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LongText Report for: 6kmo-pdb

Name Class
6kmo-pdb
HEADER    HYDROLASE                               31-JUL-19   6KMO              
TITLE     CRYSTAL STRUCTURE OF A NOVEL ESTERASE CINB FROM ENTEROBACTER ASBURIAE 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA/BETA HYDROLASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ENTEROBACTER ASBURIAE;                          
SOURCE   3 ORGANISM_TAXID: 61645;                                               
SOURCE   4 ATCC: 35953;                                                         
SOURCE   5 GENE: AN689_0218030;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    ENTEROBACTER ASBURIAE, ESTERASE, CINB, HYDROLASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.SHANG,Y.XU                                                          
REVDAT   1   04-SEP-19 6KMO    0                                                
JRNL        AUTH   F.SHANG,Y.XU                                                 
JRNL        TITL   CRYSTAL STRUCTURE OF A NOVEL ESTERASE CINB FROM ENTEROBACTER 
JRNL        TITL 2 ASBURIAE                                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.15.2_3472                                   
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) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.69                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 129082                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.128                           
REMARK   3   R VALUE            (WORKING SET) : 0.127                           
REMARK   3   FREE R VALUE                     : 0.151                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.540                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1984                            
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  3.4900 -  2.7700    1.00     9165   148  0.1308 0.1363        
REMARK   3     2  2.7700 -  2.4200    1.00     9168   138  0.1237 0.1465        
REMARK   3     3  2.4200 -  2.2000    1.00     9149   151  0.1190 0.1447        
REMARK   3     4  2.2000 -  2.0400    1.00     9092   136  0.1206 0.1559        
REMARK   3     5  2.0400 -  1.9200    1.00     9132   154  0.1235 0.1529        
REMARK   3     6  1.9200 -  1.8300    1.00     9122   127  0.1216 0.1404        
REMARK   3     7  1.8300 -  1.7500    1.00     9089   154  0.1171 0.1553        
REMARK   3     8  1.7500 -  1.6800    0.99     9060   134  0.1182 0.1542        
REMARK   3     9  1.6800 -  1.6200    0.99     9080   140  0.1196 0.1304        
REMARK   3    10  1.6200 -  1.5700    0.99     9039   144  0.1213 0.1385        
REMARK   3    11  1.5700 -  1.5300    0.99     8995   137  0.1241 0.1463        
REMARK   3    12  1.5300 -  1.4900    0.99     8971   131  0.1339 0.1569        
REMARK   3    13  1.4900 -  1.4500    0.95     8650   143  0.1503 0.1756        
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)     : 0.088            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 12.793           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 8.79                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.11                          
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           5260                                  
REMARK   3   ANGLE     :  0.978           7181                                  
REMARK   3   CHIRALITY :  0.075            801                                  
REMARK   3   PLANARITY :  0.007            951                                  
REMARK   3   DIHEDRAL  :  2.426           4135                                  
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 6KMO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-AUG-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300013237.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-APR-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 5C (4A)                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979617                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 129477                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
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     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07200                            
REMARK 200   FOR THE DATA SET  : 20.1250                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.48                     
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) : 0.22400                            
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.16 M AMMONIUM ACETATE, 0.1 M SODIUM    
REMARK 280  CITRATE TRIBASIC DEHYDRATE PH 5.6, 22% (W/V) POLYETHYLENE GLYCOL    
REMARK 280  4000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 287.15K            
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       44.69800            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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     MET A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     GLN A    21                                                      
REMARK 465     THR A    22                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     SER B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     GLN B    21                                                      
REMARK 465     THR B    22                                                      
REMARK 465     LYS B    43                                                      
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   H    GLY A    97     O    HOH A   506              1.54            
REMARK 500  HE21  GLN B   195     O    HOH B   407              1.60            
REMARK 500   OG   SER A    96     O    HOH A   501              1.80            
REMARK 500   O    HOH A   560     O    HOH A   782              1.80            
REMARK 500   O    HOH B   529     O    HOH B   730              1.83            
REMARK 500   O    HOH A   726     O    HOH A   928              1.84            
REMARK 500   O    HOH A   840     O    HOH A   904              1.84            
REMARK 500   O    HOH A   533     O    HOH A   851              1.86            
REMARK 500   O    HOH A   828     O    HOH A   908              1.91            
REMARK 500   O    HOH A   694     O    HOH A   728              1.92            
REMARK 500   O    HOH A   889     O    HOH B   797              1.93            
REMARK 500   NZ   LYS B    67     O    HOH B   401              1.94            
REMARK 500   O    HOH B   571     O    HOH B   660              1.96            
REMARK 500   O    HOH A   744     O    HOH A   753              1.97            
REMARK 500   O    HOH B   428     O    HOH B   542              1.97            
REMARK 500   O    HOH A   753     O    HOH A   941              1.98            
REMARK 500   O    HOH A   659     O    HOH A   825              2.01            
REMARK 500   O    HOH A   852     O    HOH A   896              2.02            
REMARK 500   O    HOH A   912     O    HOH A   917              2.05            
REMARK 500   O    HOH A   828     O    HOH A   947              2.05            
REMARK 500   O    HOH B   650     O    HOH B   730              2.05            
REMARK 500   O    HOH B   690     O    HOH B   718              2.06            
REMARK 500   O    HOH A   934     O    HOH B   791              2.06            
REMARK 500   O    HOH A   501     O    HOH A   848              2.06            
REMARK 500   O    HOH B   526     O    HOH B   722              2.07            
REMARK 500   O    HOH A   729     O    HOH A   805              2.07            
REMARK 500   O    HOH B   467     O    HOH B   667              2.07            
REMARK 500   O    HOH A   712     O    HOH A   942              2.08            
REMARK 500   O    HOH B   616     O    HOH B   662              2.08            
REMARK 500   O    HOH B   634     O    HOH B   807              2.09            
REMARK 500   O    HOH A   648     O    HOH A   775              2.10            
REMARK 500   O    HOH B   553     O    HOH B   721              2.10            
REMARK 500   O    HOH A   849     O    HOH A   908              2.11            
REMARK 500   O    HOH B   653     O    HOH B   826              2.11            
REMARK 500   O    HOH B   513     O    HOH B   706              2.14            
REMARK 500   O    HOH B   562     O    HOH B   682              2.14            
REMARK 500   O    HOH A   513     O    HOH A   672              2.14            
REMARK 500   O    HOH A   819     O    HOH A   833              2.14            
REMARK 500   O    HOH B   700     O    HOH B   739              2.15            
REMARK 500   O    HOH A   846     O    HOH A   890              2.15            
REMARK 500   O    HOH B   650     O    HOH B   703              2.16            
REMARK 500   O    HOH A   926     O    HOH A   958              2.17            
REMARK 500   O    HOH B   649     O    HOH B   824              2.17            
REMARK 500   O    HOH B   728     O    HOH B   817              2.17            
REMARK 500   O    HOH B   767     O    HOH B   828              2.17            
REMARK 500   O    HOH A   732     O    HOH A   827              2.18            
REMARK 500   O    HOH B   690     O    HOH B   737              2.19            
REMARK 500   O    HOH A   920     O    HOH A   958              2.19            
REMARK 500   O    HOH B   537     O    HOH B   622              2.19            
REMARK 500   O    HOH A   510     O    HOH A   530              2.19            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      52 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   OG1  THR B     3    HD22  ASN B   197     1454     1.29            
REMARK 500   O    HOH A   858     O    HOH B   611     2745     2.06            
REMARK 500   OG1  THR B     3     ND2  ASN B   197     1454     2.10            
REMARK 500   O    HOH A   820     O    HOH B   727     1455     2.17            
REMARK 500   O    HOH A   524     O    HOH B   427     2746     2.17            
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    TRP A 110      -31.50     71.28                                   
REMARK 500    ASP A 114     -173.77    178.30                                   
REMARK 500    SER A 180     -120.95     69.64                                   
REMARK 500    SER A 180     -122.67     63.56                                   
REMARK 500    TRP A 208       61.42     39.14                                   
REMARK 500    PHE A 228      -84.68     64.23                                   
REMARK 500    PHE A 228      -61.36     83.57                                   
REMARK 500    SER A 254       75.28   -118.94                                   
REMARK 500    LEU A 276       64.53   -111.29                                   
REMARK 500    TRP B 110      -26.11     72.11                                   
REMARK 500    ASP B 114     -172.32   -177.91                                   
REMARK 500    SER B 180     -119.70     68.35                                   
REMARK 500    SER B 180     -121.57     65.27                                   
REMARK 500    PHE B 228      -59.86     78.18                                   
REMARK 500    SER B 254       76.36   -118.87                                   
REMARK 500    LEU B 276       65.53   -113.47                                   
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 960        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH B 850        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH B 851        DISTANCE =  6.10 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NH4 A 401                 
DBREF1 6KMO A    1   337  UNP                  A0A1D3AXI2_ENTAS                 
DBREF2 6KMO A     A0A1D3AXI2                          1         337             
DBREF1 6KMO B    1   337  UNP                  A0A1D3AXI2_ENTAS                 
DBREF2 6KMO B     A0A1D3AXI2                          1         337             
SEQADV 6KMO ILE A    9  UNP  A0A1D3AXI VAL     9 ENGINEERED MUTATION            
SEQADV 6KMO ALA A   23  UNP  A0A1D3AXI THR    23 ENGINEERED MUTATION            
SEQADV 6KMO ILE B    9  UNP  A0A1D3AXI VAL     9 ENGINEERED MUTATION            
SEQADV 6KMO ALA B   23  UNP  A0A1D3AXI THR    23 ENGINEERED MUTATION            
SEQRES   1 A  337  MET LYS THR LEU THR ALA ILE LEU ILE SER SER VAL PHE          
SEQRES   2 A  337  ALA SER ALA ALA ALA SER ALA GLN THR ALA ASN THR PRO          
SEQRES   3 A  337  THR PRO THR ALA GLY VAL GLN ALA PHE LEU ASN VAL LEU          
SEQRES   4 A  337  ASN SER GLY LYS GLY LYS PRO MET GLU GLN MET THR PRO          
SEQRES   5 A  337  GLN GLU ALA ARG GLN VAL LEU ILE GLY ALA GLN GLN GLY          
SEQRES   6 A  337  ALA LYS LEU PRO PRO ALA GLN VAL SER GLU LYS THR ILE          
SEQRES   7 A  337  GLN VAL ASN GLY GLN ALA ILE LYS LEU LYS ILE VAL LYS          
SEQRES   8 A  337  PRO GLU ASN ALA SER GLY THR LEU PRO ALA PHE MET PHE          
SEQRES   9 A  337  PHE HIS GLY GLY GLY TRP VAL LEU GLY ASP PHE PRO THR          
SEQRES  10 A  337  HIS GLU ARG LEU ILE ARG ASP LEU VAL ARG ALA SER GLY          
SEQRES  11 A  337  ALA ALA ALA VAL TYR VAL ASP TYR THR PRO SER PRO GLU          
SEQRES  12 A  337  ALA HIS PHE PRO VAL ALA ILE ASN GLN ALA TYR GLU ALA          
SEQRES  13 A  337  THR LYS TRP VAL ALA GLU HIS GLY GLN GLU ILE GLY VAL          
SEQRES  14 A  337  ASP GLY SER ARG LEU GLY LEU VAL GLY ASN SER VAL GLY          
SEQRES  15 A  337  GLY ASN MET VAL ALA SER VAL ALA LEU GLN ALA LYS GLN          
SEQRES  16 A  337  PHE ASN GLY PRO LYS ILE ARG TYR ASN VAL MET LEU TRP          
SEQRES  17 A  337  PRO VAL THR ASP ALA ASN PHE ASP THR ALA SER TYR ASN          
SEQRES  18 A  337  GLN PHE GLU ASN GLY TYR PHE LEU SER LYS ASN MET MET          
SEQRES  19 A  337  LYS TRP PHE TRP ASP ASN TYR THR THR SER ALA ALA ASP          
SEQRES  20 A  337  ARG ASN ASN ILE LEU ALA SER PRO LEU ARG ALA SER THR          
SEQRES  21 A  337  ALA GLN LEU LYS GLY PHE PRO GLU THR LEU ILE GLN THR          
SEQRES  22 A  337  ALA GLU LEU ASP VAL LEU ARG ASP GLU GLY GLU ALA PHE          
SEQRES  23 A  337  GLY ARG LYS LEU ASP ALA ALA GLY VAL PRO VAL THR VAL          
SEQRES  24 A  337  THR ARG TYR ASN GLY MET ILE HIS ASP TYR GLY LEU LEU          
SEQRES  25 A  337  ASN PRO LEU SER GLN GLU PRO THR VAL LYS VAL ALA LEU          
SEQRES  26 A  337  GLU GLN ALA GLY ALA ALA LEU HIS GLU HIS LEU LYS              
SEQRES   1 B  337  MET LYS THR LEU THR ALA ILE LEU ILE SER SER VAL PHE          
SEQRES   2 B  337  ALA SER ALA ALA ALA SER ALA GLN THR ALA ASN THR PRO          
SEQRES   3 B  337  THR PRO THR ALA GLY VAL GLN ALA PHE LEU ASN VAL LEU          
SEQRES   4 B  337  ASN SER GLY LYS GLY LYS PRO MET GLU GLN MET THR PRO          
SEQRES   5 B  337  GLN GLU ALA ARG GLN VAL LEU ILE GLY ALA GLN GLN GLY          
SEQRES   6 B  337  ALA LYS LEU PRO PRO ALA GLN VAL SER GLU LYS THR ILE          
SEQRES   7 B  337  GLN VAL ASN GLY GLN ALA ILE LYS LEU LYS ILE VAL LYS          
SEQRES   8 B  337  PRO GLU ASN ALA SER GLY THR LEU PRO ALA PHE MET PHE          
SEQRES   9 B  337  PHE HIS GLY GLY GLY TRP VAL LEU GLY ASP PHE PRO THR          
SEQRES  10 B  337  HIS GLU ARG LEU ILE ARG ASP LEU VAL ARG ALA SER GLY          
SEQRES  11 B  337  ALA ALA ALA VAL TYR VAL ASP TYR THR PRO SER PRO GLU          
SEQRES  12 B  337  ALA HIS PHE PRO VAL ALA ILE ASN GLN ALA TYR GLU ALA          
SEQRES  13 B  337  THR LYS TRP VAL ALA GLU HIS GLY GLN GLU ILE GLY VAL          
SEQRES  14 B  337  ASP GLY SER ARG LEU GLY LEU VAL GLY ASN SER VAL GLY          
SEQRES  15 B  337  GLY ASN MET VAL ALA SER VAL ALA LEU GLN ALA LYS GLN          
SEQRES  16 B  337  PHE ASN GLY PRO LYS ILE ARG TYR ASN VAL MET LEU TRP          
SEQRES  17 B  337  PRO VAL THR ASP ALA ASN PHE ASP THR ALA SER TYR ASN          
SEQRES  18 B  337  GLN PHE GLU ASN GLY TYR PHE LEU SER LYS ASN MET MET          
SEQRES  19 B  337  LYS TRP PHE TRP ASP ASN TYR THR THR SER ALA ALA ASP          
SEQRES  20 B  337  ARG ASN ASN ILE LEU ALA SER PRO LEU ARG ALA SER THR          
SEQRES  21 B  337  ALA GLN LEU LYS GLY PHE PRO GLU THR LEU ILE GLN THR          
SEQRES  22 B  337  ALA GLU LEU ASP VAL LEU ARG ASP GLU GLY GLU ALA PHE          
SEQRES  23 B  337  GLY ARG LYS LEU ASP ALA ALA GLY VAL PRO VAL THR VAL          
SEQRES  24 B  337  THR ARG TYR ASN GLY MET ILE HIS ASP TYR GLY LEU LEU          
SEQRES  25 B  337  ASN PRO LEU SER GLN GLU PRO THR VAL LYS VAL ALA LEU          
SEQRES  26 B  337  GLU GLN ALA GLY ALA ALA LEU HIS GLU HIS LEU LYS              
FORMUL   3  HOH   *911(H2 O)                                                    
HELIX    1 AA1 THR A    3  ILE A    9  1                                   7    
HELIX    2 AA2 SER A   10  ALA A   14  5                                   5    
HELIX    3 AA3 THR A   29  GLY A   42  1                                  14    
HELIX    4 AA4 PRO A   46  MET A   50  5                                   5    
HELIX    5 AA5 THR A   51  GLN A   64  1                                  14    
HELIX    6 AA6 ASP A  114  GLY A  130  1                                  17    
HELIX    7 AA7 PRO A  147  GLY A  164  1                                  18    
HELIX    8 AA8 GLN A  165  ILE A  167  5                                   3    
HELIX    9 AA9 SER A  180  PHE A  196  1                                  17    
HELIX   10 AB1 THR A  217  PHE A  223  1                                   7    
HELIX   11 AB2 SER A  230  THR A  242  1                                  13    
HELIX   12 AB3 SER A  244  ASN A  249  1                                   6    
HELIX   13 AB4 SER A  254  ALA A  258  5                                   5    
HELIX   14 AB5 SER A  259  LYS A  264  1                                   6    
HELIX   15 AB6 LEU A  279  ALA A  293  1                                  15    
HELIX   16 AB7 LEU A  312  SER A  316  5                                   5    
HELIX   17 AB8 GLU A  318  LEU A  336  1                                  19    
HELIX   18 AB9 LEU B    4  ILE B    9  1                                   6    
HELIX   19 AC1 SER B   10  ALA B   14  5                                   5    
HELIX   20 AC2 THR B   29  GLY B   42  1                                  14    
HELIX   21 AC3 PRO B   46  MET B   50  5                                   5    
HELIX   22 AC4 THR B   51  GLN B   64  1                                  14    
HELIX   23 AC5 ASP B  114  GLY B  130  1                                  17    
HELIX   24 AC6 PRO B  147  GLY B  164  1                                  18    
HELIX   25 AC7 GLN B  165  ILE B  167  5                                   3    
HELIX   26 AC8 SER B  180  PHE B  196  1                                  17    
HELIX   27 AC9 THR B  217  PHE B  223  1                                   7    
HELIX   28 AD1 SER B  230  THR B  242  1                                  13    
HELIX   29 AD2 SER B  244  ASN B  249  1                                   6    
HELIX   30 AD3 SER B  254  ALA B  258  5                                   5    
HELIX   31 AD4 SER B  259  LYS B  264  1                                   6    
HELIX   32 AD5 LEU B  279  ALA B  293  1                                  15    
HELIX   33 AD6 LEU B  312  SER B  316  5                                   5    
HELIX   34 AD7 GLU B  318  LEU B  336  1                                  19    
SHEET    1 AA116 ALA A  71  VAL A  80  0                                        
SHEET    2 AA116 GLN A  83  PRO A  92 -1  O  GLN A  83   N  VAL A  80           
SHEET    3 AA116 ALA A 132  VAL A 136 -1  O  TYR A 135   N  LYS A  88           
SHEET    4 AA116 LEU A  99  PHE A 105  1  N  PHE A 102   O  ALA A 132           
SHEET    5 AA116 VAL A 169  ASN A 179  1  O  GLY A 175   N  MET A 103           
SHEET    6 AA116 TYR A 203  LEU A 207  1  O  LEU A 207   N  GLY A 178           
SHEET    7 AA116 THR A 269  LEU A 276  1  O  LEU A 270   N  MET A 206           
SHEET    8 AA116 VAL A 297  ILE A 306  1  O  TYR A 302   N  THR A 273           
SHEET    9 AA116 VAL B 297  ILE B 306 -1  O  ARG B 301   N  ARG A 301           
SHEET   10 AA116 THR B 269  LEU B 276  1  N  THR B 273   O  TYR B 302           
SHEET   11 AA116 TYR B 203  LEU B 207  1  N  MET B 206   O  LEU B 270           
SHEET   12 AA116 VAL B 169  ASN B 179  1  N  LEU B 176   O  VAL B 205           
SHEET   13 AA116 LEU B  99  PHE B 105  1  N  MET B 103   O  GLY B 175           
SHEET   14 AA116 ALA B 132  VAL B 136  1  O  ALA B 132   N  PHE B 102           
SHEET   15 AA116 ALA B  84  PRO B  92 -1  N  LYS B  88   O  TYR B 135           
SHEET   16 AA116 ALA B  71  GLN B  79 -1  N  GLN B  72   O  LYS B  91           
CISPEP   1 SER A  141    PRO A  142          0         4.97                     
CISPEP   2 PHE A  146    PRO A  147          0         3.30                     
CISPEP   3 GLY A  198    PRO A  199          0        -2.08                     
CISPEP   4 SER B  141    PRO B  142          0         4.33                     
CISPEP   5 PHE B  146    PRO B  147          0         2.83                     
CISPEP   6 GLY B  198    PRO B  199          0        -2.91                     
SITE     1 AC1  3 PHE A 228  LEU A 229  HIS A 307                               
CRYST1   65.086   89.396   68.929  90.00 111.26  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      0.015364  0.000000  0.005977        0.00000                         
SCALE2      0.000000  0.011186  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015567        0.00000                         
TER    5149      LYS A 337                                                      
TER   10189      LYS B 337                                                      
MASTER      357    0    0   34   16    0    1    6 5919    2    0   52          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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