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LongText Report for: 2HFJ-pdb

Name Class
2HFJ-pdb
HEADER    HYDROLASE                               24-JUN-06   2HFJ              
TITLE     PIKROMYCIN THIOESTERASE WITH COVALENT PENTAKETIDE AFFINITY            
TITLE    2 LABEL                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYPE I POLYKETIDE SYNTHASE PIKAIV;                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: THIOESTERASE DOMAIN;                                       
COMPND   5 SYNONYM: PIKROMYCIN;                                                 
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES VENEZUELAE;                        
SOURCE   3 GENE: PIKAIV;                                                        
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_COMMON: BACTERIA;                                  
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS                             
KEYWDS    ALPHA/BETA HYDROLASE, THIOESTERASE                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.L.AKEY,J.D.KITTENDORF,J.W.GIRALDES,R.A.FECIK,D.H.SHERMAN,           
AUTHOR   2 J.L.SMITH                                                            
REVDAT   1   19-SEP-06 2HFJ    0                                                
JRNL        AUTH   D.L.AKEY,J.D.KITTENDORF,J.W.GIRALDES,R.A.FECIK,              
JRNL        AUTH 2 D.H.SHERMAN,J.L.SMITH                                        
JRNL        TITL   STRUCTURAL BASIS FOR MACROLACTONIZATION BY THE               
JRNL        TITL 2 PIKROMYCIN THIOESTERASE                                      
JRNL        REF    NAT.CHEM.BIOL.                V.   2   537 2006              
JRNL        REFN                US ISSN 1548-7091                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.95 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 56330                          
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) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2932                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4040                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.76                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2770                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 203                          
REMARK   3   BIN FREE R VALUE                    : 0.3140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 4703                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.86                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.06000                                             
REMARK   3    B22 (A**2) : -0.95000                                             
REMARK   3    B33 (A**2) : 3.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.140         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.138         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.102         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.520         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4392 ; 0.012 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5997 ; 1.286 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   562 ; 5.373 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   201 ;31.498 ;22.637       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   614 ;14.936 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    43 ;16.091 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   642 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3491 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1937 ; 0.198 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2952 ; 0.302 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   354 ; 0.162 ; 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):    42 ; 0.206 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.117 ; 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):  2873 ; 2.368 ; 3.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4439 ; 3.508 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1707 ; 2.338 ; 3.500       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1558 ; 3.540 ; 5.000       
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 2HFJ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-2006.                
REMARK 100 THE RCSB ID CODE IS RCSB038290.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-APR-2006                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.60                               
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-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97922                            
REMARK 200  MONOCHROMATOR                  : APS BEAMLINE 23ID-D                
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59323                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
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     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07300                            
REMARK 200   FOR THE DATA SET  : 22.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.55900                            
REMARK 200   FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M LI2SO4, 100MM HEPES PH 7.6,         
REMARK 280  80MM MGCL2, 2MM DTT, 5% DMSO, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 296K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   1/2-X,1/2+Y,-Z                                          
REMARK 290       4555   1/2+X,1/2-Y,-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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       53.84300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       65.53150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       53.84300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       65.53150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 2 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, 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    60   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     MET A   -20                                                      
REMARK 465     GLY A   -19                                                      
REMARK 465     SER A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     HIS 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     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     VAL A    -6                                                      
REMARK 465     PRO A    -5                                                      
REMARK 465     ARG A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     ARG A    64                                                      
REMARK 465     ALA A    65                                                      
REMARK 465     THR A   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     THR A   113                                                      
REMARK 465     ILE A   293                                                      
REMARK 465     GLU A   294                                                      
REMARK 465     GLY A   295                                                      
REMARK 465     ALA A   296                                                      
REMARK 465     GLY A   297                                                      
REMARK 465     LYS A   298                                                      
REMARK 465     MET B   -20                                                      
REMARK 465     GLY B   -19                                                      
REMARK 465     SER B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     LEU B    -7                                                      
REMARK 465     VAL B    -6                                                      
REMARK 465     PRO B    -5                                                      
REMARK 465     ARG B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     MET B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     ALA B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     ARG B    64                                                      
REMARK 465     ALA B    65                                                      
REMARK 465     GLY B   110                                                      
REMARK 465     THR B   111                                                      
REMARK 465     GLY B   112                                                      
REMARK 465     THR B   113                                                      
REMARK 465     GLY B   292                                                      
REMARK 465     ILE B   293                                                      
REMARK 465     GLU B   294                                                      
REMARK 465     GLY B   295                                                      
REMARK 465     ALA B   296                                                      
REMARK 465     GLY B   297                                                      
REMARK 465     LYS B   298                                                      
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     410     O    HOH     422              2.11            
REMARK 500   OD1  ASP A   243     O    HOH       4              2.13            
REMARK 500   O    GLY A   138     O    HOH     188              2.17            
REMARK 500   O    HOH     386     O    HOH     423              2.19            
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    ILE B 186   CB  -  CA  -  C   ANGL. DEV. =  7.4 DEGREES           
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MNA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2HFK   RELATED DB: PDB                                   
DBREF  2HFJ A    1   298  UNP    Q9ZGI2   Q9ZGI2_9ACTO  1049   1346             
DBREF  2HFJ B    1   298  UNP    Q9ZGI2   Q9ZGI2_9ACTO  1049   1346             
SEQADV 2HFJ MET A  -20  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ GLY A  -19  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ SER A  -18  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ SER A  -17  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ HIS A  -16  UNP  Q9ZGI2              HIS TAG                        
SEQADV 2HFJ HIS A  -15  UNP  Q9ZGI2              HIS TAG                        
SEQADV 2HFJ HIS A  -14  UNP  Q9ZGI2              HIS TAG                        
SEQADV 2HFJ HIS A  -13  UNP  Q9ZGI2              HIS TAG                        
SEQADV 2HFJ HIS A  -12  UNP  Q9ZGI2              HIS TAG                        
SEQADV 2HFJ HIS A  -11  UNP  Q9ZGI2              HIS TAG                        
SEQADV 2HFJ SER A  -10  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ SER A   -9  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ GLY A   -8  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ LEU A   -7  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ VAL A   -6  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ PRO A   -5  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ ARG A   -4  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ GLY A   -3  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ SER A   -2  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ HIS A   -1  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ MET A    0  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ MET B  -20  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ GLY B  -19  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ SER B  -18  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ SER B  -17  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ HIS B  -16  UNP  Q9ZGI2              HIS TAG                        
SEQADV 2HFJ HIS B  -15  UNP  Q9ZGI2              HIS TAG                        
SEQADV 2HFJ HIS B  -14  UNP  Q9ZGI2              HIS TAG                        
SEQADV 2HFJ HIS B  -13  UNP  Q9ZGI2              HIS TAG                        
SEQADV 2HFJ HIS B  -12  UNP  Q9ZGI2              HIS TAG                        
SEQADV 2HFJ HIS B  -11  UNP  Q9ZGI2              HIS TAG                        
SEQADV 2HFJ SER B  -10  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ SER B   -9  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ GLY B   -8  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ LEU B   -7  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ VAL B   -6  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ PRO B   -5  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ ARG B   -4  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ GLY B   -3  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ SER B   -2  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ HIS B   -1  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQADV 2HFJ MET B    0  UNP  Q9ZGI2              CLONING ARTIFACT               
SEQRES   1 A  319  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  319  LEU VAL PRO ARG GLY SER HIS MET SER GLY ALA ASP THR          
SEQRES   3 A  319  GLY ALA GLY ALA GLY MET PHE ARG ALA LEU PHE ARG GLN          
SEQRES   4 A  319  ALA VAL GLU ASP ASP ARG TYR GLY GLU PHE LEU ASP VAL          
SEQRES   5 A  319  LEU ALA GLU ALA SER ALA PHE ARG PRO GLN PHE ALA SER          
SEQRES   6 A  319  PRO GLU ALA CYS SER GLU ARG LEU ASP PRO VAL LEU LEU          
SEQRES   7 A  319  ALA GLY GLY PRO THR ASP ARG ALA GLU GLY ARG ALA VAL          
SEQRES   8 A  319  LEU VAL GLY CYS THR GLY THR ALA ALA ASN GLY GLY PRO          
SEQRES   9 A  319  HIS GLU PHE LEU ARG LEU SER THR SER PHE GLN GLU GLU          
SEQRES  10 A  319  ARG ASP PHE LEU ALA VAL PRO LEU PRO GLY TYR GLY THR          
SEQRES  11 A  319  GLY THR GLY THR GLY THR ALA LEU LEU PRO ALA ASP LEU          
SEQRES  12 A  319  ASP THR ALA LEU ASP ALA GLN ALA ARG ALA ILE LEU ARG          
SEQRES  13 A  319  ALA ALA GLY ASP ALA PRO VAL VAL LEU LEU GLY HIS SER          
SEQRES  14 A  319  GLY GLY ALA LEU LEU ALA HIS GLU LEU ALA PHE ARG LEU          
SEQRES  15 A  319  GLU ARG ALA HIS GLY ALA PRO PRO ALA GLY ILE VAL LEU          
SEQRES  16 A  319  VAL ASP PRO TYR PRO PRO GLY HIS GLN GLU PRO ILE GLU          
SEQRES  17 A  319  VAL TRP SER ARG GLN LEU GLY GLU GLY LEU PHE ALA GLY          
SEQRES  18 A  319  GLU LEU GLU PRO MET SER ASP ALA ARG LEU LEU ALA MET          
SEQRES  19 A  319  GLY ARG TYR ALA ARG PHE LEU ALA GLY PRO ARG PRO GLY          
SEQRES  20 A  319  ARG SER SER ALA PRO VAL LEU LEU VAL ARG ALA SER GLU          
SEQRES  21 A  319  PRO LEU GLY ASP TRP GLN GLU GLU ARG GLY ASP TRP ARG          
SEQRES  22 A  319  ALA HIS TRP ASP LEU PRO HIS THR VAL ALA ASP VAL PRO          
SEQRES  23 A  319  GLY ASP HIS PHE THR MET MET ARG ASP HIS ALA PRO ALA          
SEQRES  24 A  319  VAL ALA GLU ALA VAL LEU SER TRP LEU ASP ALA ILE GLU          
SEQRES  25 A  319  GLY ILE GLU GLY ALA GLY LYS                                  
SEQRES   1 B  319  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  319  LEU VAL PRO ARG GLY SER HIS MET SER GLY ALA ASP THR          
SEQRES   3 B  319  GLY ALA GLY ALA GLY MET PHE ARG ALA LEU PHE ARG GLN          
SEQRES   4 B  319  ALA VAL GLU ASP ASP ARG TYR GLY GLU PHE LEU ASP VAL          
SEQRES   5 B  319  LEU ALA GLU ALA SER ALA PHE ARG PRO GLN PHE ALA SER          
SEQRES   6 B  319  PRO GLU ALA CYS SER GLU ARG LEU ASP PRO VAL LEU LEU          
SEQRES   7 B  319  ALA GLY GLY PRO THR ASP ARG ALA GLU GLY ARG ALA VAL          
SEQRES   8 B  319  LEU VAL GLY CYS THR GLY THR ALA ALA ASN GLY GLY PRO          
SEQRES   9 B  319  HIS GLU PHE LEU ARG LEU SER THR SER PHE GLN GLU GLU          
SEQRES  10 B  319  ARG ASP PHE LEU ALA VAL PRO LEU PRO GLY TYR GLY THR          
SEQRES  11 B  319  GLY THR GLY THR GLY THR ALA LEU LEU PRO ALA ASP LEU          
SEQRES  12 B  319  ASP THR ALA LEU ASP ALA GLN ALA ARG ALA ILE LEU ARG          
SEQRES  13 B  319  ALA ALA GLY ASP ALA PRO VAL VAL LEU LEU GLY HIS SER          
SEQRES  14 B  319  GLY GLY ALA LEU LEU ALA HIS GLU LEU ALA PHE ARG LEU          
SEQRES  15 B  319  GLU ARG ALA HIS GLY ALA PRO PRO ALA GLY ILE VAL LEU          
SEQRES  16 B  319  VAL ASP PRO TYR PRO PRO GLY HIS GLN GLU PRO ILE GLU          
SEQRES  17 B  319  VAL TRP SER ARG GLN LEU GLY GLU GLY LEU PHE ALA GLY          
SEQRES  18 B  319  GLU LEU GLU PRO MET SER ASP ALA ARG LEU LEU ALA MET          
SEQRES  19 B  319  GLY ARG TYR ALA ARG PHE LEU ALA GLY PRO ARG PRO GLY          
SEQRES  20 B  319  ARG SER SER ALA PRO VAL LEU LEU VAL ARG ALA SER GLU          
SEQRES  21 B  319  PRO LEU GLY ASP TRP GLN GLU GLU ARG GLY ASP TRP ARG          
SEQRES  22 B  319  ALA HIS TRP ASP LEU PRO HIS THR VAL ALA ASP VAL PRO          
SEQRES  23 B  319  GLY ASP HIS PHE THR MET MET ARG ASP HIS ALA PRO ALA          
SEQRES  24 B  319  VAL ALA GLU ALA VAL LEU SER TRP LEU ASP ALA ILE GLU          
SEQRES  25 B  319  GLY ILE GLU GLY ALA GLY LYS                                  
HET    SO4    501       5                                                       
HET    SO4    502       5                                                       
HET    SO4    504       5                                                       
HET     MG    509       1                                                       
HET    DMS    503       4                                                       
HET    DMS   2036       4                                                       
HET    YML  A 448      17                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     YML [(3R,4S,5S,7R)-4,8-DIHYDROXY-3,5,7-TRIMETHYL-2-                  
HETNAM   2 YML  OXOOCTYL]PHOSPHONIC ACID                                        
FORMUL   3  SO4    3(O4 S1 2-)                                                  
FORMUL   6   MG    MG1 2+                                                       
FORMUL   7  DMS    2(C2 H6 O1 S1)                                               
FORMUL   9  YML    C11 H23 O6 P1                                                
FORMUL  10  HOH   *405(H2 O1)                                                   
HELIX    1   1 GLY A   10  ASP A   22  1                                  13    
HELIX    2   2 ARG A   24  ALA A   37  1                                  14    
HELIX    3   3 SER A   44  CYS A   48  5                                   5    
HELIX    4   4 PHE A   86  SER A   92  1                                   7    
HELIX    5   5 ASP A  121  GLY A  138  1                                  18    
HELIX    6   6 SER A  148  HIS A  165  1                                  18    
HELIX    7   7 GLN A  183  TRP A  189  1                                   7    
HELIX    8   8 TRP A  189  GLY A  200  1                                  12    
HELIX    9   9 SER A  206  GLY A  222  1                                  17    
HELIX   10  10 GLN A  245  GLY A  249  5                                   5    
HELIX   11  11 PHE A  269  ASP A  274  1                                   6    
HELIX   12  12 HIS A  275  GLY A  292  1                                  18    
HELIX   13  13 GLY B   10  ASP B   22  1                                  13    
HELIX   14  14 ARG B   24  ALA B   37  1                                  14    
HELIX   15  15 SER B   44  CYS B   48  5                                   5    
HELIX   16  16 PHE B   86  THR B   91  1                                   6    
HELIX   17  17 SER B   92  GLN B   94  5                                   3    
HELIX   18  18 ASP B  121  GLY B  138  1                                  18    
HELIX   19  19 SER B  148  GLY B  166  1                                  19    
HELIX   20  20 GLN B  183  TRP B  189  1                                   7    
HELIX   21  21 TRP B  189  GLY B  200  1                                  12    
HELIX   22  22 SER B  206  GLY B  222  1                                  17    
HELIX   23  23 GLN B  245  GLY B  249  5                                   5    
HELIX   24  24 PHE B  269  ARG B  273  5                                   5    
HELIX   25  25 HIS B  275  GLU B  291  1                                  17    
SHEET    1   A 2 GLN A  41  PHE A  42  0                                        
SHEET    2   A 2 LEU A 118  PRO A 119  1  O  LEU A 118   N  PHE A  42           
SHEET    1   B 7 VAL A  55  ALA A  58  0                                        
SHEET    2   B 7 PHE A  99  VAL A 102 -1  O  PHE A  99   N  LEU A  57           
SHEET    3   B 7 VAL A  70  CYS A  74  1  N  GLY A  73   O  LEU A 100           
SHEET    4   B 7 VAL A 142  HIS A 147  1  O  LEU A 145   N  CYS A  74           
SHEET    5   B 7 GLY A 171  VAL A 175  1  O  VAL A 173   N  LEU A 144           
SHEET    6   B 7 VAL A 232  ALA A 237  1  O  LEU A 233   N  LEU A 174           
SHEET    7   B 7 THR A 260  VAL A 264  1  O  ALA A 262   N  LEU A 234           
SHEET    1   C 2 GLN B  41  PHE B  42  0                                        
SHEET    2   C 2 LEU B 118  PRO B 119  1  O  LEU B 118   N  PHE B  42           
SHEET    1   D 7 VAL B  55  ALA B  58  0                                        
SHEET    2   D 7 PHE B  99  VAL B 102 -1  O  ALA B 101   N  VAL B  55           
SHEET    3   D 7 VAL B  70  CYS B  74  1  N  GLY B  73   O  LEU B 100           
SHEET    4   D 7 VAL B 142  HIS B 147  1  O  LEU B 145   N  CYS B  74           
SHEET    5   D 7 GLY B 171  VAL B 175  1  O  VAL B 173   N  LEU B 144           
SHEET    6   D 7 VAL B 232  ALA B 237  1  O  LEU B 233   N  LEU B 174           
SHEET    7   D 7 THR B 260  VAL B 264  1  O  ALA B 262   N  LEU B 234           
LINK         OG  SER A 148                 P1  YML A 448                        
CISPEP   1 THR B   62    ASP B   63          0        -9.25                     
CRYST1  107.686  131.063   56.864  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009286  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007630  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017586        0.00000                         
TER    2142      GLY A 292                                                      
TER    4259      GLU B 291                                                      
MASTER      353    0    7   25   18    0    0    6 4703    2   41   50          
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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