Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 4BVJ-pdb

Name Class
4BVJ-pdb
HEADER    HYDROLASE                               26-JUN-13   4BVJ              
TITLE     STRUCTURE OF Y105A MUTANT OF PHAZ7 PHB DEPOLYMERASE                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHB DEPOLYMERASE PHAZ7;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 39-380;                                           
COMPND   5 EC: 3.1.1.75;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PAUCIMONAS LEMOIGNEI;                           
SOURCE   3 ORGANISM_TAXID: 29443;                                               
SOURCE   4 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;                                
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 1423;                                       
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: WB800                                      
KEYWDS    HYDROLASE, CATALYTIC TRIAD, BIOPOLYMER BINDING                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.HERMAWAN,B.SUBEDI,A.C.PAPAGEORGIOU,D.JENDROSSEK                     
REVDAT   1   18-SEP-13 4BVJ    0                                                
JRNL        AUTH   D.JENDROSSEK,S.HERMAWAN,B.SUBEDI,A.C.PAPAGEORGIOU            
JRNL        TITL   BIOCHEMICAL ANALYSIS AND STRUCTURE DETERMINATION OF          
JRNL        TITL 2 PAUCIMONAS LEMOIGNEI POLY(3-HYDROXYBUTYRATE) (PHB)           
JRNL        TITL 3 DEPOLYMERASE PHAZ7 MUTEINS REVEAL THE PHB BINDING SITE AND   
JRNL        TITL 4 DETAILS OF SUBSTRATE-ENZYME INTERACTIONS.                    
JRNL        REF    MOL.MICROBIOL.                             2013              
JRNL        REFN                   ESSN 1365-2958                               
JRNL        PMID   24007310                                                     
JRNL        DOI    10.1111/MMI.12391                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.C.PAPAGEORGIOU,S.HERMAWAN,C.B.SINGH,D.JENDROSSEK           
REMARK   1  TITL   STRUCTURAL BASIS OF POLY(3-HYDROXYBUTYRATE) HYDROLYSIS BY    
REMARK   1  TITL 2 PHAZ7 DEPOLYMERASE FROM PAUCIMONAS LEMOIGNEI.                
REMARK   1  REF    J.MOL.BIOL.                   V. 382  1184 2008              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   18706425                                                     
REMARK   1  DOI    10.1016/J.JMB.2008.07.078                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.599                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.005                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.99                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.94                          
REMARK   3   NUMBER OF REFLECTIONS             : 84894                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1569                          
REMARK   3   R VALUE            (WORKING SET) : 0.1553                          
REMARK   3   FREE R VALUE                     : 0.1887                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 4245                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 20.0066 -  4.9444    0.98     2688   142  0.1487 0.1718        
REMARK   3     2  4.9444 -  3.9343    0.99     2692   142  0.1191 0.1364        
REMARK   3     3  3.9343 -  3.4398    0.98     2670   140  0.1213 0.1475        
REMARK   3     4  3.4398 -  3.1266    0.99     2697   142  0.1341 0.1736        
REMARK   3     5  3.1266 -  2.9032    0.99     2700   142  0.1434 0.1751        
REMARK   3     6  2.9032 -  2.7325    0.99     2685   142  0.1448 0.1596        
REMARK   3     7  2.7325 -  2.5959    0.99     2689   141  0.1478 0.1605        
REMARK   3     8  2.5959 -  2.4832    0.99     2743   145  0.1480 0.1956        
REMARK   3     9  2.4832 -  2.3877    0.99     2723   143  0.1483 0.1839        
REMARK   3    10  2.3877 -  2.3055    0.99     2633   138  0.1464 0.1778        
REMARK   3    11  2.3055 -  2.2335    0.99     2739   145  0.1454 0.1875        
REMARK   3    12  2.2335 -  2.1697    1.00     2696   141  0.1395 0.1603        
REMARK   3    13  2.1697 -  2.1126    1.00     2671   141  0.1447 0.1879        
REMARK   3    14  2.1126 -  2.0612    0.99     2739   144  0.1551 0.1867        
REMARK   3    15  2.0612 -  2.0143    1.00     2687   142  0.1578 0.2155        
REMARK   3    16  2.0143 -  1.9715    1.00     2724   143  0.1579 0.2101        
REMARK   3    17  1.9715 -  1.9321    0.99     2676   141  0.1603 0.2058        
REMARK   3    18  1.9321 -  1.8957    0.99     2726   143  0.1690 0.2294        
REMARK   3    19  1.8957 -  1.8618    0.99     2677   141  0.1755 0.2302        
REMARK   3    20  1.8618 -  1.8303    1.00     2734   144  0.1801 0.1965        
REMARK   3    21  1.8303 -  1.8008    0.99     2664   140  0.1925 0.2273        
REMARK   3    22  1.8008 -  1.7731    0.99     2697   142  0.1981 0.2474        
REMARK   3    23  1.7731 -  1.7471    0.99     2721   143  0.1946 0.2322        
REMARK   3    24  1.7471 -  1.7225    0.99     2625   139  0.2014 0.2333        
REMARK   3    25  1.7225 -  1.6992    0.99     2727   143  0.2023 0.2410        
REMARK   3    26  1.6992 -  1.6771    0.99     2710   143  0.2161 0.2594        
REMARK   3    27  1.6771 -  1.6562    0.99     2632   138  0.2161 0.2501        
REMARK   3    28  1.6562 -  1.6362    0.99     2720   143  0.2303 0.2681        
REMARK   3    29  1.6362 -  1.6172    0.99     2711   143  0.2518 0.2930        
REMARK   3    30  1.6172 -  1.5991    0.92     2453   129  0.2581 0.3142        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.17             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.23            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.2                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.1                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           5251                                  
REMARK   3   ANGLE     :  1.082           7136                                  
REMARK   3   CHIRALITY :  0.074            755                                  
REMARK   3   PLANARITY :  0.005            929                                  
REMARK   3   DIHEDRAL  : 12.491           1774                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4BVJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUN-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-57421.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-NOV-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X13                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8123                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 84896                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.60                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 2.6                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.70                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.48                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.00                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4BRS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOUR DIFFUSION  HANGING DROP,          
REMARK 280  PROTEIN CONCENTRATION 10 MG/ML, 0.1 M NAOAC (PH 5.0), 0.2           
REMARK 280  M NH4CL, 20% W/V PEG6000                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000      100.02500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     TYR A 293    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN A 294    CG   OD1  ND2                                       
REMARK 470     TYR B 293    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN B 294    CG   OD1  ND2                                       
REMARK 470     ASN B 343    CA   C    O    CB   CG   OD1  ND2                   
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   NZ   LYS A    40     O    HOH A  2158              1.99            
REMARK 500   OH   TYR A   148     O    HOH A  2377              2.06            
REMARK 500   OD1  ASN A   150     O    HOH A  2383              2.01            
REMARK 500   N    GLY A   205     O    HOH A  2454              2.11            
REMARK 500   OH   TYR B   148     O    HOH B  2389              2.16            
REMARK 500   OD1  ASN B   150     O    HOH B  2397              2.18            
REMARK 500   O    TYR B   204     O    HOH B  2468              2.20            
REMARK 500   N    ASN B   343     O    HOH B  2518              2.19            
REMARK 500   O    HOH A  2039     O    HOH A  2091              2.12            
REMARK 500   O    HOH A  2039     O    HOH A  2040              2.16            
REMARK 500   O    HOH A  2040     O    HOH A  2092              2.08            
REMARK 500   O    HOH A  2041     O    HOH A  2093              2.02            
REMARK 500   O    HOH A  2055     O    HOH A  2112              2.16            
REMARK 500   O    HOH A  2056     O    HOH A  2059              2.07            
REMARK 500   O    HOH A  2059     O    HOH A  2064              2.17            
REMARK 500   O    HOH A  2062     O    HOH A  2179              1.97            
REMARK 500   O    HOH A  2072     O    HOH B  2342              2.14            
REMARK 500   O    HOH A  2072     O    HOH B  2602              2.04            
REMARK 500   O    HOH A  2075     O    HOH A  2148              1.93            
REMARK 500   O    HOH A  2081     O    HOH A  2156              1.98            
REMARK 500   O    HOH A  2096     O    HOH A  2104              2.10            
REMARK 500   O    HOH A  2111     O    HOH A  2112              1.92            
REMARK 500   O    HOH A  2121     O    HOH A  2224              2.02            
REMARK 500   O    HOH A  2126     O    HOH A  2129              2.09            
REMARK 500   O    HOH A  2144     O    HOH A  2605              2.13            
REMARK 500   O    HOH A  2149     O    HOH A  2295              1.27            
REMARK 500   O    HOH A  2150     O    HOH A  2151              1.97            
REMARK 500   O    HOH A  2152     O    HOH A  2293              2.18            
REMARK 500   O    HOH A  2171     O    HOH A  2369              2.16            
REMARK 500   O    HOH A  2173     O    HOH A  2367              2.18            
REMARK 500   O    HOH A  2173     O    HOH A  2368              1.94            
REMARK 500   O    HOH A  2187     O    HOH A  2188              2.12            
REMARK 500   O    HOH A  2218     O    HOH A  2396              2.15            
REMARK 500   O    HOH A  2233     O    HOH A  2237              1.73            
REMARK 500   O    HOH A  2242     O    HOH A  2243              2.07            
REMARK 500   O    HOH A  2246     O    HOH A  2378              1.92            
REMARK 500   O    HOH A  2253     O    HOH A  2457              2.13            
REMARK 500   O    HOH A  2273     O    HOH A  2274              2.01            
REMARK 500   O    HOH A  2283     O    HOH A  2480              2.15            
REMARK 500   O    HOH A  2291     O    HOH A  2538              1.98            
REMARK 500   O    HOH A  2302     O    HOH A  2305              1.95            
REMARK 500   O    HOH A  2318     O    HOH A  2549              2.02            
REMARK 500   O    HOH A  2319     O    HOH A  2546              2.18            
REMARK 500   O    HOH A  2324     O    HOH A  2326              2.04            
REMARK 500   O    HOH A  2325     O    HOH A  2551              2.17            
REMARK 500   O    HOH A  2368     O    HOH A  2369              2.05            
REMARK 500   O    HOH A  2397     O    HOH A  2398              2.13            
REMARK 500   O    HOH A  2535     O    HOH A  2536              2.11            
REMARK 500   O    HOH A  2548     O    HOH A  2550              2.18            
REMARK 500   O    HOH A  2560     O    HOH A  2561              1.93            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      92 CLOSE CONTACTS                                
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 A  2251     O    HOH B  2439     2545     1.97            
REMARK 500   O    HOH B  2028     O    HOH B  2377     1655     2.18            
REMARK 500   O    HOH B  2047     O    HOH B  2220     1454     2.10            
REMARK 500   O    HOH B  2163     O    HOH B  2577     1454     2.11            
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    THR A  14      116.29    -39.63                                   
REMARK 500    SER A 136     -128.05     55.49                                   
REMARK 500    ARG A 156      -62.93    -93.39                                   
REMARK 500    ALA A 177       43.77   -140.19                                   
REMARK 500    ALA A 181       63.66   -151.84                                   
REMARK 500    ASN A 210       82.27   -157.99                                   
REMARK 500    PHE A 251       48.47   -140.93                                   
REMARK 500    ALA B  23       84.91   -155.59                                   
REMARK 500    SER B 136     -128.76     58.38                                   
REMARK 500    ARG B 156      -60.75    -93.41                                   
REMARK 500    ALA B 177       36.22   -146.49                                   
REMARK 500    ALA B 181       65.54   -153.15                                   
REMARK 500    SER B 186     -153.97    -88.30                                   
REMARK 500    ASN B 210       84.44   -156.91                                   
REMARK 500    ARG B 228       64.23   -119.25                                   
REMARK 500    ALA B 295       50.60   -110.85                                   
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 A2608        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH A2609        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH A2610        DISTANCE =  7.17 ANGSTROMS                       
REMARK 525    HOH A2611        DISTANCE =  9.31 ANGSTROMS                       
REMARK 525    HOH B2066        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH B2077        DISTANCE =  7.31 ANGSTROMS                       
REMARK 525    HOH B2266        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH B2619        DISTANCE =  7.73 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 601  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2606   O                                                      
REMARK 620 2 HOH A2605   O   101.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 501  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2616   O                                                      
REMARK 620 2 HOH B2618   O   100.1                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA B 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4BTV   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF PHAZ7 PHB DEPOLYMERASE IN COMPLEX WITH                 
REMARK 900  3HB TRIMER                                                          
REMARK 900 RELATED ID: 4BVK   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF Y190E MUTANT OF PHAZ7 PHB DEPOLYMERASE                 
REMARK 900 RELATED ID: 4BVL   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF 202-208 DELETION MUTANT OF PHAZ7 PHB                   
REMARK 900  DEPOLYMERASE                                                        
DBREF  4BVJ A    1   342  UNP    Q939Q9   Q939Q9_PSELE    39    380             
DBREF  4BVJ B    1   342  UNP    Q939Q9   Q939Q9_PSELE    39    380             
SEQADV 4BVJ ALA A  105  UNP  Q939Q9    TYR   143 ENGINEERED MUTATION            
SEQADV 4BVJ ASN A  343  UNP  Q939Q9              EXPRESSION TAG                 
SEQADV 4BVJ ALA B  105  UNP  Q939Q9    TYR   143 ENGINEERED MUTATION            
SEQADV 4BVJ ASN B  343  UNP  Q939Q9              EXPRESSION TAG                 
SEQRES   1 A  343  LEU THR CYS GLY THR ASN SER GLY PHE VAL CYS LYS GLY          
SEQRES   2 A  343  THR GLN THR GLN TYR ALA GLY GLY PHE ALA PRO GLY VAL          
SEQRES   3 A  343  GLY TYR GLY GLY PHE GLY GLY GLY SER CYS THR ALA THR          
SEQRES   4 A  343  LYS THR PRO VAL ILE PHE ILE HIS GLY ASN GLY ASP ASN          
SEQRES   5 A  343  ALA ILE SER PHE ASP MET PRO PRO GLY ASN VAL SER GLY          
SEQRES   6 A  343  TYR GLY THR PRO ALA ARG SER VAL TYR ALA GLU LEU LYS          
SEQRES   7 A  343  ALA ARG GLY TYR ASN ASP CYS GLU ILE PHE GLY VAL THR          
SEQRES   8 A  343  TYR LEU SER SER SER GLU GLN GLY SER ALA GLN TYR ASN          
SEQRES   9 A  343  ALA HIS SER SER THR LYS TYR ALA ILE ILE LYS THR PHE          
SEQRES  10 A  343  ILE ASP LYS VAL LYS ALA TYR THR GLY LYS SER GLN VAL          
SEQRES  11 A  343  ASP ILE VAL ALA HIS SER MET GLY VAL SER MET SER LEU          
SEQRES  12 A  343  ALA THR LEU GLN TYR TYR ASN ASN TRP THR SER VAL ARG          
SEQRES  13 A  343  LYS PHE ILE ASN LEU ALA GLY GLY ILE ARG GLY LEU TYR          
SEQRES  14 A  343  SER CYS TYR TYR THR GLY TYR ALA ASN ALA ALA ALA PRO          
SEQRES  15 A  343  THR CYS GLY SER GLN ASN TYR TYR ASN SER TYR THR PHE          
SEQRES  16 A  343  GLY PHE PHE PRO GLU GLY TRP TYR TYR GLY VAL TRP VAL          
SEQRES  17 A  343  SER ASN PRO TRP THR GLY SER GLY SER THR ASN SER MET          
SEQRES  18 A  343  ARG ASP MET PRO ALA LYS ARG THR ALA VAL SER PHE TYR          
SEQRES  19 A  343  THR LEU SER ALA GLY PHE LYS ASP GLN VAL GLY CYS ALA          
SEQRES  20 A  343  THR ALA SER PHE TRP ALA GLY CYS ASP SER ALA ALA LYS          
SEQRES  21 A  343  PHE ALA SER THR THR SER ASN VAL LYS ALA GLN ILE ASN          
SEQRES  22 A  343  VAL GLY ALA GLY SER ASN ALA THR GLN ALA ASP TYR ASP          
SEQRES  23 A  343  TRP ALA ASP GLY MET PRO TYR ASN ALA GLY GLY GLY ASP          
SEQRES  24 A  343  THR THR ASN GLY VAL GLY HIS PHE ARG THR LYS THR ASN          
SEQRES  25 A  343  THR GLY ALA ILE ILE GLN ARG MET LEU LEU THR THR CYS          
SEQRES  26 A  343  THR GLY LEU ASP CYS ALA ALA GLU TYR THR THR GLY PRO          
SEQRES  27 A  343  LYS ALA ALA TYR ASN                                          
SEQRES   1 B  343  LEU THR CYS GLY THR ASN SER GLY PHE VAL CYS LYS GLY          
SEQRES   2 B  343  THR GLN THR GLN TYR ALA GLY GLY PHE ALA PRO GLY VAL          
SEQRES   3 B  343  GLY TYR GLY GLY PHE GLY GLY GLY SER CYS THR ALA THR          
SEQRES   4 B  343  LYS THR PRO VAL ILE PHE ILE HIS GLY ASN GLY ASP ASN          
SEQRES   5 B  343  ALA ILE SER PHE ASP MET PRO PRO GLY ASN VAL SER GLY          
SEQRES   6 B  343  TYR GLY THR PRO ALA ARG SER VAL TYR ALA GLU LEU LYS          
SEQRES   7 B  343  ALA ARG GLY TYR ASN ASP CYS GLU ILE PHE GLY VAL THR          
SEQRES   8 B  343  TYR LEU SER SER SER GLU GLN GLY SER ALA GLN TYR ASN          
SEQRES   9 B  343  ALA HIS SER SER THR LYS TYR ALA ILE ILE LYS THR PHE          
SEQRES  10 B  343  ILE ASP LYS VAL LYS ALA TYR THR GLY LYS SER GLN VAL          
SEQRES  11 B  343  ASP ILE VAL ALA HIS SER MET GLY VAL SER MET SER LEU          
SEQRES  12 B  343  ALA THR LEU GLN TYR TYR ASN ASN TRP THR SER VAL ARG          
SEQRES  13 B  343  LYS PHE ILE ASN LEU ALA GLY GLY ILE ARG GLY LEU TYR          
SEQRES  14 B  343  SER CYS TYR TYR THR GLY TYR ALA ASN ALA ALA ALA PRO          
SEQRES  15 B  343  THR CYS GLY SER GLN ASN TYR TYR ASN SER TYR THR PHE          
SEQRES  16 B  343  GLY PHE PHE PRO GLU GLY TRP TYR TYR GLY VAL TRP VAL          
SEQRES  17 B  343  SER ASN PRO TRP THR GLY SER GLY SER THR ASN SER MET          
SEQRES  18 B  343  ARG ASP MET PRO ALA LYS ARG THR ALA VAL SER PHE TYR          
SEQRES  19 B  343  THR LEU SER ALA GLY PHE LYS ASP GLN VAL GLY CYS ALA          
SEQRES  20 B  343  THR ALA SER PHE TRP ALA GLY CYS ASP SER ALA ALA LYS          
SEQRES  21 B  343  PHE ALA SER THR THR SER ASN VAL LYS ALA GLN ILE ASN          
SEQRES  22 B  343  VAL GLY ALA GLY SER ASN ALA THR GLN ALA ASP TYR ASP          
SEQRES  23 B  343  TRP ALA ASP GLY MET PRO TYR ASN ALA GLY GLY GLY ASP          
SEQRES  24 B  343  THR THR ASN GLY VAL GLY HIS PHE ARG THR LYS THR ASN          
SEQRES  25 B  343  THR GLY ALA ILE ILE GLN ARG MET LEU LEU THR THR CYS          
SEQRES  26 B  343  THR GLY LEU ASP CYS ALA ALA GLU TYR THR THR GLY PRO          
SEQRES  27 B  343  LYS ALA ALA TYR ASN                                          
HET     NA  A 501       1                                                       
HET     NA  A 601       1                                                       
HET     NA  B 501       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   2   NA    3(NA 1+)                                                     
FORMUL   3  HOH   *1230(H2 O)                                                   
HELIX    1   1 ASN A   52  MET A   58  5                                   7    
HELIX    2   2 SER A   72  ARG A   80  1                                   9    
HELIX    3   3 SER A   94  GLY A   99  1                                   6    
HELIX    4   4 SER A  100  ASN A  104  5                                   5    
HELIX    5   5 SER A  107  GLY A  126  1                                  20    
HELIX    6   6 SER A  136  ASN A  150  1                                  15    
HELIX    7   7 ASN A  151  THR A  153  5                                   3    
HELIX    8   8 LEU A  168  TYR A  172  5                                   5    
HELIX    9   9 ALA A  181  GLY A  185  5                                   5    
HELIX   10  10 SER A  220  ARG A  222  5                                   3    
HELIX   11  11 ASP A  223  ARG A  228  1                                   6    
HELIX   12  12 ALA A  238  ASP A  242  5                                   5    
HELIX   13  13 GLY A  254  ALA A  258  5                                   5    
HELIX   14  14 ASP A  286  GLY A  290  5                                   5    
HELIX   15  15 PHE A  307  ASN A  312  1                                   6    
HELIX   16  16 THR A  313  THR A  323  1                                  11    
HELIX   17  17 THR A  326  ALA A  332  5                                   7    
HELIX   18  18 ASN B   52  MET B   58  5                                   7    
HELIX   19  19 SER B   72  ARG B   80  1                                   9    
HELIX   20  20 SER B   94  GLY B   99  1                                   6    
HELIX   21  21 SER B  100  ASN B  104  5                                   5    
HELIX   22  22 SER B  107  GLY B  126  1                                  20    
HELIX   23  23 SER B  136  ASN B  150  1                                  15    
HELIX   24  24 ASN B  151  THR B  153  5                                   3    
HELIX   25  25 LEU B  168  TYR B  172  5                                   5    
HELIX   26  26 ALA B  181  GLY B  185  5                                   5    
HELIX   27  27 SER B  220  ARG B  222  5                                   3    
HELIX   28  28 ASP B  223  ARG B  228  1                                   6    
HELIX   29  29 ALA B  238  LYS B  241  5                                   4    
HELIX   30  30 ASP B  242  ALA B  247  1                                   6    
HELIX   31  31 GLY B  254  ALA B  258  5                                   5    
HELIX   32  32 ASP B  286  GLY B  290  5                                   5    
HELIX   33  33 PHE B  307  ASN B  312  1                                   6    
HELIX   34  34 THR B  313  THR B  323  1                                  11    
HELIX   35  35 THR B  326  ALA B  332  5                                   7    
SHEET    1  AA 9 THR A  16  TYR A  18  0                                        
SHEET    2  AA 9 GLY A  30  GLY A  32  1  O  GLY A  30   N  GLN A  17           
SHEET    3  AA 9 ILE A  87  VAL A  90 -1  O  GLY A  89   N  PHE A  31           
SHEET    4  AA 9 VAL A  43  ILE A  46  1  O  VAL A  43   N  PHE A  88           
SHEET    5  AA 9 VAL A 130  HIS A 135  1  O  ASP A 131   N  ILE A  44           
SHEET    6  AA 9 VAL A 155  LEU A 161  1  N  ARG A 156   O  VAL A 130           
SHEET    7  AA 9 SER A 232  SER A 237  1  O  SER A 232   N  PHE A 158           
SHEET    8  AA 9 VAL A 268  ASN A 273  1  N  LYS A 269   O  PHE A 233           
SHEET    9  AA 9 ALA A 340  ALA A 341 -1  O  ALA A 340   N  ASN A 273           
SHEET    1  AB 2 GLY A 201  TYR A 203  0                                        
SHEET    2  AB 2 VAL A 206  VAL A 208 -1  O  VAL A 206   N  TYR A 203           
SHEET    1  BA 9 THR B  16  TYR B  18  0                                        
SHEET    2  BA 9 GLY B  30  GLY B  32  1  O  GLY B  30   N  GLN B  17           
SHEET    3  BA 9 ILE B  87  VAL B  90 -1  O  GLY B  89   N  PHE B  31           
SHEET    4  BA 9 VAL B  43  ILE B  46  1  O  VAL B  43   N  PHE B  88           
SHEET    5  BA 9 VAL B 130  HIS B 135  1  O  ASP B 131   N  ILE B  44           
SHEET    6  BA 9 VAL B 155  LEU B 161  1  N  ARG B 156   O  VAL B 130           
SHEET    7  BA 9 SER B 232  SER B 237  1  O  SER B 232   N  PHE B 158           
SHEET    8  BA 9 VAL B 268  ASN B 273  1  N  LYS B 269   O  PHE B 233           
SHEET    9  BA 9 ALA B 340  ALA B 341 -1  O  ALA B 340   N  ASN B 273           
SHEET    1  BB 2 GLY B 201  TYR B 203  0                                        
SHEET    2  BB 2 VAL B 206  VAL B 208 -1  O  VAL B 206   N  TYR B 203           
SSBOND   1 CYS A    3    CYS A   11                          1555   1555  2.03  
SSBOND   2 CYS A   36    CYS A   85                          1555   1555  2.04  
SSBOND   3 CYS A  171    CYS A  184                          1555   1555  2.04  
SSBOND   4 CYS A  246    CYS A  255                          1555   1555  2.04  
SSBOND   5 CYS A  325    CYS A  330                          1555   1555  2.02  
SSBOND   6 CYS B    3    CYS B   11                          1555   1555  2.04  
SSBOND   7 CYS B   36    CYS B   85                          1555   1555  2.03  
SSBOND   8 CYS B  171    CYS B  184                          1555   1555  2.04  
SSBOND   9 CYS B  246    CYS B  255                          1555   1555  2.04  
SSBOND  10 CYS B  325    CYS B  330                          1555   1555  2.02  
LINK        NA    NA A 601                 O   HOH A2606     1555   1555  2.95  
LINK        NA    NA A 601                 O   HOH A2605     1555   1555  3.01  
LINK        NA    NA B 501                 O   HOH B2618     1555   1555  3.18  
LINK        NA    NA B 501                 O   HOH B2616     1555   1555  3.04  
SITE     1 AC1  2 ASN A  83  ASP A  84                                          
SITE     1 AC2  4 CYS A  36  THR A  37  HOH A2605  HOH A2606                    
SITE     1 AC3  4 ALA B  23  PRO B  24  GLY B  25  HOH B2616                    
CRYST1   41.370  200.050   44.180  90.00 114.28  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      0.024172  0.000000  0.010904        0.00000                         
SCALE2      0.000000  0.004999  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.024831        0.00000                         
TER    2561      ASN A 343                                                      
TER    5104      ASN B 343                                                      
MASTER      417    0    3   35   22    0    3    6 6335    2   26   54          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer