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Database: PDB
Entry: 3DGC
LinkDB: 3DGC
Original site: 3DGC 
HEADER    CYTOKINE/SIGNALING PROTEIN              13-JUN-08   3DGC              
TITLE     STRUCTURE OF IL-22/IL-22R1                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-22;                                            
COMPND   3 CHAIN: L, M;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 39-179;                                       
COMPND   5 SYNONYM: IL-22, IL-10-RELATED T-CELL-DERIVED-INDUCIBLE FACTOR, IL-   
COMPND   6 TIF;                                                                 
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTERLEUKIN-22 RECEPTOR SUBUNIT ALPHA-1;                   
COMPND  10 CHAIN: R, S;                                                         
COMPND  11 FRAGMENT: UNP RESIDUES 19-225;                                       
COMPND  12 SYNONYM: IL-22R-ALPHA-1, CYTOKINE RECEPTOR FAMILY 2 MEMBER 9, CRF2-9;
COMPND  13 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606                                                 
KEYWDS    IL-22, IL-22R1, CYTOKINE, RECEPTOR, SIGNALING MOLECULE, GLYCOPROTEIN, 
KEYWDS   2 SECRETED, MEMBRANE, TRANSMEMBRANE, CYTOKINE-SIGNALING PROTEIN        
KEYWDS   3 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.C.JONES,N.J.LOGSDON,M.R.WALTER                                      
REVDAT   5   13-JUL-11 3DGC    1       VERSN                                    
REVDAT   4   14-JUL-09 3DGC    1       REMARK                                   
REVDAT   3   24-FEB-09 3DGC    1       VERSN                                    
REVDAT   2   23-SEP-08 3DGC    1       JRNL                                     
REVDAT   1   15-JUL-08 3DGC    0                                                
JRNL        AUTH   B.C.JONES,N.J.LOGSDON,M.R.WALTER                             
JRNL        TITL   STRUCTURE OF IL-22 BOUND TO ITS HIGH-AFFINITY IL-22R1 CHAIN. 
JRNL        REF    STRUCTURE                     V.  16  1333 2008              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   18599299                                                     
JRNL        DOI    10.1016/J.STR.2008.06.005                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 25664                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1367                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5569                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 85                                      
REMARK   3   SOLVENT ATOMS            : 164                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.30                          
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3DGC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB048003.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-DEC-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.                                 
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27346                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07100                            
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: SAD                          
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       37.74000            
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, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, R                                  
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, S                                  
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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, R, M, S                            
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     ALA R    17                                                      
REMARK 465     PRO R    18                                                      
REMARK 465     GLU R    19                                                      
REMARK 465     ASP R    20                                                      
REMARK 465     PRO R    21                                                      
REMARK 465     SER R    22                                                      
REMARK 465     ARG R   225                                                      
REMARK 465     THR R   226                                                      
REMARK 465     ALA S    17                                                      
REMARK 465     PRO S    18                                                      
REMARK 465     THR S   226                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS L   61   NZ                                                  
REMARK 480     ILE L  134   CG1  CG2  CD1                                       
REMARK 480     GLU L  135   CG   CD   OE1  OE2                                  
REMARK 480     GLN L  142   CG   CD   OE1  NE2                                  
REMARK 480     LYS L  149   NZ                                                  
REMARK 480     GLU R   46   CG   CD   OE1  OE2                                  
REMARK 480     LYS R  122   CG   CD   CE   NZ                                   
REMARK 480     LYS R  131   CE   NZ                                             
REMARK 480     VAL R  132   CG1  CG2                                            
REMARK 480     GLN R  176   CG   CD   OE1  NE2                                  
REMARK 480     ILE R  201   CD1                                                 
REMARK 480     LYS R  220   CE   NZ                                             
REMARK 480     GLN M  116   CD   OE1  NE2                                       
REMARK 480     LYS S   29   CE   NZ                                             
REMARK 480     ARG S   63   CZ   NH1  NH2                                       
REMARK 480     THR S  174   CB   OG1  CG2                                       
REMARK 480     GLN S  176   CD   OE1  NE2                                       
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   OH   TYR M    90     U     U1 M     9              2.07            
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    HIS L  81       96.39    -35.49                                   
REMARK 500    GLU L 135       55.64    -95.76                                   
REMARK 500    ASP L 138       69.91   -100.22                                   
REMARK 500    LEU L 139      -70.30   -118.41                                   
REMARK 500    GLU R  46       29.08    -70.51                                   
REMARK 500    ALA R 101      -39.34    -38.71                                   
REMARK 500    TYR R 175      112.11    159.85                                   
REMARK 500    ASP R 194       46.40     36.18                                   
REMARK 500    PRO R 223      -83.23    -43.94                                   
REMARK 500    GLN M 112      -65.79    -14.45                                   
REMARK 500    LYS S 131     -168.60   -124.01                                   
REMARK 500    VAL S 171      -91.64    -94.93                                   
REMARK 500    TYR S 175      113.43   -168.68                                   
REMARK 500    ASP S 194       46.49     39.31                                   
REMARK 500    PRO S 223     -127.87    -62.89                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH M 214        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH R 256        DISTANCE =  5.22 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG R 227                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG R 228                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA R 229                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN R 230                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC R 231                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL R 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IUM M 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT M 180                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT M 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL S 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL S 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U1 L 8                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U1 L 11                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U1 R 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U1 R 4                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U1 R 6                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U1 R 7                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U1 M 9                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U1 M 10                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U1 M 12                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U1 S 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U1 S 5                    
DBREF  3DGC L   39   179  UNP    Q9GZX6   IL22_HUMAN      39    179             
DBREF  3DGC R   17   226  UNP    Q9HB22   I22R1_HUMAN     17    226             
DBREF  3DGC M   39   179  UNP    Q9GZX6   IL22_HUMAN      39    179             
DBREF  3DGC S   17   226  UNP    Q9HB22   I22R1_HUMAN     17    226             
SEQADV 3DGC GLN L   68  UNP  Q9GZX6    ASN    68 EXPRESSION TAG                 
SEQADV 3DGC GLN L   97  UNP  Q9GZX6    ASN    97 EXPRESSION TAG                 
SEQADV 3DGC ASP R   80  UNP  Q9HB22    ASN    80 EXPRESSION TAG                 
SEQADV 3DGC ASP R   87  UNP  Q9HB22    ASN    87 EXPRESSION TAG                 
SEQADV 3DGC GLN R   89  UNP  Q9HB22    THR    89 EXPRESSION TAG                 
SEQADV 3DGC GLN M   68  UNP  Q9GZX6    ASN    68 EXPRESSION TAG                 
SEQADV 3DGC GLN M   97  UNP  Q9GZX6    ASN    97 EXPRESSION TAG                 
SEQADV 3DGC ASP S   80  UNP  Q9HB22    ASN    80 EXPRESSION TAG                 
SEQADV 3DGC ASP S   87  UNP  Q9HB22    ASN    87 EXPRESSION TAG                 
SEQADV 3DGC GLN S   89  UNP  Q9HB22    THR    89 EXPRESSION TAG                 
SEQRES   1 L  141  HIS CYS ARG LEU ASP LYS SER ASN PHE GLN GLN PRO TYR          
SEQRES   2 L  141  ILE THR ASN ARG THR PHE MET LEU ALA LYS GLU ALA SER          
SEQRES   3 L  141  LEU ALA ASP GLN ASN THR ASP VAL ARG LEU ILE GLY GLU          
SEQRES   4 L  141  LYS LEU PHE HIS GLY VAL SER MET SER GLU ARG CYS TYR          
SEQRES   5 L  141  LEU MET LYS GLN VAL LEU GLN PHE THR LEU GLU GLU VAL          
SEQRES   6 L  141  LEU PHE PRO GLN SER ASP ARG PHE GLN PRO TYR MET GLN          
SEQRES   7 L  141  GLU VAL VAL PRO PHE LEU ALA ARG LEU SER ASN ARG LEU          
SEQRES   8 L  141  SER THR CYS HIS ILE GLU GLY ASP ASP LEU HIS ILE GLN          
SEQRES   9 L  141  ARG ASN VAL GLN LYS LEU LYS ASP THR VAL LYS LYS LEU          
SEQRES  10 L  141  GLY GLU SER GLY GLU ILE LYS ALA ILE GLY GLU LEU ASP          
SEQRES  11 L  141  LEU LEU PHE MET SER LEU ARG ASN ALA CYS ILE                  
SEQRES   1 R  210  ALA PRO GLU ASP PRO SER ASP LEU LEU GLN HIS VAL LYS          
SEQRES   2 R  210  PHE GLN SER SER ASN PHE GLU ASN ILE LEU THR TRP ASP          
SEQRES   3 R  210  SER GLY PRO GLU GLY THR PRO ASP THR VAL TYR SER ILE          
SEQRES   4 R  210  GLU TYR LYS THR TYR GLY GLU ARG ASP TRP VAL ALA LYS          
SEQRES   5 R  210  LYS GLY CYS GLN ARG ILE THR ARG LYS SER CYS ASP LEU          
SEQRES   6 R  210  THR VAL GLU THR GLY ASP LEU GLN GLU LEU TYR TYR ALA          
SEQRES   7 R  210  ARG VAL THR ALA VAL SER ALA GLY GLY ARG SER ALA THR          
SEQRES   8 R  210  LYS MET THR ASP ARG PHE SER SER LEU GLN HIS THR THR          
SEQRES   9 R  210  LEU LYS PRO PRO ASP VAL THR CYS ILE SER LYS VAL ARG          
SEQRES  10 R  210  SER ILE GLN MET ILE VAL HIS PRO THR PRO THR PRO ILE          
SEQRES  11 R  210  ARG ALA GLY ASP GLY HIS ARG LEU THR LEU GLU ASP ILE          
SEQRES  12 R  210  PHE HIS ASP LEU PHE TYR HIS LEU GLU LEU GLN VAL ASN          
SEQRES  13 R  210  ARG THR TYR GLN MET HIS LEU GLY GLY LYS GLN ARG GLU          
SEQRES  14 R  210  TYR GLU PHE PHE GLY LEU THR PRO ASP THR GLU PHE LEU          
SEQRES  15 R  210  GLY THR ILE MET ILE CYS VAL PRO THR TRP ALA LYS GLU          
SEQRES  16 R  210  SER ALA PRO TYR MET CYS ARG VAL LYS THR LEU PRO ASP          
SEQRES  17 R  210  ARG THR                                                      
SEQRES   1 M  141  HIS CYS ARG LEU ASP LYS SER ASN PHE GLN GLN PRO TYR          
SEQRES   2 M  141  ILE THR ASN ARG THR PHE MET LEU ALA LYS GLU ALA SER          
SEQRES   3 M  141  LEU ALA ASP GLN ASN THR ASP VAL ARG LEU ILE GLY GLU          
SEQRES   4 M  141  LYS LEU PHE HIS GLY VAL SER MET SER GLU ARG CYS TYR          
SEQRES   5 M  141  LEU MET LYS GLN VAL LEU GLN PHE THR LEU GLU GLU VAL          
SEQRES   6 M  141  LEU PHE PRO GLN SER ASP ARG PHE GLN PRO TYR MET GLN          
SEQRES   7 M  141  GLU VAL VAL PRO PHE LEU ALA ARG LEU SER ASN ARG LEU          
SEQRES   8 M  141  SER THR CYS HIS ILE GLU GLY ASP ASP LEU HIS ILE GLN          
SEQRES   9 M  141  ARG ASN VAL GLN LYS LEU LYS ASP THR VAL LYS LYS LEU          
SEQRES  10 M  141  GLY GLU SER GLY GLU ILE LYS ALA ILE GLY GLU LEU ASP          
SEQRES  11 M  141  LEU LEU PHE MET SER LEU ARG ASN ALA CYS ILE                  
SEQRES   1 S  210  ALA PRO GLU ASP PRO SER ASP LEU LEU GLN HIS VAL LYS          
SEQRES   2 S  210  PHE GLN SER SER ASN PHE GLU ASN ILE LEU THR TRP ASP          
SEQRES   3 S  210  SER GLY PRO GLU GLY THR PRO ASP THR VAL TYR SER ILE          
SEQRES   4 S  210  GLU TYR LYS THR TYR GLY GLU ARG ASP TRP VAL ALA LYS          
SEQRES   5 S  210  LYS GLY CYS GLN ARG ILE THR ARG LYS SER CYS ASP LEU          
SEQRES   6 S  210  THR VAL GLU THR GLY ASP LEU GLN GLU LEU TYR TYR ALA          
SEQRES   7 S  210  ARG VAL THR ALA VAL SER ALA GLY GLY ARG SER ALA THR          
SEQRES   8 S  210  LYS MET THR ASP ARG PHE SER SER LEU GLN HIS THR THR          
SEQRES   9 S  210  LEU LYS PRO PRO ASP VAL THR CYS ILE SER LYS VAL ARG          
SEQRES  10 S  210  SER ILE GLN MET ILE VAL HIS PRO THR PRO THR PRO ILE          
SEQRES  11 S  210  ARG ALA GLY ASP GLY HIS ARG LEU THR LEU GLU ASP ILE          
SEQRES  12 S  210  PHE HIS ASP LEU PHE TYR HIS LEU GLU LEU GLN VAL ASN          
SEQRES  13 S  210  ARG THR TYR GLN MET HIS LEU GLY GLY LYS GLN ARG GLU          
SEQRES  14 S  210  TYR GLU PHE PHE GLY LEU THR PRO ASP THR GLU PHE LEU          
SEQRES  15 S  210  GLY THR ILE MET ILE CYS VAL PRO THR TRP ALA LYS GLU          
SEQRES  16 S  210  SER ALA PRO TYR MET CYS ARG VAL LYS THR LEU PRO ASP          
SEQRES  17 S  210  ARG THR                                                      
MODRES 3DGC ASN R  172  ASN  GLYCOSYLATION SITE                                 
HET    NAG  R 227      14                                                       
HET    NAG  R 228      14                                                       
HET    BMA  R 229      11                                                       
HET    MAN  R 230      11                                                       
HET    FUC  R 231      10                                                       
HET     CL  R   3       1                                                       
HET    IUM  M   1       3                                                       
HET    ACT  M 180       4                                                       
HET    ACT  M   2       4                                                       
HET     CL  S   1       1                                                       
HET     CL  S   2       1                                                       
HET     U1  L   8       1                                                       
HET     U1  L  11       1                                                       
HET     U1  R   2       1                                                       
HET     U1  R   4       1                                                       
HET     U1  R   6       1                                                       
HET     U1  R   7       1                                                       
HET     U1  M   9       1                                                       
HET     U1  M  10       1                                                       
HET     U1  M  12       1                                                       
HET     U1  S   3       1                                                       
HET     U1  S   5       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM      CL CHLORIDE ION                                                     
HETNAM     IUM URANYL (VI) ION                                                  
HETNAM     ACT ACETATE ION                                                      
HETNAM      U1 URANIUM ATOM                                                     
FORMUL   5  NAG    2(C8 H15 N O6)                                               
FORMUL   5  BMA    C6 H12 O6                                                    
FORMUL   5  MAN    C6 H12 O6                                                    
FORMUL   5  FUC    C6 H12 O5                                                    
FORMUL   6   CL    3(CL 1-)                                                     
FORMUL   7  IUM    O2 U 2+                                                      
FORMUL   8  ACT    2(C2 H3 O2 1-)                                               
FORMUL  12   U1    11(U)                                                        
FORMUL  23  HOH   *164(H2 O)                                                    
HELIX    1   1 ASP L   43  PHE L   47  5                                   5    
HELIX    2   2 GLN L   49  ASP L   67  1                                  19    
HELIX    3   3 GLY L   76  HIS L   81  5                                   6    
HELIX    4   4 SER L   84  SER L   86  5                                   3    
HELIX    5   5 GLU L   87  VAL L  103  1                                  17    
HELIX    6   6 LEU L  104  SER L  108  5                                   5    
HELIX    7   7 TYR L  114  LEU L  129  1                                  16    
HELIX    8   8 SER L  130  CYS L  132  5                                   3    
HELIX    9   9 LEU L  139  LEU L  155  1                                  17    
HELIX   10  10 LEU L  155  GLU L  166  1                                  12    
HELIX   11  11 GLU L  166  CYS L  178  1                                  13    
HELIX   12  12 SER R  114  THR R  119  1                                   6    
HELIX   13  13 LEU R  156  PHE R  160  1                                   5    
HELIX   14  14 PRO R  206  ALA R  209  5                                   4    
HELIX   15  15 ASP M   43  PHE M   47  5                                   5    
HELIX   16  16 GLN M   49  ASP M   67  1                                  19    
HELIX   17  17 GLY M   76  HIS M   81  5                                   6    
HELIX   18  18 SER M   84  SER M   86  5                                   3    
HELIX   19  19 GLU M   87  VAL M  103  1                                  17    
HELIX   20  20 LEU M  104  SER M  108  5                                   5    
HELIX   21  21 PHE M  111  SER M  130  1                                  20    
HELIX   22  22 ASP M  138  LEU M  155  1                                  18    
HELIX   23  23 LEU M  155  GLY M  165  1                                  11    
HELIX   24  24 GLU M  166  CYS M  178  1                                  13    
HELIX   25  25 ASP S   20  LEU S   24  5                                   5    
HELIX   26  26 SER S  114  THR S  119  1                                   6    
HELIX   27  27 LEU S  156  PHE S  160  1                                   5    
HELIX   28  28 PRO S  206  ALA S  209  5                                   4    
SHEET    1   A 3 LEU R  25  SER R  33  0                                        
SHEET    2   A 3 GLU R  36  SER R  43 -1  O  ASP R  42   N  GLN R  26           
SHEET    3   A 3 SER R  78  ASP R  80 -1  O  CYS R  79   N  LEU R  39           
SHEET    1   B 4 VAL R  66  ALA R  67  0                                        
SHEET    2   B 4 VAL R  52  THR R  59 -1  N  TYR R  57   O  VAL R  66           
SHEET    3   B 4 TYR R  92  VAL R  99 -1  O  VAL R  99   N  VAL R  52           
SHEET    4   B 4 SER R 105  MET R 109 -1  O  ALA R 106   N  ALA R  98           
SHEET    1   C 3 ASP R 125  SER R 130  0                                        
SHEET    2   C 3 ILE R 135  HIS R 140 -1  O  HIS R 140   N  ASP R 125           
SHEET    3   C 3 GLU R 185  PHE R 188 -1  O  TYR R 186   N  MET R 137           
SHEET    1   D 2 PRO R 143  ARG R 147  0                                        
SHEET    2   D 2 ARG R 153  THR R 155 -1  O  LEU R 154   N  ILE R 146           
SHEET    1   E 4 TYR R 175  GLY R 181  0                                        
SHEET    2   E 4 PHE R 164  ASN R 172 -1  N  TYR R 165   O  GLY R 181           
SHEET    3   E 4 GLU R 196  VAL R 205 -1  O  LEU R 198   N  GLN R 170           
SHEET    4   E 4 LYS R 210  GLU R 211 -1  O  LYS R 210   N  VAL R 205           
SHEET    1   F 4 TYR R 175  GLY R 181  0                                        
SHEET    2   F 4 PHE R 164  ASN R 172 -1  N  TYR R 165   O  GLY R 181           
SHEET    3   F 4 GLU R 196  VAL R 205 -1  O  LEU R 198   N  GLN R 170           
SHEET    4   F 4 TYR R 215  LYS R 220 -1  O  VAL R 219   N  PHE R 197           
SHEET    1   G 3 GLN S  26  SER S  33  0                                        
SHEET    2   G 3 GLU S  36  ASP S  42 -1  O  ILE S  38   N  GLN S  31           
SHEET    3   G 3 SER S  78  ASP S  80 -1  O  CYS S  79   N  LEU S  39           
SHEET    1   H 4 VAL S  66  ALA S  67  0                                        
SHEET    2   H 4 VAL S  52  THR S  59 -1  N  TYR S  57   O  VAL S  66           
SHEET    3   H 4 TYR S  92  VAL S  99 -1  O  VAL S  99   N  VAL S  52           
SHEET    4   H 4 SER S 105  MET S 109 -1  O  LYS S 108   N  VAL S  96           
SHEET    1   I 3 VAL S 126  SER S 130  0                                        
SHEET    2   I 3 ILE S 135  VAL S 139 -1  O  GLN S 136   N  ILE S 129           
SHEET    3   I 3 GLU S 185  PHE S 188 -1  O  TYR S 186   N  MET S 137           
SHEET    1   J 2 PRO S 143  ARG S 147  0                                        
SHEET    2   J 2 ARG S 153  THR S 155 -1  O  LEU S 154   N  ILE S 146           
SHEET    1   K 4 TYR S 175  GLY S 181  0                                        
SHEET    2   K 4 PHE S 164  ASN S 172 -1  N  LEU S 167   O  LEU S 179           
SHEET    3   K 4 GLU S 196  VAL S 205 -1  O  LEU S 198   N  GLN S 170           
SHEET    4   K 4 LYS S 210  GLU S 211 -1  O  LYS S 210   N  VAL S 205           
SHEET    1   L 4 TYR S 175  GLY S 181  0                                        
SHEET    2   L 4 PHE S 164  ASN S 172 -1  N  LEU S 167   O  LEU S 179           
SHEET    3   L 4 GLU S 196  VAL S 205 -1  O  LEU S 198   N  GLN S 170           
SHEET    4   L 4 TYR S 215  LYS S 220 -1  O  VAL S 219   N  PHE S 197           
SSBOND   1 CYS L   40    CYS L  132                          1555   1555  2.04  
SSBOND   2 CYS L   89    CYS L  178                          1555   1555  2.04  
SSBOND   3 CYS R   71    CYS R   79                          1555   1555  2.04  
SSBOND   4 CYS R  128    CYS R  217                          1555   1555  2.03  
SSBOND   5 CYS M   40    CYS M  132                          1555   1555  2.03  
SSBOND   6 CYS M   89    CYS M  178                          1555   1555  2.04  
SSBOND   7 CYS S   71    CYS S   79                          1555   1555  2.05  
SSBOND   8 CYS S  128    CYS S  217                          1555   1555  2.03  
LINK         ND2 ASN R 172                 C1  NAG R 227     1555   1555  1.45  
LINK         O4  NAG R 227                 C1  NAG R 228     1555   1555  1.39  
LINK         O6  NAG R 227                 C1  FUC R 231     1555   1555  1.40  
LINK         O4  NAG R 228                 C1  BMA R 229     1555   1555  1.39  
LINK         O6  BMA R 229                 C1  MAN R 230     1555   1555  1.41  
CISPEP   1 GLN L  112    PRO L  113          0         0.15                     
SITE     1 AC1  5 VAL R 171  ASN R 172  TYR R 175  NAG R 228                    
SITE     2 AC1  5 FUC R 231                                                     
SITE     1 AC2  4 TYR M  51  NAG R 227  BMA R 229  HOH R 272                    
SITE     1 AC3  2 NAG R 228  MAN R 230                                          
SITE     1 AC4  4 ARG M  55  TYR M 114  BMA R 229  HOH R 272                    
SITE     1 AC5  6 TYR M  51  TYR R 175  GLY R 190  THR R 192                    
SITE     2 AC5  6 PHE R 197  NAG R 227                                          
SITE     1 AC6  5 THR R 142  LEU R 156  GLU R 157  ARG R 184                    
SITE     2 AC6  5 HOH R 259                                                     
SITE     1 AC7  6 ACT M   2  HIS M 140  ACT M 180  ASP S  23                    
SITE     2 AC7  6 GLU S  46  ARG S 104                                          
SITE     1 AC8  3 IUM M   1  ACT M   2  HIS M  81                               
SITE     1 AC9  7 IUM M   1  HIS M 140  ARG M 143  ACT M 180                    
SITE     2 AC9  7 GLU S  19  ASP S  20  ASP S  23                               
SITE     1 BC1  2 ARG S  76  ASP S  80                                          
SITE     1 BC2  4 THR S 142  LEU S 156  GLU S 157  ARG S 184                    
SITE     1 BC3  1 TYR L  90                                                     
SITE     1 BC4  2 GLU L 101  GLU L 102                                          
SITE     1 BC5  3 ASP R  80  HOH R 242  HOH R 243                               
SITE     1 BC6  1 ASP R 224                                                     
SITE     1 BC7  4 GLU L  77  ASP R  87  GLU R  90  ARG S 173                    
SITE     1 BC8  1 ASP R  23                                                     
SITE     1 BC9  2 TYR M  90  ASP M 138                                          
SITE     1 CC1  4 ASP M  43  ARG M 128  HOH M 187  HOH M 223                    
SITE     1 CC2  3 GLU M 101  GLU M 102  HOH M 190                               
SITE     1 CC3  3 ASP S  80  HOH S 271  HOH S 289                               
SITE     1 CC4  3 GLU M  77  ASP S  87  GLU S  90                               
CRYST1   54.509   75.480  101.140  90.00 100.89  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      0.018346  0.000000  0.003529        0.00000                         
SCALE2      0.000000  0.013249  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010069        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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