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LongText Report for: 3ESC-pdb

Name Class
3ESC-pdb
HEADER    HYDROLASE                               05-OCT-08   3ESC              
TITLE     CUT-2A; NCN-PT-PINCER-CUTINASE HYBRID                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CUTINASE 1;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CUTIN HYDROLASE 1;                                          
COMPND   5 EC: 3.1.1.74;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: FUSARIUM SOLANI F. PISI;                        
SOURCE   3 ORGANISM_TAXID: 70791;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PUC19                                     
KEYWDS    PROTEIN-METALLOPINCER COMPLEX, GLYCOPROTEIN, HYDROLASE,               
KEYWDS   2 SECRETED, SERINE ESTERASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.RUTTEN,J.P.B.A.MANNIE,M.LUTZ,P.GROS                                 
REVDAT   1   28-JUL-09 3ESC    0                                                
JRNL        AUTH   L.RUTTEN,B.WIECZOREK,J.P.B.A.MANNIE,C.A.KRUITHOF,            
JRNL        AUTH 2 H.P.DIJKSTRA,M.R.EGMOND,M.LUTZ,R.J.M.KLEIN GEBBINK,          
JRNL        AUTH 3 P.GROS,G.VAN KOTEN                                           
JRNL        TITL   SOLID-STATE STRUCTURAL CHARACTERIZATION OF                   
JRNL        TITL 2 CUTINASE-ECE-PINCER-METAL HYBRIDS                            
JRNL        REF    CHEMISTRY                     V.  15  4270 2009              
JRNL        REFN                   ISSN 0947-6539                               
JRNL        PMID   19219875                                                     
JRNL        DOI    10.1002/CHEM.200801995                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   CROSS-VALIDATION METHOD           : NULL                           
REMARK   3   FREE R VALUE TEST SET SELECTION   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.166                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.194                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 69883                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1468                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 44                                            
REMARK   3   SOLVENT ATOMS      : 393                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL                    
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL                    
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL                    
REMARK   3   NUMBER OF RESTRAINTS                     : NULL                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.020                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.030                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : NULL                    
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : NULL                    
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : NULL                    
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL                    
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL                    
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL                    
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL                    
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : NULL                                
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3ESC COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-OCT-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB049706.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69883                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10000                            
REMARK 200   FOR THE DATA SET  : 13.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.71300                            
REMARK 200   FOR SHELL         : 2.300                              
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: 1CUA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10%(W/V) PEG-3350, 25%(V/V)              
REMARK 280  GLYCEROL, 0.1M 2-(BIS(2-HYDROXYETHYL)AMINO)-2-(HYDROXYMETHYL)       
REMARK 280  PROPANE-1,3-DIOL (BISTRISP), 0.2M SODIUM CITRATE, PH 6.5,           
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 291K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
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       27.88550            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       27.88550            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       27.88550            
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 BR1  SXC A 215  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 304  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 364  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 401  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 565  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 588  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     LEU A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     GLN A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     ALA A    12                                                      
REMARK 465     ARG A    13                                                      
REMARK 465     GLN A    14                                                      
REMARK 465     LEU A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     GLY A   212                                                      
REMARK 465     SER A   213                                                      
REMARK 465     ALA A   214                                                      
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 PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  17   CD  -  NE  -  CZ  ANGL. DEV. =  11.6 DEGREES          
REMARK 500    ARG A  78   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG A  88   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    TYR A 119   CB  -  CG  -  CD2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    TYR A 119   CB  -  CG  -  CD1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ASP A 134   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG A 138   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG A 138   NE  -  CZ  -  NH2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    TYR A 149   CB  -  CG  -  CD2 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    ARG A 196   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 208   CD  -  NE  -  CZ  ANGL. DEV. = -12.8 DEGREES          
REMARK 500    ARG A 208   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.7 DEGREES          
REMARK 500    ARG A 208   NE  -  CZ  -  NH2 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG A 211   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
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 120     -123.22     62.82                                   
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 425        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH A 526        DISTANCE =  5.42 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     SXC A  215                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SXC A 215                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SEE REFERENCE 2 IN UNIPROT DATABASE P00590                           
DBREF  3ESC A    1   214  UNP    P00590   CUTI1_FUSSO     17    230             
SEQADV 3ESC ALA A   32  UNP  P00590    ARG    48 SEE REMARK 999                 
SEQADV 3ESC LYS A  172  UNP  P00590    ASN   188 ENGINEERED                     
SEQRES   1 A  214  LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG          
SEQRES   2 A  214  GLN LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY          
SEQRES   3 A  214  ASN SER ALA SER CYS ALA ASP VAL ILE PHE ILE TYR ALA          
SEQRES   4 A  214  ARG GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY          
SEQRES   5 A  214  PRO SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS          
SEQRES   6 A  214  ASP GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG          
SEQRES   7 A  214  ALA THR LEU GLY ASP ASN ALA LEU PRO ARG GLY THR SER          
SEQRES   8 A  214  SER ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN          
SEQRES   9 A  214  ALA ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY          
SEQRES  10 A  214  GLY TYR SER GLN GLY ALA ALA LEU ALA ALA ALA SER ILE          
SEQRES  11 A  214  GLU ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY          
SEQRES  12 A  214  THR VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG          
SEQRES  13 A  214  GLY ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL          
SEQRES  14 A  214  PHE CYS LYS THR GLY ASP LEU VAL CYS THR GLY SER LEU          
SEQRES  15 A  214  ILE VAL ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA          
SEQRES  16 A  214  ARG GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG          
SEQRES  17 A  214  ALA VAL ARG GLY SER ALA                                      
HET    SXC  A 215      44                                                       
HETNAM     SXC BROMO(4-{3-[(R)-ETHOXY(4-NITROPHENOXY)                           
HETNAM   2 SXC  PHOSPHORYL]PROPYL}-2,6-BIS[(METHYLSULFANYL-KAPPAS)              
HETNAM   3 SXC  METHYL]PHENYL-KAPPAC~1~)PALLADIUM(2+)                           
HETSYN     SXC ETHYL 4-NITROPHENYL P-[3-(4-(BROMOPALLADO)-1,3-                  
HETSYN   2 SXC  BIS[(METHYLTHIO)METHYL]-PHENYL)PROPYL]PHOSPHONATE               
FORMUL   2  SXC    C21 H27 BR N O5 P PD S2 2+                                   
FORMUL   3  HOH   *393(H2 O)                                                    
HELIX    1   1 LEU A   51  GLY A   64  1                                  14    
HELIX    2   2 THR A   80  LEU A   86  5                                   7    
HELIX    3   3 SER A   91  CYS A  109  1                                  19    
HELIX    4   4 SER A  120  LEU A  133  1                                  14    
HELIX    5   5 ASP A  134  ASP A  139  1                                   6    
HELIX    6   6 PRO A  163  ASP A  165  5                                   3    
HELIX    7   7 ASP A  175  GLY A  180  5                                   6    
HELIX    8   8 ALA A  185  ALA A  190  5                                   6    
HELIX    9   9 TYR A  191  GLY A  197  1                                   7    
HELIX   10  10 GLY A  197  ARG A  211  1                                  15    
SHEET    1   A 5 VAL A  68  GLY A  72  0                                        
SHEET    2   A 5 VAL A  34  ALA A  39  1  N  PHE A  36   O  TRP A  69           
SHEET    3   A 5 THR A 113  TYR A 119  1  O  THR A 113   N  ILE A  35           
SHEET    4   A 5 ILE A 141  PHE A 147  1  O  ALA A 142   N  LEU A 114           
SHEET    5   A 5 THR A 167  PHE A 170  1  O  PHE A 170   N  LEU A 146           
SSBOND   1 CYS A   31    CYS A  109                          1555   1555  2.06  
SSBOND   2 CYS A  171    CYS A  178                          1555   1555  2.10  
LINK         OG  SER A 120                 P1 ASXC A 215     1555   1555  1.59  
LINK         OG  SER A 120                 P1 BSXC A 215     1555   1555  1.55  
SITE     1 AC1  9 SER A  42  LEU A  81  ASN A  84  TYR A 119                    
SITE     2 AC1  9 SER A 120  GLN A 121  LEU A 182  ILE A 183                    
SITE     3 AC1  9 HIS A 188                                                     
CRYST1   83.949   83.949   55.771  90.00  90.00 120.00 P 63          6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011912  0.006877  0.000000        0.00000                         
SCALE2      0.000000  0.013755  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017930        0.00000                         
TER    1469      ARG A 211                                                      
MASTER      306    0    1   10    5    0    3    6 1905    1   49   17          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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