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LongText Report for: 2B61-pdb

Name Class
2B61-pdb
HEADER    TRANSFERASE                             29-SEP-05   2B61              
TITLE     CRYSTAL STRUCTURE OF HOMOSERINE TRANSACETYLASE                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HOMOSERINE O-ACETYLTRANSFERASE;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HOMOSERINE O-TRANS-ACETYLASE, HOMOSERINE                    
COMPND   5 TRANSACETYLASE, HTA;                                                 
COMPND   6 EC: 2.3.1.31;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;                         
SOURCE   3 ORGANISM_COMMON: BACTERIA;                                           
SOURCE   4 GENE: METX, MET2;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BACTERIA;                                  
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28+HOM2                                
KEYWDS    ACYL-ENZYME, ASPARTATE PATHWAY, COENZYME A, STRUCTURE-                
KEYWDS   2 FUNCTION STUDIES, ALPHA-BETA HYDROLASE FOLD                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.A.MIRZA,I.NAZI,M.KORCZYNSKA,G.D.WRIGHT,A.M.BERGHUIS                 
REVDAT   1   15-NOV-05 2B61    0                                                
JRNL        AUTH   I.A.MIRZA,I.NAZI,M.KORCZYNSKA,G.D.WRIGHT,                    
JRNL        AUTH 2 A.M.BERGHUIS                                                 
JRNL        TITL   CRYSTAL STRUCTURE OF HOMOSERINE TRANSACETYLASE               
JRNL        TITL 2 FROM HAEMOPHILUS INFLUENZAE REVEALS A NEW FAMILY             
JRNL        TITL 3 OF ALPHA/BETA-HYDROLASES.                                    
JRNL        REF    BIOCHEMISTRY                               2005              
JRNL        REFN   ASTM BICHAW  US ISSN 0006-2960                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.65 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 57586                          
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) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.187                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3071                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4195                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.51                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1980                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 243                          
REMARK   3   BIN FREE R VALUE                    : 0.2240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 3272                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.38000                                              
REMARK   3    B22 (A**2) : 0.38000                                              
REMARK   3    B33 (A**2) : -0.58000                                             
REMARK   3    B12 (A**2) : 0.19000                                              
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): 0.075         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.075         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.044         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.243         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.960                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2921 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3965 ; 1.155 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   364 ; 5.482 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   145 ;37.289 ;24.621       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   468 ;12.244 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ; 6.180 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   417 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2293 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1387 ; 0.191 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2053 ; 0.311 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   327 ; 0.113 ; 0.200       
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):    54 ; 0.147 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    29 ; 0.141 ; 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):  1837 ; 0.841 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2866 ; 1.247 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1251 ; 2.038 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1099 ; 2.926 ; 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 : 0                                 
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 0                                          
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2B61 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-OCT-2005.                
REMARK 100 THE RCSB ID CODE IS RCSB034718.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-AUG-2005                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X8C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97880                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CBASS                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57586                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, HEPES, PH 7.5, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 323K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,1/3+Z                                            
REMARK 290       3555   -X+Y,-X,2/3+Z                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,2/3-Z                                            
REMARK 290       6555   -X,-X+Y,1/3-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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.08767            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       80.17533            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       80.17533            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       40.08767            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR                     
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 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   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       40.08767            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH   386   LIES ON A SPECIAL POSITION.                         
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     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     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                             
REMARK 500   O    HOH     188     O    HOH     440              1.97            
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: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 273   CA  -  CB  -  CG  ANGL. DEV. =  7.2 DEGREES           
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE IS OBTAINED FROM WILD TYPE H.INFLUENZAE 49824           
REMARK 999 AND THE CONFLICTS ARE DUE TO DIFFERENT STRAIN.                       
DBREF  2B61 A    1   358  GB     53732708 ZP_00154944      1    358             
SEQADV 2B61 GLY A  -18  GB   53732708            CLONING ARTIFACT               
SEQADV 2B61 SER A  -17  GB   53732708            CLONING ARTIFACT               
SEQADV 2B61 SER A  -16  GB   53732708            CLONING ARTIFACT               
SEQADV 2B61 HIS A  -15  GB   53732708            HIS TAG                        
SEQADV 2B61 HIS A  -14  GB   53732708            HIS TAG                        
SEQADV 2B61 HIS A  -13  GB   53732708            HIS TAG                        
SEQADV 2B61 HIS A  -12  GB   53732708            HIS TAG                        
SEQADV 2B61 HIS A  -11  GB   53732708            HIS TAG                        
SEQADV 2B61 HIS A  -10  GB   53732708            HIS TAG                        
SEQADV 2B61 SER A   -9  GB   53732708            CLONING ARTIFACT               
SEQADV 2B61 SER A   -8  GB   53732708            CLONING ARTIFACT               
SEQADV 2B61 GLY A   -7  GB   53732708            CLONING ARTIFACT               
SEQADV 2B61 LEU A   -6  GB   53732708            CLONING ARTIFACT               
SEQADV 2B61 VAL A   -5  GB   53732708            CLONING ARTIFACT               
SEQADV 2B61 PRO A   -4  GB   53732708            CLONING ARTIFACT               
SEQADV 2B61 ARG A   -3  GB   53732708            CLONING ARTIFACT               
SEQADV 2B61 GLY A   -2  GB   53732708            CLONING ARTIFACT               
SEQADV 2B61 SER A   -1  GB   53732708            CLONING ARTIFACT               
SEQADV 2B61 HIS A    0  GB   53732708            CLONING ARTIFACT               
SEQADV 2B61 MSE A   17  GB   53732708  MET    17 MODIFIED RESIDUE               
SEQADV 2B61 MSE A   69  GB   53732708  MET    69 MODIFIED RESIDUE               
SEQADV 2B61 GLU A  129  GB   53732708  ASP   129 SEE REMARK 999                 
SEQADV 2B61 ILE A  133  GB   53732708  VAL   133 SEE REMARK 999                 
SEQADV 2B61 MSE A  147  GB   53732708  MET   147 MODIFIED RESIDUE               
SEQADV 2B61 MSE A  160  GB   53732708  MET   160 MODIFIED RESIDUE               
SEQADV 2B61 MSE A  183  GB   53732708  MET   183 MODIFIED RESIDUE               
SEQADV 2B61 MSE A  213  GB   53732708  MET   213 MODIFIED RESIDUE               
SEQADV 2B61 MSE A  216  GB   53732708  MET   216 MODIFIED RESIDUE               
SEQADV 2B61 MSE A  275  GB   53732708  MET   275 MODIFIED RESIDUE               
SEQADV 2B61 GLU A  283  GB   53732708  ASP   283 SEE REMARK 999                 
SEQRES   1 A  377  GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 A  377  VAL PRO ARG GLY SER HIS MET SER VAL GLN ASN VAL VAL          
SEQRES   3 A  377  LEU PHE ASP THR GLN PRO LEU THR LEU MSE LEU GLY GLY          
SEQRES   4 A  377  LYS LEU SER TYR ILE ASN VAL ALA TYR GLN THR TYR GLY          
SEQRES   5 A  377  THR LEU ASN ASP GLU LYS ASN ASN ALA VAL LEU ILE CYS          
SEQRES   6 A  377  HIS ALA LEU THR GLY ASP ALA GLU PRO TYR PHE ASP ASP          
SEQRES   7 A  377  GLY ARG ASP GLY TRP TRP GLN ASN PHE MSE GLY ALA GLY          
SEQRES   8 A  377  LEU ALA LEU ASP THR ASP ARG TYR PHE PHE ILE SER SER          
SEQRES   9 A  377  ASN VAL LEU GLY GLY CYS LYS GLY THR THR GLY PRO SER          
SEQRES  10 A  377  SER ILE ASN PRO GLN THR GLY LYS PRO TYR GLY SER GLN          
SEQRES  11 A  377  PHE PRO ASN ILE VAL VAL GLN ASP ILE VAL LYS VAL GLN          
SEQRES  12 A  377  LYS ALA LEU LEU GLU HIS LEU GLY ILE SER HIS LEU LYS          
SEQRES  13 A  377  ALA ILE ILE GLY GLY SER PHE GLY GLY MSE GLN ALA ASN          
SEQRES  14 A  377  GLN TRP ALA ILE ASP TYR PRO ASP PHE MSE ASP ASN ILE          
SEQRES  15 A  377  VAL ASN LEU CYS SER SER ILE TYR PHE SER ALA GLU ALA          
SEQRES  16 A  377  ILE GLY PHE ASN HIS VAL MSE ARG GLN ALA VAL ILE ASN          
SEQRES  17 A  377  ASP PRO ASN PHE ASN GLY GLY ASP TYR TYR GLU GLY THR          
SEQRES  18 A  377  PRO PRO ASP GLN GLY LEU SER ILE ALA ARG MSE LEU GLY          
SEQRES  19 A  377  MSE LEU THR TYR ARG THR ASP LEU GLN LEU ALA LYS ALA          
SEQRES  20 A  377  PHE GLY ARG ALA THR LYS SER ASP GLY SER PHE TRP GLY          
SEQRES  21 A  377  ASP TYR PHE GLN VAL GLU SER TYR LEU SER TYR GLN GLY          
SEQRES  22 A  377  LYS LYS PHE LEU GLU ARG PHE ASP ALA ASN SER TYR LEU          
SEQRES  23 A  377  HIS LEU LEU ARG ALA LEU ASP MSE TYR ASP PRO SER LEU          
SEQRES  24 A  377  GLY TYR GLU ASN VAL LYS GLU ALA LEU SER ARG ILE LYS          
SEQRES  25 A  377  ALA ARG TYR THR LEU VAL SER VAL THR THR ASP GLN LEU          
SEQRES  26 A  377  PHE LYS PRO ILE ASP LEU TYR LYS SER LYS GLN LEU LEU          
SEQRES  27 A  377  GLU GLN SER GLY VAL ASP LEU HIS PHE TYR GLU PHE PRO          
SEQRES  28 A  377  SER ASP TYR GLY HIS ASP ALA PHE LEU VAL ASP TYR ASP          
SEQRES  29 A  377  GLN PHE GLU LYS ARG ILE ARG ASP GLY LEU ALA GLY ASN          
MODRES 2B61 MSE A   17  MET  SELENOMETHIONINE                                   
MODRES 2B61 MSE A   69  MET  SELENOMETHIONINE                                   
MODRES 2B61 MSE A  147  MET  SELENOMETHIONINE                                   
MODRES 2B61 MSE A  160  MET  SELENOMETHIONINE                                   
MODRES 2B61 MSE A  183  MET  SELENOMETHIONINE                                   
MODRES 2B61 MSE A  213  MET  SELENOMETHIONINE                                   
MODRES 2B61 MSE A  216  MET  SELENOMETHIONINE                                   
MODRES 2B61 MSE A  275  MET  SELENOMETHIONINE                                   
HET    MSE  A  17       8                                                       
HET    MSE  A  69       8                                                       
HET    MSE  A 147       8                                                       
HET    MSE  A 160       8                                                       
HET    MSE  A 183       8                                                       
HET    MSE  A 213       8                                                       
HET    MSE  A 216       8                                                       
HET    MSE  A 275       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    8(C5 H11 N1 O2 SE1)                                          
FORMUL   2  HOH   *425(H2 O1)                                                   
HELIX    1   1 TRP A   65  ASN A   67  5                                   3    
HELIX    2   2 TYR A  108  PHE A  112  5                                   5    
HELIX    3   3 VAL A  116  LEU A  131  1                                  16    
HELIX    4   4 SER A  143  TYR A  156  1                                  14    
HELIX    5   5 SER A  173  ASN A  189  1                                  17    
HELIX    6   6 PHE A  193  ASP A  197  5                                   5    
HELIX    7   7 PRO A  204  ARG A  220  1                                  17    
HELIX    8   8 THR A  221  PHE A  229  1                                   9    
HELIX    9   9 PHE A  244  GLU A  259  1                                  16    
HELIX   10  10 ASP A  262  TYR A  276  1                                  15    
HELIX   11  11 ASN A  284  SER A  290  1                                   7    
HELIX   12  12 LYS A  308  SER A  322  1                                  15    
HELIX   13  13 TYR A  335  HIS A  337  5                                   3    
HELIX   14  14 ASP A  338  ASP A  343  1                                   6    
HELIX   15  15 ASP A  343  GLY A  357  1                                  15    
SHEET    1   A 8 GLN A   4  LEU A   8  0                                        
SHEET    2   A 8 ILE A  25  TYR A  32 -1  O  ILE A  25   N  LEU A   8           
SHEET    3   A 8 PHE A  81  SER A  85 -1  O  SER A  84   N  GLN A  30           
SHEET    4   A 8 ALA A  42  CYS A  46  1  N  ILE A  45   O  ILE A  83           
SHEET    5   A 8 LEU A 136  GLY A 142  1  O  ILE A 140   N  LEU A  44           
SHEET    6   A 8 MSE A 160  LEU A 166  1  O  VAL A 164   N  ILE A 139           
SHEET    7   A 8 ARG A 295  VAL A 301  1  O  THR A 297   N  ILE A 163           
SHEET    8   A 8 ASP A 325  PHE A 331  1  O  TYR A 329   N  SER A 300           
SHEET    1   B 2 LEU A  14  THR A  15  0                                        
SHEET    2   B 2 LYS A  21  LEU A  22 -1  O  LEU A  22   N  LEU A  14           
SHEET    1   C 2 MSE A  69  GLY A  70  0                                        
SHEET    2   C 2 LEU A  75  ASP A  76  1  O  LEU A  75   N  GLY A  70           
CRYST1   85.264   85.264  120.263  90.00  90.00 120.00 P 31 2 1      6          
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      0.011730  0.006770  0.000000        0.00000                         
SCALE2      0.000000  0.013540  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008310        0.00000                         
TER    2848      ASN A 358                                                      
MASTER      298    0    8   15   12    0    0    6 3272    1   64   29          
END                                                                             

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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.
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