Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 5n4e-pdb

Name Class
5n4e-pdb
HEADER    HYDROLASE                               10-FEB-17   5N4E              
TITLE     PROLYL OLIGOPEPTIDASE B FROM GALERINA MARGINATA BOUND TO 35MER        
TITLE    2 HYDROLYSIS AND MACROCYCLIZATION SUBSTRATE - H698A MUTANT             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLYL OLIGOPEPTIDASE;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ALPHA-AMANITIN PROPROTEIN;                                 
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GALERINA MARGINATA;                             
SOURCE   3 ORGANISM_TAXID: 109633;                                              
SOURCE   4 GENE: POPB;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PJ411;                                    
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: GALERINA MARGINATA;                             
SOURCE  12 ORGANISM_TAXID: 109633                                               
KEYWDS    AMANITIN BIOSYNTHESIS, PROLYL OLIGOPEPTIDASE, HYDROLASE,              
KEYWDS   2 MACROCYCLASE, PEPTIDASE, BETA-PROPELLER, CLOSED FORM                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.M.CZEKSTER,S.A.MCMAHON,H.LUDEWIG,J.H.NAISMITH                       
REVDAT   1   01-NOV-17 5N4E    0                                                
JRNL        AUTH   C.M.CZEKSTER,H.LUDEWIG,S.A.MCMAHON,J.H.NAISMITH              
JRNL        TITL   CHARACTERIZATION OF A DUAL FUNCTION MACROCYCLASE ENABLES     
JRNL        TITL 2 DESIGN AND USE OF EFFICIENT MACROCYCLIZATION SUBSTRATES      
JRNL        REF    NAT COMMUN                                 2017              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        DOI    10.1038/S41467-017-00862-4                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 89.23                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 32664                          
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) : 0.251                           
REMARK   3   R VALUE            (WORKING SET) : 0.249                           
REMARK   3   FREE R VALUE                     : 0.295                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1690                            
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2247                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.03                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3560                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 114                          
REMARK   3   BIN FREE R VALUE                    : 0.4830                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11750                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 939                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.18000                                             
REMARK   3    B22 (A**2) : -2.87000                                             
REMARK   3    B33 (A**2) : 5.05000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.555         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.380         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.150        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.909                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.867                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12085 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 10806 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 16418 ; 1.101 ; 1.938       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 25114 ; 0.865 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1474 ; 5.890 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   581 ;34.109 ;24.337       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1916 ;12.341 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    55 ;12.376 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1739 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 13582 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2581 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5923 ; 1.541 ; 3.248       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  5922 ; 1.534 ; 3.248       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7388 ; 2.639 ; 4.864       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  7389 ; 2.640 ; 4.864       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6162 ; 1.349 ; 3.344       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  6162 ; 1.348 ; 3.344       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  9031 ; 2.313 ; 4.973       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 13745 ; 5.235 ;37.367       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 13745 ; 5.234 ;37.366       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 2                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     6    727       B     6    727   45368  0.09  0.05     
REMARK   3    2     C     2     35       D     2     35    1462  0.11  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.00                                          
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 5N4E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003502.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-OCT-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 91770                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.080                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 31.990                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.4                               
REMARK 200  DATA REDUNDANCY                : 1.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 2.8100                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 27% PEGMME2000, 90 MM BICINE PH 8.7,     
REMARK 280  100 MM POTASSIUM THIOCYANATE, AND 12.5MM HEXAMMINE COBALT           
REMARK 280  CHLORIDE. CRYSTALS WERE CRYOPROTECTED WITH 13% GLYCEROL., VAPOR     
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293.15K                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       49.59000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.72500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.50000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.72500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.59000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.50000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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: 4040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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 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     SER A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     ARG A   222                                                      
REMARK 465     GLU A   223                                                      
REMARK 465     ARG A   224                                                      
REMARK 465     HIS A   225                                                      
REMARK 465     GLU A   226                                                      
REMARK 465     GLY A   227                                                      
REMARK 465     THR A   228                                                      
REMARK 465     ARG A   229                                                      
REMARK 465     THR A   728                                                      
REMARK 465     VAL A   729                                                      
REMARK 465     GLU A   730                                                      
REMARK 465     MET A   731                                                      
REMARK 465     PHE A   732                                                      
REMARK 465     ASP A   733                                                      
REMARK 465     THR A   734                                                      
REMARK 465     ASN A   735                                                      
REMARK 465     ALA A   736                                                      
REMARK 465     THR A   737                                                      
REMARK 465     ARG A   738                                                      
REMARK 465     LEU A   739                                                      
REMARK 465     PRO A   740                                                      
REMARK 465     ILE A   741                                                      
REMARK 465     TRP A   742                                                      
REMARK 465     GLY A   743                                                      
REMARK 465     ILE A   744                                                      
REMARK 465     GLY A   745                                                      
REMARK 465     CYS A   746                                                      
REMARK 465     ASN A   747                                                      
REMARK 465     PRO A   748                                                      
REMARK 465     TRP A   749                                                      
REMARK 465     THR A   750                                                      
REMARK 465     ALA A   751                                                      
REMARK 465     GLU A   752                                                      
REMARK 465     HIS A   753                                                      
REMARK 465     VAL A   754                                                      
REMARK 465     ASP A   755                                                      
REMARK 465     GLN A   756                                                      
REMARK 465     THR A   757                                                      
REMARK 465     LEU A   758                                                      
REMARK 465     ALA A   759                                                      
REMARK 465     SER A   760                                                      
REMARK 465     GLY A   761                                                      
REMARK 465     ASN A   762                                                      
REMARK 465     ASP A   763                                                      
REMARK 465     ILE A   764                                                      
REMARK 465     CYS A   765                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     HIS B   163                                                      
REMARK 465     LEU B   164                                                      
REMARK 465     GLY B   165                                                      
REMARK 465     GLY B   166                                                      
REMARK 465     ASP B   167                                                      
REMARK 465     GLU B   223                                                      
REMARK 465     ARG B   224                                                      
REMARK 465     HIS B   225                                                      
REMARK 465     GLU B   226                                                      
REMARK 465     GLY B   227                                                      
REMARK 465     THR B   228                                                      
REMARK 465     ARG B   229                                                      
REMARK 465     SER B   230                                                      
REMARK 465     GLY B   699                                                      
REMARK 465     MET B   700                                                      
REMARK 465     THR B   728                                                      
REMARK 465     VAL B   729                                                      
REMARK 465     GLU B   730                                                      
REMARK 465     MET B   731                                                      
REMARK 465     PHE B   732                                                      
REMARK 465     ASP B   733                                                      
REMARK 465     THR B   734                                                      
REMARK 465     ASN B   735                                                      
REMARK 465     ALA B   736                                                      
REMARK 465     THR B   737                                                      
REMARK 465     ARG B   738                                                      
REMARK 465     LEU B   739                                                      
REMARK 465     PRO B   740                                                      
REMARK 465     ILE B   741                                                      
REMARK 465     TRP B   742                                                      
REMARK 465     GLY B   743                                                      
REMARK 465     ILE B   744                                                      
REMARK 465     GLY B   745                                                      
REMARK 465     CYS B   746                                                      
REMARK 465     ASN B   747                                                      
REMARK 465     PRO B   748                                                      
REMARK 465     TRP B   749                                                      
REMARK 465     THR B   750                                                      
REMARK 465     ALA B   751                                                      
REMARK 465     GLU B   752                                                      
REMARK 465     HIS B   753                                                      
REMARK 465     VAL B   754                                                      
REMARK 465     ASP B   755                                                      
REMARK 465     GLN B   756                                                      
REMARK 465     THR B   757                                                      
REMARK 465     LEU B   758                                                      
REMARK 465     ALA B   759                                                      
REMARK 465     SER B   760                                                      
REMARK 465     GLY B   761                                                      
REMARK 465     ASN B   762                                                      
REMARK 465     ASP B   763                                                      
REMARK 465     ILE B   764                                                      
REMARK 465     CYS B   765                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLY C    15                                                      
REMARK 465     CYS C    16                                                      
REMARK 465     ASN C    17                                                      
REMARK 465     PRO C    18                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ILE D    14                                                      
REMARK 465     GLY D    15                                                      
REMARK 465     CYS D    16                                                      
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    ASP A 190      -45.50    -27.89                                   
REMARK 500    ALA A 311      -48.81   -145.29                                   
REMARK 500    ALA A 332       75.21   -159.58                                   
REMARK 500    TYR A 335      160.76     68.01                                   
REMARK 500    GLU A 369      -50.31     67.21                                   
REMARK 500    GLU A 452      -57.56     69.43                                   
REMARK 500    TYR A 496      -63.52   -121.65                                   
REMARK 500    ARG A 543     -113.28     56.90                                   
REMARK 500    SER A 577      -96.44     67.92                                   
REMARK 500    ALA A 605      -43.52   -158.30                                   
REMARK 500    THR A 614     -121.75     36.82                                   
REMARK 500    MET A 667      -53.12    -26.96                                   
REMARK 500    TRP A 695       87.22    -67.67                                   
REMARK 500    ALA A 698       99.49    -69.54                                   
REMARK 500    ALA B 311      -48.82   -144.95                                   
REMARK 500    ALA B 332       75.22   -159.61                                   
REMARK 500    TYR B 335      160.46     68.33                                   
REMARK 500    GLU B 369      -50.10     66.82                                   
REMARK 500    GLU B 452      -57.23     69.28                                   
REMARK 500    TYR B 496      -63.62   -121.93                                   
REMARK 500    ARG B 543     -112.78     57.08                                   
REMARK 500    SER B 577      -96.60     68.04                                   
REMARK 500    ALA B 605      -43.08   -158.18                                   
REMARK 500    THR B 614     -123.40     38.86                                   
REMARK 500    MET B 667      -53.19    -26.99                                   
REMARK 500    TRP B 695       90.78    -65.81                                   
REMARK 500    VAL C  24      -48.65    -25.25                                   
REMARK 500    VAL D  24      -49.01    -26.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1257        DISTANCE =  5.99 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 801                 
DBREF  5N4E A    1   730  UNP    H2E7Q8   H2E7Q8_9AGAR     1    730             
DBREF  5N4E B    1   730  UNP    H2E7Q8   H2E7Q8_9AGAR     1    730             
DBREF  5N4E C    1    35  UNP    H2E7Q5   H2E7Q5_9AGAR     1     35             
DBREF  5N4E D    1    35  UNP    H2E7Q5   H2E7Q5_9AGAR     1     35             
SEQADV 5N4E ALA A  698  UNP  H2E7Q8    HIS   698 ENGINEERED MUTATION            
SEQADV 5N4E MET A  731  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E PHE A  732  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ASP A  733  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E THR A  734  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ASN A  735  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ALA A  736  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E THR A  737  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ARG A  738  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E LEU A  739  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E PRO A  740  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ILE A  741  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E TRP A  742  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E GLY A  743  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ILE A  744  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E GLY A  745  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E CYS A  746  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ASN A  747  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E PRO A  748  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E TRP A  749  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E THR A  750  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ALA A  751  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E GLU A  752  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E HIS A  753  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E VAL A  754  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ASP A  755  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E GLN A  756  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E THR A  757  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E LEU A  758  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ALA A  759  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E SER A  760  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E GLY A  761  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ASN A  762  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ASP A  763  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ILE A  764  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E CYS A  765  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ALA B  698  UNP  H2E7Q8    HIS   698 ENGINEERED MUTATION            
SEQADV 5N4E MET B  731  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E PHE B  732  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ASP B  733  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E THR B  734  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ASN B  735  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ALA B  736  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E THR B  737  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ARG B  738  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E LEU B  739  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E PRO B  740  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ILE B  741  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E TRP B  742  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E GLY B  743  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ILE B  744  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E GLY B  745  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E CYS B  746  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ASN B  747  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E PRO B  748  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E TRP B  749  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E THR B  750  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ALA B  751  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E GLU B  752  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E HIS B  753  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E VAL B  754  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ASP B  755  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E GLN B  756  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E THR B  757  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E LEU B  758  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ALA B  759  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E SER B  760  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E GLY B  761  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ASN B  762  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ASP B  763  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E ILE B  764  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4E CYS B  765  UNP  H2E7Q8              EXPRESSION TAG                 
SEQRES   1 A  765  MET SER SER VAL THR TRP ALA PRO GLY ASN TYR PRO SER          
SEQRES   2 A  765  THR ARG ARG SER ASP HIS VAL ASP THR TYR GLN SER ALA          
SEQRES   3 A  765  SER LYS GLY GLU VAL PRO VAL PRO ASP PRO TYR GLN TRP          
SEQRES   4 A  765  LEU GLU GLU SER THR ASP GLU VAL ASP LYS TRP THR THR          
SEQRES   5 A  765  ALA GLN ALA ASP LEU ALA GLN SER TYR LEU ASP GLN ASN          
SEQRES   6 A  765  ALA ASP ILE GLN LYS LEU ALA GLU LYS PHE ARG ALA SER          
SEQRES   7 A  765  ARG ASN TYR ALA LYS PHE SER ALA PRO THR LEU LEU ASP          
SEQRES   8 A  765  ASP GLY HIS TRP TYR TRP PHE TYR ASN ARG GLY LEU GLN          
SEQRES   9 A  765  SER GLN SER VAL LEU TYR ARG SER LYS GLU PRO ALA LEU          
SEQRES  10 A  765  PRO ASP PHE SER LYS GLY ASP ASP ASN VAL GLY ASP VAL          
SEQRES  11 A  765  PHE PHE ASP PRO ASN VAL LEU ALA ALA ASP GLY SER ALA          
SEQRES  12 A  765  GLY MET VAL LEU CYS LYS PHE SER PRO ASP GLY LYS PHE          
SEQRES  13 A  765  PHE ALA TYR ALA VAL SER HIS LEU GLY GLY ASP TYR SER          
SEQRES  14 A  765  THR ILE TYR VAL ARG SER THR SER SER PRO LEU SER GLN          
SEQRES  15 A  765  ALA SER VAL ALA GLN GLY VAL ASP GLY ARG LEU SER ASP          
SEQRES  16 A  765  GLU VAL LYS TRP PHE LYS PHE SER THR ILE ILE TRP THR          
SEQRES  17 A  765  LYS ASP SER LYS GLY PHE LEU TYR GLN ARG TYR PRO ALA          
SEQRES  18 A  765  ARG GLU ARG HIS GLU GLY THR ARG SER ASP ARG ASN ALA          
SEQRES  19 A  765  MET MET CYS TYR HIS LYS VAL GLY THR THR GLN GLU GLU          
SEQRES  20 A  765  ASP ILE ILE VAL TYR GLN ASP ASN GLU HIS PRO GLU TRP          
SEQRES  21 A  765  ILE TYR GLY ALA ASP THR SER GLU ASP GLY LYS TYR LEU          
SEQRES  22 A  765  TYR LEU TYR GLN PHE LYS ASP THR SER LYS LYS ASN LEU          
SEQRES  23 A  765  LEU TRP VAL ALA GLU LEU ASP GLU ASP GLY VAL LYS SER          
SEQRES  24 A  765  GLY ILE HIS TRP ARG LYS VAL VAL ASN GLU TYR ALA ALA          
SEQRES  25 A  765  ASP TYR ASN ILE ILE THR ASN HIS GLY SER LEU VAL TYR          
SEQRES  26 A  765  ILE LYS THR ASN LEU ASN ALA PRO GLN TYR LYS VAL ILE          
SEQRES  27 A  765  THR ILE ASP LEU SER LYS ASP GLU PRO GLU ILE ARG ASP          
SEQRES  28 A  765  PHE ILE PRO GLU GLU LYS ASP ALA LYS LEU ALA GLN VAL          
SEQRES  29 A  765  ASN CYS ALA ASN GLU GLU TYR PHE VAL ALA ILE TYR LYS          
SEQRES  30 A  765  ARG ASN VAL LYS ASP GLU ILE TYR LEU TYR SER LYS ALA          
SEQRES  31 A  765  GLY VAL GLN LEU THR ARG LEU ALA PRO ASP PHE VAL GLY          
SEQRES  32 A  765  ALA ALA SER ILE ALA ASN ARG GLN LYS GLN THR HIS PHE          
SEQRES  33 A  765  PHE LEU THR LEU SER GLY PHE ASN THR PRO GLY THR ILE          
SEQRES  34 A  765  ALA ARG TYR ASP PHE THR ALA PRO GLU THR GLN ARG PHE          
SEQRES  35 A  765  SER ILE LEU ARG THR THR LYS VAL ASN GLU LEU ASP PRO          
SEQRES  36 A  765  ASP ASP PHE GLU SER THR GLN VAL TRP TYR GLU SER LYS          
SEQRES  37 A  765  ASP GLY THR LYS ILE PRO MET PHE ILE VAL ARG HIS LYS          
SEQRES  38 A  765  SER THR LYS PHE ASP GLY THR ALA ALA ALA ILE GLN TYR          
SEQRES  39 A  765  GLY TYR GLY GLY PHE ALA THR SER ALA ASP PRO PHE PHE          
SEQRES  40 A  765  SER PRO ILE ILE LEU THR PHE LEU GLN THR TYR GLY ALA          
SEQRES  41 A  765  ILE PHE ALA VAL PRO SER ILE ARG GLY GLY GLY GLU PHE          
SEQRES  42 A  765  GLY GLU GLU TRP HIS LYS GLY GLY ARG ARG GLU THR LYS          
SEQRES  43 A  765  VAL ASN THR PHE ASP ASP PHE ILE ALA ALA ALA GLN PHE          
SEQRES  44 A  765  LEU VAL LYS ASN LYS TYR ALA ALA PRO GLY LYS VAL ALA          
SEQRES  45 A  765  ILE ASN GLY ALA SER ASN GLY GLY LEU LEU VAL MET GLY          
SEQRES  46 A  765  SER ILE VAL ARG ALA PRO GLU GLY THR PHE GLY ALA ALA          
SEQRES  47 A  765  VAL PRO GLU GLY GLY VAL ALA ASP LEU LEU LYS PHE HIS          
SEQRES  48 A  765  LYS PHE THR GLY GLY GLN ALA TRP ILE SER GLU TYR GLY          
SEQRES  49 A  765  ASN PRO SER ILE PRO GLU GLU PHE ASP TYR ILE TYR PRO          
SEQRES  50 A  765  LEU SER PRO VAL HIS ASN VAL ARG THR ASP LYS VAL MET          
SEQRES  51 A  765  PRO ALA THR LEU ILE THR VAL ASN ILE GLY ASP GLY ARG          
SEQRES  52 A  765  VAL VAL PRO MET HIS SER PHE LYS PHE ILE ALA THR LEU          
SEQRES  53 A  765  GLN HIS ASN VAL PRO GLN ASN PRO HIS PRO LEU LEU ILE          
SEQRES  54 A  765  LYS ILE ASP LYS SER TRP LEU GLY ALA GLY MET GLY LYS          
SEQRES  55 A  765  PRO THR ASP LYS ASN VAL LYS ASP ALA ALA ASP LYS TRP          
SEQRES  56 A  765  GLY PHE ILE ALA ARG ALA LEU GLY LEU GLU LEU LYS THR          
SEQRES  57 A  765  VAL GLU MET PHE ASP THR ASN ALA THR ARG LEU PRO ILE          
SEQRES  58 A  765  TRP GLY ILE GLY CYS ASN PRO TRP THR ALA GLU HIS VAL          
SEQRES  59 A  765  ASP GLN THR LEU ALA SER GLY ASN ASP ILE CYS                  
SEQRES   1 B  765  MET SER SER VAL THR TRP ALA PRO GLY ASN TYR PRO SER          
SEQRES   2 B  765  THR ARG ARG SER ASP HIS VAL ASP THR TYR GLN SER ALA          
SEQRES   3 B  765  SER LYS GLY GLU VAL PRO VAL PRO ASP PRO TYR GLN TRP          
SEQRES   4 B  765  LEU GLU GLU SER THR ASP GLU VAL ASP LYS TRP THR THR          
SEQRES   5 B  765  ALA GLN ALA ASP LEU ALA GLN SER TYR LEU ASP GLN ASN          
SEQRES   6 B  765  ALA ASP ILE GLN LYS LEU ALA GLU LYS PHE ARG ALA SER          
SEQRES   7 B  765  ARG ASN TYR ALA LYS PHE SER ALA PRO THR LEU LEU ASP          
SEQRES   8 B  765  ASP GLY HIS TRP TYR TRP PHE TYR ASN ARG GLY LEU GLN          
SEQRES   9 B  765  SER GLN SER VAL LEU TYR ARG SER LYS GLU PRO ALA LEU          
SEQRES  10 B  765  PRO ASP PHE SER LYS GLY ASP ASP ASN VAL GLY ASP VAL          
SEQRES  11 B  765  PHE PHE ASP PRO ASN VAL LEU ALA ALA ASP GLY SER ALA          
SEQRES  12 B  765  GLY MET VAL LEU CYS LYS PHE SER PRO ASP GLY LYS PHE          
SEQRES  13 B  765  PHE ALA TYR ALA VAL SER HIS LEU GLY GLY ASP TYR SER          
SEQRES  14 B  765  THR ILE TYR VAL ARG SER THR SER SER PRO LEU SER GLN          
SEQRES  15 B  765  ALA SER VAL ALA GLN GLY VAL ASP GLY ARG LEU SER ASP          
SEQRES  16 B  765  GLU VAL LYS TRP PHE LYS PHE SER THR ILE ILE TRP THR          
SEQRES  17 B  765  LYS ASP SER LYS GLY PHE LEU TYR GLN ARG TYR PRO ALA          
SEQRES  18 B  765  ARG GLU ARG HIS GLU GLY THR ARG SER ASP ARG ASN ALA          
SEQRES  19 B  765  MET MET CYS TYR HIS LYS VAL GLY THR THR GLN GLU GLU          
SEQRES  20 B  765  ASP ILE ILE VAL TYR GLN ASP ASN GLU HIS PRO GLU TRP          
SEQRES  21 B  765  ILE TYR GLY ALA ASP THR SER GLU ASP GLY LYS TYR LEU          
SEQRES  22 B  765  TYR LEU TYR GLN PHE LYS ASP THR SER LYS LYS ASN LEU          
SEQRES  23 B  765  LEU TRP VAL ALA GLU LEU ASP GLU ASP GLY VAL LYS SER          
SEQRES  24 B  765  GLY ILE HIS TRP ARG LYS VAL VAL ASN GLU TYR ALA ALA          
SEQRES  25 B  765  ASP TYR ASN ILE ILE THR ASN HIS GLY SER LEU VAL TYR          
SEQRES  26 B  765  ILE LYS THR ASN LEU ASN ALA PRO GLN TYR LYS VAL ILE          
SEQRES  27 B  765  THR ILE ASP LEU SER LYS ASP GLU PRO GLU ILE ARG ASP          
SEQRES  28 B  765  PHE ILE PRO GLU GLU LYS ASP ALA LYS LEU ALA GLN VAL          
SEQRES  29 B  765  ASN CYS ALA ASN GLU GLU TYR PHE VAL ALA ILE TYR LYS          
SEQRES  30 B  765  ARG ASN VAL LYS ASP GLU ILE TYR LEU TYR SER LYS ALA          
SEQRES  31 B  765  GLY VAL GLN LEU THR ARG LEU ALA PRO ASP PHE VAL GLY          
SEQRES  32 B  765  ALA ALA SER ILE ALA ASN ARG GLN LYS GLN THR HIS PHE          
SEQRES  33 B  765  PHE LEU THR LEU SER GLY PHE ASN THR PRO GLY THR ILE          
SEQRES  34 B  765  ALA ARG TYR ASP PHE THR ALA PRO GLU THR GLN ARG PHE          
SEQRES  35 B  765  SER ILE LEU ARG THR THR LYS VAL ASN GLU LEU ASP PRO          
SEQRES  36 B  765  ASP ASP PHE GLU SER THR GLN VAL TRP TYR GLU SER LYS          
SEQRES  37 B  765  ASP GLY THR LYS ILE PRO MET PHE ILE VAL ARG HIS LYS          
SEQRES  38 B  765  SER THR LYS PHE ASP GLY THR ALA ALA ALA ILE GLN TYR          
SEQRES  39 B  765  GLY TYR GLY GLY PHE ALA THR SER ALA ASP PRO PHE PHE          
SEQRES  40 B  765  SER PRO ILE ILE LEU THR PHE LEU GLN THR TYR GLY ALA          
SEQRES  41 B  765  ILE PHE ALA VAL PRO SER ILE ARG GLY GLY GLY GLU PHE          
SEQRES  42 B  765  GLY GLU GLU TRP HIS LYS GLY GLY ARG ARG GLU THR LYS          
SEQRES  43 B  765  VAL ASN THR PHE ASP ASP PHE ILE ALA ALA ALA GLN PHE          
SEQRES  44 B  765  LEU VAL LYS ASN LYS TYR ALA ALA PRO GLY LYS VAL ALA          
SEQRES  45 B  765  ILE ASN GLY ALA SER ASN GLY GLY LEU LEU VAL MET GLY          
SEQRES  46 B  765  SER ILE VAL ARG ALA PRO GLU GLY THR PHE GLY ALA ALA          
SEQRES  47 B  765  VAL PRO GLU GLY GLY VAL ALA ASP LEU LEU LYS PHE HIS          
SEQRES  48 B  765  LYS PHE THR GLY GLY GLN ALA TRP ILE SER GLU TYR GLY          
SEQRES  49 B  765  ASN PRO SER ILE PRO GLU GLU PHE ASP TYR ILE TYR PRO          
SEQRES  50 B  765  LEU SER PRO VAL HIS ASN VAL ARG THR ASP LYS VAL MET          
SEQRES  51 B  765  PRO ALA THR LEU ILE THR VAL ASN ILE GLY ASP GLY ARG          
SEQRES  52 B  765  VAL VAL PRO MET HIS SER PHE LYS PHE ILE ALA THR LEU          
SEQRES  53 B  765  GLN HIS ASN VAL PRO GLN ASN PRO HIS PRO LEU LEU ILE          
SEQRES  54 B  765  LYS ILE ASP LYS SER TRP LEU GLY ALA GLY MET GLY LYS          
SEQRES  55 B  765  PRO THR ASP LYS ASN VAL LYS ASP ALA ALA ASP LYS TRP          
SEQRES  56 B  765  GLY PHE ILE ALA ARG ALA LEU GLY LEU GLU LEU LYS THR          
SEQRES  57 B  765  VAL GLU MET PHE ASP THR ASN ALA THR ARG LEU PRO ILE          
SEQRES  58 B  765  TRP GLY ILE GLY CYS ASN PRO TRP THR ALA GLU HIS VAL          
SEQRES  59 B  765  ASP GLN THR LEU ALA SER GLY ASN ASP ILE CYS                  
SEQRES   1 C   35  MET PHE ASP THR ASN ALA THR ARG LEU PRO ILE TRP GLY          
SEQRES   2 C   35  ILE GLY CYS ASN PRO TRP THR ALA GLU HIS VAL ASP GLN          
SEQRES   3 C   35  THR LEU ALA SER GLY ASN ASP ILE CYS                          
SEQRES   1 D   35  MET PHE ASP THR ASN ALA THR ARG LEU PRO ILE TRP GLY          
SEQRES   2 D   35  ILE GLY CYS ASN PRO TRP THR ALA GLU HIS VAL ASP GLN          
SEQRES   3 D   35  THR LEU ALA SER GLY ASN ASP ILE CYS                          
HET    GOL  B 801       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  GOL    C3 H8 O3                                                     
FORMUL   6  HOH   *939(H2 O)                                                    
HELIX    1 AA1 TYR A   37  GLU A   42  5                                   6    
HELIX    2 AA2 THR A   44  GLN A   64  1                                  21    
HELIX    3 AA3 ALA A   66  ASN A   80  1                                  15    
HELIX    4 AA4 ASP A  119  LYS A  122  5                                   4    
HELIX    5 AA5 GLY A  123  VAL A  127  1                                   5    
HELIX    6 AA6 ASP A  133  LEU A  137  5                                   5    
HELIX    7 AA7 SER A  181  GLY A  188  1                                   8    
HELIX    8 AA8 THR A  244  ASP A  248  5                                   5    
HELIX    9 AA9 PRO A  437  GLN A  440  5                                   4    
HELIX   10 AB1 ASP A  454  ASP A  456  5                                   3    
HELIX   11 AB2 SER A  508  GLY A  519  1                                  12    
HELIX   12 AB3 GLY A  534  GLY A  540  1                                   7    
HELIX   13 AB4 GLY A  541  THR A  545  5                                   5    
HELIX   14 AB5 LYS A  546  ASN A  563  1                                  18    
HELIX   15 AB6 SER A  577  ALA A  590  1                                  14    
HELIX   16 AB7 LYS A  609  PHE A  613  5                                   5    
HELIX   17 AB8 GLY A  615  ALA A  618  5                                   4    
HELIX   18 AB9 TRP A  619  GLY A  624  1                                   6    
HELIX   19 AC1 ILE A  628  TYR A  636  1                                   9    
HELIX   20 AC2 SER A  639  ASN A  643  5                                   5    
HELIX   21 AC3 PRO A  666  VAL A  680  1                                  15    
HELIX   22 AC4 PRO A  703  LEU A  722  1                                  20    
HELIX   23 AC5 TYR B   37  GLU B   42  5                                   6    
HELIX   24 AC6 THR B   44  GLN B   64  1                                  21    
HELIX   25 AC7 ALA B   66  ASN B   80  1                                  15    
HELIX   26 AC8 ASP B  119  LYS B  122  5                                   4    
HELIX   27 AC9 GLY B  123  VAL B  127  1                                   5    
HELIX   28 AD1 ASP B  133  LEU B  137  5                                   5    
HELIX   29 AD2 SER B  181  GLY B  188  1                                   8    
HELIX   30 AD3 THR B  244  ASP B  248  5                                   5    
HELIX   31 AD4 PRO B  437  GLN B  440  5                                   4    
HELIX   32 AD5 ASP B  454  ASP B  456  5                                   3    
HELIX   33 AD6 SER B  508  GLY B  519  1                                  12    
HELIX   34 AD7 GLY B  534  GLY B  540  1                                   7    
HELIX   35 AD8 GLY B  541  THR B  545  5                                   5    
HELIX   36 AD9 LYS B  546  ASN B  563  1                                  18    
HELIX   37 AE1 SER B  577  ALA B  590  1                                  14    
HELIX   38 AE2 LYS B  609  PHE B  613  5                                   5    
HELIX   39 AE3 GLY B  615  ALA B  618  5                                   4    
HELIX   40 AE4 TRP B  619  GLY B  624  1                                   6    
HELIX   41 AE5 ILE B  628  TYR B  636  1                                   9    
HELIX   42 AE6 SER B  639  ASN B  643  5                                   5    
HELIX   43 AE7 PRO B  666  VAL B  680  1                                  15    
HELIX   44 AE8 PRO B  703  LEU B  722  1                                  20    
HELIX   45 AE9 THR C    4  LEU C    9  5                                   6    
HELIX   46 AF1 THR C   20  VAL C   24  5                                   5    
HELIX   47 AF2 THR D    4  LEU D    9  5                                   6    
HELIX   48 AF3 THR D   20  VAL D   24  5                                   5    
SHEET    1 AA1 2 VAL A  20  SER A  25  0                                        
SHEET    2 AA1 2 GLY A  29  PRO A  34 -1  O  GLY A  29   N  SER A  25           
SHEET    1 AA2 3 LYS A  83  PHE A  84  0                                        
SHEET    2 AA2 3 TRP A  95  ASN A 100 -1  O  ASN A 100   N  LYS A  83           
SHEET    3 AA2 3 THR A  88  LEU A  89 -1  N  THR A  88   O  TYR A  96           
SHEET    1 AA3 4 LYS A  83  PHE A  84  0                                        
SHEET    2 AA3 4 TRP A  95  ASN A 100 -1  O  ASN A 100   N  LYS A  83           
SHEET    3 AA3 4 VAL A 108  SER A 112 -1  O  TYR A 110   N  TRP A  97           
SHEET    4 AA3 4 GLY A 128  PHE A 132 -1  O  PHE A 132   N  LEU A 109           
SHEET    1 AA4 4 GLY A 144  PHE A 150  0                                        
SHEET    2 AA4 4 PHE A 156  SER A 162 -1  O  SER A 162   N  GLY A 144           
SHEET    3 AA4 4 SER A 169  SER A 175 -1  O  THR A 170   N  VAL A 161           
SHEET    4 AA4 4 VAL A 197  PHE A 200 -1  O  VAL A 197   N  ILE A 171           
SHEET    1 AA5 4 ILE A 206  TRP A 207  0                                        
SHEET    2 AA5 4 GLY A 213  ARG A 218 -1  O  LEU A 215   N  ILE A 206           
SHEET    3 AA5 4 MET A 235  LYS A 240 -1  O  CYS A 237   N  TYR A 216           
SHEET    4 AA5 4 ILE A 249  TYR A 252 -1  O  TYR A 252   N  MET A 236           
SHEET    1 AA6 4 ILE A 261  THR A 266  0                                        
SHEET    2 AA6 4 TYR A 272  PHE A 278 -1  O  TYR A 274   N  ASP A 265           
SHEET    3 AA6 4 ASN A 285  GLU A 291 -1  O  ALA A 290   N  LEU A 273           
SHEET    4 AA6 4 ARG A 304  VAL A 307 -1  O  ARG A 304   N  VAL A 289           
SHEET    1 AA7 4 TYR A 314  HIS A 320  0                                        
SHEET    2 AA7 4 LEU A 323  THR A 328 -1  O  TYR A 325   N  ILE A 317           
SHEET    3 AA7 4 LYS A 336  ASP A 341 -1  O  LYS A 336   N  THR A 328           
SHEET    4 AA7 4 GLU A 348  ILE A 353 -1  O  PHE A 352   N  VAL A 337           
SHEET    1 AA8 4 LYS A 360  ALA A 367  0                                        
SHEET    2 AA8 4 TYR A 371  ARG A 378 -1  O  VAL A 373   N  ASN A 365           
SHEET    3 AA8 4 LYS A 381  TYR A 387 -1  O  TYR A 387   N  PHE A 372           
SHEET    4 AA8 4 GLN A 393  LEU A 397 -1  O  LEU A 397   N  ILE A 384           
SHEET    1 AA9 4 ALA A 404  ALA A 408  0                                        
SHEET    2 AA9 4 HIS A 415  GLY A 422 -1  O  PHE A 417   N  ALA A 408           
SHEET    3 AA9 4 THR A 425  ASP A 433 -1  O  THR A 428   N  LEU A 420           
SHEET    4 AA9 4 PHE A 442  THR A 447 -1  O  ARG A 446   N  ILE A 429           
SHEET    1 AB1 8 PHE A 458  GLU A 466  0                                        
SHEET    2 AB1 8 LYS A 472  HIS A 480 -1  O  ILE A 473   N  TYR A 465           
SHEET    3 AB1 8 ILE A 521  PRO A 525 -1  O  PHE A 522   N  VAL A 478           
SHEET    4 AB1 8 ALA A 491  TYR A 494  1  N  ILE A 492   O  ALA A 523           
SHEET    5 AB1 8 VAL A 571  ALA A 576  1  O  ALA A 572   N  GLN A 493           
SHEET    6 AB1 8 ALA A 597  GLU A 601  1  O  GLU A 601   N  GLY A 575           
SHEET    7 AB1 8 ALA A 652  ASN A 658  1  O  THR A 656   N  PRO A 600           
SHEET    8 AB1 8 LEU A 687  ASP A 692  1  O  LYS A 690   N  ILE A 655           
SHEET    1 AB2 2 VAL B  20  SER B  25  0                                        
SHEET    2 AB2 2 GLY B  29  PRO B  34 -1  O  GLY B  29   N  SER B  25           
SHEET    1 AB3 3 LYS B  83  PHE B  84  0                                        
SHEET    2 AB3 3 TRP B  95  ASN B 100 -1  O  ASN B 100   N  LYS B  83           
SHEET    3 AB3 3 THR B  88  LEU B  89 -1  N  THR B  88   O  TYR B  96           
SHEET    1 AB4 4 LYS B  83  PHE B  84  0                                        
SHEET    2 AB4 4 TRP B  95  ASN B 100 -1  O  ASN B 100   N  LYS B  83           
SHEET    3 AB4 4 VAL B 108  SER B 112 -1  O  TYR B 110   N  TRP B  97           
SHEET    4 AB4 4 GLY B 128  PHE B 132 -1  O  PHE B 132   N  LEU B 109           
SHEET    1 AB5 4 GLY B 144  PHE B 150  0                                        
SHEET    2 AB5 4 PHE B 156  SER B 162 -1  O  SER B 162   N  GLY B 144           
SHEET    3 AB5 4 SER B 169  SER B 175 -1  O  THR B 170   N  VAL B 161           
SHEET    4 AB5 4 GLU B 196  PHE B 200 -1  O  VAL B 197   N  ILE B 171           
SHEET    1 AB6 4 ILE B 206  TRP B 207  0                                        
SHEET    2 AB6 4 GLY B 213  ARG B 218 -1  O  LEU B 215   N  ILE B 206           
SHEET    3 AB6 4 MET B 235  LYS B 240 -1  O  CYS B 237   N  TYR B 216           
SHEET    4 AB6 4 ILE B 249  TYR B 252 -1  O  TYR B 252   N  MET B 236           
SHEET    1 AB7 4 ILE B 261  THR B 266  0                                        
SHEET    2 AB7 4 TYR B 272  PHE B 278 -1  O  TYR B 274   N  ASP B 265           
SHEET    3 AB7 4 LEU B 286  GLU B 291 -1  O  ALA B 290   N  LEU B 273           
SHEET    4 AB7 4 ARG B 304  VAL B 307 -1  O  ARG B 304   N  VAL B 289           
SHEET    1 AB8 4 TYR B 314  HIS B 320  0                                        
SHEET    2 AB8 4 LEU B 323  THR B 328 -1  O  TYR B 325   N  ILE B 317           
SHEET    3 AB8 4 LYS B 336  ASP B 341 -1  O  LYS B 336   N  THR B 328           
SHEET    4 AB8 4 GLU B 348  ILE B 353 -1  O  PHE B 352   N  VAL B 337           
SHEET    1 AB9 4 LYS B 360  ALA B 367  0                                        
SHEET    2 AB9 4 TYR B 371  ARG B 378 -1  O  VAL B 373   N  ASN B 365           
SHEET    3 AB9 4 LYS B 381  TYR B 387 -1  O  TYR B 387   N  PHE B 372           
SHEET    4 AB9 4 GLN B 393  LEU B 397 -1  O  LEU B 397   N  ILE B 384           
SHEET    1 AC1 4 ALA B 404  ALA B 408  0                                        
SHEET    2 AC1 4 HIS B 415  GLY B 422 -1  O  PHE B 417   N  ALA B 408           
SHEET    3 AC1 4 THR B 425  ASP B 433 -1  O  THR B 428   N  LEU B 420           
SHEET    4 AC1 4 PHE B 442  THR B 447 -1  O  ARG B 446   N  ILE B 429           
SHEET    1 AC2 8 PHE B 458  GLU B 466  0                                        
SHEET    2 AC2 8 LYS B 472  HIS B 480 -1  O  ILE B 473   N  TYR B 465           
SHEET    3 AC2 8 ILE B 521  PRO B 525 -1  O  PHE B 522   N  VAL B 478           
SHEET    4 AC2 8 ALA B 491  TYR B 494  1  N  ILE B 492   O  ALA B 523           
SHEET    5 AC2 8 VAL B 571  ALA B 576  1  O  ALA B 572   N  GLN B 493           
SHEET    6 AC2 8 ALA B 597  GLU B 601  1  O  GLU B 601   N  GLY B 575           
SHEET    7 AC2 8 ALA B 652  ASN B 658  1  O  THR B 656   N  PRO B 600           
SHEET    8 AC2 8 LEU B 687  ASP B 692  1  O  LYS B 690   N  ILE B 655           
SITE     1 AC1  4 GLU B 268  ASN B 315  ILE B 316  HOH B1153                    
CRYST1   99.180  115.000  141.450  90.00  90.00  90.00 P 21 21 21    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      0.010083  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008696  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007070        0.00000                         
TER    5666      LYS A 727                                                      
TER   11282      LYS B 727                                                      
TER   11519      CYS C  35                                                      
TER   11763      CYS D  35                                                      
MASTER      444    0    1   48   82    0    1    612695    4    6  124          
END                                                                             

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

Acknowledgements and disclaimer