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LongText Report for: 6jtt-pdb

Name Class
6jtt-pdb
HEADER    HYDROLASE                               12-APR-19   6JTT              
TITLE     MHETASE IN COMPLEX WITH BHET                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MONO(2-HYDROXYETHYL) TEREPHTHALATE HYDROLASE;              
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: FERULOYL ESTERASE DOMAIN;                                  
COMPND   5 EC: 3.1.1.102;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS;                           
SOURCE   3 ORGANISM_TAXID: 1547922;                                             
SOURCE   4 STRAIN: 201-F6;                                                      
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.-Y.SAGONG,H.SEO,K.-J.KIM                                            
REVDAT   1   15-APR-20 6JTT    0                                                
JRNL        AUTH   H.-Y.SAGONG,H.SEO,K.-J.KIM                                   
JRNL        TITL   STRUCTURAL INSIGHT INTO MHET HYDROLYSIS BY MHETASE           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.51 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0238                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.51                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.21                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 108686                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5549                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.51                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7696                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.07                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2530                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 406                          
REMARK   3   BIN FREE R VALUE                    : 0.3100                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12369                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 49                                      
REMARK   3   SOLVENT ATOMS            : 500                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.19000                                             
REMARK   3    B22 (A**2) : -1.61000                                             
REMARK   3    B33 (A**2) : 2.34000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.92000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.233         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.201         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.137         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.264         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12812 ; 0.011 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A): 11298 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 17421 ; 1.772 ; 1.641       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 26144 ; 1.407 ; 1.575       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1675 ; 7.101 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   628 ;32.338 ;21.688       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1777 ;15.550 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    84 ;21.322 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1640 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 14925 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2863 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 6JTT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-APR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300011800.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 7A (6B, 6C1)                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 114235                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.210                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 2.100                              
REMARK 200  R MERGE                    (I) : 0.08600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.7500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, HEPES, TACSIMATE PH 7.0, PH     
REMARK 280  6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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      107.62950            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       86.89950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      107.62950            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       86.89950            
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, 3                                                 
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    -9                                                      
REMARK 465     MET A    -8                                                      
REMARK 465     ILE A    -7                                                      
REMARK 465     THR A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     ARG A    -4                                                      
REMARK 465     LYS A    -3                                                      
REMARK 465     LEU A    -2                                                      
REMARK 465     PRO A    -1                                                      
REMARK 465     LEU A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     VAL A     8                                                      
REMARK 465     MET A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     GLN A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     MET A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     MET A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     CYS A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     GLY A    21                                                      
REMARK 465     GLY A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     THR A    24                                                      
REMARK 465     PRO A    25                                                      
REMARK 465     LEU A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     LEU A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     GLN A    30                                                      
REMARK 465     GLN A    31                                                      
REMARK 465     GLN A    32                                                      
REMARK 465     PRO A    33                                                      
REMARK 465     PRO A    34                                                      
REMARK 465     GLN A    35                                                      
REMARK 465     GLN A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     PRO A    38                                                      
REMARK 465     PRO A    39                                                      
REMARK 465     PRO A    40                                                      
REMARK 465     PRO A    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     ASP A    56                                                      
REMARK 465     LEU A   604                                                      
REMARK 465     GLU A   605                                                      
REMARK 465     HIS A   606                                                      
REMARK 465     HIS A   607                                                      
REMARK 465     HIS A   608                                                      
REMARK 465     HIS A   609                                                      
REMARK 465     HIS A   610                                                      
REMARK 465     HIS A   611                                                      
REMARK 465     MET B    -9                                                      
REMARK 465     MET B    -8                                                      
REMARK 465     ILE B    -7                                                      
REMARK 465     THR B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     ARG B    -4                                                      
REMARK 465     LYS B    -3                                                      
REMARK 465     LEU B    -2                                                      
REMARK 465     PRO B    -1                                                      
REMARK 465     LEU B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     VAL B     8                                                      
REMARK 465     MET B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     GLN B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     MET B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     MET B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     CYS B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     GLY B    20                                                      
REMARK 465     GLY B    21                                                      
REMARK 465     GLY B    22                                                      
REMARK 465     SER B    23                                                      
REMARK 465     THR B    24                                                      
REMARK 465     PRO B    25                                                      
REMARK 465     LEU B    26                                                      
REMARK 465     PRO B    27                                                      
REMARK 465     LEU B    28                                                      
REMARK 465     PRO B    29                                                      
REMARK 465     GLN B    30                                                      
REMARK 465     GLN B    31                                                      
REMARK 465     GLN B    32                                                      
REMARK 465     PRO B    33                                                      
REMARK 465     PRO B    34                                                      
REMARK 465     GLN B    35                                                      
REMARK 465     GLN B    36                                                      
REMARK 465     GLU B    37                                                      
REMARK 465     PRO B    38                                                      
REMARK 465     PRO B    39                                                      
REMARK 465     PRO B    40                                                      
REMARK 465     PRO B    41                                                      
REMARK 465     PRO B    42                                                      
REMARK 465     ASP B    56                                                      
REMARK 465     GLY B    57                                                      
REMARK 465     ASN B    58                                                      
REMARK 465     GLY B    59                                                      
REMARK 465     GLU B   605                                                      
REMARK 465     HIS B   606                                                      
REMARK 465     HIS B   607                                                      
REMARK 465     HIS B   608                                                      
REMARK 465     HIS B   609                                                      
REMARK 465     HIS B   610                                                      
REMARK 465     HIS B   611                                                      
REMARK 465     MET C    -9                                                      
REMARK 465     MET C    -8                                                      
REMARK 465     ILE C    -7                                                      
REMARK 465     THR C    -6                                                      
REMARK 465     LEU C    -5                                                      
REMARK 465     ARG C    -4                                                      
REMARK 465     LYS C    -3                                                      
REMARK 465     LEU C    -2                                                      
REMARK 465     PRO C    -1                                                      
REMARK 465     LEU C     0                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     ALA C     3                                                      
REMARK 465     VAL C     4                                                      
REMARK 465     ALA C     5                                                      
REMARK 465     ALA C     6                                                      
REMARK 465     GLY C     7                                                      
REMARK 465     VAL C     8                                                      
REMARK 465     MET C     9                                                      
REMARK 465     SER C    10                                                      
REMARK 465     ALA C    11                                                      
REMARK 465     GLN C    12                                                      
REMARK 465     ALA C    13                                                      
REMARK 465     MET C    14                                                      
REMARK 465     ALA C    15                                                      
REMARK 465     MET C    16                                                      
REMARK 465     ALA C    17                                                      
REMARK 465     CYS C    18                                                      
REMARK 465     ALA C    19                                                      
REMARK 465     GLY C    20                                                      
REMARK 465     GLY C    21                                                      
REMARK 465     GLY C    22                                                      
REMARK 465     SER C    23                                                      
REMARK 465     THR C    24                                                      
REMARK 465     PRO C    25                                                      
REMARK 465     LEU C    26                                                      
REMARK 465     PRO C    27                                                      
REMARK 465     LEU C    28                                                      
REMARK 465     PRO C    29                                                      
REMARK 465     GLN C    30                                                      
REMARK 465     GLN C    31                                                      
REMARK 465     GLN C    32                                                      
REMARK 465     PRO C    33                                                      
REMARK 465     PRO C    34                                                      
REMARK 465     GLN C    35                                                      
REMARK 465     GLN C    36                                                      
REMARK 465     GLU C    37                                                      
REMARK 465     PRO C    38                                                      
REMARK 465     PRO C    39                                                      
REMARK 465     PRO C    40                                                      
REMARK 465     PRO C    41                                                      
REMARK 465     PRO C    42                                                      
REMARK 465     ASP C    56                                                      
REMARK 465     GLY C    57                                                      
REMARK 465     ASN C    58                                                      
REMARK 465     GLY C    59                                                      
REMARK 465     LEU C   604                                                      
REMARK 465     GLU C   605                                                      
REMARK 465     HIS C   606                                                      
REMARK 465     HIS C   607                                                      
REMARK 465     HIS C   608                                                      
REMARK 465     HIS C   609                                                      
REMARK 465     HIS C   610                                                      
REMARK 465     HIS C   611                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU B 604    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A   225     C10  C9C A   701              1.38            
REMARK 500   OG   SER C   225     C10  C9C C   701              1.43            
REMARK 500   SG   CYS A    51     O    HOH A   936              1.46            
REMARK 500   NH2  ARG A   411     O    ALA A   494              2.09            
REMARK 500   OD1  ASP B   307     O    HOH B   801              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP B 307   CB  -  CA  -  C   ANGL. DEV. = -18.6 DEGREES          
REMARK 500    ARG B 480   CB  -  CA  -  C   ANGL. DEV. = -13.1 DEGREES          
REMARK 500    ARG B 550   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG C 480   CB  -  CA  -  C   ANGL. DEV. = -16.2 DEGREES          
REMARK 500    MET C 490   CG  -  SD  -  CE  ANGL. DEV. = -10.0 DEGREES          
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    ALA A  67       41.72    -89.77                                   
REMARK 500    ASN A 134     -144.72     57.14                                   
REMARK 500    ASN A 171       51.32    -98.81                                   
REMARK 500    TYR A 194      -40.60   -150.67                                   
REMARK 500    SER A 225     -121.68     69.15                                   
REMARK 500    ALA A 249       59.73     33.64                                   
REMARK 500    LEU A 309      115.65   -160.81                                   
REMARK 500    ASP A 311       11.41   -147.65                                   
REMARK 500    TYR A 373     -102.56   -145.77                                   
REMARK 500    SER A 383     -142.76   -143.23                                   
REMARK 500    GLU A 429       73.24   -114.80                                   
REMARK 500    SER A 456      119.50   -166.69                                   
REMARK 500    PHE A 517      -19.21   -142.15                                   
REMARK 500    ASN A 527     -145.50    -86.72                                   
REMARK 500    CYS A 529      -26.82     73.01                                   
REMARK 500    PRO A 533       68.68    -68.94                                   
REMARK 500    ALA B  67       35.63    -87.86                                   
REMARK 500    ASN B 134     -145.58     55.17                                   
REMARK 500    ASN B 156       21.26     80.70                                   
REMARK 500    ASN B 171       56.24    -93.09                                   
REMARK 500    TYR B 194      -36.76   -146.09                                   
REMARK 500    SER B 225     -119.20     64.34                                   
REMARK 500    ALA B 249       57.00     32.48                                   
REMARK 500    ASP B 311       11.72   -143.69                                   
REMARK 500    TYR B 373      -95.40   -143.61                                   
REMARK 500    SER B 383     -140.09   -140.60                                   
REMARK 500    SER B 456      114.38   -164.00                                   
REMARK 500    ASN B 527     -147.16    -79.68                                   
REMARK 500    CYS B 529      -23.80     71.43                                   
REMARK 500    TYR B 579      134.64    -38.65                                   
REMARK 500    ALA C  67       42.75    -84.91                                   
REMARK 500    ASN C 134     -141.95     62.79                                   
REMARK 500    ASN C 171       53.88    -98.48                                   
REMARK 500    TYR C 194      -33.52   -148.61                                   
REMARK 500    SER C 225     -116.14     70.35                                   
REMARK 500    ALA C 249       57.12     34.22                                   
REMARK 500    ASP C 311        4.48   -152.00                                   
REMARK 500    TYR C 373     -102.79   -139.05                                   
REMARK 500    SER C 383     -141.53   -135.12                                   
REMARK 500    SER C 404      148.03   -176.86                                   
REMARK 500    GLU C 429       74.31   -118.40                                   
REMARK 500    ASN C 527     -140.59    -87.12                                   
REMARK 500    CYS C 529      -20.59     71.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 C9C HAS A BETAHYDROXY-COVALENT INTERMEDIATE STATE WITH SERINE225.    
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     C9C A  701                                                       
REMARK 610     C9C C  701                                                       
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 A 702  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 304   O                                                      
REMARK 620 2 ASP A 304   OD1  68.7                                              
REMARK 620 3 ASP A 307   OD1  68.7 128.2                                        
REMARK 620 4 ASP A 307   OD2  78.4 141.3  49.6                                  
REMARK 620 5 LEU A 309   O    84.0  80.9 121.9  75.8                            
REMARK 620 6 ASP A 311   OD1 142.8  74.5 144.2 132.7  85.4                      
REMARK 620 7 ILE A 313   O   105.5  87.9  76.4 121.1 161.7  77.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 702  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 304   O                                                      
REMARK 620 2 ASP B 304   OD1  64.2                                              
REMARK 620 3 ASP B 307   OD1  95.0 157.5                                        
REMARK 620 4 LEU B 309   O    87.8  81.1 107.8                                  
REMARK 620 5 ASP B 311   OD1 152.5  88.8 112.5  82.4                            
REMARK 620 6 ILE B 313   O    99.5  90.8  84.2 165.5  85.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 702  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 304   O                                                      
REMARK 620 2 ASP C 304   OD2  71.1                                              
REMARK 620 3 ASP C 307   OD1  76.2 144.9                                        
REMARK 620 4 ASP C 307   OD2  64.9 122.9  48.3                                  
REMARK 620 5 LEU C 309   O    85.9  85.4  80.1 124.1                            
REMARK 620 6 ASP C 311   OD1 144.2  74.1 134.5 146.2  83.2                      
REMARK 620 7 ILE C 313   O    96.5  77.5 119.1  73.5 160.8  83.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue C9C A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue C8X B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide C9C C 701 and SER C    
REMARK 800  225                                                                 
DBREF1 6JTT A   17   603  UNP                  MHETH_IDESA                      
DBREF2 6JTT A     A0A0K8P8E7                         17         603             
DBREF1 6JTT B   17   603  UNP                  MHETH_IDESA                      
DBREF2 6JTT B     A0A0K8P8E7                         17         603             
DBREF1 6JTT C   17   603  UNP                  MHETH_IDESA                      
DBREF2 6JTT C     A0A0K8P8E7                         17         603             
SEQADV 6JTT MET A   -9  UNP  A0A0K8P8E           INITIATING METHIONINE          
SEQADV 6JTT MET A   -8  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ILE A   -7  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT THR A   -6  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT LEU A   -5  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ARG A   -4  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT LYS A   -3  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT LEU A   -2  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT PRO A   -1  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT LEU A    0  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA A    1  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT VAL A    2  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA A    3  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT VAL A    4  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA A    5  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA A    6  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT GLY A    7  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT VAL A    8  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT MET A    9  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT SER A   10  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA A   11  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT GLN A   12  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA A   13  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT MET A   14  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA A   15  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT MET A   16  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT LEU A  604  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT GLU A  605  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT HIS A  606  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT HIS A  607  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT HIS A  608  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT HIS A  609  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT HIS A  610  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT HIS A  611  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT MET B   -9  UNP  A0A0K8P8E           INITIATING METHIONINE          
SEQADV 6JTT MET B   -8  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ILE B   -7  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT THR B   -6  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT LEU B   -5  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ARG B   -4  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT LYS B   -3  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT LEU B   -2  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT PRO B   -1  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT LEU B    0  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA B    1  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT VAL B    2  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA B    3  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT VAL B    4  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA B    5  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA B    6  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT GLY B    7  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT VAL B    8  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT MET B    9  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT SER B   10  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA B   11  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT GLN B   12  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA B   13  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT MET B   14  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA B   15  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT MET B   16  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT LEU B  604  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT GLU B  605  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT HIS B  606  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT HIS B  607  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT HIS B  608  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT HIS B  609  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT HIS B  610  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT HIS B  611  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT MET C   -9  UNP  A0A0K8P8E           INITIATING METHIONINE          
SEQADV 6JTT MET C   -8  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ILE C   -7  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT THR C   -6  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT LEU C   -5  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ARG C   -4  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT LYS C   -3  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT LEU C   -2  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT PRO C   -1  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT LEU C    0  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA C    1  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT VAL C    2  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA C    3  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT VAL C    4  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA C    5  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA C    6  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT GLY C    7  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT VAL C    8  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT MET C    9  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT SER C   10  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA C   11  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT GLN C   12  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA C   13  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT MET C   14  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT ALA C   15  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT MET C   16  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT LEU C  604  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT GLU C  605  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT HIS C  606  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT HIS C  607  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT HIS C  608  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT HIS C  609  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT HIS C  610  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQADV 6JTT HIS C  611  UNP  A0A0K8P8E           EXPRESSION TAG                 
SEQRES   1 A  621  MET MET ILE THR LEU ARG LYS LEU PRO LEU ALA VAL ALA          
SEQRES   2 A  621  VAL ALA ALA GLY VAL MET SER ALA GLN ALA MET ALA MET          
SEQRES   3 A  621  ALA CYS ALA GLY GLY GLY SER THR PRO LEU PRO LEU PRO          
SEQRES   4 A  621  GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO PRO PRO PRO          
SEQRES   5 A  621  VAL PRO LEU ALA SER ARG ALA ALA CYS GLU ALA LEU LYS          
SEQRES   6 A  621  ASP GLY ASN GLY ASP MET VAL TRP PRO ASN ALA ALA THR          
SEQRES   7 A  621  VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA ALA PRO ALA          
SEQRES   8 A  621  THR ALA SER ALA ALA ALA LEU PRO GLU HIS CYS GLU VAL          
SEQRES   9 A  621  SER GLY ALA ILE ALA LYS ARG THR GLY ILE ASP GLY TYR          
SEQRES  10 A  621  PRO TYR GLU ILE LYS PHE ARG LEU ARG MET PRO ALA GLU          
SEQRES  11 A  621  TRP ASN GLY ARG PHE PHE MET GLU GLY GLY SER GLY THR          
SEQRES  12 A  621  ASN GLY SER LEU SER ALA ALA THR GLY SER ILE GLY GLY          
SEQRES  13 A  621  GLY GLN ILE ALA SER ALA LEU SER ARG ASN PHE ALA THR          
SEQRES  14 A  621  ILE ALA THR ASP GLY GLY HIS ASP ASN ALA VAL ASN ASP          
SEQRES  15 A  621  ASN PRO ASP ALA LEU GLY THR VAL ALA PHE GLY LEU ASP          
SEQRES  16 A  621  PRO GLN ALA ARG LEU ASP MET GLY TYR ASN SER TYR ASP          
SEQRES  17 A  621  GLN VAL THR GLN ALA GLY LYS ALA ALA VAL ALA ARG PHE          
SEQRES  18 A  621  TYR GLY ARG ALA ALA ASP LYS SER TYR PHE ILE GLY CYS          
SEQRES  19 A  621  SER GLU GLY GLY ARG GLU GLY MET MET LEU SER GLN ARG          
SEQRES  20 A  621  PHE PRO SER HIS TYR ASP GLY ILE VAL ALA GLY ALA PRO          
SEQRES  21 A  621  GLY TYR GLN LEU PRO LYS ALA GLY ILE SER GLY ALA TRP          
SEQRES  22 A  621  THR THR GLN SER LEU ALA PRO ALA ALA VAL GLY LEU ASP          
SEQRES  23 A  621  ALA GLN GLY VAL PRO LEU ILE ASN LYS SER PHE SER ASP          
SEQRES  24 A  621  ALA ASP LEU HIS LEU LEU SER GLN ALA ILE LEU GLY THR          
SEQRES  25 A  621  CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY ILE VAL ASP          
SEQRES  26 A  621  ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP PRO ALA THR          
SEQRES  27 A  621  ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU GLN CYS VAL          
SEQRES  28 A  621  GLY ALA LYS THR ALA ASP CYS LEU SER PRO VAL GLN VAL          
SEQRES  29 A  621  THR ALA ILE LYS ARG ALA MET ALA GLY PRO VAL ASN SER          
SEQRES  30 A  621  ALA GLY THR PRO LEU TYR ASN ARG TRP ALA TRP ASP ALA          
SEQRES  31 A  621  GLY MET SER GLY LEU SER GLY THR THR TYR ASN GLN GLY          
SEQRES  32 A  621  TRP ARG SER TRP TRP LEU GLY SER PHE ASN SER SER ALA          
SEQRES  33 A  621  ASN ASN ALA GLN ARG VAL SER GLY PHE SER ALA ARG SER          
SEQRES  34 A  621  TRP LEU VAL ASP PHE ALA THR PRO PRO GLU PRO MET PRO          
SEQRES  35 A  621  MET THR GLN VAL ALA ALA ARG MET MET LYS PHE ASP PHE          
SEQRES  36 A  621  ASP ILE ASP PRO LEU LYS ILE TRP ALA THR SER GLY GLN          
SEQRES  37 A  621  PHE THR GLN SER SER MET ASP TRP HIS GLY ALA THR SER          
SEQRES  38 A  621  THR ASP LEU ALA ALA PHE ARG ASP ARG GLY GLY LYS MET          
SEQRES  39 A  621  ILE LEU TYR HIS GLY MET SER ASP ALA ALA PHE SER ALA          
SEQRES  40 A  621  LEU ASP THR ALA ASP TYR TYR GLU ARG LEU GLY ALA ALA          
SEQRES  41 A  621  MET PRO GLY ALA ALA GLY PHE ALA ARG LEU PHE LEU VAL          
SEQRES  42 A  621  PRO GLY MET ASN HIS CYS SER GLY GLY PRO GLY THR ASP          
SEQRES  43 A  621  ARG PHE ASP MET LEU THR PRO LEU VAL ALA TRP VAL GLU          
SEQRES  44 A  621  ARG GLY GLU ALA PRO ASP GLN ILE SER ALA TRP SER GLY          
SEQRES  45 A  621  THR PRO GLY TYR PHE GLY VAL ALA ALA ARG THR ARG PRO          
SEQRES  46 A  621  LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR LYS GLY SER          
SEQRES  47 A  621  GLY ASP ILE ASN THR GLU ALA ASN PHE ALA CYS ALA ALA          
SEQRES  48 A  621  PRO PRO LEU GLU HIS HIS HIS HIS HIS HIS                      
SEQRES   1 B  621  MET MET ILE THR LEU ARG LYS LEU PRO LEU ALA VAL ALA          
SEQRES   2 B  621  VAL ALA ALA GLY VAL MET SER ALA GLN ALA MET ALA MET          
SEQRES   3 B  621  ALA CYS ALA GLY GLY GLY SER THR PRO LEU PRO LEU PRO          
SEQRES   4 B  621  GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO PRO PRO PRO          
SEQRES   5 B  621  VAL PRO LEU ALA SER ARG ALA ALA CYS GLU ALA LEU LYS          
SEQRES   6 B  621  ASP GLY ASN GLY ASP MET VAL TRP PRO ASN ALA ALA THR          
SEQRES   7 B  621  VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA ALA PRO ALA          
SEQRES   8 B  621  THR ALA SER ALA ALA ALA LEU PRO GLU HIS CYS GLU VAL          
SEQRES   9 B  621  SER GLY ALA ILE ALA LYS ARG THR GLY ILE ASP GLY TYR          
SEQRES  10 B  621  PRO TYR GLU ILE LYS PHE ARG LEU ARG MET PRO ALA GLU          
SEQRES  11 B  621  TRP ASN GLY ARG PHE PHE MET GLU GLY GLY SER GLY THR          
SEQRES  12 B  621  ASN GLY SER LEU SER ALA ALA THR GLY SER ILE GLY GLY          
SEQRES  13 B  621  GLY GLN ILE ALA SER ALA LEU SER ARG ASN PHE ALA THR          
SEQRES  14 B  621  ILE ALA THR ASP GLY GLY HIS ASP ASN ALA VAL ASN ASP          
SEQRES  15 B  621  ASN PRO ASP ALA LEU GLY THR VAL ALA PHE GLY LEU ASP          
SEQRES  16 B  621  PRO GLN ALA ARG LEU ASP MET GLY TYR ASN SER TYR ASP          
SEQRES  17 B  621  GLN VAL THR GLN ALA GLY LYS ALA ALA VAL ALA ARG PHE          
SEQRES  18 B  621  TYR GLY ARG ALA ALA ASP LYS SER TYR PHE ILE GLY CYS          
SEQRES  19 B  621  SER GLU GLY GLY ARG GLU GLY MET MET LEU SER GLN ARG          
SEQRES  20 B  621  PHE PRO SER HIS TYR ASP GLY ILE VAL ALA GLY ALA PRO          
SEQRES  21 B  621  GLY TYR GLN LEU PRO LYS ALA GLY ILE SER GLY ALA TRP          
SEQRES  22 B  621  THR THR GLN SER LEU ALA PRO ALA ALA VAL GLY LEU ASP          
SEQRES  23 B  621  ALA GLN GLY VAL PRO LEU ILE ASN LYS SER PHE SER ASP          
SEQRES  24 B  621  ALA ASP LEU HIS LEU LEU SER GLN ALA ILE LEU GLY THR          
SEQRES  25 B  621  CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY ILE VAL ASP          
SEQRES  26 B  621  ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP PRO ALA THR          
SEQRES  27 B  621  ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU GLN CYS VAL          
SEQRES  28 B  621  GLY ALA LYS THR ALA ASP CYS LEU SER PRO VAL GLN VAL          
SEQRES  29 B  621  THR ALA ILE LYS ARG ALA MET ALA GLY PRO VAL ASN SER          
SEQRES  30 B  621  ALA GLY THR PRO LEU TYR ASN ARG TRP ALA TRP ASP ALA          
SEQRES  31 B  621  GLY MET SER GLY LEU SER GLY THR THR TYR ASN GLN GLY          
SEQRES  32 B  621  TRP ARG SER TRP TRP LEU GLY SER PHE ASN SER SER ALA          
SEQRES  33 B  621  ASN ASN ALA GLN ARG VAL SER GLY PHE SER ALA ARG SER          
SEQRES  34 B  621  TRP LEU VAL ASP PHE ALA THR PRO PRO GLU PRO MET PRO          
SEQRES  35 B  621  MET THR GLN VAL ALA ALA ARG MET MET LYS PHE ASP PHE          
SEQRES  36 B  621  ASP ILE ASP PRO LEU LYS ILE TRP ALA THR SER GLY GLN          
SEQRES  37 B  621  PHE THR GLN SER SER MET ASP TRP HIS GLY ALA THR SER          
SEQRES  38 B  621  THR ASP LEU ALA ALA PHE ARG ASP ARG GLY GLY LYS MET          
SEQRES  39 B  621  ILE LEU TYR HIS GLY MET SER ASP ALA ALA PHE SER ALA          
SEQRES  40 B  621  LEU ASP THR ALA ASP TYR TYR GLU ARG LEU GLY ALA ALA          
SEQRES  41 B  621  MET PRO GLY ALA ALA GLY PHE ALA ARG LEU PHE LEU VAL          
SEQRES  42 B  621  PRO GLY MET ASN HIS CYS SER GLY GLY PRO GLY THR ASP          
SEQRES  43 B  621  ARG PHE ASP MET LEU THR PRO LEU VAL ALA TRP VAL GLU          
SEQRES  44 B  621  ARG GLY GLU ALA PRO ASP GLN ILE SER ALA TRP SER GLY          
SEQRES  45 B  621  THR PRO GLY TYR PHE GLY VAL ALA ALA ARG THR ARG PRO          
SEQRES  46 B  621  LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR LYS GLY SER          
SEQRES  47 B  621  GLY ASP ILE ASN THR GLU ALA ASN PHE ALA CYS ALA ALA          
SEQRES  48 B  621  PRO PRO LEU GLU HIS HIS HIS HIS HIS HIS                      
SEQRES   1 C  621  MET MET ILE THR LEU ARG LYS LEU PRO LEU ALA VAL ALA          
SEQRES   2 C  621  VAL ALA ALA GLY VAL MET SER ALA GLN ALA MET ALA MET          
SEQRES   3 C  621  ALA CYS ALA GLY GLY GLY SER THR PRO LEU PRO LEU PRO          
SEQRES   4 C  621  GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO PRO PRO PRO          
SEQRES   5 C  621  VAL PRO LEU ALA SER ARG ALA ALA CYS GLU ALA LEU LYS          
SEQRES   6 C  621  ASP GLY ASN GLY ASP MET VAL TRP PRO ASN ALA ALA THR          
SEQRES   7 C  621  VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA ALA PRO ALA          
SEQRES   8 C  621  THR ALA SER ALA ALA ALA LEU PRO GLU HIS CYS GLU VAL          
SEQRES   9 C  621  SER GLY ALA ILE ALA LYS ARG THR GLY ILE ASP GLY TYR          
SEQRES  10 C  621  PRO TYR GLU ILE LYS PHE ARG LEU ARG MET PRO ALA GLU          
SEQRES  11 C  621  TRP ASN GLY ARG PHE PHE MET GLU GLY GLY SER GLY THR          
SEQRES  12 C  621  ASN GLY SER LEU SER ALA ALA THR GLY SER ILE GLY GLY          
SEQRES  13 C  621  GLY GLN ILE ALA SER ALA LEU SER ARG ASN PHE ALA THR          
SEQRES  14 C  621  ILE ALA THR ASP GLY GLY HIS ASP ASN ALA VAL ASN ASP          
SEQRES  15 C  621  ASN PRO ASP ALA LEU GLY THR VAL ALA PHE GLY LEU ASP          
SEQRES  16 C  621  PRO GLN ALA ARG LEU ASP MET GLY TYR ASN SER TYR ASP          
SEQRES  17 C  621  GLN VAL THR GLN ALA GLY LYS ALA ALA VAL ALA ARG PHE          
SEQRES  18 C  621  TYR GLY ARG ALA ALA ASP LYS SER TYR PHE ILE GLY CYS          
SEQRES  19 C  621  SER GLU GLY GLY ARG GLU GLY MET MET LEU SER GLN ARG          
SEQRES  20 C  621  PHE PRO SER HIS TYR ASP GLY ILE VAL ALA GLY ALA PRO          
SEQRES  21 C  621  GLY TYR GLN LEU PRO LYS ALA GLY ILE SER GLY ALA TRP          
SEQRES  22 C  621  THR THR GLN SER LEU ALA PRO ALA ALA VAL GLY LEU ASP          
SEQRES  23 C  621  ALA GLN GLY VAL PRO LEU ILE ASN LYS SER PHE SER ASP          
SEQRES  24 C  621  ALA ASP LEU HIS LEU LEU SER GLN ALA ILE LEU GLY THR          
SEQRES  25 C  621  CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY ILE VAL ASP          
SEQRES  26 C  621  ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP PRO ALA THR          
SEQRES  27 C  621  ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU GLN CYS VAL          
SEQRES  28 C  621  GLY ALA LYS THR ALA ASP CYS LEU SER PRO VAL GLN VAL          
SEQRES  29 C  621  THR ALA ILE LYS ARG ALA MET ALA GLY PRO VAL ASN SER          
SEQRES  30 C  621  ALA GLY THR PRO LEU TYR ASN ARG TRP ALA TRP ASP ALA          
SEQRES  31 C  621  GLY MET SER GLY LEU SER GLY THR THR TYR ASN GLN GLY          
SEQRES  32 C  621  TRP ARG SER TRP TRP LEU GLY SER PHE ASN SER SER ALA          
SEQRES  33 C  621  ASN ASN ALA GLN ARG VAL SER GLY PHE SER ALA ARG SER          
SEQRES  34 C  621  TRP LEU VAL ASP PHE ALA THR PRO PRO GLU PRO MET PRO          
SEQRES  35 C  621  MET THR GLN VAL ALA ALA ARG MET MET LYS PHE ASP PHE          
SEQRES  36 C  621  ASP ILE ASP PRO LEU LYS ILE TRP ALA THR SER GLY GLN          
SEQRES  37 C  621  PHE THR GLN SER SER MET ASP TRP HIS GLY ALA THR SER          
SEQRES  38 C  621  THR ASP LEU ALA ALA PHE ARG ASP ARG GLY GLY LYS MET          
SEQRES  39 C  621  ILE LEU TYR HIS GLY MET SER ASP ALA ALA PHE SER ALA          
SEQRES  40 C  621  LEU ASP THR ALA ASP TYR TYR GLU ARG LEU GLY ALA ALA          
SEQRES  41 C  621  MET PRO GLY ALA ALA GLY PHE ALA ARG LEU PHE LEU VAL          
SEQRES  42 C  621  PRO GLY MET ASN HIS CYS SER GLY GLY PRO GLY THR ASP          
SEQRES  43 C  621  ARG PHE ASP MET LEU THR PRO LEU VAL ALA TRP VAL GLU          
SEQRES  44 C  621  ARG GLY GLU ALA PRO ASP GLN ILE SER ALA TRP SER GLY          
SEQRES  45 C  621  THR PRO GLY TYR PHE GLY VAL ALA ALA ARG THR ARG PRO          
SEQRES  46 C  621  LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR LYS GLY SER          
SEQRES  47 C  621  GLY ASP ILE ASN THR GLU ALA ASN PHE ALA CYS ALA ALA          
SEQRES  48 C  621  PRO PRO LEU GLU HIS HIS HIS HIS HIS HIS                      
HET    C9C  A 701      14                                                       
HET     CA  A 702       1                                                       
HET    C8X  B 701      18                                                       
HET     CA  B 702       1                                                       
HET    C9C  C 701      14                                                       
HET     CA  C 702       1                                                       
HETNAM     C9C 4-(2-HYDROXYETHYLOXYCARBONYL)BENZOIC ACID                        
HETNAM      CA CALCIUM ION                                                      
HETNAM     C8X BIS(2-HYDROXYETHYL) BENZENE-1,4-DICARBOXYLATE                    
HETSYN     C9C MONOHYDROXYETHYL TEREPHTHALATE                                   
HETSYN     C8X BIS(2-HYDROXYETHYL) TEREPHTHALATE                                
FORMUL   4  C9C    2(C10 H10 O5)                                                
FORMUL   5   CA    3(CA 2+)                                                     
FORMUL   6  C8X    C12 H14 O6                                                   
FORMUL  10  HOH   *500(H2 O)                                                    
HELIX    1 AA1 SER A   47  ALA A   53  1                                   7    
HELIX    2 AA2 ALA A  152  ASN A  156  5                                   5    
HELIX    3 AA3 LEU A  177  LEU A  184  5                                   8    
HELIX    4 AA4 ASP A  185  TYR A  194  1                                  10    
HELIX    5 AA5 TYR A  194  GLY A  213  1                                  20    
HELIX    6 AA6 SER A  225  PHE A  238  1                                  14    
HELIX    7 AA7 GLN A  253  PRO A  255  5                                   3    
HELIX    8 AA8 LYS A  256  ALA A  269  1                                  14    
HELIX    9 AA9 PRO A  270  ALA A  272  5                                   3    
HELIX   10 AB1 LEU A  282  PHE A  287  5                                   6    
HELIX   11 AB2 SER A  288  ASP A  304  1                                  17    
HELIX   12 AB3 ALA A  305  GLY A  308  5                                   4    
HELIX   13 AB4 ASN A  316  PHE A  324  1                                   9    
HELIX   14 AB5 SER A  350  GLY A  363  1                                  14    
HELIX   15 AB6 ASP A  379  SER A  383  5                                   5    
HELIX   16 AB7 GLY A  414  PHE A  424  1                                  11    
HELIX   17 AB8 PRO A  432  THR A  434  5                                   3    
HELIX   18 AB9 GLN A  435  LYS A  442  1                                   8    
HELIX   19 AC1 ILE A  447  TRP A  453  5                                   7    
HELIX   20 AC2 SER A  462  HIS A  467  1                                   6    
HELIX   21 AC3 LEU A  474  ARG A  480  1                                   7    
HELIX   22 AC4 SER A  496  MET A  511  1                                  16    
HELIX   23 AC5 GLY A  513  GLY A  516  5                                   4    
HELIX   24 AC6 MET A  540  GLY A  551  1                                  12    
HELIX   25 AC7 THR A  563  GLY A  568  5                                   6    
HELIX   26 AC8 THR A  593  ALA A  595  5                                   3    
HELIX   27 AC9 SER B   47  ALA B   53  1                                   7    
HELIX   28 AD1 LEU B  177  LEU B  184  5                                   8    
HELIX   29 AD2 ASP B  185  TYR B  194  1                                  10    
HELIX   30 AD3 TYR B  194  GLY B  213  1                                  20    
HELIX   31 AD4 SER B  225  PHE B  238  1                                  14    
HELIX   32 AD5 GLN B  253  PRO B  255  5                                   3    
HELIX   33 AD6 LYS B  256  ALA B  269  1                                  14    
HELIX   34 AD7 PRO B  270  ALA B  272  5                                   3    
HELIX   35 AD8 LEU B  282  SER B  286  5                                   5    
HELIX   36 AD9 SER B  288  ASP B  304  1                                  17    
HELIX   37 AE1 ALA B  305  GLY B  308  5                                   4    
HELIX   38 AE2 ASN B  316  PHE B  324  1                                   9    
HELIX   39 AE3 SER B  350  GLY B  363  1                                  14    
HELIX   40 AE4 ASP B  379  SER B  383  5                                   5    
HELIX   41 AE5 GLY B  414  PHE B  424  1                                  11    
HELIX   42 AE6 PRO B  432  THR B  434  5                                   3    
HELIX   43 AE7 GLN B  435  PHE B  443  1                                   9    
HELIX   44 AE8 ILE B  447  TRP B  453  5                                   7    
HELIX   45 AE9 SER B  462  HIS B  467  1                                   6    
HELIX   46 AF1 LEU B  474  ARG B  480  1                                   7    
HELIX   47 AF2 SER B  496  MET B  511  1                                  16    
HELIX   48 AF3 GLY B  513  GLY B  516  5                                   4    
HELIX   49 AF4 MET B  540  GLY B  551  1                                  12    
HELIX   50 AF5 THR B  563  GLY B  568  5                                   6    
HELIX   51 AF6 THR B  593  ALA B  595  5                                   3    
HELIX   52 AF7 SER C   47  ALA C   53  1                                   7    
HELIX   53 AF8 LEU C  177  LEU C  184  5                                   8    
HELIX   54 AF9 ASP C  185  TYR C  194  1                                  10    
HELIX   55 AG1 TYR C  194  GLY C  213  1                                  20    
HELIX   56 AG2 SER C  225  PHE C  238  1                                  14    
HELIX   57 AG3 GLN C  253  PRO C  255  5                                   3    
HELIX   58 AG4 LYS C  256  ALA C  269  1                                  14    
HELIX   59 AG5 PRO C  270  ALA C  272  5                                   3    
HELIX   60 AG6 LEU C  282  PHE C  287  5                                   6    
HELIX   61 AG7 SER C  288  ASP C  304  1                                  17    
HELIX   62 AG8 ALA C  305  GLY C  308  5                                   4    
HELIX   63 AG9 ASN C  316  PHE C  324  1                                   9    
HELIX   64 AH1 SER C  350  GLY C  363  1                                  14    
HELIX   65 AH2 ASP C  379  SER C  383  5                                   5    
HELIX   66 AH3 GLY C  414  PHE C  424  1                                  11    
HELIX   67 AH4 PRO C  432  THR C  434  5                                   3    
HELIX   68 AH5 GLN C  435  LYS C  442  1                                   8    
HELIX   69 AH6 ILE C  447  TRP C  453  5                                   7    
HELIX   70 AH7 SER C  462  HIS C  467  1                                   6    
HELIX   71 AH8 LEU C  474  ARG C  480  1                                   7    
HELIX   72 AH9 SER C  496  MET C  511  1                                  16    
HELIX   73 AI1 GLY C  513  GLY C  516  5                                   4    
HELIX   74 AI2 MET C  540  GLY C  551  1                                  12    
HELIX   75 AI3 THR C  563  GLY C  568  5                                   6    
HELIX   76 AI4 THR C  593  ALA C  595  5                                   3    
SHEET    1 AA1 9 THR A  68  ARG A  76  0                                        
SHEET    2 AA1 9 HIS A  91  THR A 102 -1  O  GLU A  93   N  ALA A  74           
SHEET    3 AA1 9 PRO A 108  PRO A 118 -1  O  LEU A 115   N  VAL A  94           
SHEET    4 AA1 9 ALA A 158  THR A 162 -1  O  THR A 159   N  ARG A 116           
SHEET    5 AA1 9 ARG A 124  GLU A 128  1  N  ARG A 124   O  ALA A 158           
SHEET    6 AA1 9 LYS A 218  CYS A 224  1  O  TYR A 220   N  MET A 127           
SHEET    7 AA1 9 GLY A 244  GLY A 248  1  O  GLY A 244   N  PHE A 221           
SHEET    8 AA1 9 LYS A 483  GLY A 489  1  O  ILE A 485   N  ALA A 247           
SHEET    9 AA1 9 ALA A 518  VAL A 523  1  O  VAL A 523   N  HIS A 488           
SHEET    1 AA2 2 LEU A 385  SER A 386  0                                        
SHEET    2 AA2 2 THR A 389  TYR A 390 -1  O  THR A 389   N  SER A 386           
SHEET    1 AA3 2 ILE A 557  TRP A 560  0                                        
SHEET    2 AA3 2 THR A 573  LEU A 576 -1  O  LEU A 576   N  ILE A 557           
SHEET    1 AA4 2 ILE A 582  TYR A 585  0                                        
SHEET    2 AA4 2 PHE A 597  ALA A 600 -1  O  ALA A 598   N  ARG A 584           
SHEET    1 AA5 9 THR B  68  ARG B  76  0                                        
SHEET    2 AA5 9 HIS B  91  THR B 102 -1  O  GLU B  93   N  ALA B  74           
SHEET    3 AA5 9 PRO B 108  PRO B 118 -1  O  LEU B 115   N  VAL B  94           
SHEET    4 AA5 9 ALA B 158  THR B 162 -1  O  THR B 159   N  ARG B 116           
SHEET    5 AA5 9 ARG B 124  GLU B 128  1  N  ARG B 124   O  ALA B 158           
SHEET    6 AA5 9 LYS B 218  CYS B 224  1  O  TYR B 220   N  PHE B 125           
SHEET    7 AA5 9 GLY B 244  GLY B 248  1  O  GLY B 248   N  GLY B 223           
SHEET    8 AA5 9 LYS B 483  GLY B 489  1  O  ILE B 485   N  ILE B 245           
SHEET    9 AA5 9 ALA B 518  VAL B 523  1  O  ARG B 519   N  LEU B 486           
SHEET    1 AA6 2 LEU B 385  SER B 386  0                                        
SHEET    2 AA6 2 THR B 389  TYR B 390 -1  O  THR B 389   N  SER B 386           
SHEET    1 AA7 2 ILE B 557  TRP B 560  0                                        
SHEET    2 AA7 2 THR B 573  LEU B 576 -1  O  LEU B 576   N  ILE B 557           
SHEET    1 AA8 2 ILE B 582  TYR B 585  0                                        
SHEET    2 AA8 2 PHE B 597  ALA B 600 -1  O  ALA B 600   N  ILE B 582           
SHEET    1 AA9 9 THR C  68  ARG C  76  0                                        
SHEET    2 AA9 9 HIS C  91  THR C 102 -1  O  GLU C  93   N  ALA C  74           
SHEET    3 AA9 9 PRO C 108  PRO C 118 -1  O  LEU C 115   N  VAL C  94           
SHEET    4 AA9 9 ALA C 158  THR C 162 -1  O  THR C 159   N  ARG C 116           
SHEET    5 AA9 9 ARG C 124  GLU C 128  1  N  PHE C 126   O  ALA C 158           
SHEET    6 AA9 9 LYS C 218  CYS C 224  1  O  TYR C 220   N  PHE C 125           
SHEET    7 AA9 9 GLY C 244  GLY C 248  1  O  GLY C 248   N  GLY C 223           
SHEET    8 AA9 9 LYS C 483  GLY C 489  1  O  ILE C 485   N  ILE C 245           
SHEET    9 AA9 9 ALA C 518  VAL C 523  1  O  ARG C 519   N  LEU C 486           
SHEET    1 AB1 2 LEU C 385  SER C 386  0                                        
SHEET    2 AB1 2 THR C 389  TYR C 390 -1  O  THR C 389   N  SER C 386           
SHEET    1 AB2 2 ILE C 557  TRP C 560  0                                        
SHEET    2 AB2 2 THR C 573  LEU C 576 -1  O  LEU C 576   N  ILE C 557           
SHEET    1 AB3 2 ILE C 582  TYR C 585  0                                        
SHEET    2 AB3 2 PHE C 597  ALA C 600 -1  O  ALA C 600   N  ILE C 582           
SSBOND   1 CYS A   51    CYS A   92                          1555   1555  2.04  
SSBOND   2 CYS A  224    CYS A  529                          1555   1555  2.06  
SSBOND   3 CYS A  303    CYS A  320                          1555   1555  2.12  
SSBOND   4 CYS A  340    CYS A  348                          1555   1555  2.07  
SSBOND   5 CYS A  577    CYS A  599                          1555   1555  2.01  
SSBOND   6 CYS B   51    CYS B   92                          1555   1555  2.16  
SSBOND   7 CYS B  224    CYS B  529                          1555   1555  2.09  
SSBOND   8 CYS B  303    CYS B  320                          1555   1555  2.07  
SSBOND   9 CYS B  340    CYS B  348                          1555   1555  1.84  
SSBOND  10 CYS B  577    CYS B  599                          1555   1555  2.02  
SSBOND  11 CYS C   51    CYS C   92                          1555   1555  2.16  
SSBOND  12 CYS C  224    CYS C  529                          1555   1555  2.08  
SSBOND  13 CYS C  303    CYS C  320                          1555   1555  2.09  
SSBOND  14 CYS C  340    CYS C  348                          1555   1555  2.06  
SSBOND  15 CYS C  577    CYS C  599                          1555   1555  2.02  
LINK         O   ASP A 304                CA    CA A 702     1555   1555  2.35  
LINK         OD1 ASP A 304                CA    CA A 702     1555   1555  2.31  
LINK         OD1 ASP A 307                CA    CA A 702     1555   1555  2.88  
LINK         OD2 ASP A 307                CA    CA A 702     1555   1555  2.32  
LINK         O   LEU A 309                CA    CA A 702     1555   1555  2.33  
LINK         OD1 ASP A 311                CA    CA A 702     1555   1555  2.35  
LINK         O   ILE A 313                CA    CA A 702     1555   1555  2.32  
LINK         O   ASP B 304                CA    CA B 702     1555   1555  2.36  
LINK         OD1 ASP B 304                CA    CA B 702     1555   1555  2.27  
LINK         OD1 ASP B 307                CA    CA B 702     1555   1555  2.21  
LINK         O   LEU B 309                CA    CA B 702     1555   1555  2.31  
LINK         OD1 ASP B 311                CA    CA B 702     1555   1555  2.33  
LINK         O   ILE B 313                CA    CA B 702     1555   1555  2.31  
LINK         O   ASP C 304                CA    CA C 702     1555   1555  2.32  
LINK         OD2 ASP C 304                CA    CA C 702     1555   1555  2.33  
LINK         OD1 ASP C 307                CA    CA C 702     1555   1555  2.36  
LINK         OD2 ASP C 307                CA    CA C 702     1555   1555  2.92  
LINK         O   LEU C 309                CA    CA C 702     1555   1555  2.31  
LINK         OD1 ASP C 311                CA    CA C 702     1555   1555  2.38  
LINK         O   ILE C 313                CA    CA C 702     1555   1555  2.32  
CISPEP   1 THR A  426    PRO A  427          0        -8.73                     
CISPEP   2 TYR A  579    PRO A  580          0         4.81                     
CISPEP   3 THR B  426    PRO B  427          0        -4.16                     
CISPEP   4 TYR B  579    PRO B  580          0         0.41                     
CISPEP   5 THR C  426    PRO C  427          0        -9.25                     
CISPEP   6 TYR C  579    PRO C  580          0        -0.94                     
SITE     1 AC1 13 GLY A 132  SER A 225  GLU A 226  LEU A 254                    
SITE     2 AC1 13 ALA A 257  GLY A 258  TRP A 397  ARG A 411                    
SITE     3 AC1 13 PHE A 415  SER A 416  PHE A 424  PHE A 495                    
SITE     4 AC1 13 HIS A 528                                                     
SITE     1 AC2  6 ASP A 304  ASP A 307  LEU A 309  ASP A 311                    
SITE     2 AC2  6 ILE A 313  HOH A 801                                          
SITE     1 AC3 15 GLY B 132  SER B 225  GLU B 226  LEU B 254                    
SITE     2 AC3 15 ALA B 257  GLY B 258  TRP B 397  ARG B 411                    
SITE     3 AC3 15 PHE B 415  SER B 416  TRP B 420  PHE B 424                    
SITE     4 AC3 15 PHE B 495  HIS B 528  HOH B 910                               
SITE     1 AC4  6 ASP B 304  ASP B 307  LEU B 309  ASP B 311                    
SITE     2 AC4  6 ILE B 313  HOH B 801                                          
SITE     1 AC5  6 ASP C 304  ASP C 307  LEU C 309  ASP C 311                    
SITE     2 AC5  6 ILE C 313  HOH C 809                                          
SITE     1 AC6 23 GLY C 132  CYS C 224  GLU C 226  GLY C 227                    
SITE     2 AC6 23 GLY C 228  ARG C 229  GLY C 248  ALA C 249                    
SITE     3 AC6 23 PRO C 250  GLY C 251  LEU C 254  ALA C 257                    
SITE     4 AC6 23 GLY C 258  TRP C 397  ARG C 411  PHE C 415                    
SITE     5 AC6 23 SER C 416  TRP C 420  PHE C 424  PHE C 495                    
SITE     6 AC6 23 HIS C 528  CYS C 529  HOH C 901                               
CRYST1  215.259  173.799  106.671  90.00 119.51  90.00 C 1 2 1      12          
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      0.004646  0.000000  0.002629        0.00000                         
SCALE2      0.000000  0.005754  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010772        0.00000                         
TER    4144      PRO A 603                                                      
TER    8277      LEU B 604                                                      
TER   12405      PRO C 603                                                      
MASTER      624    0    6   76   45    0   20    612918    3  102  144          
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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