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LongText Report for: 3HYS-pdb

Name Class
3HYS-pdb
HEADER    HYDROLASE                               23-JUN-09   3HYS              
TITLE     STRUCTURE OF RV0554 FROM MYCOBACTERIUM TUBERCULOSIS COMPLEXED WITH    
TITLE    2 MALONIC ACID                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN RV0554, PUTATIVE BROMOPEROXIDASE;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: POSSIBLE PEROXIDASE BPOC (NON-HAEM PEROXIDASE);             
COMPND   5 EC: 1.11.1.-;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 GENE: BPOC, MT0580, RV0554;                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROLASE, OXIDOREDUCTASE, PEROXIDASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.JOHNSTON,E.N.BAKER                                                
REVDAT   1   02-JUN-10 3HYS    0                                                
JRNL        AUTH   J.M.JOHNSTON,E.N.BAKER                                       
JRNL        TITL   STRUCTURAL AND FUNCTIONAL ANALYSIS OF RV0554 FROM            
JRNL        TITL 2 MYCOBACTERIUM TUBERCULOSIS, TESTING A PUTATIVE ROLE IN       
JRNL        TITL 3 MENAQUINONE BIOSYNTHESIS                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 31347                          
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) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1579                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2158                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1840                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 105                          
REMARK   3   BIN FREE R VALUE                    : 0.2390                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4100                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 388                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.22                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.04000                                             
REMARK   3    B22 (A**2) : -0.04000                                             
REMARK   3    B33 (A**2) : 0.08000                                              
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): 0.244         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.204         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4255 ; 0.026 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5785 ; 1.940 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   540 ; 5.707 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   195 ;33.705 ;23.179       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   633 ;15.177 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    38 ;18.678 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   640 ; 0.139 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3322 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2683 ; 1.120 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4307 ; 1.951 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1572 ; 3.379 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1475 ; 5.052 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
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   -13        A    43                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.3771 -48.1864 -11.8476              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0919 T22:   0.0746                                     
REMARK   3      T33:   0.0646 T12:   0.0095                                     
REMARK   3      T13:   0.0017 T23:  -0.0131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9454 L22:   0.7216                                     
REMARK   3      L33:   0.3700 L12:   0.8072                                     
REMARK   3      L13:  -0.1846 L23:  -0.3031                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0587 S12:   0.1241 S13:  -0.2597                       
REMARK   3      S21:  -0.1315 S22:   0.0287 S23:  -0.0613                       
REMARK   3      S31:   0.1856 S32:  -0.0351 S33:   0.0301                       
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    44        A   127                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.0478 -41.5078  -7.1605              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0357 T22:   0.0419                                     
REMARK   3      T33:   0.0316 T12:  -0.0126                                     
REMARK   3      T13:   0.0128 T23:   0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8770 L22:   1.4015                                     
REMARK   3      L33:   1.1004 L12:   0.0865                                     
REMARK   3      L13:  -0.2045 L23:   0.2978                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0007 S12:  -0.0121 S13:   0.0108                       
REMARK   3      S21:  -0.0080 S22:   0.0066 S23:   0.0629                       
REMARK   3      S31:  -0.0358 S32:  -0.0703 S33:  -0.0072                       
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   128        A   187                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4835 -34.2247 -26.0976              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0874 T22:   0.0825                                     
REMARK   3      T33:   0.0916 T12:   0.0116                                     
REMARK   3      T13:  -0.0077 T23:  -0.0134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8539 L22:   0.8854                                     
REMARK   3      L33:   1.3474 L12:   0.7522                                     
REMARK   3      L13:  -0.9970 L23:  -1.0803                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0228 S12:   0.0605 S13:  -0.0095                       
REMARK   3      S21:  -0.0597 S22:   0.0136 S23:   0.0611                       
REMARK   3      S31:   0.0679 S32:  -0.0563 S33:   0.0092                       
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   188        A   261                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.7473 -29.0427  -6.3596              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0831 T22:   0.0559                                     
REMARK   3      T33:   0.0854 T12:  -0.0057                                     
REMARK   3      T13:  -0.0067 T23:  -0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1984 L22:   0.8367                                     
REMARK   3      L33:   1.3807 L12:  -0.0763                                     
REMARK   3      L13:  -0.3783 L23:  -0.1874                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0025 S12:  -0.0901 S13:   0.0118                       
REMARK   3      S21:   0.0901 S22:  -0.0021 S23:  -0.0344                       
REMARK   3      S31:  -0.0300 S32:   0.0469 S33:  -0.0005                       
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 :   B     2        B     8                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4443 -46.9831   6.6995              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1416 T22:   0.1552                                     
REMARK   3      T33:   0.1700 T12:   0.0022                                     
REMARK   3      T13:  -0.0022 T23:   0.0237                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1125 L22:   6.0666                                     
REMARK   3      L33:   0.2956 L12:   0.3835                                     
REMARK   3      L13:   0.2194 L23:  -0.4575                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0213 S12:  -0.4037 S13:   0.2846                       
REMARK   3      S21:   0.5133 S22:  -0.1066 S23:   0.2186                       
REMARK   3      S31:   0.0650 S32:  -0.1536 S33:   0.1279                       
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 :   B     9        B   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.5092 -45.5566   4.4353              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0909 T22:   0.0991                                     
REMARK   3      T33:   0.0887 T12:   0.0071                                     
REMARK   3      T13:   0.0039 T23:   0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7222 L22:   0.8732                                     
REMARK   3      L33:   0.5778 L12:   0.2429                                     
REMARK   3      L13:   0.1070 L23:   0.0242                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0209 S12:  -0.1471 S13:  -0.0573                       
REMARK   3      S21:   0.1745 S22:  -0.0150 S23:  -0.0094                       
REMARK   3      S31:   0.0527 S32:  -0.0142 S33:  -0.0058                       
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 :   B   123        B   169                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.1724 -26.8869  -9.0230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0916 T22:   0.0964                                     
REMARK   3      T33:   0.1242 T12:  -0.0102                                     
REMARK   3      T13:   0.0046 T23:   0.0129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8626 L22:   0.8212                                     
REMARK   3      L33:   2.3425 L12:   0.0490                                     
REMARK   3      L13:   0.4356 L23:   0.0758                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0070 S12:   0.0856 S13:  -0.0582                       
REMARK   3      S21:  -0.0920 S22:  -0.0385 S23:   0.0724                       
REMARK   3      S31:   0.0224 S32:  -0.1138 S33:   0.0314                       
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   170        B   262                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.2823 -43.1363  -1.0628              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0859 T22:   0.0978                                     
REMARK   3      T33:   0.0889 T12:  -0.0060                                     
REMARK   3      T13:   0.0017 T23:   0.0059                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3122 L22:   0.8663                                     
REMARK   3      L33:   0.3515 L12:  -0.0454                                     
REMARK   3      L13:  -0.2261 L23:   0.3473                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0008 S12:  -0.0226 S13:   0.0213                       
REMARK   3      S21:   0.0348 S22:   0.0095 S23:  -0.1272                       
REMARK   3      S31:  -0.0147 S32:   0.0882 S33:  -0.0103                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : RESIDUAL ONLY                                  
REMARK   4                                                                      
REMARK   4 3HYS COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053748.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 4.92                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31386                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 8.100                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 35.6030                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 7.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 95% (0.1M NAACETATE PH 4.92, 2% MPD,     
REMARK 280  15% ETHYLENE GLYCOL) AND 5% MALONIC ACID 1.65M, VAPOR DIFFUSION,    
REMARK 280  HANGING DROP, TEMPERATURE 291K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.53200            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       50.21750            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       50.21750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       33.76600            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       50.21750            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       50.21750            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      101.29800            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       50.21750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.21750            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       33.76600            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       50.21750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.21750            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      101.29800            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       67.53200            
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: 5090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 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   -30                                                      
REMARK 465     SER A   -29                                                      
REMARK 465     TYR A   -28                                                      
REMARK 465     TYR A   -27                                                      
REMARK 465     HIS A   -26                                                      
REMARK 465     HIS A   -25                                                      
REMARK 465     HIS A   -24                                                      
REMARK 465     HIS A   -23                                                      
REMARK 465     HIS A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     ASP A   -20                                                      
REMARK 465     TYR A   -19                                                      
REMARK 465     ASP A   -18                                                      
REMARK 465     ILE A   -17                                                      
REMARK 465     PRO A   -16                                                      
REMARK 465     THR A   -15                                                      
REMARK 465     THR A   -14                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     MET B   -30                                                      
REMARK 465     SER B   -29                                                      
REMARK 465     TYR B   -28                                                      
REMARK 465     TYR B   -27                                                      
REMARK 465     HIS B   -26                                                      
REMARK 465     HIS B   -25                                                      
REMARK 465     HIS B   -24                                                      
REMARK 465     HIS B   -23                                                      
REMARK 465     HIS B   -22                                                      
REMARK 465     HIS B   -21                                                      
REMARK 465     ASP B   -20                                                      
REMARK 465     TYR B   -19                                                      
REMARK 465     ASP B   -18                                                      
REMARK 465     ILE B   -17                                                      
REMARK 465     PRO B   -16                                                      
REMARK 465     THR B   -15                                                      
REMARK 465     THR B   -14                                                      
REMARK 465     GLU B   -13                                                      
REMARK 465     ASN B   -12                                                      
REMARK 465     LEU B   -11                                                      
REMARK 465     TYR B   -10                                                      
REMARK 465     PHE B    -9                                                      
REMARK 465     GLN B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     ALA B    -6                                                      
REMARK 465     MET B    -5                                                      
REMARK 465     ASP B    -4                                                      
REMARK 465     PRO B    -3                                                      
REMARK 465     GLU B    -2                                                      
REMARK 465     PHE B    -1                                                      
REMARK 465     ARG B     0                                                      
REMARK 465     VAL B     1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   363     O    HOH B   364              2.18            
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    ASP B   8   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B 159   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    PRO B 216   C   -  N   -  CA  ANGL. DEV. =   9.5 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    SER A  87     -118.72     51.08                                   
REMARK 500    ALA A 100       56.35   -141.57                                   
REMARK 500    ASP A 117     -174.98    -66.02                                   
REMARK 500    LEU A 240       44.42    -93.18                                   
REMARK 500    ASN B  48      154.91    -48.04                                   
REMARK 500    SER B  87     -119.92     48.30                                   
REMARK 500    LEU B 240       43.86    -95.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 267  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 223   O                                                      
REMARK 620 2 LEU A 226   O    78.6                                              
REMARK 620 3 GLY A 229   O    90.1  99.7                                        
REMARK 620 4 HOH A 308   O    87.6 165.6  84.2                                  
REMARK 620 5 HOH A 309   O   161.3  94.0  74.1 100.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 267  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA B 223   O                                                      
REMARK 620 2 LEU B 226   O    83.9                                              
REMARK 620 3 HOH B 282   O    95.7 178.3                                        
REMARK 620 4 GLY B 229   O    88.2  97.2  81.1                                  
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 MLA A 5188                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 263                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 264                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 265                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 266                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 267                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLA B 5188                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 263                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 264                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 265                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 266                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 267                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: RCSB053538   RELATED DB: PDB                             
REMARK 900 RELATED ID: 3E3A RCSB048820   RELATED DB: PDB                        
DBREF  3HYS A    2   262  UNP    O06420   O06420_MYCTU     2    262             
DBREF  3HYS B    2   262  UNP    O06420   O06420_MYCTU     2    262             
SEQADV 3HYS MET A  -30  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS SER A  -29  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS TYR A  -28  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS TYR A  -27  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS HIS A  -26  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS HIS A  -25  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS HIS A  -24  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS HIS A  -23  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS HIS A  -22  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS HIS A  -21  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS ASP A  -20  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS TYR A  -19  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS ASP A  -18  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS ILE A  -17  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS PRO A  -16  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS THR A  -15  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS THR A  -14  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS GLU A  -13  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS ASN A  -12  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS LEU A  -11  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS TYR A  -10  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS PHE A   -9  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS GLN A   -8  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS GLY A   -7  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS ALA A   -6  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS MET A   -5  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS ASP A   -4  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS PRO A   -3  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS GLU A   -2  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS PHE A   -1  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS ARG A    0  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS VAL A    1  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS MET B  -30  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS SER B  -29  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS TYR B  -28  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS TYR B  -27  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS HIS B  -26  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS HIS B  -25  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS HIS B  -24  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS HIS B  -23  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS HIS B  -22  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS HIS B  -21  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS ASP B  -20  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS TYR B  -19  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS ASP B  -18  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS ILE B  -17  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS PRO B  -16  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS THR B  -15  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS THR B  -14  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS GLU B  -13  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS ASN B  -12  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS LEU B  -11  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS TYR B  -10  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS PHE B   -9  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS GLN B   -8  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS GLY B   -7  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS ALA B   -6  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS MET B   -5  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS ASP B   -4  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS PRO B   -3  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS GLU B   -2  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS PHE B   -1  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS ARG B    0  UNP  O06420              EXPRESSION TAG                 
SEQADV 3HYS VAL B    1  UNP  O06420              EXPRESSION TAG                 
SEQRES   1 A  293  MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP          
SEQRES   2 A  293  ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET          
SEQRES   3 A  293  ASP PRO GLU PHE ARG VAL ILE ASN LEU ALA TYR ASP ASP          
SEQRES   4 A  293  ASN GLY THR GLY ASP PRO VAL VAL PHE ILE ALA GLY ARG          
SEQRES   5 A  293  GLY GLY ALA GLY ARG THR TRP HIS PRO HIS GLN VAL PRO          
SEQRES   6 A  293  ALA PHE LEU ALA ALA GLY TYR ARG CYS ILE THR PHE ASP          
SEQRES   7 A  293  ASN ARG GLY ILE GLY ALA THR GLU ASN ALA GLU GLY PHE          
SEQRES   8 A  293  THR THR GLN THR MET VAL ALA ASP THR ALA ALA LEU ILE          
SEQRES   9 A  293  GLU THR LEU ASP ILE ALA PRO ALA ARG VAL VAL GLY VAL          
SEQRES  10 A  293  SER MET GLY ALA PHE ILE ALA GLN GLU LEU MET VAL VAL          
SEQRES  11 A  293  ALA PRO GLU LEU VAL SER SER ALA VAL LEU MET ALA THR          
SEQRES  12 A  293  ARG GLY ARG LEU ASP ARG ALA ARG GLN PHE PHE ASN LYS          
SEQRES  13 A  293  ALA GLU ALA GLU LEU TYR ASP SER GLY VAL GLN LEU PRO          
SEQRES  14 A  293  PRO THR TYR ASP ALA ARG ALA ARG LEU LEU GLU ASN PHE          
SEQRES  15 A  293  SER ARG LYS THR LEU ASN ASP ASP VAL ALA VAL GLY ASP          
SEQRES  16 A  293  TRP ILE ALA MET PHE SER MET TRP PRO ILE LYS SER THR          
SEQRES  17 A  293  PRO GLY LEU ARG CYS GLN LEU ASP CYS ALA PRO GLN THR          
SEQRES  18 A  293  ASN ARG LEU PRO ALA TYR ARG ASN ILE ALA ALA PRO VAL          
SEQRES  19 A  293  LEU VAL ILE GLY PHE ALA ASP ASP VAL VAL THR PRO PRO          
SEQRES  20 A  293  TYR LEU GLY ARG GLU VAL ALA ASP ALA LEU PRO ASN GLY          
SEQRES  21 A  293  ARG TYR LEU GLN ILE PRO ASP ALA GLY HIS LEU GLY PHE          
SEQRES  22 A  293  PHE GLU ARG PRO GLU ALA VAL ASN THR ALA MET LEU LYS          
SEQRES  23 A  293  PHE PHE ALA SER VAL LYS ALA                                  
SEQRES   1 B  293  MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP          
SEQRES   2 B  293  ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET          
SEQRES   3 B  293  ASP PRO GLU PHE ARG VAL ILE ASN LEU ALA TYR ASP ASP          
SEQRES   4 B  293  ASN GLY THR GLY ASP PRO VAL VAL PHE ILE ALA GLY ARG          
SEQRES   5 B  293  GLY GLY ALA GLY ARG THR TRP HIS PRO HIS GLN VAL PRO          
SEQRES   6 B  293  ALA PHE LEU ALA ALA GLY TYR ARG CYS ILE THR PHE ASP          
SEQRES   7 B  293  ASN ARG GLY ILE GLY ALA THR GLU ASN ALA GLU GLY PHE          
SEQRES   8 B  293  THR THR GLN THR MET VAL ALA ASP THR ALA ALA LEU ILE          
SEQRES   9 B  293  GLU THR LEU ASP ILE ALA PRO ALA ARG VAL VAL GLY VAL          
SEQRES  10 B  293  SER MET GLY ALA PHE ILE ALA GLN GLU LEU MET VAL VAL          
SEQRES  11 B  293  ALA PRO GLU LEU VAL SER SER ALA VAL LEU MET ALA THR          
SEQRES  12 B  293  ARG GLY ARG LEU ASP ARG ALA ARG GLN PHE PHE ASN LYS          
SEQRES  13 B  293  ALA GLU ALA GLU LEU TYR ASP SER GLY VAL GLN LEU PRO          
SEQRES  14 B  293  PRO THR TYR ASP ALA ARG ALA ARG LEU LEU GLU ASN PHE          
SEQRES  15 B  293  SER ARG LYS THR LEU ASN ASP ASP VAL ALA VAL GLY ASP          
SEQRES  16 B  293  TRP ILE ALA MET PHE SER MET TRP PRO ILE LYS SER THR          
SEQRES  17 B  293  PRO GLY LEU ARG CYS GLN LEU ASP CYS ALA PRO GLN THR          
SEQRES  18 B  293  ASN ARG LEU PRO ALA TYR ARG ASN ILE ALA ALA PRO VAL          
SEQRES  19 B  293  LEU VAL ILE GLY PHE ALA ASP ASP VAL VAL THR PRO PRO          
SEQRES  20 B  293  TYR LEU GLY ARG GLU VAL ALA ASP ALA LEU PRO ASN GLY          
SEQRES  21 B  293  ARG TYR LEU GLN ILE PRO ASP ALA GLY HIS LEU GLY PHE          
SEQRES  22 B  293  PHE GLU ARG PRO GLU ALA VAL ASN THR ALA MET LEU LYS          
SEQRES  23 B  293  PHE PHE ALA SER VAL LYS ALA                                  
HET    MLA  A5188       7                                                       
HET    TRS  A 263       8                                                       
HET    EDO  A 264       4                                                       
HET    EDO  A 265       4                                                       
HET    EDO  A 266       4                                                       
HET     NA  A 267       1                                                       
HET    MLA  B5188       7                                                       
HET    EDO  B 263       4                                                       
HET    EDO  B 264       4                                                       
HET    EDO  B 265       4                                                       
HET    EDO  B 266       4                                                       
HET     NA  B 267       1                                                       
HETNAM     MLA MALONIC ACID                                                     
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      NA SODIUM ION                                                       
HETSYN     MLA DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID;                        
HETSYN   2 MLA  METAHNEDICARBOXYLIC ACID                                        
HETSYN     TRS TRIS BUFFER                                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  MLA    2(C3 H4 O4)                                                  
FORMUL   4  TRS    C4 H12 N O3 1+                                               
FORMUL   5  EDO    7(C2 H6 O2)                                                  
FORMUL   8   NA    2(NA 1+)                                                     
FORMUL  15  HOH   *388(H2 O)                                                    
HELIX    1   1 ALA A   24  HIS A   29  5                                   6    
HELIX    2   2 GLN A   32  ALA A   39  1                                   8    
HELIX    3   3 ILE A   51  GLU A   55  5                                   5    
HELIX    4   4 THR A   61  ASP A   77  1                                  17    
HELIX    5   5 SER A   87  ALA A  100  1                                  14    
HELIX    6   6 ASP A  117  SER A  133  1                                  17    
HELIX    7   7 PRO A  138  PHE A  151  1                                  14    
HELIX    8   8 SER A  152  ASN A  157  1                                   6    
HELIX    9   9 ASP A  158  TRP A  172  1                                  15    
HELIX   10  10 THR A  177  LEU A  184  1                                   8    
HELIX   11  11 ARG A  192  ARG A  197  1                                   6    
HELIX   12  12 PRO A  215  LEU A  226  1                                  12    
HELIX   13  13 LEU A  240  ARG A  245  1                                   6    
HELIX   14  14 ARG A  245  VAL A  260  1                                  16    
HELIX   15  15 ALA B   24  HIS B   29  5                                   6    
HELIX   16  16 GLN B   32  ALA B   39  1                                   8    
HELIX   17  17 ILE B   51  GLU B   55  5                                   5    
HELIX   18  18 THR B   61  LEU B   76  1                                  16    
HELIX   19  19 SER B   87  ALA B  100  1                                  14    
HELIX   20  20 ASP B  117  SER B  133  1                                  17    
HELIX   21  21 PRO B  138  PHE B  151  1                                  14    
HELIX   22  22 SER B  152  ASN B  157  1                                   6    
HELIX   23  23 ASP B  158  TRP B  172  1                                  15    
HELIX   24  24 THR B  177  LEU B  184  1                                   8    
HELIX   25  25 ARG B  192  ARG B  197  1                                   6    
HELIX   26  26 PRO B  215  LEU B  226  1                                  12    
HELIX   27  27 LEU B  240  ARG B  245  1                                   6    
HELIX   28  28 ARG B  245  VAL B  260  1                                  16    
SHEET    1   A 8 LEU A -11  MET A  -5  0                                        
SHEET    2   A 8 VAL A   1  ASN A   9 -1  O  ILE A   2   N  GLY A  -7           
SHEET    3   A 8 TYR A  41  PHE A  46 -1  O  THR A  45   N  ASP A   7           
SHEET    4   A 8 ASP A  13  ILE A  18  1  N  VAL A  15   O  ARG A  42           
SHEET    5   A 8 ALA A  81  VAL A  86  1  O  ARG A  82   N  VAL A  16           
SHEET    6   A 8 VAL A 104  MET A 110  1  O  MET A 110   N  GLY A  85           
SHEET    7   A 8 VAL A 203  PHE A 208  1  O  ILE A 206   N  LEU A 109           
SHEET    8   A 8 GLY A 229  ILE A 234  1  O  ARG A 230   N  VAL A 205           
SHEET    1   B 7 TYR B   6  ASN B   9  0                                        
SHEET    2   B 7 ARG B  42  PHE B  46 -1  O  THR B  45   N  ASP B   7           
SHEET    3   B 7 PRO B  14  ILE B  18  1  N  VAL B  15   O  ARG B  42           
SHEET    4   B 7 ALA B  81  VAL B  86  1  O  VAL B  84   N  ILE B  18           
SHEET    5   B 7 VAL B 104  MET B 110  1  O  MET B 110   N  GLY B  85           
SHEET    6   B 7 VAL B 203  PHE B 208  1  O  ILE B 206   N  LEU B 109           
SHEET    7   B 7 GLY B 229  ILE B 234  1  O  ILE B 234   N  GLY B 207           
LINK         O   ALA A 223                NA    NA A 267     1555   1555  2.43  
LINK         O   LEU A 226                NA    NA A 267     1555   1555  2.42  
LINK         O   GLY A 229                NA    NA A 267     1555   1555  2.77  
LINK         O   ALA B 223                NA    NA B 267     1555   1555  2.44  
LINK         O   LEU B 226                NA    NA B 267     1555   1555  2.34  
LINK        NA    NA A 267                 O   HOH A 308     1555   1555  2.71  
LINK        NA    NA A 267                 O   HOH A 309     1555   1555  2.22  
LINK        NA    NA B 267                 O   HOH B 282     1555   1555  2.39  
LINK         O   GLY B 229                NA    NA B 267     1555   1555  3.04  
CISPEP   1 ALA A   79    PRO A   80          0        -3.77                     
CISPEP   2 ALA B   79    PRO B   80          0        -7.75                     
SITE     1 AC1  6 THR A  27  ARG A 146  TRP A 172  LEU A 240                    
SITE     2 AC1  6 EDO A 264  HOH A 405                                          
SITE     1 AC2  8 GLY A  20  ARG A  21  SER A  87  MET A  88                    
SITE     2 AC2  8 ARG A 113  GLN A 183  LEU A 184  HOH A 476                    
SITE     1 AC3  4 ARG A  21  GLY A  23  HOH A 400  MLA A5188                    
SITE     1 AC4  3 ALA A 161  ASP A 164  TRP A 165                               
SITE     1 AC5  6 PHE A  46  ASN A  48  ARG A  49  MET A  65                    
SITE     2 AC5  6 ASP A  68  THR A  69                                          
SITE     1 AC6  5 ALA A 223  LEU A 226  GLY A 229  HOH A 308                    
SITE     2 AC6  5 HOH A 309                                                     
SITE     1 AC7 10 GLY B  20  ARG B  21  SER B  87  MET B  88                    
SITE     2 AC7 10 ARG B 120  PHE B 123  HIS B 239  HOH B 300                    
SITE     3 AC7 10 HOH B 301  HOH B 302                                          
SITE     1 AC8  3 ARG B 146  HOH B 307  HOH B 417                               
SITE     1 AC9  7 GLY B  22  ALA B  24  ARG B  26  TRP B 172                    
SITE     2 AC9  7 PRO B 173  HOH B 417  HOH B 418                               
SITE     1 BC1  3 ALA B 119  HOH B 295  HOH B 296                               
SITE     1 BC2  3 GLY B  12  ASP B  13  GLY B  40                               
SITE     1 BC3  5 ALA B 223  ASP B 224  LEU B 226  GLY B 229                    
SITE     2 BC3  5 HOH B 282                                                     
CRYST1  100.435  100.435  135.064  90.00  90.00  90.00 P 41 21 2    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009957  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009957  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007404        0.00000                         
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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