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Database: PDB
Entry: 3OET
LinkDB: 3OET
Original site: 3OET 
HEADER    OXIDOREDUCTASE                          13-AUG-10   3OET              
TITLE     D-ERYTHRONATE-4-PHOSPHATE DEHYDROGENASE COMPLEXED WITH NAD            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ERYTHRONATE-4-PHOSPHATE DEHYDROGENASE;                     
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 EC: 1.1.1.290;                                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR     
SOURCE   3 TYPHIMURIUM;                                                         
SOURCE   4 ORGANISM_TAXID: 99287;                                               
SOURCE   5 STRAIN: LT2;                                                         
SOURCE   6 GENE: PDXB, STM2370;                                                 
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIPL;                  
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: P15TV LIC                                 
KEYWDS    STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS     
KEYWDS   2 DISEASES, CSGID, ERYTHRONATE-4-PHOSPHATE DEHYDROGENASE, NAD,         
KEYWDS   3 SALMONELLA TYPHIMURIUM LT2, OXIDOREDUCTASE                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.V.FILIPPOVA,Z.WAWRZAK,O.ONOPRIYENKO,A.SAVCHENKO,A.EDWARDS,          
AUTHOR   2 W.F.ANDERSON,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES   
AUTHOR   3 (CSGID)                                                              
REVDAT   2   08-NOV-17 3OET    1       REMARK                                   
REVDAT   1   25-AUG-10 3OET    0                                                
JRNL        AUTH   E.V.FILIPPOVA,Z.WAWRZAK,O.ONOPRIYENKO,A.SAVCHENKO,A.EDWARDS, 
JRNL        AUTH 2 W.F.ANDERSON                                                 
JRNL        TITL   D-ERYTHRONATE-4-PHOSPHATE DEHYDROGENASE COMPLEXED WITH NAD   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.36 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.36                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 122293                         
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) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6470                            
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) : 2.36                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.42                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8177                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.56                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 438                          
REMARK   3   BIN FREE R VALUE                    : 0.3130                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 22878                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 352                                     
REMARK   3   SOLVENT ATOMS            : 556                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.05000                                             
REMARK   3    B22 (A**2) : 0.13000                                              
REMARK   3    B33 (A**2) : 1.09000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.24000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.270         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.197         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.941        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 23744 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 32325 ; 1.460 ; 1.998       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2975 ; 5.802 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1020 ;35.606 ;23.245       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3843 ;16.496 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   214 ;21.222 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3749 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 17839 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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): 14860 ; 0.602 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23836 ; 1.183 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  8884 ; 2.401 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  8489 ; 3.747 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 16                                         
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    88                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.9452  25.1013   2.0831              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2685 T22:   0.3298                                     
REMARK   3      T33:   0.4166 T12:   0.1069                                     
REMARK   3      T13:  -0.0876 T23:  -0.1555                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.0341 L22:   8.3745                                     
REMARK   3      L33:   6.2361 L12:  -2.0828                                     
REMARK   3      L13:  -2.6028 L23:   5.3260                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0992 S12:  -0.0980 S13:  -1.2744                       
REMARK   3      S21:   1.0708 S22:   0.3256 S23:  -0.1273                       
REMARK   3      S31:   0.7813 S32:   0.5876 S33:  -0.2264                       
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 :   A    89        A   376                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.4367  44.1605  13.1925              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1308 T22:   0.0647                                     
REMARK   3      T33:   0.0113 T12:   0.0315                                     
REMARK   3      T13:  -0.0074 T23:  -0.0262                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0796 L22:   0.7437                                     
REMARK   3      L33:   1.5233 L12:   0.1825                                     
REMARK   3      L13:   0.5018 L23:   0.2295                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0044 S12:   0.0457 S13:  -0.0452                       
REMARK   3      S21:   0.0943 S22:   0.0208 S23:  -0.0002                       
REMARK   3      S31:  -0.0132 S32:   0.0095 S33:  -0.0164                       
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 :   B    -2        B    88                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.6898  22.7120 -25.4264              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1817 T22:   0.3052                                     
REMARK   3      T33:   0.6670 T12:  -0.1105                                     
REMARK   3      T13:  -0.1377 T23:   0.2282                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8297 L22:   3.7062                                     
REMARK   3      L33:   3.2481 L12:   1.4357                                     
REMARK   3      L13:  -0.7335 L23:  -0.8211                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0204 S12:   0.4718 S13:  -0.5599                       
REMARK   3      S21:  -0.5370 S22:   0.5677 S23:   0.9033                       
REMARK   3      S31:   0.4797 S32:  -0.4243 S33:  -0.5881                       
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 :   B    89        B   376                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.8728  42.6559 -35.2971              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0378 T22:   0.0497                                     
REMARK   3      T33:   0.0424 T12:  -0.0246                                     
REMARK   3      T13:  -0.0053 T23:   0.0271                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8551 L22:   1.3919                                     
REMARK   3      L33:   0.8740 L12:  -0.2402                                     
REMARK   3      L13:   0.0715 L23:  -0.4174                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0054 S12:  -0.0407 S13:  -0.0072                       
REMARK   3      S21:  -0.0154 S22:   0.0847 S23:   0.2117                       
REMARK   3      S31:   0.0471 S32:  -0.1466 S33:  -0.0793                       
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 :   C    -2        C    88                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.3588  95.5515  24.9304              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2444 T22:   0.4855                                     
REMARK   3      T33:   0.5349 T12:   0.1744                                     
REMARK   3      T13:   0.0391 T23:   0.2411                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9281 L22:   3.8251                                     
REMARK   3      L33:   3.1661 L12:   1.3738                                     
REMARK   3      L13:  -0.7685 L23:  -1.2649                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0396 S12:  -0.5242 S13:   0.3621                       
REMARK   3      S21:   0.2784 S22:   0.3451 S23:   0.5709                       
REMARK   3      S31:  -0.2136 S32:  -0.2942 S33:  -0.3055                       
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 :   C    89        C   376                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.7167  76.3897  35.9848              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0727 T22:   0.0334                                     
REMARK   3      T33:   0.0550 T12:   0.0369                                     
REMARK   3      T13:   0.0050 T23:   0.0208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3544 L22:   1.0486                                     
REMARK   3      L33:   1.1774 L12:   0.4542                                     
REMARK   3      L13:  -0.2580 L23:  -0.3616                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0589 S12:   0.1030 S13:   0.0894                       
REMARK   3      S21:  -0.0063 S22:   0.0355 S23:   0.1456                       
REMARK   3      S31:  -0.0549 S32:  -0.1354 S33:  -0.0944                       
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 :   D    -2        D    88                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.8499  93.5909  -1.4722              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1570 T22:   0.3163                                     
REMARK   3      T33:   0.7633 T12:  -0.0588                                     
REMARK   3      T13:   0.1190 T23:  -0.2279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5787 L22:   7.7205                                     
REMARK   3      L33:   5.8726 L12:  -0.4114                                     
REMARK   3      L13:   1.3050 L23:   4.6615                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0047 S12:   0.2429 S13:   1.4280                       
REMARK   3      S21:  -0.9091 S22:   0.2920 S23:  -0.5476                       
REMARK   3      S31:  -0.7560 S32:   0.5081 S33:  -0.2966                       
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 :   D    89        D   377                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.1934  74.8109 -12.5146              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0719 T22:   0.0160                                     
REMARK   3      T33:   0.0343 T12:  -0.0116                                     
REMARK   3      T13:   0.0170 T23:  -0.0187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0062 L22:   0.8729                                     
REMARK   3      L33:   0.9930 L12:  -0.5053                                     
REMARK   3      L13:  -0.4162 L23:   0.5170                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0592 S12:  -0.0735 S13:   0.2292                       
REMARK   3      S21:   0.0364 S22:   0.0401 S23:  -0.0741                       
REMARK   3      S31:  -0.0247 S32:   0.0820 S33:  -0.0993                       
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 :   E     1        E    88                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.4537  55.5947 -37.2762              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1255 T22:   0.1709                                     
REMARK   3      T33:   0.1682 T12:   0.0208                                     
REMARK   3      T13:   0.0219 T23:   0.0169                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4987 L22:   2.5321                                     
REMARK   3      L33:   3.9597 L12:  -1.0779                                     
REMARK   3      L13:  -2.0918 L23:   1.2512                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2201 S12:   0.1856 S13:   0.4407                       
REMARK   3      S21:  -0.1029 S22:  -0.1255 S23:  -0.2717                       
REMARK   3      S31:  -0.2750 S32:   0.1041 S33:  -0.0946                       
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 :   E    89        E   375                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.6868  35.5686 -41.3159              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0967 T22:   0.0398                                     
REMARK   3      T33:   0.0249 T12:   0.0003                                     
REMARK   3      T13:   0.0350 T23:  -0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4716 L22:   1.0263                                     
REMARK   3      L33:   1.0799 L12:   0.0923                                     
REMARK   3      L13:  -0.1096 L23:  -0.0430                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0521 S12:   0.0261 S13:  -0.0745                       
REMARK   3      S21:  -0.1246 S22:   0.0311 S23:  -0.1236                       
REMARK   3      S31:   0.0959 S32:   0.1838 S33:   0.0210                       
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 :   F     1        F    88                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.8830  66.3296  32.6281              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2436 T22:   0.3810                                     
REMARK   3      T33:   0.6304 T12:   0.1022                                     
REMARK   3      T13:  -0.0035 T23:  -0.0229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2606 L22:   2.9486                                     
REMARK   3      L33:   7.2538 L12:   0.6180                                     
REMARK   3      L13:   2.3380 L23:   0.8662                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1022 S12:  -0.0521 S13:  -0.5285                       
REMARK   3      S21:  -0.2654 S22:  -0.1688 S23:   0.0403                       
REMARK   3      S31:   0.7777 S32:   0.5162 S33:   0.0666                       
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 :   F    89        F   376                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.6560  83.3020  41.7907              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0753 T22:   0.0276                                     
REMARK   3      T33:   0.0210 T12:   0.0110                                     
REMARK   3      T13:  -0.0058 T23:   0.0114                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5034 L22:   1.3171                                     
REMARK   3      L33:   1.0449 L12:  -0.1688                                     
REMARK   3      L13:   0.1459 L23:  -0.1253                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0535 S12:  -0.0407 S13:  -0.0012                       
REMARK   3      S21:   0.1206 S22:   0.0085 S23:  -0.1339                       
REMARK   3      S31:  -0.0939 S32:   0.1213 S33:   0.0450                       
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 :   G     1        G    88                          
REMARK   3    ORIGIN FOR THE GROUP (A): -43.5761  70.5175 -10.8984              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4594 T22:   0.4578                                     
REMARK   3      T33:   0.6584 T12:  -0.1292                                     
REMARK   3      T13:  -0.0753 T23:  -0.0227                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3307 L22:   3.9849                                     
REMARK   3      L33:   1.0964 L12:   0.6677                                     
REMARK   3      L13:   1.1812 L23:   1.8410                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1932 S12:  -0.3259 S13:  -0.9001                       
REMARK   3      S21:  -0.1069 S22:  -0.1552 S23:   0.4513                       
REMARK   3      S31:   0.1685 S32:  -0.2627 S33:  -0.0380                       
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 :   G    89        G   375                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.6934  85.6189 -18.7510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0788 T22:   0.2140                                     
REMARK   3      T33:   0.1562 T12:   0.0458                                     
REMARK   3      T13:   0.0229 T23:  -0.0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3432 L22:   1.2820                                     
REMARK   3      L33:   1.5579 L12:  -0.3049                                     
REMARK   3      L13:   0.3901 L23:   0.1443                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0702 S12:   0.2577 S13:   0.1485                       
REMARK   3      S21:  -0.1016 S22:  -0.0874 S23:   0.0296                       
REMARK   3      S31:  -0.0868 S32:  -0.1298 S33:   0.0172                       
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 :   H    -1        H    88                          
REMARK   3    ORIGIN FOR THE GROUP (A): -45.5122  48.7402  10.9064              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1658 T22:   0.4161                                     
REMARK   3      T33:   0.1660 T12:   0.0587                                     
REMARK   3      T13:  -0.0019 T23:  -0.0277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7058 L22:   2.5542                                     
REMARK   3      L33:   1.3905 L12:  -0.7399                                     
REMARK   3      L13:  -0.4404 L23:  -0.0905                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1371 S12:   0.6785 S13:   0.3327                       
REMARK   3      S21:  -0.1174 S22:  -0.1791 S23:  -0.0731                       
REMARK   3      S31:  -0.0934 S32:   0.1519 S33:   0.0420                       
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 :   H    89        H   376                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.6755  33.5983  18.6402              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1577 T22:   0.1394                                     
REMARK   3      T33:   0.1251 T12:   0.0094                                     
REMARK   3      T13:   0.0533 T23:  -0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1033 L22:   1.4075                                     
REMARK   3      L33:   1.5310 L12:  -0.1324                                     
REMARK   3      L13:  -0.9842 L23:   0.1849                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0997 S12:  -0.0540 S13:  -0.4675                       
REMARK   3      S21:   0.2599 S22:  -0.0010 S23:   0.1744                       
REMARK   3      S31:   0.0269 S32:  -0.1270 S33:   0.1007                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
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 3OET COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000061025.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97950                            
REMARK 200  MONOCHROMATOR                  : SI-111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 128763                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.360                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 103.700                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.36                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MRBUMP, CCP4, PHENIX                                  
REMARK 200 STARTING MODEL: PDBID 2O4C                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350,0.2M NH4 ACETATE, 0.1M      
REMARK 280  BIS-TRIS, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K   
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       83.88250            
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, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12                   
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H                                  
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, G                                  
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: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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: 7                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 8                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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: 9                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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: 10                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 11                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G                                     
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: 12                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H                                     
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     SER A    -2                                                      
REMARK 465     ARG A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     ILE A    30                                                      
REMARK 465     ALA A   377                                                      
REMARK 465     HIS A   378                                                      
REMARK 465     ARG B    28                                                      
REMARK 465     PRO B    31                                                      
REMARK 465     ALA B   377                                                      
REMARK 465     HIS B   378                                                      
REMARK 465     PRO C    29                                                      
REMARK 465     ILE C    30                                                      
REMARK 465     PRO C    31                                                      
REMARK 465     HIS C    37                                                      
REMARK 465     ALA C    38                                                      
REMARK 465     LEU C    53                                                      
REMARK 465     ARG C   280                                                      
REMARK 465     ALA C   377                                                      
REMARK 465     HIS C   378                                                      
REMARK 465     GLY D    27                                                      
REMARK 465     ARG D    28                                                      
REMARK 465     PRO D    29                                                      
REMARK 465     ILE D    30                                                      
REMARK 465     SER D    55                                                      
REMARK 465     HIS D   378                                                      
REMARK 465     SER E    -2                                                      
REMARK 465     ASN E    -1                                                      
REMARK 465     ALA E     0                                                      
REMARK 465     PRO E   376                                                      
REMARK 465     ALA E   377                                                      
REMARK 465     HIS E   378                                                      
REMARK 465     SER F    -2                                                      
REMARK 465     ASN F    -1                                                      
REMARK 465     ALA F     0                                                      
REMARK 465     ARG F    28                                                      
REMARK 465     PRO F    29                                                      
REMARK 465     ILE F    30                                                      
REMARK 465     PRO F    31                                                      
REMARK 465     GLU F    51                                                      
REMARK 465     GLY F    56                                                      
REMARK 465     GLU F   281                                                      
REMARK 465     GLN F   282                                                      
REMARK 465     ARG F   283                                                      
REMARK 465     VAL F   284                                                      
REMARK 465     ALA F   285                                                      
REMARK 465     ALA F   377                                                      
REMARK 465     HIS F   378                                                      
REMARK 465     SER G    -2                                                      
REMARK 465     ASN G    -1                                                      
REMARK 465     ALA G     0                                                      
REMARK 465     ALA G    24                                                      
REMARK 465     VAL G    25                                                      
REMARK 465     PRO G    26                                                      
REMARK 465     GLY G    27                                                      
REMARK 465     ARG G    28                                                      
REMARK 465     PRO G   376                                                      
REMARK 465     ALA G   377                                                      
REMARK 465     HIS G   378                                                      
REMARK 465     SER H    -2                                                      
REMARK 465     ALA H   377                                                      
REMARK 465     HIS H   378                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  34    CD   OE1  OE2                                       
REMARK 470     LYS B  23    CD   CE   NZ                                        
REMARK 470     LYS B  48    CD   CE   NZ                                        
REMARK 470     ARG B 283    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS C   2    CE   NZ                                             
REMARK 470     ARG C  28    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU C  33    CG   CD   OE1  OE2                                  
REMARK 470     VAL C  62    CG1  CG2                                            
REMARK 470     GLU C 345    CD   OE1  OE2                                       
REMARK 470     LYS D   2    CD   CE   NZ                                        
REMARK 470     GLU D  14    CD   OE1  OE2                                       
REMARK 470     ARG D  44    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU D 345    CD   OE1  OE2                                       
REMARK 470     ARG E 280    NH1  NH2                                            
REMARK 470     ARG E 283    NE   CZ   NH1  NH2                                  
REMARK 470     GLU F  14    CD   OE1  OE2                                       
REMARK 470     ASN F  50    CG   OD1  ND2                                       
REMARK 470     LYS F 179    CD   CE   NZ                                        
REMARK 470     ARG F 208    NE   CZ   NH1  NH2                                  
REMARK 470     LYS F 341    CE   NZ                                             
REMARK 470     LEU G   4    CG   CD1  CD2                                       
REMARK 470     GLN G  79    CD   OE1  NE2                                       
REMARK 470     HIS G 375    ND1  CE1  NE2                                       
REMARK 470     GLU H  14    CD   OE1  OE2                                       
REMARK 470     GLU H  33    CD   OE1  OE2                                       
REMARK 470     GLU H 246    CD   OE1  OE2                                       
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    ALA A  87       63.51   -119.00                                   
REMARK 500    VAL A 124       62.60   -112.81                                   
REMARK 500    ASP A 146       80.28   -158.87                                   
REMARK 500    HIS A 174       42.96   -145.40                                   
REMARK 500    LYS A 184      122.81    -36.25                                   
REMARK 500    CYS A 207      -80.18   -107.47                                   
REMARK 500    PRO A 226       94.68    -65.30                                   
REMARK 500    GLU A 281      124.47    -37.54                                   
REMARK 500    ASN B  50     -160.14   -129.98                                   
REMARK 500    SER B  55      122.72    -36.61                                   
REMARK 500    ILE B  59      119.23    -38.13                                   
REMARK 500    ASP B 146       83.31   -162.27                                   
REMARK 500    CYS B 207      -79.93   -102.44                                   
REMARK 500    ASP B 213       99.90    -66.50                                   
REMARK 500    SER B 253       57.06    -95.33                                   
REMARK 500    ARG B 280       43.22   -100.99                                   
REMARK 500    GLU B 281      130.06    -37.72                                   
REMARK 500    VAL C  43     -146.96   -122.98                                   
REMARK 500    GLU C  51      -71.01    -45.89                                   
REMARK 500    THR C  69       34.20    -88.14                                   
REMARK 500    ASP C  70      -72.03    -26.56                                   
REMARK 500    ALA C  86     -156.46   -104.86                                   
REMARK 500    VAL C 124       64.34   -117.42                                   
REMARK 500    ASP C 146       80.80   -162.98                                   
REMARK 500    HIS C 174       54.23   -144.49                                   
REMARK 500    CYS C 207      -89.56   -100.96                                   
REMARK 500    SER C 253       55.91    -96.50                                   
REMARK 500    PHE C 277      -36.71    -37.59                                   
REMARK 500    TYR C 317      119.77   -166.36                                   
REMARK 500    VAL D  25      148.63   -171.54                                   
REMARK 500    ASN D  50     -155.26   -158.35                                   
REMARK 500    ALA D  65       43.78    -82.27                                   
REMARK 500    ALA D  86     -166.26   -103.37                                   
REMARK 500    VAL D 124       59.63   -112.61                                   
REMARK 500    ASP D 146       77.81   -160.76                                   
REMARK 500    HIS D 174       52.58   -143.47                                   
REMARK 500    ASP D 180     -166.16   -167.44                                   
REMARK 500    CYS D 207      -86.08   -100.64                                   
REMARK 500    ASP D 213       97.82    -68.84                                   
REMARK 500    GLU D 281      107.67    -54.93                                   
REMARK 500    GLU D 345      128.16    -37.54                                   
REMARK 500    ARG E  28      111.66   -176.85                                   
REMARK 500    ASP E 146       76.63   -165.26                                   
REMARK 500    HIS E 174       50.77   -146.14                                   
REMARK 500    ASP E 180     -167.46   -164.83                                   
REMARK 500    CYS E 207      -82.51   -111.17                                   
REMARK 500    PRO E 226       91.55    -68.06                                   
REMARK 500    GLU E 237      131.18    -37.28                                   
REMARK 500    GLU E 281      108.98    -35.56                                   
REMARK 500    TYR E 317      109.94   -160.17                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      91 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 379                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 379                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 379                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 379                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD E 379                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD F 379                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD G 379                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD H 379                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: IDP90820   RELATED DB: TARGETDB                          
DBREF  3OET A    1   378  UNP    P60802   PDXB_SALTY       1    378             
DBREF  3OET B    1   378  UNP    P60802   PDXB_SALTY       1    378             
DBREF  3OET C    1   378  UNP    P60802   PDXB_SALTY       1    378             
DBREF  3OET D    1   378  UNP    P60802   PDXB_SALTY       1    378             
DBREF  3OET E    1   378  UNP    P60802   PDXB_SALTY       1    378             
DBREF  3OET F    1   378  UNP    P60802   PDXB_SALTY       1    378             
DBREF  3OET G    1   378  UNP    P60802   PDXB_SALTY       1    378             
DBREF  3OET H    1   378  UNP    P60802   PDXB_SALTY       1    378             
SEQADV 3OET SER A   -2  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET ASN A   -1  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET ALA A    0  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET SER B   -2  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET ASN B   -1  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET ALA B    0  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET SER C   -2  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET ASN C   -1  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET ALA C    0  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET SER D   -2  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET ASN D   -1  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET ALA D    0  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET SER E   -2  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET ASN E   -1  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET ALA E    0  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET SER F   -2  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET ASN F   -1  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET ALA F    0  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET SER G   -2  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET ASN G   -1  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET ALA G    0  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET SER H   -2  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET ASN H   -1  UNP  P60802              EXPRESSION TAG                 
SEQADV 3OET ALA H    0  UNP  P60802              EXPRESSION TAG                 
SEQRES   1 A  381  SER ASN ALA MSE LYS ILE LEU VAL ASP GLU ASN MSE PRO          
SEQRES   2 A  381  TYR ALA ARG GLU LEU PHE SER ARG LEU GLY GLU VAL LYS          
SEQRES   3 A  381  ALA VAL PRO GLY ARG PRO ILE PRO VAL GLU GLU LEU ASN          
SEQRES   4 A  381  HIS ALA ASP ALA LEU MSE VAL ARG SER VAL THR LYS VAL          
SEQRES   5 A  381  ASN GLU SER LEU LEU SER GLY THR PRO ILE ASN PHE VAL          
SEQRES   6 A  381  GLY THR ALA THR ALA GLY THR ASP HIS VAL ASP GLU ALA          
SEQRES   7 A  381  TRP LEU LYS GLN ALA GLY ILE GLY PHE SER ALA ALA PRO          
SEQRES   8 A  381  GLY CYS ASN ALA ILE ALA VAL VAL GLU TYR VAL PHE SER          
SEQRES   9 A  381  ALA LEU LEU MSE LEU ALA GLU ARG ASP GLY PHE SER LEU          
SEQRES  10 A  381  ARG ASP ARG THR ILE GLY ILE VAL GLY VAL GLY ASN VAL          
SEQRES  11 A  381  GLY SER ARG LEU GLN THR ARG LEU GLU ALA LEU GLY ILE          
SEQRES  12 A  381  ARG THR LEU LEU CYS ASP PRO PRO ARG ALA ALA ARG GLY          
SEQRES  13 A  381  ASP GLU GLY ASP PHE ARG THR LEU ASP GLU LEU VAL GLN          
SEQRES  14 A  381  GLU ALA ASP VAL LEU THR PHE HIS THR PRO LEU TYR LYS          
SEQRES  15 A  381  ASP GLY PRO TYR LYS THR LEU HIS LEU ALA ASP GLU THR          
SEQRES  16 A  381  LEU ILE ARG ARG LEU LYS PRO GLY ALA ILE LEU ILE ASN          
SEQRES  17 A  381  ALA CYS ARG GLY PRO VAL VAL ASP ASN ALA ALA LEU LEU          
SEQRES  18 A  381  ALA ARG LEU ASN ALA GLY GLN PRO LEU SER VAL VAL LEU          
SEQRES  19 A  381  ASP VAL TRP GLU GLY GLU PRO ASP LEU ASN VAL ALA LEU          
SEQRES  20 A  381  LEU GLU ALA VAL ASP ILE GLY THR SER HIS ILE ALA GLY          
SEQRES  21 A  381  TYR THR LEU GLU GLY LYS ALA ARG GLY THR THR GLN VAL          
SEQRES  22 A  381  PHE GLU ALA TYR SER ALA PHE ILE GLY ARG GLU GLN ARG          
SEQRES  23 A  381  VAL ALA LEU GLU THR LEU LEU PRO ALA PRO GLU PHE GLY          
SEQRES  24 A  381  ARG ILE THR LEU HIS GLY PRO LEU ASP GLN PRO THR LEU          
SEQRES  25 A  381  LYS ARG LEU ALA HIS LEU VAL TYR ASP VAL ARG ARG ASP          
SEQRES  26 A  381  ASP ALA PRO LEU ARG LYS VAL ALA GLY ILE PRO GLY GLU          
SEQRES  27 A  381  PHE ASP LYS LEU ARG LYS ASN TYR LEU GLU ARG ARG GLU          
SEQRES  28 A  381  TRP SER SER LEU TYR VAL MSE CYS ASP ASP GLU THR ALA          
SEQRES  29 A  381  ALA ALA LEU LEU CYS LYS LEU GLY PHE ASN ALA VAL HIS          
SEQRES  30 A  381  HIS PRO ALA HIS                                              
SEQRES   1 B  381  SER ASN ALA MSE LYS ILE LEU VAL ASP GLU ASN MSE PRO          
SEQRES   2 B  381  TYR ALA ARG GLU LEU PHE SER ARG LEU GLY GLU VAL LYS          
SEQRES   3 B  381  ALA VAL PRO GLY ARG PRO ILE PRO VAL GLU GLU LEU ASN          
SEQRES   4 B  381  HIS ALA ASP ALA LEU MSE VAL ARG SER VAL THR LYS VAL          
SEQRES   5 B  381  ASN GLU SER LEU LEU SER GLY THR PRO ILE ASN PHE VAL          
SEQRES   6 B  381  GLY THR ALA THR ALA GLY THR ASP HIS VAL ASP GLU ALA          
SEQRES   7 B  381  TRP LEU LYS GLN ALA GLY ILE GLY PHE SER ALA ALA PRO          
SEQRES   8 B  381  GLY CYS ASN ALA ILE ALA VAL VAL GLU TYR VAL PHE SER          
SEQRES   9 B  381  ALA LEU LEU MSE LEU ALA GLU ARG ASP GLY PHE SER LEU          
SEQRES  10 B  381  ARG ASP ARG THR ILE GLY ILE VAL GLY VAL GLY ASN VAL          
SEQRES  11 B  381  GLY SER ARG LEU GLN THR ARG LEU GLU ALA LEU GLY ILE          
SEQRES  12 B  381  ARG THR LEU LEU CYS ASP PRO PRO ARG ALA ALA ARG GLY          
SEQRES  13 B  381  ASP GLU GLY ASP PHE ARG THR LEU ASP GLU LEU VAL GLN          
SEQRES  14 B  381  GLU ALA ASP VAL LEU THR PHE HIS THR PRO LEU TYR LYS          
SEQRES  15 B  381  ASP GLY PRO TYR LYS THR LEU HIS LEU ALA ASP GLU THR          
SEQRES  16 B  381  LEU ILE ARG ARG LEU LYS PRO GLY ALA ILE LEU ILE ASN          
SEQRES  17 B  381  ALA CYS ARG GLY PRO VAL VAL ASP ASN ALA ALA LEU LEU          
SEQRES  18 B  381  ALA ARG LEU ASN ALA GLY GLN PRO LEU SER VAL VAL LEU          
SEQRES  19 B  381  ASP VAL TRP GLU GLY GLU PRO ASP LEU ASN VAL ALA LEU          
SEQRES  20 B  381  LEU GLU ALA VAL ASP ILE GLY THR SER HIS ILE ALA GLY          
SEQRES  21 B  381  TYR THR LEU GLU GLY LYS ALA ARG GLY THR THR GLN VAL          
SEQRES  22 B  381  PHE GLU ALA TYR SER ALA PHE ILE GLY ARG GLU GLN ARG          
SEQRES  23 B  381  VAL ALA LEU GLU THR LEU LEU PRO ALA PRO GLU PHE GLY          
SEQRES  24 B  381  ARG ILE THR LEU HIS GLY PRO LEU ASP GLN PRO THR LEU          
SEQRES  25 B  381  LYS ARG LEU ALA HIS LEU VAL TYR ASP VAL ARG ARG ASP          
SEQRES  26 B  381  ASP ALA PRO LEU ARG LYS VAL ALA GLY ILE PRO GLY GLU          
SEQRES  27 B  381  PHE ASP LYS LEU ARG LYS ASN TYR LEU GLU ARG ARG GLU          
SEQRES  28 B  381  TRP SER SER LEU TYR VAL MSE CYS ASP ASP GLU THR ALA          
SEQRES  29 B  381  ALA ALA LEU LEU CYS LYS LEU GLY PHE ASN ALA VAL HIS          
SEQRES  30 B  381  HIS PRO ALA HIS                                              
SEQRES   1 C  381  SER ASN ALA MSE LYS ILE LEU VAL ASP GLU ASN MSE PRO          
SEQRES   2 C  381  TYR ALA ARG GLU LEU PHE SER ARG LEU GLY GLU VAL LYS          
SEQRES   3 C  381  ALA VAL PRO GLY ARG PRO ILE PRO VAL GLU GLU LEU ASN          
SEQRES   4 C  381  HIS ALA ASP ALA LEU MSE VAL ARG SER VAL THR LYS VAL          
SEQRES   5 C  381  ASN GLU SER LEU LEU SER GLY THR PRO ILE ASN PHE VAL          
SEQRES   6 C  381  GLY THR ALA THR ALA GLY THR ASP HIS VAL ASP GLU ALA          
SEQRES   7 C  381  TRP LEU LYS GLN ALA GLY ILE GLY PHE SER ALA ALA PRO          
SEQRES   8 C  381  GLY CYS ASN ALA ILE ALA VAL VAL GLU TYR VAL PHE SER          
SEQRES   9 C  381  ALA LEU LEU MSE LEU ALA GLU ARG ASP GLY PHE SER LEU          
SEQRES  10 C  381  ARG ASP ARG THR ILE GLY ILE VAL GLY VAL GLY ASN VAL          
SEQRES  11 C  381  GLY SER ARG LEU GLN THR ARG LEU GLU ALA LEU GLY ILE          
SEQRES  12 C  381  ARG THR LEU LEU CYS ASP PRO PRO ARG ALA ALA ARG GLY          
SEQRES  13 C  381  ASP GLU GLY ASP PHE ARG THR LEU ASP GLU LEU VAL GLN          
SEQRES  14 C  381  GLU ALA ASP VAL LEU THR PHE HIS THR PRO LEU TYR LYS          
SEQRES  15 C  381  ASP GLY PRO TYR LYS THR LEU HIS LEU ALA ASP GLU THR          
SEQRES  16 C  381  LEU ILE ARG ARG LEU LYS PRO GLY ALA ILE LEU ILE ASN          
SEQRES  17 C  381  ALA CYS ARG GLY PRO VAL VAL ASP ASN ALA ALA LEU LEU          
SEQRES  18 C  381  ALA ARG LEU ASN ALA GLY GLN PRO LEU SER VAL VAL LEU          
SEQRES  19 C  381  ASP VAL TRP GLU GLY GLU PRO ASP LEU ASN VAL ALA LEU          
SEQRES  20 C  381  LEU GLU ALA VAL ASP ILE GLY THR SER HIS ILE ALA GLY          
SEQRES  21 C  381  TYR THR LEU GLU GLY LYS ALA ARG GLY THR THR GLN VAL          
SEQRES  22 C  381  PHE GLU ALA TYR SER ALA PHE ILE GLY ARG GLU GLN ARG          
SEQRES  23 C  381  VAL ALA LEU GLU THR LEU LEU PRO ALA PRO GLU PHE GLY          
SEQRES  24 C  381  ARG ILE THR LEU HIS GLY PRO LEU ASP GLN PRO THR LEU          
SEQRES  25 C  381  LYS ARG LEU ALA HIS LEU VAL TYR ASP VAL ARG ARG ASP          
SEQRES  26 C  381  ASP ALA PRO LEU ARG LYS VAL ALA GLY ILE PRO GLY GLU          
SEQRES  27 C  381  PHE ASP LYS LEU ARG LYS ASN TYR LEU GLU ARG ARG GLU          
SEQRES  28 C  381  TRP SER SER LEU TYR VAL MSE CYS ASP ASP GLU THR ALA          
SEQRES  29 C  381  ALA ALA LEU LEU CYS LYS LEU GLY PHE ASN ALA VAL HIS          
SEQRES  30 C  381  HIS PRO ALA HIS                                              
SEQRES   1 D  381  SER ASN ALA MSE LYS ILE LEU VAL ASP GLU ASN MSE PRO          
SEQRES   2 D  381  TYR ALA ARG GLU LEU PHE SER ARG LEU GLY GLU VAL LYS          
SEQRES   3 D  381  ALA VAL PRO GLY ARG PRO ILE PRO VAL GLU GLU LEU ASN          
SEQRES   4 D  381  HIS ALA ASP ALA LEU MSE VAL ARG SER VAL THR LYS VAL          
SEQRES   5 D  381  ASN GLU SER LEU LEU SER GLY THR PRO ILE ASN PHE VAL          
SEQRES   6 D  381  GLY THR ALA THR ALA GLY THR ASP HIS VAL ASP GLU ALA          
SEQRES   7 D  381  TRP LEU LYS GLN ALA GLY ILE GLY PHE SER ALA ALA PRO          
SEQRES   8 D  381  GLY CYS ASN ALA ILE ALA VAL VAL GLU TYR VAL PHE SER          
SEQRES   9 D  381  ALA LEU LEU MSE LEU ALA GLU ARG ASP GLY PHE SER LEU          
SEQRES  10 D  381  ARG ASP ARG THR ILE GLY ILE VAL GLY VAL GLY ASN VAL          
SEQRES  11 D  381  GLY SER ARG LEU GLN THR ARG LEU GLU ALA LEU GLY ILE          
SEQRES  12 D  381  ARG THR LEU LEU CYS ASP PRO PRO ARG ALA ALA ARG GLY          
SEQRES  13 D  381  ASP GLU GLY ASP PHE ARG THR LEU ASP GLU LEU VAL GLN          
SEQRES  14 D  381  GLU ALA ASP VAL LEU THR PHE HIS THR PRO LEU TYR LYS          
SEQRES  15 D  381  ASP GLY PRO TYR LYS THR LEU HIS LEU ALA ASP GLU THR          
SEQRES  16 D  381  LEU ILE ARG ARG LEU LYS PRO GLY ALA ILE LEU ILE ASN          
SEQRES  17 D  381  ALA CYS ARG GLY PRO VAL VAL ASP ASN ALA ALA LEU LEU          
SEQRES  18 D  381  ALA ARG LEU ASN ALA GLY GLN PRO LEU SER VAL VAL LEU          
SEQRES  19 D  381  ASP VAL TRP GLU GLY GLU PRO ASP LEU ASN VAL ALA LEU          
SEQRES  20 D  381  LEU GLU ALA VAL ASP ILE GLY THR SER HIS ILE ALA GLY          
SEQRES  21 D  381  TYR THR LEU GLU GLY LYS ALA ARG GLY THR THR GLN VAL          
SEQRES  22 D  381  PHE GLU ALA TYR SER ALA PHE ILE GLY ARG GLU GLN ARG          
SEQRES  23 D  381  VAL ALA LEU GLU THR LEU LEU PRO ALA PRO GLU PHE GLY          
SEQRES  24 D  381  ARG ILE THR LEU HIS GLY PRO LEU ASP GLN PRO THR LEU          
SEQRES  25 D  381  LYS ARG LEU ALA HIS LEU VAL TYR ASP VAL ARG ARG ASP          
SEQRES  26 D  381  ASP ALA PRO LEU ARG LYS VAL ALA GLY ILE PRO GLY GLU          
SEQRES  27 D  381  PHE ASP LYS LEU ARG LYS ASN TYR LEU GLU ARG ARG GLU          
SEQRES  28 D  381  TRP SER SER LEU TYR VAL MSE CYS ASP ASP GLU THR ALA          
SEQRES  29 D  381  ALA ALA LEU LEU CYS LYS LEU GLY PHE ASN ALA VAL HIS          
SEQRES  30 D  381  HIS PRO ALA HIS                                              
SEQRES   1 E  381  SER ASN ALA MSE LYS ILE LEU VAL ASP GLU ASN MSE PRO          
SEQRES   2 E  381  TYR ALA ARG GLU LEU PHE SER ARG LEU GLY GLU VAL LYS          
SEQRES   3 E  381  ALA VAL PRO GLY ARG PRO ILE PRO VAL GLU GLU LEU ASN          
SEQRES   4 E  381  HIS ALA ASP ALA LEU MSE VAL ARG SER VAL THR LYS VAL          
SEQRES   5 E  381  ASN GLU SER LEU LEU SER GLY THR PRO ILE ASN PHE VAL          
SEQRES   6 E  381  GLY THR ALA THR ALA GLY THR ASP HIS VAL ASP GLU ALA          
SEQRES   7 E  381  TRP LEU LYS GLN ALA GLY ILE GLY PHE SER ALA ALA PRO          
SEQRES   8 E  381  GLY CYS ASN ALA ILE ALA VAL VAL GLU TYR VAL PHE SER          
SEQRES   9 E  381  ALA LEU LEU MSE LEU ALA GLU ARG ASP GLY PHE SER LEU          
SEQRES  10 E  381  ARG ASP ARG THR ILE GLY ILE VAL GLY VAL GLY ASN VAL          
SEQRES  11 E  381  GLY SER ARG LEU GLN THR ARG LEU GLU ALA LEU GLY ILE          
SEQRES  12 E  381  ARG THR LEU LEU CYS ASP PRO PRO ARG ALA ALA ARG GLY          
SEQRES  13 E  381  ASP GLU GLY ASP PHE ARG THR LEU ASP GLU LEU VAL GLN          
SEQRES  14 E  381  GLU ALA ASP VAL LEU THR PHE HIS THR PRO LEU TYR LYS          
SEQRES  15 E  381  ASP GLY PRO TYR LYS THR LEU HIS LEU ALA ASP GLU THR          
SEQRES  16 E  381  LEU ILE ARG ARG LEU LYS PRO GLY ALA ILE LEU ILE ASN          
SEQRES  17 E  381  ALA CYS ARG GLY PRO VAL VAL ASP ASN ALA ALA LEU LEU          
SEQRES  18 E  381  ALA ARG LEU ASN ALA GLY GLN PRO LEU SER VAL VAL LEU          
SEQRES  19 E  381  ASP VAL TRP GLU GLY GLU PRO ASP LEU ASN VAL ALA LEU          
SEQRES  20 E  381  LEU GLU ALA VAL ASP ILE GLY THR SER HIS ILE ALA GLY          
SEQRES  21 E  381  TYR THR LEU GLU GLY LYS ALA ARG GLY THR THR GLN VAL          
SEQRES  22 E  381  PHE GLU ALA TYR SER ALA PHE ILE GLY ARG GLU GLN ARG          
SEQRES  23 E  381  VAL ALA LEU GLU THR LEU LEU PRO ALA PRO GLU PHE GLY          
SEQRES  24 E  381  ARG ILE THR LEU HIS GLY PRO LEU ASP GLN PRO THR LEU          
SEQRES  25 E  381  LYS ARG LEU ALA HIS LEU VAL TYR ASP VAL ARG ARG ASP          
SEQRES  26 E  381  ASP ALA PRO LEU ARG LYS VAL ALA GLY ILE PRO GLY GLU          
SEQRES  27 E  381  PHE ASP LYS LEU ARG LYS ASN TYR LEU GLU ARG ARG GLU          
SEQRES  28 E  381  TRP SER SER LEU TYR VAL MSE CYS ASP ASP GLU THR ALA          
SEQRES  29 E  381  ALA ALA LEU LEU CYS LYS LEU GLY PHE ASN ALA VAL HIS          
SEQRES  30 E  381  HIS PRO ALA HIS                                              
SEQRES   1 F  381  SER ASN ALA MSE LYS ILE LEU VAL ASP GLU ASN MSE PRO          
SEQRES   2 F  381  TYR ALA ARG GLU LEU PHE SER ARG LEU GLY GLU VAL LYS          
SEQRES   3 F  381  ALA VAL PRO GLY ARG PRO ILE PRO VAL GLU GLU LEU ASN          
SEQRES   4 F  381  HIS ALA ASP ALA LEU MSE VAL ARG SER VAL THR LYS VAL          
SEQRES   5 F  381  ASN GLU SER LEU LEU SER GLY THR PRO ILE ASN PHE VAL          
SEQRES   6 F  381  GLY THR ALA THR ALA GLY THR ASP HIS VAL ASP GLU ALA          
SEQRES   7 F  381  TRP LEU LYS GLN ALA GLY ILE GLY PHE SER ALA ALA PRO          
SEQRES   8 F  381  GLY CYS ASN ALA ILE ALA VAL VAL GLU TYR VAL PHE SER          
SEQRES   9 F  381  ALA LEU LEU MSE LEU ALA GLU ARG ASP GLY PHE SER LEU          
SEQRES  10 F  381  ARG ASP ARG THR ILE GLY ILE VAL GLY VAL GLY ASN VAL          
SEQRES  11 F  381  GLY SER ARG LEU GLN THR ARG LEU GLU ALA LEU GLY ILE          
SEQRES  12 F  381  ARG THR LEU LEU CYS ASP PRO PRO ARG ALA ALA ARG GLY          
SEQRES  13 F  381  ASP GLU GLY ASP PHE ARG THR LEU ASP GLU LEU VAL GLN          
SEQRES  14 F  381  GLU ALA ASP VAL LEU THR PHE HIS THR PRO LEU TYR LYS          
SEQRES  15 F  381  ASP GLY PRO TYR LYS THR LEU HIS LEU ALA ASP GLU THR          
SEQRES  16 F  381  LEU ILE ARG ARG LEU LYS PRO GLY ALA ILE LEU ILE ASN          
SEQRES  17 F  381  ALA CYS ARG GLY PRO VAL VAL ASP ASN ALA ALA LEU LEU          
SEQRES  18 F  381  ALA ARG LEU ASN ALA GLY GLN PRO LEU SER VAL VAL LEU          
SEQRES  19 F  381  ASP VAL TRP GLU GLY GLU PRO ASP LEU ASN VAL ALA LEU          
SEQRES  20 F  381  LEU GLU ALA VAL ASP ILE GLY THR SER HIS ILE ALA GLY          
SEQRES  21 F  381  TYR THR LEU GLU GLY LYS ALA ARG GLY THR THR GLN VAL          
SEQRES  22 F  381  PHE GLU ALA TYR SER ALA PHE ILE GLY ARG GLU GLN ARG          
SEQRES  23 F  381  VAL ALA LEU GLU THR LEU LEU PRO ALA PRO GLU PHE GLY          
SEQRES  24 F  381  ARG ILE THR LEU HIS GLY PRO LEU ASP GLN PRO THR LEU          
SEQRES  25 F  381  LYS ARG LEU ALA HIS LEU VAL TYR ASP VAL ARG ARG ASP          
SEQRES  26 F  381  ASP ALA PRO LEU ARG LYS VAL ALA GLY ILE PRO GLY GLU          
SEQRES  27 F  381  PHE ASP LYS LEU ARG LYS ASN TYR LEU GLU ARG ARG GLU          
SEQRES  28 F  381  TRP SER SER LEU TYR VAL MSE CYS ASP ASP GLU THR ALA          
SEQRES  29 F  381  ALA ALA LEU LEU CYS LYS LEU GLY PHE ASN ALA VAL HIS          
SEQRES  30 F  381  HIS PRO ALA HIS                                              
SEQRES   1 G  381  SER ASN ALA MSE LYS ILE LEU VAL ASP GLU ASN MSE PRO          
SEQRES   2 G  381  TYR ALA ARG GLU LEU PHE SER ARG LEU GLY GLU VAL LYS          
SEQRES   3 G  381  ALA VAL PRO GLY ARG PRO ILE PRO VAL GLU GLU LEU ASN          
SEQRES   4 G  381  HIS ALA ASP ALA LEU MSE VAL ARG SER VAL THR LYS VAL          
SEQRES   5 G  381  ASN GLU SER LEU LEU SER GLY THR PRO ILE ASN PHE VAL          
SEQRES   6 G  381  GLY THR ALA THR ALA GLY THR ASP HIS VAL ASP GLU ALA          
SEQRES   7 G  381  TRP LEU LYS GLN ALA GLY ILE GLY PHE SER ALA ALA PRO          
SEQRES   8 G  381  GLY CYS ASN ALA ILE ALA VAL VAL GLU TYR VAL PHE SER          
SEQRES   9 G  381  ALA LEU LEU MSE LEU ALA GLU ARG ASP GLY PHE SER LEU          
SEQRES  10 G  381  ARG ASP ARG THR ILE GLY ILE VAL GLY VAL GLY ASN VAL          
SEQRES  11 G  381  GLY SER ARG LEU GLN THR ARG LEU GLU ALA LEU GLY ILE          
SEQRES  12 G  381  ARG THR LEU LEU CYS ASP PRO PRO ARG ALA ALA ARG GLY          
SEQRES  13 G  381  ASP GLU GLY ASP PHE ARG THR LEU ASP GLU LEU VAL GLN          
SEQRES  14 G  381  GLU ALA ASP VAL LEU THR PHE HIS THR PRO LEU TYR LYS          
SEQRES  15 G  381  ASP GLY PRO TYR LYS THR LEU HIS LEU ALA ASP GLU THR          
SEQRES  16 G  381  LEU ILE ARG ARG LEU LYS PRO GLY ALA ILE LEU ILE ASN          
SEQRES  17 G  381  ALA CYS ARG GLY PRO VAL VAL ASP ASN ALA ALA LEU LEU          
SEQRES  18 G  381  ALA ARG LEU ASN ALA GLY GLN PRO LEU SER VAL VAL LEU          
SEQRES  19 G  381  ASP VAL TRP GLU GLY GLU PRO ASP LEU ASN VAL ALA LEU          
SEQRES  20 G  381  LEU GLU ALA VAL ASP ILE GLY THR SER HIS ILE ALA GLY          
SEQRES  21 G  381  TYR THR LEU GLU GLY LYS ALA ARG GLY THR THR GLN VAL          
SEQRES  22 G  381  PHE GLU ALA TYR SER ALA PHE ILE GLY ARG GLU GLN ARG          
SEQRES  23 G  381  VAL ALA LEU GLU THR LEU LEU PRO ALA PRO GLU PHE GLY          
SEQRES  24 G  381  ARG ILE THR LEU HIS GLY PRO LEU ASP GLN PRO THR LEU          
SEQRES  25 G  381  LYS ARG LEU ALA HIS LEU VAL TYR ASP VAL ARG ARG ASP          
SEQRES  26 G  381  ASP ALA PRO LEU ARG LYS VAL ALA GLY ILE PRO GLY GLU          
SEQRES  27 G  381  PHE ASP LYS LEU ARG LYS ASN TYR LEU GLU ARG ARG GLU          
SEQRES  28 G  381  TRP SER SER LEU TYR VAL MSE CYS ASP ASP GLU THR ALA          
SEQRES  29 G  381  ALA ALA LEU LEU CYS LYS LEU GLY PHE ASN ALA VAL HIS          
SEQRES  30 G  381  HIS PRO ALA HIS                                              
SEQRES   1 H  381  SER ASN ALA MSE LYS ILE LEU VAL ASP GLU ASN MSE PRO          
SEQRES   2 H  381  TYR ALA ARG GLU LEU PHE SER ARG LEU GLY GLU VAL LYS          
SEQRES   3 H  381  ALA VAL PRO GLY ARG PRO ILE PRO VAL GLU GLU LEU ASN          
SEQRES   4 H  381  HIS ALA ASP ALA LEU MSE VAL ARG SER VAL THR LYS VAL          
SEQRES   5 H  381  ASN GLU SER LEU LEU SER GLY THR PRO ILE ASN PHE VAL          
SEQRES   6 H  381  GLY THR ALA THR ALA GLY THR ASP HIS VAL ASP GLU ALA          
SEQRES   7 H  381  TRP LEU LYS GLN ALA GLY ILE GLY PHE SER ALA ALA PRO          
SEQRES   8 H  381  GLY CYS ASN ALA ILE ALA VAL VAL GLU TYR VAL PHE SER          
SEQRES   9 H  381  ALA LEU LEU MSE LEU ALA GLU ARG ASP GLY PHE SER LEU          
SEQRES  10 H  381  ARG ASP ARG THR ILE GLY ILE VAL GLY VAL GLY ASN VAL          
SEQRES  11 H  381  GLY SER ARG LEU GLN THR ARG LEU GLU ALA LEU GLY ILE          
SEQRES  12 H  381  ARG THR LEU LEU CYS ASP PRO PRO ARG ALA ALA ARG GLY          
SEQRES  13 H  381  ASP GLU GLY ASP PHE ARG THR LEU ASP GLU LEU VAL GLN          
SEQRES  14 H  381  GLU ALA ASP VAL LEU THR PHE HIS THR PRO LEU TYR LYS          
SEQRES  15 H  381  ASP GLY PRO TYR LYS THR LEU HIS LEU ALA ASP GLU THR          
SEQRES  16 H  381  LEU ILE ARG ARG LEU LYS PRO GLY ALA ILE LEU ILE ASN          
SEQRES  17 H  381  ALA CYS ARG GLY PRO VAL VAL ASP ASN ALA ALA LEU LEU          
SEQRES  18 H  381  ALA ARG LEU ASN ALA GLY GLN PRO LEU SER VAL VAL LEU          
SEQRES  19 H  381  ASP VAL TRP GLU GLY GLU PRO ASP LEU ASN VAL ALA LEU          
SEQRES  20 H  381  LEU GLU ALA VAL ASP ILE GLY THR SER HIS ILE ALA GLY          
SEQRES  21 H  381  TYR THR LEU GLU GLY LYS ALA ARG GLY THR THR GLN VAL          
SEQRES  22 H  381  PHE GLU ALA TYR SER ALA PHE ILE GLY ARG GLU GLN ARG          
SEQRES  23 H  381  VAL ALA LEU GLU THR LEU LEU PRO ALA PRO GLU PHE GLY          
SEQRES  24 H  381  ARG ILE THR LEU HIS GLY PRO LEU ASP GLN PRO THR LEU          
SEQRES  25 H  381  LYS ARG LEU ALA HIS LEU VAL TYR ASP VAL ARG ARG ASP          
SEQRES  26 H  381  ASP ALA PRO LEU ARG LYS VAL ALA GLY ILE PRO GLY GLU          
SEQRES  27 H  381  PHE ASP LYS LEU ARG LYS ASN TYR LEU GLU ARG ARG GLU          
SEQRES  28 H  381  TRP SER SER LEU TYR VAL MSE CYS ASP ASP GLU THR ALA          
SEQRES  29 H  381  ALA ALA LEU LEU CYS LYS LEU GLY PHE ASN ALA VAL HIS          
SEQRES  30 H  381  HIS PRO ALA HIS                                              
MODRES 3OET MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE A    9  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE A   42  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE A  105  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE A  355  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE B    9  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE B   42  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE B  105  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE B  355  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE C    1  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE C    9  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE C   42  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE C  105  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE C  355  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE D    1  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE D    9  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE D   42  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE D  105  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE D  355  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE E    1  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE E    9  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE E   42  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE E  105  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE E  355  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE F    1  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE F    9  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE F   42  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE F  105  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE F  355  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE G    1  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE G    9  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE G   42  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE G  105  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE G  355  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE H    1  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE H    9  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE H   42  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE H  105  MET  SELENOMETHIONINE                                   
MODRES 3OET MSE H  355  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A   9       8                                                       
HET    MSE  A  42       8                                                       
HET    MSE  A 105       8                                                       
HET    MSE  A 355       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B   9       8                                                       
HET    MSE  B  42       8                                                       
HET    MSE  B 105       8                                                       
HET    MSE  B 355       8                                                       
HET    MSE  C   1       8                                                       
HET    MSE  C   9       8                                                       
HET    MSE  C  42       8                                                       
HET    MSE  C 105       8                                                       
HET    MSE  C 355       8                                                       
HET    MSE  D   1       8                                                       
HET    MSE  D   9       8                                                       
HET    MSE  D  42       8                                                       
HET    MSE  D 105       8                                                       
HET    MSE  D 355       8                                                       
HET    MSE  E   1       8                                                       
HET    MSE  E   9       8                                                       
HET    MSE  E  42       8                                                       
HET    MSE  E 105       8                                                       
HET    MSE  E 355       8                                                       
HET    MSE  F   1       8                                                       
HET    MSE  F   9       8                                                       
HET    MSE  F  42       8                                                       
HET    MSE  F 105       8                                                       
HET    MSE  F 355       8                                                       
HET    MSE  G   1       8                                                       
HET    MSE  G   9       8                                                       
HET    MSE  G  42       8                                                       
HET    MSE  G 105       8                                                       
HET    MSE  G 355       8                                                       
HET    MSE  H   1       8                                                       
HET    MSE  H   9       8                                                       
HET    MSE  H  42       8                                                       
HET    MSE  H 105       8                                                       
HET    MSE  H 355       8                                                       
HET    NAD  A 379      44                                                       
HET    NAD  B 379      44                                                       
HET    NAD  C 379      44                                                       
HET    NAD  D 379      44                                                       
HET    NAD  E 379      44                                                       
HET    NAD  F 379      44                                                       
HET    NAD  G 379      44                                                       
HET    NAD  H 379      44                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
FORMUL   1  MSE    40(C5 H11 N O2 SE)                                           
FORMUL   9  NAD    8(C21 H27 N7 O14 P2)                                         
FORMUL  17  HOH   *556(H2 O)                                                    
HELIX    1   1 TYR A   11  SER A   17  1                                   7    
HELIX    2   2 PRO A   31  ASN A   36  1                                   6    
HELIX    3   3 ASN A   50  SER A   55  1                                   6    
HELIX    4   4 ASP A   73  ALA A   80  1                                   8    
HELIX    5   5 ASN A   91  ASP A  110  1                                  20    
HELIX    6   6 SER A  113  ASP A  116  5                                   4    
HELIX    7   7 GLY A  125  LEU A  138  1                                  14    
HELIX    8   8 ASP A  146  ARG A  152  1                                   7    
HELIX    9   9 THR A  160  ALA A  168  1                                   9    
HELIX   10  10 ASP A  190  LEU A  197  1                                   8    
HELIX   11  11 ARG A  208  VAL A  212  5                                   5    
HELIX   12  12 ASP A  213  ALA A  223  1                                  11    
HELIX   13  13 ASN A  241  VAL A  248  1                                   8    
HELIX   14  14 THR A  259  ILE A  278  1                                  20    
HELIX   15  15 ALA A  285  LEU A  290  1                                   6    
HELIX   16  16 ASP A  305  TYR A  317  1                                  13    
HELIX   17  17 VAL A  319  ALA A  330  1                                  12    
HELIX   18  18 GLY A  334  ASN A  342  1                                   9    
HELIX   19  19 GLU A  348  SER A  351  5                                   4    
HELIX   20  20 ASP A  358  GLY A  369  1                                  12    
HELIX   21  21 TYR B   11  SER B   17  1                                   7    
HELIX   22  22 GLU B   34  ALA B   38  5                                   5    
HELIX   23  23 ASN B   50  SER B   55  1                                   6    
HELIX   24  24 ASP B   73  ALA B   80  1                                   8    
HELIX   25  25 ASN B   91  GLY B  111  1                                  21    
HELIX   26  26 SER B  113  ASP B  116  5                                   4    
HELIX   27  27 GLY B  125  LEU B  138  1                                  14    
HELIX   28  28 ASP B  146  GLY B  153  1                                   8    
HELIX   29  29 THR B  160  ALA B  168  1                                   9    
HELIX   30  30 ASP B  190  ARG B  195  1                                   6    
HELIX   31  31 ARG B  208  VAL B  212  5                                   5    
HELIX   32  32 ASP B  213  ALA B  223  1                                  11    
HELIX   33  33 ASN B  241  VAL B  248  1                                   8    
HELIX   34  34 THR B  259  ILE B  278  1                                  20    
HELIX   35  35 ALA B  285  LEU B  289  5                                   5    
HELIX   36  36 ASP B  305  TYR B  317  1                                  13    
HELIX   37  37 VAL B  319  ALA B  330  1                                  12    
HELIX   38  38 GLY B  334  ASN B  342  1                                   9    
HELIX   39  39 GLU B  348  SER B  351  5                                   4    
HELIX   40  40 ASP B  358  GLY B  369  1                                  12    
HELIX   41  41 TYR C   11  SER C   17  1                                   7    
HELIX   42  42 ARG C   18  GLY C   20  5                                   3    
HELIX   43  43 ASP C   73  ALA C   80  1                                   8    
HELIX   44  44 ASN C   91  ASP C  110  1                                  20    
HELIX   45  45 SER C  113  ASP C  116  5                                   4    
HELIX   46  46 GLY C  125  LEU C  138  1                                  14    
HELIX   47  47 ASP C  146  ARG C  152  1                                   7    
HELIX   48  48 THR C  160  ALA C  168  1                                   9    
HELIX   49  49 ASP C  190  LEU C  197  1                                   8    
HELIX   50  50 ARG C  208  VAL C  212  5                                   5    
HELIX   51  51 ASP C  213  ALA C  223  1                                  11    
HELIX   52  52 ASN C  241  VAL C  248  1                                   8    
HELIX   53  53 THR C  259  ILE C  278  1                                  20    
HELIX   54  54 ALA C  285  LEU C  289  5                                   5    
HELIX   55  55 ASP C  305  TYR C  317  1                                  13    
HELIX   56  56 VAL C  319  ALA C  330  1                                  12    
HELIX   57  57 GLY C  334  ASN C  342  1                                   9    
HELIX   58  58 GLU C  348  SER C  351  5                                   4    
HELIX   59  59 ASP C  358  GLY C  369  1                                  12    
HELIX   60  60 TYR D   11  SER D   17  1                                   7    
HELIX   61  61 PRO D   31  ASN D   36  1                                   6    
HELIX   62  62 ASP D   73  ALA D   80  1                                   8    
HELIX   63  63 ASN D   91  ASP D  110  1                                  20    
HELIX   64  64 SER D  113  ASP D  116  5                                   4    
HELIX   65  65 GLY D  125  LEU D  138  1                                  14    
HELIX   66  66 ASP D  146  GLY D  153  1                                   8    
HELIX   67  67 THR D  160  ALA D  168  1                                   9    
HELIX   68  68 ASP D  190  LEU D  197  1                                   8    
HELIX   69  69 ARG D  208  VAL D  212  5                                   5    
HELIX   70  70 ASP D  213  ALA D  223  1                                  11    
HELIX   71  71 ASN D  241  VAL D  248  1                                   8    
HELIX   72  72 THR D  259  ILE D  278  1                                  20    
HELIX   73  73 ALA D  285  LEU D  289  5                                   5    
HELIX   74  74 ASP D  305  TYR D  317  1                                  13    
HELIX   75  75 VAL D  319  ALA D  330  1                                  12    
HELIX   76  76 GLY D  334  ASN D  342  1                                   9    
HELIX   77  77 GLU D  348  SER D  351  5                                   4    
HELIX   78  78 ASP D  358  GLY D  369  1                                  12    
HELIX   79  79 TYR E   11  SER E   17  1                                   7    
HELIX   80  80 PRO E   31  ASN E   36  1                                   6    
HELIX   81  81 ASN E   50  SER E   55  1                                   6    
HELIX   82  82 ASP E   73  GLY E   81  1                                   9    
HELIX   83  83 ASN E   91  GLY E  111  1                                  21    
HELIX   84  84 SER E  113  ASP E  116  5                                   4    
HELIX   85  85 GLY E  125  LEU E  138  1                                  14    
HELIX   86  86 ASP E  146  ARG E  152  1                                   7    
HELIX   87  87 THR E  160  ALA E  168  1                                   9    
HELIX   88  88 ASP E  190  LEU E  197  1                                   8    
HELIX   89  89 ARG E  208  VAL E  212  5                                   5    
HELIX   90  90 ASP E  213  ALA E  223  1                                  11    
HELIX   91  91 ASN E  241  VAL E  248  1                                   8    
HELIX   92  92 THR E  259  ILE E  278  1                                  20    
HELIX   93  93 ALA E  285  LEU E  289  5                                   5    
HELIX   94  94 ASP E  305  TYR E  317  1                                  13    
HELIX   95  95 VAL E  319  ALA E  330  1                                  12    
HELIX   96  96 GLY E  334  ASN E  342  1                                   9    
HELIX   97  97 GLU E  348  SER E  351  5                                   4    
HELIX   98  98 ASP E  358  GLY E  369  1                                  12    
HELIX   99  99 TYR F   11  SER F   17  1                                   7    
HELIX  100 100 ASP F   73  ALA F   80  1                                   8    
HELIX  101 101 ASN F   91  ASP F  110  1                                  20    
HELIX  102 102 SER F  113  ASP F  116  5                                   4    
HELIX  103 103 GLY F  125  LEU F  138  1                                  14    
HELIX  104 104 ASP F  146  GLY F  153  1                                   8    
HELIX  105 105 THR F  160  ALA F  168  1                                   9    
HELIX  106 106 ASP F  190  LEU F  197  1                                   8    
HELIX  107 107 ARG F  208  VAL F  212  5                                   5    
HELIX  108 108 ASP F  213  GLY F  224  1                                  12    
HELIX  109 109 ASN F  241  VAL F  248  1                                   8    
HELIX  110 110 THR F  259  ILE F  278  1                                  20    
HELIX  111 111 ASP F  305  TYR F  317  1                                  13    
HELIX  112 112 VAL F  319  ALA F  330  1                                  12    
HELIX  113 113 GLY F  334  ASN F  342  1                                   9    
HELIX  114 114 GLU F  348  SER F  351  5                                   4    
HELIX  115 115 ASP F  358  GLY F  369  1                                  12    
HELIX  116 116 TYR G   11  SER G   17  1                                   7    
HELIX  117 117 PRO G   31  ASN G   36  1                                   6    
HELIX  118 118 ASN G   50  SER G   55  1                                   6    
HELIX  119 119 ASP G   73  GLY G   81  1                                   9    
HELIX  120 120 ASN G   91  GLY G  111  1                                  21    
HELIX  121 121 SER G  113  ASP G  116  5                                   4    
HELIX  122 122 GLY G  125  LEU G  138  1                                  14    
HELIX  123 123 ASP G  146  GLY G  153  1                                   8    
HELIX  124 124 THR G  160  ALA G  168  1                                   9    
HELIX  125 125 ASP G  190  ARG G  196  1                                   7    
HELIX  126 126 ARG G  208  VAL G  212  5                                   5    
HELIX  127 127 ASP G  213  ALA G  223  1                                  11    
HELIX  128 128 ASN G  241  VAL G  248  1                                   8    
HELIX  129 129 THR G  259  ILE G  278  1                                  20    
HELIX  130 130 ALA G  285  LEU G  290  1                                   6    
HELIX  131 131 ASP G  305  TYR G  317  1                                  13    
HELIX  132 132 VAL G  319  ALA G  330  1                                  12    
HELIX  133 133 GLY G  334  ASN G  342  1                                   9    
HELIX  134 134 GLU G  348  SER G  351  5                                   4    
HELIX  135 135 ASP G  358  GLY G  369  1                                  12    
HELIX  136 136 TYR H   11  SER H   17  1                                   7    
HELIX  137 137 PRO H   31  ASN H   36  1                                   6    
HELIX  138 138 ASN H   50  SER H   55  1                                   6    
HELIX  139 139 ASP H   73  GLY H   81  1                                   9    
HELIX  140 140 ASN H   91  GLY H  111  1                                  21    
HELIX  141 141 SER H  113  ASP H  116  5                                   4    
HELIX  142 142 GLY H  125  LEU H  138  1                                  14    
HELIX  143 143 ASP H  146  GLY H  153  1                                   8    
HELIX  144 144 THR H  160  ALA H  168  1                                   9    
HELIX  145 145 ASP H  190  ARG H  196  1                                   7    
HELIX  146 146 ARG H  208  VAL H  212  5                                   5    
HELIX  147 147 ASP H  213  ALA H  223  1                                  11    
HELIX  148 148 ASN H  241  VAL H  248  1                                   8    
HELIX  149 149 THR H  259  ILE H  278  1                                  20    
HELIX  150 150 ALA H  285  LEU H  289  5                                   5    
HELIX  151 151 ASP H  305  TYR H  317  1                                  13    
HELIX  152 152 VAL H  319  ALA H  330  1                                  12    
HELIX  153 153 GLY H  334  ASN H  342  1                                   9    
HELIX  154 154 GLU H  348  SER H  351  5                                   4    
HELIX  155 155 ASP H  358  GLY H  369  1                                  12    
SHEET    1   A 5 GLU A  21  VAL A  25  0                                        
SHEET    2   A 5 LYS A   2  ASP A   6  1  N  ILE A   3   O  GLU A  21           
SHEET    3   A 5 ALA A  40  VAL A  43  1  O  MSE A  42   N  LEU A   4           
SHEET    4   A 5 PHE A  61  THR A  64  1  O  GLY A  63   N  VAL A  43           
SHEET    5   A 5 GLY A  83  SER A  85  1  O  SER A  85   N  THR A  64           
SHEET    1   B 6 ARG A 141  CYS A 145  0                                        
SHEET    2   B 6 THR A 118  VAL A 122  1  N  ILE A 121   O  LEU A 143           
SHEET    3   B 6 VAL A 170  PHE A 173  1  O  VAL A 170   N  GLY A 120           
SHEET    4   B 6 ALA A 201  ASN A 205  1  O  ILE A 202   N  LEU A 171           
SHEET    5   B 6 LEU A 227  LEU A 231  1  O  SER A 228   N  LEU A 203           
SHEET    6   B 6 ILE A 250  GLY A 251  1  O  ILE A 250   N  LEU A 231           
SHEET    1   C 3 ARG A 297  LEU A 300  0                                        
SHEET    2   C 3 TYR A 353  CYS A 356  1  O  MSE A 355   N  LEU A 300           
SHEET    3   C 3 ASN A 371  HIS A 374  1  O  VAL A 373   N  VAL A 354           
SHEET    1   D 5 GLY B  20  VAL B  25  0                                        
SHEET    2   D 5 MSE B   1  ASP B   6  1  N  ILE B   3   O  GLU B  21           
SHEET    3   D 5 ALA B  40  VAL B  43  1  O  ALA B  40   N  LEU B   4           
SHEET    4   D 5 PHE B  61  THR B  64  1  O  PHE B  61   N  LEU B  41           
SHEET    5   D 5 GLY B  83  SER B  85  1  O  GLY B  83   N  VAL B  62           
SHEET    1   E 6 ARG B 141  CYS B 145  0                                        
SHEET    2   E 6 THR B 118  VAL B 122  1  N  ILE B 121   O  LEU B 143           
SHEET    3   E 6 VAL B 170  PHE B 173  1  O  VAL B 170   N  GLY B 120           
SHEET    4   E 6 ALA B 201  ASN B 205  1  O  ILE B 202   N  LEU B 171           
SHEET    5   E 6 LEU B 227  LEU B 231  1  O  SER B 228   N  LEU B 203           
SHEET    6   E 6 ILE B 250  GLY B 251  1  O  ILE B 250   N  LEU B 231           
SHEET    1   F 3 ARG B 297  LEU B 300  0                                        
SHEET    2   F 3 TYR B 353  CYS B 356  1  O  MSE B 355   N  ILE B 298           
SHEET    3   F 3 ASN B 371  HIS B 374  1  O  VAL B 373   N  CYS B 356           
SHEET    1   G 5 GLU C  21  VAL C  25  0                                        
SHEET    2   G 5 LYS C   2  ASP C   6  1  N  ILE C   3   O  GLU C  21           
SHEET    3   G 5 ALA C  40  VAL C  43  1  O  ALA C  40   N  LEU C   4           
SHEET    4   G 5 PHE C  61  THR C  64  1  O  GLY C  63   N  LEU C  41           
SHEET    5   G 5 GLY C  83  SER C  85  1  O  SER C  85   N  THR C  64           
SHEET    1   H 6 ARG C 141  CYS C 145  0                                        
SHEET    2   H 6 THR C 118  VAL C 122  1  N  ILE C 121   O  LEU C 143           
SHEET    3   H 6 VAL C 170  PHE C 173  1  O  VAL C 170   N  GLY C 120           
SHEET    4   H 6 ALA C 201  ASN C 205  1  O  ILE C 202   N  LEU C 171           
SHEET    5   H 6 LEU C 227  LEU C 231  1  O  VAL C 230   N  LEU C 203           
SHEET    6   H 6 ILE C 250  GLY C 251  1  O  ILE C 250   N  LEU C 231           
SHEET    1   I 3 ARG C 297  LEU C 300  0                                        
SHEET    2   I 3 TYR C 353  CYS C 356  1  O  MSE C 355   N  LEU C 300           
SHEET    3   I 3 ASN C 371  HIS C 374  1  O  VAL C 373   N  CYS C 356           
SHEET    1   J 5 GLY D  20  VAL D  25  0                                        
SHEET    2   J 5 MSE D   1  ASP D   6  1  N  ILE D   3   O  GLU D  21           
SHEET    3   J 5 ALA D  40  VAL D  43  1  O  ALA D  40   N  LEU D   4           
SHEET    4   J 5 PHE D  61  THR D  64  1  O  GLY D  63   N  LEU D  41           
SHEET    5   J 5 GLY D  83  SER D  85  1  O  SER D  85   N  THR D  64           
SHEET    1   K 6 ARG D 141  CYS D 145  0                                        
SHEET    2   K 6 THR D 118  VAL D 122  1  N  ILE D 119   O  LEU D 143           
SHEET    3   K 6 VAL D 170  PHE D 173  1  O  VAL D 170   N  GLY D 120           
SHEET    4   K 6 ALA D 201  ASN D 205  1  O  ILE D 202   N  LEU D 171           
SHEET    5   K 6 LEU D 227  LEU D 231  1  O  SER D 228   N  ALA D 201           
SHEET    6   K 6 ILE D 250  GLY D 251  1  O  ILE D 250   N  LEU D 231           
SHEET    1   L 6 ASN D 371  HIS D 374  0                                        
SHEET    2   L 6 TYR D 353  CYS D 356  1  N  CYS D 356   O  VAL D 373           
SHEET    3   L 6 PHE D 295  LEU D 300  1  N  GLY D 296   O  TYR D 353           
SHEET    4   L 6 ARG G 297  LEU G 300 -1  O  THR G 299   N  ARG D 297           
SHEET    5   L 6 TYR G 353  CYS G 356  1  O  MSE G 355   N  ILE G 298           
SHEET    6   L 6 ASN G 371  HIS G 374  1  O  VAL G 373   N  CYS G 356           
SHEET    1   M 5 GLU E  21  VAL E  25  0                                        
SHEET    2   M 5 LYS E   2  ASP E   6  1  N  ILE E   3   O  GLU E  21           
SHEET    3   M 5 ALA E  40  VAL E  43  1  O  ALA E  40   N  LEU E   4           
SHEET    4   M 5 PHE E  61  THR E  64  1  O  GLY E  63   N  VAL E  43           
SHEET    5   M 5 GLY E  83  SER E  85  1  O  SER E  85   N  THR E  64           
SHEET    1   N 6 ARG E 141  CYS E 145  0                                        
SHEET    2   N 6 THR E 118  VAL E 122  1  N  ILE E 121   O  LEU E 143           
SHEET    3   N 6 VAL E 170  PHE E 173  1  O  VAL E 170   N  GLY E 120           
SHEET    4   N 6 ALA E 201  ASN E 205  1  O  ILE E 204   N  LEU E 171           
SHEET    5   N 6 LEU E 227  LEU E 231  1  O  SER E 228   N  ALA E 201           
SHEET    6   N 6 ILE E 250  GLY E 251  1  O  ILE E 250   N  LEU E 231           
SHEET    1   O 3 ARG E 297  LEU E 300  0                                        
SHEET    2   O 3 TYR E 353  CYS E 356  1  O  MSE E 355   N  ILE E 298           
SHEET    3   O 3 ASN E 371  HIS E 374  1  O  VAL E 373   N  CYS E 356           
SHEET    1   P 3 GLU F  21  VAL F  25  0                                        
SHEET    2   P 3 LYS F   2  ASP F   6  1  N  ILE F   3   O  GLU F  21           
SHEET    3   P 3 ALA F  40  MSE F  42  1  O  ALA F  40   N  LEU F   4           
SHEET    1   Q 2 PHE F  61  GLY F  63  0                                        
SHEET    2   Q 2 GLY F  83  SER F  85  1  O  GLY F  83   N  VAL F  62           
SHEET    1   R 6 ARG F 141  CYS F 145  0                                        
SHEET    2   R 6 THR F 118  VAL F 122  1  N  ILE F 121   O  LEU F 143           
SHEET    3   R 6 VAL F 170  PHE F 173  1  O  VAL F 170   N  GLY F 120           
SHEET    4   R 6 ALA F 201  ASN F 205  1  O  ILE F 204   N  LEU F 171           
SHEET    5   R 6 LEU F 227  LEU F 231  1  O  SER F 228   N  ALA F 201           
SHEET    6   R 6 ILE F 250  GLY F 251  1  O  ILE F 250   N  LEU F 231           
SHEET    1   S 3 ARG F 297  LEU F 300  0                                        
SHEET    2   S 3 TYR F 353  CYS F 356  1  O  MSE F 355   N  LEU F 300           
SHEET    3   S 3 ASN F 371  HIS F 374  1  O  VAL F 373   N  CYS F 356           
SHEET    1   T 5 GLU G  21  VAL G  22  0                                        
SHEET    2   T 5 LYS G   2  VAL G   5  1  N  ILE G   3   O  GLU G  21           
SHEET    3   T 5 ALA G  40  VAL G  43  1  O  ALA G  40   N  LEU G   4           
SHEET    4   T 5 PHE G  61  THR G  64  1  O  GLY G  63   N  VAL G  43           
SHEET    5   T 5 GLY G  83  SER G  85  1  O  SER G  85   N  THR G  64           
SHEET    1   U 6 ARG G 141  CYS G 145  0                                        
SHEET    2   U 6 THR G 118  VAL G 122  1  N  ILE G 119   O  LEU G 143           
SHEET    3   U 6 VAL G 170  PHE G 173  1  O  VAL G 170   N  GLY G 120           
SHEET    4   U 6 ALA G 201  ASN G 205  1  O  ILE G 202   N  LEU G 171           
SHEET    5   U 6 LEU G 227  LEU G 231  1  O  VAL G 230   N  LEU G 203           
SHEET    6   U 6 ILE G 250  GLY G 251  1  O  ILE G 250   N  LEU G 231           
SHEET    1   V 5 GLY H  20  VAL H  25  0                                        
SHEET    2   V 5 MSE H   1  ASP H   6  1  N  VAL H   5   O  VAL H  25           
SHEET    3   V 5 ALA H  40  VAL H  43  1  O  MSE H  42   N  LEU H   4           
SHEET    4   V 5 PHE H  61  THR H  64  1  O  GLY H  63   N  VAL H  43           
SHEET    5   V 5 GLY H  83  SER H  85  1  O  GLY H  83   N  VAL H  62           
SHEET    1   W 6 ARG H 141  CYS H 145  0                                        
SHEET    2   W 6 THR H 118  VAL H 122  1  N  ILE H 119   O  ARG H 141           
SHEET    3   W 6 VAL H 170  PHE H 173  1  O  VAL H 170   N  GLY H 120           
SHEET    4   W 6 ALA H 201  ASN H 205  1  O  ILE H 204   N  LEU H 171           
SHEET    5   W 6 LEU H 227  LEU H 231  1  O  SER H 228   N  LEU H 203           
SHEET    6   W 6 ILE H 250  GLY H 251  1  O  ILE H 250   N  LEU H 231           
SHEET    1   X 3 ARG H 297  LEU H 300  0                                        
SHEET    2   X 3 TYR H 353  CYS H 356  1  O  MSE H 355   N  LEU H 300           
SHEET    3   X 3 ASN H 371  HIS H 374  1  O  VAL H 373   N  VAL H 354           
LINK         C   ALA A   0                 N   MSE A   1     1555   1555  1.33  
LINK         C   MSE A   1                 N   LYS A   2     1555   1555  1.34  
LINK         C   ASN A   8                 N   MSE A   9     1555   1555  1.34  
LINK         C   MSE A   9                 N   PRO A  10     1555   1555  1.34  
LINK         C   LEU A  41                 N   MSE A  42     1555   1555  1.34  
LINK         C   MSE A  42                 N   VAL A  43     1555   1555  1.32  
LINK         C   LEU A 104                 N   MSE A 105     1555   1555  1.31  
LINK         C   MSE A 105                 N   LEU A 106     1555   1555  1.33  
LINK         C   VAL A 354                 N   MSE A 355     1555   1555  1.32  
LINK         C   MSE A 355                 N   CYS A 356     1555   1555  1.33  
LINK         C   ALA B   0                 N   MSE B   1     1555   1555  1.33  
LINK         C   MSE B   1                 N   LYS B   2     1555   1555  1.33  
LINK         C   ASN B   8                 N   MSE B   9     1555   1555  1.32  
LINK         C   MSE B   9                 N   PRO B  10     1555   1555  1.34  
LINK         C   LEU B  41                 N   MSE B  42     1555   1555  1.34  
LINK         C   MSE B  42                 N   VAL B  43     1555   1555  1.33  
LINK         C   LEU B 104                 N   MSE B 105     1555   1555  1.32  
LINK         C   MSE B 105                 N   LEU B 106     1555   1555  1.33  
LINK         C   VAL B 354                 N   MSE B 355     1555   1555  1.32  
LINK         C   MSE B 355                 N   CYS B 356     1555   1555  1.33  
LINK         C   ALA C   0                 N   MSE C   1     1555   1555  1.33  
LINK         C   MSE C   1                 N   LYS C   2     1555   1555  1.33  
LINK         C   ASN C   8                 N   MSE C   9     1555   1555  1.34  
LINK         C   MSE C   9                 N   PRO C  10     1555   1555  1.35  
LINK         C   LEU C  41                 N   MSE C  42     1555   1555  1.34  
LINK         C   MSE C  42                 N   VAL C  43     1555   1555  1.33  
LINK         C   LEU C 104                 N   MSE C 105     1555   1555  1.33  
LINK         C   MSE C 105                 N   LEU C 106     1555   1555  1.33  
LINK         C   VAL C 354                 N   MSE C 355     1555   1555  1.33  
LINK         C   MSE C 355                 N   CYS C 356     1555   1555  1.33  
LINK         C   ALA D   0                 N   MSE D   1     1555   1555  1.34  
LINK         C   MSE D   1                 N   LYS D   2     1555   1555  1.33  
LINK         C   ASN D   8                 N   MSE D   9     1555   1555  1.32  
LINK         C   MSE D   9                 N   PRO D  10     1555   1555  1.34  
LINK         C   LEU D  41                 N   MSE D  42     1555   1555  1.33  
LINK         C   MSE D  42                 N   VAL D  43     1555   1555  1.33  
LINK         C   LEU D 104                 N   MSE D 105     1555   1555  1.32  
LINK         C   MSE D 105                 N   LEU D 106     1555   1555  1.32  
LINK         C   VAL D 354                 N   MSE D 355     1555   1555  1.33  
LINK         C   MSE D 355                 N   CYS D 356     1555   1555  1.34  
LINK         C   MSE E   1                 N   LYS E   2     1555   1555  1.33  
LINK         C   ASN E   8                 N   MSE E   9     1555   1555  1.32  
LINK         C   MSE E   9                 N   PRO E  10     1555   1555  1.35  
LINK         C   LEU E  41                 N   MSE E  42     1555   1555  1.33  
LINK         C   MSE E  42                 N   VAL E  43     1555   1555  1.32  
LINK         C   LEU E 104                 N   MSE E 105     1555   1555  1.33  
LINK         C   MSE E 105                 N   LEU E 106     1555   1555  1.33  
LINK         C   VAL E 354                 N   MSE E 355     1555   1555  1.31  
LINK         C   MSE E 355                 N   CYS E 356     1555   1555  1.32  
LINK         C   MSE F   1                 N   LYS F   2     1555   1555  1.33  
LINK         C   ASN F   8                 N   MSE F   9     1555   1555  1.33  
LINK         C   MSE F   9                 N   PRO F  10     1555   1555  1.35  
LINK         C   LEU F  41                 N   MSE F  42     1555   1555  1.33  
LINK         C   MSE F  42                 N   VAL F  43     1555   1555  1.33  
LINK         C   LEU F 104                 N   MSE F 105     1555   1555  1.33  
LINK         C   MSE F 105                 N   LEU F 106     1555   1555  1.33  
LINK         C   VAL F 354                 N   MSE F 355     1555   1555  1.31  
LINK         C   MSE F 355                 N   CYS F 356     1555   1555  1.33  
LINK         C   MSE G   1                 N   LYS G   2     1555   1555  1.33  
LINK         C   ASN G   8                 N   MSE G   9     1555   1555  1.33  
LINK         C   MSE G   9                 N   PRO G  10     1555   1555  1.34  
LINK         C   LEU G  41                 N   MSE G  42     1555   1555  1.33  
LINK         C   MSE G  42                 N   VAL G  43     1555   1555  1.33  
LINK         C   LEU G 104                 N   MSE G 105     1555   1555  1.33  
LINK         C   MSE G 105                 N   LEU G 106     1555   1555  1.34  
LINK         C   VAL G 354                 N   MSE G 355     1555   1555  1.33  
LINK         C   MSE G 355                 N   CYS G 356     1555   1555  1.33  
LINK         C   ALA H   0                 N   MSE H   1     1555   1555  1.33  
LINK         C   MSE H   1                 N   LYS H   2     1555   1555  1.33  
LINK         C   ASN H   8                 N   MSE H   9     1555   1555  1.32  
LINK         C   MSE H   9                 N   PRO H  10     1555   1555  1.34  
LINK         C   LEU H  41                 N   MSE H  42     1555   1555  1.34  
LINK         C   MSE H  42                 N   VAL H  43     1555   1555  1.32  
LINK         C   LEU H 104                 N   MSE H 105     1555   1555  1.33  
LINK         C   MSE H 105                 N   LEU H 106     1555   1555  1.32  
LINK         C   VAL H 354                 N   MSE H 355     1555   1555  1.32  
LINK         C   MSE H 355                 N   CYS H 356     1555   1555  1.32  
CISPEP   1 GLU A  237    PRO A  238          0        -0.89                     
CISPEP   2 GLU B  237    PRO B  238          0         0.94                     
CISPEP   3 GLU C  237    PRO C  238          0         5.87                     
CISPEP   4 GLU D  237    PRO D  238          0         3.05                     
CISPEP   5 ARG E   28    PRO E   29          0        -2.59                     
CISPEP   6 GLU E  237    PRO E  238          0         2.94                     
CISPEP   7 GLU F  237    PRO F  238          0         7.33                     
CISPEP   8 GLU G  237    PRO G  238          0         3.62                     
CISPEP   9 ARG H   28    PRO H   29          0        -5.18                     
CISPEP  10 GLU H  237    PRO H  238          0         1.99                     
SITE     1 AC1 27 ASN A  91  VAL A  95  GLY A 123  GLY A 125                    
SITE     2 AC1 27 ASN A 126  VAL A 127  CYS A 145  ASP A 146                    
SITE     3 AC1 27 PRO A 147  PRO A 148  HIS A 174  THR A 175                    
SITE     4 AC1 27 PRO A 176  TYR A 183  THR A 185  ALA A 206                    
SITE     5 AC1 27 CYS A 207  ARG A 208  ASP A 232  HIS A 254                    
SITE     6 AC1 27 ALA A 256  GLY A 257  HOH A 382  HOH A 394                    
SITE     7 AC1 27 HOH A 401  HOH A 411  HOH A 422                               
SITE     1 AC2 25 ASN B  91  VAL B  95  GLY B 123  GLY B 125                    
SITE     2 AC2 25 ASN B 126  VAL B 127  ASP B 146  PRO B 147                    
SITE     3 AC2 25 PRO B 148  HIS B 174  THR B 175  PRO B 176                    
SITE     4 AC2 25 TYR B 183  THR B 185  ALA B 206  CYS B 207                    
SITE     5 AC2 25 ARG B 208  ASP B 232  HIS B 254  ALA B 256                    
SITE     6 AC2 25 GLY B 257  HOH B 388  HOH B 403  HOH B 407                    
SITE     7 AC2 25 HOH B 555                                                     
SITE     1 AC3 27 ASN C  91  VAL C  95  GLY C 123  VAL C 124                    
SITE     2 AC3 27 GLY C 125  ASN C 126  VAL C 127  ASP C 146                    
SITE     3 AC3 27 PRO C 147  PRO C 148  HIS C 174  THR C 175                    
SITE     4 AC3 27 PRO C 176  TYR C 178  TYR C 183  THR C 185                    
SITE     5 AC3 27 ALA C 206  CYS C 207  ARG C 208  ASP C 232                    
SITE     6 AC3 27 HIS C 254  ALA C 256  GLY C 257  HOH C 380                    
SITE     7 AC3 27 HOH C 393  HOH C 402  HOH C 423                               
SITE     1 AC4 27 ASN D  91  VAL D  95  GLY D 123  GLY D 125                    
SITE     2 AC4 27 ASN D 126  VAL D 127  CYS D 145  ASP D 146                    
SITE     3 AC4 27 PRO D 147  PRO D 148  HIS D 174  THR D 175                    
SITE     4 AC4 27 PRO D 176  TYR D 178  TYR D 183  THR D 185                    
SITE     5 AC4 27 ALA D 206  CYS D 207  ARG D 208  ASP D 232                    
SITE     6 AC4 27 HIS D 254  ALA D 256  GLY D 257  HOH D 398                    
SITE     7 AC4 27 HOH D 413  HOH D 414  HOH D 519                               
SITE     1 AC5 25 ASN E  91  VAL E  95  GLY E 123  GLY E 125                    
SITE     2 AC5 25 ASN E 126  VAL E 127  ASP E 146  PRO E 147                    
SITE     3 AC5 25 PRO E 148  ARG E 149  HIS E 174  THR E 175                    
SITE     4 AC5 25 PRO E 176  TYR E 178  TYR E 183  THR E 185                    
SITE     5 AC5 25 ALA E 206  CYS E 207  ARG E 208  ASP E 232                    
SITE     6 AC5 25 HIS E 254  ALA E 256  GLY E 257  HOH E 393                    
SITE     7 AC5 25 HOH E 440                                                     
SITE     1 AC6 25 ASN F  91  VAL F  95  GLY F 123  VAL F 124                    
SITE     2 AC6 25 GLY F 125  ASN F 126  VAL F 127  CYS F 145                    
SITE     3 AC6 25 ASP F 146  PRO F 147  PRO F 148  HIS F 174                    
SITE     4 AC6 25 THR F 175  PRO F 176  TYR F 178  TYR F 183                    
SITE     5 AC6 25 THR F 185  ALA F 206  CYS F 207  ASP F 232                    
SITE     6 AC6 25 HIS F 254  GLY F 257  HOH F 383  HOH F 404                    
SITE     7 AC6 25 HOH F 412                                                     
SITE     1 AC7 26 ASN G  91  VAL G  95  GLY G 123  VAL G 124                    
SITE     2 AC7 26 GLY G 125  ASN G 126  VAL G 127  CYS G 145                    
SITE     3 AC7 26 ASP G 146  PRO G 147  PRO G 148  HIS G 174                    
SITE     4 AC7 26 THR G 175  PRO G 176  TYR G 183  THR G 185                    
SITE     5 AC7 26 ALA G 206  CYS G 207  ARG G 208  ASP G 232                    
SITE     6 AC7 26 HIS G 254  ALA G 256  GLY G 257  HOH G 386                    
SITE     7 AC7 26 HOH G 393  HOH G 399                                          
SITE     1 AC8 25 ASN H  91  VAL H  95  VAL H 122  GLY H 123                    
SITE     2 AC8 25 GLY H 125  ASN H 126  VAL H 127  CYS H 145                    
SITE     3 AC8 25 ASP H 146  PRO H 147  PRO H 148  HIS H 174                    
SITE     4 AC8 25 THR H 175  PRO H 176  TYR H 183  THR H 185                    
SITE     5 AC8 25 ALA H 206  CYS H 207  ARG H 208  ASP H 232                    
SITE     6 AC8 25 VAL H 233  HIS H 254  ALA H 256  GLY H 257                    
SITE     7 AC8 25 HOH H 383                                                     
CRYST1   93.279  167.765  103.949  90.00  93.88  90.00 P 1 21 1     16          
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      0.010721  0.000000  0.000726        0.00000                         
SCALE2      0.000000  0.005961  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009642        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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