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LongText Report for: 5tyk-pdb

Name Class
5tyk-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           21-NOV-16   5TYK              
TITLE     ALPHA-ESTERASE-7 IN COMPLEX WITH 3-CHLORO-4-[(2-FLUOROPHENYL)         
TITLE    2 METHOXY]PHENYLBORINIC ACID                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.1.-;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LUCILIA CUPRINA;                                
SOURCE   3 ORGANISM_COMMON: GREEN BOTTLE FLY;                                   
SOURCE   4 ORGANISM_TAXID: 7375;                                                
SOURCE   5 GENE: LCAE7;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CARBOXYLESTERASE, INSECTICIDE RESISTANCE, COVALENT INHIBITOR,         
KEYWDS   2 ORGANOPHOSPHATE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.J.CORREY,C.J.JACKSON                                                
REVDAT   1   06-DEC-17 5TYK    0                                                
JRNL        AUTH   G.J.CORREY,C.J.JACKSON                                       
JRNL        TITL   COMPUTATIONAL DESIGN OF COVALENT CARBOXYLESTERASE INHIBITORS 
JRNL        TITL 2 THAT ABOLISH ORGANOPHOSPHATE INSECTICIDE RESISTANCE          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 64943                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3242                            
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 45.8992 -  4.6910    1.00     2878   153  0.1663 0.1930        
REMARK   3     2  4.6910 -  3.7239    1.00     2753   142  0.1516 0.1854        
REMARK   3     3  3.7239 -  3.2533    1.00     2747   133  0.1656 0.1932        
REMARK   3     4  3.2533 -  2.9559    1.00     2692   150  0.1740 0.2054        
REMARK   3     5  2.9559 -  2.7441    1.00     2741   131  0.1771 0.2052        
REMARK   3     6  2.7441 -  2.5823    1.00     2692   147  0.1857 0.2286        
REMARK   3     7  2.5823 -  2.4530    1.00     2684   130  0.1872 0.2340        
REMARK   3     8  2.4530 -  2.3462    1.00     2697   139  0.1857 0.2437        
REMARK   3     9  2.3462 -  2.2559    1.00     2671   125  0.1891 0.2267        
REMARK   3    10  2.2559 -  2.1781    1.00     2666   147  0.1865 0.1906        
REMARK   3    11  2.1781 -  2.1100    1.00     2704   131  0.1848 0.2228        
REMARK   3    12  2.1100 -  2.0496    1.00     2639   155  0.1945 0.2396        
REMARK   3    13  2.0496 -  1.9957    1.00     2613   139  0.1955 0.2453        
REMARK   3    14  1.9957 -  1.9470    1.00     2689   159  0.1975 0.2775        
REMARK   3    15  1.9470 -  1.9027    1.00     2649   138  0.2145 0.2253        
REMARK   3    16  1.9027 -  1.8622    1.00     2639   138  0.2249 0.2636        
REMARK   3    17  1.8622 -  1.8250    1.00     2692   124  0.2378 0.2931        
REMARK   3    18  1.8250 -  1.7905    1.00     2669   122  0.2507 0.2810        
REMARK   3    19  1.7905 -  1.7586    1.00     2641   148  0.2634 0.3159        
REMARK   3    20  1.7586 -  1.7288    1.00     2659   153  0.2882 0.3076        
REMARK   3    21  1.7288 -  1.7009    1.00     2628   149  0.3011 0.3661        
REMARK   3    22  1.7009 -  1.6747    1.00     2662   148  0.3069 0.3275        
REMARK   3    23  1.6747 -  1.6501    0.99     2596   141  0.3265 0.3446        
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)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.330           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.007           4709                                  
REMARK   3   ANGLE     :  1.094           6375                                  
REMARK   3   CHIRALITY :  0.045            678                                  
REMARK   3   PLANARITY :  0.005            823                                  
REMARK   3   DIHEDRAL  : 13.795           1759                                  
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 5TYK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000225040.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-NOV-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64943                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 14.00                              
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.68                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.90                              
REMARK 200  R MERGE FOR SHELL          (I) : 2.20000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5CH3                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE PH 5.0, 22% PEG    
REMARK 280  550 MME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K            
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      110.90900            
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      110.90900            
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       23.89950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.39600            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       23.89950            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.39600            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      110.90900            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       23.89950            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       50.39600            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      110.90900            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       23.89950            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       50.39600            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 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 A 841  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 966  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    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     PHE A     3                                                      
REMARK 465     ASN A     4                                                      
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   OE1  GLU A   124     O    HOH A   701              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    ALA A    83     ND2  ASN A   523     5545     2.14            
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    SER A   6       79.50   -112.41                                   
REMARK 500    LEU A   7      -56.55      1.73                                   
REMARK 500    SER A 218     -122.82     60.05                                   
REMARK 500    TYR A 350       59.49   -147.09                                   
REMARK 500    PHE A 421      -58.33   -132.62                                   
REMARK 500    HIS A 435       44.66   -142.20                                   
REMARK 500    HIS A 471      129.31    -38.74                                   
REMARK 500    THR A 472       -7.77     81.93                                   
REMARK 500    SER A 542     -142.59   -130.54                                   
REMARK 500    HIS A 566       55.05   -142.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 MET A    8     GLU A    9                  138.49                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7N4 A 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5TYM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5TYJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5TYL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5TYN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5TYO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5TYP   RELATED DB: PDB                                   
DBREF  5TYK A    1   570  UNP    Q25252   Q25252_LUCCU     1    570             
SEQADV 5TYK MET A   -6  UNP  Q25252              INITIATING METHIONINE          
SEQADV 5TYK HIS A   -5  UNP  Q25252              EXPRESSION TAG                 
SEQADV 5TYK HIS A   -4  UNP  Q25252              EXPRESSION TAG                 
SEQADV 5TYK HIS A   -3  UNP  Q25252              EXPRESSION TAG                 
SEQADV 5TYK HIS A   -2  UNP  Q25252              EXPRESSION TAG                 
SEQADV 5TYK HIS A   -1  UNP  Q25252              EXPRESSION TAG                 
SEQADV 5TYK HIS A    0  UNP  Q25252              EXPRESSION TAG                 
SEQADV 5TYK ALA A   83  UNP  Q25252    ASP    83 ENGINEERED MUTATION            
SEQADV 5TYK LEU A  364  UNP  Q25252    MET   364 ENGINEERED MUTATION            
SEQADV 5TYK PHE A  419  UNP  Q25252    ILE   419 ENGINEERED MUTATION            
SEQADV 5TYK THR A  472  UNP  Q25252    ALA   472 ENGINEERED MUTATION            
SEQADV 5TYK THR A  505  UNP  Q25252    ILE   505 ENGINEERED MUTATION            
SEQADV 5TYK GLU A  530  UNP  Q25252    LYS   530 CONFLICT                       
SEQADV 5TYK GLY A  554  UNP  Q25252    ASP   554 ENGINEERED MUTATION            
SEQRES   1 A  577  MET HIS HIS HIS HIS HIS HIS MET ASN PHE ASN VAL SER          
SEQRES   2 A  577  LEU MET GLU LYS LEU LYS TRP LYS ILE LYS CYS ILE GLU          
SEQRES   3 A  577  ASN LYS PHE LEU ASN TYR ARG LEU THR THR ASN GLU THR          
SEQRES   4 A  577  VAL VAL ALA GLU THR GLU TYR GLY LYS VAL LYS GLY VAL          
SEQRES   5 A  577  LYS ARG LEU THR VAL TYR ASP ASP SER TYR TYR SER PHE          
SEQRES   6 A  577  GLU GLY ILE PRO TYR ALA GLN PRO PRO VAL GLY GLU LEU          
SEQRES   7 A  577  ARG PHE LYS ALA PRO GLN ARG PRO THR PRO TRP ALA GLY          
SEQRES   8 A  577  VAL ARG ASP CYS CYS ASN HIS LYS ASP LYS SER VAL GLN          
SEQRES   9 A  577  VAL ASP PHE ILE THR GLY LYS VAL CYS GLY SER GLU ASP          
SEQRES  10 A  577  CYS LEU TYR LEU SER VAL TYR THR ASN ASN LEU ASN PRO          
SEQRES  11 A  577  GLU THR LYS ARG PRO VAL LEU VAL TYR ILE HIS GLY GLY          
SEQRES  12 A  577  GLY PHE ILE ILE GLY GLU ASN HIS ARG ASP MET TYR GLY          
SEQRES  13 A  577  PRO ASP TYR PHE ILE LYS LYS ASP VAL VAL LEU ILE ASN          
SEQRES  14 A  577  ILE GLN TYR ARG LEU GLY ALA LEU GLY PHE LEU SER LEU          
SEQRES  15 A  577  ASN SER GLU ASP LEU ASN VAL PRO GLY ASN ALA GLY LEU          
SEQRES  16 A  577  LYS ASP GLN VAL MET ALA LEU ARG TRP ILE LYS ASN ASN          
SEQRES  17 A  577  CYS ALA ASN PHE GLY GLY ASN PRO ASP ASN ILE THR VAL          
SEQRES  18 A  577  PHE GLY GLU SER ALA GLY ALA ALA SER THR HIS TYR MET          
SEQRES  19 A  577  MET LEU THR GLU GLN THR ARG GLY LEU PHE HIS ARG GLY          
SEQRES  20 A  577  ILE LEU MET SER GLY ASN ALA ILE CYS PRO TRP ALA ASN          
SEQRES  21 A  577  THR GLN CYS GLN HIS ARG ALA PHE THR LEU ALA LYS LEU          
SEQRES  22 A  577  ALA GLY TYR LYS GLY GLU ASP ASN ASP LYS ASP VAL LEU          
SEQRES  23 A  577  GLU PHE LEU MET LYS ALA LYS PRO GLN ASP LEU ILE LYS          
SEQRES  24 A  577  LEU GLU GLU LYS VAL LEU THR LEU GLU GLU ARG THR ASN          
SEQRES  25 A  577  LYS VAL MET PHE PRO PHE GLY PRO THR VAL GLU PRO TYR          
SEQRES  26 A  577  GLN THR ALA ASP CYS VAL LEU PRO LYS HIS PRO ARG GLU          
SEQRES  27 A  577  MET VAL LYS THR ALA TRP GLY ASN SER ILE PRO THR MET          
SEQRES  28 A  577  MET GLY ASN THR SER TYR GLU GLY LEU PHE PHE THR SER          
SEQRES  29 A  577  ILE LEU LYS GLN MET PRO LEU LEU VAL LYS GLU LEU GLU          
SEQRES  30 A  577  THR CYS VAL ASN PHE VAL PRO SER GLU LEU ALA ASP ALA          
SEQRES  31 A  577  GLU ARG THR ALA PRO GLU THR LEU GLU MET GLY ALA LYS          
SEQRES  32 A  577  ILE LYS LYS ALA HIS VAL THR GLY GLU THR PRO THR ALA          
SEQRES  33 A  577  ASP ASN PHE MET ASP LEU CYS SER HIS PHE TYR PHE TRP          
SEQRES  34 A  577  PHE PRO MET HIS ARG LEU LEU GLN LEU ARG PHE ASN HIS          
SEQRES  35 A  577  THR SER GLY THR PRO VAL TYR LEU TYR ARG PHE ASP PHE          
SEQRES  36 A  577  ASP SER GLU ASP LEU ILE ASN PRO TYR ARG ILE MET ARG          
SEQRES  37 A  577  SER GLY ARG GLY VAL LYS GLY VAL SER HIS THR ASP GLU          
SEQRES  38 A  577  LEU THR TYR PHE PHE TRP ASN GLN LEU ALA LYS ARG MET          
SEQRES  39 A  577  PRO LYS GLU SER ARG GLU TYR LYS THR ILE GLU ARG MET          
SEQRES  40 A  577  THR GLY ILE TRP THR GLN PHE ALA THR THR GLY ASN PRO          
SEQRES  41 A  577  TYR SER ASN GLU ILE GLU GLY MET GLU ASN VAL SER TRP          
SEQRES  42 A  577  ASP PRO ILE GLU LYS SER ASP GLU VAL TYR LYS CYS LEU          
SEQRES  43 A  577  ASN ILE SER ASP GLU LEU LYS MET ILE ASP VAL PRO GLU          
SEQRES  44 A  577  MET GLY LYS ILE LYS GLN TRP GLU SER MET PHE GLU LYS          
SEQRES  45 A  577  HIS ARG ASP LEU PHE                                          
HET    7N4  A 601      18                                                       
HETNAM     7N4 {3-CHLORO-4-[(2-FLUOROPHENYL)METHOXY]PHENYL}BORINIC              
HETNAM   2 7N4  ACID                                                            
FORMUL   2  7N4    C13 H11 B CL F O2                                            
FORMUL   3  HOH   *266(H2 O)                                                    
HELIX    1 AA1 MET A    8  LEU A   27  1                                  20    
HELIX    2 AA2 VAL A   68  ARG A   72  5                                   5    
HELIX    3 AA3 TYR A  152  LYS A  156  5                                   5    
HELIX    4 AA4 LEU A  167  LEU A  173  1                                   7    
HELIX    5 AA5 SER A  177  ASN A  181  5                                   5    
HELIX    6 AA6 ASN A  185  CYS A  202  1                                  18    
HELIX    7 AA7 ALA A  203  PHE A  205  5                                   3    
HELIX    8 AA8 SER A  218  THR A  230  1                                  13    
HELIX    9 AA9 GLU A  231  ARG A  234  5                                   4    
HELIX   10 AB1 CYS A  249  ASN A  253  5                                   5    
HELIX   11 AB2 HIS A  258  ALA A  267  1                                  10    
HELIX   12 AB3 ASN A  274  ALA A  285  1                                  12    
HELIX   13 AB4 LYS A  286  GLU A  294  1                                   9    
HELIX   14 AB5 GLU A  295  VAL A  297  5                                   3    
HELIX   15 AB6 THR A  299  ASN A  305  1                                   7    
HELIX   16 AB7 HIS A  328  VAL A  333  1                                   6    
HELIX   17 AB8 LYS A  334  ILE A  341  5                                   8    
HELIX   18 AB9 TYR A  350  PHE A  354  5                                   5    
HELIX   19 AC1 PHE A  355  MET A  362  1                                   8    
HELIX   20 AC2 PRO A  363  THR A  371  5                                   9    
HELIX   21 AC3 CYS A  372  VAL A  376  5                                   5    
HELIX   22 AC4 ALA A  387  VAL A  402  1                                  16    
HELIX   23 AC5 THR A  408  PHE A  421  1                                  14    
HELIX   24 AC6 PHE A  421  PHE A  433  1                                  13    
HELIX   25 AC7 PRO A  456  ARG A  461  1                                   6    
HELIX   26 AC8 THR A  472  PHE A  478  5                                   7    
HELIX   27 AC9 SER A  491  GLY A  511  1                                  21    
HELIX   28 AD1 GLU A  552  SER A  561  1                                  10    
HELIX   29 AD2 MET A  562  GLU A  564  5                                   3    
HELIX   30 AD3 HIS A  566  PHE A  570  5                                   5    
SHEET    1 AA1 3 THR A  28  ALA A  35  0                                        
SHEET    2 AA1 3 LYS A  41  LEU A  48 -1  O  GLY A  44   N  VAL A  33           
SHEET    3 AA1 3 VAL A  85  ASP A  87  1  O  ARG A  86   N  LYS A  41           
SHEET    1 AA212 THR A  28  ALA A  35  0                                        
SHEET    2 AA212 LYS A  41  LEU A  48 -1  O  GLY A  44   N  VAL A  33           
SHEET    3 AA212 SER A  54  PRO A  62 -1  O  TYR A  55   N  ARG A  47           
SHEET    4 AA212 TYR A 113  THR A 118 -1  O  THR A 118   N  TYR A  56           
SHEET    5 AA212 VAL A 159  ILE A 163 -1  O  LEU A 160   N  TYR A 117           
SHEET    6 AA212 ARG A 127  ILE A 133  1  N  LEU A 130   O  VAL A 159           
SHEET    7 AA212 GLY A 207  GLU A 217  1  O  ASN A 208   N  ARG A 127           
SHEET    8 AA212 ARG A 239  MET A 243  1  O  MET A 243   N  GLY A 216           
SHEET    9 AA212 THR A 343  THR A 348  1  O  MET A 344   N  LEU A 242           
SHEET   10 AA212 VAL A 441  PHE A 446  1  O  TYR A 442   N  MET A 345           
SHEET   11 AA212 LYS A 537  ILE A 541  1  O  ILE A 541   N  ARG A 445           
SHEET   12 AA212 LEU A 545  ASP A 549 -1  O  LYS A 546   N  ASN A 540           
SHEET    1 AA3 2 GLN A  97  VAL A  98  0                                        
SHEET    2 AA3 2 VAL A 105  CYS A 106 -1  O  CYS A 106   N  GLN A  97           
LINK         OG  SER A 218                 B02 7N4 A 601     1555   1555  1.37  
SITE     1 AC1 10 GLY A 136  GLY A 137  SER A 218  ALA A 219                    
SITE     2 AC1 10 MET A 308  PHE A 354  PHE A 355  MET A 460                    
SITE     3 AC1 10 HIS A 471  HOH A 964                                          
CRYST1   47.799  100.792  221.818  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020921  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009921  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004508        0.00000                         
TER    4573      PHE A 570                                                      
MASTER      335    0    1   30   17    0    3    6 4841    1   19   45          
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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