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LongText Report for: 6n00-pdb

Name Class
6n00-pdb
HEADER    HYDROLASE                               06-NOV-18   6N00              
TITLE     FLUOROACETATE DEHALOGENASE, ROOM TEMPERATURE STRUCTURE, USING LAST 1  
TITLE    2 DEGREE OF TOTAL 3 DEGREE OSCILLATION AND 144 KGY DOSE                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FLUOROACETATE DEHALOGENASE;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.8.1.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS (STRAIN ATCC BAA-98  
SOURCE   3 / CGA009);                                                           
SOURCE   4 ORGANISM_TAXID: 258594;                                              
SOURCE   5 STRAIN: ATCC BAA-98 / CGA009;                                        
SOURCE   6 GENE: RPA1163;                                                       
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    DEHALOGENASE, DEFLUORINASE, HYDROLASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.D.FINKE,J.L.WIERMAN,O.PARE-LABROSSE,A.SARRACHINI,J.BESAW,P.MEHRABI, 
AUTHOR   2 S.M.GRUNER,R.J.D.MILLER                                              
REVDAT   1   27-MAR-19 6N00    0                                                
JRNL        AUTH   J.L.WIERMAN,O.PARE-LABROSSE,A.SARRACINI,J.E.BESAW,M.J.COOK,  
JRNL        AUTH 2 S.OGHBAEY,H.DAOUD,P.MEHRABI,I.KRIKSUNOV,A.KUO,D.J.SCHULLER,  
JRNL        AUTH 3 S.SMITH,O.P.ERNST,D.M.E.SZEBENYI,S.M.GRUNER,R.J.D.MILLER,    
JRNL        AUTH 4 A.D.FINKE                                                    
JRNL        TITL   FIXED-TARGET SERIAL OSCILLATION CRYSTALLOGRAPHY AT ROOM      
JRNL        TITL 2 TEMPERATURE.                                                 
JRNL        REF    IUCRJ                         V.   6   305 2019              
JRNL        REFN                   ESSN 2052-2525                               
JRNL        PMID   30867928                                                     
JRNL        DOI    10.1107/S2052252519001453                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.14_3260                                     
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.43                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 41313                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2066                            
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 40.8400 -  4.6800    0.98     2666   142  0.1454 0.1814        
REMARK   3     2  4.6800 -  3.7200    0.99     2626   133  0.1209 0.1427        
REMARK   3     3  3.7200 -  3.2500    0.99     2639   140  0.1396 0.1998        
REMARK   3     4  3.2500 -  2.9500    0.99     2638   139  0.1714 0.2203        
REMARK   3     5  2.9500 -  2.7400    1.00     2626   139  0.1823 0.2579        
REMARK   3     6  2.7400 -  2.5800    0.99     2651   139  0.1860 0.2597        
REMARK   3     7  2.5800 -  2.4500    0.99     2593   136  0.1945 0.2498        
REMARK   3     8  2.4500 -  2.3400    0.99     2628   136  0.2021 0.2446        
REMARK   3     9  2.3400 -  2.2500    0.99     2614   139  0.2111 0.2762        
REMARK   3    10  2.2500 -  2.1700    0.99     2613   138  0.2336 0.2865        
REMARK   3    11  2.1700 -  2.1100    0.99     2631   139  0.2729 0.2783        
REMARK   3    12  2.1100 -  2.0500    0.99     2604   139  0.2921 0.3843        
REMARK   3    13  2.0500 -  1.9900    0.99     2594   138  0.3062 0.3750        
REMARK   3    14  1.9900 -  1.9400    0.96     2564   133  0.3453 0.3567        
REMARK   3    15  1.9400 -  1.9000    0.98     2560   136  0.3878 0.4413        
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)     : 0.341            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.953           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.81                          
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      :  0.007           4914                                  
REMARK   3   ANGLE     :  0.928           6698                                  
REMARK   3   CHIRALITY :  0.050            684                                  
REMARK   3   PLANARITY :  0.006            879                                  
REMARK   3   DIHEDRAL  : 16.090           3964                                  
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 6N00 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-NOV-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000237941.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : G3                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.216                              
REMARK 200  MONOCHROMATOR                  : W/B4C MULTILAYER                   
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 1M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41428                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.430                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 4.9700                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 0.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6FSX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16-20% PEG 3350, 100MM TRIS-CL PH 8.5,   
REMARK 280  AND 200MM CACL2., BATCH MODE, TEMPERATURE 295K                      
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       39.55000            
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: 2390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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     GLY A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     ALA A   301                                                      
REMARK 465     PRO A   302                                                      
REMARK 465     GLY A   303                                                      
REMARK 465     SER A   304                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     ALA B   301                                                      
REMARK 465     PRO B   302                                                      
REMARK 465     GLY B   303                                                      
REMARK 465     SER B   304                                                      
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   OE1  GLU A   140     NH2  ARG A   144              2.05            
REMARK 500   OD1  ASP B   173     O    HOH B   501              2.10            
REMARK 500   O    HOH A   451     O    HOH A   516              2.12            
REMARK 500   OD1  ASN A   168     O    HOH A   401              2.14            
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   401     O    HOH A   508     2547     2.18            
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    PRO A  66      124.11    -39.71                                   
REMARK 500    ASP A 110     -126.58     60.70                                   
REMARK 500    ILE A 153       54.55   -115.72                                   
REMARK 500    ASP A 173       68.01   -151.53                                   
REMARK 500    TYR A 224      -90.35   -120.60                                   
REMARK 500    PRO B  41       64.42   -103.96                                   
REMARK 500    ASP B  77     -163.69   -129.39                                   
REMARK 500    ASP B 110     -128.03     58.19                                   
REMARK 500    ASP B 173       73.04   -163.19                                   
REMARK 500    TYR B 224      -98.78   -117.43                                   
REMARK 500    SER B 256      -94.18   -170.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              CA B 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 173   OD2                                                    
REMARK 620 2 HOH A 401   O   110.2                                              
REMARK 620 3 HOH A 423   O   100.1  74.1                                        
REMARK 620 4 ALA A 236   O    74.6  43.4  57.0                                  
REMARK 620 5 HOH A 445   O    87.1 147.5  75.8 124.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 401                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6MZZ   RELATED DB: PDB                                   
REMARK 900 SAME DATASET BUT WITH FIRST 1 DEGREE OF OSCILLATION PER CRYSTAL USED 
REMARK 900 RELATED ID: 6MUY   RELATED DB: PDB                                   
REMARK 900 SAME DATASET BUT ALL 3 DEGREES OF DATA COLLECTED USED                
DBREF  6N00 A    1   302  UNP    Q6NAM1   DEHA_RHOPA       1    302             
DBREF  6N00 B    1   302  UNP    Q6NAM1   DEHA_RHOPA       1    302             
SEQADV 6N00 GLY A   -1  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 6N00 HIS A    0  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 6N00 GLY A  303  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 6N00 SER A  304  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 6N00 GLY B   -1  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 6N00 HIS B    0  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 6N00 GLY B  303  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 6N00 SER B  304  UNP  Q6NAM1              EXPRESSION TAG                 
SEQRES   1 A  306  GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE          
SEQRES   2 A  306  GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE          
SEQRES   3 A  306  ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU          
SEQRES   4 A  306  HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL          
SEQRES   5 A  306  ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA          
SEQRES   6 A  306  ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER          
SEQRES   7 A  306  ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA          
SEQRES   8 A  306  LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL          
SEQRES   9 A  306  HIS PHE ALA LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL          
SEQRES  10 A  306  SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER          
SEQRES  11 A  306  LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR          
SEQRES  12 A  306  TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR          
SEQRES  13 A  306  HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU          
SEQRES  14 A  306  ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA          
SEQRES  15 A  306  LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA          
SEQRES  16 A  306  PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE          
SEQRES  17 A  306  ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP TYR          
SEQRES  18 A  306  ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE          
SEQRES  19 A  306  ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU          
SEQRES  20 A  306  ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA          
SEQRES  21 A  306  THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL          
SEQRES  22 A  306  GLN GLY ALA PRO ILE GLU SER GLY HIS PHE LEU PRO GLU          
SEQRES  23 A  306  GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE          
SEQRES  24 A  306  PHE SER ALA ALA PRO GLY SER                                  
SEQRES   1 B  306  GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE          
SEQRES   2 B  306  GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE          
SEQRES   3 B  306  ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU          
SEQRES   4 B  306  HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL          
SEQRES   5 B  306  ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA          
SEQRES   6 B  306  ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER          
SEQRES   7 B  306  ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA          
SEQRES   8 B  306  LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL          
SEQRES   9 B  306  HIS PHE ALA LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL          
SEQRES  10 B  306  SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER          
SEQRES  11 B  306  LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR          
SEQRES  12 B  306  TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR          
SEQRES  13 B  306  HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU          
SEQRES  14 B  306  ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA          
SEQRES  15 B  306  LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA          
SEQRES  16 B  306  PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE          
SEQRES  17 B  306  ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP TYR          
SEQRES  18 B  306  ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE          
SEQRES  19 B  306  ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU          
SEQRES  20 B  306  ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA          
SEQRES  21 B  306  THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL          
SEQRES  22 B  306  GLN GLY ALA PRO ILE GLU SER GLY HIS PHE LEU PRO GLU          
SEQRES  23 B  306  GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE          
SEQRES  24 B  306  PHE SER ALA ALA PRO GLY SER                                  
HET     CA  B 401       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  HOH   *217(H2 O)                                                    
HELIX    1 AA1 THR A   43  HIS A   48  5                                   6    
HELIX    2 AA2 VAL A   50  GLU A   56  1                                   7    
HELIX    3 AA3 HIS A   80  TYR A   83  5                                   4    
HELIX    4 AA4 THR A   84  LEU A   99  1                                  16    
HELIX    5 AA5 ASP A  110  SER A  123  1                                  14    
HELIX    6 AA6 PRO A  137  ARG A  144  1                                   8    
HELIX    7 AA7 ASN A  146  ILE A  153  1                                   8    
HELIX    8 AA8 TYR A  154  LEU A  159  1                                   6    
HELIX    9 AA9 PRO A  164  GLY A  171  1                                   8    
HELIX   10 AB1 ASP A  173  THR A  186  1                                  14    
HELIX   11 AB2 ASP A  195  ALA A  207  1                                  13    
HELIX   12 AB3 ASP A  208  TYR A  224  1                                  17    
HELIX   13 AB4 TYR A  224  GLY A  237  1                                  14    
HELIX   14 AB5 ILE A  253  ALA A  257  5                                   5    
HELIX   15 AB6 THR A  259  ALA A  268  1                                  10    
HELIX   16 AB7 PHE A  281  ALA A  286  1                                   6    
HELIX   17 AB8 ALA A  286  ALA A  300  1                                  15    
HELIX   18 AB9 THR B   43  HIS B   48  5                                   6    
HELIX   19 AC1 VAL B   50  ALA B   55  1                                   6    
HELIX   20 AC2 HIS B   80  TYR B   83  5                                   4    
HELIX   21 AC3 THR B   84  LEU B   99  1                                  16    
HELIX   22 AC4 ASP B  110  SER B  123  1                                  14    
HELIX   23 AC5 PRO B  137  ARG B  144  1                                   8    
HELIX   24 AC6 ASN B  146  ILE B  153  1                                   8    
HELIX   25 AC7 ILE B  153  LEU B  159  1                                   7    
HELIX   26 AC8 PRO B  164  GLY B  171  1                                   8    
HELIX   27 AC9 ASP B  173  TRP B  185  1                                  13    
HELIX   28 AD1 ASP B  195  ALA B  207  1                                  13    
HELIX   29 AD2 ASP B  208  TYR B  224  1                                  17    
HELIX   30 AD3 TYR B  224  GLY B  237  1                                  14    
HELIX   31 AD4 THR B  259  ALA B  268  1                                  10    
HELIX   32 AD5 PHE B  281  ALA B  286  1                                   6    
HELIX   33 AD6 ALA B  286  ALA B  300  1                                  15    
SHEET    1 AA1 8 GLY A  12  ILE A  16  0                                        
SHEET    2 AA1 8 ILE A  23  GLY A  29 -1  O  VAL A  27   N  GLY A  12           
SHEET    3 AA1 8 LYS A  59  ALA A  63 -1  O  VAL A  62   N  ARG A  26           
SHEET    4 AA1 8 PRO A  33  LEU A  37  1  N  LEU A  34   O  LYS A  59           
SHEET    5 AA1 8 PHE A 104  HIS A 109  1  O  ALA A 105   N  LEU A  35           
SHEET    6 AA1 8 LEU A 127  LEU A 133  1  O  ALA A 131   N  LEU A 106           
SHEET    7 AA1 8 MET A 244  GLY A 249  1  O  LEU A 245   N  VAL A 132           
SHEET    8 AA1 8 VAL A 271  ILE A 276  1  O  GLN A 272   N  ALA A 246           
SHEET    1 AA2 8 GLY B  12  ILE B  16  0                                        
SHEET    2 AA2 8 ILE B  23  GLY B  28 -1  O  VAL B  27   N  GLY B  12           
SHEET    3 AA2 8 LYS B  59  ALA B  63 -1  O  VAL B  62   N  ARG B  26           
SHEET    4 AA2 8 PRO B  33  LEU B  37  1  N  LEU B  34   O  LYS B  59           
SHEET    5 AA2 8 PHE B 104  HIS B 109  1  O  ALA B 105   N  LEU B  35           
SHEET    6 AA2 8 LEU B 127  LEU B 133  1  O  ALA B 131   N  LEU B 106           
SHEET    7 AA2 8 MET B 244  GLY B 249  1  O  LEU B 245   N  LEU B 130           
SHEET    8 AA2 8 VAL B 271  ILE B 276  1  O  GLN B 272   N  ALA B 246           
LINK         OD2 ASP B 173                CA    CA B 401     1555   1555  2.41  
LINK        CA    CA B 401                 O   HOH A 401     1555   1555  2.88  
LINK        CA    CA B 401                 O   HOH A 423     1555   1555  2.66  
LINK         O   ALA A 236                CA    CA B 401     1555   2557  2.55  
LINK        CA    CA B 401                 O   HOH A 445     1555   2547  2.41  
CISPEP   1 PHE A   40    PRO A   41          0        -4.34                     
CISPEP   2 ALA A  163    PRO A  164          0         1.72                     
CISPEP   3 PHE B   40    PRO B   41          0        -6.08                     
CISPEP   4 ALA B  163    PRO B  164          0         2.13                     
SITE     1 AC1  3 HOH A 401  HOH A 423  ASP B 173                               
CRYST1   41.600   79.100   83.800  90.00 103.00  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      0.024038  0.000000  0.005550        0.00000                         
SCALE2      0.000000  0.012642  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012247        0.00000                         
TER    2387      ALA A 300                                                      
TER    4756      ALA B 300                                                      
MASTER      307    0    1   33   16    0    1    6 4922    2    4   48          
END                                                                             

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