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LongText Report for: 8bhh-pdb

Name Class
8bhh-pdb
HEADER    HYDROLASE                               31-OCT-22   8BHH              
TITLE     THE CRYSTAL STRUCTURE OF A FERULOYL ESTERASE C FROM FUSARIUM OXYSPORUM
TITLE    2 IN COMPLEX WITH P-COUMARIC ACID                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.1.1.-;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: FUSARIUM OXYSPORUM;                             
SOURCE   3 ORGANISM_TAXID: 5507;                                                
SOURCE   4 GENE: FAEC;                                                          
SOURCE   5 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4922                                        
KEYWDS    FERULIC ACID ESTERASE, COUMMARIC ACID, TANNASE-LIKE, FERULOYL         
KEYWDS   2 ESTERASE, HYDROLASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.DIMAROGONA,E.TOPAKAS,C.KOSINAS,C.FEROUSI,E.NIKOLAIVITS              
REVDAT   1   05-JUL-23 8BHH    0                                                
JRNL        AUTH   C.KOSINAS,A.ZERVA,E.TOPAKAS,M.DIMAROGONA                     
JRNL        TITL   STRUCTURE-FUNCTION STUDIES OF A NOVEL LACCASE-LIKE           
JRNL        TITL 2 MULTICOPPER OXIDASE FROM THERMOTHELOMYCES THERMOPHILA        
JRNL        TITL 3 PROVIDE INSIGHTS INTO ITS BIOLOGICAL ROLE.                   
JRNL        REF    ACTA CRYSTALLOGR D STRUCT                  2023              
JRNL        REF  2 BIOL                                                         
JRNL        REFN                   ISSN 2059-7983                               
JRNL        PMID   37326583                                                     
JRNL        DOI    10.1107/S2059798323004175                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.69 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0267                                      
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) : 1.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 113.51                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 69.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 99895                          
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) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5158                            
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) : 1.69                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 637                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 5.98                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2900                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 30                           
REMARK   3   BIN FREE R VALUE                    : 0.2790                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7844                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 581                                     
REMARK   3   SOLVENT ATOMS            : 891                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.19000                                             
REMARK   3    B22 (A**2) : -0.31000                                             
REMARK   3    B33 (A**2) : 0.33000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.26000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.129         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.129         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.081         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.564         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8807 ; 0.013 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  7819 ; 0.002 ; 0.015       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11907 ; 1.831 ; 1.728       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 18132 ; 1.417 ; 1.649       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1029 ; 7.094 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   426 ;33.374 ;22.606       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1270 ;14.849 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    43 ;19.907 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1178 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9683 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2004 ; 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):  4090 ; 2.558 ; 2.806       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4088 ; 2.558 ; 2.806       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5120 ; 3.257 ; 4.196       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  5121 ; 3.257 ; 4.197       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4717 ; 3.416 ; 3.135       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4717 ; 3.416 ; 3.135       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  6786 ; 4.808 ; 4.572       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 10439 ; 6.049 ;34.609       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 10439 ; 6.050 ;34.609       
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 8BHH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-NOV-22.                  
REMARK 100 THE DEPOSITION ID IS D_1292126207.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-DEC-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PETRA III, EMBL C/O DESY           
REMARK 200  BEAMLINE                       : P13 (MX1)                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97624                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : AUTOPROCESS                        
REMARK 200  DATA SCALING SOFTWARE          : AUTOPROCESS                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 105053                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.690                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 113.510                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 69.5                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: 6FAT                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG400, TRIS HCL PH 8.5, VAPOR           
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293.15K                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       44.81850            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G, I                               
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     ASP A    36                                                      
REMARK 465     PHE A    37                                                      
REMARK 465     ALA A    38                                                      
REMARK 465     ALA A    39                                                      
REMARK 465     LYS A    40                                                      
REMARK 465     SER B   297                                                      
REMARK 465     LYS B   298                                                      
REMARK 465     GLY B   299                                                      
REMARK 465     GLN B   300                                                      
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   OG1  THR B   370     O    HOH B   701              2.03            
REMARK 500   O4   NAG G     2     O5   BMA G     3              2.04            
REMARK 500   O2   MAN C     8     C2   MAN C     9              2.09            
REMARK 500   O4   NAG E     1     O5   NAG E     2              2.13            
REMARK 500   O4   NAG C     1     O5   NAG C     2              2.16            
REMARK 500   O    HOH B  1101     O    HOH B  1197              2.18            
REMARK 500   NE2  GLN B   490     O    HOH B   702              2.19            
REMARK 500   O    SER A   297     O    HOH A   701              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O6   MAN I    10     O    HOH B  1078     2544     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B 422   CD    GLU B 422   OE1    -0.077                       
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    ARG A 229   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 314   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG A 526   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG B 229   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG B 229   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 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    GLU A  59      113.40   -167.53                                   
REMARK 500    TYR A 170      -33.42   -149.27                                   
REMARK 500    SER A 201     -111.90     72.25                                   
REMARK 500    ALA A 225       49.35     37.90                                   
REMARK 500    ALA A 227       34.17    -78.49                                   
REMARK 500    ASP A 270      -96.17    -86.28                                   
REMARK 500    LYS A 298      109.67    -49.78                                   
REMARK 500    TYR A 329      147.91   -170.59                                   
REMARK 500    ASN A 383       66.19     38.34                                   
REMARK 500    CYS A 453      -21.03     74.28                                   
REMARK 500    TYR B 170      -31.68   -150.16                                   
REMARK 500    SER B 201     -114.08     72.84                                   
REMARK 500    SER B 201     -124.40     69.08                                   
REMARK 500    ALA B 227       36.90    -78.00                                   
REMARK 500    ASP B 270      -93.04    -86.28                                   
REMARK 500    PHE B 441      -14.14   -144.66                                   
REMARK 500    CYS B 453      -19.49     73.20                                   
REMARK 500    LYS B 527      -53.99   -125.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 607  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 270   OD1                                                    
REMARK 620 2 ASP A 274   OD1 104.2                                              
REMARK 620 3 ASP A 274   OD2  97.5  54.6                                        
REMARK 620 4 VAL A 276   O    82.5  72.9 126.0                                  
REMARK 620 5 ASP A 278   OD1  94.1 140.4 157.0  75.1                            
REMARK 620 6 ILE A 280   O    79.7 131.7  77.1 152.7  85.6                      
REMARK 620 7 HOH A 824   O   163.3  91.1  85.9 108.6  77.5  85.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 614  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 270   OD1                                                    
REMARK 620 2 ASP B 274   OD1 103.7                                              
REMARK 620 3 ASP B 274   OD2  98.4  55.8                                        
REMARK 620 4 VAL B 276   O    78.0  78.5 132.2                                  
REMARK 620 5 ASP B 278   OD1  94.2 141.6 154.3  72.4                            
REMARK 620 6 ILE B 280   O    78.4 132.5  76.8 144.9  83.9                      
REMARK 620 7 HOH B 826   O   162.6  92.9  86.3 111.2  75.5  86.5                
REMARK 620 N                    1     2     3     4     5     6                 
DBREF1 8BHH A   36   543  UNP                  A0A1D3S5H0_FUSOX                 
DBREF2 8BHH A     A0A1D3S5H0                         36         543             
DBREF1 8BHH B   36   543  UNP                  A0A1D3S5H0_FUSOX                 
DBREF2 8BHH B     A0A1D3S5H0                         36         543             
SEQRES   1 A  508  ASP PHE ALA ALA LYS CYS ALA GLY PHE LYS THR SER LEU          
SEQRES   2 A  508  LYS LEU PRO ASN THR LYS VAL TRP PHE THR GLU HIS VAL          
SEQRES   3 A  508  PRO ALA GLY LYS ASN ILE THR PHE PRO ASP ASN HIS PRO          
SEQRES   4 A  508  THR CYS THR PRO LYS SER THR ILE THR ASP VAL GLU ILE          
SEQRES   5 A  508  CYS ARG VAL ALA MET PHE VAL THR THR GLY PRO LYS SER          
SEQRES   6 A  508  ASN LEU THR LEU GLU ALA TRP LEU PRO SER ASN TRP THR          
SEQRES   7 A  508  GLY ARG PHE LEU SER THR GLY ASN GLY GLY MET ALA GLY          
SEQRES   8 A  508  CYS ILE GLN TYR ASP ASP VAL ALA TYR GLY ALA GLY PHE          
SEQRES   9 A  508  GLY PHE ALA THR VAL GLY ALA ASN ASN GLY HIS ASN GLY          
SEQRES  10 A  508  THR SER ALA VAL SER MET TYR LYS ASN SER GLY VAL VAL          
SEQRES  11 A  508  GLU ASP TYR VAL TYR ARG SER VAL HIS THR GLY THR VAL          
SEQRES  12 A  508  LEU GLY LYS GLU LEU THR LYS LYS PHE TYR GLY LYS LYS          
SEQRES  13 A  508  HIS THR LYS SER TYR TYR LEU GLY CYS SER THR GLY GLY          
SEQRES  14 A  508  ARG GLN GLY TRP LYS GLU ALA GLN SER PHE PRO ASP ASP          
SEQRES  15 A  508  PHE ASP GLY ILE VAL ALA GLY ALA PRO ALA MET ARG PHE          
SEQRES  16 A  508  ASN GLY LEU GLN SER ARG SER GLY SER PHE TRP GLY ILE          
SEQRES  17 A  508  THR GLY PRO PRO GLY ALA PRO THR HIS LEU SER PRO GLU          
SEQRES  18 A  508  GLU TRP ALA MET VAL GLN LYS ASN VAL LEU VAL GLN CYS          
SEQRES  19 A  508  ASP GLU PRO LEU ASP GLY VAL ALA ASP GLY ILE LEU GLU          
SEQRES  20 A  508  ASP PRO ASN LEU CYS GLN TYR ARG PRO GLU ALA LEU VAL          
SEQRES  21 A  508  CYS SER LYS GLY GLN THR LYS ASN CYS LEU THR GLY PRO          
SEQRES  22 A  508  GLN ILE GLU THR VAL ARG LYS VAL PHE GLY PRO LEU TYR          
SEQRES  23 A  508  GLY ASN ASN GLY THR TYR ILE TYR PRO ARG ILE PRO PRO          
SEQRES  24 A  508  GLY ALA ASP GLN GLY PHE GLY PHE ALA ILE GLY GLU GLN          
SEQRES  25 A  508  PRO PHE PRO TYR SER THR GLU TRP PHE GLN TYR VAL ILE          
SEQRES  26 A  508  TRP ASN ASP THR LYS TRP ASP PRO ASN THR ILE GLY PRO          
SEQRES  27 A  508  ASN ASP TYR GLN LYS ALA SER GLU VAL ASN PRO PHE ASN          
SEQRES  28 A  508  VAL GLU THR TRP GLU GLY ASP LEU SER LYS PHE ARG LYS          
SEQRES  29 A  508  ARG GLY SER LYS ILE ILE HIS TRP HIS GLY LEU GLU ASP          
SEQRES  30 A  508  GLY LEU ILE SER SER ASP ASN SER MET GLU TYR TYR ASN          
SEQRES  31 A  508  HIS VAL SER ALA THR MET GLY LEU SER ASN THR GLU LEU          
SEQRES  32 A  508  ASP GLU PHE TYR ARG TYR PHE ARG VAL SER GLY CYS GLY          
SEQRES  33 A  508  HIS CYS SER GLY GLY ILE GLY ALA ASN ARG ILE GLY ASN          
SEQRES  34 A  508  ASN ARG ALA ASN LEU GLY GLY LYS GLU ALA LYS ASN ASN          
SEQRES  35 A  508  VAL LEU LEU ALA LEU VAL LYS TRP VAL GLU GLU GLY GLN          
SEQRES  36 A  508  ALA PRO GLU THR ILE THR GLY VAL ARG TYR VAL ASN GLY          
SEQRES  37 A  508  ALA THR THR GLY LYS VAL GLU VAL GLU ARG ARG HIS CYS          
SEQRES  38 A  508  ARG TYR PRO TYR ARG ASN VAL TRP ASP ARG LYS GLY ASN          
SEQRES  39 A  508  TYR LYS ASN PRO ASP SER TRP LYS CYS GLU LEU PRO LEU          
SEQRES  40 A  508  GLU                                                          
SEQRES   1 B  508  ASP PHE ALA ALA LYS CYS ALA GLY PHE LYS THR SER LEU          
SEQRES   2 B  508  LYS LEU PRO ASN THR LYS VAL TRP PHE THR GLU HIS VAL          
SEQRES   3 B  508  PRO ALA GLY LYS ASN ILE THR PHE PRO ASP ASN HIS PRO          
SEQRES   4 B  508  THR CYS THR PRO LYS SER THR ILE THR ASP VAL GLU ILE          
SEQRES   5 B  508  CYS ARG VAL ALA MET PHE VAL THR THR GLY PRO LYS SER          
SEQRES   6 B  508  ASN LEU THR LEU GLU ALA TRP LEU PRO SER ASN TRP THR          
SEQRES   7 B  508  GLY ARG PHE LEU SER THR GLY ASN GLY GLY MET ALA GLY          
SEQRES   8 B  508  CYS ILE GLN TYR ASP ASP VAL ALA TYR GLY ALA GLY PHE          
SEQRES   9 B  508  GLY PHE ALA THR VAL GLY ALA ASN ASN GLY HIS ASN GLY          
SEQRES  10 B  508  THR SER ALA VAL SER MET TYR LYS ASN SER GLY VAL VAL          
SEQRES  11 B  508  GLU ASP TYR VAL TYR ARG SER VAL HIS THR GLY THR VAL          
SEQRES  12 B  508  LEU GLY LYS GLU LEU THR LYS LYS PHE TYR GLY LYS LYS          
SEQRES  13 B  508  HIS THR LYS SER TYR TYR LEU GLY CYS SER THR GLY GLY          
SEQRES  14 B  508  ARG GLN GLY TRP LYS GLU ALA GLN SER PHE PRO ASP ASP          
SEQRES  15 B  508  PHE ASP GLY ILE VAL ALA GLY ALA PRO ALA MET ARG PHE          
SEQRES  16 B  508  ASN GLY LEU GLN SER ARG SER GLY SER PHE TRP GLY ILE          
SEQRES  17 B  508  THR GLY PRO PRO GLY ALA PRO THR HIS LEU SER PRO GLU          
SEQRES  18 B  508  GLU TRP ALA MET VAL GLN LYS ASN VAL LEU VAL GLN CYS          
SEQRES  19 B  508  ASP GLU PRO LEU ASP GLY VAL ALA ASP GLY ILE LEU GLU          
SEQRES  20 B  508  ASP PRO ASN LEU CYS GLN TYR ARG PRO GLU ALA LEU VAL          
SEQRES  21 B  508  CYS SER LYS GLY GLN THR LYS ASN CYS LEU THR GLY PRO          
SEQRES  22 B  508  GLN ILE GLU THR VAL ARG LYS VAL PHE GLY PRO LEU TYR          
SEQRES  23 B  508  GLY ASN ASN GLY THR TYR ILE TYR PRO ARG ILE PRO PRO          
SEQRES  24 B  508  GLY ALA ASP GLN GLY PHE GLY PHE ALA ILE GLY GLU GLN          
SEQRES  25 B  508  PRO PHE PRO TYR SER THR GLU TRP PHE GLN TYR VAL ILE          
SEQRES  26 B  508  TRP ASN ASP THR LYS TRP ASP PRO ASN THR ILE GLY PRO          
SEQRES  27 B  508  ASN ASP TYR GLN LYS ALA SER GLU VAL ASN PRO PHE ASN          
SEQRES  28 B  508  VAL GLU THR TRP GLU GLY ASP LEU SER LYS PHE ARG LYS          
SEQRES  29 B  508  ARG GLY SER LYS ILE ILE HIS TRP HIS GLY LEU GLU ASP          
SEQRES  30 B  508  GLY LEU ILE SER SER ASP ASN SER MET GLU TYR TYR ASN          
SEQRES  31 B  508  HIS VAL SER ALA THR MET GLY LEU SER ASN THR GLU LEU          
SEQRES  32 B  508  ASP GLU PHE TYR ARG TYR PHE ARG VAL SER GLY CYS GLY          
SEQRES  33 B  508  HIS CYS SER GLY GLY ILE GLY ALA ASN ARG ILE GLY ASN          
SEQRES  34 B  508  ASN ARG ALA ASN LEU GLY GLY LYS GLU ALA LYS ASN ASN          
SEQRES  35 B  508  VAL LEU LEU ALA LEU VAL LYS TRP VAL GLU GLU GLY GLN          
SEQRES  36 B  508  ALA PRO GLU THR ILE THR GLY VAL ARG TYR VAL ASN GLY          
SEQRES  37 B  508  ALA THR THR GLY LYS VAL GLU VAL GLU ARG ARG HIS CYS          
SEQRES  38 B  508  ARG TYR PRO TYR ARG ASN VAL TRP ASP ARG LYS GLY ASN          
SEQRES  39 B  508  TYR LYS ASN PRO ASP SER TRP LYS CYS GLU LEU PRO LEU          
SEQRES  40 B  508  GLU                                                          
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    BMA  C   3      11                                                       
HET    MAN  C   4      11                                                       
HET    MAN  C   5      11                                                       
HET    MAN  C   6      11                                                       
HET    MAN  C   7      11                                                       
HET    MAN  C   8      11                                                       
HET    MAN  C   9      11                                                       
HET    MAN  C  10      11                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    BMA  G   3      11                                                       
HET    MAN  G   4      11                                                       
HET    MAN  G   5      11                                                       
HET    MAN  G   6      11                                                       
HET    MAN  G   7      11                                                       
HET    MAN  G   8      11                                                       
HET    MAN  G   9      11                                                       
HET    MAN  G  10      11                                                       
HET    NAG  I   1      14                                                       
HET    NAG  I   2      14                                                       
HET    BMA  I   3      11                                                       
HET    MAN  I   4      11                                                       
HET    MAN  I   5      11                                                       
HET    MAN  I   6      11                                                       
HET    MAN  I   7      11                                                       
HET    MAN  I   8      11                                                       
HET    MAN  I   9      11                                                       
HET    MAN  I  10      11                                                       
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    BMA  E   3      11                                                       
HET    MAN  E   4      11                                                       
HET    MAN  E   5      11                                                       
HET    MAN  E   6      11                                                       
HET    HC4  A 601      12                                                       
HET    NAG  A 602      14                                                       
HET    EDO  A 603       4                                                       
HET    EDO  A 604       4                                                       
HET    EDO  A 605       4                                                       
HET    EDO  A 606       4                                                       
HET     CA  A 607       1                                                       
HET    PG4  B 601      13                                                       
HET    P6G  B 602      19                                                       
HET    NAG  B 603      14                                                       
HET    HC4  B 604      12                                                       
HET    EDO  B 605       4                                                       
HET    EDO  B 606       4                                                       
HET    EDO  B 607       4                                                       
HET    EDO  B 608       4                                                       
HET    PEG  B 609       7                                                       
HET    EDO  B 610       4                                                       
HET    NAG  B 611      14                                                       
HET    NAG  B 612      14                                                       
HET    EDO  B 613       4                                                       
HET     CA  B 614       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     HC4 4'-HYDROXYCINNAMIC ACID                                          
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      CA CALCIUM ION                                                      
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE                               
HETSYN     MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE                              
HETSYN     HC4 PARA-COUMARIC ACID                                               
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
FORMUL   3  NAG    12(C8 H15 N O6)                                              
FORMUL   3  BMA    4(C6 H12 O6)                                                 
FORMUL   3  MAN    24(C6 H12 O6)                                                
FORMUL   7  HC4    2(C9 H8 O3)                                                  
FORMUL   9  EDO    10(C2 H6 O2)                                                 
FORMUL  13   CA    2(CA 2+)                                                     
FORMUL  14  PG4    C8 H18 O5                                                    
FORMUL  15  P6G    C12 H26 O7                                                   
FORMUL  22  PEG    C4 H10 O3                                                    
FORMUL  28  HOH   *891(H2 O)                                                    
HELIX    1 AA1 GLY A   43  LEU A   48  1                                   6    
HELIX    2 AA2 GLN A  129  PHE A  139  1                                  11    
HELIX    3 AA3 ALA A  155  TYR A  159  5                                   5    
HELIX    4 AA4 ASN A  161  TYR A  170  1                                  10    
HELIX    5 AA5 TYR A  170  GLY A  189  1                                  20    
HELIX    6 AA6 SER A  201  PHE A  214  1                                  14    
HELIX    7 AA7 ARG A  229  GLY A  245  1                                  17    
HELIX    8 AA8 SER A  254  ASP A  270  1                                  17    
HELIX    9 AA9 ASP A  270  GLY A  275  1                                   6    
HELIX   10 AB1 ASP A  283  CYS A  287  5                                   5    
HELIX   11 AB2 ARG A  290  VAL A  295  5                                   6    
HELIX   12 AB3 THR A  306  PHE A  317  1                                  12    
HELIX   13 AB4 ASN A  323  GLY A  325  5                                   3    
HELIX   14 AB5 PHE A  349  VAL A  359  1                                  11    
HELIX   15 AB6 ASP A  367  ILE A  371  5                                   5    
HELIX   16 AB7 GLY A  372  ASN A  383  1                                  12    
HELIX   17 AB8 PRO A  384  VAL A  387  5                                   4    
HELIX   18 AB9 LEU A  394  ARG A  400  1                                   7    
HELIX   19 AC1 SER A  416  GLY A  432  1                                  17    
HELIX   20 AC2 SER A  434  ASP A  439  1                                   6    
HELIX   21 AC3 GLU A  473  ASN A  476  5                                   4    
HELIX   22 AC4 ASN A  477  GLY A  489  1                                  13    
HELIX   23 AC5 ASN A  502  ALA A  504  5                                   3    
HELIX   24 AC6 ASN A  532  ASP A  534  5                                   3    
HELIX   25 AC7 PHE B   37  LEU B   48  1                                  12    
HELIX   26 AC8 GLN B  129  PHE B  139  1                                  11    
HELIX   27 AC9 ALA B  155  TYR B  159  5                                   5    
HELIX   28 AD1 ASN B  161  TYR B  170  1                                  10    
HELIX   29 AD2 TYR B  170  GLY B  189  1                                  20    
HELIX   30 AD3 SER B  201  PHE B  214  1                                  14    
HELIX   31 AD4 ARG B  229  GLY B  245  1                                  17    
HELIX   32 AD5 SER B  254  ASP B  270  1                                  17    
HELIX   33 AD6 ASP B  270  GLY B  275  1                                   6    
HELIX   34 AD7 ASP B  283  CYS B  287  5                                   5    
HELIX   35 AD8 ARG B  290  VAL B  295  5                                   6    
HELIX   36 AD9 THR B  306  PHE B  317  1                                  12    
HELIX   37 AE1 ASN B  323  GLY B  325  5                                   3    
HELIX   38 AE2 PHE B  349  VAL B  359  1                                  11    
HELIX   39 AE3 ASP B  367  ILE B  371  5                                   5    
HELIX   40 AE4 GLY B  372  ASN B  383  1                                  12    
HELIX   41 AE5 PRO B  384  VAL B  387  5                                   4    
HELIX   42 AE6 LEU B  394  GLY B  401  1                                   8    
HELIX   43 AE7 SER B  416  GLY B  432  1                                  17    
HELIX   44 AE8 SER B  434  ASP B  439  1                                   6    
HELIX   45 AE9 ASN B  465  LEU B  469  5                                   5    
HELIX   46 AF1 GLU B  473  ASN B  476  5                                   4    
HELIX   47 AF2 ASN B  477  GLY B  489  1                                  13    
HELIX   48 AF3 ASN B  502  ALA B  504  5                                   3    
HELIX   49 AF4 ASN B  532  ASP B  534  5                                   3    
SHEET    1 AA1 3 THR A  53  PHE A  57  0                                        
SHEET    2 AA1 3 ILE A  87  GLY A  97 -1  O  PHE A  93   N  LYS A  54           
SHEET    3 AA1 3 HIS A  60  VAL A  61 -1  N  VAL A  61   O  ILE A  87           
SHEET    1 AA2 9 THR A  53  PHE A  57  0                                        
SHEET    2 AA2 9 ILE A  87  GLY A  97 -1  O  PHE A  93   N  LYS A  54           
SHEET    3 AA2 9 SER A 100  PRO A 109 -1  O  ALA A 106   N  VAL A  90           
SHEET    4 AA2 9 ALA A 142  ALA A 146 -1  O  THR A 143   N  TRP A 107           
SHEET    5 AA2 9 PHE A 116  SER A 118  1  N  LEU A 117   O  VAL A 144           
SHEET    6 AA2 9 SER A 195  CYS A 200  1  O  TYR A 196   N  SER A 118           
SHEET    7 AA2 9 GLY A 220  GLY A 224  1  O  GLY A 224   N  GLY A 199           
SHEET    8 AA2 9 LYS A 403  GLY A 409  1  O  ILE A 405   N  ILE A 221           
SHEET    9 AA2 9 TYR A 442  VAL A 447  1  O  ARG A 443   N  HIS A 406           
SHEET    1 AA3 2 ASN A  66  THR A  68  0                                        
SHEET    2 AA3 2 SER A  80  ILE A  82 -1  O  THR A  81   N  ILE A  67           
SHEET    1 AA4 2 LEU A 320  TYR A 321  0                                        
SHEET    2 AA4 2 TYR A 327  TYR A 329 -1  O  TYR A 329   N  LEU A 320           
SHEET    1 AA5 2 THR A 494  TYR A 500  0                                        
SHEET    2 AA5 2 VAL A 509  CYS A 516 -1  O  GLU A 510   N  ARG A 499           
SHEET    1 AA6 2 ARG A 521  TRP A 524  0                                        
SHEET    2 AA6 2 TRP A 536  GLU A 539 -1  O  GLU A 539   N  ARG A 521           
SHEET    1 AA7 9 THR B  53  VAL B  61  0                                        
SHEET    2 AA7 9 ILE B  87  GLY B  97 -1  O  ARG B  89   N  GLU B  59           
SHEET    3 AA7 9 SER B 100  PRO B 109 -1  O  ALA B 106   N  VAL B  90           
SHEET    4 AA7 9 ALA B 142  ALA B 146 -1  O  THR B 143   N  TRP B 107           
SHEET    5 AA7 9 PHE B 116  SER B 118  1  N  LEU B 117   O  VAL B 144           
SHEET    6 AA7 9 SER B 195  CYS B 200  1  O  TYR B 196   N  PHE B 116           
SHEET    7 AA7 9 GLY B 220  GLY B 224  1  O  VAL B 222   N  TYR B 197           
SHEET    8 AA7 9 LYS B 403  GLY B 409  1  O  ILE B 405   N  ILE B 221           
SHEET    9 AA7 9 TYR B 442  VAL B 447  1  O  PHE B 445   N  HIS B 406           
SHEET    1 AA8 2 ASN B  66  THR B  68  0                                        
SHEET    2 AA8 2 SER B  80  ILE B  82 -1  O  THR B  81   N  ILE B  67           
SHEET    1 AA9 2 LEU B 320  TYR B 321  0                                        
SHEET    2 AA9 2 TYR B 327  TYR B 329 -1  O  TYR B 329   N  LEU B 320           
SHEET    1 AB1 2 THR B 494  TYR B 500  0                                        
SHEET    2 AB1 2 VAL B 509  CYS B 516 -1  O  GLU B 510   N  ARG B 499           
SHEET    1 AB2 2 ARG B 521  TRP B 524  0                                        
SHEET    2 AB2 2 TRP B 536  GLU B 539 -1  O  GLU B 539   N  ARG B 521           
SSBOND   1 CYS A   41    CYS A   88                          1555   1555  2.11  
SSBOND   2 CYS A   76    CYS A  127                          1555   1555  2.11  
SSBOND   3 CYS A  200    CYS A  453                          1555   1555  2.07  
SSBOND   4 CYS A  269    CYS A  287                          1555   1555  2.10  
SSBOND   5 CYS A  296    CYS A  304                          1555   1555  2.10  
SSBOND   6 CYS A  516    CYS A  538                          1555   1555  2.09  
SSBOND   7 CYS B   41    CYS B   88                          1555   1555  2.19  
SSBOND   8 CYS B   76    CYS B  127                          1555   1555  2.15  
SSBOND   9 CYS B  200    CYS B  453                          1555   1555  2.17  
SSBOND  10 CYS B  269    CYS B  287                          1555   1555  2.11  
SSBOND  11 CYS B  296    CYS B  304                          1555   1555  2.11  
SSBOND  12 CYS B  516    CYS B  538                          1555   1555  2.04  
LINK         ND2 ASN A 101                 C1  NAG A 602     1555   1555  1.43  
LINK         ND2 ASN A 151                 C1  NAG E   1     1555   1555  1.43  
LINK         ND2 ASN A 362                 C1  NAG C   1     1555   1555  1.41  
LINK         ND2 ASN B  66                 C1  NAG B 611     1555   1555  1.45  
LINK         ND2 ASN B 101                 C1  NAG B 603     1555   1555  1.43  
LINK         ND2 ASN B 111                 C1  NAG B 612     1555   1555  1.45  
LINK         ND2 ASN B 151                 C1  NAG G   1     1555   1555  1.43  
LINK         ND2 ASN B 362                 C1  NAG I   1     1555   1555  1.45  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.43  
LINK         O4  NAG C   2                 C1  BMA C   3     1555   1555  1.46  
LINK         O3  BMA C   3                 C1  MAN C   4     1555   1555  1.37  
LINK         O6  BMA C   3                 C1  MAN C   7     1555   1555  1.53  
LINK         O2  MAN C   4                 C1  MAN C   5     1555   1555  1.46  
LINK         O2  MAN C   5                 C1  MAN C   6     1555   1555  1.45  
LINK         O6  MAN C   7                 C1  MAN C   8     1555   1555  1.43  
LINK         O3  MAN C   7                 C1  MAN C  10     1555   1555  1.45  
LINK         O2  MAN C   8                 C1  MAN C   9     1555   1555  1.46  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.45  
LINK         O4  NAG G   2                 C1  BMA G   3     1555   1555  1.51  
LINK         O3  BMA G   3                 C1  MAN G   4     1555   1555  1.36  
LINK         O6  BMA G   3                 C1  MAN G   7     1555   1555  1.40  
LINK         O2  MAN G   4                 C1  MAN G   5     1555   1555  1.38  
LINK         O2  MAN G   5                 C1  MAN G   6     1555   1555  1.46  
LINK         O6  MAN G   7                 C1  MAN G   8     1555   1555  1.44  
LINK         O3  MAN G   7                 C1  MAN G  10     1555   1555  1.41  
LINK         O2  MAN G   8                 C1  MAN G   9     1555   1555  1.44  
LINK         O4  NAG I   1                 C1  NAG I   2     1555   1555  1.41  
LINK         O4  NAG I   2                 C1  BMA I   3     1555   1555  1.49  
LINK         O3  BMA I   3                 C1  MAN I   4     1555   1555  1.43  
LINK         O6  BMA I   3                 C1  MAN I   7     1555   1555  1.45  
LINK         O2  MAN I   4                 C1  MAN I   5     1555   1555  1.45  
LINK         O2  MAN I   5                 C1  MAN I   6     1555   1555  1.41  
LINK         O6  MAN I   7                 C1  MAN I   8     1555   1555  1.38  
LINK         O3  MAN I   7                 C1  MAN I  10     1555   1555  1.43  
LINK         O2  MAN I   8                 C1  MAN I   9     1555   1555  1.42  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.45  
LINK         O4  NAG E   2                 C1  BMA E   3     1555   1555  1.51  
LINK         O6  BMA E   3                 C1  MAN E   4     1555   1555  1.34  
LINK         O6  MAN E   4                 C1  MAN E   5     1555   1555  1.35  
LINK         O2  MAN E   5                 C1  MAN E   6     1555   1555  1.47  
LINK         OD1 ASP A 270                CA    CA A 607     1555   1555  2.29  
LINK         OD1 ASP A 274                CA    CA A 607     1555   1555  2.39  
LINK         OD2 ASP A 274                CA    CA A 607     1555   1555  2.48  
LINK         O   VAL A 276                CA    CA A 607     1555   1555  2.38  
LINK         OD1 ASP A 278                CA    CA A 607     1555   1555  2.33  
LINK         O   ILE A 280                CA    CA A 607     1555   1555  2.31  
LINK        CA    CA A 607                 O   HOH A 824     1555   1555  2.39  
LINK         OD1 ASP B 270                CA    CA B 614     1555   1555  2.25  
LINK         OD1 ASP B 274                CA    CA B 614     1555   1555  2.36  
LINK         OD2 ASP B 274                CA    CA B 614     1555   1555  2.46  
LINK         O   VAL B 276                CA    CA B 614     1555   1555  2.41  
LINK         OD1 ASP B 278                CA    CA B 614     1555   1555  2.34  
LINK         O   ILE B 280                CA    CA B 614     1555   1555  2.33  
LINK        CA    CA B 614                 O   HOH B 826     1555   1555  2.41  
CISPEP   1 THR A   77    PRO A   78          0        -5.31                     
CISPEP   2 ALA A  125    GLY A  126          0        -9.06                     
CISPEP   3 TYR A  518    PRO A  519          0         1.26                     
CISPEP   4 THR B   77    PRO B   78          0        -3.35                     
CISPEP   5 ALA B  125    GLY B  126          0        -6.94                     
CISPEP   6 TYR B  518    PRO B  519          0         3.19                     
CRYST1   67.704   89.637  116.978  90.00 103.99  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014770  0.000000  0.003679        0.00000                         
SCALE2      0.000000  0.011156  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008810        0.00000                         
TER    3969      GLU A 543                                                      
TER    7940      GLU B 543                                                      
MASTER      390    0   57   49   37    0    0    6 9316    2  629   80          
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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