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LongText Report for: 5xo6-pdb

Name Class
5xo6-pdb
HEADER    HYDROLASE                               27-MAY-17   5XO6              
TITLE     CRYSTAL STRUCTURE OF A NOVEL ZEN LACTONASE MUTANT                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LACTONASE FOR PROTEIN;                                     
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHINOCLADIELLA MACKENZIEI CBS 650.93;           
SOURCE   3 ORGANISM_TAXID: 1442369;                                             
SOURCE   4 GENE: Z518_04590;                                                    
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,W.T.LIU,W.D.LIU,C.C.CHEN,R.T.GUO                            
REVDAT   1   02-MAY-18 5XO6    0                                                
JRNL        AUTH   Y.Y.ZHENG,W.T.LIU,C.C.CHEN,X.Y.HU,W.D.LIU,T.P.KO,X.K.TANG,   
JRNL        AUTH 2 H.L.WEI,J.W.HUANG,R.T.GUO                                    
JRNL        TITL   CRYSTAL STRUCTURE OF A MYCOESTROGEN-DETOXIFYING LACTONASE    
JRNL        TITL 2 FROM RHINOCLADIELLA MACKENZIEI: MOLECULAR INSIGHT INTO ZHD   
JRNL        TITL 3 SUBSTRATE SELECTIVITY                                        
JRNL        REF    ACS CATALYSIS                 V.   8  4294 2018              
JRNL        REFN                   ESSN 2155-5435                               
JRNL        DOI    10.1021/ACSCATAL.8B00464                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.38 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.38                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.81                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 112520                         
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) : 0.167                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1955                            
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) : 2.38                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7752                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.08                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2820                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 131                          
REMARK   3   BIN FREE R VALUE                    : 0.2890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 16344                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 587                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : -0.01000                                             
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): 0.249         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.203         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.162         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.176         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 16942 ; 0.016 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 15650 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 23132 ; 1.756 ; 1.961       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 36206 ; 1.057 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2096 ; 7.106 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   736 ;35.328 ;23.587       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2616 ;15.353 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   104 ;15.520 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2520 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 19088 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  3736 ; 0.002 ; 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):  8408 ; 4.359 ; 5.144       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  8407 ; 4.357 ; 5.144       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10496 ; 6.351 ; 7.703       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 10497 ; 6.351 ; 7.704       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  8534 ; 4.970 ; 5.678       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  8534 ; 4.969 ; 5.678       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 12637 ; 7.537 ; 8.312       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 19630 ; 9.602 ;41.719       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 19445 ; 9.606 ;41.686       
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 : 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 5XO6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300003869.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-APR-17                          
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                       : TPS 05A                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9998                             
REMARK 200  MONOCHROMATOR                  : LN2 COOLED SI(111) DOUBLE          
REMARK 200                                   CRYSTAL MONOCHROMATOR              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300-HS                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 114582                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.380                              
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     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.38                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000                            
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   (%): 61.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.085M SODIUM     
REMARK 280  CACODYLATE PH 6.5, 25-28%(W/V) POLYETHYLENE GLYCOL 8000 AND 15%     
REMARK 280  (V/V) GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     ALA C     3                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     ALA D     3                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     ALA E     3                                                      
REMARK 465     LYS E   266                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ALA F     2                                                      
REMARK 465     ALA F     3                                                      
REMARK 465     LEU F   138                                                      
REMARK 465     LEU F   139                                                      
REMARK 465     HIS F   140                                                      
REMARK 465     ILE F   141                                                      
REMARK 465     MET G     1                                                      
REMARK 465     ALA G     2                                                      
REMARK 465     ALA G     3                                                      
REMARK 465     HIS G   140                                                      
REMARK 465     ILE G   141                                                      
REMARK 465     HIS G   142                                                      
REMARK 465     GLU G   143                                                      
REMARK 465     VAL G   144                                                      
REMARK 465     ASP G   145                                                      
REMARK 465     MET H     1                                                      
REMARK 465     ALA H     2                                                      
REMARK 465     ALA H     3                                                      
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    PRO C  72   C   -  N   -  CA  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    PRO C 146   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    PRO C 190   C   -  N   -  CA  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    PRO E  72   C   -  N   -  CA  ANGL. DEV. =  12.7 DEGREES          
REMARK 500    PRO F 172   C   -  N   -  CA  ANGL. DEV. =  11.7 DEGREES          
REMARK 500    PRO G 119   C   -  N   -  CA  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    PRO G 172   C   -  N   -  CA  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    PRO H  72   C   -  N   -  CA  ANGL. DEV. =  13.1 DEGREES          
REMARK 500    PRO H 146   C   -  N   -  CA  ANGL. DEV. =  11.1 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  65     -121.09     48.75                                   
REMARK 500    ALA A 105     -112.90     57.13                                   
REMARK 500    GLU A 129       74.92     51.02                                   
REMARK 500    ASN A 163       96.56   -178.46                                   
REMARK 500    TYR A 189      -64.00   -108.48                                   
REMARK 500    ASN A 242     -108.10   -136.88                                   
REMARK 500    SER B  65     -121.45     46.98                                   
REMARK 500    ALA B 105     -115.30     57.55                                   
REMARK 500    GLU B 129       71.09     53.71                                   
REMARK 500    ASN B 163       95.78   -174.98                                   
REMARK 500    ASN B 242     -109.60   -135.86                                   
REMARK 500    LYS C  13       -0.94    -59.67                                   
REMARK 500    SER C  65     -121.40     48.08                                   
REMARK 500    TYR C  75       28.84   -144.98                                   
REMARK 500    ALA C 105     -119.10     55.68                                   
REMARK 500    GLU C 129       71.36     52.78                                   
REMARK 500    HIS C 140       51.63   -146.48                                   
REMARK 500    ASN C 163       92.83   -177.18                                   
REMARK 500    ALA C 169        8.57    -68.19                                   
REMARK 500    TYR C 189      -60.88   -107.18                                   
REMARK 500    ASN C 242     -119.47   -132.60                                   
REMARK 500    LYS D  13        3.81    -68.52                                   
REMARK 500    SER D  65     -122.81     50.60                                   
REMARK 500    ALA D 105     -118.58     62.04                                   
REMARK 500    GLU D 129       72.89     52.53                                   
REMARK 500    ASN D 163       92.15   -176.20                                   
REMARK 500    TYR D 189      -65.86   -102.56                                   
REMARK 500    ASN D 242     -113.91   -128.98                                   
REMARK 500    SER E  65     -116.42     44.87                                   
REMARK 500    ALA E 105     -125.16     56.48                                   
REMARK 500    TYR E 118       47.23   -144.52                                   
REMARK 500    GLU E 129       74.43     48.80                                   
REMARK 500    ASN E 163       97.12   -174.53                                   
REMARK 500    LYS E 206      -41.04   -152.99                                   
REMARK 500    ASN E 242     -110.18   -118.76                                   
REMARK 500    LYS F  13       -8.63    -57.82                                   
REMARK 500    ASP F  34     -158.81    -80.11                                   
REMARK 500    SER F  65     -122.21     39.02                                   
REMARK 500    TYR F  75       30.32   -140.74                                   
REMARK 500    ALA F 105     -116.35     60.07                                   
REMARK 500    TYR F 118       40.49   -143.07                                   
REMARK 500    GLU F 129       70.95     54.84                                   
REMARK 500    ASN F 163       93.52   -175.33                                   
REMARK 500    ALA F 169        1.36    -69.22                                   
REMARK 500    TYR F 189      -68.47    -93.99                                   
REMARK 500    ASN F 242     -114.81   -124.74                                   
REMARK 500    ASP G  34     -156.78    -78.97                                   
REMARK 500    SER G  65     -121.68     45.64                                   
REMARK 500    ASP G  69       82.53    -64.07                                   
REMARK 500    ALA G 105     -120.82     52.64                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      62 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5XO7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5XO8   RELATED DB: PDB                                   
DBREF1 5XO6 A    1   266  UNP                  A0A0D2ILK1_9EURO                 
DBREF2 5XO6 A     A0A0D2ILK1                          1         266             
DBREF1 5XO6 B    1   266  UNP                  A0A0D2ILK1_9EURO                 
DBREF2 5XO6 B     A0A0D2ILK1                          1         266             
DBREF1 5XO6 C    1   266  UNP                  A0A0D2ILK1_9EURO                 
DBREF2 5XO6 C     A0A0D2ILK1                          1         266             
DBREF1 5XO6 D    1   266  UNP                  A0A0D2ILK1_9EURO                 
DBREF2 5XO6 D     A0A0D2ILK1                          1         266             
DBREF1 5XO6 E    1   266  UNP                  A0A0D2ILK1_9EURO                 
DBREF2 5XO6 E     A0A0D2ILK1                          1         266             
DBREF1 5XO6 F    1   266  UNP                  A0A0D2ILK1_9EURO                 
DBREF2 5XO6 F     A0A0D2ILK1                          1         266             
DBREF1 5XO6 G    1   266  UNP                  A0A0D2ILK1_9EURO                 
DBREF2 5XO6 G     A0A0D2ILK1                          1         266             
DBREF1 5XO6 H    1   266  UNP                  A0A0D2ILK1_9EURO                 
DBREF2 5XO6 H     A0A0D2ILK1                          1         266             
SEQADV 5XO6 ALA A  105  UNP  A0A0D2ILK SER   105 ENGINEERED MUTATION            
SEQADV 5XO6 ALA B  105  UNP  A0A0D2ILK SER   105 ENGINEERED MUTATION            
SEQADV 5XO6 ALA C  105  UNP  A0A0D2ILK SER   105 ENGINEERED MUTATION            
SEQADV 5XO6 ALA D  105  UNP  A0A0D2ILK SER   105 ENGINEERED MUTATION            
SEQADV 5XO6 ALA E  105  UNP  A0A0D2ILK SER   105 ENGINEERED MUTATION            
SEQADV 5XO6 ALA F  105  UNP  A0A0D2ILK SER   105 ENGINEERED MUTATION            
SEQADV 5XO6 ALA G  105  UNP  A0A0D2ILK SER   105 ENGINEERED MUTATION            
SEQADV 5XO6 ALA H  105  UNP  A0A0D2ILK SER   105 ENGINEERED MUTATION            
SEQRES   1 A  266  MET ALA ALA THR ARG THR ARG GLY TYR VAL THR THR LYS          
SEQRES   2 A  266  ASP GLY ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY          
SEQRES   3 A  266  PRO ASP VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS          
SEQRES   4 A  266  GLN MET PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN          
SEQRES   5 A  266  GLY PHE ARG VAL THR THR PHE ASP MET PRO GLY MET SER          
SEQRES   6 A  266  ARG SER SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE          
SEQRES   7 A  266  THR GLY ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU          
SEQRES   8 A  266  ASP THR LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS          
SEQRES   9 A  266  ALA SER GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP          
SEQRES  10 A  266  TYR PRO GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL          
SEQRES  11 A  266  PRO THR GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU          
SEQRES  12 A  266  VAL ASP PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN          
SEQRES  13 A  266  SER ARG ALA TYR SER GLY ASN VAL GLU ALA TRP ASP ALA          
SEQRES  14 A  266  LEU GLY PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR          
SEQRES  15 A  266  PRO ARG TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO          
SEQRES  16 A  266  SER ALA PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO          
SEQRES  17 A  266  ILE ASP TRP THR VAL GLY ALA SER THR PRO THR LYS LEU          
SEQRES  18 A  266  PHE PHE GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE          
SEQRES  19 A  266  ASN ILE GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL          
SEQRES  20 A  266  SER HIS PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR          
SEQRES  21 A  266  SER ARG LYS TYR LEU LYS                                      
SEQRES   1 B  266  MET ALA ALA THR ARG THR ARG GLY TYR VAL THR THR LYS          
SEQRES   2 B  266  ASP GLY ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY          
SEQRES   3 B  266  PRO ASP VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS          
SEQRES   4 B  266  GLN MET PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN          
SEQRES   5 B  266  GLY PHE ARG VAL THR THR PHE ASP MET PRO GLY MET SER          
SEQRES   6 B  266  ARG SER SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE          
SEQRES   7 B  266  THR GLY ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU          
SEQRES   8 B  266  ASP THR LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS          
SEQRES   9 B  266  ALA SER GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP          
SEQRES  10 B  266  TYR PRO GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL          
SEQRES  11 B  266  PRO THR GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU          
SEQRES  12 B  266  VAL ASP PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN          
SEQRES  13 B  266  SER ARG ALA TYR SER GLY ASN VAL GLU ALA TRP ASP ALA          
SEQRES  14 B  266  LEU GLY PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR          
SEQRES  15 B  266  PRO ARG TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO          
SEQRES  16 B  266  SER ALA PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO          
SEQRES  17 B  266  ILE ASP TRP THR VAL GLY ALA SER THR PRO THR LYS LEU          
SEQRES  18 B  266  PHE PHE GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE          
SEQRES  19 B  266  ASN ILE GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL          
SEQRES  20 B  266  SER HIS PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR          
SEQRES  21 B  266  SER ARG LYS TYR LEU LYS                                      
SEQRES   1 C  266  MET ALA ALA THR ARG THR ARG GLY TYR VAL THR THR LYS          
SEQRES   2 C  266  ASP GLY ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY          
SEQRES   3 C  266  PRO ASP VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS          
SEQRES   4 C  266  GLN MET PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN          
SEQRES   5 C  266  GLY PHE ARG VAL THR THR PHE ASP MET PRO GLY MET SER          
SEQRES   6 C  266  ARG SER SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE          
SEQRES   7 C  266  THR GLY ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU          
SEQRES   8 C  266  ASP THR LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS          
SEQRES   9 C  266  ALA SER GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP          
SEQRES  10 C  266  TYR PRO GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL          
SEQRES  11 C  266  PRO THR GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU          
SEQRES  12 C  266  VAL ASP PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN          
SEQRES  13 C  266  SER ARG ALA TYR SER GLY ASN VAL GLU ALA TRP ASP ALA          
SEQRES  14 C  266  LEU GLY PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR          
SEQRES  15 C  266  PRO ARG TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO          
SEQRES  16 C  266  SER ALA PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO          
SEQRES  17 C  266  ILE ASP TRP THR VAL GLY ALA SER THR PRO THR LYS LEU          
SEQRES  18 C  266  PHE PHE GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE          
SEQRES  19 C  266  ASN ILE GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL          
SEQRES  20 C  266  SER HIS PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR          
SEQRES  21 C  266  SER ARG LYS TYR LEU LYS                                      
SEQRES   1 D  266  MET ALA ALA THR ARG THR ARG GLY TYR VAL THR THR LYS          
SEQRES   2 D  266  ASP GLY ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY          
SEQRES   3 D  266  PRO ASP VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS          
SEQRES   4 D  266  GLN MET PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN          
SEQRES   5 D  266  GLY PHE ARG VAL THR THR PHE ASP MET PRO GLY MET SER          
SEQRES   6 D  266  ARG SER SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE          
SEQRES   7 D  266  THR GLY ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU          
SEQRES   8 D  266  ASP THR LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS          
SEQRES   9 D  266  ALA SER GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP          
SEQRES  10 D  266  TYR PRO GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL          
SEQRES  11 D  266  PRO THR GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU          
SEQRES  12 D  266  VAL ASP PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN          
SEQRES  13 D  266  SER ARG ALA TYR SER GLY ASN VAL GLU ALA TRP ASP ALA          
SEQRES  14 D  266  LEU GLY PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR          
SEQRES  15 D  266  PRO ARG TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO          
SEQRES  16 D  266  SER ALA PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO          
SEQRES  17 D  266  ILE ASP TRP THR VAL GLY ALA SER THR PRO THR LYS LEU          
SEQRES  18 D  266  PHE PHE GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE          
SEQRES  19 D  266  ASN ILE GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL          
SEQRES  20 D  266  SER HIS PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR          
SEQRES  21 D  266  SER ARG LYS TYR LEU LYS                                      
SEQRES   1 E  266  MET ALA ALA THR ARG THR ARG GLY TYR VAL THR THR LYS          
SEQRES   2 E  266  ASP GLY ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY          
SEQRES   3 E  266  PRO ASP VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS          
SEQRES   4 E  266  GLN MET PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN          
SEQRES   5 E  266  GLY PHE ARG VAL THR THR PHE ASP MET PRO GLY MET SER          
SEQRES   6 E  266  ARG SER SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE          
SEQRES   7 E  266  THR GLY ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU          
SEQRES   8 E  266  ASP THR LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS          
SEQRES   9 E  266  ALA SER GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP          
SEQRES  10 E  266  TYR PRO GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL          
SEQRES  11 E  266  PRO THR GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU          
SEQRES  12 E  266  VAL ASP PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN          
SEQRES  13 E  266  SER ARG ALA TYR SER GLY ASN VAL GLU ALA TRP ASP ALA          
SEQRES  14 E  266  LEU GLY PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR          
SEQRES  15 E  266  PRO ARG TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO          
SEQRES  16 E  266  SER ALA PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO          
SEQRES  17 E  266  ILE ASP TRP THR VAL GLY ALA SER THR PRO THR LYS LEU          
SEQRES  18 E  266  PHE PHE GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE          
SEQRES  19 E  266  ASN ILE GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL          
SEQRES  20 E  266  SER HIS PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR          
SEQRES  21 E  266  SER ARG LYS TYR LEU LYS                                      
SEQRES   1 F  266  MET ALA ALA THR ARG THR ARG GLY TYR VAL THR THR LYS          
SEQRES   2 F  266  ASP GLY ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY          
SEQRES   3 F  266  PRO ASP VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS          
SEQRES   4 F  266  GLN MET PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN          
SEQRES   5 F  266  GLY PHE ARG VAL THR THR PHE ASP MET PRO GLY MET SER          
SEQRES   6 F  266  ARG SER SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE          
SEQRES   7 F  266  THR GLY ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU          
SEQRES   8 F  266  ASP THR LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS          
SEQRES   9 F  266  ALA SER GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP          
SEQRES  10 F  266  TYR PRO GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL          
SEQRES  11 F  266  PRO THR GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU          
SEQRES  12 F  266  VAL ASP PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN          
SEQRES  13 F  266  SER ARG ALA TYR SER GLY ASN VAL GLU ALA TRP ASP ALA          
SEQRES  14 F  266  LEU GLY PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR          
SEQRES  15 F  266  PRO ARG TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO          
SEQRES  16 F  266  SER ALA PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO          
SEQRES  17 F  266  ILE ASP TRP THR VAL GLY ALA SER THR PRO THR LYS LEU          
SEQRES  18 F  266  PHE PHE GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE          
SEQRES  19 F  266  ASN ILE GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL          
SEQRES  20 F  266  SER HIS PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR          
SEQRES  21 F  266  SER ARG LYS TYR LEU LYS                                      
SEQRES   1 G  266  MET ALA ALA THR ARG THR ARG GLY TYR VAL THR THR LYS          
SEQRES   2 G  266  ASP GLY ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY          
SEQRES   3 G  266  PRO ASP VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS          
SEQRES   4 G  266  GLN MET PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN          
SEQRES   5 G  266  GLY PHE ARG VAL THR THR PHE ASP MET PRO GLY MET SER          
SEQRES   6 G  266  ARG SER SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE          
SEQRES   7 G  266  THR GLY ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU          
SEQRES   8 G  266  ASP THR LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS          
SEQRES   9 G  266  ALA SER GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP          
SEQRES  10 G  266  TYR PRO GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL          
SEQRES  11 G  266  PRO THR GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU          
SEQRES  12 G  266  VAL ASP PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN          
SEQRES  13 G  266  SER ARG ALA TYR SER GLY ASN VAL GLU ALA TRP ASP ALA          
SEQRES  14 G  266  LEU GLY PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR          
SEQRES  15 G  266  PRO ARG TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO          
SEQRES  16 G  266  SER ALA PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO          
SEQRES  17 G  266  ILE ASP TRP THR VAL GLY ALA SER THR PRO THR LYS LEU          
SEQRES  18 G  266  PHE PHE GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE          
SEQRES  19 G  266  ASN ILE GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL          
SEQRES  20 G  266  SER HIS PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR          
SEQRES  21 G  266  SER ARG LYS TYR LEU LYS                                      
SEQRES   1 H  266  MET ALA ALA THR ARG THR ARG GLY TYR VAL THR THR LYS          
SEQRES   2 H  266  ASP GLY ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY          
SEQRES   3 H  266  PRO ASP VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS          
SEQRES   4 H  266  GLN MET PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN          
SEQRES   5 H  266  GLY PHE ARG VAL THR THR PHE ASP MET PRO GLY MET SER          
SEQRES   6 H  266  ARG SER SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE          
SEQRES   7 H  266  THR GLY ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU          
SEQRES   8 H  266  ASP THR LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS          
SEQRES   9 H  266  ALA SER GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP          
SEQRES  10 H  266  TYR PRO GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL          
SEQRES  11 H  266  PRO THR GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU          
SEQRES  12 H  266  VAL ASP PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN          
SEQRES  13 H  266  SER ARG ALA TYR SER GLY ASN VAL GLU ALA TRP ASP ALA          
SEQRES  14 H  266  LEU GLY PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR          
SEQRES  15 H  266  PRO ARG TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO          
SEQRES  16 H  266  SER ALA PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO          
SEQRES  17 H  266  ILE ASP TRP THR VAL GLY ALA SER THR PRO THR LYS LEU          
SEQRES  18 H  266  PHE PHE GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE          
SEQRES  19 H  266  ASN ILE GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL          
SEQRES  20 H  266  SER HIS PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR          
SEQRES  21 H  266  SER ARG LYS TYR LEU LYS                                      
HET    1PE  A 301      16                                                       
HET    1PE  B 301      16                                                       
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETSYN     1PE PEG400                                                           
FORMUL   9  1PE    2(C10 H22 O6)                                                
FORMUL  11  HOH   *587(H2 O)                                                    
HELIX    1 AA1 GLU A   38  MET A   41  5                                   4    
HELIX    2 AA2 PHE A   42  SER A   51  1                                  10    
HELIX    3 AA3 MET A   64  SER A   68  5                                   5    
HELIX    4 AA4 PRO A   71  GLN A   76  5                                   6    
HELIX    5 AA5 THR A   79  LEU A   94  1                                  16    
HELIX    6 AA6 ALA A  105  TYR A  118  1                                  14    
HELIX    7 AA7 PRO A  135  LEU A  139  5                                   5    
HELIX    8 AA8 HIS A  140  VAL A  144  5                                   5    
HELIX    9 AA9 ASP A  145  TYR A  160  1                                  16    
HELIX   10 AB1 ASN A  163  ALA A  169  1                                   7    
HELIX   11 AB2 GLY A  171  TYR A  189  1                                  19    
HELIX   12 AB3 ILE A  193  ALA A  197  5                                   5    
HELIX   13 AB4 LYS A  200  LEU A  204  5                                   5    
HELIX   14 AB5 PHE A  222  GLY A  233  1                                  12    
HELIX   15 AB6 PHE A  244  HIS A  249  1                                   6    
HELIX   16 AB7 HIS A  249  LYS A  263  1                                  15    
HELIX   17 AB8 GLU B   38  MET B   41  5                                   4    
HELIX   18 AB9 PHE B   42  SER B   51  1                                  10    
HELIX   19 AC1 MET B   64  SER B   68  5                                   5    
HELIX   20 AC2 PRO B   71  GLN B   76  5                                   6    
HELIX   21 AC3 THR B   79  LEU B   94  1                                  16    
HELIX   22 AC4 ALA B  105  TYR B  118  1                                  14    
HELIX   23 AC5 PRO B  135  LEU B  139  5                                   5    
HELIX   24 AC6 HIS B  140  VAL B  144  5                                   5    
HELIX   25 AC7 ASP B  145  TYR B  160  1                                  16    
HELIX   26 AC8 ASN B  163  ALA B  169  1                                   7    
HELIX   27 AC9 GLY B  171  TYR B  189  1                                  19    
HELIX   28 AD1 ILE B  193  ALA B  197  5                                   5    
HELIX   29 AD2 LYS B  200  LEU B  204  5                                   5    
HELIX   30 AD3 PHE B  222  GLY B  233  1                                  12    
HELIX   31 AD4 PHE B  244  HIS B  249  1                                   6    
HELIX   32 AD5 HIS B  249  LYS B  263  1                                  15    
HELIX   33 AD6 GLU C   38  MET C   41  5                                   4    
HELIX   34 AD7 PHE C   42  SER C   51  1                                  10    
HELIX   35 AD8 MET C   64  SER C   68  5                                   5    
HELIX   36 AD9 PRO C   71  GLN C   76  5                                   6    
HELIX   37 AE1 THR C   79  LEU C   94  1                                  16    
HELIX   38 AE2 ALA C  105  TYR C  118  1                                  14    
HELIX   39 AE3 ASP C  145  TYR C  160  1                                  16    
HELIX   40 AE4 ASN C  163  ALA C  169  1                                   7    
HELIX   41 AE5 GLY C  171  TYR C  189  1                                  19    
HELIX   42 AE6 ILE C  193  ALA C  197  5                                   5    
HELIX   43 AE7 LYS C  200  LEU C  204  5                                   5    
HELIX   44 AE8 PHE C  222  GLU C  232  1                                  11    
HELIX   45 AE9 PHE C  244  HIS C  249  1                                   6    
HELIX   46 AF1 HIS C  249  LYS C  263  1                                  15    
HELIX   47 AF2 GLU D   38  MET D   41  5                                   4    
HELIX   48 AF3 PHE D   42  SER D   51  1                                  10    
HELIX   49 AF4 MET D   64  SER D   68  5                                   5    
HELIX   50 AF5 PRO D   71  GLN D   76  5                                   6    
HELIX   51 AF6 THR D   79  LEU D   94  1                                  16    
HELIX   52 AF7 ALA D  105  TYR D  118  1                                  14    
HELIX   53 AF8 PRO D  135  LEU D  139  5                                   5    
HELIX   54 AF9 ASP D  145  TYR D  160  1                                  16    
HELIX   55 AG1 ASN D  163  ALA D  169  1                                   7    
HELIX   56 AG2 GLY D  171  TYR D  189  1                                  19    
HELIX   57 AG3 ILE D  193  ALA D  197  5                                   5    
HELIX   58 AG4 LYS D  200  LEU D  204  5                                   5    
HELIX   59 AG5 PHE D  222  GLU D  232  1                                  11    
HELIX   60 AG6 PHE D  244  HIS D  249  1                                   6    
HELIX   61 AG7 HIS D  249  LYS D  263  1                                  15    
HELIX   62 AG8 GLU E   38  MET E   41  5                                   4    
HELIX   63 AG9 PHE E   42  SER E   51  1                                  10    
HELIX   64 AH1 MET E   64  SER E   68  5                                   5    
HELIX   65 AH2 PRO E   71  GLN E   76  5                                   6    
HELIX   66 AH3 THR E   79  LEU E   94  1                                  16    
HELIX   67 AH4 ALA E  105  TYR E  118  1                                  14    
HELIX   68 AH5 PRO E  135  LEU E  139  5                                   5    
HELIX   69 AH6 ASP E  145  TYR E  160  1                                  16    
HELIX   70 AH7 ASN E  163  ALA E  169  1                                   7    
HELIX   71 AH8 GLY E  171  TYR E  189  1                                  19    
HELIX   72 AH9 LYS E  200  HIS E  205  1                                   6    
HELIX   73 AI1 PHE E  222  ARG E  231  1                                  10    
HELIX   74 AI2 PHE E  244  HIS E  249  1                                   6    
HELIX   75 AI3 HIS E  249  LYS E  263  1                                  15    
HELIX   76 AI4 GLU F   38  MET F   41  5                                   4    
HELIX   77 AI5 PHE F   42  SER F   51  1                                  10    
HELIX   78 AI6 MET F   64  SER F   68  5                                   5    
HELIX   79 AI7 PRO F   71  GLN F   76  5                                   6    
HELIX   80 AI8 THR F   79  LEU F   94  1                                  16    
HELIX   81 AI9 ALA F  105  TYR F  118  1                                  14    
HELIX   82 AJ1 ASP F  145  TYR F  160  1                                  16    
HELIX   83 AJ2 ASN F  163  ALA F  169  1                                   7    
HELIX   84 AJ3 GLY F  171  TYR F  189  1                                  19    
HELIX   85 AJ4 ILE F  193  ALA F  197  5                                   5    
HELIX   86 AJ5 LYS F  200  HIS F  205  5                                   6    
HELIX   87 AJ6 PHE F  222  GLU F  232  1                                  11    
HELIX   88 AJ7 PHE F  244  HIS F  249  1                                   6    
HELIX   89 AJ8 HIS F  249  LYS F  263  1                                  15    
HELIX   90 AJ9 GLU G   38  MET G   41  5                                   4    
HELIX   91 AK1 PHE G   42  SER G   51  1                                  10    
HELIX   92 AK2 MET G   64  SER G   68  5                                   5    
HELIX   93 AK3 PRO G   72  GLN G   76  5                                   5    
HELIX   94 AK4 THR G   79  LEU G   94  1                                  16    
HELIX   95 AK5 ALA G  105  TYR G  118  1                                  14    
HELIX   96 AK6 PRO G  135  LEU G  139  5                                   5    
HELIX   97 AK7 ALA G  147  TYR G  160  1                                  14    
HELIX   98 AK8 ASN G  163  ALA G  169  1                                   7    
HELIX   99 AK9 GLY G  171  TYR G  189  1                                  19    
HELIX  100 AL1 ILE G  193  ALA G  197  5                                   5    
HELIX  101 AL2 THR G  201  HIS G  205  5                                   5    
HELIX  102 AL3 PRO G  218  LEU G  221  5                                   4    
HELIX  103 AL4 PHE G  222  GLU G  232  1                                  11    
HELIX  104 AL5 PHE G  244  HIS G  249  1                                   6    
HELIX  105 AL6 HIS G  249  LYS G  263  1                                  15    
HELIX  106 AL7 GLU H   38  MET H   41  5                                   4    
HELIX  107 AL8 PHE H   42  SER H   51  1                                  10    
HELIX  108 AL9 MET H   64  SER H   68  5                                   5    
HELIX  109 AM1 PRO H   71  GLN H   76  5                                   6    
HELIX  110 AM2 THR H   79  LEU H   94  1                                  16    
HELIX  111 AM3 ALA H  105  TYR H  118  1                                  14    
HELIX  112 AM4 PRO H  135  LEU H  139  5                                   5    
HELIX  113 AM5 HIS H  140  VAL H  144  5                                   5    
HELIX  114 AM6 ASP H  145  TYR H  160  1                                  16    
HELIX  115 AM7 ASN H  163  ALA H  169  1                                   7    
HELIX  116 AM8 GLY H  171  TYR H  189  1                                  19    
HELIX  117 AM9 PHE H  222  GLU H  232  1                                  11    
HELIX  118 AN1 PHE H  244  HIS H  249  1                                   6    
HELIX  119 AN2 HIS H  249  LYS H  263  1                                  15    
SHEET    1 AA1 6 THR A   6  THR A  11  0                                        
SHEET    2 AA1 6 LYS A  17  GLU A  23 -1  O  GLN A  22   N  THR A   6           
SHEET    3 AA1 6 ARG A  55  PHE A  59 -1  O  VAL A  56   N  GLU A  23           
SHEET    4 AA1 6 ASP A  28  ILE A  32  1  N  LEU A  31   O  THR A  57           
SHEET    5 AA1 6 ALA A  99  CYS A 104  1  O  SER A 100   N  VAL A  30           
SHEET    6 AA1 6 VAL A 122  HIS A 128  1  O  MET A 126   N  VAL A 101           
SHEET    1 AA2 2 ASP A 210  GLY A 214  0                                        
SHEET    2 AA2 2 ASN A 235  LEU A 239  1  O  ASN A 235   N  TRP A 211           
SHEET    1 AA3 6 THR B   6  THR B  11  0                                        
SHEET    2 AA3 6 LYS B  17  GLU B  23 -1  O  TYR B  20   N  GLY B   8           
SHEET    3 AA3 6 ARG B  55  PHE B  59 -1  O  VAL B  56   N  GLU B  23           
SHEET    4 AA3 6 ASP B  28  ILE B  32  1  N  LEU B  31   O  THR B  57           
SHEET    5 AA3 6 ALA B  99  CYS B 104  1  O  SER B 100   N  VAL B  30           
SHEET    6 AA3 6 VAL B 122  HIS B 128  1  O  MET B 126   N  VAL B 101           
SHEET    1 AA4 2 ASP B 210  GLY B 214  0                                        
SHEET    2 AA4 2 ASN B 235  LEU B 239  1  O  ASN B 235   N  TRP B 211           
SHEET    1 AA5 6 ARG C   5  THR C  11  0                                        
SHEET    2 AA5 6 LYS C  17  GLU C  23 -1  O  TYR C  20   N  GLY C   8           
SHEET    3 AA5 6 ARG C  55  PHE C  59 -1  O  VAL C  56   N  GLU C  23           
SHEET    4 AA5 6 ASP C  28  ILE C  32  1  N  VAL C  29   O  THR C  57           
SHEET    5 AA5 6 ALA C  99  CYS C 104  1  O  TRP C 102   N  ILE C  32           
SHEET    6 AA5 6 VAL C 122  HIS C 128  1  O  MET C 126   N  VAL C 101           
SHEET    1 AA6 2 ASP C 210  GLY C 214  0                                        
SHEET    2 AA6 2 ASN C 235  LEU C 239  1  O  ASN C 235   N  TRP C 211           
SHEET    1 AA7 6 THR D   6  THR D  11  0                                        
SHEET    2 AA7 6 LYS D  17  GLU D  23 -1  O  TRP D  18   N  VAL D  10           
SHEET    3 AA7 6 ARG D  55  PHE D  59 -1  O  VAL D  56   N  GLU D  23           
SHEET    4 AA7 6 ASP D  28  ILE D  32  1  N  LEU D  31   O  THR D  57           
SHEET    5 AA7 6 ALA D  99  CYS D 104  1  O  TRP D 102   N  ILE D  32           
SHEET    6 AA7 6 VAL D 122  HIS D 128  1  O  MET D 126   N  VAL D 101           
SHEET    1 AA8 2 ASP D 210  GLY D 214  0                                        
SHEET    2 AA8 2 ASN D 235  LEU D 239  1  O  ASN D 235   N  TRP D 211           
SHEET    1 AA9 6 ARG E   5  THR E  11  0                                        
SHEET    2 AA9 6 LYS E  17  GLU E  23 -1  O  GLN E  22   N  THR E   6           
SHEET    3 AA9 6 ARG E  55  PHE E  59 -1  O  THR E  58   N  GLU E  21           
SHEET    4 AA9 6 ASP E  28  ILE E  32  1  N  VAL E  29   O  ARG E  55           
SHEET    5 AA9 6 ALA E  99  CYS E 104  1  O  SER E 100   N  VAL E  30           
SHEET    6 AA9 6 VAL E 122  HIS E 128  1  O  MET E 126   N  VAL E 101           
SHEET    1 AB1 2 ASP E 210  GLY E 214  0                                        
SHEET    2 AB1 2 ASN E 235  LEU E 239  1  O  ASN E 235   N  TRP E 211           
SHEET    1 AB2 6 THR F   6  THR F  11  0                                        
SHEET    2 AB2 6 LYS F  17  GLU F  23 -1  O  TYR F  20   N  GLY F   8           
SHEET    3 AB2 6 ARG F  55  PHE F  59 -1  O  VAL F  56   N  GLU F  23           
SHEET    4 AB2 6 ASP F  28  ILE F  32  1  N  LEU F  31   O  THR F  57           
SHEET    5 AB2 6 ALA F  99  CYS F 104  1  O  SER F 100   N  VAL F  30           
SHEET    6 AB2 6 VAL F 122  HIS F 128  1  O  MET F 126   N  VAL F 101           
SHEET    1 AB3 2 ASP F 210  GLY F 214  0                                        
SHEET    2 AB3 2 ASN F 235  LEU F 239  1  O  ASN F 235   N  TRP F 211           
SHEET    1 AB4 6 THR G   6  THR G  11  0                                        
SHEET    2 AB4 6 LYS G  17  GLU G  23 -1  O  TYR G  20   N  GLY G   8           
SHEET    3 AB4 6 ARG G  55  PHE G  59 -1  O  VAL G  56   N  GLU G  23           
SHEET    4 AB4 6 ASP G  28  ILE G  32  1  N  LEU G  31   O  THR G  57           
SHEET    5 AB4 6 ALA G  99  CYS G 104  1  O  SER G 100   N  VAL G  30           
SHEET    6 AB4 6 VAL G 122  HIS G 128  1  O  MET G 126   N  VAL G 101           
SHEET    1 AB5 2 ASP G 210  GLY G 214  0                                        
SHEET    2 AB5 2 ASN G 235  LEU G 239  1  O  ASN G 235   N  TRP G 211           
SHEET    1 AB6 6 ARG H   5  THR H  11  0                                        
SHEET    2 AB6 6 LYS H  17  GLU H  23 -1  O  TYR H  20   N  GLY H   8           
SHEET    3 AB6 6 ARG H  55  PHE H  59 -1  O  VAL H  56   N  GLU H  23           
SHEET    4 AB6 6 ASP H  28  ILE H  32  1  N  VAL H  29   O  THR H  57           
SHEET    5 AB6 6 ALA H  99  CYS H 104  1  O  SER H 100   N  VAL H  30           
SHEET    6 AB6 6 VAL H 122  HIS H 128  1  O  ASN H 124   N  VAL H 101           
SHEET    1 AB7 2 ASP H 210  GLY H 214  0                                        
SHEET    2 AB7 2 ASN H 235  LEU H 239  1  O  ASN H 235   N  TRP H 211           
SITE     1 AC1 10 GLY A  35  LEU A  36  ALA A 105  SER A 106                    
SITE     2 AC1 10 MET A 153  SER A 157  TRP A 185  PHE A 222                    
SITE     3 AC1 10 HIS A 243  HOH A 505                                          
SITE     1 AC2  9 ASP B  34  GLY B  35  ALA B 105  SER B 106                    
SITE     2 AC2  9 MET B 153  SER B 157  TYR B 160  TRP B 185                    
SITE     3 AC2  9 HIS B 243                                                     
CRYST1   76.012   96.887  101.895  88.96  87.70  87.96 P 1           8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013156 -0.000470 -0.000521        0.00000                         
SCALE2      0.000000  0.010328 -0.000174        0.00000                         
SCALE3      0.000000  0.000000  0.009823        0.00000                         
TER    2056      LYS A 266                                                      
TER    4112      LYS B 266                                                      
TER    6168      LYS C 266                                                      
TER    8224      LYS D 266                                                      
TER   10270      LEU E 265                                                      
TER   12292      LYS F 266                                                      
TER   14296      LYS G 266                                                      
TER   16352      LYS H 266                                                      
MASTER      416    0    2  119   64    0    6    616963    8   32  168          
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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