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Database: PDB
Entry: 1P7G
LinkDB: 1P7G
Original site: 1P7G 
HEADER    OXIDOREDUCTASE                          01-MAY-03   1P7G              
TITLE     CRYSTAL STRUCTURE OF SUPEROXIDE DISMUTASE FROM PYROBACULUM            
TITLE    2 AEROPHILUM                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q,            
COMPND   4 R, S, T, U, V, W, X;                                                 
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PYROBACULUM AEROPHILUM;                         
SOURCE   3 ORGANISM_TAXID: 13773;                                               
SOURCE   4 GENE: SOD OR PAE0274;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PQE-30                                    
KEYWDS    ALPHA-BETA, OXIDOREDUCTASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.LEE,M.R.SAWAYA,D.EISENBERG                                          
REVDAT   2   24-FEB-09 1P7G    1       VERSN                                    
REVDAT   1   02-DEC-03 1P7G    0                                                
JRNL        AUTH   S.LEE,M.R.SAWAYA,D.EISENBERG                                 
JRNL        TITL   STRUCTURE OF SUPEROXIDE DISMUTASE FROM PYROBACULUM           
JRNL        TITL 2 AEROPHILUM PRESENTS A CHALLENGING CASE IN                    
JRNL        TITL 3 MOLECULAR REPLACEMENT WITH MULTIPLE MOLECULES,               
JRNL        TITL 4 PSEUDO-SYMMETRY AND TWINNING.                                
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  59  2191 2003              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   14646077                                                     
JRNL        DOI    10.1107/S0907444903019942                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.45                          
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)   (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 460759                         
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) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 37229                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.86                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2430                       
REMARK   3   BIN FREE R VALUE                    : 0.2650                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 3093                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 41127                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 124                                     
REMARK   3   SOLVENT ATOMS            : 2536                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.32900                                              
REMARK   3    B22 (A**2) : 0.32900                                              
REMARK   3    B33 (A**2) : -0.65900                                             
REMARK   3    B12 (A**2) : -0.71700                                             
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) : 0.18                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.18                            
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) : 0.23                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.17                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.86                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
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 : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: PARTIAL TWINNING INCORPORATED WITH        
REMARK   3  THE TWINNING FRACTION BEING 0.463.                                  
REMARK   4                                                                      
REMARK   4 1P7G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAY-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019102.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUN-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X8C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9785, 0.9708, 0.9787, 0.9863     
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 465126                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.510                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.07600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: GLRF                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1SSS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3000, CALCIUM ACETATE, HEPES,        
REMARK 280  PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      114.77933            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       57.38967            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER. THERE ARE SIX         
REMARK 300 TETRAMERS IN THE ASYMMETRIC UNIT.                                    
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17090 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 25170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17440 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 25510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17170 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 25420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17470 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 25460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O, P                            
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: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17470 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 25390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, R, S, T                            
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: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17680 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 25070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: U, V, W, X                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     HIS A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     HIS B     9                                                      
REMARK 465     HIS B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ARG C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     HIS C     5                                                      
REMARK 465     HIS C     6                                                      
REMARK 465     HIS C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     HIS C     9                                                      
REMARK 465     HIS C    10                                                      
REMARK 465     GLY C    11                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ARG D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     HIS D     5                                                      
REMARK 465     HIS D     6                                                      
REMARK 465     HIS D     7                                                      
REMARK 465     HIS D     8                                                      
REMARK 465     HIS D     9                                                      
REMARK 465     HIS D    10                                                      
REMARK 465     GLY D    11                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ARG E     2                                                      
REMARK 465     GLY E     3                                                      
REMARK 465     SER E     4                                                      
REMARK 465     HIS E     5                                                      
REMARK 465     HIS E     6                                                      
REMARK 465     HIS E     7                                                      
REMARK 465     HIS E     8                                                      
REMARK 465     HIS E     9                                                      
REMARK 465     HIS E    10                                                      
REMARK 465     GLY E    11                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ARG F     2                                                      
REMARK 465     GLY F     3                                                      
REMARK 465     SER F     4                                                      
REMARK 465     HIS F     5                                                      
REMARK 465     HIS F     6                                                      
REMARK 465     HIS F     7                                                      
REMARK 465     HIS F     8                                                      
REMARK 465     HIS F     9                                                      
REMARK 465     HIS F    10                                                      
REMARK 465     GLY F    11                                                      
REMARK 465     MET G     1                                                      
REMARK 465     ARG G     2                                                      
REMARK 465     GLY G     3                                                      
REMARK 465     SER G     4                                                      
REMARK 465     HIS G     5                                                      
REMARK 465     HIS G     6                                                      
REMARK 465     HIS G     7                                                      
REMARK 465     HIS G     8                                                      
REMARK 465     HIS G     9                                                      
REMARK 465     HIS G    10                                                      
REMARK 465     GLY G    11                                                      
REMARK 465     MET H     1                                                      
REMARK 465     ARG H     2                                                      
REMARK 465     GLY H     3                                                      
REMARK 465     SER H     4                                                      
REMARK 465     HIS H     5                                                      
REMARK 465     HIS H     6                                                      
REMARK 465     HIS H     7                                                      
REMARK 465     HIS H     8                                                      
REMARK 465     HIS H     9                                                      
REMARK 465     HIS H    10                                                      
REMARK 465     GLY H    11                                                      
REMARK 465     LEU H   222                                                      
REMARK 465     MET I     1                                                      
REMARK 465     ARG I     2                                                      
REMARK 465     GLY I     3                                                      
REMARK 465     SER I     4                                                      
REMARK 465     HIS I     5                                                      
REMARK 465     HIS I     6                                                      
REMARK 465     HIS I     7                                                      
REMARK 465     HIS I     8                                                      
REMARK 465     HIS I     9                                                      
REMARK 465     HIS I    10                                                      
REMARK 465     GLY I    11                                                      
REMARK 465     MET J     1                                                      
REMARK 465     ARG J     2                                                      
REMARK 465     GLY J     3                                                      
REMARK 465     SER J     4                                                      
REMARK 465     HIS J     5                                                      
REMARK 465     HIS J     6                                                      
REMARK 465     HIS J     7                                                      
REMARK 465     HIS J     8                                                      
REMARK 465     HIS J     9                                                      
REMARK 465     HIS J    10                                                      
REMARK 465     GLY J    11                                                      
REMARK 465     MET K     1                                                      
REMARK 465     ARG K     2                                                      
REMARK 465     GLY K     3                                                      
REMARK 465     SER K     4                                                      
REMARK 465     HIS K     5                                                      
REMARK 465     HIS K     6                                                      
REMARK 465     HIS K     7                                                      
REMARK 465     HIS K     8                                                      
REMARK 465     HIS K     9                                                      
REMARK 465     HIS K    10                                                      
REMARK 465     GLY K    11                                                      
REMARK 465     MET L     1                                                      
REMARK 465     ARG L     2                                                      
REMARK 465     GLY L     3                                                      
REMARK 465     SER L     4                                                      
REMARK 465     HIS L     5                                                      
REMARK 465     HIS L     6                                                      
REMARK 465     HIS L     7                                                      
REMARK 465     HIS L     8                                                      
REMARK 465     HIS L     9                                                      
REMARK 465     HIS L    10                                                      
REMARK 465     GLY L    11                                                      
REMARK 465     MET M     1                                                      
REMARK 465     ARG M     2                                                      
REMARK 465     GLY M     3                                                      
REMARK 465     SER M     4                                                      
REMARK 465     HIS M     5                                                      
REMARK 465     HIS M     6                                                      
REMARK 465     HIS M     7                                                      
REMARK 465     HIS M     8                                                      
REMARK 465     HIS M     9                                                      
REMARK 465     HIS M    10                                                      
REMARK 465     GLY M    11                                                      
REMARK 465     MET N     1                                                      
REMARK 465     ARG N     2                                                      
REMARK 465     GLY N     3                                                      
REMARK 465     SER N     4                                                      
REMARK 465     HIS N     5                                                      
REMARK 465     HIS N     6                                                      
REMARK 465     HIS N     7                                                      
REMARK 465     HIS N     8                                                      
REMARK 465     HIS N     9                                                      
REMARK 465     HIS N    10                                                      
REMARK 465     GLY N    11                                                      
REMARK 465     MET O     1                                                      
REMARK 465     ARG O     2                                                      
REMARK 465     GLY O     3                                                      
REMARK 465     SER O     4                                                      
REMARK 465     HIS O     5                                                      
REMARK 465     HIS O     6                                                      
REMARK 465     HIS O     7                                                      
REMARK 465     HIS O     8                                                      
REMARK 465     HIS O     9                                                      
REMARK 465     HIS O    10                                                      
REMARK 465     GLY O    11                                                      
REMARK 465     MET P     1                                                      
REMARK 465     ARG P     2                                                      
REMARK 465     GLY P     3                                                      
REMARK 465     SER P     4                                                      
REMARK 465     HIS P     5                                                      
REMARK 465     HIS P     6                                                      
REMARK 465     HIS P     7                                                      
REMARK 465     HIS P     8                                                      
REMARK 465     HIS P     9                                                      
REMARK 465     HIS P    10                                                      
REMARK 465     GLY P    11                                                      
REMARK 465     MET Q     1                                                      
REMARK 465     ARG Q     2                                                      
REMARK 465     GLY Q     3                                                      
REMARK 465     SER Q     4                                                      
REMARK 465     HIS Q     5                                                      
REMARK 465     HIS Q     6                                                      
REMARK 465     HIS Q     7                                                      
REMARK 465     HIS Q     8                                                      
REMARK 465     HIS Q     9                                                      
REMARK 465     HIS Q    10                                                      
REMARK 465     GLY Q    11                                                      
REMARK 465     MET R     1                                                      
REMARK 465     ARG R     2                                                      
REMARK 465     GLY R     3                                                      
REMARK 465     SER R     4                                                      
REMARK 465     HIS R     5                                                      
REMARK 465     HIS R     6                                                      
REMARK 465     HIS R     7                                                      
REMARK 465     HIS R     8                                                      
REMARK 465     HIS R     9                                                      
REMARK 465     HIS R    10                                                      
REMARK 465     GLY R    11                                                      
REMARK 465     MET S     1                                                      
REMARK 465     ARG S     2                                                      
REMARK 465     GLY S     3                                                      
REMARK 465     SER S     4                                                      
REMARK 465     HIS S     5                                                      
REMARK 465     HIS S     6                                                      
REMARK 465     HIS S     7                                                      
REMARK 465     HIS S     8                                                      
REMARK 465     HIS S     9                                                      
REMARK 465     HIS S    10                                                      
REMARK 465     GLY S    11                                                      
REMARK 465     MET T     1                                                      
REMARK 465     ARG T     2                                                      
REMARK 465     GLY T     3                                                      
REMARK 465     SER T     4                                                      
REMARK 465     HIS T     5                                                      
REMARK 465     HIS T     6                                                      
REMARK 465     HIS T     7                                                      
REMARK 465     HIS T     8                                                      
REMARK 465     HIS T     9                                                      
REMARK 465     HIS T    10                                                      
REMARK 465     GLY T    11                                                      
REMARK 465     MET U     1                                                      
REMARK 465     ARG U     2                                                      
REMARK 465     GLY U     3                                                      
REMARK 465     SER U     4                                                      
REMARK 465     HIS U     5                                                      
REMARK 465     HIS U     6                                                      
REMARK 465     HIS U     7                                                      
REMARK 465     HIS U     8                                                      
REMARK 465     HIS U     9                                                      
REMARK 465     HIS U    10                                                      
REMARK 465     GLY U    11                                                      
REMARK 465     MET V     1                                                      
REMARK 465     ARG V     2                                                      
REMARK 465     GLY V     3                                                      
REMARK 465     SER V     4                                                      
REMARK 465     HIS V     5                                                      
REMARK 465     HIS V     6                                                      
REMARK 465     HIS V     7                                                      
REMARK 465     HIS V     8                                                      
REMARK 465     HIS V     9                                                      
REMARK 465     HIS V    10                                                      
REMARK 465     GLY V    11                                                      
REMARK 465     MET W     1                                                      
REMARK 465     ARG W     2                                                      
REMARK 465     GLY W     3                                                      
REMARK 465     SER W     4                                                      
REMARK 465     HIS W     5                                                      
REMARK 465     HIS W     6                                                      
REMARK 465     HIS W     7                                                      
REMARK 465     HIS W     8                                                      
REMARK 465     HIS W     9                                                      
REMARK 465     HIS W    10                                                      
REMARK 465     GLY W    11                                                      
REMARK 465     MET X     1                                                      
REMARK 465     ARG X     2                                                      
REMARK 465     GLY X     3                                                      
REMARK 465     SER X     4                                                      
REMARK 465     HIS X     5                                                      
REMARK 465     HIS X     6                                                      
REMARK 465     HIS X     7                                                      
REMARK 465     HIS X     8                                                      
REMARK 465     HIS X     9                                                      
REMARK 465     HIS X    10                                                      
REMARK 465     GLY X    11                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU F   31   CG    CD    OE1   OE2                               
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   O    TYR F    27     N    ALA F    29              2.13            
REMARK 500   O    SER P    35     O    HOH P  2938              2.17            
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    TYR F  25   N   -  CA  -  C   ANGL. DEV. = -17.1 DEGREES          
REMARK 500    ALA F  29   N   -  CA  -  C   ANGL. DEV. = -26.7 DEGREES          
REMARK 500    PRO H  32   CA  -  N   -  CD  ANGL. DEV. = -10.0 DEGREES          
REMARK 500    PRO H  32   C   -  N   -  CA  ANGL. DEV. =  38.8 DEGREES          
REMARK 500    PRO H  32   C   -  N   -  CD  ANGL. DEV. = -47.2 DEGREES          
REMARK 500    ALA O 142   N   -  CA  -  C   ANGL. DEV. = -16.3 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    LYS A  45      -60.55   -104.41                                   
REMARK 500    GLU A 151       71.21     46.87                                   
REMARK 500    LYS A 160     -125.00     57.37                                   
REMARK 500    ASP A 168      -12.85     79.64                                   
REMARK 500    TYR A 182      -19.91   -150.53                                   
REMARK 500    LYS A 187     -141.85     58.40                                   
REMARK 500    LYS B  45      -62.78    -94.87                                   
REMARK 500    GLU B 151       73.28     48.54                                   
REMARK 500    LYS B 160     -133.45     58.32                                   
REMARK 500    ASP B 168      -21.67     79.42                                   
REMARK 500    TYR B 182      -13.22   -157.07                                   
REMARK 500    LYS B 187     -120.36     61.38                                   
REMARK 500    LYS C 160     -125.11     62.53                                   
REMARK 500    ASP C 168      -17.07     66.65                                   
REMARK 500    TYR C 182      -24.44   -153.24                                   
REMARK 500    LYS C 187     -138.83     55.53                                   
REMARK 500    LYS D  45      -70.99    -90.81                                   
REMARK 500    ILE D  71      145.01   -175.35                                   
REMARK 500    PRO D 100      143.85    -39.00                                   
REMARK 500    GLU D 151       66.18     39.42                                   
REMARK 500    LYS D 160     -127.21     58.06                                   
REMARK 500    ASP D 168      -25.34     79.18                                   
REMARK 500    TYR D 182      -27.95   -149.26                                   
REMARK 500    LYS D 187     -127.17     55.09                                   
REMARK 500    ALA D 219       43.74    -74.23                                   
REMARK 500    LYS E  45      -64.12   -109.48                                   
REMARK 500    ALA E  69      149.00   -179.25                                   
REMARK 500    GLN E  70     -154.45    -84.30                                   
REMARK 500    ILE E  71      135.99    176.88                                   
REMARK 500    LEU E 149      -38.34    -37.60                                   
REMARK 500    GLU E 151       94.96     44.79                                   
REMARK 500    GLN E 152      146.69   -176.70                                   
REMARK 500    LYS E 160     -128.66     52.84                                   
REMARK 500    ASP E 168      -20.40     74.75                                   
REMARK 500    TYR E 182      -19.80   -154.14                                   
REMARK 500    LYS E 187     -135.99     52.35                                   
REMARK 500    TRP E 198       -8.46    -58.36                                   
REMARK 500    PRO F  21      166.10    -48.52                                   
REMARK 500    LEU F  23      -20.15    109.79                                   
REMARK 500    PRO F  24      138.12    -22.60                                   
REMARK 500    TYR F  25        7.29    109.93                                   
REMARK 500    ALA F  26      152.69    -13.27                                   
REMARK 500    TYR F  27      127.67     11.99                                   
REMARK 500    ASN F  28       -0.69     37.15                                   
REMARK 500    LEU F  30      127.05    171.77                                   
REMARK 500    GLU F  31      138.99    -14.07                                   
REMARK 500    SER F  35      159.99    -41.65                                   
REMARK 500    LYS F  45      -67.46    -99.83                                   
REMARK 500    PRO F 100      162.33    -40.79                                   
REMARK 500    ASN F 135       20.92    -79.35                                   
REMARK 500    GLU F 137      103.32    -56.33                                   
REMARK 500    GLU F 151       72.92     35.91                                   
REMARK 500    LYS F 160     -118.42     64.03                                   
REMARK 500    ASP F 168      -14.70     73.17                                   
REMARK 500    HIS F 180       28.41    -74.61                                   
REMARK 500    TYR F 182      -40.73   -144.62                                   
REMARK 500    LEU F 184      -27.50    129.77                                   
REMARK 500    GLN F 185      -51.26   -123.77                                   
REMARK 500    LYS F 187     -134.51     58.62                                   
REMARK 500    SER F 192      -20.85   -155.10                                   
REMARK 500    ASN F 196       -4.48    -56.93                                   
REMARK 500    ASN F 199       13.86    -64.28                                   
REMARK 500    VAL F 200       17.69   -148.21                                   
REMARK 500    ALA F 219       44.83    -89.68                                   
REMARK 500    LYS G  45      -69.07    -95.99                                   
REMARK 500    PRO G 100      129.32    -39.33                                   
REMARK 500    LYS G 117      -84.84    -66.10                                   
REMARK 500    SER G 121      165.75    163.37                                   
REMARK 500    PRO G 148      -71.06    -52.27                                   
REMARK 500    LEU G 149      -67.78    -28.20                                   
REMARK 500    LYS G 160     -131.13     63.34                                   
REMARK 500    ASP G 168      -16.10     61.56                                   
REMARK 500    TYR G 182      -18.82   -150.70                                   
REMARK 500    LYS G 187     -132.24     57.79                                   
REMARK 500    TYR H  25     -149.66   -110.82                                   
REMARK 500    PRO H  32        3.08    102.56                                   
REMARK 500    ALA H  36        7.81    -66.43                                   
REMARK 500    GLU H  37      -76.20    -90.99                                   
REMARK 500    LYS H  45      -66.91    -96.42                                   
REMARK 500    ALA H  69      144.56    165.88                                   
REMARK 500    GLN H  70     -172.67    -62.06                                   
REMARK 500    PRO H 100      144.94    -39.69                                   
REMARK 500    GLU H 151       72.91     49.52                                   
REMARK 500    LYS H 160     -124.88     66.14                                   
REMARK 500    ASP H 168      -10.47     65.08                                   
REMARK 500    TYR H 182     -126.35   -147.96                                   
REMARK 500    TYR H 183      -72.32     57.75                                   
REMARK 500    LEU H 184      -17.44    -45.10                                   
REMARK 500    LYS H 187     -117.40     52.59                                   
REMARK 500    ASP H 189       82.95    -62.77                                   
REMARK 500    ALA H 219       46.93    -79.72                                   
REMARK 500    LYS I  45      -62.88   -108.71                                   
REMARK 500    GLN I  70     -169.15    -77.22                                   
REMARK 500    ILE I  71      137.07   -170.11                                   
REMARK 500    LYS I 160     -126.83     57.27                                   
REMARK 500    ALA I 167      130.83    -39.39                                   
REMARK 500    ASP I 168      -18.24     75.71                                   
REMARK 500    TYR I 182      -19.78   -151.98                                   
REMARK 500    LYS I 187     -141.41     51.48                                   
REMARK 500    ALA I 219       55.62    -91.13                                   
REMARK 500    LYS I 221       71.16     47.52                                   
REMARK 500    LYS J  45      -68.16   -100.97                                   
REMARK 500    LYS J 160     -129.56     60.09                                   
REMARK 500    ASP J 168      -26.06     76.12                                   
REMARK 500    TYR J 182      -22.06   -145.83                                   
REMARK 500    LYS J 187     -135.33     60.95                                   
REMARK 500    LYS J 221       83.14     46.62                                   
REMARK 500    GLU K 151       70.30     48.75                                   
REMARK 500    LYS K 160     -128.09     57.32                                   
REMARK 500    ASP K 168      -21.94     78.64                                   
REMARK 500    TYR K 182      -26.98   -152.94                                   
REMARK 500    LYS K 187     -142.18     52.63                                   
REMARK 500    ALA K 219       66.79   -104.93                                   
REMARK 500    LYS L  45      -63.99   -103.01                                   
REMARK 500    ILE L  71      145.08   -171.04                                   
REMARK 500    LYS L 160     -135.93     59.75                                   
REMARK 500    ASP L 168      -21.67     71.76                                   
REMARK 500    TYR L 182      -19.27   -154.29                                   
REMARK 500    LYS L 187     -137.16     52.82                                   
REMARK 500    ALA L 219       49.86    -80.26                                   
REMARK 500    LYS M  45      -63.17    -92.77                                   
REMARK 500    GLU M 151       81.50     50.07                                   
REMARK 500    LYS M 160     -128.87     58.98                                   
REMARK 500    ASP M 168      -19.31     74.47                                   
REMARK 500    TYR M 182      -16.24   -148.88                                   
REMARK 500    LYS M 187     -138.22     55.91                                   
REMARK 500    ASN M 199        0.42    -65.54                                   
REMARK 500    LYS M 221       79.69     50.17                                   
REMARK 500    LYS N  45      -64.17   -100.82                                   
REMARK 500    ALA N  69      136.92   -172.35                                   
REMARK 500    GLN N  70     -178.21    -69.29                                   
REMARK 500    LYS N 160     -123.53     57.34                                   
REMARK 500    ASP N 168      -18.03     65.23                                   
REMARK 500    TYR N 182      -17.62   -149.42                                   
REMARK 500    LYS N 187     -131.95     52.89                                   
REMARK 500    ALA N 219       49.51    -80.22                                   
REMARK 500    LYS N 221       62.59     66.24                                   
REMARK 500    LYS O  45      -67.56    -95.67                                   
REMARK 500    ALA O  69      138.68    176.62                                   
REMARK 500    GLN O  70     -145.31    -71.22                                   
REMARK 500    ILE O  71      145.39    175.53                                   
REMARK 500    GLU O 151       85.70     49.44                                   
REMARK 500    LYS O 160     -127.17     56.55                                   
REMARK 500    ASP O 168      -26.18     77.58                                   
REMARK 500    TYR O 182      -14.53   -151.48                                   
REMARK 500    LYS O 187     -135.05     52.72                                   
REMARK 500    ALA O 219       49.92    -86.11                                   
REMARK 500    LYS P  45      -60.92   -101.69                                   
REMARK 500    GLU P 151       70.99     49.29                                   
REMARK 500    LYS P 160     -117.19     58.69                                   
REMARK 500    ASP P 168      -14.71     72.77                                   
REMARK 500    TYR P 182      -26.74   -154.26                                   
REMARK 500    LYS P 187     -138.23     55.36                                   
REMARK 500    LYS P 221        6.64     54.09                                   
REMARK 500    GLU Q 151       74.43     34.40                                   
REMARK 500    LYS Q 160     -133.37     60.86                                   
REMARK 500    ASP Q 168      -20.77     74.42                                   
REMARK 500    TYR Q 182      -22.60   -159.83                                   
REMARK 500    LYS Q 187     -136.97     51.43                                   
REMARK 500    LYS Q 221      -53.61   -127.55                                   
REMARK 500    GLU R  31      -38.81    -39.22                                   
REMARK 500    PRO R  32      -70.37    -57.73                                   
REMARK 500    LYS R  45      -64.29   -103.37                                   
REMARK 500    GLU R 151       70.61     52.68                                   
REMARK 500    LYS R 160     -128.69     57.74                                   
REMARK 500    ASP R 168      -23.27     77.48                                   
REMARK 500    HIS R 180        3.17    -67.06                                   
REMARK 500    TYR R 182      -14.00   -162.27                                   
REMARK 500    LYS R 187     -132.47     56.87                                   
REMARK 500    LYS S 160     -127.56     60.38                                   
REMARK 500    ASP S 168      -11.29     71.87                                   
REMARK 500    TYR S 182      -23.35   -154.05                                   
REMARK 500    LYS S 187     -136.84     59.10                                   
REMARK 500    LYS S 221      102.38     53.33                                   
REMARK 500    LYS T  45      -76.46    -99.50                                   
REMARK 500    ALA T  69      159.71    179.20                                   
REMARK 500    PRO T 100      134.76    -38.29                                   
REMARK 500    GLU T 151       72.67     47.20                                   
REMARK 500    LYS T 160     -131.94     59.04                                   
REMARK 500    ASP T 168      -16.39     81.13                                   
REMARK 500    HIS T 180        5.74    -59.69                                   
REMARK 500    TYR T 182      -30.48   -153.44                                   
REMARK 500    LYS T 187     -134.08     60.59                                   
REMARK 500    TRP T 198       12.38    -65.78                                   
REMARK 500    LYS T 221       82.04     57.54                                   
REMARK 500    LYS U  45      -66.93    -96.36                                   
REMARK 500    ILE U  71      125.15   -171.87                                   
REMARK 500    GLU U 151       72.20     47.59                                   
REMARK 500    LYS U 160     -133.45     54.59                                   
REMARK 500    ASP U 168      -26.43     73.51                                   
REMARK 500    TYR U 182      -14.14   -149.52                                   
REMARK 500    LYS U 187     -132.28     55.05                                   
REMARK 500    ALA U 219       55.16    -96.82                                   
REMARK 500    LEU U 220      -74.12   -108.82                                   
REMARK 500    LYS U 221       96.16    -62.33                                   
REMARK 500    LYS V  45      -70.30    -98.76                                   
REMARK 500    ALA V  69      165.98    177.73                                   
REMARK 500    PRO V  99      150.08    -49.65                                   
REMARK 500    LYS V 160     -129.30     62.23                                   
REMARK 500    ASP V 168      -23.30     68.32                                   
REMARK 500    TYR V 182      -21.83   -152.03                                   
REMARK 500    LYS V 187     -136.59     56.52                                   
REMARK 500    GLU W 151       74.38     47.76                                   
REMARK 500    LYS W 160     -132.81     54.13                                   
REMARK 500    ASP W 168      -21.48     78.22                                   
REMARK 500    TYR W 182      -20.33   -147.84                                   
REMARK 500    LYS W 187     -135.83     54.99                                   
REMARK 500    LYS X  45      -65.13   -103.03                                   
REMARK 500    PRO X 100      144.80    -38.39                                   
REMARK 500    SER X 121      170.45    173.38                                   
REMARK 500    GLU X 151       76.67     45.01                                   
REMARK 500    LYS X 160     -121.39     59.75                                   
REMARK 500    ASP X 168      -11.39     72.83                                   
REMARK 500    HIS X 180        7.49    -69.95                                   
REMARK 500    TYR X 182      -17.58   -159.16                                   
REMARK 500    LYS X 187     -131.23     52.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR B  18         0.07    SIDE_CHAIN                              
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 ACT B 302                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 304                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 305                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F 306                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT H 308                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT J 310                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT L 312                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT M 313                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT N 314                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT O 315                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT P 316                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT Q 317                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT R 318                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT S 319                 
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT T 320                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT U 321                 
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT V 322                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT W 323                 
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT X 324                 
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 402                 
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME D 404                 
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME F 406                 
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME H 408                 
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME I 410                 
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME K 412                 
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME N 414                 
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME P 416                 
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME Q 418                 
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME T 420                 
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME V 422                 
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME X 424                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1IKS   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH A METAL ION.                         
DBREF  1P7G A   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G B   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G C   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G D   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G E   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G F   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G G   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G H   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G I   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G J   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G K   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G L   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G M   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G N   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G O   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G P   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G Q   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G R   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G S   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G T   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G U   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G V   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G W   13   222  UNP    O93724   SODF_PYRAE       2    211             
DBREF  1P7G X   13   222  UNP    O93724   SODF_PYRAE       2    211             
SEQADV 1P7G MET A    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG A    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY A    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER A    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS A    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS A    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS A    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS A    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS A    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS A   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY A   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER A   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE A   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE A   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE A  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET B    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG B    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY B    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER B    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS B    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS B    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS B    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS B    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS B    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS B   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY B   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER B   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE B   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE B   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE B  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET C    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG C    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY C    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER C    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS C    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS C    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS C    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS C    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS C    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS C   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY C   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER C   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE C   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE C   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE C  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET D    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG D    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY D    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER D    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS D    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS D    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS D    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS D    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS D    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS D   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY D   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER D   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE D   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE D   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE D  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET E    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG E    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY E    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER E    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS E    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS E    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS E    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS E    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS E    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS E   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY E   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER E   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE E   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE E   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE E  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET F    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG F    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY F    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER F    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS F    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS F    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS F    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS F    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS F    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS F   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY F   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER F   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE F   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE F   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE F  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET G    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG G    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY G    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER G    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS G    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS G    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS G    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS G    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS G    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS G   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY G   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER G   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE G   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE G   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE G  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET H    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG H    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY H    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER H    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS H    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS H    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS H    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS H    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS H    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS H   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY H   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER H   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE H   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE H   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE H  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET I    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG I    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY I    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER I    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS I    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS I    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS I    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS I    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS I    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS I   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY I   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER I   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE I   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE I   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE I  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET J    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG J    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY J    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER J    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS J    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS J    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS J    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS J    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS J    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS J   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY J   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER J   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE J   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE J   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE J  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET K    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG K    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY K    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER K    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS K    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS K    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS K    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS K    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS K    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS K   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY K   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER K   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE K   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE K   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE K  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET L    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG L    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY L    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER L    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS L    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS L    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS L    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS L    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS L    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS L   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY L   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER L   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE L   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE L   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE L  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET M    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG M    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY M    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER M    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS M    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS M    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS M    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS M    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS M    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS M   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY M   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER M   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE M   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE M   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE M  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET N    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG N    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY N    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER N    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS N    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS N    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS N    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS N    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS N    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS N   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY N   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER N   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE N   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE N   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE N  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET O    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG O    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY O    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER O    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS O    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS O    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS O    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS O    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS O    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS O   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY O   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER O   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE O   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE O   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE O  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET P    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG P    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY P    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER P    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS P    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS P    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS P    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS P    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS P    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS P   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY P   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER P   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE P   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE P   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE P  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET Q    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG Q    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY Q    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER Q    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS Q    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS Q    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS Q    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS Q    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS Q    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS Q   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY Q   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER Q   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE Q   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE Q   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE Q  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET R    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG R    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY R    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER R    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS R    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS R    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS R    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS R    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS R    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS R   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY R   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER R   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE R   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE R   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE R  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET S    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG S    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY S    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER S    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS S    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS S    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS S    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS S    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS S    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS S   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY S   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER S   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE S   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE S   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE S  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET T    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG T    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY T    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER T    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS T    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS T    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS T    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS T    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS T    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS T   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY T   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER T   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE T   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE T   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE T  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET U    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG U    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY U    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER U    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS U    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS U    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS U    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS U    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS U    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS U   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY U   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER U   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE U   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE U   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE U  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET V    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG V    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY V    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER V    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS V    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS V    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS V    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS V    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS V    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS V   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY V   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER V   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE V   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE V   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE V  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET W    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG W    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY W    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER W    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS W    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS W    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS W    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS W    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS W    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS W   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY W   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER W   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE W   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE W   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE W  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQADV 1P7G MET X    1  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G ARG X    2  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY X    3  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER X    4  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS X    5  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS X    6  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS X    7  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS X    8  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS X    9  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G HIS X   10  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G GLY X   11  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G SER X   12  UNP  O93724              CLONING ARTIFACT               
SEQADV 1P7G MSE X   39  UNP  O93724    MET    28 MODIFIED RESIDUE               
SEQADV 1P7G MSE X   97  UNP  O93724    MET    86 MODIFIED RESIDUE               
SEQADV 1P7G MSE X  164  UNP  O93724    MET   153 MODIFIED RESIDUE               
SEQRES   1 A  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 A  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 A  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 A  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 A  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 A  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 A  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 A  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 A  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 A  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 A  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 A  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 A  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 A  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 A  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 A  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 A  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 A  222  LEU                                                          
SEQRES   1 B  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 B  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 B  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 B  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 B  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 B  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 B  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 B  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 B  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 B  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 B  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 B  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 B  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 B  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 B  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 B  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 B  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 B  222  LEU                                                          
SEQRES   1 C  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 C  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 C  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 C  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 C  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 C  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 C  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 C  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 C  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 C  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 C  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 C  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 C  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 C  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 C  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 C  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 C  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 C  222  LEU                                                          
SEQRES   1 D  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 D  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 D  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 D  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 D  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 D  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 D  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 D  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 D  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 D  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 D  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 D  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 D  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 D  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 D  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 D  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 D  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 D  222  LEU                                                          
SEQRES   1 E  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 E  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 E  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 E  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 E  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 E  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 E  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 E  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 E  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 E  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 E  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 E  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 E  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 E  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 E  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 E  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 E  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 E  222  LEU                                                          
SEQRES   1 F  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 F  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 F  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 F  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 F  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 F  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 F  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 F  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 F  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 F  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 F  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 F  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 F  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 F  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 F  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 F  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 F  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 F  222  LEU                                                          
SEQRES   1 G  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 G  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 G  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 G  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 G  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 G  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 G  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 G  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 G  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 G  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 G  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 G  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 G  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 G  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 G  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 G  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 G  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 G  222  LEU                                                          
SEQRES   1 H  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 H  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 H  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 H  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 H  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 H  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 H  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 H  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 H  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 H  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 H  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 H  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 H  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 H  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 H  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 H  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 H  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 H  222  LEU                                                          
SEQRES   1 I  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 I  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 I  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 I  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 I  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 I  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 I  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 I  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 I  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 I  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 I  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 I  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 I  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 I  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 I  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 I  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 I  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 I  222  LEU                                                          
SEQRES   1 J  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 J  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 J  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 J  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 J  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 J  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 J  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 J  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 J  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 J  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 J  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 J  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 J  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 J  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 J  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 J  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 J  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 J  222  LEU                                                          
SEQRES   1 K  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 K  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 K  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 K  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 K  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 K  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 K  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 K  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 K  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 K  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 K  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 K  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 K  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 K  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 K  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 K  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 K  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 K  222  LEU                                                          
SEQRES   1 L  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 L  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 L  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 L  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 L  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 L  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 L  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 L  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 L  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 L  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 L  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 L  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 L  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 L  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 L  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 L  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 L  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 L  222  LEU                                                          
SEQRES   1 M  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 M  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 M  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 M  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 M  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 M  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 M  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 M  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 M  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 M  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 M  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 M  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 M  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 M  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 M  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 M  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 M  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 M  222  LEU                                                          
SEQRES   1 N  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 N  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 N  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 N  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 N  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 N  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 N  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 N  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 N  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 N  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 N  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 N  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 N  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 N  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 N  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 N  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 N  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 N  222  LEU                                                          
SEQRES   1 O  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 O  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 O  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 O  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 O  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 O  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 O  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 O  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 O  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 O  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 O  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 O  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 O  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 O  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 O  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 O  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 O  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 O  222  LEU                                                          
SEQRES   1 P  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 P  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 P  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 P  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 P  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 P  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 P  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 P  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 P  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 P  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 P  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 P  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 P  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 P  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 P  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 P  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 P  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 P  222  LEU                                                          
SEQRES   1 Q  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 Q  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 Q  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 Q  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 Q  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 Q  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 Q  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 Q  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 Q  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 Q  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 Q  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 Q  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 Q  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 Q  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 Q  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 Q  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 Q  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 Q  222  LEU                                                          
SEQRES   1 R  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 R  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 R  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 R  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 R  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 R  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 R  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 R  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 R  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 R  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 R  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 R  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 R  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 R  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 R  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 R  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 R  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 R  222  LEU                                                          
SEQRES   1 S  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 S  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 S  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 S  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 S  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 S  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 S  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 S  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 S  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 S  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 S  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 S  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 S  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 S  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 S  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 S  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 S  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 S  222  LEU                                                          
SEQRES   1 T  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 T  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 T  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 T  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 T  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 T  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 T  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 T  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 T  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 T  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 T  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 T  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 T  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 T  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 T  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 T  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 T  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 T  222  LEU                                                          
SEQRES   1 U  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 U  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 U  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 U  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 U  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 U  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 U  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 U  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 U  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 U  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 U  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 U  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 U  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 U  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 U  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 U  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 U  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 U  222  LEU                                                          
SEQRES   1 V  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 V  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 V  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 V  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 V  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 V  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 V  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 V  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 V  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 V  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 V  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 V  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 V  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 V  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 V  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 V  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 V  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 V  222  LEU                                                          
SEQRES   1 W  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 W  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 W  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 W  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 W  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 W  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 W  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 W  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 W  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 W  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 W  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 W  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 W  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 W  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 W  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 W  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 W  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 W  222  LEU                                                          
SEQRES   1 X  222  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER VAL          
SEQRES   2 X  222  THR THR LYS ARG TYR THR LEU PRO PRO LEU PRO TYR ALA          
SEQRES   3 X  222  TYR ASN ALA LEU GLU PRO TYR ILE SER ALA GLU ILE MSE          
SEQRES   4 X  222  GLN LEU HIS HIS GLN LYS HIS HIS GLN GLY TYR VAL ASN          
SEQRES   5 X  222  GLY ALA ASN ALA ALA LEU GLU LYS LEU GLU LYS PHE ARG          
SEQRES   6 X  222  LYS GLY GLU ALA GLN ILE ASP ILE ARG ALA VAL LEU ARG          
SEQRES   7 X  222  ASP LEU SER PHE HIS LEU ASN GLY HIS ILE LEU HIS SER          
SEQRES   8 X  222  ILE PHE TRP PRO ASN MSE ALA PRO PRO GLY LYS GLY GLY          
SEQRES   9 X  222  GLY LYS PRO GLY GLY LYS ILE ALA ASP LEU ILE ASN LYS          
SEQRES  10 X  222  PHE PHE GLY SER PHE GLU LYS PHE LYS GLU GLU PHE SER          
SEQRES  11 X  222  GLN ALA ALA LYS ASN VAL GLU GLY VAL GLY TRP ALA ILE          
SEQRES  12 X  222  LEU VAL TYR GLU PRO LEU GLU GLU GLN LEU LEU ILE LEU          
SEQRES  13 X  222  GLN ILE GLU LYS HIS ASN LEU MSE HIS ALA ALA ASP ALA          
SEQRES  14 X  222  GLN VAL LEU LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  15 X  222  TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR VAL ASP          
SEQRES  16 X  222  ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL GLU ARG          
SEQRES  17 X  222  ARG LEU GLN LYS ALA LEU ASN GLY GLN ILE ALA LEU LYS          
SEQRES  18 X  222  LEU                                                          
MODRES 1P7G MSE A   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE A   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE A  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE B   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE B   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE B  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE C   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE C   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE C  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE D   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE D   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE D  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE E   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE E   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE E  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE F   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE F   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE F  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE G   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE G   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE G  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE H   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE H   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE H  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE I   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE I   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE I  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE J   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE J   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE J  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE K   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE K   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE K  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE L   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE L   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE L  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE M   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE M   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE M  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE N   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE N   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE N  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE O   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE O   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE O  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE P   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE P   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE P  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE Q   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE Q   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE Q  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE R   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE R   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE R  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE S   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE S   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE S  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE T   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE T   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE T  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE U   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE U   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE U  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE V   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE V   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE V  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE W   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE W   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE W  164  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE X   39  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE X   97  MET  SELENOMETHIONINE                                   
MODRES 1P7G MSE X  164  MET  SELENOMETHIONINE                                   
HET    MSE  A  39       8                                                       
HET    MSE  A  97       8                                                       
HET    MSE  A 164       8                                                       
HET    MSE  B  39       8                                                       
HET    MSE  B  97       8                                                       
HET    MSE  B 164       8                                                       
HET    MSE  C  39       8                                                       
HET    MSE  C  97       8                                                       
HET    MSE  C 164       8                                                       
HET    MSE  D  39       8                                                       
HET    MSE  D  97       8                                                       
HET    MSE  D 164       8                                                       
HET    MSE  E  39       8                                                       
HET    MSE  E  97       8                                                       
HET    MSE  E 164       8                                                       
HET    MSE  F  39       8                                                       
HET    MSE  F  97       8                                                       
HET    MSE  F 164       8                                                       
HET    MSE  G  39       8                                                       
HET    MSE  G  97       8                                                       
HET    MSE  G 164       8                                                       
HET    MSE  H  39       8                                                       
HET    MSE  H  97       8                                                       
HET    MSE  H 164       8                                                       
HET    MSE  I  39       8                                                       
HET    MSE  I  97       8                                                       
HET    MSE  I 164       8                                                       
HET    MSE  J  39       8                                                       
HET    MSE  J  97       8                                                       
HET    MSE  J 164       8                                                       
HET    MSE  K  39       8                                                       
HET    MSE  K  97       8                                                       
HET    MSE  K 164       8                                                       
HET    MSE  L  39       8                                                       
HET    MSE  L  97       8                                                       
HET    MSE  L 164       8                                                       
HET    MSE  M  39       8                                                       
HET    MSE  M  97       8                                                       
HET    MSE  M 164       8                                                       
HET    MSE  N  39       8                                                       
HET    MSE  N  97       8                                                       
HET    MSE  N 164       8                                                       
HET    MSE  O  39       8                                                       
HET    MSE  O  97       8                                                       
HET    MSE  O 164       8                                                       
HET    MSE  P  39       8                                                       
HET    MSE  P  97       8                                                       
HET    MSE  P 164       8                                                       
HET    MSE  Q  39       8                                                       
HET    MSE  Q  97       8                                                       
HET    MSE  Q 164       8                                                       
HET    MSE  R  39       8                                                       
HET    MSE  R  97       8                                                       
HET    MSE  R 164       8                                                       
HET    MSE  S  39       8                                                       
HET    MSE  S  97       8                                                       
HET    MSE  S 164       8                                                       
HET    MSE  T  39       8                                                       
HET    MSE  T  97       8                                                       
HET    MSE  T 164       8                                                       
HET    MSE  U  39       8                                                       
HET    MSE  U  97       8                                                       
HET    MSE  U 164       8                                                       
HET    MSE  V  39       8                                                       
HET    MSE  V  97       8                                                       
HET    MSE  V 164       8                                                       
HET    MSE  W  39       8                                                       
HET    MSE  W  97       8                                                       
HET    MSE  W 164       8                                                       
HET    MSE  X  39       8                                                       
HET    MSE  X  97       8                                                       
HET    MSE  X 164       8                                                       
HET    ACT  B 302       4                                                       
HET    ACT  D 304       4                                                       
HET    ACT  E 305       4                                                       
HET    ACT  F 306       4                                                       
HET    ACT  H 308       4                                                       
HET    ACT  J 310       4                                                       
HET    ACT  L 312       4                                                       
HET    ACT  M 313       4                                                       
HET    ACT  N 314       4                                                       
HET    ACT  O 315       4                                                       
HET    ACT  P 316       4                                                       
HET    ACT  Q 317       4                                                       
HET    ACT  R 318       4                                                       
HET    ACT  S 319       4                                                       
HET    ACT  T 320       4                                                       
HET    ACT  U 321       4                                                       
HET    ACT  V 322       4                                                       
HET    ACT  W 323       4                                                       
HET    ACT  X 324       4                                                       
HET    BME  B 402       4                                                       
HET    BME  D 404       4                                                       
HET    BME  F 406       4                                                       
HET    BME  H 408       4                                                       
HET    BME  I 410       4                                                       
HET    BME  K 412       4                                                       
HET    BME  N 414       4                                                       
HET    BME  P 416       4                                                       
HET    BME  Q 418       4                                                       
HET    BME  T 420       4                                                       
HET    BME  V 422       4                                                       
HET    BME  X 424       4                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     ACT ACETATE ION                                                      
HETNAM     BME BETA-MERCAPTOETHANOL                                             
FORMUL   1  MSE    72(C5 H11 N O2 SE)                                           
FORMUL  25  ACT    19(C2 H3 O2 1-)                                              
FORMUL  44  BME    12(C2 H6 O S)                                                
FORMUL  56  HOH   *2536(H2 O)                                                   
HELIX    1   1 SER A   35  LYS A   45  1                                  11    
HELIX    2   2 LYS A   45  LYS A   66  1                                  22    
HELIX    3   3 ASP A   72  TRP A   94  1                                  23    
HELIX    4   4 GLY A  108  GLY A  120  1                                  13    
HELIX    5   5 SER A  121  ASN A  135  1                                  15    
HELIX    6   6 TRP A  178  ALA A  181  5                                   4    
HELIX    7   7 TYR A  182  LYS A  187  1                                   6    
HELIX    8   8 ASP A  189  TRP A  198  1                                  10    
HELIX    9   9 ASN A  199  VAL A  201  5                                   3    
HELIX   10  10 ASN A  202  ASN A  215  1                                  14    
HELIX   11  11 SER B   35  LYS B   45  1                                  11    
HELIX   12  12 LYS B   45  LYS B   66  1                                  22    
HELIX   13  13 ASP B   72  TRP B   94  1                                  23    
HELIX   14  14 GLY B  108  GLY B  120  1                                  13    
HELIX   15  15 SER B  121  ASN B  135  1                                  15    
HELIX   16  16 TRP B  178  ALA B  181  5                                   4    
HELIX   17  17 TYR B  182  LYS B  187  1                                   6    
HELIX   18  18 ASP B  189  TRP B  198  1                                  10    
HELIX   19  19 ASN B  202  ASN B  215  1                                  14    
HELIX   20  20 ALA C   26  GLU C   31  5                                   6    
HELIX   21  21 SER C   35  LYS C   45  1                                  11    
HELIX   22  22 LYS C   45  LYS C   66  1                                  22    
HELIX   23  23 ASP C   72  TRP C   94  1                                  23    
HELIX   24  24 GLY C  108  GLY C  120  1                                  13    
HELIX   25  25 SER C  121  ASN C  135  1                                  15    
HELIX   26  26 TRP C  178  ALA C  181  5                                   4    
HELIX   27  27 TYR C  182  LYS C  187  1                                   6    
HELIX   28  28 ASP C  189  TRP C  198  1                                  10    
HELIX   29  29 ASN C  199  VAL C  201  5                                   3    
HELIX   30  30 ASN C  202  ASN C  215  1                                  14    
HELIX   31  31 ALA D   26  GLU D   31  5                                   6    
HELIX   32  32 SER D   35  LYS D   45  1                                  11    
HELIX   33  33 LYS D   45  GLY D   67  1                                  23    
HELIX   34  34 ASP D   72  TRP D   94  1                                  23    
HELIX   35  35 GLY D  109  GLY D  120  1                                  12    
HELIX   36  36 SER D  121  ASN D  135  1                                  15    
HELIX   37  37 TRP D  178  ALA D  181  5                                   4    
HELIX   38  38 TYR D  182  LYS D  187  1                                   6    
HELIX   39  39 ASP D  189  TRP D  198  1                                  10    
HELIX   40  40 ASN D  202  ASN D  215  1                                  14    
HELIX   41  41 SER E   35  LYS E   45  1                                  11    
HELIX   42  42 LYS E   45  LYS E   66  1                                  22    
HELIX   43  43 ASP E   72  TRP E   94  1                                  23    
HELIX   44  44 GLY E  108  GLY E  120  1                                  13    
HELIX   45  45 SER E  121  ASN E  135  1                                  15    
HELIX   46  46 PRO E  148  GLU E  151  5                                   4    
HELIX   47  47 TRP E  178  ALA E  181  5                                   4    
HELIX   48  48 TYR E  182  LYS E  187  1                                   6    
HELIX   49  49 ASP E  189  TRP E  198  1                                  10    
HELIX   50  50 ASN E  202  ASN E  215  1                                  14    
HELIX   51  51 SER F   35  GLN F   44  1                                  10    
HELIX   52  52 LYS F   45  GLY F   67  1                                  23    
HELIX   53  53 ASP F   72  MSE F   97  1                                  26    
HELIX   54  54 GLY F  109  GLY F  120  1                                  12    
HELIX   55  55 SER F  121  ASN F  135  1                                  15    
HELIX   56  56 TRP F  178  TYR F  182  5                                   5    
HELIX   57  57 VAL F  194  ASN F  199  1                                   6    
HELIX   58  58 ASN F  202  ASN F  215  1                                  14    
HELIX   59  59 SER G   35  LYS G   45  1                                  11    
HELIX   60  60 LYS G   45  LYS G   66  1                                  22    
HELIX   61  61 ASP G   72  TRP G   94  1                                  23    
HELIX   62  62 GLY G  108  GLY G  120  1                                  13    
HELIX   63  63 SER G  121  ASN G  135  1                                  15    
HELIX   64  64 TRP G  178  ALA G  181  5                                   4    
HELIX   65  65 TYR G  182  LYS G  187  1                                   6    
HELIX   66  66 ASP G  189  TRP G  198  1                                  10    
HELIX   67  67 ASN G  202  ASN G  215  1                                  14    
HELIX   68  68 GLU H   37  LYS H   45  1                                   9    
HELIX   69  69 LYS H   45  LYS H   66  1                                  22    
HELIX   70  70 ASP H   72  TRP H   94  1                                  23    
HELIX   71  71 GLY H  108  GLY H  120  1                                  13    
HELIX   72  72 SER H  121  ASN H  135  1                                  15    
HELIX   73  73 TRP H  178  TYR H  182  5                                   5    
HELIX   74  74 ASP H  189  TRP H  198  1                                  10    
HELIX   75  75 ASN H  202  ASN H  215  1                                  14    
HELIX   76  76 SER I   35  LYS I   45  1                                  11    
HELIX   77  77 LYS I   45  LYS I   66  1                                  22    
HELIX   78  78 ASP I   72  TRP I   94  1                                  23    
HELIX   79  79 GLY I  108  GLY I  120  1                                  13    
HELIX   80  80 SER I  121  ASN I  135  1                                  15    
HELIX   81  81 TRP I  178  ALA I  181  5                                   4    
HELIX   82  82 TYR I  182  LYS I  187  1                                   6    
HELIX   83  83 ASP I  189  TRP I  198  1                                  10    
HELIX   84  84 ASN I  199  VAL I  201  5                                   3    
HELIX   85  85 ASN I  202  ASN I  215  1                                  14    
HELIX   86  86 SER J   35  LYS J   45  1                                  11    
HELIX   87  87 LYS J   45  GLY J   67  1                                  23    
HELIX   88  88 ASP J   72  TRP J   94  1                                  23    
HELIX   89  89 GLY J  108  GLY J  120  1                                  13    
HELIX   90  90 SER J  121  ASN J  135  1                                  15    
HELIX   91  91 TRP J  178  ALA J  181  5                                   4    
HELIX   92  92 TYR J  182  LYS J  187  1                                   6    
HELIX   93  93 ASP J  189  TRP J  198  1                                  10    
HELIX   94  94 ASN J  199  VAL J  201  5                                   3    
HELIX   95  95 ASN J  202  ASN J  215  1                                  14    
HELIX   96  96 SER K   35  LYS K   45  1                                  11    
HELIX   97  97 LYS K   45  LYS K   66  1                                  22    
HELIX   98  98 ASP K   72  TRP K   94  1                                  23    
HELIX   99  99 GLY K  108  GLY K  120  1                                  13    
HELIX  100 100 SER K  121  ASN K  135  1                                  15    
HELIX  101 101 TRP K  178  ALA K  181  5                                   4    
HELIX  102 102 TYR K  182  LYS K  187  1                                   6    
HELIX  103 103 ASP K  189  TRP K  198  1                                  10    
HELIX  104 104 ASN K  199  VAL K  201  5                                   3    
HELIX  105 105 ASN K  202  ASN K  215  1                                  14    
HELIX  106 106 SER L   35  LYS L   45  1                                  11    
HELIX  107 107 LYS L   45  LYS L   66  1                                  22    
HELIX  108 108 ASP L   72  TRP L   94  1                                  23    
HELIX  109 109 GLY L  108  GLY L  120  1                                  13    
HELIX  110 110 SER L  121  ASN L  135  1                                  15    
HELIX  111 111 TRP L  178  ALA L  181  5                                   4    
HELIX  112 112 TYR L  182  LYS L  187  1                                   6    
HELIX  113 113 ASP L  189  TRP L  198  1                                  10    
HELIX  114 114 ASN L  199  VAL L  201  5                                   3    
HELIX  115 115 ASN L  202  ASN L  215  1                                  14    
HELIX  116 116 SER M   35  LYS M   45  1                                  11    
HELIX  117 117 LYS M   45  LYS M   66  1                                  22    
HELIX  118 118 ASP M   72  TRP M   94  1                                  23    
HELIX  119 119 GLY M  108  GLY M  120  1                                  13    
HELIX  120 120 SER M  121  ASN M  135  1                                  15    
HELIX  121 121 TRP M  178  ALA M  181  5                                   4    
HELIX  122 122 TYR M  182  LYS M  187  1                                   6    
HELIX  123 123 ASP M  189  TRP M  198  1                                  10    
HELIX  124 124 ASN M  199  VAL M  201  5                                   3    
HELIX  125 125 ASN M  202  ASN M  215  1                                  14    
HELIX  126 126 SER N   35  LYS N   45  1                                  11    
HELIX  127 127 LYS N   45  LYS N   66  1                                  22    
HELIX  128 128 ASP N   72  TRP N   94  1                                  23    
HELIX  129 129 GLY N  108  GLY N  120  1                                  13    
HELIX  130 130 SER N  121  ASN N  135  1                                  15    
HELIX  131 131 TRP N  178  ALA N  181  5                                   4    
HELIX  132 132 TYR N  182  LYS N  187  1                                   6    
HELIX  133 133 ASP N  189  TRP N  198  1                                  10    
HELIX  134 134 ASN N  199  VAL N  201  5                                   3    
HELIX  135 135 ASN N  202  ASN N  215  1                                  14    
HELIX  136 136 SER O   35  LYS O   45  1                                  11    
HELIX  137 137 LYS O   45  LYS O   66  1                                  22    
HELIX  138 138 ASP O   72  TRP O   94  1                                  23    
HELIX  139 139 GLY O  108  GLY O  120  1                                  13    
HELIX  140 140 SER O  121  ASN O  135  1                                  15    
HELIX  141 141 TRP O  178  ALA O  181  5                                   4    
HELIX  142 142 TYR O  182  LYS O  187  1                                   6    
HELIX  143 143 ASP O  189  TRP O  198  1                                  10    
HELIX  144 144 ASN O  199  VAL O  201  5                                   3    
HELIX  145 145 ASN O  202  ASN O  215  1                                  14    
HELIX  146 146 SER P   35  LYS P   45  1                                  11    
HELIX  147 147 LYS P   45  LYS P   66  1                                  22    
HELIX  148 148 ASP P   72  TRP P   94  1                                  23    
HELIX  149 149 GLY P  108  GLY P  120  1                                  13    
HELIX  150 150 SER P  121  ASN P  135  1                                  15    
HELIX  151 151 TRP P  178  ALA P  181  5                                   4    
HELIX  152 152 TYR P  182  LYS P  187  1                                   6    
HELIX  153 153 ASP P  189  TRP P  198  1                                  10    
HELIX  154 154 ASN P  199  VAL P  201  5                                   3    
HELIX  155 155 ASN P  202  ASN P  215  1                                  14    
HELIX  156 156 SER Q   35  LYS Q   45  1                                  11    
HELIX  157 157 LYS Q   45  LYS Q   66  1                                  22    
HELIX  158 158 ASP Q   72  TRP Q   94  1                                  23    
HELIX  159 159 GLY Q  109  GLY Q  120  1                                  12    
HELIX  160 160 SER Q  121  ASN Q  135  1                                  15    
HELIX  161 161 TRP Q  178  ALA Q  181  5                                   4    
HELIX  162 162 TYR Q  182  LYS Q  187  1                                   6    
HELIX  163 163 ASP Q  189  TRP Q  198  1                                  10    
HELIX  164 164 ASN Q  199  VAL Q  201  5                                   3    
HELIX  165 165 ASN Q  202  ASN Q  215  1                                  14    
HELIX  166 166 SER R   35  LYS R   45  1                                  11    
HELIX  167 167 LYS R   45  LYS R   66  1                                  22    
HELIX  168 168 ASP R   72  TRP R   94  1                                  23    
HELIX  169 169 GLY R  108  GLY R  120  1                                  13    
HELIX  170 170 SER R  121  ASN R  135  1                                  15    
HELIX  171 171 TRP R  178  ALA R  181  5                                   4    
HELIX  172 172 TYR R  182  LYS R  187  1                                   6    
HELIX  173 173 ASP R  189  TRP R  198  1                                  10    
HELIX  174 174 ASN R  199  VAL R  201  5                                   3    
HELIX  175 175 ASN R  202  ASN R  215  1                                  14    
HELIX  176 176 SER S   35  LYS S   45  1                                  11    
HELIX  177 177 LYS S   45  LYS S   66  1                                  22    
HELIX  178 178 ASP S   72  TRP S   94  1                                  23    
HELIX  179 179 GLY S  108  GLY S  120  1                                  13    
HELIX  180 180 SER S  121  ASN S  135  1                                  15    
HELIX  181 181 TRP S  178  ALA S  181  5                                   4    
HELIX  182 182 TYR S  182  LYS S  187  1                                   6    
HELIX  183 183 ASP S  189  TRP S  198  1                                  10    
HELIX  184 184 ASN S  199  VAL S  201  5                                   3    
HELIX  185 185 ASN S  202  ASN S  215  1                                  14    
HELIX  186 186 SER T   35  LYS T   45  1                                  11    
HELIX  187 187 LYS T   45  GLY T   67  1                                  23    
HELIX  188 188 ASP T   72  TRP T   94  1                                  23    
HELIX  189 189 GLY T  108  GLY T  120  1                                  13    
HELIX  190 190 SER T  121  ASN T  135  1                                  15    
HELIX  191 191 TRP T  178  ALA T  181  5                                   4    
HELIX  192 192 TYR T  182  LYS T  187  1                                   6    
HELIX  193 193 ASP T  189  TRP T  198  1                                  10    
HELIX  194 194 ASN T  202  ASN T  215  1                                  14    
HELIX  195 195 SER U   35  LYS U   45  1                                  11    
HELIX  196 196 LYS U   45  LYS U   66  1                                  22    
HELIX  197 197 ASP U   72  TRP U   94  1                                  23    
HELIX  198 198 GLY U  108  GLY U  120  1                                  13    
HELIX  199 199 SER U  121  ASN U  135  1                                  15    
HELIX  200 200 TRP U  178  ALA U  181  5                                   4    
HELIX  201 201 TYR U  182  LYS U  187  1                                   6    
HELIX  202 202 ASP U  189  TRP U  198  1                                  10    
HELIX  203 203 ASN U  199  VAL U  201  5                                   3    
HELIX  204 204 ASN U  202  ASN U  215  1                                  14    
HELIX  205 205 SER V   35  LYS V   45  1                                  11    
HELIX  206 206 LYS V   45  LYS V   66  1                                  22    
HELIX  207 207 ASP V   72  TRP V   94  1                                  23    
HELIX  208 208 GLY V  108  GLY V  120  1                                  13    
HELIX  209 209 SER V  121  ASN V  135  1                                  15    
HELIX  210 210 TRP V  178  ALA V  181  5                                   4    
HELIX  211 211 TYR V  182  LYS V  187  1                                   6    
HELIX  212 212 ASP V  189  TRP V  198  1                                  10    
HELIX  213 213 ASN V  199  VAL V  201  5                                   3    
HELIX  214 214 ASN V  202  ASN V  215  1                                  14    
HELIX  215 215 SER W   35  LYS W   45  1                                  11    
HELIX  216 216 LYS W   45  LYS W   66  1                                  22    
HELIX  217 217 ASP W   72  TRP W   94  1                                  23    
HELIX  218 218 GLY W  108  GLY W  120  1                                  13    
HELIX  219 219 SER W  121  ASN W  135  1                                  15    
HELIX  220 220 TRP W  178  ALA W  181  5                                   4    
HELIX  221 221 TYR W  182  LYS W  187  1                                   6    
HELIX  222 222 ASP W  189  TRP W  198  1                                  10    
HELIX  223 223 ASN W  202  ASN W  215  1                                  14    
HELIX  224 224 SER X   35  LYS X   45  1                                  11    
HELIX  225 225 LYS X   45  LYS X   66  1                                  22    
HELIX  226 226 ASP X   72  TRP X   94  1                                  23    
HELIX  227 227 GLY X  108  GLY X  120  1                                  13    
HELIX  228 228 SER X  121  ASN X  135  1                                  15    
HELIX  229 229 TRP X  178  ALA X  181  5                                   4    
HELIX  230 230 TYR X  182  LYS X  187  1                                   6    
HELIX  231 231 ASP X  189  TRP X  198  1                                  10    
HELIX  232 232 ASN X  199  VAL X  201  5                                   3    
HELIX  233 233 ASN X  202  ASN X  215  1                                  14    
SHEET    1   A 3 GLN A 152  GLU A 159  0                                        
SHEET    2   A 3 GLY A 140  GLU A 147 -1  N  GLU A 147   O  GLN A 152           
SHEET    3   A 3 GLN A 170  ASP A 176 -1  O  LEU A 175   N  ALA A 142           
SHEET    1   B 3 GLN B 152  GLU B 159  0                                        
SHEET    2   B 3 GLY B 140  GLU B 147 -1  N  VAL B 145   O  LEU B 154           
SHEET    3   B 3 GLN B 170  ASP B 176 -1  O  LEU B 172   N  LEU B 144           
SHEET    1   C 3 GLN C 152  GLU C 159  0                                        
SHEET    2   C 3 GLY C 140  GLU C 147 -1  N  GLU C 147   O  GLN C 152           
SHEET    3   C 3 GLN C 170  ASP C 176 -1  O  LEU C 172   N  LEU C 144           
SHEET    1   D 3 GLN D 152  GLU D 159  0                                        
SHEET    2   D 3 GLY D 140  GLU D 147 -1  N  GLU D 147   O  GLN D 152           
SHEET    3   D 3 GLN D 170  ASP D 176 -1  O  LEU D 172   N  LEU D 144           
SHEET    1   E 3 LEU E 153  GLU E 159  0                                        
SHEET    2   E 3 GLY E 140  TYR E 146 -1  N  TRP E 141   O  ILE E 158           
SHEET    3   E 3 GLN E 170  ASP E 176 -1  O  LEU E 173   N  LEU E 144           
SHEET    1   F 3 GLN F 152  GLU F 159  0                                        
SHEET    2   F 3 GLY F 140  GLU F 147 -1  N  TRP F 141   O  ILE F 158           
SHEET    3   F 3 GLN F 170  ASP F 176 -1  O  LEU F 172   N  LEU F 144           
SHEET    1   G 3 GLN G 152  GLU G 159  0                                        
SHEET    2   G 3 GLY G 140  GLU G 147 -1  N  GLU G 147   O  GLN G 152           
SHEET    3   G 3 GLN G 170  ASP G 176 -1  O  LEU G 172   N  LEU G 144           
SHEET    1   H 3 GLN H 152  GLU H 159  0                                        
SHEET    2   H 3 GLY H 140  GLU H 147 -1  N  GLU H 147   O  GLN H 152           
SHEET    3   H 3 GLN H 170  ASP H 176 -1  O  LEU H 172   N  LEU H 144           
SHEET    1   I 3 GLN I 152  GLU I 159  0                                        
SHEET    2   I 3 GLY I 140  GLU I 147 -1  N  GLU I 147   O  GLN I 152           
SHEET    3   I 3 GLN I 170  ASP I 176 -1  O  LEU I 172   N  LEU I 144           
SHEET    1   J 3 GLN J 152  GLU J 159  0                                        
SHEET    2   J 3 GLY J 140  GLU J 147 -1  N  TRP J 141   O  ILE J 158           
SHEET    3   J 3 GLN J 170  ASP J 176 -1  O  LEU J 172   N  LEU J 144           
SHEET    1   K 3 GLN K 152  GLU K 159  0                                        
SHEET    2   K 3 GLY K 140  GLU K 147 -1  N  VAL K 145   O  LEU K 154           
SHEET    3   K 3 GLN K 170  ASP K 176 -1  O  LEU K 172   N  LEU K 144           
SHEET    1   L 3 GLN L 152  GLU L 159  0                                        
SHEET    2   L 3 GLY L 140  GLU L 147 -1  N  GLU L 147   O  GLN L 152           
SHEET    3   L 3 GLN L 170  ASP L 176 -1  O  LEU L 172   N  LEU L 144           
SHEET    1   M 3 GLN M 152  GLU M 159  0                                        
SHEET    2   M 3 GLY M 140  GLU M 147 -1  N  GLU M 147   O  GLN M 152           
SHEET    3   M 3 GLN M 170  ASP M 176 -1  O  LEU M 172   N  LEU M 144           
SHEET    1   N 3 GLN N 152  GLU N 159  0                                        
SHEET    2   N 3 GLY N 140  GLU N 147 -1  N  GLU N 147   O  GLN N 152           
SHEET    3   N 3 GLN N 170  ASP N 176 -1  O  LEU N 172   N  LEU N 144           
SHEET    1   O 3 GLN O 152  GLU O 159  0                                        
SHEET    2   O 3 GLY O 140  GLU O 147 -1  N  GLU O 147   O  GLN O 152           
SHEET    3   O 3 GLN O 170  ASP O 176 -1  O  LEU O 172   N  LEU O 144           
SHEET    1   P 3 GLN P 152  GLU P 159  0                                        
SHEET    2   P 3 GLY P 140  GLU P 147 -1  N  GLU P 147   O  GLN P 152           
SHEET    3   P 3 GLN P 170  ASP P 176 -1  O  LEU P 172   N  LEU P 144           
SHEET    1   Q 3 GLN Q 152  GLU Q 159  0                                        
SHEET    2   Q 3 GLY Q 140  GLU Q 147 -1  N  GLU Q 147   O  GLN Q 152           
SHEET    3   Q 3 GLN Q 170  ASP Q 176 -1  O  LEU Q 172   N  LEU Q 144           
SHEET    1   R 3 GLN R 152  GLU R 159  0                                        
SHEET    2   R 3 GLY R 140  GLU R 147 -1  N  TRP R 141   O  ILE R 158           
SHEET    3   R 3 GLN R 170  ASP R 176 -1  O  LEU R 172   N  LEU R 144           
SHEET    1   S 3 GLN S 152  GLU S 159  0                                        
SHEET    2   S 3 GLY S 140  GLU S 147 -1  N  GLU S 147   O  GLN S 152           
SHEET    3   S 3 GLN S 170  ASP S 176 -1  O  LEU S 175   N  ALA S 142           
SHEET    1   T 3 GLN T 152  GLU T 159  0                                        
SHEET    2   T 3 GLY T 140  GLU T 147 -1  N  VAL T 145   O  LEU T 154           
SHEET    3   T 3 GLN T 170  ASP T 176 -1  O  LEU T 172   N  LEU T 144           
SHEET    1   U 3 GLN U 152  GLU U 159  0                                        
SHEET    2   U 3 GLY U 140  GLU U 147 -1  N  GLU U 147   O  GLN U 152           
SHEET    3   U 3 GLN U 170  ASP U 176 -1  O  LEU U 172   N  LEU U 144           
SHEET    1   V 3 GLN V 152  GLU V 159  0                                        
SHEET    2   V 3 GLY V 140  GLU V 147 -1  N  GLU V 147   O  GLN V 152           
SHEET    3   V 3 GLN V 170  ASP V 176 -1  O  LEU V 172   N  LEU V 144           
SHEET    1   W 3 GLN W 152  GLU W 159  0                                        
SHEET    2   W 3 GLY W 140  GLU W 147 -1  N  TRP W 141   O  ILE W 158           
SHEET    3   W 3 GLN W 170  ASP W 176 -1  O  LEU W 172   N  LEU W 144           
SHEET    1   X 3 GLN X 152  GLU X 159  0                                        
SHEET    2   X 3 GLY X 140  GLU X 147 -1  N  GLU X 147   O  GLN X 152           
SHEET    3   X 3 GLN X 170  ASP X 176 -1  O  LEU X 175   N  ALA X 142           
LINK         C   ILE A  38                 N   MSE A  39     1555   1555  1.33  
LINK         C   MSE A  39                 N   GLN A  40     1555   1555  1.33  
LINK         C   ASN A  96                 N   MSE A  97     1555   1555  1.33  
LINK         C   MSE A  97                 N   ALA A  98     1555   1555  1.33  
LINK         C   LEU A 163                 N   MSE A 164     1555   1555  1.33  
LINK         C   MSE A 164                 N   HIS A 165     1555   1555  1.33  
LINK         C   ILE B  38                 N   MSE B  39     1555   1555  1.33  
LINK         C   MSE B  39                 N   GLN B  40     1555   1555  1.33  
LINK         C   ASN B  96                 N   MSE B  97     1555   1555  1.33  
LINK         C   MSE B  97                 N   ALA B  98     1555   1555  1.33  
LINK         C   LEU B 163                 N   MSE B 164     1555   1555  1.33  
LINK         C   MSE B 164                 N   HIS B 165     1555   1555  1.33  
LINK         C   ILE C  38                 N   MSE C  39     1555   1555  1.34  
LINK         C   MSE C  39                 N   GLN C  40     1555   1555  1.33  
LINK         C   ASN C  96                 N   MSE C  97     1555   1555  1.33  
LINK         C   MSE C  97                 N   ALA C  98     1555   1555  1.33  
LINK         C   LEU C 163                 N   MSE C 164     1555   1555  1.33  
LINK         C   MSE C 164                 N   HIS C 165     1555   1555  1.33  
LINK         C   ILE D  38                 N   MSE D  39     1555   1555  1.33  
LINK         C   MSE D  39                 N   GLN D  40     1555   1555  1.33  
LINK         C   ASN D  96                 N   MSE D  97     1555   1555  1.33  
LINK         C   MSE D  97                 N   ALA D  98     1555   1555  1.33  
LINK         C   LEU D 163                 N   MSE D 164     1555   1555  1.33  
LINK         C   MSE D 164                 N   HIS D 165     1555   1555  1.33  
LINK         C   ILE E  38                 N   MSE E  39     1555   1555  1.33  
LINK         C   MSE E  39                 N   GLN E  40     1555   1555  1.33  
LINK         C   ASN E  96                 N   MSE E  97     1555   1555  1.34  
LINK         C   MSE E  97                 N   ALA E  98     1555   1555  1.33  
LINK         C   LEU E 163                 N   MSE E 164     1555   1555  1.34  
LINK         C   MSE E 164                 N   HIS E 165     1555   1555  1.33  
LINK         C   ILE F  38                 N   MSE F  39     1555   1555  1.33  
LINK         C   MSE F  39                 N   GLN F  40     1555   1555  1.33  
LINK         C   ASN F  96                 N   MSE F  97     1555   1555  1.33  
LINK         C   MSE F  97                 N   ALA F  98     1555   1555  1.33  
LINK         C   LEU F 163                 N   MSE F 164     1555   1555  1.33  
LINK         C   MSE F 164                 N   HIS F 165     1555   1555  1.33  
LINK         C   ILE G  38                 N   MSE G  39     1555   1555  1.33  
LINK         C   MSE G  39                 N   GLN G  40     1555   1555  1.33  
LINK         C   ASN G  96                 N   MSE G  97     1555   1555  1.33  
LINK         C   MSE G  97                 N   ALA G  98     1555   1555  1.33  
LINK         C   LEU G 163                 N   MSE G 164     1555   1555  1.34  
LINK         C   MSE G 164                 N   HIS G 165     1555   1555  1.33  
LINK         C   ILE H  38                 N   MSE H  39     1555   1555  1.33  
LINK         C   MSE H  39                 N   GLN H  40     1555   1555  1.33  
LINK         C   ASN H  96                 N   MSE H  97     1555   1555  1.33  
LINK         C   MSE H  97                 N   ALA H  98     1555   1555  1.33  
LINK         C   LEU H 163                 N   MSE H 164     1555   1555  1.34  
LINK         C   MSE H 164                 N   HIS H 165     1555   1555  1.33  
LINK         C   ILE I  38                 N   MSE I  39     1555   1555  1.33  
LINK         C   MSE I  39                 N   GLN I  40     1555   1555  1.33  
LINK         C   ASN I  96                 N   MSE I  97     1555   1555  1.33  
LINK         C   MSE I  97                 N   ALA I  98     1555   1555  1.33  
LINK         C   LEU I 163                 N   MSE I 164     1555   1555  1.33  
LINK         C   MSE I 164                 N   HIS I 165     1555   1555  1.32  
LINK         C   ILE J  38                 N   MSE J  39     1555   1555  1.33  
LINK         C   MSE J  39                 N   GLN J  40     1555   1555  1.33  
LINK         C   ASN J  96                 N   MSE J  97     1555   1555  1.33  
LINK         C   MSE J  97                 N   ALA J  98     1555   1555  1.33  
LINK         C   LEU J 163                 N   MSE J 164     1555   1555  1.34  
LINK         C   MSE J 164                 N   HIS J 165     1555   1555  1.33  
LINK         C   ILE K  38                 N   MSE K  39     1555   1555  1.33  
LINK         C   MSE K  39                 N   GLN K  40     1555   1555  1.33  
LINK         C   ASN K  96                 N   MSE K  97     1555   1555  1.33  
LINK         C   MSE K  97                 N   ALA K  98     1555   1555  1.33  
LINK         C   LEU K 163                 N   MSE K 164     1555   1555  1.33  
LINK         C   MSE K 164                 N   HIS K 165     1555   1555  1.34  
LINK         C   ILE L  38                 N   MSE L  39     1555   1555  1.33  
LINK         C   MSE L  39                 N   GLN L  40     1555   1555  1.33  
LINK         C   ASN L  96                 N   MSE L  97     1555   1555  1.33  
LINK         C   MSE L  97                 N   ALA L  98     1555   1555  1.33  
LINK         C   LEU L 163                 N   MSE L 164     1555   1555  1.34  
LINK         C   MSE L 164                 N   HIS L 165     1555   1555  1.33  
LINK         C   ILE M  38                 N   MSE M  39     1555   1555  1.33  
LINK         C   MSE M  39                 N   GLN M  40     1555   1555  1.33  
LINK         C   ASN M  96                 N   MSE M  97     1555   1555  1.33  
LINK         C   MSE M  97                 N   ALA M  98     1555   1555  1.33  
LINK         C   LEU M 163                 N   MSE M 164     1555   1555  1.33  
LINK         C   MSE M 164                 N   HIS M 165     1555   1555  1.33  
LINK         C   ILE N  38                 N   MSE N  39     1555   1555  1.33  
LINK         C   MSE N  39                 N   GLN N  40     1555   1555  1.33  
LINK         C   ASN N  96                 N   MSE N  97     1555   1555  1.33  
LINK         C   MSE N  97                 N   ALA N  98     1555   1555  1.33  
LINK         C   LEU N 163                 N   MSE N 164     1555   1555  1.33  
LINK         C   MSE N 164                 N   HIS N 165     1555   1555  1.33  
LINK         C   ILE O  38                 N   MSE O  39     1555   1555  1.33  
LINK         C   MSE O  39                 N   GLN O  40     1555   1555  1.33  
LINK         C   ASN O  96                 N   MSE O  97     1555   1555  1.33  
LINK         C   MSE O  97                 N   ALA O  98     1555   1555  1.33  
LINK         C   LEU O 163                 N   MSE O 164     1555   1555  1.33  
LINK         C   MSE O 164                 N   HIS O 165     1555   1555  1.33  
LINK         C   ILE P  38                 N   MSE P  39     1555   1555  1.33  
LINK         C   MSE P  39                 N   GLN P  40     1555   1555  1.33  
LINK         C   ASN P  96                 N   MSE P  97     1555   1555  1.33  
LINK         C   MSE P  97                 N   ALA P  98     1555   1555  1.33  
LINK         C   LEU P 163                 N   MSE P 164     1555   1555  1.33  
LINK         C   MSE P 164                 N   HIS P 165     1555   1555  1.33  
LINK         C   ILE Q  38                 N   MSE Q  39     1555   1555  1.33  
LINK         C   MSE Q  39                 N   GLN Q  40     1555   1555  1.33  
LINK         C   ASN Q  96                 N   MSE Q  97     1555   1555  1.33  
LINK         C   MSE Q  97                 N   ALA Q  98     1555   1555  1.33  
LINK         C   LEU Q 163                 N   MSE Q 164     1555   1555  1.34  
LINK         C   MSE Q 164                 N   HIS Q 165     1555   1555  1.33  
LINK         C   ILE R  38                 N   MSE R  39     1555   1555  1.33  
LINK         C   MSE R  39                 N   GLN R  40     1555   1555  1.33  
LINK         C   ASN R  96                 N   MSE R  97     1555   1555  1.33  
LINK         C   MSE R  97                 N   ALA R  98     1555   1555  1.33  
LINK         C   LEU R 163                 N   MSE R 164     1555   1555  1.34  
LINK         C   MSE R 164                 N   HIS R 165     1555   1555  1.33  
LINK         C   ILE S  38                 N   MSE S  39     1555   1555  1.34  
LINK         C   MSE S  39                 N   GLN S  40     1555   1555  1.33  
LINK         C   ASN S  96                 N   MSE S  97     1555   1555  1.33  
LINK         C   MSE S  97                 N   ALA S  98     1555   1555  1.33  
LINK         C   LEU S 163                 N   MSE S 164     1555   1555  1.33  
LINK         C   MSE S 164                 N   HIS S 165     1555   1555  1.32  
LINK         C   ILE T  38                 N   MSE T  39     1555   1555  1.33  
LINK         C   MSE T  39                 N   GLN T  40     1555   1555  1.33  
LINK         C   ASN T  96                 N   MSE T  97     1555   1555  1.33  
LINK         C   MSE T  97                 N   ALA T  98     1555   1555  1.33  
LINK         C   LEU T 163                 N   MSE T 164     1555   1555  1.33  
LINK         C   MSE T 164                 N   HIS T 165     1555   1555  1.33  
LINK         C   ILE U  38                 N   MSE U  39     1555   1555  1.33  
LINK         C   MSE U  39                 N   GLN U  40     1555   1555  1.33  
LINK         C   ASN U  96                 N   MSE U  97     1555   1555  1.33  
LINK         C   MSE U  97                 N   ALA U  98     1555   1555  1.33  
LINK         C   LEU U 163                 N   MSE U 164     1555   1555  1.34  
LINK         C   MSE U 164                 N   HIS U 165     1555   1555  1.33  
LINK         C   ILE V  38                 N   MSE V  39     1555   1555  1.34  
LINK         C   MSE V  39                 N   GLN V  40     1555   1555  1.33  
LINK         C   ASN V  96                 N   MSE V  97     1555   1555  1.33  
LINK         C   MSE V  97                 N   ALA V  98     1555   1555  1.33  
LINK         C   LEU V 163                 N   MSE V 164     1555   1555  1.34  
LINK         C   MSE V 164                 N   HIS V 165     1555   1555  1.32  
LINK         C   ILE W  38                 N   MSE W  39     1555   1555  1.33  
LINK         C   MSE W  39                 N   GLN W  40     1555   1555  1.33  
LINK         C   ASN W  96                 N   MSE W  97     1555   1555  1.33  
LINK         C   MSE W  97                 N   ALA W  98     1555   1555  1.33  
LINK         C   LEU W 163                 N   MSE W 164     1555   1555  1.33  
LINK         C   MSE W 164                 N   HIS W 165     1555   1555  1.33  
LINK         C   ILE X  38                 N   MSE X  39     1555   1555  1.33  
LINK         C   MSE X  39                 N   GLN X  40     1555   1555  1.33  
LINK         C   ASN X  96                 N   MSE X  97     1555   1555  1.33  
LINK         C   MSE X  97                 N   ALA X  98     1555   1555  1.33  
LINK         C   LEU X 163                 N   MSE X 164     1555   1555  1.33  
LINK         C   MSE X 164                 N   HIS X 165     1555   1555  1.33  
CISPEP   1 GLU A   31    PRO A   32          0         0.11                     
CISPEP   2 GLU B   31    PRO B   32          0         0.39                     
CISPEP   3 GLU C   31    PRO C   32          0         0.12                     
CISPEP   4 GLU D   31    PRO D   32          0         0.41                     
CISPEP   5 GLU E   31    PRO E   32          0         0.04                     
CISPEP   6 GLU G   31    PRO G   32          0        -0.06                     
CISPEP   7 GLU I   31    PRO I   32          0        -3.47                     
CISPEP   8 GLU J   31    PRO J   32          0         0.37                     
CISPEP   9 GLU K   31    PRO K   32          0         0.38                     
CISPEP  10 GLU L   31    PRO L   32          0         0.33                     
CISPEP  11 GLU M   31    PRO M   32          0         0.31                     
CISPEP  12 GLU N   31    PRO N   32          0         0.04                     
CISPEP  13 GLU O   31    PRO O   32          0         0.71                     
CISPEP  14 GLU P   31    PRO P   32          0         0.42                     
CISPEP  15 GLU Q   31    PRO Q   32          0         0.19                     
CISPEP  16 GLU S   31    PRO S   32          0         0.02                     
CISPEP  17 GLU T   31    PRO T   32          0         0.10                     
CISPEP  18 GLU U   31    PRO U   32          0         0.14                     
CISPEP  19 GLU V   31    PRO V   32          0         0.31                     
CISPEP  20 GLU W   31    PRO W   32          0         0.17                     
CISPEP  21 GLU X   31    PRO X   32          0        -0.10                     
SITE     1 AC1  4 SER B  91  ARG B 209  LEU B 220  LYS B 221                    
SITE     1 AC2  4 SER D  91  ARG D 209  LEU D 220  LYS D 221                    
SITE     1 AC3  5 ARG E 209  LEU E 220  LYS E 221  HOH E1169                    
SITE     2 AC3  5 HOH E2727                                                     
SITE     1 AC4  5 SER F  91  ARG F 209  LEU F 220  LYS F 221                    
SITE     2 AC4  5 LEU F 222                                                     
SITE     1 AC5  4 SER H  91  ARG H 209  LEU H 220  LYS H 221                    
SITE     1 AC6  3 ARG J 209  LEU J 220  LYS J 221                               
SITE     1 AC7  6 SER L  91  ARG L 209  LEU L 220  LYS L 221                    
SITE     2 AC7  6 HOH L2798  HOH L2894                                          
SITE     1 AC8  5 SER M  91  ARG M 209  LEU M 220  LYS M 221                    
SITE     2 AC8  5 HOH M2853                                                     
SITE     1 AC9  4 SER N  91  ARG N 209  LEU N 220  LYS N 221                    
SITE     1 BC1  6 SER O  91  ILE O  92  ARG O 209  LEU O 220                    
SITE     2 BC1  6 LYS O 221  HOH O2743                                          
SITE     1 BC2  4 SER P  91  ARG P 209  LEU P 220  LYS P 221                    
SITE     1 BC3  4 SER Q  91  ARG Q 209  LEU Q 220  LYS Q 221                    
SITE     1 BC4  4 SER R  91  ARG R 209  LEU R 220  LYS R 221                    
SITE     1 BC5  5 SER S  91  ARG S 209  LEU S 220  LYS S 221                    
SITE     2 BC5  5 HOH S2761                                                     
SITE     1 BC6  5 LEU Q 149  SER T  91  ARG T 209  LEU T 220                    
SITE     2 BC6  5 LYS T 221                                                     
SITE     1 BC7  3 SER U  91  ARG U 209  LEU U 220                               
SITE     1 BC8  4 SER V  91  ARG V 209  LEU V 220  LYS V 221                    
SITE     1 BC9  4 SER W  91  ARG W 209  LEU W 220  LYS W 221                    
SITE     1 CC1  4 SER X  91  ARG X 209  LEU X 220  LYS X 221                    
SITE     1 CC2  7 ALA A  75  ARG A  78  ASP A  79  ASP B  72                    
SITE     2 CC2  7 ARG B  74  ALA B  75  ARG B  78                               
SITE     1 CC3  8 ALA C  75  ARG C  78  ASP C  79  ASP D  72                    
SITE     2 CC3  8 ARG D  74  ALA D  75  ARG D  78  HOH D2716                    
SITE     1 CC4  6 ALA E  75  ASP E  79  ASP F  72  ARG F  74                    
SITE     2 CC4  6 ALA F  75  ARG F  78                                          
SITE     1 CC5  7 ALA G  75  ARG G  78  ASP G  79  ASP H  72                    
SITE     2 CC5  7 ARG H  74  ALA H  75  ARG H  78                               
SITE     1 CC6  9 ALA I  75  ARG I  78  ASP I  79  HOH I 762                    
SITE     2 CC6  9 ASP J  72  ARG J  74  ALA J  75  ARG J  78                    
SITE     3 CC6  9 HOH J2728                                                     
SITE     1 CC7  7 ALA K  75  ARG K  78  ASP K  79  ARG L  74                    
SITE     2 CC7  7 ALA L  75  ARG L  78  HOH L2549                               
SITE     1 CC8  9 ALA M  75  ARG M  78  ASP M  79  HOH M2911                    
SITE     2 CC8  9 ASP N  72  ARG N  74  ALA N  75  ARG N  78                    
SITE     3 CC8  9 HOH N1513                                                     
SITE     1 CC9  7 ALA O  75  ARG O  78  ASP O  79  ASP P  72                    
SITE     2 CC9  7 ARG P  74  ALA P  75  ARG P  78                               
SITE     1 DC1  8 ALA Q  75  ARG Q  78  ASP Q  79  ASP R  72                    
SITE     2 DC1  8 ARG R  74  ALA R  75  ARG R  78  HOH R2742                    
SITE     1 DC2  7 ALA S  75  ARG S  78  ASP S  79  ASP T  72                    
SITE     2 DC2  7 ARG T  74  ALA T  75  ARG T  78                               
SITE     1 DC3  6 ALA U  75  ARG U  78  ASP U  79  ARG V  74                    
SITE     2 DC3  6 ALA V  75  ARG V  78                                          
SITE     1 DC4  9 ALA W  75  ARG W  78  ASP W  79  HOH W2726                    
SITE     2 DC4  9 ASP X  72  ARG X  74  ALA X  75  ARG X  78                    
SITE     3 DC4  9 HOH X1887                                                     
CRYST1  163.429  163.429  172.169  90.00  90.00 120.00 P 32         72          
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      0.006119  0.003533  0.000000        0.00000                         
SCALE2      0.000000  0.007065  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005808        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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