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LongText Report for: 7atq-pdb

Name Class
7atq-pdb
HEADER    HYDROLASE                               30-OCT-20   7ATQ              
TITLE     STRUCTURE OF ESTD11 IN COMPLEX WITH CYCLOHEXANE CARBOXYLIC ACID       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ESTD11;                                                    
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;                           
SOURCE   3 ORGANISM_TAXID: 77133;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET22                                     
KEYWDS    ESTERASE HORMONE-SENSITIVE LIPASE METAGENOME LIBRARY CRYSTAL          
KEYWDS   2 STRUCTURE, HYDROLASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.MIGUEL-RUANO,I.RIVERA,J.A.HERMOSO                                   
REVDAT   1   03-MAR-21 7ATQ    0                                                
JRNL        AUTH   V.MIGUEL-RUANO,I.RIVERA,J.RAJKOVIC,K.KNAPIK,A.TORRADO,       
JRNL        AUTH 2 J.M.OTERO,E.BENEVENTI,M.BECERRA,M.SANCHEZ-COSTA,A.HIDALGO,   
JRNL        AUTH 3 J.BERENGUER,M.I.GONZALEZ-SISO,J.CRUCES,M.L.RUA,J.A.HERMOSO   
JRNL        TITL   BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF A NOVEL       
JRNL        TITL 2 THERMOPHILIC ESTERASE ESTD11 PROVIDE CATALYTIC INSIGHTS FOR  
JRNL        TITL 3 THE HSL FAMILY                                               
JRNL        REF    COMPUT STRUCT BIOTECHNOL J                 2021              
JRNL        REFN                   ESSN 2001-0370                               
JRNL        DOI    10.1016/J.CSBJ.2021.01.047                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.59 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0267                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.59                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.47                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 71814                          
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) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.191                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3872                            
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) : 1.59                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.63                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5221                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3310                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 292                          
REMARK   3   BIN FREE R VALUE                    : 0.3720                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4496                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 654                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.68                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.18000                                             
REMARK   3    B22 (A**2) : 0.98000                                              
REMARK   3    B33 (A**2) : -0.79000                                             
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): 0.092         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.085         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.062         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.845         
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):  4826 ; 0.007 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  4686 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6604 ; 1.448 ; 1.650       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10772 ; 1.381 ; 1.580       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   632 ; 6.091 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   251 ;28.138 ;20.120       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   778 ;13.716 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    52 ;21.953 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   626 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5561 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1075 ; 0.004 ; 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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     B     2    296       A     2    296    9707 0.100 0.050     
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 U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 7ATQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-OCT-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292112078.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUL-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 291                                
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALBA                               
REMARK 200  BEAMLINE                       : XALOC                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 75769                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.590                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.190                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.10600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.62                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.28600                            
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: PHASER                                                
REMARK 200 STARTING MODEL: 7AT0                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.2M SODIUM FORMATE + 0.1M CITRATE PH    
REMARK 280  5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       23.92400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.29100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.11000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       72.29100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.92400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.11000            
REMARK 290   SMTRY3   4  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 300 REMARK: GEL FILTRATION                                               
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 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 B     1                                                      
REMARK 465     MET A     1                                                      
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   O    HOH B  1139     O    HOH B  1251              1.73            
REMARK 500   O    HOH A   604     O    HOH A   739              1.79            
REMARK 500   O    HOH B  1031     O    HOH B  1275              1.99            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B  1086     O    HOH B  1173     4555     2.01            
REMARK 500   O    HOH B  1215     O    HOH A   790     4545     2.10            
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 B 144     -118.40     57.76                                   
REMARK 500    ALA B 237       47.29    -94.84                                   
REMARK 500    SER A   3      151.52    -48.98                                   
REMARK 500    SER A 144     -119.77     57.74                                   
REMARK 500    VAL A 190      -63.03   -127.49                                   
REMARK 500    ASP A 191      114.20    -28.82                                   
REMARK 500    ASP A 265       -1.16     74.92                                   
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 B1331        DISTANCE =  6.15 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 905                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 906                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue RXK A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue RXK A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 504                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 7AT0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 7AT2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 7AT3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 7ATD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 7ATF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 7AT4   RELATED DB: PDB                                   
DBREF  7ATQ B    1   296  PDB    7ATQ     7ATQ             1    296             
DBREF  7ATQ A    1   296  PDB    7ATQ     7ATQ             1    296             
SEQRES   1 B  296  MET ALA SER GLU ALA LEU THR MET ILE VAL ASN LEU LEU          
SEQRES   2 B  296  ARG SER GLN ARG PRO LEU GLN GLU PRO THR VAL GLU GLN          
SEQRES   3 B  296  MET ARG ALA GLY LEU GLU ALA MET ALA GLN MET SER PRO          
SEQRES   4 B  296  LEU PRO ALA ASP VAL GLU LEU THR THR VAL ASP ALA GLY          
SEQRES   5 B  296  GLY VAL PRO GLY ALA TRP VAL ARG VAL PRO GLU SER ASP          
SEQRES   6 B  296  PRO ASP ARG VAL VAL LEU TYR LEU HIS GLY GLY GLY TYR          
SEQRES   7 B  296  VAL ILE GLY SER ILE ARG THR HIS ARG ASP LEU ALA GLN          
SEQRES   8 B  296  ARG ILE ALA ARG ALA ALA ARG CYS ARG VAL LEU LEU ILE          
SEQRES   9 B  296  ASP TYR ARG LEU ALA PRO GLU HIS PRO HIS PRO ALA ALA          
SEQRES  10 B  296  VAL GLU ASP SER THR ARG ALA TYR ARG TRP LEU LEU GLU          
SEQRES  11 B  296  THR GLY SER ASP PRO LYS ARG MET ALA ILE ALA GLY ASP          
SEQRES  12 B  296  SER ALA GLY GLY GLY LEU THR VAL ALA THR LEU VAL ALA          
SEQRES  13 B  296  LEU ARG ASP ALA GLY VAL PRO LEU PRO ALA ALA ALA VAL          
SEQRES  14 B  296  CYS LEU SER PRO TRP VAL ASP LEU GLU GLY ILE GLY GLU          
SEQRES  15 B  296  SER MET THR THR LYS ALA ALA VAL ASP PRO MET VAL GLN          
SEQRES  16 B  296  ARG GLU PRO LEU LEU ARG MET ALA SER MET TYR LEU ALA          
SEQRES  17 B  296  GLY GLN ASP PRO ARG THR PRO LEU ALA ALA PRO LEU TYR          
SEQRES  18 B  296  ALA ASP LEU ARG GLY LEU PRO PRO LEU LEU ILE GLN VAL          
SEQRES  19 B  296  GLY THR ALA GLU THR LEU LEU ASP ASP SER VAL ARG LEU          
SEQRES  20 B  296  ALA GLU ARG ALA ARG ALA ALA GLY VAL GLN VAL THR LEU          
SEQRES  21 B  296  GLU PRO TRP GLU ASP MET ILE HIS VAL TRP GLN ALA PHE          
SEQRES  22 B  296  ALA ALA MET LEU PRO GLU GLY GLN GLN ALA ILE GLU ARG          
SEQRES  23 B  296  ILE GLY GLU PHE LEU ARG GLN HIS TRP GLN                      
SEQRES   1 A  296  MET ALA SER GLU ALA LEU THR MET ILE VAL ASN LEU LEU          
SEQRES   2 A  296  ARG SER GLN ARG PRO LEU GLN GLU PRO THR VAL GLU GLN          
SEQRES   3 A  296  MET ARG ALA GLY LEU GLU ALA MET ALA GLN MET SER PRO          
SEQRES   4 A  296  LEU PRO ALA ASP VAL GLU LEU THR THR VAL ASP ALA GLY          
SEQRES   5 A  296  GLY VAL PRO GLY ALA TRP VAL ARG VAL PRO GLU SER ASP          
SEQRES   6 A  296  PRO ASP ARG VAL VAL LEU TYR LEU HIS GLY GLY GLY TYR          
SEQRES   7 A  296  VAL ILE GLY SER ILE ARG THR HIS ARG ASP LEU ALA GLN          
SEQRES   8 A  296  ARG ILE ALA ARG ALA ALA ARG CYS ARG VAL LEU LEU ILE          
SEQRES   9 A  296  ASP TYR ARG LEU ALA PRO GLU HIS PRO HIS PRO ALA ALA          
SEQRES  10 A  296  VAL GLU ASP SER THR ARG ALA TYR ARG TRP LEU LEU GLU          
SEQRES  11 A  296  THR GLY SER ASP PRO LYS ARG MET ALA ILE ALA GLY ASP          
SEQRES  12 A  296  SER ALA GLY GLY GLY LEU THR VAL ALA THR LEU VAL ALA          
SEQRES  13 A  296  LEU ARG ASP ALA GLY VAL PRO LEU PRO ALA ALA ALA VAL          
SEQRES  14 A  296  CYS LEU SER PRO TRP VAL ASP LEU GLU GLY ILE GLY GLU          
SEQRES  15 A  296  SER MET THR THR LYS ALA ALA VAL ASP PRO MET VAL GLN          
SEQRES  16 A  296  ARG GLU PRO LEU LEU ARG MET ALA SER MET TYR LEU ALA          
SEQRES  17 A  296  GLY GLN ASP PRO ARG THR PRO LEU ALA ALA PRO LEU TYR          
SEQRES  18 A  296  ALA ASP LEU ARG GLY LEU PRO PRO LEU LEU ILE GLN VAL          
SEQRES  19 A  296  GLY THR ALA GLU THR LEU LEU ASP ASP SER VAL ARG LEU          
SEQRES  20 A  296  ALA GLU ARG ALA ARG ALA ALA GLY VAL GLN VAL THR LEU          
SEQRES  21 A  296  GLU PRO TRP GLU ASP MET ILE HIS VAL TRP GLN ALA PHE          
SEQRES  22 A  296  ALA ALA MET LEU PRO GLU GLY GLN GLN ALA ILE GLU ARG          
SEQRES  23 A  296  ILE GLY GLU PHE LEU ARG GLN HIS TRP GLN                      
HET    FMT  B 901       3                                                       
HET    FMT  B 902       3                                                       
HET    FMT  B 903       3                                                       
HET    FMT  B 904       3                                                       
HET    FMT  B 905       3                                                       
HET    ACT  B 906       4                                                       
HET    RXK  A 501       9                                                       
HET    RXK  A 502       9                                                       
HET    FMT  A 503       3                                                       
HET    ACT  A 504       4                                                       
HETNAM     FMT FORMIC ACID                                                      
HETNAM     ACT ACETATE ION                                                      
HETNAM     RXK CYCLOHEXANECARBOXYLIC ACID                                       
FORMUL   3  FMT    6(C H2 O2)                                                   
FORMUL   8  ACT    2(C2 H3 O2 1-)                                               
FORMUL   9  RXK    2()                                                          
FORMUL  13  HOH   *654(H2 O)                                                    
HELIX    1 AA1 GLU B    4  ARG B   17  1                                  14    
HELIX    2 AA2 PRO B   18  GLU B   21  5                                   4    
HELIX    3 AA3 THR B   23  GLN B   36  1                                  14    
HELIX    4 AA4 SER B   82  ARG B   98  1                                  17    
HELIX    5 AA5 PRO B  115  THR B  131  1                                  17    
HELIX    6 AA6 ASP B  134  LYS B  136  5                                   3    
HELIX    7 AA7 SER B  144  ALA B  160  1                                  17    
HELIX    8 AA8 GLY B  181  LYS B  187  1                                   7    
HELIX    9 AA9 GLN B  195  ALA B  208  1                                  14    
HELIX   10 AB1 ALA B  218  ALA B  222  5                                   5    
HELIX   11 AB2 LEU B  240  ALA B  254  1                                  15    
HELIX   12 AB3 VAL B  269  ALA B  274  5                                   6    
HELIX   13 AB4 LEU B  277  GLN B  296  1                                  20    
HELIX   14 AB5 SER A    3  ARG A   17  1                                  15    
HELIX   15 AB6 PRO A   18  GLU A   21  5                                   4    
HELIX   16 AB7 THR A   23  GLN A   36  1                                  14    
HELIX   17 AB8 SER A   82  ARG A   98  1                                  17    
HELIX   18 AB9 PRO A  115  THR A  131  1                                  17    
HELIX   19 AC1 ASP A  134  LYS A  136  5                                   3    
HELIX   20 AC2 SER A  144  ALA A  160  1                                  17    
HELIX   21 AC3 GLU A  182  LYS A  187  1                                   6    
HELIX   22 AC4 GLN A  195  ALA A  208  1                                  14    
HELIX   23 AC5 ALA A  218  ALA A  222  5                                   5    
HELIX   24 AC6 LEU A  240  ALA A  254  1                                  15    
HELIX   25 AC7 VAL A  269  ALA A  274  5                                   6    
HELIX   26 AC8 LEU A  277  TRP A  295  1                                  19    
SHEET    1 AA1 8 GLU B  45  ASP B  50  0                                        
SHEET    2 AA1 8 PRO B  55  ARG B  60 -1  O  TRP B  58   N  THR B  47           
SHEET    3 AA1 8 CYS B  99  ILE B 104 -1  O  VAL B 101   N  VAL B  59           
SHEET    4 AA1 8 ASP B  65  LEU B  73  1  N  TYR B  72   O  LEU B 102           
SHEET    5 AA1 8 MET B 138  ASP B 143  1  O  ALA B 141   N  LEU B  73           
SHEET    6 AA1 8 ALA B 167  LEU B 171  1  O  LEU B 171   N  GLY B 142           
SHEET    7 AA1 8 LEU B 230  GLY B 235  1  O  LEU B 231   N  CYS B 170           
SHEET    8 AA1 8 VAL B 258  TRP B 263  1  O  GLU B 261   N  ILE B 232           
SHEET    1 AA2 8 GLU A  45  ASP A  50  0                                        
SHEET    2 AA2 8 PRO A  55  ARG A  60 -1  O  TRP A  58   N  THR A  47           
SHEET    3 AA2 8 CYS A  99  ILE A 104 -1  O  VAL A 101   N  VAL A  59           
SHEET    4 AA2 8 ASP A  65  LEU A  73  1  N  TYR A  72   O  LEU A 102           
SHEET    5 AA2 8 MET A 138  ASP A 143  1  O  ALA A 141   N  LEU A  73           
SHEET    6 AA2 8 ALA A 167  LEU A 171  1  O  LEU A 171   N  GLY A 142           
SHEET    7 AA2 8 LEU A 230  GLY A 235  1  O  LEU A 231   N  CYS A 170           
SHEET    8 AA2 8 VAL A 258  TRP A 263  1  O  GLU A 261   N  ILE A 232           
CISPEP   1 ALA B  109    PRO B  110          0        -1.24                     
CISPEP   2 HIS B  114    PRO B  115          0         7.58                     
CISPEP   3 ALA A  109    PRO A  110          0         1.47                     
CISPEP   4 HIS A  114    PRO A  115          0         6.72                     
SITE     1 AC1  7 VAL A 258  THR A 259  PRO B  22  ARG B 201                    
SITE     2 AC1  7 MET B 205  HOH B1019  HOH B1094                               
SITE     1 AC2  2 PHE B 273  MET B 276                                          
SITE     1 AC3  4 TRP B  58  ARG B  60  ARG B 100  HOH B1025                    
SITE     1 AC4  1 ARG B  98                                                     
SITE     1 AC5  1 THR B  85                                                     
SITE     1 AC6  5 GLY B  76  GLY B  77  SER B 144  ALA B 145                    
SITE     2 AC6  5 HIS B 268                                                     
SITE     1 AC7  8 TYR A 221  ASP A 223  ARG A 250  HOH A 608                    
SITE     2 AC7  8 HOH A 634  ASN B  11  ARG B  14  SER B  15                    
SITE     1 AC8  5 THR A  85  MET A 193  ALA A 272  HOH A 603                    
SITE     2 AC8  5 HOH A 777                                                     
SITE     1 AC9  3 VAL A  49  HOH A 622  HOH A 641                               
SITE     1 AD1  5 GLY A  76  GLY A  77  SER A 144  ALA A 145                    
SITE     2 AD1  5 HIS A 268                                                     
CRYST1   47.848   80.220  144.582  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020900  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012466  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006916        0.00000                         
TER    2325      GLN B 296                                                      
TER    4676      GLN A 296                                                      
MASTER      372    0   10   26   16    0   15    6 5194    2   44   46          
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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