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LongText Report for: 3ESA-pdb

Name Class
3ESA-pdb
HEADER    HYDROLASE                               05-OCT-08   3ESA              
TITLE     CUT-1B; NCN-PT-PINCER-CUTINASE HYBRID                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CUTINASE 1;                                                
COMPND   3 CHAIN: A, B;                                                         
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 3ESA    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.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0008                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 20936                          
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) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1122                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1508                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.38                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2640                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 88                           
REMARK   3   BIN FREE R VALUE                    : 0.3240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2901                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 48                                      
REMARK   3   SOLVENT ATOMS            : 220                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.65                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.27000                                              
REMARK   3    B22 (A**2) : -2.46000                                             
REMARK   3    B33 (A**2) : -2.72000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.39000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.251         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.201         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.179         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.778        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.909                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3007 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4093 ; 1.596 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   396 ; 5.845 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   120 ;34.122 ;23.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   459 ;15.198 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;16.456 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   454 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2290 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1529 ; 0.202 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2069 ; 0.304 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   252 ; 0.146 ; 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):    59 ; 0.296 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    16 ; 0.197 ; 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):  1993 ; 0.581 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3095 ; 0.906 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1186 ; 1.532 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   994 ; 2.139 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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 3ESA COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-OCT-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB049704.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9395                             
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22076                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
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) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.400                              
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: PDB ENTRY 1CUA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 33.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22%(W/V) PEG-6000, 0.1M SODIUM           
REMARK 280  ACETATE, 0.2M SODIUM CHLORIDE, PH 5.5, VAPOR DIFFUSION,             
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       35.92950            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A   213                                                      
REMARK 465     ALA A   214                                                      
REMARK 465     LEU B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     ASN B     5                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     ALA B     7                                                      
REMARK 465     GLN B     8                                                      
REMARK 465     GLU B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     ALA B    12                                                      
REMARK 465     ARG B    13                                                      
REMARK 465     GLN B    14                                                      
REMARK 465     LEU B    15                                                      
REMARK 465     GLY B    16                                                      
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   OG   SER B   120     O1   NXC B   215              2.17            
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  30       70.95   -151.61                                   
REMARK 500    SER A 120     -129.85     57.13                                   
REMARK 500    SER B  30       54.86   -143.93                                   
REMARK 500    THR B  43       -4.08     77.26                                   
REMARK 500    SER B 120     -119.21     60.71                                   
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 ARG B   17     THR B   18                  136.98                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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     NXC A  215                                                       
REMARK 610     NXC B  215                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NXC A 215                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NXC B 215                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3EF3   RELATED DB: PDB                                   
REMARK 900 CUT-1A; NCN-PT-PINCER-CUTINASE HYBRID                                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SEE REFERENCE 2 IN UNIPROT DATABASE P00590                           
DBREF  3ESA A    1   214  UNP    P00590   CUTI1_FUSSO     17    230             
DBREF  3ESA B    1   214  UNP    P00590   CUTI1_FUSSO     17    230             
SEQADV 3ESA ALA A   32  UNP  P00590    ARG    48 SEE REMARK 999                 
SEQADV 3ESA LYS A  172  UNP  P00590    ASN   188 ENGINEERED                     
SEQADV 3ESA ALA B   32  UNP  P00590    ARG    48 SEE REMARK 999                 
SEQADV 3ESA LYS B  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                                      
SEQRES   1 B  214  LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG          
SEQRES   2 B  214  GLN LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY          
SEQRES   3 B  214  ASN SER ALA SER CYS ALA ASP VAL ILE PHE ILE TYR ALA          
SEQRES   4 B  214  ARG GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY          
SEQRES   5 B  214  PRO SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS          
SEQRES   6 B  214  ASP GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG          
SEQRES   7 B  214  ALA THR LEU GLY ASP ASN ALA LEU PRO ARG GLY THR SER          
SEQRES   8 B  214  SER ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN          
SEQRES   9 B  214  ALA ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY          
SEQRES  10 B  214  GLY TYR SER GLN GLY ALA ALA LEU ALA ALA ALA SER ILE          
SEQRES  11 B  214  GLU ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY          
SEQRES  12 B  214  THR VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG          
SEQRES  13 B  214  GLY ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL          
SEQRES  14 B  214  PHE CYS LYS THR GLY ASP LEU VAL CYS THR GLY SER LEU          
SEQRES  15 B  214  ILE VAL ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA          
SEQRES  16 B  214  ARG GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG          
SEQRES  17 B  214  ALA VAL ARG GLY SER ALA                                      
HET    NXC  A 215      24                                                       
HET    NXC  B 215      24                                                       
HETNAM     NXC (2,6-BIS[(DIMETHYLAMINO-KAPPAN)METHYL]-4-{3-[(S)-                
HETNAM   2 NXC  ETHOXY(4-NITROPHENOXY)PHOSPHORYL]PROPYL}PHENYL-                 
HETNAM   3 NXC  KAPPAC~1~)(CHLORO)PLATINUM(2+)                                  
HETSYN     NXC ETHYL 4-NITROPHENYL P-[3-(4-(CHLOROPLATINO)-1,3-BIS >            
HETSYN   2 NXC  [(DIMETHYLAMINO)METHYL]-PHENYL)PROPYL]PHOSPHONATE               
FORMUL   3  NXC    2(C23 H33 CL N3 O5 P PT 2+)                                  
FORMUL   5  HOH   *220(H2 O)                                                    
HELIX    1   1 ASN A   27  CYS A   31  5                                   5    
HELIX    2   2 LEU A   51  GLY A   64  1                                  14    
HELIX    3   3 THR A   80  LEU A   86  5                                   7    
HELIX    4   4 SER A   91  CYS A  109  1                                  19    
HELIX    5   5 SER A  120  LEU A  133  1                                  14    
HELIX    6   6 ASP A  134  LYS A  140  1                                   7    
HELIX    7   7 PRO A  163  ASP A  165  5                                   3    
HELIX    8   8 ASP A  175  GLY A  180  5                                   6    
HELIX    9   9 ALA A  185  ALA A  190  5                                   6    
HELIX   10  10 TYR A  191  GLY A  197  1                                   7    
HELIX   11  11 GLY A  197  GLY A  212  1                                  16    
HELIX   12  12 LEU B   51  GLY B   64  1                                  14    
HELIX   13  13 LEU B   81  LEU B   86  5                                   6    
HELIX   14  14 SER B   91  CYS B  109  1                                  19    
HELIX   15  15 SER B  120  LEU B  133  1                                  14    
HELIX   16  16 ASP B  134  ASP B  139  1                                   6    
HELIX   17  17 PRO B  163  ASP B  165  5                                   3    
HELIX   18  18 ASP B  175  GLY B  180  5                                   6    
HELIX   19  19 ALA B  185  ALA B  190  5                                   6    
HELIX   20  20 TYR B  191  GLY B  197  1                                   7    
HELIX   21  21 GLY B  197  GLY B  212  1                                  16    
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  ILE A 115   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           
SHEET    1   B 5 VAL B  68  GLY B  72  0                                        
SHEET    2   B 5 VAL B  34  ALA B  39  1  N  PHE B  36   O  TRP B  69           
SHEET    3   B 5 THR B 113  TYR B 119  1  O  THR B 113   N  ILE B  35           
SHEET    4   B 5 ILE B 141  PHE B 147  1  O  ALA B 142   N  LEU B 114           
SHEET    5   B 5 THR B 167  PHE B 170  1  O  PHE B 170   N  LEU B 146           
SSBOND   1 CYS A   31    CYS A  109                          1555   1555  2.04  
SSBOND   2 CYS A  171    CYS A  178                          1555   1555  2.00  
SSBOND   3 CYS B   31    CYS B  109                          1555   1555  2.05  
SSBOND   4 CYS B  171    CYS B  178                          1555   1555  2.04  
LINK         OG  SER A 120                 P   NXC A 215     1555   1555  1.59  
LINK         OG  SER B 120                 P   NXC B 215     1555   1555  1.59  
SITE     1 AC1 10 GLY A  41  SER A  42  SER A 120  GLN A 121                    
SITE     2 AC1 10 LEU A 182  VAL A 184  HIS A 188  VAL B 184                    
SITE     3 AC1 10 ALA B 186  LEU B 189                                          
SITE     1 AC2 12 VAL A 184  ALA A 186  LEU A 189  GLY B  41                    
SITE     2 AC2 12 SER B  42  ASN B  84  SER B 120  GLN B 121                    
SITE     3 AC2 12 LEU B 182  VAL B 184  HIS B 188  HOH B 277                    
CRYST1   33.970   71.859   68.568  90.00  96.94  90.00 P 1 21 1      4          
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      0.029438  0.000000  0.003585        0.00000                         
SCALE2      0.000000  0.013916  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014692        0.00000                         
TER    1446      GLY A 212                                                      
TER    2903      ALA B 214                                                      
MASTER      341    0    2   21   10    0    6    6 3169    2   58   34          
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.
For technical information about these pages see:
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