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LongText Report for: 2QZP-pdb

Name Class
2QZP-pdb
HEADER    HYDROLASE                               17-AUG-07   2QZP              
TITLE     CRYSTAL STRUCTURE OF MUTATION OF AN ACYLPTIDE                         
TITLE    2 HYDROLASE/ESTERASE FROM AEROPYRUM PERNIX K1                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACYLAMINO-ACID-RELEASING ENZYME;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 21-582;                                           
COMPND   5 SYNONYM: AARE, ACYL-PEPTIDE HYDROLASE, APH, ACYLAMINOACYL-           
COMPND   6 PEPTIDASE;                                                           
COMPND   7 EC: 3.4.19.1;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AEROPYRUM PERNIX;                               
SOURCE   3 ORGANISM_COMMON: ARCHAEA;                                            
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET11A                                    
KEYWDS    CRYSTAL STRUCTURE, TRUNCATED, ACYLPEPTIDE HYDROLASE,                  
KEYWDS   2 AEROPYRUM PERNIX K1, CYTOPLASM                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.F.ZHANG,B.S.ZHENG,Z.RAO                                             
REVDAT   1   02-OCT-07 2QZP    0                                                
JRNL        AUTH   H.F.ZHANG,B.S.ZHENG,Z.RAO                                    
JRNL        TITL   EXPRESSION, PURIFICATION AND CRYSTAL STRUCTURE OF            
JRNL        TITL 2 A TRUNCATED ACYLPEPTIDE HYDROLASE FROM AEROPYRUM             
JRNL        TITL 3 PERNIX K1                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.70 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.11                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 27467                          
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 SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1393                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3106                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3160                       
REMARK   3   BIN FREE R VALUE                    : 0.4030                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.40                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 176                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.030                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8515                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 366                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.44000                                             
REMARK   3    B22 (A**2) : -6.83000                                             
REMARK   3    B33 (A**2) : 8.27000                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.33                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.41                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.40                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.52                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : CNS BULK SOLVENT MODEL USED                          
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 67.97                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER_REP.TOP                                  
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2QZP COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.                               
REMARK 100 THE RCSB ID CODE IS RCSB044247.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-2004                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.60                               
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                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC MIRROR                       
REMARK 200  OPTICS                         : OSMIC MIRROR                       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35191                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.17700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.77700                            
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: CNS                                                   
REMARK 200 STARTING MODEL: 1VE6                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NAAC, PEG3000, PH 4.6, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
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   1/2-X,-Y,1/2+Z                                          
REMARK 290       3555   -X,1/2+Y,1/2-Z                                          
REMARK 290       4555   1/2+X,1/2-Y,-Z                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       31.55850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       81.79700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.09150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       81.79700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.55850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       51.09150            
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 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: MONOMER                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMER                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                 
REMARK 465                                                                      
REMARK 465   M RES C  SSEQI                                                     
REMARK 465     ALA A    21                                                      
REMARK 465     ARG A   582                                                      
REMARK 465     ARG B   582                                                      
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                             
REMARK 500   OG1  THR A   130     OD1  ASP A   132              2.10            
REMARK 500   O    ARG A   511     O    HOH A   630              2.10            
REMARK 500   O    ARG B   327     O    HOH B   720              2.11            
REMARK 500   N    SER A   116     O    HOH A   677              2.13            
REMARK 500   O    GLU A   562     N    ALA A   564              2.17            
REMARK 500   OD2  ASP A   563     O    HOH A   585              2.18            
REMARK 500   N    GLY A   417     OE2  GLU A   419              2.18            
REMARK 500   O    THR B   451     O    HOH B   615              2.18            
REMARK 500   O    LYS B   463     O    HOH B   689              2.19            
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    ASP A  32       18.14     45.66                                   
REMARK 500    SER A  42      171.81    -48.65                                   
REMARK 500    GLU A  43       79.34      4.09                                   
REMARK 500    ARG A  61      -72.77    -90.75                                   
REMARK 500    ILE A  64     -157.55    -87.52                                   
REMARK 500    ASN A  65      -39.35   -132.19                                   
REMARK 500    TYR A  72      131.60    -13.45                                   
REMARK 500    ARG A  76      155.53    176.66                                   
REMARK 500    LYS A  85       79.23     66.24                                   
REMARK 500    ALA A  87       -9.09    -56.09                                   
REMARK 500    GLU A  88        6.77     81.35                                   
REMARK 500    ARG A  99       73.74   -112.01                                   
REMARK 500    LEU A 106       82.62    -57.19                                   
REMARK 500    ALA A 108       37.27    -82.15                                   
REMARK 500    MET A 112     -158.34   -157.05                                   
REMARK 500    SER A 116      158.36    166.25                                   
REMARK 500    PHE A 126      161.27    173.83                                   
REMARK 500    ARG A 133      162.70    177.49                                   
REMARK 500    PHE A 153      119.81    -33.69                                   
REMARK 500    LEU A 187      138.63   -177.23                                   
REMARK 500    SER A 199      155.11    171.46                                   
REMARK 500    SER A 201      131.78   -171.39                                   
REMARK 500    ARG A 216     -102.17    -76.90                                   
REMARK 500    GLU A 217     -130.40   -121.60                                   
REMARK 500    THR A 222       72.68   -118.28                                   
REMARK 500    ALA A 247      114.10   -161.71                                   
REMARK 500    ARG A 264      157.59    179.45                                   
REMARK 500    GLU A 276       99.56    -56.94                                   
REMARK 500    ARG A 287      126.40    -31.63                                   
REMARK 500    THR A 297     -169.63   -127.99                                   
REMARK 500    THR A 300      135.27   -173.98                                   
REMARK 500    PRO A 306      132.74    -38.43                                   
REMARK 500    PRO A 323      171.02    -58.37                                   
REMARK 500    ASP A 342       20.92    -74.16                                   
REMARK 500    PRO A 347      101.17    -58.09                                   
REMARK 500    SER A 353       76.23   -103.11                                   
REMARK 500    ARG A 355       22.47    -75.13                                   
REMARK 500    PHE A 371       52.46    -62.31                                   
REMARK 500    ALA A 372     -154.12   -128.05                                   
REMARK 500    GLU A 373      161.66    176.86                                   
REMARK 500    ASN A 396       70.88   -104.54                                   
REMARK 500    TRP A 429      -70.86    -33.84                                   
REMARK 500    ALA A 430      -68.43    -26.60                                   
REMARK 500    SER A 445     -121.25     67.27                                   
REMARK 500    PRO A 459       63.23    -61.55                                   
REMARK 500    GLU A 479        5.83    -69.23                                   
REMARK 500    LEU A 492       -3.08    -58.56                                   
REMARK 500    GLU A 498       -5.99    -44.30                                   
REMARK 500    ARG A 501      -61.84    -97.45                                   
REMARK 500    PRO A 515      179.34    -55.41                                   
REMARK 500    LEU A 516      126.41   -172.18                                   
REMARK 500    ARG A 526      -61.67    -98.89                                   
REMARK 500    ARG A 542       28.13    -79.55                                   
REMARK 500    ASP A 553       40.78     37.71                                   
REMARK 500    GLU A 562      -73.81    -56.93                                   
REMARK 500    ASP A 563        8.49    -44.12                                   
REMARK 500    ILE A 567       62.66   -104.79                                   
REMARK 500    LEU A 568        6.09   -179.40                                   
REMARK 500    ARG A 579      -61.16    -23.47                                   
REMARK 500    GLU A 580       41.92    -74.62                                   
REMARK 500    ASP B  34       82.06   -150.23                                   
REMARK 500    LYS B  35      109.35   -160.38                                   
REMARK 500    PHE B  41       79.95   -107.13                                   
REMARK 500    SER B  42     -154.72   -167.67                                   
REMARK 500    SER B  45     -140.77   -177.41                                   
REMARK 500    ASN B  60     -144.13    -69.47                                   
REMARK 500    ARG B  61      -87.76   -159.24                                   
REMARK 500    LEU B  68      176.02    -57.51                                   
REMARK 500    TYR B  72      122.07    -25.47                                   
REMARK 500    VAL B  74      145.47    -33.67                                   
REMARK 500    GLU B  88       11.95     83.78                                   
REMARK 500    THR B  97      -37.94    -37.06                                   
REMARK 500    ARG B  99       83.03   -150.21                                   
REMARK 500    GLU B 107      -22.96    -35.06                                   
REMARK 500    MET B 112     -154.10   -136.12                                   
REMARK 500    SER B 116     -161.89   -168.70                                   
REMARK 500    THR B 120      -83.45    -83.69                                   
REMARK 500    GLU B 122      -17.59   -165.66                                   
REMARK 500    VAL B 124       79.50   -111.43                                   
REMARK 500    ARG B 133      145.53   -173.89                                   
REMARK 500    ASP B 140     -168.96   -163.01                                   
REMARK 500    ARG B 160      103.43   -165.05                                   
REMARK 500    SER B 180     -177.92    179.88                                   
REMARK 500    LEU B 187      119.30    169.35                                   
REMARK 500    SER B 201      121.36   -172.08                                   
REMARK 500    MET B 206       47.66    101.61                                   
REMARK 500    ALA B 210       94.22    174.72                                   
REMARK 500    ASP B 232      169.91    -40.86                                   
REMARK 500    LYS B 238       64.61   -109.67                                   
REMARK 500    ARG B 244       60.73     25.58                                   
REMARK 500    THR B 249      -72.46    -68.02                                   
REMARK 500    ASP B 256       -2.52    -46.12                                   
REMARK 500    ARG B 292       49.54     77.67                                   
REMARK 500    SER B 301      159.32    168.82                                   
REMARK 500    LEU B 302      -35.73    -39.85                                   
REMARK 500    THR B 304      120.26    179.68                                   
REMARK 500    PRO B 306      104.91    -49.76                                   
REMARK 500    PRO B 323      163.93    -39.63                                   
REMARK 500    PRO B 361      108.42    -52.66                                   
REMARK 500    HIS B 367     -164.59    -69.39                                   
REMARK 500    PHE B 371       72.79    -47.07                                   
REMARK 500    SER B 375     -151.00   -131.28                                   
REMARK 500    ASP B 376       48.23    -97.61                                   
REMARK 500    THR B 380      -75.00    -39.10                                   
REMARK 500    PHE B 381      -38.09    -37.95                                   
REMARK 500    ASN B 396       58.24   -108.63                                   
REMARK 500    CYS B 416       68.82     69.97                                   
REMARK 500    ALA B 427      -70.94    -53.88                                   
REMARK 500    TRP B 429      -72.35    -35.40                                   
REMARK 500    ALA B 430      -27.10    -39.41                                   
REMARK 500    SER B 445     -124.47     53.33                                   
REMARK 500    VAL B 472      -73.86    -67.51                                   
REMARK 500    LEU B 480       41.94   -106.63                                   
REMARK 500    SER B 496      125.77     -5.72                                   
REMARK 500    GLU B 498      -44.18    -27.79                                   
REMARK 500    PRO B 505      -10.30    -40.21                                   
REMARK 500    ASP B 510        1.85    -64.96                                   
REMARK 500    PRO B 521      106.93    -57.58                                   
REMARK 500    LYS B 530      -72.78    -58.31                                   
REMARK 500    PRO B 531      -37.35    -39.94                                   
REMARK 500    LYS B 544      110.90    -16.54                                   
REMARK 500    PHE B 546      131.89   -172.87                                   
REMARK 500    THR B 560      160.46    167.03                                   
REMARK 500    GLU B 562       33.79    -68.71                                   
REMARK 500    ASP B 563       15.51   -154.54                                   
REMARK 500    LYS B 566        0.99    -58.55                                   
REMARK 500    GLU B 580       14.46    -59.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2QZP A   21   582  UNP    Q9YBQ2   APEH_AERPE      21    582             
DBREF  2QZP B   21   582  UNP    Q9YBQ2   APEH_AERPE      21    582             
SEQRES   1 A  562  ALA VAL GLU LYS TYR SER LEU GLN GLY VAL VAL ASP GLY          
SEQRES   2 A  562  ASP LYS LEU LEU VAL VAL GLY PHE SER GLU GLY SER VAL          
SEQRES   3 A  562  ASN ALA TYR LEU TYR ASP GLY GLY GLU THR VAL LYS LEU          
SEQRES   4 A  562  ASN ARG GLU PRO ILE ASN SER VAL LEU ASP PRO HIS TYR          
SEQRES   5 A  562  GLY VAL GLY ARG VAL ILE LEU VAL ARG ASP VAL SER LYS          
SEQRES   6 A  562  GLY ALA GLU GLN HIS ALA LEU PHE LYS VAL ASN THR SER          
SEQRES   7 A  562  ARG PRO GLY GLU GLU GLN ARG LEU GLU ALA VAL LYS PRO          
SEQRES   8 A  562  MET ARG ILE LEU SER GLY VAL ASP THR GLY GLU ALA VAL          
SEQRES   9 A  562  VAL PHE THR GLY ALA THR GLU ASP ARG VAL ALA LEU TYR          
SEQRES  10 A  562  ALA LEU ASP GLY GLY GLY LEU ARG GLU LEU ALA ARG LEU          
SEQRES  11 A  562  PRO GLY PHE GLY PHE VAL SER ASP ILE ARG GLY ASP LEU          
SEQRES  12 A  562  ILE ALA GLY LEU GLY PHE PHE GLY GLY GLY ARG VAL SER          
SEQRES  13 A  562  LEU PHE THR SER ASN LEU SER SER GLY GLY LEU ARG VAL          
SEQRES  14 A  562  PHE ASP SER GLY GLU GLY SER PHE SER SER ALA SER ILE          
SEQRES  15 A  562  SER PRO GLY MET LYS VAL THR ALA GLY LEU GLU THR ALA          
SEQRES  16 A  562  ARG GLU ALA ARG LEU VAL THR VAL ASP PRO ARG ASP GLY          
SEQRES  17 A  562  SER VAL GLU ASP LEU GLU LEU PRO SER LYS ASP PHE SER          
SEQRES  18 A  562  SER TYR ARG PRO THR ALA ILE THR TRP LEU GLY TYR LEU          
SEQRES  19 A  562  PRO ASP GLY ARG LEU ALA VAL VAL ALA ARG ARG GLU GLY          
SEQRES  20 A  562  ARG SER ALA VAL PHE ILE ASP GLY GLU ARG VAL GLU ALA          
SEQRES  21 A  562  PRO GLN GLY ASN HIS GLY ARG VAL VAL LEU TRP ARG GLY          
SEQRES  22 A  562  LYS LEU VAL THR SER HIS THR SER LEU SER THR PRO PRO          
SEQRES  23 A  562  ARG ILE VAL SER LEU PRO SER GLY GLU PRO LEU LEU GLU          
SEQRES  24 A  562  GLY GLY LEU PRO GLU ASP LEU ARG ARG SER ILE ALA GLY          
SEQRES  25 A  562  SER ARG LEU VAL TRP VAL GLU SER PHE ASP GLY SER ARG          
SEQRES  26 A  562  VAL PRO THR TYR VAL LEU GLU SER GLY ARG ALA PRO THR          
SEQRES  27 A  562  PRO GLY PRO THR VAL VAL LEU VAL HIS GLY GLY PRO PHE          
SEQRES  28 A  562  ALA GLU ASP SER ASP SER TRP ASP THR PHE ALA ALA SER          
SEQRES  29 A  562  LEU ALA ALA ALA GLY PHE HIS VAL VAL MET PRO ASN TYR          
SEQRES  30 A  562  ARG GLY SER THR GLY TYR GLY GLU GLU TRP ARG LEU LYS          
SEQRES  31 A  562  ILE ILE GLY ASP PRO CYS GLY GLY GLU LEU GLU ASP VAL          
SEQRES  32 A  562  SER ALA ALA ALA ARG TRP ALA ARG GLU SER GLY LEU ALA          
SEQRES  33 A  562  SER GLU LEU TYR ILE MET GLY TYR SER TYR GLY GLY TYR          
SEQRES  34 A  562  MET THR LEU CYS ALA LEU THR MET LYS PRO GLY LEU PHE          
SEQRES  35 A  562  LYS ALA GLY VAL ALA GLY ALA SER VAL VAL ASP TRP GLU          
SEQRES  36 A  562  GLU MET TYR GLU LEU SER ASP ALA ALA PHE ARG ASN PHE          
SEQRES  37 A  562  ILE GLU GLN LEU THR GLY GLY SER ARG GLU ILE MET ARG          
SEQRES  38 A  562  SER ARG SER PRO ILE ASN HIS VAL ASP ARG ILE LYS GLU          
SEQRES  39 A  562  PRO LEU ALA LEU ILE HIS PRO GLN ASN ASP SER ARG THR          
SEQRES  40 A  562  PRO LEU LYS PRO LEU LEU ARG LEU MET GLY GLU LEU LEU          
SEQRES  41 A  562  ALA ARG GLY LYS THR PHE GLU ALA HIS ILE ILE PRO ASP          
SEQRES  42 A  562  ALA GLY HIS ALA ILE ASN THR MET GLU ASP ALA VAL LYS          
SEQRES  43 A  562  ILE LEU LEU PRO ALA VAL PHE PHE LEU ALA THR GLN ARG          
SEQRES  44 A  562  GLU ARG ARG                                                  
SEQRES   1 B  562  ALA VAL GLU LYS TYR SER LEU GLN GLY VAL VAL ASP GLY          
SEQRES   2 B  562  ASP LYS LEU LEU VAL VAL GLY PHE SER GLU GLY SER VAL          
SEQRES   3 B  562  ASN ALA TYR LEU TYR ASP GLY GLY GLU THR VAL LYS LEU          
SEQRES   4 B  562  ASN ARG GLU PRO ILE ASN SER VAL LEU ASP PRO HIS TYR          
SEQRES   5 B  562  GLY VAL GLY ARG VAL ILE LEU VAL ARG ASP VAL SER LYS          
SEQRES   6 B  562  GLY ALA GLU GLN HIS ALA LEU PHE LYS VAL ASN THR SER          
SEQRES   7 B  562  ARG PRO GLY GLU GLU GLN ARG LEU GLU ALA VAL LYS PRO          
SEQRES   8 B  562  MET ARG ILE LEU SER GLY VAL ASP THR GLY GLU ALA VAL          
SEQRES   9 B  562  VAL PHE THR GLY ALA THR GLU ASP ARG VAL ALA LEU TYR          
SEQRES  10 B  562  ALA LEU ASP GLY GLY GLY LEU ARG GLU LEU ALA ARG LEU          
SEQRES  11 B  562  PRO GLY PHE GLY PHE VAL SER ASP ILE ARG GLY ASP LEU          
SEQRES  12 B  562  ILE ALA GLY LEU GLY PHE PHE GLY GLY GLY ARG VAL SER          
SEQRES  13 B  562  LEU PHE THR SER ASN LEU SER SER GLY GLY LEU ARG VAL          
SEQRES  14 B  562  PHE ASP SER GLY GLU GLY SER PHE SER SER ALA SER ILE          
SEQRES  15 B  562  SER PRO GLY MET LYS VAL THR ALA GLY LEU GLU THR ALA          
SEQRES  16 B  562  ARG GLU ALA ARG LEU VAL THR VAL ASP PRO ARG ASP GLY          
SEQRES  17 B  562  SER VAL GLU ASP LEU GLU LEU PRO SER LYS ASP PHE SER          
SEQRES  18 B  562  SER TYR ARG PRO THR ALA ILE THR TRP LEU GLY TYR LEU          
SEQRES  19 B  562  PRO ASP GLY ARG LEU ALA VAL VAL ALA ARG ARG GLU GLY          
SEQRES  20 B  562  ARG SER ALA VAL PHE ILE ASP GLY GLU ARG VAL GLU ALA          
SEQRES  21 B  562  PRO GLN GLY ASN HIS GLY ARG VAL VAL LEU TRP ARG GLY          
SEQRES  22 B  562  LYS LEU VAL THR SER HIS THR SER LEU SER THR PRO PRO          
SEQRES  23 B  562  ARG ILE VAL SER LEU PRO SER GLY GLU PRO LEU LEU GLU          
SEQRES  24 B  562  GLY GLY LEU PRO GLU ASP LEU ARG ARG SER ILE ALA GLY          
SEQRES  25 B  562  SER ARG LEU VAL TRP VAL GLU SER PHE ASP GLY SER ARG          
SEQRES  26 B  562  VAL PRO THR TYR VAL LEU GLU SER GLY ARG ALA PRO THR          
SEQRES  27 B  562  PRO GLY PRO THR VAL VAL LEU VAL HIS GLY GLY PRO PHE          
SEQRES  28 B  562  ALA GLU ASP SER ASP SER TRP ASP THR PHE ALA ALA SER          
SEQRES  29 B  562  LEU ALA ALA ALA GLY PHE HIS VAL VAL MET PRO ASN TYR          
SEQRES  30 B  562  ARG GLY SER THR GLY TYR GLY GLU GLU TRP ARG LEU LYS          
SEQRES  31 B  562  ILE ILE GLY ASP PRO CYS GLY GLY GLU LEU GLU ASP VAL          
SEQRES  32 B  562  SER ALA ALA ALA ARG TRP ALA ARG GLU SER GLY LEU ALA          
SEQRES  33 B  562  SER GLU LEU TYR ILE MET GLY TYR SER TYR GLY GLY TYR          
SEQRES  34 B  562  MET THR LEU CYS ALA LEU THR MET LYS PRO GLY LEU PHE          
SEQRES  35 B  562  LYS ALA GLY VAL ALA GLY ALA SER VAL VAL ASP TRP GLU          
SEQRES  36 B  562  GLU MET TYR GLU LEU SER ASP ALA ALA PHE ARG ASN PHE          
SEQRES  37 B  562  ILE GLU GLN LEU THR GLY GLY SER ARG GLU ILE MET ARG          
SEQRES  38 B  562  SER ARG SER PRO ILE ASN HIS VAL ASP ARG ILE LYS GLU          
SEQRES  39 B  562  PRO LEU ALA LEU ILE HIS PRO GLN ASN ASP SER ARG THR          
SEQRES  40 B  562  PRO LEU LYS PRO LEU LEU ARG LEU MET GLY GLU LEU LEU          
SEQRES  41 B  562  ALA ARG GLY LYS THR PHE GLU ALA HIS ILE ILE PRO ASP          
SEQRES  42 B  562  ALA GLY HIS ALA ILE ASN THR MET GLU ASP ALA VAL LYS          
SEQRES  43 B  562  ILE LEU LEU PRO ALA VAL PHE PHE LEU ALA THR GLN ARG          
SEQRES  44 B  562  GLU ARG ARG                                                  
FORMUL   3  HOH   *366(H2 O)                                                    
HELIX    1   1 ASP A  239  ARG A  244  1                                   6    
HELIX    2   2 ASP A  379  ALA A  388  1                                  10    
HELIX    3   3 GLY A  404  LEU A  409  1                                   6    
HELIX    4   4 GLY A  417  SER A  433  1                                  17    
HELIX    5   5 SER A  445  MET A  457  1                                  13    
HELIX    6   6 ASP A  473  LEU A  480  1                                   8    
HELIX    7   7 ASP A  482  THR A  493  1                                  12    
HELIX    8   8 SER A  496  ARG A  503  1                                   8    
HELIX    9   9 SER A  504  VAL A  509  5                                   6    
HELIX   10  10 LEU A  529  ARG A  542  1                                  14    
HELIX   11  11 MET A  561  LEU A  568  5                                   8    
HELIX   12  12 LEU A  569  GLU A  580  1                                  12    
HELIX   13  13 GLU B  324  SER B  329  1                                   6    
HELIX   14  14 ASP B  379  ALA B  388  1                                  10    
HELIX   15  15 GLY B  404  LEU B  409  1                                   6    
HELIX   16  16 GLY B  417  SER B  433  1                                  17    
HELIX   17  17 SER B  445  LYS B  458  1                                  14    
HELIX   18  18 TRP B  474  LEU B  480  1                                   7    
HELIX   19  19 ASP B  482  THR B  493  1                                  12    
HELIX   20  20 SER B  496  ARG B  503  1                                   8    
HELIX   21  21 SER B  504  ILE B  512  5                                   9    
HELIX   22  22 PRO B  528  ARG B  542  1                                  15    
HELIX   23  23 LEU B  568  GLU B  580  1                                  13    
SHEET    1   A 4 TYR A  25  VAL A  31  0                                        
SHEET    2   A 4 LYS A  35  GLY A  40 -1  O  LEU A  37   N  GLY A  29           
SHEET    3   A 4 ASN A  47  TYR A  51 -1  O  TYR A  49   N  VAL A  38           
SHEET    4   A 4 VAL A  57  LYS A  58 -1  O  VAL A  57   N  LEU A  50           
SHEET    1   B 3 SER A  66  VAL A  67  0                                        
SHEET    2   B 3 VAL A  77  ASP A  82 -1  O  VAL A  80   N  SER A  66           
SHEET    3   B 3 HIS A  90  VAL A  95 -1  O  VAL A  95   N  VAL A  77           
SHEET    1   C 5 ASP A  69  PRO A  70  0                                        
SHEET    2   C 5 ARG A 113  ASP A 119  1  O  ASP A 119   N  ASP A  69           
SHEET    3   C 5 VAL A 124  ALA A 129 -1  O  THR A 127   N  SER A 116           
SHEET    4   C 5 VAL A 134  ASP A 140 -1  O  LEU A 139   N  VAL A 124           
SHEET    5   C 5 GLY A 143  LEU A 150 -1  O  LEU A 147   N  LEU A 136           
SHEET    1   D 4 GLY A 154  ARG A 160  0                                        
SHEET    2   D 4 LEU A 163  GLY A 171 -1  O  ALA A 165   N  ASP A 158           
SHEET    3   D 4 ARG A 174  ASN A 181 -1  O  SER A 176   N  GLY A 168           
SHEET    4   D 4 ARG A 188  PHE A 190 -1  O  PHE A 190   N  LEU A 177           
SHEET    1   E 4 GLY A 195  SER A 201  0                                        
SHEET    2   E 4 VAL A 208  THR A 214 -1  O  GLU A 213   N  SER A 196           
SHEET    3   E 4 ALA A 218  VAL A 223 -1  O  ARG A 219   N  LEU A 212           
SHEET    4   E 4 VAL A 230  ASP A 232 -1  O  GLU A 231   N  THR A 222           
SHEET    1   F 4 TRP A 250  TYR A 253  0                                        
SHEET    2   F 4 LEU A 259  ARG A 265 -1  O  VAL A 262   N  TRP A 250           
SHEET    3   F 4 ARG A 268  ILE A 273 -1  O  ARG A 268   N  ARG A 265           
SHEET    4   F 4 GLU A 276  VAL A 278 -1  O  VAL A 278   N  VAL A 271           
SHEET    1   G 4 VAL A 289  TRP A 291  0                                        
SHEET    2   G 4 LYS A 294  THR A 297 -1  O  LYS A 294   N  TRP A 291           
SHEET    3   G 4 ILE A 308  SER A 310 -1  O  VAL A 309   N  THR A 297           
SHEET    4   G 4 PRO A 316  LEU A 318 -1  O  LEU A 318   N  ILE A 308           
SHEET    1   H12 ARG A 334  GLU A 339  0                                        
SHEET    2   H12 ARG A 345  LEU A 351 -1  O  VAL A 350   N  ARG A 334           
SHEET    3   H12 HIS A 391  PRO A 395 -1  O  MET A 394   N  TYR A 349           
SHEET    4   H12 GLY A 360  VAL A 366  1  N  VAL A 363   O  HIS A 391           
SHEET    5   H12 ALA A 436  TYR A 444  1  O  TYR A 440   N  VAL A 364           
SHEET    6   H12 ALA A 464  GLY A 468  1  O  ALA A 464   N  ILE A 441           
SHEET    7   H12 LEU A 516  PRO A 521  1  O  ALA A 517   N  ALA A 467           
SHEET    8   H12 GLU A 547  ILE A 551  1  O  HIS A 549   N  HIS A 520           
SHEET    9   H12 PHE B 546  ILE B 551 -1  O  ALA B 548   N  ILE A 550           
SHEET   10   H12 LEU B 516  PRO B 521  1  N  HIS B 520   O  HIS B 549           
SHEET   11   H12 ALA B 464  GLY B 468  1  N  ALA B 467   O  ALA B 517           
SHEET   12   H12 TYR B 440  TYR B 444  1  N  ILE B 441   O  VAL B 466           
SHEET    1   I 3 LYS B  24  TYR B  25  0                                        
SHEET    2   I 3 LEU B  36  PHE B  41 -1  O  PHE B  41   N  LYS B  24           
SHEET    3   I 3 ASN B  47  TYR B  51 -1  O  ASN B  47   N  GLY B  40           
SHEET    1   J 4 SER B  66  VAL B  67  0                                        
SHEET    2   J 4 ARG B  76  ASP B  82 -1  O  VAL B  80   N  SER B  66           
SHEET    3   J 4 HIS B  90  ASN B  96 -1  O  PHE B  93   N  LEU B  79           
SHEET    4   J 4 GLN B 104  ARG B 105 -1  O  GLN B 104   N  LYS B  94           
SHEET    1   K 4 ASP B  69  PRO B  70  0                                        
SHEET    2   K 4 VAL B 118  ASP B 119  1  O  ASP B 119   N  ASP B  69           
SHEET    3   K 4 VAL B 124  ALA B 129 -1  O  VAL B 125   N  VAL B 118           
SHEET    4   K 4 ARG B 113  ILE B 114 -1  N  ARG B 113   O  ALA B 129           
SHEET    1   L 5 ASP B  69  PRO B  70  0                                        
SHEET    2   L 5 VAL B 118  ASP B 119  1  O  ASP B 119   N  ASP B  69           
SHEET    3   L 5 VAL B 124  ALA B 129 -1  O  VAL B 125   N  VAL B 118           
SHEET    4   L 5 VAL B 134  ASP B 140 -1  O  TYR B 137   N  PHE B 126           
SHEET    5   L 5 GLY B 143  LEU B 150 -1  O  GLY B 143   N  ASP B 140           
SHEET    1   M 4 PHE B 153  ARG B 160  0                                        
SHEET    2   M 4 LEU B 163  GLY B 171 -1  O  ALA B 165   N  ASP B 158           
SHEET    3   M 4 ARG B 174  PHE B 178 -1  O  SER B 176   N  GLY B 168           
SHEET    4   M 4 VAL B 189  PHE B 190 -1  O  PHE B 190   N  LEU B 177           
SHEET    1   N 3 GLY B 195  PHE B 197  0                                        
SHEET    2   N 3 LEU B 212  THR B 214 -1  O  GLU B 213   N  SER B 196           
SHEET    3   N 3 ALA B 218  ARG B 219 -1  O  ARG B 219   N  LEU B 212           
SHEET    1   O 2 SER B 201  ILE B 202  0                                        
SHEET    2   O 2 VAL B 208  THR B 209 -1  O  THR B 209   N  SER B 201           
SHEET    1   P 4 ILE B 248  TYR B 253  0                                        
SHEET    2   P 4 LEU B 259  ARG B 265 -1  O  VAL B 262   N  TRP B 250           
SHEET    3   P 4 ARG B 268  ILE B 273 -1  O  PHE B 272   N  VAL B 261           
SHEET    4   P 4 GLU B 276  ARG B 277 -1  O  GLU B 276   N  ILE B 273           
SHEET    1   Q 4 VAL B 289  LEU B 290  0                                        
SHEET    2   Q 4 LEU B 295  SER B 301 -1  O  VAL B 296   N  VAL B 289           
SHEET    3   Q 4 THR B 304  SER B 310 -1  O  THR B 304   N  SER B 301           
SHEET    4   Q 4 GLU B 315  LEU B 318 -1  O  GLU B 315   N  SER B 310           
SHEET    1   R 5 ARG B 334  VAL B 338  0                                        
SHEET    2   R 5 VAL B 346  LEU B 351 -1  O  VAL B 346   N  VAL B 338           
SHEET    3   R 5 HIS B 391  PRO B 395 -1  O  VAL B 392   N  LEU B 351           
SHEET    4   R 5 GLY B 360  VAL B 364  1  N  VAL B 363   O  VAL B 393           
SHEET    5   R 5 ALA B 436  GLU B 438  1  O  GLU B 438   N  THR B 362           
SSBOND   1 CYS A  416    CYS A  453                        1555   1555    2.03  
SSBOND   2 CYS B  416    CYS B  453                        1555   1555    2.04  
CISPEP   1 LEU A  311    PRO A  312          0        -0.50                     
CISPEP   2 THR A  358    PRO A  359          0        -0.05                     
CISPEP   3 GLY A  369    PRO A  370          0         0.42                     
CISPEP   4 LEU B  311    PRO B  312          0        -0.18                     
CISPEP   5 THR B  358    PRO B  359          0         0.36                     
CISPEP   6 GLY B  369    PRO B  370          0        -0.23                     
CRYST1   63.117  102.183  163.594  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      0.015844  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009786  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006113        0.00000                         
TER    4256      ARG A 581                                                      
TER    8517      ARG B 581                                                      
MASTER      392    0    0   23   78    0    0    6 8881    2    4   88          
END                                                                             

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