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Database: PDB
Entry: 2B0P
LinkDB: 2B0P
Original site: 2B0P 
HEADER    HYDROLASE                               14-SEP-05   2B0P              
TITLE     TRUNCATED S. AUREUS LYTM, P212121 CRYSTAL FORM                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCYL-GLYCINE ENDOPEPTIDASE LYTM;                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: AUTOLYSIN LYTM;                                             
COMPND   5 EC: 3.4.24.75;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 GENE: LYTM;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    LYTM, LYSOSTAPHIN, PEPTIDOGLYCAN AMIDASE, PEPTIDASE, HYDROLASE        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.FIRCZUK,A.MUCHA,M.BOCHTLER                                          
REVDAT   4   23-AUG-23 2B0P    1       REMARK LINK                              
REVDAT   3   13-JUL-11 2B0P    1       VERSN                                    
REVDAT   2   25-MAR-08 2B0P    1       REMARK VERSN                             
REVDAT   1   10-JAN-06 2B0P    0                                                
JRNL        AUTH   M.FIRCZUK,A.MUCHA,M.BOCHTLER                                 
JRNL        TITL   CRYSTAL STRUCTURES OF ACTIVE LYTM.                           
JRNL        REF    J.MOL.BIOL.                   V. 354   578 2005              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   16269153                                                     
JRNL        DOI    10.1016/J.JMB.2005.09.082                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.G.ODINTSOV,I.SABALA,M.MARCYJANIAK,M.BOCHTLER               
REMARK   1  TITL   LATENT LYTM AT 1.3A RESOLUTION.                              
REMARK   1  REF    J.MOL.BIOL.                   V. 335   775 2004              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   14687573                                                     
REMARK   1  DOI    10.1016/J.JMB.2003.11.009                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.84                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 39977                          
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) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2082                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2849                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2680                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 170                          
REMARK   3   BIN FREE R VALUE                    : 0.2550                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1980                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 385                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 13.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.04000                                              
REMARK   3    B22 (A**2) : -0.46000                                             
REMARK   3    B33 (A**2) : -1.58000                                             
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): 0.077         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.083         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.080         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.205         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2051 ; 0.017 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1653 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2787 ; 1.703 ; 1.909       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3858 ; 4.003 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   256 ; 7.232 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   274 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2396 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   426 ; 0.015 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   365 ; 0.193 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1856 ; 0.296 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   997 ; 0.114 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   260 ; 0.174 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.094 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     5 ; 0.082 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    39 ; 0.332 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    32 ; 0.212 ; 0.200       
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):  1275 ; 1.075 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2014 ; 1.668 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   776 ; 2.616 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   773 ; 3.884 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
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   188        A   316                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.2780  -3.7800   0.3210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0002 T22:   0.1962                                     
REMARK   3      T33:   0.1806 T12:   0.0046                                     
REMARK   3      T13:  -0.0037 T23:  -0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2403 L22:   1.0336                                     
REMARK   3      L33:   1.2332 L12:   0.0854                                     
REMARK   3      L13:   0.1711 L23:   0.4367                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0103 S12:  -0.0477 S13:   0.0174                       
REMARK   3      S21:   0.0006 S22:  -0.0058 S23:  -0.0420                       
REMARK   3      S31:   0.0404 S32:  -0.0278 S33:  -0.0045                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   188        B   316                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.7030 -13.1700 -26.4790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0200 T22:   0.1818                                     
REMARK   3      T33:   0.1888 T12:  -0.0073                                     
REMARK   3      T13:   0.0020 T23:   0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4382 L22:   0.8072                                     
REMARK   3      L33:   0.7195 L12:   0.0199                                     
REMARK   3      L13:  -0.0222 L23:   0.0179                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0107 S12:   0.0297 S13:  -0.0326                       
REMARK   3      S21:   0.0168 S22:   0.0011 S23:  -0.0022                       
REMARK   3      S31:   0.0082 S32:  -0.0135 S33:  -0.0119                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 2B0P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-SEP-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000034529.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MPG/DESY, HAMBURG                  
REMARK 200  BEAMLINE                       : BW6                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.05                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42130                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : 0.06800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.25600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
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: 1QWY                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M SODIUM     
REMARK 280  CACODYLATE, 0.1 M SODIUM ACETATE, PH 6.8, VAPOR DIFFUSION,          
REMARK 280  SITTING DROP, TEMPERATURE 294K                                      
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       16.04650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.02450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.13050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.02450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.04650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.13050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   183                                                      
REMARK 465     ALA A   184                                                      
REMARK 465     HIS A   185                                                      
REMARK 465     ALA A   186                                                      
REMARK 465     LYS A   187                                                      
REMARK 465     MET B   183                                                      
REMARK 465     ALA B   184                                                      
REMARK 465     HIS B   185                                                      
REMARK 465     ALA B   186                                                      
REMARK 465     LYS B   187                                                      
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 228   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 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    ASN A 253       59.41    -94.70                                   
REMARK 500    ASN A 262     -121.58    -87.15                                   
REMARK 500    ALA B 234      105.40   -161.38                                   
REMARK 500    ASN B 262     -114.93    -89.90                                   
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                              ZN A 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 210   NE2                                                    
REMARK 620 2 ASP A 214   OD1 103.3                                              
REMARK 620 3 HIS A 293   ND1 105.8 103.7                                        
REMARK 620 4 CAC A 500   O2   99.2 136.5 105.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 210   NE2                                                    
REMARK 620 2 ASP B 214   OD1 103.0                                              
REMARK 620 3 HIS B 293   ND1 104.9 103.0                                        
REMARK 620 4 CAC B 501   O2  102.8 133.0 107.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 400                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 701                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QWY   RELATED DB: PDB                                   
REMARK 900 FULL-LENGTH LYTM                                                     
REMARK 900 RELATED ID: 2B13   RELATED DB: PDB                                   
REMARK 900 TRUNCATED LYTM, DIFFERENT CRYSTAL FORM                               
REMARK 900 RELATED ID: 2B44   RELATED DB: PDB                                   
REMARK 900 TRUNCATED S. AUREUS LYTM, P 32 2 1 CRYSTAL FORM                      
DBREF  2B0P A  185   316  UNP    O33599   LYTM_STAAU     185    316             
DBREF  2B0P B  185   316  UNP    O33599   LYTM_STAAU     185    316             
SEQRES   1 A  134  MET ALA HIS ALA LYS ASP ALA SER TRP LEU THR SER ARG          
SEQRES   2 A  134  LYS GLN LEU GLN PRO TYR GLY GLN TYR HIS GLY GLY GLY          
SEQRES   3 A  134  ALA HIS TYR GLY VAL ASP TYR ALA MET PRO GLU ASN SER          
SEQRES   4 A  134  PRO VAL TYR SER LEU THR ASP GLY THR VAL VAL GLN ALA          
SEQRES   5 A  134  GLY TRP SER ASN TYR GLY GLY GLY ASN GLN VAL THR ILE          
SEQRES   6 A  134  LYS GLU ALA ASN SER ASN ASN TYR GLN TRP TYR MET HIS          
SEQRES   7 A  134  ASN ASN ARG LEU THR VAL SER ALA GLY ASP LYS VAL LYS          
SEQRES   8 A  134  ALA GLY ASP GLN ILE ALA TYR SER GLY SER THR GLY ASN          
SEQRES   9 A  134  SER THR ALA PRO HIS VAL HIS PHE GLN ARG MET SER GLY          
SEQRES  10 A  134  GLY ILE GLY ASN GLN TYR ALA VAL ASP PRO THR SER TYR          
SEQRES  11 A  134  LEU GLN SER ARG                                              
SEQRES   1 B  134  MET ALA HIS ALA LYS ASP ALA SER TRP LEU THR SER ARG          
SEQRES   2 B  134  LYS GLN LEU GLN PRO TYR GLY GLN TYR HIS GLY GLY GLY          
SEQRES   3 B  134  ALA HIS TYR GLY VAL ASP TYR ALA MET PRO GLU ASN SER          
SEQRES   4 B  134  PRO VAL TYR SER LEU THR ASP GLY THR VAL VAL GLN ALA          
SEQRES   5 B  134  GLY TRP SER ASN TYR GLY GLY GLY ASN GLN VAL THR ILE          
SEQRES   6 B  134  LYS GLU ALA ASN SER ASN ASN TYR GLN TRP TYR MET HIS          
SEQRES   7 B  134  ASN ASN ARG LEU THR VAL SER ALA GLY ASP LYS VAL LYS          
SEQRES   8 B  134  ALA GLY ASP GLN ILE ALA TYR SER GLY SER THR GLY ASN          
SEQRES   9 B  134  SER THR ALA PRO HIS VAL HIS PHE GLN ARG MET SER GLY          
SEQRES  10 B  134  GLY ILE GLY ASN GLN TYR ALA VAL ASP PRO THR SER TYR          
SEQRES  11 B  134  LEU GLN SER ARG                                              
HET     ZN  A 400       1                                                       
HET    CAC  A 500       5                                                       
HET    ACT  A 700       4                                                       
HET    ACT  A 702       4                                                       
HET     ZN  B 401       1                                                       
HET    CAC  B 501       5                                                       
HET    ACT  B 701       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     CAC CACODYLATE ION                                                   
HETNAM     ACT ACETATE ION                                                      
HETSYN     CAC DIMETHYLARSINATE                                                 
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  CAC    2(C2 H6 AS O2 1-)                                            
FORMUL   5  ACT    3(C2 H3 O2 1-)                                               
FORMUL  10  HOH   *385(H2 O)                                                    
HELIX    1   1 ALA A  189  SER A  194  1                                   6    
HELIX    2   2 GLY A  302  GLN A  304  5                                   3    
HELIX    3   3 PRO A  309  ARG A  316  1                                   8    
HELIX    4   4 ALA B  189  SER B  194  1                                   6    
HELIX    5   5 GLY B  302  GLN B  304  5                                   3    
HELIX    6   6 PRO B  309  SER B  315  1                                   7    
SHEET    1   A 7 GLN A 197  GLN A 199  0                                        
SHEET    2   A 7 VAL A 213  ALA A 216 -1  O  ASP A 214   N  GLN A 199           
SHEET    3   A 7 HIS A 291  SER A 298 -1  O  VAL A 292   N  TYR A 215           
SHEET    4   A 7 ASN A 254  ASN A 261 -1  N  TYR A 255   O  MET A 297           
SHEET    5   A 7 GLY A 242  GLU A 249 -1  N  GLU A 249   O  ASN A 254           
SHEET    6   A 7 GLY A 229  SER A 237 -1  N  THR A 230   O  LYS A 248           
SHEET    7   A 7 LYS A 271  VAL A 272 -1  O  VAL A 272   N  GLY A 229           
SHEET    1   B 4 GLN A 197  GLN A 199  0                                        
SHEET    2   B 4 VAL A 213  ALA A 216 -1  O  ASP A 214   N  GLN A 199           
SHEET    3   B 4 HIS A 291  SER A 298 -1  O  VAL A 292   N  TYR A 215           
SHEET    4   B 4 ALA A 306  VAL A 307 -1  O  VAL A 307   N  ARG A 296           
SHEET    1   C 2 GLY A 202  GLN A 203  0                                        
SHEET    2   C 2 ALA A 209  HIS A 210 -1  O  HIS A 210   N  GLY A 202           
SHEET    1   D 2 PRO A 222  TYR A 224  0                                        
SHEET    2   D 2 GLN A 277  TYR A 280 -1  O  ILE A 278   N  VAL A 223           
SHEET    1   E 7 GLN B 197  GLN B 199  0                                        
SHEET    2   E 7 VAL B 213  ALA B 216 -1  O  ASP B 214   N  GLN B 199           
SHEET    3   E 7 HIS B 291  SER B 298 -1  O  VAL B 292   N  TYR B 215           
SHEET    4   E 7 ASN B 254  ASN B 261 -1  N  TYR B 255   O  MET B 297           
SHEET    5   E 7 GLY B 242  GLU B 249 -1  N  GLU B 249   O  ASN B 254           
SHEET    6   E 7 GLY B 229  SER B 237 -1  N  THR B 230   O  LYS B 248           
SHEET    7   E 7 LYS B 271  VAL B 272 -1  O  VAL B 272   N  GLY B 229           
SHEET    1   F 4 GLN B 197  GLN B 199  0                                        
SHEET    2   F 4 VAL B 213  ALA B 216 -1  O  ASP B 214   N  GLN B 199           
SHEET    3   F 4 HIS B 291  SER B 298 -1  O  VAL B 292   N  TYR B 215           
SHEET    4   F 4 ALA B 306  VAL B 307 -1  O  VAL B 307   N  ARG B 296           
SHEET    1   G 2 GLY B 202  GLN B 203  0                                        
SHEET    2   G 2 ALA B 209  HIS B 210 -1  O  HIS B 210   N  GLY B 202           
SHEET    1   H 2 PRO B 222  TYR B 224  0                                        
SHEET    2   H 2 GLN B 277  TYR B 280 -1  O  ALA B 279   N  VAL B 223           
LINK         NE2 HIS A 210                ZN    ZN A 400     1555   1555  2.08  
LINK         OD1 ASP A 214                ZN    ZN A 400     1555   1555  1.99  
LINK         ND1 HIS A 293                ZN    ZN A 400     1555   1555  2.12  
LINK        ZN    ZN A 400                 O2  CAC A 500     1555   1555  1.95  
LINK         NE2 HIS B 210                ZN    ZN B 401     1555   1555  2.10  
LINK         OD1 ASP B 214                ZN    ZN B 401     1555   1555  2.05  
LINK         ND1 HIS B 293                ZN    ZN B 401     1555   1555  2.06  
LINK        ZN    ZN B 401                 O2  CAC B 501     1555   1555  1.88  
SITE     1 AC1  4 HIS A 210  ASP A 214  HIS A 293  CAC A 500                    
SITE     1 AC2  8 TYR A 204  HIS A 210  ASP A 214  HIS A 260                    
SITE     2 AC2  8 ASN A 286  HIS A 291  HIS A 293   ZN A 400                    
SITE     1 AC3  3 ASN A 220  ARG A 263  HOH A 716                               
SITE     1 AC4  6 LYS A 248  ALA A 250  ASN A 251  HOH A 731                    
SITE     2 AC4  6 HOH A 778  SER B 311                                          
SITE     1 AC5  4 HIS B 210  ASP B 214  HIS B 293  CAC B 501                    
SITE     1 AC6  8 TYR B 204  HIS B 210  ASP B 214  HIS B 260                    
SITE     2 AC6  8 ASN B 286  HIS B 291  HIS B 293   ZN B 401                    
SITE     1 AC7  5 ASN B 220  ARG B 263  TYR B 280  HOH B 719                    
SITE     2 AC7  5 HOH B 832                                                     
CRYST1   32.093   78.261  102.049  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      0.031159  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012778  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009799        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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