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Database: PDB
Entry: 5WJN
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HEADER    IMMUNE SYSTEM                           23-JUL-17   5WJN              
TITLE     CRYSTAL STRUCTURE OF HLA-A*11:01-GTS3                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-11 ALPHA CHAIN;  
COMPND   3 CHAIN: A, D, G;                                                      
COMPND   4 SYNONYM: MHC CLASS I ANTIGEN A*11;                                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: BETA-2-MICROGLOBULIN;                                      
COMPND   8 CHAIN: B, E, H;                                                      
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: GTS3 PEPTIDE;                                              
COMPND  12 CHAIN: C, F, I;                                                      
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HLA-A, HLAA;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET30;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: B2M, CDABP0092, HDCMA22P;                                      
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET30;                                    
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 SYNTHETIC: YES;                                                      
SOURCE  23 ORGANISM_SCIENTIFIC: DENGUE VIRUS 3;                                 
SOURCE  24 ORGANISM_TAXID: 11069;                                               
SOURCE  25 OTHER_DETAILS: GL BIOCHEM                                            
KEYWDS    HLA, TCR, DENGUE, CD8 T CELLS, IMMUNE SYSTEM                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.GRAS,J.ROSSJOHN                                                     
REVDAT   3   25-OCT-17 5WJN    1       JRNL                                     
REVDAT   2   11-OCT-17 5WJN    1       JRNL                                     
REVDAT   1   20-SEP-17 5WJN    0                                                
JRNL        AUTH   A.CULSHAW,K.LADELL,S.GRAS,J.E.MCLAREN,K.L.MINERS,C.FARENC,   
JRNL        AUTH 2 H.VAN DEN HEUVEL,E.GOSTICK,W.DEJNIRATTISAI,                  
JRNL        AUTH 3 A.WANGTEERAPRASERT,T.DUANGCHINDA,P.CHOTIYARNWONG,            
JRNL        AUTH 4 W.LIMPITIKUL,S.VASANAWATHANA,P.MALASIT,T.DONG,J.ROSSJOHN,    
JRNL        AUTH 5 J.MONGKOLSAPAYA,D.A.PRICE,G.R.SCREATON                       
JRNL        TITL   GERMLINE BIAS DICTATES CROSS-SEROTYPE REACTIVITY IN A COMMON 
JRNL        TITL 2 DENGUE-VIRUS-SPECIFIC CD8(+) T CELL RESPONSE.                
JRNL        REF    NAT. IMMUNOL.                 V.  18  1228 2017              
JRNL        REFN                   ESSN 1529-2916                               
JRNL        PMID   28945243                                                     
JRNL        DOI    10.1038/NI.3850                                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.0                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 47215                          
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)  : 0.202                          
REMARK   3   R VALUE            (WORKING SET)  : 0.201                          
REMARK   3   FREE R VALUE                      : 0.230                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.060                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2388                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.85                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.92                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 98.09                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3567                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2549                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3424                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2536                   
REMARK   3   BIN FREE R VALUE                        : 0.2884                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.01                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 143                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9429                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 339                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 65.69                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.21320                                              
REMARK   3    B22 (A**2) : 0.97340                                              
REMARK   3    B33 (A**2) : -1.18660                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.50220                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.402               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.598               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.292               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.631               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.299               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.925                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.901                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 9695   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 13148  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 3354   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 279    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1406   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 9695   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 1      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1201   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 10569  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.007                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.99                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.45                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.72                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5WJN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229145.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.954                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.21                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47263                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.670                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.14700                            
REMARK 200  R SYM                      (I) : 0.14700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.05200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4-1.8M NH4SO4, 0.1M NA-CACODYLATE      
REMARK 280  PH6.5, 200MM NACL, 2% ETHYLEN GLYCOL, PH 8.5, VAPOR DIFFUSION,      
REMARK 280  TEMPERATURE 277K                                                    
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       79.16250            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.76100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       79.16250            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       72.76100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: 4470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 4370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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: 3                                                       
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: 4420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I                               
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 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   OH   TYR D    85     OD2  ASP D   137              2.19            
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    ASP A  29     -122.27     62.25                                   
REMARK 500    ARG A 114      115.01   -163.97                                   
REMARK 500    TYR A 123      -72.87   -109.05                                   
REMARK 500    ILE C   7       69.09     61.34                                   
REMARK 500    ASP D  29     -122.12     62.43                                   
REMARK 500    LEU D  81       -9.93    -56.17                                   
REMARK 500    ASN D  86       50.61     70.15                                   
REMARK 500    ARG D 114      110.36   -163.39                                   
REMARK 500    TYR D 123      -72.99   -109.23                                   
REMARK 500    LYS E  48       61.64     60.32                                   
REMARK 500    ILE F   7       69.73     61.33                                   
REMARK 500    ASP G  29     -122.62     62.37                                   
REMARK 500    ARG G 114      112.33   -162.81                                   
REMARK 500    TYR G 123      -73.02   -114.71                                   
REMARK 500    ASP H  98       45.27     86.95                                   
REMARK 500    PRO I   6      -70.12    -65.31                                   
REMARK 500    ILE I   7       69.92     61.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 362        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH A 363        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH A 364        DISTANCE =  6.83 ANGSTROMS                       
REMARK 525    HOH A 365        DISTANCE =  7.99 ANGSTROMS                       
REMARK 525    HOH A 366        DISTANCE =  8.46 ANGSTROMS                       
REMARK 525    HOH A 367        DISTANCE =  8.71 ANGSTROMS                       
REMARK 525    HOH A 368        DISTANCE =  8.86 ANGSTROMS                       
REMARK 525    HOH A 369        DISTANCE =  9.33 ANGSTROMS                       
REMARK 525    HOH A 370        DISTANCE =  9.35 ANGSTROMS                       
REMARK 525    HOH A 371        DISTANCE =  9.38 ANGSTROMS                       
REMARK 525    HOH A 372        DISTANCE =  9.77 ANGSTROMS                       
REMARK 525    HOH A 373        DISTANCE = 10.31 ANGSTROMS                       
REMARK 525    HOH A 374        DISTANCE = 10.35 ANGSTROMS                       
REMARK 525    HOH B 243        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH B 244        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH B 245        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH B 246        DISTANCE =  7.54 ANGSTROMS                       
REMARK 525    HOH B 247        DISTANCE =  8.42 ANGSTROMS                       
REMARK 525    HOH D 379        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH D 380        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH D 381        DISTANCE =  6.54 ANGSTROMS                       
REMARK 525    HOH D 382        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH D 383        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH D 384        DISTANCE =  7.04 ANGSTROMS                       
REMARK 525    HOH D 385        DISTANCE =  7.88 ANGSTROMS                       
REMARK 525    HOH D 386        DISTANCE = 10.17 ANGSTROMS                       
REMARK 525    HOH D 387        DISTANCE = 12.14 ANGSTROMS                       
REMARK 525    HOH E 132        DISTANCE =  8.72 ANGSTROMS                       
REMARK 525    HOH E 133        DISTANCE =  9.49 ANGSTROMS                       
REMARK 525    HOH E 134        DISTANCE =  9.91 ANGSTROMS                       
REMARK 525    HOH E 135        DISTANCE = 11.12 ANGSTROMS                       
REMARK 525    HOH E 136        DISTANCE = 12.61 ANGSTROMS                       
REMARK 525    HOH G 344        DISTANCE =  6.92 ANGSTROMS                       
REMARK 525    HOH G 345        DISTANCE =  7.05 ANGSTROMS                       
REMARK 525    HOH G 346        DISTANCE =  7.10 ANGSTROMS                       
REMARK 525    HOH G 347        DISTANCE =  7.39 ANGSTROMS                       
REMARK 525    HOH G 348        DISTANCE =  7.68 ANGSTROMS                       
REMARK 525    HOH G 349        DISTANCE =  8.68 ANGSTROMS                       
REMARK 525    HOH G 350        DISTANCE =  8.71 ANGSTROMS                       
REMARK 525    HOH G 351        DISTANCE =  9.47 ANGSTROMS                       
REMARK 525    HOH G 352        DISTANCE =  9.95 ANGSTROMS                       
REMARK 525    HOH G 353        DISTANCE =  9.99 ANGSTROMS                       
REMARK 525    HOH G 354        DISTANCE = 11.21 ANGSTROMS                       
REMARK 525    HOH G 355        DISTANCE = 13.45 ANGSTROMS                       
REMARK 525    HOH G 356        DISTANCE = 14.53 ANGSTROMS                       
REMARK 525    HOH G 357        DISTANCE = 14.58 ANGSTROMS                       
REMARK 525    HOH H 116        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH H 117        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH H 118        DISTANCE =  6.85 ANGSTROMS                       
REMARK 525    HOH H 119        DISTANCE =  7.16 ANGSTROMS                       
REMARK 525    HOH H 120        DISTANCE =  7.48 ANGSTROMS                       
REMARK 525    HOH H 121        DISTANCE =  8.85 ANGSTROMS                       
REMARK 525    HOH H 122        DISTANCE = 14.57 ANGSTROMS                       
REMARK 525    HOH I 105        DISTANCE =  7.21 ANGSTROMS                       
REMARK 525    HOH I 106        DISTANCE = 12.07 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 101   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B  83   OD1                                                    
REMARK 620 2 HIS B  84   O    71.0                                              
REMARK 620 3 LEU B  87   O    92.9  67.4                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 101                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5WJL   RELATED DB: PDB                                   
DBREF  5WJN A    1   274  UNP    P13746   1A11_HUMAN      25    298             
DBREF  5WJN B    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  5WJN C    1    10  PDB    5WJN     5WJN             1     10             
DBREF  5WJN D    1   274  UNP    P13746   1A11_HUMAN      25    298             
DBREF  5WJN E    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  5WJN F    1    10  PDB    5WJN     5WJN             1     10             
DBREF  5WJN G    1   274  UNP    P13746   1A11_HUMAN      25    298             
DBREF  5WJN H    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  5WJN I    1    10  PDB    5WJN     5WJN             1     10             
SEQADV 5WJN MET B    0  UNP  P61769              INITIATING METHIONINE          
SEQADV 5WJN MET E    0  UNP  P61769              INITIATING METHIONINE          
SEQADV 5WJN MET H    0  UNP  P61769              INITIATING METHIONINE          
SEQRES   1 A  274  GLY SER HIS SER MET ARG TYR PHE TYR THR SER VAL SER          
SEQRES   2 A  274  ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY          
SEQRES   3 A  274  TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP          
SEQRES   4 A  274  ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE          
SEQRES   5 A  274  GLU GLN GLU GLY PRO GLU TYR TRP ASP GLN GLU THR ARG          
SEQRES   6 A  274  ASN VAL LYS ALA GLN SER GLN THR ASP ARG VAL ASP LEU          
SEQRES   7 A  274  GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ASP GLY          
SEQRES   8 A  274  SER HIS THR ILE GLN ILE MET TYR GLY CYS ASP VAL GLY          
SEQRES   9 A  274  PRO ASP GLY ARG PHE LEU ARG GLY TYR ARG GLN ASP ALA          
SEQRES  10 A  274  TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP LEU          
SEQRES  11 A  274  ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR          
SEQRES  12 A  274  LYS ARG LYS TRP GLU ALA ALA HIS ALA ALA GLU GLN GLN          
SEQRES  13 A  274  ARG ALA TYR LEU GLU GLY ARG CYS VAL GLU TRP LEU ARG          
SEQRES  14 A  274  ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR          
SEQRES  15 A  274  ASP PRO PRO LYS THR HIS MET THR HIS HIS PRO ILE SER          
SEQRES  16 A  274  ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY PHE          
SEQRES  17 A  274  TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY          
SEQRES  18 A  274  GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG          
SEQRES  19 A  274  PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL          
SEQRES  20 A  274  VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS          
SEQRES  21 A  274  VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG          
SEQRES  22 A  274  TRP                                                          
SEQRES   1 B  100  MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG          
SEQRES   2 B  100  HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS          
SEQRES   3 B  100  TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP          
SEQRES   4 B  100  LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS          
SEQRES   5 B  100  SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU          
SEQRES   6 B  100  LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU          
SEQRES   7 B  100  TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO          
SEQRES   8 B  100  LYS ILE VAL LYS TRP ASP ARG ASP MET                          
SEQRES   1 C   10  GLY THR SER GLY SER PRO ILE ILE ASN ARG                      
SEQRES   1 D  274  GLY SER HIS SER MET ARG TYR PHE TYR THR SER VAL SER          
SEQRES   2 D  274  ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY          
SEQRES   3 D  274  TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP          
SEQRES   4 D  274  ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE          
SEQRES   5 D  274  GLU GLN GLU GLY PRO GLU TYR TRP ASP GLN GLU THR ARG          
SEQRES   6 D  274  ASN VAL LYS ALA GLN SER GLN THR ASP ARG VAL ASP LEU          
SEQRES   7 D  274  GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ASP GLY          
SEQRES   8 D  274  SER HIS THR ILE GLN ILE MET TYR GLY CYS ASP VAL GLY          
SEQRES   9 D  274  PRO ASP GLY ARG PHE LEU ARG GLY TYR ARG GLN ASP ALA          
SEQRES  10 D  274  TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP LEU          
SEQRES  11 D  274  ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR          
SEQRES  12 D  274  LYS ARG LYS TRP GLU ALA ALA HIS ALA ALA GLU GLN GLN          
SEQRES  13 D  274  ARG ALA TYR LEU GLU GLY ARG CYS VAL GLU TRP LEU ARG          
SEQRES  14 D  274  ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR          
SEQRES  15 D  274  ASP PRO PRO LYS THR HIS MET THR HIS HIS PRO ILE SER          
SEQRES  16 D  274  ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY PHE          
SEQRES  17 D  274  TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY          
SEQRES  18 D  274  GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG          
SEQRES  19 D  274  PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL          
SEQRES  20 D  274  VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS          
SEQRES  21 D  274  VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG          
SEQRES  22 D  274  TRP                                                          
SEQRES   1 E  100  MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG          
SEQRES   2 E  100  HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS          
SEQRES   3 E  100  TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP          
SEQRES   4 E  100  LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS          
SEQRES   5 E  100  SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU          
SEQRES   6 E  100  LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU          
SEQRES   7 E  100  TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO          
SEQRES   8 E  100  LYS ILE VAL LYS TRP ASP ARG ASP MET                          
SEQRES   1 F   10  GLY THR SER GLY SER PRO ILE ILE ASN ARG                      
SEQRES   1 G  274  GLY SER HIS SER MET ARG TYR PHE TYR THR SER VAL SER          
SEQRES   2 G  274  ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY          
SEQRES   3 G  274  TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP          
SEQRES   4 G  274  ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE          
SEQRES   5 G  274  GLU GLN GLU GLY PRO GLU TYR TRP ASP GLN GLU THR ARG          
SEQRES   6 G  274  ASN VAL LYS ALA GLN SER GLN THR ASP ARG VAL ASP LEU          
SEQRES   7 G  274  GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ASP GLY          
SEQRES   8 G  274  SER HIS THR ILE GLN ILE MET TYR GLY CYS ASP VAL GLY          
SEQRES   9 G  274  PRO ASP GLY ARG PHE LEU ARG GLY TYR ARG GLN ASP ALA          
SEQRES  10 G  274  TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP LEU          
SEQRES  11 G  274  ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR          
SEQRES  12 G  274  LYS ARG LYS TRP GLU ALA ALA HIS ALA ALA GLU GLN GLN          
SEQRES  13 G  274  ARG ALA TYR LEU GLU GLY ARG CYS VAL GLU TRP LEU ARG          
SEQRES  14 G  274  ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR          
SEQRES  15 G  274  ASP PRO PRO LYS THR HIS MET THR HIS HIS PRO ILE SER          
SEQRES  16 G  274  ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY PHE          
SEQRES  17 G  274  TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY          
SEQRES  18 G  274  GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG          
SEQRES  19 G  274  PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL          
SEQRES  20 G  274  VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS          
SEQRES  21 G  274  VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG          
SEQRES  22 G  274  TRP                                                          
SEQRES   1 H  100  MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG          
SEQRES   2 H  100  HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS          
SEQRES   3 H  100  TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP          
SEQRES   4 H  100  LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS          
SEQRES   5 H  100  SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU          
SEQRES   6 H  100  LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU          
SEQRES   7 H  100  TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO          
SEQRES   8 H  100  LYS ILE VAL LYS TRP ASP ARG ASP MET                          
SEQRES   1 I   10  GLY THR SER GLY SER PRO ILE ILE ASN ARG                      
HET      K  B 101       1                                                       
HETNAM       K POTASSIUM ION                                                    
FORMUL  10    K    K 1+                                                         
FORMUL  11  HOH   *339(H2 O)                                                    
HELIX    1 AA1 ALA A   49  GLU A   53  5                                   5    
HELIX    2 AA2 GLY A   56  TYR A   85  1                                  30    
HELIX    3 AA3 ASP A  137  ALA A  150  1                                  14    
HELIX    4 AA4 HIS A  151  GLY A  162  1                                  12    
HELIX    5 AA5 GLY A  162  GLY A  175  1                                  14    
HELIX    6 AA6 GLY A  175  GLN A  180  1                                   6    
HELIX    7 AA7 GLU A  253  GLN A  255  5                                   3    
HELIX    8 AA8 GLY D   56  ASN D   86  1                                  31    
HELIX    9 AA9 ASP D  137  ALA D  150  1                                  14    
HELIX   10 AB1 HIS D  151  GLY D  162  1                                  12    
HELIX   11 AB2 GLY D  162  GLY D  175  1                                  14    
HELIX   12 AB3 GLY D  175  GLN D  180  1                                   6    
HELIX   13 AB4 GLU D  253  GLN D  255  5                                   3    
HELIX   14 AB5 ALA G   49  GLU G   53  5                                   5    
HELIX   15 AB6 GLY G   56  TYR G   85  1                                  30    
HELIX   16 AB7 ASP G  137  ALA G  150  1                                  14    
HELIX   17 AB8 HIS G  151  GLY G  162  1                                  12    
HELIX   18 AB9 GLY G  162  GLY G  175  1                                  14    
HELIX   19 AC1 GLY G  175  GLN G  180  1                                   6    
HELIX   20 AC2 GLU G  253  GLN G  255  5                                   3    
SHEET    1 AA1 8 GLU A  46  PRO A  47  0                                        
SHEET    2 AA1 8 THR A  31  ASP A  37 -1  N  ARG A  35   O  GLU A  46           
SHEET    3 AA1 8 ARG A  21  VAL A  28 -1  N  GLY A  26   O  PHE A  33           
SHEET    4 AA1 8 HIS A   3  VAL A  12 -1  N  ARG A   6   O  TYR A  27           
SHEET    5 AA1 8 THR A  94  VAL A 103 -1  O  VAL A 103   N  HIS A   3           
SHEET    6 AA1 8 PHE A 109  TYR A 118 -1  O  TYR A 113   N  GLY A 100           
SHEET    7 AA1 8 LYS A 121  LEU A 126 -1  O  LEU A 126   N  ARG A 114           
SHEET    8 AA1 8 TRP A 133  ALA A 135 -1  O  THR A 134   N  ALA A 125           
SHEET    1 AA2 4 LYS A 186  PRO A 193  0                                        
SHEET    2 AA2 4 GLU A 198  PHE A 208 -1  O  LEU A 206   N  LYS A 186           
SHEET    3 AA2 4 PHE A 241  PRO A 250 -1  O  VAL A 249   N  ALA A 199           
SHEET    4 AA2 4 THR A 228  LEU A 230 -1  N  GLU A 229   O  ALA A 246           
SHEET    1 AA3 4 LYS A 186  PRO A 193  0                                        
SHEET    2 AA3 4 GLU A 198  PHE A 208 -1  O  LEU A 206   N  LYS A 186           
SHEET    3 AA3 4 PHE A 241  PRO A 250 -1  O  VAL A 249   N  ALA A 199           
SHEET    4 AA3 4 ARG A 234  PRO A 235 -1  N  ARG A 234   O  GLN A 242           
SHEET    1 AA4 4 GLU A 222  GLN A 224  0                                        
SHEET    2 AA4 4 ILE A 213  ARG A 219 -1  N  ARG A 219   O  GLU A 222           
SHEET    3 AA4 4 TYR A 257  HIS A 263 -1  O  HIS A 260   N  THR A 216           
SHEET    4 AA4 4 LEU A 270  ARG A 273 -1  O  LEU A 272   N  CYS A 259           
SHEET    1 AA5 4 VAL B   9  SER B  11  0                                        
SHEET    2 AA5 4 ASN B  21  PHE B  30 -1  O  ASN B  24   N  TYR B  10           
SHEET    3 AA5 4 PHE B  62  PHE B  70 -1  O  PHE B  70   N  ASN B  21           
SHEET    4 AA5 4 GLU B  50  HIS B  51 -1  N  GLU B  50   O  TYR B  67           
SHEET    1 AA6 4 VAL B   9  SER B  11  0                                        
SHEET    2 AA6 4 ASN B  21  PHE B  30 -1  O  ASN B  24   N  TYR B  10           
SHEET    3 AA6 4 PHE B  62  PHE B  70 -1  O  PHE B  70   N  ASN B  21           
SHEET    4 AA6 4 SER B  55  PHE B  56 -1  N  SER B  55   O  TYR B  63           
SHEET    1 AA7 4 GLU B  44  ARG B  45  0                                        
SHEET    2 AA7 4 GLU B  36  LYS B  41 -1  N  LYS B  41   O  GLU B  44           
SHEET    3 AA7 4 TYR B  78  ASN B  83 -1  O  ARG B  81   N  ASP B  38           
SHEET    4 AA7 4 LYS B  91  LYS B  94 -1  O  LYS B  91   N  VAL B  82           
SHEET    1 AA8 8 GLU D  46  PRO D  47  0                                        
SHEET    2 AA8 8 THR D  31  ASP D  37 -1  N  ARG D  35   O  GLU D  46           
SHEET    3 AA8 8 ARG D  21  VAL D  28 -1  N  VAL D  28   O  THR D  31           
SHEET    4 AA8 8 HIS D   3  VAL D  12 -1  N  ARG D   6   O  TYR D  27           
SHEET    5 AA8 8 THR D  94  VAL D 103 -1  O  VAL D 103   N  HIS D   3           
SHEET    6 AA8 8 PHE D 109  TYR D 118 -1  O  TYR D 113   N  GLY D 100           
SHEET    7 AA8 8 LYS D 121  LEU D 126 -1  O  LEU D 126   N  ARG D 114           
SHEET    8 AA8 8 TRP D 133  ALA D 135 -1  O  THR D 134   N  ALA D 125           
SHEET    1 AA9 4 LYS D 186  PRO D 193  0                                        
SHEET    2 AA9 4 GLU D 198  PHE D 208 -1  O  LEU D 206   N  LYS D 186           
SHEET    3 AA9 4 PHE D 241  PRO D 250 -1  O  VAL D 249   N  ALA D 199           
SHEET    4 AA9 4 THR D 228  LEU D 230 -1  N  GLU D 229   O  ALA D 246           
SHEET    1 AB1 4 LYS D 186  PRO D 193  0                                        
SHEET    2 AB1 4 GLU D 198  PHE D 208 -1  O  LEU D 206   N  LYS D 186           
SHEET    3 AB1 4 PHE D 241  PRO D 250 -1  O  VAL D 249   N  ALA D 199           
SHEET    4 AB1 4 ARG D 234  PRO D 235 -1  N  ARG D 234   O  GLN D 242           
SHEET    1 AB2 4 GLU D 222  GLN D 224  0                                        
SHEET    2 AB2 4 ILE D 213  ARG D 219 -1  N  TRP D 217   O  GLN D 224           
SHEET    3 AB2 4 TYR D 257  HIS D 263 -1  O  HIS D 260   N  THR D 216           
SHEET    4 AB2 4 LEU D 270  ARG D 273 -1  O  LEU D 272   N  CYS D 259           
SHEET    1 AB3 4 VAL E   9  SER E  11  0                                        
SHEET    2 AB3 4 ASN E  21  PHE E  30 -1  O  ASN E  24   N  TYR E  10           
SHEET    3 AB3 4 PHE E  62  PHE E  70 -1  O  PHE E  70   N  ASN E  21           
SHEET    4 AB3 4 GLU E  50  HIS E  51 -1  N  GLU E  50   O  TYR E  67           
SHEET    1 AB4 4 VAL E   9  SER E  11  0                                        
SHEET    2 AB4 4 ASN E  21  PHE E  30 -1  O  ASN E  24   N  TYR E  10           
SHEET    3 AB4 4 PHE E  62  PHE E  70 -1  O  PHE E  70   N  ASN E  21           
SHEET    4 AB4 4 SER E  55  PHE E  56 -1  N  SER E  55   O  TYR E  63           
SHEET    1 AB5 4 GLU E  44  ARG E  45  0                                        
SHEET    2 AB5 4 GLU E  36  LYS E  41 -1  N  LYS E  41   O  GLU E  44           
SHEET    3 AB5 4 TYR E  78  ASN E  83 -1  O  ARG E  81   N  ASP E  38           
SHEET    4 AB5 4 LYS E  91  LYS E  94 -1  O  LYS E  91   N  VAL E  82           
SHEET    1 AB6 8 GLU G  46  PRO G  47  0                                        
SHEET    2 AB6 8 THR G  31  ASP G  37 -1  N  ARG G  35   O  GLU G  46           
SHEET    3 AB6 8 ARG G  21  VAL G  28 -1  N  VAL G  28   O  THR G  31           
SHEET    4 AB6 8 HIS G   3  VAL G  12 -1  N  ARG G   6   O  TYR G  27           
SHEET    5 AB6 8 THR G  94  VAL G 103 -1  O  VAL G 103   N  HIS G   3           
SHEET    6 AB6 8 PHE G 109  TYR G 118 -1  O  ARG G 111   N  ASP G 102           
SHEET    7 AB6 8 LYS G 121  LEU G 126 -1  O  LEU G 126   N  ARG G 114           
SHEET    8 AB6 8 TRP G 133  ALA G 135 -1  O  THR G 134   N  ALA G 125           
SHEET    1 AB7 4 LYS G 186  PRO G 193  0                                        
SHEET    2 AB7 4 GLU G 198  PHE G 208 -1  O  LEU G 206   N  LYS G 186           
SHEET    3 AB7 4 PHE G 241  PRO G 250 -1  O  VAL G 249   N  ALA G 199           
SHEET    4 AB7 4 THR G 228  LEU G 230 -1  N  GLU G 229   O  ALA G 246           
SHEET    1 AB8 4 LYS G 186  PRO G 193  0                                        
SHEET    2 AB8 4 GLU G 198  PHE G 208 -1  O  LEU G 206   N  LYS G 186           
SHEET    3 AB8 4 PHE G 241  PRO G 250 -1  O  VAL G 249   N  ALA G 199           
SHEET    4 AB8 4 ARG G 234  PRO G 235 -1  N  ARG G 234   O  GLN G 242           
SHEET    1 AB9 4 GLU G 222  GLN G 224  0                                        
SHEET    2 AB9 4 ILE G 213  ARG G 219 -1  N  ARG G 219   O  GLU G 222           
SHEET    3 AB9 4 TYR G 257  HIS G 263 -1  O  HIS G 260   N  THR G 216           
SHEET    4 AB9 4 LEU G 270  ARG G 273 -1  O  LEU G 272   N  CYS G 259           
SHEET    1 AC1 4 VAL H   9  SER H  11  0                                        
SHEET    2 AC1 4 ASN H  21  PHE H  30 -1  O  ASN H  24   N  TYR H  10           
SHEET    3 AC1 4 PHE H  62  PHE H  70 -1  O  TYR H  66   N  CYS H  25           
SHEET    4 AC1 4 GLU H  50  HIS H  51 -1  N  GLU H  50   O  TYR H  67           
SHEET    1 AC2 4 VAL H   9  SER H  11  0                                        
SHEET    2 AC2 4 ASN H  21  PHE H  30 -1  O  ASN H  24   N  TYR H  10           
SHEET    3 AC2 4 PHE H  62  PHE H  70 -1  O  TYR H  66   N  CYS H  25           
SHEET    4 AC2 4 SER H  55  PHE H  56 -1  N  SER H  55   O  TYR H  63           
SHEET    1 AC3 4 GLU H  44  ARG H  45  0                                        
SHEET    2 AC3 4 GLU H  36  LYS H  41 -1  N  LYS H  41   O  GLU H  44           
SHEET    3 AC3 4 TYR H  78  ASN H  83 -1  O  ARG H  81   N  ASP H  38           
SHEET    4 AC3 4 LYS H  91  LYS H  94 -1  O  LYS H  91   N  VAL H  82           
SSBOND   1 CYS A  101    CYS A  164                          1555   1555  2.81  
SSBOND   2 CYS A  203    CYS A  259                          1555   1555  2.99  
SSBOND   3 CYS B   25    CYS B   80                          1555   1555  2.68  
SSBOND   4 CYS D  101    CYS D  164                          1555   1555  2.75  
SSBOND   5 CYS E   25    CYS E   80                          1555   1555  2.70  
SSBOND   6 CYS G  101    CYS G  164                          1555   1555  2.80  
SSBOND   7 CYS H   25    CYS H   80                          1555   1555  2.72  
LINK         OD1 ASN B  83                 K     K B 101     1555   1555  2.72  
LINK         O   HIS B  84                 K     K B 101     1555   1555  2.88  
LINK         O   LEU B  87                 K     K B 101     1555   1555  2.32  
CISPEP   1 TYR A  209    PRO A  210          0        -0.12                     
CISPEP   2 HIS B   31    PRO B   32          0         2.03                     
CISPEP   3 SER C    5    PRO C    6          0        10.30                     
CISPEP   4 TYR D  209    PRO D  210          0         0.00                     
CISPEP   5 HIS E   31    PRO E   32          0         3.45                     
CISPEP   6 SER F    5    PRO F    6          0        10.71                     
CISPEP   7 TYR G  209    PRO G  210          0        -0.10                     
CISPEP   8 HIS H   31    PRO H   32          0         2.92                     
CISPEP   9 SER I    5    PRO I    6          0         9.96                     
SITE     1 AC1  3 ASN B  83  HIS B  84  LEU B  87                               
CRYST1  158.325  145.522  106.303  90.00 121.14  90.00 C 1 2 1      12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006316  0.000000  0.003816        0.00000                         
SCALE2      0.000000  0.006872  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010991        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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