Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 4QLO-pdb

Name Class
4QLO-pdb
HEADER    TRANSFERASE                             12-JUN-14   4QLO              
TITLE     CRYSTAL STRUCTURE OF HOMOSERINE O-ACETYLTRANSFERASE FROM              
TITLE    2 STAPHYLOCOCCUS AUREUS                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HOMOSERINE O-ACETYLTRANSFERASE;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.3.1.31;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS;            
SOURCE   3 ORGANISM_TAXID: 451516;                                              
SOURCE   4 STRAIN: TCH1516;                                                     
SOURCE   5 GENE: AZ30_00060, METX, SACOL0012, USA300HOU_0012;                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDEST42                                   
KEYWDS    ROSSMANN FOLD, ACETYLTRANSFERASE, ACETYLCO-A BINDING, TRANSFERASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.THANGAVELU,A.G.PAVLOVSKY,R.E.VIOLA                                  
REVDAT   1   20-AUG-14 4QLO    0                                                
JRNL        AUTH   B.THANGAVELU,A.G.PAVLOVSKY,R.E.VIOLA                         
JRNL        TITL   CRYSTAL STRUCTURE OF HOMOSERINE O-ACETYLTRANSFERASE FROM     
JRNL        TITL 2 STAPHYLOCOCCUS AUREUS                                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
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) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 80.24                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 12155                          
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) : 0.242                           
REMARK   3   R VALUE            (WORKING SET) : 0.240                           
REMARK   3   FREE R VALUE                     : 0.291                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 635                             
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) : 2.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.52                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 561                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 60.68                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3560                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 30                           
REMARK   3   BIN FREE R VALUE                    : 0.2900                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2652                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 28                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.23000                                              
REMARK   3    B22 (A**2) : 2.23000                                              
REMARK   3    B33 (A**2) : -7.23000                                             
REMARK   3    B12 (A**2) : 1.11000                                              
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): 0.853         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.352         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.295         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.646        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2733 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2529 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3708 ; 1.359 ; 1.938       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5790 ; 0.796 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   328 ; 7.500 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   146 ;36.573 ;23.425       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   438 ;17.401 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;17.485 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   393 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3147 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   708 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1309 ; 2.915 ; 5.605       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1308 ; 2.914 ; 5.602       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1635 ; 4.483 ; 8.399       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1636 ; 4.425 ; 8.736       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1424 ; 3.061 ; 6.061       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1425 ; 3.042 ; 6.243       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2073 ; 4.821 ; 9.244       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3122 ; 6.882 ;47.943       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3122 ; 6.878 ;47.954       
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  : NULL                                       
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                                                           
REMARK   4                                                                      
REMARK   4 4QLO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUN-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB086211.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI 111              
REMARK 200  OPTICS                         : HORIZONTALLY AND VERTICALLY        
REMARK 200                                   FOCUSING BIMORPH MIRRORS IN        
REMARK 200                                   KIRKPATRICK-BAEZ CONFIGURATION     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12887                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.15300                            
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) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39000                            
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: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.7 M AMMONIUM FORMATE, 100 MM           
REMARK 280  IMIDAZOLE HYDROCHLORIDE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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      160.47233            
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      320.94467            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      240.70850            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      401.18083            
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       80.23617            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      160.47233            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      320.94467            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      401.18083            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      240.70850            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       80.23617            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
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       80.23617            
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     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     VAL A   330                                                      
REMARK 465     VAL A   331                                                      
REMARK 465     ILE A   332                                                      
REMARK 465     ASN A   333                                                      
REMARK 465     SER A   334                                                      
REMARK 465     LYS A   335                                                      
REMARK 465     LEU A   336                                                      
REMARK 465     GLU A   337                                                      
REMARK 465     GLY A   338                                                      
REMARK 465     LYS A   339                                                      
REMARK 465     PRO A   340                                                      
REMARK 465     ILE A   341                                                      
REMARK 465     PRO A   342                                                      
REMARK 465     ASN A   343                                                      
REMARK 465     PRO A   344                                                      
REMARK 465     LEU A   345                                                      
REMARK 465     LEU A   346                                                      
REMARK 465     GLY A   347                                                      
REMARK 465     LEU A   348                                                      
REMARK 465     ASP A   349                                                      
REMARK 465     SER A   350                                                      
REMARK 465     THR A   351                                                      
REMARK 465     ARG A   352                                                      
REMARK 465     THR A   353                                                      
REMARK 465     GLY A   354                                                      
REMARK 465     HIS A   355                                                      
REMARK 465     HIS A   356                                                      
REMARK 465     HIS A   357                                                      
REMARK 465     HIS A   358                                                      
REMARK 465     HIS A   359                                                      
REMARK 465     HIS A   360                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 198    CG   CD   CE   NZ                                   
REMARK 470     LYS A 283    CG   CD   CE   NZ                                   
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   CG2  THR A   205     OE1  GLU A   208              1.71            
REMARK 500   O    PHE A   326     O    LYS A   329              1.78            
REMARK 500   O    ILE A   116     O    LEU A   119              2.13            
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    TYR A  58       72.39   -119.32                                   
REMARK 500    ASP A 122      -50.48   -136.71                                   
REMARK 500    SER A 197     -128.87    -89.20                                   
REMARK 500    LYS A 198        4.07    -55.42                                   
REMARK 500    PHE A 204     -104.50    -53.29                                   
REMARK 500    ASP A 207      -32.50     94.17                                   
REMARK 500    ASN A 240      111.06   -170.61                                   
REMARK 500    ASN A 293      106.98   -163.22                                   
REMARK 500    LYS A 317       36.27   -171.37                                   
REMARK 500    ASP A 323      -38.97    106.14                                   
REMARK 500    LEU A 327       69.21    -68.48                                   
REMARK 500    TYR A 328       48.13    178.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4QLO A    1   322  UNP    A8YYT5   A8YYT5_STAAT     1    322             
SEQADV 4QLO ASP A  323  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO PRO A  324  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO ALA A  325  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO PHE A  326  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO LEU A  327  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO TYR A  328  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO LYS A  329  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO VAL A  330  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO VAL A  331  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO ILE A  332  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO ASN A  333  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO SER A  334  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO LYS A  335  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO LEU A  336  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO GLU A  337  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO GLY A  338  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO LYS A  339  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO PRO A  340  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO ILE A  341  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO PRO A  342  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO ASN A  343  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO PRO A  344  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO LEU A  345  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO LEU A  346  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO GLY A  347  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO LEU A  348  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO ASP A  349  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO SER A  350  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO THR A  351  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO ARG A  352  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO THR A  353  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO GLY A  354  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO HIS A  355  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO HIS A  356  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO HIS A  357  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO HIS A  358  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO HIS A  359  UNP  A8YYT5              EXPRESSION TAG                 
SEQADV 4QLO HIS A  360  UNP  A8YYT5              EXPRESSION TAG                 
SEQRES   1 A  360  MET THR ASN TYR THR VAL ASP THR LEU ASN LEU GLY GLU          
SEQRES   2 A  360  PHE ILE THR GLU SER GLY GLU VAL ILE ASP ASN LEU ARG          
SEQRES   3 A  360  LEU ARG TYR GLU HIS VAL GLY TYR HIS GLY GLN PRO LEU          
SEQRES   4 A  360  VAL VAL VAL CYS HIS ALA LEU THR GLY ASN HIS LEU THR          
SEQRES   5 A  360  TYR GLY THR ASP ASP TYR PRO GLY TRP TRP ARG GLU ILE          
SEQRES   6 A  360  ILE ASP GLY GLY TYR ILE PRO ILE HIS ASP TYR GLN PHE          
SEQRES   7 A  360  LEU THR PHE ASP VAL ILE GLY SER PRO PHE GLY SER SER          
SEQRES   8 A  360  SER PRO LEU ASN ASP PRO HIS PHE PRO LYS LYS LEU THR          
SEQRES   9 A  360  LEU ARG ASP ILE VAL ARG ALA ASN GLU ARG GLY ILE GLN          
SEQRES  10 A  360  ALA LEU GLY TYR ASP LYS ILE ASN ILE LEU ILE GLY GLY          
SEQRES  11 A  360  SER LEU GLY GLY MET GLN ALA MET GLU LEU LEU TYR ASN          
SEQRES  12 A  360  GLN GLN PHE GLU VAL ASP LYS ALA ILE ILE LEU ALA ALA          
SEQRES  13 A  360  THR SER ARG THR SER SER TYR SER ARG ALA PHE ASN GLU          
SEQRES  14 A  360  ILE ALA ARG GLN ALA ILE HIS LEU GLY GLY LYS GLU GLY          
SEQRES  15 A  360  LEU SER ILE ALA ARG GLN LEU GLY PHE LEU THR TYR ARG          
SEQRES  16 A  360  SER SER LYS SER TYR ASP GLU ARG PHE THR PRO ASP GLU          
SEQRES  17 A  360  VAL VAL ALA TYR GLN GLN HIS GLN GLY ASN LYS PHE LYS          
SEQRES  18 A  360  GLU HIS PHE ASP LEU ASN CYS TYR LEU THR LEU LEU ASP          
SEQRES  19 A  360  VAL LEU ASP SER HIS ASN ILE ASP ARG GLY ARG THR ASP          
SEQRES  20 A  360  VAL THR HIS VAL PHE LYS ASN LEU GLU THR LYS VAL LEU          
SEQRES  21 A  360  THR MET GLY PHE ILE ASP ASP LEU LEU TYR PRO ASP ASP          
SEQRES  22 A  360  GLN VAL ARG ALA LEU GLY GLU ARG PHE LYS TYR HIS ARG          
SEQRES  23 A  360  HIS PHE PHE VAL PRO ASP ASN VAL GLY HIS ASP GLY PHE          
SEQRES  24 A  360  LEU LEU ASN PHE SER THR TRP ALA PRO ASN LEU TYR HIS          
SEQRES  25 A  360  PHE LEU ASN LEU LYS HIS PHE LYS ARG LYS ASP PRO ALA          
SEQRES  26 A  360  PHE LEU TYR LYS VAL VAL ILE ASN SER LYS LEU GLU GLY          
SEQRES  27 A  360  LYS PRO ILE PRO ASN PRO LEU LEU GLY LEU ASP SER THR          
SEQRES  28 A  360  ARG THR GLY HIS HIS HIS HIS HIS HIS                          
FORMUL   2  HOH   *28(H2 O)                                                     
HELIX    1   1 TRP A   62  GLY A   68  1                                   7    
HELIX    2   2 THR A  104  LEU A  119  1                                  16    
HELIX    3   3 SER A  131  GLN A  144  1                                  14    
HELIX    4   4 SER A  161  GLY A  179  1                                  19    
HELIX    5   5 GLY A  179  LEU A  189  1                                  11    
HELIX    6   6 GLY A  190  TYR A  194  5                                   5    
HELIX    7   7 LYS A  198  ARG A  203  1                                   6    
HELIX    8   8 VAL A  209  PHE A  224  1                                  16    
HELIX    9   9 ASP A  225  SER A  238  1                                  14    
HELIX   10  10 ASP A  247  ASN A  254  1                                   8    
HELIX   11  11 PRO A  271  GLU A  280  1                                  10    
HELIX   12  12 GLY A  295  PHE A  299  5                                   5    
HELIX   13  13 ASN A  302  THR A  305  5                                   4    
HELIX   14  14 TRP A  306  ASN A  315  1                                  10    
HELIX   15  15 ASP A  323  LEU A  327  5                                   5    
SHEET    1   A 8 TYR A   4  ASN A  10  0                                        
SHEET    2   A 8 ARG A  26  VAL A  32 -1  O  HIS A  31   N  THR A   5           
SHEET    3   A 8 GLN A  77  PHE A  81 -1  O  PHE A  78   N  VAL A  32           
SHEET    4   A 8 LEU A  39  CYS A  43  1  N  VAL A  40   O  GLN A  77           
SHEET    5   A 8 LYS A 123  GLY A 130  1  O  ILE A 128   N  CYS A  43           
SHEET    6   A 8 GLU A 147  LEU A 154  1  O  LYS A 150   N  ASN A 125           
SHEET    7   A 8 LYS A 258  PHE A 264  1  O  LEU A 260   N  ALA A 151           
SHEET    8   A 8 TYR A 284  VAL A 290  1  O  ARG A 286   N  THR A 261           
SHEET    1   B 2 PHE A  14  ILE A  15  0                                        
SHEET    2   B 2 VAL A  21  ILE A  22 -1  O  ILE A  22   N  PHE A  14           
CISPEP   1 GLY A  130    SER A  131          0        -1.72                     
CISPEP   2 TYR A  328    LYS A  329          0        -6.50                     
CRYST1   49.155   49.155  481.417  90.00  90.00 120.00 P 61 2 2     12          
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      0.020344  0.011746  0.000000        0.00000                         
SCALE2      0.000000  0.023491  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002077        0.00000                         
TER    2661      LYS A 329                                                      
MASTER      371    0    0   15   10    0    0    6 2680    1    0   28          
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
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer