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LongText Report for: 5zrs-pdb

Name Class
5zrs-pdb
HEADER    HYDROLASE                               25-APR-18   5ZRS              
TITLE     CRYSTAL STRUCTURE OF PET-DEGRADING CUTINASE CUT190 S176A/S226P/R228S  
TITLE    2 MUTANT IN MONOETHYL ADIPATE BOUND STATE                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA/BETA HYDROLASE FAMILY PROTEIN;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CUTINASE;                                                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMONOSPORA VIRIDIS;                      
SOURCE   3 ORGANISM_TAXID: 1852;                                                
SOURCE   4 GENE: CUT190, SAMN02982918_2340;                                     
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: ROSETTA-GAMI B (DE3);                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PQE80L                                    
KEYWDS    POLYESTERASE, ALPHA/BETA-HYDROLASE FOLD, PROTEIN ENGINEERING,         
KEYWDS   2 THERMOSTABILITY, HYDROLASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.NUMOTO,N.KAMIYA,G.J.BEKKER,Y.YAMAGAMI,S.INABA,K.ISHII,S.UCHIYAMA,   
AUTHOR   2 F.KAWAI,N.ITO,M.ODA                                                  
REVDAT   1   12-SEP-18 5ZRS    0                                                
JRNL        AUTH   N.NUMOTO,N.KAMIYA,G.J.BEKKER,Y.YAMAGAMI,S.INABA,K.ISHII,     
JRNL        AUTH 2 S.UCHIYAMA,F.KAWAI,N.ITO,M.ODA                               
JRNL        TITL   STRUCTURAL DYNAMICS OF THE PET-DEGRADING CUTINASE-LIKE       
JRNL        TITL 2 ENZYME FROM SACCHAROMONOSPORA VIRIDIS AHK190 IN              
JRNL        TITL 3 SUBSTRATE-BOUND STATES ELUCIDATES THE CA2+-DRIVEN CATALYTIC  
JRNL        TITL 4 CYCLE.                                                       
JRNL        REF    BIOCHEMISTRY                               2018              
JRNL        REFN                   ISSN 1520-4995                               
JRNL        PMID   30110540                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.8B00624                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.61                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.349                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 50518                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.192                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.004                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2528                            
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 49.6389 -  3.6743    1.00     2861   150  0.1451 0.1696        
REMARK   3     2  3.6743 -  2.9165    1.00     2725   143  0.1380 0.1639        
REMARK   3     3  2.9165 -  2.5478    1.00     2712   142  0.1470 0.1700        
REMARK   3     4  2.5478 -  2.3149    1.00     2705   145  0.1421 0.1643        
REMARK   3     5  2.3149 -  2.1490    1.00     2685   139  0.1379 0.1801        
REMARK   3     6  2.1490 -  2.0223    1.00     2647   139  0.1409 0.1799        
REMARK   3     7  2.0223 -  1.9210    1.00     2665   140  0.1407 0.1712        
REMARK   3     8  1.9210 -  1.8374    1.00     2656   143  0.1465 0.2022        
REMARK   3     9  1.8374 -  1.7666    1.00     2660   139  0.1528 0.1750        
REMARK   3    10  1.7666 -  1.7057    1.00     2651   138  0.1670 0.2043        
REMARK   3    11  1.7057 -  1.6523    1.00     2666   142  0.1696 0.2311        
REMARK   3    12  1.6523 -  1.6051    1.00     2635   141  0.1805 0.2118        
REMARK   3    13  1.6051 -  1.5628    1.00     2618   135  0.1951 0.2100        
REMARK   3    14  1.5628 -  1.5247    1.00     2647   137  0.2072 0.2281        
REMARK   3    15  1.5247 -  1.4900    1.00     2610   137  0.2349 0.2585        
REMARK   3    16  1.4900 -  1.4583    1.00     2655   143  0.2512 0.2803        
REMARK   3    17  1.4583 -  1.4291    1.00     2633   138  0.2709 0.3152        
REMARK   3    18  1.4291 -  1.4022    0.99     2559   137  0.2997 0.2994        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.121            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.674           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 10.04                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.78                          
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      :  0.009           2127                                  
REMARK   3   ANGLE     :  1.342           2893                                  
REMARK   3   CHIRALITY :  0.086            308                                  
REMARK   3   PLANARITY :  0.007            383                                  
REMARK   3   DIHEDRAL  : 11.424            789                                  
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 5ZRS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-MAY-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300007545.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-NOV-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-1A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1000                             
REMARK 200  MONOCHROMATOR                  : CRYO-COOLED CHANNEL-CUT SI(111)    
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 4M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50522                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11900                            
REMARK 200   FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.80400                            
REMARK 200   FOR SHELL         : 2.100                              
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: 4WFJ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01 M ZNSO4 0.1 M MES PH 6.5 25% V/V    
REMARK 280  PEG MME 550, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K        
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       25.22850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.39250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.92800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.39250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.22850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.92800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 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     LEU A   306                                                      
REMARK 465     ASN A   307                                                      
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 A   501     O    HOH A   573              2.04            
REMARK 500   O    HOH A   739     O    HOH A   775              2.07            
REMARK 500   O3   GOL A   407     O    HOH A   501              2.10            
REMARK 500   O    HOH A   504     O    HOH A   606              2.13            
REMARK 500   O    HOH A   509     O    HOH A   742              2.14            
REMARK 500   O    HOH A   638     O    HOH A   750              2.15            
REMARK 500   OAI  9J6 A   401     O    HOH A   502              2.17            
REMARK 500   O    HOH A   782     O    HOH A   879              2.17            
REMARK 500   O    HOH A   730     O    HOH A   806              2.18            
REMARK 500   O    HOH A   579     O    HOH A   685              2.19            
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    ASN A  47      109.63   -162.94                                   
REMARK 500    THR A 107       -3.74     70.73                                   
REMARK 500    ALA A 176     -119.66     66.30                                   
REMARK 500    THR A 199       57.86     32.44                                   
REMARK 500    HIS A 230      -88.42   -117.16                                   
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 A 890        DISTANCE =  6.56 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                              ZN A 404  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A  43   N                                                      
REMARK 620 2 GLY A  43   O    77.6                                              
REMARK 620 3 ASP A  46   OD1 143.0  84.7                                        
REMARK 620 4 ASP A  46   OD2  91.5  84.5  54.2                                  
REMARK 620 5 GLU A  50   OE2 119.9 103.1  95.5 148.5                            
REMARK 620 6 HOH A 653   O    91.9 168.7 101.8  91.9  85.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 405  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  76   O                                                      
REMARK 620 2 ALA A  78   O   100.4                                              
REMARK 620 3 PHE A  81   O   100.7  82.8                                        
REMARK 620 4 HOH A 617   O   165.8  93.5  83.8                                  
REMARK 620 5 HOH A 660   O    88.6 166.5  85.6  78.3                            
REMARK 620 6 HOH A 772   O    96.6  93.0 162.7  79.7  96.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 403  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 204   OD1                                                    
REMARK 620 2 THR A 206   O    93.1                                              
REMARK 620 3 THR A 206   OG1  85.2  80.2                                        
REMARK 620 4 HOH A 663   O    87.9 156.5  76.5                                  
REMARK 620 5 HOH A 662   O   164.2  78.3  80.3  94.8                            
REMARK 620 6 HOH A 652   O   106.4  81.4 158.7 120.8  85.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 220   OE1                                                    
REMARK 620 2 GLU A 220   OE2  55.4                                              
REMARK 620 3 ASP A 250   OD1 100.7 155.9                                        
REMARK 620 4 GLU A 296   OE1 104.9  86.6  98.1                                  
REMARK 620 5 GLU A 118   OE2  61.7 108.8  49.6  80.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9J6 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 407                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5ZNO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5ZRQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5ZRR   RELATED DB: PDB                                   
DBREF  5ZRS A   45   304  UNP    W0TJ64   W0TJ64_9PSEU    45    304             
SEQADV 5ZRS GLY A   43  UNP  W0TJ64              EXPRESSION TAG                 
SEQADV 5ZRS PRO A   44  UNP  W0TJ64              EXPRESSION TAG                 
SEQADV 5ZRS ALA A  176  UNP  W0TJ64    SER   176 ENGINEERED MUTATION            
SEQADV 5ZRS PRO A  226  UNP  W0TJ64    SER   226 ENGINEERED MUTATION            
SEQADV 5ZRS SER A  228  UNP  W0TJ64    ARG   228 ENGINEERED MUTATION            
SEQADV 5ZRS LYS A  305  UNP  W0TJ64              EXPRESSION TAG                 
SEQADV 5ZRS LEU A  306  UNP  W0TJ64              EXPRESSION TAG                 
SEQADV 5ZRS ASN A  307  UNP  W0TJ64              EXPRESSION TAG                 
SEQRES   1 A  265  GLY PRO GLN ASP ASN PRO TYR GLU ARG GLY PRO ASP PRO          
SEQRES   2 A  265  THR GLU ASP SER ILE GLU ALA ILE ARG GLY PRO PHE SER          
SEQRES   3 A  265  VAL ALA THR GLU ARG VAL SER SER PHE ALA SER GLY PHE          
SEQRES   4 A  265  GLY GLY GLY THR ILE TYR TYR PRO ARG GLU THR ASP GLU          
SEQRES   5 A  265  GLY THR PHE GLY ALA VAL ALA VAL ALA PRO GLY PHE THR          
SEQRES   6 A  265  ALA SER GLN GLY SER MET SER TRP TYR GLY GLU ARG VAL          
SEQRES   7 A  265  ALA SER GLN GLY PHE ILE VAL PHE THR ILE ASP THR ASN          
SEQRES   8 A  265  THR ARG LEU ASP GLN PRO GLY GLN ARG GLY ARG GLN LEU          
SEQRES   9 A  265  LEU ALA ALA LEU ASP TYR LEU VAL GLU ARG SER ASP ARG          
SEQRES  10 A  265  LYS VAL ARG GLU ARG LEU ASP PRO ASN ARG LEU ALA VAL          
SEQRES  11 A  265  MET GLY HIS ALA MET GLY GLY GLY GLY SER LEU GLU ALA          
SEQRES  12 A  265  THR VAL MHO ARG PRO SER LEU LYS ALA SER ILE PRO LEU          
SEQRES  13 A  265  THR PRO TRP ASN LEU ASP LYS THR TRP GLY GLN VAL GLN          
SEQRES  14 A  265  VAL PRO THR PHE ILE ILE GLY ALA GLU LEU ASP THR ILE          
SEQRES  15 A  265  ALA PRO VAL SER THR HIS ALA LYS PRO PHE TYR GLU SER          
SEQRES  16 A  265  LEU PRO SER SER LEU PRO LYS ALA TYR MET GLU LEU ASP          
SEQRES  17 A  265  GLY ALA THR HIS PHE ALA PRO ASN ILE PRO ASN THR THR          
SEQRES  18 A  265  ILE ALA LYS TYR VAL ILE SER TRP LEU LYS ARG PHE VAL          
SEQRES  19 A  265  ASP GLU ASP THR ARG TYR SER GLN PHE LEU CYS PRO ASN          
SEQRES  20 A  265  PRO THR ASP ARG ALA ILE GLU GLU TYR ARG SER THR CYS          
SEQRES  21 A  265  PRO TYR LYS LEU ASN                                          
MODRES 5ZRS MHO A  188  MET  MODIFIED RESIDUE                                   
HET    MHO  A 188       9                                                       
HET    9J6  A 401      12                                                       
HET     ZN  A 402       1                                                       
HET     ZN  A 403       1                                                       
HET     ZN  A 404       1                                                       
HET     CA  A 405       1                                                       
HET    GOL  A 406       6                                                       
HET    GOL  A 407       6                                                       
HETNAM     MHO S-OXYMETHIONINE                                                  
HETNAM     9J6 6-ETHOXY-6-OXOHEXANOIC ACID                                      
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     9J6 ADIPIC ACID MONOETHYL ESTER                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MHO    C5 H11 N O3 S                                                
FORMUL   2  9J6    C8 H14 O4                                                    
FORMUL   3   ZN    3(ZN 2+)                                                     
FORMUL   6   CA    CA 2+                                                        
FORMUL   7  GOL    2(C3 H8 O3)                                                  
FORMUL   9  HOH   *390(H2 O)                                                    
HELIX    1 AA1 THR A   56  ALA A   62  1                                   7    
HELIX    2 AA2 SER A  109  MET A  113  5                                   5    
HELIX    3 AA3 SER A  114  SER A  122  1                                   9    
HELIX    4 AA4 GLN A  138  ARG A  156  1                                  19    
HELIX    5 AA5 ASP A  158  GLU A  163  1                                   6    
HELIX    6 AA6 ALA A  176  ARG A  189  1                                  14    
HELIX    7 AA7 HIS A  230  LEU A  238  1                                   9    
HELIX    8 AA8 PHE A  255  ILE A  259  5                                   5    
HELIX    9 AA9 ASN A  261  ASP A  277  1                                  17    
HELIX   10 AB1 ASP A  279  ARG A  281  5                                   3    
HELIX   11 AB2 TYR A  282  CYS A  287  1                                   6    
SHEET    1 AA1 6 VAL A  69  VAL A  74  0                                        
SHEET    2 AA1 6 GLY A  84  PRO A  89 -1  O  ILE A  86   N  GLU A  72           
SHEET    3 AA1 6 ILE A 126  ILE A 130 -1  O  VAL A 127   N  TYR A  87           
SHEET    4 AA1 6 PHE A  97  ALA A 103  1  N  VAL A 102   O  PHE A 128           
SHEET    5 AA1 6 LEU A 165  HIS A 175  1  O  ASP A 166   N  PHE A  97           
SHEET    6 AA1 6 ALA A 194  LEU A 198  1  O  LEU A 198   N  GLY A 174           
SHEET    1 AA2 3 THR A 214  ALA A 219  0                                        
SHEET    2 AA2 3 LYS A 244  LEU A 249  1  O  LEU A 249   N  GLY A 218           
SHEET    3 AA2 3 ILE A 295  SER A 300 -1  O  GLU A 297   N  GLU A 248           
SSBOND   1 CYS A  287    CYS A  302                          1555   1555  2.04  
LINK         N   GLY A  43                ZN    ZN A 404     1555   1555  2.16  
LINK         O   GLY A  43                ZN    ZN A 404     1555   1555  2.21  
LINK         OD1 ASP A  46                ZN    ZN A 404     1555   1555  1.96  
LINK         OD2 ASP A  46                ZN    ZN A 404     1555   1555  2.66  
LINK         OE2 GLU A  50                ZN    ZN A 404     1555   1555  2.04  
LINK         O   SER A  76                CA    CA A 405     1555   1555  2.29  
LINK         O   ALA A  78                CA    CA A 405     1555   1555  2.31  
LINK         O   PHE A  81                CA    CA A 405     1555   1555  2.34  
LINK         C   VAL A 187                 N   MHO A 188     1555   1555  1.33  
LINK         C   MHO A 188                 N   ARG A 189     1555   1555  1.33  
LINK         OD1 ASP A 204                ZN    ZN A 403     1555   1555  2.25  
LINK         O   THR A 206                ZN    ZN A 403     1555   1555  2.15  
LINK         OG1 THR A 206                ZN    ZN A 403     1555   1555  2.33  
LINK         OE1 GLU A 220                ZN    ZN A 402     1555   1555  2.00  
LINK         OE2 GLU A 220                ZN    ZN A 402     1555   1555  2.58  
LINK         OD1 ASP A 250                ZN    ZN A 402     1555   1555  1.96  
LINK         OE1 GLU A 296                ZN    ZN A 402     1555   1555  1.93  
LINK        ZN    ZN A 403                 O   HOH A 663     1555   1555  2.34  
LINK        ZN    ZN A 403                 O   HOH A 662     1555   1555  2.42  
LINK        ZN    ZN A 403                 O   HOH A 652     1555   1555  2.24  
LINK        ZN    ZN A 404                 O   HOH A 653     1555   1555  2.18  
LINK        CA    CA A 405                 O   HOH A 617     1555   1555  2.60  
LINK        CA    CA A 405                 O   HOH A 660     1555   1555  2.40  
LINK        CA    CA A 405                 O   HOH A 772     1555   1555  2.36  
LINK         OE2 GLU A 118                ZN    ZN A 402     1555   3455  1.94  
CISPEP   1 CYS A  287    PRO A  288          0        -1.69                     
CISPEP   2 CYS A  302    PRO A  303          0        -2.98                     
SITE     1 AC1 13 GLY A 105  PHE A 106  ALA A 176  MET A 177                    
SITE     2 AC1 13 TRP A 201  GLY A 208  ILE A 224  SER A 237                    
SITE     3 AC1 13 HIS A 254  HOH A 502  HOH A 546  HOH A 664                    
SITE     4 AC1 13 HOH A 703                                                     
SITE     1 AC2  4 GLU A 118  GLU A 220  ASP A 250  GLU A 296                    
SITE     1 AC3  5 ASP A 204  THR A 206  HOH A 652  HOH A 662                    
SITE     2 AC3  5 HOH A 663                                                     
SITE     1 AC4  4 GLY A  43  ASP A  46  GLU A  50  HOH A 653                    
SITE     1 AC5  6 SER A  76  ALA A  78  PHE A  81  HOH A 617                    
SITE     2 AC5  6 HOH A 660  HOH A 772                                          
SITE     1 AC6  7 ARG A  64  LYS A 232  GLU A 248  GLU A 296                    
SITE     2 AC6  7 GLU A 297  HOH A 557  HOH A 578                               
SITE     1 AC7  7 GLY A  52  PRO A  53  GLU A  91  ASP A  93                    
SITE     2 AC7  7 GLU A  94  HOH A 501  HOH A 608                               
CRYST1   50.457   63.856   78.785  90.00  90.00  90.00 P 21 21 21    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      0.019819  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015660  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012693        0.00000                         
TER    2049      LYS A 305                                                      
MASTER      348    0    8   11    9    0   14    6 2460    1   66   21          
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:
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