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Database: PDB
Entry: 3V56
LinkDB: 3V56
Original site: 3V56 
HEADER    IMMUNE SYSTEM                           16-DEC-11   3V56              
TITLE     RE-REFINEMENT OF PDB ENTRY 1OSG - COMPLEX BETWEEN BAFF AND A BR3      
TITLE    2 DERIVED PEPTIDE PRESENTED IN A BETA-HAIRPIN SCAFFOLD - REVEALS AN    
TITLE    3 ADDITONAL COPY OF THE PEPTIDE.                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 13B;       
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: B LYMPHOCYTE STIMULATOR, BLYS, B-CELL-ACTIVATING FACTOR,    
COMPND   5 BAFF, DENDRITIC CELL-DERIVED TNF-LIKE MOLECULE, TNF- AND APOL-RELATED
COMPND   6 LEUKOCYTE EXPRESSED LIGAND 1, TALL-1, TUMOR NECROSIS FACTOR LIGAND   
COMPND   7 SUPERFAMILY MEMBER 13B, MEMBRANE FORM, TUMOR NECROSIS FACTOR LIGAND  
COMPND   8 SUPERFAMILY MEMBER 13B, SOLUBLE FORM;                                
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: BR3 DERIVED PEPTIVE;                                       
COMPND  12 CHAIN: G, H, I, J, K, L, Z;                                          
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: TNFSF13B, BAFF, BLYS, TALL1, TNFSF20, ZTNF4, UNQ401/PRO738;    
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: PET15B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES                                                       
KEYWDS    JELLY-ROLL, BETA HAIRPIN, PROTEIN-PEPTIDE COMPLEX, IMMUNE SYSTEM      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.S.SMART,T.O.WOMACK,C.FLENSBURG,P.KELLER,A.SHARFF,W.PACIOREK,        
AUTHOR   2 C.VONRHEIN,G.BRICOGNE                                                
REVDAT   3   24-JAN-18 3V56    1       JRNL                                     
REVDAT   2   20-FEB-13 3V56    1       JRNL                                     
REVDAT   1   28-MAR-12 3V56    0                                                
JRNL        AUTH   O.S.SMART,T.O.WOMACK,C.FLENSBURG,P.KELLER,W.PACIOREK,        
JRNL        AUTH 2 A.SHARFF,C.VONRHEIN,G.BRICOGNE                               
JRNL        TITL   EXPLOITING STRUCTURE SIMILARITY IN REFINEMENT: AUTOMATED NCS 
JRNL        TITL 2 AND TARGET-STRUCTURE RESTRAINTS IN BUSTER.                   
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  68   368 2012              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   22505257                                                     
JRNL        DOI    10.1107/S0907444911056058                                    
REMARK   0                                                                      
REMARK   0 THIS ENTRY 3V56 REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL     
REMARK   0 STRUCTURAL DATA OF R1OSGTSF DETERMINED BY THE AUTHORS OF THE PDB     
REMARK   0 ENTRY 1OSG: N.C.GORDON,B.PAN,S.G.HYMOWITZ,J.P.YIN,R.F.KELLEY,        
REMARK   0 A.G.COCHRAN,M.YAN,V.M.DIXIT,W.J.FAIRBROTHER,M.A.STAROVASNIK          
REMARK   0 ORIGINAL DATA REFERENCE 1                                            
REMARK   0  PDB ID: 1OSG                                                        
REMARK   0  AUTH   N.C.GORDON,B.PAN,S.G.HYMOWITZ,J.P.YIN,R.F KELLEY,            
REMARK   0  AUTH 2 A.G.COCHRAN,M.YAN,V.M.DIXIT,W.J.FAIRBROTHER,M.A.STAROVASNIK  
REMARK   0  TITL   BAFF/BLYS RECEPTOR 3 COMPRISES A MINIMAL TNF RECEPTOR-LIKE   
REMARK   0  TITL 2 MODULE THAT ENCODES A HIGHLY FOCUSED LIGAND-BINDING SITE     
REMARK   0  REF    BIOCHEMISTRY                  V.  42  5977 2003              
REMARK   0  REFN                   ISSN 0006-2960                               
REMARK   0  PMID   12755599                                                     
REMARK   0  DOI    10.1021/BI034017G                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.13.0                                        
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.85                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 26306                          
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)  : 0.165                          
REMARK   3   R VALUE            (WORKING SET)  : 0.162                          
REMARK   3   FREE R VALUE                      : 0.200                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 9.640                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2536                           
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               : 13                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.00                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.12                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.67                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2973                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2165                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2665                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2090                   
REMARK   3   BIN FREE R VALUE                        : 0.2849                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 10.36                    
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 308                      
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            : 7406                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 18                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.47800                                              
REMARK   3    B22 (A**2) : 1.47800                                              
REMARK   3    B33 (A**2) : -2.95610                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.339               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 7595   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 10339  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2520   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 189    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1088   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 7595   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1002   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : 12     ; 1.000  ; HARMONIC            
REMARK   3    UTILITY ANGLES            : 12     ; 1.000  ; HARMONIC            
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 8381   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.20                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.15                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.75                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 13                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   76.9820   19.4174   -5.3574           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0887 T22:   -0.1417                                    
REMARK   3     T33:   -0.1272 T12:   -0.0088                                    
REMARK   3     T13:   -0.0711 T23:    0.0309                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1063 L22:    2.3334                                    
REMARK   3     L33:    2.2385 L12:   -0.9582                                    
REMARK   3     L13:    0.2243 L23:   -0.3460                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2172 S12:   -0.0567 S13:    0.1162                     
REMARK   3     S21:    0.5091 S22:    0.1543 S23:   -0.1268                     
REMARK   3     S31:   -0.2989 S32:    0.0328 S33:    0.0629                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   77.2238    5.4476  -23.8906           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0014 T22:   -0.0482                                    
REMARK   3     T33:   -0.1147 T12:   -0.0521                                    
REMARK   3     T13:    0.0032 T23:   -0.0161                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.5818 L22:    2.1475                                    
REMARK   3     L33:    2.1172 L12:    0.1793                                    
REMARK   3     L13:    0.4859 L23:    0.0260                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0773 S12:    0.3129 S13:    0.0002                     
REMARK   3     S21:   -0.1598 S22:    0.0009 S23:   -0.1003                     
REMARK   3     S31:    0.3098 S32:    0.1138 S33:    0.0764                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   70.7837   27.5423  -26.3224           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0197 T22:   -0.0575                                    
REMARK   3     T33:   -0.1323 T12:   -0.0166                                    
REMARK   3     T13:   -0.0774 T23:    0.1261                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6996 L22:    2.1902                                    
REMARK   3     L33:    2.1678 L12:    0.1457                                    
REMARK   3     L13:    0.2455 L23:    0.8493                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0871 S12:    0.3696 S13:    0.1928                     
REMARK   3     S21:   -0.2631 S22:   -0.0923 S23:    0.0956                     
REMARK   3     S31:   -0.3806 S32:   -0.1461 S33:    0.1795                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   77.3637   -2.3576   23.6635           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1557 T22:   -0.2188                                    
REMARK   3     T33:   -0.1783 T12:   -0.0089                                    
REMARK   3     T13:    0.0533 T23:   -0.0150                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.7909 L22:    3.0579                                    
REMARK   3     L33:    2.4235 L12:   -0.3906                                    
REMARK   3     L13:   -0.3316 L23:   -0.2387                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2030 S12:   -0.3457 S13:    0.1567                     
REMARK   3     S21:    0.6533 S22:   -0.0943 S23:   -0.0814                     
REMARK   3     S31:   -0.4737 S32:   -0.1903 S33:   -0.1087                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { E|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   71.6579  -24.5783   26.5059           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1125 T22:   -0.1176                                    
REMARK   3     T33:   -0.1325 T12:   -0.0935                                    
REMARK   3     T13:    0.0160 T23:    0.1039                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.6100 L22:    2.4053                                    
REMARK   3     L33:    2.0295 L12:    0.1726                                    
REMARK   3     L13:    0.1505 L23:    0.4201                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2454 S12:   -0.1444 S13:   -0.1881                     
REMARK   3     S21:    0.7780 S22:   -0.2141 S23:   -0.0115                     
REMARK   3     S31:    0.2782 S32:   -0.2442 S33:   -0.0312                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { F|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   77.5137  -16.2961    5.3864           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0145 T22:   -0.1285                                    
REMARK   3     T33:   -0.0930 T12:    0.0338                                    
REMARK   3     T13:    0.0468 T23:    0.0309                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1775 L22:    3.4437                                    
REMARK   3     L33:    2.3117 L12:    0.3735                                    
REMARK   3     L13:    0.3637 L23:   -0.7815                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0060 S12:    0.0513 S13:   -0.1591                     
REMARK   3     S21:   -0.0973 S22:    0.1034 S23:   -0.0837                     
REMARK   3     S31:    0.0542 S32:   -0.0743 S33:   -0.1094                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { G|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   97.2025   12.2883   -5.2573           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1296 T22:   -0.0696                                    
REMARK   3     T33:    0.1741 T12:    0.1023                                    
REMARK   3     T13:   -0.2133 T23:    0.0700                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.5217 L22:    0.5488                                    
REMARK   3     L33:    6.8377 L12:   -4.9404                                    
REMARK   3     L13:    6.5352 L23:   -2.0101                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0232 S12:   -0.1892 S13:   -0.3221                     
REMARK   3     S21:   -0.1856 S22:   -0.0543 S23:   -1.0284                     
REMARK   3     S31:    0.0771 S32:    0.7528 S33:    0.0311                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: { H|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   90.7706   12.7890  -38.9737           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0323 T22:    0.3499                                    
REMARK   3     T33:   -0.3886 T12:   -0.2433                                    
REMARK   3     T13:    0.1186 T23:    0.0424                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   -2.2361 L22:    6.1831                                    
REMARK   3     L33:    6.2246 L12:    0.1516                                    
REMARK   3     L13:   -2.2220 L23:   -1.8680                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0540 S12:    0.5115 S13:    0.0132                     
REMARK   3     S21:   -0.6878 S22:   -0.0830 S23:   -0.7584                     
REMARK   3     S31:   -0.4261 S32:    0.2584 S33:    0.0290                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: { I|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   86.5999   40.6107  -20.1043           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1173 T22:   -0.2826                                    
REMARK   3     T33:    0.1557 T12:   -0.1509                                    
REMARK   3     T13:   -0.3866 T23:    0.1278                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   -0.0076 L22:    9.4295                                    
REMARK   3     L33:    1.5175 L12:   -2.4693                                    
REMARK   3     L13:    5.3987 L23:    1.0947                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0706 S12:   -0.4391 S13:    0.7191                     
REMARK   3     S21:    0.4861 S22:    0.1169 S23:   -0.5362                     
REMARK   3     S31:   -0.4844 S32:    0.4024 S33:   -0.0462                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: { J|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   91.0778   -9.0637   39.0814           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.5716 T22:    0.0068                                    
REMARK   3     T33:   -0.4420 T12:   -0.0403                                    
REMARK   3     T13:   -0.3467 T23:    0.0565                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   -1.1676 L22:    3.0556                                    
REMARK   3     L33:    5.7299 L12:    0.1291                                    
REMARK   3     L13:    4.5841 L23:   -3.7666                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0912 S12:   -0.5657 S13:   -0.2699                     
REMARK   3     S21:    0.4576 S22:    0.0354 S23:   -0.7171                     
REMARK   3     S31:    0.1645 S32:    0.5081 S33:    0.0558                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: { K|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   87.9735  -37.1544   20.2413           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.3841 T22:   -0.2710                                    
REMARK   3     T33:   -0.1101 T12:    0.0431                                    
REMARK   3     T13:   -0.1439 T23:    0.0611                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   -0.6863 L22:   11.7027                                    
REMARK   3     L33:    0.0521 L12:   -0.7420                                    
REMARK   3     L13:   -5.2731 L23:    1.1422                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1826 S12:    0.5319 S13:   -0.2898                     
REMARK   3     S21:   -0.2749 S22:    0.1174 S23:   -0.2836                     
REMARK   3     S31:    0.5371 S32:    0.6177 S33:    0.0652                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: { L|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   97.2764   -8.3136    5.5517           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0611 T22:   -0.1864                                    
REMARK   3     T33:    0.2240 T12:   -0.1473                                    
REMARK   3     T13:    0.2538 T23:    0.0067                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.5466 L22:    6.9937                                    
REMARK   3     L33:   10.3443 L12:    6.5025                                    
REMARK   3     L13:   -0.7518 L23:   -4.6627                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0720 S12:    0.1451 S13:    0.2202                     
REMARK   3     S21:   -0.0774 S22:    0.2150 S23:   -0.7546                     
REMARK   3     S31:   -0.3948 S32:    0.7325 S33:   -0.1429                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: { Z|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   84.5100  -45.6626   25.5181           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1631 T22:   -0.3337                                    
REMARK   3     T33:    0.1753 T12:   -0.0219                                    
REMARK   3     T13:   -0.0401 T23:    0.3229                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.4355 L22:    7.3952                                    
REMARK   3     L33:    1.1489 L12:   -2.1667                                    
REMARK   3     L13:   -1.7271 L23:   -4.9478                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1034 S12:   -0.0363 S13:    0.0345                     
REMARK   3     S21:    0.0819 S22:   -0.2654 S23:    0.2091                     
REMARK   3     S31:    0.0941 S32:   -0.0704 S33:    0.1621                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 1. X-RAY WEIGHT: 14.83. 2. VOID           
REMARK   3  CORRECTION : ON. 3. SIMILARITY, NCS REPRESENTATION : RESTRAINT      
REMARK   3  LSSR, TARGET RESTRAINTS: NONE, TARGET STRUCTURE : NULL. 4.          
REMARK   3  MOLECULES SO4 A 499, SO4 D 499, HOH A 500, HOH D 500 ARE MODELED    
REMARK   3  INTO DENSITY ON NCS 3 FOLD AXES WHERE MAP INTERPRETATION IS         
REMARK   3  DIFFICULT, AND SO SHOULD BE TREATED WITH CAUTION. 5. DUE TO         
REMARK   3  RADIATION DAMAGE OR ONLY PARTIAL OXIDATION RESIDUES CYS 232 AND     
REMARK   3  CYS 245 IN THE A, B, C, D, E AND F CHAINS FORM ONLY A PARTIAL       
REMARK   3  DISULFIDE BOND. THE DISULFIDE BOND IS MODELED AS THE A ALTERNATE    
REMARK   3  WHEREAS THE B ALTERNATE REPRESENTS THE REDUCED CYS RESIDUES.        
REMARK   4                                                                      
REMARK   4 3V56 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000069608.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: RE-REFINEMENT                
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1OSG WITH WATER MOLECULES AND IONS REMOVED.          
REMARK 200                                                                      
REMARK 200 REMARK: AUTHOR USED THE SF DATA FROM THE ENTRY 1OSG.                 
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      104.80933            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       52.40467            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       78.60700            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       26.20233            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      131.01167            
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 300 REMARK: THE BIOLOGICALLY RELEVANT ASSEMBLY OF BAFF IS A TRIMER. THE  
REMARK 300 CRYSTALLOGRAPHIC ASYMMETRIC UNIT CONTAINS TWO TRIMERS. EACH          
REMARK 300 INDIVIDUAL BAFF TRIMER BINDS 3 COPIES OF BR3 PEPTIDE. AN ADDITIONAL  
REMARK 300 COPY OF THE BR3 PEPTIDE WAS LOCATED IN THIS RE-REFINEMENT AT A       
REMARK 300 CRYSTAL CONTACT (MODELED AS THE Z CHAIN). THE ADDITIONAL BR3         
REMARK 300 PEPTIDE IS NOT BIOLOGICALLY RELEVANT.                                
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8880 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, J, K, L                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Z                                     
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     GLY A    78                                                      
REMARK 465     SER A    79                                                      
REMARK 465     HIS A    80                                                      
REMARK 465     MET A    81                                                      
REMARK 465     GLU A    82                                                      
REMARK 465     LEU A    83                                                      
REMARK 465     GLN A    84                                                      
REMARK 465     GLY A    85                                                      
REMARK 465     HIS A    86                                                      
REMARK 465     HIS A    87                                                      
REMARK 465     ALA A    88                                                      
REMARK 465     GLU A    89                                                      
REMARK 465     LYS A    90                                                      
REMARK 465     LEU A    91                                                      
REMARK 465     PRO A    92                                                      
REMARK 465     ALA A    93                                                      
REMARK 465     GLY A    94                                                      
REMARK 465     ALA A    95                                                      
REMARK 465     GLY A    96                                                      
REMARK 465     ALA A    97                                                      
REMARK 465     PRO A    98                                                      
REMARK 465     LYS A    99                                                      
REMARK 465     ALA A   100                                                      
REMARK 465     GLY A   101                                                      
REMARK 465     LEU A   102                                                      
REMARK 465     GLU A   103                                                      
REMARK 465     GLU A   104                                                      
REMARK 465     ALA A   105                                                      
REMARK 465     PRO A   106                                                      
REMARK 465     ALA A   107                                                      
REMARK 465     VAL A   108                                                      
REMARK 465     THR A   109                                                      
REMARK 465     ALA A   110                                                      
REMARK 465     GLY A   111                                                      
REMARK 465     LEU A   112                                                      
REMARK 465     LYS A   113                                                      
REMARK 465     ILE A   114                                                      
REMARK 465     PHE A   115                                                      
REMARK 465     GLU A   116                                                      
REMARK 465     PRO A   117                                                      
REMARK 465     PRO A   118                                                      
REMARK 465     ALA A   119                                                      
REMARK 465     PRO A   120                                                      
REMARK 465     GLY A   121                                                      
REMARK 465     GLU A   122                                                      
REMARK 465     GLY A   123                                                      
REMARK 465     ASN A   124                                                      
REMARK 465     SER A   125                                                      
REMARK 465     SER A   126                                                      
REMARK 465     GLN A   127                                                      
REMARK 465     ASN A   128                                                      
REMARK 465     SER A   129                                                      
REMARK 465     ARG A   130                                                      
REMARK 465     ASN A   131                                                      
REMARK 465     LYS A   132                                                      
REMARK 465     ARG A   133                                                      
REMARK 465     ALA A   134                                                      
REMARK 465     VAL A   135                                                      
REMARK 465     GLN A   136                                                      
REMARK 465     GLY A   137                                                      
REMARK 465     PRO A   138                                                      
REMARK 465     GLU A   139                                                      
REMARK 465     GLU A   140                                                      
REMARK 465     THR A   141                                                      
REMARK 465     GLY B    78                                                      
REMARK 465     SER B    79                                                      
REMARK 465     HIS B    80                                                      
REMARK 465     MET B    81                                                      
REMARK 465     GLU B    82                                                      
REMARK 465     LEU B    83                                                      
REMARK 465     GLN B    84                                                      
REMARK 465     GLY B    85                                                      
REMARK 465     HIS B    86                                                      
REMARK 465     HIS B    87                                                      
REMARK 465     ALA B    88                                                      
REMARK 465     GLU B    89                                                      
REMARK 465     LYS B    90                                                      
REMARK 465     LEU B    91                                                      
REMARK 465     PRO B    92                                                      
REMARK 465     ALA B    93                                                      
REMARK 465     GLY B    94                                                      
REMARK 465     ALA B    95                                                      
REMARK 465     GLY B    96                                                      
REMARK 465     ALA B    97                                                      
REMARK 465     PRO B    98                                                      
REMARK 465     LYS B    99                                                      
REMARK 465     ALA B   100                                                      
REMARK 465     GLY B   101                                                      
REMARK 465     LEU B   102                                                      
REMARK 465     GLU B   103                                                      
REMARK 465     GLU B   104                                                      
REMARK 465     ALA B   105                                                      
REMARK 465     PRO B   106                                                      
REMARK 465     ALA B   107                                                      
REMARK 465     VAL B   108                                                      
REMARK 465     THR B   109                                                      
REMARK 465     ALA B   110                                                      
REMARK 465     GLY B   111                                                      
REMARK 465     LEU B   112                                                      
REMARK 465     LYS B   113                                                      
REMARK 465     ILE B   114                                                      
REMARK 465     PHE B   115                                                      
REMARK 465     GLU B   116                                                      
REMARK 465     PRO B   117                                                      
REMARK 465     PRO B   118                                                      
REMARK 465     ALA B   119                                                      
REMARK 465     PRO B   120                                                      
REMARK 465     GLY B   121                                                      
REMARK 465     GLU B   122                                                      
REMARK 465     GLY B   123                                                      
REMARK 465     ASN B   124                                                      
REMARK 465     SER B   125                                                      
REMARK 465     SER B   126                                                      
REMARK 465     GLN B   127                                                      
REMARK 465     ASN B   128                                                      
REMARK 465     SER B   129                                                      
REMARK 465     ARG B   130                                                      
REMARK 465     ASN B   131                                                      
REMARK 465     LYS B   132                                                      
REMARK 465     ARG B   133                                                      
REMARK 465     ALA B   134                                                      
REMARK 465     VAL B   135                                                      
REMARK 465     GLN B   136                                                      
REMARK 465     GLY B   137                                                      
REMARK 465     PRO B   138                                                      
REMARK 465     GLU B   139                                                      
REMARK 465     GLU B   140                                                      
REMARK 465     THR B   141                                                      
REMARK 465     GLY C    78                                                      
REMARK 465     SER C    79                                                      
REMARK 465     HIS C    80                                                      
REMARK 465     MET C    81                                                      
REMARK 465     GLU C    82                                                      
REMARK 465     LEU C    83                                                      
REMARK 465     GLN C    84                                                      
REMARK 465     GLY C    85                                                      
REMARK 465     HIS C    86                                                      
REMARK 465     HIS C    87                                                      
REMARK 465     ALA C    88                                                      
REMARK 465     GLU C    89                                                      
REMARK 465     LYS C    90                                                      
REMARK 465     LEU C    91                                                      
REMARK 465     PRO C    92                                                      
REMARK 465     ALA C    93                                                      
REMARK 465     GLY C    94                                                      
REMARK 465     ALA C    95                                                      
REMARK 465     GLY C    96                                                      
REMARK 465     ALA C    97                                                      
REMARK 465     PRO C    98                                                      
REMARK 465     LYS C    99                                                      
REMARK 465     ALA C   100                                                      
REMARK 465     GLY C   101                                                      
REMARK 465     LEU C   102                                                      
REMARK 465     GLU C   103                                                      
REMARK 465     GLU C   104                                                      
REMARK 465     ALA C   105                                                      
REMARK 465     PRO C   106                                                      
REMARK 465     ALA C   107                                                      
REMARK 465     VAL C   108                                                      
REMARK 465     THR C   109                                                      
REMARK 465     ALA C   110                                                      
REMARK 465     GLY C   111                                                      
REMARK 465     LEU C   112                                                      
REMARK 465     LYS C   113                                                      
REMARK 465     ILE C   114                                                      
REMARK 465     PHE C   115                                                      
REMARK 465     GLU C   116                                                      
REMARK 465     PRO C   117                                                      
REMARK 465     PRO C   118                                                      
REMARK 465     ALA C   119                                                      
REMARK 465     PRO C   120                                                      
REMARK 465     GLY C   121                                                      
REMARK 465     GLU C   122                                                      
REMARK 465     GLY C   123                                                      
REMARK 465     ASN C   124                                                      
REMARK 465     SER C   125                                                      
REMARK 465     SER C   126                                                      
REMARK 465     GLN C   127                                                      
REMARK 465     ASN C   128                                                      
REMARK 465     SER C   129                                                      
REMARK 465     ARG C   130                                                      
REMARK 465     ASN C   131                                                      
REMARK 465     LYS C   132                                                      
REMARK 465     ARG C   133                                                      
REMARK 465     ALA C   134                                                      
REMARK 465     VAL C   135                                                      
REMARK 465     GLN C   136                                                      
REMARK 465     GLY C   137                                                      
REMARK 465     PRO C   138                                                      
REMARK 465     GLU C   139                                                      
REMARK 465     GLU C   140                                                      
REMARK 465     THR C   141                                                      
REMARK 465     GLY D    78                                                      
REMARK 465     SER D    79                                                      
REMARK 465     HIS D    80                                                      
REMARK 465     MET D    81                                                      
REMARK 465     GLU D    82                                                      
REMARK 465     LEU D    83                                                      
REMARK 465     GLN D    84                                                      
REMARK 465     GLY D    85                                                      
REMARK 465     HIS D    86                                                      
REMARK 465     HIS D    87                                                      
REMARK 465     ALA D    88                                                      
REMARK 465     GLU D    89                                                      
REMARK 465     LYS D    90                                                      
REMARK 465     LEU D    91                                                      
REMARK 465     PRO D    92                                                      
REMARK 465     ALA D    93                                                      
REMARK 465     GLY D    94                                                      
REMARK 465     ALA D    95                                                      
REMARK 465     GLY D    96                                                      
REMARK 465     ALA D    97                                                      
REMARK 465     PRO D    98                                                      
REMARK 465     LYS D    99                                                      
REMARK 465     ALA D   100                                                      
REMARK 465     GLY D   101                                                      
REMARK 465     LEU D   102                                                      
REMARK 465     GLU D   103                                                      
REMARK 465     GLU D   104                                                      
REMARK 465     ALA D   105                                                      
REMARK 465     PRO D   106                                                      
REMARK 465     ALA D   107                                                      
REMARK 465     VAL D   108                                                      
REMARK 465     THR D   109                                                      
REMARK 465     ALA D   110                                                      
REMARK 465     GLY D   111                                                      
REMARK 465     LEU D   112                                                      
REMARK 465     LYS D   113                                                      
REMARK 465     ILE D   114                                                      
REMARK 465     PHE D   115                                                      
REMARK 465     GLU D   116                                                      
REMARK 465     PRO D   117                                                      
REMARK 465     PRO D   118                                                      
REMARK 465     ALA D   119                                                      
REMARK 465     PRO D   120                                                      
REMARK 465     GLY D   121                                                      
REMARK 465     GLU D   122                                                      
REMARK 465     GLY D   123                                                      
REMARK 465     ASN D   124                                                      
REMARK 465     SER D   125                                                      
REMARK 465     SER D   126                                                      
REMARK 465     GLN D   127                                                      
REMARK 465     ASN D   128                                                      
REMARK 465     SER D   129                                                      
REMARK 465     ARG D   130                                                      
REMARK 465     ASN D   131                                                      
REMARK 465     LYS D   132                                                      
REMARK 465     ARG D   133                                                      
REMARK 465     ALA D   134                                                      
REMARK 465     VAL D   135                                                      
REMARK 465     GLN D   136                                                      
REMARK 465     GLY D   137                                                      
REMARK 465     PRO D   138                                                      
REMARK 465     GLU D   139                                                      
REMARK 465     GLU D   140                                                      
REMARK 465     THR D   141                                                      
REMARK 465     GLY E    78                                                      
REMARK 465     SER E    79                                                      
REMARK 465     HIS E    80                                                      
REMARK 465     MET E    81                                                      
REMARK 465     GLU E    82                                                      
REMARK 465     LEU E    83                                                      
REMARK 465     GLN E    84                                                      
REMARK 465     GLY E    85                                                      
REMARK 465     HIS E    86                                                      
REMARK 465     HIS E    87                                                      
REMARK 465     ALA E    88                                                      
REMARK 465     GLU E    89                                                      
REMARK 465     LYS E    90                                                      
REMARK 465     LEU E    91                                                      
REMARK 465     PRO E    92                                                      
REMARK 465     ALA E    93                                                      
REMARK 465     GLY E    94                                                      
REMARK 465     ALA E    95                                                      
REMARK 465     GLY E    96                                                      
REMARK 465     ALA E    97                                                      
REMARK 465     PRO E    98                                                      
REMARK 465     LYS E    99                                                      
REMARK 465     ALA E   100                                                      
REMARK 465     GLY E   101                                                      
REMARK 465     LEU E   102                                                      
REMARK 465     GLU E   103                                                      
REMARK 465     GLU E   104                                                      
REMARK 465     ALA E   105                                                      
REMARK 465     PRO E   106                                                      
REMARK 465     ALA E   107                                                      
REMARK 465     VAL E   108                                                      
REMARK 465     THR E   109                                                      
REMARK 465     ALA E   110                                                      
REMARK 465     GLY E   111                                                      
REMARK 465     LEU E   112                                                      
REMARK 465     LYS E   113                                                      
REMARK 465     ILE E   114                                                      
REMARK 465     PHE E   115                                                      
REMARK 465     GLU E   116                                                      
REMARK 465     PRO E   117                                                      
REMARK 465     PRO E   118                                                      
REMARK 465     ALA E   119                                                      
REMARK 465     PRO E   120                                                      
REMARK 465     GLY E   121                                                      
REMARK 465     GLU E   122                                                      
REMARK 465     GLY E   123                                                      
REMARK 465     ASN E   124                                                      
REMARK 465     SER E   125                                                      
REMARK 465     SER E   126                                                      
REMARK 465     GLN E   127                                                      
REMARK 465     ASN E   128                                                      
REMARK 465     SER E   129                                                      
REMARK 465     ARG E   130                                                      
REMARK 465     ASN E   131                                                      
REMARK 465     LYS E   132                                                      
REMARK 465     ARG E   133                                                      
REMARK 465     ALA E   134                                                      
REMARK 465     VAL E   135                                                      
REMARK 465     GLN E   136                                                      
REMARK 465     GLY E   137                                                      
REMARK 465     PRO E   138                                                      
REMARK 465     GLU E   139                                                      
REMARK 465     GLU E   140                                                      
REMARK 465     THR E   141                                                      
REMARK 465     GLY F    78                                                      
REMARK 465     SER F    79                                                      
REMARK 465     HIS F    80                                                      
REMARK 465     MET F    81                                                      
REMARK 465     GLU F    82                                                      
REMARK 465     LEU F    83                                                      
REMARK 465     GLN F    84                                                      
REMARK 465     GLY F    85                                                      
REMARK 465     HIS F    86                                                      
REMARK 465     HIS F    87                                                      
REMARK 465     ALA F    88                                                      
REMARK 465     GLU F    89                                                      
REMARK 465     LYS F    90                                                      
REMARK 465     LEU F    91                                                      
REMARK 465     PRO F    92                                                      
REMARK 465     ALA F    93                                                      
REMARK 465     GLY F    94                                                      
REMARK 465     ALA F    95                                                      
REMARK 465     GLY F    96                                                      
REMARK 465     ALA F    97                                                      
REMARK 465     PRO F    98                                                      
REMARK 465     LYS F    99                                                      
REMARK 465     ALA F   100                                                      
REMARK 465     GLY F   101                                                      
REMARK 465     LEU F   102                                                      
REMARK 465     GLU F   103                                                      
REMARK 465     GLU F   104                                                      
REMARK 465     ALA F   105                                                      
REMARK 465     PRO F   106                                                      
REMARK 465     ALA F   107                                                      
REMARK 465     VAL F   108                                                      
REMARK 465     THR F   109                                                      
REMARK 465     ALA F   110                                                      
REMARK 465     GLY F   111                                                      
REMARK 465     LEU F   112                                                      
REMARK 465     LYS F   113                                                      
REMARK 465     ILE F   114                                                      
REMARK 465     PHE F   115                                                      
REMARK 465     GLU F   116                                                      
REMARK 465     PRO F   117                                                      
REMARK 465     PRO F   118                                                      
REMARK 465     ALA F   119                                                      
REMARK 465     PRO F   120                                                      
REMARK 465     GLY F   121                                                      
REMARK 465     GLU F   122                                                      
REMARK 465     GLY F   123                                                      
REMARK 465     ASN F   124                                                      
REMARK 465     SER F   125                                                      
REMARK 465     SER F   126                                                      
REMARK 465     GLN F   127                                                      
REMARK 465     ASN F   128                                                      
REMARK 465     SER F   129                                                      
REMARK 465     ARG F   130                                                      
REMARK 465     ASN F   131                                                      
REMARK 465     LYS F   132                                                      
REMARK 465     ARG F   133                                                      
REMARK 465     ALA F   134                                                      
REMARK 465     VAL F   135                                                      
REMARK 465     GLN F   136                                                      
REMARK 465     GLY F   137                                                      
REMARK 465     PRO F   138                                                      
REMARK 465     GLU F   139                                                      
REMARK 465     GLU F   140                                                      
REMARK 465     THR F   141                                                      
REMARK 465     ACE H    22                                                      
REMARK 465     ACE I    22                                                      
REMARK 465     ACE J    22                                                      
REMARK 465     ACE K    22                                                      
REMARK 465     ACE L    22                                                      
REMARK 465     ACE Z    22                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 160    CG   CD   CE   NZ                                   
REMARK 470     LEU A 169    CG   CD1  CD2                                       
REMARK 470     LYS A 181    CG   CD   CE   NZ                                   
REMARK 470     LYS A 184    CE   NZ                                             
REMARK 470     LYS A 204    CG   CD   CE   NZ                                   
REMARK 470     LYS A 215    CE   NZ                                             
REMARK 470     GLU A 238    CD   OE1  OE2                                       
REMARK 470     LYS B 160    CG   CD   CE   NZ                                   
REMARK 470     LYS B 173    CE   NZ                                             
REMARK 470     LYS B 181    CG   CD   CE   NZ                                   
REMARK 470     LYS B 184    CE   NZ                                             
REMARK 470     LYS B 188    CE   NZ                                             
REMARK 470     LYS B 204    CG   CD   CE   NZ                                   
REMARK 470     LYS B 215    CD   CE   NZ                                        
REMARK 470     GLU B 238    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 252    CD   CE   NZ                                        
REMARK 470     LYS C 160    CG   CD   CE   NZ                                   
REMARK 470     LYS C 181    CG   CD   CE   NZ                                   
REMARK 470     LYS C 184    CE   NZ                                             
REMARK 470     LYS C 188    CE   NZ                                             
REMARK 470     LYS C 204    CG   CD   CE   NZ                                   
REMARK 470     LYS C 215    CD   CE   NZ                                        
REMARK 470     GLU C 238    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 266    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 160    CG   CD   CE   NZ                                   
REMARK 470     LYS D 181    CG   CD   CE   NZ                                   
REMARK 470     LYS D 184    CE   NZ                                             
REMARK 470     LYS D 188    CE   NZ                                             
REMARK 470     LYS D 204    CG   CD   CE   NZ                                   
REMARK 470     LYS D 215    CD   CE   NZ                                        
REMARK 470     LYS D 216    CG   CD   CE   NZ                                   
REMARK 470     VAL D 219    CG1  CG2                                            
REMARK 470     PHE D 220    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP D 222    CG   OD1  OD2                                       
REMARK 470     GLU D 238    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 266    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 160    CG   CD   CE   NZ                                   
REMARK 470     LYS E 173    CE   NZ                                             
REMARK 470     LYS E 181    CG   CD   CE   NZ                                   
REMARK 470     LYS E 184    CE   NZ                                             
REMARK 470     LYS E 188    NZ                                                  
REMARK 470     LYS E 204    CG   CD   CE   NZ                                   
REMARK 470     LYS E 215    CD   CE   NZ                                        
REMARK 470     GLU E 238    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 266    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 160    CG   CD   CE   NZ                                   
REMARK 470     LYS F 181    CG   CD   CE   NZ                                   
REMARK 470     LYS F 184    CE   NZ                                             
REMARK 470     LYS F 204    CG   CD   CE   NZ                                   
REMARK 470     LYS F 215    CE   NZ                                             
REMARK 470     GLU F 238    CG   CD   OE1  OE2                                  
REMARK 470     VAL G  33    CG1  CG2                                            
REMARK 470     HIS H  24    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG H  30    NE   CZ   NH1  NH2                                  
REMARK 470     VAL H  33    CG1  CG2                                            
REMARK 470     HIS I  24    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG I  30    NE   CZ   NH1  NH2                                  
REMARK 470     VAL I  33    CG1  CG2                                            
REMARK 470     HIS J  24    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG J  30    NE   CZ   NH1  NH2                                  
REMARK 470     VAL J  33    CG1  CG2                                            
REMARK 470     VAL K  33    CG1  CG2                                            
REMARK 470     VAL L  33    CG1  CG2                                            
REMARK 470     HIS Z  24    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU Z  27    CG   CD1  CD2                                       
REMARK 470     LEU Z  28    CG   CD1  CD2                                       
REMARK 470     VAL Z  29    CG1  CG2                                            
REMARK 470     ARG Z  30    CG   CD   NE   CZ   NH1  NH2                        
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    TYR A 206      -37.22    -39.34                                   
REMARK 500    ASN A 242       89.98   -153.73                                   
REMARK 500    TYR B 206      -37.00    -39.42                                   
REMARK 500    TYR C 206      -37.33    -39.46                                   
REMARK 500    TYR D 206      -37.12    -38.63                                   
REMARK 500    TYR E 206      -37.26    -39.42                                   
REMARK 500    ASN E 242       89.41   -153.53                                   
REMARK 500    ASN E 267       60.74     39.40                                   
REMARK 500    TYR F 206      -37.09    -38.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 499                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1OSG   RELATED DB: PDB                                   
REMARK 900 THIS ENTRY 3V56 REFLECTS AN ALTERNATIVE MODELING OF X-RAY DATA       
REMARK 900 R1OSGSF                                                              
DBREF  3V56 A   82   285  UNP    Q9Y275   TN13B_HUMAN     82    285             
DBREF  3V56 B   82   285  UNP    Q9Y275   TN13B_HUMAN     82    285             
DBREF  3V56 C   82   285  UNP    Q9Y275   TN13B_HUMAN     82    285             
DBREF  3V56 D   82   285  UNP    Q9Y275   TN13B_HUMAN     82    285             
DBREF  3V56 E   82   285  UNP    Q9Y275   TN13B_HUMAN     82    285             
DBREF  3V56 F   82   285  UNP    Q9Y275   TN13B_HUMAN     82    285             
DBREF  3V56 G   22    35  PDB    3V56     3V56            22     35             
DBREF  3V56 H   22    35  PDB    3V56     3V56            22     35             
DBREF  3V56 I   22    35  PDB    3V56     3V56            22     35             
DBREF  3V56 J   22    35  PDB    3V56     3V56            22     35             
DBREF  3V56 K   22    35  PDB    3V56     3V56            22     35             
DBREF  3V56 L   22    35  PDB    3V56     3V56            22     35             
DBREF  3V56 Z   22    35  PDB    3V56     3V56            22     35             
SEQADV 3V56 GLY A   78  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 SER A   79  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 HIS A   80  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 MET A   81  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 GLY B   78  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 SER B   79  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 HIS B   80  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 MET B   81  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 GLY C   78  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 SER C   79  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 HIS C   80  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 MET C   81  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 GLY D   78  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 SER D   79  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 HIS D   80  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 MET D   81  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 GLY E   78  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 SER E   79  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 HIS E   80  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 MET E   81  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 GLY F   78  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 SER F   79  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 HIS F   80  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 3V56 MET F   81  UNP  Q9Y275              EXPRESSION TAG                 
SEQRES   1 A  208  GLY SER HIS MET GLU LEU GLN GLY HIS HIS ALA GLU LYS          
SEQRES   2 A  208  LEU PRO ALA GLY ALA GLY ALA PRO LYS ALA GLY LEU GLU          
SEQRES   3 A  208  GLU ALA PRO ALA VAL THR ALA GLY LEU LYS ILE PHE GLU          
SEQRES   4 A  208  PRO PRO ALA PRO GLY GLU GLY ASN SER SER GLN ASN SER          
SEQRES   5 A  208  ARG ASN LYS ARG ALA VAL GLN GLY PRO GLU GLU THR VAL          
SEQRES   6 A  208  THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU THR          
SEQRES   7 A  208  PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO TRP          
SEQRES   8 A  208  LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU LYS          
SEQRES   9 A  208  GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE PHE          
SEQRES  10 A  208  ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR ALA          
SEQRES  11 A  208  MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL PHE          
SEQRES  12 A  208  GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS ILE          
SEQRES  13 A  208  GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS TYR          
SEQRES  14 A  208  SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU LEU          
SEQRES  15 A  208  GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER LEU          
SEQRES  16 A  208  ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU LEU          
SEQRES   1 B  208  GLY SER HIS MET GLU LEU GLN GLY HIS HIS ALA GLU LYS          
SEQRES   2 B  208  LEU PRO ALA GLY ALA GLY ALA PRO LYS ALA GLY LEU GLU          
SEQRES   3 B  208  GLU ALA PRO ALA VAL THR ALA GLY LEU LYS ILE PHE GLU          
SEQRES   4 B  208  PRO PRO ALA PRO GLY GLU GLY ASN SER SER GLN ASN SER          
SEQRES   5 B  208  ARG ASN LYS ARG ALA VAL GLN GLY PRO GLU GLU THR VAL          
SEQRES   6 B  208  THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU THR          
SEQRES   7 B  208  PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO TRP          
SEQRES   8 B  208  LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU LYS          
SEQRES   9 B  208  GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE PHE          
SEQRES  10 B  208  ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR ALA          
SEQRES  11 B  208  MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL PHE          
SEQRES  12 B  208  GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS ILE          
SEQRES  13 B  208  GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS TYR          
SEQRES  14 B  208  SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU LEU          
SEQRES  15 B  208  GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER LEU          
SEQRES  16 B  208  ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU LEU          
SEQRES   1 C  208  GLY SER HIS MET GLU LEU GLN GLY HIS HIS ALA GLU LYS          
SEQRES   2 C  208  LEU PRO ALA GLY ALA GLY ALA PRO LYS ALA GLY LEU GLU          
SEQRES   3 C  208  GLU ALA PRO ALA VAL THR ALA GLY LEU LYS ILE PHE GLU          
SEQRES   4 C  208  PRO PRO ALA PRO GLY GLU GLY ASN SER SER GLN ASN SER          
SEQRES   5 C  208  ARG ASN LYS ARG ALA VAL GLN GLY PRO GLU GLU THR VAL          
SEQRES   6 C  208  THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU THR          
SEQRES   7 C  208  PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO TRP          
SEQRES   8 C  208  LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU LYS          
SEQRES   9 C  208  GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE PHE          
SEQRES  10 C  208  ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR ALA          
SEQRES  11 C  208  MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL PHE          
SEQRES  12 C  208  GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS ILE          
SEQRES  13 C  208  GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS TYR          
SEQRES  14 C  208  SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU LEU          
SEQRES  15 C  208  GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER LEU          
SEQRES  16 C  208  ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU LEU          
SEQRES   1 D  208  GLY SER HIS MET GLU LEU GLN GLY HIS HIS ALA GLU LYS          
SEQRES   2 D  208  LEU PRO ALA GLY ALA GLY ALA PRO LYS ALA GLY LEU GLU          
SEQRES   3 D  208  GLU ALA PRO ALA VAL THR ALA GLY LEU LYS ILE PHE GLU          
SEQRES   4 D  208  PRO PRO ALA PRO GLY GLU GLY ASN SER SER GLN ASN SER          
SEQRES   5 D  208  ARG ASN LYS ARG ALA VAL GLN GLY PRO GLU GLU THR VAL          
SEQRES   6 D  208  THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU THR          
SEQRES   7 D  208  PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO TRP          
SEQRES   8 D  208  LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU LYS          
SEQRES   9 D  208  GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE PHE          
SEQRES  10 D  208  ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR ALA          
SEQRES  11 D  208  MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL PHE          
SEQRES  12 D  208  GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS ILE          
SEQRES  13 D  208  GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS TYR          
SEQRES  14 D  208  SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU LEU          
SEQRES  15 D  208  GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER LEU          
SEQRES  16 D  208  ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU LEU          
SEQRES   1 E  208  GLY SER HIS MET GLU LEU GLN GLY HIS HIS ALA GLU LYS          
SEQRES   2 E  208  LEU PRO ALA GLY ALA GLY ALA PRO LYS ALA GLY LEU GLU          
SEQRES   3 E  208  GLU ALA PRO ALA VAL THR ALA GLY LEU LYS ILE PHE GLU          
SEQRES   4 E  208  PRO PRO ALA PRO GLY GLU GLY ASN SER SER GLN ASN SER          
SEQRES   5 E  208  ARG ASN LYS ARG ALA VAL GLN GLY PRO GLU GLU THR VAL          
SEQRES   6 E  208  THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU THR          
SEQRES   7 E  208  PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO TRP          
SEQRES   8 E  208  LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU LYS          
SEQRES   9 E  208  GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE PHE          
SEQRES  10 E  208  ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR ALA          
SEQRES  11 E  208  MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL PHE          
SEQRES  12 E  208  GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS ILE          
SEQRES  13 E  208  GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS TYR          
SEQRES  14 E  208  SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU LEU          
SEQRES  15 E  208  GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER LEU          
SEQRES  16 E  208  ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU LEU          
SEQRES   1 F  208  GLY SER HIS MET GLU LEU GLN GLY HIS HIS ALA GLU LYS          
SEQRES   2 F  208  LEU PRO ALA GLY ALA GLY ALA PRO LYS ALA GLY LEU GLU          
SEQRES   3 F  208  GLU ALA PRO ALA VAL THR ALA GLY LEU LYS ILE PHE GLU          
SEQRES   4 F  208  PRO PRO ALA PRO GLY GLU GLY ASN SER SER GLN ASN SER          
SEQRES   5 F  208  ARG ASN LYS ARG ALA VAL GLN GLY PRO GLU GLU THR VAL          
SEQRES   6 F  208  THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU THR          
SEQRES   7 F  208  PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO TRP          
SEQRES   8 F  208  LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU LYS          
SEQRES   9 F  208  GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE PHE          
SEQRES  10 F  208  ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR ALA          
SEQRES  11 F  208  MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL PHE          
SEQRES  12 F  208  GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS ILE          
SEQRES  13 F  208  GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS TYR          
SEQRES  14 F  208  SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU LEU          
SEQRES  15 F  208  GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER LEU          
SEQRES  16 F  208  ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU LEU          
SEQRES   1 G   14  ACE CYS HIS TRP ASP LEU LEU VAL ARG HIS TRP VAL CYS          
SEQRES   2 G   14  NH2                                                          
SEQRES   1 H   14  ACE CYS HIS TRP ASP LEU LEU VAL ARG HIS TRP VAL CYS          
SEQRES   2 H   14  NH2                                                          
SEQRES   1 I   14  ACE CYS HIS TRP ASP LEU LEU VAL ARG HIS TRP VAL CYS          
SEQRES   2 I   14  NH2                                                          
SEQRES   1 J   14  ACE CYS HIS TRP ASP LEU LEU VAL ARG HIS TRP VAL CYS          
SEQRES   2 J   14  NH2                                                          
SEQRES   1 K   14  ACE CYS HIS TRP ASP LEU LEU VAL ARG HIS TRP VAL CYS          
SEQRES   2 K   14  NH2                                                          
SEQRES   1 L   14  ACE CYS HIS TRP ASP LEU LEU VAL ARG HIS TRP VAL CYS          
SEQRES   2 L   14  NH2                                                          
SEQRES   1 Z   14  ACE CYS HIS TRP ASP LEU LEU VAL ARG HIS TRP VAL CYS          
SEQRES   2 Z   14  NH2                                                          
HET    ACE  G  22       3                                                       
HET    NH2  G  35       1                                                       
HET    NH2  H  35       1                                                       
HET    NH2  I  35       1                                                       
HET    NH2  J  35       1                                                       
HET    NH2  K  35       1                                                       
HET    NH2  L  35       1                                                       
HET    NH2  Z  35       1                                                       
HET    SO4  A 499       5                                                       
HET    SO4  D 499       5                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     NH2 AMINO GROUP                                                      
HETNAM     SO4 SULFATE ION                                                      
FORMUL   7  ACE    C2 H4 O                                                      
FORMUL   7  NH2    7(H2 N)                                                      
FORMUL  14  SO4    2(O4 S 2-)                                                   
FORMUL  16  HOH   *18(H2 O)                                                     
SHEET    1   A 5 TRP A 168  ARG A 174  0                                        
SHEET    2   A 5 CYS A 146  ALA A 151 -1  N  CYS A 146   O  ARG A 174           
SHEET    3   A 5 PHE A 278  LYS A 283 -1  O  PHE A 279   N  LEU A 149           
SHEET    4   A 5 GLY A 191  TYR A 201 -1  N  PHE A 194   O  LEU A 282           
SHEET    5   A 5 ASN A 243  LEU A 253 -1  O  ASN A 243   N  TYR A 201           
SHEET    1   B 5 TRP A 168  ARG A 174  0                                        
SHEET    2   B 5 CYS A 146  ALA A 151 -1  N  CYS A 146   O  ARG A 174           
SHEET    3   B 5 PHE A 278  LYS A 283 -1  O  PHE A 279   N  LEU A 149           
SHEET    4   B 5 GLY A 191  TYR A 201 -1  N  PHE A 194   O  LEU A 282           
SHEET    5   B 5 ILE A 270  SER A 271 -1  O  SER A 271   N  LEU A 200           
SHEET    1   C 4 THR A 164  PHE A 165  0                                        
SHEET    2   C 4 GLU A 258  ILE A 263 -1  O  ILE A 263   N  THR A 164           
SHEET    3   C 4 LYS A 184  VAL A 187 -1  N  ILE A 185   O  LEU A 259           
SHEET    4   C 4 LEU A 178  LYS A 181 -1  N  GLU A 179   O  LEU A 186           
SHEET    1   D 4 THR A 164  PHE A 165  0                                        
SHEET    2   D 4 GLU A 258  ILE A 263 -1  O  ILE A 263   N  THR A 164           
SHEET    3   D 4 LEU A 211  LYS A 215 -1  N  LYS A 215   O  GLU A 258           
SHEET    4   D 4 LEU A 226  ARG A 231 -1  O  PHE A 230   N  ILE A 212           
SHEET    1   E 2 ALA A 207  MET A 208  0                                        
SHEET    2   E 2 GLN A 234  ASN A 235 -1  O  GLN A 234   N  MET A 208           
SHEET    1   F 5 TRP B 168  ARG B 174  0                                        
SHEET    2   F 5 CYS B 146  ALA B 151 -1  N  ILE B 150   O  LEU B 169           
SHEET    3   F 5 PHE B 278  LYS B 283 -1  O  PHE B 279   N  LEU B 149           
SHEET    4   F 5 GLY B 191  TYR B 201 -1  N  GLN B 198   O  PHE B 278           
SHEET    5   F 5 ASN B 243  LEU B 253 -1  O  ASN B 243   N  TYR B 201           
SHEET    1   G 5 TRP B 168  ARG B 174  0                                        
SHEET    2   G 5 CYS B 146  ALA B 151 -1  N  ILE B 150   O  LEU B 169           
SHEET    3   G 5 PHE B 278  LYS B 283 -1  O  PHE B 279   N  LEU B 149           
SHEET    4   G 5 GLY B 191  TYR B 201 -1  N  GLN B 198   O  PHE B 278           
SHEET    5   G 5 ILE B 270  SER B 271 -1  O  SER B 271   N  LEU B 200           
SHEET    1   H 5 ILE B 158  LYS B 160  0                                        
SHEET    2   H 5 TYR B 163  PHE B 165 -1  O  PHE B 165   N  ILE B 158           
SHEET    3   H 5 GLU B 258  ILE B 263 -1  O  ILE B 263   N  THR B 164           
SHEET    4   H 5 LYS B 184  VAL B 187 -1  N  ILE B 185   O  LEU B 259           
SHEET    5   H 5 LEU B 178  LYS B 181 -1  N  GLU B 179   O  LEU B 186           
SHEET    1   I 5 ILE B 158  LYS B 160  0                                        
SHEET    2   I 5 TYR B 163  PHE B 165 -1  O  PHE B 165   N  ILE B 158           
SHEET    3   I 5 GLU B 258  ILE B 263 -1  O  ILE B 263   N  THR B 164           
SHEET    4   I 5 LEU B 211  LYS B 215 -1  N  LYS B 215   O  GLU B 258           
SHEET    5   I 5 LEU B 226  ARG B 231 -1  O  PHE B 230   N  ILE B 212           
SHEET    1   J 2 ALA B 207  MET B 208  0                                        
SHEET    2   J 2 GLN B 234  ASN B 235 -1  O  GLN B 234   N  MET B 208           
SHEET    1   K 5 TRP C 168  ARG C 174  0                                        
SHEET    2   K 5 CYS C 146  ALA C 151 -1  N  CYS C 146   O  ARG C 174           
SHEET    3   K 5 PHE C 278  LYS C 283 -1  O  PHE C 279   N  LEU C 149           
SHEET    4   K 5 GLY C 191  TYR C 201 -1  N  PHE C 194   O  LEU C 282           
SHEET    5   K 5 ASN C 243  LEU C 253 -1  O  ASN C 243   N  TYR C 201           
SHEET    1   L 5 TRP C 168  ARG C 174  0                                        
SHEET    2   L 5 CYS C 146  ALA C 151 -1  N  CYS C 146   O  ARG C 174           
SHEET    3   L 5 PHE C 278  LYS C 283 -1  O  PHE C 279   N  LEU C 149           
SHEET    4   L 5 GLY C 191  TYR C 201 -1  N  PHE C 194   O  LEU C 282           
SHEET    5   L 5 ILE C 270  SER C 271 -1  O  SER C 271   N  LEU C 200           
SHEET    1   M 5 ILE C 158  LYS C 160  0                                        
SHEET    2   M 5 TYR C 163  PHE C 165 -1  O  PHE C 165   N  ILE C 158           
SHEET    3   M 5 GLU C 258  ILE C 263 -1  O  ILE C 263   N  THR C 164           
SHEET    4   M 5 LYS C 184  VAL C 187 -1  N  ILE C 185   O  LEU C 259           
SHEET    5   M 5 LEU C 178  LYS C 181 -1  N  GLU C 179   O  LEU C 186           
SHEET    1   N 5 ILE C 158  LYS C 160  0                                        
SHEET    2   N 5 TYR C 163  PHE C 165 -1  O  PHE C 165   N  ILE C 158           
SHEET    3   N 5 GLU C 258  ILE C 263 -1  O  ILE C 263   N  THR C 164           
SHEET    4   N 5 LEU C 211  LYS C 215 -1  N  LYS C 215   O  GLU C 258           
SHEET    5   N 5 LEU C 226  ARG C 231 -1  O  LEU C 229   N  ILE C 212           
SHEET    1   O 2 ALA C 207  MET C 208  0                                        
SHEET    2   O 2 GLN C 234  ASN C 235 -1  O  GLN C 234   N  MET C 208           
SHEET    1   P 5 TRP D 168  ARG D 174  0                                        
SHEET    2   P 5 CYS D 146  ALA D 151 -1  N  ILE D 150   O  LEU D 169           
SHEET    3   P 5 PHE D 278  LYS D 283 -1  O  PHE D 279   N  LEU D 149           
SHEET    4   P 5 GLY D 191  TYR D 201 -1  N  PHE D 194   O  LEU D 282           
SHEET    5   P 5 ASN D 243  LEU D 253 -1  O  ASN D 243   N  TYR D 201           
SHEET    1   Q 5 TRP D 168  ARG D 174  0                                        
SHEET    2   Q 5 CYS D 146  ALA D 151 -1  N  ILE D 150   O  LEU D 169           
SHEET    3   Q 5 PHE D 278  LYS D 283 -1  O  PHE D 279   N  LEU D 149           
SHEET    4   Q 5 GLY D 191  TYR D 201 -1  N  PHE D 194   O  LEU D 282           
SHEET    5   Q 5 ILE D 270  SER D 271 -1  O  SER D 271   N  LEU D 200           
SHEET    1   R 4 THR D 164  PHE D 165  0                                        
SHEET    2   R 4 GLU D 258  ILE D 263 -1  O  ILE D 263   N  THR D 164           
SHEET    3   R 4 LYS D 184  VAL D 187 -1  N  ILE D 185   O  LEU D 259           
SHEET    4   R 4 LEU D 178  LYS D 181 -1  N  GLU D 179   O  LEU D 186           
SHEET    1   S 4 THR D 164  PHE D 165  0                                        
SHEET    2   S 4 GLU D 258  ILE D 263 -1  O  ILE D 263   N  THR D 164           
SHEET    3   S 4 LEU D 211  LYS D 215 -1  N  LYS D 215   O  GLU D 258           
SHEET    4   S 4 LEU D 226  ARG D 231 -1  O  LEU D 229   N  ILE D 212           
SHEET    1   T 2 ALA D 207  MET D 208  0                                        
SHEET    2   T 2 GLN D 234  ASN D 235 -1  O  GLN D 234   N  MET D 208           
SHEET    1   U 5 TRP E 168  ARG E 174  0                                        
SHEET    2   U 5 CYS E 146  ALA E 151 -1  N  CYS E 146   O  ARG E 174           
SHEET    3   U 5 PHE E 278  LYS E 283 -1  O  PHE E 279   N  LEU E 149           
SHEET    4   U 5 GLY E 191  TYR E 201 -1  N  PHE E 194   O  LEU E 282           
SHEET    5   U 5 ASN E 243  LEU E 253 -1  O  LEU E 253   N  GLY E 191           
SHEET    1   V 5 TRP E 168  ARG E 174  0                                        
SHEET    2   V 5 CYS E 146  ALA E 151 -1  N  CYS E 146   O  ARG E 174           
SHEET    3   V 5 PHE E 278  LYS E 283 -1  O  PHE E 279   N  LEU E 149           
SHEET    4   V 5 GLY E 191  TYR E 201 -1  N  PHE E 194   O  LEU E 282           
SHEET    5   V 5 ILE E 270  SER E 271 -1  O  SER E 271   N  LEU E 200           
SHEET    1   W 5 ILE E 158  LYS E 160  0                                        
SHEET    2   W 5 TYR E 163  PHE E 165 -1  O  PHE E 165   N  ILE E 158           
SHEET    3   W 5 GLU E 258  ILE E 263 -1  O  ILE E 263   N  THR E 164           
SHEET    4   W 5 LYS E 184  VAL E 187 -1  N  ILE E 185   O  LEU E 259           
SHEET    5   W 5 LEU E 178  LYS E 181 -1  N  GLU E 179   O  LEU E 186           
SHEET    1   X 5 ILE E 158  LYS E 160  0                                        
SHEET    2   X 5 TYR E 163  PHE E 165 -1  O  PHE E 165   N  ILE E 158           
SHEET    3   X 5 GLU E 258  ILE E 263 -1  O  ILE E 263   N  THR E 164           
SHEET    4   X 5 LEU E 211  LYS E 215 -1  N  LYS E 215   O  GLU E 258           
SHEET    5   X 5 LEU E 226  ARG E 231 -1  O  PHE E 230   N  ILE E 212           
SHEET    1   Y 2 ALA E 207  MET E 208  0                                        
SHEET    2   Y 2 GLN E 234  ASN E 235 -1  O  GLN E 234   N  MET E 208           
SHEET    1   Z 5 TRP F 168  ARG F 174  0                                        
SHEET    2   Z 5 CYS F 146  ALA F 151 -1  N  CYS F 146   O  ARG F 174           
SHEET    3   Z 5 PHE F 278  LYS F 283 -1  O  PHE F 279   N  LEU F 149           
SHEET    4   Z 5 GLY F 191  TYR F 201 -1  N  PHE F 194   O  LEU F 282           
SHEET    5   Z 5 ASN F 243  LEU F 253 -1  O  ASN F 243   N  TYR F 201           
SHEET    1  AA 5 TRP F 168  ARG F 174  0                                        
SHEET    2  AA 5 CYS F 146  ALA F 151 -1  N  CYS F 146   O  ARG F 174           
SHEET    3  AA 5 PHE F 278  LYS F 283 -1  O  PHE F 279   N  LEU F 149           
SHEET    4  AA 5 GLY F 191  TYR F 201 -1  N  PHE F 194   O  LEU F 282           
SHEET    5  AA 5 ILE F 270  SER F 271 -1  O  SER F 271   N  LEU F 200           
SHEET    1  AB 5 ILE F 158  LYS F 160  0                                        
SHEET    2  AB 5 TYR F 163  PHE F 165 -1  O  PHE F 165   N  ILE F 158           
SHEET    3  AB 5 GLU F 258  ILE F 263 -1  O  ILE F 263   N  THR F 164           
SHEET    4  AB 5 LYS F 184  VAL F 187 -1  N  ILE F 185   O  LEU F 259           
SHEET    5  AB 5 LEU F 178  LYS F 181 -1  N  GLU F 179   O  LEU F 186           
SHEET    1  AC 5 ILE F 158  LYS F 160  0                                        
SHEET    2  AC 5 TYR F 163  PHE F 165 -1  O  PHE F 165   N  ILE F 158           
SHEET    3  AC 5 GLU F 258  ILE F 263 -1  O  ILE F 263   N  THR F 164           
SHEET    4  AC 5 LEU F 211  LYS F 215 -1  N  LYS F 215   O  GLU F 258           
SHEET    5  AC 5 LEU F 226  ARG F 231 -1  O  LEU F 229   N  ILE F 212           
SHEET    1  AD 2 ALA F 207  MET F 208  0                                        
SHEET    2  AD 2 GLN F 234  ASN F 235 -1  O  GLN F 234   N  MET F 208           
SHEET    1  AE 2 HIS G  24  ASP G  26  0                                        
SHEET    2  AE 2 HIS G  31  VAL G  33 -1  O  VAL G  33   N  HIS G  24           
SHEET    1  AF 2 HIS H  24  ASP H  26  0                                        
SHEET    2  AF 2 HIS H  31  VAL H  33 -1  O  HIS H  31   N  ASP H  26           
SHEET    1  AG 2 HIS I  24  ASP I  26  0                                        
SHEET    2  AG 2 HIS I  31  VAL I  33 -1  O  HIS I  31   N  ASP I  26           
SHEET    1  AH 2 HIS J  24  ASP J  26  0                                        
SHEET    2  AH 2 HIS J  31  VAL J  33 -1  O  VAL J  33   N  HIS J  24           
SHEET    1  AI 4 HIS K  31  VAL K  33  0                                        
SHEET    2  AI 4 HIS K  24  ASP K  26 -1  N  ASP K  26   O  HIS K  31           
SHEET    3  AI 4 HIS Z  31  CYS Z  34  1  O  TRP Z  32   N  TRP K  25           
SHEET    4  AI 4 HIS Z  24  ASP Z  26 -1  N  HIS Z  24   O  VAL Z  33           
SHEET    1  AJ 2 HIS L  24  ASP L  26  0                                        
SHEET    2  AJ 2 HIS L  31  VAL L  33 -1  O  HIS L  31   N  ASP L  26           
SSBOND   1 CYS A  232    CYS A  245                          1555   1555  2.03  
SSBOND   2 CYS B  232    CYS B  245                          1555   1555  2.03  
SSBOND   3 CYS C  232    CYS C  245                          1555   1555  2.03  
SSBOND   4 CYS D  232    CYS D  245                          1555   1555  2.03  
SSBOND   5 CYS E  232    CYS E  245                          1555   1555  2.04  
SSBOND   6 CYS F  232    CYS F  245                          1555   1555  2.04  
SSBOND   7 CYS G   23    CYS G   34                          1555   1555  2.04  
SSBOND   8 CYS H   23    CYS H   34                          1555   1555  2.03  
SSBOND   9 CYS I   23    CYS I   34                          1555   1555  2.03  
SSBOND  10 CYS J   23    CYS J   34                          1555   1555  2.03  
SSBOND  11 CYS K   23    CYS K   34                          1555   1555  2.03  
SSBOND  12 CYS L   23    CYS L   34                          1555   1555  2.03  
SSBOND  13 CYS Z   23    CYS Z   34                          1555   1555  2.03  
LINK         C   ACE G  22                 N   CYS G  23     1555   1555  1.33  
LINK         C   CYS G  34                 N   NH2 G  35     1555   1555  1.34  
LINK         C   CYS H  34                 N   NH2 H  35     1555   1555  1.34  
LINK         C   CYS I  34                 N   NH2 I  35     1555   1555  1.34  
LINK         C   CYS J  34                 N   NH2 J  35     1555   1555  1.34  
LINK         C   CYS K  34                 N   NH2 K  35     1555   1555  1.34  
LINK         C   CYS L  34                 N   NH2 L  35     1555   1555  1.34  
LINK         C   CYS Z  34                 N   NH2 Z  35     1555   1555  1.34  
SITE     1 AC1  9 GLN A 234  ASN A 235  ASN A 243  GLN B 234                    
SITE     2 AC1  9 ASN B 235  ASN B 243  GLN C 234  ASN C 235                    
SITE     3 AC1  9 ASN C 243                                                     
SITE     1 AC2  9 GLN D 234  ASN D 235  ASN D 243  GLN E 234                    
SITE     2 AC2  9 ASN E 235  ASN E 243  GLN F 234  ASN F 235                    
SITE     3 AC2  9 ASN F 243                                                     
CRYST1  121.633  121.633  157.214  90.00  90.00 120.00 P 65         42          
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      0.008221  0.004747  0.000000        0.00000                         
SCALE2      0.000000  0.009493  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006361        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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