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Database: PDB
Entry: 3DI2
LinkDB: 3DI2
Original site: 3DI2 
HEADER    CYTOKINE/CYTOKINE RECEPTOR              19-JUN-08   3DI2              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX OF HUMAN INTERLEUKIN-7               
TITLE    2 WITH UNGLYCOSYLATED HUMAN INTERLEUKIN-7 RECEPTOR ALPHA               
TITLE    3 ECTODOMAIN                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-7;                                             
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 26 TO 177;                                    
COMPND   5 SYNONYM: IL-7;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTERLEUKIN-7 RECEPTOR SUBUNIT ALPHA;                      
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: UNP RESIDUES 21 TO 239 (LIGAND BINDING                     
COMPND  12 ECTODOMAIN);                                                         
COMPND  13 SYNONYM: IL-7R-ALPHA, CD127 ANTIGEN, CDW127;                         
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: IL7;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS RP;                   
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-15B;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: IL7R;                                                          
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS RP;                   
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET-15B                                   
KEYWDS    INTERLEUKIN, CYTOKINE, CYTOKINE RECEPTOR, ECTODOMAIN,                 
KEYWDS   2 GLYCOPROTEIN, GROWTH FACTOR, SECRETED, ALTERNATIVE SPLICING,         
KEYWDS   3 DISEASE MUTATION, MEMBRANE, PHOSPHOPROTEIN, POLYMORPHISM,            
KEYWDS   4 RECEPTOR, SCID, TRANSMEMBRANE, CYTOKINE/CYTOKINE RECEPTOR            
KEYWDS   5 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.A.MCELROY,J.A.DOHM,S.T.R.WALSH                                      
REVDAT   1   27-JAN-09 3DI2    0                                                
JRNL        AUTH   C.A.MCELROY,J.A.DOHM,S.T.WALSH                               
JRNL        TITL   STRUCTURAL AND BIOPHYSICAL STUDIES OF THE HUMAN              
JRNL        TITL 2 IL-7/IL-7RALPHA COMPLEX.                                     
JRNL        REF    STRUCTURE                     V.  17    54 2009              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   19141282                                                     
JRNL        DOI    10.1016/J.STR.2008.10.019                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 69.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 16902                          
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) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1335                            
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            : 4774                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 28                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.03600                                              
REMARK   3    B22 (A**2) : -5.38600                                             
REMARK   3    B33 (A**2) : 1.35000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.33200                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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) : 0.009                           
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) : 1.416 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.534 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.770 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.879 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 34.18                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : 1PE_XPLOR.PARAM                                
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  PARAMETER FILE  7  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : 1PE_XPLOR.TOP                                  
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3  TOPOLOGY FILE  7   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3DI2 COMPLIES WITH FORMAT V. 3.20, 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 RCSB048063.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97932                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21610                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
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     (%) : 88.2                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.34000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% W/V PEG 8000, 0.1M MES, 0.2 M        
REMARK 280  CALCIUM ACETATE, PH 6.0, SITTING DROP, TEMPERATURE 292K             
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       56.51050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1880 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1440 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     MET A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     ASP A     1                                                      
REMARK 465     CYS A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     CYS A    92                                                      
REMARK 465     THR A    93                                                      
REMARK 465     GLY A    94                                                      
REMARK 465     GLN A    95                                                      
REMARK 465     VAL A    96                                                      
REMARK 465     LYS A    97                                                      
REMARK 465     GLY A    98                                                      
REMARK 465     ARG A    99                                                      
REMARK 465     LYS A   100                                                      
REMARK 465     PRO A   101                                                      
REMARK 465     ALA A   102                                                      
REMARK 465     ALA A   103                                                      
REMARK 465     LEU A   104                                                      
REMARK 465     GLY A   105                                                      
REMARK 465     ALA A   106                                                      
REMARK 465     ALA A   107                                                      
REMARK 465     GLN A   108                                                      
REMARK 465     PRO A   109                                                      
REMARK 465     THR A   110                                                      
REMARK 465     LYS A   111                                                      
REMARK 465     SER A   112                                                      
REMARK 465     LEU A   113                                                      
REMARK 465     GLU A   114                                                      
REMARK 465     GLU A   115                                                      
REMARK 465     ASN A   116                                                      
REMARK 465     LYS A   117                                                      
REMARK 465     SER A   118                                                      
REMARK 465     LEU A   119                                                      
REMARK 465     LYS A   120                                                      
REMARK 465     GLU A   121                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     MET B     0                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     TYR B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     GLN B     6                                                      
REMARK 465     ASN B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     ASP B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     ASP B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     LEU B    15                                                      
REMARK 465     ASP B    16                                                      
REMARK 465     ASN B   212                                                      
REMARK 465     ASN B   213                                                      
REMARK 465     SER B   214                                                      
REMARK 465     SER B   215                                                      
REMARK 465     GLY B   216                                                      
REMARK 465     GLU B   217                                                      
REMARK 465     MET B   218                                                      
REMARK 465     ASP B   219                                                      
REMARK 465     MET C    -1                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     ASP C     1                                                      
REMARK 465     CYS C     2                                                      
REMARK 465     ASP C     3                                                      
REMARK 465     ILE C     4                                                      
REMARK 465     GLU C     5                                                      
REMARK 465     GLY C     6                                                      
REMARK 465     LYS C     7                                                      
REMARK 465     ASN C    91                                                      
REMARK 465     CYS C    92                                                      
REMARK 465     THR C    93                                                      
REMARK 465     GLY C    94                                                      
REMARK 465     GLN C    95                                                      
REMARK 465     VAL C    96                                                      
REMARK 465     LYS C    97                                                      
REMARK 465     GLY C    98                                                      
REMARK 465     ARG C    99                                                      
REMARK 465     LYS C   100                                                      
REMARK 465     PRO C   101                                                      
REMARK 465     ALA C   102                                                      
REMARK 465     ALA C   103                                                      
REMARK 465     LEU C   104                                                      
REMARK 465     GLY C   105                                                      
REMARK 465     ALA C   106                                                      
REMARK 465     ALA C   107                                                      
REMARK 465     GLN C   108                                                      
REMARK 465     PRO C   109                                                      
REMARK 465     THR C   110                                                      
REMARK 465     LYS C   111                                                      
REMARK 465     SER C   112                                                      
REMARK 465     LEU C   113                                                      
REMARK 465     GLU C   114                                                      
REMARK 465     GLU C   115                                                      
REMARK 465     ASN C   116                                                      
REMARK 465     LYS C   117                                                      
REMARK 465     SER C   118                                                      
REMARK 465     LEU C   119                                                      
REMARK 465     LYS C   120                                                      
REMARK 465     GLU C   121                                                      
REMARK 465     GLN C   122                                                      
REMARK 465     LYS C   150                                                      
REMARK 465     GLU C   151                                                      
REMARK 465     HIS C   152                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     SER D    -2                                                      
REMARK 465     HIS D    -1                                                      
REMARK 465     MET D     0                                                      
REMARK 465     GLU D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     TYR D     4                                                      
REMARK 465     ALA D     5                                                      
REMARK 465     GLN D     6                                                      
REMARK 465     ASN D     7                                                      
REMARK 465     GLY D     8                                                      
REMARK 465     ASP D     9                                                      
REMARK 465     LEU D    10                                                      
REMARK 465     GLU D    11                                                      
REMARK 465     ASP D    12                                                      
REMARK 465     ALA D    13                                                      
REMARK 465     GLU D   210                                                      
REMARK 465     ILE D   211                                                      
REMARK 465     ASN D   212                                                      
REMARK 465     ASN D   213                                                      
REMARK 465     SER D   214                                                      
REMARK 465     SER D   215                                                      
REMARK 465     GLY D   216                                                      
REMARK 465     GLU D   217                                                      
REMARK 465     MET D   218                                                      
REMARK 465     ASP D   219                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  10    CG   CD   CE   NZ                                   
REMARK 470     GLU A  13    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  28    CD   CE   NZ                                        
REMARK 470     GLU A  29    CG   CD   OE1  OE2                                  
REMARK 470     ILE A  30    CG1  CD1                                            
REMARK 470     SER A  32    OG                                                  
REMARK 470     LEU A  35    CD1  CD2                                            
REMARK 470     ASN A  37    OD1  ND2                                            
REMARK 470     ARG A  44    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  51    CG   CD   CE   NZ                                   
REMARK 470     MET A  54    CG   SD   CE                                        
REMARK 470     LYS A  68    CD   CE   NZ                                        
REMARK 470     MET A  69    CG   SD   CE                                        
REMARK 470     ASN A  70    CG   OD1  ND2                                       
REMARK 470     THR A  72    OG1  CG2                                            
REMARK 470     ASN A  91    CG   OD1  ND2                                       
REMARK 470     GLN A 122    CD   OE1  NE2                                       
REMARK 470     LYS A 124    CD   CE   NZ                                        
REMARK 470     LYS A 150    CG   CD   CE   NZ                                   
REMARK 470     HIS A 152    ND1  CD2  CE1  NE2                                  
REMARK 470     ASN B  29    OD1  ND2                                            
REMARK 470     ASN B  48    CG   OD1  ND2                                       
REMARK 470     LYS B  61    CD   CE   NZ                                        
REMARK 470     GLU B  70    CG   CD   OE1  OE2                                  
REMARK 470     VAL B  91    CG1  CG2                                            
REMARK 470     GLU B  93    CD   OE1  OE2                                       
REMARK 470     LYS B  94    CG   CD   CE   NZ                                   
REMARK 470     SER B  95    OG                                                  
REMARK 470     LYS B 153    CG   CD   CE   NZ                                   
REMARK 470     ASN B 156    CG   OD1  ND2                                       
REMARK 470     LYS B 157    CG   CD   CE   NZ                                   
REMARK 470     GLN B 176    CD   OE1  NE2                                       
REMARK 470     ILE B 211    CG1  CG2  CD1                                       
REMARK 470     LYS C  10    CG   CD   CE   NZ                                   
REMARK 470     GLU C  13    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  28    CD   CE   NZ                                        
REMARK 470     GLU C  29    CG   CD   OE1  OE2                                  
REMARK 470     ILE C  30    CG1  CD1                                            
REMARK 470     SER C  32    OG                                                  
REMARK 470     ASN C  33    CG   OD1  ND2                                       
REMARK 470     LEU C  35    CG   CD1  CD2                                       
REMARK 470     ASN C  37    OD1  ND2                                            
REMARK 470     GLU C  38    CD   OE1  OE2                                       
REMARK 470     ARG C  44    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  51    CG   CD   CE   NZ                                   
REMARK 470     MET C  54    CG   SD   CE                                        
REMARK 470     ARG C  58    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG C  61    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS C  68    CG   CD   CE   NZ                                   
REMARK 470     MET C  69    CG   SD   CE                                        
REMARK 470     ASN C  70    CG   OD1  ND2                                       
REMARK 470     LYS C 123    CG   CD   CE   NZ                                   
REMARK 470     LYS C 124    CG   CD   CE   NZ                                   
REMARK 470     LYS C 144    CD   CE   NZ                                        
REMARK 470     ILE C 145    CG2  CD1                                            
REMARK 470     MET C 147    CG   SD   CE                                        
REMARK 470     THR C 149    OG1  CG2                                            
REMARK 470     GLU D  14    CG   CD   OE1  OE2                                  
REMARK 470     LEU D  15    CG   CD1  CD2                                       
REMARK 470     ASP D  16    CG   OD1  OD2                                       
REMARK 470     ASN D  29    OD1  ND2                                            
REMARK 470     ASN D  48    CG   OD1  ND2                                       
REMARK 470     LYS D  61    CD   CE   NZ                                        
REMARK 470     GLU D  70    CG   CD   OE1  OE2                                  
REMARK 470     ASN D  86    CG   OD1  ND2                                       
REMARK 470     LYS D  90    CG   CD   CE   NZ                                   
REMARK 470     VAL D  91    CG1  CG2                                            
REMARK 470     GLU D  93    CD   OE1  OE2                                       
REMARK 470     LYS D  94    CG   CD   CE   NZ                                   
REMARK 470     SER D  95    OG                                                  
REMARK 470     LYS D 100    CG   CD   CE   NZ                                   
REMARK 470     TYR D 119    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU D 121    CG   CD   OE1  OE2                                  
REMARK 470     PHE D 126    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS D 141    CD   CE   NZ                                        
REMARK 470     LYS D 153    CG   CD   CE   NZ                                   
REMARK 470     ASN D 156    CG   OD1  ND2                                       
REMARK 470     LYS D 157    CG   CD   CE   NZ                                   
REMARK 470     GLN D 172    CD   OE1  NE2                                       
REMARK 470     LYS D 174    CD   CE   NZ                                        
REMARK 470     GLN D 176    CD   OE1  NE2                                       
REMARK 470     MET D 180    CG   SD   CE                                        
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    SER A  32       34.99    -64.81                                   
REMARK 500    ASN A  33      -11.93   -149.23                                   
REMARK 500    LEU A  35      102.67    -54.56                                   
REMARK 500    ASN A  37      102.04    -32.91                                   
REMARK 500    GLU A  38      144.77    -33.92                                   
REMARK 500    ALA A  49      126.54    -32.39                                   
REMARK 500    LYS A  51       15.22   -178.59                                   
REMARK 500    GLN A  65       -3.97    -58.50                                   
REMARK 500    SER A  71       56.35    -62.98                                   
REMARK 500    LEU A  90      -72.21   -109.41                                   
REMARK 500    LEU A 146      -72.28    -73.39                                   
REMARK 500    MET A 147       24.02    -62.50                                   
REMARK 500    GLU A 151      -70.90   -112.75                                   
REMARK 500    THR B  46       58.82   -110.14                                   
REMARK 500    ASN B  48      -13.90   -145.68                                   
REMARK 500    VAL B  58      -80.38   -116.07                                   
REMARK 500    GLN B  69     -109.58     90.20                                   
REMARK 500    GLU B  93        1.04   -161.94                                   
REMARK 500    LEU B 103      -14.95    -41.16                                   
REMARK 500    SER B 116      116.17   -170.68                                   
REMARK 500    TYR B 139      -78.55    -96.88                                   
REMARK 500    LYS B 157       78.43   -109.19                                   
REMARK 500    ALA B 178       75.38     34.13                                   
REMARK 500    ASP B 190       -5.13   -140.98                                   
REMARK 500    HIS B 191     -109.29   -106.20                                   
REMARK 500    SER C  32       42.71    -65.28                                   
REMARK 500    ASN C  33       -6.61   -161.47                                   
REMARK 500    LEU C  35      102.81    -53.69                                   
REMARK 500    ASN C  37      105.56    -31.25                                   
REMARK 500    GLU C  38      128.55    -35.72                                   
REMARK 500    ALA C  49      127.22    -37.45                                   
REMARK 500    ASN C  50       69.28     39.92                                   
REMARK 500    LYS C  51       13.79   -179.81                                   
REMARK 500    SER C  71       57.97    -65.19                                   
REMARK 500    LEU C 146      -74.71    -72.82                                   
REMARK 500    MET C 147       18.47    -59.96                                   
REMARK 500    LEU D  15       29.78    -61.44                                   
REMARK 500    THR D  46       57.94   -110.07                                   
REMARK 500    ASN D  48      -11.54   -146.14                                   
REMARK 500    VAL D  58      -82.43   -116.28                                   
REMARK 500    GLN D  69     -107.25     86.95                                   
REMARK 500    GLU D  93        1.03   -162.96                                   
REMARK 500    LEU D 103      -17.85    -38.26                                   
REMARK 500    SER D 116      115.37   -172.51                                   
REMARK 500    TYR D 139      -81.32    -94.64                                   
REMARK 500    ASN D 156        1.92     57.52                                   
REMARK 500    LYS D 157       77.35   -108.24                                   
REMARK 500    ALA D 178       75.60     37.58                                   
REMARK 500    HIS D 191     -110.29   -107.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 340                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3DI3   RELATED DB: PDB                                   
DBREF  3DI2 A    1   152  UNP    P13232   IL7_HUMAN       26    177             
DBREF  3DI2 B    1   219  UNP    P16871   IL7RA_HUMAN     21    239             
DBREF  3DI2 C    1   152  UNP    P13232   IL7_HUMAN       26    177             
DBREF  3DI2 D    1   219  UNP    P16871   IL7RA_HUMAN     21    239             
SEQADV 3DI2 MET A   -1  UNP  P13232              EXPRESSION TAG                 
SEQADV 3DI2 GLY A    0  UNP  P13232              EXPRESSION TAG                 
SEQADV 3DI2 ALA A  106  UNP  P13232    GLU   131 ENGINEERED                     
SEQADV 3DI2 GLY B   -3  UNP  P16871              EXPRESSION TAG                 
SEQADV 3DI2 SER B   -2  UNP  P16871              EXPRESSION TAG                 
SEQADV 3DI2 HIS B   -1  UNP  P16871              EXPRESSION TAG                 
SEQADV 3DI2 MET B    0  UNP  P16871              EXPRESSION TAG                 
SEQADV 3DI2 VAL B  118  UNP  P16871    ILE   138 ENGINEERED                     
SEQADV 3DI2 MET C   -1  UNP  P13232              EXPRESSION TAG                 
SEQADV 3DI2 GLY C    0  UNP  P13232              EXPRESSION TAG                 
SEQADV 3DI2 ALA C  106  UNP  P13232    GLU   131 ENGINEERED                     
SEQADV 3DI2 GLY D   -3  UNP  P16871              EXPRESSION TAG                 
SEQADV 3DI2 SER D   -2  UNP  P16871              EXPRESSION TAG                 
SEQADV 3DI2 HIS D   -1  UNP  P16871              EXPRESSION TAG                 
SEQADV 3DI2 MET D    0  UNP  P16871              EXPRESSION TAG                 
SEQADV 3DI2 VAL D  118  UNP  P16871    ILE   138 ENGINEERED                     
SEQRES   1 A  154  MET GLY ASP CYS ASP ILE GLU GLY LYS ASP GLY LYS GLN          
SEQRES   2 A  154  TYR GLU SER VAL LEU MET VAL SER ILE ASP GLN LEU LEU          
SEQRES   3 A  154  ASP SER MET LYS GLU ILE GLY SER ASN CYS LEU ASN ASN          
SEQRES   4 A  154  GLU PHE ASN PHE PHE LYS ARG HIS ILE CYS ASP ALA ASN          
SEQRES   5 A  154  LYS GLU GLY MET PHE LEU PHE ARG ALA ALA ARG LYS LEU          
SEQRES   6 A  154  ARG GLN PHE LEU LYS MET ASN SER THR GLY ASP PHE ASP          
SEQRES   7 A  154  LEU HIS LEU LEU LYS VAL SER GLU GLY THR THR ILE LEU          
SEQRES   8 A  154  LEU ASN CYS THR GLY GLN VAL LYS GLY ARG LYS PRO ALA          
SEQRES   9 A  154  ALA LEU GLY ALA ALA GLN PRO THR LYS SER LEU GLU GLU          
SEQRES  10 A  154  ASN LYS SER LEU LYS GLU GLN LYS LYS LEU ASN ASP LEU          
SEQRES  11 A  154  CYS PHE LEU LYS ARG LEU LEU GLN GLU ILE LYS THR CYS          
SEQRES  12 A  154  TRP ASN LYS ILE LEU MET GLY THR LYS GLU HIS                  
SEQRES   1 B  223  GLY SER HIS MET GLU SER GLY TYR ALA GLN ASN GLY ASP          
SEQRES   2 B  223  LEU GLU ASP ALA GLU LEU ASP ASP TYR SER PHE SER CYS          
SEQRES   3 B  223  TYR SER GLN LEU GLU VAL ASN GLY SER GLN HIS SER LEU          
SEQRES   4 B  223  THR CYS ALA PHE GLU ASP PRO ASP VAL ASN THR THR ASN          
SEQRES   5 B  223  LEU GLU PHE GLU ILE CYS GLY ALA LEU VAL GLU VAL LYS          
SEQRES   6 B  223  CYS LEU ASN PHE ARG LYS LEU GLN GLU ILE TYR PHE ILE          
SEQRES   7 B  223  GLU THR LYS LYS PHE LEU LEU ILE GLY LYS SER ASN ILE          
SEQRES   8 B  223  CYS VAL LYS VAL GLY GLU LYS SER LEU THR CYS LYS LYS          
SEQRES   9 B  223  ILE ASP LEU THR THR ILE VAL LYS PRO GLU ALA PRO PHE          
SEQRES  10 B  223  ASP LEU SER VAL VAL TYR ARG GLU GLY ALA ASN ASP PHE          
SEQRES  11 B  223  VAL VAL THR PHE ASN THR SER HIS LEU GLN LYS LYS TYR          
SEQRES  12 B  223  VAL LYS VAL LEU MET HIS ASP VAL ALA TYR ARG GLN GLU          
SEQRES  13 B  223  LYS ASP GLU ASN LYS TRP THR HIS VAL ASN LEU SER SER          
SEQRES  14 B  223  THR LYS LEU THR LEU LEU GLN ARG LYS LEU GLN PRO ALA          
SEQRES  15 B  223  ALA MET TYR GLU ILE LYS VAL ARG SER ILE PRO ASP HIS          
SEQRES  16 B  223  TYR PHE LYS GLY PHE TRP SER GLU TRP SER PRO SER TYR          
SEQRES  17 B  223  TYR PHE ARG THR PRO GLU ILE ASN ASN SER SER GLY GLU          
SEQRES  18 B  223  MET ASP                                                      
SEQRES   1 C  154  MET GLY ASP CYS ASP ILE GLU GLY LYS ASP GLY LYS GLN          
SEQRES   2 C  154  TYR GLU SER VAL LEU MET VAL SER ILE ASP GLN LEU LEU          
SEQRES   3 C  154  ASP SER MET LYS GLU ILE GLY SER ASN CYS LEU ASN ASN          
SEQRES   4 C  154  GLU PHE ASN PHE PHE LYS ARG HIS ILE CYS ASP ALA ASN          
SEQRES   5 C  154  LYS GLU GLY MET PHE LEU PHE ARG ALA ALA ARG LYS LEU          
SEQRES   6 C  154  ARG GLN PHE LEU LYS MET ASN SER THR GLY ASP PHE ASP          
SEQRES   7 C  154  LEU HIS LEU LEU LYS VAL SER GLU GLY THR THR ILE LEU          
SEQRES   8 C  154  LEU ASN CYS THR GLY GLN VAL LYS GLY ARG LYS PRO ALA          
SEQRES   9 C  154  ALA LEU GLY ALA ALA GLN PRO THR LYS SER LEU GLU GLU          
SEQRES  10 C  154  ASN LYS SER LEU LYS GLU GLN LYS LYS LEU ASN ASP LEU          
SEQRES  11 C  154  CYS PHE LEU LYS ARG LEU LEU GLN GLU ILE LYS THR CYS          
SEQRES  12 C  154  TRP ASN LYS ILE LEU MET GLY THR LYS GLU HIS                  
SEQRES   1 D  223  GLY SER HIS MET GLU SER GLY TYR ALA GLN ASN GLY ASP          
SEQRES   2 D  223  LEU GLU ASP ALA GLU LEU ASP ASP TYR SER PHE SER CYS          
SEQRES   3 D  223  TYR SER GLN LEU GLU VAL ASN GLY SER GLN HIS SER LEU          
SEQRES   4 D  223  THR CYS ALA PHE GLU ASP PRO ASP VAL ASN THR THR ASN          
SEQRES   5 D  223  LEU GLU PHE GLU ILE CYS GLY ALA LEU VAL GLU VAL LYS          
SEQRES   6 D  223  CYS LEU ASN PHE ARG LYS LEU GLN GLU ILE TYR PHE ILE          
SEQRES   7 D  223  GLU THR LYS LYS PHE LEU LEU ILE GLY LYS SER ASN ILE          
SEQRES   8 D  223  CYS VAL LYS VAL GLY GLU LYS SER LEU THR CYS LYS LYS          
SEQRES   9 D  223  ILE ASP LEU THR THR ILE VAL LYS PRO GLU ALA PRO PHE          
SEQRES  10 D  223  ASP LEU SER VAL VAL TYR ARG GLU GLY ALA ASN ASP PHE          
SEQRES  11 D  223  VAL VAL THR PHE ASN THR SER HIS LEU GLN LYS LYS TYR          
SEQRES  12 D  223  VAL LYS VAL LEU MET HIS ASP VAL ALA TYR ARG GLN GLU          
SEQRES  13 D  223  LYS ASP GLU ASN LYS TRP THR HIS VAL ASN LEU SER SER          
SEQRES  14 D  223  THR LYS LEU THR LEU LEU GLN ARG LYS LEU GLN PRO ALA          
SEQRES  15 D  223  ALA MET TYR GLU ILE LYS VAL ARG SER ILE PRO ASP HIS          
SEQRES  16 D  223  TYR PHE LYS GLY PHE TRP SER GLU TRP SER PRO SER TYR          
SEQRES  17 D  223  TYR PHE ARG THR PRO GLU ILE ASN ASN SER SER GLY GLU          
SEQRES  18 D  223  MET ASP                                                      
HET    1PE  A 340      16                                                       
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETSYN     1PE PEG400                                                           
FORMUL   5  1PE    C10 H22 O6                                                   
FORMUL   6  HOH   *28(H2 O)                                                     
HELIX    1   1 ASP A    8  VAL A   15  1                                   8    
HELIX    2   2 VAL A   15  SER A   26  1                                  12    
HELIX    3   3 PHE A   39  HIS A   45  1                                   7    
HELIX    4   4 LYS A   51  GLN A   65  1                                  15    
HELIX    5   5 GLY A   73  ASN A   91  1                                  19    
HELIX    6   6 ASP A  127  MET A  147  1                                  21    
HELIX    7   7 THR B  132  LYS B  137  5                                   6    
HELIX    8   8 ARG B  173  LEU B  175  5                                   3    
HELIX    9   9 ASP C    8  VAL C   15  1                                   8    
HELIX   10  10 VAL C   15  SER C   26  1                                  12    
HELIX   11  11 PHE C   39  HIS C   45  1                                   7    
HELIX   12  12 LYS C   51  GLN C   65  1                                  15    
HELIX   13  13 GLY C   73  LEU C   90  1                                  18    
HELIX   14  14 ASP C  127  MET C  147  1                                  21    
HELIX   15  15 THR D  132  LYS D  137  5                                   6    
HELIX   16  16 ARG D  173  LEU D  175  5                                   3    
SHEET    1   A 4 PHE B  20  ASN B  29  0                                        
SHEET    2   A 4 GLN B  32  PHE B  39 -1  O  SER B  34   N  GLN B  25           
SHEET    3   A 4 ILE B  71  THR B  76 -1  O  THR B  76   N  HIS B  33           
SHEET    4   A 4 ARG B  66  LEU B  68 -1  N  LEU B  68   O  ILE B  71           
SHEET    1   B 4 CYS B  62  ASN B  64  0                                        
SHEET    2   B 4 LEU B  49  CYS B  54 -1  N  ILE B  53   O  LEU B  63           
SHEET    3   B 4 SER B  85  VAL B  91 -1  O  LYS B  90   N  GLU B  50           
SHEET    4   B 4 LYS B  94  ILE B 101 -1  O  ILE B 101   N  SER B  85           
SHEET    1   C 3 PHE B 113  SER B 116  0                                        
SHEET    2   C 3 ASP B 125  ASN B 131 -1  O  ASN B 131   N  PHE B 113           
SHEET    3   C 3 TYR B 119  ARG B 120 -1  N  ARG B 120   O  ASP B 125           
SHEET    1   D 3 PHE B 113  SER B 116  0                                        
SHEET    2   D 3 ASP B 125  ASN B 131 -1  O  ASN B 131   N  PHE B 113           
SHEET    3   D 3 LYS B 167  LEU B 171 -1  O  LEU B 168   N  VAL B 128           
SHEET    1   E 4 THR B 159  LEU B 163  0                                        
SHEET    2   E 4 LEU B 143  GLN B 151 -1  N  TYR B 149   O  THR B 159           
SHEET    3   E 4 ALA B 179  PRO B 189 -1  O  LYS B 184   N  ALA B 148           
SHEET    4   E 4 TYR B 204  THR B 208 -1  O  PHE B 206   N  TYR B 181           
SHEET    1   F 4 PHE D  20  ASN D  29  0                                        
SHEET    2   F 4 GLN D  32  PHE D  39 -1  O  SER D  34   N  GLN D  25           
SHEET    3   F 4 ILE D  71  THR D  76 -1  O  THR D  76   N  HIS D  33           
SHEET    4   F 4 ARG D  66  LEU D  68 -1  N  LEU D  68   O  ILE D  71           
SHEET    1   G 4 CYS D  62  ASN D  64  0                                        
SHEET    2   G 4 LEU D  49  CYS D  54 -1  N  ILE D  53   O  LEU D  63           
SHEET    3   G 4 SER D  85  VAL D  91 -1  O  LYS D  90   N  GLU D  50           
SHEET    4   G 4 SER D  95  ILE D 101 -1  O  ILE D 101   N  SER D  85           
SHEET    1   H 3 PHE D 113  SER D 116  0                                        
SHEET    2   H 3 ASP D 125  ASN D 131 -1  O  ASN D 131   N  PHE D 113           
SHEET    3   H 3 TYR D 119  ARG D 120 -1  N  ARG D 120   O  ASP D 125           
SHEET    1   I 3 PHE D 113  SER D 116  0                                        
SHEET    2   I 3 ASP D 125  ASN D 131 -1  O  ASN D 131   N  PHE D 113           
SHEET    3   I 3 LYS D 167  LEU D 171 -1  O  LEU D 168   N  VAL D 128           
SHEET    1   J 3 THR D 159  LEU D 163  0                                        
SHEET    2   J 3 LEU D 143  GLN D 151 -1  N  TYR D 149   O  THR D 159           
SHEET    3   J 3 SER D 187  PRO D 189 -1  O  ILE D 188   N  MET D 144           
SHEET    1   K 4 THR D 159  LEU D 163  0                                        
SHEET    2   K 4 LEU D 143  GLN D 151 -1  N  TYR D 149   O  THR D 159           
SHEET    3   K 4 ALA D 179  LYS D 184 -1  O  LYS D 184   N  ALA D 148           
SHEET    4   K 4 TYR D 204  THR D 208 -1  O  PHE D 206   N  TYR D 181           
SSBOND   1 CYS A   34    CYS A  129                          1555   1555  2.03  
SSBOND   2 CYS A   47    CYS A  141                          1555   1555  2.03  
SSBOND   3 CYS B   22    CYS B   37                          1555   1555  2.04  
SSBOND   4 CYS B   54    CYS B   62                          1555   1555  2.04  
SSBOND   5 CYS B   88    CYS B   98                          1555   1555  2.04  
SSBOND   6 CYS C   34    CYS C  129                          1555   1555  2.03  
SSBOND   7 CYS C   47    CYS C  141                          1555   1555  2.03  
SSBOND   8 CYS D   22    CYS D   37                          1555   1555  2.04  
SSBOND   9 CYS D   54    CYS D   62                          1555   1555  2.04  
SSBOND  10 CYS D   88    CYS D   98                          1555   1555  2.04  
SITE     1 AC1  2 ASP A   8  ASN A  91                                          
CRYST1   47.202  113.021   87.534  90.00 105.10  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      0.021186  0.000000  0.005716        0.00000                         
SCALE2      0.000000  0.008848  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011833        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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