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LongText Report for: 7xtr-pdb

Name Class
7xtr-pdb
HEADER    HYDROLASE                               18-MAY-22   7XTR              
TITLE     THE APO STRUCTURE OF THE ENGINEERED TFCUT                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA/BETA HYDROLASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CUTINASE;                                                   
COMPND   5 EC: 3.1.1.74;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: GB:PZN61876.1                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOBIFIDA FUSCA;                             
SOURCE   3 ORGANISM_COMMON: THERMOMONOSPORA FUSCA;                              
SOURCE   4 ORGANISM_TAXID: 2021;                                                
SOURCE   5 GENE: CUT-2.KW3;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    PETASE, CUTINASE, ENZYME ENGINEERING, PBAT DEGRADATION, HYDROLASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.YANG,P.C.JIANG,J.-W.HUANG,C.-C.CHEN,R.-T.GUO                        
REVDAT   1   29-MAR-23 7XTR    0                                                
JRNL        AUTH   Y.YANG,P.C.JIANG,J.-W.HUANG,C.-C.CHEN,R.-T.GUO               
JRNL        TITL   COMPLETE BIO-DEGRADATION OF POLY(BUTYLENE                    
JRNL        TITL 2 ADIPATE-CO-TEREPHTHALATE) VIA ENGINEERED CUTINASES           
JRNL        REF    NAT COMMUN                                                   
JRNL        REFN                   ESSN 2041-1723                               
JRNL        DOI    HTTPS://DOI.ORG/10.1038/S41467-023-37374-3                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.17                                          
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.68                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 38580                          
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) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.180                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3542                            
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 32.6800 -  6.4200    0.91     1444   157  0.1639 0.1771        
REMARK   3     2  6.4200 -  5.1000    0.92     1438   155  0.1788 0.2061        
REMARK   3     3  5.1000 -  4.4600    0.91     1454   150  0.1440 0.1762        
REMARK   3     4  4.4600 -  4.0500    0.90     1429   148  0.1372 0.1564        
REMARK   3     5  4.0500 -  3.7600    0.90     1400   147  0.1460 0.1729        
REMARK   3     6  3.7600 -  3.5400    0.89     1409   142  0.1596 0.1957        
REMARK   3     7  3.5400 -  3.3600    0.91     1481   145  0.1741 0.2431        
REMARK   3     8  3.3600 -  3.2200    0.93     1458   137  0.1702 0.2198        
REMARK   3     9  3.2200 -  3.0900    0.92     1501   142  0.1851 0.2718        
REMARK   3    10  3.0900 -  2.9900    0.93     1420   150  0.1822 0.2444        
REMARK   3    11  2.9900 -  2.8900    0.92     1497   139  0.1883 0.3289        
REMARK   3    12  2.8900 -  2.8100    0.93     1468   158  0.2050 0.2810        
REMARK   3    13  2.8100 -  2.7400    0.91     1455   159  0.1904 0.2535        
REMARK   3    14  2.7400 -  2.6700    0.93     1490   140  0.1855 0.2478        
REMARK   3    15  2.6700 -  2.6100    0.89     1362   131  0.1959 0.3046        
REMARK   3    16  2.6100 -  2.5500    0.86     1431   139  0.1894 0.3209        
REMARK   3    17  2.5500 -  2.5000    0.86     1364   143  0.2000 0.2951        
REMARK   3    18  2.5000 -  2.4500    0.86     1312   144  0.1811 0.2586        
REMARK   3    19  2.4500 -  2.4100    0.84     1408   133  0.1894 0.2752        
REMARK   3    20  2.4100 -  2.3700    0.86     1318   117  0.1646 0.2953        
REMARK   3    21  2.3700 -  2.3300    0.80     1237   143  0.1648 0.2408        
REMARK   3    22  2.3300 -  2.3000    0.80     1307   125  0.1717 0.2535        
REMARK   3    23  2.3000 -  2.2600    0.82     1281   136  0.1859 0.2725        
REMARK   3    24  2.2600 -  2.2300    0.84     1321   131  0.1766 0.3233        
REMARK   3    25  2.2300 -  2.2000    0.85     1353   131  0.1724 0.2938        
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)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.740           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.29                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
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 7XTR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-MAY-22.                  
REMARK 100 THE DEPOSITION ID IS D_1300028968.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-NOV-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : LIQUID ANODE                       
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : BRUKER METALJET                    
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.34138                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CMOS                               
REMARK 200  DETECTOR MANUFACTURER          : BRUKER PHOTON 100                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT                              
REMARK 200  DATA SCALING SOFTWARE          : SAINT                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38580                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.09900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 4CG2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% W/V PEG3350, 0.2 M SODIUM NITRATE,   
REMARK 280  0.1 M BIS-TRIS PROPANE 8.5, PH 8.5, EVAPORATION, TEMPERATURE 273K   
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       20.98050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 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     LEU A   288                                                      
REMARK 465     PHE A   289                                                      
REMARK 465     ARG B   285                                                      
REMARK 465     GLY B   287                                                      
REMARK 465     LEU B   288                                                      
REMARK 465     PHE B   289                                                      
REMARK 465     GLY B   290                                                      
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   639     O    HOH A   665              2.13            
REMARK 500   OG   SER B   170     O    HOH B   501              2.13            
REMARK 500   O    HOH A   609     O    HOH A   632              2.14            
REMARK 500   O2   SO4 A   401     O1   GOL A   402              2.17            
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   NH1  ARG B    86     NH2  ARG B   150     2545     1.55            
REMARK 500   O    HOH A   524     O    HOH B   608     2546     2.05            
REMARK 500   O    HOH A   579     O    HOH A   619     2546     2.12            
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 170     -115.44     62.78                                   
REMARK 500    THR A 193       58.04     30.99                                   
REMARK 500    SER A 224      -70.04   -124.17                                   
REMARK 500    ASP A 286     -149.44   -109.64                                   
REMARK 500    THR A 298       32.14    -97.04                                   
REMARK 500    THR B 101       13.30     59.49                                   
REMARK 500    SER B 170     -114.98     51.16                                   
REMARK 500    THR B 193       56.06     32.33                                   
REMARK 500    SER B 224      -76.53   -133.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ILE A  124     ASP A  125                  149.70                    
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 677        DISTANCE =  6.23 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                              LI A 404  LI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 214   OD2                                                    
REMARK 620 2 ASP A 244   OD1  86.1                                              
REMARK 620 3 ASN B 230   O    58.2  29.9                                        
REMARK 620 4 LEU B 232   O    60.6  27.2   2.8                                  
REMARK 620 N                    1     2     3                                   
DBREF  7XTR A   41   301  PDB    7XTR     7XTR            41    301             
DBREF  7XTR B   41   301  PDB    7XTR     7XTR            41    301             
SEQRES   1 A  261  MET ASN PRO TYR GLU ARG GLY PRO ASN PRO THR ASP ALA          
SEQRES   2 A  261  LEU LEU GLU ALA ARG SER GLY PRO PHE SER VAL SER GLU          
SEQRES   3 A  261  GLU ASN VAL SER ARG LEU SER ALA SER GLY PHE GLY GLY          
SEQRES   4 A  261  GLY THR ILE TYR TYR PRO ARG GLU ASN ASN THR TYR GLY          
SEQRES   5 A  261  ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR GLU ALA          
SEQRES   6 A  261  SER ILE ALA TRP LEU GLY GLU ARG ILE ALA SER HIS GLY          
SEQRES   7 A  261  PHE VAL VAL ILE THR ILE ASP THR ILE THR THR LEU ASP          
SEQRES   8 A  261  GLN PRO ASP SER ARG ALA GLU GLN LEU ASN ALA ALA LEU          
SEQRES   9 A  261  ASN HIS MET ILE ASN ARG ALA SER SER THR VAL ARG SER          
SEQRES  10 A  261  ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY HIS SER          
SEQRES  11 A  261  MET GLY GLY GLY GLY SER LEU ARG LEU ALA SER GLN ARG          
SEQRES  12 A  261  PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO TRP HIS          
SEQRES  13 A  261  LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO THR LEU          
SEQRES  14 A  261  ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO VAL ALA          
SEQRES  15 A  261  THR SER ALA LYS PRO ILE TYR ASN SER LEU PRO SER SER          
SEQRES  16 A  261  ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA THR HIS          
SEQRES  17 A  261  PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY LYS TYR          
SEQRES  18 A  261  SER VAL ALA TRP LEU LYS ARG PHE VAL ASP ASN ASP THR          
SEQRES  19 A  261  ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG ASP GLY          
SEQRES  20 A  261  LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR CYS PRO          
SEQRES  21 A  261  PHE                                                          
SEQRES   1 B  261  MET ASN PRO TYR GLU ARG GLY PRO ASN PRO THR ASP ALA          
SEQRES   2 B  261  LEU LEU GLU ALA ARG SER GLY PRO PHE SER VAL SER GLU          
SEQRES   3 B  261  GLU ASN VAL SER ARG LEU SER ALA SER GLY PHE GLY GLY          
SEQRES   4 B  261  GLY THR ILE TYR TYR PRO ARG GLU ASN ASN THR TYR GLY          
SEQRES   5 B  261  ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR GLU ALA          
SEQRES   6 B  261  SER ILE ALA TRP LEU GLY GLU ARG ILE ALA SER HIS GLY          
SEQRES   7 B  261  PHE VAL VAL ILE THR ILE ASP THR ILE THR THR LEU ASP          
SEQRES   8 B  261  GLN PRO ASP SER ARG ALA GLU GLN LEU ASN ALA ALA LEU          
SEQRES   9 B  261  ASN HIS MET ILE ASN ARG ALA SER SER THR VAL ARG SER          
SEQRES  10 B  261  ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY HIS SER          
SEQRES  11 B  261  MET GLY GLY GLY GLY SER LEU ARG LEU ALA SER GLN ARG          
SEQRES  12 B  261  PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO TRP HIS          
SEQRES  13 B  261  LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO THR LEU          
SEQRES  14 B  261  ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO VAL ALA          
SEQRES  15 B  261  THR SER ALA LYS PRO ILE TYR ASN SER LEU PRO SER SER          
SEQRES  16 B  261  ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA THR HIS          
SEQRES  17 B  261  PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY LYS TYR          
SEQRES  18 B  261  SER VAL ALA TRP LEU LYS ARG PHE VAL ASP ASN ASP THR          
SEQRES  19 B  261  ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG ASP GLY          
SEQRES  20 B  261  LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR CYS PRO          
SEQRES  21 B  261  PHE                                                          
HET    SO4  A 401       5                                                       
HET    GOL  A 402       6                                                       
HET    GOL  A 403       6                                                       
HET     LI  A 404       1                                                       
HET    SO4  B 401       5                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM      LI LITHIUM ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   4  GOL    2(C3 H8 O3)                                                  
FORMUL   6   LI    LI 1+                                                        
FORMUL   8  HOH   *338(H2 O)                                                    
HELIX    1 AA1 THR A   51  ALA A   57  1                                   7    
HELIX    2 AA2 THR A  103  SER A  106  5                                   4    
HELIX    3 AA3 ILE A  107  SER A  116  1                                  10    
HELIX    4 AA4 GLN A  132  ARG A  150  1                                  19    
HELIX    5 AA5 SER A  152  SER A  157  1                                   6    
HELIX    6 AA6 SER A  170  ARG A  183  1                                  14    
HELIX    7 AA7 SER A  224  LEU A  232  1                                   9    
HELIX    8 AA8 PHE A  249  ILE A  253  5                                   5    
HELIX    9 AA9 ASN A  255  ASP A  271  1                                  17    
HELIX   10 AB1 ASP A  273  ARG A  275  5                                   3    
HELIX   11 AB2 TYR A  276  CYS A  281  1                                   6    
HELIX   12 AB3 THR B   51  ALA B   57  1                                   7    
HELIX   13 AB4 THR B  103  SER B  106  5                                   4    
HELIX   14 AB5 ILE B  107  SER B  116  1                                  10    
HELIX   15 AB6 GLN B  132  ARG B  150  1                                  19    
HELIX   16 AB7 SER B  152  SER B  157  1                                   6    
HELIX   17 AB8 SER B  170  ARG B  183  1                                  14    
HELIX   18 AB9 SER B  224  LEU B  232  1                                   9    
HELIX   19 AC1 PHE B  249  ILE B  253  5                                   5    
HELIX   20 AC2 ASN B  255  ASP B  271  1                                  17    
HELIX   21 AC3 ASP B  273  ARG B  275  5                                   3    
HELIX   22 AC4 TYR B  276  CYS B  281  1                                   6    
SHEET    1 AA1 6 VAL A  64  VAL A  69  0                                        
SHEET    2 AA1 6 GLY A  80  PRO A  85 -1  O  ILE A  82   N  GLU A  67           
SHEET    3 AA1 6 VAL A 120  ILE A 124 -1  O  VAL A 121   N  TYR A  83           
SHEET    4 AA1 6 TYR A  91  SER A  97  1  N  VAL A  94   O  VAL A 120           
SHEET    5 AA1 6 ILE A 159  HIS A 169  1  O  MET A 167   N  ALA A  95           
SHEET    6 AA1 6 ALA A 188  LEU A 192  1  O  LEU A 192   N  GLY A 168           
SHEET    1 AA2 3 THR A 208  ALA A 213  0                                        
SHEET    2 AA2 3 LYS A 238  LEU A 243  1  O  LEU A 243   N  GLY A 212           
SHEET    3 AA2 3 VAL A 292  SER A 297 -1  O  ARG A 296   N  TYR A 240           
SHEET    1 AA3 6 VAL B  64  VAL B  69  0                                        
SHEET    2 AA3 6 GLY B  80  PRO B  85 -1  O  GLY B  80   N  VAL B  69           
SHEET    3 AA3 6 VAL B 120  ILE B 124 -1  O  VAL B 121   N  TYR B  83           
SHEET    4 AA3 6 TYR B  91  SER B  97  1  N  VAL B  94   O  VAL B 120           
SHEET    5 AA3 6 ILE B 159  HIS B 169  1  O  ASP B 160   N  TYR B  91           
SHEET    6 AA3 6 ALA B 188  LEU B 192  1  O  LEU B 192   N  GLY B 168           
SHEET    1 AA4 3 THR B 208  ALA B 213  0                                        
SHEET    2 AA4 3 LYS B 238  LEU B 243  1  O  LEU B 243   N  GLY B 212           
SHEET    3 AA4 3 VAL B 292  SER B 297 -1  O  GLU B 294   N  GLU B 242           
SSBOND   1 CYS A  281    CYS A  299                          1555   1555  2.06  
SSBOND   2 CYS B  281    CYS B  299                          1555   1555  2.03  
LINK         OD2 ASP A 214                LI    LI A 404     1555   1555  2.23  
LINK         OD1 ASP A 244                LI    LI A 404     1555   1555  2.32  
LINK        LI    LI A 404                 O   ASN B 230     1455   1555  2.21  
LINK        LI    LI A 404                 O   LEU B 232     1455   1555  2.39  
CISPEP   1 CYS A  281    PRO A  282          0         1.11                     
CISPEP   2 CYS A  299    PRO A  300          0        13.05                     
CISPEP   3 CYS B  281    PRO B  282          0        11.18                     
CISPEP   4 CYS B  299    PRO B  300          0        -6.19                     
CRYST1   65.689   41.961   80.767  90.00  92.61  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      0.015223  0.000000  0.000694        0.00000                         
SCALE2      0.000000  0.023832  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012394        0.00000                         
TER    1970      PHE A 301                                                      
TER    3921      PHE B 301                                                      
MASTER      322    0    5   22   18    0    0    6 4280    2   29   42          
END                                                                             

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