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Database: PDB
Entry: 2I3O
LinkDB: 2I3O
Original site: 2I3O 
HEADER    TRANSFERASE                             19-AUG-06   2I3O              
TITLE     CRYSTAL STRUCTURE OF GAMMA-GLUTAMYL TRANSFERASE RELATED               
TITLE    2 PROTEIN FROM THERMOPLASMA ACIDOPHILUM                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GAMMA-GLUTAMYLTRANSFERASE RELATED PROTEIN;                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOPLASMA ACIDOPHILUM;                       
SOURCE   3 ORGANISM_TAXID: 2303;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CRYSTAL STRUCTURE, GAMMA-GLUTAMYL TRANSFERASE RELATED                 
KEYWDS   2 PROTEIN, THERMOPLASMA ACIDOPHILUM, 6324D, STRUCTURAL                 
KEYWDS   3 GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX            
KEYWDS   4 RESEARCH CENTER FOR STRUCTURAL GENOMICS, NYSGXRC                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.N.RAO,S.ESWARAMOORTHY,S.K.BURLEY,S.SWAMINATHAN,NEW YORK             
AUTHOR   2 SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)                
REVDAT   2   24-FEB-09 2I3O    1       VERSN                                    
REVDAT   1   29-AUG-06 2I3O    0                                                
JRNL        AUTH   K.N.RAO,S.ESWARAMOORTHY,S.K.BURLEY,S.SWAMINATHAN             
JRNL        TITL   CRYSTAL STRUCTURE OF GAMMA-GLUTAMYL TRANSFERASE              
JRNL        TITL 2 RELATED PROTEIN FROM THERMOPLASMA ACIDOPHILUM                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.03 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.03                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.47                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 92146.530                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 151643                         
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) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3836                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.03                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 22791                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2000                       
REMARK   3   BIN FREE R VALUE                    : 0.2350                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 2.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 574                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.010                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15495                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 887                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 11.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.36000                                             
REMARK   3    B22 (A**2) : 0.70000                                              
REMARK   3    B33 (A**2) : -0.34000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.53000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.12                            
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) : 0.24                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.17                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.87                            
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) : 1.160 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.680 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.290 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.240 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 40.62                                                
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: RESIDUES LISTED IN REMARK 465 AND         
REMARK   3  ATOMS LISTED IN REMARK 470 WERE NOT MODELED DUE TO LACK OF          
REMARK   3  ELECTRON DENSITY. RESIDUE ASN254 IN ALL FOUR CHAINS DOES NOT        
REMARK   3  HAVE GOOD GEOMETRY. HOWEVER, THEY FIT THE ELECTRON DENSITY          
REMARK   3  VERY WELL. RESIDUAL DENSITIES NEAR THE ACTIVE SITES HAVE BEEN       
REMARK   3  MODELED AS WATER (39, 40, 45, 167) BUT THEY COULD BE METAL          
REMARK   3  IONS. N TERMINAL SELENOMETHIONINE IS VISIBLE ONLY IN CHAINS A       
REMARK   3  AND D.                                                              
REMARK   4                                                                      
REMARK   4 2I3O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB039096.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUN-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 156657                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.030                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.09500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.38000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELX, SHARP                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MAGNESIUM FORMATE, PH 5.5, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       47.73550            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     ILE A   307                                                      
REMARK 465     ALA A   308                                                      
REMARK 465     GLN A   309                                                      
REMARK 465     HIS A   310                                                      
REMARK 465     ASP A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     ALA A   313                                                      
REMARK 465     ASN A   314                                                      
REMARK 465     GLY A   315                                                      
REMARK 465     LYS A   316                                                      
REMARK 465     LYS A   317                                                      
REMARK 465     ASP A   318                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     ILE B   307                                                      
REMARK 465     ALA B   308                                                      
REMARK 465     GLN B   309                                                      
REMARK 465     HIS B   310                                                      
REMARK 465     ASP B   311                                                      
REMARK 465     SER B   312                                                      
REMARK 465     ALA B   313                                                      
REMARK 465     ASN B   314                                                      
REMARK 465     GLY B   315                                                      
REMARK 465     LYS B   316                                                      
REMARK 465     LYS B   317                                                      
REMARK 465     ASP B   318                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     ILE C   307                                                      
REMARK 465     ALA C   308                                                      
REMARK 465     GLN C   309                                                      
REMARK 465     HIS C   310                                                      
REMARK 465     ASP C   311                                                      
REMARK 465     SER C   312                                                      
REMARK 465     ALA C   313                                                      
REMARK 465     ASN C   314                                                      
REMARK 465     GLY C   315                                                      
REMARK 465     LYS C   316                                                      
REMARK 465     LYS C   317                                                      
REMARK 465     ASP C   318                                                      
REMARK 465     LYS D   317                                                      
REMARK 465     ASP D   318                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  83    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 137    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 281    CG   CD   CE   NZ                                   
REMARK 470     LYS A 298    CG   CD   CE   NZ                                   
REMARK 470     ASN A 306    CG   OD1  ND2                                       
REMARK 470     LYS A 322    CG   CD   CE   NZ                                   
REMARK 470     HIS A 325    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 476    CG   CD   CE   NZ                                   
REMARK 470     ARG A 496    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 137    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 281    CG   CD   CE   NZ                                   
REMARK 470     LYS B 298    CG   CD   CE   NZ                                   
REMARK 470     ASN B 306    CG   OD1  ND2                                       
REMARK 470     LYS B 322    CG   CD   CE   NZ                                   
REMARK 470     LYS B 470    CG   CD   CE   NZ                                   
REMARK 470     ARG B 475    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 496    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  31    CG   CD   CE   NZ                                   
REMARK 470     ARG C 226    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 298    CG   CD   CE   NZ                                   
REMARK 470     LYS C 322    CG   CD   CE   NZ                                   
REMARK 470     ASP C 324    CG   OD1  OD2                                       
REMARK 470     HIS C 325    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS C 361    CG   CD   CE   NZ                                   
REMARK 470     ARG C 466    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 470    CG   CD   CE   NZ                                   
REMARK 470     ARG C 496    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 137    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN D 309    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 322    CG   CD   CE   NZ                                   
REMARK 470     LYS D 470    CG   CD   CE   NZ                                   
REMARK 470     LYS D 476    CG   CD   CE   NZ                                   
REMARK 470     ARG D 496    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    SER D 252   C     PRO D 253   N       0.148                       
REMARK 500    ASN D 254   C     SER D 255   N      -0.164                       
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    ASN A 254   C   -  N   -  CA  ANGL. DEV. =  17.9 DEGREES          
REMARK 500    ASN B 254   C   -  N   -  CA  ANGL. DEV. =  17.9 DEGREES          
REMARK 500    ASN B 254   CA  -  C   -  N   ANGL. DEV. =  13.3 DEGREES          
REMARK 500    SER C 252   CA  -  C   -  N   ANGL. DEV. =  18.0 DEGREES          
REMARK 500    SER C 252   O   -  C   -  N   ANGL. DEV. = -17.8 DEGREES          
REMARK 500    ASN C 254   C   -  N   -  CA  ANGL. DEV. =  17.9 DEGREES          
REMARK 500    ASN D 254   C   -  N   -  CA  ANGL. DEV. =  17.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    CYS A  55     -169.26   -173.06                                   
REMARK 500    ASP A 244     -130.07     62.11                                   
REMARK 500    THR A 300     -160.71   -167.69                                   
REMARK 500    HIS A 403       -6.53     75.15                                   
REMARK 500    TYR A 448      138.71   -175.28                                   
REMARK 500    CYS B  55     -167.85   -172.90                                   
REMARK 500    ASP B 244     -133.79     62.60                                   
REMARK 500    THR B 300     -162.68   -167.59                                   
REMARK 500    LYS B 361      121.83    -37.40                                   
REMARK 500    HIS B 403       -4.16     71.13                                   
REMARK 500    TYR B 406      -50.58   -120.10                                   
REMARK 500    TYR B 448      140.20   -176.45                                   
REMARK 500    ARG C   3       92.36     74.95                                   
REMARK 500    ARG C  12      -60.11   -121.25                                   
REMARK 500    CYS C  55     -166.34   -169.15                                   
REMARK 500    ASP C 244     -129.79     58.87                                   
REMARK 500    THR C 300     -162.95   -169.35                                   
REMARK 500    HIS C 403       -5.51     74.36                                   
REMARK 500    TYR C 448      137.55   -175.36                                   
REMARK 500    CYS D  55     -166.22   -171.24                                   
REMARK 500    ASP D 244     -132.19     58.45                                   
REMARK 500    THR D 300     -160.29   -169.83                                   
REMARK 500    ASP D 324       48.23   -146.90                                   
REMARK 500    HIS D 403       -6.77     77.20                                   
REMARK 500    TYR D 448      137.04   -177.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-T2112   RELATED DB: TARGETDB                     
DBREF  2I3O A    1   516  UNP    Q9HJH4   Q9HJH4_THEAC     1    516             
DBREF  2I3O B    1   516  UNP    Q9HJH4   Q9HJH4_THEAC     1    516             
DBREF  2I3O C    1   516  UNP    Q9HJH4   Q9HJH4_THEAC     1    516             
DBREF  2I3O D    1   516  UNP    Q9HJH4   Q9HJH4_THEAC     1    516             
SEQADV 2I3O MSE A    1  UNP  Q9HJH4    MET     1 MODIFIED RESIDUE               
SEQADV 2I3O MSE A   46  UNP  Q9HJH4    MET    46 MODIFIED RESIDUE               
SEQADV 2I3O MSE A   73  UNP  Q9HJH4    MET    73 MODIFIED RESIDUE               
SEQADV 2I3O MSE A   93  UNP  Q9HJH4    MET    93 MODIFIED RESIDUE               
SEQADV 2I3O MSE A  126  UNP  Q9HJH4    MET   126 MODIFIED RESIDUE               
SEQADV 2I3O MSE A  171  UNP  Q9HJH4    MET   171 MODIFIED RESIDUE               
SEQADV 2I3O MSE A  195  UNP  Q9HJH4    MET   195 MODIFIED RESIDUE               
SEQADV 2I3O MSE A  267  UNP  Q9HJH4    MET   267 MODIFIED RESIDUE               
SEQADV 2I3O MSE A  277  UNP  Q9HJH4    MET   277 MODIFIED RESIDUE               
SEQADV 2I3O MSE A  289  UNP  Q9HJH4    MET   289 MODIFIED RESIDUE               
SEQADV 2I3O MSE A  305  UNP  Q9HJH4    MET   305 MODIFIED RESIDUE               
SEQADV 2I3O MSE A  352  UNP  Q9HJH4    MET   352 MODIFIED RESIDUE               
SEQADV 2I3O MSE A  385  UNP  Q9HJH4    MET   385 MODIFIED RESIDUE               
SEQADV 2I3O MSE A  398  UNP  Q9HJH4    MET   398 MODIFIED RESIDUE               
SEQADV 2I3O MSE A  412  UNP  Q9HJH4    MET   412 MODIFIED RESIDUE               
SEQADV 2I3O MSE A  422  UNP  Q9HJH4    MET   422 MODIFIED RESIDUE               
SEQADV 2I3O MSE A  426  UNP  Q9HJH4    MET   426 MODIFIED RESIDUE               
SEQADV 2I3O MSE B    1  UNP  Q9HJH4    MET     1 MODIFIED RESIDUE               
SEQADV 2I3O MSE B   46  UNP  Q9HJH4    MET    46 MODIFIED RESIDUE               
SEQADV 2I3O MSE B   73  UNP  Q9HJH4    MET    73 MODIFIED RESIDUE               
SEQADV 2I3O MSE B   93  UNP  Q9HJH4    MET    93 MODIFIED RESIDUE               
SEQADV 2I3O MSE B  126  UNP  Q9HJH4    MET   126 MODIFIED RESIDUE               
SEQADV 2I3O MSE B  171  UNP  Q9HJH4    MET   171 MODIFIED RESIDUE               
SEQADV 2I3O MSE B  195  UNP  Q9HJH4    MET   195 MODIFIED RESIDUE               
SEQADV 2I3O MSE B  267  UNP  Q9HJH4    MET   267 MODIFIED RESIDUE               
SEQADV 2I3O MSE B  277  UNP  Q9HJH4    MET   277 MODIFIED RESIDUE               
SEQADV 2I3O MSE B  289  UNP  Q9HJH4    MET   289 MODIFIED RESIDUE               
SEQADV 2I3O MSE B  305  UNP  Q9HJH4    MET   305 MODIFIED RESIDUE               
SEQADV 2I3O MSE B  352  UNP  Q9HJH4    MET   352 MODIFIED RESIDUE               
SEQADV 2I3O MSE B  385  UNP  Q9HJH4    MET   385 MODIFIED RESIDUE               
SEQADV 2I3O MSE B  398  UNP  Q9HJH4    MET   398 MODIFIED RESIDUE               
SEQADV 2I3O MSE B  412  UNP  Q9HJH4    MET   412 MODIFIED RESIDUE               
SEQADV 2I3O MSE B  422  UNP  Q9HJH4    MET   422 MODIFIED RESIDUE               
SEQADV 2I3O MSE B  426  UNP  Q9HJH4    MET   426 MODIFIED RESIDUE               
SEQADV 2I3O MSE C    1  UNP  Q9HJH4    MET     1 MODIFIED RESIDUE               
SEQADV 2I3O MSE C   46  UNP  Q9HJH4    MET    46 MODIFIED RESIDUE               
SEQADV 2I3O MSE C   73  UNP  Q9HJH4    MET    73 MODIFIED RESIDUE               
SEQADV 2I3O MSE C   93  UNP  Q9HJH4    MET    93 MODIFIED RESIDUE               
SEQADV 2I3O MSE C  126  UNP  Q9HJH4    MET   126 MODIFIED RESIDUE               
SEQADV 2I3O MSE C  171  UNP  Q9HJH4    MET   171 MODIFIED RESIDUE               
SEQADV 2I3O MSE C  195  UNP  Q9HJH4    MET   195 MODIFIED RESIDUE               
SEQADV 2I3O MSE C  267  UNP  Q9HJH4    MET   267 MODIFIED RESIDUE               
SEQADV 2I3O MSE C  277  UNP  Q9HJH4    MET   277 MODIFIED RESIDUE               
SEQADV 2I3O MSE C  289  UNP  Q9HJH4    MET   289 MODIFIED RESIDUE               
SEQADV 2I3O MSE C  305  UNP  Q9HJH4    MET   305 MODIFIED RESIDUE               
SEQADV 2I3O MSE C  352  UNP  Q9HJH4    MET   352 MODIFIED RESIDUE               
SEQADV 2I3O MSE C  385  UNP  Q9HJH4    MET   385 MODIFIED RESIDUE               
SEQADV 2I3O MSE C  398  UNP  Q9HJH4    MET   398 MODIFIED RESIDUE               
SEQADV 2I3O MSE C  412  UNP  Q9HJH4    MET   412 MODIFIED RESIDUE               
SEQADV 2I3O MSE C  422  UNP  Q9HJH4    MET   422 MODIFIED RESIDUE               
SEQADV 2I3O MSE C  426  UNP  Q9HJH4    MET   426 MODIFIED RESIDUE               
SEQADV 2I3O MSE D    1  UNP  Q9HJH4    MET     1 MODIFIED RESIDUE               
SEQADV 2I3O MSE D   46  UNP  Q9HJH4    MET    46 MODIFIED RESIDUE               
SEQADV 2I3O MSE D   73  UNP  Q9HJH4    MET    73 MODIFIED RESIDUE               
SEQADV 2I3O MSE D   93  UNP  Q9HJH4    MET    93 MODIFIED RESIDUE               
SEQADV 2I3O MSE D  126  UNP  Q9HJH4    MET   126 MODIFIED RESIDUE               
SEQADV 2I3O MSE D  171  UNP  Q9HJH4    MET   171 MODIFIED RESIDUE               
SEQADV 2I3O MSE D  195  UNP  Q9HJH4    MET   195 MODIFIED RESIDUE               
SEQADV 2I3O MSE D  267  UNP  Q9HJH4    MET   267 MODIFIED RESIDUE               
SEQADV 2I3O MSE D  277  UNP  Q9HJH4    MET   277 MODIFIED RESIDUE               
SEQADV 2I3O MSE D  289  UNP  Q9HJH4    MET   289 MODIFIED RESIDUE               
SEQADV 2I3O MSE D  305  UNP  Q9HJH4    MET   305 MODIFIED RESIDUE               
SEQADV 2I3O MSE D  352  UNP  Q9HJH4    MET   352 MODIFIED RESIDUE               
SEQADV 2I3O MSE D  385  UNP  Q9HJH4    MET   385 MODIFIED RESIDUE               
SEQADV 2I3O MSE D  398  UNP  Q9HJH4    MET   398 MODIFIED RESIDUE               
SEQADV 2I3O MSE D  412  UNP  Q9HJH4    MET   412 MODIFIED RESIDUE               
SEQADV 2I3O MSE D  422  UNP  Q9HJH4    MET   422 MODIFIED RESIDUE               
SEQADV 2I3O MSE D  426  UNP  Q9HJH4    MET   426 MODIFIED RESIDUE               
SEQRES   1 A  516  MSE PHE ARG SER ARG PRO ASN ALA LEU SER GLN ARG SER          
SEQRES   2 A  516  VAL ILE ALA SER SER SER GLU LEU ALA SER LEU ALA GLY          
SEQRES   3 A  516  ARG ASP ILE LEU LYS ARG GLY GLY ASN ILE PHE ASP ALA          
SEQRES   4 A  516  ALA LEU ALA VAL SER ALA MSE LEU CYS VAL THR GLN ASN          
SEQRES   5 A  516  ASN LEU CYS GLY LEU GLY GLY ASP LEU PHE ALA LEU ILE          
SEQRES   6 A  516  ARG ASP GLU ASN GLY GLN ILE MSE ASP LEU ASN GLY SER          
SEQRES   7 A  516  GLY GLN ALA SER ARG ALA VAL SER ILE ASP TYR TYR GLU          
SEQRES   8 A  516  SER MSE GLY LEU THR LYS ILE PRO GLU ARG GLY PRO TYR          
SEQRES   9 A  516  ALA ALA ILE THR VAL PRO GLY ILE ALA GLY SER TRP ASP          
SEQRES  10 A  516  GLU ILE PHE ARG LYS PHE ALA THR MSE ASP ILE ALA ASP          
SEQRES  11 A  516  ILE LEU GLU PRO ALA ILE ARG THR ALA SER ALA GLY PHE          
SEQRES  12 A  516  PRO ILE THR GLN ASN TYR SER ASP SER ILE ALA ARG SER          
SEQRES  13 A  516  ALA PRO VAL ILE GLY GLN TYR ARG GLY TRP SER SER ILE          
SEQRES  14 A  516  PHE MSE PRO ASN GLY SER VAL PRO VAL ALA GLY GLU ILE          
SEQRES  15 A  516  LEU LYS GLN PRO ASP LEU ALA GLU SER PHE ARG LEU MSE          
SEQRES  16 A  516  SER GLU GLU GLY PHE ARG SER PHE TYR ASP GLY SER LEU          
SEQRES  17 A  516  ALA ASP ILE ILE ILE ALA GLY LEU GLU GLY THR GLY SER          
SEQRES  18 A  516  PRO LEU SER ASP ARG ASP LEU ARG VAL TYR ARG PRO LEU          
SEQRES  19 A  516  ILE GLY LYS PRO VAL PHE THR ASP LEU ASP GLU PHE ARG          
SEQRES  20 A  516  ILE TYR GLU THR SER PRO ASN SER GLN GLY ILE THR VAL          
SEQRES  21 A  516  ILE GLU TRP ILE ARG GLY MSE GLU SER HIS GLY TYR ASP          
SEQRES  22 A  516  SER ARG THR MSE TRP GLU ALA LYS ILE GLU ASP ILE PHE          
SEQRES  23 A  516  GLU THR MSE GLU GLU ALA TYR ASP LYS ARG ARG LYS ILE          
SEQRES  24 A  516  THR ASP PRO SER TYR MSE ASN ILE ALA GLN HIS ASP SER          
SEQRES  25 A  516  ALA ASN GLY LYS LYS ASP GLY LEU PRO LYS ARG ASP HIS          
SEQRES  26 A  516  ASN ASP ILE GLY ASP THR THR TYR PHE SER ILE SER ASP          
SEQRES  27 A  516  SER GLU GLY ARG SER VAL SER ILE ILE GLN SER ASN TYR          
SEQRES  28 A  516  MSE GLY PHE GLY SER GLY ILE VAL PRO LYS GLY THR GLY          
SEQRES  29 A  516  PHE VAL LEU GLN ASN ARG GLY SER TYR PHE THR LEU GLN          
SEQRES  30 A  516  ARG ASP HIS PRO ASN ALA LEU MSE PRO GLY LYS ARG THR          
SEQRES  31 A  516  PHE HIS THR LEU ALA ALA CYS MSE VAL GLU LYS GLU HIS          
SEQRES  32 A  516  ASP LEU TYR ALA SER LEU GLY SER MSE GLY GLY ASP ILE          
SEQRES  33 A  516  GLN PRO GLN VAL GLN MSE GLN ILE LEU MSE GLU ILE LEU          
SEQRES  34 A  516  LYS ASP ASN THR ASP PRO GLN ALA ILE LEU ASP LYS PRO          
SEQRES  35 A  516  ARG TRP THR GLU PRO TYR THR ILE TYR GLU ALA PRO GLY          
SEQRES  36 A  516  ALA VAL TYR VAL GLU SER GLU GLU LEU TYR ARG ASN VAL          
SEQRES  37 A  516  SER LYS GLN ILE SER GLY ARG LYS VAL VAL LEU ARG ASP          
SEQRES  38 A  516  VAL SER GLN GLU PHE GLY THR ALA GLN ILE THR THR LEU          
SEQRES  39 A  516  ILE ARG GLY ASP VAL VAL VAL GLY ALA ALA ASP PRO ARG          
SEQRES  40 A  516  GLY ASP GLY ILE ALA ILE PRO TYR SER                          
SEQRES   1 B  516  MSE PHE ARG SER ARG PRO ASN ALA LEU SER GLN ARG SER          
SEQRES   2 B  516  VAL ILE ALA SER SER SER GLU LEU ALA SER LEU ALA GLY          
SEQRES   3 B  516  ARG ASP ILE LEU LYS ARG GLY GLY ASN ILE PHE ASP ALA          
SEQRES   4 B  516  ALA LEU ALA VAL SER ALA MSE LEU CYS VAL THR GLN ASN          
SEQRES   5 B  516  ASN LEU CYS GLY LEU GLY GLY ASP LEU PHE ALA LEU ILE          
SEQRES   6 B  516  ARG ASP GLU ASN GLY GLN ILE MSE ASP LEU ASN GLY SER          
SEQRES   7 B  516  GLY GLN ALA SER ARG ALA VAL SER ILE ASP TYR TYR GLU          
SEQRES   8 B  516  SER MSE GLY LEU THR LYS ILE PRO GLU ARG GLY PRO TYR          
SEQRES   9 B  516  ALA ALA ILE THR VAL PRO GLY ILE ALA GLY SER TRP ASP          
SEQRES  10 B  516  GLU ILE PHE ARG LYS PHE ALA THR MSE ASP ILE ALA ASP          
SEQRES  11 B  516  ILE LEU GLU PRO ALA ILE ARG THR ALA SER ALA GLY PHE          
SEQRES  12 B  516  PRO ILE THR GLN ASN TYR SER ASP SER ILE ALA ARG SER          
SEQRES  13 B  516  ALA PRO VAL ILE GLY GLN TYR ARG GLY TRP SER SER ILE          
SEQRES  14 B  516  PHE MSE PRO ASN GLY SER VAL PRO VAL ALA GLY GLU ILE          
SEQRES  15 B  516  LEU LYS GLN PRO ASP LEU ALA GLU SER PHE ARG LEU MSE          
SEQRES  16 B  516  SER GLU GLU GLY PHE ARG SER PHE TYR ASP GLY SER LEU          
SEQRES  17 B  516  ALA ASP ILE ILE ILE ALA GLY LEU GLU GLY THR GLY SER          
SEQRES  18 B  516  PRO LEU SER ASP ARG ASP LEU ARG VAL TYR ARG PRO LEU          
SEQRES  19 B  516  ILE GLY LYS PRO VAL PHE THR ASP LEU ASP GLU PHE ARG          
SEQRES  20 B  516  ILE TYR GLU THR SER PRO ASN SER GLN GLY ILE THR VAL          
SEQRES  21 B  516  ILE GLU TRP ILE ARG GLY MSE GLU SER HIS GLY TYR ASP          
SEQRES  22 B  516  SER ARG THR MSE TRP GLU ALA LYS ILE GLU ASP ILE PHE          
SEQRES  23 B  516  GLU THR MSE GLU GLU ALA TYR ASP LYS ARG ARG LYS ILE          
SEQRES  24 B  516  THR ASP PRO SER TYR MSE ASN ILE ALA GLN HIS ASP SER          
SEQRES  25 B  516  ALA ASN GLY LYS LYS ASP GLY LEU PRO LYS ARG ASP HIS          
SEQRES  26 B  516  ASN ASP ILE GLY ASP THR THR TYR PHE SER ILE SER ASP          
SEQRES  27 B  516  SER GLU GLY ARG SER VAL SER ILE ILE GLN SER ASN TYR          
SEQRES  28 B  516  MSE GLY PHE GLY SER GLY ILE VAL PRO LYS GLY THR GLY          
SEQRES  29 B  516  PHE VAL LEU GLN ASN ARG GLY SER TYR PHE THR LEU GLN          
SEQRES  30 B  516  ARG ASP HIS PRO ASN ALA LEU MSE PRO GLY LYS ARG THR          
SEQRES  31 B  516  PHE HIS THR LEU ALA ALA CYS MSE VAL GLU LYS GLU HIS          
SEQRES  32 B  516  ASP LEU TYR ALA SER LEU GLY SER MSE GLY GLY ASP ILE          
SEQRES  33 B  516  GLN PRO GLN VAL GLN MSE GLN ILE LEU MSE GLU ILE LEU          
SEQRES  34 B  516  LYS ASP ASN THR ASP PRO GLN ALA ILE LEU ASP LYS PRO          
SEQRES  35 B  516  ARG TRP THR GLU PRO TYR THR ILE TYR GLU ALA PRO GLY          
SEQRES  36 B  516  ALA VAL TYR VAL GLU SER GLU GLU LEU TYR ARG ASN VAL          
SEQRES  37 B  516  SER LYS GLN ILE SER GLY ARG LYS VAL VAL LEU ARG ASP          
SEQRES  38 B  516  VAL SER GLN GLU PHE GLY THR ALA GLN ILE THR THR LEU          
SEQRES  39 B  516  ILE ARG GLY ASP VAL VAL VAL GLY ALA ALA ASP PRO ARG          
SEQRES  40 B  516  GLY ASP GLY ILE ALA ILE PRO TYR SER                          
SEQRES   1 C  516  MSE PHE ARG SER ARG PRO ASN ALA LEU SER GLN ARG SER          
SEQRES   2 C  516  VAL ILE ALA SER SER SER GLU LEU ALA SER LEU ALA GLY          
SEQRES   3 C  516  ARG ASP ILE LEU LYS ARG GLY GLY ASN ILE PHE ASP ALA          
SEQRES   4 C  516  ALA LEU ALA VAL SER ALA MSE LEU CYS VAL THR GLN ASN          
SEQRES   5 C  516  ASN LEU CYS GLY LEU GLY GLY ASP LEU PHE ALA LEU ILE          
SEQRES   6 C  516  ARG ASP GLU ASN GLY GLN ILE MSE ASP LEU ASN GLY SER          
SEQRES   7 C  516  GLY GLN ALA SER ARG ALA VAL SER ILE ASP TYR TYR GLU          
SEQRES   8 C  516  SER MSE GLY LEU THR LYS ILE PRO GLU ARG GLY PRO TYR          
SEQRES   9 C  516  ALA ALA ILE THR VAL PRO GLY ILE ALA GLY SER TRP ASP          
SEQRES  10 C  516  GLU ILE PHE ARG LYS PHE ALA THR MSE ASP ILE ALA ASP          
SEQRES  11 C  516  ILE LEU GLU PRO ALA ILE ARG THR ALA SER ALA GLY PHE          
SEQRES  12 C  516  PRO ILE THR GLN ASN TYR SER ASP SER ILE ALA ARG SER          
SEQRES  13 C  516  ALA PRO VAL ILE GLY GLN TYR ARG GLY TRP SER SER ILE          
SEQRES  14 C  516  PHE MSE PRO ASN GLY SER VAL PRO VAL ALA GLY GLU ILE          
SEQRES  15 C  516  LEU LYS GLN PRO ASP LEU ALA GLU SER PHE ARG LEU MSE          
SEQRES  16 C  516  SER GLU GLU GLY PHE ARG SER PHE TYR ASP GLY SER LEU          
SEQRES  17 C  516  ALA ASP ILE ILE ILE ALA GLY LEU GLU GLY THR GLY SER          
SEQRES  18 C  516  PRO LEU SER ASP ARG ASP LEU ARG VAL TYR ARG PRO LEU          
SEQRES  19 C  516  ILE GLY LYS PRO VAL PHE THR ASP LEU ASP GLU PHE ARG          
SEQRES  20 C  516  ILE TYR GLU THR SER PRO ASN SER GLN GLY ILE THR VAL          
SEQRES  21 C  516  ILE GLU TRP ILE ARG GLY MSE GLU SER HIS GLY TYR ASP          
SEQRES  22 C  516  SER ARG THR MSE TRP GLU ALA LYS ILE GLU ASP ILE PHE          
SEQRES  23 C  516  GLU THR MSE GLU GLU ALA TYR ASP LYS ARG ARG LYS ILE          
SEQRES  24 C  516  THR ASP PRO SER TYR MSE ASN ILE ALA GLN HIS ASP SER          
SEQRES  25 C  516  ALA ASN GLY LYS LYS ASP GLY LEU PRO LYS ARG ASP HIS          
SEQRES  26 C  516  ASN ASP ILE GLY ASP THR THR TYR PHE SER ILE SER ASP          
SEQRES  27 C  516  SER GLU GLY ARG SER VAL SER ILE ILE GLN SER ASN TYR          
SEQRES  28 C  516  MSE GLY PHE GLY SER GLY ILE VAL PRO LYS GLY THR GLY          
SEQRES  29 C  516  PHE VAL LEU GLN ASN ARG GLY SER TYR PHE THR LEU GLN          
SEQRES  30 C  516  ARG ASP HIS PRO ASN ALA LEU MSE PRO GLY LYS ARG THR          
SEQRES  31 C  516  PHE HIS THR LEU ALA ALA CYS MSE VAL GLU LYS GLU HIS          
SEQRES  32 C  516  ASP LEU TYR ALA SER LEU GLY SER MSE GLY GLY ASP ILE          
SEQRES  33 C  516  GLN PRO GLN VAL GLN MSE GLN ILE LEU MSE GLU ILE LEU          
SEQRES  34 C  516  LYS ASP ASN THR ASP PRO GLN ALA ILE LEU ASP LYS PRO          
SEQRES  35 C  516  ARG TRP THR GLU PRO TYR THR ILE TYR GLU ALA PRO GLY          
SEQRES  36 C  516  ALA VAL TYR VAL GLU SER GLU GLU LEU TYR ARG ASN VAL          
SEQRES  37 C  516  SER LYS GLN ILE SER GLY ARG LYS VAL VAL LEU ARG ASP          
SEQRES  38 C  516  VAL SER GLN GLU PHE GLY THR ALA GLN ILE THR THR LEU          
SEQRES  39 C  516  ILE ARG GLY ASP VAL VAL VAL GLY ALA ALA ASP PRO ARG          
SEQRES  40 C  516  GLY ASP GLY ILE ALA ILE PRO TYR SER                          
SEQRES   1 D  516  MSE PHE ARG SER ARG PRO ASN ALA LEU SER GLN ARG SER          
SEQRES   2 D  516  VAL ILE ALA SER SER SER GLU LEU ALA SER LEU ALA GLY          
SEQRES   3 D  516  ARG ASP ILE LEU LYS ARG GLY GLY ASN ILE PHE ASP ALA          
SEQRES   4 D  516  ALA LEU ALA VAL SER ALA MSE LEU CYS VAL THR GLN ASN          
SEQRES   5 D  516  ASN LEU CYS GLY LEU GLY GLY ASP LEU PHE ALA LEU ILE          
SEQRES   6 D  516  ARG ASP GLU ASN GLY GLN ILE MSE ASP LEU ASN GLY SER          
SEQRES   7 D  516  GLY GLN ALA SER ARG ALA VAL SER ILE ASP TYR TYR GLU          
SEQRES   8 D  516  SER MSE GLY LEU THR LYS ILE PRO GLU ARG GLY PRO TYR          
SEQRES   9 D  516  ALA ALA ILE THR VAL PRO GLY ILE ALA GLY SER TRP ASP          
SEQRES  10 D  516  GLU ILE PHE ARG LYS PHE ALA THR MSE ASP ILE ALA ASP          
SEQRES  11 D  516  ILE LEU GLU PRO ALA ILE ARG THR ALA SER ALA GLY PHE          
SEQRES  12 D  516  PRO ILE THR GLN ASN TYR SER ASP SER ILE ALA ARG SER          
SEQRES  13 D  516  ALA PRO VAL ILE GLY GLN TYR ARG GLY TRP SER SER ILE          
SEQRES  14 D  516  PHE MSE PRO ASN GLY SER VAL PRO VAL ALA GLY GLU ILE          
SEQRES  15 D  516  LEU LYS GLN PRO ASP LEU ALA GLU SER PHE ARG LEU MSE          
SEQRES  16 D  516  SER GLU GLU GLY PHE ARG SER PHE TYR ASP GLY SER LEU          
SEQRES  17 D  516  ALA ASP ILE ILE ILE ALA GLY LEU GLU GLY THR GLY SER          
SEQRES  18 D  516  PRO LEU SER ASP ARG ASP LEU ARG VAL TYR ARG PRO LEU          
SEQRES  19 D  516  ILE GLY LYS PRO VAL PHE THR ASP LEU ASP GLU PHE ARG          
SEQRES  20 D  516  ILE TYR GLU THR SER PRO ASN SER GLN GLY ILE THR VAL          
SEQRES  21 D  516  ILE GLU TRP ILE ARG GLY MSE GLU SER HIS GLY TYR ASP          
SEQRES  22 D  516  SER ARG THR MSE TRP GLU ALA LYS ILE GLU ASP ILE PHE          
SEQRES  23 D  516  GLU THR MSE GLU GLU ALA TYR ASP LYS ARG ARG LYS ILE          
SEQRES  24 D  516  THR ASP PRO SER TYR MSE ASN ILE ALA GLN HIS ASP SER          
SEQRES  25 D  516  ALA ASN GLY LYS LYS ASP GLY LEU PRO LYS ARG ASP HIS          
SEQRES  26 D  516  ASN ASP ILE GLY ASP THR THR TYR PHE SER ILE SER ASP          
SEQRES  27 D  516  SER GLU GLY ARG SER VAL SER ILE ILE GLN SER ASN TYR          
SEQRES  28 D  516  MSE GLY PHE GLY SER GLY ILE VAL PRO LYS GLY THR GLY          
SEQRES  29 D  516  PHE VAL LEU GLN ASN ARG GLY SER TYR PHE THR LEU GLN          
SEQRES  30 D  516  ARG ASP HIS PRO ASN ALA LEU MSE PRO GLY LYS ARG THR          
SEQRES  31 D  516  PHE HIS THR LEU ALA ALA CYS MSE VAL GLU LYS GLU HIS          
SEQRES  32 D  516  ASP LEU TYR ALA SER LEU GLY SER MSE GLY GLY ASP ILE          
SEQRES  33 D  516  GLN PRO GLN VAL GLN MSE GLN ILE LEU MSE GLU ILE LEU          
SEQRES  34 D  516  LYS ASP ASN THR ASP PRO GLN ALA ILE LEU ASP LYS PRO          
SEQRES  35 D  516  ARG TRP THR GLU PRO TYR THR ILE TYR GLU ALA PRO GLY          
SEQRES  36 D  516  ALA VAL TYR VAL GLU SER GLU GLU LEU TYR ARG ASN VAL          
SEQRES  37 D  516  SER LYS GLN ILE SER GLY ARG LYS VAL VAL LEU ARG ASP          
SEQRES  38 D  516  VAL SER GLN GLU PHE GLY THR ALA GLN ILE THR THR LEU          
SEQRES  39 D  516  ILE ARG GLY ASP VAL VAL VAL GLY ALA ALA ASP PRO ARG          
SEQRES  40 D  516  GLY ASP GLY ILE ALA ILE PRO TYR SER                          
MODRES 2I3O MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE A   46  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE A   73  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE A   93  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE A  126  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE A  171  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE A  195  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE A  267  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE A  277  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE A  289  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE A  305  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE A  352  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE A  385  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE A  398  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE A  412  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE A  422  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE A  426  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE B   46  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE B   73  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE B   93  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE B  126  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE B  171  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE B  195  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE B  267  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE B  277  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE B  289  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE B  305  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE B  352  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE B  385  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE B  398  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE B  412  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE B  422  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE B  426  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE C   46  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE C   73  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE C   93  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE C  126  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE C  171  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE C  195  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE C  267  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE C  277  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE C  289  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE C  305  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE C  352  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE C  385  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE C  398  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE C  412  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE C  422  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE C  426  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE D    1  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE D   46  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE D   73  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE D   93  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE D  126  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE D  171  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE D  195  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE D  267  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE D  277  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE D  289  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE D  305  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE D  352  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE D  385  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE D  398  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE D  412  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE D  422  MET  SELENOMETHIONINE                                   
MODRES 2I3O MSE D  426  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  46       8                                                       
HET    MSE  A  73       8                                                       
HET    MSE  A  93       8                                                       
HET    MSE  A 126       8                                                       
HET    MSE  A 171       8                                                       
HET    MSE  A 195       8                                                       
HET    MSE  A 267       8                                                       
HET    MSE  A 277       8                                                       
HET    MSE  A 289       8                                                       
HET    MSE  A 305       8                                                       
HET    MSE  A 352       8                                                       
HET    MSE  A 385       8                                                       
HET    MSE  A 398       8                                                       
HET    MSE  A 412       8                                                       
HET    MSE  A 422       8                                                       
HET    MSE  A 426       8                                                       
HET    MSE  B  46       8                                                       
HET    MSE  B  73       8                                                       
HET    MSE  B  93       8                                                       
HET    MSE  B 126       8                                                       
HET    MSE  B 171       8                                                       
HET    MSE  B 195       8                                                       
HET    MSE  B 267       8                                                       
HET    MSE  B 277       8                                                       
HET    MSE  B 289       8                                                       
HET    MSE  B 305       8                                                       
HET    MSE  B 352       8                                                       
HET    MSE  B 385       8                                                       
HET    MSE  B 398       8                                                       
HET    MSE  B 412       8                                                       
HET    MSE  B 422       8                                                       
HET    MSE  B 426       8                                                       
HET    MSE  C  46       8                                                       
HET    MSE  C  73       8                                                       
HET    MSE  C  93       8                                                       
HET    MSE  C 126       8                                                       
HET    MSE  C 171       8                                                       
HET    MSE  C 195       8                                                       
HET    MSE  C 267       8                                                       
HET    MSE  C 277       8                                                       
HET    MSE  C 289       8                                                       
HET    MSE  C 305       8                                                       
HET    MSE  C 352       8                                                       
HET    MSE  C 385       8                                                       
HET    MSE  C 398       8                                                       
HET    MSE  C 412       8                                                       
HET    MSE  C 422       8                                                       
HET    MSE  C 426       8                                                       
HET    MSE  D   1       8                                                       
HET    MSE  D  46       8                                                       
HET    MSE  D  73       8                                                       
HET    MSE  D  93       8                                                       
HET    MSE  D 126       8                                                       
HET    MSE  D 171       8                                                       
HET    MSE  D 195       8                                                       
HET    MSE  D 267       8                                                       
HET    MSE  D 277       8                                                       
HET    MSE  D 289       8                                                       
HET    MSE  D 305       8                                                       
HET    MSE  D 352       8                                                       
HET    MSE  D 385       8                                                       
HET    MSE  D 398       8                                                       
HET    MSE  D 412       8                                                       
HET    MSE  D 422       8                                                       
HET    MSE  D 426       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    66(C5 H11 N O2 SE)                                           
FORMUL   5  HOH   *887(H2 O)                                                    
HELIX    1   1 SER A   19  ARG A   32  1                                  14    
HELIX    2   2 ASN A   35  GLN A   51  1                                  17    
HELIX    3   3 SER A   86  SER A   92  1                                   7    
HELIX    4   4 GLY A  111  ALA A  124  1                                  14    
HELIX    5   5 ASP A  127  GLY A  142  1                                  16    
HELIX    6   6 THR A  146  GLY A  161  1                                  16    
HELIX    7   7 TYR A  163  MSE A  171  1                                   9    
HELIX    8   8 GLN A  185  GLY A  199  1                                  15    
HELIX    9   9 ARG A  201  GLY A  206  1                                   6    
HELIX   10  10 GLY A  206  GLY A  215  1                                  10    
HELIX   11  11 SER A  224  TYR A  231  1                                   8    
HELIX   12  12 GLY A  257  HIS A  270  1                                  14    
HELIX   13  13 THR A  276  ALA A  280  5                                   5    
HELIX   14  14 LYS A  281  ARG A  297  1                                  17    
HELIX   15  15 ASP A  301  MSE A  305  5                                   5    
HELIX   16  16 ASN A  369  PHE A  374  5                                   6    
HELIX   17  17 ILE A  416  LEU A  429  1                                  14    
HELIX   18  18 ASP A  434  LYS A  441  1                                   8    
HELIX   19  19 SER A  461  ILE A  472  1                                  12    
HELIX   20  20 SER A  483  GLY A  487  5                                   5    
HELIX   21  21 ARG A  496  ASP A  498  5                                   3    
HELIX   22  22 SER B   19  ARG B   32  1                                  14    
HELIX   23  23 ASN B   35  GLN B   51  1                                  17    
HELIX   24  24 SER B   86  GLY B   94  1                                   9    
HELIX   25  25 GLY B  111  ALA B  124  1                                  14    
HELIX   26  26 ASP B  127  GLY B  142  1                                  16    
HELIX   27  27 THR B  146  GLY B  161  1                                  16    
HELIX   28  28 TYR B  163  MSE B  171  1                                   9    
HELIX   29  29 GLN B  185  GLY B  199  1                                  15    
HELIX   30  30 ARG B  201  GLY B  206  1                                   6    
HELIX   31  31 GLY B  206  GLY B  215  1                                  10    
HELIX   32  32 SER B  224  TYR B  231  1                                   8    
HELIX   33  33 GLY B  257  SER B  269  1                                  13    
HELIX   34  34 THR B  276  ALA B  280  5                                   5    
HELIX   35  35 LYS B  281  ARG B  296  1                                  16    
HELIX   36  36 ARG B  297  ILE B  299  5                                   3    
HELIX   37  37 ASP B  301  MSE B  305  5                                   5    
HELIX   38  38 ASN B  369  PHE B  374  5                                   6    
HELIX   39  39 ILE B  416  LEU B  429  1                                  14    
HELIX   40  40 ASP B  434  LYS B  441  1                                   8    
HELIX   41  41 SER B  461  ILE B  472  1                                  12    
HELIX   42  42 SER B  483  GLY B  487  5                                   5    
HELIX   43  43 ARG B  496  ASP B  498  5                                   3    
HELIX   44  44 SER C   19  ARG C   32  1                                  14    
HELIX   45  45 ASN C   35  GLN C   51  1                                  17    
HELIX   46  46 SER C   86  GLY C   94  1                                   9    
HELIX   47  47 GLY C  111  ALA C  124  1                                  14    
HELIX   48  48 ASP C  127  GLY C  142  1                                  16    
HELIX   49  49 THR C  146  GLY C  161  1                                  16    
HELIX   50  50 TYR C  163  MSE C  171  1                                   9    
HELIX   51  51 GLN C  185  GLY C  199  1                                  15    
HELIX   52  52 ARG C  201  GLY C  206  1                                   6    
HELIX   53  53 GLY C  206  GLY C  215  1                                  10    
HELIX   54  54 SER C  224  TYR C  231  1                                   8    
HELIX   55  55 GLY C  257  HIS C  270  1                                  14    
HELIX   56  56 THR C  276  ALA C  280  5                                   5    
HELIX   57  57 LYS C  281  ARG C  297  1                                  17    
HELIX   58  58 ASP C  301  MSE C  305  5                                   5    
HELIX   59  59 ASN C  369  PHE C  374  5                                   6    
HELIX   60  60 ILE C  416  ASP C  431  1                                  16    
HELIX   61  61 ASP C  434  LYS C  441  1                                   8    
HELIX   62  62 SER C  461  ILE C  472  1                                  12    
HELIX   63  63 SER C  483  GLY C  487  5                                   5    
HELIX   64  64 ARG C  496  ASP C  498  5                                   3    
HELIX   65  65 SER D   19  ARG D   32  1                                  14    
HELIX   66  66 ASN D   35  GLN D   51  1                                  17    
HELIX   67  67 SER D   86  MSE D   93  1                                   8    
HELIX   68  68 GLY D  111  ALA D  124  1                                  14    
HELIX   69  69 ASP D  127  GLY D  142  1                                  16    
HELIX   70  70 THR D  146  GLY D  161  1                                  16    
HELIX   71  71 TYR D  163  MSE D  171  1                                   9    
HELIX   72  72 GLN D  185  GLY D  199  1                                  15    
HELIX   73  73 ARG D  201  GLY D  206  1                                   6    
HELIX   74  74 GLY D  206  GLY D  215  1                                  10    
HELIX   75  75 SER D  224  VAL D  230  1                                   7    
HELIX   76  76 GLY D  257  HIS D  270  1                                  14    
HELIX   77  77 THR D  276  ALA D  280  5                                   5    
HELIX   78  78 LYS D  281  ARG D  296  1                                  16    
HELIX   79  79 ARG D  297  ILE D  299  5                                   3    
HELIX   80  80 ASP D  311  GLY D  315  5                                   5    
HELIX   81  81 ASN D  369  PHE D  374  5                                   6    
HELIX   82  82 ILE D  416  ASP D  431  1                                  16    
HELIX   83  83 ASP D  434  LYS D  441  1                                   8    
HELIX   84  84 SER D  461  ILE D  472  1                                  12    
HELIX   85  85 SER D  483  GLY D  487  5                                   5    
HELIX   86  86 ARG D  496  ASP D  498  5                                   3    
SHEET    1   A 7 ALA A   8  SER A  10  0                                        
SHEET    2   A 7 VAL A 499  ALA A 504 -1  O  GLY A 502   N  ALA A   8           
SHEET    3   A 7 ALA A 489  ILE A 495 -1  N  ILE A 495   O  VAL A 499           
SHEET    4   A 7 ASP A 404  SER A 411 -1  N  SER A 408   O  THR A 492           
SHEET    5   A 7 CYS A 397  LYS A 401 -1  N  VAL A 399   O  ALA A 407           
SHEET    6   A 7 PHE A 246  GLU A 250 -1  N  TYR A 249   O  MSE A 398           
SHEET    7   A 7 VAL A 239  LEU A 243 -1  N  LEU A 243   O  PHE A 246           
SHEET    1   B 7 LEU A 234  GLY A 236  0                                        
SHEET    2   B 7 ILE A  72  GLY A  77 -1  N  ASN A  76   O  LEU A 234           
SHEET    3   B 7 ASP A  60  ARG A  66 -1  N  ALA A  63   O  LEU A  75           
SHEET    4   B 7 SER A 343  TYR A 351 -1  O  SER A 343   N  ARG A  66           
SHEET    5   B 7 ASP A 330  ASP A 338 -1  N  ASP A 330   O  TYR A 351           
SHEET    6   B 7 SER A  13  SER A  17 -1  N  ALA A  16   O  SER A 335           
SHEET    7   B 7 ILE A 511  TYR A 515 -1  O  ILE A 513   N  ILE A  15           
SHEET    1   C 2 PHE A 143  PRO A 144  0                                        
SHEET    2   C 2 ILE A 182  LEU A 183 -1  O  LEU A 183   N  PHE A 143           
SHEET    1   D 3 TRP A 444  THR A 445  0                                        
SHEET    2   D 3 VAL A 457  VAL A 459 -1  O  TYR A 458   N  THR A 445           
SHEET    3   D 3 VAL A 477  LEU A 479  1  O  VAL A 478   N  VAL A 457           
SHEET    1   E 7 ALA B   8  SER B  10  0                                        
SHEET    2   E 7 VAL B 499  ALA B 504 -1  O  VAL B 500   N  SER B  10           
SHEET    3   E 7 THR B 488  ILE B 495 -1  N  THR B 493   O  VAL B 501           
SHEET    4   E 7 ASP B 404  MSE B 412 -1  N  MSE B 412   O  THR B 488           
SHEET    5   E 7 CYS B 397  LYS B 401 -1  N  VAL B 399   O  ALA B 407           
SHEET    6   E 7 PHE B 246  GLU B 250 -1  N  TYR B 249   O  MSE B 398           
SHEET    7   E 7 VAL B 239  LEU B 243 -1  N  THR B 241   O  ILE B 248           
SHEET    1   F 7 LEU B 234  GLY B 236  0                                        
SHEET    2   F 7 ILE B  72  GLY B  77 -1  N  ASN B  76   O  LEU B 234           
SHEET    3   F 7 ASP B  60  ARG B  66 -1  N  ALA B  63   O  LEU B  75           
SHEET    4   F 7 SER B 343  TYR B 351 -1  O  SER B 343   N  ARG B  66           
SHEET    5   F 7 ASP B 330  ASP B 338 -1  N  ASP B 330   O  TYR B 351           
SHEET    6   F 7 SER B  13  SER B  17 -1  N  ALA B  16   O  SER B 335           
SHEET    7   F 7 ILE B 511  TYR B 515 -1  O  ILE B 513   N  ILE B  15           
SHEET    1   G 2 PHE B 143  PRO B 144  0                                        
SHEET    2   G 2 ILE B 182  LEU B 183 -1  O  LEU B 183   N  PHE B 143           
SHEET    1   H 3 TRP B 444  THR B 445  0                                        
SHEET    2   H 3 VAL B 457  VAL B 459 -1  O  TYR B 458   N  THR B 445           
SHEET    3   H 3 VAL B 477  LEU B 479  1  O  VAL B 478   N  VAL B 457           
SHEET    1   I 7 ALA C   8  SER C  10  0                                        
SHEET    2   I 7 VAL C 499  ALA C 504 -1  O  VAL C 500   N  SER C  10           
SHEET    3   I 7 ALA C 489  ILE C 495 -1  N  ILE C 495   O  VAL C 499           
SHEET    4   I 7 ASP C 404  SER C 411 -1  N  SER C 408   O  THR C 492           
SHEET    5   I 7 CYS C 397  LYS C 401 -1  N  VAL C 399   O  ALA C 407           
SHEET    6   I 7 PHE C 246  GLU C 250 -1  N  TYR C 249   O  MSE C 398           
SHEET    7   I 7 VAL C 239  LEU C 243 -1  N  LEU C 243   O  PHE C 246           
SHEET    1   J 7 LEU C 234  GLY C 236  0                                        
SHEET    2   J 7 ILE C  72  GLY C  77 -1  N  ASN C  76   O  LEU C 234           
SHEET    3   J 7 ASP C  60  ARG C  66 -1  N  ALA C  63   O  LEU C  75           
SHEET    4   J 7 SER C 343  TYR C 351 -1  O  SER C 343   N  ARG C  66           
SHEET    5   J 7 ASP C 330  ASP C 338 -1  N  ASP C 330   O  TYR C 351           
SHEET    6   J 7 SER C  13  SER C  17 -1  N  ALA C  16   O  SER C 335           
SHEET    7   J 7 ILE C 511  TYR C 515 -1  O  ILE C 513   N  ILE C  15           
SHEET    1   K 2 PHE C 143  PRO C 144  0                                        
SHEET    2   K 2 ILE C 182  LEU C 183 -1  O  LEU C 183   N  PHE C 143           
SHEET    1   L 3 TRP C 444  THR C 445  0                                        
SHEET    2   L 3 VAL C 457  VAL C 459 -1  O  TYR C 458   N  THR C 445           
SHEET    3   L 3 VAL C 477  LEU C 479  1  O  VAL C 478   N  VAL C 457           
SHEET    1   M 7 ALA D   8  SER D  10  0                                        
SHEET    2   M 7 VAL D 499  ALA D 504 -1  O  VAL D 500   N  SER D  10           
SHEET    3   M 7 ALA D 489  ILE D 495 -1  N  THR D 493   O  VAL D 501           
SHEET    4   M 7 ASP D 404  SER D 411 -1  N  SER D 408   O  THR D 492           
SHEET    5   M 7 CYS D 397  LYS D 401 -1  N  VAL D 399   O  ALA D 407           
SHEET    6   M 7 PHE D 246  GLU D 250 -1  N  TYR D 249   O  MSE D 398           
SHEET    7   M 7 VAL D 239  LEU D 243 -1  N  LEU D 243   O  PHE D 246           
SHEET    1   N 7 LEU D 234  GLY D 236  0                                        
SHEET    2   N 7 ILE D  72  GLY D  77 -1  N  ASN D  76   O  LEU D 234           
SHEET    3   N 7 ASP D  60  ARG D  66 -1  N  ALA D  63   O  LEU D  75           
SHEET    4   N 7 SER D 343  TYR D 351 -1  O  SER D 343   N  ARG D  66           
SHEET    5   N 7 ASP D 330  ASP D 338 -1  N  ASP D 330   O  TYR D 351           
SHEET    6   N 7 SER D  13  SER D  17 -1  N  ALA D  16   O  SER D 335           
SHEET    7   N 7 ILE D 511  TYR D 515 -1  O  ILE D 513   N  ILE D  15           
SHEET    1   O 2 PHE D 143  PRO D 144  0                                        
SHEET    2   O 2 ILE D 182  LEU D 183 -1  O  LEU D 183   N  PHE D 143           
SHEET    1   P 3 TRP D 444  THR D 445  0                                        
SHEET    2   P 3 VAL D 457  VAL D 459 -1  O  TYR D 458   N  THR D 445           
SHEET    3   P 3 VAL D 477  LEU D 479  1  O  VAL D 478   N  VAL D 457           
LINK         C   MSE A   1                 N   PHE A   2     1555   1555  1.33  
LINK         C   ALA A  45                 N   MSE A  46     1555   1555  1.33  
LINK         C   MSE A  46                 N   LEU A  47     1555   1555  1.33  
LINK         C   ILE A  72                 N   MSE A  73     1555   1555  1.33  
LINK         C   MSE A  73                 N   ASP A  74     1555   1555  1.33  
LINK         C   SER A  92                 N   MSE A  93     1555   1555  1.33  
LINK         C   MSE A  93                 N   GLY A  94     1555   1555  1.33  
LINK         C   THR A 125                 N   MSE A 126     1555   1555  1.33  
LINK         C   MSE A 126                 N   ASP A 127     1555   1555  1.33  
LINK         C   PHE A 170                 N   MSE A 171     1555   1555  1.33  
LINK         C   MSE A 171                 N   PRO A 172     1555   1555  1.34  
LINK         C   LEU A 194                 N   MSE A 195     1555   1555  1.33  
LINK         C   MSE A 195                 N   SER A 196     1555   1555  1.33  
LINK         C   GLY A 266                 N   MSE A 267     1555   1555  1.33  
LINK         C   MSE A 267                 N   GLU A 268     1555   1555  1.33  
LINK         C   THR A 276                 N   MSE A 277     1555   1555  1.33  
LINK         C   MSE A 277                 N   TRP A 278     1555   1555  1.33  
LINK         C   THR A 288                 N   MSE A 289     1555   1555  1.33  
LINK         C   MSE A 289                 N   GLU A 290     1555   1555  1.33  
LINK         C   TYR A 304                 N   MSE A 305     1555   1555  1.33  
LINK         C   MSE A 305                 N   ASN A 306     1555   1555  1.33  
LINK         C   TYR A 351                 N   MSE A 352     1555   1555  1.33  
LINK         C   MSE A 352                 N   GLY A 353     1555   1555  1.33  
LINK         C   LEU A 384                 N   MSE A 385     1555   1555  1.33  
LINK         C   MSE A 385                 N   PRO A 386     1555   1555  1.34  
LINK         C   CYS A 397                 N   MSE A 398     1555   1555  1.33  
LINK         C   MSE A 398                 N   VAL A 399     1555   1555  1.33  
LINK         C   SER A 411                 N   MSE A 412     1555   1555  1.33  
LINK         C   MSE A 412                 N   GLY A 413     1555   1555  1.33  
LINK         C   GLN A 421                 N   MSE A 422     1555   1555  1.33  
LINK         C   MSE A 422                 N   GLN A 423     1555   1555  1.33  
LINK         C   LEU A 425                 N   MSE A 426     1555   1555  1.33  
LINK         C   MSE A 426                 N   GLU A 427     1555   1555  1.33  
LINK         C   ALA B  45                 N   MSE B  46     1555   1555  1.33  
LINK         C   MSE B  46                 N   LEU B  47     1555   1555  1.33  
LINK         C   ILE B  72                 N   MSE B  73     1555   1555  1.33  
LINK         C   MSE B  73                 N   ASP B  74     1555   1555  1.33  
LINK         C   SER B  92                 N   MSE B  93     1555   1555  1.33  
LINK         C   MSE B  93                 N   GLY B  94     1555   1555  1.33  
LINK         C   THR B 125                 N   MSE B 126     1555   1555  1.33  
LINK         C   MSE B 126                 N   ASP B 127     1555   1555  1.33  
LINK         C   PHE B 170                 N   MSE B 171     1555   1555  1.33  
LINK         C   MSE B 171                 N   PRO B 172     1555   1555  1.34  
LINK         C   LEU B 194                 N   MSE B 195     1555   1555  1.33  
LINK         C   MSE B 195                 N   SER B 196     1555   1555  1.33  
LINK         C   GLY B 266                 N   MSE B 267     1555   1555  1.33  
LINK         C   MSE B 267                 N   GLU B 268     1555   1555  1.33  
LINK         C   THR B 276                 N   MSE B 277     1555   1555  1.33  
LINK         C   MSE B 277                 N   TRP B 278     1555   1555  1.33  
LINK         C   THR B 288                 N   MSE B 289     1555   1555  1.33  
LINK         C   MSE B 289                 N   GLU B 290     1555   1555  1.33  
LINK         C   TYR B 304                 N   MSE B 305     1555   1555  1.33  
LINK         C   MSE B 305                 N   ASN B 306     1555   1555  1.33  
LINK         C   TYR B 351                 N   MSE B 352     1555   1555  1.33  
LINK         C   MSE B 352                 N   GLY B 353     1555   1555  1.33  
LINK         C   LEU B 384                 N   MSE B 385     1555   1555  1.33  
LINK         C   MSE B 385                 N   PRO B 386     1555   1555  1.34  
LINK         C   CYS B 397                 N   MSE B 398     1555   1555  1.33  
LINK         C   MSE B 398                 N   VAL B 399     1555   1555  1.33  
LINK         C   SER B 411                 N   MSE B 412     1555   1555  1.33  
LINK         C   MSE B 412                 N   GLY B 413     1555   1555  1.33  
LINK         C   GLN B 421                 N   MSE B 422     1555   1555  1.33  
LINK         C   MSE B 422                 N   GLN B 423     1555   1555  1.33  
LINK         C   LEU B 425                 N   MSE B 426     1555   1555  1.33  
LINK         C   MSE B 426                 N   GLU B 427     1555   1555  1.33  
LINK         C   ALA C  45                 N   MSE C  46     1555   1555  1.33  
LINK         C   MSE C  46                 N   LEU C  47     1555   1555  1.33  
LINK         C   ILE C  72                 N   MSE C  73     1555   1555  1.33  
LINK         C   MSE C  73                 N   ASP C  74     1555   1555  1.33  
LINK         C   SER C  92                 N   MSE C  93     1555   1555  1.33  
LINK         C   MSE C  93                 N   GLY C  94     1555   1555  1.33  
LINK         C   THR C 125                 N   MSE C 126     1555   1555  1.33  
LINK         C   MSE C 126                 N   ASP C 127     1555   1555  1.33  
LINK         C   PHE C 170                 N   MSE C 171     1555   1555  1.33  
LINK         C   MSE C 171                 N   PRO C 172     1555   1555  1.34  
LINK         C   LEU C 194                 N   MSE C 195     1555   1555  1.33  
LINK         C   MSE C 195                 N   SER C 196     1555   1555  1.33  
LINK         C   GLY C 266                 N   MSE C 267     1555   1555  1.33  
LINK         C   MSE C 267                 N   GLU C 268     1555   1555  1.33  
LINK         C   THR C 276                 N   MSE C 277     1555   1555  1.33  
LINK         C   MSE C 277                 N   TRP C 278     1555   1555  1.33  
LINK         C   THR C 288                 N   MSE C 289     1555   1555  1.33  
LINK         C   MSE C 289                 N   GLU C 290     1555   1555  1.33  
LINK         C   TYR C 304                 N   MSE C 305     1555   1555  1.33  
LINK         C   MSE C 305                 N   ASN C 306     1555   1555  1.33  
LINK         C   TYR C 351                 N   MSE C 352     1555   1555  1.33  
LINK         C   MSE C 352                 N   GLY C 353     1555   1555  1.33  
LINK         C   LEU C 384                 N   MSE C 385     1555   1555  1.33  
LINK         C   MSE C 385                 N   PRO C 386     1555   1555  1.34  
LINK         C   CYS C 397                 N   MSE C 398     1555   1555  1.33  
LINK         C   MSE C 398                 N   VAL C 399     1555   1555  1.33  
LINK         C   SER C 411                 N   MSE C 412     1555   1555  1.32  
LINK         C   MSE C 412                 N   GLY C 413     1555   1555  1.33  
LINK         C   GLN C 421                 N   MSE C 422     1555   1555  1.33  
LINK         C   MSE C 422                 N   GLN C 423     1555   1555  1.33  
LINK         C   LEU C 425                 N   MSE C 426     1555   1555  1.33  
LINK         C   MSE C 426                 N   GLU C 427     1555   1555  1.33  
LINK         C   MSE D   1                 N   PHE D   2     1555   1555  1.33  
LINK         C   ALA D  45                 N   MSE D  46     1555   1555  1.33  
LINK         C   MSE D  46                 N   LEU D  47     1555   1555  1.33  
LINK         C   ILE D  72                 N   MSE D  73     1555   1555  1.33  
LINK         C   MSE D  73                 N   ASP D  74     1555   1555  1.33  
LINK         C   SER D  92                 N   MSE D  93     1555   1555  1.33  
LINK         C   MSE D  93                 N   GLY D  94     1555   1555  1.33  
LINK         C   THR D 125                 N   MSE D 126     1555   1555  1.33  
LINK         C   MSE D 126                 N   ASP D 127     1555   1555  1.33  
LINK         C   PHE D 170                 N   MSE D 171     1555   1555  1.33  
LINK         C   MSE D 171                 N   PRO D 172     1555   1555  1.35  
LINK         C   LEU D 194                 N   MSE D 195     1555   1555  1.33  
LINK         C   MSE D 195                 N   SER D 196     1555   1555  1.33  
LINK         C   GLY D 266                 N   MSE D 267     1555   1555  1.33  
LINK         C   MSE D 267                 N   GLU D 268     1555   1555  1.33  
LINK         C   THR D 276                 N   MSE D 277     1555   1555  1.33  
LINK         C   MSE D 277                 N   TRP D 278     1555   1555  1.33  
LINK         C   THR D 288                 N   MSE D 289     1555   1555  1.33  
LINK         C   MSE D 289                 N   GLU D 290     1555   1555  1.33  
LINK         C   TYR D 304                 N   MSE D 305     1555   1555  1.33  
LINK         C   MSE D 305                 N   ASN D 306     1555   1555  1.33  
LINK         C   TYR D 351                 N   MSE D 352     1555   1555  1.33  
LINK         C   MSE D 352                 N   GLY D 353     1555   1555  1.33  
LINK         C   LEU D 384                 N   MSE D 385     1555   1555  1.33  
LINK         C   MSE D 385                 N   PRO D 386     1555   1555  1.34  
LINK         C   CYS D 397                 N   MSE D 398     1555   1555  1.33  
LINK         C   MSE D 398                 N   VAL D 399     1555   1555  1.33  
LINK         C   SER D 411                 N   MSE D 412     1555   1555  1.33  
LINK         C   MSE D 412                 N   GLY D 413     1555   1555  1.33  
LINK         C   GLN D 421                 N   MSE D 422     1555   1555  1.33  
LINK         C   MSE D 422                 N   GLN D 423     1555   1555  1.33  
LINK         C   LEU D 425                 N   MSE D 426     1555   1555  1.33  
LINK         C   MSE D 426                 N   GLU D 427     1555   1555  1.33  
CISPEP   1 PRO A  253    ASN A  254          0        20.89                     
CISPEP   2 PRO B  253    ASN B  254          0        20.95                     
CISPEP   3 PRO C  253    ASN C  254          0        20.95                     
CISPEP   4 PRO D  253    ASN D  254          0        20.94                     
CRYST1  116.080   95.471  119.040  90.00 109.79  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008615  0.000000  0.003100        0.00000                         
SCALE2      0.000000  0.010474  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008928        0.00000                         
HETATM    1  N   MSE A   1      30.610 -54.669 -13.327  1.00 52.77           N  
HETATM    2  CA  MSE A   1      29.783 -54.540 -12.089  1.00 52.38           C  
HETATM    3  C   MSE A   1      28.734 -55.645 -11.983  1.00 47.18           C  
HETATM    4  O   MSE A   1      27.908 -55.827 -12.873  1.00 46.41           O  
HETATM    5  CB  MSE A   1      29.119 -53.159 -12.051  1.00 59.89           C  
HETATM    6  CG  MSE A   1      28.461 -52.733 -13.357  1.00 69.33           C  
HETATM    7 SE   MSE A   1      26.648 -53.375 -13.585  1.00 84.13          SE  
HETATM    8  CE  MSE A   1      25.719 -51.840 -12.859  1.00 79.90           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system