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LongText Report for: 5hq3-pdb

Name Class
5hq3-pdb
HEADER    DE NOVO PROTEIN                         21-JAN-16   5HQ3              
TITLE     HUMAN ACETYLCHOLINESTERASE DESIGN                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DESIGN OF HUMAN ACETYLCHOLINESTERASE;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: DESIGN OF HUMAN ACETYLCHOLINESTERASE;                      
COMPND   7 CHAIN: B;                                                            
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    DESIGN, DE NOVO PROTEIN                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.GOLDENZWEIG,M.GOLDSMITH,S.E.HILL,O.GERTMAN,P.LAURINO,Y.ASHANI,      
AUTHOR   2 O.DYM,S.ALBECK,T.UNGER,J.PRILUSKY,R.L.LIEBERMAN,A.AHARONI,I.SILMAN,  
AUTHOR   3 J.L.SUSSMAN,D.S.TAWFIK,S.J.FLEISHMAN                                 
REVDAT   1   27-JUL-16 5HQ3    0                                                
JRNL        AUTH   A.GOLDENZWEIG,M.GOLDSMITH,S.E.HILL,O.GERTMAN,P.LAURINO,      
JRNL        AUTH 2 Y.ASHANI,O.DYM,T.UNGER,S.ALBECK,J.PRILUSKY,R.L.LIEBERMAN,    
JRNL        AUTH 3 A.AHARONI,I.SILMAN,J.L.SUSSMAN,D.S.TAWFIK,S.J.FLEISHMAN      
JRNL        TITL   AUTOMATED STRUCTURE- AND SEQUENCE-BASED DESIGN OF PROTEINS   
JRNL        TITL 2 FOR HIGH BACTERIAL EXPRESSION AND STABILITY                  
JRNL        REF    MOL.CELL                                   2016              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        DOI    10.1016/J.MOLCEL.2016.06.012                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 48279                          
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) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2498                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3484                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.75                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 172                          
REMARK   3   BIN FREE R VALUE                    : 0.3560                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8313                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 1                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.02000                                             
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): 0.399         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.279         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.209         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.988         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8626 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  7946 ; 0.009 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11785 ; 1.713 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 18228 ; 1.005 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1055 ; 6.980 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   410 ;33.186 ;22.756       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1232 ;16.203 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    77 ;19.719 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1230 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9868 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2105 ; 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):  4226 ; 2.999 ; 3.935       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4225 ; 2.974 ; 3.934       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5273 ; 4.580 ; 5.891       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  5274 ; 4.581 ; 5.892       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4400 ; 3.285 ; 4.221       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4401 ; 3.285 ; 4.221       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  6511 ; 5.063 ; 6.217       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  9579 ; 6.701 ;31.399       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  9577 ; 6.702 ;31.397       
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 5HQ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000217525.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95372                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50786                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 98.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 9.700                              
REMARK 200  R MERGE                    (I) : 0.10700                            
REMARK 200  R SYM                      (I) : 0.10700                            
REMARK 200   FOR THE DATA SET  : 6.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.300                              
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: 4EY4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 6000 0.1M MGCL2 0.1M MES PH=6,    
REMARK 280  PH 6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      197.65250            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       44.76700            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       44.76700            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      296.47875            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       44.76700            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       44.76700            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       98.82625            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       44.76700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       44.76700            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      296.47875            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       44.76700            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       44.76700            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       98.82625            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      197.65250            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: 3460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     0                                                      
REMARK 465     GLU A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     THR A   262                                                      
REMARK 465     GLY A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     ASP A   494                                                      
REMARK 465     PRO A   495                                                      
REMARK 465     LYS A   496                                                      
REMARK 465     ALA A   497                                                      
REMARK 465     THR A   543                                                      
REMARK 465     ASP A   544                                                      
REMARK 465     THR A   545                                                      
REMARK 465     LEU A   546                                                      
REMARK 465     ASP A   547                                                      
REMARK 465     MET B     0                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     ASP B     5                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     THR B   262                                                      
REMARK 465     GLY B   263                                                      
REMARK 465     GLY B   264                                                      
REMARK 465     ARG B   493                                                      
REMARK 465     ASP B   494                                                      
REMARK 465     PRO B   495                                                      
REMARK 465     LYS B   496                                                      
REMARK 465     ALA B   497                                                      
REMARK 465     ASP B   544                                                      
REMARK 465     THR B   545                                                      
REMARK 465     LEU B   546                                                      
REMARK 465     ASP B   547                                                      
REMARK 465     GLU B   548                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 109    CE   NZ                                             
REMARK 470     GLN A 291    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 292    CD   OE1  OE2                                       
REMARK 470     LYS A 322    CD   CE   NZ                                        
REMARK 470     GLU A 357    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 417    CZ   NH1  NH2                                       
REMARK 470     LYS A 467    CG   CD   CE   NZ                                   
REMARK 470     LEU A 540    CG   CD1  CD2                                       
REMARK 470     ARG B  21    CZ   NH1  NH2                                       
REMARK 470     TYR B 105    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B 109    CG   CD   CE   NZ                                   
REMARK 470     ARG B 143    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 165    NE   CZ   NH1  NH2                                  
REMARK 470     GLN B 291    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 292    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 357    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 506    OD1  OD2                                            
REMARK 470     LEU B 540    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A   203     O2    VX A   601              1.91            
REMARK 500   OG   SER A   203     O1    VX A   601              2.05            
REMARK 500   OG   SER A   203     C1    VX A   601              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 296   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A 424   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B 274   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 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    PHE A  47       -3.55     63.98                                   
REMARK 500    ALA A 167       69.20   -151.24                                   
REMARK 500    ASN A 170       19.08     56.78                                   
REMARK 500    SER A 203     -123.19     60.48                                   
REMARK 500    ASP A 306      -74.91   -127.06                                   
REMARK 500    GLU A 351        4.28    -69.02                                   
REMARK 500    LEU A 353       88.66    -67.97                                   
REMARK 500    VAL A 407      -52.81   -125.96                                   
REMARK 500    ASP A 514     -157.73   -158.92                                   
REMARK 500    SER A 541       56.17    -69.80                                   
REMARK 500    GLU B   7      -37.31     81.71                                   
REMARK 500    PHE B  47       -4.94     73.26                                   
REMARK 500    PRO B 111      115.45    -39.07                                   
REMARK 500    PHE B 123        5.09     59.30                                   
REMARK 500    PHE B 158       -0.95   -143.40                                   
REMARK 500    SER B 203     -127.33     65.30                                   
REMARK 500    ASN B 233       32.18    -95.28                                   
REMARK 500    ASP B 306      -87.83   -132.84                                   
REMARK 500    SER B 347      145.93    171.13                                   
REMARK 500    HIS B 387       54.97   -140.81                                   
REMARK 500    PRO B 388        2.82    -68.81                                   
REMARK 500    TRP B 442      -45.45    122.18                                   
REMARK 500    ASP B 514     -155.92   -160.03                                   
REMARK 500    ARG B 525       56.99     36.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA B    6     GLU B    7                 -146.33                    
REMARK 500 ASN B  265     ASP B  266                  146.96                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue VX A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue VX B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 602                 
DBREF  5HQ3 A    0   547  PDB    5HQ3     5HQ3             0    547             
DBREF  5HQ3 B    0   548  PDB    5HQ3     5HQ3             0    548             
SEQRES   1 A  548  MET GLU GLY ARG GLU ASP ALA GLU LEU LEU VAL THR THR          
SEQRES   2 A  548  ARG GLY GLY ARG LEU ARG GLY ILE ARG LEU THR THR PRO          
SEQRES   3 A  548  GLY GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA          
SEQRES   4 A  548  GLU PRO PRO VAL GLY PRO ARG ARG PHE ARG PRO PRO GLU          
SEQRES   5 A  548  PRO LYS GLN PRO TRP SER GLY VAL TRP ASP ALA THR THR          
SEQRES   6 A  548  PHE GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR          
SEQRES   7 A  548  PRO GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG          
SEQRES   8 A  548  ASN LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR          
SEQRES   9 A  548  PRO TYR PRO ARG PRO LYS ASN PRO ALA PRO VAL MET VAL          
SEQRES  10 A  548  TRP ILE TYR GLY GLY GLY PHE TYR SER GLY SER SER SER          
SEQRES  11 A  548  LEU ASP VAL TYR ASP GLY ARG PHE LEU VAL ARG THR GLU          
SEQRES  12 A  548  ARG VAL VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA          
SEQRES  13 A  548  PHE GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO          
SEQRES  14 A  548  GLY ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN          
SEQRES  15 A  548  TRP VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO          
SEQRES  16 A  548  THR SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA          
SEQRES  17 A  548  SER VAL GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY          
SEQRES  18 A  548  LEU PHE HIS ARG ALA ILE LEU GLN SER GLY ALA PRO ASN          
SEQRES  19 A  548  ALA PRO TRP ALA TYR VAL SER ARG GLU GLU ALA ARG ARG          
SEQRES  20 A  548  ARG ALA LEU GLN LEU ALA LYS LEU VAL GLY CYS PRO PRO          
SEQRES  21 A  548  GLY GLY THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS          
SEQRES  22 A  548  LEU ARG ASN ARG PRO PRO GLN GLU LEU VAL ASN HIS GLU          
SEQRES  23 A  548  TRP HIS VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER          
SEQRES  24 A  548  PHE VAL PRO VAL VAL ASP GLY ASP PHE LEU PRO ASP THR          
SEQRES  25 A  548  PRO GLU ALA LEU ILE ASN ASN GLY ASP PHE LYS GLY LEU          
SEQRES  26 A  548  ASP VAL LEU VAL GLY VAL ASN LYS ASP GLU GLY SER TYR          
SEQRES  27 A  548  PHE LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN          
SEQRES  28 A  548  GLU SER LEU ILE SER ARG GLU GLU PHE LEU GLU GLY VAL          
SEQRES  29 A  548  ARG VAL GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU          
SEQRES  30 A  548  ALA ILE VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU          
SEQRES  31 A  548  ASP PRO ALA LYS ASN ARG ASP ALA LEU SER ASP VAL VAL          
SEQRES  32 A  548  GLY ASP HIS ASN VAL ILE CYS PRO VAL ALA GLN PHE ALA          
SEQRES  33 A  548  GLN ARG TYR ALA ALA ASN GLY ALA ARG VAL TYR ALA TYR          
SEQRES  34 A  548  VAL PHE GLU HIS ARG SER SER THR LEU PRO TRP PRO GLU          
SEQRES  35 A  548  TRP MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE          
SEQRES  36 A  548  PHE GLY ILE PRO LEU ASP PRO SER ARG ASN TYR THR LYS          
SEQRES  37 A  548  GLU GLU LYS ILE PHE ALA ARG ARG LEU MET ARG TYR TRP          
SEQRES  38 A  548  ALA ASN PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG          
SEQRES  39 A  548  ASP PRO LYS ALA PRO GLN TRP PRO PRO TYR THR ALA ASP          
SEQRES  40 A  548  GLU GLN LYS TYR VAL SER LEU ASP LEU ARG PRO LEU GLU          
SEQRES  41 A  548  VAL ARG ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP          
SEQRES  42 A  548  ASN ARG PHE LEU PRO LYS LEU LEU SER ALA THR ASP THR          
SEQRES  43 A  548  LEU ASP                                                      
SEQRES   1 B  549  MET GLU GLY ARG GLU ASP ALA GLU LEU LEU VAL THR THR          
SEQRES   2 B  549  ARG GLY GLY ARG LEU ARG GLY ILE ARG LEU THR THR PRO          
SEQRES   3 B  549  GLY GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA          
SEQRES   4 B  549  GLU PRO PRO VAL GLY PRO ARG ARG PHE ARG PRO PRO GLU          
SEQRES   5 B  549  PRO LYS GLN PRO TRP SER GLY VAL TRP ASP ALA THR THR          
SEQRES   6 B  549  PHE GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR          
SEQRES   7 B  549  PRO GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG          
SEQRES   8 B  549  ASN LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR          
SEQRES   9 B  549  PRO TYR PRO ARG PRO LYS ASN PRO ALA PRO VAL MET VAL          
SEQRES  10 B  549  TRP ILE TYR GLY GLY GLY PHE TYR SER GLY SER SER SER          
SEQRES  11 B  549  LEU ASP VAL TYR ASP GLY ARG PHE LEU VAL ARG THR GLU          
SEQRES  12 B  549  ARG VAL VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA          
SEQRES  13 B  549  PHE GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO          
SEQRES  14 B  549  GLY ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN          
SEQRES  15 B  549  TRP VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO          
SEQRES  16 B  549  THR SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA          
SEQRES  17 B  549  SER VAL GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY          
SEQRES  18 B  549  LEU PHE HIS ARG ALA ILE LEU GLN SER GLY ALA PRO ASN          
SEQRES  19 B  549  ALA PRO TRP ALA TYR VAL SER ARG GLU GLU ALA ARG ARG          
SEQRES  20 B  549  ARG ALA LEU GLN LEU ALA LYS LEU VAL GLY CYS PRO PRO          
SEQRES  21 B  549  GLY GLY THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS          
SEQRES  22 B  549  LEU ARG ASN ARG PRO PRO GLN GLU LEU VAL ASN HIS GLU          
SEQRES  23 B  549  TRP HIS VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER          
SEQRES  24 B  549  PHE VAL PRO VAL VAL ASP GLY ASP PHE LEU PRO ASP THR          
SEQRES  25 B  549  PRO GLU ALA LEU ILE ASN ASN GLY ASP PHE LYS GLY LEU          
SEQRES  26 B  549  ASP VAL LEU VAL GLY VAL ASN LYS ASP GLU GLY SER TYR          
SEQRES  27 B  549  PHE LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN          
SEQRES  28 B  549  GLU SER LEU ILE SER ARG GLU GLU PHE LEU GLU GLY VAL          
SEQRES  29 B  549  ARG VAL GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU          
SEQRES  30 B  549  ALA ILE VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU          
SEQRES  31 B  549  ASP PRO ALA LYS ASN ARG ASP ALA LEU SER ASP VAL VAL          
SEQRES  32 B  549  GLY ASP HIS ASN VAL ILE CYS PRO VAL ALA GLN PHE ALA          
SEQRES  33 B  549  GLN ARG TYR ALA ALA ASN GLY ALA ARG VAL TYR ALA TYR          
SEQRES  34 B  549  VAL PHE GLU HIS ARG SER SER THR LEU PRO TRP PRO GLU          
SEQRES  35 B  549  TRP MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE          
SEQRES  36 B  549  PHE GLY ILE PRO LEU ASP PRO SER ARG ASN TYR THR LYS          
SEQRES  37 B  549  GLU GLU LYS ILE PHE ALA ARG ARG LEU MET ARG TYR TRP          
SEQRES  38 B  549  ALA ASN PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG          
SEQRES  39 B  549  ASP PRO LYS ALA PRO GLN TRP PRO PRO TYR THR ALA ASP          
SEQRES  40 B  549  GLU GLN LYS TYR VAL SER LEU ASP LEU ARG PRO LEU GLU          
SEQRES  41 B  549  VAL ARG ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP          
SEQRES  42 B  549  ASN ARG PHE LEU PRO LYS LEU LEU SER ALA THR ASP THR          
SEQRES  43 B  549  LEU ASP GLU                                                  
HET     VX  A 601       6                                                       
HET    MES  A 602      12                                                       
HET     VX  B 601       6                                                       
HET    MES  B 602      12                                                       
HETNAM      VX O-ETHYLMETHYLPHOSPHONIC ACID ESTER GROUP                         
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
FORMUL   3   VX    2(C3 H9 O3 P)                                                
FORMUL   4  MES    2(C6 H13 N O4 S)                                             
FORMUL   7  HOH   *(H2 O)                                                       
HELIX    1 AA1 VAL A   42  ARG A   46  5                                   5    
HELIX    2 AA2 PHE A   80  MET A   85  1                                   6    
HELIX    3 AA3 LEU A  130  ASP A  134  5                                   5    
HELIX    4 AA4 GLY A  135  ARG A  143  1                                   9    
HELIX    5 AA5 VAL A  153  LEU A  159  1                                   7    
HELIX    6 AA6 ASN A  170  ILE A  187  1                                  18    
HELIX    7 AA7 ALA A  188  PHE A  190  5                                   3    
HELIX    8 AA8 SER A  203  SER A  215  1                                  13    
HELIX    9 AA9 PRO A  216  PHE A  222  5                                   7    
HELIX   10 AB1 SER A  240  VAL A  255  1                                  16    
HELIX   11 AB2 ASP A  266  ARG A  276  1                                  11    
HELIX   12 AB3 PRO A  277  GLU A  285  1                                   9    
HELIX   13 AB4 TRP A  286  LEU A  289  5                                   4    
HELIX   14 AB5 THR A  311  ASN A  318  1                                   8    
HELIX   15 AB6 GLY A  335  VAL A  340  1                                   6    
HELIX   16 AB7 SER A  355  VAL A  367  1                                  13    
HELIX   17 AB8 SER A  371  TYR A  382  1                                  12    
HELIX   18 AB9 ASP A  390  VAL A  407  1                                  18    
HELIX   19 AC1 VAL A  407  ASN A  421  1                                  15    
HELIX   20 AC2 PRO A  440  GLY A  444  5                                   5    
HELIX   21 AC3 GLU A  450  PHE A  455  1                                   6    
HELIX   22 AC4 GLY A  456  ASP A  460  5                                   5    
HELIX   23 AC5 THR A  466  GLY A  487  1                                  22    
HELIX   24 AC6 ARG A  525  ARG A  534  1                                  10    
HELIX   25 AC7 ARG A  534  SER A  541  1                                   8    
HELIX   26 AC8 VAL B   42  ARG B   46  5                                   5    
HELIX   27 AC9 PHE B   80  MET B   85  1                                   6    
HELIX   28 AD1 LEU B  130  ASP B  134  5                                   5    
HELIX   29 AD2 GLY B  135  ARG B  143  1                                   9    
HELIX   30 AD3 VAL B  153  LEU B  159  1                                   7    
HELIX   31 AD4 ASN B  170  ILE B  187  1                                  18    
HELIX   32 AD5 ALA B  188  PHE B  190  5                                   3    
HELIX   33 AD6 SER B  203  LEU B  214  1                                  12    
HELIX   34 AD7 SER B  215  ARG B  219  5                                   5    
HELIX   35 AD8 SER B  240  VAL B  255  1                                  16    
HELIX   36 AD9 ASP B  266  ARG B  276  1                                  11    
HELIX   37 AE1 PRO B  277  ASN B  283  1                                   7    
HELIX   38 AE2 HIS B  284  LEU B  289  5                                   6    
HELIX   39 AE3 THR B  311  ASN B  318  1                                   8    
HELIX   40 AE4 GLY B  335  VAL B  340  1                                   6    
HELIX   41 AE5 SER B  355  VAL B  367  1                                  13    
HELIX   42 AE6 SER B  371  TYR B  382  1                                  12    
HELIX   43 AE7 ASP B  390  VAL B  407  1                                  18    
HELIX   44 AE8 VAL B  407  ASN B  421  1                                  15    
HELIX   45 AE9 GLU B  450  PHE B  455  1                                   6    
HELIX   46 AF1 GLY B  456  ASP B  460  5                                   5    
HELIX   47 AF2 THR B  466  GLY B  487  1                                  22    
HELIX   48 AF3 ARG B  525  ARG B  534  1                                  10    
HELIX   49 AF4 ARG B  534  SER B  541  1                                   8    
SHEET    1 AA1 3 LEU A   9  THR A  12  0                                        
SHEET    2 AA1 3 GLY A  15  ARG A  18 -1  O  LEU A  17   N  VAL A  10           
SHEET    3 AA1 3 VAL A  59  ASP A  61  1  O  TRP A  60   N  ARG A  16           
SHEET    1 AA211 ILE A  20  LEU A  22  0                                        
SHEET    2 AA211 VAL A  29  PRO A  36 -1  O  ALA A  31   N  ILE A  20           
SHEET    3 AA211 TYR A  98  PRO A 104 -1  O  THR A 103   N  SER A  30           
SHEET    4 AA211 VAL A 145  MET A 149 -1  O  SER A 148   N  ASN A 100           
SHEET    5 AA211 ALA A 112  ILE A 118  1  N  PRO A 113   O  VAL A 145           
SHEET    6 AA211 GLY A 192  GLU A 202  1  O  ASP A 193   N  ALA A 112           
SHEET    7 AA211 ARG A 224  GLN A 228  1  O  GLN A 228   N  GLY A 201           
SHEET    8 AA211 ASP A 325  ASN A 331  1  O  LEU A 327   N  LEU A 227           
SHEET    9 AA211 ARG A 424  PHE A 430  1  O  PHE A 430   N  VAL A 330           
SHEET   10 AA211 LYS A 509  LEU A 513  1  O  LEU A 513   N  VAL A 429           
SHEET   11 AA211 GLU A 519  ARG A 522 -1  O  ARG A 521   N  TYR A 510           
SHEET    1 AA3 2 VAL A  68  CYS A  69  0                                        
SHEET    2 AA3 2 LEU A  92  SER A  93  1  O  SER A  93   N  VAL A  68           
SHEET    1 AA4 3 LEU B   9  THR B  12  0                                        
SHEET    2 AA4 3 GLY B  15  ARG B  18 -1  O  LEU B  17   N  VAL B  10           
SHEET    3 AA4 3 VAL B  59  ASP B  61  1  O  TRP B  60   N  ARG B  16           
SHEET    1 AA511 ILE B  20  LEU B  22  0                                        
SHEET    2 AA511 VAL B  29  PRO B  36 -1  O  ALA B  31   N  ILE B  20           
SHEET    3 AA511 TYR B  98  PRO B 104 -1  O  THR B 103   N  SER B  30           
SHEET    4 AA511 VAL B 145  MET B 149 -1  O  SER B 148   N  ASN B 100           
SHEET    5 AA511 ALA B 112  ILE B 118  1  N  TRP B 117   O  VAL B 147           
SHEET    6 AA511 GLY B 192  GLU B 202  1  O  THR B 198   N  VAL B 114           
SHEET    7 AA511 ARG B 224  GLN B 228  1  O  GLN B 228   N  GLY B 201           
SHEET    8 AA511 VAL B 326  ASN B 331  1  O  LEU B 327   N  ALA B 225           
SHEET    9 AA511 VAL B 425  PHE B 430  1  O  TYR B 426   N  VAL B 328           
SHEET   10 AA511 LYS B 509  LEU B 513  1  O  VAL B 511   N  ALA B 427           
SHEET   11 AA511 GLU B 519  ARG B 522 -1  O  ARG B 521   N  TYR B 510           
SHEET    1 AA6 2 VAL B  68  CYS B  69  0                                        
SHEET    2 AA6 2 LEU B  92  SER B  93  1  O  SER B  93   N  VAL B  68           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.06  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.06  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.05  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.05  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.05  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.01  
LINK         OG  SER A 203                 P1   VX A 601     1555   1555  1.55  
LINK         OG  SER B 203                 P1   VX B 601     1555   1555  1.52  
CISPEP   1 TYR A  105    PRO A  106          0        -4.66                     
CISPEP   2 TYR B  105    PRO B  106          0        -1.91                     
SITE     1 AC1  6 GLY A 121  GLY A 122  SER A 203  ALA A 204                    
SITE     2 AC1  6 TRP A 236  HIS A 447                                          
SITE     1 AC2  4 TRP A 286  SER A 293  PHE A 295  TYR A 341                    
SITE     1 AC3  8 GLY B 121  GLY B 122  TYR B 124  SER B 203                    
SITE     2 AC3  8 ALA B 204  TRP B 236  PHE B 295  HIS B 447                    
SITE     1 AC4  4 TRP B 286  VAL B 294  PHE B 295  TYR B 341                    
CRYST1   89.534   89.534  395.305  90.00  90.00  90.00 P 43 21 2     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      0.011169  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011169  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002530        0.00000                         
TER    4174      ALA A 542                                                      
TER    8321      THR B 543                                                      
MASTER      429    0    4   49   32    0    6    6 8350    2   50   86          
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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