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Database: PDB
Entry: 6G56
LinkDB: 6G56
Original site: 6G56 
HEADER    BIOSYNTHETIC PROTEIN                    29-MAR-18   6G56              
TITLE     APO-STRUCTURE OF THE ALANINE RACEMASE FROM STAPHYLOCOCCUS AUREUS      
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 (STRAIN MU50 / ATCC       
SOURCE   3 700699);                                                             
SOURCE   4 ORGANISM_TAXID: 158878;                                              
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 6G56    1       JRNL                                     
REVDAT   2   17-OCT-18 6G56    1       JRNL                                     
REVDAT   1   30-MAY-18 6G56    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.    2.15 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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 84.78                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 48216                          
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) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2538                            
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) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3359                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.59                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5310                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 177                          
REMARK   3   BIN FREE R VALUE                    : 0.5220                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6000                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 138                                     
REMARK   3   SOLVENT ATOMS            : 297                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.60000                                             
REMARK   3    B22 (A**2) : 1.12000                                              
REMARK   3    B33 (A**2) : -0.52000                                             
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): 0.257         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.205         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.154         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.272        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6273 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5774 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8526 ; 1.428 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13426 ; 0.940 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   777 ; 6.392 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   279 ;35.492 ;24.910       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1091 ;12.904 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;17.648 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   988 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6857 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1183 ; 0.001 ; 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):  3072 ; 2.161 ; 1.372       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3071 ; 2.160 ; 1.372       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3843 ; 3.271 ; 2.048       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3844 ; 3.271 ; 2.049       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3201 ; 4.241 ; 1.751       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3201 ; 4.235 ; 1.751       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4678 ; 5.704 ; 2.511       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6818 ; 7.793 ;17.009       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  6818 ; 7.787 ;17.009       
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     2    381       B     2    381   24086  0.09  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     2        A    52                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.6530 -15.3560 -46.1950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1880 T22:   0.0693                                     
REMARK   3      T33:   0.0637 T12:   0.0014                                     
REMARK   3      T13:  -0.0039 T23:  -0.0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1362 L22:   0.3423                                     
REMARK   3      L33:   3.3664 L12:  -0.0656                                     
REMARK   3      L13:  -0.2046 L23:   0.9075                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0270 S12:   0.0713 S13:   0.0618                       
REMARK   3      S21:  -0.0371 S22:   0.0973 S23:  -0.0906                       
REMARK   3      S31:  -0.0728 S32:   0.2821 S33:  -0.0703                       
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):   2.1990  -5.9860 -54.7240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1931 T22:   0.0283                                     
REMARK   3      T33:   0.0327 T12:  -0.0065                                     
REMARK   3      T13:  -0.0055 T23:   0.0069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8471 L22:   1.8027                                     
REMARK   3      L33:   1.9240 L12:   0.2805                                     
REMARK   3      L13:   0.1397 L23:   0.3426                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0040 S12:  -0.0360 S13:   0.2352                       
REMARK   3      S21:  -0.0820 S22:  -0.0799 S23:  -0.1033                       
REMARK   3      S31:  -0.1614 S32:   0.0918 S33:   0.0759                       
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): -10.2730 -16.1850 -62.2290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1624 T22:   0.1174                                     
REMARK   3      T33:   0.0135 T12:  -0.0085                                     
REMARK   3      T13:  -0.0045 T23:  -0.0296                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7448 L22:   4.1760                                     
REMARK   3      L33:   2.2477 L12:  -0.9195                                     
REMARK   3      L13:   0.7766 L23:  -0.2648                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0580 S12:  -0.0096 S13:   0.0249                       
REMARK   3      S21:   0.0211 S22:   0.0288 S23:   0.1313                       
REMARK   3      S31:  -0.0973 S32:  -0.1316 S33:   0.0292                       
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):   7.7400 -25.4060 -46.7960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1995 T22:   0.0405                                     
REMARK   3      T33:   0.0449 T12:   0.0221                                     
REMARK   3      T13:   0.0089 T23:  -0.0048                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9810 L22:   0.6615                                     
REMARK   3      L33:   2.9118 L12:  -0.0101                                     
REMARK   3      L13:   0.6229 L23:   0.0258                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0514 S12:   0.0177 S13:  -0.1557                       
REMARK   3      S21:   0.0662 S22:   0.0082 S23:  -0.1009                       
REMARK   3      S31:   0.3962 S32:   0.0945 S33:  -0.0597                       
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):  10.9640 -20.9390 -17.4330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4630 T22:   0.2441                                     
REMARK   3      T33:   0.0625 T12:  -0.0058                                     
REMARK   3      T13:  -0.0693 T23:   0.0517                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0860 L22:   2.7383                                     
REMARK   3      L33:   3.1063 L12:  -0.0770                                     
REMARK   3      L13:   0.0634 L23:   1.1285                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0624 S12:  -0.6419 S13:  -0.1988                       
REMARK   3      S21:   0.7950 S22:  -0.0004 S23:  -0.2066                       
REMARK   3      S31:   0.6032 S32:   0.1036 S33:  -0.0620                       
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):   5.7000 -27.6800 -31.9420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2775 T22:   0.0691                                     
REMARK   3      T33:   0.0262 T12:   0.0125                                     
REMARK   3      T13:  -0.0222 T23:   0.0199                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9838 L22:   2.4633                                     
REMARK   3      L33:   2.9636 L12:  -1.0513                                     
REMARK   3      L13:   1.8880 L23:   0.1197                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1575 S12:  -0.2411 S13:  -0.4161                       
REMARK   3      S21:   0.2186 S22:  -0.0016 S23:   0.0271                       
REMARK   3      S31:   0.3854 S32:   0.1446 S33:  -0.1559                       
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):  12.4900  -9.9020 -36.1630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2146 T22:   0.1213                                     
REMARK   3      T33:   0.0491 T12:   0.0014                                     
REMARK   3      T13:   0.0062 T23:   0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3322 L22:   3.7847                                     
REMARK   3      L33:   4.1276 L12:   0.6184                                     
REMARK   3      L13:   0.5090 L23:   3.1082                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0804 S12:   0.1447 S13:   0.1228                       
REMARK   3      S21:  -0.1305 S22:   0.1379 S23:  -0.3442                       
REMARK   3      S31:  -0.2332 S32:   0.4492 S33:  -0.2183                       
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):  -9.1510   3.9660 -27.9880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2120 T22:   0.1421                                     
REMARK   3      T33:   0.1062 T12:  -0.0182                                     
REMARK   3      T13:   0.0070 T23:  -0.0878                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0131 L22:   1.2376                                     
REMARK   3      L33:   8.2730 L12:  -0.4961                                     
REMARK   3      L13:  -0.5530 L23:   3.0657                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0072 S12:  -0.0986 S13:   0.1490                       
REMARK   3      S21:  -0.2076 S22:  -0.0822 S23:   0.0163                       
REMARK   3      S31:  -0.6042 S32:  -0.2025 S33:   0.0894                       
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):   4.2570   4.6610 -21.5880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2261 T22:   0.1049                                     
REMARK   3      T33:   0.0304 T12:  -0.0312                                     
REMARK   3      T13:   0.0117 T23:  -0.0350                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8570 L22:   1.6497                                     
REMARK   3      L33:   1.4952 L12:  -0.3788                                     
REMARK   3      L13:   0.1485 L23:   0.7856                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0108 S12:  -0.0943 S13:   0.1976                       
REMARK   3      S21:  -0.0391 S22:  -0.0069 S23:   0.0711                       
REMARK   3      S31:  -0.1671 S32:  -0.0064 S33:  -0.0038                       
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):  21.4540   3.0050 -15.7460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2015 T22:   0.1673                                     
REMARK   3      T33:   0.0613 T12:  -0.0327                                     
REMARK   3      T13:  -0.0050 T23:  -0.0462                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9432 L22:   4.2471                                     
REMARK   3      L33:   6.4124 L12:   0.2917                                     
REMARK   3      L13:  -0.1967 L23:  -1.3442                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0165 S12:   0.3331 S13:   0.0600                       
REMARK   3      S21:   0.0765 S22:  -0.0498 S23:  -0.3523                       
REMARK   3      S31:  -0.2976 S32:   0.4974 S33:   0.0663                       
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):   7.2570  -1.8830  -3.1410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3040 T22:   0.1730                                     
REMARK   3      T33:   0.0688 T12:  -0.0479                                     
REMARK   3      T13:   0.0183 T23:  -0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6744 L22:   1.1489                                     
REMARK   3      L33:   2.5814 L12:   0.3951                                     
REMARK   3      L13:   1.1490 L23:   0.4905                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1020 S12:  -0.3306 S13:  -0.5357                       
REMARK   3      S21:   0.2627 S22:  -0.0827 S23:   0.0602                       
REMARK   3      S31:   0.3479 S32:  -0.3512 S33:  -0.0193                       
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): -16.2670 -14.0800 -35.3410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2093 T22:   0.2274                                     
REMARK   3      T33:   0.1457 T12:  -0.0575                                     
REMARK   3      T13:   0.0185 T23:  -0.0833                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0758 L22:   0.9533                                     
REMARK   3      L33:   3.1137 L12:   0.1210                                     
REMARK   3      L13:   0.5685 L23:   0.2404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0666 S12:  -0.0560 S13:  -0.1805                       
REMARK   3      S21:  -0.0079 S22:  -0.2432 S23:   0.3082                       
REMARK   3      S31:   0.3094 S32:  -0.5315 S33:   0.1766                       
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): -14.1520 -14.9430 -25.1390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2891 T22:   0.2448                                     
REMARK   3      T33:   0.0973 T12:  -0.1564                                     
REMARK   3      T13:   0.0702 T23:  -0.0856                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5015 L22:   3.3240                                     
REMARK   3      L33:   4.5580 L12:  -3.8404                                     
REMARK   3      L13:   0.6559 L23:  -0.2171                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0134 S12:   0.0231 S13:  -0.3007                       
REMARK   3      S21:   0.0995 S22:  -0.1171 S23:   0.3024                       
REMARK   3      S31:   0.4581 S32:  -0.6184 S33:   0.1304                       
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):  -5.1640  -1.1940 -35.0630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2147 T22:   0.1447                                     
REMARK   3      T33:   0.1560 T12:   0.0100                                     
REMARK   3      T13:   0.0059 T23:  -0.0718                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5329 L22:   2.3868                                     
REMARK   3      L33:   4.1964 L12:   0.6978                                     
REMARK   3      L13:  -0.5066 L23:   0.5314                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0362 S12:  -0.0558 S13:   0.1676                       
REMARK   3      S21:  -0.0975 S22:  -0.0703 S23:   0.1466                       
REMARK   3      S31:  -0.3813 S32:  -0.1338 S33:   0.0340                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.00                                          
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 6G56 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009431.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-APR-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               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51458                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 84.780                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.16600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.73000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.400                              
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   (%): 52.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULPHATE, 50MM SODIUM        
REMARK 280  ACETATE, PH 6, VAPOR DIFFUSION, SITTING DROP, 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       32.35050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.04650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.26050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       63.04650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.35050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.26050            
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: 11570 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 27600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -346.0 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     PHE A     1                                                      
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 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     PHE B   1    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     MET B 178    CG   SD   CE                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS A   112     O2   SO4 B   410     2454     2.02            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS B 171   CA  -  CB  -  SG  ANGL. DEV. =   8.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 138     -128.33    -97.24                                   
REMARK 500    ASN A 203     -157.08    -91.36                                   
REMARK 500    ASN A 334       43.68    -90.88                                   
REMARK 500    THR A 351     -159.86   -149.23                                   
REMARK 500    ASN B 203     -155.65    -91.74                                   
REMARK 500    ALA B 259      119.09    -35.39                                   
REMARK 500    SER B 264     -175.36     71.41                                   
REMARK 500    ASN B 334       44.31    -90.59                                   
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 SO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 415                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 416                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 417                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 418                 
DBREF  6G56 A    2   382  UNP    P63479   ALR1_STAAM       2    382             
DBREF  6G56 B    2   382  UNP    P63479   ALR1_STAAM       2    382             
SEQADV 6G56 MET A  -21  UNP  P63479              INITIATING METHIONINE          
SEQADV 6G56 ALA A  -20  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 SER A  -19  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 TRP A  -18  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 SER A  -17  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 HIS A  -16  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 PRO A  -15  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 GLN A  -14  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 PHE A  -13  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 GLU A  -12  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 LYS A  -11  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 GLY A  -10  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 ALA A   -9  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 VAL A   -8  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 THR A   -7  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 SER A   -6  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 LEU A   -5  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 TYR A   -4  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 LYS A   -3  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 LYS A   -2  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 ALA A   -1  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 GLY A    0  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 PHE A    1  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 MET B  -21  UNP  P63479              INITIATING METHIONINE          
SEQADV 6G56 ALA B  -20  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 SER B  -19  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 TRP B  -18  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 SER B  -17  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 HIS B  -16  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 PRO B  -15  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 GLN B  -14  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 PHE B  -13  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 GLU B  -12  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 LYS B  -11  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 GLY B  -10  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 ALA B   -9  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 VAL B   -8  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 THR B   -7  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 SER B   -6  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 LEU B   -5  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 TYR B   -4  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 LYS B   -3  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 LYS B   -2  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 ALA B   -1  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 GLY B    0  UNP  P63479              EXPRESSION TAG                 
SEQADV 6G56 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    SO4  A 401       5                                                       
HET    SO4  A 402       5                                                       
HET    SO4  A 403       5                                                       
HET    SO4  A 404       5                                                       
HET    SO4  A 405       5                                                       
HET    SO4  A 406       5                                                       
HET    SO4  A 407       5                                                       
HET    SO4  A 408       5                                                       
HET    GOL  A 409       6                                                       
HET    SO4  B 401       5                                                       
HET    SO4  B 402       5                                                       
HET    SO4  B 403       5                                                       
HET    SO4  B 404       5                                                       
HET    SO4  B 405       5                                                       
HET    SO4  B 406       5                                                       
HET    SO4  B 407       5                                                       
HET    SO4  B 408       5                                                       
HET    SO4  B 409       5                                                       
HET    SO4  B 410       5                                                       
HET    SO4  B 411       5                                                       
HET    SO4  B 412       5                                                       
HET    SO4  B 413       5                                                       
HET    SO4  B 414       5                                                       
HET    SO4  B 415       5                                                       
HET    SO4  B 416       5                                                       
HET    GOL  B 417       6                                                       
HET    GOL  B 418       6                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  SO4    24(O4 S 2-)                                                  
FORMUL  11  GOL    3(C3 H8 O3)                                                  
FORMUL  30  HOH   *297(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  GLU A   56  1                                  11    
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  ILE A  118  1                                  12    
HELIX    8 AA8 ASP A  143  TYR A  157  1                                  15    
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 GLY A  283  GLY A  287  5                                   5    
HELIX   14 AB5 LEU A  289  GLN A  293  5                                   5    
HELIX   15 AB6 SER A  341  GLN A  349  1                                   9    
HELIX   16 AB7 ILE A  352  LEU A  360  1                                   9    
HELIX   17 AB8 ASN A  378  LYS A  382  5                                   5    
HELIX   18 AB9 LEU B   15  HIS B   29  1                                  15    
HELIX   19 AC1 VAL B   38  GLY B   44  1                                   7    
HELIX   20 AC2 GLY B   46  GLU B   56  1                                  11    
HELIX   21 AC3 THR B   66  HIS B   76  1                                  11    
HELIX   22 AC4 PRO B   89  LYS B   91  5                                   3    
HELIX   23 AC5 ASP B   92  HIS B   99  1                                   8    
HELIX   24 AC6 SER B  107  ASN B  117  1                                  11    
HELIX   25 AC7 ASP B  143  TYR B  157  1                                  15    
HELIX   26 AC8 ASP B  177  ASN B  191  1                                  15    
HELIX   27 AC9 ASN B  203  MET B  210  1                                   8    
HELIX   28 AD1 GLY B  221  GLY B  226  5                                   6    
HELIX   29 AD2 SER B  230  VAL B  237  1                                   8    
HELIX   30 AD3 SER B  264  THR B  268  5                                   5    
HELIX   31 AD4 GLY B  283  GLY B  287  5                                   5    
HELIX   32 AD5 LEU B  289  GLN B  293  5                                   5    
HELIX   33 AD6 SER B  341  GLN B  349  1                                   9    
HELIX   34 AD7 ILE B  352  LEU B  360  1                                   9    
HELIX   35 AD8 ASN B  378  LYS B  382  5                                   5    
SHEET    1 AA110 GLN A 253  LEU A 257  0                                        
SHEET    2 AA110 THR A 275  LEU A 280 -1  O  ILE A 277   N  LYS A 255           
SHEET    3 AA110 THR A 315  VAL A 319 -1  O  THR A 315   N  LEU A 280           
SHEET    4 AA110 HIS A 302  ILE A 307 -1  N  GLU A 305   O  LYS A 318           
SHEET    5 AA110 PHE A 296  VAL A 299 -1  N  VAL A 299   O  HIS A 302           
SHEET    6 AA110 SER A 328  ILE A 332 -1  O  ILE A 330   N  ASN A 298           
SHEET    7 AA110 VAL A 245  ASN A 250 -1  N  LEU A 247   O  LEU A 331           
SHEET    8 AA110 ALA A   9  ASP A  14 -1  N  TYR A  10   O  ILE A 248           
SHEET    9 AA110 ARG A 366  ASP A 370  1  O  ILE A 367   N  MET A  11           
SHEET   10 AA110 GLN A 373  THR A 377 -1  O  PHE A 375   N  TYR A 368           
SHEET    1 AA2 9 THR A  33  VAL A  37  0                                        
SHEET    2 AA2 9 PHE A  61  VAL A  64  1  O  ALA A  63   N  ALA A  36           
SHEET    3 AA2 9 LYS A  81  VAL A  84  1  O  LYS A  81   N  PHE A  62           
SHEET    4 AA2 9 ALA A 102  VAL A 105  1  O  ALA A 102   N  ILE A  82           
SHEET    5 AA2 9 LEU A 126  LYS A 131  1  O  HIS A 129   N  LEU A 103           
SHEET    6 AA2 9 LEU A 160  PHE A 166  1  O  GLY A 164   N  ILE A 130           
SHEET    7 AA2 9 TYR A 198  HIS A 200  1  O  TYR A 198   N  VAL A 165           
SHEET    8 AA2 9 ALA A 217  ILE A 218  1  N  ALA A 217   O  ILE A 199           
SHEET    9 AA2 9 THR A  33  VAL A  37  1  N  MET A  35   O  ILE A 218           
SHEET    1 AA3 2 SER A 262  SER A 264  0                                        
SHEET    2 AA3 2 THR A 268  THR A 270 -1  O  TYR A 269   N  VAL A 263           
SHEET    1 AA410 GLN B 253  LEU B 257  0                                        
SHEET    2 AA410 THR B 275  LEU B 280 -1  O  ILE B 277   N  LYS B 255           
SHEET    3 AA410 THR B 315  VAL B 319 -1  O  THR B 315   N  LEU B 280           
SHEET    4 AA410 HIS B 302  ILE B 307 -1  N  GLU B 305   O  LYS B 318           
SHEET    5 AA410 PHE B 296  VAL B 299 -1  N  VAL B 299   O  HIS B 302           
SHEET    6 AA410 SER B 328  ILE B 332 -1  O  ILE B 330   N  ASN B 298           
SHEET    7 AA410 VAL B 245  ASN B 250 -1  N  LEU B 247   O  LEU B 331           
SHEET    8 AA410 ALA B   9  ASP B  14 -1  N  TYR B  10   O  ILE B 248           
SHEET    9 AA410 ARG B 366  ASP B 370  1  O  ILE B 367   N  MET B  11           
SHEET   10 AA410 GLN B 373  THR B 377 -1  O  PHE B 375   N  TYR B 368           
SHEET    1 AA5 9 THR B  33  VAL B  37  0                                        
SHEET    2 AA5 9 PHE B  61  VAL B  64  1  O  ALA B  63   N  ALA B  36           
SHEET    3 AA5 9 LYS B  81  VAL B  84  1  O  LYS B  81   N  PHE B  62           
SHEET    4 AA5 9 ALA B 102  VAL B 105  1  O  ALA B 102   N  ILE B  82           
SHEET    5 AA5 9 LEU B 126  LYS B 131  1  O  HIS B 129   N  LEU B 103           
SHEET    6 AA5 9 LEU B 160  PHE B 166  1  O  GLY B 164   N  ILE B 130           
SHEET    7 AA5 9 TYR B 198  HIS B 200  1  O  TYR B 198   N  VAL B 165           
SHEET    8 AA5 9 ALA B 217  ILE B 218  1  N  ALA B 217   O  ILE B 199           
SHEET    9 AA5 9 THR B  33  VAL B  37  1  N  MET B  35   O  ILE B 218           
SHEET    1 AA6 2 SER B 262  VAL B 263  0                                        
SHEET    2 AA6 2 TYR B 269  THR B 270 -1  O  TYR B 269   N  VAL B 263           
SITE     1 AC1  7 TYR A  43  ASN A 203  SER A 204  GLY A 221                    
SITE     2 AC1  7 ILE A 222  TYR A 354  HOH A 536                               
SITE     1 AC2  7 HIS A  29  PRO A  30  ASN A  31  LYS A  32                    
SITE     2 AC2  7 ASP A 211  GLN A 213  HOH A 621                               
SITE     1 AC3  7 TYR A 228  GLN A 234  HIS A 240  LEU A 241                    
SITE     2 AC3  7 ARG A 336  HOH A 561  HOH A 580                               
SITE     1 AC4  6 TYR A 183  LYS A 187  CYS A 212  GLN A 213                    
SITE     2 AC4  6 PHE A 214  HOH A 502                                          
SITE     1 AC5  4 LYS A  23  GLN A 184  LYS A 187  HOH A 550                    
SITE     1 AC6  4 SER A 107  LYS A 108  GLN A 109  HOH B 608                    
SITE     1 AC7  7 SER A 264  GLY A 266  HOH A 510  ARG B 138                    
SITE     2 AC7  7 HIS B 168  PHE B 169  CYS B 171                               
SITE     1 AC8  4 ASN A  16  ALA A  19  HIS A  53  ASN A  57                    
SITE     1 AC9  7 CYS A 311  MET A 312  ASP A 313  GLN A 314                    
SITE     2 AC9  7 LYS B  39  ARG B 138  GOL B 418                               
SITE     1 AD1  8 TYR B  43  ASN B 203  SER B 204  GLY B 221                    
SITE     2 AD1  8 ILE B 222  TYR B 354  HOH B 507  HOH B 578                    
SITE     1 AD2  7 TYR B 228  GLN B 234  HIS B 240  LEU B 241                    
SITE     2 AD2  7 ARG B 336  HOH B 532  HOH B 561                               
SITE     1 AD3  5 TYR B 183  LYS B 187  CYS B 212  GLN B 213                    
SITE     2 AD3  5 PHE B 214                                                     
SITE     1 AD4  3 ASP B 143  THR B 144  ARG B 185                               
SITE     1 AD5  2 GLN B 184  LYS B 187                                          
SITE     1 AD6  5 ARG A  74  HIS A  99  HOH A 600  GLU B 149                    
SITE     2 AD6  5 GLU B 152                                                     
SITE     1 AD7  5 ARG A 100  LYS A 124  LYS B 108  LYS B 112                    
SITE     2 AD7  5 GLU B 149                                                     
SITE     1 AD8  3 LYS B 142  ASP B 143  THR B 146                               
SITE     1 AD9  4 LYS A 116  MET B 210  ASP B 211  CYS B 212                    
SITE     1 AE1  8 LYS A 108  LYS A 112  HIS B  29  PRO B  30                    
SITE     2 AE1  8 ASN B  31  LYS B  32  GLN B 213  HOH B 509                    
SITE     1 AE2  4 ASN B  16  ALA B  19  HIS B  53  ASN B  57                    
SITE     1 AE3  3 LYS B  49  ARG B  52  HIS B  76                               
SITE     1 AE4  3 ARG B  74  HIS B  99  ARG B 100                               
SITE     1 AE5  2 LYS B 124  LYS B 125                                          
SITE     1 AE6  5 GLU A 197  TYR B 157  GLU B 158  GLN B 159                    
SITE     2 AE6  5 HOH B 571                                                     
SITE     1 AE7  3 GLU B 174  SER B 230  GLU B 231                               
SITE     1 AE8  6 LYS A  39  TYR B 265  CYS B 311  MET B 312                    
SITE     2 AE8  6 ASP B 313  HOH B 580                                          
SITE     1 AE9  8 GOL A 409  ARG B 138  PHE B 166  HIS B 168                    
SITE     2 AE9  8 ASN B 203  ARG B 219  HOH B 501  HOH B 550                    
CRYST1   64.701  114.521  126.093  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      0.015456  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008732  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007931        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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