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Database: PDB
Entry: 4DOH
LinkDB: 4DOH
Original site: 4DOH 
HEADER    SIGNALING PROTEIN                       09-FEB-12   4DOH              
TITLE     IL20/IL201/IL20R2 TERNARY COMPLEX                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-20;                                            
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: IL-20, CYTOKINE ZCYTO10;                                    
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: INTERLEUKIN-20 RECEPTOR SUBUNIT BETA;                      
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 SYNONYM: IL-20 RECEPTOR SUBUNIT BETA, IL-20R-BETA, IL-20RB, IL-20R2; 
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: INTERLEUKIN-20 RECEPTOR SUBUNIT ALPHA;                     
COMPND  14 CHAIN: R, E;                                                         
COMPND  15 SYNONYM: IL-20 RECEPTOR SUBUNIT ALPHA, IL-20R-ALPHA, IL-20RA,        
COMPND  16 CYTOKINE RECEPTOR CLASS-II MEMBER 8, CYTOKINE RECEPTOR FAMILY 2      
COMPND  17 MEMBER 8, CRF2-8, IL-20R1, ZCYTOR7;                                  
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: IL20, ZCYTO10, UNQ852/PRO1801;                                 
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA;                                       
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FRUIT FLIES;                               
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7215;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: IL20RB, DIRS1, UNQ557/PRO1114;                                 
SOURCE  14 EXPRESSION_SYSTEM: DROSOPHILA;                                       
SOURCE  15 EXPRESSION_SYSTEM_COMMON: FRUIT FLIES;                               
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7215;                                       
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 GENE: IL20RA, UNQ681/PRO1315;                                        
SOURCE  22 EXPRESSION_SYSTEM: DROSOPHILA;                                       
SOURCE  23 EXPRESSION_SYSTEM_COMMON: FRUIT FLIES;                               
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 7215                                        
KEYWDS    IL10 FAMILY CYTOKINE RECEPTOR COMPLEX, ALPHA HELICAL CYTOKINE FOLD    
KEYWDS   2 BETA SANDWHICH RECEPTOR FOLD, SIGNALING COMPLEX, EXTRACELLULAR,      
KEYWDS   3 SIGNALING PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.J.LOGSDON,M.R.WALTER                                                
REVDAT   5   29-JUL-20 4DOH    1       COMPND REMARK SEQADV HETNAM              
REVDAT   5 2                   1       SITE                                     
REVDAT   4   16-OCT-13 4DOH    1       REMARK                                   
REVDAT   3   02-JAN-13 4DOH    1       JRNL                                     
REVDAT   2   08-AUG-12 4DOH    1       JRNL                                     
REVDAT   1   18-JUL-12 4DOH    0                                                
JRNL        AUTH   N.J.LOGSDON,A.DESHPANDE,B.D.HARRIS,K.R.RAJASHANKAR,          
JRNL        AUTH 2 M.R.WALTER                                                   
JRNL        TITL   STRUCTURAL BASIS FOR RECEPTOR SHARING AND ACTIVATION BY      
JRNL        TITL 2 INTERLEUKIN-20 RECEPTOR-2 (IL-20R2) BINDING CYTOKINES.       
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109 12704 2012              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   22802649                                                     
JRNL        DOI    10.1073/PNAS.1117551109                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 35822                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1952                            
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            : 8822                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 57                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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 4DOH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000070584.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
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                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38635                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.7                               
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) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.7                               
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: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 19% PEG 6000, 0.1M ADA, 0.1M MGCL2, PH   
REMARK 280  6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
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       51.55750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.16700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.88200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.16700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       51.55750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.88200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E                               
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 B    29                                                      
REMARK 465     ASP B    30                                                      
REMARK 465     GLU B    31                                                      
REMARK 465     VAL B    32                                                      
REMARK 465     ALA B    33                                                      
REMARK 465     GLN B   227                                                      
REMARK 465     GLY B   228                                                      
REMARK 465     GLU B   229                                                      
REMARK 465     ALA B   230                                                      
REMARK 465     ILE B   231                                                      
REMARK 465     GLU B   232                                                      
REMARK 465     GLY B   233                                                      
REMARK 465     ARG B   234                                                      
REMARK 465     ALA R    29                                                      
REMARK 465     VAL R    30                                                      
REMARK 465     PRO R    31                                                      
REMARK 465     CYS R    32                                                      
REMARK 465     VAL R    33                                                      
REMARK 465     SER R    34                                                      
REMARK 465     GLY R    35                                                      
REMARK 465     GLY R    36                                                      
REMARK 465     LEU R    37                                                      
REMARK 465     PRO R    38                                                      
REMARK 465     GLN R   243                                                      
REMARK 465     SER R   244                                                      
REMARK 465     SER R   245                                                      
REMARK 465     ILE R   246                                                      
REMARK 465     GLU R   247                                                      
REMARK 465     GLY R   248                                                      
REMARK 465     ARG R   249                                                      
REMARK 465     ALA D    29                                                      
REMARK 465     ASP D    30                                                      
REMARK 465     GLU D    31                                                      
REMARK 465     VAL D    32                                                      
REMARK 465     ALA D    33                                                      
REMARK 465     GLN D   227                                                      
REMARK 465     GLY D   228                                                      
REMARK 465     GLU D   229                                                      
REMARK 465     ALA D   230                                                      
REMARK 465     ILE D   231                                                      
REMARK 465     GLU D   232                                                      
REMARK 465     GLY D   233                                                      
REMARK 465     ARG D   234                                                      
REMARK 465     ALA E    29                                                      
REMARK 465     VAL E    30                                                      
REMARK 465     PRO E    31                                                      
REMARK 465     CYS E    32                                                      
REMARK 465     VAL E    33                                                      
REMARK 465     SER E    34                                                      
REMARK 465     GLY E    35                                                      
REMARK 465     GLY E    36                                                      
REMARK 465     LEU E    37                                                      
REMARK 465     PRO E    38                                                      
REMARK 465     GLN E   243                                                      
REMARK 465     SER E   244                                                      
REMARK 465     SER E   245                                                      
REMARK 465     ILE E   246                                                      
REMARK 465     GLU E   247                                                      
REMARK 465     GLY E   248                                                      
REMARK 465     ARG E   249                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ALA A  24    CB                                                  
REMARK 470     VAL B 167    CG1  CG2                                            
REMARK 470     LYS R  39    CG   CD   CE   NZ                                   
REMARK 470     LYS R 241    CG   CD   CE   NZ                                   
REMARK 470     ALA C  24    CB                                                  
REMARK 470     VAL D 167    CG1  CG2                                            
REMARK 470     LYS E  39    CG   CD   CE   NZ                                   
REMARK 470     LYS E 241    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN E   182     C1   NAG E   301              2.14            
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    LEU A  30       61.22   -118.17                                   
REMARK 500    ARG A  67      -19.29    114.92                                   
REMARK 500    VAL A  94      -74.57   -104.90                                   
REMARK 500    PRO A 154      -85.32    -32.84                                   
REMARK 500    GLU B  62     -157.81    -69.69                                   
REMARK 500    THR B  79       59.34   -147.28                                   
REMARK 500    CYS B  89       62.81   -116.36                                   
REMARK 500    LEU B  91       71.19     72.96                                   
REMARK 500    PRO B  95       45.10    -76.02                                   
REMARK 500    SER B 122     -176.87    -68.26                                   
REMARK 500    ARG B 172       77.64    -67.92                                   
REMARK 500    ALA B 200      118.56     91.47                                   
REMARK 500    PRO R  40      170.12    -58.28                                   
REMARK 500    MET R  50       -1.84     83.95                                   
REMARK 500    PRO R  59     -108.16    -56.04                                   
REMARK 500    GLU R  60      -11.95   -149.60                                   
REMARK 500    GLN R  63      -65.29   -127.69                                   
REMARK 500    TYR R  76      125.56    -37.18                                   
REMARK 500    GLU R  86        1.66    -65.67                                   
REMARK 500    ASN R  89       87.77     53.00                                   
REMARK 500    TRP R 116      -97.34   -115.78                                   
REMARK 500    LYS R 122     -117.63    -17.06                                   
REMARK 500    ASN R 191       18.48     58.76                                   
REMARK 500    PRO R 231      122.00    -39.23                                   
REMARK 500    ARG C  67      -45.00    116.19                                   
REMARK 500    ARG C  93       18.61   -143.17                                   
REMARK 500    ASP C 102      108.72    -45.20                                   
REMARK 500    THR C 131       11.67   -141.15                                   
REMARK 500    CYS C 132       58.62   -119.30                                   
REMARK 500    PRO C 154      -72.50    -21.84                                   
REMARK 500    LEU D  35      104.84    -51.16                                   
REMARK 500    PRO D  38      144.88    -34.52                                   
REMARK 500    GLN D  40       82.32     44.31                                   
REMARK 500    SER D  80       -7.78    -56.51                                   
REMARK 500    LEU D  91       65.80     82.99                                   
REMARK 500    PRO D  95       34.01    -84.97                                   
REMARK 500    ALA D 176      162.82    -48.26                                   
REMARK 500    ALA D 200      125.56     98.75                                   
REMARK 500    MET E  50       10.02     59.15                                   
REMARK 500    PRO E  58      142.78    -34.68                                   
REMARK 500    PRO E  59     -119.86    -57.07                                   
REMARK 500    GLN E  63      -68.35   -127.36                                   
REMARK 500    VAL E  65      -36.05    -38.89                                   
REMARK 500    LYS E  66       70.17   -105.63                                   
REMARK 500    GLU E  86       -8.83    -56.18                                   
REMARK 500    ASN E  89       91.64     49.49                                   
REMARK 500    ARG E  92      171.50    -54.48                                   
REMARK 500    TRP E 116      -97.99   -116.55                                   
REMARK 500    LYS E 122     -150.32     13.49                                   
REMARK 500    ASP E 147     -119.57   -104.35                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY B  198     ALA B  199                 -145.98                    
REMARK 500 GLY D  187     ILE D  188                 -149.94                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG B  301                                                       
REMARK 610     NAG R  301                                                       
REMARK 610     NAG R  302                                                       
REMARK 610     NAG D  301                                                       
REMARK 610     NAG E  301                                                       
DBREF  4DOH A   25   176  UNP    Q9NYY1   IL20_HUMAN      25    176             
DBREF  4DOH B   30   231  UNP    Q6UXL0   I20RB_HUMAN     30    231             
DBREF  4DOH R   29   245  UNP    Q9UHF4   I20RA_HUMAN     29    245             
DBREF  4DOH C   25   176  UNP    Q9NYY1   IL20_HUMAN      25    176             
DBREF  4DOH D   30   231  UNP    Q6UXL0   I20RB_HUMAN     30    231             
DBREF  4DOH E   29   245  UNP    Q9UHF4   I20RA_HUMAN     29    245             
SEQADV 4DOH ALA A   24  UNP  Q9NYY1              EXPRESSION TAG                 
SEQADV 4DOH ALA B   29  UNP  Q6UXL0              EXPRESSION TAG                 
SEQADV 4DOH GLN B   40  UNP  Q6UXL0    ASN    40 ENGINEERED MUTATION            
SEQADV 4DOH GLN B  134  UNP  Q6UXL0    ASN   134 ENGINEERED MUTATION            
SEQADV 4DOH GLU B  232  UNP  Q6UXL0              EXPRESSION TAG                 
SEQADV 4DOH GLY B  233  UNP  Q6UXL0              EXPRESSION TAG                 
SEQADV 4DOH ARG B  234  UNP  Q6UXL0              EXPRESSION TAG                 
SEQADV 4DOH ARG R  111  UNP  Q9UHF4    LYS   111 ENGINEERED MUTATION            
SEQADV 4DOH ARG R  113  UNP  Q9UHF4    LYS   113 ENGINEERED MUTATION            
SEQADV 4DOH ILE R  246  UNP  Q9UHF4              EXPRESSION TAG                 
SEQADV 4DOH GLU R  247  UNP  Q9UHF4              EXPRESSION TAG                 
SEQADV 4DOH GLY R  248  UNP  Q9UHF4              EXPRESSION TAG                 
SEQADV 4DOH ARG R  249  UNP  Q9UHF4              EXPRESSION TAG                 
SEQADV 4DOH ALA C   24  UNP  Q9NYY1              EXPRESSION TAG                 
SEQADV 4DOH ALA D   29  UNP  Q6UXL0              EXPRESSION TAG                 
SEQADV 4DOH GLN D   40  UNP  Q6UXL0    ASN    40 ENGINEERED MUTATION            
SEQADV 4DOH GLN D  134  UNP  Q6UXL0    ASN   134 ENGINEERED MUTATION            
SEQADV 4DOH GLU D  232  UNP  Q6UXL0              EXPRESSION TAG                 
SEQADV 4DOH GLY D  233  UNP  Q6UXL0              EXPRESSION TAG                 
SEQADV 4DOH ARG D  234  UNP  Q6UXL0              EXPRESSION TAG                 
SEQADV 4DOH ARG E  111  UNP  Q9UHF4    LYS   111 ENGINEERED MUTATION            
SEQADV 4DOH ARG E  113  UNP  Q9UHF4    LYS   113 ENGINEERED MUTATION            
SEQADV 4DOH ILE E  246  UNP  Q9UHF4              EXPRESSION TAG                 
SEQADV 4DOH GLU E  247  UNP  Q9UHF4              EXPRESSION TAG                 
SEQADV 4DOH GLY E  248  UNP  Q9UHF4              EXPRESSION TAG                 
SEQADV 4DOH ARG E  249  UNP  Q9UHF4              EXPRESSION TAG                 
SEQRES   1 A  153  ALA LEU LYS THR LEU ASN LEU GLY SER CYS VAL ILE ALA          
SEQRES   2 A  153  THR ASN LEU GLN GLU ILE ARG ASN GLY PHE SER GLU ILE          
SEQRES   3 A  153  ARG GLY SER VAL GLN ALA LYS ASP GLY ASN ILE ASP ILE          
SEQRES   4 A  153  ARG ILE LEU ARG ARG THR GLU SER LEU GLN ASP THR LYS          
SEQRES   5 A  153  PRO ALA ASN ARG CYS CYS LEU LEU ARG HIS LEU LEU ARG          
SEQRES   6 A  153  LEU TYR LEU ASP ARG VAL PHE LYS ASN TYR GLN THR PRO          
SEQRES   7 A  153  ASP HIS TYR THR LEU ARG LYS ILE SER SER LEU ALA ASN          
SEQRES   8 A  153  SER PHE LEU THR ILE LYS LYS ASP LEU ARG LEU CYS HIS          
SEQRES   9 A  153  ALA HIS MET THR CYS HIS CYS GLY GLU GLU ALA MET LYS          
SEQRES  10 A  153  LYS TYR SER GLN ILE LEU SER HIS PHE GLU LYS LEU GLU          
SEQRES  11 A  153  PRO GLN ALA ALA VAL VAL LYS ALA LEU GLY GLU LEU ASP          
SEQRES  12 A  153  ILE LEU LEU GLN TRP MET GLU GLU THR GLU                      
SEQRES   1 B  206  ALA ASP GLU VAL ALA ILE LEU PRO ALA PRO GLN GLN LEU          
SEQRES   2 B  206  SER VAL LEU SER THR ASN MET LYS HIS LEU LEU MET TRP          
SEQRES   3 B  206  SER PRO VAL ILE ALA PRO GLY GLU THR VAL TYR TYR SER          
SEQRES   4 B  206  VAL GLU TYR GLN GLY GLU TYR GLU SER LEU TYR THR SER          
SEQRES   5 B  206  HIS ILE TRP ILE PRO SER SER TRP CYS SER LEU THR GLU          
SEQRES   6 B  206  GLY PRO GLU CYS ASP VAL THR ASP ASP ILE THR ALA THR          
SEQRES   7 B  206  VAL PRO TYR ASN LEU ARG VAL ARG ALA THR LEU GLY SER          
SEQRES   8 B  206  GLN THR SER ALA TRP SER ILE LEU LYS HIS PRO PHE ASN          
SEQRES   9 B  206  ARG GLN SER THR ILE LEU THR ARG PRO GLY MET GLU ILE          
SEQRES  10 B  206  THR LYS ASP GLY PHE HIS LEU VAL ILE GLU LEU GLU ASP          
SEQRES  11 B  206  LEU GLY PRO GLN PHE GLU PHE LEU VAL ALA TYR TRP ARG          
SEQRES  12 B  206  ARG GLU PRO GLY ALA GLU GLU HIS VAL LYS MET VAL ARG          
SEQRES  13 B  206  SER GLY GLY ILE PRO VAL HIS LEU GLU THR MET GLU PRO          
SEQRES  14 B  206  GLY ALA ALA TYR CYS VAL LYS ALA GLN THR PHE VAL LYS          
SEQRES  15 B  206  ALA ILE GLY ARG TYR SER ALA PHE SER GLN THR GLU CYS          
SEQRES  16 B  206  VAL GLU VAL GLN GLY GLU ALA ILE GLU GLY ARG                  
SEQRES   1 R  221  ALA VAL PRO CYS VAL SER GLY GLY LEU PRO LYS PRO ALA          
SEQRES   2 R  221  ASN ILE THR PHE LEU SER ILE ASN MET LYS ASN VAL LEU          
SEQRES   3 R  221  GLN TRP THR PRO PRO GLU GLY LEU GLN GLY VAL LYS VAL          
SEQRES   4 R  221  THR TYR THR VAL GLN TYR PHE ILE TYR GLY GLN LYS LYS          
SEQRES   5 R  221  TRP LEU ASN LYS SER GLU CYS ARG ASN ILE ASN ARG THR          
SEQRES   6 R  221  TYR CYS ASP LEU SER ALA GLU THR SER ASP TYR GLU HIS          
SEQRES   7 R  221  GLN TYR TYR ALA ARG VAL ARG ALA ILE TRP GLY THR LYS          
SEQRES   8 R  221  CYS SER LYS TRP ALA GLU SER GLY ARG PHE TYR PRO PHE          
SEQRES   9 R  221  LEU GLU THR GLN ILE GLY PRO PRO GLU VAL ALA LEU THR          
SEQRES  10 R  221  THR ASP GLU LYS SER ILE SER VAL VAL LEU THR ALA PRO          
SEQRES  11 R  221  GLU LYS TRP LYS ARG ASN PRO GLU ASP LEU PRO VAL SER          
SEQRES  12 R  221  MET GLN GLN ILE TYR SER ASN LEU LYS TYR ASN VAL SER          
SEQRES  13 R  221  VAL LEU ASN THR LYS SER ASN ARG THR TRP SER GLN CYS          
SEQRES  14 R  221  VAL THR ASN HIS THR LEU VAL LEU THR TRP LEU GLU PRO          
SEQRES  15 R  221  ASN THR LEU TYR CYS VAL HIS VAL GLU SER PHE VAL PRO          
SEQRES  16 R  221  GLY PRO PRO ARG ARG ALA GLN PRO SER GLU LYS GLN CYS          
SEQRES  17 R  221  ALA ARG THR LEU LYS ASP GLN SER SER ILE GLU GLY ARG          
SEQRES   1 C  153  ALA LEU LYS THR LEU ASN LEU GLY SER CYS VAL ILE ALA          
SEQRES   2 C  153  THR ASN LEU GLN GLU ILE ARG ASN GLY PHE SER GLU ILE          
SEQRES   3 C  153  ARG GLY SER VAL GLN ALA LYS ASP GLY ASN ILE ASP ILE          
SEQRES   4 C  153  ARG ILE LEU ARG ARG THR GLU SER LEU GLN ASP THR LYS          
SEQRES   5 C  153  PRO ALA ASN ARG CYS CYS LEU LEU ARG HIS LEU LEU ARG          
SEQRES   6 C  153  LEU TYR LEU ASP ARG VAL PHE LYS ASN TYR GLN THR PRO          
SEQRES   7 C  153  ASP HIS TYR THR LEU ARG LYS ILE SER SER LEU ALA ASN          
SEQRES   8 C  153  SER PHE LEU THR ILE LYS LYS ASP LEU ARG LEU CYS HIS          
SEQRES   9 C  153  ALA HIS MET THR CYS HIS CYS GLY GLU GLU ALA MET LYS          
SEQRES  10 C  153  LYS TYR SER GLN ILE LEU SER HIS PHE GLU LYS LEU GLU          
SEQRES  11 C  153  PRO GLN ALA ALA VAL VAL LYS ALA LEU GLY GLU LEU ASP          
SEQRES  12 C  153  ILE LEU LEU GLN TRP MET GLU GLU THR GLU                      
SEQRES   1 D  206  ALA ASP GLU VAL ALA ILE LEU PRO ALA PRO GLN GLN LEU          
SEQRES   2 D  206  SER VAL LEU SER THR ASN MET LYS HIS LEU LEU MET TRP          
SEQRES   3 D  206  SER PRO VAL ILE ALA PRO GLY GLU THR VAL TYR TYR SER          
SEQRES   4 D  206  VAL GLU TYR GLN GLY GLU TYR GLU SER LEU TYR THR SER          
SEQRES   5 D  206  HIS ILE TRP ILE PRO SER SER TRP CYS SER LEU THR GLU          
SEQRES   6 D  206  GLY PRO GLU CYS ASP VAL THR ASP ASP ILE THR ALA THR          
SEQRES   7 D  206  VAL PRO TYR ASN LEU ARG VAL ARG ALA THR LEU GLY SER          
SEQRES   8 D  206  GLN THR SER ALA TRP SER ILE LEU LYS HIS PRO PHE ASN          
SEQRES   9 D  206  ARG GLN SER THR ILE LEU THR ARG PRO GLY MET GLU ILE          
SEQRES  10 D  206  THR LYS ASP GLY PHE HIS LEU VAL ILE GLU LEU GLU ASP          
SEQRES  11 D  206  LEU GLY PRO GLN PHE GLU PHE LEU VAL ALA TYR TRP ARG          
SEQRES  12 D  206  ARG GLU PRO GLY ALA GLU GLU HIS VAL LYS MET VAL ARG          
SEQRES  13 D  206  SER GLY GLY ILE PRO VAL HIS LEU GLU THR MET GLU PRO          
SEQRES  14 D  206  GLY ALA ALA TYR CYS VAL LYS ALA GLN THR PHE VAL LYS          
SEQRES  15 D  206  ALA ILE GLY ARG TYR SER ALA PHE SER GLN THR GLU CYS          
SEQRES  16 D  206  VAL GLU VAL GLN GLY GLU ALA ILE GLU GLY ARG                  
SEQRES   1 E  221  ALA VAL PRO CYS VAL SER GLY GLY LEU PRO LYS PRO ALA          
SEQRES   2 E  221  ASN ILE THR PHE LEU SER ILE ASN MET LYS ASN VAL LEU          
SEQRES   3 E  221  GLN TRP THR PRO PRO GLU GLY LEU GLN GLY VAL LYS VAL          
SEQRES   4 E  221  THR TYR THR VAL GLN TYR PHE ILE TYR GLY GLN LYS LYS          
SEQRES   5 E  221  TRP LEU ASN LYS SER GLU CYS ARG ASN ILE ASN ARG THR          
SEQRES   6 E  221  TYR CYS ASP LEU SER ALA GLU THR SER ASP TYR GLU HIS          
SEQRES   7 E  221  GLN TYR TYR ALA ARG VAL ARG ALA ILE TRP GLY THR LYS          
SEQRES   8 E  221  CYS SER LYS TRP ALA GLU SER GLY ARG PHE TYR PRO PHE          
SEQRES   9 E  221  LEU GLU THR GLN ILE GLY PRO PRO GLU VAL ALA LEU THR          
SEQRES  10 E  221  THR ASP GLU LYS SER ILE SER VAL VAL LEU THR ALA PRO          
SEQRES  11 E  221  GLU LYS TRP LYS ARG ASN PRO GLU ASP LEU PRO VAL SER          
SEQRES  12 E  221  MET GLN GLN ILE TYR SER ASN LEU LYS TYR ASN VAL SER          
SEQRES  13 E  221  VAL LEU ASN THR LYS SER ASN ARG THR TRP SER GLN CYS          
SEQRES  14 E  221  VAL THR ASN HIS THR LEU VAL LEU THR TRP LEU GLU PRO          
SEQRES  15 E  221  ASN THR LEU TYR CYS VAL HIS VAL GLU SER PHE VAL PRO          
SEQRES  16 E  221  GLY PRO PRO ARG ARG ALA GLN PRO SER GLU LYS GLN CYS          
SEQRES  17 E  221  ALA ARG THR LEU LYS ASP GLN SER SER ILE GLU GLY ARG          
HET    NAG  B 301      14                                                       
HET    NAG  R 301      14                                                       
HET    NAG  R 302      14                                                       
HET    NAG  D 301      14                                                       
HET    NAG  E 301      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   7  NAG    5(C8 H15 N O6)                                               
FORMUL  12  HOH   *57(H2 O)                                                     
HELIX    1   1 ASN A   38  GLU A   48  1                                  11    
HELIX    2   2 ILE A   49  LYS A   56  1                                   8    
HELIX    3   3 LYS A   75  VAL A   94  1                                  20    
HELIX    4   4 PHE A   95  TYR A   98  5                                   4    
HELIX    5   5 ASP A  102  HIS A  129  1                                  28    
HELIX    6   6 GLY A  135  LEU A  152  1                                  18    
HELIX    7   7 GLU A  153  GLY A  163  1                                  11    
HELIX    8   8 GLU A  164  THR A  175  1                                  12    
HELIX    9   9 GLU B   73  THR B   79  1                                   7    
HELIX   10  10 ASN B  132  THR B  136  5                                   5    
HELIX   11  11 LYS B  210  GLY B  213  5                                   4    
HELIX   12  12 SER R   85  ARG R   88  5                                   4    
HELIX   13  13 TYR R  130  THR R  135  1                                   6    
HELIX   14  14 SER R  171  TYR R  176  1                                   6    
HELIX   15  15 ASN C   38  LYS C   56  1                                  19    
HELIX   16  16 LYS C   75  VAL C   94  1                                  20    
HELIX   17  17 ASP C  102  HIS C  129  1                                  28    
HELIX   18  18 GLY C  135  LEU C  152  1                                  18    
HELIX   19  19 GLU C  153  GLU C  164  1                                  12    
HELIX   20  20 GLU C  164  GLU C  174  1                                  11    
HELIX   21  21 GLY D   72  THR D   79  1                                   8    
HELIX   22  22 ASN D  132  THR D  136  5                                   5    
HELIX   23  23 SER E   85  ARG E   88  5                                   4    
HELIX   24  24 TYR E  130  THR E  135  1                                   6    
HELIX   25  25 SER E  171  TYR E  176  1                                   6    
SHEET    1   A 2 LYS A  26  LEU A  30  0                                        
SHEET    2   A 2 CYS A  33  THR A  37 -1  O  THR A  37   N  LYS A  26           
SHEET    1   B 3 SER B  42  THR B  46  0                                        
SHEET    2   B 3 LYS B  49  MET B  53 -1  O  LEU B  51   N  LEU B  44           
SHEET    3   B 3 GLU B  96  ASP B  98 -1  O  CYS B  97   N  LEU B  52           
SHEET    1   C 4 ILE B  84  THR B  92  0                                        
SHEET    2   C 4 TYR B  65  GLY B  72 -1  N  TYR B  70   O  ILE B  84           
SHEET    3   C 4 TYR B 109  LEU B 117 -1  O  ASN B 110   N  GLN B  71           
SHEET    4   C 4 GLN B 120  THR B 121 -1  O  GLN B 120   N  LEU B 117           
SHEET    1   D 4 ILE B  84  THR B  92  0                                        
SHEET    2   D 4 TYR B  65  GLY B  72 -1  N  TYR B  70   O  ILE B  84           
SHEET    3   D 4 TYR B 109  LEU B 117 -1  O  ASN B 110   N  GLN B  71           
SHEET    4   D 4 SER B 125  ILE B 126 -1  O  SER B 125   N  VAL B 113           
SHEET    1   E 3 MET B 143  ASP B 148  0                                        
SHEET    2   E 3 HIS B 151  LEU B 156 -1  O  VAL B 153   N  THR B 146           
SHEET    3   E 3 PRO B 189  THR B 194 -1  O  VAL B 190   N  ILE B 154           
SHEET    1   F 4 HIS B 179  VAL B 183  0                                        
SHEET    2   F 4 GLU B 164  ARG B 171 -1  N  VAL B 167   O  LYS B 181           
SHEET    3   F 4 TYR B 201  VAL B 209 -1  O  GLN B 206   N  LEU B 166           
SHEET    4   F 4 ARG B 214  TYR B 215 -1  O  ARG B 214   N  VAL B 209           
SHEET    1   G 4 HIS B 179  VAL B 183  0                                        
SHEET    2   G 4 GLU B 164  ARG B 171 -1  N  VAL B 167   O  LYS B 181           
SHEET    3   G 4 TYR B 201  VAL B 209 -1  O  GLN B 206   N  LEU B 166           
SHEET    4   G 4 GLU B 222  VAL B 224 -1  O  GLU B 222   N  VAL B 203           
SHEET    1   H 3 ALA R  41  ILE R  48  0                                        
SHEET    2   H 3 LYS R  51  THR R  57 -1  O  THR R  57   N  ALA R  41           
SHEET    3   H 3 TYR R  94  ASP R  96 -1  O  CYS R  95   N  LEU R  54           
SHEET    1   I 4 LEU R  82  ASN R  83  0                                        
SHEET    2   I 4 THR R  68  ILE R  75 -1  N  TYR R  73   O  LEU R  82           
SHEET    3   I 4 TYR R 108  ILE R 115 -1  O  ARG R 111   N  GLN R  72           
SHEET    4   I 4 ALA R 124  GLU R 125 -1  O  ALA R 124   N  VAL R 112           
SHEET    1   J 3 GLU R 141  THR R 145  0                                        
SHEET    2   J 3 ILE R 151  THR R 156 -1  O  SER R 152   N  THR R 145           
SHEET    3   J 3 THR R 202  LEU R 205 -1  O  LEU R 205   N  ILE R 151           
SHEET    1   K 4 ARG R 192  VAL R 198  0                                        
SHEET    2   K 4 LYS R 180  ASN R 187 -1  N  VAL R 183   O  GLN R 196           
SHEET    3   K 4 LEU R 213  PHE R 221 -1  O  CYS R 215   N  LEU R 186           
SHEET    4   K 4 GLU R 233  ARG R 238 -1  O  ALA R 237   N  TYR R 214           
SHEET    1   L 2 LYS C  26  LEU C  30  0                                        
SHEET    2   L 2 CYS C  33  THR C  37 -1  O  ILE C  35   N  LEU C  28           
SHEET    1   M 3 GLN D  39  THR D  46  0                                        
SHEET    2   M 3 LYS D  49  SER D  55 -1  O  SER D  55   N  GLN D  39           
SHEET    3   M 3 GLU D  96  ASP D  98 -1  O  CYS D  97   N  LEU D  52           
SHEET    1   N 4 ILE D  84  THR D  92  0                                        
SHEET    2   N 4 TYR D  65  GLN D  71 -1  N  TYR D  70   O  ILE D  84           
SHEET    3   N 4 ASN D 110  LEU D 117 -1  O  ARG D 112   N  GLU D  69           
SHEET    4   N 4 GLN D 120  THR D 121 -1  N  GLN D 120   O  LEU D 117           
SHEET    1   O 4 ILE D  84  THR D  92  0                                        
SHEET    2   O 4 TYR D  65  GLN D  71 -1  N  TYR D  70   O  ILE D  84           
SHEET    3   O 4 ASN D 110  LEU D 117 -1  O  ARG D 112   N  GLU D  69           
SHEET    4   O 4 SER D 125  ILE D 126 -1  O  SER D 125   N  VAL D 113           
SHEET    1   P 3 MET D 143  ASP D 148  0                                        
SHEET    2   P 3 HIS D 151  LEU D 156 -1  O  HIS D 151   N  ASP D 148           
SHEET    3   P 3 VAL D 190  THR D 194 -1  O  VAL D 190   N  ILE D 154           
SHEET    1   Q 4 HIS D 179  VAL D 183  0                                        
SHEET    2   Q 4 GLU D 164  ARG D 171 -1  N  VAL D 167   O  LYS D 181           
SHEET    3   Q 4 TYR D 201  PHE D 208 -1  O  LYS D 204   N  ALA D 168           
SHEET    4   Q 4 GLU D 222  VAL D 224 -1  O  GLU D 222   N  VAL D 203           
SHEET    1   R 3 ALA E  41  ILE E  48  0                                        
SHEET    2   R 3 LYS E  51  THR E  57 -1  O  THR E  57   N  ALA E  41           
SHEET    3   R 3 TYR E  94  ASP E  96 -1  O  CYS E  95   N  LEU E  54           
SHEET    1   S 4 LEU E  82  ASN E  83  0                                        
SHEET    2   S 4 THR E  68  ILE E  75 -1  N  TYR E  73   O  LEU E  82           
SHEET    3   S 4 TYR E 108  ILE E 115 -1  O  ILE E 115   N  THR E  68           
SHEET    4   S 4 ALA E 124  GLU E 125 -1  O  ALA E 124   N  VAL E 112           
SHEET    1   T 3 GLU E 141  THR E 146  0                                        
SHEET    2   T 3 ILE E 151  THR E 156 -1  O  SER E 152   N  THR E 145           
SHEET    3   T 3 THR E 202  LEU E 205 -1  O  LEU E 205   N  ILE E 151           
SHEET    1   U 4 ARG E 192  VAL E 198  0                                        
SHEET    2   U 4 LYS E 180  ASN E 187 -1  N  VAL E 185   O  TRP E 194           
SHEET    3   U 4 LEU E 213  PHE E 221 -1  O  GLU E 219   N  ASN E 182           
SHEET    4   U 4 GLN E 235  ARG E 238 -1  O  GLN E 235   N  VAL E 216           
SSBOND   1 CYS A   33    CYS A  126                          1555   1555  2.05  
SSBOND   2 CYS A   80    CYS A  132                          1555   1555  2.04  
SSBOND   3 CYS A   81    CYS A  134                          1555   1555  2.04  
SSBOND   4 CYS B   89    CYS B   97                          1555   1555  2.04  
SSBOND   5 CYS B  202    CYS B  223                          1555   1555  2.05  
SSBOND   6 CYS R   87    CYS R   95                          1555   1555  2.04  
SSBOND   7 CYS R  215    CYS R  236                          1555   1555  2.04  
SSBOND   8 CYS C   33    CYS C  126                          1555   1555  2.05  
SSBOND   9 CYS C   80    CYS C  132                          1555   1555  2.04  
SSBOND  10 CYS C   81    CYS C  134                          1555   1555  2.05  
SSBOND  11 CYS D   89    CYS D   97                          1555   1555  2.03  
SSBOND  12 CYS D  202    CYS D  223                          1555   1555  2.04  
SSBOND  13 CYS E   87    CYS E   95                          1555   1555  2.05  
SSBOND  14 CYS E  215    CYS E  236                          1555   1555  2.04  
CRYST1  103.115  111.764  136.334  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009698  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008947  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007335        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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