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Database: PDB
Entry: 5M2M
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Original site: 5M2M 
HEADER    CYTOKINE                                13-OCT-16   5M2M              
TITLE     COMPLEX BETWEEN HUMAN TNF ALPHA AND LLAMA VHH3                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR;                                     
COMPND   3 CHAIN: A, B, C, G, I, M;                                             
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: LLAMA NANOBODY VHH3;                                       
COMPND   9 CHAIN: D, E, F, H, J, N;                                             
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_TAXID: 9844;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 511693                                      
KEYWDS    HUMAN TNF ALPHA, LLAMA NANOBODY, CYTOKINE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.CAMBILLAU,S.SPINELLI,A.DESMYTER,H.DE HAARD                          
REVDAT   2   06-SEP-17 5M2M    1       JRNL                                     
REVDAT   1   30-AUG-17 5M2M    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.    2.30 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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.59                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 62613                          
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)  : 0.213                          
REMARK   3   R VALUE            (WORKING SET)  : 0.211                          
REMARK   3   FREE R VALUE                      : 0.248                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.160                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3229                           
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) : 2.30                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.36                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.98                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 4594                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2126                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 4363                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2109                   
REMARK   3   BIN FREE R VALUE                        : 0.2447                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.03                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 231                      
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            : 12805                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 711                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.04                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.06                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.70620                                              
REMARK   3    B22 (A**2) : -5.39790                                             
REMARK   3    B33 (A**2) : 1.69170                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.70100                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.396               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.622               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.261               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.610               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.264               
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      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 13110  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 17843  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 4338   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 314    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1929   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 13110  ; 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   : 1675   ; 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   : 14630  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.11                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.10                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 23.16                    
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):  -11.3716   -3.4466   62.4341           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0286 T22:   -0.3040                                    
REMARK   3     T33:    0.1218 T12:    0.0770                                    
REMARK   3     T13:    0.0161 T23:   -0.0053                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.2703 L22:    0.1724                                    
REMARK   3     L33:    1.5319 L12:    1.2014                                    
REMARK   3     L13:   -0.7485 L23:   -0.2723                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0124 S12:    0.0511 S13:   -0.0804                     
REMARK   3     S21:    0.0866 S22:   -0.0151 S23:   -0.0940                     
REMARK   3     S31:    0.0340 S32:    0.0489 S33:    0.0275                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -32.8997   -5.7967   62.1030           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0294 T22:   -0.3040                                    
REMARK   3     T33:    0.1159 T12:   -0.0105                                    
REMARK   3     T13:    0.0060 T23:   -0.0377                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.4369 L22:    2.1049                                    
REMARK   3     L33:    2.4141 L12:   -0.1578                                    
REMARK   3     L13:    0.6764 L23:    0.8532                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0222 S12:   -0.1761 S13:   -0.0326                     
REMARK   3     S21:   -0.0645 S22:   -0.0150 S23:    0.0882                     
REMARK   3     S31:    0.0162 S32:   -0.0899 S33:    0.0371                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -24.2337   14.1139   62.2129           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0177 T22:   -0.3040                                    
REMARK   3     T33:    0.1102 T12:   -0.0313                                    
REMARK   3     T13:   -0.0030 T23:   -0.0111                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.4647 L22:    0.7986                                    
REMARK   3     L33:    2.8891 L12:   -0.8764                                    
REMARK   3     L13:    0.4344 L23:   -0.3379                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0786 S12:   -0.0647 S13:    0.0567                     
REMARK   3     S21:    0.0038 S22:   -0.0684 S23:   -0.0189                     
REMARK   3     S31:   -0.0598 S32:    0.0172 S33:   -0.0102                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -35.1076  -26.5489   40.7932           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0326 T22:   -0.2910                                    
REMARK   3     T33:    0.1218 T12:   -0.0355                                    
REMARK   3     T13:    0.0408 T23:   -0.0179                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.2969 L22:    2.2900                                    
REMARK   3     L33:    2.3580 L12:   -1.5120                                    
REMARK   3     L13:    1.0713 L23:    0.6743                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0034 S12:    0.0838 S13:   -0.0147                     
REMARK   3     S21:   -0.0325 S22:   -0.0423 S23:    0.0705                     
REMARK   3     S31:   -0.0132 S32:   -0.0591 S33:    0.0457                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { E|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -40.8997   26.4330   40.6153           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0163 T22:   -0.2726                                    
REMARK   3     T33:    0.1374 T12:   -0.0224                                    
REMARK   3     T13:    0.0074 T23:    0.0224                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1236 L22:    1.6008                                    
REMARK   3     L33:    2.5832 L12:   -0.1453                                    
REMARK   3     L13:    0.6182 L23:   -1.2955                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0240 S12:    0.1107 S13:    0.0551                     
REMARK   3     S21:   -0.0256 S22:    0.0721 S23:    0.0717                     
REMARK   3     S31:    0.0179 S32:    0.0089 S33:   -0.0481                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { F|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    7.8090    4.9896   40.8240           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0323 T22:   -0.2557                                    
REMARK   3     T33:    0.1294 T12:   -0.0019                                    
REMARK   3     T13:    0.0149 T23:    0.0488                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2743 L22:    2.5715                                    
REMARK   3     L33:    1.9522 L12:    0.4689                                    
REMARK   3     L13:   -0.9439 L23:    0.4896                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0271 S12:    0.1016 S13:   -0.0415                     
REMARK   3     S21:   -0.0667 S22:   -0.0263 S23:   -0.0276                     
REMARK   3     S31:    0.0199 S32:    0.0909 S33:    0.0534                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { G|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   14.0794   35.8148    3.7986           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2730 T22:    0.3040                                    
REMARK   3     T33:   -0.3349 T12:    0.0071                                    
REMARK   3     T13:   -0.0068 T23:   -0.0315                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.3011 L22:    0.3897                                    
REMARK   3     L33:    1.2279 L12:   -0.2142                                    
REMARK   3     L13:    0.2127 L23:    0.6427                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0108 S12:   -0.0649 S13:    0.0053                     
REMARK   3     S21:   -0.0201 S22:    0.0088 S23:    0.0587                     
REMARK   3     S31:    0.0069 S32:   -0.0106 S33:    0.0020                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: { H|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   11.8876   15.1586  -17.6858           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2581 T22:    0.3040                                    
REMARK   3     T33:   -0.2130 T12:   -0.0134                                    
REMARK   3     T13:   -0.0059 T23:    0.0372                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9828 L22:    1.1834                                    
REMARK   3     L33:    2.2439 L12:   -1.2564                                    
REMARK   3     L13:    0.4232 L23:    1.1947                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0015 S12:   -0.0319 S13:   -0.0066                     
REMARK   3     S21:   -0.0400 S22:   -0.0379 S23:    0.0545                     
REMARK   3     S31:   -0.0217 S32:    0.0292 S33:    0.0394                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: { I|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   35.5586   38.2153    3.7482           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2644 T22:    0.3040                                    
REMARK   3     T33:   -0.3207 T12:   -0.0041                                    
REMARK   3     T13:   -0.0033 T23:    0.0120                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.5539 L22:    0.3052                                    
REMARK   3     L33:    2.0841 L12:   -0.0345                                    
REMARK   3     L13:   -0.1807 L23:   -0.8976                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0134 S12:   -0.0765 S13:   -0.0387                     
REMARK   3     S21:    0.0171 S22:    0.0020 S23:   -0.0414                     
REMARK   3     S31:    0.0401 S32:    0.0062 S33:   -0.0155                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: { J|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   54.7986   46.6130  -17.6826           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2543 T22:    0.3040                                    
REMARK   3     T33:   -0.1824 T12:    0.0382                                    
REMARK   3     T13:   -0.0184 T23:   -0.0560                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.3661 L22:    0.6608                                    
REMARK   3     L33:    2.1704 L12:    0.9732                                    
REMARK   3     L13:    0.0537 L23:    0.2157                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0037 S12:   -0.0503 S13:   -0.0366                     
REMARK   3     S21:   -0.0619 S22:    0.0036 S23:   -0.0356                     
REMARK   3     S31:    0.0525 S32:   -0.0223 S33:    0.0001                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: { M|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   22.7813   55.9018    4.1362           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2759 T22:    0.3040                                    
REMARK   3     T33:   -0.3257 T12:    0.0232                                    
REMARK   3     T13:   -0.0087 T23:   -0.0465                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.3612 L22:    0.2826                                    
REMARK   3     L33:    3.1218 L12:   -0.8975                                    
REMARK   3     L13:   -0.5665 L23:    0.1245                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0033 S12:   -0.0325 S13:    0.0391                     
REMARK   3     S21:   -0.0020 S22:    0.0005 S23:   -0.0093                     
REMARK   3     S31:   -0.0260 S32:   -0.0329 S33:   -0.0038                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: { N|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    6.0125   68.1998  -17.8746           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2865 T22:    0.3040                                    
REMARK   3     T33:   -0.2301 T12:   -0.0487                                    
REMARK   3     T13:   -0.0240 T23:    0.0197                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.0998 L22:    0.1775                                    
REMARK   3     L33:    5.2670 L12:   -0.2651                                    
REMARK   3     L13:   -0.0452 L23:   -1.0893                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0131 S12:   -0.0256 S13:    0.0229                     
REMARK   3     S21:   -0.0476 S22:    0.0201 S23:    0.0550                     
REMARK   3     S31:   -0.0101 S32:    0.0429 S33:   -0.0070                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5M2M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-OCT-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001810.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7 - 9                              
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.931                              
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   : 62613                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.100                              
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: 5M2I                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MIXING 100 TO 300 NL OF PROTEIN (9 MG    
REMARK 280  PER ML IN HEPES 10 MM PH 7.0) WITH 100 NL OF PRECIPITANT            
REMARK 280  SOLUTION CONTAINING: 9% PEG3350, 8% PEG-MME550, 130 MM NASO4, 70    
REMARK 280  MM BTP, 30 MM MES, AND 3 MM ZNSO4, 8.5, VAPOR DIFFUSION, SITTING    
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       72.69000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.92200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       72.69000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       41.92200            
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, M, N                      
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    72                                                      
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     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     SER C    71                                                      
REMARK 465     GLN D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 465     GLN E     1                                                      
REMARK 465     VAL E     2                                                      
REMARK 465     GLN F     1                                                      
REMARK 465     VAL F     2                                                      
REMARK 465     VAL G     1                                                      
REMARK 465     ARG G     2                                                      
REMARK 465     SER G     3                                                      
REMARK 465     SER G     4                                                      
REMARK 465     SER G     5                                                      
REMARK 465     ARG G     6                                                      
REMARK 465     SER G    71                                                      
REMARK 465     GLN H     1                                                      
REMARK 465     VAL H     2                                                      
REMARK 465     VAL I     1                                                      
REMARK 465     ARG I     2                                                      
REMARK 465     SER I     3                                                      
REMARK 465     SER I     4                                                      
REMARK 465     SER I     5                                                      
REMARK 465     ARG I     6                                                      
REMARK 465     THR I    72                                                      
REMARK 465     GLN J     1                                                      
REMARK 465     VAL J     2                                                      
REMARK 465     VAL M     1                                                      
REMARK 465     ARG M     2                                                      
REMARK 465     SER M     3                                                      
REMARK 465     SER M     4                                                      
REMARK 465     SER M     5                                                      
REMARK 465     ARG M     6                                                      
REMARK 465     SER M    71                                                      
REMARK 465     THR M    72                                                      
REMARK 465     TYR M   141                                                      
REMARK 465     GLN N     1                                                      
REMARK 465     VAL N     2                                                      
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     GLN A 102    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 107    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 110    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 112    CG   CD   CE   NZ                                   
REMARK 470     GLN B 102    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 107    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 110    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 102    CG   CD   OE1  NE2                                  
REMARK 470     ARG C 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 107    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 110    CG   CD   OE1  OE2                                  
REMARK 470     GLN G 102    CG   CD   OE1  NE2                                  
REMARK 470     ARG G 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU G 107    CG   CD   OE1  OE2                                  
REMARK 470     GLU G 110    CG   CD   OE1  OE2                                  
REMARK 470     ARG I 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU I 110    CG   CD   OE1  OE2                                  
REMARK 470     LYS I 112    CG   CD   CE   NZ                                   
REMARK 470     GLN M 102    CG   CD   OE1  NE2                                  
REMARK 470     ARG M 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU M 107    CG   CD   OE1  OE2                                  
REMARK 470     GLU M 110    CG   CD   OE1  OE2                                  
REMARK 470     LYS M 112    CG   CD   CE   NZ                                   
REMARK 470     ARG N  27    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       95.54   -166.57                                   
REMARK 500    ARG A  44      -77.69    -99.78                                   
REMARK 500    ASP A  45       61.47   -112.09                                   
REMARK 500    GLN A  88       -6.01     67.14                                   
REMARK 500    GLU A 107      -48.73    -21.59                                   
REMARK 500    LEU B  37       95.27   -165.36                                   
REMARK 500    ARG B  44      -79.88   -100.13                                   
REMARK 500    ASP B  45       63.82   -111.36                                   
REMARK 500    GLN B  88       -5.70     66.90                                   
REMARK 500    GLU B 107      -53.25    -20.40                                   
REMARK 500    LEU C  37       95.86   -167.30                                   
REMARK 500    ARG C  44      -78.66   -100.34                                   
REMARK 500    ASP C  45       62.56   -111.95                                   
REMARK 500    GLN C  88       -6.18     66.94                                   
REMARK 500    GLU C 107      -50.02    -23.31                                   
REMARK 500    ARG G  31       47.03    -87.98                                   
REMARK 500    LEU G  37       94.63   -167.52                                   
REMARK 500    ARG G  44      -78.94   -100.35                                   
REMARK 500    ASP G  45       62.20   -110.32                                   
REMARK 500    GLN G  88       -5.84     67.12                                   
REMARK 500    GLU G 107      -54.55    -20.85                                   
REMARK 500    LEU I  37       94.44   -167.34                                   
REMARK 500    ARG I  44      -79.26   -100.13                                   
REMARK 500    ASP I  45       62.73   -110.37                                   
REMARK 500    SER I  71     -126.37   -168.35                                   
REMARK 500    GLN I  88       -5.95     66.88                                   
REMARK 500    GLU I 107      102.20    -54.49                                   
REMARK 500    LEU M  37       94.57   -167.31                                   
REMARK 500    ARG M  44      -78.73   -100.27                                   
REMARK 500    ASP M  45       62.45   -110.83                                   
REMARK 500    GLN M  88       -5.68     67.02                                   
REMARK 500    CYS M 101     -178.22     66.27                                   
REMARK 500    GLN M 102      -49.93   -160.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH E 288        DISTANCE =  6.04 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5M2I   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5M2J   RELATED DB: PDB                                   
DBREF  5M2M A    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5M2M B    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5M2M C    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5M2M D    1   129  PDB    5M2M     5M2M             1    129             
DBREF  5M2M E    1   129  PDB    5M2M     5M2M             1    129             
DBREF  5M2M F    1   129  PDB    5M2M     5M2M             1    129             
DBREF  5M2M G    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5M2M H    1   129  PDB    5M2M     5M2M             1    129             
DBREF  5M2M I    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5M2M J    1   129  PDB    5M2M     5M2M             1    129             
DBREF  5M2M M    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5M2M N    1   129  PDB    5M2M     5M2M             1    129             
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  129  GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 D  129  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 D  129  ARG THR PHE SER ASP HIS SER GLY TYR THR TYR THR ILE          
SEQRES   4 D  129  GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE          
SEQRES   5 D  129  VAL ALA ARG ILE TYR TRP SER SER GLY ASN THR TYR TYR          
SEQRES   6 D  129  ALA ASP SER VAL LYS GLY ARG PHE ALA ILE SER ARG ASP          
SEQRES   7 D  129  ILE ALA LYS ASN THR VAL ASP LEU THR MET ASN ASN LEU          
SEQRES   8 D  129  GLU PRO GLU ASP THR ALA VAL TYR TYR CYS ALA ALA ARG          
SEQRES   9 D  129  ASP GLY ILE PRO THR SER ARG SER VAL GLU SER TYR ASN          
SEQRES  10 D  129  TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER              
SEQRES   1 E  129  GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 E  129  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 E  129  ARG THR PHE SER ASP HIS SER GLY TYR THR TYR THR ILE          
SEQRES   4 E  129  GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE          
SEQRES   5 E  129  VAL ALA ARG ILE TYR TRP SER SER GLY ASN THR TYR TYR          
SEQRES   6 E  129  ALA ASP SER VAL LYS GLY ARG PHE ALA ILE SER ARG ASP          
SEQRES   7 E  129  ILE ALA LYS ASN THR VAL ASP LEU THR MET ASN ASN LEU          
SEQRES   8 E  129  GLU PRO GLU ASP THR ALA VAL TYR TYR CYS ALA ALA ARG          
SEQRES   9 E  129  ASP GLY ILE PRO THR SER ARG SER VAL GLU SER TYR ASN          
SEQRES  10 E  129  TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER              
SEQRES   1 F  129  GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 F  129  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 F  129  ARG THR PHE SER ASP HIS SER GLY TYR THR TYR THR ILE          
SEQRES   4 F  129  GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE          
SEQRES   5 F  129  VAL ALA ARG ILE TYR TRP SER SER GLY ASN THR TYR TYR          
SEQRES   6 F  129  ALA ASP SER VAL LYS GLY ARG PHE ALA ILE SER ARG ASP          
SEQRES   7 F  129  ILE ALA LYS ASN THR VAL ASP LEU THR MET ASN ASN LEU          
SEQRES   8 F  129  GLU PRO GLU ASP THR ALA VAL TYR TYR CYS ALA ALA ARG          
SEQRES   9 F  129  ASP GLY ILE PRO THR SER ARG SER VAL GLU SER TYR ASN          
SEQRES  10 F  129  TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER              
SEQRES   1 G  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 G  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 G  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 G  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 G  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 G  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 G  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR LYS VAL          
SEQRES   8 G  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 G  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 G  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 G  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 G  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 G  157  LEU                                                          
SEQRES   1 H  129  GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 H  129  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 H  129  ARG THR PHE SER ASP HIS SER GLY TYR THR TYR THR ILE          
SEQRES   4 H  129  GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE          
SEQRES   5 H  129  VAL ALA ARG ILE TYR TRP SER SER GLY ASN THR TYR TYR          
SEQRES   6 H  129  ALA ASP SER VAL LYS GLY ARG PHE ALA ILE SER ARG ASP          
SEQRES   7 H  129  ILE ALA LYS ASN THR VAL ASP LEU THR MET ASN ASN LEU          
SEQRES   8 H  129  GLU PRO GLU ASP THR ALA VAL TYR TYR CYS ALA ALA ARG          
SEQRES   9 H  129  ASP GLY ILE PRO THR SER ARG SER VAL GLU SER TYR ASN          
SEQRES  10 H  129  TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER              
SEQRES   1 I  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 I  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 I  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 I  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 I  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 I  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 I  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR LYS VAL          
SEQRES   8 I  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 I  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 I  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 I  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 I  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 I  157  LEU                                                          
SEQRES   1 J  129  GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 J  129  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 J  129  ARG THR PHE SER ASP HIS SER GLY TYR THR TYR THR ILE          
SEQRES   4 J  129  GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE          
SEQRES   5 J  129  VAL ALA ARG ILE TYR TRP SER SER GLY ASN THR TYR TYR          
SEQRES   6 J  129  ALA ASP SER VAL LYS GLY ARG PHE ALA ILE SER ARG ASP          
SEQRES   7 J  129  ILE ALA LYS ASN THR VAL ASP LEU THR MET ASN ASN LEU          
SEQRES   8 J  129  GLU PRO GLU ASP THR ALA VAL TYR TYR CYS ALA ALA ARG          
SEQRES   9 J  129  ASP GLY ILE PRO THR SER ARG SER VAL GLU SER TYR ASN          
SEQRES  10 J  129  TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER              
SEQRES   1 M  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 M  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 M  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 M  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 M  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 M  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 M  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR LYS VAL          
SEQRES   8 M  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 M  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 M  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 M  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 M  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 M  157  LEU                                                          
SEQRES   1 N  129  GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 N  129  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 N  129  ARG THR PHE SER ASP HIS SER GLY TYR THR TYR THR ILE          
SEQRES   4 N  129  GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE          
SEQRES   5 N  129  VAL ALA ARG ILE TYR TRP SER SER GLY ASN THR TYR TYR          
SEQRES   6 N  129  ALA ASP SER VAL LYS GLY ARG PHE ALA ILE SER ARG ASP          
SEQRES   7 N  129  ILE ALA LYS ASN THR VAL ASP LEU THR MET ASN ASN LEU          
SEQRES   8 N  129  GLU PRO GLU ASP THR ALA VAL TYR TYR CYS ALA ALA ARG          
SEQRES   9 N  129  ASP GLY ILE PRO THR SER ARG SER VAL GLU SER TYR ASN          
SEQRES  10 N  129  TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER              
FORMUL  13  HOH   *711(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 GLU D   92  THR D   96  5                                   5    
HELIX    5 AA5 SER D  112  TYR D  116  5                                   5    
HELIX    6 AA6 GLU E   92  THR E   96  5                                   5    
HELIX    7 AA7 SER E  112  TYR E  116  5                                   5    
HELIX    8 AA8 GLU F   92  THR F   96  5                                   5    
HELIX    9 AA9 SER F  112  TYR F  116  5                                   5    
HELIX   10 AB1 ARG G  138  LEU G  142  5                                   5    
HELIX   11 AB2 GLU H   92  THR H   96  5                                   5    
HELIX   12 AB3 SER H  112  TYR H  116  5                                   5    
HELIX   13 AB4 ARG I  138  LEU I  142  5                                   5    
HELIX   14 AB5 GLU J   92  THR J   96  5                                   5    
HELIX   15 AB6 SER J  112  TYR J  116  5                                   5    
HELIX   16 AB7 GLU N   92  THR N   96  5                                   5    
HELIX   17 AB8 SER N  112  TYR N  116  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  LEU A 120   N  SER A  60           
SHEET    1 AA3 5 GLU A  42  LEU A  43  0                                        
SHEET    2 AA3 5 LEU A  48  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  ILE A  83 -1  N  ILE A  83   O  ARG A 131           
SHEET    5 AA3 5 LYS A  90  LYS A  98 -1  O  LEU A  93   N  ILE A  80           
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  LEU B  43  0                                        
SHEET    2 AA6 5 LEU B  48  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  ILE B  83 -1  N  ILE B  83   O  ARG B 131           
SHEET    5 AA6 5 LYS B  90  LYS B  98 -1  O  LEU B  94   N  ILE B  80           
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  LEU C  36   N  HIS C  15           
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  LEU C  43  0                                        
SHEET    2 AA9 5 LEU C  48  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  ILE C  83 -1  N  ILE C  83   O  ARG C 131           
SHEET    5 AA9 5 LYS C  90  LYS C  98 -1  O  LYS C  98   N  LEU C  76           
SHEET    1 AB1 4 LEU D   4  SER D   7  0                                        
SHEET    2 AB1 4 LEU D  18  ALA D  24 -1  O  SER D  21   N  SER D   7           
SHEET    3 AB1 4 THR D  83  MET D  88 -1  O  MET D  88   N  LEU D  18           
SHEET    4 AB1 4 PHE D  73  ASP D  78 -1  N  ASP D  78   O  THR D  83           
SHEET    1 AB2 6 GLY D  10  VAL D  12  0                                        
SHEET    2 AB2 6 THR D 123  VAL D 127  1  O  THR D 126   N  GLY D  10           
SHEET    3 AB2 6 ALA D  97  ASP D 105 -1  N  TYR D  99   O  THR D 123           
SHEET    4 AB2 6 TYR D  37  GLN D  44 -1  N  GLY D  40   O  ALA D 102           
SHEET    5 AB2 6 GLU D  51  TYR D  57 -1  O  GLU D  51   N  ARG D  43           
SHEET    6 AB2 6 THR D  63  TYR D  65 -1  O  TYR D  64   N  ARG D  55           
SHEET    1 AB3 4 GLY D  10  VAL D  12  0                                        
SHEET    2 AB3 4 THR D 123  VAL D 127  1  O  THR D 126   N  GLY D  10           
SHEET    3 AB3 4 ALA D  97  ASP D 105 -1  N  TYR D  99   O  THR D 123           
SHEET    4 AB3 4 TYR D 118  TRP D 119 -1  O  TYR D 118   N  ALA D 103           
SHEET    1 AB4 4 LEU E   4  SER E   7  0                                        
SHEET    2 AB4 4 LEU E  18  ALA E  24 -1  O  ALA E  23   N  GLN E   5           
SHEET    3 AB4 4 THR E  83  MET E  88 -1  O  MET E  88   N  LEU E  18           
SHEET    4 AB4 4 PHE E  73  ASP E  78 -1  N  ALA E  74   O  THR E  87           
SHEET    1 AB5 6 GLY E  10  VAL E  12  0                                        
SHEET    2 AB5 6 THR E 123  VAL E 127  1  O  THR E 126   N  GLY E  10           
SHEET    3 AB5 6 ALA E  97  ASP E 105 -1  N  TYR E  99   O  THR E 123           
SHEET    4 AB5 6 TYR E  37  GLN E  44 -1  N  GLY E  40   O  ALA E 102           
SHEET    5 AB5 6 GLU E  51  TYR E  57 -1  O  GLU E  51   N  ARG E  43           
SHEET    6 AB5 6 THR E  63  TYR E  65 -1  O  TYR E  64   N  ARG E  55           
SHEET    1 AB6 4 GLY E  10  VAL E  12  0                                        
SHEET    2 AB6 4 THR E 123  VAL E 127  1  O  THR E 126   N  GLY E  10           
SHEET    3 AB6 4 ALA E  97  ASP E 105 -1  N  TYR E  99   O  THR E 123           
SHEET    4 AB6 4 TYR E 118  TRP E 119 -1  O  TYR E 118   N  ALA E 103           
SHEET    1 AB7 4 LEU F   4  SER F   7  0                                        
SHEET    2 AB7 4 LEU F  18  ALA F  24 -1  O  SER F  21   N  SER F   7           
SHEET    3 AB7 4 THR F  83  MET F  88 -1  O  MET F  88   N  LEU F  18           
SHEET    4 AB7 4 PHE F  73  ASP F  78 -1  N  ALA F  74   O  THR F  87           
SHEET    1 AB8 6 GLY F  10  VAL F  12  0                                        
SHEET    2 AB8 6 THR F 123  VAL F 127  1  O  THR F 126   N  GLY F  10           
SHEET    3 AB8 6 ALA F  97  ASP F 105 -1  N  TYR F  99   O  THR F 123           
SHEET    4 AB8 6 TYR F  37  GLN F  44 -1  N  GLY F  40   O  ALA F 102           
SHEET    5 AB8 6 GLU F  51  TYR F  57 -1  O  GLU F  51   N  ARG F  43           
SHEET    6 AB8 6 THR F  63  TYR F  65 -1  O  TYR F  64   N  ARG F  55           
SHEET    1 AB9 4 GLY F  10  VAL F  12  0                                        
SHEET    2 AB9 4 THR F 123  VAL F 127  1  O  THR F 126   N  GLY F  10           
SHEET    3 AB9 4 ALA F  97  ASP F 105 -1  N  TYR F  99   O  THR F 123           
SHEET    4 AB9 4 TYR F 118  TRP F 119 -1  O  TYR F 118   N  ALA F 103           
SHEET    1 AC1 3 TRP G  28  LEU G  29  0                                        
SHEET    2 AC1 3 VAL G  13  ALA G  18 -1  N  VAL G  17   O  LEU G  29           
SHEET    3 AC1 3 LEU G  36  ALA G  38 -1  O  LEU G  36   N  HIS G  15           
SHEET    1 AC2 5 TRP G  28  LEU G  29  0                                        
SHEET    2 AC2 5 VAL G  13  ALA G  18 -1  N  VAL G  17   O  LEU G  29           
SHEET    3 AC2 5 TYR G 151  ALA G 156 -1  O  PHE G 152   N  VAL G  16           
SHEET    4 AC2 5 GLY G  54  GLN G  67 -1  N  TYR G  59   O  GLY G 153           
SHEET    5 AC2 5 PRO G 113  LEU G 126 -1  O  GLY G 122   N  ILE G  58           
SHEET    1 AC3 5 GLU G  42  LEU G  43  0                                        
SHEET    2 AC3 5 LEU G  48  VAL G  49 -1  O  VAL G  49   N  GLU G  42           
SHEET    3 AC3 5 ARG G 131  ILE G 136 -1  O  LEU G 132   N  LEU G  48           
SHEET    4 AC3 5 LEU G  76  ILE G  83 -1  N  ILE G  83   O  ARG G 131           
SHEET    5 AC3 5 LYS G  90  LYS G  98 -1  O  LEU G  94   N  ILE G  80           
SHEET    1 AC4 4 LEU H   4  SER H   7  0                                        
SHEET    2 AC4 4 LEU H  18  ALA H  24 -1  O  SER H  21   N  SER H   7           
SHEET    3 AC4 4 THR H  83  MET H  88 -1  O  LEU H  86   N  LEU H  20           
SHEET    4 AC4 4 PHE H  73  ASP H  78 -1  N  ALA H  74   O  THR H  87           
SHEET    1 AC5 6 GLY H  10  VAL H  12  0                                        
SHEET    2 AC5 6 THR H 123  VAL H 127  1  O  THR H 126   N  GLY H  10           
SHEET    3 AC5 6 ALA H  97  ASP H 105 -1  N  TYR H  99   O  THR H 123           
SHEET    4 AC5 6 TYR H  37  GLN H  44 -1  N  GLY H  40   O  ALA H 102           
SHEET    5 AC5 6 GLU H  51  TYR H  57 -1  O  GLU H  51   N  ARG H  43           
SHEET    6 AC5 6 THR H  63  TYR H  65 -1  O  TYR H  64   N  ARG H  55           
SHEET    1 AC6 4 GLY H  10  VAL H  12  0                                        
SHEET    2 AC6 4 THR H 123  VAL H 127  1  O  THR H 126   N  GLY H  10           
SHEET    3 AC6 4 ALA H  97  ASP H 105 -1  N  TYR H  99   O  THR H 123           
SHEET    4 AC6 4 TYR H 118  TRP H 119 -1  O  TYR H 118   N  ALA H 103           
SHEET    1 AC7 3 TRP I  28  LEU I  29  0                                        
SHEET    2 AC7 3 VAL I  13  ALA I  18 -1  N  VAL I  17   O  LEU I  29           
SHEET    3 AC7 3 LEU I  36  ALA I  38 -1  O  LEU I  36   N  HIS I  15           
SHEET    1 AC8 5 TRP I  28  LEU I  29  0                                        
SHEET    2 AC8 5 VAL I  13  ALA I  18 -1  N  VAL I  17   O  LEU I  29           
SHEET    3 AC8 5 TYR I 151  ALA I 156 -1  O  PHE I 152   N  VAL I  16           
SHEET    4 AC8 5 GLY I  54  GLN I  67 -1  N  TYR I  59   O  GLY I 153           
SHEET    5 AC8 5 PRO I 113  LEU I 126 -1  O  TRP I 114   N  GLY I  66           
SHEET    1 AC9 5 GLU I  42  LEU I  43  0                                        
SHEET    2 AC9 5 LEU I  48  VAL I  49 -1  O  VAL I  49   N  GLU I  42           
SHEET    3 AC9 5 ARG I 131  ILE I 136 -1  O  LEU I 132   N  LEU I  48           
SHEET    4 AC9 5 LEU I  76  ILE I  83 -1  N  ILE I  83   O  ARG I 131           
SHEET    5 AC9 5 LYS I  90  LYS I  98 -1  O  LEU I  94   N  ILE I  80           
SHEET    1 AD1 4 LEU J   4  SER J   7  0                                        
SHEET    2 AD1 4 LEU J  18  ALA J  24 -1  O  SER J  21   N  SER J   7           
SHEET    3 AD1 4 THR J  83  MET J  88 -1  O  MET J  88   N  LEU J  18           
SHEET    4 AD1 4 PHE J  73  ASP J  78 -1  N  ASP J  78   O  THR J  83           
SHEET    1 AD2 6 GLY J  10  VAL J  12  0                                        
SHEET    2 AD2 6 THR J 123  VAL J 127  1  O  THR J 126   N  GLY J  10           
SHEET    3 AD2 6 ALA J  97  ASP J 105 -1  N  TYR J  99   O  THR J 123           
SHEET    4 AD2 6 TYR J  37  GLN J  44 -1  N  GLY J  40   O  ALA J 102           
SHEET    5 AD2 6 GLU J  51  TYR J  57 -1  O  GLU J  51   N  ARG J  43           
SHEET    6 AD2 6 THR J  63  TYR J  65 -1  O  TYR J  64   N  ARG J  55           
SHEET    1 AD3 4 GLY J  10  VAL J  12  0                                        
SHEET    2 AD3 4 THR J 123  VAL J 127  1  O  THR J 126   N  GLY J  10           
SHEET    3 AD3 4 ALA J  97  ASP J 105 -1  N  TYR J  99   O  THR J 123           
SHEET    4 AD3 4 TYR J 118  TRP J 119 -1  O  TYR J 118   N  ALA J 103           
SHEET    1 AD4 3 TRP M  28  LEU M  29  0                                        
SHEET    2 AD4 3 VAL M  13  ALA M  18 -1  N  VAL M  17   O  LEU M  29           
SHEET    3 AD4 3 LEU M  36  ALA M  38 -1  O  LEU M  36   N  HIS M  15           
SHEET    1 AD5 5 TRP M  28  LEU M  29  0                                        
SHEET    2 AD5 5 VAL M  13  ALA M  18 -1  N  VAL M  17   O  LEU M  29           
SHEET    3 AD5 5 TYR M 151  ALA M 156 -1  O  PHE M 152   N  VAL M  16           
SHEET    4 AD5 5 GLY M  54  GLN M  67 -1  N  TYR M  59   O  GLY M 153           
SHEET    5 AD5 5 PRO M 113  LEU M 126 -1  O  GLY M 122   N  ILE M  58           
SHEET    1 AD6 5 GLU M  42  LEU M  43  0                                        
SHEET    2 AD6 5 LEU M  48  VAL M  49 -1  O  VAL M  49   N  GLU M  42           
SHEET    3 AD6 5 ARG M 131  ILE M 136 -1  O  LEU M 132   N  LEU M  48           
SHEET    4 AD6 5 LEU M  76  ILE M  83 -1  N  ILE M  83   O  ARG M 131           
SHEET    5 AD6 5 LYS M  90  LYS M  98 -1  O  LEU M  93   N  ILE M  80           
SHEET    1 AD7 4 LEU N   4  SER N   7  0                                        
SHEET    2 AD7 4 LEU N  18  ALA N  24 -1  O  ALA N  23   N  GLN N   5           
SHEET    3 AD7 4 THR N  83  MET N  88 -1  O  MET N  88   N  LEU N  18           
SHEET    4 AD7 4 PHE N  73  ASP N  78 -1  N  ASP N  78   O  THR N  83           
SHEET    1 AD8 6 GLY N  10  VAL N  12  0                                        
SHEET    2 AD8 6 THR N 123  VAL N 127  1  O  THR N 126   N  GLY N  10           
SHEET    3 AD8 6 ALA N  97  ASP N 105 -1  N  TYR N  99   O  THR N 123           
SHEET    4 AD8 6 TYR N  37  GLN N  44 -1  N  GLY N  40   O  ALA N 102           
SHEET    5 AD8 6 GLU N  51  TYR N  57 -1  O  GLU N  51   N  ARG N  43           
SHEET    6 AD8 6 THR N  63  TYR N  65 -1  O  TYR N  64   N  ARG N  55           
SHEET    1 AD9 4 GLY N  10  VAL N  12  0                                        
SHEET    2 AD9 4 THR N 123  VAL N 127  1  O  THR N 126   N  GLY N  10           
SHEET    3 AD9 4 ALA N  97  ASP N 105 -1  N  TYR N  99   O  THR N 123           
SHEET    4 AD9 4 TYR N 118  TRP N 119 -1  O  TYR N 118   N  ALA N 103           
SSBOND   1 CYS A   69    CYS A  101                          1555   1555  2.03  
SSBOND   2 CYS B   69    CYS B  101                          1555   1555  2.03  
SSBOND   3 CYS C   69    CYS C  101                          1555   1555  2.04  
SSBOND   4 CYS D   22    CYS D  101                          1555   1555  2.01  
SSBOND   5 CYS E   22    CYS E  101                          1555   1555  2.02  
SSBOND   6 CYS F   22    CYS F  101                          1555   1555  2.02  
SSBOND   7 CYS G   69    CYS G  101                          1555   1555  2.03  
SSBOND   8 CYS H   22    CYS H  101                          1555   1555  2.02  
SSBOND   9 CYS I   69    CYS I  101                          1555   1555  2.03  
SSBOND  10 CYS J   22    CYS J  101                          1555   1555  2.03  
SSBOND  11 CYS M   69    CYS M  101                          1555   1555  2.04  
SSBOND  12 CYS N   22    CYS N  101                          1555   1555  2.01  
CRYST1  145.380   83.844  150.063  90.00 128.77  90.00 C 1 2 1      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      0.006879  0.000000  0.005525        0.00000                         
SCALE2      0.000000  0.011927  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008547        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system