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Database: PDB
Entry: 2GLF
LinkDB: 2GLF
Original site: 2GLF 
HEADER    HYDROLASE                               04-APR-06   2GLF              
TITLE     CRYSTAL STRUCTURE OF AMINIPEPTIDASE (M18 FAMILY) FROM THERMOTOGA      
TITLE    2 MARITIMA                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE M18-FAMILY AMINOPEPTIDASE 1;                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 3.4.11.-;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;                            
SOURCE   3 ORGANISM_TAXID: 2336;                                                
SOURCE   4 GENE: APEA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PUTATIVE, AMINOPEPTIDASE 1, NYSGXRC, STRUCTURAL GENOMICS, PSI,        
KEYWDS   2 PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR       
KEYWDS   3 STRUCTURAL GENOMICS, HYDROLASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.MIN,L.SHAPIRO,S.K.BURLEY,NEW YORK SGX RESEARCH CENTER FOR           
AUTHOR   2 STRUCTURAL GENOMICS (NYSGXRC)                                        
REVDAT   3   13-JUL-11 2GLF    1       VERSN                                    
REVDAT   2   24-FEB-09 2GLF    1       VERSN                                    
REVDAT   1   13-JUN-06 2GLF    0                                                
JRNL        AUTH   T.MIN,L.SHAPIRO                                              
JRNL        TITL   CRYSTAL STRUCTURE OF AMINIPEPTIDASE (M18 FAMILY) FROM        
JRNL        TITL 2 THERMOTOGA MARITIMA                                          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.83                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 138976.290                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 98451                          
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) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4797                            
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.97                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 73.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 12889                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2210                       
REMARK   3   BIN FREE R VALUE                    : 0.3090                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 698                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14156                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 479                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.31                            
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) : 0.37                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.45                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.85                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : GROUP                                     
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 : FLAT MODEL                                           
REMARK   3   KSOL        : 0.31                                                 
REMARK   3   BSOL        : 26.96                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2GLF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB037264.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-MAY-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : SI(111)DOUBLE CRYSTAL              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CBASS, DENZO                       
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51206                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M NACL, 7% ETOH, 0.1M MNCL2, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3                           
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       95.61250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       95.61250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       95.61250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       95.61250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       95.61250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       95.61250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       95.61250            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       95.61250            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       95.61250            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       95.61250            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       95.61250            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       95.61250            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       95.61250            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       95.61250            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       95.61250            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       95.61250            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       95.61250            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       95.61250            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 103730 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 150390 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -591.0 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   BIOMT1   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3   3  1.000000  0.000000  0.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH C5082  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C5081  LIES ON A SPECIAL POSITION.                          
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   OE2  GLU D    41     NH1  ARG D    44              2.18            
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  14      102.19     87.86                                   
REMARK 500    ALA A  32       76.40   -110.19                                   
REMARK 500    GLU A  48     -161.82    -79.48                                   
REMARK 500    SER A  49      -21.65     60.86                                   
REMARK 500    LEU A  54      155.14    -47.73                                   
REMARK 500    GLU A  55      -45.97     79.90                                   
REMARK 500    PHE A  57      -95.06    -68.77                                   
REMARK 500    ALA A  58       97.37     66.19                                   
REMARK 500    ASP A  60       96.08     80.17                                   
REMARK 500    ASN A  70      -85.22    -68.58                                   
REMARK 500    ARG A  99     -160.84   -160.74                                   
REMARK 500    ASN A 105       77.75   -115.58                                   
REMARK 500    LYS A 126      -55.81     96.89                                   
REMARK 500    GLU A 179     -151.03    -97.93                                   
REMARK 500    LYS A 180      -76.03     71.57                                   
REMARK 500    ASP A 251       93.14    -61.01                                   
REMARK 500    ASP A 252      -14.01     81.59                                   
REMARK 500    GLU A 281       -3.74    -59.28                                   
REMARK 500    SER A 284       36.73     79.67                                   
REMARK 500    LYS A 291       63.00     63.33                                   
REMARK 500    ALA A 292       17.03   -151.92                                   
REMARK 500    ARG A 293      -41.77     71.35                                   
REMARK 500    SER A 311      -77.45     79.15                                   
REMARK 500    THR A 322      109.05     88.77                                   
REMARK 500    PRO A 335      -68.34    -22.10                                   
REMARK 500    ASN A 345       28.44   -140.30                                   
REMARK 500    THR A 359       86.08   -150.88                                   
REMARK 500    ALA A 361     -130.78   -129.93                                   
REMARK 500    ARG A 362       69.64    -49.56                                   
REMARK 500    ALA A 370      126.27    -37.24                                   
REMARK 500    HIS A 427       -6.41     76.27                                   
REMARK 500    PHE A 430       78.71   -150.48                                   
REMARK 500    MSE B   4       89.53     59.67                                   
REMARK 500    ALA B  58      -35.46   -131.00                                   
REMARK 500    ASN B  63       74.69   -154.74                                   
REMARK 500    ASN B  70      -83.05    -85.06                                   
REMARK 500    GLU B 157      -27.92    153.50                                   
REMARK 500    SER B 178      -70.88    -51.91                                   
REMARK 500    LYS B 180      133.46     70.24                                   
REMARK 500    PHE B 181       72.94     72.94                                   
REMARK 500    ASP B 251       85.24    -58.22                                   
REMARK 500    ASP B 252      -12.34     82.61                                   
REMARK 500    LYS B 279       18.55     45.18                                   
REMARK 500    ALA B 292       33.50    -90.51                                   
REMARK 500    ARG B 293      -25.37     66.04                                   
REMARK 500    THR B 322      111.76     85.42                                   
REMARK 500    ASP B 328      138.51     54.35                                   
REMARK 500    PRO B 335      -64.62    -22.65                                   
REMARK 500    THR B 359       73.28   -106.92                                   
REMARK 500    ALA B 361      109.41    156.74                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     111 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASP B 252        24.8      L          L   OUTSIDE RANGE           
REMARK 500    ARG C  13        24.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B5108        DISTANCE =  5.43 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A5001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  94   NE2                                                    
REMARK 620 2 ASP A 251   OD1  88.7                                              
REMARK 620 3 ASP A 328   OD1  96.9 145.6                                        
REMARK 620 4 ASP A 328   OD2 104.1  93.5  52.2                                  
REMARK 620 5 HOH A5079   O   166.9  80.4  88.3  69.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A5002  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 281   OE1                                                    
REMARK 620 2 HIS A 427   NE2  80.8                                              
REMARK 620 3 ASP A 251   OD2 142.6  83.1                                        
REMARK 620 4 GLU A 281   OE2  53.4 102.0  98.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B5003  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 281   OE1                                                    
REMARK 620 2 GLU B 281   OE2  54.3                                              
REMARK 620 3 HIS B 427   NE2  91.6  93.6                                        
REMARK 620 4 ASP B 251   OD2 148.8  95.1  83.8                                  
REMARK 620 5 HOH B5072   O    97.0 132.9 127.0 110.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B5004  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 328   OD1                                                    
REMARK 620 2 ASP B 251   OD1 149.7                                              
REMARK 620 3 HIS B  94   NE2 102.8  86.0                                        
REMARK 620 4 ASP B 328   OD2  52.9  99.6  87.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C5006  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  94   NE2                                                    
REMARK 620 2 ASP C 328   OD1  94.3                                              
REMARK 620 3 ASP C 251   OD1  91.1 148.6                                        
REMARK 620 4 ASP C 328   OD2  92.6  52.1  96.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C5007  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 427   NE2                                                    
REMARK 620 2 GLU C 281   OE1  88.5                                              
REMARK 620 3 GLU C 281   OE2  81.1  54.3                                        
REMARK 620 4 ASP C 251   OD2  83.6  90.5 141.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D5008  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 328   OD2                                                    
REMARK 620 2 HIS D  94   NE2 107.5                                              
REMARK 620 3 ASP D 251   OD1 108.6  86.2                                        
REMARK 620 4 HOH D5083   O    86.4 164.4  82.4                                  
REMARK 620 5 ASP D 328   OD1  52.4  92.6 159.6 101.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D5009  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D5096   O                                                      
REMARK 620 2 ASP D 251   OD2 115.3                                              
REMARK 620 3 GLU D 281   OE1 127.0 103.3                                        
REMARK 620 4 HIS D 427   NE2 110.3  87.5 106.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 5001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 5002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 5003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 5004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 5006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 5007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 5008                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 5009                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-T1806   RELATED DB: TARGETDB                     
DBREF  2GLF A    3   452  UNP    Q9WYJ9   APEA_THEMA       2    451             
DBREF  2GLF B    3   452  UNP    Q9WYJ9   APEA_THEMA       2    451             
DBREF  2GLF C    3   452  UNP    Q9WYJ9   APEA_THEMA       2    451             
DBREF  2GLF D    3   452  UNP    Q9WYJ9   APEA_THEMA       2    451             
SEQADV 2GLF MSE A    4  UNP  Q9WYJ9    MET     3 MODIFIED RESIDUE               
SEQADV 2GLF MSE A   26  UNP  Q9WYJ9    MET    25 MODIFIED RESIDUE               
SEQADV 2GLF MSE A   29  UNP  Q9WYJ9    MET    28 MODIFIED RESIDUE               
SEQADV 2GLF MSE A   37  UNP  Q9WYJ9    MET    36 MODIFIED RESIDUE               
SEQADV 2GLF MSE A   62  UNP  Q9WYJ9    MET    61 MODIFIED RESIDUE               
SEQADV 2GLF MSE A   64  UNP  Q9WYJ9    MET    63 MODIFIED RESIDUE               
SEQADV 2GLF MSE A  187  UNP  Q9WYJ9    MET   186 MODIFIED RESIDUE               
SEQADV 2GLF MSE A  214  UNP  Q9WYJ9    MET   213 MODIFIED RESIDUE               
SEQADV 2GLF MSE A  240  UNP  Q9WYJ9    MET   239 MODIFIED RESIDUE               
SEQADV 2GLF MSE A  305  UNP  Q9WYJ9    MET   304 MODIFIED RESIDUE               
SEQADV 2GLF MSE A  419  UNP  Q9WYJ9    MET   418 MODIFIED RESIDUE               
SEQADV 2GLF MSE A  426  UNP  Q9WYJ9    MET   425 MODIFIED RESIDUE               
SEQADV 2GLF MSE A  449  UNP  Q9WYJ9    MET   448 MODIFIED RESIDUE               
SEQADV 2GLF MSE B    4  UNP  Q9WYJ9    MET     3 MODIFIED RESIDUE               
SEQADV 2GLF MSE B   26  UNP  Q9WYJ9    MET    25 MODIFIED RESIDUE               
SEQADV 2GLF MSE B   29  UNP  Q9WYJ9    MET    28 MODIFIED RESIDUE               
SEQADV 2GLF MSE B   37  UNP  Q9WYJ9    MET    36 MODIFIED RESIDUE               
SEQADV 2GLF MSE B   62  UNP  Q9WYJ9    MET    61 MODIFIED RESIDUE               
SEQADV 2GLF MSE B   64  UNP  Q9WYJ9    MET    63 MODIFIED RESIDUE               
SEQADV 2GLF MSE B  187  UNP  Q9WYJ9    MET   186 MODIFIED RESIDUE               
SEQADV 2GLF MSE B  214  UNP  Q9WYJ9    MET   213 MODIFIED RESIDUE               
SEQADV 2GLF MSE B  240  UNP  Q9WYJ9    MET   239 MODIFIED RESIDUE               
SEQADV 2GLF MSE B  305  UNP  Q9WYJ9    MET   304 MODIFIED RESIDUE               
SEQADV 2GLF MSE B  419  UNP  Q9WYJ9    MET   418 MODIFIED RESIDUE               
SEQADV 2GLF MSE B  426  UNP  Q9WYJ9    MET   425 MODIFIED RESIDUE               
SEQADV 2GLF MSE B  449  UNP  Q9WYJ9    MET   448 MODIFIED RESIDUE               
SEQADV 2GLF MSE C    4  UNP  Q9WYJ9    MET     3 MODIFIED RESIDUE               
SEQADV 2GLF MSE C   26  UNP  Q9WYJ9    MET    25 MODIFIED RESIDUE               
SEQADV 2GLF MSE C   29  UNP  Q9WYJ9    MET    28 MODIFIED RESIDUE               
SEQADV 2GLF MSE C   37  UNP  Q9WYJ9    MET    36 MODIFIED RESIDUE               
SEQADV 2GLF MSE C   62  UNP  Q9WYJ9    MET    61 MODIFIED RESIDUE               
SEQADV 2GLF MSE C   64  UNP  Q9WYJ9    MET    63 MODIFIED RESIDUE               
SEQADV 2GLF MSE C  187  UNP  Q9WYJ9    MET   186 MODIFIED RESIDUE               
SEQADV 2GLF MSE C  214  UNP  Q9WYJ9    MET   213 MODIFIED RESIDUE               
SEQADV 2GLF MSE C  240  UNP  Q9WYJ9    MET   239 MODIFIED RESIDUE               
SEQADV 2GLF MSE C  305  UNP  Q9WYJ9    MET   304 MODIFIED RESIDUE               
SEQADV 2GLF MSE C  419  UNP  Q9WYJ9    MET   418 MODIFIED RESIDUE               
SEQADV 2GLF MSE C  426  UNP  Q9WYJ9    MET   425 MODIFIED RESIDUE               
SEQADV 2GLF MSE C  449  UNP  Q9WYJ9    MET   448 MODIFIED RESIDUE               
SEQADV 2GLF MSE D    4  UNP  Q9WYJ9    MET     3 MODIFIED RESIDUE               
SEQADV 2GLF MSE D   26  UNP  Q9WYJ9    MET    25 MODIFIED RESIDUE               
SEQADV 2GLF MSE D   29  UNP  Q9WYJ9    MET    28 MODIFIED RESIDUE               
SEQADV 2GLF MSE D   37  UNP  Q9WYJ9    MET    36 MODIFIED RESIDUE               
SEQADV 2GLF MSE D   62  UNP  Q9WYJ9    MET    61 MODIFIED RESIDUE               
SEQADV 2GLF MSE D   64  UNP  Q9WYJ9    MET    63 MODIFIED RESIDUE               
SEQADV 2GLF MSE D  187  UNP  Q9WYJ9    MET   186 MODIFIED RESIDUE               
SEQADV 2GLF MSE D  214  UNP  Q9WYJ9    MET   213 MODIFIED RESIDUE               
SEQADV 2GLF MSE D  240  UNP  Q9WYJ9    MET   239 MODIFIED RESIDUE               
SEQADV 2GLF MSE D  305  UNP  Q9WYJ9    MET   304 MODIFIED RESIDUE               
SEQADV 2GLF MSE D  419  UNP  Q9WYJ9    MET   418 MODIFIED RESIDUE               
SEQADV 2GLF MSE D  426  UNP  Q9WYJ9    MET   425 MODIFIED RESIDUE               
SEQADV 2GLF MSE D  449  UNP  Q9WYJ9    MET   448 MODIFIED RESIDUE               
SEQRES   1 A  450  LYS MSE GLU ARG LYS ASN VAL TRP HIS HIS ARG LYS LYS          
SEQRES   2 A  450  GLU GLU ILE GLU ALA PHE SER LYS GLU TYR MSE GLU PHE          
SEQRES   3 A  450  MSE SER LYS ALA LYS THR GLU ARG MSE THR VAL LYS GLU          
SEQRES   4 A  450  ILE LYS ARG ILE LEU ASP GLU SER GLY PHE VAL PRO LEU          
SEQRES   5 A  450  GLU ASP PHE ALA GLY ASP PRO MSE ASN MSE THR VAL TYR          
SEQRES   6 A  450  ALA VAL ASN ARG GLY LYS ALA ILE ALA ALA PHE ARG VAL          
SEQRES   7 A  450  VAL ASP ASP LEU LYS ARG GLY LEU ASN LEU VAL VAL ALA          
SEQRES   8 A  450  HIS ILE ASP SER PRO ARG LEU ASP PHE LYS PRO ASN PRO          
SEQRES   9 A  450  LEU ILE GLU ASP GLU GLN ILE ALA LEU PHE LYS THR HIS          
SEQRES  10 A  450  TYR TYR GLY GLY ILE LYS LYS TYR HIS TRP LEU SER ILE          
SEQRES  11 A  450  PRO LEU GLU ILE HIS GLY VAL LEU PHE LYS ASN ASP GLY          
SEQRES  12 A  450  THR GLU ILE GLU ILE HIS ILE GLY ASP LYS PRO GLU ASP          
SEQRES  13 A  450  PRO VAL PHE THR ILE PRO ASP LEU LEU PRO HIS LEU ASP          
SEQRES  14 A  450  LYS GLU ASP ALA LYS ILE SER GLU LYS PHE LYS GLY GLU          
SEQRES  15 A  450  ASN LEU MSE LEU ILE ALA GLY THR ILE PRO LEU SER GLY          
SEQRES  16 A  450  GLU GLU LYS GLU ALA VAL LYS THR ASN VAL LEU LYS ILE          
SEQRES  17 A  450  LEU ASN GLU MSE TYR GLY ILE THR GLU GLU ASP PHE VAL          
SEQRES  18 A  450  SER GLY GLU ILE GLU VAL VAL PRO ALA PHE SER PRO ARG          
SEQRES  19 A  450  GLU VAL GLY MSE ASP ARG SER LEU ILE GLY ALA TYR GLY          
SEQRES  20 A  450  GLN ASP ASP ARG ILE CYS ALA TYR THR ALA LEU ARG ALA          
SEQRES  21 A  450  LEU LEU SER ALA ASN PRO GLU LYS SER ILE GLY VAL ILE          
SEQRES  22 A  450  PHE PHE ASP LYS GLU GLU ILE GLY SER ASP GLY ASN THR          
SEQRES  23 A  450  GLY ALA LYS ALA ARG PHE TYR LEU LYS ALA LEU ARG GLN          
SEQRES  24 A  450  ILE LEU LYS MSE GLN GLY ALA LYS ASP SER GLU PHE VAL          
SEQRES  25 A  450  LEU ASP GLU VAL LEU GLU ASN THR SER VAL ILE SER GLY          
SEQRES  26 A  450  ASP VAL CYS ALA ALA VAL ASN PRO PRO TYR LYS ASP VAL          
SEQRES  27 A  450  HIS ASP LEU HIS ASN ALA PRO LYS LEU GLY TYR GLY VAL          
SEQRES  28 A  450  ALA LEU VAL LYS TYR THR GLY ALA ARG GLY LYS TYR SER          
SEQRES  29 A  450  THR ASN ASP ALA HIS ALA GLU PHE VAL ALA ARG VAL ARG          
SEQRES  30 A  450  LYS VAL LEU ASN GLU GLN GLY VAL ILE TRP GLN VAL ALA          
SEQRES  31 A  450  THR LEU GLY LYS VAL ASP GLN GLY GLY GLY GLY THR ILE          
SEQRES  32 A  450  ALA LYS PHE PHE ALA GLU ARG GLY SER ASP VAL ILE ASP          
SEQRES  33 A  450  MSE GLY PRO ALA LEU LEU GLY MSE HIS SER PRO PHE GLU          
SEQRES  34 A  450  ILE SER SER LYS ALA ASP LEU PHE GLU THR TYR VAL ALA          
SEQRES  35 A  450  TYR ARG SER LEU MSE GLU LYS LEU                              
SEQRES   1 B  450  LYS MSE GLU ARG LYS ASN VAL TRP HIS HIS ARG LYS LYS          
SEQRES   2 B  450  GLU GLU ILE GLU ALA PHE SER LYS GLU TYR MSE GLU PHE          
SEQRES   3 B  450  MSE SER LYS ALA LYS THR GLU ARG MSE THR VAL LYS GLU          
SEQRES   4 B  450  ILE LYS ARG ILE LEU ASP GLU SER GLY PHE VAL PRO LEU          
SEQRES   5 B  450  GLU ASP PHE ALA GLY ASP PRO MSE ASN MSE THR VAL TYR          
SEQRES   6 B  450  ALA VAL ASN ARG GLY LYS ALA ILE ALA ALA PHE ARG VAL          
SEQRES   7 B  450  VAL ASP ASP LEU LYS ARG GLY LEU ASN LEU VAL VAL ALA          
SEQRES   8 B  450  HIS ILE ASP SER PRO ARG LEU ASP PHE LYS PRO ASN PRO          
SEQRES   9 B  450  LEU ILE GLU ASP GLU GLN ILE ALA LEU PHE LYS THR HIS          
SEQRES  10 B  450  TYR TYR GLY GLY ILE LYS LYS TYR HIS TRP LEU SER ILE          
SEQRES  11 B  450  PRO LEU GLU ILE HIS GLY VAL LEU PHE LYS ASN ASP GLY          
SEQRES  12 B  450  THR GLU ILE GLU ILE HIS ILE GLY ASP LYS PRO GLU ASP          
SEQRES  13 B  450  PRO VAL PHE THR ILE PRO ASP LEU LEU PRO HIS LEU ASP          
SEQRES  14 B  450  LYS GLU ASP ALA LYS ILE SER GLU LYS PHE LYS GLY GLU          
SEQRES  15 B  450  ASN LEU MSE LEU ILE ALA GLY THR ILE PRO LEU SER GLY          
SEQRES  16 B  450  GLU GLU LYS GLU ALA VAL LYS THR ASN VAL LEU LYS ILE          
SEQRES  17 B  450  LEU ASN GLU MSE TYR GLY ILE THR GLU GLU ASP PHE VAL          
SEQRES  18 B  450  SER GLY GLU ILE GLU VAL VAL PRO ALA PHE SER PRO ARG          
SEQRES  19 B  450  GLU VAL GLY MSE ASP ARG SER LEU ILE GLY ALA TYR GLY          
SEQRES  20 B  450  GLN ASP ASP ARG ILE CYS ALA TYR THR ALA LEU ARG ALA          
SEQRES  21 B  450  LEU LEU SER ALA ASN PRO GLU LYS SER ILE GLY VAL ILE          
SEQRES  22 B  450  PHE PHE ASP LYS GLU GLU ILE GLY SER ASP GLY ASN THR          
SEQRES  23 B  450  GLY ALA LYS ALA ARG PHE TYR LEU LYS ALA LEU ARG GLN          
SEQRES  24 B  450  ILE LEU LYS MSE GLN GLY ALA LYS ASP SER GLU PHE VAL          
SEQRES  25 B  450  LEU ASP GLU VAL LEU GLU ASN THR SER VAL ILE SER GLY          
SEQRES  26 B  450  ASP VAL CYS ALA ALA VAL ASN PRO PRO TYR LYS ASP VAL          
SEQRES  27 B  450  HIS ASP LEU HIS ASN ALA PRO LYS LEU GLY TYR GLY VAL          
SEQRES  28 B  450  ALA LEU VAL LYS TYR THR GLY ALA ARG GLY LYS TYR SER          
SEQRES  29 B  450  THR ASN ASP ALA HIS ALA GLU PHE VAL ALA ARG VAL ARG          
SEQRES  30 B  450  LYS VAL LEU ASN GLU GLN GLY VAL ILE TRP GLN VAL ALA          
SEQRES  31 B  450  THR LEU GLY LYS VAL ASP GLN GLY GLY GLY GLY THR ILE          
SEQRES  32 B  450  ALA LYS PHE PHE ALA GLU ARG GLY SER ASP VAL ILE ASP          
SEQRES  33 B  450  MSE GLY PRO ALA LEU LEU GLY MSE HIS SER PRO PHE GLU          
SEQRES  34 B  450  ILE SER SER LYS ALA ASP LEU PHE GLU THR TYR VAL ALA          
SEQRES  35 B  450  TYR ARG SER LEU MSE GLU LYS LEU                              
SEQRES   1 C  450  LYS MSE GLU ARG LYS ASN VAL TRP HIS HIS ARG LYS LYS          
SEQRES   2 C  450  GLU GLU ILE GLU ALA PHE SER LYS GLU TYR MSE GLU PHE          
SEQRES   3 C  450  MSE SER LYS ALA LYS THR GLU ARG MSE THR VAL LYS GLU          
SEQRES   4 C  450  ILE LYS ARG ILE LEU ASP GLU SER GLY PHE VAL PRO LEU          
SEQRES   5 C  450  GLU ASP PHE ALA GLY ASP PRO MSE ASN MSE THR VAL TYR          
SEQRES   6 C  450  ALA VAL ASN ARG GLY LYS ALA ILE ALA ALA PHE ARG VAL          
SEQRES   7 C  450  VAL ASP ASP LEU LYS ARG GLY LEU ASN LEU VAL VAL ALA          
SEQRES   8 C  450  HIS ILE ASP SER PRO ARG LEU ASP PHE LYS PRO ASN PRO          
SEQRES   9 C  450  LEU ILE GLU ASP GLU GLN ILE ALA LEU PHE LYS THR HIS          
SEQRES  10 C  450  TYR TYR GLY GLY ILE LYS LYS TYR HIS TRP LEU SER ILE          
SEQRES  11 C  450  PRO LEU GLU ILE HIS GLY VAL LEU PHE LYS ASN ASP GLY          
SEQRES  12 C  450  THR GLU ILE GLU ILE HIS ILE GLY ASP LYS PRO GLU ASP          
SEQRES  13 C  450  PRO VAL PHE THR ILE PRO ASP LEU LEU PRO HIS LEU ASP          
SEQRES  14 C  450  LYS GLU ASP ALA LYS ILE SER GLU LYS PHE LYS GLY GLU          
SEQRES  15 C  450  ASN LEU MSE LEU ILE ALA GLY THR ILE PRO LEU SER GLY          
SEQRES  16 C  450  GLU GLU LYS GLU ALA VAL LYS THR ASN VAL LEU LYS ILE          
SEQRES  17 C  450  LEU ASN GLU MSE TYR GLY ILE THR GLU GLU ASP PHE VAL          
SEQRES  18 C  450  SER GLY GLU ILE GLU VAL VAL PRO ALA PHE SER PRO ARG          
SEQRES  19 C  450  GLU VAL GLY MSE ASP ARG SER LEU ILE GLY ALA TYR GLY          
SEQRES  20 C  450  GLN ASP ASP ARG ILE CYS ALA TYR THR ALA LEU ARG ALA          
SEQRES  21 C  450  LEU LEU SER ALA ASN PRO GLU LYS SER ILE GLY VAL ILE          
SEQRES  22 C  450  PHE PHE ASP LYS GLU GLU ILE GLY SER ASP GLY ASN THR          
SEQRES  23 C  450  GLY ALA LYS ALA ARG PHE TYR LEU LYS ALA LEU ARG GLN          
SEQRES  24 C  450  ILE LEU LYS MSE GLN GLY ALA LYS ASP SER GLU PHE VAL          
SEQRES  25 C  450  LEU ASP GLU VAL LEU GLU ASN THR SER VAL ILE SER GLY          
SEQRES  26 C  450  ASP VAL CYS ALA ALA VAL ASN PRO PRO TYR LYS ASP VAL          
SEQRES  27 C  450  HIS ASP LEU HIS ASN ALA PRO LYS LEU GLY TYR GLY VAL          
SEQRES  28 C  450  ALA LEU VAL LYS TYR THR GLY ALA ARG GLY LYS TYR SER          
SEQRES  29 C  450  THR ASN ASP ALA HIS ALA GLU PHE VAL ALA ARG VAL ARG          
SEQRES  30 C  450  LYS VAL LEU ASN GLU GLN GLY VAL ILE TRP GLN VAL ALA          
SEQRES  31 C  450  THR LEU GLY LYS VAL ASP GLN GLY GLY GLY GLY THR ILE          
SEQRES  32 C  450  ALA LYS PHE PHE ALA GLU ARG GLY SER ASP VAL ILE ASP          
SEQRES  33 C  450  MSE GLY PRO ALA LEU LEU GLY MSE HIS SER PRO PHE GLU          
SEQRES  34 C  450  ILE SER SER LYS ALA ASP LEU PHE GLU THR TYR VAL ALA          
SEQRES  35 C  450  TYR ARG SER LEU MSE GLU LYS LEU                              
SEQRES   1 D  450  LYS MSE GLU ARG LYS ASN VAL TRP HIS HIS ARG LYS LYS          
SEQRES   2 D  450  GLU GLU ILE GLU ALA PHE SER LYS GLU TYR MSE GLU PHE          
SEQRES   3 D  450  MSE SER LYS ALA LYS THR GLU ARG MSE THR VAL LYS GLU          
SEQRES   4 D  450  ILE LYS ARG ILE LEU ASP GLU SER GLY PHE VAL PRO LEU          
SEQRES   5 D  450  GLU ASP PHE ALA GLY ASP PRO MSE ASN MSE THR VAL TYR          
SEQRES   6 D  450  ALA VAL ASN ARG GLY LYS ALA ILE ALA ALA PHE ARG VAL          
SEQRES   7 D  450  VAL ASP ASP LEU LYS ARG GLY LEU ASN LEU VAL VAL ALA          
SEQRES   8 D  450  HIS ILE ASP SER PRO ARG LEU ASP PHE LYS PRO ASN PRO          
SEQRES   9 D  450  LEU ILE GLU ASP GLU GLN ILE ALA LEU PHE LYS THR HIS          
SEQRES  10 D  450  TYR TYR GLY GLY ILE LYS LYS TYR HIS TRP LEU SER ILE          
SEQRES  11 D  450  PRO LEU GLU ILE HIS GLY VAL LEU PHE LYS ASN ASP GLY          
SEQRES  12 D  450  THR GLU ILE GLU ILE HIS ILE GLY ASP LYS PRO GLU ASP          
SEQRES  13 D  450  PRO VAL PHE THR ILE PRO ASP LEU LEU PRO HIS LEU ASP          
SEQRES  14 D  450  LYS GLU ASP ALA LYS ILE SER GLU LYS PHE LYS GLY GLU          
SEQRES  15 D  450  ASN LEU MSE LEU ILE ALA GLY THR ILE PRO LEU SER GLY          
SEQRES  16 D  450  GLU GLU LYS GLU ALA VAL LYS THR ASN VAL LEU LYS ILE          
SEQRES  17 D  450  LEU ASN GLU MSE TYR GLY ILE THR GLU GLU ASP PHE VAL          
SEQRES  18 D  450  SER GLY GLU ILE GLU VAL VAL PRO ALA PHE SER PRO ARG          
SEQRES  19 D  450  GLU VAL GLY MSE ASP ARG SER LEU ILE GLY ALA TYR GLY          
SEQRES  20 D  450  GLN ASP ASP ARG ILE CYS ALA TYR THR ALA LEU ARG ALA          
SEQRES  21 D  450  LEU LEU SER ALA ASN PRO GLU LYS SER ILE GLY VAL ILE          
SEQRES  22 D  450  PHE PHE ASP LYS GLU GLU ILE GLY SER ASP GLY ASN THR          
SEQRES  23 D  450  GLY ALA LYS ALA ARG PHE TYR LEU LYS ALA LEU ARG GLN          
SEQRES  24 D  450  ILE LEU LYS MSE GLN GLY ALA LYS ASP SER GLU PHE VAL          
SEQRES  25 D  450  LEU ASP GLU VAL LEU GLU ASN THR SER VAL ILE SER GLY          
SEQRES  26 D  450  ASP VAL CYS ALA ALA VAL ASN PRO PRO TYR LYS ASP VAL          
SEQRES  27 D  450  HIS ASP LEU HIS ASN ALA PRO LYS LEU GLY TYR GLY VAL          
SEQRES  28 D  450  ALA LEU VAL LYS TYR THR GLY ALA ARG GLY LYS TYR SER          
SEQRES  29 D  450  THR ASN ASP ALA HIS ALA GLU PHE VAL ALA ARG VAL ARG          
SEQRES  30 D  450  LYS VAL LEU ASN GLU GLN GLY VAL ILE TRP GLN VAL ALA          
SEQRES  31 D  450  THR LEU GLY LYS VAL ASP GLN GLY GLY GLY GLY THR ILE          
SEQRES  32 D  450  ALA LYS PHE PHE ALA GLU ARG GLY SER ASP VAL ILE ASP          
SEQRES  33 D  450  MSE GLY PRO ALA LEU LEU GLY MSE HIS SER PRO PHE GLU          
SEQRES  34 D  450  ILE SER SER LYS ALA ASP LEU PHE GLU THR TYR VAL ALA          
SEQRES  35 D  450  TYR ARG SER LEU MSE GLU LYS LEU                              
MODRES 2GLF MSE A    4  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE A   26  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE A   29  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE A   37  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE A   62  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE A   64  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE A  187  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE A  214  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE A  240  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE A  305  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE A  419  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE A  426  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE A  449  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE B    4  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE B   26  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE B   29  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE B   37  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE B   62  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE B   64  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE B  187  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE B  214  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE B  240  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE B  305  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE B  419  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE B  426  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE B  449  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE C    4  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE C   26  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE C   29  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE C   37  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE C   62  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE C   64  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE C  187  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE C  214  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE C  240  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE C  305  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE C  419  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE C  426  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE C  449  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE D    4  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE D   26  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE D   29  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE D   37  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE D   62  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE D   64  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE D  187  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE D  214  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE D  240  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE D  305  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE D  419  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE D  426  MET  SELENOMETHIONINE                                   
MODRES 2GLF MSE D  449  MET  SELENOMETHIONINE                                   
HET    MSE  A   4       8                                                       
HET    MSE  A  26       8                                                       
HET    MSE  A  29       8                                                       
HET    MSE  A  37       8                                                       
HET    MSE  A  62       8                                                       
HET    MSE  A  64       8                                                       
HET    MSE  A 187       8                                                       
HET    MSE  A 214       8                                                       
HET    MSE  A 240       8                                                       
HET    MSE  A 305       8                                                       
HET    MSE  A 419       8                                                       
HET    MSE  A 426       8                                                       
HET    MSE  A 449       8                                                       
HET    MSE  B   4       8                                                       
HET    MSE  B  26       8                                                       
HET    MSE  B  29       8                                                       
HET    MSE  B  37       8                                                       
HET    MSE  B  62       8                                                       
HET    MSE  B  64       8                                                       
HET    MSE  B 187       8                                                       
HET    MSE  B 214       8                                                       
HET    MSE  B 240       8                                                       
HET    MSE  B 305       8                                                       
HET    MSE  B 419       8                                                       
HET    MSE  B 426       8                                                       
HET    MSE  B 449       8                                                       
HET    MSE  C   4       8                                                       
HET    MSE  C  26       8                                                       
HET    MSE  C  29       8                                                       
HET    MSE  C  37       8                                                       
HET    MSE  C  62       8                                                       
HET    MSE  C  64       8                                                       
HET    MSE  C 187       8                                                       
HET    MSE  C 214       8                                                       
HET    MSE  C 240       8                                                       
HET    MSE  C 305       8                                                       
HET    MSE  C 419       8                                                       
HET    MSE  C 426       8                                                       
HET    MSE  C 449       8                                                       
HET    MSE  D   4       8                                                       
HET    MSE  D  26       8                                                       
HET    MSE  D  29       8                                                       
HET    MSE  D  37       8                                                       
HET    MSE  D  62       8                                                       
HET    MSE  D  64       8                                                       
HET    MSE  D 187       8                                                       
HET    MSE  D 214       8                                                       
HET    MSE  D 240       8                                                       
HET    MSE  D 305       8                                                       
HET    MSE  D 419       8                                                       
HET    MSE  D 426       8                                                       
HET    MSE  D 449       8                                                       
HET     MN  A5001       1                                                       
HET     MN  A5002       1                                                       
HET     MN  B5003       1                                                       
HET     MN  B5004       1                                                       
HET     MN  C5006       1                                                       
HET     MN  C5007       1                                                       
HET     MN  D5008       1                                                       
HET     MN  D5009       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   1  MSE    52(C5 H11 N O2 SE)                                           
FORMUL   5   MN    8(MN 2+)                                                     
FORMUL  13  HOH   *479(H2 O)                                                    
HELIX    1   1 ASN A    8  HIS A   12  5                                   5    
HELIX    2   2 LYS A   14  ALA A   32  1                                  19    
HELIX    3   3 THR A   34  GLU A   48  1                                  15    
HELIX    4   4 ASP A   83  GLY A   87  5                                   5    
HELIX    5   5 LYS A  126  LEU A  130  5                                   5    
HELIX    6   6 LEU A  167  ASP A  171  5                                   5    
HELIX    7   7 LYS A  182  ASN A  185  5                                   4    
HELIX    8   8 GLU A  201  GLY A  216  1                                  16    
HELIX    9   9 THR A  218  VAL A  223  5                                   6    
HELIX   10  10 GLY A  249  ALA A  266  1                                  18    
HELIX   11  11 LYS A  279  GLY A  283  5                                   5    
HELIX   12  12 ARG A  293  GLN A  306  1                                  14    
HELIX   13  13 SER A  311  ASN A  321  1                                  11    
HELIX   14  14 ASN A  334  HIS A  341  5                                   8    
HELIX   15  15 ASP A  342  ALA A  346  5                                   5    
HELIX   16  16 HIS A  371  GLN A  385  1                                  15    
HELIX   17  17 ILE A  405  GLU A  411  1                                   7    
HELIX   18  18 LYS A  435  LEU A  452  1                                  18    
HELIX   19  19 ASN B    8  HIS B   12  5                                   5    
HELIX   20  20 LYS B   14  SER B   30  1                                  17    
HELIX   21  21 THR B   34  SER B   49  1                                  16    
HELIX   22  22 GLU B   55  PHE B   57  5                                   3    
HELIX   23  23 ASP B   83  GLY B   87  5                                   5    
HELIX   24  24 LYS B  125  LEU B  130  5                                   6    
HELIX   25  25 LYS B  182  ASN B  185  5                                   4    
HELIX   26  26 GLU B  201  GLY B  216  1                                  16    
HELIX   27  27 THR B  218  VAL B  223  5                                   6    
HELIX   28  28 GLY B  249  ALA B  266  1                                  18    
HELIX   29  29 LYS B  279  GLY B  283  5                                   5    
HELIX   30  30 ARG B  293  GLN B  306  1                                  14    
HELIX   31  31 ASP B  310  ASN B  321  1                                  12    
HELIX   32  32 ASN B  334  HIS B  341  5                                   8    
HELIX   33  33 ASP B  342  ALA B  346  5                                   5    
HELIX   34  34 HIS B  371  GLN B  385  1                                  15    
HELIX   35  35 ILE B  405  GLU B  411  1                                   7    
HELIX   36  36 LYS B  435  LEU B  452  1                                  18    
HELIX   37  37 ASN C    8  HIS C   12  5                                   5    
HELIX   38  38 LYS C   14  SER C   30  1                                  17    
HELIX   39  39 THR C   34  GLU C   48  1                                  15    
HELIX   40  40 SER C   49  PHE C   51  5                                   3    
HELIX   41  41 GLU C   55  PHE C   57  5                                   3    
HELIX   42  42 ASP C   83  ARG C   86  5                                   4    
HELIX   43  43 LYS C  125  LEU C  130  5                                   6    
HELIX   44  44 LYS C  182  LEU C  186  5                                   5    
HELIX   45  45 GLU C  201  GLY C  216  1                                  16    
HELIX   46  46 THR C  218  VAL C  223  5                                   6    
HELIX   47  47 GLY C  249  ALA C  266  1                                  18    
HELIX   48  48 LYS C  279  GLY C  283  5                                   5    
HELIX   49  49 ARG C  293  GLN C  306  1                                  14    
HELIX   50  50 ASP C  310  ASN C  321  1                                  12    
HELIX   51  51 ASN C  334  HIS C  341  5                                   8    
HELIX   52  52 ASP C  342  ALA C  346  5                                   5    
HELIX   53  53 HIS C  371  GLN C  385  1                                  15    
HELIX   54  54 ILE C  405  GLU C  411  1                                   7    
HELIX   55  55 LYS C  435  LEU C  452  1                                  18    
HELIX   56  56 ASN D    8  HIS D   12  5                                   5    
HELIX   57  57 LYS D   14  SER D   30  1                                  17    
HELIX   58  58 THR D   34  SER D   49  1                                  16    
HELIX   59  59 GLU D   55  PHE D   57  5                                   3    
HELIX   60  60 ASP D   83  ARG D   86  5                                   4    
HELIX   61  61 LYS D  125  LEU D  130  5                                   6    
HELIX   62  62 LYS D  182  ASN D  185  5                                   4    
HELIX   63  63 GLU D  201  GLY D  216  1                                  16    
HELIX   64  64 THR D  218  PHE D  222  5                                   5    
HELIX   65  65 GLY D  249  ALA D  266  1                                  18    
HELIX   66  66 LYS D  279  GLY D  283  5                                   5    
HELIX   67  67 ARG D  293  GLN D  306  1                                  14    
HELIX   68  68 ASP D  310  ASN D  321  1                                  12    
HELIX   69  69 ASN D  334  HIS D  341  5                                   8    
HELIX   70  70 ASP D  342  ALA D  346  5                                   5    
HELIX   71  71 HIS D  371  GLN D  385  1                                  15    
HELIX   72  72 ALA D  406  GLU D  411  1                                   6    
HELIX   73  73 LYS D  435  LEU D  452  1                                  18    
SHEET    1   A 9 VAL A  52  PRO A  53  0                                        
SHEET    2   A 9 VAL A  66  VAL A  69  1  O  TYR A  67   N  VAL A  52           
SHEET    3   A 9 ILE A  75  ARG A  79 -1  O  ALA A  76   N  ALA A  68           
SHEET    4   A 9 ILE A 272  PHE A 277 -1  O  VAL A 274   N  ALA A  77           
SHEET    5   A 9 ASN A  89  HIS A  94  1  N  ALA A  93   O  PHE A 277           
SHEET    6   A 9 SER A 323  GLY A 327  1  O  GLY A 327   N  VAL A  92           
SHEET    7   A 9 VAL A 416  GLY A 420  1  O  MSE A 419   N  SER A 326           
SHEET    8   A 9 VAL A 353  VAL A 356 -1  N  ALA A 354   O  GLY A 420           
SHEET    9   A 9 TRP A 389  VAL A 391  1  O  GLN A 390   N  VAL A 353           
SHEET    1   B 6 GLU A 147  ILE A 152  0                                        
SHEET    2   B 6 LEU A 134  PHE A 141 -1  N  ILE A 136   O  ILE A 152           
SHEET    3   B 6 GLY A 225  PRO A 231 -1  O  GLU A 228   N  HIS A 137           
SHEET    4   B 6 ARG A  99  ASP A 110 -1  N  LEU A 100   O  VAL A 229           
SHEET    5   B 6 ILE A 113  TYR A 121 -1  O  LEU A 115   N  ILE A 108           
SHEET    6   B 6 MSE A 187  GLY A 191 -1  O  ALA A 190   N  ALA A 114           
SHEET    1   C 3 ARG A 236  VAL A 238  0                                        
SHEET    2   C 3 LEU A 244  ALA A 247 -1  O  GLY A 246   N  ARG A 236           
SHEET    3   C 3 GLU A 431  SER A 434 -1  O  SER A 433   N  ILE A 245           
SHEET    1   D 2 CYS A 330  ALA A 331  0                                        
SHEET    2   D 2 ALA A 422  LEU A 423  1  O  LEU A 423   N  CYS A 330           
SHEET    1   E 9 VAL B  52  PRO B  53  0                                        
SHEET    2   E 9 MSE B  64  VAL B  69  1  O  THR B  65   N  VAL B  52           
SHEET    3   E 9 ILE B  75  VAL B  80 -1  O  ALA B  76   N  ALA B  68           
SHEET    4   E 9 ILE B 272  PHE B 277 -1  O  VAL B 274   N  ALA B  77           
SHEET    5   E 9 ASN B  89  HIS B  94  1  N  ALA B  93   O  PHE B 277           
SHEET    6   E 9 SER B 323  SER B 326  1  O  ILE B 325   N  LEU B  90           
SHEET    7   E 9 ASP B 415  GLY B 420  1  O  ASP B 415   N  VAL B 324           
SHEET    8   E 9 VAL B 353  VAL B 356 -1  N  ALA B 354   O  GLY B 420           
SHEET    9   E 9 TRP B 389  VAL B 391  1  O  GLN B 390   N  LEU B 355           
SHEET    1   F 6 GLU B 147  ILE B 152  0                                        
SHEET    2   F 6 LEU B 134  PHE B 141 -1  N  LEU B 140   O  ILE B 148           
SHEET    3   F 6 GLY B 225  PRO B 231 -1  O  GLU B 228   N  HIS B 137           
SHEET    4   F 6 ARG B  99  GLU B 109 -1  N  LEU B 100   O  VAL B 229           
SHEET    5   F 6 ALA B 114  TYR B 121 -1  O  TYR B 121   N  ARG B  99           
SHEET    6   F 6 MSE B 187  GLY B 191 -1  O  ALA B 190   N  ALA B 114           
SHEET    1   G 3 ARG B 236  VAL B 238  0                                        
SHEET    2   G 3 LEU B 244  ALA B 247 -1  O  GLY B 246   N  ARG B 236           
SHEET    3   G 3 GLU B 431  SER B 434 -1  O  SER B 433   N  ILE B 245           
SHEET    1   H 2 CYS B 330  ALA B 331  0                                        
SHEET    2   H 2 ALA B 422  LEU B 423  1  O  LEU B 423   N  CYS B 330           
SHEET    1   I 9 VAL C  52  PRO C  53  0                                        
SHEET    2   I 9 MSE C  64  VAL C  69  1  O  TYR C  67   N  VAL C  52           
SHEET    3   I 9 ILE C  75  VAL C  80 -1  O  VAL C  80   N  MSE C  64           
SHEET    4   I 9 SER C 271  PHE C 277 -1  O  PHE C 276   N  ILE C  75           
SHEET    5   I 9 LEU C  88  HIS C  94  1  N  ALA C  93   O  PHE C 277           
SHEET    6   I 9 SER C 323  GLY C 327  1  O  ILE C 325   N  LEU C  90           
SHEET    7   I 9 ASP C 415  GLY C 420  1  O  MSE C 419   N  SER C 326           
SHEET    8   I 9 VAL C 353  VAL C 356 -1  N  VAL C 356   O  ASP C 418           
SHEET    9   I 9 TRP C 389  VAL C 391  1  O  GLN C 390   N  LEU C 355           
SHEET    1   J 6 GLU C 147  ILE C 152  0                                        
SHEET    2   J 6 LEU C 134  PHE C 141 -1  N  GLY C 138   O  ILE C 150           
SHEET    3   J 6 GLY C 225  PRO C 231 -1  O  GLU C 228   N  HIS C 137           
SHEET    4   J 6 ARG C  99  ASP C 110 -1  N  LEU C 100   O  VAL C 229           
SHEET    5   J 6 ILE C 113  TYR C 121 -1  O  LYS C 117   N  PRO C 106           
SHEET    6   J 6 LEU C 188  GLY C 191 -1  O  ALA C 190   N  ALA C 114           
SHEET    1   K 3 ARG C 236  VAL C 238  0                                        
SHEET    2   K 3 LEU C 244  ALA C 247 -1  O  GLY C 246   N  ARG C 236           
SHEET    3   K 3 GLU C 431  SER C 434 -1  O  SER C 433   N  ILE C 245           
SHEET    1   L 2 CYS C 330  ALA C 331  0                                        
SHEET    2   L 2 ALA C 422  LEU C 423  1  O  LEU C 423   N  CYS C 330           
SHEET    1   M 9 VAL D  52  PRO D  53  0                                        
SHEET    2   M 9 MSE D  64  VAL D  69  1  O  THR D  65   N  VAL D  52           
SHEET    3   M 9 ILE D  75  VAL D  80 -1  O  ALA D  76   N  ALA D  68           
SHEET    4   M 9 SER D 271  PHE D 277 -1  O  VAL D 274   N  ALA D  77           
SHEET    5   M 9 LEU D  88  HIS D  94  1  N  ALA D  93   O  PHE D 277           
SHEET    6   M 9 SER D 323  SER D 326  1  O  ILE D 325   N  LEU D  90           
SHEET    7   M 9 ASP D 415  GLY D 420  1  O  ASP D 415   N  VAL D 324           
SHEET    8   M 9 VAL D 353  VAL D 356 -1  N  ALA D 354   O  GLY D 420           
SHEET    9   M 9 TRP D 389  VAL D 391  1  O  GLN D 390   N  VAL D 353           
SHEET    1   N 3 PHE D 102  GLU D 109  0                                        
SHEET    2   N 3 ALA D 114  THR D 118 -1  O  LEU D 115   N  ILE D 108           
SHEET    3   N 3 MSE D 187  ILE D 189 -1  O  LEU D 188   N  PHE D 116           
SHEET    1   O 3 GLU D 147  ILE D 152  0                                        
SHEET    2   O 3 LEU D 134  PHE D 141 -1  N  LEU D 140   O  ILE D 148           
SHEET    3   O 3 GLY D 225  PRO D 231 -1  O  GLU D 228   N  HIS D 137           
SHEET    1   P 3 ARG D 236  VAL D 238  0                                        
SHEET    2   P 3 LEU D 244  ALA D 247 -1  O  LEU D 244   N  VAL D 238           
SHEET    3   P 3 GLU D 431  SER D 434 -1  O  SER D 433   N  ILE D 245           
SHEET    1   Q 2 CYS D 330  ALA D 331  0                                        
SHEET    2   Q 2 ALA D 422  LEU D 423  1  O  LEU D 423   N  CYS D 330           
LINK         C   LYS A   3                 N   MSE A   4     1555   1555  1.33  
LINK         C   MSE A   4                 N   GLU A   5     1555   1555  1.33  
LINK         C   TYR A  25                 N   MSE A  26     1555   1555  1.33  
LINK         C   MSE A  26                 N   GLU A  27     1555   1555  1.33  
LINK         C   PHE A  28                 N   MSE A  29     1555   1555  1.33  
LINK         C   MSE A  29                 N   SER A  30     1555   1555  1.33  
LINK         C   ARG A  36                 N   MSE A  37     1555   1555  1.33  
LINK         C   MSE A  37                 N   THR A  38     1555   1555  1.33  
LINK         C   PRO A  61                 N   MSE A  62     1555   1555  1.33  
LINK         C   MSE A  62                 N   ASN A  63     1555   1555  1.33  
LINK         C   ASN A  63                 N   MSE A  64     1555   1555  1.33  
LINK         C   MSE A  64                 N   THR A  65     1555   1555  1.33  
LINK         C   LEU A 186                 N   MSE A 187     1555   1555  1.33  
LINK         C   MSE A 187                 N   LEU A 188     1555   1555  1.33  
LINK         C   GLU A 213                 N   MSE A 214     1555   1555  1.33  
LINK         C   MSE A 214                 N   TYR A 215     1555   1555  1.33  
LINK         C   GLY A 239                 N   MSE A 240     1555   1555  1.33  
LINK         C   MSE A 240                 N   ASP A 241     1555   1555  1.33  
LINK         C   LYS A 304                 N   MSE A 305     1555   1555  1.33  
LINK         C   MSE A 305                 N   GLN A 306     1555   1555  1.33  
LINK         C   ASP A 418                 N   MSE A 419     1555   1555  1.33  
LINK         C   MSE A 419                 N   GLY A 420     1555   1555  1.33  
LINK         C   GLY A 425                 N   MSE A 426     1555   1555  1.33  
LINK         C   MSE A 426                 N   HIS A 427     1555   1555  1.33  
LINK         C   LEU A 448                 N   MSE A 449     1555   1555  1.33  
LINK         C   MSE A 449                 N   GLU A 450     1555   1555  1.33  
LINK        MN    MN A5001                 NE2 HIS A  94     1555   1555  2.44  
LINK        MN    MN A5001                 OD1 ASP A 251     1555   1555  2.32  
LINK        MN    MN A5001                 OD1 ASP A 328     1555   1555  2.55  
LINK        MN    MN A5001                 OD2 ASP A 328     1555   1555  2.40  
LINK        MN    MN A5001                 O   HOH A5079     1555   1555  2.36  
LINK        MN    MN A5002                 OE1 GLU A 281     1555   1555  2.64  
LINK        MN    MN A5002                 NE2 HIS A 427     1555   1555  2.42  
LINK        MN    MN A5002                 OD2 ASP A 251     1555   1555  2.41  
LINK        MN    MN A5002                 OE2 GLU A 281     1555   1555  2.04  
LINK         C   LYS B   3                 N   MSE B   4     1555   1555  1.33  
LINK         C   MSE B   4                 N   GLU B   5     1555   1555  1.33  
LINK         C   TYR B  25                 N   MSE B  26     1555   1555  1.33  
LINK         C   MSE B  26                 N   GLU B  27     1555   1555  1.33  
LINK         C   PHE B  28                 N   MSE B  29     1555   1555  1.33  
LINK         C   MSE B  29                 N   SER B  30     1555   1555  1.32  
LINK         C   ARG B  36                 N   MSE B  37     1555   1555  1.33  
LINK         C   MSE B  37                 N   THR B  38     1555   1555  1.33  
LINK         C   PRO B  61                 N   MSE B  62     1555   1555  1.33  
LINK         C   MSE B  62                 N   ASN B  63     1555   1555  1.32  
LINK         C   ASN B  63                 N   MSE B  64     1555   1555  1.33  
LINK         C   MSE B  64                 N   THR B  65     1555   1555  1.33  
LINK         C   LEU B 186                 N   MSE B 187     1555   1555  1.33  
LINK         C   MSE B 187                 N   LEU B 188     1555   1555  1.33  
LINK         C   GLU B 213                 N   MSE B 214     1555   1555  1.33  
LINK         C   MSE B 214                 N   TYR B 215     1555   1555  1.33  
LINK         C   GLY B 239                 N   MSE B 240     1555   1555  1.33  
LINK         C   MSE B 240                 N   ASP B 241     1555   1555  1.33  
LINK         C   LYS B 304                 N   MSE B 305     1555   1555  1.33  
LINK         C   MSE B 305                 N   GLN B 306     1555   1555  1.33  
LINK         C   ASP B 418                 N   MSE B 419     1555   1555  1.33  
LINK         C   MSE B 419                 N   GLY B 420     1555   1555  1.33  
LINK         C   GLY B 425                 N   MSE B 426     1555   1555  1.33  
LINK         C   MSE B 426                 N   HIS B 427     1555   1555  1.33  
LINK         C   LEU B 448                 N   MSE B 449     1555   1555  1.33  
LINK         C   MSE B 449                 N   GLU B 450     1555   1555  1.33  
LINK        MN    MN B5003                 OE1 GLU B 281     1555   1555  2.56  
LINK        MN    MN B5003                 OE2 GLU B 281     1555   1555  2.18  
LINK        MN    MN B5003                 NE2 HIS B 427     1555   1555  2.23  
LINK        MN    MN B5003                 OD2 ASP B 251     1555   1555  2.26  
LINK        MN    MN B5003                 O   HOH B5072     1555   1555  2.22  
LINK        MN    MN B5004                 OD1 ASP B 328     1555   1555  2.71  
LINK        MN    MN B5004                 OD1 ASP B 251     1555   1555  2.27  
LINK        MN    MN B5004                 NE2 HIS B  94     1555   1555  2.32  
LINK        MN    MN B5004                 OD2 ASP B 328     1555   1555  2.04  
LINK         C   LYS C   3                 N   MSE C   4     1555   1555  1.33  
LINK         C   MSE C   4                 N   GLU C   5     1555   1555  1.33  
LINK         C   TYR C  25                 N   MSE C  26     1555   1555  1.33  
LINK         C   MSE C  26                 N   GLU C  27     1555   1555  1.33  
LINK         C   PHE C  28                 N   MSE C  29     1555   1555  1.33  
LINK         C   MSE C  29                 N   SER C  30     1555   1555  1.33  
LINK         C   ARG C  36                 N   MSE C  37     1555   1555  1.33  
LINK         C   MSE C  37                 N   THR C  38     1555   1555  1.33  
LINK         C   PRO C  61                 N   MSE C  62     1555   1555  1.33  
LINK         C   MSE C  62                 N   ASN C  63     1555   1555  1.33  
LINK         C   ASN C  63                 N   MSE C  64     1555   1555  1.33  
LINK         C   MSE C  64                 N   THR C  65     1555   1555  1.33  
LINK         C   LEU C 186                 N   MSE C 187     1555   1555  1.33  
LINK         C   MSE C 187                 N   LEU C 188     1555   1555  1.33  
LINK         C   GLU C 213                 N   MSE C 214     1555   1555  1.33  
LINK         C   MSE C 214                 N   TYR C 215     1555   1555  1.33  
LINK         C   GLY C 239                 N   MSE C 240     1555   1555  1.33  
LINK         C   MSE C 240                 N   ASP C 241     1555   1555  1.33  
LINK         C   LYS C 304                 N   MSE C 305     1555   1555  1.33  
LINK         C   MSE C 305                 N   GLN C 306     1555   1555  1.33  
LINK         C   ASP C 418                 N   MSE C 419     1555   1555  1.33  
LINK         C   MSE C 419                 N   GLY C 420     1555   1555  1.33  
LINK         C   GLY C 425                 N   MSE C 426     1555   1555  1.33  
LINK         C   MSE C 426                 N   HIS C 427     1555   1555  1.33  
LINK         C   LEU C 448                 N   MSE C 449     1555   1555  1.33  
LINK         C   MSE C 449                 N   GLU C 450     1555   1555  1.33  
LINK        MN    MN C5006                 NE2 HIS C  94     1555   1555  2.29  
LINK        MN    MN C5006                 OD1 ASP C 328     1555   1555  2.65  
LINK        MN    MN C5006                 OD1 ASP C 251     1555   1555  2.28  
LINK        MN    MN C5006                 OD2 ASP C 328     1555   1555  2.27  
LINK        MN    MN C5007                 NE2 HIS C 427     1555   1555  2.40  
LINK        MN    MN C5007                 OE1 GLU C 281     1555   1555  2.13  
LINK        MN    MN C5007                 OE2 GLU C 281     1555   1555  2.59  
LINK        MN    MN C5007                 OD2 ASP C 251     1555   1555  2.57  
LINK         C   LYS D   3                 N   MSE D   4     1555   1555  1.34  
LINK         C   MSE D   4                 N   GLU D   5     1555   1555  1.33  
LINK         C   TYR D  25                 N   MSE D  26     1555   1555  1.33  
LINK         C   MSE D  26                 N   GLU D  27     1555   1555  1.33  
LINK         C   PHE D  28                 N   MSE D  29     1555   1555  1.33  
LINK         C   MSE D  29                 N   SER D  30     1555   1555  1.33  
LINK         C   ARG D  36                 N   MSE D  37     1555   1555  1.33  
LINK         C   MSE D  37                 N   THR D  38     1555   1555  1.33  
LINK         C   PRO D  61                 N   MSE D  62     1555   1555  1.33  
LINK         C   MSE D  62                 N   ASN D  63     1555   1555  1.33  
LINK         C   ASN D  63                 N   MSE D  64     1555   1555  1.33  
LINK         C   MSE D  64                 N   THR D  65     1555   1555  1.33  
LINK         C   LEU D 186                 N   MSE D 187     1555   1555  1.33  
LINK         C   MSE D 187                 N   LEU D 188     1555   1555  1.33  
LINK         C   GLU D 213                 N   MSE D 214     1555   1555  1.33  
LINK         C   MSE D 214                 N   TYR D 215     1555   1555  1.33  
LINK         C   GLY D 239                 N   MSE D 240     1555   1555  1.33  
LINK         C   MSE D 240                 N   ASP D 241     1555   1555  1.33  
LINK         C   LYS D 304                 N   MSE D 305     1555   1555  1.33  
LINK         C   MSE D 305                 N   GLN D 306     1555   1555  1.33  
LINK         C   ASP D 418                 N   MSE D 419     1555   1555  1.33  
LINK         C   MSE D 419                 N   GLY D 420     1555   1555  1.33  
LINK         C   GLY D 425                 N   MSE D 426     1555   1555  1.33  
LINK         C   MSE D 426                 N   HIS D 427     1555   1555  1.33  
LINK         C   LEU D 448                 N   MSE D 449     1555   1555  1.33  
LINK         C   MSE D 449                 N   GLU D 450     1555   1555  1.33  
LINK        MN    MN D5008                 OD2 ASP D 328     1555   1555  2.19  
LINK        MN    MN D5008                 NE2 HIS D  94     1555   1555  2.31  
LINK        MN    MN D5008                 OD1 ASP D 251     1555   1555  2.20  
LINK        MN    MN D5008                 O   HOH D5083     1555   1555  2.06  
LINK        MN    MN D5008                 OD1 ASP D 328     1555   1555  2.68  
LINK        MN    MN D5009                 O   HOH D5096     1555   1555  2.25  
LINK        MN    MN D5009                 OD2 ASP D 251     1555   1555  2.52  
LINK        MN    MN D5009                 OE1 GLU D 281     1555   1555  2.12  
LINK        MN    MN D5009                 NE2 HIS D 427     1555   1555  2.33  
SITE     1 AC1  6 HIS A  94  ASP A 251  GLU A 280  ASP A 328                    
SITE     2 AC1  6  MN A5002  HOH A5079                                          
SITE     1 AC2  5 ASP A 251  GLU A 281  MSE A 426  HIS A 427                    
SITE     2 AC2  5  MN A5001                                                     
SITE     1 AC3  6 ASP B 251  GLU B 281  MSE B 426  HIS B 427                    
SITE     2 AC3  6  MN B5004  HOH B5072                                          
SITE     1 AC4  6 HIS B  94  ASP B 251  GLU B 280  ASP B 328                    
SITE     2 AC4  6  MN B5003  HOH B5072                                          
SITE     1 AC5  5 HIS C  94  ASP C 251  GLU C 280  ASP C 328                    
SITE     2 AC5  5  MN C5007                                                     
SITE     1 AC6  6 ASP C 251  GLU C 280  GLU C 281  MSE C 426                    
SITE     2 AC6  6 HIS C 427   MN C5006                                          
SITE     1 AC7  6 HIS D  94  ASP D 251  GLU D 280  ASP D 328                    
SITE     2 AC7  6  MN D5009  HOH D5083                                          
SITE     1 AC8  6 ASP D 251  GLU D 281  MSE D 426  HIS D 427                    
SITE     2 AC8  6  MN D5008  HOH D5096                                          
CRYST1  191.225  191.225  191.225  90.00  90.00  90.00 P 21 3       48          
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      0.005229  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005229  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005229        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system