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LongText Report for: 6vap-pdb

Name Class
6vap-pdb
HEADER    BIOSYNTHETIC PROTEIN                    17-DEC-19   6VAP              
TITLE     STRUCTURE OF THE TYPE II THIOESTERASE BORB FROM THE BORRELIDIN        
TITLE    2 BIOSYNTHETIC CLUSTER                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THIOESTERASE;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES SP. WAC02707;                      
SOURCE   3 ORGANISM_TAXID: 2487417;                                             
SOURCE   4 GENE: EF919_13485;                                                   
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    THIOESTERASE, BIOSYNTHETIC PROTEIN                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.H.PEREIRA,S.C.CURRAN,M.-J.BALUYOT,J.LAKE,H.PUTZ,D.ROSENBURG,        
AUTHOR   2 J.KEASLING,P.D.ADAMS                                                 
REVDAT   1   06-MAY-20 6VAP    0                                                
JRNL        AUTH   S.C.CURRAN,J.H.PEREIRA,M.J.BALUYOT,J.LAKE,H.PUETZ,           
JRNL        AUTH 2 D.J.ROSENBURG,P.ADAMS,J.D.KEASLING                           
JRNL        TITL   STRUCTURE AND FUNCTION OF BORB, THE TYPE II THIOESTERASE     
JRNL        TITL 2 FROM THE BORRELIDIN BIOSYNTHETIC GENE CLUSTER.               
JRNL        REF    BIOCHEMISTRY                               2020              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   32250597                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.0C00126                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.93 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.17.1_3660                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.93                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.18                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 37938                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.960                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1883                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.1800 -  4.5400    1.00     2939   149  0.1791 0.2162        
REMARK   3     2  4.5400 -  3.6000    1.00     2830   159  0.1649 0.1842        
REMARK   3     3  3.6000 -  3.1500    1.00     2824   135  0.1774 0.2394        
REMARK   3     4  3.1500 -  2.8600    1.00     2805   142  0.1933 0.2175        
REMARK   3     5  2.8600 -  2.6500    1.00     2742   170  0.2040 0.2525        
REMARK   3     6  2.6500 -  2.5000    1.00     2805   126  0.1967 0.2262        
REMARK   3     7  2.5000 -  2.3700    1.00     2762   138  0.2004 0.2201        
REMARK   3     8  2.3700 -  2.2700    0.99     2737   145  0.2250 0.3020        
REMARK   3     9  2.2700 -  2.1800    0.96     2656   145  0.4217 0.4858        
REMARK   3    10  2.1800 -  2.1100    0.99     2737   147  0.2366 0.2956        
REMARK   3    11  2.1100 -  2.0400    0.99     2765   136  0.2535 0.2757        
REMARK   3    12  2.0400 -  1.9800    0.99     2733   147  0.2724 0.3382        
REMARK   3    13  1.9800 -  1.9300    0.99     2720   144  0.3923 0.4514        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.302            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.312           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.26                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.68                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011           3846                                  
REMARK   3   ANGLE     :  0.983           5240                                  
REMARK   3   CHIRALITY :  0.055            575                                  
REMARK   3   PLANARITY :  0.008            698                                  
REMARK   3   DIHEDRAL  : 19.777           1419                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6VAP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-DEC-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000246099.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-OCT-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39997                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.890                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.230                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY                : 8.000                              
REMARK 200  R MERGE                    (I) : 0.14300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.0700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.96                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 3FLA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE, 0.1 M HEPES    
REMARK 280  PH 7.5, 22% POLY (ACRYLIC ACID SODIUM SALT) 5100, VAPOR             
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.07000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.07000            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       36.22500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.18000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       36.22500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.18000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       75.07000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       36.22500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       46.18000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       75.07000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       36.22500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       46.18000            
REMARK 290   SMTRY3   8  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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 B 338  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 377  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     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     MET A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     ASN A     7                                                      
REMARK 465     THR A   152                                                      
REMARK 465     LEU A   153                                                      
REMARK 465     ASP A   154                                                      
REMARK 465     GLY A   155                                                      
REMARK 465     THR A   156                                                      
REMARK 465     ALA A   157                                                      
REMARK 465     GLU A   158                                                      
REMARK 465     GLN A   159                                                      
REMARK 465     VAL A   160                                                      
REMARK 465     PHE A   161                                                      
REMARK 465     HIS A   162                                                      
REMARK 465     ASP A   163                                                      
REMARK 465     GLU A   164                                                      
REMARK 465     GLU A   165                                                      
REMARK 465     ALA A   256                                                      
REMARK 465     PRO A   257                                                      
REMARK 465     GLY A   258                                                      
REMARK 465     ASP A   259                                                      
REMARK 465     ARG A   260                                                      
REMARK 465     SER A   261                                                      
REMARK 465     GLY A   262                                                      
REMARK 465     LEU A   263                                                      
REMARK 465     THR A   264                                                      
REMARK 465     ARG A   265                                                      
REMARK 465     GLU A   266                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     HIS B     2                                                      
REMARK 465     MET B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     THR B     6                                                      
REMARK 465     THR B   252                                                      
REMARK 465     CYS B   253                                                      
REMARK 465     SER B   254                                                      
REMARK 465     ARG B   255                                                      
REMARK 465     ALA B   256                                                      
REMARK 465     PRO B   257                                                      
REMARK 465     GLY B   258                                                      
REMARK 465     ASP B   259                                                      
REMARK 465     ARG B   260                                                      
REMARK 465     SER B   261                                                      
REMARK 465     GLY B   262                                                      
REMARK 465     LEU B   263                                                      
REMARK 465     THR B   264                                                      
REMARK 465     ARG B   265                                                      
REMARK 465     GLU B   266                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 194   C     PRO A 195   N       0.161                       
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    GLN A  62     -120.63     52.71                                   
REMARK 500    SER A  98     -121.67     56.23                                   
REMARK 500    GLN B  62     -130.21     54.40                                   
REMARK 500    SER B  98     -125.49     52.05                                   
REMARK 500    LEU B 153      -38.76     65.68                                   
REMARK 500    ALA B 157     -157.39   -105.10                                   
REMARK 500    GLU B 158       56.21   -113.16                                   
REMARK 500    GLN B 159       92.11    103.09                                   
REMARK 500    VAL B 160      -66.76   -104.02                                   
REMARK 500    PHE B 161       72.54   -102.60                                   
REMARK 500    ASP B 163       74.80    -68.50                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 476        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH A 477        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH A 478        DISTANCE =  7.21 ANGSTROMS                       
REMARK 525    HOH B 488        DISTANCE =  6.39 ANGSTROMS                       
DBREF1 6VAP A    3   266  UNP                  A0A454WD44_9ACTN                 
DBREF2 6VAP A     A0A454WD44                          1         264             
DBREF1 6VAP B    3   266  UNP                  A0A454WD44_9ACTN                 
DBREF2 6VAP B     A0A454WD44                          1         264             
SEQADV 6VAP GLY A    1  UNP  A0A454WD4           EXPRESSION TAG                 
SEQADV 6VAP HIS A    2  UNP  A0A454WD4           EXPRESSION TAG                 
SEQADV 6VAP GLY B    1  UNP  A0A454WD4           EXPRESSION TAG                 
SEQADV 6VAP HIS B    2  UNP  A0A454WD4           EXPRESSION TAG                 
SEQRES   1 A  266  GLY HIS MET THR GLY THR ASN THR HIS SER ASP VAL TRP          
SEQRES   2 A  266  ILE ARG GLN TYR ARG PRO ALA HIS PRO THR ALA PRO GLN          
SEQRES   3 A  266  LEU ILE CYS LEU PRO HIS ALA GLY GLY SER ALA THR PHE          
SEQRES   4 A  266  TYR HIS PRO VAL ALA ALA ALA LEU ALA PRO ARG CYS ASP          
SEQRES   5 A  266  VAL LEU ALA VAL GLN TYR PRO GLY ARG GLN ASP ARG ARG          
SEQRES   6 A  266  ALA GLU LYS PRO LEU GLU ASP ILE ASP GLU LEU ALA ASN          
SEQRES   7 A  266  GLN LEU PHE PRO VAL LEU ARG ALA ARG VAL HIS GLN PRO          
SEQRES   8 A  266  VAL ALA LEU PHE GLY HIS SER MET GLY ALA THR LEU ALA          
SEQRES   9 A  266  PHE GLU LEU ALA ARG ARG PHE GLU SER ALA GLY ILE SER          
SEQRES  10 A  266  LEU GLU ALA LEU LEU VAL SER ALA ARG PRO ALA PRO SER          
SEQRES  11 A  266  ARG GLN ARG THR GLY GLY THR VAL HIS LEU LEU SER ASP          
SEQRES  12 A  266  GLU GLU LEU VAL ALA GLU LEU ARG THR LEU ASP GLY THR          
SEQRES  13 A  266  ALA GLU GLN VAL PHE HIS ASP GLU GLU LEU VAL ARG MET          
SEQRES  14 A  266  ALA LEU PRO ALA ILE ARG GLY ASP TYR ARG ALA ALA GLU          
SEQRES  15 A  266  THR TYR ARG TYR ARG PRO GLY PRO LYS LEU ARG CYS PRO          
SEQRES  16 A  266  ILE HIS ALA LEU THR GLY ASP ASP ASP PRO MET VAL THR          
SEQRES  17 A  266  PRO VAL GLU ALA ARG ALA TRP SER GLU HIS THR ASP GLY          
SEQRES  18 A  266  PRO PHE THR LEU ASP THR PHE ALA GLY GLY HIS PHE TYR          
SEQRES  19 A  266  LEU LEU GLU HIS ARG ASP ALA ILE LEU GLY ILE ILE ALA          
SEQRES  20 A  266  GLU HIS LEU ARG THR CYS SER ARG ALA PRO GLY ASP ARG          
SEQRES  21 A  266  SER GLY LEU THR ARG GLU                                      
SEQRES   1 B  266  GLY HIS MET THR GLY THR ASN THR HIS SER ASP VAL TRP          
SEQRES   2 B  266  ILE ARG GLN TYR ARG PRO ALA HIS PRO THR ALA PRO GLN          
SEQRES   3 B  266  LEU ILE CYS LEU PRO HIS ALA GLY GLY SER ALA THR PHE          
SEQRES   4 B  266  TYR HIS PRO VAL ALA ALA ALA LEU ALA PRO ARG CYS ASP          
SEQRES   5 B  266  VAL LEU ALA VAL GLN TYR PRO GLY ARG GLN ASP ARG ARG          
SEQRES   6 B  266  ALA GLU LYS PRO LEU GLU ASP ILE ASP GLU LEU ALA ASN          
SEQRES   7 B  266  GLN LEU PHE PRO VAL LEU ARG ALA ARG VAL HIS GLN PRO          
SEQRES   8 B  266  VAL ALA LEU PHE GLY HIS SER MET GLY ALA THR LEU ALA          
SEQRES   9 B  266  PHE GLU LEU ALA ARG ARG PHE GLU SER ALA GLY ILE SER          
SEQRES  10 B  266  LEU GLU ALA LEU LEU VAL SER ALA ARG PRO ALA PRO SER          
SEQRES  11 B  266  ARG GLN ARG THR GLY GLY THR VAL HIS LEU LEU SER ASP          
SEQRES  12 B  266  GLU GLU LEU VAL ALA GLU LEU ARG THR LEU ASP GLY THR          
SEQRES  13 B  266  ALA GLU GLN VAL PHE HIS ASP GLU GLU LEU VAL ARG MET          
SEQRES  14 B  266  ALA LEU PRO ALA ILE ARG GLY ASP TYR ARG ALA ALA GLU          
SEQRES  15 B  266  THR TYR ARG TYR ARG PRO GLY PRO LYS LEU ARG CYS PRO          
SEQRES  16 B  266  ILE HIS ALA LEU THR GLY ASP ASP ASP PRO MET VAL THR          
SEQRES  17 B  266  PRO VAL GLU ALA ARG ALA TRP SER GLU HIS THR ASP GLY          
SEQRES  18 B  266  PRO PHE THR LEU ASP THR PHE ALA GLY GLY HIS PHE TYR          
SEQRES  19 B  266  LEU LEU GLU HIS ARG ASP ALA ILE LEU GLY ILE ILE ALA          
SEQRES  20 B  266  GLU HIS LEU ARG THR CYS SER ARG ALA PRO GLY ASP ARG          
SEQRES  21 B  266  SER GLY LEU THR ARG GLU                                      
FORMUL   3  HOH   *366(H2 O)                                                    
HELIX    1 AA1 SER A   36  PHE A   39  5                                   4    
HELIX    2 AA2 TYR A   40  ALA A   48  1                                   9    
HELIX    3 AA3 ARG A   61  ARG A   65  5                                   5    
HELIX    4 AA4 ASP A   72  VAL A   88  1                                  17    
HELIX    5 AA5 SER A   98  ALA A  114  1                                  17    
HELIX    6 AA6 ALA A  128  GLN A  132  5                                   5    
HELIX    7 AA7 THR A  137  LEU A  141  5                                   5    
HELIX    8 AA8 SER A  142  LEU A  150  1                                   9    
HELIX    9 AA9 VAL A  167  THR A  183  1                                  17    
HELIX   10 AB1 THR A  208  ALA A  214  1                                   7    
HELIX   11 AB2 TRP A  215  THR A  219  5                                   5    
HELIX   12 AB3 PHE A  233  GLU A  237  5                                   5    
HELIX   13 AB4 HIS A  238  ARG A  251  1                                  14    
HELIX   14 AB5 SER B   36  PHE B   39  5                                   4    
HELIX   15 AB6 TYR B   40  ALA B   48  1                                   9    
HELIX   16 AB7 ARG B   61  ARG B   65  5                                   5    
HELIX   17 AB8 ASP B   72  VAL B   88  1                                  17    
HELIX   18 AB9 SER B   98  ALA B  114  1                                  17    
HELIX   19 AC1 ALA B  128  GLN B  132  5                                   5    
HELIX   20 AC2 THR B  137  LEU B  141  5                                   5    
HELIX   21 AC3 SER B  142  GLY B  155  1                                  14    
HELIX   22 AC4 ASP B  163  ALA B  170  1                                   8    
HELIX   23 AC5 ALA B  170  TYR B  184  1                                  15    
HELIX   24 AC6 THR B  208  ALA B  214  1                                   7    
HELIX   25 AC7 TRP B  215  THR B  219  5                                   5    
HELIX   26 AC8 PHE B  233  HIS B  238  1                                   6    
HELIX   27 AC9 HIS B  238  LEU B  250  1                                  13    
SHEET    1 AA1 7 ILE A  14  ARG A  15  0                                        
SHEET    2 AA1 7 ASP A  52  VAL A  56 -1  O  ALA A  55   N  ARG A  15           
SHEET    3 AA1 7 GLN A  26  LEU A  30  1  N  LEU A  27   O  LEU A  54           
SHEET    4 AA1 7 VAL A  92  HIS A  97  1  O  PHE A  95   N  LEU A  30           
SHEET    5 AA1 7 ALA A 120  SER A 124  1  O  LEU A 122   N  LEU A  94           
SHEET    6 AA1 7 ILE A 196  GLY A 201  1  O  HIS A 197   N  LEU A 121           
SHEET    7 AA1 7 PHE A 223  PHE A 228  1  O  THR A 224   N  ALA A 198           
SHEET    1 AA2 7 ILE B  14  ARG B  15  0                                        
SHEET    2 AA2 7 ASP B  52  VAL B  56 -1  O  ALA B  55   N  ARG B  15           
SHEET    3 AA2 7 GLN B  26  LEU B  30  1  N  LEU B  27   O  LEU B  54           
SHEET    4 AA2 7 VAL B  92  HIS B  97  1  O  PHE B  95   N  ILE B  28           
SHEET    5 AA2 7 ALA B 120  SER B 124  1  O  LEU B 122   N  LEU B  94           
SHEET    6 AA2 7 ILE B 196  GLY B 201  1  O  HIS B 197   N  LEU B 121           
SHEET    7 AA2 7 PHE B 223  PHE B 228  1  O  THR B 224   N  ALA B 198           
CISPEP   1 ALA A   48    PRO A   49          0         0.66                     
CISPEP   2 GLN A   90    PRO A   91          0         1.48                     
CISPEP   3 ALA B   48    PRO B   49          0         1.39                     
CISPEP   4 GLN B   90    PRO B   91          0         2.96                     
CRYST1   72.450   92.360  150.140  90.00  90.00  90.00 C 2 2 21     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013803  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010827  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006660        0.00000                         
TER    3639      ARG A 255                                                      
TER    7435      ARG B 251                                                      
MASTER      359    0    0   27   14    0    0    6 4113    2    0   42          
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:
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