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LongText Report for: 3BXP-pdb

Name Class
3BXP-pdb
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   14-JAN-08   3BXP              
TITLE     CRYSTAL STRUCTURE OF PUTATIVE CARBOXYLESTERASE                        
TITLE    2 (NP_786266.1) FROM LACTOBACILLUS PLANTARUM AT 1.70 A                 
TITLE    3 RESOLUTION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE LIPASE/ESTERASE;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LACTOBACILLUS PLANTARUM WCFS1;                  
SOURCE   3 ORGANISM_COMMON: BACTERIA;                                           
SOURCE   4 STRAIN: WCFS1 / NCIMB 8826;                                          
SOURCE   5 ATCC: BAA-793;                                                       
SOURCE   6 GENE: NP_786266.1, LP_2923;                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: HK100;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: SPEEDET                                   
KEYWDS    NP_786266.1, PUTATIVE CARBOXYLESTERASE, STRUCTURAL GENOMICS,          
KEYWDS   2 JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN                  
KEYWDS   3 STRUCTURE INITIATIVE, PSI-2, STRUCTURAL GENOMICS, UNKNOWN            
KEYWDS   4 FUNCTION                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                           
REVDAT   1   29-JAN-08 3BXP    0                                                
JRNL        AUTH   JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                  
JRNL        TITL   CRYSTAL STRUCTURE OF PUTATIVE CARBOXYLESTERASE               
JRNL        TITL 2 (NP_786266.1) FROM LACTOBACILLUS PLANTARUM AT 1.70           
JRNL        TITL 3 A RESOLUTION                                                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.70 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0067                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.43                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 59208                          
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) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.197                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2995                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3704                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2110                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 199                          
REMARK   3   BIN FREE R VALUE                    : 0.2830                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 4563                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.46                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.68                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.32000                                              
REMARK   3    B22 (A**2) : -0.74000                                             
REMARK   3    B33 (A**2) : -0.20000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.04000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.101         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.098         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.066         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.975         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4298 ; 0.017 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2733 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5899 ; 1.527 ; 1.929       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6676 ; 1.079 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   548 ; 6.153 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   183 ;32.966 ;23.880       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   612 ;11.926 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;16.119 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   664 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4877 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   876 ; 0.002 ; 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):  2681 ; 1.917 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1081 ; 0.587 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4324 ; 2.766 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1617 ; 4.129 ; 8.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1575 ; 5.611 ;11.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 0                                 
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     0        A   273                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.9313  31.5463  44.6912              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0215 T22:  -0.0208                                     
REMARK   3      T33:  -0.0313 T12:  -0.0111                                     
REMARK   3      T13:   0.0063 T23:  -0.0085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5254 L22:   0.6750                                     
REMARK   3      L33:   0.3616 L12:   0.0481                                     
REMARK   3      L13:   0.1517 L23:  -0.0103                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0070 S12:  -0.0370 S13:  -0.0193                       
REMARK   3      S21:   0.0030 S22:  -0.0106 S23:   0.0644                       
REMARK   3      S31:  -0.0487 S32:  -0.0211 S33:   0.0035                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     0        B   273                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.1381  48.2340  16.4949              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0470 T22:  -0.0244                                     
REMARK   3      T33:  -0.0203 T12:  -0.0077                                     
REMARK   3      T13:   0.0024 T23:  -0.0118                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2831 L22:   0.7687                                     
REMARK   3      L33:   0.8606 L12:  -0.0972                                     
REMARK   3      L13:   0.0345 L23:  -0.0731                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0031 S12:   0.0132 S13:  -0.0236                       
REMARK   3      S21:   0.0258 S22:  -0.0086 S23:   0.0398                       
REMARK   3      S31:   0.0156 S32:  -0.0474 S33:   0.0055                       
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: 1. HYDROGENS HAVE BEEN ADDED IN THE       
REMARK   3  RIDING POSITIONS. 2. ATOM RECORD CONTAINS RESIDUAL B FACTORS        
REMARK   3  ONLY. 3. A MET-INHIBITION PROTOCOL WAS USED FOR                     
REMARK   3  SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE       
REMARK   3  OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO        
REMARK   3  0.75 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO             
REMARK   3  PARTIAL S-MET INCORPORATION. 4. CHLORIDE ION, HEPES AND 1,2-        
REMARK   3  PROPANEDIOL MOLECULES FROM CRYSTALLIZATION ARE MODELED IN THIS      
REMARK   3  STRUCTURE.                                                          
REMARK   4                                                                      
REMARK   4 3BXP COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007                        
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.                               
REMARK 100 THE RCSB ID CODE IS RCSB046086.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-NOV-2007                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97901                            
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL SI(111) BENT        
REMARK 200                                   (HORIZONTAL FOCUSING)              
REMARK 200  OPTICS                         : FLAT MIRROR (VERTICAL              
REMARK 200                                   FOCUSING)                          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59209                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.433                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : 0.06800                            
REMARK 200   FOR THE DATA SET  : 6.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.53200                            
REMARK 200   FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NANODROP, 30.0% 1,2-PROPANEDIOL,         
REMARK 280  20.0% PEG 400, 0.1M HEPES PH 7.5, VAPOR DIFFUSION, SITTING          
REMARK 280  DROP, TEMPERATURE 277K                                              
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,1/2+Y,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       47.11100            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER                      
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 AVERAGE BURIED SURFACE AREA: 1800 ANGSTROM**2                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                 
REMARK 465                                                                      
REMARK 465   M RES C  SSEQI                                                     
REMARK 465     ILE A   232                                                      
REMARK 465     HIS A   233                                                      
REMARK 465     GLY A   234                                                      
REMARK 465     LEU A   235                                                      
REMARK 465     ALA A   236                                                      
REMARK 465     LEU A   237                                                      
REMARK 465     ALA A   238                                                      
REMARK 465     ASN A   239                                                      
REMARK 465     HIS A   240                                                      
REMARK 465     VAL A   241                                                      
REMARK 465     THR A   242                                                      
REMARK 465     GLN A   243                                                      
REMARK 465     LYS A   244                                                      
REMARK 465     PRO A   245                                                      
REMARK 465     GLY A   246                                                      
REMARK 465     LYS A   247                                                      
REMARK 465     GLY A   274                                                      
REMARK 465     ASN A   275                                                      
REMARK 465     TYR A   276                                                      
REMARK 465     ASN B   239                                                      
REMARK 465     HIS B   240                                                      
REMARK 465     VAL B   241                                                      
REMARK 465     THR B   242                                                      
REMARK 465     GLN B   243                                                      
REMARK 465     LYS B   244                                                      
REMARK 465     PRO B   245                                                      
REMARK 465     GLY B   246                                                      
REMARK 465     LYS B   247                                                      
REMARK 465     ASP B   248                                                      
REMARK 465     LYS B   249                                                      
REMARK 465     TYR B   250                                                      
REMARK 465     GLY B   274                                                      
REMARK 465     ASN B   275                                                      
REMARK 465     TYR B   276                                                      
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     GLN A   2    CD    OE1   NE2                                     
REMARK 470     ARG A  51    CZ    NH1   NH2                                     
REMARK 470     GLU A 133    CD    OE1   OE2                                     
REMARK 470     ARG A 137    NE    CZ    NH1   NH2                               
REMARK 470     GLU A 202    CG    CD    OE1   OE2                               
REMARK 470     ASP A 248    CG    OD1   OD2                                     
REMARK 470     LYS A 249    CG    CD    CE    NZ                                
REMARK 470     LEU A 251    CG    CD1   CD2                                     
REMARK 470     ASN A 252    CG    OD1   ND2                                     
REMARK 470     ASP A 253    OD1   OD2                                           
REMARK 470     ASP B  27    CG    OD1   OD2                                     
REMARK 470     ARG B  51    CZ    NH1   NH2                                     
REMARK 470     GLU B 133    CG    CD    OE1   OE2                               
REMARK 470     ARG B 178    CZ    NH1   NH2                                     
REMARK 470     GLU B 202    CG    CD    OE1   OE2                               
REMARK 470     ASP B 253    CG    OD1   OD2                                     
REMARK 470     GLN B 254    CG    CD    OE1   NE2                               
REMARK 470     ARG B 264    CD    NE    CZ    NH1   NH2                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI                             
REMARK 500   NH2  ARG B   135     O    LEU B   140              1.77            
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 NUCELIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    HIS A 142   N   -  CA  -  CB  ANGL. DEV. = -12.3 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    HIS A 104       67.79     63.12                                   
REMARK 500    SER A 116     -116.71     50.27                                   
REMARK 500    LEU A 159       11.31    -69.32                                   
REMARK 500    ALA A 161       46.57   -101.41                                   
REMARK 500    SER A 203     -162.49   -160.70                                   
REMARK 500    HIS B 104       70.64     67.31                                   
REMARK 500    SER B 116     -124.40     47.86                                   
REMARK 500    TYR B 154       57.28     34.04                                   
REMARK 500    THR B 174      141.61   -176.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 SITE_DESCRIPTION: EPE BINDING SITE FOR RESIDUE B 278                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 SITE_DESCRIPTION: EPE BINDING SITE FOR RESIDUE A 277                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 SITE_DESCRIPTION: PGO BINDING SITE FOR RESIDUE B 279                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 SITE_DESCRIPTION: PGR BINDING SITE FOR RESIDUE A 278                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 SITE_DESCRIPTION: PGR BINDING SITE FOR RESIDUE B 280                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 SITE_DESCRIPTION: PGR BINDING SITE FOR RESIDUE B 281                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 SITE_DESCRIPTION: PGO BINDING SITE FOR RESIDUE A 279                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 SITE_DESCRIPTION: PGO BINDING SITE FOR RESIDUE A 280                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 SITE_DESCRIPTION: PGO BINDING SITE FOR RESIDUE A 281                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 379483   RELATED DB: TARGETDB                            
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG                  
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE           
REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.          
DBREF  3BXP A    1   276  UNP    Q88TL9   Q88TL9_LACPL     1    276             
DBREF  3BXP B    1   276  UNP    Q88TL9   Q88TL9_LACPL     1    276             
SEQADV 3BXP GLY A    0  UNP  Q88TL9              LEADER SEQUENCE                
SEQADV 3BXP GLY B    0  UNP  Q88TL9              LEADER SEQUENCE                
SEQRES   1 A  277  GLY MSE GLN VAL GLU GLN ARG THR LEU ASN THR ALA ALA          
SEQRES   2 A  277  HIS PRO PHE GLN ILE THR ALA TYR TRP LEU ASP GLN ILE          
SEQRES   3 A  277  SER ASP PHE GLU THR ALA VAL ASP TYR PRO ILE MSE ILE          
SEQRES   4 A  277  ILE CYS PRO GLY GLY GLY PHE THR TYR HIS SER GLY ARG          
SEQRES   5 A  277  GLU GLU ALA PRO ILE ALA THR ARG MSE MSE ALA ALA GLY          
SEQRES   6 A  277  MSE HIS THR VAL VAL LEU ASN TYR GLN LEU ILE VAL GLY          
SEQRES   7 A  277  ASP GLN SER VAL TYR PRO TRP ALA LEU GLN GLN LEU GLY          
SEQRES   8 A  277  ALA THR ILE ASP TRP ILE THR THR GLN ALA SER ALA HIS          
SEQRES   9 A  277  HIS VAL ASP CYS GLN ARG ILE ILE LEU ALA GLY PHE SER          
SEQRES  10 A  277  ALA GLY GLY HIS VAL VAL ALA THR TYR ASN GLY VAL ALA          
SEQRES  11 A  277  THR GLN PRO GLU LEU ARG THR ARG TYR HIS LEU ASP HIS          
SEQRES  12 A  277  TYR GLN GLY GLN HIS ALA ALA ILE ILE LEU GLY TYR PRO          
SEQRES  13 A  277  VAL ILE ASP LEU THR ALA GLY PHE PRO THR THR SER ALA          
SEQRES  14 A  277  ALA ARG ASN GLN ILE THR THR ASP ALA ARG LEU TRP ALA          
SEQRES  15 A  277  ALA GLN ARG LEU VAL THR PRO ALA SER LYS PRO ALA PHE          
SEQRES  16 A  277  VAL TRP GLN THR ALA THR ASP GLU SER VAL PRO PRO ILE          
SEQRES  17 A  277  ASN SER LEU LYS TYR VAL GLN ALA MSE LEU GLN HIS GLN          
SEQRES  18 A  277  VAL ALA THR ALA TYR HIS LEU PHE GLY SER GLY ILE HIS          
SEQRES  19 A  277  GLY LEU ALA LEU ALA ASN HIS VAL THR GLN LYS PRO GLY          
SEQRES  20 A  277  LYS ASP LYS TYR LEU ASN ASP GLN ALA ALA ILE TRP PRO          
SEQRES  21 A  277  GLN LEU ALA LEU ARG TRP LEU GLN GLU GLN GLY LEU LEU          
SEQRES  22 A  277  ALA GLY ASN TYR                                              
SEQRES   1 B  277  GLY MSE GLN VAL GLU GLN ARG THR LEU ASN THR ALA ALA          
SEQRES   2 B  277  HIS PRO PHE GLN ILE THR ALA TYR TRP LEU ASP GLN ILE          
SEQRES   3 B  277  SER ASP PHE GLU THR ALA VAL ASP TYR PRO ILE MSE ILE          
SEQRES   4 B  277  ILE CYS PRO GLY GLY GLY PHE THR TYR HIS SER GLY ARG          
SEQRES   5 B  277  GLU GLU ALA PRO ILE ALA THR ARG MSE MSE ALA ALA GLY          
SEQRES   6 B  277  MSE HIS THR VAL VAL LEU ASN TYR GLN LEU ILE VAL GLY          
SEQRES   7 B  277  ASP GLN SER VAL TYR PRO TRP ALA LEU GLN GLN LEU GLY          
SEQRES   8 B  277  ALA THR ILE ASP TRP ILE THR THR GLN ALA SER ALA HIS          
SEQRES   9 B  277  HIS VAL ASP CYS GLN ARG ILE ILE LEU ALA GLY PHE SER          
SEQRES  10 B  277  ALA GLY GLY HIS VAL VAL ALA THR TYR ASN GLY VAL ALA          
SEQRES  11 B  277  THR GLN PRO GLU LEU ARG THR ARG TYR HIS LEU ASP HIS          
SEQRES  12 B  277  TYR GLN GLY GLN HIS ALA ALA ILE ILE LEU GLY TYR PRO          
SEQRES  13 B  277  VAL ILE ASP LEU THR ALA GLY PHE PRO THR THR SER ALA          
SEQRES  14 B  277  ALA ARG ASN GLN ILE THR THR ASP ALA ARG LEU TRP ALA          
SEQRES  15 B  277  ALA GLN ARG LEU VAL THR PRO ALA SER LYS PRO ALA PHE          
SEQRES  16 B  277  VAL TRP GLN THR ALA THR ASP GLU SER VAL PRO PRO ILE          
SEQRES  17 B  277  ASN SER LEU LYS TYR VAL GLN ALA MSE LEU GLN HIS GLN          
SEQRES  18 B  277  VAL ALA THR ALA TYR HIS LEU PHE GLY SER GLY ILE HIS          
SEQRES  19 B  277  GLY LEU ALA LEU ALA ASN HIS VAL THR GLN LYS PRO GLY          
SEQRES  20 B  277  LYS ASP LYS TYR LEU ASN ASP GLN ALA ALA ILE TRP PRO          
SEQRES  21 B  277  GLN LEU ALA LEU ARG TRP LEU GLN GLU GLN GLY LEU LEU          
SEQRES  22 B  277  ALA GLY ASN TYR                                              
MODRES 3BXP MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 3BXP MSE A   37  MET  SELENOMETHIONINE                                   
MODRES 3BXP MSE A   60  MET  SELENOMETHIONINE                                   
MODRES 3BXP MSE A   61  MET  SELENOMETHIONINE                                   
MODRES 3BXP MSE A   65  MET  SELENOMETHIONINE                                   
MODRES 3BXP MSE A  216  MET  SELENOMETHIONINE                                   
MODRES 3BXP MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 3BXP MSE B   37  MET  SELENOMETHIONINE                                   
MODRES 3BXP MSE B   60  MET  SELENOMETHIONINE                                   
MODRES 3BXP MSE B   61  MET  SELENOMETHIONINE                                   
MODRES 3BXP MSE B   65  MET  SELENOMETHIONINE                                   
MODRES 3BXP MSE B  216  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  37       8                                                       
HET    MSE  A  60       8                                                       
HET    MSE  A  61       8                                                       
HET    MSE  A  65       8                                                       
HET    MSE  A 216       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B  37       8                                                       
HET    MSE  B  60       8                                                       
HET    MSE  B  61       8                                                       
HET    MSE  B  65       8                                                       
HET    MSE  B 216       8                                                       
HET     CL  B 277       1                                                       
HET    EPE  A 277      15                                                       
HET    PGR  A 278       5                                                       
HET    PGO  A 279       5                                                       
HET    PGO  A 280       5                                                       
HET    PGO  A 281       5                                                       
HET    EPE  B 278      15                                                       
HET    PGO  B 279       5                                                       
HET    PGR  B 280       5                                                       
HET    PGR  B 281       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CL CHLORIDE ION                                                     
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM     PGR R-1,2-PROPANEDIOL                                                
HETNAM     PGO S-1,2-PROPANEDIOL                                                
HETSYN     EPE HEPES                                                            
FORMUL   1  MSE    12(C5 H11 N O2 SE)                                           
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  EPE    2(C8 H18 N2 O4 S)                                            
FORMUL   5  PGR    3(C3 H8 O2)                                                  
FORMUL   6  PGO    4(C3 H8 O2)                                                  
FORMUL  13  HOH   *383(H2 O)                                                    
HELIX    1   1 GLU A   52  ALA A   63  1                                  12    
HELIX    2   2 PRO A   83  HIS A  104  1                                  22    
HELIX    3   3 SER A  116  ALA A  129  1                                  14    
HELIX    4   4 GLN A  131  TYR A  138  1                                   8    
HELIX    5   5 THR A  166  THR A  174  1                                   9    
HELIX    6   6 ASP A  176  TRP A  180  5                                   5    
HELIX    7   7 ALA A  181  VAL A  186  5                                   6    
HELIX    8   8 PRO A  206  HIS A  219  1                                  14    
HELIX    9   9 ASP A  248  GLN A  269  1                                  22    
HELIX   10  10 GLU B   52  ALA B   63  1                                  12    
HELIX   11  11 PRO B   83  GLN B   99  1                                  17    
HELIX   12  12 GLN B   99  HIS B  104  1                                   6    
HELIX   13  13 ALA B  117  ALA B  129  1                                  13    
HELIX   14  14 GLN B  131  TYR B  138  1                                   8    
HELIX   15  15 THR B  166  THR B  174  1                                   9    
HELIX   16  16 ASP B  176  TRP B  180  5                                   5    
HELIX   17  17 ALA B  181  VAL B  186  5                                   6    
HELIX   18  18 PRO B  206  HIS B  219  1                                  14    
HELIX   19  19 SER B  230  LEU B  235  5                                   6    
HELIX   20  20 ALA B  256  GLN B  269  1                                  14    
SHEET    1   A16 MSE A   1  LEU A   8  0                                        
SHEET    2   A16 PHE A  15  LEU A  22 -1  O  ALA A  19   N  GLU A   4           
SHEET    3   A16 HIS A  66  ASN A  71 -1  O  THR A  67   N  TYR A  20           
SHEET    4   A16 TYR A  34  CYS A  40  1  N  ILE A  39   O  VAL A  68           
SHEET    5   A16 VAL A 105  PHE A 115  1  O  ALA A 113   N  CYS A  40           
SHEET    6   A16 ALA A 149  GLY A 153  1  O  ILE A 151   N  LEU A 112           
SHEET    7   A16 ALA A 193  GLN A 197  1  O  PHE A 194   N  LEU A 152           
SHEET    8   A16 THR A 223  LEU A 227  1  O  ALA A 224   N  VAL A 195           
SHEET    9   A16 THR B 223  PHE B 228 -1  O  TYR B 225   N  LEU A 227           
SHEET   10   A16 ALA B 193  THR B 198  1  N  VAL B 195   O  ALA B 224           
SHEET   11   A16 ALA B 149  GLY B 153  1  N  LEU B 152   O  PHE B 194           
SHEET   12   A16 VAL B 105  PHE B 115  1  N  GLY B 114   O  GLY B 153           
SHEET   13   A16 TYR B  34  CYS B  40  1  N  ILE B  38   O  ALA B 113           
SHEET   14   A16 HIS B  66  ASN B  71  1  O  VAL B  68   N  ILE B  39           
SHEET   15   A16 PHE B  15  LEU B  22 -1  N  TYR B  20   O  THR B  67           
SHEET   16   A16 MSE B   1  LEU B   8 -1  N  GLU B   4   O  ALA B  19           
CISPEP   1 TYR A   82    PRO A   83          0         4.86                     
CISPEP   2 PHE A  163    PRO A  164          0         1.02                     
CISPEP   3 TYR B   82    PRO B   83          0         4.56                     
CISPEP   4 PHE B  163    PRO B  164          0         3.41                     
SITE     1 AC1  5 ASP B  78  GLN B  79  SER B  80  TRP B  84                    
SITE     2 AC1  5 GLN B 172                                                     
SITE     1 AC2  5 ASP A  78  GLN A  79  SER A  80  TRP A  84                    
SITE     2 AC2  5 GLN A 172                                                     
SITE     1 AC3  4 TYR B  20  ALA B  54  ALA B  57  THR B  58                    
SITE     1 AC4  8 ALA A 224  HIS A 226  LEU A 261  GLU A 268                    
SITE     2 AC4  8 PHE B 228  GLY B 229  SER B 230  HIS B 233                    
SITE     1 AC5  3 GLN A 214  PRO B 206  ILE B 207                               
SITE     1 AC6  4 ASP A  33  ALA A 100  SER A 101  ASP B  33                    
SITE     1 AC7  8 ARG A 135  ASP A 141  TYR A 143  GLN A 144                    
SITE     2 AC7  8 ARG B 135  ASP B 141  TYR B 143  GLN B 144                    
SITE     1 AC8  4 GLN A 108  GLN A 146  ALA A 148  LYS A 191                    
SITE     1 AC9  2 ALA A  54  THR A  58                                          
CRYST1   53.595   94.222   58.758  90.00 107.47  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      0.018659  0.000000  0.005871        0.00000                         
SCALE2      0.000000  0.010613  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017841        0.00000                         
TER    2053      ALA A 273                                                      
TER    4116      ALA B 273                                                      
MASTER      414    0   22   20   16    0   13    6 4563    2  161   44          
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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