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Database: PDB
Entry: 5J12
LinkDB: 5J12
Original site: 5J12 
HEADER    SIGNALING PROTEIN                       28-MAR-16   5J12              
TITLE     STRUCTURE OF HUMAN TSLP:TSLPR IN COMPLEX WITH MOUSE IL-7RALPHA        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THYMIC STROMAL LYMPHOPOIETIN;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 OTHER_DETAILS: THE SIGNAL PEPTIDE (RESIDUES 1 - 28) IS REMOVED FROM  
COMPND   7 THE MATURE PROTEIN.;                                                 
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTERLEUKIN-7 RECEPTOR SUBUNIT ALPHA;                      
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: IL-7RA;                                                     
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 OTHER_DETAILS: BEFORE CRYSTALLISATION, THE N-TERMINAL HIS-TAG        
COMPND  14 (RESIDUES 1 - 17, MGSSHHHHHHSSGLVPR) WAS REMOVED BY THROMBIN         
COMPND  15 CLEAVAGE.;                                                           
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: CYTOKINE RECEPTOR-LIKE FACTOR 2;                           
COMPND  18 CHAIN: C;                                                            
COMPND  19 SYNONYM: CYTOKINE RECEPTOR-LIKE 2,IL-XR,THYMIC STROMAL LYMPHOPOIETIN 
COMPND  20 PROTEIN RECEPTOR,TSLP RECEPTOR;                                      
COMPND  21 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TSLP;                                                          
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK293S MGAT1-/-;                       
SOURCE  10 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-3022;                             
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PHL-HTSLP-N64Q-K126S-DELTA127-131;        
SOURCE  13 MOL_ID: 2;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  15 ORGANISM_COMMON: MOUSE;                                              
SOURCE  16 ORGANISM_TAXID: 10090;                                               
SOURCE  17 GENE: IL7R;                                                          
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PET15B-MIL7ALPHA;                         
SOURCE  22 MOL_ID: 3;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_COMMON: HUMAN;                                              
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 GENE: CRLF2, CRL2, ILXR, TSLPR;                                      
SOURCE  27 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  28 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  29 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  30 EXPRESSION_SYSTEM_CELL_LINE: HEK293S MGAT1-/-;                       
SOURCE  31 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-3022;                             
SOURCE  32 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  33 EXPRESSION_SYSTEM_PLASMID: PHL-HTSLPR                                
KEYWDS    CYTOKINE INFLAMMATION TSLP SIGNALING COMPLEX, SIGNALING PROTEIN       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.VERSTRAETE,S.N.SAVVIDES                                             
REVDAT   3   29-JUL-20 5J12    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE                                     
REVDAT   2   28-FEB-18 5J12    1       SOURCE                                   
REVDAT   1   05-APR-17 5J12    0                                                
JRNL        AUTH   K.VERSTRAETE,S.N.SAVVIDES                                    
JRNL        TITL   STRUCTURE OF HUMAN TSLP:TSLPR IN COMPLEX WITH MOUSE          
JRNL        TITL 2 IL-7RALPHA                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.43                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 11336                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.215                          
REMARK   3   R VALUE            (WORKING SET)  : 0.214                          
REMARK   3   FREE R VALUE                      : 0.225                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 567                            
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               : 6                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.55                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.89                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 98.58                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2631                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2210                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2500                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2188                   
REMARK   3   BIN FREE R VALUE                        : 0.2645                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.98                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 131                      
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            : 3757                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 57                                      
REMARK   3   SOLVENT ATOMS            : 5                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 125.1                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 152.3                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.73010                                              
REMARK   3    B22 (A**2) : 8.73010                                              
REMARK   3    B33 (A**2) : -17.46020                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.475               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.467               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.920                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3921   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5390   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1196   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 70     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 593    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3921   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 568    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 4185   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.011                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.19                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.86                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.85                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: {A|29 - 501}                                           
REMARK   3    ORIGIN FOR THE GROUP (A):   -9.5352  -37.0244  -21.4558           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2385 T22:    0.0335                                    
REMARK   3     T33:   -0.0822 T12:    0.1247                                    
REMARK   3     T13:   -0.0870 T23:    0.0810                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4312 L22:    3.5439                                    
REMARK   3     L33:    3.4050 L12:   -1.7510                                    
REMARK   3     L13:    0.2285 L23:    0.6601                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1012 S12:   -0.1277 S13:   -0.0299                     
REMARK   3     S21:    0.2946 S22:    0.2107 S23:   -0.3610                     
REMARK   3     S31:   -0.2491 S32:    0.6593 S33:   -0.1096                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: {B|38 - 125}                                           
REMARK   3    ORIGIN FOR THE GROUP (A):   -7.5029  -67.7469  -26.4044           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.6146 T22:   -0.5777                                    
REMARK   3     T33:   -0.6841 T12:    0.6875                                    
REMARK   3     T13:   -0.3381 T23:   -0.0354                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.1297 L22:   12.5486                                    
REMARK   3     L33:    2.5255 L12:   -1.4518                                    
REMARK   3     L13:   -1.1765 L23:    1.8853                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0788 S12:    0.6451 S13:   -0.2833                     
REMARK   3     S21:   -1.7896 S22:   -0.0029 S23:    0.3197                     
REMARK   3     S31:    1.5389 S32:    0.3029 S33:   -0.0758                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: {B|126 - 232}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -29.1279  -67.4043   -6.5947           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0911 T22:   -0.7772                                    
REMARK   3     T33:    0.5742 T12:   -0.0293                                    
REMARK   3     T13:    0.1034 T23:    0.4398                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    6.2041 L22:    2.6692                                    
REMARK   3     L33:    7.5059 L12:    4.1026                                    
REMARK   3     L13:   -4.0871 L23:   -3.8197                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2978 S12:   -0.7045 S13:   -0.3887                     
REMARK   3     S21:    0.3275 S22:   -0.0419 S23:    1.6609                     
REMARK   3     S31:    1.1707 S32:   -0.7436 S33:   -0.2559                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: {C|30 - 116}                                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -16.0846  -19.2450   -1.5883           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0240 T22:   -0.1502                                    
REMARK   3     T33:   -0.2508 T12:    0.0369                                    
REMARK   3     T13:   -0.0918 T23:   -0.0414                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   10.4038 L22:    7.2369                                    
REMARK   3     L33:    4.1361 L12:    2.2788                                    
REMARK   3     L13:   -0.4937 L23:    2.1449                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1003 S12:   -0.9916 S13:    0.8087                     
REMARK   3     S21:    0.0129 S22:    0.1183 S23:   -0.5228                     
REMARK   3     S31:   -1.2427 S32:    0.8426 S33:   -0.2186                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: {C|117 -501}                                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -35.6692  -43.6683   -2.7882           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2663 T22:   -0.3255                                    
REMARK   3     T33:   -0.0054 T12:    0.0245                                    
REMARK   3     T13:    0.1870 T23:    0.0870                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.7096 L22:    7.8994                                    
REMARK   3     L33:    7.7617 L12:    2.0537                                    
REMARK   3     L13:   -0.2224 L23:    2.1505                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1167 S12:   -1.0315 S13:   -0.7610                     
REMARK   3     S21:    0.7488 S22:   -0.7289 S23:    1.4459                     
REMARK   3     S31:    1.1574 S32:   -1.1161 S33:    0.8457                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  - RIGID BODY REFINEMENT (SINGLE RIGID BODY PER DOMAIN) IN PHENIX    
REMARK   3                                                                      
REMARK   3  - ITERATIVE CYCLES OF REFINEMENT IN AUTOBUSTER, MODEL (RE)BUILDING  
REMARK   3  AND VALIDATION:                                                     
REMARK   3  XYZ COORDINATE REFINEMENT                                           
REMARK   3  INDIVIDUAL B-FACTORS                                                
REMARK   3  TLS PARAMETERISATION WITH ONE TLS-GROUP PER DOMAIN                  
REMARK   3  TARGET RESTRAINTS:                                                  
REMARK   3  CHAIN A,C --> CHAIN A,C IN THE 2.55 ANGSTROM STRUCTURE OF THE       
REMARK   3  HUMAN TERNARY TSLP COMPLEX                                          
REMARK   3  CHAIN B --> CHAIN B OF PDB 2NN5                                     
REMARK   3  AUTOMATIC X-RAY WEIGHT OPTIMISATION                                 
REMARK   3  STRUCTURE VALIDATION IN COOT, PHENIX (MOLPROBITY) AND PDB_REDO      
REMARK   4                                                                      
REMARK   4 5J12 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000219513.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS VERSION JANUARY 10, 2014       
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11341                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 10.70                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.50                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB 4NN5                                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.53 M AMMONIUM SULFATE 0.1 M SODIUM     
REMARK 280  CHLORIDE 0.1 M BIS-TRIS PH 7.0, VAPOR DIFFUSION, SITTING DROP,      
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      129.71533            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       64.85767            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       97.28650            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       32.42883            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      162.14417            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      129.71533            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       64.85767            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       32.42883            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       97.28650            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      162.14417            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     PHE A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     PHE A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     TYR A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     VAL A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     PHE A    14                                                      
REMARK 465     ARG A    15                                                      
REMARK 465     LYS A    16                                                      
REMARK 465     ILE A    17                                                      
REMARK 465     PHE A    18                                                      
REMARK 465     ILE A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     GLN A    21                                                      
REMARK 465     LEU A    22                                                      
REMARK 465     VAL A    23                                                      
REMARK 465     GLY A    24                                                      
REMARK 465     LEU A    25                                                      
REMARK 465     VAL A    26                                                      
REMARK 465     LEU A    27                                                      
REMARK 465     THR A    28                                                      
REMARK 465     GLN A   127                                                      
REMARK 465     ALA A   128                                                      
REMARK 465     MET A   129                                                      
REMARK 465     LYS A   130                                                      
REMARK 465     SER A   131                                                      
REMARK 465     VAL A   132                                                      
REMARK 465     HIS A   167                                                      
REMARK 465     HIS A   168                                                      
REMARK 465     GLY B    17                                                      
REMARK 465     SER B    18                                                      
REMARK 465     HIS B    19                                                      
REMARK 465     MET B    20                                                      
REMARK 465     GLU B    21                                                      
REMARK 465     SER B    22                                                      
REMARK 465     GLY B    23                                                      
REMARK 465     ASN B    24                                                      
REMARK 465     ALA B    25                                                      
REMARK 465     GLN B    26                                                      
REMARK 465     ASP B    27                                                      
REMARK 465     GLY B    28                                                      
REMARK 465     ASP B    29                                                      
REMARK 465     LEU B    30                                                      
REMARK 465     GLU B    31                                                      
REMARK 465     ASP B    32                                                      
REMARK 465     ALA B    33                                                      
REMARK 465     ASP B    34                                                      
REMARK 465     ALA B    35                                                      
REMARK 465     ASP B    36                                                      
REMARK 465     ASP B    37                                                      
REMARK 465     PRO B   232                                                      
REMARK 465     LYS B   233                                                      
REMARK 465     ASN B   234                                                      
REMARK 465     GLN B   235                                                      
REMARK 465     GLY B   236                                                      
REMARK 465     GLY B   237                                                      
REMARK 465     TRP B   238                                                      
REMARK 465     ASP B   239                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     ARG C     3                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     VAL C     5                                                      
REMARK 465     LEU C     6                                                      
REMARK 465     LEU C     7                                                      
REMARK 465     TRP C     8                                                      
REMARK 465     GLY C     9                                                      
REMARK 465     ALA C    10                                                      
REMARK 465     ALA C    11                                                      
REMARK 465     VAL C    12                                                      
REMARK 465     PHE C    13                                                      
REMARK 465     LEU C    14                                                      
REMARK 465     LEU C    15                                                      
REMARK 465     GLY C    16                                                      
REMARK 465     GLY C    17                                                      
REMARK 465     TRP C    18                                                      
REMARK 465     MET C    19                                                      
REMARK 465     ALA C    20                                                      
REMARK 465     LEU C    21                                                      
REMARK 465     GLY C    22                                                      
REMARK 465     GLN C    23                                                      
REMARK 465     GLY C    24                                                      
REMARK 465     GLY C    25                                                      
REMARK 465     ALA C    26                                                      
REMARK 465     ALA C    27                                                      
REMARK 465     GLU C    28                                                      
REMARK 465     GLY C    29                                                      
REMARK 465     ALA C   219                                                      
REMARK 465     GLU C   220                                                      
REMARK 465     THR C   221                                                      
REMARK 465     GLY C   222                                                      
REMARK 465     THR C   223                                                      
REMARK 465     LYS C   224                                                      
REMARK 465     HIS C   225                                                      
REMARK 465     HIS C   226                                                      
REMARK 465     HIS C   227                                                      
REMARK 465     HIS C   228                                                      
REMARK 465     HIS C   229                                                      
REMARK 465     HIS C   230                                                      
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  38    CD   CE   NZ                                        
REMARK 470     LYS A  59    CG   CD   CE   NZ                                   
REMARK 470     LYS A  95    CG   CD   CE   NZ                                   
REMARK 470     LYS A 103    CE   NZ                                             
REMARK 470     THR A 121    OG1  CG2                                            
REMARK 470     ASN A 135    CG   OD1  ND2                                       
REMARK 470     LYS A 136    CG   CD   CE   NZ                                   
REMARK 470     LYS A 157    CG   CD   CE   NZ                                   
REMARK 470     LYS A 162    CE   NZ                                             
REMARK 470     SER B  39    OG                                                  
REMARK 470     ASP B  49    CG   OD1  OD2                                       
REMARK 470     ASP B  63    CG   OD1  OD2                                       
REMARK 470     ASN B  65    CG   OD1  ND2                                       
REMARK 470     LEU B  69    CG   CD1  CD2                                       
REMARK 470     GLU B  70    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  79    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B  81    O    CG   CD   CE   NZ                              
REMARK 470     GLN B  89    CG   CD   OE1  NE2                                  
REMARK 470     ASP B  90    CG   OD1  OD2                                       
REMARK 470     GLN B 113    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 114    CG   CD   CE   NZ                                   
REMARK 470     LYS B 119    CG   CD   CE   NZ                                   
REMARK 470     LYS B 128    CG   CD   CE   NZ                                   
REMARK 470     LYS B 136    CE   NZ                                             
REMARK 470     TYR B 139    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG B 140    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 141    CG   CD   CE   NZ                                   
REMARK 470     GLU B 142    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 144    CG   OD1  ND2                                       
REMARK 470     PHE B 146    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU B 147    CG   CD1  CD2                                       
REMARK 470     LYS B 156    CG   CD   CE   NZ                                   
REMARK 470     LYS B 157    CG   CD   CE   NZ                                   
REMARK 470     LYS B 158    CG   CD   CE   NZ                                   
REMARK 470     LYS B 161    CE   NZ                                             
REMARK 470     LYS B 162    CD   CE   NZ                                        
REMARK 470     LYS B 164    CD   CE   NZ                                        
REMARK 470     TYR B 169    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG B 170    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 173    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 175    CG   CD   OE1  OE2                                  
REMARK 470     SER B 176    OG                                                  
REMARK 470     ASN B 177    CG   OD1  ND2                                       
REMARK 470     THR B 179    OG1  CG2                                            
REMARK 470     HIS B 180    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL B 181    CG1  CG2                                            
REMARK 470     SER B 182    OG                                                  
REMARK 470     HIS B 185    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG B 187    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 190    CG1  CG2  CD1                                       
REMARK 470     ARG B 193    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 194    CG   CD   CE   NZ                                   
REMARK 470     LEU B 195    CG   CD1  CD2                                       
REMARK 470     ARG B 196    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 198    CG   CD   CE   NZ                                   
REMARK 470     MET B 200    CG   SD   CE                                        
REMARK 470     TYR B 201    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B 202    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 203    CG1  CG2  CD1                                       
REMARK 470     LYS B 204    CG   CD   CE   NZ                                   
REMARK 470     ASP B 212    CG   OD1  OD2                                       
REMARK 470     LYS B 215    CG   CD   CE   NZ                                   
REMARK 470     SER B 225    OG                                                  
REMARK 470     PHE B 227    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 228    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 231    CG   CD   OE1  OE2                                  
REMARK 470     GLN C  31    CG   CD   OE1  NE2                                  
REMARK 470     LYS C  50    CG   CD   CE   NZ                                   
REMARK 470     ARG C  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C  66    CD   OE1  OE2                                       
REMARK 470     GLN C  70    CG   CD   OE1  NE2                                  
REMARK 470     GLN C  77    CG   CD   OE1  NE2                                  
REMARK 470     GLU C  78    CG   CD   OE1  OE2                                  
REMARK 470     HIS C  80    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU C  89    CG   CD   OE1  OE2                                  
REMARK 470     GLN C  90    CG   CD   OE1  NE2                                  
REMARK 470     ARG C  91    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASN C 101    CG   OD1  ND2                                       
REMARK 470     ARG C 111    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 123    CG   CD   CE   NZ                                   
REMARK 470     ARG C 126    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 131    CG   CD   OE1  NE2                                  
REMARK 470     ASP C 132    CG   OD1  OD2                                       
REMARK 470     PHE C 156    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU C 159    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 161    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 163    CE   NZ                                             
REMARK 470     GLU C 173    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 176    CG   OD1  OD2                                       
REMARK 470     GLU C 178    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 179    CG   CD   CE   NZ                                   
REMARK 470     GLU C 205    CG   CD   OE1  OE2                                  
REMARK 470     TRP C 209    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP C 209    CZ3  CH2                                            
REMARK 470     GLN C 210    CG   CD   OE1  NE2                                  
REMARK 470     ARG C 211    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 213    CG   CD   OE1  OE2                                  
REMARK 470     ILE C 214    CG1  CG2  CD1                                       
REMARK 470     ARG C 215    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 216    CG   OD1  OD2                                       
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  70      -98.39   -104.44                                   
REMARK 500    ASN A 119       57.58    -97.20                                   
REMARK 500    THR A 161     -167.86   -116.49                                   
REMARK 500    LYS A 162       90.32     65.66                                   
REMARK 500    HIS A 163       66.14   -159.39                                   
REMARK 500    GLN B  89     -120.00     54.15                                   
REMARK 500    LEU B 160       71.40     62.92                                   
REMARK 500    TYR B 213      -54.02   -127.94                                   
REMARK 500    ASN C  38       29.03     48.63                                   
REMARK 500    TYR C  51       43.62    -92.75                                   
REMARK 500    ARG C  53       33.07    -81.75                                   
REMARK 500    ASP C  65       78.65    -69.43                                   
REMARK 500    GLN C 131     -107.00     55.65                                   
REMARK 500    ASP C 132       48.23   -107.57                                   
REMARK 500    ASN C 169       86.51   -162.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5J12 A    1   159  UNP    Q969D9   TSLP_HUMAN       1    159             
DBREF  5J12 B   21   239  UNP    P16872   IL7RA_MOUSE     21    239             
DBREF  5J12 C    1   221  UNP    Q9HC73   CRLF2_HUMAN      1    221             
SEQADV 5J12 GLN A   64  UNP  Q969D9    ASN    64 ENGINEERED MUTATION            
SEQADV 5J12     A       UNP  Q969D9    LYS   126 DELETION                       
SEQADV 5J12     A       UNP  Q969D9    ARG   127 DELETION                       
SEQADV 5J12     A       UNP  Q969D9    ARG   128 DELETION                       
SEQADV 5J12     A       UNP  Q969D9    LYS   129 DELETION                       
SEQADV 5J12     A       UNP  Q969D9    ARG   130 DELETION                       
SEQADV 5J12 SER A  131  UNP  Q969D9    LYS   131 ENGINEERED MUTATION            
SEQADV 5J12 GLY A  160  UNP  Q969D9              EXPRESSION TAG                 
SEQADV 5J12 THR A  161  UNP  Q969D9              EXPRESSION TAG                 
SEQADV 5J12 LYS A  162  UNP  Q969D9              EXPRESSION TAG                 
SEQADV 5J12 HIS A  163  UNP  Q969D9              EXPRESSION TAG                 
SEQADV 5J12 HIS A  164  UNP  Q969D9              EXPRESSION TAG                 
SEQADV 5J12 HIS A  165  UNP  Q969D9              EXPRESSION TAG                 
SEQADV 5J12 HIS A  166  UNP  Q969D9              EXPRESSION TAG                 
SEQADV 5J12 HIS A  167  UNP  Q969D9              EXPRESSION TAG                 
SEQADV 5J12 HIS A  168  UNP  Q969D9              EXPRESSION TAG                 
SEQADV 5J12 GLY B   17  UNP  P16872              EXPRESSION TAG                 
SEQADV 5J12 SER B   18  UNP  P16872              EXPRESSION TAG                 
SEQADV 5J12 HIS B   19  UNP  P16872              EXPRESSION TAG                 
SEQADV 5J12 MET B   20  UNP  P16872              EXPRESSION TAG                 
SEQADV 5J12 GLY C  222  UNP  Q9HC73              EXPRESSION TAG                 
SEQADV 5J12 THR C  223  UNP  Q9HC73              EXPRESSION TAG                 
SEQADV 5J12 LYS C  224  UNP  Q9HC73              EXPRESSION TAG                 
SEQADV 5J12 HIS C  225  UNP  Q9HC73              EXPRESSION TAG                 
SEQADV 5J12 HIS C  226  UNP  Q9HC73              EXPRESSION TAG                 
SEQADV 5J12 HIS C  227  UNP  Q9HC73              EXPRESSION TAG                 
SEQADV 5J12 HIS C  228  UNP  Q9HC73              EXPRESSION TAG                 
SEQADV 5J12 HIS C  229  UNP  Q9HC73              EXPRESSION TAG                 
SEQADV 5J12 HIS C  230  UNP  Q9HC73              EXPRESSION TAG                 
SEQRES   1 A  163  MET PHE PRO PHE ALA LEU LEU TYR VAL LEU SER VAL SER          
SEQRES   2 A  163  PHE ARG LYS ILE PHE ILE LEU GLN LEU VAL GLY LEU VAL          
SEQRES   3 A  163  LEU THR TYR ASP PHE THR ASN CYS ASP PHE GLU LYS ILE          
SEQRES   4 A  163  LYS ALA ALA TYR LEU SER THR ILE SER LYS ASP LEU ILE          
SEQRES   5 A  163  THR TYR MET SER GLY THR LYS SER THR GLU PHE GLN ASN          
SEQRES   6 A  163  THR VAL SER CYS SER ASN ARG PRO HIS CYS LEU THR GLU          
SEQRES   7 A  163  ILE GLN SER LEU THR PHE ASN PRO THR ALA GLY CYS ALA          
SEQRES   8 A  163  SER LEU ALA LYS GLU MET PHE ALA MET LYS THR LYS ALA          
SEQRES   9 A  163  ALA LEU ALA ILE TRP CYS PRO GLY TYR SER GLU THR GLN          
SEQRES  10 A  163  ILE ASN ALA THR GLN ALA MET LYS SER VAL THR THR ASN          
SEQRES  11 A  163  LYS CYS LEU GLU GLN VAL SER GLN LEU GLN GLY LEU TRP          
SEQRES  12 A  163  ARG ARG PHE ASN ARG PRO LEU LEU LYS GLN GLN GLY THR          
SEQRES  13 A  163  LYS HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 B  223  GLY SER HIS MET GLU SER GLY ASN ALA GLN ASP GLY ASP          
SEQRES   2 B  223  LEU GLU ASP ALA ASP ALA ASP ASP HIS SER PHE TRP CYS          
SEQRES   3 B  223  HIS SER GLN LEU GLU VAL ASP GLY SER GLN HIS LEU LEU          
SEQRES   4 B  223  THR CYS ALA PHE ASN ASP SER ASP ILE ASN THR ALA ASN          
SEQRES   5 B  223  LEU GLU PHE GLN ILE CYS GLY ALA LEU LEU ARG VAL LYS          
SEQRES   6 B  223  CYS LEU THR LEU ASN LYS LEU GLN ASP ILE TYR PHE ILE          
SEQRES   7 B  223  LYS THR SER GLU PHE LEU LEU ILE GLY SER SER ASN ILE          
SEQRES   8 B  223  CYS VAL LYS LEU GLY GLN LYS ASN LEU THR CYS LYS ASN          
SEQRES   9 B  223  MET ALA ILE ASN THR ILE VAL LYS ALA GLU ALA PRO SER          
SEQRES  10 B  223  ASP LEU LYS VAL VAL TYR ARG LYS GLU ALA ASN ASP PHE          
SEQRES  11 B  223  LEU VAL THR PHE ASN ALA PRO HIS LEU LYS LYS LYS TYR          
SEQRES  12 B  223  LEU LYS LYS VAL LYS HIS ASP VAL ALA TYR ARG PRO ALA          
SEQRES  13 B  223  ARG GLY GLU SER ASN TRP THR HIS VAL SER LEU PHE HIS          
SEQRES  14 B  223  THR ARG THR THR ILE PRO GLN ARG LYS LEU ARG PRO LYS          
SEQRES  15 B  223  ALA MET TYR GLU ILE LYS VAL ARG SER ILE PRO HIS ASN          
SEQRES  16 B  223  ASP TYR PHE LYS GLY PHE TRP SER GLU TRP SER PRO SER          
SEQRES  17 B  223  SER THR PHE GLU THR PRO GLU PRO LYS ASN GLN GLY GLY          
SEQRES  18 B  223  TRP ASP                                                      
SEQRES   1 C  230  MET GLY ARG LEU VAL LEU LEU TRP GLY ALA ALA VAL PHE          
SEQRES   2 C  230  LEU LEU GLY GLY TRP MET ALA LEU GLY GLN GLY GLY ALA          
SEQRES   3 C  230  ALA GLU GLY VAL GLN ILE GLN ILE ILE TYR PHE ASN LEU          
SEQRES   4 C  230  GLU THR VAL GLN VAL THR TRP ASN ALA SER LYS TYR SER          
SEQRES   5 C  230  ARG THR ASN LEU THR PHE HIS TYR ARG PHE ASN GLY ASP          
SEQRES   6 C  230  GLU ALA TYR ASP GLN CYS THR ASN TYR LEU LEU GLN GLU          
SEQRES   7 C  230  GLY HIS THR SER GLY CYS LEU LEU ASP ALA GLU GLN ARG          
SEQRES   8 C  230  ASP ASP ILE LEU TYR PHE SER ILE ARG ASN GLY THR HIS          
SEQRES   9 C  230  PRO VAL PHE THR ALA SER ARG TRP MET VAL TYR TYR LEU          
SEQRES  10 C  230  LYS PRO SER SER PRO LYS HIS VAL ARG PHE SER TRP HIS          
SEQRES  11 C  230  GLN ASP ALA VAL THR VAL THR CYS SER ASP LEU SER TYR          
SEQRES  12 C  230  GLY ASP LEU LEU TYR GLU VAL GLN TYR ARG SER PRO PHE          
SEQRES  13 C  230  ASP THR GLU TRP GLN SER LYS GLN GLU ASN THR CYS ASN          
SEQRES  14 C  230  VAL THR ILE GLU GLY LEU ASP ALA GLU LYS CYS TYR SER          
SEQRES  15 C  230  PHE TRP VAL ARG VAL LYS ALA MET GLU ASP VAL TYR GLY          
SEQRES  16 C  230  PRO ASP THR TYR PRO SER ASP TRP SER GLU VAL THR CYS          
SEQRES  17 C  230  TRP GLN ARG GLY GLU ILE ARG ASP ALA CYS ALA GLU THR          
SEQRES  18 C  230  GLY THR LYS HIS HIS HIS HIS HIS HIS                          
HET    NAG  A 500      14                                                       
HET    SO4  C 301       5                                                       
HET    SO4  C 302       5                                                       
HET    SO4  C 303       5                                                       
HET    NAG  C 304      14                                                       
HET    NAG  C 305      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL   4  NAG    3(C8 H15 N O6)                                               
FORMUL   5  SO4    3(O4 S 2-)                                                   
FORMUL  10  HOH   *5(H2 O)                                                      
HELIX    1 AA1 ASP A   30  CYS A   34  5                                   5    
HELIX    2 AA2 ASP A   35  THR A   46  1                                  12    
HELIX    3 AA3 THR A   46  SER A   56  1                                  11    
HELIX    4 AA4 LYS A   59  PHE A   63  5                                   5    
HELIX    5 AA5 ASN A   71  ASN A   85  1                                  15    
HELIX    6 AA6 GLU A   96  CYS A  110  1                                  15    
HELIX    7 AA7 THR A  134  ASN A  152  1                                  19    
HELIX    8 AA8 ALA B  122  ILE B  126  5                                   5    
HELIX    9 AA9 ALA B  152  LYS B  157  5                                   6    
HELIX   10 AB1 ARG B  193  LEU B  195  5                                   3    
HELIX   11 AB2 ALA C   48  THR C   54  5                                   7    
HELIX   12 AB3 MET C  190  GLY C  195  1                                   6    
SHEET    1 AA1 4 PHE B  40  GLN B  45  0                                        
SHEET    2 AA1 4 HIS B  53  PHE B  59 -1  O  LEU B  54   N  GLN B  45           
SHEET    3 AA1 4 ILE B  91  THR B  96 -1  O  TYR B  92   N  CYS B  57           
SHEET    4 AA1 4 ASN B  86  LEU B  88 -1  N  ASN B  86   O  PHE B  93           
SHEET    1 AA2 4 LEU B  83  THR B  84  0                                        
SHEET    2 AA2 4 LEU B  69  CYS B  74 -1  N  ILE B  73   O  LEU B  83           
SHEET    3 AA2 4 SER B 105  LEU B 111 -1  O  LYS B 110   N  GLU B  70           
SHEET    4 AA2 4 LYS B 114  MET B 121 -1  O  MET B 121   N  SER B 105           
SHEET    1 AA3 2 VAL B 127  LYS B 128  0                                        
SHEET    2 AA3 2 GLY B 216  PHE B 217  1  O  PHE B 217   N  VAL B 127           
SHEET    1 AA4 3 SER B 133  ARG B 140  0                                        
SHEET    2 AA4 3 ASP B 145  ASN B 151 -1  O  ASN B 151   N  SER B 133           
SHEET    3 AA4 3 ARG B 187  PRO B 191 -1  O  THR B 188   N  VAL B 148           
SHEET    1 AA5 4 THR B 179  LEU B 183  0                                        
SHEET    2 AA5 4 VAL B 163  PRO B 171 -1  N  HIS B 165   O  LEU B 183           
SHEET    3 AA5 4 MET B 200  PRO B 209 -1  O  GLU B 202   N  ARG B 170           
SHEET    4 AA5 4 SER B 225  GLU B 228 -1  O  PHE B 227   N  TYR B 201           
SHEET    1 AA6 5 TYR C  74  GLN C  77  0                                        
SHEET    2 AA6 5 HIS C  80  ASP C  87 -1  O  SER C  82   N  LEU C  75           
SHEET    3 AA6 5 THR C  41  ASN C  47 -1  N  VAL C  42   O  LEU C  86           
SHEET    4 AA6 5 GLN C  31  PHE C  37 -1  N  ILE C  35   O  GLN C  43           
SHEET    5 AA6 5 LEU C 117  LYS C 118  1  O  LYS C 118   N  TYR C  36           
SHEET    1 AA7 4 ASP C  69  GLN C  70  0                                        
SHEET    2 AA7 4 THR C  57  PHE C  62 -1  N  TYR C  60   O  ASP C  69           
SHEET    3 AA7 4 ILE C  94  ASN C 101 -1  O  TYR C  96   N  ARG C  61           
SHEET    4 AA7 4 HIS C 104  TRP C 112 -1  O  ALA C 109   N  PHE C  97           
SHEET    1 AA8 3 ARG C 126  TRP C 129  0                                        
SHEET    2 AA8 3 ALA C 133  THR C 137 -1  O  THR C 137   N  ARG C 126           
SHEET    3 AA8 3 ASN C 169  GLU C 173 -1  O  ILE C 172   N  VAL C 134           
SHEET    1 AA9 5 GLN C 161  GLU C 165  0                                        
SHEET    2 AA9 5 LEU C 146  ARG C 153 -1  N  TYR C 148   O  GLU C 165           
SHEET    3 AA9 5 TYR C 181  ALA C 189 -1  O  TRP C 184   N  GLN C 151           
SHEET    4 AA9 5 THR C 207  GLN C 210 -1  O  THR C 207   N  PHE C 183           
SHEET    5 AA9 5 GLU C 213  ARG C 215 -1  O  ARG C 215   N  CYS C 208           
SSBOND   1 CYS A   34    CYS A  110                          1555   1555  2.06  
SSBOND   2 CYS A   69    CYS A   75                          1555   1555  2.05  
SSBOND   3 CYS A   90    CYS A  137                          1555   1555  2.04  
SSBOND   4 CYS B   42    CYS B   57                          1555   1555  2.03  
SSBOND   5 CYS B   74    CYS B   82                          1555   1555  2.04  
SSBOND   6 CYS B  108    CYS B  118                          1555   1555  2.04  
SSBOND   7 CYS C   71    CYS C   84                          1555   1555  2.05  
SSBOND   8 CYS C  138    CYS C  168                          1555   1555  2.04  
SSBOND   9 CYS C  180    CYS C  218                          1555   1555  2.04  
LINK         ND2 ASN A 119                 C1  NAG A 500     1555   1555  1.44  
LINK         ND2 ASN C  47                 C1  NAG C 305     1555   1555  1.44  
LINK         ND2 ASN C  55                 C1  NAG C 304     1555   1555  1.43  
CRYST1  125.442  125.442  194.573  90.00  90.00 120.00 P 65 2 2     12          
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      0.007972  0.004603  0.000000        0.00000                         
SCALE2      0.000000  0.009205  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005139        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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