Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 6rzn-pdb

Name Class
6rzn-pdb
HEADER    HYDROLASE                               13-JUN-19   6RZN              
TITLE     CRYSTAL STRUCTURE OF THE N-TERMINAL CARBOHYDRATE BINDING MODULE FAMILY
TITLE    2 48 AND FERULIC ACID ESTERASE FROM THE MULTI-ENZYME CE1-GH62-GH10     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FERULIC ACID ESTERASE;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.1.1.73;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: THE ELECTRON DENSITY IS LACKING FOR THE N-TERMINAL AND
COMPND   7 TWO LOOPS.                                                           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;                           
SOURCE   3 ORGANISM_TAXID: 77133;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    FERULIC ACID ESTEREASE, CARBOHYDRATE ESTERASE FAMILY 1, CE1, CBM48,   
KEYWDS   2 CARBOHYDRATE BINDING MODULE FAMILY 48, HYDROLASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.FREDSLUND,D.H.WELNER,C.WILKENS                                      
REVDAT   1   25-SEP-19 6RZN    0                                                
JRNL        AUTH   J.HOLCK,F.FREDSLUND,M.S.MOELLER,J.BRASK,K.B.R.M.KROGH,       
JRNL        AUTH 2 L.LANGE,D.H.WELNER,B.SVENSSON,S.JANECEK,C.WILKENS            
JRNL        TITL   CARBOHYDRATE BINDING MODULE OF FAMILY 48 ENABLES ACTION OF   
JRNL        TITL 2 FERULIC ACID ESTERASES ON POLYMERIC ARABINOXYLAN             
JRNL        REF    J.BIOL.CHEM.                               2019              
JRNL        REFN                   ESSN 1083-351X                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.91 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.13_2998: ???)                              
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) : 1.91                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 54.86                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.310                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 68019                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.130                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3488                            
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 54.8864 -  5.5738    0.96     2703   155  0.1944 0.1975        
REMARK   3     2  5.5738 -  4.4247    0.99     2685   142  0.1545 0.1529        
REMARK   3     3  4.4247 -  3.8656    0.99     2643   135  0.1493 0.1544        
REMARK   3     4  3.8656 -  3.5122    0.99     2637   147  0.1578 0.1774        
REMARK   3     5  3.5122 -  3.2605    0.99     2604   169  0.1631 0.2011        
REMARK   3     6  3.2605 -  3.0683    0.97     2568   119  0.1786 0.1901        
REMARK   3     7  3.0683 -  2.9146    0.93     2453   149  0.1728 0.2554        
REMARK   3     8  2.9146 -  2.7878    0.98     2569   133  0.1749 0.1922        
REMARK   3     9  2.7878 -  2.6804    0.98     2578   136  0.1677 0.2076        
REMARK   3    10  2.6804 -  2.5880    0.98     2573   151  0.1659 0.2096        
REMARK   3    11  2.5880 -  2.5070    0.99     2554   137  0.1725 0.1932        
REMARK   3    12  2.5070 -  2.4354    0.99     2557   135  0.1714 0.2276        
REMARK   3    13  2.4354 -  2.3713    0.98     2593   139  0.1762 0.2237        
REMARK   3    14  2.3713 -  2.3134    0.98     2550   161  0.1706 0.2319        
REMARK   3    15  2.3134 -  2.2608    0.98     2517   122  0.1759 0.2095        
REMARK   3    16  2.2608 -  2.2127    0.98     2569   136  0.1801 0.2301        
REMARK   3    17  2.2127 -  2.1684    0.99     2590   125  0.1845 0.2074        
REMARK   3    18  2.1684 -  2.1275    0.99     2559   119  0.1841 0.2188        
REMARK   3    19  2.1275 -  2.0895    0.99     2598   128  0.1908 0.2385        
REMARK   3    20  2.0895 -  2.0541    0.99     2583   135  0.1994 0.2533        
REMARK   3    21  2.0541 -  2.0210    0.99     2567   156  0.2155 0.2531        
REMARK   3    22  2.0210 -  1.9899    1.00     2540   142  0.2182 0.2733        
REMARK   3    23  1.9899 -  1.9606    1.00     2599   132  0.2240 0.2579        
REMARK   3    24  1.9606 -  1.9330    1.00     2571   138  0.2251 0.2649        
REMARK   3    25  1.9330 -  1.9069    1.00     2571   147  0.2275 0.2471        
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)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.520           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.003           5500                                  
REMARK   3   ANGLE     :  0.623           7447                                  
REMARK   3   CHIRALITY :  0.046            788                                  
REMARK   3   PLANARITY :  0.004            965                                  
REMARK   3   DIHEDRAL  : 11.239           3225                                  
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 6RZN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292102768.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-AUG-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-3                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9677                             
REMARK 200  MONOCHROMATOR                  : NULL                               
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          : AUTOPROC                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 68057                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.907                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 54.860                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 6.7300                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.8.1                                          
REMARK 200 STARTING MODEL: 1JT2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM AMMONIUM SULFATE, 50 MM BIS        
REMARK 280  -TRIS/HCL 6.5,30 % (V/V) PENTAERYTHRITOL ETHOXYLATE (15/4_EO/OH,    
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 298K                                   
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       32.82500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.64000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.95000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.64000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.82500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       49.95000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLN A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     ARG A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     ALA A    12                                                      
REMARK 465     ARG A    13                                                      
REMARK 465     PRO A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     PHE A    16                                                      
REMARK 465     ARG A    17                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     PRO A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     ARG A    21                                                      
REMARK 465     PRO A   223                                                      
REMARK 465     VAL A   224                                                      
REMARK 465     THR A   225                                                      
REMARK 465     GLN A   226                                                      
REMARK 465     GLY A   227                                                      
REMARK 465     GLN A   228                                                      
REMARK 465     GLN A   229                                                      
REMARK 465     GLY A   230                                                      
REMARK 465     ILE A   231                                                      
REMARK 465     PRO A   232                                                      
REMARK 465     SER A   233                                                      
REMARK 465     GLY A   234                                                      
REMARK 465     SER A   235                                                      
REMARK 465     GLY A   236                                                      
REMARK 465     MET A   237                                                      
REMARK 465     MET A   300                                                      
REMARK 465     ALA A   301                                                      
REMARK 465     GLY A   302                                                      
REMARK 465     ARG A   303                                                      
REMARK 465     GLN A   304                                                      
REMARK 465     GLN A   305                                                      
REMARK 465     GLY A   306                                                      
REMARK 465     ALA A   307                                                      
REMARK 465     ASP A   308                                                      
REMARK 465     ALA A   309                                                      
REMARK 465     GLU A   310                                                      
REMARK 465     LYS A   311                                                      
REMARK 465     GLN B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     ARG B     5                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     GLU B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     PRO B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     ALA B    12                                                      
REMARK 465     ARG B    13                                                      
REMARK 465     PRO B    14                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     PHE B    16                                                      
REMARK 465     ARG B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     PRO B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     ARG B    21                                                      
REMARK 465     PRO B   223                                                      
REMARK 465     VAL B   224                                                      
REMARK 465     THR B   225                                                      
REMARK 465     GLN B   226                                                      
REMARK 465     GLY B   227                                                      
REMARK 465     GLN B   228                                                      
REMARK 465     GLN B   229                                                      
REMARK 465     GLY B   230                                                      
REMARK 465     ILE B   231                                                      
REMARK 465     PRO B   232                                                      
REMARK 465     SER B   233                                                      
REMARK 465     GLY B   234                                                      
REMARK 465     SER B   235                                                      
REMARK 465     GLY B   236                                                      
REMARK 465     MET B   237                                                      
REMARK 465     MET B   300                                                      
REMARK 465     ALA B   301                                                      
REMARK 465     GLY B   302                                                      
REMARK 465     ARG B   303                                                      
REMARK 465     GLN B   304                                                      
REMARK 465     GLN B   305                                                      
REMARK 465     GLY B   306                                                      
REMARK 465     ALA B   307                                                      
REMARK 465     ASP B   308                                                      
REMARK 465     ALA B   309                                                      
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   OE2  GLU B   321     HD1  HIS B   355              1.57            
REMARK 500   O    HOH B   823     O    HOH B   836              1.98            
REMARK 500   OG1  THR A   238     O    HOH A   401              2.00            
REMARK 500   O    HOH B   664     O    HOH B   774              2.01            
REMARK 500   O    HOH A   768     O    HOH A   834              2.02            
REMARK 500   O    HOH B   625     O    HOH B   674              2.02            
REMARK 500   O    HOH A   570     O    HOH A   734              2.02            
REMARK 500   O    HOH B   786     O    HOH B   828              2.04            
REMARK 500   O    HOH B   747     O    HOH B   831              2.04            
REMARK 500   O    HOH B   691     O    HOH B   739              2.04            
REMARK 500   O    HOH A   597     O    HOH A   669              2.05            
REMARK 500   O    HOH A   420     O    HOH B   582              2.06            
REMARK 500   O    HOH A   806     O    HOH A   831              2.06            
REMARK 500   O    HOH B   537     O    HOH B   813              2.07            
REMARK 500   O    HOH A   702     O    HOH A   771              2.07            
REMARK 500   O    HOH B   413     O    HOH B   739              2.08            
REMARK 500   O    HOH B   516     O    HOH B   558              2.08            
REMARK 500   O    HOH A   855     O    HOH A   857              2.10            
REMARK 500   O    HOH B   582     O    HOH B   602              2.12            
REMARK 500   O    HOH B   728     O    HOH B   754              2.13            
REMARK 500   O    HOH B   755     O    HOH B   782              2.15            
REMARK 500   O    HOH A   423     O    HOH A   433              2.15            
REMARK 500   O    HOH A   438     O    HOH A   578              2.16            
REMARK 500   O    HOH B   796     O    HOH B   854              2.19            
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   708     O    HOH B   402     3656     2.00            
REMARK 500   O    HOH A   837     O    HOH B   772     1455     2.16            
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    GLU A  79      168.50    177.80                                   
REMARK 500    SER A 272     -116.44     49.89                                   
REMARK 500    SER B  39      118.81   -166.69                                   
REMARK 500    GLU B  79      168.02    177.68                                   
REMARK 500    SER B 272     -117.75     52.87                                   
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 859        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH A 860        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH A 861        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH A 862        DISTANCE =  6.36 ANGSTROMS                       
REMARK 525    HOH A 863        DISTANCE =  6.38 ANGSTROMS                       
REMARK 525    HOH A 864        DISTANCE =  6.38 ANGSTROMS                       
REMARK 525    HOH A 865        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH A 866        DISTANCE =  6.61 ANGSTROMS                       
REMARK 525    HOH A 867        DISTANCE =  6.81 ANGSTROMS                       
REMARK 525    HOH A 868        DISTANCE =  7.01 ANGSTROMS                       
REMARK 525    HOH B 868        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH B 869        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH B 870        DISTANCE =  6.25 ANGSTROMS                       
REMARK 525    HOH B 871        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH B 872        DISTANCE =  6.66 ANGSTROMS                       
REMARK 525    HOH B 873        DISTANCE =  7.16 ANGSTROMS                       
REMARK 525    HOH B 874        DISTANCE =  7.55 ANGSTROMS                       
DBREF  6RZN A    1   386  PDB    6RZN     6RZN             1    386             
DBREF  6RZN B    1   386  PDB    6RZN     6RZN             1    386             
SEQRES   1 A  386  GLN VAL THR PRO ARG PRO GLU ALA ALA PRO GLY ALA ARG          
SEQRES   2 A  386  PRO GLY PHE ARG ALA PRO ALA ARG ILE ILE SER PRO GLU          
SEQRES   3 A  386  ILE MET PRO ASP ASN LYS VAL THR PHE ARG VAL TYR SER          
SEQRES   4 A  386  LYS ASP ALA SER LYS VAL THR ILE THR GLY GLU TRP GLN          
SEQRES   5 A  386  THR GLY PRO GLY GLY VAL GLU GLU LEU VAL LYS ASN ASP          
SEQRES   6 A  386  THR GLY MET PHE SER ILE THR VAL GLY PRO LEU LYS PRO          
SEQRES   7 A  386  GLU LEU TYR ALA TYR ASN PHE THR VAL ASP GLY VAL LYS          
SEQRES   8 A  386  ALA LEU ASP ALA ASN ASN VAL GLN VAL ARG ARG ASP GLY          
SEQRES   9 A  386  THR ASN TYR GLN ASN PHE PHE ILE ILE PRO GLY PRO GLU          
SEQRES  10 A  386  SER ASP LEU TYR PHE HIS LYS ASN ASN VAL PRO HIS GLY          
SEQRES  11 A  386  THR VAL THR LYS VAL TRP TYR LYS SER SER VAL ILE GLY          
SEQRES  12 A  386  PHE ASP ARG ARG MET TYR VAL TYR THR PRO ALA GLY TYR          
SEQRES  13 A  386  GLU GLY ASP THR GLN ARG TYR PRO VAL PHE TYR LEU LEU          
SEQRES  14 A  386  HIS GLY ALA GLY GLY ASP GLU ASP ALA TRP THR ASN MET          
SEQRES  15 A  386  GLY ARG THR ALA GLN ILE MET ASP ASN LEU ILE ALA GLN          
SEQRES  16 A  386  GLY LYS ALA LYS PRO MET ILE VAL VAL MET THR ASN GLY          
SEQRES  17 A  386  ASN ALA ASN GLN ALA GLY ALA GLN ASN GLU VAL PRO PRO          
SEQRES  18 A  386  VAL PRO VAL THR GLN GLY GLN GLN GLY ILE PRO SER GLY          
SEQRES  19 A  386  SER GLY MET THR GLY LYS PHE GLU GLU HIS LEU VAL LYS          
SEQRES  20 A  386  ASP VAL VAL PRO PHE ILE GLU LYS ASN PHE ARG ALA LEU          
SEQRES  21 A  386  THR GLY LYS ASP ASN ARG ALA ILE ALA GLY LEU SER MET          
SEQRES  22 A  386  GLY GLY GLY HIS THR GLN THR ILE THR ASN ASP ASN PRO          
SEQRES  23 A  386  GLY MET PHE SER TYR ILE GLY VAL PHE SER MET GLY ILE          
SEQRES  24 A  386  MET ALA GLY ARG GLN GLN GLY ALA ASP ALA GLU LYS ILE          
SEQRES  25 A  386  GLU LYS GLU ARG ASP ALA LYS ILE GLU ALA LEU LYS LYS          
SEQRES  26 A  386  SER GLY TYR LYS LEU TYR TRP ILE ALA CYS GLY LYS ASP          
SEQRES  27 A  386  ASP PHE VAL TYR GLN SER ALA LEU THR LEU ARG ASN THR          
SEQRES  28 A  386  LEU ASP LYS HIS ASN PHE LYS TYR VAL TYR ARG GLU SER          
SEQRES  29 A  386  THR GLY GLY HIS THR TRP ALA ASN TRP ARG ILE TYR LEU          
SEQRES  30 A  386  SER GLU PHE ALA PRO MET LEU PHE LYS                          
SEQRES   1 B  386  GLN VAL THR PRO ARG PRO GLU ALA ALA PRO GLY ALA ARG          
SEQRES   2 B  386  PRO GLY PHE ARG ALA PRO ALA ARG ILE ILE SER PRO GLU          
SEQRES   3 B  386  ILE MET PRO ASP ASN LYS VAL THR PHE ARG VAL TYR SER          
SEQRES   4 B  386  LYS ASP ALA SER LYS VAL THR ILE THR GLY GLU TRP GLN          
SEQRES   5 B  386  THR GLY PRO GLY GLY VAL GLU GLU LEU VAL LYS ASN ASP          
SEQRES   6 B  386  THR GLY MET PHE SER ILE THR VAL GLY PRO LEU LYS PRO          
SEQRES   7 B  386  GLU LEU TYR ALA TYR ASN PHE THR VAL ASP GLY VAL LYS          
SEQRES   8 B  386  ALA LEU ASP ALA ASN ASN VAL GLN VAL ARG ARG ASP GLY          
SEQRES   9 B  386  THR ASN TYR GLN ASN PHE PHE ILE ILE PRO GLY PRO GLU          
SEQRES  10 B  386  SER ASP LEU TYR PHE HIS LYS ASN ASN VAL PRO HIS GLY          
SEQRES  11 B  386  THR VAL THR LYS VAL TRP TYR LYS SER SER VAL ILE GLY          
SEQRES  12 B  386  PHE ASP ARG ARG MET TYR VAL TYR THR PRO ALA GLY TYR          
SEQRES  13 B  386  GLU GLY ASP THR GLN ARG TYR PRO VAL PHE TYR LEU LEU          
SEQRES  14 B  386  HIS GLY ALA GLY GLY ASP GLU ASP ALA TRP THR ASN MET          
SEQRES  15 B  386  GLY ARG THR ALA GLN ILE MET ASP ASN LEU ILE ALA GLN          
SEQRES  16 B  386  GLY LYS ALA LYS PRO MET ILE VAL VAL MET THR ASN GLY          
SEQRES  17 B  386  ASN ALA ASN GLN ALA GLY ALA GLN ASN GLU VAL PRO PRO          
SEQRES  18 B  386  VAL PRO VAL THR GLN GLY GLN GLN GLY ILE PRO SER GLY          
SEQRES  19 B  386  SER GLY MET THR GLY LYS PHE GLU GLU HIS LEU VAL LYS          
SEQRES  20 B  386  ASP VAL VAL PRO PHE ILE GLU LYS ASN PHE ARG ALA LEU          
SEQRES  21 B  386  THR GLY LYS ASP ASN ARG ALA ILE ALA GLY LEU SER MET          
SEQRES  22 B  386  GLY GLY GLY HIS THR GLN THR ILE THR ASN ASP ASN PRO          
SEQRES  23 B  386  GLY MET PHE SER TYR ILE GLY VAL PHE SER MET GLY ILE          
SEQRES  24 B  386  MET ALA GLY ARG GLN GLN GLY ALA ASP ALA GLU LYS ILE          
SEQRES  25 B  386  GLU LYS GLU ARG ASP ALA LYS ILE GLU ALA LEU LYS LYS          
SEQRES  26 B  386  SER GLY TYR LYS LEU TYR TRP ILE ALA CYS GLY LYS ASP          
SEQRES  27 B  386  ASP PHE VAL TYR GLN SER ALA LEU THR LEU ARG ASN THR          
SEQRES  28 B  386  LEU ASP LYS HIS ASN PHE LYS TYR VAL TYR ARG GLU SER          
SEQRES  29 B  386  THR GLY GLY HIS THR TRP ALA ASN TRP ARG ILE TYR LEU          
SEQRES  30 B  386  SER GLU PHE ALA PRO MET LEU PHE LYS                          
FORMUL   3  HOH   *942(H2 O)                                                    
HELIX    1 AA1 GLY A   54  VAL A   58  5                                   5    
HELIX    2 AA2 GLY A  115  PHE A  122  5                                   8    
HELIX    3 AA3 ASP A  177  MET A  182  1                                   6    
HELIX    4 AA4 ARG A  184  GLN A  195  1                                  12    
HELIX    5 AA5 GLY A  239  ASP A  248  1                                  10    
HELIX    6 AA6 ASP A  248  PHE A  257  1                                  10    
HELIX    7 AA7 GLY A  262  ASP A  264  5                                   3    
HELIX    8 AA8 SER A  272  ASN A  285  1                                  14    
HELIX    9 AA9 GLU A  313  LYS A  325  1                                  13    
HELIX   10 AB1 VAL A  341  HIS A  355  1                                  15    
HELIX   11 AB2 THR A  369  ALA A  381  1                                  13    
HELIX   12 AB3 PRO A  382  LEU A  384  5                                   3    
HELIX   13 AB4 GLY B  115  PHE B  122  5                                   8    
HELIX   14 AB5 ASP B  177  MET B  182  1                                   6    
HELIX   15 AB6 ARG B  184  GLN B  195  1                                  12    
HELIX   16 AB7 GLY B  239  ASP B  248  1                                  10    
HELIX   17 AB8 ASP B  248  PHE B  257  1                                  10    
HELIX   18 AB9 GLY B  262  ASP B  264  5                                   3    
HELIX   19 AC1 SER B  272  ASN B  285  1                                  14    
HELIX   20 AC2 LYS B  311  LYS B  325  1                                  15    
HELIX   21 AC3 VAL B  341  HIS B  355  1                                  15    
HELIX   22 AC4 THR B  369  ALA B  381  1                                  13    
HELIX   23 AC5 PRO B  382  LEU B  384  5                                   3    
SHEET    1 AA1 4 GLU A  26  ILE A  27  0                                        
SHEET    2 AA1 4 VAL A  33  TYR A  38 -1  O  THR A  34   N  GLU A  26           
SHEET    3 AA1 4 MET A  68  VAL A  73 -1  O  PHE A  69   N  VAL A  37           
SHEET    4 AA1 4 VAL A  62  LYS A  63 -1  N  VAL A  62   O  SER A  70           
SHEET    1 AA2 4 GLU A  59  GLU A  60  0                                        
SHEET    2 AA2 4 VAL A  45  GLY A  49 -1  N  ILE A  47   O  GLU A  59           
SHEET    3 AA2 4 LEU A  80  VAL A  87 -1  O  ASN A  84   N  THR A  48           
SHEET    4 AA2 4 VAL A  90  ALA A  92 -1  O  VAL A  90   N  VAL A  87           
SHEET    1 AA3 5 GLU A  59  GLU A  60  0                                        
SHEET    2 AA3 5 VAL A  45  GLY A  49 -1  N  ILE A  47   O  GLU A  59           
SHEET    3 AA3 5 LEU A  80  VAL A  87 -1  O  ASN A  84   N  THR A  48           
SHEET    4 AA3 5 ASN A 106  ILE A 112 -1  O  PHE A 111   N  TYR A  81           
SHEET    5 AA3 5 VAL A 100  ASP A 103 -1  N  ARG A 101   O  GLN A 108           
SHEET    1 AA416 VAL A 360  SER A 364  0                                        
SHEET    2 AA416 LEU A 330  GLY A 336  1  N  ILE A 333   O  ARG A 362           
SHEET    3 AA416 TYR A 291  PHE A 295  1  N  ILE A 292   O  TRP A 332           
SHEET    4 AA416 ARG A 266  LEU A 271  1  N  GLY A 270   O  PHE A 295           
SHEET    5 AA416 VAL A 165  LEU A 169  1  N  TYR A 167   O  ALA A 267           
SHEET    6 AA416 ILE A 202  MET A 205  1  O  ILE A 202   N  PHE A 166           
SHEET    7 AA416 ARG A 146  THR A 152 -1  N  TYR A 151   O  VAL A 203           
SHEET    8 AA416 THR A 131  TYR A 137 -1  N  THR A 133   O  VAL A 150           
SHEET    9 AA416 THR B 131  TYR B 137 -1  O  VAL B 132   N  LYS A 134           
SHEET   10 AA416 ARG B 146  THR B 152 -1  O  VAL B 150   N  THR B 133           
SHEET   11 AA416 ILE B 202  MET B 205 -1  O  MET B 205   N  TYR B 149           
SHEET   12 AA416 VAL B 165  LEU B 169  1  N  PHE B 166   O  ILE B 202           
SHEET   13 AA416 ARG B 266  LEU B 271  1  O  ALA B 267   N  TYR B 167           
SHEET   14 AA416 TYR B 291  PHE B 295  1  O  PHE B 295   N  GLY B 270           
SHEET   15 AA416 LEU B 330  GLY B 336  1  O  TRP B 332   N  ILE B 292           
SHEET   16 AA416 VAL B 360  SER B 364  1  O  VAL B 360   N  ILE B 333           
SHEET    1 AA5 4 GLU B  26  ILE B  27  0                                        
SHEET    2 AA5 4 VAL B  33  TYR B  38 -1  O  THR B  34   N  GLU B  26           
SHEET    3 AA5 4 MET B  68  VAL B  73 -1  O  PHE B  69   N  VAL B  37           
SHEET    4 AA5 4 VAL B  62  LYS B  63 -1  N  VAL B  62   O  SER B  70           
SHEET    1 AA6 4 GLU B  59  GLU B  60  0                                        
SHEET    2 AA6 4 VAL B  45  GLY B  49 -1  N  ILE B  47   O  GLU B  59           
SHEET    3 AA6 4 GLU B  79  VAL B  87 -1  O  ASN B  84   N  THR B  48           
SHEET    4 AA6 4 VAL B  90  ALA B  92 -1  O  VAL B  90   N  VAL B  87           
SHEET    1 AA7 5 GLU B  59  GLU B  60  0                                        
SHEET    2 AA7 5 VAL B  45  GLY B  49 -1  N  ILE B  47   O  GLU B  59           
SHEET    3 AA7 5 GLU B  79  VAL B  87 -1  O  ASN B  84   N  THR B  48           
SHEET    4 AA7 5 ASN B 106  ILE B 113 -1  O  PHE B 111   N  TYR B  81           
SHEET    5 AA7 5 VAL B 100  ASP B 103 -1  N  ARG B 101   O  GLN B 108           
CISPEP   1 SER A   24    PRO A   25          0        -1.83                     
CISPEP   2 GLY A   74    PRO A   75          0         5.49                     
CISPEP   3 SER B   24    PRO B   25          0        -1.79                     
CISPEP   4 GLY B   74    PRO B   75          0         4.05                     
CRYST1   65.650   99.900  133.280  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      0.015232  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010010  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007503        0.00000                         
TER    5274      LYS A 386                                                      
TER   10592      LYS B 386                                                      
MASTER      422    0    0   23   42    0    0    6 6308    2    0   60          
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