Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 5z7w-pdb

Name Class
5z7w-pdb
HEADER    HYDROLASE                               30-JAN-18   5Z7W              
TITLE     CRYSTAL STRUCTURE OF STRIGA HERMONTHICA HTL1 (SHHTL1)                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYPOSENSITIVE TO LIGHT 1;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HYDROLASE, ALPHA/BETA FOLD FAMILY PROTEIN;                  
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STRIGA HERMONTHICA;                             
SOURCE   3 ORGANISM_COMMON: PURPLE WITCHWEED;                                   
SOURCE   4 ORGANISM_TAXID: 68872;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    HYDROLASE ACTIVITY, PUTATIVE RECEPTOR OF KARRIKIN, HYDROLASE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.XU,T.MIYAKAWA,A.NAKAMURA,M.TANOKURA                                 
REVDAT   1   29-AUG-18 5Z7W    0                                                
JRNL        AUTH   Y.XU,T.MIYAKAWA,S.NOSAKI,A.NAKAMURA,Y.LYU,H.NAKAMURA,U.OHTO, 
JRNL        AUTH 2 H.ISHIDA,T.SHIMIZU,T.ASAMI,M.TANOKURA                        
JRNL        TITL   COMPREHENSIVE STRUCTURAL STUDIES REVEAL EVOLUTION OF         
JRNL        TITL 2 STRIGOLACTONE/KARRIKIN SELECTIVITY OF HTL AND D14 PROTEINS   
JRNL        TITL 3 IN STRIGA                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.66 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
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) : 1.66                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.95                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 127260                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6415                            
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 38.9640 -  5.1450    1.00     4080   197  0.1654 0.2051        
REMARK   3     2  5.1450 -  4.0851    1.00     4045   218  0.1382 0.1604        
REMARK   3     3  4.0851 -  3.5692    1.00     4019   244  0.1418 0.1678        
REMARK   3     4  3.5692 -  3.2430    1.00     4048   219  0.1507 0.1836        
REMARK   3     5  3.2430 -  3.0107    1.00     4082   186  0.1495 0.1640        
REMARK   3     6  3.0107 -  2.8332    1.00     4048   212  0.1562 0.1623        
REMARK   3     7  2.8332 -  2.6914    1.00     4044   242  0.1668 0.1958        
REMARK   3     8  2.6914 -  2.5742    1.00     3997   223  0.1707 0.2035        
REMARK   3     9  2.5742 -  2.4751    1.00     4005   262  0.1635 0.1971        
REMARK   3    10  2.4751 -  2.3897    1.00     4063   228  0.1664 0.1913        
REMARK   3    11  2.3897 -  2.3150    1.00     4066   216  0.1661 0.2137        
REMARK   3    12  2.3150 -  2.2489    1.00     4023   211  0.1698 0.2014        
REMARK   3    13  2.2489 -  2.1897    1.00     4074   230  0.1636 0.2178        
REMARK   3    14  2.1897 -  2.1362    1.00     4011   204  0.1694 0.1812        
REMARK   3    15  2.1362 -  2.0877    1.00     4078   243  0.1762 0.2102        
REMARK   3    16  2.0877 -  2.0433    1.00     4084   183  0.1778 0.2556        
REMARK   3    17  2.0433 -  2.0024    1.00     4111   178  0.1884 0.2235        
REMARK   3    18  2.0024 -  1.9646    1.00     4005   236  0.1946 0.2082        
REMARK   3    19  1.9646 -  1.9295    1.00     4086   185  0.2040 0.2538        
REMARK   3    20  1.9295 -  1.8968    1.00     4023   203  0.2048 0.2181        
REMARK   3    21  1.8968 -  1.8662    1.00     4079   214  0.1939 0.2284        
REMARK   3    22  1.8662 -  1.8375    1.00     4048   238  0.1978 0.2445        
REMARK   3    23  1.8375 -  1.8105    1.00     4022   220  0.2190 0.2879        
REMARK   3    24  1.8105 -  1.7850    1.00     4045   223  0.2153 0.2594        
REMARK   3    25  1.7850 -  1.7609    1.00     4030   202  0.2288 0.2616        
REMARK   3    26  1.7609 -  1.7380    1.00     4077   223  0.2337 0.2429        
REMARK   3    27  1.7380 -  1.7163    0.99     4010   226  0.2480 0.2828        
REMARK   3    28  1.7163 -  1.6956    0.98     3957   174  0.2527 0.3008        
REMARK   3    29  1.6956 -  1.6759    0.97     4045   153  0.2678 0.2566        
REMARK   3    30  1.6759 -  1.6570    0.89     3540   222  0.2798 0.3105        
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)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.150           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           4316                                  
REMARK   3   ANGLE     :  0.657           5890                                  
REMARK   3   CHIRALITY :  0.050            678                                  
REMARK   3   PLANARITY :  0.005            757                                  
REMARK   3   DIHEDRAL  : 12.723           2544                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  14.6835  25.3781  15.3325              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0867 T22:   0.0860                                     
REMARK   3      T33:   0.0571 T12:  -0.0017                                     
REMARK   3      T13:   0.0059 T23:   0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2793 L22:   0.2991                                     
REMARK   3      L33:   0.0174 L12:  -0.0576                                     
REMARK   3      L13:  -0.0115 L23:   0.0606                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0004 S12:   0.0070 S13:  -0.0296                       
REMARK   3      S21:   0.0105 S22:  -0.0069 S23:  -0.0124                       
REMARK   3      S31:  -0.0110 S32:  -0.0007 S33:   0.0000                       
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 5Z7W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300006457.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-FEB-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-5A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 127266                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.657                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 18.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 4JYP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL (PH 8.5), 200MM MGCL2,     
REMARK 280  30% (W/V) PEG 4000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE      
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       40.58500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       69.38500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.58500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       69.38500            
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 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 631  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 644  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 710  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 730  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 733  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 777  LIES ON A SPECIAL POSITION.                          
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    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     LEU A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     PRO A   271                                                      
REMARK 465     ASN A   272                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     PRO B    -3                                                      
REMARK 465     LEU B    -2                                                      
REMARK 465     ARG B   270                                                      
REMARK 465     PRO B   271                                                      
REMARK 465     ASN B   272                                                      
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    THR A  28     -161.44   -121.12                                   
REMARK 500    PHE A  62      121.82    -39.45                                   
REMARK 500    SER A  95     -119.46     49.09                                   
REMARK 500    ARG A 123      123.98   -171.29                                   
REMARK 500    LEU A 247       55.86   -119.45                                   
REMARK 500    MET B   1       35.62    -83.80                                   
REMARK 500    THR B  28     -163.65   -121.62                                   
REMARK 500    PRO B  59       12.48    -64.03                                   
REMARK 500    SER B  95     -119.48     53.04                                   
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 792        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH A 793        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH A 794        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH A 795        DISTANCE =  6.33 ANGSTROMS                       
REMARK 525    HOH A 796        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH A 797        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH A 798        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH A 799        DISTANCE =  6.88 ANGSTROMS                       
REMARK 525    HOH A 800        DISTANCE =  6.90 ANGSTROMS                       
REMARK 525    HOH A 801        DISTANCE =  7.10 ANGSTROMS                       
REMARK 525    HOH B 801        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH B 802        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH B 803        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH B 804        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH B 805        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH B 806        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH B 807        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH B 808        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH B 809        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH B 810        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH B 811        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH B 812        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH B 813        DISTANCE =  6.79 ANGSTROMS                       
REMARK 525    HOH B 814        DISTANCE =  6.80 ANGSTROMS                       
REMARK 525    HOH B 815        DISTANCE =  7.41 ANGSTROMS                       
REMARK 525    HOH B 816        DISTANCE =  7.49 ANGSTROMS                       
REMARK 525    HOH B 817        DISTANCE =  8.14 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 303  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO A 109   O                                                      
REMARK 620 2 PHE A 112   O    87.2                                              
REMARK 620 3 HOH A 647   O    86.5 173.7                                        
REMARK 620 4 HOH A 651   O   110.9  88.6  93.3                                  
REMARK 620 5 HOH A 658   O   138.8  94.3  90.7 110.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 129   OD2                                                    
REMARK 620 2 HOH A 611   O    92.9                                              
REMARK 620 3 HOH A 700   O   159.4 105.7                                        
REMARK 620 4 HOH A 655   O   101.5 104.3  82.6                                  
REMARK 620 5 HOH B 421   O    82.7  96.3  86.4 158.6                            
REMARK 620 6 HOH B 487   O    71.9 164.2  88.8  83.3  78.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 303  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO B 109   O                                                      
REMARK 620 2 PHE B 112   O    69.4                                              
REMARK 620 3 HOH B 655   O   152.7  85.0                                        
REMARK 620 4 HOH B 728   O   109.5 156.5  90.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 302  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 503   O                                                      
REMARK 620 2 HOH B 706   O    49.5                                              
REMARK 620 3 HOH B 401   O    53.4  62.3                                        
REMARK 620 4 GLU A 141   OE2  59.0  30.3  38.9                                  
REMARK 620 5 HOH A 670   O    59.4 108.8  74.1 107.3                            
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 MG A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 304                 
DBREF1 5Z7W A    1   272  UNP                  A0A0M4AV81_STRHE                 
DBREF2 5Z7W A     A0A0M4AV81                          1         272             
DBREF1 5Z7W B    1   272  UNP                  A0A0M4AV81_STRHE                 
DBREF2 5Z7W B     A0A0M4AV81                          1         272             
SEQADV 5Z7W GLY A   -4  UNP  A0A0M4AV8           EXPRESSION TAG                 
SEQADV 5Z7W PRO A   -3  UNP  A0A0M4AV8           EXPRESSION TAG                 
SEQADV 5Z7W LEU A   -2  UNP  A0A0M4AV8           EXPRESSION TAG                 
SEQADV 5Z7W GLY A   -1  UNP  A0A0M4AV8           EXPRESSION TAG                 
SEQADV 5Z7W SER A    0  UNP  A0A0M4AV8           EXPRESSION TAG                 
SEQADV 5Z7W GLY B   -4  UNP  A0A0M4AV8           EXPRESSION TAG                 
SEQADV 5Z7W PRO B   -3  UNP  A0A0M4AV8           EXPRESSION TAG                 
SEQADV 5Z7W LEU B   -2  UNP  A0A0M4AV8           EXPRESSION TAG                 
SEQADV 5Z7W GLY B   -1  UNP  A0A0M4AV8           EXPRESSION TAG                 
SEQADV 5Z7W SER B    0  UNP  A0A0M4AV8           EXPRESSION TAG                 
SEQRES   1 A  277  GLY PRO LEU GLY SER MET GLY LEU ALA GLN GLU ALA HIS          
SEQRES   2 A  277  ASN VAL ARG VAL LEU GLY SER GLY PRO GLN THR VAL VAL          
SEQRES   3 A  277  LEU ALA HIS GLY PHE GLY THR ASP GLN SER VAL TRP LYS          
SEQRES   4 A  277  TYR LEU VAL PRO HIS LEU VAL GLU ASP TYR ARG VAL VAL          
SEQRES   5 A  277  LEU PHE ASP ILE MET GLY ALA GLY THR THR ASN PRO THR          
SEQRES   6 A  277  TYR PHE ASN PHE GLU ARG TYR SER SER LEU GLU GLY TYR          
SEQRES   7 A  277  ALA GLY ASP VAL ILE ALA ILE LEU GLU GLU LEU GLN ILE          
SEQRES   8 A  277  SER SER CYS VAL TYR VAL GLY HIS SER VAL SER ALA MET          
SEQRES   9 A  277  ILE GLY VAL ILE ALA SER VAL THR ARG PRO ASP LEU PHE          
SEQRES  10 A  277  THR LYS LEU VAL THR VAL ALA GLY SER PRO ARG TYR LEU          
SEQRES  11 A  277  ASN ASP PRO ASP TYR PHE GLY GLY PHE ASP LEU ASP GLU          
SEQRES  12 A  277  LEU HIS GLU LEU PHE GLU ALA MET LYS GLU ASN TYR LYS          
SEQRES  13 A  277  ALA TRP CYS SER GLY PHE ALA PRO LEU CYS VAL GLY ALA          
SEQRES  14 A  277  ASP MET GLU SER LEU ALA VAL GLN GLU PHE SER ARG THR          
SEQRES  15 A  277  LEU PHE ASN MET ARG PRO ASP ILE ALA LEU SER ILE LEU          
SEQRES  16 A  277  GLN THR ILE PHE TYR SER ASP VAL ARG PRO LEU LEU PRO          
SEQRES  17 A  277  HIS VAL THR VAL PRO CYS HIS ILE ILE GLN SER VAL LYS          
SEQRES  18 A  277  ASP LEU ALA VAL PRO VAL ALA VAL SER GLU TYR ILE HIS          
SEQRES  19 A  277  GLN SER LEU GLY GLY GLU SER ILE LEU GLU VAL MET ALA          
SEQRES  20 A  277  THR GLU GLY HIS LEU PRO GLN LEU SER SER PRO ASP VAL          
SEQRES  21 A  277  VAL VAL PRO VAL LEU LEU ARG HIS ILE ARG TYR ALA ILE          
SEQRES  22 A  277  ALA ARG PRO ASN                                              
SEQRES   1 B  277  GLY PRO LEU GLY SER MET GLY LEU ALA GLN GLU ALA HIS          
SEQRES   2 B  277  ASN VAL ARG VAL LEU GLY SER GLY PRO GLN THR VAL VAL          
SEQRES   3 B  277  LEU ALA HIS GLY PHE GLY THR ASP GLN SER VAL TRP LYS          
SEQRES   4 B  277  TYR LEU VAL PRO HIS LEU VAL GLU ASP TYR ARG VAL VAL          
SEQRES   5 B  277  LEU PHE ASP ILE MET GLY ALA GLY THR THR ASN PRO THR          
SEQRES   6 B  277  TYR PHE ASN PHE GLU ARG TYR SER SER LEU GLU GLY TYR          
SEQRES   7 B  277  ALA GLY ASP VAL ILE ALA ILE LEU GLU GLU LEU GLN ILE          
SEQRES   8 B  277  SER SER CYS VAL TYR VAL GLY HIS SER VAL SER ALA MET          
SEQRES   9 B  277  ILE GLY VAL ILE ALA SER VAL THR ARG PRO ASP LEU PHE          
SEQRES  10 B  277  THR LYS LEU VAL THR VAL ALA GLY SER PRO ARG TYR LEU          
SEQRES  11 B  277  ASN ASP PRO ASP TYR PHE GLY GLY PHE ASP LEU ASP GLU          
SEQRES  12 B  277  LEU HIS GLU LEU PHE GLU ALA MET LYS GLU ASN TYR LYS          
SEQRES  13 B  277  ALA TRP CYS SER GLY PHE ALA PRO LEU CYS VAL GLY ALA          
SEQRES  14 B  277  ASP MET GLU SER LEU ALA VAL GLN GLU PHE SER ARG THR          
SEQRES  15 B  277  LEU PHE ASN MET ARG PRO ASP ILE ALA LEU SER ILE LEU          
SEQRES  16 B  277  GLN THR ILE PHE TYR SER ASP VAL ARG PRO LEU LEU PRO          
SEQRES  17 B  277  HIS VAL THR VAL PRO CYS HIS ILE ILE GLN SER VAL LYS          
SEQRES  18 B  277  ASP LEU ALA VAL PRO VAL ALA VAL SER GLU TYR ILE HIS          
SEQRES  19 B  277  GLN SER LEU GLY GLY GLU SER ILE LEU GLU VAL MET ALA          
SEQRES  20 B  277  THR GLU GLY HIS LEU PRO GLN LEU SER SER PRO ASP VAL          
SEQRES  21 B  277  VAL VAL PRO VAL LEU LEU ARG HIS ILE ARG TYR ALA ILE          
SEQRES  22 B  277  ALA ARG PRO ASN                                              
HET     MG  A 301       1                                                       
HET     MG  A 302       1                                                       
HET     NA  A 303       1                                                       
HET    GOL  A 304       6                                                       
HET     MG  B 301       1                                                       
HET     NA  B 302       1                                                       
HET     NA  B 303       1                                                       
HET    GOL  B 304       6                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      NA SODIUM ION                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   MG    3(MG 2+)                                                     
FORMUL   5   NA    3(NA 1+)                                                     
FORMUL   6  GOL    2(C3 H8 O3)                                                  
FORMUL  11  HOH   *818(H2 O)                                                    
HELIX    1 AA1 GLY A    2  HIS A    8  1                                   7    
HELIX    2 AA2 ASP A   29  LYS A   34  5                                   6    
HELIX    3 AA3 LEU A   36  LEU A   40  5                                   5    
HELIX    4 AA4 GLU A   65  SER A   68  5                                   4    
HELIX    5 AA5 SER A   69  LEU A   84  1                                  16    
HELIX    6 AA6 SER A   95  ARG A  108  1                                  14    
HELIX    7 AA7 ASP A  135  ASN A  149  1                                  15    
HELIX    8 AA8 ASN A  149  GLY A  163  1                                  15    
HELIX    9 AA9 SER A  168  ASN A  180  1                                  13    
HELIX   10 AB1 ARG A  182  TYR A  195  1                                  14    
HELIX   11 AB2 VAL A  198  VAL A  205  5                                   8    
HELIX   12 AB3 PRO A  221  LEU A  232  1                                  12    
HELIX   13 AB4 LEU A  247  SER A  252  1                                   6    
HELIX   14 AB5 SER A  252  TYR A  266  1                                  15    
HELIX   15 AB6 GLY B    2  HIS B    8  1                                   7    
HELIX   16 AB7 ASP B   29  LYS B   34  5                                   6    
HELIX   17 AB8 LEU B   36  LEU B   40  5                                   5    
HELIX   18 AB9 GLU B   65  SER B   68  5                                   4    
HELIX   19 AC1 SER B   69  LEU B   84  1                                  16    
HELIX   20 AC2 SER B   95  ARG B  108  1                                  14    
HELIX   21 AC3 ASP B  135  ASN B  149  1                                  15    
HELIX   22 AC4 ASN B  149  GLY B  163  1                                  15    
HELIX   23 AC5 SER B  168  ASN B  180  1                                  13    
HELIX   24 AC6 ARG B  182  TYR B  195  1                                  14    
HELIX   25 AC7 VAL B  198  VAL B  205  5                                   8    
HELIX   26 AC8 PRO B  221  LEU B  232  1                                  12    
HELIX   27 AC9 LEU B  247  SER B  252  1                                   6    
HELIX   28 AD1 SER B  252  TYR B  266  1                                  15    
SHEET    1 AA1 7 ARG A  11  GLY A  14  0                                        
SHEET    2 AA1 7 ARG A  45  PHE A  49 -1  O  LEU A  48   N  ARG A  11           
SHEET    3 AA1 7 THR A  19  ALA A  23  1  N  VAL A  20   O  ARG A  45           
SHEET    4 AA1 7 CYS A  89  HIS A  94  1  O  VAL A  90   N  VAL A  21           
SHEET    5 AA1 7 PHE A 112  VAL A 118  1  O  VAL A 116   N  GLY A  93           
SHEET    6 AA1 7 CYS A 209  LYS A 216  1  O  HIS A 210   N  LEU A 115           
SHEET    7 AA1 7 SER A 236  GLU A 244  1  O  ILE A 237   N  ILE A 211           
SHEET    1 AA2 7 ARG B  11  GLY B  14  0                                        
SHEET    2 AA2 7 ARG B  45  PHE B  49 -1  O  VAL B  46   N  LEU B  13           
SHEET    3 AA2 7 THR B  19  ALA B  23  1  N  VAL B  20   O  ARG B  45           
SHEET    4 AA2 7 CYS B  89  HIS B  94  1  O  VAL B  92   N  VAL B  21           
SHEET    5 AA2 7 PHE B 112  VAL B 118  1  O  VAL B 116   N  TYR B  91           
SHEET    6 AA2 7 CYS B 209  LYS B 216  1  O  HIS B 210   N  LEU B 115           
SHEET    7 AA2 7 SER B 236  GLU B 244  1  O  MET B 241   N  GLN B 213           
LINK         OG  SER A  95                MG    MG A 302     1555   1555  2.83  
LINK         O   PRO A 109                NA    NA A 303     1555   1555  2.38  
LINK         O   PHE A 112                NA    NA A 303     1555   1555  2.32  
LINK         OD2 ASP A 129                MG    MG A 301     1555   1555  2.05  
LINK         OG  SER B  95                MG    MG B 301     1555   1555  2.86  
LINK         O   PRO B 109                NA    NA B 303     1555   1555  2.64  
LINK         O   PHE B 112                NA    NA B 303     1555   1555  2.63  
LINK        MG    MG A 301                 O   HOH A 611     1555   1555  2.13  
LINK        NA    NA A 303                 O   HOH A 647     1555   1555  2.43  
LINK        NA    NA A 303                 O   HOH A 651     1555   1555  2.46  
LINK        NA    NA A 303                 O   HOH A 658     1555   1555  2.34  
LINK        NA    NA B 302                 O   HOH B 503     1555   1555  3.18  
LINK        NA    NA B 302                 O   HOH B 706     1555   1555  2.75  
LINK        NA    NA B 302                 O   HOH B 401     1555   1555  2.73  
LINK        NA    NA B 303                 O   HOH B 655     1555   1555  2.45  
LINK        NA    NA B 303                 O   HOH B 728     1555   1555  2.42  
LINK         OE2 GLU A 141                NA    NA B 302     1555   3546  2.98  
LINK        MG    MG A 301                 O   HOH A 700     1555   2655  2.58  
LINK        MG    MG A 301                 O   HOH A 655     1555   2655  2.05  
LINK        MG    MG A 301                 O   HOH B 421     1555   3546  2.49  
LINK        MG    MG A 301                 O   HOH B 487     1555   3546  2.63  
LINK        NA    NA B 302                 O   HOH A 670     1555   3556  2.41  
SITE     1 AC1  6 ASP A 129  HOH A 611  HOH A 655  HOH A 700                    
SITE     2 AC1  6 HOH B 421  HOH B 487                                          
SITE     1 AC2  4 PHE A  26  SER A  95  VAL A  96  GOL A 304                    
SITE     1 AC3  5 PRO A 109  PHE A 112  HOH A 647  HOH A 651                    
SITE     2 AC3  5 HOH A 658                                                     
SITE     1 AC4  6 SER A  95  PHE A 157  ILE A 193  HIS A 246                    
SITE     2 AC4  6  MG A 302  HOH A 414                                          
SITE     1 AC5  4 PHE B  26  SER B  95  VAL B  96  GOL B 304                    
SITE     1 AC6  4 GLU A 141  HOH A 670  HOH B 401  HOH B 706                    
SITE     1 AC7  5 PRO B 109  PHE B 112  VAL B 207  HOH B 655                    
SITE     2 AC7  5 HOH B 728                                                     
SITE     1 AC8  6 SER B  95  PHE B 157  ALA B 219  HIS B 246                    
SITE     2 AC8  6  MG B 301  HOH B 521                                          
CRYST1   81.170  138.770   49.410  90.00  90.00  90.00 P 21 21 2     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      0.012320  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007206  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020239        0.00000                         
TER    2106      ARG A 270                                                      
TER    4201      ALA B 269                                                      
MASTER      415    0    8   28   14    0   13    6 5017    2   35   44          
END                                                                             

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

Acknowledgements and disclaimer