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Database: PDB
Entry: 5M2I
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HEADER    CYTOKINE                                13-OCT-16   5M2I              
TITLE     STRUCTURE OF HUMAN TUMOR NECROSIS FACTOR (TNF) IN COMPLEX WITH THE    
TITLE    2 LLAMA VHH1                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR;                                     
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: CACHECTIN,TNF-ALPHA,TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY
COMPND   5 MEMBER 2,TNF-A;                                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: VHH1;                                                      
COMPND   9 CHAIN: G, H, I, J, K, L;                                             
COMPND  10 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: TNF, TNFA, TNFSF2;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: LAMA GLAMA;                                     
SOURCE  10 ORGANISM_COMMON: LLAMA;                                              
SOURCE  11 ORGANISM_TAXID: 9844;                                                
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 511693                                      
KEYWDS    HUMAN TUMOR NECROSIS FACTOR (TNF) LLAMA VHH1, CYTOKINE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.CAMBILLAU,S.SPINELLI,A.DESMYTER,H.DE HAARD                          
REVDAT   2   06-SEP-17 5M2I    1       JRNL                                     
REVDAT   1   30-AUG-17 5M2I    0                                                
JRNL        AUTH   E.BEIRNAERT,A.DESMYTER,S.SPINELLI,M.LAUWEREYS,L.AARDEN,      
JRNL        AUTH 2 T.DREIER,R.LORIS,K.SILENCE,C.POLLET,C.CAMBILLAU,H.DE HAARD   
JRNL        TITL   BIVALENT LLAMA SINGLE-DOMAIN ANTIBODY FRAGMENTS AGAINST      
JRNL        TITL 2 TUMOR NECROSIS FACTOR HAVE PICOMOLAR POTENCIES DUE TO        
JRNL        TITL 3 INTRAMOLECULAR INTERACTIONS.                                 
JRNL        REF    FRONT IMMUNOL                 V.   8   867 2017              
JRNL        REFN                   ESSN 1664-3224                               
JRNL        PMID   28824615                                                     
JRNL        DOI    10.3389/FIMMU.2017.00867                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.1                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.68                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 100502                         
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)  : 0.208                          
REMARK   3   R VALUE            (WORKING SET)  : 0.207                          
REMARK   3   FREE R VALUE                      : 0.238                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 5026                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.15                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.21                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.86                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 7371                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2343                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 7002                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2330                   
REMARK   3   BIN FREE R VALUE                        : 0.2588                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.01                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 369                      
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            : 12509                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 747                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.47                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.22                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -9.21250                                             
REMARK   3    B22 (A**2) : 5.16760                                              
REMARK   3    B33 (A**2) : 4.04480                                              
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) : 0.317               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.240               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.185               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.235               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.186               
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      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 12819  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 17438  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 4297   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 322    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1858   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 12819  ; 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   : 1601   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 14497  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.17                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.36                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.70                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -2.0072    3.0232  -51.1148           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0879 T22:   -0.1065                                    
REMARK   3     T33:   -0.0303 T12:    0.0002                                    
REMARK   3     T13:   -0.0152 T23:   -0.0517                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3086 L22:    1.8939                                    
REMARK   3     L33:    1.3639 L12:   -0.6440                                    
REMARK   3     L13:   -0.1910 L23:   -0.1804                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0062 S12:    0.0824 S13:   -0.0457                     
REMARK   3     S21:   -0.0356 S22:    0.0811 S23:    0.0008                     
REMARK   3     S31:    0.0220 S32:    0.0470 S33:   -0.0873                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    5.9215    1.7096  -30.8930           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1659 T22:   -0.0880                                    
REMARK   3     T33:   -0.0727 T12:    0.0206                                    
REMARK   3     T13:   -0.0028 T23:   -0.0025                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.1552 L22:    0.4726                                    
REMARK   3     L33:    1.2601 L12:   -0.2876                                    
REMARK   3     L13:   -0.1156 L23:   -0.0614                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0134 S12:   -0.0014 S13:   -0.0567                     
REMARK   3     S21:   -0.0056 S22:   -0.0322 S23:    0.0166                     
REMARK   3     S31:    0.0555 S32:    0.0736 S33:    0.0188                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -0.2706   20.9633  -39.1217           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1039 T22:   -0.0642                                    
REMARK   3     T33:   -0.0594 T12:    0.0476                                    
REMARK   3     T13:    0.0732 T23:    0.0366                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9749 L22:    0.6137                                    
REMARK   3     L33:    1.3143 L12:    0.2602                                    
REMARK   3     L13:    0.1919 L23:    0.0266                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0042 S12:   -0.0241 S13:    0.0262                     
REMARK   3     S21:    0.0418 S22:    0.0183 S23:   -0.0511                     
REMARK   3     S31:   -0.0280 S32:    0.0183 S33:   -0.0141                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -1.9400  -27.4681  -90.8468           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0653 T22:   -0.0936                                    
REMARK   3     T33:   -0.0312 T12:   -0.0112                                    
REMARK   3     T13:   -0.0148 T23:   -0.0467                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3722 L22:    2.0682                                    
REMARK   3     L33:    1.4068 L12:    0.8949                                    
REMARK   3     L13:    0.2886 L23:    0.3335                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0035 S12:   -0.0714 S13:    0.0624                     
REMARK   3     S21:    0.0251 S22:    0.0618 S23:    0.0173                     
REMARK   3     S31:   -0.0287 S32:    0.0483 S33:   -0.0653                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { E|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    6.5723  -26.1735 -110.8680           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1076 T22:   -0.0418                                    
REMARK   3     T33:   -0.0545 T12:   -0.0294                                    
REMARK   3     T13:    0.0031 T23:   -0.0130                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3298 L22:    0.7570                                    
REMARK   3     L33:    1.0817 L12:   -0.0368                                    
REMARK   3     L13:    0.2074 L23:   -0.2240                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0105 S12:    0.0015 S13:    0.0512                     
REMARK   3     S21:    0.0251 S22:   -0.0265 S23:    0.0166                     
REMARK   3     S31:   -0.0701 S32:    0.0952 S33:    0.0160                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { F|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -0.1919  -45.4250 -102.7390           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0610 T22:   -0.0494                                    
REMARK   3     T33:   -0.0433 T12:   -0.0301                                    
REMARK   3     T13:   -0.0653 T23:    0.0307                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8224 L22:    0.6304                                    
REMARK   3     L33:    1.4743 L12:   -0.4854                                    
REMARK   3     L13:    0.0232 L23:    0.1735                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0075 S12:    0.0201 S13:   -0.0401                     
REMARK   3     S21:   -0.0385 S22:   -0.0114 S23:   -0.0540                     
REMARK   3     S31:    0.0381 S32:    0.0034 S33:    0.0189                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { G|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    6.8765    9.2296   -8.0579           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.2213 T22:   -0.1393                                    
REMARK   3     T33:   -0.1187 T12:   -0.0088                                    
REMARK   3     T13:    0.0038 T23:    0.0188                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3730 L22:    1.3922                                    
REMARK   3     L33:    2.5154 L12:   -0.1319                                    
REMARK   3     L13:    0.8314 L23:    0.1009                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0004 S12:    0.0050 S13:   -0.0111                     
REMARK   3     S21:    0.0213 S22:   -0.0210 S23:   -0.0298                     
REMARK   3     S31:   -0.0079 S32:   -0.0117 S33:    0.0205                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: { H|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -6.5016  -20.0025  -54.8114           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1800 T22:   -0.1620                                    
REMARK   3     T33:   -0.0523 T12:    0.0347                                    
REMARK   3     T13:   -0.0891 T23:   -0.0708                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    4.0303                                    
REMARK   3     L33:    1.4631 L12:    0.5165                                    
REMARK   3     L13:   -0.3774 L23:    0.9915                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0017 S12:   -0.0089 S13:    0.0506                     
REMARK   3     S21:    0.0082 S22:   -0.0089 S23:    0.0266                     
REMARK   3     S31:    0.0235 S32:    0.0122 S33:    0.0072                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: { I|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -13.6682   35.1386  -52.8483           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1045 T22:   -0.1078                                    
REMARK   3     T33:   -0.0838 T12:    0.0170                                    
REMARK   3     T13:    0.0541 T23:    0.0062                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.4240 L22:    3.2486                                    
REMARK   3     L33:    1.6827 L12:   -0.5002                                    
REMARK   3     L13:    0.8639 L23:   -0.1964                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0156 S12:   -0.0399 S13:   -0.0247                     
REMARK   3     S21:   -0.0147 S22:    0.0484 S23:    0.0569                     
REMARK   3     S31:   -0.0377 S32:   -0.0186 S33:   -0.0328                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: { J|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    6.9969  -33.6168 -133.7940           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1367 T22:   -0.0986                                    
REMARK   3     T33:   -0.0886 T12:    0.0261                                    
REMARK   3     T13:   -0.0182 T23:    0.0162                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.4930 L22:    1.4903                                    
REMARK   3     L33:    2.5258 L12:    0.5391                                    
REMARK   3     L13:   -1.1756 L23:    0.1153                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0033 S12:   -0.0023 S13:    0.0204                     
REMARK   3     S21:   -0.0269 S22:   -0.0176 S23:   -0.0289                     
REMARK   3     S31:    0.0149 S32:    0.0272 S33:    0.0208                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: { K|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -6.4005   -4.3997  -86.9883           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1496 T22:   -0.1464                                    
REMARK   3     T33:   -0.0385 T12:   -0.0227                                    
REMARK   3     T13:    0.0502 T23:   -0.0756                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    4.0131                                    
REMARK   3     L33:    1.4206 L12:   -0.1213                                    
REMARK   3     L13:    0.3780 L23:    0.8909                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0010 S12:    0.0059 S13:   -0.0490                     
REMARK   3     S21:    0.0111 S22:    0.0017 S23:    0.0194                     
REMARK   3     S31:   -0.0286 S32:    0.0116 S33:   -0.0008                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: { L|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -13.7656  -59.4581  -89.0684           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.2130 T22:   -0.1619                                    
REMARK   3     T33:   -0.1236 T12:   -0.0096                                    
REMARK   3     T13:   -0.0179 T23:    0.0047                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.1631 L22:    3.1765                                    
REMARK   3     L33:    2.5461 L12:    0.6430                                    
REMARK   3     L13:   -0.5788 L23:    0.3740                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0196 S12:    0.0404 S13:    0.0422                     
REMARK   3     S21:    0.0285 S22:    0.0312 S23:    0.0767                     
REMARK   3     S31:    0.0597 S32:   -0.0236 S33:   -0.0115                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5M2I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-OCT-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001802.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93100                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 100770                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.150                              
REMARK 200  R MERGE                    (I) : 0.12700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.11000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1TNF                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MIXED 100 NL OF PROTEIN 8 MG PER ML IN   
REMARK 280  HEPES 10 MM PH 7.0 WITH 100 NL OF PRECIPITANT SOLUTION              
REMARK 280  CONTAINING 20% PEG3000 AND 0.2M NACL AND 0.1M HEPES AT PH 7.5.,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       55.16500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.94500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.70500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.94500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       55.16500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       58.70500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13520 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 30730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 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: 13490 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 30560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 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 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     VAL A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     VAL B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     VAL C     1                                                      
REMARK 465     ARG C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     ARG C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     PRO C     8                                                      
REMARK 465     SER C     9                                                      
REMARK 465     VAL D     1                                                      
REMARK 465     ARG D     2                                                      
REMARK 465     SER D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     SER D     5                                                      
REMARK 465     ARG D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     PRO D     8                                                      
REMARK 465     SER D     9                                                      
REMARK 465     VAL E     1                                                      
REMARK 465     ARG E     2                                                      
REMARK 465     SER E     3                                                      
REMARK 465     SER E     4                                                      
REMARK 465     SER E     5                                                      
REMARK 465     ARG E     6                                                      
REMARK 465     THR E     7                                                      
REMARK 465     PRO E     8                                                      
REMARK 465     SER E     9                                                      
REMARK 465     GLU E   107                                                      
REMARK 465     GLY E   108                                                      
REMARK 465     VAL F     1                                                      
REMARK 465     ARG F     2                                                      
REMARK 465     SER F     3                                                      
REMARK 465     SER F     4                                                      
REMARK 465     SER F     5                                                      
REMARK 465     ARG F     6                                                      
REMARK 465     THR F     7                                                      
REMARK 465     PRO F     8                                                      
REMARK 465     SER F     9                                                      
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  11    CG   CD   CE   NZ                                   
REMARK 470     ARG A  31    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 107    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  10    CG   OD1  OD2                                       
REMARK 470     ARG B  31    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN B 102    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 104    CG   CD   OE1  OE2                                  
REMARK 470     ARG C  31    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS D  11    CG   CD   CE   NZ                                   
REMARK 470     ARG D  31    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG D 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP E  10    CG   OD1  OD2                                       
REMARK 470     ARG E  31    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN E 102    CG   CD   OE1  NE2                                  
REMARK 470     ARG E 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E 104    CG   CD   OE1  OE2                                  
REMARK 470     PRO E 106    CG   CD                                             
REMARK 470     ARG F  31    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    LEU A  37       94.39   -170.75                                   
REMARK 500    GLU A 107      100.89     34.26                                   
REMARK 500    HIS B  15       76.91   -157.39                                   
REMARK 500    LEU B  37       93.28   -169.33                                   
REMARK 500    ARG B 103      -83.66     64.48                                   
REMARK 500    GLU B 104       54.08     13.22                                   
REMARK 500    PRO B 106       97.16    -69.35                                   
REMARK 500    HIS C  15       86.84   -156.15                                   
REMARK 500    LEU C  37       92.41   -170.55                                   
REMARK 500    ASN C  46       -1.50     71.35                                   
REMARK 500    LEU D  37       94.53   -173.17                                   
REMARK 500    THR D 105       74.13   -160.66                                   
REMARK 500    HIS E  15       74.56   -163.09                                   
REMARK 500    LEU E  37       89.31   -170.68                                   
REMARK 500    SER E  71       47.75    -95.18                                   
REMARK 500    ARG E 103     -139.48     61.20                                   
REMARK 500    GLU E 104      150.87     60.51                                   
REMARK 500    THR E 105      -27.08   -161.91                                   
REMARK 500    LEU F  37       89.47   -169.09                                   
REMARK 500    SER G  28       66.58     37.06                                   
REMARK 500    SER H  28       66.10     36.32                                   
REMARK 500    SER I  28       66.85     35.90                                   
REMARK 500    SER J  28       65.97     38.51                                   
REMARK 500    SER K  28       65.80     36.49                                   
REMARK 500    SER L  28       65.27     38.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR E  105     PRO E  106                 -143.63                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    THR E 105        -17.85                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5M2I A    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5M2I B    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5M2I C    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5M2I D    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5M2I E    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5M2I F    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5M2I G    2   122  PDB    5M2I     5M2I             2    122             
DBREF  5M2I H    2   122  PDB    5M2I     5M2I             2    122             
DBREF  5M2I I    2   122  PDB    5M2I     5M2I             2    122             
DBREF  5M2I J    2   122  PDB    5M2I     5M2I             2    122             
DBREF  5M2I K    2   122  PDB    5M2I     5M2I             2    122             
DBREF  5M2I L    2   122  PDB    5M2I     5M2I             2    122             
SEQRES   1 A  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 A  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 A  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 A  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 A  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 A  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 A  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR LYS VAL          
SEQRES   8 A  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 A  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 A  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 A  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 A  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 A  157  LEU                                                          
SEQRES   1 B  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 B  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 B  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 B  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 B  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 B  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 B  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR LYS VAL          
SEQRES   8 B  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 B  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 B  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 B  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 B  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 B  157  LEU                                                          
SEQRES   1 C  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 C  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 C  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 C  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 C  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 C  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 C  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR LYS VAL          
SEQRES   8 C  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 C  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 C  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 C  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 C  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 C  157  LEU                                                          
SEQRES   1 D  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 D  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 D  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 D  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 D  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 D  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 D  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR LYS VAL          
SEQRES   8 D  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 D  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 D  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 D  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 D  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 D  157  LEU                                                          
SEQRES   1 E  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 E  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 E  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 E  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 E  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 E  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 E  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR LYS VAL          
SEQRES   8 E  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 E  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 E  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 E  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 E  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 E  157  LEU                                                          
SEQRES   1 F  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 F  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 F  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 F  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 F  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 F  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 F  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR LYS VAL          
SEQRES   8 F  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 F  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 F  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 F  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 F  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 F  157  LEU                                                          
SEQRES   1 G  121  VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN ALA          
SEQRES   2 G  121  GLY GLY SER LEU SER LEU SER CYS SER ALA SER GLY ARG          
SEQRES   3 G  121  SER LEU SER ASN TYR TYR MET GLY TRP PHE ARG GLN ALA          
SEQRES   4 G  121  PRO GLY LYS GLU ARG GLU LEU LEU GLY ASN ILE SER TRP          
SEQRES   5 G  121  ARG GLY TYR ASN ILE TYR TYR LYS ASP SER VAL LYS GLY          
SEQRES   6 G  121  ARG PHE THR ILE SER ARG ASP ASP ALA LYS ASN THR ILE          
SEQRES   7 G  121  TYR LEU GLN MET ASN ARG LEU LYS PRO GLU ASP THR ALA          
SEQRES   8 G  121  VAL TYR TYR CYS ALA ALA SER ILE LEU PRO LEU SER ASP          
SEQRES   9 G  121  ASP PRO GLY TRP ASN THR TYR TRP GLY GLN GLY THR GLN          
SEQRES  10 G  121  VAL THR VAL SER                                              
SEQRES   1 H  121  VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN ALA          
SEQRES   2 H  121  GLY GLY SER LEU SER LEU SER CYS SER ALA SER GLY ARG          
SEQRES   3 H  121  SER LEU SER ASN TYR TYR MET GLY TRP PHE ARG GLN ALA          
SEQRES   4 H  121  PRO GLY LYS GLU ARG GLU LEU LEU GLY ASN ILE SER TRP          
SEQRES   5 H  121  ARG GLY TYR ASN ILE TYR TYR LYS ASP SER VAL LYS GLY          
SEQRES   6 H  121  ARG PHE THR ILE SER ARG ASP ASP ALA LYS ASN THR ILE          
SEQRES   7 H  121  TYR LEU GLN MET ASN ARG LEU LYS PRO GLU ASP THR ALA          
SEQRES   8 H  121  VAL TYR TYR CYS ALA ALA SER ILE LEU PRO LEU SER ASP          
SEQRES   9 H  121  ASP PRO GLY TRP ASN THR TYR TRP GLY GLN GLY THR GLN          
SEQRES  10 H  121  VAL THR VAL SER                                              
SEQRES   1 I  121  VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN ALA          
SEQRES   2 I  121  GLY GLY SER LEU SER LEU SER CYS SER ALA SER GLY ARG          
SEQRES   3 I  121  SER LEU SER ASN TYR TYR MET GLY TRP PHE ARG GLN ALA          
SEQRES   4 I  121  PRO GLY LYS GLU ARG GLU LEU LEU GLY ASN ILE SER TRP          
SEQRES   5 I  121  ARG GLY TYR ASN ILE TYR TYR LYS ASP SER VAL LYS GLY          
SEQRES   6 I  121  ARG PHE THR ILE SER ARG ASP ASP ALA LYS ASN THR ILE          
SEQRES   7 I  121  TYR LEU GLN MET ASN ARG LEU LYS PRO GLU ASP THR ALA          
SEQRES   8 I  121  VAL TYR TYR CYS ALA ALA SER ILE LEU PRO LEU SER ASP          
SEQRES   9 I  121  ASP PRO GLY TRP ASN THR TYR TRP GLY GLN GLY THR GLN          
SEQRES  10 I  121  VAL THR VAL SER                                              
SEQRES   1 J  121  VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN ALA          
SEQRES   2 J  121  GLY GLY SER LEU SER LEU SER CYS SER ALA SER GLY ARG          
SEQRES   3 J  121  SER LEU SER ASN TYR TYR MET GLY TRP PHE ARG GLN ALA          
SEQRES   4 J  121  PRO GLY LYS GLU ARG GLU LEU LEU GLY ASN ILE SER TRP          
SEQRES   5 J  121  ARG GLY TYR ASN ILE TYR TYR LYS ASP SER VAL LYS GLY          
SEQRES   6 J  121  ARG PHE THR ILE SER ARG ASP ASP ALA LYS ASN THR ILE          
SEQRES   7 J  121  TYR LEU GLN MET ASN ARG LEU LYS PRO GLU ASP THR ALA          
SEQRES   8 J  121  VAL TYR TYR CYS ALA ALA SER ILE LEU PRO LEU SER ASP          
SEQRES   9 J  121  ASP PRO GLY TRP ASN THR TYR TRP GLY GLN GLY THR GLN          
SEQRES  10 J  121  VAL THR VAL SER                                              
SEQRES   1 K  121  VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN ALA          
SEQRES   2 K  121  GLY GLY SER LEU SER LEU SER CYS SER ALA SER GLY ARG          
SEQRES   3 K  121  SER LEU SER ASN TYR TYR MET GLY TRP PHE ARG GLN ALA          
SEQRES   4 K  121  PRO GLY LYS GLU ARG GLU LEU LEU GLY ASN ILE SER TRP          
SEQRES   5 K  121  ARG GLY TYR ASN ILE TYR TYR LYS ASP SER VAL LYS GLY          
SEQRES   6 K  121  ARG PHE THR ILE SER ARG ASP ASP ALA LYS ASN THR ILE          
SEQRES   7 K  121  TYR LEU GLN MET ASN ARG LEU LYS PRO GLU ASP THR ALA          
SEQRES   8 K  121  VAL TYR TYR CYS ALA ALA SER ILE LEU PRO LEU SER ASP          
SEQRES   9 K  121  ASP PRO GLY TRP ASN THR TYR TRP GLY GLN GLY THR GLN          
SEQRES  10 K  121  VAL THR VAL SER                                              
SEQRES   1 L  121  VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN ALA          
SEQRES   2 L  121  GLY GLY SER LEU SER LEU SER CYS SER ALA SER GLY ARG          
SEQRES   3 L  121  SER LEU SER ASN TYR TYR MET GLY TRP PHE ARG GLN ALA          
SEQRES   4 L  121  PRO GLY LYS GLU ARG GLU LEU LEU GLY ASN ILE SER TRP          
SEQRES   5 L  121  ARG GLY TYR ASN ILE TYR TYR LYS ASP SER VAL LYS GLY          
SEQRES   6 L  121  ARG PHE THR ILE SER ARG ASP ASP ALA LYS ASN THR ILE          
SEQRES   7 L  121  TYR LEU GLN MET ASN ARG LEU LYS PRO GLU ASP THR ALA          
SEQRES   8 L  121  VAL TYR TYR CYS ALA ALA SER ILE LEU PRO LEU SER ASP          
SEQRES   9 L  121  ASP PRO GLY TRP ASN THR TYR TRP GLY GLN GLY THR GLN          
SEQRES  10 L  121  VAL THR VAL SER                                              
FORMUL  13  HOH   *747(H2 O)                                                    
HELIX    1 AA1 ARG A  138  LEU A  142  5                                   5    
HELIX    2 AA2 ARG B  138  LEU B  142  5                                   5    
HELIX    3 AA3 ARG C  138  LEU C  142  5                                   5    
HELIX    4 AA4 ARG D  138  LEU D  142  5                                   5    
HELIX    5 AA5 ARG E  138  LEU E  142  5                                   5    
HELIX    6 AA6 ARG F  138  LEU F  142  5                                   5    
HELIX    7 AA7 SER G   28  TYR G   32  5                                   5    
HELIX    8 AA8 TRP G   53  TYR G   56  5                                   4    
HELIX    9 AA9 ASP G   62  LYS G   65  5                                   4    
HELIX   10 AB1 LYS G   87  THR G   91  5                                   5    
HELIX   11 AB2 SER H   28  TYR H   32  5                                   5    
HELIX   12 AB3 TRP H   53  TYR H   56  5                                   4    
HELIX   13 AB4 ASP H   62  LYS H   65  5                                   4    
HELIX   14 AB5 LYS H   87  THR H   91  5                                   5    
HELIX   15 AB6 SER I   28  TYR I   32  5                                   5    
HELIX   16 AB7 TRP I   53  TYR I   56  5                                   4    
HELIX   17 AB8 ASP I   62  LYS I   65  5                                   4    
HELIX   18 AB9 LYS I   87  THR I   91  5                                   5    
HELIX   19 AC1 SER J   28  TYR J   32  5                                   5    
HELIX   20 AC2 TRP J   53  TYR J   56  5                                   4    
HELIX   21 AC3 ASP J   62  LYS J   65  5                                   4    
HELIX   22 AC4 LYS J   87  THR J   91  5                                   5    
HELIX   23 AC5 SER K   28  TYR K   32  5                                   5    
HELIX   24 AC6 TRP K   53  TYR K   56  5                                   4    
HELIX   25 AC7 ASP K   62  LYS K   65  5                                   4    
HELIX   26 AC8 LYS K   87  THR K   91  5                                   5    
HELIX   27 AC9 SER L   28  TYR L   32  5                                   5    
HELIX   28 AD1 TRP L   53  TYR L   56  5                                   4    
HELIX   29 AD2 ASP L   62  LYS L   65  5                                   4    
HELIX   30 AD3 LYS L   87  THR L   91  5                                   5    
SHEET    1 AA1 3 TRP A  28  LEU A  29  0                                        
SHEET    2 AA1 3 VAL A  13  ALA A  18 -1  N  VAL A  17   O  LEU A  29           
SHEET    3 AA1 3 LEU A  36  ALA A  38 -1  O  LEU A  36   N  HIS A  15           
SHEET    1 AA2 5 TRP A  28  LEU A  29  0                                        
SHEET    2 AA2 5 VAL A  13  ALA A  18 -1  N  VAL A  17   O  LEU A  29           
SHEET    3 AA2 5 TYR A 151  ALA A 156 -1  O  PHE A 152   N  VAL A  16           
SHEET    4 AA2 5 GLY A  54  GLN A  67 -1  N  TYR A  59   O  GLY A 153           
SHEET    5 AA2 5 PRO A 113  LEU A 126 -1  O  GLY A 122   N  ILE A  58           
SHEET    1 AA3 5 GLU A  42  ARG A  44  0                                        
SHEET    2 AA3 5 GLN A  47  VAL A  49 -1  O  VAL A  49   N  GLU A  42           
SHEET    3 AA3 5 ARG A 131  ILE A 136 -1  O  LEU A 132   N  LEU A  48           
SHEET    4 AA3 5 LEU A  76  ALA A  84 -1  N  THR A  79   O  GLU A 135           
SHEET    5 AA3 5 THR A  89  LYS A  98 -1  O  VAL A  91   N  ARG A  82           
SHEET    1 AA4 3 TRP B  28  LEU B  29  0                                        
SHEET    2 AA4 3 VAL B  13  ALA B  18 -1  N  VAL B  17   O  LEU B  29           
SHEET    3 AA4 3 LEU B  36  ALA B  38 -1  O  LEU B  36   N  HIS B  15           
SHEET    1 AA5 5 TRP B  28  LEU B  29  0                                        
SHEET    2 AA5 5 VAL B  13  ALA B  18 -1  N  VAL B  17   O  LEU B  29           
SHEET    3 AA5 5 TYR B 151  ALA B 156 -1  O  PHE B 152   N  VAL B  16           
SHEET    4 AA5 5 GLY B  54  GLN B  67 -1  N  TYR B  59   O  GLY B 153           
SHEET    5 AA5 5 PRO B 113  LEU B 126 -1  O  GLY B 122   N  ILE B  58           
SHEET    1 AA6 5 GLU B  42  ARG B  44  0                                        
SHEET    2 AA6 5 GLN B  47  VAL B  49 -1  O  VAL B  49   N  GLU B  42           
SHEET    3 AA6 5 ARG B 131  ILE B 136 -1  O  LEU B 132   N  LEU B  48           
SHEET    4 AA6 5 LEU B  76  ALA B  84 -1  N  THR B  79   O  GLU B 135           
SHEET    5 AA6 5 THR B  89  LYS B  98 -1  O  LYS B  98   N  LEU B  76           
SHEET    1 AA7 3 TRP C  28  LEU C  29  0                                        
SHEET    2 AA7 3 VAL C  13  ALA C  18 -1  N  VAL C  17   O  LEU C  29           
SHEET    3 AA7 3 LEU C  36  ALA C  38 -1  O  ALA C  38   N  VAL C  13           
SHEET    1 AA8 5 TRP C  28  LEU C  29  0                                        
SHEET    2 AA8 5 VAL C  13  ALA C  18 -1  N  VAL C  17   O  LEU C  29           
SHEET    3 AA8 5 TYR C 151  ALA C 156 -1  O  PHE C 152   N  VAL C  16           
SHEET    4 AA8 5 GLY C  54  GLN C  67 -1  N  TYR C  59   O  GLY C 153           
SHEET    5 AA8 5 PRO C 113  LEU C 126 -1  O  GLY C 122   N  ILE C  58           
SHEET    1 AA9 5 GLU C  42  ARG C  44  0                                        
SHEET    2 AA9 5 GLN C  47  VAL C  49 -1  O  VAL C  49   N  GLU C  42           
SHEET    3 AA9 5 ARG C 131  ILE C 136 -1  O  LEU C 132   N  LEU C  48           
SHEET    4 AA9 5 LEU C  76  ALA C  84 -1  N  THR C  79   O  GLU C 135           
SHEET    5 AA9 5 THR C  89  LYS C  98 -1  O  LYS C  98   N  LEU C  76           
SHEET    1 AB1 3 TRP D  28  LEU D  29  0                                        
SHEET    2 AB1 3 VAL D  13  ALA D  18 -1  N  VAL D  17   O  LEU D  29           
SHEET    3 AB1 3 LEU D  36  ALA D  38 -1  O  LEU D  36   N  HIS D  15           
SHEET    1 AB2 5 TRP D  28  LEU D  29  0                                        
SHEET    2 AB2 5 VAL D  13  ALA D  18 -1  N  VAL D  17   O  LEU D  29           
SHEET    3 AB2 5 TYR D 151  ALA D 156 -1  O  PHE D 152   N  VAL D  16           
SHEET    4 AB2 5 GLY D  54  GLN D  67 -1  N  TYR D  59   O  GLY D 153           
SHEET    5 AB2 5 PRO D 113  LEU D 126 -1  O  GLY D 122   N  ILE D  58           
SHEET    1 AB3 5 GLU D  42  ARG D  44  0                                        
SHEET    2 AB3 5 GLN D  47  VAL D  49 -1  O  VAL D  49   N  GLU D  42           
SHEET    3 AB3 5 ARG D 131  ILE D 136 -1  O  LEU D 132   N  LEU D  48           
SHEET    4 AB3 5 LEU D  76  ALA D  84 -1  N  THR D  79   O  GLU D 135           
SHEET    5 AB3 5 THR D  89  LYS D  98 -1  O  VAL D  91   N  ARG D  82           
SHEET    1 AB4 3 TRP E  28  LEU E  29  0                                        
SHEET    2 AB4 3 VAL E  13  ALA E  18 -1  N  VAL E  17   O  LEU E  29           
SHEET    3 AB4 3 LEU E  36  ALA E  38 -1  O  ALA E  38   N  VAL E  13           
SHEET    1 AB5 5 TRP E  28  LEU E  29  0                                        
SHEET    2 AB5 5 VAL E  13  ALA E  18 -1  N  VAL E  17   O  LEU E  29           
SHEET    3 AB5 5 TYR E 151  ALA E 156 -1  O  PHE E 152   N  VAL E  16           
SHEET    4 AB5 5 GLY E  54  GLN E  67 -1  N  TYR E  59   O  GLY E 153           
SHEET    5 AB5 5 PRO E 113  LEU E 126 -1  O  GLY E 122   N  ILE E  58           
SHEET    1 AB6 5 GLU E  42  ARG E  44  0                                        
SHEET    2 AB6 5 GLN E  47  VAL E  49 -1  O  VAL E  49   N  GLU E  42           
SHEET    3 AB6 5 ARG E 131  ILE E 136 -1  O  LEU E 132   N  LEU E  48           
SHEET    4 AB6 5 LEU E  76  ALA E  84 -1  N  THR E  79   O  GLU E 135           
SHEET    5 AB6 5 THR E  89  LYS E  98 -1  O  LYS E  98   N  LEU E  76           
SHEET    1 AB7 3 TRP F  28  LEU F  29  0                                        
SHEET    2 AB7 3 VAL F  13  ALA F  18 -1  N  VAL F  17   O  LEU F  29           
SHEET    3 AB7 3 LEU F  36  ALA F  38 -1  O  ALA F  38   N  VAL F  13           
SHEET    1 AB8 5 TRP F  28  LEU F  29  0                                        
SHEET    2 AB8 5 VAL F  13  ALA F  18 -1  N  VAL F  17   O  LEU F  29           
SHEET    3 AB8 5 TYR F 151  ALA F 156 -1  O  PHE F 152   N  VAL F  16           
SHEET    4 AB8 5 GLY F  54  GLN F  67 -1  N  TYR F  59   O  GLY F 153           
SHEET    5 AB8 5 PRO F 113  LEU F 126 -1  O  GLY F 122   N  ILE F  58           
SHEET    1 AB9 5 GLU F  42  ARG F  44  0                                        
SHEET    2 AB9 5 GLN F  47  VAL F  49 -1  O  VAL F  49   N  GLU F  42           
SHEET    3 AB9 5 ARG F 131  ILE F 136 -1  O  LEU F 132   N  LEU F  48           
SHEET    4 AB9 5 LEU F  76  ALA F  84 -1  N  THR F  79   O  GLU F 135           
SHEET    5 AB9 5 THR F  89  LYS F  98 -1  O  LYS F  98   N  LEU F  76           
SHEET    1 AC1 4 GLN G   3  SER G   7  0                                        
SHEET    2 AC1 4 LEU G  18  SER G  25 -1  O  SER G  21   N  SER G   7           
SHEET    3 AC1 4 THR G  78  MET G  83 -1  O  MET G  83   N  LEU G  18           
SHEET    4 AC1 4 PHE G  68  ASP G  73 -1  N  THR G  69   O  GLN G  82           
SHEET    1 AC2 6 GLY G  10  VAL G  12  0                                        
SHEET    2 AC2 6 THR G 117  VAL G 121  1  O  THR G 120   N  GLY G  10           
SHEET    3 AC2 6 ALA G  92  SER G  99 -1  N  TYR G  94   O  THR G 117           
SHEET    4 AC2 6 TYR G  33  GLN G  39 -1  N  TYR G  33   O  SER G  99           
SHEET    5 AC2 6 GLU G  46  ILE G  51 -1  O  ILE G  51   N  MET G  34           
SHEET    6 AC2 6 ILE G  58  TYR G  60 -1  O  TYR G  59   N  ASN G  50           
SHEET    1 AC3 4 GLY G  10  VAL G  12  0                                        
SHEET    2 AC3 4 THR G 117  VAL G 121  1  O  THR G 120   N  GLY G  10           
SHEET    3 AC3 4 ALA G  92  SER G  99 -1  N  TYR G  94   O  THR G 117           
SHEET    4 AC3 4 THR G 111  TRP G 113 -1  O  TYR G 112   N  ALA G  98           
SHEET    1 AC4 4 GLN H   3  SER H   7  0                                        
SHEET    2 AC4 4 LEU H  18  SER H  25 -1  O  SER H  23   N  VAL H   5           
SHEET    3 AC4 4 THR H  78  MET H  83 -1  O  MET H  83   N  LEU H  18           
SHEET    4 AC4 4 PHE H  68  ASP H  73 -1  N  ASP H  73   O  THR H  78           
SHEET    1 AC5 6 GLY H  10  VAL H  12  0                                        
SHEET    2 AC5 6 THR H 117  VAL H 121  1  O  THR H 120   N  GLY H  10           
SHEET    3 AC5 6 ALA H  92  SER H  99 -1  N  TYR H  94   O  THR H 117           
SHEET    4 AC5 6 TYR H  33  GLN H  39 -1  N  TYR H  33   O  SER H  99           
SHEET    5 AC5 6 GLU H  46  ILE H  51 -1  O  ILE H  51   N  MET H  34           
SHEET    6 AC5 6 ILE H  58  TYR H  60 -1  O  TYR H  59   N  ASN H  50           
SHEET    1 AC6 4 GLY H  10  VAL H  12  0                                        
SHEET    2 AC6 4 THR H 117  VAL H 121  1  O  THR H 120   N  GLY H  10           
SHEET    3 AC6 4 ALA H  92  SER H  99 -1  N  TYR H  94   O  THR H 117           
SHEET    4 AC6 4 THR H 111  TRP H 113 -1  O  TYR H 112   N  ALA H  98           
SHEET    1 AC7 4 GLN I   3  SER I   7  0                                        
SHEET    2 AC7 4 LEU I  18  SER I  25 -1  O  SER I  23   N  VAL I   5           
SHEET    3 AC7 4 THR I  78  MET I  83 -1  O  MET I  83   N  LEU I  18           
SHEET    4 AC7 4 PHE I  68  ASP I  73 -1  N  THR I  69   O  GLN I  82           
SHEET    1 AC8 6 GLY I  10  VAL I  12  0                                        
SHEET    2 AC8 6 THR I 117  VAL I 121  1  O  GLN I 118   N  GLY I  10           
SHEET    3 AC8 6 ALA I  92  SER I  99 -1  N  TYR I  94   O  THR I 117           
SHEET    4 AC8 6 TYR I  33  GLN I  39 -1  N  TYR I  33   O  SER I  99           
SHEET    5 AC8 6 GLU I  46  ILE I  51 -1  O  LEU I  48   N  TRP I  36           
SHEET    6 AC8 6 ILE I  58  TYR I  60 -1  O  TYR I  59   N  ASN I  50           
SHEET    1 AC9 4 GLY I  10  VAL I  12  0                                        
SHEET    2 AC9 4 THR I 117  VAL I 121  1  O  GLN I 118   N  GLY I  10           
SHEET    3 AC9 4 ALA I  92  SER I  99 -1  N  TYR I  94   O  THR I 117           
SHEET    4 AC9 4 THR I 111  TRP I 113 -1  O  TYR I 112   N  ALA I  98           
SHEET    1 AD1 4 GLN J   3  SER J   7  0                                        
SHEET    2 AD1 4 LEU J  18  SER J  25 -1  O  SER J  21   N  SER J   7           
SHEET    3 AD1 4 THR J  78  MET J  83 -1  O  MET J  83   N  LEU J  18           
SHEET    4 AD1 4 PHE J  68  ASP J  73 -1  N  THR J  69   O  GLN J  82           
SHEET    1 AD2 6 GLY J  10  VAL J  12  0                                        
SHEET    2 AD2 6 THR J 117  VAL J 121  1  O  THR J 120   N  VAL J  12           
SHEET    3 AD2 6 ALA J  92  SER J  99 -1  N  TYR J  94   O  THR J 117           
SHEET    4 AD2 6 TYR J  33  GLN J  39 -1  N  TYR J  33   O  SER J  99           
SHEET    5 AD2 6 GLU J  46  ILE J  51 -1  O  LEU J  48   N  TRP J  36           
SHEET    6 AD2 6 ILE J  58  TYR J  60 -1  O  TYR J  59   N  ASN J  50           
SHEET    1 AD3 4 GLY J  10  VAL J  12  0                                        
SHEET    2 AD3 4 THR J 117  VAL J 121  1  O  THR J 120   N  VAL J  12           
SHEET    3 AD3 4 ALA J  92  SER J  99 -1  N  TYR J  94   O  THR J 117           
SHEET    4 AD3 4 THR J 111  TRP J 113 -1  O  TYR J 112   N  ALA J  98           
SHEET    1 AD4 4 GLN K   3  SER K   7  0                                        
SHEET    2 AD4 4 LEU K  18  SER K  25 -1  O  SER K  23   N  VAL K   5           
SHEET    3 AD4 4 THR K  78  MET K  83 -1  O  MET K  83   N  LEU K  18           
SHEET    4 AD4 4 PHE K  68  ASP K  73 -1  N  ASP K  73   O  THR K  78           
SHEET    1 AD5 6 GLY K  10  VAL K  12  0                                        
SHEET    2 AD5 6 THR K 117  VAL K 121  1  O  THR K 120   N  GLY K  10           
SHEET    3 AD5 6 ALA K  92  SER K  99 -1  N  TYR K  94   O  THR K 117           
SHEET    4 AD5 6 TYR K  33  GLN K  39 -1  N  TYR K  33   O  SER K  99           
SHEET    5 AD5 6 GLU K  46  ILE K  51 -1  O  ILE K  51   N  MET K  34           
SHEET    6 AD5 6 ILE K  58  TYR K  60 -1  O  TYR K  59   N  ASN K  50           
SHEET    1 AD6 4 GLY K  10  VAL K  12  0                                        
SHEET    2 AD6 4 THR K 117  VAL K 121  1  O  THR K 120   N  GLY K  10           
SHEET    3 AD6 4 ALA K  92  SER K  99 -1  N  TYR K  94   O  THR K 117           
SHEET    4 AD6 4 THR K 111  TRP K 113 -1  O  TYR K 112   N  ALA K  98           
SHEET    1 AD7 4 GLN L   3  SER L   7  0                                        
SHEET    2 AD7 4 LEU L  18  SER L  25 -1  O  SER L  23   N  VAL L   5           
SHEET    3 AD7 4 THR L  78  MET L  83 -1  O  MET L  83   N  LEU L  18           
SHEET    4 AD7 4 PHE L  68  ASP L  73 -1  N  THR L  69   O  GLN L  82           
SHEET    1 AD8 6 GLY L  10  VAL L  12  0                                        
SHEET    2 AD8 6 THR L 117  VAL L 121  1  O  GLN L 118   N  GLY L  10           
SHEET    3 AD8 6 ALA L  92  SER L  99 -1  N  TYR L  94   O  THR L 117           
SHEET    4 AD8 6 TYR L  33  GLN L  39 -1  N  TYR L  33   O  SER L  99           
SHEET    5 AD8 6 GLU L  46  ILE L  51 -1  O  LEU L  48   N  TRP L  36           
SHEET    6 AD8 6 ILE L  58  TYR L  60 -1  O  TYR L  59   N  ASN L  50           
SHEET    1 AD9 4 GLY L  10  VAL L  12  0                                        
SHEET    2 AD9 4 THR L 117  VAL L 121  1  O  GLN L 118   N  GLY L  10           
SHEET    3 AD9 4 ALA L  92  SER L  99 -1  N  TYR L  94   O  THR L 117           
SHEET    4 AD9 4 THR L 111  TRP L 113 -1  O  TYR L 112   N  ALA L  98           
SSBOND   1 CYS A   69    CYS A  101                          1555   1555  2.04  
SSBOND   2 CYS B   69    CYS B  101                          1555   1555  2.04  
SSBOND   3 CYS C   69    CYS C  101                          1555   1555  2.05  
SSBOND   4 CYS D   69    CYS D  101                          1555   1555  2.03  
SSBOND   5 CYS E   69    CYS E  101                          1555   1555  2.04  
SSBOND   6 CYS F   69    CYS F  101                          1555   1555  2.05  
SSBOND   7 CYS G   22    CYS G   96                          1555   1555  2.05  
SSBOND   8 CYS H   22    CYS H   96                          1555   1555  2.04  
SSBOND   9 CYS I   22    CYS I   96                          1555   1555  2.03  
SSBOND  10 CYS J   22    CYS J   96                          1555   1555  2.05  
SSBOND  11 CYS K   22    CYS K   96                          1555   1555  2.04  
SSBOND  12 CYS L   22    CYS L   96                          1555   1555  2.03  
CRYST1  110.330  117.410  141.890  90.00  90.00  90.00 P 21 21 21   24          
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      0.009064  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008517  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007048        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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