNP  P01584              EXPRESSION TAG                 
SEQADV 3O4O PRO A   -3  UNP  P01584              EXPRESSION TAG                 
SEQADV 3O4O LEU A   -2  UNP  P01584              EXPRESSION TAG                 
SEQADV 3O4O GLY A   -1  UNP  P01584              EXPRESSION TAG                 
SEQADV 3O4O SER A    0  UNP  P01584              EXPRESSION TAG                 
SEQADV 3O4O ALA C   -2  UNP  P27930              EXPRESSION TAG                 
SEQADV 3O4O ASP C   -1  UNP  P27930              EXPRESSION TAG                 
SEQADV 3O4O PRO C    0  UNP  P27930              EXPRESSION TAG                 
SEQADV 3O4O HIS C  331  UNP  P27930              EXPRESSION TAG                 
SEQADV 3O4O HIS C  332  UNP  P27930              EXPRESSION TAG                 
SEQADV 3O4O HIS C  333  UNP  P27930              EXPRESSION TAG                 
SEQADV 3O4O HIS C  334  UNP  P27930              EXPRESSION TAG                 
SEQADV 3O4O HIS C  335  UNP  P27930              EXPRESSION TAG                 
SEQADV 3O4O HIS C  336  UNP  P27930              EXPRESSION TAG                 
SEQADV 3O4O ALA B   -2  UNP  Q9NPH3              EXPRESSION TAG                 
SEQADV 3O4O ASP B   -1  UNP  Q9NPH3              EXPRESSION TAG                 
SEQADV 3O4O PRO B    0  UNP  Q9NPH3              EXPRESSION TAG                 
SEQADV 3O4O HIS B  331  UNP  Q9NPH3              EXPRESSION TAG                 
SEQADV 3O4O HIS B  332  UNP  Q9NPH3              EXPRESSION TAG                 
SEQADV 3O4O HIS B  333  UNP  Q9NPH3              EXPRESSION TAG                 
SEQADV 3O4O HIS B  334  UNP  Q9NPH3              EXPRESSION TAG                 
SEQADV 3O4O HIS B  335  UNP  Q9NPH3              EXPRESSION TAG                 
SEQADV 3O4O HIS B  336  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 C  339  ALA ASP PRO PHE THR LEU GLN PRO ALA ALA HIS THR GLY          
SEQRES   2 C  339  ALA ALA ARG SER CYS ARG PHE ARG GLY ARG HIS TYR LYS          
SEQRES   3 C  339  ARG GLU PHE ARG LEU GLU GLY GLU PRO VAL ALA LEU ARG          
SEQRES   4 C  339  CYS PRO GLN VAL PRO TYR TRP LEU TRP ALA SER VAL SER          
SEQRES   5 C  339  PRO ARG ILE ASN LEU THR TRP HIS LYS ASN ASP SER ALA          
SEQRES   6 C  339  ARG THR VAL PRO GLY GLU GLU GLU THR ARG MET TRP ALA          
SEQRES   7 C  339  GLN ASP GLY ALA LEU TRP LEU LEU PRO ALA LEU GLN GLU          
SEQRES   8 C  339  ASP SER GLY THR TYR VAL CYS THR THR ARG ASN ALA SER          
SEQRES   9 C  339  TYR CYS ASP LYS MET SER ILE GLU LEU ARG VAL PHE GLU          
SEQRES  10 C  339  ASN THR ASP ALA PHE LEU PRO PHE ILE SER TYR PRO GLN          
SEQRES  11 C  339  ILE LEU THR LEU SER THR SER GLY VAL LEU VAL CYS PRO          
SEQRES  12 C  339  ASP LEU SER GLU PHE THR ARG ASP LYS THR ASP VAL LYS          
SEQRES  13 C  339  ILE GLN TRP TYR LYS ASP SER LEU LEU LEU ASP LYS ASP          
SEQRES  14 C  339  ASN GLU LYS PHE LEU SER VAL ARG GLY THR THR HIS LEU          
SEQRES  15 C  339  LEU VAL HIS ASP VAL ALA LEU GLU ASP ALA GLY TYR TYR          
SEQRES  16 C  339  ARG CYS VAL LEU THR PHE ALA HIS GLU GLY GLN GLN TYR          
SEQRES  17 C  339  ASN ILE THR ARG SER ILE GLU LEU ARG ILE LYS LYS LYS          
SEQRES  18 C  339  LYS GLU GLU THR ILE PRO VAL ILE ILE SER PRO LEU LYS          
SEQRES  19 C  339  THR ILE SER ALA SER LEU GLY SER ARG LEU THR ILE PRO          
SEQRES  20 C  339  CYS LYS VAL PHE LEU GLY THR GLY THR PRO LEU THR THR          
SEQRES  21 C  339  MET LEU TRP TRP THR ALA ASN ASP THR HIS ILE GLU SER          
SEQRES  22 C  339  ALA TYR PRO GLY GLY ARG VAL THR GLU GLY PRO ARG GLN          
SEQRES  23 C  339  GLU TYR SER GLU ASN ASN GLU ASN TYR ILE GLU VAL PRO          
SEQRES  24 C  339  LEU ILE PHE ASP PRO VAL THR ARG GLU ASP LEU HIS MET          
SEQRES  25 C  339  ASP PHE LYS CYS VAL VAL HIS ASN THR LEU SER PHE GLN          
SEQRES  26 C  339  THR LEU ARG THR THR VAL LYS GLU HIS HIS HIS HIS HIS          
SEQRES  27 C  339  HIS                                                          
SEQRES   1 B  339  ALA ASP PRO SER GLU ARG CYS ASP ASP TRP GLY LEU ASP          
SEQRES   2 B  339  THR MET ARG GLN ILE GLN VAL PHE GLU ASP GLU PRO ALA          
SEQRES   3 B  339  ARG ILE LYS CYS PRO LEU PHE GLU HIS PHE LEU LYS PHE          
SEQRES   4 B  339  ASN TYR SER THR ALA HIS SER ALA GLY LEU THR LEU ILE          
SEQRES   5 B  339  TRP TYR TRP THR ARG GLN ASP ARG ASP LEU GLU GLU PRO          
SEQRES   6 B  339  ILE ASN PHE ARG LEU PRO GLU ASN ARG ILE SER LYS GLU          
SEQRES   7 B  339  LYS ASP VAL LEU TRP PHE ARG PRO THR LEU LEU ASN ASP          
SEQRES   8 B  339  THR GLY ASN TYR THR CYS MET LEU ARG ASN THR THR TYR          
SEQRES   9 B  339  CYS SER LYS VAL ALA PHE PRO LEU GLU VAL VAL GLN LYS          
SEQRES  10 B  339  ASP SER CYS PHE ASN SER PRO MET LYS LEU PRO VAL HIS          
SEQRES  11 B  339  LYS LEU TYR ILE GLU TYR GLY ILE GLN ARG ILE THR CYS          
SEQRES  12 B  339  PRO ASN VAL ASP GLY TYR PHE PRO SER SER VAL LYS PRO          
SEQRES  13 B  339  THR ILE THR TRP TYR MET GLY CYS TYR LYS ILE GLN ASN          
SEQRES  14 B  339  PHE ASN ASN VAL ILE PRO GLU GLY MET ASN LEU SER PHE          
SEQRES  15 B  339  LEU ILE ALA LEU ILE SER ASN ASN GLY ASN TYR THR CYS          
SEQRES  16 B  339  VAL VAL THR TYR PRO GLU ASN GLY ARG THR PHE HIS LEU          
SEQRES  17 B  339  THR ARG THR LEU THR VAL LYS VAL VAL GLY SER PRO LYS          
SEQRES  18 B  339  ASN ALA VAL PRO PRO VAL ILE HIS SER PRO ASN ASP HIS          
SEQRES  19 B  339  VAL VAL TYR GLU LYS GLU PRO GLY GLU GLU LEU LEU ILE          
SEQRES  20 B  339  PRO CYS THR VAL TYR PHE SER PHE LEU MET ASP SER ARG          
SEQRES  21 B  339  ASN GLU VAL TRP TRP THR ILE ASP GLY LYS LYS PRO ASP          
SEQRES  22 B  339  ASP ILE THR ILE ASP VAL THR ILE ASN GLU SER ILE SER          
SEQRES  23 B  339  HIS SER ARG THR GLU ASP GLU THR ARG THR GLN ILE LEU          
SEQRES  24 B  339  SER ILE LYS LYS VAL THR SER GLU ASP LEU LYS ARG SER          
SEQRES  25 B  339  TYR VAL CYS HIS ALA ARG SER ALA LYS GLY GLU VAL ALA          
SEQRES  26 B  339  LYS ALA ALA LYS VAL LYS GLN LYS HIS HIS HIS HIS HIS          
SEQRES  27 B  339  HIS                                                          
MODRES 3O4O ASN B   87  ASN  GLYCOSYLATION SITE                                 
MODRES 3O4O ASN B   98  ASN  GLYCOSYLATION SITE                                 
MODRES 3O4O ASN C   99  ASN  GLYCOSYLATION SITE                                 
MODRES 3O4O ASN C  206  ASN  GLYCOSYLATION SITE                                 
MODRES 3O4O ASN B  189  ASN  GLYCOSYLATION SITE                                 
MODRES 3O4O ASN B   91  ASN  GLYCOSYLATION SITE                                 
HET    NAG  B 337      14                                                       
HET    NAG  B 338      14                                                       
HET    NAG  B 339      14                                                       
HET    NAG  B 340      14                                                       
HET    NAG  B 341      14                                                       
HET    NAG  B 342      14                                                       
HET    NAG  C 337      14                                                       
HET    NAG  C 338      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   4  NAG    8(C8 H15 N O6)                                               
HELIX    1   1 GLN A   32  GLN A   39  5                                   8    
HELIX    2   2 THR C  116  ALA C  118  5                                   3    
HELIX    3   3 PHE C  119  SER C  124  1                                   6    
HELIX    4   4 ALA C  185  ALA C  189  5                                   5    
HELIX    5   5 LEU B   85  THR B   89  5                                   5    
HELIX    6   6 LEU B  183  ASN B  187  5                                   5    
HELIX    7   7 SER B  216  ALA B  220  5                                   5    
SHEET    1   A 7 SER A   5  ASP A  12  0                                        
SHEET    2   A 7 PHE A  42  PHE A  46 -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 PHE A 101  ILE A 106 -1  O  PHE A 101   N  VAL A  58           
SHEET    5   A 7 LYS A 109  SER A 114 -1  O  LYS A 109   N  ILE A 106           
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  ARG A  11   O  THR A 147           
SHEET    1   B 2 SER A  17  MET A  20  0                                        
SHEET    2   B 2 LEU A  26  LEU A  29 -1  O  LYS A  27   N  VAL A  19           
SHEET    1   C 2 LEU A  67  LEU A  73  0                                        
SHEET    2   C 2 PRO A  78  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 4 ARG C  16  ARG C  20  0                                        
SHEET    2   E 4 TYR C 102  PHE C 113  1  O  LYS C 105   N  ARG C  18           
SHEET    3   E 4 GLY C  91  VAL C  94 -1  N  GLY C  91   O  LEU C 110           
SHEET    4   E 4 HIS C  57  LYS C  58 -1  N  HIS C  57   O  VAL C  94           
SHEET    1   F 3 GLU C  25  LEU C  28  0                                        
SHEET    2   F 3 TYR C 102  PHE C 113  1  O  PHE C 113   N  ARG C  27           
SHEET    3   F 3 THR C  97  ASN C  99 -1  N  ASN C  99   O  TYR C 102           
SHEET    1   G 3 ALA C  34  ARG C  36  0                                        
SHEET    2   G 3 ALA C  79  LEU C  82 -1  O  LEU C  80   N  LEU C  35           
SHEET    3   G 3 MET C  73  GLN C  76 -1  N  GLN C  76   O  ALA C  79           
SHEET    1   H 4 TYR C 125  THR C 130  0                                        
SHEET    2   H 4 ASN C 206  LYS C 216  1  O  GLU C 212   N  TYR C 125           
SHEET    3   H 4 GLY C 190  THR C 197 -1  N  TYR C 192   O  ILE C 211           
SHEET    4   H 4 TYR C 157  LYS C 158 -1  N  TYR C 157   O  ARG C 193           
SHEET    1   I 3 GLY C 135  VAL C 138  0                                        
SHEET    2   I 3 HIS C 178  VAL C 181 -1  O  LEU C 179   N  LEU C 137           
SHEET    3   I 3 PHE C 170  SER C 172 -1  N  LEU C 171   O  LEU C 180           
SHEET    1   J 4 VAL C 225  ILE C 226  0                                        
SHEET    2   J 4 VAL C 247  LEU C 249 -1  O  PHE C 248   N  VAL C 225           
SHEET    3   J 4 TYR C 292  VAL C 295 -1  O  TYR C 292   N  LEU C 249           
SHEET    4   J 4 GLN C 283  GLU C 284 -1  N  GLN C 283   O  VAL C 295           
SHEET    1   K 3 MET C 258  THR C 262  0                                        
SHEET    2   K 3 LYS C 312  ASN C 317 -1  O  HIS C 316   N  MET C 258           
SHEET    3   K 3 SER C 320  GLN C 322 -1  O  GLN C 322   N  VAL C 315           
SHEET    1   L 2 THR C 278  GLU C 279  0                                        
SHEET    2   L 2 ILE C 298  PHE C 299 -1  O  PHE C 299   N  THR C 278           
SHEET    1   M 3 ASP B   5  TRP B   7  0                                        
SHEET    2   M 3 SER B 103  VAL B 112  1  O  LYS B 104   N  TRP B   7           
SHEET    3   M 3 ILE B  15  PHE B  18  1  N  VAL B  17   O  VAL B 112           
SHEET    1   N 4 ASP B   5  TRP B   7  0                                        
SHEET    2   N 4 SER B 103  VAL B 112  1  O  LYS B 104   N  TRP B   7           
SHEET    3   N 4 GLY B  90  ARG B  97 -1  N  GLY B  90   O  LEU B 109           
SHEET    4   N 4 THR B  47  TRP B  52 -1  N  ILE B  49   O  MET B  95           
SHEET    1   O 4 VAL B 126  TYR B 130  0                                        
SHEET    2   O 4 THR B 202  VAL B 214  1  O  VAL B 214   N  LEU B 129           
SHEET    3   O 4 GLY B 188  PRO B 197 -1  N  TYR B 190   O  LEU B 209           
SHEET    4   O 4 THR B 154  TYR B 158 -1  N  THR B 154   O  THR B 195           
SHEET    1   P 3 GLN B 136  THR B 139  0                                        
SHEET    2   P 3 ASN B 176  PHE B 179 -1  O  LEU B 177   N  ILE B 138           
SHEET    3   P 3 VAL B 170  GLU B 173 -1  N  GLU B 173   O  ASN B 176           
SHEET    1   Q 4 VAL B 224  ILE B 225  0                                        
SHEET    2   Q 4 CYS B 246  TYR B 249 -1  O  TYR B 249   N  VAL B 224           
SHEET    3   Q 4 GLU B 290  ILE B 298 -1  O  ARG B 292   N  VAL B 248           
SHEET    4   Q 4 VAL B 276  HIS B 284 -1  N  SER B 283   O  THR B 291           
SHEET    1   R 3 GLU B 259  THR B 263  0                                        
SHEET    2   R 3 VAL B 311  ARG B 315 -1  O  VAL B 311   N  THR B 263           
SHEET    3   R 3 GLY B 319  LYS B 323 -1  O  GLU B 320   N  ALA B 314           
SSBOND   1 CYS C   15    CYS C  103                          1555   1555  1.90  
SSBOND   2 CYS C   37    CYS C   95                          1555   1555  1.99  
SSBOND   3 CYS C  139    CYS C  194                          1555   1555  1.86  
SSBOND   4 CYS C  245    CYS C  313                          1555   1555  1.82  
SSBOND   5 CYS B    4    CYS B  102                          1555   1555  2.00  
SSBOND   6 CYS B   27    CYS B   94                          1555   1555  2.08  
SSBOND   7 CYS B  117    CYS B  161                          1555   1555  2.20  
SSBOND   8 CYS B  140    CYS B  192                          1555   1555  2.10  
SSBOND   9 CYS B  246    CYS B  312                          1555   1555  2.03  
LINK         ND2 ASN B  87                 C1  NAG B 337     1555   1555  1.44  
LINK         ND2 ASN B  98                 C1  NAG B 340     1555   1555  1.44  
LINK         ND2 ASN C  99                 C1  NAG C 337     1555   1555  1.44  
LINK         O4  NAG B 341                 C1  NAG B 342     1555   1555  1.44  
LINK         O4  NAG B 338                 C1  NAG B 339     1555   1555  1.44  
LINK         ND2 ASN C 206                 C1  NAG C 338     1555   1555  1.45  
LINK         ND2 ASN B 189                 C1  NAG B 341     1555   1555  1.46  
LINK         ND2 ASN B  91                 C1  NAG B 338     1555   1555  1.46  
CISPEP   1 GLY A   22    PRO A   23          0        -0.17                     
CISPEP   2 TYR A   90    PRO A   91          0        -3.41                     
CISPEP   3 VAL C   65    PRO C   66          0         1.99                     
CISPEP   4 LEU C   83    PRO C   84          0        -6.12                     
CISPEP   5 LEU B   67    PRO B   68          0        -0.72                     
CISPEP   6 ARG B   82    PRO B   83          0        -5.61                     
SITE     1 AC1  1 ASN B  87                                                     
SITE     1 AC2  6 LEU B   9  ARG B  54  GLN B  55  GLY B  90                    
SITE     2 AC2  6 ASN B  91  NAG B 339                                          
SITE     1 AC3  1 NAG B 338                                                     
SITE     1 AC4  2 ASN B  98  TYR B 101                                          
SITE     1 AC5  2 ASN B 189  NAG B 342                                          
SITE     1 AC6  1 NAG B 341                                                     
SITE     1 AC7  2 ASN C  99  TYR C 102                                          
SITE     1 AC8  2 TYR C 157  ASN C 206                                          
CRYST1   44.830  177.470  180.660  90.00  90.00  90.00 P 21 21 21    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      0.022306  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005635  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005535        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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