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Database: PDB
Entry: 6G58
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HEADER    BIOSYNTHETIC PROTEIN                    29-MAR-18   6G58              
TITLE     STRUCTURE OF THE ALANINE RACEMASE FROM STAPHYLOCOCCUS AUREUS IN       
TITLE    2 COMPLEX WITH A PYRIDOXAL 5' PHOSPHATE-DERIVATIVE                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALANINE RACEMASE 1;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 5.1.1.1;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: N-TERMINAL STREP-TAG                                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 158878;                                              
SOURCE   4 STRAIN: MU50 / ATCC 700699;                                          
SOURCE   5 ATCC: 700699;                                                        
SOURCE   6 GENE: ALR1, ALR, SAV2070;                                            
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PYRIDOXAL 5 PHOSPHATE DEPENDENT, D-ALANINE BIOSYNTHESIS, BIOSYNTHETIC 
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.HOEGL,S.A.SIEBER,S.SCHNEIDER                                        
REVDAT   3   05-DEC-18 6G58    1       JRNL                                     
REVDAT   2   17-OCT-18 6G58    1       JRNL                                     
REVDAT   1   30-MAY-18 6G58    0                                                
JRNL        AUTH   A.HOEGL,M.B.NODWELL,V.C.KIRSCH,N.C.BACH,M.PFANZELT,M.STAHL,  
JRNL        AUTH 2 S.SCHNEIDER,S.A.SIEBER                                       
JRNL        TITL   MINING THE CELLULAR INVENTORY OF PYRIDOXAL                   
JRNL        TITL 2 PHOSPHATE-DEPENDENT ENZYMES WITH FUNCTIONALIZED COFACTOR     
JRNL        TITL 3 MIMICS.                                                      
JRNL        REF    NAT CHEM                      V.  10  1234 2018              
JRNL        REFN                   ESSN 1755-4349                               
JRNL        PMID   30297752                                                     
JRNL        DOI    10.1038/S41557-018-0144-2                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.40                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 90599                          
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) : 0.152                           
REMARK   3   R VALUE            (WORKING SET) : 0.151                           
REMARK   3   FREE R VALUE                     : 0.170                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4787                            
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) : 1.89                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.94                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5966                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.42                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3440                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 333                          
REMARK   3   BIN FREE R VALUE                    : 0.3490                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6020                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 145                                     
REMARK   3   SOLVENT ATOMS            : 482                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.23000                                              
REMARK   3    B22 (A**2) : 0.27000                                              
REMARK   3    B33 (A**2) : -0.50000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.095         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.089         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.074         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.279         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.975                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.969                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6368 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5993 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8656 ; 1.519 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13901 ; 0.933 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   794 ; 5.940 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   283 ;37.315 ;24.700       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1109 ;11.828 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;15.480 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   993 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7025 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1224 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3110 ; 1.732 ; 1.808       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3103 ; 1.652 ; 1.801       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3892 ; 2.451 ; 2.690       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3893 ; 2.454 ; 2.691       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3258 ; 3.234 ; 2.265       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3258 ; 3.232 ; 2.264       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4755 ; 4.906 ; 3.248       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  7105 ; 6.808 ;23.138       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  7105 ; 6.809 ;23.137       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     1    382       B     1    382   24958  0.06  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
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    52                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.7370  16.0050  31.3020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1538 T22:   0.0971                                     
REMARK   3      T33:   0.0336 T12:   0.0557                                     
REMARK   3      T13:  -0.0281 T23:  -0.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2369 L22:   1.2216                                     
REMARK   3      L33:   3.7782 L12:   0.9386                                     
REMARK   3      L13:   1.4294 L23:   1.5450                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1114 S12:   0.1761 S13:   0.1465                       
REMARK   3      S21:  -0.3103 S22:   0.0064 S23:   0.1311                       
REMARK   3      S31:  -0.3897 S32:   0.1257 S33:   0.1049                       
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    53        A   102                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.5580  10.1300  33.7700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0956 T22:   0.0989                                     
REMARK   3      T33:   0.0853 T12:   0.0677                                     
REMARK   3      T13:  -0.0525 T23:  -0.0677                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4544 L22:   2.5736                                     
REMARK   3      L33:   2.8165 L12:   0.8237                                     
REMARK   3      L13:   0.2131 L23:   0.2992                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0091 S12:   0.0219 S13:   0.0693                       
REMARK   3      S21:  -0.0013 S22:  -0.1466 S23:   0.3379                       
REMARK   3      S31:  -0.1376 S32:  -0.2915 S33:   0.1375                       
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 :   A   103        A   195                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.1620  -6.0560  27.0120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1719 T22:   0.1140                                     
REMARK   3      T33:   0.0975 T12:   0.0019                                     
REMARK   3      T13:  -0.0493 T23:  -0.0652                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7627 L22:   2.4581                                     
REMARK   3      L33:   2.6313 L12:  -0.5574                                     
REMARK   3      L13:  -0.5378 L23:   1.0407                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0423 S12:  -0.0806 S13:  -0.1798                       
REMARK   3      S21:   0.1142 S22:  -0.1079 S23:   0.3170                       
REMARK   3      S31:   0.3013 S32:  -0.2256 S33:   0.1502                       
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 :   A   196        A   255                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.0400   6.7070  27.1430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1290 T22:   0.1576                                     
REMARK   3      T33:   0.0100 T12:   0.0519                                     
REMARK   3      T13:   0.0055 T23:  -0.0283                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9043 L22:   1.5848                                     
REMARK   3      L33:   2.3910 L12:   0.9009                                     
REMARK   3      L13:   1.2659 L23:   1.3732                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0125 S12:   0.3670 S13:  -0.0937                       
REMARK   3      S21:  -0.2020 S22:   0.1258 S23:  -0.1070                       
REMARK   3      S31:  -0.0357 S32:   0.4396 S33:  -0.1383                       
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 :   A   256        A   336                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.6580  14.5400  50.4090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0487 T22:   0.2367                                     
REMARK   3      T33:   0.1057 T12:   0.0109                                     
REMARK   3      T13:  -0.0047 T23:  -0.0517                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8350 L22:   2.2233                                     
REMARK   3      L33:   3.2974 L12:  -0.1590                                     
REMARK   3      L13:   0.6917 L23:   0.0278                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0352 S12:   0.0842 S13:   0.1427                       
REMARK   3      S21:   0.0474 S22:   0.1096 S23:  -0.4444                       
REMARK   3      S31:  -0.1171 S32:   0.7598 S33:  -0.0744                       
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 :   A   337        A   353                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.5900   5.3260  38.1300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1175 T22:   0.2727                                     
REMARK   3      T33:   0.1171 T12:   0.0474                                     
REMARK   3      T13:   0.0288 T23:  -0.1287                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0954 L22:   7.2171                                     
REMARK   3      L33:   4.6399 L12:   4.9077                                     
REMARK   3      L13:   0.1993 L23:  -1.7790                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2066 S12:   0.1923 S13:  -0.3440                       
REMARK   3      S21:  -0.4662 S22:   0.1933 S23:  -0.5336                       
REMARK   3      S31:   0.3813 S32:   0.5329 S33:   0.0134                       
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 :   A   354        A   382                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.2510  19.2840  41.8140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0937 T22:   0.1277                                     
REMARK   3      T33:   0.0811 T12:   0.0008                                     
REMARK   3      T13:  -0.0421 T23:   0.0244                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1613 L22:   3.1909                                     
REMARK   3      L33:   4.2250 L12:  -0.0569                                     
REMARK   3      L13:   0.3808 L23:   1.3882                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1220 S12:   0.1762 S13:   0.1944                       
REMARK   3      S21:  -0.2193 S22:   0.0364 S23:   0.2126                       
REMARK   3      S31:  -0.4303 S32:  -0.0732 S33:   0.0856                       
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 :   B     1        B    30                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.3450   8.0300  62.9080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0909 T22:   0.0908                                     
REMARK   3      T33:   0.0867 T12:  -0.0028                                     
REMARK   3      T13:   0.0234 T23:   0.0101                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7030 L22:   0.9529                                     
REMARK   3      L33:   8.8272 L12:   1.1715                                     
REMARK   3      L13:   3.5373 L23:   2.1150                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0418 S12:  -0.2949 S13:  -0.0082                       
REMARK   3      S21:  -0.0019 S22:  -0.0877 S23:   0.1742                       
REMARK   3      S31:  -0.1348 S32:  -0.6432 S33:   0.1295                       
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 :   B    31        B    90                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.2930  20.7010  63.7220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0169 T22:   0.0605                                     
REMARK   3      T33:   0.0174 T12:   0.0140                                     
REMARK   3      T13:  -0.0000 T23:  -0.0257                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8067 L22:   1.3731                                     
REMARK   3      L33:   1.5257 L12:   0.1308                                     
REMARK   3      L13:   0.1040 L23:   0.0823                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0516 S12:  -0.0895 S13:   0.0533                       
REMARK   3      S21:   0.0661 S22:  -0.0615 S23:   0.0891                       
REMARK   3      S31:   0.0053 S32:  -0.1306 S33:   0.0099                       
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 :   B    91        B   127                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.1600  36.0810  60.7570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1011 T22:   0.0373                                     
REMARK   3      T33:   0.1003 T12:   0.0094                                     
REMARK   3      T13:  -0.0411 T23:  -0.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8033 L22:   3.2197                                     
REMARK   3      L33:   3.5119 L12:  -0.2470                                     
REMARK   3      L13:   0.3837 L23:  -0.9652                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1268 S12:   0.0591 S13:   0.7637                       
REMARK   3      S21:  -0.1301 S22:  -0.0085 S23:   0.0172                       
REMARK   3      S31:  -0.4076 S32:   0.0165 S33:   0.1353                       
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 :   B   128        B   220                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.5200  22.2460  72.5850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0438 T22:   0.0976                                     
REMARK   3      T33:   0.0149 T12:   0.0123                                     
REMARK   3      T13:  -0.0170 T23:  -0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5144 L22:   2.8403                                     
REMARK   3      L33:   1.2524 L12:   0.3737                                     
REMARK   3      L13:   0.2009 L23:  -0.4401                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0095 S12:  -0.1494 S13:   0.0479                       
REMARK   3      S21:   0.1570 S22:  -0.0716 S23:  -0.1060                       
REMARK   3      S31:   0.0407 S32:   0.1046 S33:   0.0621                       
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 :   B   221        B   336                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.1800  -7.7110  51.2990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2330 T22:   0.0454                                     
REMARK   3      T33:   0.1469 T12:  -0.0267                                     
REMARK   3      T13:  -0.0481 T23:  -0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4358 L22:   1.1089                                     
REMARK   3      L33:   2.9145 L12:  -0.1331                                     
REMARK   3      L13:   0.7093 L23:   0.3202                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2028 S12:   0.0306 S13:  -0.3644                       
REMARK   3      S21:   0.0081 S22:  -0.1135 S23:   0.1879                       
REMARK   3      S31:   0.7148 S32:  -0.2037 S33:  -0.0893                       
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 :   B   337        B   352                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.1370  -5.1850  57.5830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1855 T22:   0.0643                                     
REMARK   3      T33:   0.1211 T12:   0.0444                                     
REMARK   3      T13:  -0.0873 T23:   0.0160                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6943 L22:   6.2997                                     
REMARK   3      L33:   4.4881 L12:   4.0996                                     
REMARK   3      L13:  -0.5945 L23:   0.6346                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2282 S12:  -0.2812 S13:  -0.5332                       
REMARK   3      S21:   0.1173 S22:  -0.2057 S23:  -0.1438                       
REMARK   3      S31:   0.5258 S32:   0.3175 S33:  -0.0225                       
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 :   B   353        B   382                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.7160   8.4010  54.1160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1126 T22:   0.0768                                     
REMARK   3      T33:   0.0982 T12:  -0.0112                                     
REMARK   3      T13:   0.0102 T23:  -0.0364                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9335 L22:   1.0251                                     
REMARK   3      L33:   2.6392 L12:  -1.5921                                     
REMARK   3      L13:   1.3702 L23:   0.2189                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0131 S12:  -0.0885 S13:  -0.0559                       
REMARK   3      S21:   0.0138 S22:  -0.0922 S23:   0.1513                       
REMARK   3      S31:  -0.0284 S32:  -0.2647 S33:   0.0792                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.10                                          
REMARK   3   ION PROBE RADIUS   : 0.70                                          
REMARK   3   SHRINKAGE RADIUS   : 0.70                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6G58 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-APR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009440.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-SEP-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 95389                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.96                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4A3Q                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE PH 4, 10 %(V/V)     
REMARK 280  MPD, VAPOR DIFFUSION, TEMPERATURE 277K                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       42.77150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.41750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       53.38350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.41750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.77150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       53.38350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11560 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 27170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -183.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -21                                                      
REMARK 465     ALA A   -20                                                      
REMARK 465     SER A   -19                                                      
REMARK 465     TRP A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     PRO A   -15                                                      
REMARK 465     GLN A   -14                                                      
REMARK 465     PHE A   -13                                                      
REMARK 465     GLU A   -12                                                      
REMARK 465     LYS A   -11                                                      
REMARK 465     GLY A   -10                                                      
REMARK 465     ALA A    -9                                                      
REMARK 465     VAL A    -8                                                      
REMARK 465     THR A    -7                                                      
REMARK 465     SER A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     TYR A    -4                                                      
REMARK 465     LYS A    -3                                                      
REMARK 465     LYS A    -2                                                      
REMARK 465     ALA A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     MET B   -21                                                      
REMARK 465     ALA B   -20                                                      
REMARK 465     SER B   -19                                                      
REMARK 465     TRP B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     PRO B   -15                                                      
REMARK 465     GLN B   -14                                                      
REMARK 465     PHE B   -13                                                      
REMARK 465     GLU B   -12                                                      
REMARK 465     LYS B   -11                                                      
REMARK 465     GLY B   -10                                                      
REMARK 465     ALA B    -9                                                      
REMARK 465     VAL B    -8                                                      
REMARK 465     THR B    -7                                                      
REMARK 465     SER B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     TYR B    -4                                                      
REMARK 465     LYS B    -3                                                      
REMARK 465     LYS B    -2                                                      
REMARK 465     ALA B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LYS A  39   CD  -  CE  -  NZ  ANGL. DEV. = -15.7 DEGREES          
REMARK 500    ARG A 100   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 100   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    LYS B  39   CD  -  CE  -  NZ  ANGL. DEV. = -16.1 DEGREES          
REMARK 500    ARG B 100   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG B 100   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG B 309   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 138     -145.01    -98.15                                   
REMARK 500    CYS A 201      -10.89   -140.63                                   
REMARK 500    SER A 264     -176.53     72.32                                   
REMARK 500    ASN A 334       43.68    -89.01                                   
REMARK 500    ARG B 138     -143.46    -99.53                                   
REMARK 500    SER B 264     -178.08     72.72                                   
REMARK 500    ASN B 334       44.44    -89.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 741        DISTANCE =  5.95 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 403  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE A 154   O                                                      
REMARK 620 2 TYR A 157   O    80.7                                              
REMARK 620 3 LEU A 160   O   107.7  87.2                                        
REMARK 620 4 HOH A 629   O    96.5  80.9 150.9                                  
REMARK 620 5 HOH A 709   O    94.9 173.4  98.8  94.9                            
REMARK 620 6 HOH A 607   O   173.5  92.9  70.4  83.7  91.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 404  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 284   OH                                                     
REMARK 620 2 HOH A 554   O   106.0                                              
REMARK 620 3 ACT A 408   O    79.3 119.5                                        
REMARK 620 4 HOH A 726   O   122.9 111.8 114.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 359   O                                                      
REMARK 620 2 HOH A 676   O    77.6                                              
REMARK 620 3 HOH B 502   O   110.5  55.0                                        
REMARK 620 4 HOH B 629   O    96.1 111.9  65.6                                  
REMARK 620 5 HOH B 680   O   132.7  67.2  74.0 125.3                            
REMARK 620 6 HOH B 706   O   104.6 141.3 144.5 106.3  86.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE B 154   O                                                      
REMARK 620 2 TYR B 157   O    80.7                                              
REMARK 620 3 LEU B 160   O   104.3  88.9                                        
REMARK 620 4 HOH B 566   O   175.1  97.0  71.3                                  
REMARK 620 5 HOH B 711   O    92.6 171.8  97.4  90.1                            
REMARK 620 6 HOH B 610   O    95.7  82.6 156.6  88.2  93.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 404  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN B 213   O                                                      
REMARK 620 2 CYS B 215   O    83.8                                              
REMARK 620 3 HOH B 697   O   103.1 106.0                                        
REMARK 620 4 HOH B 569   O   160.4 101.5  93.7                                  
REMARK 620 5 HOH B 698   O    71.8  80.7 171.2  90.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 403  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR B 284   OH                                                     
REMARK 620 2 HOH B 726   O   119.7                                              
REMARK 620 3 ACT B 412   OXT  80.6 112.5                                        
REMARK 620 4 HOH B 585   O   108.0 110.2 123.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EOW A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MRD B 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide EOW B 401 and LYS B    
REMARK 800  39                                                                  
DBREF  6G58 A    2   382  UNP    P63479   ALR1_STAAM       2    382             
DBREF  6G58 B    2   382  UNP    P63479   ALR1_STAAM       2    382             
SEQADV 6G58 MET A  -21  UNP  P63479              INITIATING METHIONINE          
SEQADV 6G58 ALA A  -20  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 SER A  -19  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 TRP A  -18  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 SER A  -17  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 HIS A  -16  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 PRO A  -15  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 GLN A  -14  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 PHE A  -13  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 GLU A  -12  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 LYS A  -11  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 GLY A  -10  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 ALA A   -9  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 VAL A   -8  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 THR A   -7  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 SER A   -6  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 LEU A   -5  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 TYR A   -4  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 LYS A   -3  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 LYS A   -2  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 ALA A   -1  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 GLY A    0  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 PHE A    1  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 MET B  -21  UNP  P63479              INITIATING METHIONINE          
SEQADV 6G58 ALA B  -20  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 SER B  -19  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 TRP B  -18  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 SER B  -17  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 HIS B  -16  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 PRO B  -15  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 GLN B  -14  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 PHE B  -13  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 GLU B  -12  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 LYS B  -11  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 GLY B  -10  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 ALA B   -9  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 VAL B   -8  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 THR B   -7  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 SER B   -6  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 LEU B   -5  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 TYR B   -4  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 LYS B   -3  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 LYS B   -2  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 ALA B   -1  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 GLY B    0  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G58 PHE B    1  UNP  P63479              EXPRESSION TAG                 
SEQRES   1 A  404  MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA          
SEQRES   2 A  404  VAL THR SER LEU TYR LYS LYS ALA GLY PHE SER ASP LYS          
SEQRES   3 A  404  TYR TYR ARG SER ALA TYR MET ASN VAL ASP LEU ASN ALA          
SEQRES   4 A  404  VAL ALA SER ASN PHE LYS VAL PHE SER THR LEU HIS PRO          
SEQRES   5 A  404  ASN LYS THR VAL MET ALA VAL VAL LYS ALA ASN ALA TYR          
SEQRES   6 A  404  GLY LEU GLY SER VAL LYS VAL ALA ARG HIS LEU MET GLU          
SEQRES   7 A  404  ASN GLY ALA THR PHE PHE ALA VAL ALA THR LEU ASP GLU          
SEQRES   8 A  404  ALA ILE GLU LEU ARG MET HIS GLY ILE THR ALA LYS ILE          
SEQRES   9 A  404  LEU VAL LEU GLY VAL LEU PRO ALA LYS ASP ILE ASP LYS          
SEQRES  10 A  404  ALA ILE GLN HIS ARG VAL ALA LEU THR VAL PRO SER LYS          
SEQRES  11 A  404  GLN TRP LEU LYS GLU ALA ILE LYS ASN ILE SER GLY GLU          
SEQRES  12 A  404  GLN GLU LYS LYS LEU TRP LEU HIS ILE LYS LEU ASP THR          
SEQRES  13 A  404  GLY MET GLY ARG LEU GLY ILE LYS ASP THR ASN THR TYR          
SEQRES  14 A  404  GLN GLU VAL ILE GLU ILE ILE GLN GLN TYR GLU GLN LEU          
SEQRES  15 A  404  VAL PHE GLU GLY VAL PHE THR HIS PHE ALA CYS ALA ASP          
SEQRES  16 A  404  GLU PRO GLY ASP MET THR THR GLU GLN TYR GLN ARG PHE          
SEQRES  17 A  404  LYS ASP MET VAL ASN GLU ALA ILE LYS PRO GLU TYR ILE          
SEQRES  18 A  404  HIS CYS GLN ASN SER ALA GLY SER LEU LEU MET ASP CYS          
SEQRES  19 A  404  GLN PHE CYS ASN ALA ILE ARG PRO GLY ILE SER LEU TYR          
SEQRES  20 A  404  GLY TYR TYR PRO SER GLU TYR VAL GLN GLN LYS VAL LYS          
SEQRES  21 A  404  VAL HIS LEU LYS PRO SER VAL GLN LEU ILE ALA ASN VAL          
SEQRES  22 A  404  VAL GLN THR LYS THR LEU GLN ALA GLY GLU SER VAL SER          
SEQRES  23 A  404  TYR GLY ALA THR TYR THR ALA THR ASP PRO THR THR ILE          
SEQRES  24 A  404  ALA LEU LEU PRO ILE GLY TYR ALA ASP GLY TYR LEU ARG          
SEQRES  25 A  404  ILE MET GLN GLY SER PHE VAL ASN VAL ASN GLY HIS GLN          
SEQRES  26 A  404  CYS GLU VAL ILE GLY ARG VAL CYS MET ASP GLN THR ILE          
SEQRES  27 A  404  VAL LYS VAL PRO ASP GLN VAL LYS ALA GLY ASP SER VAL          
SEQRES  28 A  404  ILE LEU ILE ASP ASN HIS ARG GLU SER PRO GLN SER VAL          
SEQRES  29 A  404  GLU VAL VAL ALA GLU LYS GLN HIS THR ILE ASN TYR GLU          
SEQRES  30 A  404  VAL LEU CYS ASN LEU SER ARG ARG LEU PRO ARG ILE TYR          
SEQRES  31 A  404  HIS ASP GLY ASP GLN ARG PHE VAL THR ASN GLU LEU LEU          
SEQRES  32 A  404  LYS                                                          
SEQRES   1 B  404  MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA          
SEQRES   2 B  404  VAL THR SER LEU TYR LYS LYS ALA GLY PHE SER ASP LYS          
SEQRES   3 B  404  TYR TYR ARG SER ALA TYR MET ASN VAL ASP LEU ASN ALA          
SEQRES   4 B  404  VAL ALA SER ASN PHE LYS VAL PHE SER THR LEU HIS PRO          
SEQRES   5 B  404  ASN LYS THR VAL MET ALA VAL VAL LYS ALA ASN ALA TYR          
SEQRES   6 B  404  GLY LEU GLY SER VAL LYS VAL ALA ARG HIS LEU MET GLU          
SEQRES   7 B  404  ASN GLY ALA THR PHE PHE ALA VAL ALA THR LEU ASP GLU          
SEQRES   8 B  404  ALA ILE GLU LEU ARG MET HIS GLY ILE THR ALA LYS ILE          
SEQRES   9 B  404  LEU VAL LEU GLY VAL LEU PRO ALA LYS ASP ILE ASP LYS          
SEQRES  10 B  404  ALA ILE GLN HIS ARG VAL ALA LEU THR VAL PRO SER LYS          
SEQRES  11 B  404  GLN TRP LEU LYS GLU ALA ILE LYS ASN ILE SER GLY GLU          
SEQRES  12 B  404  GLN GLU LYS LYS LEU TRP LEU HIS ILE LYS LEU ASP THR          
SEQRES  13 B  404  GLY MET GLY ARG LEU GLY ILE LYS ASP THR ASN THR TYR          
SEQRES  14 B  404  GLN GLU VAL ILE GLU ILE ILE GLN GLN TYR GLU GLN LEU          
SEQRES  15 B  404  VAL PHE GLU GLY VAL PHE THR HIS PHE ALA CYS ALA ASP          
SEQRES  16 B  404  GLU PRO GLY ASP MET THR THR GLU GLN TYR GLN ARG PHE          
SEQRES  17 B  404  LYS ASP MET VAL ASN GLU ALA ILE LYS PRO GLU TYR ILE          
SEQRES  18 B  404  HIS CYS GLN ASN SER ALA GLY SER LEU LEU MET ASP CYS          
SEQRES  19 B  404  GLN PHE CYS ASN ALA ILE ARG PRO GLY ILE SER LEU TYR          
SEQRES  20 B  404  GLY TYR TYR PRO SER GLU TYR VAL GLN GLN LYS VAL LYS          
SEQRES  21 B  404  VAL HIS LEU LYS PRO SER VAL GLN LEU ILE ALA ASN VAL          
SEQRES  22 B  404  VAL GLN THR LYS THR LEU GLN ALA GLY GLU SER VAL SER          
SEQRES  23 B  404  TYR GLY ALA THR TYR THR ALA THR ASP PRO THR THR ILE          
SEQRES  24 B  404  ALA LEU LEU PRO ILE GLY TYR ALA ASP GLY TYR LEU ARG          
SEQRES  25 B  404  ILE MET GLN GLY SER PHE VAL ASN VAL ASN GLY HIS GLN          
SEQRES  26 B  404  CYS GLU VAL ILE GLY ARG VAL CYS MET ASP GLN THR ILE          
SEQRES  27 B  404  VAL LYS VAL PRO ASP GLN VAL LYS ALA GLY ASP SER VAL          
SEQRES  28 B  404  ILE LEU ILE ASP ASN HIS ARG GLU SER PRO GLN SER VAL          
SEQRES  29 B  404  GLU VAL VAL ALA GLU LYS GLN HIS THR ILE ASN TYR GLU          
SEQRES  30 B  404  VAL LEU CYS ASN LEU SER ARG ARG LEU PRO ARG ILE TYR          
SEQRES  31 B  404  HIS ASP GLY ASP GLN ARG PHE VAL THR ASN GLU LEU LEU          
SEQRES  32 B  404  LYS                                                          
HET    EOW  A 401      18                                                       
HET     NA  A 402       1                                                       
HET     NA  A 403       1                                                       
HET     NA  A 404       1                                                       
HET    MPD  A 405       8                                                       
HET    MPD  A 406       8                                                       
HET    MPD  A 407       8                                                       
HET    ACT  A 408       4                                                       
HET    ACT  A 409       4                                                       
HET    ACT  A 410       4                                                       
HET    ACT  A 411       4                                                       
HET    ACT  A 412       4                                                       
HET    EOW  B 401      18                                                       
HET     NA  B 402       1                                                       
HET     NA  B 403       1                                                       
HET     NA  B 404       1                                                       
HET     CL  B 405       1                                                       
HET    MPD  B 406       8                                                       
HET    MPD  B 407       8                                                       
HET    MPD  B 408       8                                                       
HET    MPD  B 409       8                                                       
HET    MPD  B 410       8                                                       
HET    MRD  B 411       8                                                       
HET    ACT  B 412       4                                                       
HET    GOL  B 413       6                                                       
HETNAM     EOW (6-BUT-3-YNYL-4-METHYL-5-OXIDANYL-PYRIDIN-3-YL)METHYL            
HETNAM   2 EOW  DIHYDROGEN PHOSPHATE                                            
HETNAM      NA SODIUM ION                                                       
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETNAM     ACT ACETATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     MRD (4R)-2-METHYLPENTANE-2,4-DIOL                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  EOW    2(C11 H14 N O5 P)                                            
FORMUL   4   NA    6(NA 1+)                                                     
FORMUL   7  MPD    8(C6 H14 O2)                                                 
FORMUL  10  ACT    6(C2 H3 O2 1-)                                               
FORMUL  19   CL    CL 1-                                                        
FORMUL  25  MRD    C6 H14 O2                                                    
FORMUL  27  GOL    C3 H8 O3                                                     
FORMUL  28  HOH   *482(H2 O)                                                    
HELIX    1 AA1 LEU A   15  HIS A   29  1                                  15    
HELIX    2 AA2 VAL A   38  GLY A   44  1                                   7    
HELIX    3 AA3 GLY A   46  ASN A   57  1                                  12    
HELIX    4 AA4 THR A   66  HIS A   76  1                                  11    
HELIX    5 AA5 PRO A   89  LYS A   91  5                                   3    
HELIX    6 AA6 ASP A   92  HIS A   99  1                                   8    
HELIX    7 AA7 SER A  107  ASN A  117  1                                  11    
HELIX    8 AA8 ASP A  143  GLN A  156  1                                  14    
HELIX    9 AA9 ASP A  177  ASN A  191  1                                  15    
HELIX   10 AB1 ASN A  203  MET A  210  1                                   8    
HELIX   11 AB2 GLY A  221  GLY A  226  5                                   6    
HELIX   12 AB3 SER A  230  VAL A  237  1                                   8    
HELIX   13 AB4 SER A  264  THR A  268  5                                   5    
HELIX   14 AB5 GLY A  283  GLY A  287  5                                   5    
HELIX   15 AB6 LEU A  289  GLN A  293  5                                   5    
HELIX   16 AB7 SER A  341  GLN A  349  1                                   9    
HELIX   17 AB8 ILE A  352  ASN A  359  1                                   8    
HELIX   18 AB9 ASN A  378  LYS A  382  5                                   5    
HELIX   19 AC1 LEU B   15  HIS B   29  1                                  15    
HELIX   20 AC2 VAL B   38  GLY B   44  1                                   7    
HELIX   21 AC3 GLY B   46  ASN B   57  1                                  12    
HELIX   22 AC4 THR B   66  HIS B   76  1                                  11    
HELIX   23 AC5 PRO B   89  LYS B   91  5                                   3    
HELIX   24 AC6 ASP B   92  HIS B   99  1                                   8    
HELIX   25 AC7 SER B  107  ASN B  117  1                                  11    
HELIX   26 AC8 ASP B  143  GLN B  156  1                                  14    
HELIX   27 AC9 ASP B  177  ASN B  191  1                                  15    
HELIX   28 AD1 ASN B  203  MET B  210  1                                   8    
HELIX   29 AD2 GLY B  221  GLY B  226  5                                   6    
HELIX   30 AD3 SER B  230  VAL B  237  1                                   8    
HELIX   31 AD4 SER B  264  THR B  268  5                                   5    
HELIX   32 AD5 GLY B  283  GLY B  287  5                                   5    
HELIX   33 AD6 LEU B  289  GLN B  293  5                                   5    
HELIX   34 AD7 SER B  341  GLN B  349  1                                   9    
HELIX   35 AD8 ILE B  352  ASN B  359  1                                   8    
HELIX   36 AD9 ASN B  378  LYS B  382  5                                   5    
SHEET    1 AA1 7 HIS A 302  GLU A 305  0                                        
SHEET    2 AA1 7 PHE A 296  VAL A 299 -1  N  VAL A 297   O  CYS A 304           
SHEET    3 AA1 7 SER A 328  ILE A 332 -1  O  ILE A 330   N  ASN A 298           
SHEET    4 AA1 7 VAL A 245  ASN A 250 -1  N  LEU A 247   O  LEU A 331           
SHEET    5 AA1 7 ALA A   9  ASP A  14 -1  N  TYR A  10   O  ILE A 248           
SHEET    6 AA1 7 ARG A 366  ASP A 370  1  O  ILE A 367   N  MET A  11           
SHEET    7 AA1 7 GLN A 373  THR A 377 -1  O  PHE A 375   N  TYR A 368           
SHEET    1 AA2 2 THR A  33  VAL A  34  0                                        
SHEET    2 AA2 2 ALA A 217  ILE A 218  1  O  ILE A 218   N  THR A  33           
SHEET    1 AA3 7 ALA A  36  VAL A  37  0                                        
SHEET    2 AA3 7 PHE A  61  VAL A  64  1  O  ALA A  63   N  ALA A  36           
SHEET    3 AA3 7 LYS A  81  VAL A  84  1  O  LEU A  83   N  VAL A  64           
SHEET    4 AA3 7 ALA A 102  VAL A 105  1  O  ALA A 102   N  ILE A  82           
SHEET    5 AA3 7 LEU A 126  LYS A 131  1  O  HIS A 129   N  LEU A 103           
SHEET    6 AA3 7 LEU A 160  PHE A 166  1  O  VAL A 161   N  LEU A 126           
SHEET    7 AA3 7 TYR A 198  HIS A 200  1  O  TYR A 198   N  GLU A 163           
SHEET    1 AA4 3 GLN A 253  LEU A 257  0                                        
SHEET    2 AA4 3 THR A 275  LEU A 280 -1  O  ILE A 277   N  LYS A 255           
SHEET    3 AA4 3 THR A 315  LYS A 318 -1  O  VAL A 317   N  ALA A 278           
SHEET    1 AA5 2 SER A 262  VAL A 263  0                                        
SHEET    2 AA5 2 TYR A 269  THR A 270 -1  O  TYR A 269   N  VAL A 263           
SHEET    1 AA6 7 HIS B 302  GLU B 305  0                                        
SHEET    2 AA6 7 PHE B 296  VAL B 299 -1  N  VAL B 297   O  CYS B 304           
SHEET    3 AA6 7 SER B 328  ILE B 332 -1  O  ILE B 330   N  ASN B 298           
SHEET    4 AA6 7 VAL B 245  ASN B 250 -1  N  LEU B 247   O  LEU B 331           
SHEET    5 AA6 7 ALA B   9  ASP B  14 -1  N  TYR B  10   O  ILE B 248           
SHEET    6 AA6 7 ARG B 366  ASP B 370  1  O  ILE B 367   N  MET B  11           
SHEET    7 AA6 7 GLN B 373  THR B 377 -1  O  PHE B 375   N  TYR B 368           
SHEET    1 AA7 2 THR B  33  VAL B  34  0                                        
SHEET    2 AA7 2 ALA B 217  ILE B 218  1  O  ILE B 218   N  THR B  33           
SHEET    1 AA8 7 ALA B  36  VAL B  37  0                                        
SHEET    2 AA8 7 PHE B  61  VAL B  64  1  O  ALA B  63   N  ALA B  36           
SHEET    3 AA8 7 LYS B  81  VAL B  84  1  O  LEU B  83   N  VAL B  64           
SHEET    4 AA8 7 ALA B 102  VAL B 105  1  O  ALA B 102   N  ILE B  82           
SHEET    5 AA8 7 LEU B 126  LYS B 131  1  O  HIS B 129   N  LEU B 103           
SHEET    6 AA8 7 LEU B 160  PHE B 166  1  O  VAL B 161   N  LEU B 126           
SHEET    7 AA8 7 TYR B 198  HIS B 200  1  O  TYR B 198   N  GLU B 163           
SHEET    1 AA9 3 GLN B 253  LEU B 257  0                                        
SHEET    2 AA9 3 THR B 275  LEU B 280 -1  O  ILE B 277   N  LYS B 255           
SHEET    3 AA9 3 THR B 315  VAL B 319 -1  O  VAL B 317   N  ALA B 278           
SHEET    1 AB1 2 SER B 262  VAL B 263  0                                        
SHEET    2 AB1 2 TYR B 269  THR B 270 -1  O  TYR B 269   N  VAL B 263           
LINK         NZ  LYS A  39                 C4A EOW A 401     1555   1555  1.28  
LINK         O   ILE A 154                NA    NA A 403     1555   1555  2.40  
LINK         O   TYR A 157                NA    NA A 403     1555   1555  2.45  
LINK         O   LEU A 160                NA    NA A 403     1555   1555  2.33  
LINK         OH  TYR A 284                NA    NA A 404     1555   1555  2.85  
LINK         O   ASN A 359                NA    NA A 402     1555   1555  2.52  
LINK         NZ  LYS B  39                 C4A EOW B 401     1555   1555  1.28  
LINK         O   ILE B 154                NA    NA B 402     1555   1555  2.45  
LINK         O   TYR B 157                NA    NA B 402     1555   1555  2.35  
LINK         O   LEU B 160                NA    NA B 402     1555   1555  2.37  
LINK         O   GLN B 213                NA    NA B 404     1555   1555  2.65  
LINK         O   CYS B 215                NA    NA B 404     1555   1555  2.48  
LINK         OH  TYR B 284                NA    NA B 403     1555   1555  2.72  
LINK        NA    NA A 402                 O   HOH A 676     1555   1555  3.13  
LINK        NA    NA A 402                 O   HOH B 502     1555   1555  2.45  
LINK        NA    NA A 402                 O   HOH B 629     1555   1555  2.71  
LINK        NA    NA A 402                 O   HOH B 680     1555   1555  2.61  
LINK        NA    NA A 402                 O   HOH B 706     1555   1555  2.15  
LINK        NA    NA A 403                 O   HOH A 629     1555   1555  2.56  
LINK        NA    NA A 403                 O   HOH A 709     1555   1555  2.32  
LINK        NA    NA A 403                 O   HOH A 607     1555   1555  2.58  
LINK        NA    NA A 404                 O   HOH A 554     1555   1555  2.90  
LINK        NA    NA A 404                 O   ACT A 408     1555   1555  2.54  
LINK        NA    NA A 404                 O   HOH A 726     1555   1555  2.44  
LINK        NA    NA B 402                 O   HOH B 566     1555   1555  2.65  
LINK        NA    NA B 402                 O   HOH B 711     1555   1555  2.34  
LINK        NA    NA B 402                 O   HOH B 610     1555   1555  2.45  
LINK        NA    NA B 403                 O   HOH B 726     1555   1555  2.54  
LINK        NA    NA B 403                 OXT ACT B 412     1555   1555  2.51  
LINK        NA    NA B 403                 O   HOH B 585     1555   1555  2.82  
LINK        NA    NA B 404                 O   HOH B 697     1555   1555  2.32  
LINK        NA    NA B 404                 O   HOH B 569     1555   1555  2.33  
LINK        NA    NA B 404                 O   HOH B 698     1555   1555  2.73  
SITE     1 AC1 16 LYS A  39  TYR A  43  LEU A  85  LYS A 131                    
SITE     2 AC1 16 ARG A 138  HIS A 168  ASN A 203  SER A 204                    
SITE     3 AC1 16 ARG A 219  GLY A 221  ILE A 222  TYR A 354                    
SITE     4 AC1 16 HOH A 587  HOH A 663  ACT B 412  HOH B 559                    
SITE     1 AC2  5 ASN A 359  HOH B 502  HOH B 629  HOH B 680                    
SITE     2 AC2  5 HOH B 706                                                     
SITE     1 AC3  6 ILE A 154  TYR A 157  LEU A 160  HOH A 607                    
SITE     2 AC3  6 HOH A 629  HOH A 709                                          
SITE     1 AC4  4 TYR A 284  ACT A 408  HOH A 554  HOH A 726                    
SITE     1 AC5  4 ARG A 290  ARG A 309  HOH A 544  HOH A 680                    
SITE     1 AC6  4 LEU A 209  MET A 210  HOH A 550  HOH A 667                    
SITE     1 AC7  2 THR A  79  ARG A 100                                          
SITE     1 AC8  9 TYR A 265  TYR A 284  CYS A 311  MET A 312                    
SITE     2 AC8  9  NA A 404  HOH A 537  HOH A 553  LYS B  39                    
SITE     3 AC8  9 EOW B 401                                                     
SITE     1 AC9  4 SER A   8  VAL A 251  GLY A 326  PRO B  89                    
SITE     1 AD1  4 ASN A  31  LYS A  32  GLN A 213  CYS A 215                    
SITE     1 AD2  3 LYS A 236  SER B 207  MET B 210                               
SITE     1 AD3  5 TYR A   5  TYR A  10  ILE A 367  ARG A 374                    
SITE     2 AD3  5 HOH A 604                                                     
SITE     1 AD4  6 ILE B 154  TYR B 157  LEU B 160  HOH B 566                    
SITE     2 AD4  6 HOH B 610  HOH B 711                                          
SITE     1 AD5  5 TYR B 265  TYR B 284  ACT B 412  HOH B 585                    
SITE     2 AD5  5 HOH B 726                                                     
SITE     1 AD6  5 GLN B 213  CYS B 215  HOH B 569  HOH B 697                    
SITE     2 AD6  5 HOH B 698                                                     
SITE     1 AD7  3 LYS B 131  MET B 136  ARG B 138                               
SITE     1 AD8  2 ARG B 290  HOH B 541                                          
SITE     1 AD9  5 TYR A   5  TYR A   6  SER A   8  LYS B  91                    
SITE     2 AD9  5 ASP B  92                                                     
SITE     1 AE1  4 GLN A 258  ARG B  74  THR B  79  ARG B 100                    
SITE     1 AE2  2 PRO B  30  ASN B  31                                          
SITE     1 AE3  4 GLU B  56  GLY B  77  THR B  79  HOH B 555                    
SITE     1 AE4  3 ILE B 118  GLN B 159  HOH B 554                               
SITE     1 AE5  9 LYS A  39  EOW A 401  TYR B 265  TYR B 284                    
SITE     2 AE5  9 CYS B 311  MET B 312   NA B 403  HOH B 516                    
SITE     3 AE5  9 HOH B 559                                                     
SITE     1 AE6  9 VAL A 252  PRO A 281  GLN A 314  GLY B  86                    
SITE     2 AE6  9 VAL B  87  HOH B 525  HOH B 535  HOH B 573                    
SITE     3 AE6  9 HOH B 686                                                     
SITE     1 AE7 25 MET A 312  ASP A 313  ACT A 408  HOH A 553                    
SITE     2 AE7 25 HOH A 658  VAL B  37  VAL B  38  ALA B  40                    
SITE     3 AE7 25 ASN B  41  ALA B  42  TYR B  43  ALA B  63                    
SITE     4 AE7 25 ALA B  65  GLU B  69  LEU B  85  LYS B 131                    
SITE     5 AE7 25 ARG B 138  HIS B 168  ASN B 203  SER B 204                    
SITE     6 AE7 25 ARG B 219  GLY B 221  ILE B 222  TYR B 354                    
SITE     7 AE7 25 HOH B 579                                                     
CRYST1   85.543  106.767  130.835  90.00  90.00  90.00 P 21 21 21    8          
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      0.011690  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009366  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007643        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system