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LongText Report for: 5ie6-pdb

Name Class
5ie6-pdb
HEADER    HYDROLASE                               25-FEB-16   5IE6              
TITLE     CRYSTAL STRUCTURE OF A LACTONASE MUTANT IN COMPLEX WITH SUBSTRATE B   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ZEARALENONE HYDROLASE;                                     
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: LACTONASE;                                                  
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLONOSTACHYS ROSEA;                             
SOURCE   3 ORGANISM_TAXID: 29856;                                               
SOURCE   4 GENE: ZHD101;                                                        
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: PET-46 EK/LIC                             
KEYWDS    ALPHA/BETA-HYDROLASE, LACTONASE, ZEARALENONE, HYDROLASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.Y.ZHENG,Z.X.XU,W.D.LIU,C.C.CHEN,R.T.GUO                             
REVDAT   1   04-JAN-17 5IE6    0                                                
JRNL        AUTH   Z.X.XU,W.D.LIU,C.C.CHEN,Q.LI,J.W.HUANG,T.P.KO,G.LIU,W.LIU,   
JRNL        AUTH 2 W.PENG,Y.S.CHENG,Y.CHEN,J.JIN,H.LI,Y.Y.ZHENG,R.T.GUO         
JRNL        TITL   ENHANCED ALPH-ZEARALENOL HYDROLYZING ACTIVITY OF A           
JRNL        TITL 2 MYCOESTROGEN-DETOXIFYING LACTONASE BY STRUCTURE-BASED        
JRNL        TITL 3 ENGINEERING                                                  
JRNL        REF    ACS CATALYSIS                 V.   6  7657 2016              
JRNL        REFN                   ESSN 2155-5435                               
JRNL        DOI    10.1021/ACSCATAL.6B01826                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.67 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.67                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 28626                          
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) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1516                            
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) : 2.67                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2017                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.39                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2440                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 114                          
REMARK   3   BIN FREE R VALUE                    : 0.2800                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5028                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 46                                      
REMARK   3   SOLVENT ATOMS            : 228                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.59                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.19000                                              
REMARK   3    B22 (A**2) : 2.19000                                              
REMARK   3    B33 (A**2) : -7.11000                                             
REMARK   3    B12 (A**2) : 1.10000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.511         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.329         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.214         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.514        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.887                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5202 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4881 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7101 ; 1.529 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11269 ; 0.969 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   644 ; 8.934 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   206 ;37.330 ;24.029       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   798 ;19.765 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;17.869 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   811 ; 0.106 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5778 ; 0.019 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1110 ; 0.009 ; 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):  2609 ; 4.463 ; 4.248       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2608 ; 4.463 ; 4.247       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3242 ; 6.328 ; 6.347       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3243 ; 6.327 ; 6.347       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2593 ; 4.852 ; 4.607       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2593 ; 4.848 ; 4.607       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3860 ; 6.974 ; 6.771       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6024 ; 8.971 ;34.895       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5988 ; 8.970 ;34.763       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     1    264       B     1    264   30536  0.10  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
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                                                           
REMARK   4                                                                      
REMARK   4 5IE6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000218713.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-SEP-15                          
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               : NSRRC                              
REMARK 200  BEAMLINE                       : BL13B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97622                            
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30272                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.670                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : 0.04500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.67                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.77                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3WZL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG 2000 MME, 0.1M BIS-TRIS, PH      
REMARK 280  6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      156.70367            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      313.40733            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      235.05550            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      391.75917            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       78.35183            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      156.70367            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      313.40733            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      391.75917            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      235.05550            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       78.35183            
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
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 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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 C     1                                                      
REMARK 465     ARG C     2                                                      
REMARK 465     THR C     3                                                      
REMARK 465     ARG C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     THR C     6                                                      
REMARK 465     ILE C     7                                                      
REMARK 465     SER C     8                                                      
REMARK 465     THR C     9                                                      
REMARK 465     PRO C    10                                                      
REMARK 465     ASN C    11                                                      
REMARK 465     GLY C    12                                                      
REMARK 465     ILE C    13                                                      
REMARK 465     THR C    14                                                      
REMARK 465     ASP C    31                                                      
REMARK 465     GLY C    32                                                      
REMARK 465     LEU C    33                                                      
REMARK 465     GLY C    34                                                      
REMARK 465     GLU C    35                                                      
REMARK 465     CYS C    36                                                      
REMARK 465     GLN C    37                                                      
REMARK 465     MET C    38                                                      
REMARK 465     PHE C    39                                                      
REMARK 465     ASP C    40                                                      
REMARK 465     SER C    41                                                      
REMARK 465     SER C    42                                                      
REMARK 465     VAL C    43                                                      
REMARK 465     SER C    44                                                      
REMARK 465     GLN C    45                                                      
REMARK 465     ILE C    46                                                      
REMARK 465     ALA C    47                                                      
REMARK 465     ALA C    48                                                      
REMARK 465     GLN C    49                                                      
REMARK 465     GLY C    50                                                      
REMARK 465     PHE C    51                                                      
REMARK 465     THR C    54                                                      
REMARK 465     THR C    55                                                      
REMARK 465     PHE C    56                                                      
REMARK 465     ASP C    57                                                      
REMARK 465     ARG C    63                                                      
REMARK 465     SER C    64                                                      
REMARK 465     ALA C    65                                                      
REMARK 465     LYS C    66                                                      
REMARK 465     GLN C    78                                                      
REMARK 465     LYS C    79                                                      
REMARK 465     LEU C    80                                                      
REMARK 465     ALA C    81                                                      
REMARK 465     GLU C   126                                                      
REMARK 465     LEU C   127                                                      
REMARK 465     PRO C   128                                                      
REMARK 465     THR C   129                                                      
REMARK 465     LYS C   130                                                      
REMARK 465     LEU C   131                                                      
REMARK 465     LEU C   132                                                      
REMARK 465     ASP C   133                                                      
REMARK 465     HIS C   134                                                      
REMARK 465     LEU C   135                                                      
REMARK 465     SER C   136                                                      
REMARK 465     ASN C   137                                                      
REMARK 465     THR C   138                                                      
REMARK 465     ALA C   139                                                      
REMARK 465     VAL C   140                                                      
REMARK 465     LEU C   141                                                      
REMARK 465     GLU C   142                                                      
REMARK 465     ASP C   143                                                      
REMARK 465     GLU C   144                                                      
REMARK 465     GLU C   145                                                      
REMARK 465     ILE C   146                                                      
REMARK 465     SER C   147                                                      
REMARK 465     LYS C   148                                                      
REMARK 465     ILE C   149                                                      
REMARK 465     LEU C   150                                                      
REMARK 465     ALA C   151                                                      
REMARK 465     ASN C   152                                                      
REMARK 465     VAL C   153                                                      
REMARK 465     MET C   154                                                      
REMARK 465     LEU C   155                                                      
REMARK 465     ASN C   156                                                      
REMARK 465     ASP C   157                                                      
REMARK 465     VAL C   158                                                      
REMARK 465     SER C   159                                                      
REMARK 465     GLY C   160                                                      
REMARK 465     GLY C   161                                                      
REMARK 465     SER C   162                                                      
REMARK 465     GLU C   163                                                      
REMARK 465     ALA C   164                                                      
REMARK 465     TRP C   165                                                      
REMARK 465     GLN C   166                                                      
REMARK 465     ALA C   167                                                      
REMARK 465     MET C   168                                                      
REMARK 465     GLY C   169                                                      
REMARK 465     ASP C   170                                                      
REMARK 465     GLU C   171                                                      
REMARK 465     VAL C   172                                                      
REMARK 465     HIS C   173                                                      
REMARK 465     ALA C   174                                                      
REMARK 465     ARG C   175                                                      
REMARK 465     LEU C   176                                                      
REMARK 465     HIS C   177                                                      
REMARK 465     LYS C   178                                                      
REMARK 465     ASN C   179                                                      
REMARK 465     ALA C   184                                                      
REMARK 465     ARG C   185                                                      
REMARK 465     GLY C   186                                                      
REMARK 465     TYR C   187                                                      
REMARK 465     PRO C   188                                                      
REMARK 465     ARG C   189                                                      
REMARK 465     THR C   190                                                      
REMARK 465     TRP C   210                                                      
REMARK 465     THR C   211                                                      
REMARK 465     VAL C   212                                                      
REMARK 465     GLY C   213                                                      
REMARK 465     ALA C   214                                                      
REMARK 465     ALA C   215                                                      
REMARK 465     ILE C   225                                                      
REMARK 465     VAL C   226                                                      
REMARK 465     THR C   227                                                      
REMARK 465     ALA C   228                                                      
REMARK 465     THR C   229                                                      
REMARK 465     LYS C   230                                                      
REMARK 465     ALA C   231                                                      
REMARK 465     GLY C   232                                                      
REMARK 465     VAL C   233                                                      
REMARK 465     ASN C   234                                                      
REMARK 465     ILE C   235                                                      
REMARK 465     GLY C   236                                                      
REMARK 465     LEU C   237                                                      
REMARK 465     LEU C   238                                                      
REMARK 465     PRO C   239                                                      
REMARK 465     GLY C   240                                                      
REMARK 465     MET C   241                                                      
REMARK 465     HIS C   242                                                      
REMARK 465     PHE C   243                                                      
REMARK 465     PRO C   244                                                      
REMARK 465     TYR C   245                                                      
REMARK 465     VAL C   246                                                      
REMARK 465     SER C   247                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    TYR C   255     OG1  THR C   259              2.03            
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    GLN A  49   N   -  CA  -  C   ANGL. DEV. = -16.6 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    SER A  62     -126.99     41.75                                   
REMARK 500    ALA A 102     -123.05     62.41                                   
REMARK 500    GLU A 126       77.68     52.65                                   
REMARK 500    PRO A 196       43.44    -94.25                                   
REMARK 500    MET A 241     -108.91   -136.86                                   
REMARK 500    ASP B  31     -171.90    -69.93                                   
REMARK 500    SER B  62     -125.79     43.95                                   
REMARK 500    ALA B 102     -125.81     59.49                                   
REMARK 500    GLU B 126       72.90     53.33                                   
REMARK 500    PRO B 196       50.00    -92.67                                   
REMARK 500    PHE B 222      -56.67    -28.84                                   
REMARK 500    MET B 241     -108.79   -137.30                                   
REMARK 500    GLN C  19      126.33   -173.02                                   
REMARK 500    GLU C  74       76.58     40.45                                   
REMARK 500    CYS C 101      -78.18    -95.32                                   
REMARK 500    ALA C 102      -66.43   -100.14                                   
REMARK 500    SER C 106      -44.54    -29.00                                   
REMARK 500    PRO C 196       39.60    -70.75                                   
REMARK 500    ASP C 250      -37.64     69.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR C  216     PRO C  217                 -146.44                    
REMARK 500 PRO C  217     THR C  218                 -143.16                    
REMARK 500 PHE C  221     PHE C  222                  149.44                    
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 473        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH A 474        DISTANCE =  7.88 ANGSTROMS                       
REMARK 525    HOH A 475        DISTANCE =  8.18 ANGSTROMS                       
REMARK 525    HOH B 459        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH B 460        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH B 461        DISTANCE =  7.06 ANGSTROMS                       
REMARK 525    HOH B 462        DISTANCE =  7.88 ANGSTROMS                       
REMARK 525    HOH B 463        DISTANCE =  7.88 ANGSTROMS                       
REMARK 525    HOH C 368        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH C 369        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH C 370        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH C 371        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH C 372        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH C 373        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH C 374        DISTANCE =  6.12 ANGSTROMS                       
REMARK 525    HOH C 375        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH C 376        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH C 377        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH C 378        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH C 379        DISTANCE =  6.44 ANGSTROMS                       
REMARK 525    HOH C 380        DISTANCE =  6.61 ANGSTROMS                       
REMARK 525    HOH C 381        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH C 382        DISTANCE =  6.79 ANGSTROMS                       
REMARK 525    HOH C 383        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH C 384        DISTANCE =  6.94 ANGSTROMS                       
REMARK 525    HOH C 385        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH C 386        DISTANCE =  7.11 ANGSTROMS                       
REMARK 525    HOH C 387        DISTANCE =  7.31 ANGSTROMS                       
REMARK 525    HOH C 388        DISTANCE =  7.39 ANGSTROMS                       
REMARK 525    HOH C 389        DISTANCE =  8.04 ANGSTROMS                       
REMARK 525    HOH C 390        DISTANCE =  9.92 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZHB A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZHB B 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5IE4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5IE5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5IE7   RELATED DB: PDB                                   
DBREF  5IE6 A    1   264  UNP    Q8NKB0   Q8NKB0_BIOOC     1    264             
DBREF  5IE6 B    1   264  UNP    Q8NKB0   Q8NKB0_BIOOC     1    264             
DBREF  5IE6 C    1   264  UNP    Q8NKB0   Q8NKB0_BIOOC     1    264             
SEQADV 5IE6 ALA A  102  UNP  Q8NKB0    SER   102 ENGINEERED MUTATION            
SEQADV 5IE6 ALA B  102  UNP  Q8NKB0    SER   102 ENGINEERED MUTATION            
SEQADV 5IE6 ALA C  102  UNP  Q8NKB0    SER   102 ENGINEERED MUTATION            
SEQRES   1 A  264  MET ARG THR ARG SER THR ILE SER THR PRO ASN GLY ILE          
SEQRES   2 A  264  THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP VAL          
SEQRES   3 A  264  VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MET PHE          
SEQRES   4 A  264  ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE ARG          
SEQRES   5 A  264  VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER ALA          
SEQRES   6 A  264  LYS ALA PRO PRO GLU THR TYR THR GLU VAL THR ALA GLN          
SEQRES   7 A  264  LYS LEU ALA SER TYR VAL ILE SER VAL LEU ASP ALA LEU          
SEQRES   8 A  264  ASP ILE LYS HIS ALA THR VAL TRP GLY CYS ALA SER GLY          
SEQRES   9 A  264  ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO ASP          
SEQRES  10 A  264  ARG ILE ARG ASN ALA MET CYS HIS GLU LEU PRO THR LYS          
SEQRES  11 A  264  LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU ASP          
SEQRES  12 A  264  GLU GLU ILE SER LYS ILE LEU ALA ASN VAL MET LEU ASN          
SEQRES  13 A  264  ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA MET GLY          
SEQRES  14 A  264  ASP GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO VAL          
SEQRES  15 A  264  TRP ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER ALA          
SEQRES  16 A  264  PRO VAL LYS ASP LEU GLU ALA LEU ARG GLY LYS PRO LEU          
SEQRES  17 A  264  ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER PHE          
SEQRES  18 A  264  PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL ASN          
SEQRES  19 A  264  ILE GLY LEU LEU PRO GLY MET HIS PHE PRO TYR VAL SER          
SEQRES  20 A  264  HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR THR          
SEQRES  21 A  264  GLN LYS HIS LEU                                              
SEQRES   1 B  264  MET ARG THR ARG SER THR ILE SER THR PRO ASN GLY ILE          
SEQRES   2 B  264  THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP VAL          
SEQRES   3 B  264  VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MET PHE          
SEQRES   4 B  264  ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE ARG          
SEQRES   5 B  264  VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER ALA          
SEQRES   6 B  264  LYS ALA PRO PRO GLU THR TYR THR GLU VAL THR ALA GLN          
SEQRES   7 B  264  LYS LEU ALA SER TYR VAL ILE SER VAL LEU ASP ALA LEU          
SEQRES   8 B  264  ASP ILE LYS HIS ALA THR VAL TRP GLY CYS ALA SER GLY          
SEQRES   9 B  264  ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO ASP          
SEQRES  10 B  264  ARG ILE ARG ASN ALA MET CYS HIS GLU LEU PRO THR LYS          
SEQRES  11 B  264  LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU ASP          
SEQRES  12 B  264  GLU GLU ILE SER LYS ILE LEU ALA ASN VAL MET LEU ASN          
SEQRES  13 B  264  ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA MET GLY          
SEQRES  14 B  264  ASP GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO VAL          
SEQRES  15 B  264  TRP ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER ALA          
SEQRES  16 B  264  PRO VAL LYS ASP LEU GLU ALA LEU ARG GLY LYS PRO LEU          
SEQRES  17 B  264  ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER PHE          
SEQRES  18 B  264  PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL ASN          
SEQRES  19 B  264  ILE GLY LEU LEU PRO GLY MET HIS PHE PRO TYR VAL SER          
SEQRES  20 B  264  HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR THR          
SEQRES  21 B  264  GLN LYS HIS LEU                                              
SEQRES   1 C  264  MET ARG THR ARG SER THR ILE SER THR PRO ASN GLY ILE          
SEQRES   2 C  264  THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP VAL          
SEQRES   3 C  264  VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MET PHE          
SEQRES   4 C  264  ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE ARG          
SEQRES   5 C  264  VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER ALA          
SEQRES   6 C  264  LYS ALA PRO PRO GLU THR TYR THR GLU VAL THR ALA GLN          
SEQRES   7 C  264  LYS LEU ALA SER TYR VAL ILE SER VAL LEU ASP ALA LEU          
SEQRES   8 C  264  ASP ILE LYS HIS ALA THR VAL TRP GLY CYS ALA SER GLY          
SEQRES   9 C  264  ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO ASP          
SEQRES  10 C  264  ARG ILE ARG ASN ALA MET CYS HIS GLU LEU PRO THR LYS          
SEQRES  11 C  264  LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU ASP          
SEQRES  12 C  264  GLU GLU ILE SER LYS ILE LEU ALA ASN VAL MET LEU ASN          
SEQRES  13 C  264  ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA MET GLY          
SEQRES  14 C  264  ASP GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO VAL          
SEQRES  15 C  264  TRP ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER ALA          
SEQRES  16 C  264  PRO VAL LYS ASP LEU GLU ALA LEU ARG GLY LYS PRO LEU          
SEQRES  17 C  264  ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER PHE          
SEQRES  18 C  264  PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL ASN          
SEQRES  19 C  264  ILE GLY LEU LEU PRO GLY MET HIS PHE PRO TYR VAL SER          
SEQRES  20 C  264  HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR THR          
SEQRES  21 C  264  GLN LYS HIS LEU                                              
HET    ZHB  A 300      23                                                       
HET    ZHB  B 301      23                                                       
HETNAM     ZHB (3S,7S,11E)-7,14,16-TRIHYDROXY-3-METHYL-3,4,5,6,7,8,9,           
HETNAM   2 ZHB  10-OCTAHYDRO-1H-2-BENZOXACYCLOTETRADECIN-1-ONE                  
FORMUL   4  ZHB    2(C18 H24 O5)                                                
FORMUL   6  HOH   *228(H2 O)                                                    
HELIX    1 AA1 GLU A   35  MET A   38  5                                   4    
HELIX    2 AA2 PHE A   39  GLN A   49  1                                  11    
HELIX    3 AA3 MET A   61  ALA A   65  5                                   5    
HELIX    4 AA4 PRO A   68  TYR A   72  5                                   5    
HELIX    5 AA5 THR A   76  LEU A   91  1                                  16    
HELIX    6 AA6 ALA A  102  TYR A  115  1                                  14    
HELIX    7 AA7 LEU A  132  ASN A  137  1                                   6    
HELIX    8 AA8 THR A  138  LEU A  141  5                                   4    
HELIX    9 AA9 GLU A  142  ASP A  157  1                                  16    
HELIX   10 AB1 GLY A  161  MET A  168  1                                   8    
HELIX   11 AB2 GLY A  169  TYR A  187  1                                  19    
HELIX   12 AB3 ILE A  191  ALA A  195  5                                   5    
HELIX   13 AB4 ASP A  199  ARG A  204  1                                   6    
HELIX   14 AB5 PHE A  221  ALA A  231  1                                  11    
HELIX   15 AB6 PHE A  243  HIS A  248  1                                   6    
HELIX   16 AB7 HIS A  248  LYS A  262  1                                  15    
HELIX   17 AB8 GLU B   35  MET B   38  5                                   4    
HELIX   18 AB9 PHE B   39  ALA B   48  1                                  10    
HELIX   19 AC1 MET B   61  ALA B   65  5                                   5    
HELIX   20 AC2 PRO B   68  TYR B   72  5                                   5    
HELIX   21 AC3 THR B   76  LEU B   91  1                                  16    
HELIX   22 AC4 ALA B  102  TYR B  115  1                                  14    
HELIX   23 AC5 LEU B  132  ASN B  137  1                                   6    
HELIX   24 AC6 THR B  138  LEU B  141  5                                   4    
HELIX   25 AC7 GLU B  142  ASP B  157  1                                  16    
HELIX   26 AC8 GLY B  161  MET B  168  1                                   8    
HELIX   27 AC9 GLY B  169  TYR B  187  1                                  19    
HELIX   28 AD1 ILE B  191  ALA B  195  5                                   5    
HELIX   29 AD2 ASP B  199  ARG B  204  1                                   6    
HELIX   30 AD3 PHE B  221  ALA B  231  1                                  11    
HELIX   31 AD4 PHE B  243  HIS B  248  1                                   6    
HELIX   32 AD5 HIS B  248  LYS B  262  1                                  15    
HELIX   33 AD6 PRO C   68  TYR C   72  5                                   5    
HELIX   34 AD7 TYR C   83  ASP C   89  1                                   7    
HELIX   35 AD8 ALA C  102  TYR C  115  1                                  14    
HELIX   36 AD9 PRO C  217  PHE C  222  1                                   6    
HELIX   37 AE1 ASP C  250  LYS C  262  1                                  13    
SHEET    1 AA1 8 THR A   3  THR A   9  0                                        
SHEET    2 AA1 8 ILE A  13  GLU A  20 -1  O  GLN A  19   N  THR A   3           
SHEET    3 AA1 8 ARG A  52  PHE A  56 -1  O  VAL A  53   N  GLU A  20           
SHEET    4 AA1 8 ASP A  25  VAL A  29  1  N  LEU A  28   O  THR A  54           
SHEET    5 AA1 8 ALA A  96  CYS A 101  1  O  THR A  97   N  VAL A  27           
SHEET    6 AA1 8 ILE A 119  HIS A 125  1  O  MET A 123   N  VAL A  98           
SHEET    7 AA1 8 LEU A 208  GLY A 213  1  O  THR A 211   N  CYS A 124           
SHEET    8 AA1 8 ASN A 234  LEU A 238  1  O  ASN A 234   N  TRP A 210           
SHEET    1 AA2 8 THR B   3  SER B   8  0                                        
SHEET    2 AA2 8 THR B  14  GLU B  20 -1  O  GLN B  19   N  THR B   3           
SHEET    3 AA2 8 ARG B  52  PHE B  56 -1  O  VAL B  53   N  GLU B  20           
SHEET    4 AA2 8 ASP B  25  VAL B  29  1  N  VAL B  26   O  THR B  54           
SHEET    5 AA2 8 ALA B  96  CYS B 101  1  O  THR B  97   N  VAL B  27           
SHEET    6 AA2 8 ILE B 119  HIS B 125  1  O  MET B 123   N  VAL B  98           
SHEET    7 AA2 8 LEU B 208  GLY B 213  1  O  ASP B 209   N  ALA B 122           
SHEET    8 AA2 8 ILE B 235  LEU B 238  1  O  GLY B 236   N  TRP B 210           
SHEET    1 AA3 4 ASP C  25  LEU C  28  0                                        
SHEET    2 AA3 4 ALA C  96  GLY C 100  1  O  TRP C  99   N  VAL C  27           
SHEET    3 AA3 4 ILE C 119  CYS C 124  1  O  ARG C 120   N  ALA C  96           
SHEET    4 AA3 4 LEU C 208  ASP C 209  1  O  ASP C 209   N  CYS C 124           
SITE     1 AC1 13 GLY A  32  ALA A 102  SER A 103  PRO A 128                    
SITE     2 AC1 13 LEU A 132  LEU A 135  VAL A 158  TRP A 183                    
SITE     3 AC1 13 TYR A 187  PRO A 188  ILE A 191  PRO A 192                    
SITE     4 AC1 13 HIS A 242                                                     
SITE     1 AC2 13 GLY B  32  ALA B 102  SER B 103  PRO B 128                    
SITE     2 AC2 13 LEU B 135  MET B 154  VAL B 158  TRP B 183                    
SITE     3 AC2 13 TYR B 187  PRO B 188  ILE B 191  PRO B 192                    
SITE     4 AC2 13 HIS B 242                                                     
CRYST1   86.043   86.043  470.111  90.00  90.00 120.00 P 61 2 2     36          
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      0.011622  0.006710  0.000000        0.00000                         
SCALE2      0.000000  0.013420  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002127        0.00000                         
TER    2021      LEU A 264                                                      
TER    4042      LEU B 264                                                      
TER    5031      LEU C 264                                                      
MASTER      559    0    2   37   20    0    8    6 5302    3   46   63          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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