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Database: PDB
Entry: 2XQB
LinkDB: 2XQB
Original site: 2XQB 
HEADER    IMMUNE SYSTEM                           01-SEP-10   2XQB              
TITLE     CRYSTAL STRUCTURE OF ANTI-IL-15 ANTIBODY IN COMPLEX WITH HUMAN IL-15  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN 15;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: ANTI-IL-15 ANTIBODY;                                       
COMPND   7 CHAIN: H;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: ANTI-IL-15 ANTIBODY;                                       
COMPND  11 CHAIN: L;                                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: STAR;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PT7#3.3;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  15 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  17 EXPRESSION_SYSTEM_CELL_LINE: HEK293/EBNA;                            
SOURCE  18 MOL_ID: 3;                                                           
SOURCE  19 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  20 ORGANISM_COMMON: HUMAN;                                              
SOURCE  21 ORGANISM_TAXID: 9606;                                                
SOURCE  22 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  23 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  25 EXPRESSION_SYSTEM_CELL_LINE: HEK293/EBNA                             
KEYWDS    IMMUNE SYSTEM, AFFINITY MATURATION                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.C.LOWE,S.GERHARDT,A.WARD,D.HARGREAVES,M.ANDERSON,S.STGALLAY,        
AUTHOR   2 K.VOUSDEN,F.FERRARO,R.A.PAUPTIT,D.COCHRANE,D.V.PATTISON,C.BUCHANAN,  
AUTHOR   3 B.POPOVIC,D.K.FINCH,T.WILKINSON,M.SLEEMAN,T.J.VAUGHAN,S.CRUWYS,      
AUTHOR   4 P.R.MALLINDER                                                        
REVDAT   3   04-APR-18 2XQB    1       SOURCE REMARK                            
REVDAT   2   06-APR-11 2XQB    1       JRNL                                     
REVDAT   1   29-DEC-10 2XQB    0                                                
JRNL        AUTH   D.C.LOWE,S.GERHARDT,A.WARD,D.HARGREAVES,M.ANDERSON,          
JRNL        AUTH 2 F.FERRARO,R.A.PAUPTIT,D.V.PATTISON,C.BUCHANAN,B.POPOVIC,     
JRNL        AUTH 3 D.K.FINCH,T.WILKINSON,M.SLEEMAN,T.J.VAUGHAN,P.R.MALLINDER    
JRNL        TITL   ENGINEERING A HIGH AFFINITY ANTI-IL-15 ANTIBODY: CRYSTAL     
JRNL        TITL 2 STRUCTURE REVEALS AN ALPHA-HELIX IN VH CDR3 AS KEY COMPONENT 
JRNL        TITL 3 OF PARATOPE.                                                 
JRNL        REF    J.MOL.BIOL.                   V. 406   160 2011              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   21167836                                                     
JRNL        DOI    10.1016/J.JMB.2010.12.017                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0069                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 69.71                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 16532                          
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) : 0.248                           
REMARK   3   R VALUE            (WORKING SET) : 0.244                           
REMARK   3   FREE R VALUE                     : 0.318                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 883                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1218                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3420                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 56                           
REMARK   3   BIN FREE R VALUE                    : 0.4300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3982                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 66                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.22                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.35000                                              
REMARK   3    B22 (A**2) : 1.52000                                              
REMARK   3    B33 (A**2) : -1.79000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.36000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 2.527         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.419         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.339         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.940        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.922                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.859                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4094 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2659 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5592 ; 1.605 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6521 ; 1.851 ; 3.004       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   527 ; 6.158 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   147 ;36.175 ;24.762       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   620 ;21.725 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;23.399 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   643 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4537 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   777 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2660 ; 0.255 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1069 ; 0.039 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4283 ; 0.472 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1434 ; 0.714 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1309 ; 1.216 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     1        H   114                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.9997   1.6341  28.9464              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1108 T22:  -0.2110                                     
REMARK   3      T33:  -0.1425 T12:  -0.0190                                     
REMARK   3      T13:   0.0174 T23:  -0.0112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9163 L22:   1.5732                                     
REMARK   3      L33:   1.9249 L12:  -0.4074                                     
REMARK   3      L13:  -0.0973 L23:   0.0013                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1572 S12:   0.1833 S13:   0.0602                       
REMARK   3      S21:  -0.0530 S22:  -0.1520 S23:   0.0680                       
REMARK   3      S31:   0.0983 S32:  -0.2237 S33:  -0.0052                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     5        L   108                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.6460  -2.4744   7.5739              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0002 T22:   0.0617                                     
REMARK   3      T33:  -0.1895 T12:   0.0937                                     
REMARK   3      T13:  -0.0021 T23:  -0.0186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4587 L22:   2.5460                                     
REMARK   3      L33:   3.5854 L12:   1.6970                                     
REMARK   3      L13:   1.8570 L23:   1.3843                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0478 S12:   0.5957 S13:  -0.1265                       
REMARK   3      S21:  -0.3496 S22:  -0.0283 S23:   0.0487                       
REMARK   3      S31:   0.0654 S32:   0.0872 S33:  -0.0195                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   115        H   215                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6445 -10.0386  23.8519              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0481 T22:   0.0479                                     
REMARK   3      T33:  -0.0001 T12:   0.0238                                     
REMARK   3      T13:  -0.0569 T23:  -0.0440                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0291 L22:   3.0784                                     
REMARK   3      L33:   3.8451 L12:   1.2921                                     
REMARK   3      L13:   1.0530 L23:   0.9884                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0676 S12:   0.2081 S13:  -0.1070                       
REMARK   3      S21:  -0.3255 S22:   0.1312 S23:   0.1357                       
REMARK   3      S31:   0.3846 S32:   0.1443 S33:  -0.1988                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   109        L   209                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.8989   0.8652  12.6323              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0161 T22:   0.0893                                     
REMARK   3      T33:   0.1216 T12:  -0.0384                                     
REMARK   3      T13:   0.0365 T23:  -0.0352                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6758 L22:   0.8900                                     
REMARK   3      L33:   4.4852 L12:  -0.7226                                     
REMARK   3      L13:  -1.3123 L23:  -0.5614                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2686 S12:   0.2295 S13:   0.1568                       
REMARK   3      S21:  -0.1441 S22:   0.1185 S23:   0.0422                       
REMARK   3      S31:  -0.1156 S32:   0.0137 S33:  -0.3871                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   113                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.6301  -1.0893  19.4312              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1178 T22:   0.1174                                     
REMARK   3      T33:   0.0516 T12:   0.0415                                     
REMARK   3      T13:   0.0913 T23:   0.0205                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5375 L22:   5.7358                                     
REMARK   3      L33:   4.9151 L12:   0.3245                                     
REMARK   3      L13:   0.4119 L23:  -1.5527                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1752 S12:   0.4717 S13:  -0.0558                       
REMARK   3      S21:  -0.3124 S22:  -0.3262 S23:  -0.4497                       
REMARK   3      S31:   0.1153 S32:   0.5577 S33:   0.1510                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B           
REMARK   3  FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U           
REMARK   3  FACTORS.                                                            
REMARK   4                                                                      
REMARK   4 2XQB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-SEP-10.                  
REMARK 100 THE DEPOSITION ID IS D_1290045242.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-FEB-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC                              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU CCD                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17425                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 69.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1AQK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 32.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PCTP 100MM, PH 9.5, 25 %W/V PEG-3350,    
REMARK 280  200MM AMMONIUM SULPHATE                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       92.59300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       21.87700            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       92.59300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       21.87700            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L                               
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     SER A    18                                                      
REMARK 465     MET A    19                                                      
REMARK 465     HIS A    20                                                      
REMARK 465     SER A    76                                                      
REMARK 465     ASN A    77                                                      
REMARK 465     GLY A    78                                                      
REMARK 465     ASN A    79                                                      
REMARK 465     VAL A    80                                                      
REMARK 465     SER A   114                                                      
REMARK 465     CYS H   216                                                      
REMARK 465     ASP H   217                                                      
REMARK 465     LYS H   218                                                      
REMARK 465     THR H   219                                                      
REMARK 465     HIS H   220                                                      
REMARK 465     GLN H   221                                                      
REMARK 465     TYR H   222                                                      
REMARK 465     VAL H   223                                                      
REMARK 465     LEU H   224                                                      
REMARK 465     SER L    28                                                      
REMARK 465     ASN L    29                                                      
REMARK 465     LEU L    30                                                      
REMARK 465     LYS L    30A                                                     
REMARK 465     ARG L    30B                                                     
REMARK 465     GLN L   167                                                      
REMARK 465     GLU L   210                                                      
REMARK 465     CYS L   211                                                      
REMARK 465     SER L   212                                                      
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     ASN A   1    CG   OD1  ND2                                       
REMARK 470     LEU A  15    CG   CD1  CD2                                       
REMARK 470     ILE A  16    CG1  CG2  CD1                                       
REMARK 470     GLN A  17    CG   CD   OE1  NE2                                  
REMARK 470     ILE A  21    CG1  CG2  CD1                                       
REMARK 470     ASP A  22    CG   OD1  OD2                                       
REMARK 470     ASP A  30    CG   OD1  OD2                                       
REMARK 470     HIS A  32    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR A  81    OG1  CG2                                            
REMARK 470     LYS A  86    CG   CD   CE   NZ                                   
REMARK 470     ASN A  95    CG   OD1  ND2                                       
REMARK 470     ILE A  96    CG1  CG2  CD1                                       
REMARK 470     LYS A  97    CG   CD   CE   NZ                                   
REMARK 470     GLN H   1    CG   CD   OE1  NE2                                  
REMARK 470     ARG H 210    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS H 214    CG   CD   CE   NZ                                   
REMARK 470     ARG L  18    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG L  52    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG L  93    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS L 156    CG   CD   CE   NZ                                   
REMARK 470     TYR L 172    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS L 186    CG   CD   CE   NZ                                   
REMARK 470     ARG L 189    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LYS A    10     OD1  ASP A    14              0.99            
REMARK 500   OG   SER H   132     N    GLY H   133              1.78            
REMARK 500   O    SER H   127     OG1  THR H   131              1.90            
REMARK 500   O    LYS A    10     CG   ASP A    14              2.14            
REMARK 500   OD1  ASP A    56     OG   SER A    58              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    SER H 132   CB  -  CA  -  C   ANGL. DEV. = -12.5 DEGREES          
REMARK 500    PRO L  59   C   -  N   -  CA  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    PRO L 109   C   -  N   -  CD  ANGL. DEV. = -20.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  13        5.84    -54.43                                   
REMARK 500    ASP A  14      -70.92   -123.53                                   
REMARK 500    LEU A  15       -9.74    -38.47                                   
REMARK 500    ASP A  22     -165.33    167.27                                   
REMARK 500    ALA A  23     -154.33   -118.75                                   
REMARK 500    ASP A  30       24.25    -75.95                                   
REMARK 500    VAL A  31       97.02    -56.16                                   
REMARK 500    CYS A  35       22.87   -156.38                                   
REMARK 500    ASN A 112       21.89    -73.15                                   
REMARK 500    PHE H  32     -156.81   -123.33                                   
REMARK 500    GLN H  43     -167.54   -128.31                                   
REMARK 500    GLN H  61      -31.14    -37.17                                   
REMARK 500    ALA H  88      149.24    177.10                                   
REMARK 500    ASP H 101      117.29   -164.44                                   
REMARK 500    SER H 113       33.20    -74.67                                   
REMARK 500    SER H 115     -169.81   -128.49                                   
REMARK 500    SER H 132     -158.17   -177.37                                   
REMARK 500    PHE H 146      136.45   -177.82                                   
REMARK 500    PRO H 147     -141.18    -89.64                                   
REMARK 500    SER H 156       43.70     70.54                                   
REMARK 500    ALA H 158      -78.85    -52.45                                   
REMARK 500    SER H 161     -124.86    -43.42                                   
REMARK 500    VAL H 182      117.14   -167.14                                   
REMARK 500    SER H 186      -18.78    -49.46                                   
REMARK 500    THR H 191      -78.18   -132.82                                   
REMARK 500    PRO L  40      -86.47    -20.09                                   
REMARK 500    ASP L  51      -61.43     82.19                                   
REMARK 500    THR L  69       65.05   -101.84                                   
REMARK 500    SER L  70      128.39    171.04                                   
REMARK 500    LEU L  78      131.66     -7.13                                   
REMARK 500    ALA L  84     -178.32   -172.10                                   
REMARK 500    GLN L 108       -7.52   -154.13                                   
REMARK 500    PRO L 109     -129.92   -160.79                                   
REMARK 500    ALA L 111      150.40    175.77                                   
REMARK 500    ASN L 128       27.08     81.89                                   
REMARK 500    ASP L 151     -106.25     61.23                                   
REMARK 500    SER L 165     -160.14   -114.33                                   
REMARK 500    ASN L 170      -17.04     89.83                                   
REMARK 500    PRO L 208       48.44    -56.89                                   
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 SO4 H 1216                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 1217                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 1210                
DBREF  2XQB A    1   114  UNP    P40933   IL15_HUMAN      49    162             
DBREF  2XQB H    1   224  PDB    2XQB     2XQB             1    224             
DBREF  2XQB L    5   212  PDB    2XQB     2XQB             5    212             
SEQRES   1 A  114  ASN TRP VAL ASN VAL ILE SER ASP LEU LYS LYS ILE GLU          
SEQRES   2 A  114  ASP LEU ILE GLN SER MET HIS ILE ASP ALA THR LEU TYR          
SEQRES   3 A  114  THR GLU SER ASP VAL HIS PRO SER CYS LYS VAL THR ALA          
SEQRES   4 A  114  MET LYS CYS PHE LEU LEU GLU LEU GLN VAL ILE SER LEU          
SEQRES   5 A  114  GLU SER GLY ASP ALA SER ILE HIS ASP THR VAL GLU ASN          
SEQRES   6 A  114  LEU ILE ILE LEU ALA ASN ASN SER LEU SER SER ASN GLY          
SEQRES   7 A  114  ASN VAL THR GLU SER GLY CYS LYS GLU CYS GLU GLU LEU          
SEQRES   8 A  114  GLU GLU LYS ASN ILE LYS GLU PHE LEU GLN SER PHE VAL          
SEQRES   9 A  114  HIS ILE VAL GLN MET PHE ILE ASN THR SER                      
SEQRES   1 H  236  GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 H  236  PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY          
SEQRES   3 H  236  TYR SER PHE SER SER PHE GLY ILE SER TRP VAL ARG GLN          
SEQRES   4 H  236  ALA PRO GLY GLN GLY LEU GLU TRP LEU GLY TRP ILE SER          
SEQRES   5 H  236  ALA PHE ASN GLY TYR THR LYS TYR ALA GLN LYS PHE GLN          
SEQRES   6 H  236  ASP ARG VAL THR MET THR THR ASP THR SER THR SER THR          
SEQRES   7 H  236  ALA TYR MET GLU LEU ARG SER LEU ARG SER ASP ASP THR          
SEQRES   8 H  236  ALA VAL TYR TYR CYS ALA ARG ASP PRO ALA ALA TRP PRO          
SEQRES   9 H  236  LEU GLN GLN SER LEU ALA TRP PHE ASP PRO TRP GLY GLN          
SEQRES  10 H  236  GLY THR MET VAL THR VAL SER SER ALA SER THR LYS GLY          
SEQRES  11 H  236  PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR          
SEQRES  12 H  236  SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP          
SEQRES  13 H  236  TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY          
SEQRES  14 H  236  ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU          
SEQRES  15 H  236  GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR          
SEQRES  16 H  236  VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS          
SEQRES  17 H  236  ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS          
SEQRES  18 H  236  ARG VAL GLU PRO LYS SER CYS ASP LYS THR HIS GLN TYR          
SEQRES  19 H  236  VAL LEU                                                      
SEQRES   1 L  211  THR GLN PRO PRO SER ALA SER GLY THR PRO GLY GLN ARG          
SEQRES   2 L  211  VAL THR ILE SER CYS SER GLY SER THR SER ASN LEU LYS          
SEQRES   3 L  211  ARG ASN TYR VAL TYR TRP TYR GLN GLN LEU PRO GLY THR          
SEQRES   4 L  211  ALA PRO LYS LEU LEU ILE TYR ARG ASP ARG ARG ARG PRO          
SEQRES   5 L  211  SER GLY VAL PRO ASP ARG PHE SER GLY SER LYS SER GLY          
SEQRES   6 L  211  THR SER ALA SER LEU ALA ILE SER GLY LEU ARG SER GLU          
SEQRES   7 L  211  ASP GLU ALA ASP TYR TYR CYS ALA TRP TYR ASP ARG GLU          
SEQRES   8 L  211  LEU SER GLU TRP VAL PHE GLY GLY GLY THR LYS LEU THR          
SEQRES   9 L  211  VAL LEU GLN PRO LYS ALA ALA PRO SER VAL THR LEU PHE          
SEQRES  10 L  211  PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA THR          
SEQRES  11 L  211  LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA VAL          
SEQRES  12 L  211  THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL LYS ALA          
SEQRES  13 L  211  GLY VAL GLU THR THR THR PRO SER LYS GLN SER ASN ASN          
SEQRES  14 L  211  LYS TYR ALA ALA SER SER TYR LEU SER LEU THR PRO GLU          
SEQRES  15 L  211  GLN TRP LYS SER HIS ARG SER TYR SER CYS GLN VAL THR          
SEQRES  16 L  211  HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO THR          
SEQRES  17 L  211  GLU CYS SER                                                  
HET    SO4  H1216       5                                                       
HET    SO4  H1217       5                                                       
HET    SO4  L1210       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   4  SO4    3(O4 S 2-)                                                   
FORMUL   7  HOH   *66(H2 O)                                                     
HELIX    1   1 VAL A    3  ILE A   16  1                                  14    
HELIX    2   2 HIS A   32  SER A   34  5                                   3    
HELIX    3   3 CYS A   35  SER A   54  1                                  20    
HELIX    4   4 ALA A   57  SER A   75  1                                  19    
HELIX    5   5 GLU A   87  LEU A   91  5                                   5    
HELIX    6   6 ASN A   95  ASN A  112  1                                  18    
HELIX    7   7 SER H   28  SER H   31  5                                   4    
HELIX    8   8 ARG H   83  THR H   87  5                                   5    
HELIX    9   9 TRP H   99  ALA H  100F 5                                   8    
HELIX   10  10 SER H  156  ALA H  158  5                                   3    
HELIX   11  11 LYS H  201  ASN H  204  5                                   4    
HELIX   12  12 ARG L   79  GLU L   83  5                                   5    
HELIX   13  13 SER L  121  GLN L  126  1                                   6    
HELIX   14  14 THR L  181  SER L  187  1                                   7    
SHEET    1  AA 2 LEU A  25  THR A  27  0                                        
SHEET    2  AA 2 GLU A  92  LYS A  94 -1  O  GLU A  92   N  THR A  27           
SHEET    1  HA 4 GLN H   3  GLN H   6  0                                        
SHEET    2  HA 4 VAL H  18  SER H  25 -1  O  LYS H  23   N  VAL H   5           
SHEET    3  HA 4 THR H  77  LEU H  82 -1  O  ALA H  78   N  CYS H  22           
SHEET    4  HA 4 VAL H  67  ASP H  72 -1  O  THR H  68   N  GLU H  81           
SHEET    1  HB 6 GLU H  10  LYS H  12  0                                        
SHEET    2  HB 6 THR H 107  VAL H 111  1  O  MET H 108   N  GLU H  10           
SHEET    3  HB 6 ALA H  88  ASP H  95 -1  O  ALA H  88   N  VAL H 109           
SHEET    4  HB 6 GLY H  33  GLN H  39 -1  O  GLY H  33   N  ASP H  95           
SHEET    5  HB 6 LEU H  45  SER H  52 -1  O  GLU H  46   N  ARG H  38           
SHEET    6  HB 6 THR H  57  TYR H  59 -1  O  LYS H  58   N  TRP H  50           
SHEET    1  HC 4 SER H 120  LEU H 124  0                                        
SHEET    2  HC 4 THR H 135  TYR H 145 -1  O  GLY H 139   N  LEU H 124           
SHEET    3  HC 4 TYR H 176  PRO H 185 -1  O  TYR H 176   N  TYR H 145           
SHEET    4  HC 4 VAL H 169  LEU H 170  1  N  VAL H 169   O  SER H 177           
SHEET    1  HD 4 SER H 120  LEU H 124  0                                        
SHEET    2  HD 4 THR H 135  TYR H 145 -1  O  GLY H 139   N  LEU H 124           
SHEET    3  HD 4 TYR H 176  PRO H 185 -1  O  TYR H 176   N  TYR H 145           
SHEET    4  HD 4 GLY H 162  THR H 165 -1  O  GLY H 162   N  THR H 183           
SHEET    1  HE 2 VAL H 169  LEU H 170  0                                        
SHEET    2  HE 2 TYR H 176  PRO H 185  1  O  SER H 177   N  VAL H 169           
SHEET    1  HF 3 THR H 151  TRP H 154  0                                        
SHEET    2  HF 3 TYR H 194  HIS H 200 -1  O  ASN H 197   N  SER H 153           
SHEET    3  HF 3 THR H 205  VAL H 211 -1  O  THR H 205   N  HIS H 200           
SHEET    1  LA 4 SER L   9  GLY L  13  0                                        
SHEET    2  LA 4 THR L 102  VAL L 106  1  O  LYS L 103   N  ALA L  11           
SHEET    3  LA 4 ALA L  84  ASP L  92 -1  O  ALA L  84   N  LEU L 104           
SHEET    4  LA 4 GLU L  95B PHE L  98  1  O  GLU L  95B  N  ASP L  92           
SHEET    1  LB 5 SER L   9  GLY L  13  0                                        
SHEET    2  LB 5 THR L 102  VAL L 106  1  O  LYS L 103   N  ALA L  11           
SHEET    3  LB 5 ALA L  84  ASP L  92 -1  O  ALA L  84   N  LEU L 104           
SHEET    4  LB 5 VAL L  33  GLN L  38 -1  O  TYR L  34   N  ALA L  89           
SHEET    5  LB 5 LYS L  45  ILE L  48 -1  O  LYS L  45   N  GLN L  37           
SHEET    1  LC 2 GLU L  95B PHE L  98  0                                        
SHEET    2  LC 2 ALA L  84  ASP L  92  1  O  TRP L  90   N  VAL L  97           
SHEET    1  LD 3 VAL L  19  SER L  24  0                                        
SHEET    2  LD 3 SER L  70  ILE L  75 -1  O  ALA L  71   N  CYS L  23           
SHEET    3  LD 3 PHE L  62  LYS L  66 -1  O  SER L  63   N  ALA L  74           
SHEET    1  LE 4 SER L 114  PHE L 118  0                                        
SHEET    2  LE 4 ALA L 130  PHE L 139 -1  O  VAL L 133   N  PHE L 118           
SHEET    3  LE 4 TYR L 172  LEU L 180 -1  O  TYR L 172   N  PHE L 139           
SHEET    4  LE 4 VAL L 159  THR L 161 -1  O  GLU L 160   N  TYR L 177           
SHEET    1  LF 4 SER L 153  VAL L 155  0                                        
SHEET    2  LF 4 THR L 145  ALA L 150 -1  O  TRP L 148   N  VAL L 155           
SHEET    3  LF 4 TYR L 191  HIS L 197 -1  O  SER L 192   N  LYS L 149           
SHEET    4  LF 4 SER L 200  VAL L 206 -1  O  SER L 200   N  HIS L 197           
SSBOND   1 CYS A   35    CYS A   85                          1555   1555  2.03  
SSBOND   2 CYS A   42    CYS A   88                          1555   1555  2.03  
SSBOND   3 CYS H   22    CYS H   92                          1555   1555  2.04  
SSBOND   4 CYS H  140    CYS H  196                          1555   1555  2.03  
SSBOND   5 CYS L   23    CYS L   88                          1555   1555  2.03  
SSBOND   6 CYS L  134    CYS L  193                          1555   1555  2.03  
CISPEP   1 ASP H  101    PRO H  102          0        -5.22                     
CISPEP   2 THR H  131    SER H  132          0        15.61                     
CISPEP   3 PHE H  146    PRO H  147          0        -7.27                     
CISPEP   4 GLU H  148    PRO H  149          0         4.79                     
CISPEP   5 TYR L  140    PRO L  141          0        -0.62                     
SITE     1 AC1  6 SER H  25  ASN H  54  GLY H  55  THR H  71                    
SITE     2 AC1  6 HOH H2044  HOH H2045                                          
SITE     1 AC2  5 LYS A  41  TRP H  99  PRO H 100  LEU H 100A                   
SITE     2 AC2  5 HOH H2046                                                     
SITE     1 AC3  3 ARG L  52  ARG L  54  SER L  63                               
CRYST1  185.186   43.754   70.087  90.00  95.95  90.00 C 1 2 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      0.005400  0.000000  0.000563        0.00000                         
SCALE2      0.000000  0.022855  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014345        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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