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LongText Report for: 7nei-pdb

Name Class
7nei-pdb
HEADER    HYDROLASE                               04-FEB-21   7NEI              
TITLE     NOVEL POLYESTER HYDROLASE LEIPZIG 7 (PHL-7)                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLYESTER HYDROLASE LEIPZIG 7 (PHL-7);                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: UNIDENTIFIED;                                   
SOURCE   3 ORGANISM_TAXID: 32644;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PETASE, CUTINASE, POLYETHYLENE TEREPHTHALATE, HYDROLASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.K.RICHTER,N.STRATER                                                 
REVDAT   1   23-JUN-21 7NEI    0                                                
JRNL        AUTH   C.SONNENDECKER,J.OESER,P.K.RICHTER,P.HILLE,Z.ZHAO,C.FISCHER, 
JRNL        AUTH 2 H.LIPPOLD,P.BLAZQUEZ-SANCHEZ,F.ENGELBERGER,                  
JRNL        AUTH 3 C.A.RAMIREZ-SARMIENTO,T.OESER,Y.LIHANOVA,R.FRANK,H.G.JAHNKE, 
JRNL        AUTH 4 S.BILLIG,B.ABEL,N.STRATER,J.MATYSIK,W.ZIMMERMANN             
JRNL        TITL   LOW CARBON FOOTPRINT RECYCLING OF POST-CONSUMER PET PLASTIC  
JRNL        TITL 2 WITH A METAGENOMIC POLYESTER HYDROLASE.                      
JRNL        REF    CHEMSUSCHEM                                2021              
JRNL        REFN                   ISSN 1864-564X                               
JRNL        PMID   34129279                                                     
JRNL        DOI    10.1002/CSSC.202101062                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.18.2-3874                                   
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.22                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 127577                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.133                           
REMARK   3   R VALUE            (WORKING SET) : 0.132                           
REMARK   3   FREE R VALUE                     : 0.159                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.860                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6202                            
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 49.2200 -  4.0400    0.99     4617   264  0.1347 0.1456        
REMARK   3     2  4.0400 -  3.2100    1.00     4491   235  0.1301 0.1681        
REMARK   3     3  3.2100 -  2.8000    1.00     4448   181  0.1275 0.1499        
REMARK   3     4  2.8000 -  2.5400    1.00     4411   242  0.1207 0.1273        
REMARK   3     5  2.5400 -  2.3600    1.00     4400   199  0.1124 0.1513        
REMARK   3     6  2.3600 -  2.2200    1.00     4396   203  0.1140 0.1369        
REMARK   3     7  2.2200 -  2.1100    1.00     4335   274  0.1155 0.1374        
REMARK   3     8  2.1100 -  2.0200    1.00     4319   234  0.1259 0.1520        
REMARK   3     9  2.0200 -  1.9400    1.00     4334   222  0.1237 0.1483        
REMARK   3    10  1.9400 -  1.8700    1.00     4345   229  0.1217 0.1579        
REMARK   3    11  1.8700 -  1.8200    1.00     4334   238  0.1234 0.1638        
REMARK   3    12  1.8200 -  1.7600    1.00     4341   236  0.1241 0.1524        
REMARK   3    13  1.7600 -  1.7200    1.00     4358   203  0.1270 0.1781        
REMARK   3    14  1.7200 -  1.6800    0.99     4313   228  0.1221 0.1417        
REMARK   3    15  1.6800 -  1.6400    1.00     4325   237  0.1215 0.1617        
REMARK   3    16  1.6400 -  1.6000    1.00     4370   195  0.1204 0.1480        
REMARK   3    17  1.6000 -  1.5700    1.00     4314   224  0.1221 0.1579        
REMARK   3    18  1.5700 -  1.5400    1.00     4302   209  0.1269 0.1724        
REMARK   3    19  1.5400 -  1.5100    1.00     4288   242  0.1306 0.1652        
REMARK   3    20  1.5100 -  1.4900    1.00     4329   217  0.1388 0.1844        
REMARK   3    21  1.4900 -  1.4600    0.98     4231   206  0.1575 0.2150        
REMARK   3    22  1.4600 -  1.4400    0.96     4168   198  0.1678 0.2141        
REMARK   3    23  1.4400 -  1.4200    0.93     4029   184  0.1833 0.2346        
REMARK   3    24  1.4200 -  1.4000    0.88     3810   202  0.2038 0.2319        
REMARK   3    25  1.4000 -  1.3800    0.83     3588   166  0.2063 0.2652        
REMARK   3    26  1.3800 -  1.3600    0.76     3310   133  0.2163 0.2663        
REMARK   3    27  1.3600 -  1.3500    0.72     3118   161  0.2268 0.2664        
REMARK   3    28  1.3500 -  1.3300    0.66     2833   168  0.2372 0.2693        
REMARK   3    29  1.3300 -  1.3100    0.60     2558   148  0.2538 0.2697        
REMARK   3    30  1.3100 -  1.3000    0.54     2360   124  0.2618 0.3123        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.116            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.325           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.55                          
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      :  0.006           4204                                  
REMARK   3   ANGLE     :  0.936           5785                                  
REMARK   3   CHIRALITY :  0.078            649                                  
REMARK   3   PLANARITY :  0.007            772                                  
REMARK   3   DIHEDRAL  : 26.163           1565                                  
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 : 1                                           
REMARK   3   NCS GROUP : ens_1                                                  
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: NULL                                        
REMARK   3     SELECTION          : (chain "A" and (resid 2 through 9 or        
REMARK   3                          resid 11 through 12 or resid 15 through     
REMARK   3                          18 or resid 20 through 24 or resid 26       
REMARK   3                          through 32 or (resid 33 and (name N or      
REMARK   3                          name CA or name C or name O or name CB ))   
REMARK   3                          or resid 34 through 35 or resid 37          
REMARK   3                          through 66 or resid 68 or resid 70          
REMARK   3                          through 100 or resid 102 through 113 or     
REMARK   3                          resid 115 through 124 or resid 126          
REMARK   3                          through 130 or resid 132 through 138 or     
REMARK   3                          resid 140 through 145 or resid 147          
REMARK   3                          through 158 or resid 160 or resid 162       
REMARK   3                          through 194 or resid 196 through 201 or     
REMARK   3                          resid 203 through 213 or resid 215          
REMARK   3                          through 246 or resid 248 through 249 or     
REMARK   3                          resid 251 or resid 254 through 259 or       
REMARK   3                          resid 300))                                 
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: NULL                                        
REMARK   3     SELECTION          : (chain "B" and (resid 2 through 9 or        
REMARK   3                          resid 11 through 12 or resid 15 through     
REMARK   3                          18 or resid 20 through 24 or resid 26       
REMARK   3                          through 35 or resid 37 through 66 or        
REMARK   3                          resid 68 or resid 70 through 100 or resid   
REMARK   3                          102 through 113 or resid 115 through 124    
REMARK   3                          or resid 126 through 130 or resid 132       
REMARK   3                          through 138 or resid 140 through 145 or     
REMARK   3                          resid 147 through 158 or resid 160 or       
REMARK   3                          resid 162 through 194 or resid 196          
REMARK   3                          through 201 or resid 203 through 213 or     
REMARK   3                          resid 215 through 246 or resid 248          
REMARK   3                          through 249 or resid 251 or resid 254       
REMARK   3                          through 258 or (resid 259 and (name N or    
REMARK   3                          name CA or name C or name O or name CB or   
REMARK   3                          name CG or name CD1 or name CD2 or name     
REMARK   3                          CE1 or name CE2 or name CZ )) or resid      
REMARK   3                          300))                                       
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7NEI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-FEB-21.                  
REMARK 100 THE DEPOSITION ID IS D_1292113698.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-OCT-20                          
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               : PETRA III, EMBL C/O DESY           
REMARK 200  BEAMLINE                       : P14 (MX2)                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976260                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS 20200417                       
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.7.4                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 127681                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.350                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : 12.10                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 18.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 56.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.40400                            
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 2.8.3                                          
REMARK 200 STARTING MODEL: HOMOLOGY MODEL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE 20 % (W/V) PEG     
REMARK 280  4,000 20 % (V/V) 2-PROPANOL, PH 5.6, VAPOR DIFFUSION, HANGING       
REMARK 280  DROP, TEMPERATURE 292K                                              
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       28.17500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.55000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.84000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.55000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.17500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.84000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     LEU A   260                                                      
REMARK 465     GLU A   261                                                      
REMARK 465     HIS A   262                                                      
REMARK 465     HIS A   263                                                      
REMARK 465     HIS A   264                                                      
REMARK 465     HIS A   265                                                      
REMARK 465     HIS A   266                                                      
REMARK 465     HIS A   267                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LEU B   260                                                      
REMARK 465     GLU B   261                                                      
REMARK 465     HIS B   262                                                      
REMARK 465     HIS B   263                                                      
REMARK 465     HIS B   264                                                      
REMARK 465     HIS B   265                                                      
REMARK 465     HIS B   266                                                      
REMARK 465     HIS B   267                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU B  33    CG   CD1  CD2                                       
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   415     O    HOH A   511              1.96            
REMARK 500   O    HOH B   656     O    HOH B   805              2.01            
REMARK 500   OD2  ASP A    10     O    HOH A   401              2.03            
REMARK 500   O    HOH A   803     O    HOH A   813              2.10            
REMARK 500   O    HOH B   598     O    HOH B   778              2.12            
REMARK 500   O    HOH A   780     O    HOH A   801              2.14            
REMARK 500   O    HOH B   510     O    HOH B   757              2.16            
REMARK 500   O    HOH B   791     O    HOH B   828              2.17            
REMARK 500   O    HOH A   789     O    HOH A   793              2.18            
REMARK 500   O    HOH A   707     O    HOH A   717              2.18            
REMARK 500   O    ALA A    35     O    HOH A   402              2.19            
REMARK 500   O    HOH A   812     O    HOH A   816              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   421     O    HOH B   425     2555     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 131     -125.40     60.03                                   
REMARK 500    SER A 131     -126.77     62.16                                   
REMARK 500    HIS A 185      -94.95   -118.55                                   
REMARK 500    PRO A 243     -150.27    -81.01                                   
REMARK 500    SER B 131     -127.89     63.80                                   
REMARK 500    SER B 131     -127.04     62.52                                   
REMARK 500    ASN B 144       92.36   -161.65                                   
REMARK 500    HIS B 185      -96.27   -118.58                                   
REMARK 500    PRO B 243     -156.07    -79.31                                   
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 815        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH A 816        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH B 832        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH B 833        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH B 834        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH B 835        DISTANCE =  6.67 ANGSTROMS                       
REMARK 525    HOH B 836        DISTANCE =  7.11 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 300  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 148   OE2                                                    
REMARK 620 2 PHE A 230   O   105.0                                              
REMARK 620 3 ASP A 233   OD1 165.2  87.1                                        
REMARK 620 4 HOH A 575   O    73.3  84.5 117.2                                  
REMARK 620 5 HOH A 589   O    81.8  84.6  90.9 149.1                            
REMARK 620 6 HOH A 658   O    85.4 169.6  82.5  99.8  96.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 300  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 148   OE2                                                    
REMARK 620 2 PHE B 230   O   104.1                                              
REMARK 620 3 ASP B 233   OD1 162.5  88.4                                        
REMARK 620 4 HOH B 589   O    70.7  83.3 123.8                                  
REMARK 620 5 HOH B 622   O    80.9  86.6  87.9 146.3                            
REMARK 620 6 HOH B 701   O    81.4 174.5  86.4  97.9  95.2                      
REMARK 620 N                    1     2     3     4     5                       
DBREF  7NEI A    1   267  PDB    7NEI     7NEI             1    267             
DBREF  7NEI B    1   267  PDB    7NEI     7NEI             1    267             
SEQRES   1 A  267  MET ALA ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU          
SEQRES   2 A  267  SER SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA          
SEQRES   3 A  267  GLN THR THR VAL SER ARG LEU GLN ALA ASP GLY PHE GLY          
SEQRES   4 A  267  GLY GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY          
SEQRES   5 A  267  THR PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA          
SEQRES   6 A  267  GLY GLN GLU SER ILE ALA TRP LEU GLY PRO ARG ILE ALA          
SEQRES   7 A  267  SER GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR          
SEQRES   8 A  267  ARG LEU ASP GLN PRO ASP SER ARG GLY ARG GLN LEU GLN          
SEQRES   9 A  267  ALA ALA LEU ASP HIS LEU ARG THR ASN SER VAL VAL ARG          
SEQRES  10 A  267  ASN ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS          
SEQRES  11 A  267  SER MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA ASN          
SEQRES  12 A  267  ASN THR SER LEU GLU ALA ALA ILE PRO LEU GLN GLY TRP          
SEQRES  13 A  267  HIS THR ARG LYS ASN TRP SER SER VAL ARG THR PRO THR          
SEQRES  14 A  267  LEU VAL VAL GLY ALA GLN LEU ASP THR ILE ALA PRO VAL          
SEQRES  15 A  267  SER SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER          
SEQRES  16 A  267  ASP LEU ASP LYS ALA TYR MET GLU LEU ARG GLY ALA SER          
SEQRES  17 A  267  HIS LEU VAL SER ASN THR PRO ASP THR THR THR ALA LYS          
SEQRES  18 A  267  TYR SER ILE ALA TRP LEU LYS ARG PHE VAL ASP ASP ASP          
SEQRES  19 A  267  LEU ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP          
SEQRES  20 A  267  PHE ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE LEU          
SEQRES  21 A  267  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 B  267  MET ALA ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU          
SEQRES   2 B  267  SER SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA          
SEQRES   3 B  267  GLN THR THR VAL SER ARG LEU GLN ALA ASP GLY PHE GLY          
SEQRES   4 B  267  GLY GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY          
SEQRES   5 B  267  THR PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA          
SEQRES   6 B  267  GLY GLN GLU SER ILE ALA TRP LEU GLY PRO ARG ILE ALA          
SEQRES   7 B  267  SER GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR          
SEQRES   8 B  267  ARG LEU ASP GLN PRO ASP SER ARG GLY ARG GLN LEU GLN          
SEQRES   9 B  267  ALA ALA LEU ASP HIS LEU ARG THR ASN SER VAL VAL ARG          
SEQRES  10 B  267  ASN ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS          
SEQRES  11 B  267  SER MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA ASN          
SEQRES  12 B  267  ASN THR SER LEU GLU ALA ALA ILE PRO LEU GLN GLY TRP          
SEQRES  13 B  267  HIS THR ARG LYS ASN TRP SER SER VAL ARG THR PRO THR          
SEQRES  14 B  267  LEU VAL VAL GLY ALA GLN LEU ASP THR ILE ALA PRO VAL          
SEQRES  15 B  267  SER SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER          
SEQRES  16 B  267  ASP LEU ASP LYS ALA TYR MET GLU LEU ARG GLY ALA SER          
SEQRES  17 B  267  HIS LEU VAL SER ASN THR PRO ASP THR THR THR ALA LYS          
SEQRES  18 B  267  TYR SER ILE ALA TRP LEU LYS ARG PHE VAL ASP ASP ASP          
SEQRES  19 B  267  LEU ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP          
SEQRES  20 B  267  PHE ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE LEU          
SEQRES  21 B  267  GLU HIS HIS HIS HIS HIS HIS                                  
HET     NA  A 300       1                                                       
HET     NA  B 300       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   3   NA    2(NA 1+)                                                     
FORMUL   5  HOH   *852(H2 O)                                                    
HELIX    1 AA1 THR A   12  ALA A   18  1                                   7    
HELIX    2 AA2 GLY A   66  ALA A   71  5                                   6    
HELIX    3 AA3 TRP A   72  SER A   79  1                                   8    
HELIX    4 AA4 GLN A   95  ARG A  111  1                                  17    
HELIX    5 AA5 VAL A  116  ASN A  118  5                                   3    
HELIX    6 AA6 SER A  131  ASN A  143  1                                  13    
HELIX    7 AA7 HIS A  185  LEU A  193  1                                   9    
HELIX    8 AA8 SER A  208  THR A  214  5                                   7    
HELIX    9 AA9 ASP A  216  ASP A  232  1                                  17    
HELIX   10 AB1 ASP A  234  LEU A  241  5                                   8    
HELIX   11 AB2 THR B   12  ALA B   18  1                                   7    
HELIX   12 AB3 GLY B   66  ALA B   71  5                                   6    
HELIX   13 AB4 TRP B   72  SER B   79  1                                   8    
HELIX   14 AB5 GLN B   95  ARG B  111  1                                  17    
HELIX   15 AB6 VAL B  116  ASN B  118  5                                   3    
HELIX   16 AB7 SER B  131  ASN B  143  1                                  13    
HELIX   17 AB8 HIS B  185  LEU B  193  1                                   9    
HELIX   18 AB9 SER B  208  THR B  214  5                                   7    
HELIX   19 AC1 ASP B  216  ASP B  232  1                                  17    
HELIX   20 AC2 ASP B  234  LEU B  241  5                                   8    
SHEET    1 AA1 6 VAL A  25  VAL A  30  0                                        
SHEET    2 AA1 6 GLY A  41  PRO A  46 -1  O  ILE A  43   N  THR A  28           
SHEET    3 AA1 6 VAL A  83  ILE A  87 -1  O  VAL A  84   N  TYR A  44           
SHEET    4 AA1 6 PHE A  54  SER A  60  1  N  VAL A  57   O  ILE A  85           
SHEET    5 AA1 6 ILE A 120  HIS A 130  1  O  ASP A 121   N  PHE A  54           
SHEET    6 AA1 6 ALA A 149  LEU A 153  1  O  LEU A 153   N  GLY A 129           
SHEET    1 AA2 3 THR A 169  ALA A 174  0                                        
SHEET    2 AA2 3 LYS A 199  LEU A 204  1  O  ALA A 200   N  VAL A 171           
SHEET    3 AA2 3 ILE A 250  SER A 255 -1  O  ARG A 254   N  TYR A 201           
SHEET    1 AA3 6 VAL B  25  VAL B  30  0                                        
SHEET    2 AA3 6 GLY B  41  PRO B  46 -1  O  GLY B  41   N  VAL B  30           
SHEET    3 AA3 6 VAL B  83  ILE B  87 -1  O  VAL B  84   N  TYR B  44           
SHEET    4 AA3 6 PHE B  54  SER B  60  1  N  VAL B  57   O  ILE B  85           
SHEET    5 AA3 6 ILE B 120  HIS B 130  1  O  MET B 128   N  ALA B  58           
SHEET    6 AA3 6 ALA B 149  LEU B 153  1  O  LEU B 153   N  GLY B 129           
SHEET    1 AA4 3 THR B 169  ALA B 174  0                                        
SHEET    2 AA4 3 LYS B 199  LEU B 204  1  O  ALA B 200   N  VAL B 171           
SHEET    3 AA4 3 ILE B 250  SER B 255 -1  O  ARG B 254   N  TYR B 201           
SSBOND   1 CYS A  242    CYS A  257                          1555   1555  2.02  
SSBOND   2 CYS B  242    CYS B  257                          1555   1555  2.02  
LINK         OE2 GLU A 148                NA    NA A 300     1555   1555  2.41  
LINK         O   PHE A 230                NA    NA A 300     1555   1555  2.28  
LINK         OD1 ASP A 233                NA    NA A 300     1555   1555  2.46  
LINK        NA    NA A 300                 O   HOH A 575     1555   1555  2.51  
LINK        NA    NA A 300                 O   HOH A 589     1555   1555  2.51  
LINK        NA    NA A 300                 O   HOH A 658     1555   1555  2.40  
LINK         OE2 GLU B 148                NA    NA B 300     1555   1555  2.57  
LINK         O   PHE B 230                NA    NA B 300     1555   1555  2.29  
LINK         OD1 ASP B 233                NA    NA B 300     1555   1555  2.43  
LINK        NA    NA B 300                 O   HOH B 589     1555   1555  2.54  
LINK        NA    NA B 300                 O   HOH B 622     1555   1555  2.51  
LINK        NA    NA B 300                 O   HOH B 701     1555   1555  2.37  
CISPEP   1 CYS A  242    PRO A  243          0        -8.72                     
CISPEP   2 CYS A  257    PRO A  258          0        -3.67                     
CISPEP   3 CYS B  242    PRO B  243          0        -8.98                     
CISPEP   4 CYS B  257    PRO B  258          0        -3.52                     
CRYST1   56.350   97.680  101.100  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      0.017746  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010238  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009891        0.00000                         
MTRIX1   1 -0.999992 -0.002693 -0.002949       56.24773    1                    
MTRIX2   1 -0.002935  0.996359  0.085204        4.38351    1                    
MTRIX3   1  0.002709  0.085212 -0.996359      -53.93749    1                    
TER    4028      PHE A 259                                                      
TER    8074      PHE B 259                                                      
MASTER      415    0    2   20   18    0    0    9 4773    2   20   42          
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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