GenomeNet

Database: PDB
Entry: 6FXN
LinkDB: 6FXN
Original site: 6FXN 
HEADER    IMMUNE SYSTEM                           09-MAR-18   6FXN              
TITLE     CRYSTAL STRUCTURE OF HUMAN BAFF IN COMPLEX WITH FAB FRAGMENT OF ANTI- 
TITLE    2 BAFF ANTIBODY BELIMUMAB                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 13B;       
COMPND   3 CHAIN: A, B, C, J, K, L;                                             
COMPND   4 SYNONYM: B LYMPHOCYTE STIMULATOR,BLYS,B-CELL-ACTIVATING FACTOR,BAFF, 
COMPND   5 DENDRITIC CELL-DERIVED TNF-LIKE MOLECULE,TNF- AND APOL-RELATED       
COMPND   6 LEUKOCYTE EXPRESSED LIGAND 1,TALL-1;                                 
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: BELIMUMAB HEAVY CHAIN;                                     
COMPND  11 CHAIN: D, F, H, M, O, Q;                                             
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: BELIMUMAB LIGHT CHAIN;                                     
COMPND  15 CHAIN: E, G, I, N, P, R;                                             
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TNFSF13B, BAFF, BLYS, TALL1, TNFSF20, ZTNF4, UNQ401/PRO738;    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 10090                                       
KEYWDS    IMMUNOLOGY, B CELL, CYTOKINE, BAFF, ANTIBODY, PROTEROS, IMMUNE SYSTEM 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.LAMMENS,K.MASKOS,L.WILLEN,X.JIANG,P.SCHNEIDER                       
REVDAT   1   04-APR-18 6FXN    0                                                
SPRSDE     04-APR-18 6FXN      6ERX                                             
JRNL        AUTH   M.VIGOLO,M.G.CHAMBERS,L.WILLEN,D.CHEVALLEY,K.MASKOS,         
JRNL        AUTH 2 A.LAMMENS,A.TARDIVEL,D.DAS,C.KOWALCZYK-QUINTAS,              
JRNL        AUTH 3 S.SCHUEPBACH-MALLEPELL,C.R.SMULSKI,M.ESLAMI,A.ROLINK,        
JRNL        AUTH 4 E.HUMMLER,E.SAMY,Y.FOMEKONG NANFACK,F.MACKAY,M.LIAO,H.HESS,  
JRNL        AUTH 5 X.JIANG,P.SCHNEIDER                                          
JRNL        TITL   A LOOP REGION OF BAFF CONTROLS B CELL SURVIVAL AND REGULATES 
JRNL        TITL 2 RECOGNITION BY DIFFERENT INHIBITORS.                         
JRNL        REF    NAT COMMUN                    V.   9  1199 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   29572442                                                     
JRNL        DOI    10.1038/S41467-018-03323-8                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 138.11                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 108711                         
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) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 0.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 654                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7410                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.20                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3330                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 34                           
REMARK   3   BIN FREE R VALUE                    : 0.3140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 25879                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 270                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.89000                                              
REMARK   3    B22 (A**2) : 0.29000                                              
REMARK   3    B33 (A**2) : -1.08000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.56000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.124         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.328         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.269         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.652        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 25944 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 23679 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 35416 ; 1.524 ; 1.948       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 54474 ; 1.197 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3402 ; 7.616 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   980 ;38.688 ;24.684       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3851 ;13.846 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    87 ;16.333 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4063 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 29817 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  5746 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 13668 ; 2.222 ; 3.904       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2): 13667 ; 2.222 ; 3.904       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17050 ; 3.571 ; 6.582       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 17051 ; 3.571 ; 6.582       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 12276 ; 3.125 ; 4.170       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2): 12277 ; 3.125 ; 4.170       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 18367 ; 4.689 ; 6.903       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 25075 ; 6.105 ;34.152       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 25070 ; 6.104 ;34.150       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 30                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   500                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0330 108.3120  17.1730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0872 T22:   0.0351                                     
REMARK   3      T33:   0.1163 T12:  -0.0543                                     
REMARK   3      T13:  -0.0625 T23:   0.0357                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1552 L22:   4.7333                                     
REMARK   3      L33:   3.4542 L12:  -2.0008                                     
REMARK   3      L13:  -0.6585 L23:   0.8792                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0309 S12:   0.0778 S13:  -0.2636                       
REMARK   3      S21:   0.0676 S22:  -0.0645 S23:   0.1232                       
REMARK   3      S31:   0.3489 S32:  -0.2119 S33:   0.0954                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   500                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.1160 126.3610   4.2560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0999 T22:   0.0869                                     
REMARK   3      T33:   0.1794 T12:  -0.0050                                     
REMARK   3      T13:  -0.0407 T23:   0.0334                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4586 L22:   2.9261                                     
REMARK   3      L33:   4.6579 L12:  -1.1542                                     
REMARK   3      L13:  -0.2845 L23:   1.3933                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0822 S12:   0.3539 S13:   0.0555                       
REMARK   3      S21:  -0.4577 S22:  -0.0335 S23:  -0.0731                       
REMARK   3      S31:  -0.1621 S32:   0.0821 S33:  -0.0487                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   500                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.9600 120.4550  23.5110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0720 T22:   0.0203                                     
REMARK   3      T33:   0.2028 T12:   0.0021                                     
REMARK   3      T13:  -0.1066 T23:  -0.0170                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0213 L22:   2.6641                                     
REMARK   3      L33:   3.5972 L12:  -0.6495                                     
REMARK   3      L13:  -1.8999 L23:   1.0263                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0032 S12:  -0.1666 S13:  -0.0605                       
REMARK   3      S21:   0.0862 S22:   0.0896 S23:  -0.4355                       
REMARK   3      S31:  -0.0657 S32:   0.2643 S33:  -0.0928                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   123                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.5170 109.7240  47.1980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1923 T22:   0.6701                                     
REMARK   3      T33:   0.4430 T12:   0.0020                                     
REMARK   3      T13:   0.0102 T23:  -0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2387 L22:   2.4528                                     
REMARK   3      L33:   7.4298 L12:  -0.1116                                     
REMARK   3      L13:  -4.1775 L23:  -2.5572                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1322 S12:  -0.2313 S13:  -0.0997                       
REMARK   3      S21:   0.3515 S22:   0.4186 S23:   0.5631                       
REMARK   3      S31:  -0.1697 S32:  -0.6154 S33:  -0.2865                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   124        D   300                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2390 107.6650  79.5930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6790 T22:   0.2652                                     
REMARK   3      T33:   0.9290 T12:   0.1080                                     
REMARK   3      T13:   0.1851 T23:   0.0587                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8261 L22:   2.2669                                     
REMARK   3      L33:   3.1006 L12:   0.6670                                     
REMARK   3      L13:   0.7732 L23:  -0.5611                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1122 S12:  -0.0425 S13:   1.0220                       
REMARK   3      S21:   0.4231 S22:  -0.0776 S23:   0.3213                       
REMARK   3      S31:  -0.4362 S32:  -0.1222 S33:   0.1899                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E   109                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.0690  96.8070  49.3240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2127 T22:   0.5117                                     
REMARK   3      T33:   0.3090 T12:   0.0049                                     
REMARK   3      T13:   0.0334 T23:   0.1705                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0477 L22:   3.5814                                     
REMARK   3      L33:   5.3103 L12:  -1.8835                                     
REMARK   3      L13:   2.0258 L23:  -2.1504                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2615 S12:  -1.0162 S13:  -0.6094                       
REMARK   3      S21:   0.2168 S22:   0.1509 S23:  -0.0192                       
REMARK   3      S31:   0.4118 S32:  -0.0202 S33:   0.1107                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   110        E   300                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.8550  91.6770  84.4500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4361 T22:   0.1011                                     
REMARK   3      T33:   0.4415 T12:  -0.1172                                     
REMARK   3      T13:   0.0802 T23:   0.0305                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7956 L22:   2.5810                                     
REMARK   3      L33:   5.6888 L12:  -1.5481                                     
REMARK   3      L13:  -1.9352 L23:   0.0835                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4118 S12:  -0.2078 S13:   0.3365                       
REMARK   3      S21:   0.4630 S22:  -0.2071 S23:   0.3346                       
REMARK   3      S31:  -0.3202 S32:  -0.4029 S33:  -0.2048                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     1        F   123                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.6420 143.0570   2.7390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0340 T22:   0.0819                                     
REMARK   3      T33:   0.1583 T12:   0.0158                                     
REMARK   3      T13:  -0.0426 T23:  -0.0244                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6694 L22:   6.3067                                     
REMARK   3      L33:   2.0698 L12:  -3.6891                                     
REMARK   3      L13:   2.8016 L23:  -1.7951                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1064 S12:  -0.4526 S13:   0.1950                       
REMARK   3      S21:   0.1170 S22:   0.0676 S23:   0.0781                       
REMARK   3      S31:  -0.1037 S32:  -0.1619 S33:   0.0387                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   124        F   300                          
REMARK   3    ORIGIN FOR THE GROUP (A): -42.4970 142.0230   4.0010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4598 T22:   0.1856                                     
REMARK   3      T33:   0.1887 T12:   0.0935                                     
REMARK   3      T13:  -0.1257 T23:  -0.0282                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1538 L22:   7.4220                                     
REMARK   3      L33:   2.1776 L12:   3.5347                                     
REMARK   3      L13:  -1.0295 L23:   0.3391                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1109 S12:  -0.5082 S13:  -0.1444                       
REMARK   3      S21:   1.3711 S22:   0.0949 S23:  -0.3181                       
REMARK   3      S31:   0.5238 S32:   0.1737 S33:  -0.2058                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     1        G   109                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.8860 124.0050  -8.0690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2002 T22:   0.0423                                     
REMARK   3      T33:   0.1999 T12:   0.0788                                     
REMARK   3      T13:  -0.0619 T23:   0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3150 L22:   2.1373                                     
REMARK   3      L33:   5.1456 L12:   0.3589                                     
REMARK   3      L13:   2.5987 L23:   1.1609                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2393 S12:   0.1447 S13:  -0.4961                       
REMARK   3      S21:  -0.2809 S22:  -0.1019 S23:  -0.2217                       
REMARK   3      S31:   0.1950 S32:   0.1238 S33:  -0.1374                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   110        G   300                          
REMARK   3    ORIGIN FOR THE GROUP (A): -49.9910 137.5200 -10.6900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0984 T22:   0.0775                                     
REMARK   3      T33:   0.1487 T12:  -0.0600                                     
REMARK   3      T13:  -0.0815 T23:   0.0672                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6898 L22:   8.1789                                     
REMARK   3      L33:   3.8524 L12:  -2.9782                                     
REMARK   3      L13:  -1.3468 L23:   2.8281                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0001 S12:   0.0973 S13:   0.1085                       
REMARK   3      S21:   0.0857 S22:   0.0421 S23:   0.2969                       
REMARK   3      S31:  -0.1083 S32:  -0.1641 S33:  -0.0421                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     1        H   123                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.9750 150.9430  38.6480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1683 T22:   0.0710                                     
REMARK   3      T33:   0.1318 T12:   0.0577                                     
REMARK   3      T13:  -0.0588 T23:   0.0064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4306 L22:   4.8147                                     
REMARK   3      L33:   6.4176 L12:   2.7661                                     
REMARK   3      L13:   2.1112 L23:   3.7152                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1003 S12:  -0.2124 S13:   0.1703                       
REMARK   3      S21:   0.2059 S22:  -0.1549 S23:   0.2598                       
REMARK   3      S31:  -0.0343 S32:  -0.2597 S33:   0.0547                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   124        H   300                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.1100 181.8480  37.5490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3848 T22:   0.5571                                     
REMARK   3      T33:   0.4819 T12:  -0.3322                                     
REMARK   3      T13:   0.1812 T23:  -0.2637                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1544 L22:   4.3683                                     
REMARK   3      L33:   8.3764 L12:  -1.1088                                     
REMARK   3      L13:  -1.6177 L23:  -1.4484                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4703 S12:   0.2678 S13:  -0.3493                       
REMARK   3      S21:   0.3928 S22:  -0.1060 S23:   0.5815                       
REMARK   3      S31:   1.0177 S32:  -1.6955 S33:   0.5764                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I     1        I   109                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.8410 151.1670  20.1730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1725 T22:   0.1149                                     
REMARK   3      T33:   0.1350 T12:   0.0186                                     
REMARK   3      T13:  -0.0539 T23:  -0.0646                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7620 L22:   6.2620                                     
REMARK   3      L33:   2.8900 L12:   1.9018                                     
REMARK   3      L13:  -1.1907 L23:   0.6026                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0328 S12:   0.1994 S13:  -0.1017                       
REMARK   3      S21:  -0.4521 S22:   0.2361 S23:  -0.3637                       
REMARK   3      S31:  -0.0458 S32:   0.2675 S33:  -0.2034                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I   110        I   300                          
REMARK   3    ORIGIN FOR THE GROUP (A):  46.6780 187.3740  32.8750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1727 T22:   0.1144                                     
REMARK   3      T33:   0.1680 T12:  -0.0597                                     
REMARK   3      T13:  -0.0916 T23:   0.0342                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4110 L22:   4.7915                                     
REMARK   3      L33:   8.6207 L12:  -0.3038                                     
REMARK   3      L13:  -2.4496 L23:   3.6028                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2606 S12:  -0.2019 S13:   0.1044                       
REMARK   3      S21:   0.2746 S22:  -0.0633 S23:   0.1322                       
REMARK   3      S31:   0.1872 S32:   0.2580 S33:   0.3238                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J     1        J   500                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.6570 166.7830  84.9920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1001 T22:   0.0240                                     
REMARK   3      T33:   0.1008 T12:  -0.0268                                     
REMARK   3      T13:  -0.0638 T23:   0.0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0854 L22:   3.6194                                     
REMARK   3      L33:   3.4119 L12:  -1.3355                                     
REMARK   3      L13:   0.8008 L23:  -0.5903                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0565 S12:   0.0343 S13:   0.2289                       
REMARK   3      S21:  -0.0322 S22:   0.0324 S23:  -0.0512                       
REMARK   3      S31:  -0.3778 S32:   0.0468 S33:   0.0240                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K     1        K   500                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.0500 148.0760  71.9870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0624 T22:   0.0371                                     
REMARK   3      T33:   0.1492 T12:   0.0244                                     
REMARK   3      T13:  -0.0799 T23:  -0.0366                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7146 L22:   2.9180                                     
REMARK   3      L33:   4.5510 L12:  -1.2258                                     
REMARK   3      L13:   0.7418 L23:  -1.6305                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0975 S12:   0.2752 S13:  -0.0161                       
REMARK   3      S21:  -0.2417 S22:  -0.1008 S23:   0.0676                       
REMARK   3      S31:   0.2490 S32:   0.0138 S33:   0.0034                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     1        L   500                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.8970 153.9720  90.4200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1144 T22:   0.1093                                     
REMARK   3      T33:   0.1697 T12:   0.0390                                     
REMARK   3      T13:   0.0119 T23:   0.0536                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7404 L22:   2.8758                                     
REMARK   3      L33:   2.6095 L12:   0.0529                                     
REMARK   3      L13:   0.8683 L23:  -0.9919                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0591 S12:  -0.0577 S13:   0.1070                       
REMARK   3      S21:   0.1076 S22:   0.2142 S23:   0.5545                       
REMARK   3      S31:  -0.1307 S32:  -0.5075 S33:  -0.1550                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M     1        M   123                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.6520 167.1810 115.5800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1021 T22:   0.2143                                     
REMARK   3      T33:   0.2113 T12:   0.0312                                     
REMARK   3      T13:  -0.0505 T23:   0.0573                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3876 L22:   1.9719                                     
REMARK   3      L33:   5.9106 L12:   1.8583                                     
REMARK   3      L13:   4.0947 L23:   3.2039                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0988 S12:  -0.0666 S13:  -0.2025                       
REMARK   3      S21:   0.2669 S22:   0.0460 S23:  -0.1940                       
REMARK   3      S31:   0.4293 S32:   0.2949 S33:  -0.1448                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M   124        M   300                          
REMARK   3    ORIGIN FOR THE GROUP (A):  67.8060 167.6770 147.1780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2884 T22:   0.0957                                     
REMARK   3      T33:   0.4900 T12:   0.0853                                     
REMARK   3      T13:  -0.0634 T23:  -0.1039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9041 L22:   2.3888                                     
REMARK   3      L33:   3.7016 L12:   0.0702                                     
REMARK   3      L13:  -2.2216 L23:  -0.0998                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1210 S12:   0.2219 S13:  -1.1698                       
REMARK   3      S21:   0.1419 S22:  -0.1593 S23:  -0.0250                       
REMARK   3      S31:   0.5655 S32:   0.2102 S33:   0.2802                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   N     1        N   109                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.9070 178.4170 116.1030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1116 T22:   0.2480                                     
REMARK   3      T33:   0.1753 T12:  -0.0129                                     
REMARK   3      T13:  -0.1181 T23:  -0.0295                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9401 L22:   5.0186                                     
REMARK   3      L33:   7.0772 L12:  -1.6591                                     
REMARK   3      L13:  -0.3519 L23:   2.8961                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1142 S12:  -0.2088 S13:   0.2152                       
REMARK   3      S21:   0.0213 S22:  -0.1671 S23:   0.1139                       
REMARK   3      S31:  -0.4575 S32:  -0.3049 S33:   0.2812                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   N   110        N   300                          
REMARK   3    ORIGIN FOR THE GROUP (A):  63.5140 183.3070 152.4640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0771 T22:   0.0266                                     
REMARK   3      T33:   0.1858 T12:  -0.0037                                     
REMARK   3      T13:  -0.0064 T23:   0.0056                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2402 L22:   2.3599                                     
REMARK   3      L33:   5.6037 L12:  -1.3168                                     
REMARK   3      L13:   1.9515 L23:   0.2083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0811 S12:  -0.1996 S13:   0.0679                       
REMARK   3      S21:   0.1927 S22:  -0.0706 S23:  -0.1422                       
REMARK   3      S31:   0.1566 S32:   0.1925 S33:  -0.0106                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   O     1        O   123                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.3190 124.0780 106.6660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3785 T22:   0.2124                                     
REMARK   3      T33:   0.1946 T12:  -0.0281                                     
REMARK   3      T13:  -0.1049 T23:   0.0157                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0154 L22:   5.8451                                     
REMARK   3      L33:   5.2751 L12:   3.1478                                     
REMARK   3      L13:  -1.7948 L23:  -3.4573                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2641 S12:  -0.5258 S13:  -0.2927                       
REMARK   3      S21:   0.4625 S22:  -0.2098 S23:  -0.0840                       
REMARK   3      S31:   0.1743 S32:  -0.1509 S33:  -0.0542                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   O   124        O   300                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.7350  92.2970 106.5870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5204 T22:   0.7513                                     
REMARK   3      T33:   0.6491 T12:  -0.3587                                     
REMARK   3      T13:  -0.0563 T23:  -0.0176                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1811 L22:   2.9304                                     
REMARK   3      L33:   6.3914 L12:  -0.9482                                     
REMARK   3      L13:   0.0413 L23:   2.1498                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0008 S12:  -0.3425 S13:  -0.0109                       
REMARK   3      S21:  -0.0206 S22:   0.2253 S23:  -0.5201                       
REMARK   3      S31:  -0.3408 S32:   1.1149 S33:  -0.2245                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   P     1        P   109                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.6740 122.7790  88.0580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2023 T22:   0.2959                                     
REMARK   3      T33:   0.1763 T12:  -0.0258                                     
REMARK   3      T13:  -0.0858 T23:   0.1284                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6003 L22:   6.6589                                     
REMARK   3      L33:   2.7031 L12:   1.6827                                     
REMARK   3      L13:   0.7394 L23:   0.3023                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0501 S12:   0.1876 S13:   0.0434                       
REMARK   3      S21:  -0.2035 S22:   0.0793 S23:   0.3001                       
REMARK   3      S31:   0.1354 S32:  -0.5450 S33:  -0.1293                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   P   110        P   300                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.9600  86.9280 102.6950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4578 T22:   0.4739                                     
REMARK   3      T33:   0.3588 T12:  -0.3217                                     
REMARK   3      T13:  -0.0160 T23:  -0.0288                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4416 L22:   4.5673                                     
REMARK   3      L33:   5.8153 L12:  -0.2207                                     
REMARK   3      L13:   0.8576 L23:  -1.9353                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0108 S12:  -0.6972 S13:  -0.1673                       
REMARK   3      S21:   0.3237 S22:  -0.1137 S23:  -0.1249                       
REMARK   3      S31:   0.0474 S32:  -0.0060 S33:   0.1246                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Q     1        Q   123                          
REMARK   3    ORIGIN FOR THE GROUP (A):  79.1320 132.3790  72.3160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1337 T22:   0.0435                                     
REMARK   3      T33:   0.1805 T12:   0.0013                                     
REMARK   3      T13:  -0.1340 T23:   0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7791 L22:   5.7101                                     
REMARK   3      L33:   2.0873 L12:  -3.8437                                     
REMARK   3      L13:  -2.9483 L23:   1.0330                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1436 S12:  -0.4438 S13:  -0.1815                       
REMARK   3      S21:   0.1425 S22:   0.1474 S23:   0.0553                       
REMARK   3      S31:   0.0820 S32:   0.2935 S33:  -0.0037                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Q   124        Q   300                          
REMARK   3    ORIGIN FOR THE GROUP (A): 109.4840 133.4580  73.2270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4761 T22:   0.2263                                     
REMARK   3      T33:   0.3428 T12:   0.0331                                     
REMARK   3      T13:   0.0656 T23:  -0.0286                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5246 L22:   6.9833                                     
REMARK   3      L33:   2.1032 L12:   3.5709                                     
REMARK   3      L13:   0.4465 L23:  -0.2882                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5080 S12:  -0.4867 S13:   0.1102                       
REMARK   3      S21:   1.1579 S22:  -0.2375 S23:   0.4289                       
REMARK   3      S31:  -0.2669 S32:   0.1239 S33:  -0.2704                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   R     1        R   109                          
REMARK   3    ORIGIN FOR THE GROUP (A):  80.3630 150.9000  60.5640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2254 T22:   0.0694                                     
REMARK   3      T33:   0.1723 T12:   0.1019                                     
REMARK   3      T13:  -0.0147 T23:   0.0211                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0389 L22:   3.1360                                     
REMARK   3      L33:   3.7637 L12:   0.6155                                     
REMARK   3      L13:  -1.9261 L23:  -1.0610                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2483 S12:   0.3707 S13:   0.3357                       
REMARK   3      S21:  -0.2653 S22:  -0.1801 S23:  -0.1511                       
REMARK   3      S31:  -0.2224 S32:   0.0298 S33:  -0.0682                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   R   110        R   300                          
REMARK   3    ORIGIN FOR THE GROUP (A): 116.4670 137.0680  58.1270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2375 T22:   0.0963                                     
REMARK   3      T33:   0.2953 T12:   0.0122                                     
REMARK   3      T13:  -0.0212 T23:  -0.1128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0203 L22:   6.9419                                     
REMARK   3      L33:   3.7033 L12:  -2.3890                                     
REMARK   3      L13:   0.5782 L23:  -2.5176                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1246 S12:   0.0823 S13:  -0.0356                       
REMARK   3      S21:  -0.1969 S22:  -0.0340 S23:  -0.1696                       
REMARK   3      S31:   0.0724 S32:   0.1467 S33:  -0.0907                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6FXN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009070.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-APR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 109365                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 138.110                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 3.360                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.050                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1KD7 , 7FAB                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 9% (W/V) PEG4000, 0.1 M MGCL2, 0.1 M     
REMARK 280  HEPES PH 7.5, VAPOR DIFFUSION, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       67.74950            
REMARK 290   SMTRY3   2  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: NONAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 21980 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 72550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, 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: NONAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 21760 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 72010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -123.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, L, M, N, O, P, Q, R             
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     MET A   122                                                      
REMARK 465     ARG A   123                                                      
REMARK 465     GLY A   124                                                      
REMARK 465     SER A   125                                                      
REMARK 465     HIS A   126                                                      
REMARK 465     HIS A   127                                                      
REMARK 465     HIS A   128                                                      
REMARK 465     HIS A   129                                                      
REMARK 465     HIS A   130                                                      
REMARK 465     HIS A   131                                                      
REMARK 465     GLY A   132                                                      
REMARK 465     SER A   133                                                      
REMARK 465     ALA A   134                                                      
REMARK 465     VAL A   135                                                      
REMARK 465     GLN A   136                                                      
REMARK 465     GLY A   137                                                      
REMARK 465     PRO A   138                                                      
REMARK 465     GLU A   139                                                      
REMARK 465     GLU A   140                                                      
REMARK 465     THR A   141                                                      
REMARK 465     MET B   122                                                      
REMARK 465     ARG B   123                                                      
REMARK 465     GLY B   124                                                      
REMARK 465     SER B   125                                                      
REMARK 465     HIS B   126                                                      
REMARK 465     HIS B   127                                                      
REMARK 465     HIS B   128                                                      
REMARK 465     HIS B   129                                                      
REMARK 465     HIS B   130                                                      
REMARK 465     HIS B   131                                                      
REMARK 465     GLY B   132                                                      
REMARK 465     SER B   133                                                      
REMARK 465     ALA B   134                                                      
REMARK 465     VAL B   135                                                      
REMARK 465     GLN B   136                                                      
REMARK 465     GLY B   137                                                      
REMARK 465     PRO B   138                                                      
REMARK 465     GLU B   139                                                      
REMARK 465     GLU B   140                                                      
REMARK 465     THR B   141                                                      
REMARK 465     MET C   122                                                      
REMARK 465     ARG C   123                                                      
REMARK 465     GLY C   124                                                      
REMARK 465     SER C   125                                                      
REMARK 465     HIS C   126                                                      
REMARK 465     HIS C   127                                                      
REMARK 465     HIS C   128                                                      
REMARK 465     HIS C   129                                                      
REMARK 465     HIS C   130                                                      
REMARK 465     HIS C   131                                                      
REMARK 465     GLY C   132                                                      
REMARK 465     SER C   133                                                      
REMARK 465     ALA C   134                                                      
REMARK 465     VAL C   135                                                      
REMARK 465     GLN C   136                                                      
REMARK 465     GLY C   137                                                      
REMARK 465     PRO C   138                                                      
REMARK 465     GLU C   139                                                      
REMARK 465     GLU C   140                                                      
REMARK 465     THR C   141                                                      
REMARK 465     SER D   138                                                      
REMARK 465     LYS D   139                                                      
REMARK 465     SER D   140                                                      
REMARK 465     THR D   141                                                      
REMARK 465     SER D   142                                                      
REMARK 465     GLY D   143                                                      
REMARK 465     GLY D   144                                                      
REMARK 465     PRO D   223                                                      
REMARK 465     LYS D   224                                                      
REMARK 465     SER D   225                                                      
REMARK 465     SER E     1                                                      
REMARK 465     SER E     2                                                      
REMARK 465     GLU E   212                                                      
REMARK 465     CYS E   213                                                      
REMARK 465     SER E   214                                                      
REMARK 465     GLN F     1                                                      
REMARK 465     SER F   138                                                      
REMARK 465     LYS F   139                                                      
REMARK 465     SER F   140                                                      
REMARK 465     SER F   225                                                      
REMARK 465     SER G     1                                                      
REMARK 465     GLU G   212                                                      
REMARK 465     CYS G   213                                                      
REMARK 465     SER G   214                                                      
REMARK 465     GLN H     1                                                      
REMARK 465     SER H   138                                                      
REMARK 465     LYS H   139                                                      
REMARK 465     SER H   140                                                      
REMARK 465     THR H   141                                                      
REMARK 465     SER H   142                                                      
REMARK 465     GLY H   143                                                      
REMARK 465     GLY H   144                                                      
REMARK 465     SER H   225                                                      
REMARK 465     SER I     1                                                      
REMARK 465     GLU I   212                                                      
REMARK 465     CYS I   213                                                      
REMARK 465     SER I   214                                                      
REMARK 465     MET J   122                                                      
REMARK 465     ARG J   123                                                      
REMARK 465     GLY J   124                                                      
REMARK 465     SER J   125                                                      
REMARK 465     HIS J   126                                                      
REMARK 465     HIS J   127                                                      
REMARK 465     HIS J   128                                                      
REMARK 465     HIS J   129                                                      
REMARK 465     HIS J   130                                                      
REMARK 465     HIS J   131                                                      
REMARK 465     GLY J   132                                                      
REMARK 465     SER J   133                                                      
REMARK 465     ALA J   134                                                      
REMARK 465     VAL J   135                                                      
REMARK 465     GLN J   136                                                      
REMARK 465     GLY J   137                                                      
REMARK 465     PRO J   138                                                      
REMARK 465     GLU J   139                                                      
REMARK 465     GLU J   140                                                      
REMARK 465     THR J   141                                                      
REMARK 465     MET K   122                                                      
REMARK 465     ARG K   123                                                      
REMARK 465     GLY K   124                                                      
REMARK 465     SER K   125                                                      
REMARK 465     HIS K   126                                                      
REMARK 465     HIS K   127                                                      
REMARK 465     HIS K   128                                                      
REMARK 465     HIS K   129                                                      
REMARK 465     HIS K   130                                                      
REMARK 465     HIS K   131                                                      
REMARK 465     GLY K   132                                                      
REMARK 465     SER K   133                                                      
REMARK 465     ALA K   134                                                      
REMARK 465     VAL K   135                                                      
REMARK 465     GLN K   136                                                      
REMARK 465     GLY K   137                                                      
REMARK 465     PRO K   138                                                      
REMARK 465     GLU K   139                                                      
REMARK 465     GLU K   140                                                      
REMARK 465     THR K   141                                                      
REMARK 465     MET L   122                                                      
REMARK 465     ARG L   123                                                      
REMARK 465     GLY L   124                                                      
REMARK 465     SER L   125                                                      
REMARK 465     HIS L   126                                                      
REMARK 465     HIS L   127                                                      
REMARK 465     HIS L   128                                                      
REMARK 465     HIS L   129                                                      
REMARK 465     HIS L   130                                                      
REMARK 465     HIS L   131                                                      
REMARK 465     GLY L   132                                                      
REMARK 465     SER L   133                                                      
REMARK 465     ALA L   134                                                      
REMARK 465     VAL L   135                                                      
REMARK 465     GLN L   136                                                      
REMARK 465     GLY L   137                                                      
REMARK 465     PRO L   138                                                      
REMARK 465     GLU L   139                                                      
REMARK 465     GLU L   140                                                      
REMARK 465     THR L   141                                                      
REMARK 465     GLN M     1                                                      
REMARK 465     SER M   138                                                      
REMARK 465     LYS M   139                                                      
REMARK 465     SER M   140                                                      
REMARK 465     THR M   141                                                      
REMARK 465     SER M   142                                                      
REMARK 465     GLY M   143                                                      
REMARK 465     GLY M   144                                                      
REMARK 465     LYS M   224                                                      
REMARK 465     SER M   225                                                      
REMARK 465     SER N     1                                                      
REMARK 465     GLU N   212                                                      
REMARK 465     CYS N   213                                                      
REMARK 465     SER N   214                                                      
REMARK 465     SER O   137                                                      
REMARK 465     SER O   138                                                      
REMARK 465     LYS O   139                                                      
REMARK 465     SER O   140                                                      
REMARK 465     THR O   141                                                      
REMARK 465     SER O   142                                                      
REMARK 465     GLY O   143                                                      
REMARK 465     GLY O   144                                                      
REMARK 465     LYS O   224                                                      
REMARK 465     SER O   225                                                      
REMARK 465     SER P     1                                                      
REMARK 465     GLU P   212                                                      
REMARK 465     CYS P   213                                                      
REMARK 465     SER P   214                                                      
REMARK 465     GLN Q     1                                                      
REMARK 465     SER Q   138                                                      
REMARK 465     LYS Q   139                                                      
REMARK 465     SER Q   140                                                      
REMARK 465     THR Q   141                                                      
REMARK 465     SER Q   142                                                      
REMARK 465     GLY Q   143                                                      
REMARK 465     GLY Q   144                                                      
REMARK 465     LYS Q   224                                                      
REMARK 465     SER Q   225                                                      
REMARK 465     SER R     1                                                      
REMARK 465     THR R   211                                                      
REMARK 465     GLU R   212                                                      
REMARK 465     CYS R   213                                                      
REMARK 465     SER R   214                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     VAL A  142   CG1  CG2                                            
REMARK 480     LYS A  160   CE   NZ                                             
REMARK 480     LYS A  181   CD   CE   NZ                                        
REMARK 480     GLU A  182   CD   OE1  OE2                                       
REMARK 480     LYS A  184   NZ                                                  
REMARK 480     LYS A  204   CE   NZ                                             
REMARK 480     ILE A  212   CD1                                                 
REMARK 480     LYS A  215   CD   CE   NZ                                        
REMARK 480     LEU A  285   CD1  CD2                                            
REMARK 480     VAL B  142   CG1  CG2                                            
REMARK 480     GLU B  154   CD   OE1  OE2                                       
REMARK 480     LYS B  160   CD   CE   NZ                                        
REMARK 480     LYS B  181   CD   CE   NZ                                        
REMARK 480     LYS B  184   NZ                                                  
REMARK 480     LYS B  188   CE   NZ                                             
REMARK 480     LYS B  204   CD   CE   NZ                                        
REMARK 480     LYS B  215   CD   CE   NZ                                        
REMARK 480     GLU B  254   CD   OE1  OE2                                       
REMARK 480     LEU B  285   CD1  CD2                                            
REMARK 480     VAL C  142   CG1  CG2                                            
REMARK 480     GLU C  154   CD   OE1  OE2                                       
REMARK 480     LYS C  160   CD   CE   NZ                                        
REMARK 480     LYS C  181   CG   CD   CE   NZ                                   
REMARK 480     LYS C  184   CE   NZ                                             
REMARK 480     LYS C  204   CE   NZ                                             
REMARK 480     LYS C  215   NZ                                                  
REMARK 480     LYS C  252   CE   NZ                                             
REMARK 480     LEU C  285   CD1  CD2                                            
REMARK 480     GLN D    1   CG   CD   OE1  NE2                                  
REMARK 480     VAL D    2   CG1  CG2                                            
REMARK 480     GLN D    3   CD   OE1  NE2                                       
REMARK 480     GLN D    5   CD   OE1  NE2                                       
REMARK 480     LYS D   12   NZ                                                  
REMARK 480     LYS D   13   CD   CE   NZ                                        
REMARK 480     LYS D   23   CD   CE   NZ                                        
REMARK 480     SER D   25   OG                                                  
REMARK 480     ILE D   34   CD1                                                 
REMARK 480     LYS D   59   NZ                                                  
REMARK 480     GLN D   62   CD   OE1  NE2                                       
REMARK 480     LEU D   83   CD1  CD2                                            
REMARK 480     SER D   84   OG                                                  
REMARK 480     SER D   85   OG                                                  
REMARK 480     ARG D   87   CZ   NH1  NH2                                       
REMARK 480     ARG D  115   CD   NE   CZ   NH1  NH2                             
REMARK 480     SER D  125   OG                                                  
REMARK 480     LYS D  127   CG   CD   CE   NZ                                   
REMARK 480     SER D  130   OG                                                  
REMARK 480     LEU D  148   CD1  CD2                                            
REMARK 480     LYS D  153   CD   CE   NZ                                        
REMARK 480     SER D  182   OG                                                  
REMARK 480     LEU D  185   CD1  CD2                                            
REMARK 480     LEU D  199   CD1  CD2                                            
REMARK 480     THR D  201   OG1  CG2                                            
REMARK 480     ILE D  205   CD1                                                 
REMARK 480     VAL D  208   CG1  CG2                                            
REMARK 480     LYS D  211   CE   NZ                                             
REMARK 480     LYS D  216   CE   NZ                                             
REMARK 480     LYS D  219   CE   NZ                                             
REMARK 480     LYS D  220   NZ                                                  
REMARK 480     VAL D  221   CG1  CG2                                            
REMARK 480     GLU D  222   CG   CD   OE1  OE2                                  
REMARK 480     GLU E    3   CD   OE1  OE2                                       
REMARK 480     LEU E   14   CD1  CD2                                            
REMARK 480     LYS E   50   CE   NZ                                             
REMARK 480     ASP E   59   CG   OD1  OD2                                       
REMARK 480     LEU E  108   CD1  CD2                                            
REMARK 480     LYS E  112   NZ                                                  
REMARK 480     SER E  124   OG                                                  
REMARK 480     GLU E  125   CD   OE1  OE2                                       
REMARK 480     GLN E  128   CG   CD   OE1  NE2                                  
REMARK 480     LYS E  131   CE   NZ                                             
REMARK 480     LYS E  158   CD   CE   NZ                                        
REMARK 480     LYS E  168   CE   NZ                                             
REMARK 480     GLU E  185   CD   OE1  OE2                                       
REMARK 480     LYS E  188   CD   CE   NZ                                        
REMARK 480     ARG E  191   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS E  206   NZ                                                  
REMARK 480     LYS F   13   NZ                                                  
REMARK 480     ARG F   19   CZ   NH1  NH2                                       
REMARK 480     LYS F   23   CD   CE   NZ                                        
REMARK 480     GLN F   62   CD   OE1  NE2                                       
REMARK 480     GLU F   82   CD   OE1  OE2                                       
REMARK 480     ARG F  115   CD   NE   CZ   NH1  NH2                             
REMARK 480     SER F  137   OG                                                  
REMARK 480     THR F  141   OG1  CG2                                            
REMARK 480     SER F  142   OG                                                  
REMARK 480     THR F  201   OG1  CG2                                            
REMARK 480     ILE F  205   CD1                                                 
REMARK 480     LYS F  211   NZ                                                  
REMARK 480     LYS F  216   CD   CE   NZ                                        
REMARK 480     LYS F  219   NZ                                                  
REMARK 480     LYS F  220   CE   NZ                                             
REMARK 480     LYS F  224   CD   CE   NZ                                        
REMARK 480     LYS G   50   CE   NZ                                             
REMARK 480     LYS G  131   CD   CE   NZ                                        
REMARK 480     LYS G  151   CE   NZ                                             
REMARK 480     LYS G  158   CD   CE   NZ                                        
REMARK 480     LYS G  173   NZ                                                  
REMARK 480     LYS G  188   CE   NZ                                             
REMARK 480     ARG G  191   CD   NE   CZ   NH1  NH2                             
REMARK 480     THR G  211   OG1  CG2                                            
REMARK 480     LYS H   13   CE   NZ                                             
REMARK 480     LYS H   23   NZ                                                  
REMARK 480     GLN H   43   CD   OE1  NE2                                       
REMARK 480     LYS H   59   NZ                                                  
REMARK 480     GLU H   89   CD   OE1  OE2                                       
REMARK 480     ARG H  115   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     SER H  125   OG                                                  
REMARK 480     LYS H  127   CG   CD   CE   NZ                                   
REMARK 480     LYS H  153   CE   NZ                                             
REMARK 480     LEU H  169   CD1  CD2                                            
REMARK 480     SER H  182   OG                                                  
REMARK 480     ILE H  205   CD1                                                 
REMARK 480     LYS H  211   CG   CD   CE   NZ                                   
REMARK 480     ASN H  214   CG   OD1  ND2                                       
REMARK 480     LYS H  216   CD   CE   NZ                                        
REMARK 480     LYS H  220   CD   CE   NZ                                        
REMARK 480     GLU H  222   CG   CD   OE1  OE2                                  
REMARK 480     LYS H  224   CG   CD   CE   NZ                                   
REMARK 480     GLU I    3   CD   OE1  OE2                                       
REMARK 480     ASP I   25   CG   OD1  OD2                                       
REMARK 480     LYS I  112   CG   CD   CE   NZ                                   
REMARK 480     LYS I  131   CE   NZ                                             
REMARK 480     LYS I  151   NZ                                                  
REMARK 480     LYS I  158   CD   CE   NZ                                        
REMARK 480     LYS I  168   CE   NZ                                             
REMARK 480     LYS I  188   CE   NZ                                             
REMARK 480     ARG I  191   CZ   NH1  NH2                                       
REMARK 480     VAL J  142   CG1  CG2                                            
REMARK 480     GLU J  154   CD   OE1  OE2                                       
REMARK 480     LYS J  160   CG   CD   CE   NZ                                   
REMARK 480     LYS J  181   CE   NZ                                             
REMARK 480     GLU J  182   CD   OE1  OE2                                       
REMARK 480     LYS J  184   NZ                                                  
REMARK 480     LYS J  188   NZ                                                  
REMARK 480     LYS J  215   NZ                                                  
REMARK 480     PHE J  220   CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 480     LYS J  252   CD   CE   NZ                                        
REMARK 480     LEU J  285   CD1  CD2                                            
REMARK 480     VAL K  142   CG1  CG2                                            
REMARK 480     GLU K  154   CD   OE1  OE2                                       
REMARK 480     LYS K  160   NZ                                                  
REMARK 480     LYS K  181   CG   CD   CE   NZ                                   
REMARK 480     LYS K  184   NZ                                                  
REMARK 480     LYS K  204   CE   NZ                                             
REMARK 480     LYS K  215   NZ                                                  
REMARK 480     LYS K  252   CE   NZ                                             
REMARK 480     LEU K  285   CD1  CD2                                            
REMARK 480     VAL L  142   CG1  CG2                                            
REMARK 480     GLU L  154   CD   OE1  OE2                                       
REMARK 480     LYS L  160   CD   CE   NZ                                        
REMARK 480     SER L  176   OG                                                  
REMARK 480     LYS L  181   CD   CE   NZ                                        
REMARK 480     GLU L  182   CD   OE1  OE2                                       
REMARK 480     LYS L  184   CE   NZ                                             
REMARK 480     LYS L  188   CE   NZ                                             
REMARK 480     LYS L  204   NZ                                                  
REMARK 480     LYS L  215   CE   NZ                                             
REMARK 480     LYS L  252   CD   CE   NZ                                        
REMARK 480     GLU L  254   CD   OE1  OE2                                       
REMARK 480     LEU L  285   CD1  CD2                                            
REMARK 480     VAL M    2   CG1  CG2                                            
REMARK 480     GLU M   10   CD   OE1  OE2                                       
REMARK 480     LYS M   13   CE   NZ                                             
REMARK 480     LYS M   23   CE   NZ                                             
REMARK 480     GLU M   89   CD   OE1  OE2                                       
REMARK 480     ARG M  115   CD   NE   CZ   NH1  NH2                             
REMARK 480     ILE M  205   CD1                                                 
REMARK 480     LYS M  211   CE   NZ                                             
REMARK 480     LYS M  216   CD   CE   NZ                                        
REMARK 480     LYS M  219   CE   NZ                                             
REMARK 480     GLU M  222   CG   CD   OE1  OE2                                  
REMARK 480     GLU N    3   CD   OE1  OE2                                       
REMARK 480     LYS N   50   NZ                                                  
REMARK 480     GLU N   80   CD   OE1  OE2                                       
REMARK 480     LYS N  112   NZ                                                  
REMARK 480     GLU N  125   CD   OE1  OE2                                       
REMARK 480     LYS N  131   NZ                                                  
REMARK 480     LYS N  158   CD   CE   NZ                                        
REMARK 480     GLU N  185   CG   CD   OE1  OE2                                  
REMARK 480     LYS N  188   CD   CE   NZ                                        
REMARK 480     ARG N  191   CZ   NH1  NH2                                       
REMARK 480     THR N  211   OG1  CG2                                            
REMARK 480     GLN O    1   CG   CD   OE1  NE2                                  
REMARK 480     VAL O    2   CG1  CG2                                            
REMARK 480     ARG O   19   CZ   NH1  NH2                                       
REMARK 480     LYS O   23   NZ                                                  
REMARK 480     SER O   25   OG                                                  
REMARK 480     LYS O   59   CE   NZ                                             
REMARK 480     GLU O   82   CD   OE1  OE2                                       
REMARK 480     SER O   88   OG                                                  
REMARK 480     ARG O  115   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS O  127   CE   NZ                                             
REMARK 480     LEU O  148   CD1  CD2                                            
REMARK 480     LYS O  153   NZ                                                  
REMARK 480     SER O  163   OG                                                  
REMARK 480     LEU O  169   CG   CD1  CD2                                       
REMARK 480     ILE O  205   CD1                                                 
REMARK 480     VAL O  208   CG1  CG2                                            
REMARK 480     LYS O  211   CE   NZ                                             
REMARK 480     LYS O  216   CE   NZ                                             
REMARK 480     VAL O  217   CG1  CG2                                            
REMARK 480     LYS O  219   CE   NZ                                             
REMARK 480     LYS O  220   CD   CE   NZ                                        
REMARK 480     GLU O  222   CD   OE1  OE2                                       
REMARK 480     GLU P    3   CG   CD   OE1  OE2                                  
REMARK 480     LYS P   50   CG   CD   CE   NZ                                   
REMARK 480     LYS P  112   CE   NZ                                             
REMARK 480     GLU P  125   CD   OE1  OE2                                       
REMARK 480     GLN P  128   CD   OE1  NE2                                       
REMARK 480     LYS P  131   CD   CE   NZ                                        
REMARK 480     LYS P  151   CE   NZ                                             
REMARK 480     SER P  154   OG                                                  
REMARK 480     LYS P  158   CG   CD   CE   NZ                                   
REMARK 480     LYS P  168   NZ                                                  
REMARK 480     LYS P  173   NZ                                                  
REMARK 480     LYS P  188   CD   CE   NZ                                        
REMARK 480     ARG P  191   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS P  206   NZ                                                  
REMARK 480     THR P  211   OG1  CG2                                            
REMARK 480     LYS Q   13   CE   NZ                                             
REMARK 480     LYS Q   23   CD   CE   NZ                                        
REMARK 480     LYS Q   59   NZ                                                  
REMARK 480     ARG Q  115   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS Q  127   NZ                                                  
REMARK 480     THR Q  170   OG1  CG2                                            
REMARK 480     SER Q  182   OG                                                  
REMARK 480     SER Q  197   OG                                                  
REMARK 480     ILE Q  205   CD1                                                 
REMARK 480     LYS Q  211   CD   CE   NZ                                        
REMARK 480     LYS Q  216   CE   NZ                                             
REMARK 480     LYS Q  219   NZ                                                  
REMARK 480     LYS Q  220   CD   CE   NZ                                        
REMARK 480     GLU Q  222   CG   CD   OE1  OE2                                  
REMARK 480     GLU R    3   CD   OE1  OE2                                       
REMARK 480     GLU R   80   CD   OE1  OE2                                       
REMARK 480     LYS R  131   CE   NZ                                             
REMARK 480     LYS R  151   CD   CE   NZ                                        
REMARK 480     LYS R  158   CD   CE   NZ                                        
REMARK 480     LYS R  188   CE   NZ                                             
REMARK 480     ARG R  191   NE   CZ   NH1  NH2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG N 191   NE    ARG N 191   CZ      0.082                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU D  83   CB  -  CG  -  CD1 ANGL. DEV. =  17.4 DEGREES          
REMARK 500    LEU D  83   CB  -  CG  -  CD2 ANGL. DEV. = -10.6 DEGREES          
REMARK 500    ARG D  87   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG F  19   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    VAL L 142   CA  -  CB  -  CG2 ANGL. DEV. =   9.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 182       58.12     38.48                                   
REMARK 500    ASN A 242       91.61   -165.16                                   
REMARK 500    LEU B 272       51.02   -105.22                                   
REMARK 500    ASN C 242       89.72   -168.77                                   
REMARK 500    ASN D  30     -138.70     59.12                                   
REMARK 500    GLN D  62       44.32    -82.02                                   
REMARK 500    ASN D  63       34.90   -141.11                                   
REMARK 500    SER D  85       60.24     60.00                                   
REMARK 500    ALA D 109     -155.82   -100.49                                   
REMARK 500    HIS E  96     -167.16     62.18                                   
REMARK 500    ALA E 145      108.67   -160.54                                   
REMARK 500    ASP E 153     -119.49     62.27                                   
REMARK 500    LYS E 158      -71.12    -67.41                                   
REMARK 500    ASN F  30     -125.02     57.63                                   
REMARK 500    GLN F  62       41.92   -101.93                                   
REMARK 500    ASN F  63       42.42   -149.00                                   
REMARK 500    ALA F 109     -163.81   -108.32                                   
REMARK 500    SER F 142       95.01   -161.15                                   
REMARK 500    ASP F 154       71.25     57.83                                   
REMARK 500    THR F 170      -60.15    -97.70                                   
REMARK 500    SER G  66      103.01   -161.15                                   
REMARK 500    ALA G  83     -179.06   -171.72                                   
REMARK 500    HIS G  96     -165.71     60.28                                   
REMARK 500    ASP G 153     -130.55     56.51                                   
REMARK 500    ASN H  30     -121.80     53.31                                   
REMARK 500    ALA H 109     -163.25   -115.89                                   
REMARK 500    ASP H 154       74.40     50.55                                   
REMARK 500    THR H 201      -60.91   -145.23                                   
REMARK 500    SER I  64      144.31   -175.76                                   
REMARK 500    SER I  66      112.79   -162.12                                   
REMARK 500    HIS I  96     -155.85    -90.25                                   
REMARK 500    ASP I 153     -113.28     52.45                                   
REMARK 500    LYS I 158      -78.94    -65.71                                   
REMARK 500    ASN J 242       91.46   -160.54                                   
REMARK 500    ASN K 242       88.92   -160.06                                   
REMARK 500    ASN M  30     -137.25     60.57                                   
REMARK 500    ASP M 154       77.33     59.56                                   
REMARK 500    SER N  66       96.23   -162.64                                   
REMARK 500    HIS N  96     -165.63     65.34                                   
REMARK 500    ASP N 153     -111.89     53.01                                   
REMARK 500    LYS N 158      -73.94    -69.61                                   
REMARK 500    ASN N 172       -2.37     69.27                                   
REMARK 500    ASN O  30     -121.41     50.73                                   
REMARK 500    ALA O 109     -165.40   -103.15                                   
REMARK 500    SER O 111      139.14   -175.12                                   
REMARK 500    ASP O 154       72.54     60.42                                   
REMARK 500    GLU P  82      103.20    -51.33                                   
REMARK 500    HIS P  96     -169.43     65.53                                   
REMARK 500    ASP P 153     -117.14     56.85                                   
REMARK 500    LYS P 158      -73.31    -74.36                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      59 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6FXN A  134   285  UNP    Q9Y275   TN13B_HUMAN    134    285             
DBREF  6FXN B  134   285  UNP    Q9Y275   TN13B_HUMAN    134    285             
DBREF  6FXN C  134   285  UNP    Q9Y275   TN13B_HUMAN    134    285             
DBREF  6FXN D    1   225  PDB    6FXN     6FXN             1    225             
DBREF  6FXN E    1   214  PDB    6FXN     6FXN             1    214             
DBREF  6FXN F    1   225  PDB    6FXN     6FXN             1    225             
DBREF  6FXN G    1   214  PDB    6FXN     6FXN             1    214             
DBREF  6FXN H    1   225  PDB    6FXN     6FXN             1    225             
DBREF  6FXN I    1   214  PDB    6FXN     6FXN             1    214             
DBREF  6FXN J  134   285  UNP    Q9Y275   TN13B_HUMAN    134    285             
DBREF  6FXN K  134   285  UNP    Q9Y275   TN13B_HUMAN    134    285             
DBREF  6FXN L  134   285  UNP    Q9Y275   TN13B_HUMAN    134    285             
DBREF  6FXN M    1   225  PDB    6FXN     6FXN             1    225             
DBREF  6FXN N    1   214  PDB    6FXN     6FXN             1    214             
DBREF  6FXN O    1   225  PDB    6FXN     6FXN             1    225             
DBREF  6FXN P    1   214  PDB    6FXN     6FXN             1    214             
DBREF  6FXN Q    1   225  PDB    6FXN     6FXN             1    225             
DBREF  6FXN R    1   214  PDB    6FXN     6FXN             1    214             
SEQADV 6FXN MET A  122  UNP  Q9Y275              INITIATING METHIONINE          
SEQADV 6FXN ARG A  123  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN GLY A  124  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN SER A  125  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS A  126  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS A  127  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS A  128  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS A  129  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS A  130  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS A  131  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN GLY A  132  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN SER A  133  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN ALA A  218  UNP  Q9Y275    HIS   218 ENGINEERED MUTATION            
SEQADV 6FXN MET B  122  UNP  Q9Y275              INITIATING METHIONINE          
SEQADV 6FXN ARG B  123  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN GLY B  124  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN SER B  125  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS B  126  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS B  127  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS B  128  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS B  129  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS B  130  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS B  131  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN GLY B  132  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN SER B  133  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN ALA B  218  UNP  Q9Y275    HIS   218 ENGINEERED MUTATION            
SEQADV 6FXN MET C  122  UNP  Q9Y275              INITIATING METHIONINE          
SEQADV 6FXN ARG C  123  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN GLY C  124  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN SER C  125  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS C  126  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS C  127  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS C  128  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS C  129  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS C  130  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS C  131  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN GLY C  132  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN SER C  133  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN ALA C  218  UNP  Q9Y275    HIS   218 ENGINEERED MUTATION            
SEQADV 6FXN MET J  122  UNP  Q9Y275              INITIATING METHIONINE          
SEQADV 6FXN ARG J  123  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN GLY J  124  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN SER J  125  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS J  126  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS J  127  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS J  128  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS J  129  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS J  130  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS J  131  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN GLY J  132  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN SER J  133  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN ALA J  218  UNP  Q9Y275    HIS   218 ENGINEERED MUTATION            
SEQADV 6FXN MET K  122  UNP  Q9Y275              INITIATING METHIONINE          
SEQADV 6FXN ARG K  123  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN GLY K  124  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN SER K  125  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS K  126  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS K  127  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS K  128  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS K  129  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS K  130  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS K  131  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN GLY K  132  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN SER K  133  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN ALA K  218  UNP  Q9Y275    HIS   218 ENGINEERED MUTATION            
SEQADV 6FXN MET L  122  UNP  Q9Y275              INITIATING METHIONINE          
SEQADV 6FXN ARG L  123  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN GLY L  124  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN SER L  125  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS L  126  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS L  127  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS L  128  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS L  129  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS L  130  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN HIS L  131  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN GLY L  132  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN SER L  133  UNP  Q9Y275              EXPRESSION TAG                 
SEQADV 6FXN ALA L  218  UNP  Q9Y275    HIS   218 ENGINEERED MUTATION            
SEQRES   1 A  164  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA          
SEQRES   2 A  164  VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS LEU          
SEQRES   3 A  164  GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN LYS          
SEQRES   4 A  164  GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE LYS          
SEQRES   5 A  164  ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE LEU          
SEQRES   6 A  164  VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN VAL          
SEQRES   7 A  164  LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU ILE          
SEQRES   8 A  164  GLN ARG LYS LYS VAL ALA VAL PHE GLY ASP GLU LEU SER          
SEQRES   9 A  164  LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO GLU          
SEQRES  10 A  164  THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE ALA          
SEQRES  11 A  164  LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE PRO          
SEQRES  12 A  164  ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL THR          
SEQRES  13 A  164  PHE PHE GLY ALA LEU LYS LEU LEU                              
SEQRES   1 B  164  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA          
SEQRES   2 B  164  VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS LEU          
SEQRES   3 B  164  GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN LYS          
SEQRES   4 B  164  GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE LYS          
SEQRES   5 B  164  ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE LEU          
SEQRES   6 B  164  VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN VAL          
SEQRES   7 B  164  LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU ILE          
SEQRES   8 B  164  GLN ARG LYS LYS VAL ALA VAL PHE GLY ASP GLU LEU SER          
SEQRES   9 B  164  LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO GLU          
SEQRES  10 B  164  THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE ALA          
SEQRES  11 B  164  LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE PRO          
SEQRES  12 B  164  ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL THR          
SEQRES  13 B  164  PHE PHE GLY ALA LEU LYS LEU LEU                              
SEQRES   1 C  164  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA          
SEQRES   2 C  164  VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS LEU          
SEQRES   3 C  164  GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN LYS          
SEQRES   4 C  164  GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE LYS          
SEQRES   5 C  164  ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE LEU          
SEQRES   6 C  164  VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN VAL          
SEQRES   7 C  164  LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU ILE          
SEQRES   8 C  164  GLN ARG LYS LYS VAL ALA VAL PHE GLY ASP GLU LEU SER          
SEQRES   9 C  164  LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO GLU          
SEQRES  10 C  164  THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE ALA          
SEQRES  11 C  164  LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE PRO          
SEQRES  12 C  164  ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL THR          
SEQRES  13 C  164  PHE PHE GLY ALA LEU LYS LEU LEU                              
SEQRES   1 D  225  GLN VAL GLN LEU GLN GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 D  225  PRO GLY SER SER VAL ARG VAL SER CYS LYS ALA SER GLY          
SEQRES   3 D  225  GLY THR PHE ASN ASN ASN ALA ILE ASN TRP VAL ARG GLN          
SEQRES   4 D  225  ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE          
SEQRES   5 D  225  PRO MET PHE GLY THR ALA LYS TYR SER GLN ASN PHE GLN          
SEQRES   6 D  225  GLY ARG VAL ALA ILE THR ALA ASP GLU SER THR GLY THR          
SEQRES   7 D  225  ALA SER MET GLU LEU SER SER LEU ARG SER GLU ASP THR          
SEQRES   8 D  225  ALA VAL TYR TYR CYS ALA ARG SER ARG ASP LEU LEU LEU          
SEQRES   9 D  225  PHE PRO HIS HIS ALA LEU SER PRO TRP GLY ARG GLY THR          
SEQRES  10 D  225  MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER          
SEQRES  11 D  225  VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY          
SEQRES  12 D  225  GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE          
SEQRES  13 D  225  PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU          
SEQRES  14 D  225  THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER          
SEQRES  15 D  225  SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO          
SEQRES  16 D  225  SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL          
SEQRES  17 D  225  ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL          
SEQRES  18 D  225  GLU PRO LYS SER                                              
SEQRES   1 E  214  SER SER GLU LEU THR GLN ASP PRO ALA VAL SER VAL ALA          
SEQRES   2 E  214  LEU GLY GLN THR VAL ARG VAL THR CYS GLN GLY ASP SER          
SEQRES   3 E  214  LEU ARG SER TYR TYR ALA SER TRP TYR GLN GLN LYS PRO          
SEQRES   4 E  214  GLY GLN ALA PRO VAL LEU VAL ILE TYR GLY LYS ASN ASN          
SEQRES   5 E  214  ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY SER SER          
SEQRES   6 E  214  SER GLY ASN THR ALA SER LEU THR ILE THR GLY ALA GLN          
SEQRES   7 E  214  ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SER ARG ASP          
SEQRES   8 E  214  SER SER GLY ASN HIS TRP VAL PHE GLY GLY GLY THR GLU          
SEQRES   9 E  214  LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL          
SEQRES  10 E  214  THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN          
SEQRES  11 E  214  LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO          
SEQRES  12 E  214  GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO          
SEQRES  13 E  214  VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN          
SEQRES  14 E  214  SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU          
SEQRES  15 E  214  THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS          
SEQRES  16 E  214  GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL          
SEQRES  17 E  214  ALA PRO THR GLU CYS SER                                      
SEQRES   1 F  225  GLN VAL GLN LEU GLN GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 F  225  PRO GLY SER SER VAL ARG VAL SER CYS LYS ALA SER GLY          
SEQRES   3 F  225  GLY THR PHE ASN ASN ASN ALA ILE ASN TRP VAL ARG GLN          
SEQRES   4 F  225  ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE          
SEQRES   5 F  225  PRO MET PHE GLY THR ALA LYS TYR SER GLN ASN PHE GLN          
SEQRES   6 F  225  GLY ARG VAL ALA ILE THR ALA ASP GLU SER THR GLY THR          
SEQRES   7 F  225  ALA SER MET GLU LEU SER SER LEU ARG SER GLU ASP THR          
SEQRES   8 F  225  ALA VAL TYR TYR CYS ALA ARG SER ARG ASP LEU LEU LEU          
SEQRES   9 F  225  PHE PRO HIS HIS ALA LEU SER PRO TRP GLY ARG GLY THR          
SEQRES  10 F  225  MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER          
SEQRES  11 F  225  VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY          
SEQRES  12 F  225  GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE          
SEQRES  13 F  225  PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU          
SEQRES  14 F  225  THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER          
SEQRES  15 F  225  SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO          
SEQRES  16 F  225  SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL          
SEQRES  17 F  225  ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL          
SEQRES  18 F  225  GLU PRO LYS SER                                              
SEQRES   1 G  214  SER SER GLU LEU THR GLN ASP PRO ALA VAL SER VAL ALA          
SEQRES   2 G  214  LEU GLY GLN THR VAL ARG VAL THR CYS GLN GLY ASP SER          
SEQRES   3 G  214  LEU ARG SER TYR TYR ALA SER TRP TYR GLN GLN LYS PRO          
SEQRES   4 G  214  GLY GLN ALA PRO VAL LEU VAL ILE TYR GLY LYS ASN ASN          
SEQRES   5 G  214  ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY SER SER          
SEQRES   6 G  214  SER GLY ASN THR ALA SER LEU THR ILE THR GLY ALA GLN          
SEQRES   7 G  214  ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SER ARG ASP          
SEQRES   8 G  214  SER SER GLY ASN HIS TRP VAL PHE GLY GLY GLY THR GLU          
SEQRES   9 G  214  LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL          
SEQRES  10 G  214  THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN          
SEQRES  11 G  214  LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO          
SEQRES  12 G  214  GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO          
SEQRES  13 G  214  VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN          
SEQRES  14 G  214  SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU          
SEQRES  15 G  214  THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS          
SEQRES  16 G  214  GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL          
SEQRES  17 G  214  ALA PRO THR GLU CYS SER                                      
SEQRES   1 H  225  GLN VAL GLN LEU GLN GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 H  225  PRO GLY SER SER VAL ARG VAL SER CYS LYS ALA SER GLY          
SEQRES   3 H  225  GLY THR PHE ASN ASN ASN ALA ILE ASN TRP VAL ARG GLN          
SEQRES   4 H  225  ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE          
SEQRES   5 H  225  PRO MET PHE GLY THR ALA LYS TYR SER GLN ASN PHE GLN          
SEQRES   6 H  225  GLY ARG VAL ALA ILE THR ALA ASP GLU SER THR GLY THR          
SEQRES   7 H  225  ALA SER MET GLU LEU SER SER LEU ARG SER GLU ASP THR          
SEQRES   8 H  225  ALA VAL TYR TYR CYS ALA ARG SER ARG ASP LEU LEU LEU          
SEQRES   9 H  225  PHE PRO HIS HIS ALA LEU SER PRO TRP GLY ARG GLY THR          
SEQRES  10 H  225  MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER          
SEQRES  11 H  225  VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY          
SEQRES  12 H  225  GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE          
SEQRES  13 H  225  PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU          
SEQRES  14 H  225  THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER          
SEQRES  15 H  225  SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO          
SEQRES  16 H  225  SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL          
SEQRES  17 H  225  ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL          
SEQRES  18 H  225  GLU PRO LYS SER                                              
SEQRES   1 I  214  SER SER GLU LEU THR GLN ASP PRO ALA VAL SER VAL ALA          
SEQRES   2 I  214  LEU GLY GLN THR VAL ARG VAL THR CYS GLN GLY ASP SER          
SEQRES   3 I  214  LEU ARG SER TYR TYR ALA SER TRP TYR GLN GLN LYS PRO          
SEQRES   4 I  214  GLY GLN ALA PRO VAL LEU VAL ILE TYR GLY LYS ASN ASN          
SEQRES   5 I  214  ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY SER SER          
SEQRES   6 I  214  SER GLY ASN THR ALA SER LEU THR ILE THR GLY ALA GLN          
SEQRES   7 I  214  ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SER ARG ASP          
SEQRES   8 I  214  SER SER GLY ASN HIS TRP VAL PHE GLY GLY GLY THR GLU          
SEQRES   9 I  214  LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL          
SEQRES  10 I  214  THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN          
SEQRES  11 I  214  LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO          
SEQRES  12 I  214  GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO          
SEQRES  13 I  214  VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN          
SEQRES  14 I  214  SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU          
SEQRES  15 I  214  THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS          
SEQRES  16 I  214  GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL          
SEQRES  17 I  214  ALA PRO THR GLU CYS SER                                      
SEQRES   1 J  164  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA          
SEQRES   2 J  164  VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS LEU          
SEQRES   3 J  164  GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN LYS          
SEQRES   4 J  164  GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE LYS          
SEQRES   5 J  164  ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE LEU          
SEQRES   6 J  164  VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN VAL          
SEQRES   7 J  164  LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU ILE          
SEQRES   8 J  164  GLN ARG LYS LYS VAL ALA VAL PHE GLY ASP GLU LEU SER          
SEQRES   9 J  164  LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO GLU          
SEQRES  10 J  164  THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE ALA          
SEQRES  11 J  164  LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE PRO          
SEQRES  12 J  164  ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL THR          
SEQRES  13 J  164  PHE PHE GLY ALA LEU LYS LEU LEU                              
SEQRES   1 K  164  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA          
SEQRES   2 K  164  VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS LEU          
SEQRES   3 K  164  GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN LYS          
SEQRES   4 K  164  GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE LYS          
SEQRES   5 K  164  ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE LEU          
SEQRES   6 K  164  VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN VAL          
SEQRES   7 K  164  LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU ILE          
SEQRES   8 K  164  GLN ARG LYS LYS VAL ALA VAL PHE GLY ASP GLU LEU SER          
SEQRES   9 K  164  LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO GLU          
SEQRES  10 K  164  THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE ALA          
SEQRES  11 K  164  LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE PRO          
SEQRES  12 K  164  ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL THR          
SEQRES  13 K  164  PHE PHE GLY ALA LEU LYS LEU LEU                              
SEQRES   1 L  164  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA          
SEQRES   2 L  164  VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS LEU          
SEQRES   3 L  164  GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN LYS          
SEQRES   4 L  164  GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE LYS          
SEQRES   5 L  164  ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE LEU          
SEQRES   6 L  164  VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN VAL          
SEQRES   7 L  164  LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU ILE          
SEQRES   8 L  164  GLN ARG LYS LYS VAL ALA VAL PHE GLY ASP GLU LEU SER          
SEQRES   9 L  164  LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO GLU          
SEQRES  10 L  164  THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE ALA          
SEQRES  11 L  164  LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE PRO          
SEQRES  12 L  164  ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL THR          
SEQRES  13 L  164  PHE PHE GLY ALA LEU LYS LEU LEU                              
SEQRES   1 M  225  GLN VAL GLN LEU GLN GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 M  225  PRO GLY SER SER VAL ARG VAL SER CYS LYS ALA SER GLY          
SEQRES   3 M  225  GLY THR PHE ASN ASN ASN ALA ILE ASN TRP VAL ARG GLN          
SEQRES   4 M  225  ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE          
SEQRES   5 M  225  PRO MET PHE GLY THR ALA LYS TYR SER GLN ASN PHE GLN          
SEQRES   6 M  225  GLY ARG VAL ALA ILE THR ALA ASP GLU SER THR GLY THR          
SEQRES   7 M  225  ALA SER MET GLU LEU SER SER LEU ARG SER GLU ASP THR          
SEQRES   8 M  225  ALA VAL TYR TYR CYS ALA ARG SER ARG ASP LEU LEU LEU          
SEQRES   9 M  225  PHE PRO HIS HIS ALA LEU SER PRO TRP GLY ARG GLY THR          
SEQRES  10 M  225  MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER          
SEQRES  11 M  225  VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY          
SEQRES  12 M  225  GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE          
SEQRES  13 M  225  PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU          
SEQRES  14 M  225  THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER          
SEQRES  15 M  225  SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO          
SEQRES  16 M  225  SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL          
SEQRES  17 M  225  ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL          
SEQRES  18 M  225  GLU PRO LYS SER                                              
SEQRES   1 N  214  SER SER GLU LEU THR GLN ASP PRO ALA VAL SER VAL ALA          
SEQRES   2 N  214  LEU GLY GLN THR VAL ARG VAL THR CYS GLN GLY ASP SER          
SEQRES   3 N  214  LEU ARG SER TYR TYR ALA SER TRP TYR GLN GLN LYS PRO          
SEQRES   4 N  214  GLY GLN ALA PRO VAL LEU VAL ILE TYR GLY LYS ASN ASN          
SEQRES   5 N  214  ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY SER SER          
SEQRES   6 N  214  SER GLY ASN THR ALA SER LEU THR ILE THR GLY ALA GLN          
SEQRES   7 N  214  ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SER ARG ASP          
SEQRES   8 N  214  SER SER GLY ASN HIS TRP VAL PHE GLY GLY GLY THR GLU          
SEQRES   9 N  214  LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL          
SEQRES  10 N  214  THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN          
SEQRES  11 N  214  LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO          
SEQRES  12 N  214  GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO          
SEQRES  13 N  214  VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN          
SEQRES  14 N  214  SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU          
SEQRES  15 N  214  THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS          
SEQRES  16 N  214  GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL          
SEQRES  17 N  214  ALA PRO THR GLU CYS SER                                      
SEQRES   1 O  225  GLN VAL GLN LEU GLN GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 O  225  PRO GLY SER SER VAL ARG VAL SER CYS LYS ALA SER GLY          
SEQRES   3 O  225  GLY THR PHE ASN ASN ASN ALA ILE ASN TRP VAL ARG GLN          
SEQRES   4 O  225  ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE          
SEQRES   5 O  225  PRO MET PHE GLY THR ALA LYS TYR SER GLN ASN PHE GLN          
SEQRES   6 O  225  GLY ARG VAL ALA ILE THR ALA ASP GLU SER THR GLY THR          
SEQRES   7 O  225  ALA SER MET GLU LEU SER SER LEU ARG SER GLU ASP THR          
SEQRES   8 O  225  ALA VAL TYR TYR CYS ALA ARG SER ARG ASP LEU LEU LEU          
SEQRES   9 O  225  PHE PRO HIS HIS ALA LEU SER PRO TRP GLY ARG GLY THR          
SEQRES  10 O  225  MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER          
SEQRES  11 O  225  VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY          
SEQRES  12 O  225  GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE          
SEQRES  13 O  225  PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU          
SEQRES  14 O  225  THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER          
SEQRES  15 O  225  SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO          
SEQRES  16 O  225  SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL          
SEQRES  17 O  225  ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL          
SEQRES  18 O  225  GLU PRO LYS SER                                              
SEQRES   1 P  214  SER SER GLU LEU THR GLN ASP PRO ALA VAL SER VAL ALA          
SEQRES   2 P  214  LEU GLY GLN THR VAL ARG VAL THR CYS GLN GLY ASP SER          
SEQRES   3 P  214  LEU ARG SER TYR TYR ALA SER TRP TYR GLN GLN LYS PRO          
SEQRES   4 P  214  GLY GLN ALA PRO VAL LEU VAL ILE TYR GLY LYS ASN ASN          
SEQRES   5 P  214  ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY SER SER          
SEQRES   6 P  214  SER GLY ASN THR ALA SER LEU THR ILE THR GLY ALA GLN          
SEQRES   7 P  214  ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SER ARG ASP          
SEQRES   8 P  214  SER SER GLY ASN HIS TRP VAL PHE GLY GLY GLY THR GLU          
SEQRES   9 P  214  LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL          
SEQRES  10 P  214  THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN          
SEQRES  11 P  214  LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO          
SEQRES  12 P  214  GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO          
SEQRES  13 P  214  VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN          
SEQRES  14 P  214  SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU          
SEQRES  15 P  214  THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS          
SEQRES  16 P  214  GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL          
SEQRES  17 P  214  ALA PRO THR GLU CYS SER                                      
SEQRES   1 Q  225  GLN VAL GLN LEU GLN GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 Q  225  PRO GLY SER SER VAL ARG VAL SER CYS LYS ALA SER GLY          
SEQRES   3 Q  225  GLY THR PHE ASN ASN ASN ALA ILE ASN TRP VAL ARG GLN          
SEQRES   4 Q  225  ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE          
SEQRES   5 Q  225  PRO MET PHE GLY THR ALA LYS TYR SER GLN ASN PHE GLN          
SEQRES   6 Q  225  GLY ARG VAL ALA ILE THR ALA ASP GLU SER THR GLY THR          
SEQRES   7 Q  225  ALA SER MET GLU LEU SER SER LEU ARG SER GLU ASP THR          
SEQRES   8 Q  225  ALA VAL TYR TYR CYS ALA ARG SER ARG ASP LEU LEU LEU          
SEQRES   9 Q  225  PHE PRO HIS HIS ALA LEU SER PRO TRP GLY ARG GLY THR          
SEQRES  10 Q  225  MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER          
SEQRES  11 Q  225  VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY          
SEQRES  12 Q  225  GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE          
SEQRES  13 Q  225  PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU          
SEQRES  14 Q  225  THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER          
SEQRES  15 Q  225  SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO          
SEQRES  16 Q  225  SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL          
SEQRES  17 Q  225  ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL          
SEQRES  18 Q  225  GLU PRO LYS SER                                              
SEQRES   1 R  214  SER SER GLU LEU THR GLN ASP PRO ALA VAL SER VAL ALA          
SEQRES   2 R  214  LEU GLY GLN THR VAL ARG VAL THR CYS GLN GLY ASP SER          
SEQRES   3 R  214  LEU ARG SER TYR TYR ALA SER TRP TYR GLN GLN LYS PRO          
SEQRES   4 R  214  GLY GLN ALA PRO VAL LEU VAL ILE TYR GLY LYS ASN ASN          
SEQRES   5 R  214  ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY SER SER          
SEQRES   6 R  214  SER GLY ASN THR ALA SER LEU THR ILE THR GLY ALA GLN          
SEQRES   7 R  214  ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SER ARG ASP          
SEQRES   8 R  214  SER SER GLY ASN HIS TRP VAL PHE GLY GLY GLY THR GLU          
SEQRES   9 R  214  LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL          
SEQRES  10 R  214  THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN          
SEQRES  11 R  214  LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO          
SEQRES  12 R  214  GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO          
SEQRES  13 R  214  VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN          
SEQRES  14 R  214  SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU          
SEQRES  15 R  214  THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS          
SEQRES  16 R  214  GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL          
SEQRES  17 R  214  ALA PRO THR GLU CYS SER                                      
FORMUL  19  HOH   *270(H2 O)                                                    
HELIX    1 AA1 ARG D   87  THR D   91  5                                   5    
HELIX    2 AA2 SER D  166  ALA D  168  5                                   3    
HELIX    3 AA3 ASP E   25  SER E   29  5                                   5    
HELIX    4 AA4 GLN E   78  GLU E   82  5                                   5    
HELIX    5 AA5 SER E  123  ALA E  129  1                                   7    
HELIX    6 AA6 THR E  183  HIS E  190  1                                   8    
HELIX    7 AA7 ARG F   87  THR F   91  5                                   5    
HELIX    8 AA8 SER F  197  LEU F  199  5                                   3    
HELIX    9 AA9 ASP G   25  SER G   29  5                                   5    
HELIX   10 AB1 GLN G   78  GLU G   82  5                                   5    
HELIX   11 AB2 SER G  123  ALA G  129  1                                   7    
HELIX   12 AB3 THR G  183  HIS G  190  1                                   8    
HELIX   13 AB4 GLN H   62  GLN H   65  5                                   4    
HELIX   14 AB5 ARG H   87  THR H   91  5                                   5    
HELIX   15 AB6 LYS H  211  ASN H  214  5                                   4    
HELIX   16 AB7 ASP I   25  SER I   29  5                                   5    
HELIX   17 AB8 GLN I   78  GLU I   82  5                                   5    
HELIX   18 AB9 SER I  123  ALA I  129  1                                   7    
HELIX   19 AC1 THR I  183  SER I  189  1                                   7    
HELIX   20 AC2 ARG M   87  THR M   91  5                                   5    
HELIX   21 AC3 PRO M  195  LEU M  199  5                                   5    
HELIX   22 AC4 ASP N   25  SER N   29  5                                   5    
HELIX   23 AC5 GLN N   78  GLU N   82  5                                   5    
HELIX   24 AC6 SER N  123  ALA N  129  1                                   7    
HELIX   25 AC7 THR N  183  HIS N  190  1                                   8    
HELIX   26 AC8 GLN O   62  GLN O   65  5                                   4    
HELIX   27 AC9 ARG O   87  THR O   91  5                                   5    
HELIX   28 AD1 ASP P   25  SER P   29  5                                   5    
HELIX   29 AD2 GLN P   78  GLU P   82  5                                   5    
HELIX   30 AD3 SER P  123  ALA P  129  1                                   7    
HELIX   31 AD4 THR P  183  HIS P  190  1                                   8    
HELIX   32 AD5 ARG Q   87  THR Q   91  5                                   5    
HELIX   33 AD6 ASP R   25  SER R   29  5                                   5    
HELIX   34 AD7 GLN R   78  GLU R   82  5                                   5    
HELIX   35 AD8 SER R  123  ALA R  129  1                                   7    
HELIX   36 AD9 THR R  183  HIS R  190  1                                   8    
SHEET    1 AA1 5 TRP A 168  ARG A 174  0                                        
SHEET    2 AA1 5 CYS A 146  ALA A 151 -1  N  CYS A 146   O  ARG A 174           
SHEET    3 AA1 5 PHE A 278  LYS A 283 -1  O  PHE A 279   N  LEU A 149           
SHEET    4 AA1 5 GLY A 191  TYR A 201 -1  N  TYR A 196   O  GLY A 280           
SHEET    5 AA1 5 ASN A 243  LEU A 253 -1  O  ALA A 251   N  PHE A 193           
SHEET    1 AA2 5 TRP A 168  ARG A 174  0                                        
SHEET    2 AA2 5 CYS A 146  ALA A 151 -1  N  CYS A 146   O  ARG A 174           
SHEET    3 AA2 5 PHE A 278  LYS A 283 -1  O  PHE A 279   N  LEU A 149           
SHEET    4 AA2 5 GLY A 191  TYR A 201 -1  N  TYR A 196   O  GLY A 280           
SHEET    5 AA2 5 ILE A 270  SER A 271 -1  O  SER A 271   N  LEU A 200           
SHEET    1 AA3 5 ILE A 158  LYS A 160  0                                        
SHEET    2 AA3 5 TYR A 163  PHE A 165 -1  O  PHE A 165   N  ILE A 158           
SHEET    3 AA3 5 GLU A 258  ILE A 263 -1  O  ILE A 263   N  THR A 164           
SHEET    4 AA3 5 LYS A 184  VAL A 187 -1  N  ILE A 185   O  LEU A 259           
SHEET    5 AA3 5 LEU A 178  LYS A 181 -1  N  GLU A 179   O  LEU A 186           
SHEET    1 AA4 5 ILE A 158  LYS A 160  0                                        
SHEET    2 AA4 5 TYR A 163  PHE A 165 -1  O  PHE A 165   N  ILE A 158           
SHEET    3 AA4 5 GLU A 258  ILE A 263 -1  O  ILE A 263   N  THR A 164           
SHEET    4 AA4 5 ALA A 207  LYS A 215 -1  N  LEU A 211   O  ALA A 262           
SHEET    5 AA4 5 LEU A 226  ASN A 235 -1  O  VAL A 227   N  ARG A 214           
SHEET    1 AA5 5 TRP B 168  ARG B 174  0                                        
SHEET    2 AA5 5 CYS B 146  ALA B 151 -1  N  ILE B 150   O  LEU B 169           
SHEET    3 AA5 5 PHE B 278  LYS B 283 -1  O  PHE B 279   N  LEU B 149           
SHEET    4 AA5 5 GLY B 191  TYR B 201 -1  N  TYR B 196   O  GLY B 280           
SHEET    5 AA5 5 ASN B 243  LEU B 253 -1  O  GLY B 249   N  ILE B 195           
SHEET    1 AA6 5 ILE B 158  LYS B 160  0                                        
SHEET    2 AA6 5 TYR B 163  PHE B 165 -1  O  PHE B 165   N  ILE B 158           
SHEET    3 AA6 5 GLU B 258  ILE B 263 -1  O  ILE B 263   N  THR B 164           
SHEET    4 AA6 5 LYS B 184  VAL B 187 -1  N  ILE B 185   O  LEU B 259           
SHEET    5 AA6 5 LEU B 178  LYS B 181 -1  N  GLU B 179   O  LEU B 186           
SHEET    1 AA7 5 ILE B 158  LYS B 160  0                                        
SHEET    2 AA7 5 TYR B 163  PHE B 165 -1  O  PHE B 165   N  ILE B 158           
SHEET    3 AA7 5 GLU B 258  ILE B 263 -1  O  ILE B 263   N  THR B 164           
SHEET    4 AA7 5 ALA B 207  LYS B 215 -1  N  LYS B 215   O  GLU B 258           
SHEET    5 AA7 5 LEU B 226  ASN B 235 -1  O  LEU B 229   N  ILE B 212           
SHEET    1 AA8 5 TRP C 168  ARG C 174  0                                        
SHEET    2 AA8 5 CYS C 146  ALA C 151 -1  N  CYS C 146   O  ARG C 174           
SHEET    3 AA8 5 PHE C 278  LYS C 283 -1  O  PHE C 279   N  LEU C 149           
SHEET    4 AA8 5 GLY C 191  TYR C 201 -1  N  PHE C 194   O  LEU C 282           
SHEET    5 AA8 5 ASN C 243  LEU C 253 -1  O  GLY C 249   N  ILE C 195           
SHEET    1 AA9 5 ILE C 158  LYS C 160  0                                        
SHEET    2 AA9 5 TYR C 163  PHE C 165 -1  O  PHE C 165   N  ILE C 158           
SHEET    3 AA9 5 GLU C 258  ILE C 263 -1  O  ILE C 263   N  THR C 164           
SHEET    4 AA9 5 LYS C 184  VAL C 187 -1  N  ILE C 185   O  LEU C 259           
SHEET    5 AA9 5 LEU C 178  LYS C 181 -1  N  GLU C 179   O  LEU C 186           
SHEET    1 AB1 5 ILE C 158  LYS C 160  0                                        
SHEET    2 AB1 5 TYR C 163  PHE C 165 -1  O  PHE C 165   N  ILE C 158           
SHEET    3 AB1 5 GLU C 258  ILE C 263 -1  O  ILE C 263   N  THR C 164           
SHEET    4 AB1 5 ALA C 207  LYS C 215 -1  N  LEU C 211   O  ALA C 262           
SHEET    5 AB1 5 LEU C 226  ASN C 235 -1  O  VAL C 227   N  ARG C 214           
SHEET    1 AB2 4 GLN D   3  GLN D   6  0                                        
SHEET    2 AB2 4 VAL D  18  SER D  25 -1  O  LYS D  23   N  GLN D   5           
SHEET    3 AB2 4 THR D  78  LEU D  83 -1  O  MET D  81   N  VAL D  20           
SHEET    4 AB2 4 VAL D  68  ASP D  73 -1  N  ASP D  73   O  THR D  78           
SHEET    1 AB3 6 GLU D  10  LYS D  12  0                                        
SHEET    2 AB3 6 THR D 117  VAL D 121  1  O  THR D 120   N  LYS D  12           
SHEET    3 AB3 6 ALA D  92  ALA D  97 -1  N  ALA D  92   O  VAL D 119           
SHEET    4 AB3 6 ILE D  34  GLN D  39 -1  N  VAL D  37   O  TYR D  95           
SHEET    5 AB3 6 LEU D  45  ILE D  51 -1  O  GLY D  49   N  TRP D  36           
SHEET    6 AB3 6 LYS D  59  TYR D  60 -1  O  LYS D  59   N  GLY D  50           
SHEET    1 AB4 4 SER D 130  LEU D 134  0                                        
SHEET    2 AB4 4 ALA D 146  TYR D 155 -1  O  LEU D 151   N  PHE D 132           
SHEET    3 AB4 4 TYR D 186  VAL D 194 -1  O  TYR D 186   N  TYR D 155           
SHEET    4 AB4 4 VAL D 173  THR D 175 -1  N  HIS D 174   O  VAL D 191           
SHEET    1 AB5 4 SER D 130  LEU D 134  0                                        
SHEET    2 AB5 4 ALA D 146  TYR D 155 -1  O  LEU D 151   N  PHE D 132           
SHEET    3 AB5 4 TYR D 186  VAL D 194 -1  O  TYR D 186   N  TYR D 155           
SHEET    4 AB5 4 VAL D 179  LEU D 180 -1  N  VAL D 179   O  SER D 187           
SHEET    1 AB6 3 THR D 161  TRP D 164  0                                        
SHEET    2 AB6 3 ILE D 205  HIS D 210 -1  O  ASN D 207   N  SER D 163           
SHEET    3 AB6 3 THR D 215  LYS D 220 -1  O  VAL D 217   N  VAL D 208           
SHEET    1 AB7 4 THR E   5  GLN E   6  0                                        
SHEET    2 AB7 4 VAL E  18  GLN E  23 -1  O  GLN E  23   N  THR E   5           
SHEET    3 AB7 4 THR E  69  ILE E  74 -1  O  ALA E  70   N  CYS E  22           
SHEET    4 AB7 4 PHE E  61  SER E  66 -1  N  SER E  62   O  THR E  73           
SHEET    1 AB8 5 ALA E   9  ALA E  13  0                                        
SHEET    2 AB8 5 THR E 103  LEU E 108  1  O  GLU E 104   N  VAL E  10           
SHEET    3 AB8 5 ASP E  84  SER E  89 -1  N  TYR E  85   O  THR E 103           
SHEET    4 AB8 5 SER E  33  GLN E  37 -1  N  SER E  33   O  SER E  88           
SHEET    5 AB8 5 VAL E  44  TYR E  48 -1  O  VAL E  44   N  GLN E  36           
SHEET    1 AB9 4 ALA E   9  ALA E  13  0                                        
SHEET    2 AB9 4 THR E 103  LEU E 108  1  O  GLU E 104   N  VAL E  10           
SHEET    3 AB9 4 ASP E  84  SER E  89 -1  N  TYR E  85   O  THR E 103           
SHEET    4 AB9 4 VAL E  98  PHE E  99 -1  O  VAL E  98   N  SER E  89           
SHEET    1 AC1 4 SER E 116  PHE E 120  0                                        
SHEET    2 AC1 4 ALA E 132  PHE E 141 -1  O  LEU E 137   N  THR E 118           
SHEET    3 AC1 4 TYR E 174  LEU E 182 -1  O  LEU E 182   N  ALA E 132           
SHEET    4 AC1 4 VAL E 161  THR E 163 -1  N  GLU E 162   O  TYR E 179           
SHEET    1 AC2 4 SER E 116  PHE E 120  0                                        
SHEET    2 AC2 4 ALA E 132  PHE E 141 -1  O  LEU E 137   N  THR E 118           
SHEET    3 AC2 4 TYR E 174  LEU E 182 -1  O  LEU E 182   N  ALA E 132           
SHEET    4 AC2 4 SER E 167  LYS E 168 -1  N  SER E 167   O  ALA E 175           
SHEET    1 AC3 4 SER E 155  PRO E 156  0                                        
SHEET    2 AC3 4 THR E 147  ALA E 152 -1  N  ALA E 152   O  SER E 155           
SHEET    3 AC3 4 TYR E 193  HIS E 199 -1  O  GLN E 196   N  ALA E 149           
SHEET    4 AC3 4 SER E 202  VAL E 208 -1  O  VAL E 204   N  VAL E 197           
SHEET    1 AC4 4 LEU F   4  GLN F   6  0                                        
SHEET    2 AC4 4 VAL F  18  ALA F  24 -1  O  LYS F  23   N  GLN F   5           
SHEET    3 AC4 4 THR F  78  LEU F  83 -1  O  ALA F  79   N  CYS F  22           
SHEET    4 AC4 4 VAL F  68  ASP F  73 -1  N  ALA F  69   O  GLU F  82           
SHEET    1 AC5 6 GLU F  10  LYS F  12  0                                        
SHEET    2 AC5 6 THR F 117  VAL F 121  1  O  THR F 120   N  LYS F  12           
SHEET    3 AC5 6 ALA F  92  SER F  99 -1  N  ALA F  92   O  VAL F 119           
SHEET    4 AC5 6 ALA F  33  GLN F  39 -1  N  ALA F  33   O  SER F  99           
SHEET    5 AC5 6 GLU F  46  ILE F  51 -1  O  ILE F  51   N  ILE F  34           
SHEET    6 AC5 6 LYS F  59  TYR F  60 -1  O  LYS F  59   N  GLY F  50           
SHEET    1 AC6 4 SER F 130  LEU F 134  0                                        
SHEET    2 AC6 4 THR F 145  TYR F 155 -1  O  LEU F 151   N  PHE F 132           
SHEET    3 AC6 4 TYR F 186  PRO F 195 -1  O  LEU F 188   N  VAL F 152           
SHEET    4 AC6 4 VAL F 173  THR F 175 -1  N  HIS F 174   O  VAL F 191           
SHEET    1 AC7 4 SER F 130  LEU F 134  0                                        
SHEET    2 AC7 4 THR F 145  TYR F 155 -1  O  LEU F 151   N  PHE F 132           
SHEET    3 AC7 4 TYR F 186  PRO F 195 -1  O  LEU F 188   N  VAL F 152           
SHEET    4 AC7 4 VAL F 179  LEU F 180 -1  N  VAL F 179   O  SER F 187           
SHEET    1 AC8 3 THR F 161  TRP F 164  0                                        
SHEET    2 AC8 3 TYR F 204  HIS F 210 -1  O  ASN F 207   N  SER F 163           
SHEET    3 AC8 3 THR F 215  VAL F 221 -1  O  VAL F 221   N  TYR F 204           
SHEET    1 AC9 4 THR G   5  GLN G   6  0                                        
SHEET    2 AC9 4 VAL G  18  GLN G  23 -1  O  GLN G  23   N  THR G   5           
SHEET    3 AC9 4 THR G  69  ILE G  74 -1  O  ALA G  70   N  CYS G  22           
SHEET    4 AC9 4 PHE G  61  SER G  66 -1  N  SER G  62   O  THR G  73           
SHEET    1 AD1 5 ALA G   9  ALA G  13  0                                        
SHEET    2 AD1 5 THR G 103  LEU G 108  1  O  LEU G 108   N  VAL G  12           
SHEET    3 AD1 5 ASP G  84  SER G  89 -1  N  TYR G  85   O  THR G 103           
SHEET    4 AD1 5 SER G  33  GLN G  37 -1  N  GLN G  37   O  ASP G  84           
SHEET    5 AD1 5 VAL G  44  ILE G  47 -1  O  VAL G  46   N  TRP G  34           
SHEET    1 AD2 4 ALA G   9  ALA G  13  0                                        
SHEET    2 AD2 4 THR G 103  LEU G 108  1  O  LEU G 108   N  VAL G  12           
SHEET    3 AD2 4 ASP G  84  SER G  89 -1  N  TYR G  85   O  THR G 103           
SHEET    4 AD2 4 VAL G  98  PHE G  99 -1  O  VAL G  98   N  SER G  89           
SHEET    1 AD3 4 SER G 116  PHE G 120  0                                        
SHEET    2 AD3 4 ALA G 132  PHE G 141 -1  O  LEU G 137   N  THR G 118           
SHEET    3 AD3 4 TYR G 174  LEU G 182 -1  O  LEU G 182   N  ALA G 132           
SHEET    4 AD3 4 VAL G 161  THR G 163 -1  N  GLU G 162   O  TYR G 179           
SHEET    1 AD4 4 SER G 116  PHE G 120  0                                        
SHEET    2 AD4 4 ALA G 132  PHE G 141 -1  O  LEU G 137   N  THR G 118           
SHEET    3 AD4 4 TYR G 174  LEU G 182 -1  O  LEU G 182   N  ALA G 132           
SHEET    4 AD4 4 SER G 167  LYS G 168 -1  N  SER G 167   O  ALA G 175           
SHEET    1 AD5 4 SER G 155  PRO G 156  0                                        
SHEET    2 AD5 4 THR G 147  ALA G 152 -1  N  ALA G 152   O  SER G 155           
SHEET    3 AD5 4 TYR G 193  HIS G 199 -1  O  THR G 198   N  THR G 147           
SHEET    4 AD5 4 SER G 202  VAL G 208 -1  O  VAL G 208   N  TYR G 193           
SHEET    1 AD6 4 LEU H   4  GLN H   6  0                                        
SHEET    2 AD6 4 CYS H  22  ALA H  24 -1  O  LYS H  23   N  GLN H   5           
SHEET    3 AD6 4 THR H  78  LEU H  83 -1  O  ALA H  79   N  CYS H  22           
SHEET    4 AD6 4 VAL H  18  ARG H  19 -1  N  VAL H  18   O  LEU H  83           
SHEET    1 AD7 4 LEU H   4  GLN H   6  0                                        
SHEET    2 AD7 4 CYS H  22  ALA H  24 -1  O  LYS H  23   N  GLN H   5           
SHEET    3 AD7 4 THR H  78  LEU H  83 -1  O  ALA H  79   N  CYS H  22           
SHEET    4 AD7 4 VAL H  68  ASP H  73 -1  N  ALA H  69   O  GLU H  82           
SHEET    1 AD8 6 GLU H  10  LYS H  12  0                                        
SHEET    2 AD8 6 THR H 117  VAL H 121  1  O  THR H 120   N  LYS H  12           
SHEET    3 AD8 6 ALA H  92  ARG H 100 -1  N  TYR H  94   O  THR H 117           
SHEET    4 AD8 6 ASN H  32  GLN H  39 -1  N  VAL H  37   O  TYR H  95           
SHEET    5 AD8 6 LEU H  45  ILE H  51 -1  O  ILE H  51   N  ILE H  34           
SHEET    6 AD8 6 LYS H  59  TYR H  60 -1  O  LYS H  59   N  GLY H  50           
SHEET    1 AD9 4 SER H 130  LEU H 134  0                                        
SHEET    2 AD9 4 ALA H 146  TYR H 155 -1  O  LYS H 153   N  SER H 130           
SHEET    3 AD9 4 TYR H 186  VAL H 194 -1  O  TYR H 186   N  TYR H 155           
SHEET    4 AD9 4 VAL H 173  THR H 175 -1  N  HIS H 174   O  VAL H 191           
SHEET    1 AE1 4 SER H 130  LEU H 134  0                                        
SHEET    2 AE1 4 ALA H 146  TYR H 155 -1  O  LYS H 153   N  SER H 130           
SHEET    3 AE1 4 TYR H 186  VAL H 194 -1  O  TYR H 186   N  TYR H 155           
SHEET    4 AE1 4 VAL H 179  LEU H 180 -1  N  VAL H 179   O  SER H 187           
SHEET    1 AE2 3 THR H 161  TRP H 164  0                                        
SHEET    2 AE2 3 TYR H 204  HIS H 210 -1  O  ASN H 209   N  THR H 161           
SHEET    3 AE2 3 THR H 215  VAL H 221 -1  O  VAL H 221   N  TYR H 204           
SHEET    1 AE3 4 THR I   5  GLN I   6  0                                        
SHEET    2 AE3 4 VAL I  18  GLN I  23 -1  O  GLN I  23   N  THR I   5           
SHEET    3 AE3 4 THR I  69  ILE I  74 -1  O  ALA I  70   N  CYS I  22           
SHEET    4 AE3 4 PHE I  61  SER I  62 -1  N  SER I  62   O  THR I  73           
SHEET    1 AE4 4 THR I   5  GLN I   6  0                                        
SHEET    2 AE4 4 VAL I  18  GLN I  23 -1  O  GLN I  23   N  THR I   5           
SHEET    3 AE4 4 THR I  69  ILE I  74 -1  O  ALA I  70   N  CYS I  22           
SHEET    4 AE4 4 SER I  65  SER I  66 -1  N  SER I  66   O  THR I  69           
SHEET    1 AE5 5 ALA I   9  ALA I  13  0                                        
SHEET    2 AE5 5 THR I 103  LEU I 108  1  O  LEU I 108   N  VAL I  12           
SHEET    3 AE5 5 ASP I  84  SER I  89 -1  N  TYR I  85   O  THR I 103           
SHEET    4 AE5 5 SER I  33  GLN I  37 -1  N  GLN I  37   O  ASP I  84           
SHEET    5 AE5 5 VAL I  44  ILE I  47 -1  O  VAL I  44   N  GLN I  36           
SHEET    1 AE6 4 ALA I   9  ALA I  13  0                                        
SHEET    2 AE6 4 THR I 103  LEU I 108  1  O  LEU I 108   N  VAL I  12           
SHEET    3 AE6 4 ASP I  84  SER I  89 -1  N  TYR I  85   O  THR I 103           
SHEET    4 AE6 4 VAL I  98  PHE I  99 -1  O  VAL I  98   N  SER I  89           
SHEET    1 AE7 4 SER I 116  PHE I 120  0                                        
SHEET    2 AE7 4 ALA I 132  PHE I 141 -1  O  LEU I 137   N  THR I 118           
SHEET    3 AE7 4 TYR I 174  LEU I 182 -1  O  ALA I 176   N  ILE I 138           
SHEET    4 AE7 4 VAL I 161  THR I 163 -1  N  GLU I 162   O  TYR I 179           
SHEET    1 AE8 4 SER I 116  PHE I 120  0                                        
SHEET    2 AE8 4 ALA I 132  PHE I 141 -1  O  LEU I 137   N  THR I 118           
SHEET    3 AE8 4 TYR I 174  LEU I 182 -1  O  ALA I 176   N  ILE I 138           
SHEET    4 AE8 4 SER I 167  LYS I 168 -1  N  SER I 167   O  ALA I 175           
SHEET    1 AE9 4 SER I 155  PRO I 156  0                                        
SHEET    2 AE9 4 THR I 147  ALA I 152 -1  N  ALA I 152   O  SER I 155           
SHEET    3 AE9 4 TYR I 193  HIS I 199 -1  O  THR I 198   N  THR I 147           
SHEET    4 AE9 4 SER I 202  VAL I 208 -1  O  SER I 202   N  HIS I 199           
SHEET    1 AF1 5 TRP J 168  ARG J 174  0                                        
SHEET    2 AF1 5 CYS J 146  ALA J 151 -1  N  ILE J 150   O  LEU J 169           
SHEET    3 AF1 5 PHE J 278  LYS J 283 -1  O  PHE J 279   N  LEU J 149           
SHEET    4 AF1 5 GLY J 191  TYR J 201 -1  N  GLN J 198   O  PHE J 278           
SHEET    5 AF1 5 ASN J 243  LEU J 253 -1  O  ASN J 243   N  TYR J 201           
SHEET    1 AF2 2 ILE J 158  LYS J 160  0                                        
SHEET    2 AF2 2 TYR J 163  PHE J 165 -1  O  PHE J 165   N  ILE J 158           
SHEET    1 AF3 5 LEU J 178  LYS J 181  0                                        
SHEET    2 AF3 5 LYS J 184  VAL J 187 -1  O  LEU J 186   N  GLU J 179           
SHEET    3 AF3 5 GLU J 258  ALA J 262 -1  O  LEU J 259   N  ILE J 185           
SHEET    4 AF3 5 ALA J 207  LYS J 215 -1  N  LEU J 211   O  ALA J 262           
SHEET    5 AF3 5 LEU J 226  ASN J 235 -1  O  VAL J 227   N  ARG J 214           
SHEET    1 AF4 5 TRP K 168  ARG K 174  0                                        
SHEET    2 AF4 5 CYS K 146  ALA K 151 -1  N  CYS K 146   O  ARG K 174           
SHEET    3 AF4 5 PHE K 278  LYS K 283 -1  O  PHE K 279   N  LEU K 149           
SHEET    4 AF4 5 GLY K 191  TYR K 201 -1  N  TYR K 196   O  GLY K 280           
SHEET    5 AF4 5 ASN K 243  LEU K 253 -1  O  ALA K 251   N  PHE K 193           
SHEET    1 AF5 2 ILE K 158  LYS K 160  0                                        
SHEET    2 AF5 2 TYR K 163  PHE K 165 -1  O  PHE K 165   N  ILE K 158           
SHEET    1 AF6 5 LEU K 178  LYS K 181  0                                        
SHEET    2 AF6 5 LYS K 184  VAL K 187 -1  O  LEU K 186   N  GLU K 179           
SHEET    3 AF6 5 GLU K 258  ALA K 262 -1  O  LEU K 259   N  ILE K 185           
SHEET    4 AF6 5 ALA K 207  LYS K 215 -1  N  LYS K 215   O  GLU K 258           
SHEET    5 AF6 5 LEU K 226  ASN K 235 -1  O  VAL K 227   N  ARG K 214           
SHEET    1 AF7 5 TRP L 168  ARG L 174  0                                        
SHEET    2 AF7 5 CYS L 146  ALA L 151 -1  N  ILE L 150   O  LEU L 169           
SHEET    3 AF7 5 PHE L 278  LYS L 283 -1  O  PHE L 279   N  LEU L 149           
SHEET    4 AF7 5 GLY L 191  TYR L 201 -1  N  PHE L 194   O  LEU L 282           
SHEET    5 AF7 5 ASN L 243  LEU L 253 -1  O  GLY L 249   N  ILE L 195           
SHEET    1 AF8 2 ILE L 158  LYS L 160  0                                        
SHEET    2 AF8 2 TYR L 163  PHE L 165 -1  O  PHE L 165   N  ILE L 158           
SHEET    1 AF9 5 LEU L 178  GLU L 180  0                                        
SHEET    2 AF9 5 ILE L 185  VAL L 187 -1  O  LEU L 186   N  GLU L 179           
SHEET    3 AF9 5 GLU L 258  ALA L 262 -1  O  LEU L 259   N  ILE L 185           
SHEET    4 AF9 5 ALA L 207  LYS L 215 -1  N  LEU L 211   O  ALA L 262           
SHEET    5 AF9 5 LEU L 226  ASN L 235 -1  O  VAL L 227   N  ARG L 214           
SHEET    1 AG1 4 LEU M   4  GLN M   6  0                                        
SHEET    2 AG1 4 VAL M  18  ALA M  24 -1  O  LYS M  23   N  GLN M   5           
SHEET    3 AG1 4 THR M  78  LEU M  83 -1  O  MET M  81   N  VAL M  20           
SHEET    4 AG1 4 VAL M  68  ASP M  73 -1  N  ALA M  69   O  GLU M  82           
SHEET    1 AG2 6 VAL M  11  LYS M  12  0                                        
SHEET    2 AG2 6 THR M 117  VAL M 121  1  O  THR M 120   N  LYS M  12           
SHEET    3 AG2 6 ALA M  92  SER M  99 -1  N  TYR M  94   O  THR M 117           
SHEET    4 AG2 6 ALA M  33  GLN M  39 -1  N  ALA M  33   O  SER M  99           
SHEET    5 AG2 6 GLU M  46  ILE M  51 -1  O  ILE M  51   N  ILE M  34           
SHEET    6 AG2 6 LYS M  59  TYR M  60 -1  O  LYS M  59   N  GLY M  50           
SHEET    1 AG3 4 VAL M  11  LYS M  12  0                                        
SHEET    2 AG3 4 THR M 117  VAL M 121  1  O  THR M 120   N  LYS M  12           
SHEET    3 AG3 4 ALA M  92  SER M  99 -1  N  TYR M  94   O  THR M 117           
SHEET    4 AG3 4 LEU M 110  TRP M 113 -1  O  SER M 111   N  ARG M  98           
SHEET    1 AG4 4 SER M 130  LEU M 134  0                                        
SHEET    2 AG4 4 ALA M 146  TYR M 155 -1  O  LYS M 153   N  SER M 130           
SHEET    3 AG4 4 TYR M 186  VAL M 194 -1  O  TYR M 186   N  TYR M 155           
SHEET    4 AG4 4 VAL M 173  THR M 175 -1  N  HIS M 174   O  VAL M 191           
SHEET    1 AG5 4 SER M 130  LEU M 134  0                                        
SHEET    2 AG5 4 ALA M 146  TYR M 155 -1  O  LYS M 153   N  SER M 130           
SHEET    3 AG5 4 TYR M 186  VAL M 194 -1  O  TYR M 186   N  TYR M 155           
SHEET    4 AG5 4 VAL M 179  LEU M 180 -1  N  VAL M 179   O  SER M 187           
SHEET    1 AG6 3 THR M 161  TRP M 164  0                                        
SHEET    2 AG6 3 TYR M 204  HIS M 210 -1  O  ASN M 209   N  THR M 161           
SHEET    3 AG6 3 THR M 215  VAL M 221 -1  O  THR M 215   N  HIS M 210           
SHEET    1 AG7 4 THR N   5  GLN N   6  0                                        
SHEET    2 AG7 4 VAL N  18  GLN N  23 -1  O  GLN N  23   N  THR N   5           
SHEET    3 AG7 4 THR N  69  ILE N  74 -1  O  LEU N  72   N  VAL N  20           
SHEET    4 AG7 4 PHE N  61  SER N  66 -1  N  SER N  66   O  THR N  69           
SHEET    1 AG8 5 ALA N   9  ALA N  13  0                                        
SHEET    2 AG8 5 THR N 103  LEU N 108  1  O  GLU N 104   N  VAL N  10           
SHEET    3 AG8 5 ALA N  83  SER N  89 -1  N  ALA N  83   O  LEU N 105           
SHEET    4 AG8 5 SER N  33  GLN N  37 -1  N  GLN N  37   O  ASP N  84           
SHEET    5 AG8 5 VAL N  44  TYR N  48 -1  O  ILE N  47   N  TRP N  34           
SHEET    1 AG9 4 ALA N   9  ALA N  13  0                                        
SHEET    2 AG9 4 THR N 103  LEU N 108  1  O  GLU N 104   N  VAL N  10           
SHEET    3 AG9 4 ALA N  83  SER N  89 -1  N  ALA N  83   O  LEU N 105           
SHEET    4 AG9 4 VAL N  98  PHE N  99 -1  O  VAL N  98   N  SER N  89           
SHEET    1 AH1 4 SER N 116  PHE N 120  0                                        
SHEET    2 AH1 4 ALA N 132  PHE N 141 -1  O  LEU N 137   N  THR N 118           
SHEET    3 AH1 4 TYR N 174  LEU N 182 -1  O  TYR N 174   N  PHE N 141           
SHEET    4 AH1 4 VAL N 161  THR N 163 -1  N  GLU N 162   O  TYR N 179           
SHEET    1 AH2 4 SER N 116  PHE N 120  0                                        
SHEET    2 AH2 4 ALA N 132  PHE N 141 -1  O  LEU N 137   N  THR N 118           
SHEET    3 AH2 4 TYR N 174  LEU N 182 -1  O  TYR N 174   N  PHE N 141           
SHEET    4 AH2 4 SER N 167  LYS N 168 -1  N  SER N 167   O  ALA N 175           
SHEET    1 AH3 4 SER N 155  PRO N 156  0                                        
SHEET    2 AH3 4 THR N 147  ALA N 152 -1  N  ALA N 152   O  SER N 155           
SHEET    3 AH3 4 TYR N 193  HIS N 199 -1  O  GLN N 196   N  ALA N 149           
SHEET    4 AH3 4 SER N 202  VAL N 208 -1  O  VAL N 204   N  VAL N 197           
SHEET    1 AH4 4 GLN O   3  GLN O   6  0                                        
SHEET    2 AH4 4 VAL O  18  SER O  25 -1  O  LYS O  23   N  GLN O   5           
SHEET    3 AH4 4 THR O  78  LEU O  83 -1  O  LEU O  83   N  VAL O  18           
SHEET    4 AH4 4 VAL O  68  ASP O  73 -1  N  THR O  71   O  SER O  80           
SHEET    1 AH5 6 GLU O  10  LYS O  12  0                                        
SHEET    2 AH5 6 THR O 117  VAL O 121  1  O  THR O 120   N  LYS O  12           
SHEET    3 AH5 6 ALA O  92  SER O  99 -1  N  TYR O  94   O  THR O 117           
SHEET    4 AH5 6 ALA O  33  GLN O  39 -1  N  ALA O  33   O  SER O  99           
SHEET    5 AH5 6 LEU O  45  ILE O  51 -1  O  GLY O  49   N  TRP O  36           
SHEET    6 AH5 6 LYS O  59  TYR O  60 -1  O  LYS O  59   N  GLY O  50           
SHEET    1 AH6 4 SER O 130  LEU O 134  0                                        
SHEET    2 AH6 4 ALA O 146  TYR O 155 -1  O  GLY O 149   N  LEU O 134           
SHEET    3 AH6 4 TYR O 186  VAL O 194 -1  O  LEU O 188   N  VAL O 152           
SHEET    4 AH6 4 VAL O 173  THR O 175 -1  N  HIS O 174   O  VAL O 191           
SHEET    1 AH7 4 SER O 130  LEU O 134  0                                        
SHEET    2 AH7 4 ALA O 146  TYR O 155 -1  O  GLY O 149   N  LEU O 134           
SHEET    3 AH7 4 TYR O 186  VAL O 194 -1  O  LEU O 188   N  VAL O 152           
SHEET    4 AH7 4 VAL O 179  LEU O 180 -1  N  VAL O 179   O  SER O 187           
SHEET    1 AH8 3 THR O 161  TRP O 164  0                                        
SHEET    2 AH8 3 ILE O 205  HIS O 210 -1  O  ASN O 207   N  SER O 163           
SHEET    3 AH8 3 THR O 215  LYS O 220 -1  O  THR O 215   N  HIS O 210           
SHEET    1 AH9 4 THR P   5  GLN P   6  0                                        
SHEET    2 AH9 4 VAL P  18  GLN P  23 -1  O  GLN P  23   N  THR P   5           
SHEET    3 AH9 4 THR P  69  ILE P  74 -1  O  ALA P  70   N  CYS P  22           
SHEET    4 AH9 4 PHE P  61  SER P  66 -1  N  SER P  64   O  SER P  71           
SHEET    1 AI1 5 ALA P   9  ALA P  13  0                                        
SHEET    2 AI1 5 THR P 103  LEU P 108  1  O  LEU P 108   N  VAL P  12           
SHEET    3 AI1 5 ASP P  84  SER P  89 -1  N  TYR P  85   O  THR P 103           
SHEET    4 AI1 5 SER P  33  GLN P  37 -1  N  GLN P  37   O  ASP P  84           
SHEET    5 AI1 5 VAL P  44  ILE P  47 -1  O  ILE P  47   N  TRP P  34           
SHEET    1 AI2 4 ALA P   9  ALA P  13  0                                        
SHEET    2 AI2 4 THR P 103  LEU P 108  1  O  LEU P 108   N  VAL P  12           
SHEET    3 AI2 4 ASP P  84  SER P  89 -1  N  TYR P  85   O  THR P 103           
SHEET    4 AI2 4 VAL P  98  PHE P  99 -1  O  VAL P  98   N  SER P  89           
SHEET    1 AI3 4 SER P 116  PHE P 120  0                                        
SHEET    2 AI3 4 ALA P 132  PHE P 141 -1  O  LEU P 137   N  THR P 118           
SHEET    3 AI3 4 TYR P 174  LEU P 182 -1  O  ALA P 176   N  ILE P 138           
SHEET    4 AI3 4 VAL P 161  THR P 163 -1  N  GLU P 162   O  TYR P 179           
SHEET    1 AI4 4 SER P 116  PHE P 120  0                                        
SHEET    2 AI4 4 ALA P 132  PHE P 141 -1  O  LEU P 137   N  THR P 118           
SHEET    3 AI4 4 TYR P 174  LEU P 182 -1  O  ALA P 176   N  ILE P 138           
SHEET    4 AI4 4 SER P 167  LYS P 168 -1  N  SER P 167   O  ALA P 175           
SHEET    1 AI5 4 SER P 155  PRO P 156  0                                        
SHEET    2 AI5 4 THR P 147  ALA P 152 -1  N  ALA P 152   O  SER P 155           
SHEET    3 AI5 4 TYR P 193  HIS P 199 -1  O  GLN P 196   N  ALA P 149           
SHEET    4 AI5 4 SER P 202  VAL P 208 -1  O  VAL P 204   N  VAL P 197           
SHEET    1 AI6 4 LEU Q   4  GLN Q   6  0                                        
SHEET    2 AI6 4 VAL Q  18  ALA Q  24 -1  O  LYS Q  23   N  GLN Q   5           
SHEET    3 AI6 4 THR Q  78  LEU Q  83 -1  O  MET Q  81   N  VAL Q  20           
SHEET    4 AI6 4 VAL Q  68  ASP Q  73 -1  N  THR Q  71   O  SER Q  80           
SHEET    1 AI7 6 GLU Q  10  LYS Q  12  0                                        
SHEET    2 AI7 6 THR Q 117  VAL Q 121  1  O  THR Q 120   N  GLU Q  10           
SHEET    3 AI7 6 ALA Q  92  SER Q  99 -1  N  ALA Q  92   O  VAL Q 119           
SHEET    4 AI7 6 ALA Q  33  GLN Q  39 -1  N  ALA Q  33   O  SER Q  99           
SHEET    5 AI7 6 LEU Q  45  ILE Q  51 -1  O  ILE Q  51   N  ILE Q  34           
SHEET    6 AI7 6 LYS Q  59  TYR Q  60 -1  O  LYS Q  59   N  GLY Q  50           
SHEET    1 AI8 4 SER Q 130  LEU Q 134  0                                        
SHEET    2 AI8 4 ALA Q 146  TYR Q 155 -1  O  GLY Q 149   N  LEU Q 134           
SHEET    3 AI8 4 TYR Q 186  VAL Q 194 -1  O  TYR Q 186   N  TYR Q 155           
SHEET    4 AI8 4 VAL Q 173  THR Q 175 -1  N  HIS Q 174   O  VAL Q 191           
SHEET    1 AI9 4 SER Q 130  LEU Q 134  0                                        
SHEET    2 AI9 4 ALA Q 146  TYR Q 155 -1  O  GLY Q 149   N  LEU Q 134           
SHEET    3 AI9 4 TYR Q 186  VAL Q 194 -1  O  TYR Q 186   N  TYR Q 155           
SHEET    4 AI9 4 VAL Q 179  LEU Q 180 -1  N  VAL Q 179   O  SER Q 187           
SHEET    1 AJ1 3 THR Q 161  TRP Q 164  0                                        
SHEET    2 AJ1 3 ILE Q 205  HIS Q 210 -1  O  ASN Q 207   N  SER Q 163           
SHEET    3 AJ1 3 THR Q 215  LYS Q 220 -1  O  VAL Q 217   N  VAL Q 208           
SHEET    1 AJ2 4 THR R   5  GLN R   6  0                                        
SHEET    2 AJ2 4 VAL R  18  GLN R  23 -1  O  GLN R  23   N  THR R   5           
SHEET    3 AJ2 4 THR R  69  ILE R  74 -1  O  ALA R  70   N  CYS R  22           
SHEET    4 AJ2 4 PHE R  61  SER R  66 -1  N  SER R  64   O  SER R  71           
SHEET    1 AJ3 5 ALA R   9  ALA R  13  0                                        
SHEET    2 AJ3 5 THR R 103  LEU R 108  1  O  LEU R 108   N  VAL R  12           
SHEET    3 AJ3 5 ASP R  84  SER R  89 -1  N  TYR R  85   O  THR R 103           
SHEET    4 AJ3 5 SER R  33  GLN R  37 -1  N  GLN R  37   O  ASP R  84           
SHEET    5 AJ3 5 VAL R  44  ILE R  47 -1  O  VAL R  46   N  TRP R  34           
SHEET    1 AJ4 4 ALA R   9  ALA R  13  0                                        
SHEET    2 AJ4 4 THR R 103  LEU R 108  1  O  LEU R 108   N  VAL R  12           
SHEET    3 AJ4 4 ASP R  84  SER R  89 -1  N  TYR R  85   O  THR R 103           
SHEET    4 AJ4 4 VAL R  98  PHE R  99 -1  O  VAL R  98   N  SER R  89           
SHEET    1 AJ5 4 SER R 116  PHE R 120  0                                        
SHEET    2 AJ5 4 ALA R 132  PHE R 141 -1  O  LEU R 137   N  THR R 118           
SHEET    3 AJ5 4 TYR R 174  LEU R 182 -1  O  LEU R 182   N  ALA R 132           
SHEET    4 AJ5 4 VAL R 161  THR R 163 -1  N  GLU R 162   O  TYR R 179           
SHEET    1 AJ6 4 SER R 116  PHE R 120  0                                        
SHEET    2 AJ6 4 ALA R 132  PHE R 141 -1  O  LEU R 137   N  THR R 118           
SHEET    3 AJ6 4 TYR R 174  LEU R 182 -1  O  LEU R 182   N  ALA R 132           
SHEET    4 AJ6 4 SER R 167  LYS R 168 -1  N  SER R 167   O  ALA R 175           
SHEET    1 AJ7 4 SER R 155  PRO R 156  0                                        
SHEET    2 AJ7 4 THR R 147  ALA R 152 -1  N  ALA R 152   O  SER R 155           
SHEET    3 AJ7 4 TYR R 193  HIS R 199 -1  O  GLN R 196   N  ALA R 149           
SHEET    4 AJ7 4 SER R 202  VAL R 208 -1  O  SER R 202   N  HIS R 199           
SSBOND   1 CYS A  232    CYS A  245                          1555   1555  2.07  
SSBOND   2 CYS B  232    CYS B  245                          1555   1555  2.06  
SSBOND   3 CYS C  232    CYS C  245                          1555   1555  2.07  
SSBOND   4 CYS D   22    CYS D   96                          1555   1555  2.04  
SSBOND   5 CYS D  150    CYS D  206                          1555   1555  2.03  
SSBOND   6 CYS E   22    CYS E   87                          1555   1555  2.04  
SSBOND   7 CYS E  136    CYS E  195                          1555   1555  2.05  
SSBOND   8 CYS F   22    CYS F   96                          1555   1555  2.03  
SSBOND   9 CYS F  150    CYS F  206                          1555   1555  2.03  
SSBOND  10 CYS G   22    CYS G   87                          1555   1555  2.03  
SSBOND  11 CYS G  136    CYS G  195                          1555   1555  2.05  
SSBOND  12 CYS H   22    CYS H   96                          1555   1555  2.03  
SSBOND  13 CYS H  150    CYS H  206                          1555   1555  2.04  
SSBOND  14 CYS I   22    CYS I   87                          1555   1555  2.05  
SSBOND  15 CYS I  136    CYS I  195                          1555   1555  2.05  
SSBOND  16 CYS J  232    CYS J  245                          1555   1555  2.06  
SSBOND  17 CYS K  232    CYS K  245                          1555   1555  2.06  
SSBOND  18 CYS L  232    CYS L  245                          1555   1555  2.06  
SSBOND  19 CYS M   22    CYS M   96                          1555   1555  2.03  
SSBOND  20 CYS M  150    CYS M  206                          1555   1555  2.02  
SSBOND  21 CYS N   22    CYS N   87                          1555   1555  2.04  
SSBOND  22 CYS N  136    CYS N  195                          1555   1555  2.05  
SSBOND  23 CYS O   22    CYS O   96                          1555   1555  2.04  
SSBOND  24 CYS O  150    CYS O  206                          1555   1555  2.05  
SSBOND  25 CYS P   22    CYS P   87                          1555   1555  2.04  
SSBOND  26 CYS P  136    CYS P  195                          1555   1555  2.04  
SSBOND  27 CYS Q   22    CYS Q   96                          1555   1555  2.05  
SSBOND  28 CYS Q  150    CYS Q  206                          1555   1555  2.02  
SSBOND  29 CYS R   22    CYS R   87                          1555   1555  2.04  
SSBOND  30 CYS R  136    CYS R  195                          1555   1555  2.04  
CISPEP   1 SER D  111    PRO D  112          0        -3.39                     
CISPEP   2 PHE D  156    PRO D  157          0        -5.57                     
CISPEP   3 GLU D  158    PRO D  159          0        -5.21                     
CISPEP   4 TYR E  142    PRO E  143          0        -1.39                     
CISPEP   5 SER F  111    PRO F  112          0         1.08                     
CISPEP   6 PHE F  156    PRO F  157          0        -5.50                     
CISPEP   7 GLU F  158    PRO F  159          0         1.72                     
CISPEP   8 TYR G  142    PRO G  143          0        -1.64                     
CISPEP   9 SER H  111    PRO H  112          0        -3.55                     
CISPEP  10 PHE H  156    PRO H  157          0       -17.59                     
CISPEP  11 GLU H  158    PRO H  159          0        -1.13                     
CISPEP  12 TYR I  142    PRO I  143          0        -2.60                     
CISPEP  13 SER M  111    PRO M  112          0        -1.16                     
CISPEP  14 PHE M  156    PRO M  157          0        -4.67                     
CISPEP  15 GLU M  158    PRO M  159          0        -2.71                     
CISPEP  16 TYR N  142    PRO N  143          0        -0.95                     
CISPEP  17 SER O  111    PRO O  112          0        -5.33                     
CISPEP  18 PHE O  156    PRO O  157          0        -0.51                     
CISPEP  19 GLU O  158    PRO O  159          0        -5.95                     
CISPEP  20 TYR P  142    PRO P  143          0        -2.00                     
CISPEP  21 SER Q  111    PRO Q  112          0        -6.16                     
CISPEP  22 PHE Q  156    PRO Q  157          0        -1.93                     
CISPEP  23 GLU Q  158    PRO Q  159          0         4.43                     
CISPEP  24 TYR R  142    PRO R  143          0        -4.01                     
CRYST1  135.687  135.499  138.180  90.00  91.88  90.00 P 1 21 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007370  0.000000  0.000242        0.00000                         
SCALE2      0.000000  0.007380  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007241        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system