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LongText Report for: 4PO3-pdb

Name Class
4PO3-pdb
HEADER    HYDROLASE                               24-FEB-14   4PO3              
TITLE     CRYSTAL STRUCTURE OF A C4-C4 SN3 TRIBUTYRIN PHOSPHONATE INHIBITED BY  
TITLE    2 ESTERASE B FROM LACTOBACILLUS RHAMNOSIS                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ESTERASE B;                                                
COMPND   3 CHAIN: X;                                                            
COMPND   4 SYNONYM: ESTERASE/LIPASE;                                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LACTOBACILLUS RHAMNOSUS;                        
SOURCE   3 ORGANISM_TAXID: 486408;                                              
SOURCE   4 STRAIN: HN001;                                                       
SOURCE   5 GENE: LRH_10360;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PGEX 6P3;                             
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX_6P3_ESTB                             
KEYWDS    ESTERASE/LIPASE, TRIACYLGLYCERASE, HYDROLYSIS, HYDROLASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.D.BENNETT,B.F.ANDERSON,G.E.NORRIS,D.A.COLBERT                       
REVDAT   1   11-JUN-14 4PO3    0                                                
JRNL        AUTH   M.D.BENNETT,D.A.COLBERT,B.F.ANDERSON,G.E.NORRIS              
JRNL        TITL   CRYSTAL STRUCTURE OF A C4-C4 SN3 TRIBUTYRIN PHODPHONATE      
JRNL        TITL 2 INHIBITED ESTERASE B FROM LACTOBACILLUS RHAMNOSIS            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.96 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.84                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 24173                          
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) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.164                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1249                            
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) : 1.96                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.01                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1796                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 89                           
REMARK   3   BIN FREE R VALUE                    : 0.2760                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2450                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 19                                      
REMARK   3   SOLVENT ATOMS            : 191                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.146         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.138         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.078         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.670         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2551 ; 0.019 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2346 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3466 ; 1.864 ; 1.943       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5382 ; 0.904 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   313 ; 6.352 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   132 ;35.136 ;24.545       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   399 ;14.136 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;21.221 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   366 ; 0.121 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2950 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   624 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4PO3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-APR-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB085009.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JUL-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-002                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : CAPILLARY FOCUSING OPTICS AND      
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR                       
REMARK 200  DATA SCALING SOFTWARE          : CRYSTALCLEAR                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24173                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.440                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.840                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.2                               
REMARK 200  DATA REDUNDANCY                : 3.730                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 7.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.44                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 25.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.26                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4N5H                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 AMMONIUM PHOSPHATE, 0.1M TRISHCL,    
REMARK 280  PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 297K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       8555   Y+1/2,-X+1/2,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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  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       54.92650            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       54.92650            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       29.66750            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       54.92650            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       54.92650            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       29.66750            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       54.92650            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       54.92650            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       29.66750            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       54.92650            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       54.92650            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       29.66750            
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: X                                     
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 X 660  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH X 678  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH X 689  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 X     1                                                      
REMARK 465     GLU X   194                                                      
REMARK 465     ALA X   195                                                      
REMARK 465     ALA X   196                                                      
REMARK 465     GLY X   197                                                      
REMARK 465     ASP X   198                                                      
REMARK 465     PHE X   316                                                      
REMARK 465     GLU X   317                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU X   5    CD   OE1  OE2                                       
REMARK 470     LYS X  60    CD   CE   NZ                                        
REMARK 470     ARG X  62    CD   NE   CZ   NH1  NH2                             
REMARK 470     LEU X 192    CD1                                                 
REMARK 470     LYS X 277    NZ                                                  
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   ND1  HIS X   284     O    HOH X   616              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TRP X  37   CE3   TRP X  37   CZ3     0.108                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ASP X  28   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG X  86   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG X  90   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG X 124   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 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    ASP X   3      132.74    169.59                                   
REMARK 500    ASP X  34       38.37     71.63                                   
REMARK 500    GLN X  51       52.08    -93.61                                   
REMARK 500    TRP X  77      -12.76     68.59                                   
REMARK 500    SER X 146     -119.08     60.28                                   
REMARK 500    ASN X 174       46.79    -87.19                                   
REMARK 500    CYS X 184       55.67     36.58                                   
REMARK 500    VAL X 186       70.96   -105.86                                   
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 X 660        DISTANCE = 10.14 ANGSTROMS                       
REMARK 525    HOH X 678        DISTANCE = 11.02 ANGSTROMS                       
REMARK 525    HOH X 689        DISTANCE = 12.12 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HY4 X 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4N5H   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN                                                         
REMARK 900 RELATED ID: 4N5I   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN                                                         
REMARK 900 RELATED ID: 4OUK   RELATED DB: PDB                                   
DBREF  4PO3 X    1   317  UNP    B2CZF4   B2CZF4_LACRH     1    317             
SEQADV 4PO3 VAL X  218  UNP  B2CZF4    ALA   218 ENGINEERED MUTATION            
SEQRES   1 X  317  MET ALA ASP GLU GLU ALA MET LEU ALA LYS VAL GLN ALA          
SEQRES   2 X  317  SER TRP ALA GLN THR ALA ALA ARG ASP LYS ALA ARG TYR          
SEQRES   3 X  317  ALA ASP GLU ARG VAL PRO GLU ASP VAL HIS TRP GLU THR          
SEQRES   4 X  317  GLU TYR ARG TYR GLU GLN SER ALA ASP PRO GLN GLN THR          
SEQRES   5 X  317  LEU ASN LEU TYR TYR PRO ALA LYS ARG ARG ASN ALA THR          
SEQRES   6 X  317  MET PRO THR VAL ILE ASP ILE HIS GLY GLY GLY TRP PHE          
SEQRES   7 X  317  TYR GLY ASP ARG ASN LEU ASN ARG ASN TYR CYS ARG TYR          
SEQRES   8 X  317  LEU ALA SER GLN GLY TYR ALA VAL MET GLY MET GLY TYR          
SEQRES   9 X  317  ARG LEU LEU PRO ASP VAL ASP LEU ARG GLY GLN ILE GLN          
SEQRES  10 X  317  ASP ILE PHE ALA SER LEU ARG TRP LEU SER HIS PHE GLY          
SEQRES  11 X  317  PRO GLN ARG GLY PHE ASP LEU ASP HIS VAL LEU LEU THR          
SEQRES  12 X  317  GLY ASP SER ALA GLY GLY HIS LEU ALA SER LEU VAL ALA          
SEQRES  13 X  317  CYS ILE GLN GLN SER ALA GLU LEU GLN GLU LEU PHE GLY          
SEQRES  14 X  317  VAL SER ARG VAL ASN PHE ASN PHE THR LEU VAL ALA LEU          
SEQRES  15 X  317  VAL CYS PRO VAL ALA GLU PRO SER LYS LEU PRO GLU ALA          
SEQRES  16 X  317  ALA GLY ASP MET SER ASP MET ALA ALA PHE TYR LEU ASP          
SEQRES  17 X  317  LYS LEU SER GLY GLY ASP GLN ALA LEU VAL ASP HIS LEU          
SEQRES  18 X  317  ASN PHE SER GLN VAL VAL LYS GLY LEU ASP LEU PRO PRO          
SEQRES  19 X  317  PHE MET LEU ILE GLY GLY GLN ASN ASP SER PHE TYR LEU          
SEQRES  20 X  317  GLN SER GLN ALA LEU LEU LYS VAL PHE ASP ALA ASN HIS          
SEQRES  21 X  317  VAL THR TYR THR THR LYS LEU TRP PRO ALA SER ALA GLY          
SEQRES  22 X  317  PRO HIS LEU LYS HIS VAL PHE ASN VAL GLN HIS TRP GLU          
SEQRES  23 X  317  TRP PRO GLU SER ILE GLU THR ASN LEU GLU MET LEU ARG          
SEQRES  24 X  317  THR PHE ASP ALA LEU SER LYS GLN GLN ASP GLN ALA GLU          
SEQRES  25 X  317  GLU ASN GLU PHE GLU                                          
HET    HY4  X 401      19                                                       
HETNAM     HY4 (2R)-2,3-DIBUTOXYPROPYL HYDROGEN (S)-PROPYLPHOSPHONATE           
FORMUL   2  HY4    C14 H31 O5 P                                                 
FORMUL   3  HOH   *191(H2 O)                                                    
HELIX    1   1 ASP X    3  GLU X   29  1                                  27    
HELIX    2   2 ASN X   85  GLN X   95  1                                  11    
HELIX    3   3 ASP X  111  GLY X  130  1                                  20    
HELIX    4   4 PRO X  131  ARG X  133  5                                   3    
HELIX    5   5 SER X  146  SER X  161  1                                  16    
HELIX    6   6 SER X  161  GLY X  169  1                                   9    
HELIX    7   7 GLU X  188  LEU X  192  5                                   5    
HELIX    8   8 SER X  200  GLY X  212  1                                  13    
HELIX    9   9 ASP X  214  ASP X  219  1                                   6    
HELIX   10  10 ASN X  222  VAL X  227  1                                   6    
HELIX   11  11 PHE X  245  ASN X  259  1                                  15    
HELIX   12  12 PRO X  269  GLY X  273  5                                   5    
HELIX   13  13 VAL X  279  HIS X  284  1                                   6    
HELIX   14  14 TRP X  287  GLU X  312  1                                  26    
SHEET    1   A 8 VAL X  35  ARG X  42  0                                        
SHEET    2   A 8 THR X  52  PRO X  58 -1  O  LEU X  55   N  GLU X  38           
SHEET    3   A 8 ALA X  98  MET X 102 -1  O  VAL X  99   N  TYR X  56           
SHEET    4   A 8 MET X  66  ILE X  72  1  N  ASP X  71   O  MET X 100           
SHEET    5   A 8 PHE X 135  ASP X 145  1  O  THR X 143   N  ILE X  70           
SHEET    6   A 8 LEU X 179  VAL X 183  1  O  VAL X 183   N  GLY X 144           
SHEET    7   A 8 PHE X 235  GLY X 240  1  O  MET X 236   N  LEU X 182           
SHEET    8   A 8 TYR X 263  TRP X 268  1  O  TRP X 268   N  GLY X 239           
LINK         OG  SER X 146                 P13 HY4 X 401     1555   1555  1.61  
CISPEP   1 LEU X  107    PRO X  108          0         7.95                     
SITE     1 AC1  9 SER X  14  TRP X  15  GLY X  75  GLY X  76                    
SITE     2 AC1  9 SER X 146  ALA X 147  TYR X 206  PHE X 245                    
SITE     3 AC1  9 HIS X 278                                                     
CRYST1  109.853  109.853   59.335  90.00  90.00  90.00 I 4           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      0.009103  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009103  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016853        0.00000                         
TER    2467      GLU X 315                                                      
MASTER      391    0    1   14    8    0    3    6 2660    1   20   25          
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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