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Database: PDB
Entry: 3WEX
LinkDB: 3WEX
Original site: 3WEX 
HEADER    IMMUNE SYSTEM                           16-JUL-13   3WEX              
TITLE     CRYSTAL STRUCTURE OF HLA-DP5 IN COMPLEX WITH CRY J 1-DERIVED PEPTIDE  
TITLE    2 (RESIDUES 214-222)                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MHC CLASS II ANTIGEN;                                      
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN, UNP RESIDUES 32-212;                 
COMPND   5 SYNONYM: HLA-DP5 ALPHA CHAIN;                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: MHC CLASS II ANTIGEN;                                      
COMPND   9 CHAIN: B, D, F, H;                                                   
COMPND  10 FRAGMENT: EXTRACELLULAR DOMAIN, UNP RESIDUES 1-184;                  
COMPND  11 SYNONYM: HLA-DP5 BETA CHAIN;                                         
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: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: BACULOVIRUS;                              
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: BACULOVIRUS                               
KEYWDS    IMMUNOGLOBULIN FOLD, ANTIGEN PRESENTATION, T CELL RECEPTOR, CELL      
KEYWDS   2 SURFACE, IMMUNE SYSTEM                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.KUSANO,M.KUKIMOTO-NIINO,M.SHIROUZU,S.YOKOYAMA                       
REVDAT   3   29-JUL-20 3WEX    1       COMPND REMARK SEQADV HETNAM              
REVDAT   3 2                   1       LINK   SITE                              
REVDAT   2   26-APR-17 3WEX    1       JRNL                                     
REVDAT   1   23-JUL-14 3WEX    0                                                
JRNL        AUTH   S.KUSANO,M.KUKIMOTO-NIINO,Y.SATTA,N.OHSAWA,T.UCHIKUBO-KAMO,  
JRNL        AUTH 2 M.WAKIYAMA,M.IKEDA,T.TERADA,K.YAMAMOTO,Y.NISHIMURA,          
JRNL        AUTH 3 M.SHIROUZU,T.SASAZUKI,S.YOKOYAMA                             
JRNL        TITL   STRUCTURAL BASIS FOR THE SPECIFIC RECOGNITION OF THE MAJOR   
JRNL        TITL 2 ANTIGENIC PEPTIDE FROM THE JAPANESE CEDAR POLLEN ALLERGEN    
JRNL        TITL 3 CRY J 1 BY HLA-DP5                                           
JRNL        REF    J. MOL. BIOL.                 V. 426  3016 2014              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   25020231                                                     
JRNL        DOI    10.1016/J.JMB.2014.06.020                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 64.28                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 70389                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3520                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 64.3019 -  7.0149    0.98     2693   142  0.1926 0.2477        
REMARK   3     2  7.0149 -  5.5689    1.00     2708   143  0.2083 0.2238        
REMARK   3     3  5.5689 -  4.8653    0.99     2739   144  0.1682 0.2183        
REMARK   3     4  4.8653 -  4.4205    0.99     2735   144  0.1508 0.1733        
REMARK   3     5  4.4205 -  4.1038    0.99     2701   142  0.1578 0.1697        
REMARK   3     6  4.1038 -  3.8618    0.99     2730   144  0.1742 0.2030        
REMARK   3     7  3.8618 -  3.6685    0.99     2740   144  0.1749 0.1924        
REMARK   3     8  3.6685 -  3.5088    0.99     2706   143  0.1818 0.2123        
REMARK   3     9  3.5088 -  3.3737    0.99     2697   141  0.1761 0.2146        
REMARK   3    10  3.3737 -  3.2573    0.98     2713   143  0.1961 0.2231        
REMARK   3    11  3.2573 -  3.1555    0.99     2721   144  0.2010 0.2383        
REMARK   3    12  3.1555 -  3.0653    0.98     2675   140  0.2065 0.2553        
REMARK   3    13  3.0653 -  2.9846    0.98     2736   144  0.2129 0.2684        
REMARK   3    14  2.9846 -  2.9117    0.98     2645   140  0.2130 0.2611        
REMARK   3    15  2.9117 -  2.8456    0.97     2695   141  0.2161 0.2342        
REMARK   3    16  2.8456 -  2.7850    0.97     2629   139  0.2229 0.2740        
REMARK   3    17  2.7850 -  2.7293    0.96     2724   143  0.2436 0.3014        
REMARK   3    18  2.7293 -  2.6778    0.96     2573   136  0.2562 0.2973        
REMARK   3    19  2.6778 -  2.6300    0.94     2639   138  0.2713 0.3353        
REMARK   3    20  2.6300 -  2.5854    0.95     2598   136  0.2719 0.2898        
REMARK   3    21  2.5854 -  2.5437    0.94     2576   136  0.2709 0.3553        
REMARK   3    22  2.5437 -  2.5045    0.95     2621   138  0.2798 0.2815        
REMARK   3    23  2.5045 -  2.4677    0.95     2618   138  0.2777 0.3185        
REMARK   3    24  2.4677 -  2.4329    0.96     2607   137  0.2943 0.3266        
REMARK   3    25  2.4329 -  2.4001    0.95     2650   140  0.2860 0.3279        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.930           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.06                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005          12796                                  
REMARK   3   ANGLE     :  1.071          17396                                  
REMARK   3   CHIRALITY :  0.064           1848                                  
REMARK   3   PLANARITY :  0.005           2300                                  
REMARK   3   DIHEDRAL  : 14.516           4664                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3WEX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-AUG-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000096249.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-SEP-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS, XSCALE                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70445                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 64.280                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.20100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.3100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
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 ENTRY 3LQZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% (W/V) PEG 3350, 0.2M AMMONIUM        
REMARK 280  NITRATE, PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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   182                                                      
REMARK 465     GLY A   183                                                      
REMARK 465     PRO A   184                                                      
REMARK 465     SER A   185                                                      
REMARK 465     SER A   186                                                      
REMARK 465     GLY A   187                                                      
REMARK 465     GLU A   188                                                      
REMARK 465     ASN A   189                                                      
REMARK 465     LEU A   190                                                      
REMARK 465     TYR A   191                                                      
REMARK 465     PHE A   192                                                      
REMARK 465     GLN A   193                                                      
REMARK 465     GLY B   -10                                                      
REMARK 465     GLY B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     LEU B    -7                                                      
REMARK 465     VAL B    -6                                                      
REMARK 465     PRO B    -5                                                      
REMARK 465     ARG B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     SER B   190                                                      
REMARK 465     GLY B   191                                                      
REMARK 465     PRO B   192                                                      
REMARK 465     SER B   193                                                      
REMARK 465     SER B   194                                                      
REMARK 465     GLY B   195                                                      
REMARK 465     GLU B   196                                                      
REMARK 465     ASN B   197                                                      
REMARK 465     LEU B   198                                                      
REMARK 465     TYR B   199                                                      
REMARK 465     PHE B   200                                                      
REMARK 465     GLN B   201                                                      
REMARK 465     SER C   182                                                      
REMARK 465     GLY C   183                                                      
REMARK 465     PRO C   184                                                      
REMARK 465     SER C   185                                                      
REMARK 465     SER C   186                                                      
REMARK 465     GLY C   187                                                      
REMARK 465     GLU C   188                                                      
REMARK 465     ASN C   189                                                      
REMARK 465     LEU C   190                                                      
REMARK 465     TYR C   191                                                      
REMARK 465     PHE C   192                                                      
REMARK 465     GLN C   193                                                      
REMARK 465     GLY D   -10                                                      
REMARK 465     GLY D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     LEU D    -7                                                      
REMARK 465     VAL D    -6                                                      
REMARK 465     PRO D    -5                                                      
REMARK 465     ARG D    -4                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     SER D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     SER D     3                                                      
REMARK 465     SER D   190                                                      
REMARK 465     GLY D   191                                                      
REMARK 465     PRO D   192                                                      
REMARK 465     SER D   193                                                      
REMARK 465     SER D   194                                                      
REMARK 465     GLY D   195                                                      
REMARK 465     GLU D   196                                                      
REMARK 465     ASN D   197                                                      
REMARK 465     LEU D   198                                                      
REMARK 465     TYR D   199                                                      
REMARK 465     PHE D   200                                                      
REMARK 465     GLN D   201                                                      
REMARK 465     SER E   182                                                      
REMARK 465     GLY E   183                                                      
REMARK 465     PRO E   184                                                      
REMARK 465     SER E   185                                                      
REMARK 465     SER E   186                                                      
REMARK 465     GLY E   187                                                      
REMARK 465     GLU E   188                                                      
REMARK 465     ASN E   189                                                      
REMARK 465     LEU E   190                                                      
REMARK 465     TYR E   191                                                      
REMARK 465     PHE E   192                                                      
REMARK 465     GLN E   193                                                      
REMARK 465     GLY F   -10                                                      
REMARK 465     GLY F    -9                                                      
REMARK 465     SER F    -8                                                      
REMARK 465     LEU F    -7                                                      
REMARK 465     VAL F    -6                                                      
REMARK 465     PRO F    -5                                                      
REMARK 465     ARG F    -4                                                      
REMARK 465     GLY F    -3                                                      
REMARK 465     SER F    -2                                                      
REMARK 465     GLY F    -1                                                      
REMARK 465     GLY F     0                                                      
REMARK 465     GLY F     1                                                      
REMARK 465     GLY F     2                                                      
REMARK 465     SER F     3                                                      
REMARK 465     SER F   190                                                      
REMARK 465     GLY F   191                                                      
REMARK 465     PRO F   192                                                      
REMARK 465     SER F   193                                                      
REMARK 465     SER F   194                                                      
REMARK 465     GLY F   195                                                      
REMARK 465     GLU F   196                                                      
REMARK 465     ASN F   197                                                      
REMARK 465     LEU F   198                                                      
REMARK 465     TYR F   199                                                      
REMARK 465     PHE F   200                                                      
REMARK 465     GLN F   201                                                      
REMARK 465     SER G   182                                                      
REMARK 465     GLY G   183                                                      
REMARK 465     PRO G   184                                                      
REMARK 465     SER G   185                                                      
REMARK 465     SER G   186                                                      
REMARK 465     GLY G   187                                                      
REMARK 465     GLU G   188                                                      
REMARK 465     ASN G   189                                                      
REMARK 465     LEU G   190                                                      
REMARK 465     TYR G   191                                                      
REMARK 465     PHE G   192                                                      
REMARK 465     GLN G   193                                                      
REMARK 465     GLY H   -10                                                      
REMARK 465     GLY H    -9                                                      
REMARK 465     SER H    -8                                                      
REMARK 465     LEU H    -7                                                      
REMARK 465     VAL H    -6                                                      
REMARK 465     PRO H    -5                                                      
REMARK 465     ARG H    -4                                                      
REMARK 465     GLY H    -3                                                      
REMARK 465     SER H    -2                                                      
REMARK 465     GLY H    -1                                                      
REMARK 465     GLY H     0                                                      
REMARK 465     GLY H     1                                                      
REMARK 465     GLY H     2                                                      
REMARK 465     SER H     3                                                      
REMARK 465     SER H   190                                                      
REMARK 465     GLY H   191                                                      
REMARK 465     PRO H   192                                                      
REMARK 465     SER H   193                                                      
REMARK 465     SER H   194                                                      
REMARK 465     GLY H   195                                                      
REMARK 465     GLU H   196                                                      
REMARK 465     ASN H   197                                                      
REMARK 465     LEU H   198                                                      
REMARK 465     TYR H   199                                                      
REMARK 465     PHE H   200                                                      
REMARK 465     GLN H   201                                                      
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   OE2  GLU H    44     NH1  ARG H    46              1.96            
REMARK 500   OD1  ASP F    74     NH1  ARG F    78              2.02            
REMARK 500   OE1  GLU B    50     NH2  ARG B    53              2.04            
REMARK 500   ND2  ASN A   118     C2   NAG A   201              2.10            
REMARK 500   ND2  ASN G   118     C2   NAG G   201              2.16            
REMARK 500   OE1  GLU F     5     OH   TYR F     7              2.16            
REMARK 500   NH1  ARG C   164     OE2  GLU C   166              2.17            
REMARK 500   NE   ARG F    53     OE2  GLU F    57              2.17            
REMARK 500   ND2  ASN C   118     C2   NAG C   201              2.18            
REMARK 500   OD2  ASP C   162     O    HOH C   335              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH2  ARG D   128     O    ASN F   132     1455     2.01            
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    PRO F 106   C   -  N   -  CA  ANGL. DEV. =   9.7 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    ASN B  19     -121.45     54.40                                   
REMARK 500    ASN B  31     -107.37     55.13                                   
REMARK 500    ARG B  75      -79.90   -100.10                                   
REMARK 500    VAL B  87      -69.66   -126.62                                   
REMARK 500    PRO B 106     -179.46    -63.73                                   
REMARK 500    ASN D  19     -124.40     57.41                                   
REMARK 500    ASN D  31     -106.78     55.14                                   
REMARK 500    ARG D  75      -80.41   -100.90                                   
REMARK 500    VAL D  87      -70.97   -125.92                                   
REMARK 500    PRO D 106     -152.50    -70.95                                   
REMARK 500    ASN D 144     -178.78     72.93                                   
REMARK 500    ASN F  19     -121.80     51.90                                   
REMARK 500    ASN F  31     -108.57     54.20                                   
REMARK 500    ARG F  75      -81.87    -97.80                                   
REMARK 500    VAL F  87      -69.10   -127.13                                   
REMARK 500    LYS F 104     -137.33    -94.52                                   
REMARK 500    GLN F 108       78.74   -100.53                                   
REMARK 500    HIS F 109     -179.71   -171.72                                   
REMARK 500    ASN H  19     -125.97     57.33                                   
REMARK 500    ASN H  31     -107.93     54.52                                   
REMARK 500    ARG H  75      -78.95   -101.37                                   
REMARK 500    VAL H  87      -70.44   -125.83                                   
REMARK 500    GLN H 108       -1.19     75.58                                   
REMARK 500    ASN H 144     -175.65     71.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3WEY   RELATED DB: PDB                                   
DBREF  3WEX A    1   181  UNP    I2G9G1   I2G9G1_HUMAN    32    212             
DBREF  3WEX B    6   189  UNP    I2FL84   I2FL84_HUMAN     1    184             
DBREF  3WEX C    1   181  UNP    I2G9G1   I2G9G1_HUMAN    32    212             
DBREF  3WEX D    6   189  UNP    I2FL84   I2FL84_HUMAN     1    184             
DBREF  3WEX E    1   181  UNP    I2G9G1   I2G9G1_HUMAN    32    212             
DBREF  3WEX F    6   189  UNP    I2FL84   I2FL84_HUMAN     1    184             
DBREF  3WEX G    1   181  UNP    I2G9G1   I2G9G1_HUMAN    32    212             
DBREF  3WEX H    6   189  UNP    I2FL84   I2FL84_HUMAN     1    184             
SEQADV 3WEX SER A  182  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX GLY A  183  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX PRO A  184  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX SER A  185  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX SER A  186  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX GLY A  187  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX GLU A  188  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX ASN A  189  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX LEU A  190  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX TYR A  191  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX PHE A  192  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX GLN A  193  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX LYS B  -19  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX VAL B  -18  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX THR B  -17  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX VAL B  -16  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX ALA B  -15  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PHE B  -14  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX ASN B  -13  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLN B  -12  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PHE B  -11  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY B  -10  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY B   -9  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER B   -8  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX LEU B   -7  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX VAL B   -6  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PRO B   -5  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX ARG B   -4  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY B   -3  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER B   -2  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY B   -1  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY B    0  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY B    1  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY B    2  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER B    3  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PRO B    4  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLU B    5  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER B  190  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY B  191  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PRO B  192  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER B  193  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER B  194  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY B  195  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLU B  196  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX ASN B  197  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX LEU B  198  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX TYR B  199  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PHE B  200  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLN B  201  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER C  182  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX GLY C  183  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX PRO C  184  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX SER C  185  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX SER C  186  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX GLY C  187  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX GLU C  188  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX ASN C  189  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX LEU C  190  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX TYR C  191  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX PHE C  192  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX GLN C  193  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX LYS D  -19  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX VAL D  -18  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX THR D  -17  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX VAL D  -16  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX ALA D  -15  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PHE D  -14  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX ASN D  -13  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLN D  -12  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PHE D  -11  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY D  -10  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY D   -9  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER D   -8  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX LEU D   -7  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX VAL D   -6  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PRO D   -5  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX ARG D   -4  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY D   -3  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER D   -2  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY D   -1  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY D    0  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY D    1  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY D    2  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER D    3  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PRO D    4  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLU D    5  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER D  190  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY D  191  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PRO D  192  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER D  193  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER D  194  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY D  195  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLU D  196  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX ASN D  197  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX LEU D  198  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX TYR D  199  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PHE D  200  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLN D  201  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER E  182  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX GLY E  183  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX PRO E  184  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX SER E  185  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX SER E  186  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX GLY E  187  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX GLU E  188  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX ASN E  189  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX LEU E  190  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX TYR E  191  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX PHE E  192  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX GLN E  193  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX LYS F  -19  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX VAL F  -18  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX THR F  -17  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX VAL F  -16  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX ALA F  -15  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PHE F  -14  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX ASN F  -13  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLN F  -12  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PHE F  -11  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY F  -10  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY F   -9  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER F   -8  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX LEU F   -7  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX VAL F   -6  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PRO F   -5  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX ARG F   -4  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY F   -3  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER F   -2  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY F   -1  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY F    0  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY F    1  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY F    2  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER F    3  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PRO F    4  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLU F    5  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER F  190  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY F  191  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PRO F  192  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER F  193  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER F  194  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY F  195  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLU F  196  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX ASN F  197  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX LEU F  198  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX TYR F  199  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PHE F  200  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLN F  201  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER G  182  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX GLY G  183  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX PRO G  184  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX SER G  185  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX SER G  186  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX GLY G  187  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX GLU G  188  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX ASN G  189  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX LEU G  190  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX TYR G  191  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX PHE G  192  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX GLN G  193  UNP  I2G9G1              EXPRESSION TAG                 
SEQADV 3WEX LYS H  -19  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX VAL H  -18  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX THR H  -17  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX VAL H  -16  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX ALA H  -15  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PHE H  -14  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX ASN H  -13  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLN H  -12  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PHE H  -11  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY H  -10  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY H   -9  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER H   -8  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX LEU H   -7  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX VAL H   -6  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PRO H   -5  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX ARG H   -4  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY H   -3  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER H   -2  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY H   -1  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY H    0  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY H    1  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY H    2  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER H    3  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PRO H    4  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLU H    5  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER H  190  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY H  191  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PRO H  192  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER H  193  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX SER H  194  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLY H  195  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLU H  196  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX ASN H  197  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX LEU H  198  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX TYR H  199  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX PHE H  200  UNP  I2FL84              EXPRESSION TAG                 
SEQADV 3WEX GLN H  201  UNP  I2FL84              EXPRESSION TAG                 
SEQRES   1 A  193  ILE LYS ALA ASP HIS VAL SER THR TYR ALA MET PHE VAL          
SEQRES   2 A  193  GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE          
SEQRES   3 A  193  ASP GLU ASP GLU GLN PHE TYR VAL ASP LEU ASP LYS LYS          
SEQRES   4 A  193  GLU THR VAL TRP HIS LEU GLU GLU PHE GLY ARG ALA PHE          
SEQRES   5 A  193  SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE          
SEQRES   6 A  193  LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN          
SEQRES   7 A  193  HIS THR GLN ALA ALA ASN ASP PRO PRO GLU VAL THR VAL          
SEQRES   8 A  193  PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR          
SEQRES   9 A  193  LEU ILE CYS HIS ILE ASP ARG PHE PHE PRO PRO VAL LEU          
SEQRES  10 A  193  ASN VAL THR TRP LEU CYS ASN GLY GLU PRO VAL THR GLU          
SEQRES  11 A  193  GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR          
SEQRES  12 A  193  SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER          
SEQRES  13 A  193  ALA GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 A  193  LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN SER          
SEQRES  15 A  193  GLY PRO SER SER GLY GLU ASN LEU TYR PHE GLN                  
SEQRES   1 B  221  LYS VAL THR VAL ALA PHE ASN GLN PHE GLY GLY SER LEU          
SEQRES   2 B  221  VAL PRO ARG GLY SER GLY GLY GLY GLY SER PRO GLU ASN          
SEQRES   3 B  221  TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR ALA PHE ASN          
SEQRES   4 B  221  GLY THR GLN ARG PHE LEU GLU ARG TYR ILE TYR ASN ARG          
SEQRES   5 B  221  GLU GLU LEU VAL ARG PHE ASP SER ASP VAL GLY GLU PHE          
SEQRES   6 B  221  ARG ALA VAL THR GLU LEU GLY ARG PRO GLU ALA GLU TYR          
SEQRES   7 B  221  TRP ASN SER GLN LYS ASP ILE LEU GLU GLU LYS ARG ALA          
SEQRES   8 B  221  VAL PRO ASP ARG MET CYS ARG HIS ASN TYR GLU LEU ASP          
SEQRES   9 B  221  GLU ALA VAL THR LEU GLN ARG ARG VAL GLN PRO LYS VAL          
SEQRES  10 B  221  ASN VAL SER PRO SER LYS LYS GLY PRO LEU GLN HIS HIS          
SEQRES  11 B  221  ASN LEU LEU VAL CYS HIS VAL THR ASP PHE TYR PRO GLY          
SEQRES  12 B  221  SER ILE GLN VAL ARG TRP PHE LEU ASN GLY GLN GLU GLU          
SEQRES  13 B  221  THR ALA GLY VAL VAL SER THR ASN LEU ILE ARG ASN GLY          
SEQRES  14 B  221  ASP TRP THR PHE GLN ILE LEU VAL MET LEU GLU MET THR          
SEQRES  15 B  221  PRO GLN GLN GLY ASP VAL TYR ILE CYS GLN VAL GLU HIS          
SEQRES  16 B  221  THR SER LEU ASP SER PRO VAL THR VAL GLU TRP LYS ALA          
SEQRES  17 B  221  GLN SER GLY PRO SER SER GLY GLU ASN LEU TYR PHE GLN          
SEQRES   1 C  193  ILE LYS ALA ASP HIS VAL SER THR TYR ALA MET PHE VAL          
SEQRES   2 C  193  GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE          
SEQRES   3 C  193  ASP GLU ASP GLU GLN PHE TYR VAL ASP LEU ASP LYS LYS          
SEQRES   4 C  193  GLU THR VAL TRP HIS LEU GLU GLU PHE GLY ARG ALA PHE          
SEQRES   5 C  193  SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE          
SEQRES   6 C  193  LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN          
SEQRES   7 C  193  HIS THR GLN ALA ALA ASN ASP PRO PRO GLU VAL THR VAL          
SEQRES   8 C  193  PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR          
SEQRES   9 C  193  LEU ILE CYS HIS ILE ASP ARG PHE PHE PRO PRO VAL LEU          
SEQRES  10 C  193  ASN VAL THR TRP LEU CYS ASN GLY GLU PRO VAL THR GLU          
SEQRES  11 C  193  GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR          
SEQRES  12 C  193  SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER          
SEQRES  13 C  193  ALA GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 C  193  LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN SER          
SEQRES  15 C  193  GLY PRO SER SER GLY GLU ASN LEU TYR PHE GLN                  
SEQRES   1 D  221  LYS VAL THR VAL ALA PHE ASN GLN PHE GLY GLY SER LEU          
SEQRES   2 D  221  VAL PRO ARG GLY SER GLY GLY GLY GLY SER PRO GLU ASN          
SEQRES   3 D  221  TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR ALA PHE ASN          
SEQRES   4 D  221  GLY THR GLN ARG PHE LEU GLU ARG TYR ILE TYR ASN ARG          
SEQRES   5 D  221  GLU GLU LEU VAL ARG PHE ASP SER ASP VAL GLY GLU PHE          
SEQRES   6 D  221  ARG ALA VAL THR GLU LEU GLY ARG PRO GLU ALA GLU TYR          
SEQRES   7 D  221  TRP ASN SER GLN LYS ASP ILE LEU GLU GLU LYS ARG ALA          
SEQRES   8 D  221  VAL PRO ASP ARG MET CYS ARG HIS ASN TYR GLU LEU ASP          
SEQRES   9 D  221  GLU ALA VAL THR LEU GLN ARG ARG VAL GLN PRO LYS VAL          
SEQRES  10 D  221  ASN VAL SER PRO SER LYS LYS GLY PRO LEU GLN HIS HIS          
SEQRES  11 D  221  ASN LEU LEU VAL CYS HIS VAL THR ASP PHE TYR PRO GLY          
SEQRES  12 D  221  SER ILE GLN VAL ARG TRP PHE LEU ASN GLY GLN GLU GLU          
SEQRES  13 D  221  THR ALA GLY VAL VAL SER THR ASN LEU ILE ARG ASN GLY          
SEQRES  14 D  221  ASP TRP THR PHE GLN ILE LEU VAL MET LEU GLU MET THR          
SEQRES  15 D  221  PRO GLN GLN GLY ASP VAL TYR ILE CYS GLN VAL GLU HIS          
SEQRES  16 D  221  THR SER LEU ASP SER PRO VAL THR VAL GLU TRP LYS ALA          
SEQRES  17 D  221  GLN SER GLY PRO SER SER GLY GLU ASN LEU TYR PHE GLN          
SEQRES   1 E  193  ILE LYS ALA ASP HIS VAL SER THR TYR ALA MET PHE VAL          
SEQRES   2 E  193  GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE          
SEQRES   3 E  193  ASP GLU ASP GLU GLN PHE TYR VAL ASP LEU ASP LYS LYS          
SEQRES   4 E  193  GLU THR VAL TRP HIS LEU GLU GLU PHE GLY ARG ALA PHE          
SEQRES   5 E  193  SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE          
SEQRES   6 E  193  LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN          
SEQRES   7 E  193  HIS THR GLN ALA ALA ASN ASP PRO PRO GLU VAL THR VAL          
SEQRES   8 E  193  PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR          
SEQRES   9 E  193  LEU ILE CYS HIS ILE ASP ARG PHE PHE PRO PRO VAL LEU          
SEQRES  10 E  193  ASN VAL THR TRP LEU CYS ASN GLY GLU PRO VAL THR GLU          
SEQRES  11 E  193  GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR          
SEQRES  12 E  193  SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER          
SEQRES  13 E  193  ALA GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 E  193  LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN SER          
SEQRES  15 E  193  GLY PRO SER SER GLY GLU ASN LEU TYR PHE GLN                  
SEQRES   1 F  221  LYS VAL THR VAL ALA PHE ASN GLN PHE GLY GLY SER LEU          
SEQRES   2 F  221  VAL PRO ARG GLY SER GLY GLY GLY GLY SER PRO GLU ASN          
SEQRES   3 F  221  TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR ALA PHE ASN          
SEQRES   4 F  221  GLY THR GLN ARG PHE LEU GLU ARG TYR ILE TYR ASN ARG          
SEQRES   5 F  221  GLU GLU LEU VAL ARG PHE ASP SER ASP VAL GLY GLU PHE          
SEQRES   6 F  221  ARG ALA VAL THR GLU LEU GLY ARG PRO GLU ALA GLU TYR          
SEQRES   7 F  221  TRP ASN SER GLN LYS ASP ILE LEU GLU GLU LYS ARG ALA          
SEQRES   8 F  221  VAL PRO ASP ARG MET CYS ARG HIS ASN TYR GLU LEU ASP          
SEQRES   9 F  221  GLU ALA VAL THR LEU GLN ARG ARG VAL GLN PRO LYS VAL          
SEQRES  10 F  221  ASN VAL SER PRO SER LYS LYS GLY PRO LEU GLN HIS HIS          
SEQRES  11 F  221  ASN LEU LEU VAL CYS HIS VAL THR ASP PHE TYR PRO GLY          
SEQRES  12 F  221  SER ILE GLN VAL ARG TRP PHE LEU ASN GLY GLN GLU GLU          
SEQRES  13 F  221  THR ALA GLY VAL VAL SER THR ASN LEU ILE ARG ASN GLY          
SEQRES  14 F  221  ASP TRP THR PHE GLN ILE LEU VAL MET LEU GLU MET THR          
SEQRES  15 F  221  PRO GLN GLN GLY ASP VAL TYR ILE CYS GLN VAL GLU HIS          
SEQRES  16 F  221  THR SER LEU ASP SER PRO VAL THR VAL GLU TRP LYS ALA          
SEQRES  17 F  221  GLN SER GLY PRO SER SER GLY GLU ASN LEU TYR PHE GLN          
SEQRES   1 G  193  ILE LYS ALA ASP HIS VAL SER THR TYR ALA MET PHE VAL          
SEQRES   2 G  193  GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE          
SEQRES   3 G  193  ASP GLU ASP GLU GLN PHE TYR VAL ASP LEU ASP LYS LYS          
SEQRES   4 G  193  GLU THR VAL TRP HIS LEU GLU GLU PHE GLY ARG ALA PHE          
SEQRES   5 G  193  SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE          
SEQRES   6 G  193  LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN          
SEQRES   7 G  193  HIS THR GLN ALA ALA ASN ASP PRO PRO GLU VAL THR VAL          
SEQRES   8 G  193  PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR          
SEQRES   9 G  193  LEU ILE CYS HIS ILE ASP ARG PHE PHE PRO PRO VAL LEU          
SEQRES  10 G  193  ASN VAL THR TRP LEU CYS ASN GLY GLU PRO VAL THR GLU          
SEQRES  11 G  193  GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR          
SEQRES  12 G  193  SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER          
SEQRES  13 G  193  ALA GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 G  193  LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN SER          
SEQRES  15 G  193  GLY PRO SER SER GLY GLU ASN LEU TYR PHE GLN                  
SEQRES   1 H  221  LYS VAL THR VAL ALA PHE ASN GLN PHE GLY GLY SER LEU          
SEQRES   2 H  221  VAL PRO ARG GLY SER GLY GLY GLY GLY SER PRO GLU ASN          
SEQRES   3 H  221  TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR ALA PHE ASN          
SEQRES   4 H  221  GLY THR GLN ARG PHE LEU GLU ARG TYR ILE TYR ASN ARG          
SEQRES   5 H  221  GLU GLU LEU VAL ARG PHE ASP SER ASP VAL GLY GLU PHE          
SEQRES   6 H  221  ARG ALA VAL THR GLU LEU GLY ARG PRO GLU ALA GLU TYR          
SEQRES   7 H  221  TRP ASN SER GLN LYS ASP ILE LEU GLU GLU LYS ARG ALA          
SEQRES   8 H  221  VAL PRO ASP ARG MET CYS ARG HIS ASN TYR GLU LEU ASP          
SEQRES   9 H  221  GLU ALA VAL THR LEU GLN ARG ARG VAL GLN PRO LYS VAL          
SEQRES  10 H  221  ASN VAL SER PRO SER LYS LYS GLY PRO LEU GLN HIS HIS          
SEQRES  11 H  221  ASN LEU LEU VAL CYS HIS VAL THR ASP PHE TYR PRO GLY          
SEQRES  12 H  221  SER ILE GLN VAL ARG TRP PHE LEU ASN GLY GLN GLU GLU          
SEQRES  13 H  221  THR ALA GLY VAL VAL SER THR ASN LEU ILE ARG ASN GLY          
SEQRES  14 H  221  ASP TRP THR PHE GLN ILE LEU VAL MET LEU GLU MET THR          
SEQRES  15 H  221  PRO GLN GLN GLY ASP VAL TYR ILE CYS GLN VAL GLU HIS          
SEQRES  16 H  221  THR SER LEU ASP SER PRO VAL THR VAL GLU TRP LYS ALA          
SEQRES  17 H  221  GLN SER GLY PRO SER SER GLY GLU ASN LEU TYR PHE GLN          
MODRES 3WEX ASN G  118  ASN  GLYCOSYLATION SITE                                 
MODRES 3WEX ASN A  118  ASN  GLYCOSYLATION SITE                                 
MODRES 3WEX ASN E  118  ASN  GLYCOSYLATION SITE                                 
MODRES 3WEX ASN C  118  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 201      14                                                       
HET    NAG  C 201      14                                                       
HET    NAG  E 201      14                                                       
HET    NAG  G 201      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   9  NAG    4(C8 H15 N O6)                                               
FORMUL  13  HOH   *267(H2 O)                                                    
HELIX    1   1 LEU A   45  PHE A   52  1                                   8    
HELIX    2   2 ALA A   56  SER A   77  1                                  22    
HELIX    3   3 THR B   49  LEU B   51  5                                   3    
HELIX    4   4 GLY B   52  ASN B   60  1                                   9    
HELIX    5   5 GLN B   62  ALA B   71  1                                  10    
HELIX    6   6 ARG B   75  VAL B   87  1                                  13    
HELIX    7   7 THR B   88  ARG B   91  5                                   4    
HELIX    8   8 LEU C   45  PHE C   52  1                                   8    
HELIX    9   9 ALA C   56  SER C   77  1                                  22    
HELIX   10  10 THR D   49  LEU D   51  5                                   3    
HELIX   11  11 GLY D   52  ASN D   60  1                                   9    
HELIX   12  12 GLN D   62  ALA D   71  1                                  10    
HELIX   13  13 ARG D   75  VAL D   87  1                                  13    
HELIX   14  14 THR D   88  ARG D   91  5                                   4    
HELIX   15  15 LEU E   45  PHE E   52  1                                   8    
HELIX   16  16 GLU E   55  SER E   77  1                                  23    
HELIX   17  17 THR F   49  LEU F   51  5                                   3    
HELIX   18  18 GLY F   52  ASN F   60  1                                   9    
HELIX   19  19 GLN F   62  ALA F   71  1                                  10    
HELIX   20  20 ARG F   75  VAL F   87  1                                  13    
HELIX   21  21 THR F   88  ARG F   91  5                                   4    
HELIX   22  22 LEU G   45  PHE G   52  1                                   8    
HELIX   23  23 ALA G   56  SER G   77  1                                  22    
HELIX   24  24 THR H   49  LEU H   51  5                                   3    
HELIX   25  25 GLY H   52  ASN H   60  1                                   9    
HELIX   26  26 GLN H   62  ALA H   71  1                                  10    
HELIX   27  27 ARG H   75  VAL H   87  1                                  13    
HELIX   28  28 THR H   88  ARG H   91  5                                   4    
SHEET    1   A 8 GLU A  40  TRP A  43  0                                        
SHEET    2   A 8 ASP A  29  ASP A  35 -1  N  TYR A  33   O  VAL A  42           
SHEET    3   A 8 GLY A  20  PHE A  26 -1  N  PHE A  24   O  PHE A  32           
SHEET    4   A 8 HIS A   5  GLN A  14 -1  N  THR A   8   O  GLU A  25           
SHEET    5   A 8 LEU B   8  PHE B  18 -1  O  CYS B  15   N  SER A   7           
SHEET    6   A 8 THR B  21  TYR B  30 -1  O  ILE B  29   N  GLN B  10           
SHEET    7   A 8 GLU B  33  ASP B  39 -1  O  LEU B  35   N  TYR B  28           
SHEET    8   A 8 PHE B  45  ALA B  47 -1  O  ARG B  46   N  ARG B  37           
SHEET    1   B 4 GLU A  88  PRO A  93  0                                        
SHEET    2   B 4 ASN A 103  PHE A 112 -1  O  ASP A 110   N  GLU A  88           
SHEET    3   B 4 PHE A 145  PHE A 153 -1  O  LEU A 151   N  LEU A 105           
SHEET    4   B 4 VAL A 132  GLU A 134 -1  N  ALA A 133   O  TYR A 150           
SHEET    1   C 4 GLU A  88  PRO A  93  0                                        
SHEET    2   C 4 ASN A 103  PHE A 112 -1  O  ASP A 110   N  GLU A  88           
SHEET    3   C 4 PHE A 145  PHE A 153 -1  O  LEU A 151   N  LEU A 105           
SHEET    4   C 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  HIS A 146           
SHEET    1   D 4 GLU A 126  PRO A 127  0                                        
SHEET    2   D 4 ASN A 118  CYS A 123 -1  N  CYS A 123   O  GLU A 126           
SHEET    3   D 4 VAL A 160  GLU A 166 -1  O  ARG A 164   N  THR A 120           
SHEET    4   D 4 LEU A 174  GLU A 179 -1  O  LEU A 174   N  VAL A 165           
SHEET    1   E 4 LYS B  96  PRO B 101  0                                        
SHEET    2   E 4 ASN B 111  PHE B 120 -1  O  HIS B 116   N  ASN B  98           
SHEET    3   E 4 PHE B 153  MET B 161 -1  O  ILE B 155   N  VAL B 117           
SHEET    4   E 4 VAL B 140  SER B 142 -1  N  VAL B 141   O  MET B 158           
SHEET    1   F 4 LYS B  96  PRO B 101  0                                        
SHEET    2   F 4 ASN B 111  PHE B 120 -1  O  HIS B 116   N  ASN B  98           
SHEET    3   F 4 PHE B 153  MET B 161 -1  O  ILE B 155   N  VAL B 117           
SHEET    4   F 4 ILE B 146  ARG B 147 -1  N  ILE B 146   O  GLN B 154           
SHEET    1   G 4 GLN B 134  GLU B 135  0                                        
SHEET    2   G 4 GLN B 126  LEU B 131 -1  N  LEU B 131   O  GLN B 134           
SHEET    3   G 4 VAL B 168  GLU B 174 -1  O  GLN B 172   N  ARG B 128           
SHEET    4   G 4 VAL B 182  LYS B 187 -1  O  VAL B 182   N  VAL B 173           
SHEET    1   H 8 GLU C  40  TRP C  43  0                                        
SHEET    2   H 8 ASP C  29  ASP C  35 -1  N  ASP C  35   O  GLU C  40           
SHEET    3   H 8 GLY C  20  PHE C  26 -1  N  PHE C  24   O  GLN C  31           
SHEET    4   H 8 HIS C   5  GLN C  14 -1  N  THR C   8   O  GLU C  25           
SHEET    5   H 8 LEU D   8  PHE D  18 -1  O  CYS D  15   N  SER C   7           
SHEET    6   H 8 THR D  21  TYR D  30 -1  O  LEU D  25   N  GLU D  14           
SHEET    7   H 8 GLU D  33  ASP D  39 -1  O  LEU D  35   N  TYR D  28           
SHEET    8   H 8 PHE D  45  ALA D  47 -1  O  ARG D  46   N  ARG D  37           
SHEET    1   I 4 GLU C  88  PRO C  93  0                                        
SHEET    2   I 4 ASN C 103  PHE C 112 -1  O  HIS C 108   N  THR C  90           
SHEET    3   I 4 PHE C 145  PHE C 153 -1  O  LEU C 151   N  LEU C 105           
SHEET    4   I 4 VAL C 132  GLU C 134 -1  N  ALA C 133   O  TYR C 150           
SHEET    1   J 4 GLU C  88  PRO C  93  0                                        
SHEET    2   J 4 ASN C 103  PHE C 112 -1  O  HIS C 108   N  THR C  90           
SHEET    3   J 4 PHE C 145  PHE C 153 -1  O  LEU C 151   N  LEU C 105           
SHEET    4   J 4 LEU C 138  PRO C 139 -1  N  LEU C 138   O  HIS C 146           
SHEET    1   K 4 GLU C 126  VAL C 128  0                                        
SHEET    2   K 4 ASN C 118  CYS C 123 -1  N  CYS C 123   O  GLU C 126           
SHEET    3   K 4 TYR C 161  GLU C 166 -1  O  ARG C 164   N  THR C 120           
SHEET    4   K 4 LEU C 174  TRP C 178 -1  O  LEU C 174   N  VAL C 165           
SHEET    1   L 4 LYS D  96  PRO D 101  0                                        
SHEET    2   L 4 ASN D 111  PHE D 120 -1  O  HIS D 116   N  ASN D  98           
SHEET    3   L 4 PHE D 153  MET D 161 -1  O  ILE D 155   N  VAL D 117           
SHEET    4   L 4 VAL D 140  SER D 142 -1  N  VAL D 141   O  MET D 158           
SHEET    1   M 4 LYS D  96  PRO D 101  0                                        
SHEET    2   M 4 ASN D 111  PHE D 120 -1  O  HIS D 116   N  ASN D  98           
SHEET    3   M 4 PHE D 153  MET D 161 -1  O  ILE D 155   N  VAL D 117           
SHEET    4   M 4 ILE D 146  ARG D 147 -1  N  ILE D 146   O  GLN D 154           
SHEET    1   N 4 GLN D 134  GLU D 135  0                                        
SHEET    2   N 4 GLN D 126  LEU D 131 -1  N  LEU D 131   O  GLN D 134           
SHEET    3   N 4 VAL D 168  GLU D 174 -1  O  GLN D 172   N  ARG D 128           
SHEET    4   N 4 VAL D 182  LYS D 187 -1  O  VAL D 182   N  VAL D 173           
SHEET    1   O 8 GLU E  40  TRP E  43  0                                        
SHEET    2   O 8 ASP E  29  ASP E  35 -1  N  TYR E  33   O  VAL E  42           
SHEET    3   O 8 GLY E  20  PHE E  26 -1  N  PHE E  24   O  GLN E  31           
SHEET    4   O 8 HIS E   5  GLN E  14 -1  N  THR E   8   O  GLU E  25           
SHEET    5   O 8 LEU F   8  PHE F  18 -1  O  CYS F  15   N  SER E   7           
SHEET    6   O 8 THR F  21  TYR F  30 -1  O  ILE F  29   N  GLN F  10           
SHEET    7   O 8 GLU F  33  ASP F  39 -1  O  LEU F  35   N  TYR F  28           
SHEET    8   O 8 PHE F  45  ALA F  47 -1  O  ARG F  46   N  ARG F  37           
SHEET    1   P 4 GLU E  88  PRO E  93  0                                        
SHEET    2   P 4 ASN E 103  PHE E 112 -1  O  HIS E 108   N  THR E  90           
SHEET    3   P 4 PHE E 145  PHE E 153 -1  O  LEU E 151   N  LEU E 105           
SHEET    4   P 4 VAL E 132  GLU E 134 -1  N  ALA E 133   O  TYR E 150           
SHEET    1   Q 4 GLU E  88  PRO E  93  0                                        
SHEET    2   Q 4 ASN E 103  PHE E 112 -1  O  HIS E 108   N  THR E  90           
SHEET    3   Q 4 PHE E 145  PHE E 153 -1  O  LEU E 151   N  LEU E 105           
SHEET    4   Q 4 LEU E 138  PRO E 139 -1  N  LEU E 138   O  HIS E 146           
SHEET    1   R 4 GLU E 126  PRO E 127  0                                        
SHEET    2   R 4 ASN E 118  CYS E 123 -1  N  CYS E 123   O  GLU E 126           
SHEET    3   R 4 TYR E 161  GLU E 166 -1  O  ARG E 164   N  THR E 120           
SHEET    4   R 4 LEU E 174  TRP E 178 -1  O  LEU E 174   N  VAL E 165           
SHEET    1   S 4 LYS F  96  PRO F 101  0                                        
SHEET    2   S 4 ASN F 111  PHE F 120 -1  O  VAL F 114   N  SER F 100           
SHEET    3   S 4 PHE F 153  MET F 161 -1  O  MET F 161   N  ASN F 111           
SHEET    4   S 4 VAL F 140  SER F 142 -1  N  VAL F 141   O  MET F 158           
SHEET    1   T 4 LYS F  96  PRO F 101  0                                        
SHEET    2   T 4 ASN F 111  PHE F 120 -1  O  VAL F 114   N  SER F 100           
SHEET    3   T 4 PHE F 153  MET F 161 -1  O  MET F 161   N  ASN F 111           
SHEET    4   T 4 ILE F 146  ARG F 147 -1  N  ILE F 146   O  GLN F 154           
SHEET    1   U 4 GLN F 134  GLU F 135  0                                        
SHEET    2   U 4 GLN F 126  LEU F 131 -1  N  LEU F 131   O  GLN F 134           
SHEET    3   U 4 VAL F 168  GLU F 174 -1  O  GLN F 172   N  ARG F 128           
SHEET    4   U 4 VAL F 182  LYS F 187 -1  O  TRP F 186   N  TYR F 169           
SHEET    1   V 8 GLU G  40  TRP G  43  0                                        
SHEET    2   V 8 ASP G  29  ASP G  35 -1  N  TYR G  33   O  VAL G  42           
SHEET    3   V 8 GLY G  20  PHE G  26 -1  N  PHE G  24   O  GLN G  31           
SHEET    4   V 8 HIS G   5  GLN G  14 -1  N  THR G   8   O  GLU G  25           
SHEET    5   V 8 LEU H   8  PHE H  18 -1  O  CYS H  15   N  SER G   7           
SHEET    6   V 8 THR H  21  TYR H  30 -1  O  ILE H  29   N  GLN H  10           
SHEET    7   V 8 GLU H  33  ASP H  39 -1  O  LEU H  35   N  TYR H  28           
SHEET    8   V 8 PHE H  45  ALA H  47 -1  O  ARG H  46   N  ARG H  37           
SHEET    1   W 4 GLU G  88  PRO G  93  0                                        
SHEET    2   W 4 ASN G 103  PHE G 112 -1  O  ASP G 110   N  GLU G  88           
SHEET    3   W 4 PHE G 145  PHE G 153 -1  O  LEU G 151   N  LEU G 105           
SHEET    4   W 4 VAL G 132  GLU G 134 -1  N  ALA G 133   O  TYR G 150           
SHEET    1   X 4 GLU G  88  PRO G  93  0                                        
SHEET    2   X 4 ASN G 103  PHE G 112 -1  O  ASP G 110   N  GLU G  88           
SHEET    3   X 4 PHE G 145  PHE G 153 -1  O  LEU G 151   N  LEU G 105           
SHEET    4   X 4 LEU G 138  PRO G 139 -1  N  LEU G 138   O  HIS G 146           
SHEET    1   Y 4 GLU G 126  VAL G 128  0                                        
SHEET    2   Y 4 ASN G 118  CYS G 123 -1  N  CYS G 123   O  GLU G 126           
SHEET    3   Y 4 TYR G 161  GLU G 166 -1  O  ARG G 164   N  THR G 120           
SHEET    4   Y 4 LEU G 174  TRP G 178 -1  O  LEU G 174   N  VAL G 165           
SHEET    1   Z 4 LYS H  96  PRO H 101  0                                        
SHEET    2   Z 4 ASN H 111  PHE H 120 -1  O  HIS H 116   N  ASN H  98           
SHEET    3   Z 4 PHE H 153  MET H 161 -1  O  ILE H 155   N  VAL H 117           
SHEET    4   Z 4 VAL H 140  SER H 142 -1  N  VAL H 141   O  MET H 158           
SHEET    1  AA 4 LYS H  96  PRO H 101  0                                        
SHEET    2  AA 4 ASN H 111  PHE H 120 -1  O  HIS H 116   N  ASN H  98           
SHEET    3  AA 4 PHE H 153  MET H 161 -1  O  ILE H 155   N  VAL H 117           
SHEET    4  AA 4 ILE H 146  ARG H 147 -1  N  ILE H 146   O  GLN H 154           
SHEET    1  AB 4 GLN H 134  GLU H 136  0                                        
SHEET    2  AB 4 GLN H 126  LEU H 131 -1  N  TRP H 129   O  GLU H 136           
SHEET    3  AB 4 VAL H 168  GLU H 174 -1  O  ILE H 170   N  PHE H 130           
SHEET    4  AB 4 VAL H 182  LYS H 187 -1  O  TRP H 186   N  TYR H 169           
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.04  
SSBOND   2 CYS B   15    CYS B   77                          1555   1555  2.03  
SSBOND   3 CYS B  115    CYS B  171                          1555   1555  2.02  
SSBOND   4 CYS C  107    CYS C  163                          1555   1555  2.04  
SSBOND   5 CYS D   15    CYS D   77                          1555   1555  2.04  
SSBOND   6 CYS D  115    CYS D  171                          1555   1555  2.03  
SSBOND   7 CYS E  107    CYS E  163                          1555   1555  2.04  
SSBOND   8 CYS F   15    CYS F   77                          1555   1555  2.03  
SSBOND   9 CYS F  115    CYS F  171                          1555   1555  2.03  
SSBOND  10 CYS G  107    CYS G  163                          1555   1555  2.04  
SSBOND  11 CYS H   15    CYS H   77                          1555   1555  2.03  
SSBOND  12 CYS H  115    CYS H  171                          1555   1555  2.03  
LINK         ND2 ASN A 118                 C1  NAG A 201     1555   1555  1.44  
LINK         ND2 ASN C 118                 C1  NAG C 201     1555   1555  1.44  
LINK         ND2 ASN E 118                 C1  NAG E 201     1555   1555  1.44  
LINK         ND2 ASN G 118                 C1  NAG G 201     1555   1555  1.44  
CISPEP   1 ARG A   17    PRO A   18          0        -0.35                     
CISPEP   2 PHE A  113    PRO A  114          0         1.69                     
CISPEP   3 TYR B  121    PRO B  122          0        -0.29                     
CISPEP   4 ARG C   17    PRO C   18          0         0.82                     
CISPEP   5 PHE C  113    PRO C  114          0         0.70                     
CISPEP   6 TYR D  121    PRO D  122          0         1.21                     
CISPEP   7 ARG E   17    PRO E   18          0         1.50                     
CISPEP   8 PHE E  113    PRO E  114          0         1.32                     
CISPEP   9 PRO F  106    LEU F  107          0        11.83                     
CISPEP  10 TYR F  121    PRO F  122          0         1.35                     
CISPEP  11 GLN F  165    GLY F  166          0        11.85                     
CISPEP  12 ARG G   17    PRO G   18          0        -0.66                     
CISPEP  13 PHE G  113    PRO G  114          0         1.55                     
CISPEP  14 TYR H  121    PRO H  122          0         0.72                     
CRYST1   61.150   64.370  130.360  92.99  97.53 109.41 P 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      0.016353  0.005762  0.002766        0.00000                         
SCALE2      0.000000  0.016471  0.001694        0.00000                         
SCALE3      0.000000  0.000000  0.007779        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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