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Database: PDB
Entry: 1ZMB
LinkDB: 1ZMB
Original site: 1ZMB 
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   10-MAY-05   1ZMB              
TITLE     CRYSTAL STRUCTURE OF THE PUTATIVE ACETYLXYLAN ESTERASE FROM           
TITLE    2 CLOSTRIDIUM ACETOBUTYLICUM, NORTHEAST STRUCTURAL GENOMICS TARGET CAR6
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLXYLAN ESTERASE RELATED ENZYME;                       
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM ACETOBUTYLICUM;                     
SOURCE   3 ORGANISM_TAXID: 272562;                                              
SOURCE   4 STRAIN: ATCC 824;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;                           
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET21(BL21)                               
KEYWDS    ALPHA-BETA PROTEIN, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE       
KEYWDS   2 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, UNKNOWN  
KEYWDS   3 FUNCTION                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.FOROUHAR,S.M.VOROBIEV,M.ABASHIDZE,M.CIAO,T.B.ACTON,G.T.MONTELIONE,  
AUTHOR   2 J.F.HUNT,L.TONG,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)      
REVDAT   3   13-JUL-11 1ZMB    1       VERSN                                    
REVDAT   2   24-FEB-09 1ZMB    1       VERSN                                    
REVDAT   1   17-MAY-05 1ZMB    0                                                
JRNL        AUTH   F.FOROUHAR,S.M.VOROBIEV,M.ABASHIDZE,M.CIAO,T.B.ACTON,        
JRNL        AUTH 2 G.T.MONTELIONE,J.F.HUNT,L.TONG                               
JRNL        TITL   CRYSTAL STRUCTURE OF THE PUTATIVE ACETYLXYLAN ESTERASE FROM  
JRNL        TITL 2 CLOSTRIDIUM ACETOBUTYLICUM, NORTHEAST STRUCTURAL GENOMICS    
JRNL        TITL 3 TARGET CAR6                                                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : XTALVIEW, CNS 1.1                                    
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 243470.200                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 82.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 104393                         
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) : 0.243                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 10170                           
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.76                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 55.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 10598                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3040                       
REMARK   3   BIN FREE R VALUE                    : 0.3150                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1090                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.010                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13668                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 123                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.50000                                              
REMARK   3    B22 (A**2) : -1.07000                                             
REMARK   3    B33 (A**2) : 0.57000                                              
REMARK   3    B12 (A**2) : 3.94000                                              
REMARK   3    B13 (A**2) : 1.70000                                              
REMARK   3    B23 (A**2) : 6.87000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.36                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.41                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.40                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.47                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.72                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : OVERALL                                   
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        : 0.32                                                 
REMARK   3   BSOL        : 13.29                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ZMB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAY-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB032887.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-FEB-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97914                            
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 118658                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : 0.07600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.34100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXS, SOLVE/RESOLVE                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 10% PEG 20K, AND 5 MM DTT,   
REMARK 280  PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A   285                                                      
REMARK 465     HIS A   286                                                      
REMARK 465     HIS A   287                                                      
REMARK 465     HIS A   288                                                      
REMARK 465     HIS A   289                                                      
REMARK 465     HIS A   290                                                      
REMARK 465     HIS B   285                                                      
REMARK 465     HIS B   286                                                      
REMARK 465     HIS B   287                                                      
REMARK 465     HIS B   288                                                      
REMARK 465     HIS B   289                                                      
REMARK 465     HIS B   290                                                      
REMARK 465     HIS C   285                                                      
REMARK 465     HIS C   286                                                      
REMARK 465     HIS C   287                                                      
REMARK 465     HIS C   288                                                      
REMARK 465     HIS C   289                                                      
REMARK 465     HIS C   290                                                      
REMARK 465     HIS D   285                                                      
REMARK 465     HIS D   286                                                      
REMARK 465     HIS D   287                                                      
REMARK 465     HIS D   288                                                      
REMARK 465     HIS D   289                                                      
REMARK 465     HIS D   290                                                      
REMARK 465     HIS E   285                                                      
REMARK 465     HIS E   286                                                      
REMARK 465     HIS E   287                                                      
REMARK 465     HIS E   288                                                      
REMARK 465     HIS E   289                                                      
REMARK 465     HIS E   290                                                      
REMARK 465     HIS F   285                                                      
REMARK 465     HIS F   286                                                      
REMARK 465     HIS F   287                                                      
REMARK 465     HIS F   288                                                      
REMARK 465     HIS F   289                                                      
REMARK 465     HIS F   290                                                      
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    ASN A  35       63.08     36.18                                   
REMARK 500    ASN A  46       77.70   -102.55                                   
REMARK 500    SER A 108       17.38   -159.00                                   
REMARK 500    SER A 123       36.26    -92.16                                   
REMARK 500    ASN A 125       62.64     24.21                                   
REMARK 500    ASN A 127       10.77     47.60                                   
REMARK 500    LYS A 164      -47.40   -143.03                                   
REMARK 500    ARG A 166     -113.73     16.58                                   
REMARK 500    LEU A 283      -81.47    -77.21                                   
REMARK 500    ASN B  35       62.89     36.67                                   
REMARK 500    ASN B  46       78.79   -103.55                                   
REMARK 500    SER B 108       16.02   -159.52                                   
REMARK 500    SER B 123       37.22    -90.02                                   
REMARK 500    ASN B 125       63.37     25.25                                   
REMARK 500    ASN B 127       10.97     47.73                                   
REMARK 500    LYS B 164      -48.62   -142.79                                   
REMARK 500    ARG B 166     -113.81     16.53                                   
REMARK 500    LEU B 283      -91.08    -75.80                                   
REMARK 500    ASN C  35       64.32     38.00                                   
REMARK 500    ASN C  46       78.94   -101.67                                   
REMARK 500    SER C 108       17.89   -159.82                                   
REMARK 500    SER C 123       35.31    -89.70                                   
REMARK 500    ASN C 125       63.03     22.52                                   
REMARK 500    ASN C 127       10.38     47.83                                   
REMARK 500    LYS C 164      -48.08   -141.66                                   
REMARK 500    ARG C 166     -114.25     15.91                                   
REMARK 500    ASP C 204       -6.90    -59.99                                   
REMARK 500    ARG C 247      135.37    -39.78                                   
REMARK 500    LEU C 283      -96.95    -73.91                                   
REMARK 500    ASN D  35       64.56     37.69                                   
REMARK 500    ASN D  46       78.61   -101.60                                   
REMARK 500    CYS D  78       28.46   -141.39                                   
REMARK 500    SER D 108       17.80   -157.75                                   
REMARK 500    SER D 123       35.93    -89.81                                   
REMARK 500    ASN D 125       62.50     24.41                                   
REMARK 500    ASN D 127       10.82     48.05                                   
REMARK 500    LYS D 164      -48.30   -143.12                                   
REMARK 500    ARG D 166     -114.35     16.15                                   
REMARK 500    LEU D 283      -91.82    -75.52                                   
REMARK 500    ASN E  35       62.52     37.88                                   
REMARK 500    ASN E  46       79.71   -102.35                                   
REMARK 500    SER E 108       16.95   -158.19                                   
REMARK 500    SER E 123       36.12    -90.83                                   
REMARK 500    ASN E 125       63.73     24.25                                   
REMARK 500    ASN E 127       11.06     47.15                                   
REMARK 500    LYS E 164      -47.00   -142.72                                   
REMARK 500    ARG E 166     -112.88     16.41                                   
REMARK 500    LEU E 283      -93.08    -76.77                                   
REMARK 500    ASN F  35       63.51     37.80                                   
REMARK 500    ASN F  46       79.04   -103.50                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      58 RAMACHANDRAN OUTLIERS.                        
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 A 315        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH F 307        DISTANCE =  5.74 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: CAR6   RELATED DB: TARGETDB                              
DBREF  1ZMB A    1   282  UNP    Q97LM8   Q97LM8_CLOAB     1    282             
DBREF  1ZMB B    1   282  UNP    Q97LM8   Q97LM8_CLOAB     1    282             
DBREF  1ZMB C    1   282  UNP    Q97LM8   Q97LM8_CLOAB     1    282             
DBREF  1ZMB D    1   282  UNP    Q97LM8   Q97LM8_CLOAB     1    282             
DBREF  1ZMB E    1   282  UNP    Q97LM8   Q97LM8_CLOAB     1    282             
DBREF  1ZMB F    1   282  UNP    Q97LM8   Q97LM8_CLOAB     1    282             
SEQADV 1ZMB MSE A    1  UNP  Q97LM8    MET     1 MODIFIED RESIDUE               
SEQADV 1ZMB MSE A    7  UNP  Q97LM8    MET     7 MODIFIED RESIDUE               
SEQADV 1ZMB MSE A   13  UNP  Q97LM8    MET    13 MODIFIED RESIDUE               
SEQADV 1ZMB MSE A   24  UNP  Q97LM8    MET    24 MODIFIED RESIDUE               
SEQADV 1ZMB MSE A   32  UNP  Q97LM8    MET    32 MODIFIED RESIDUE               
SEQADV 1ZMB MSE A   40  UNP  Q97LM8    MET    40 MODIFIED RESIDUE               
SEQADV 1ZMB MSE A   41  UNP  Q97LM8    MET    41 MODIFIED RESIDUE               
SEQADV 1ZMB MSE A  106  UNP  Q97LM8    MET   106 MODIFIED RESIDUE               
SEQADV 1ZMB MSE A  260  UNP  Q97LM8    MET   260 MODIFIED RESIDUE               
SEQADV 1ZMB MSE A  277  UNP  Q97LM8    MET   277 MODIFIED RESIDUE               
SEQADV 1ZMB LEU A  283  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB GLU A  284  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS A  285  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS A  286  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS A  287  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS A  288  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS A  289  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS A  290  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB MSE B    1  UNP  Q97LM8    MET     1 MODIFIED RESIDUE               
SEQADV 1ZMB MSE B    7  UNP  Q97LM8    MET     7 MODIFIED RESIDUE               
SEQADV 1ZMB MSE B   13  UNP  Q97LM8    MET    13 MODIFIED RESIDUE               
SEQADV 1ZMB MSE B   24  UNP  Q97LM8    MET    24 MODIFIED RESIDUE               
SEQADV 1ZMB MSE B   32  UNP  Q97LM8    MET    32 MODIFIED RESIDUE               
SEQADV 1ZMB MSE B   40  UNP  Q97LM8    MET    40 MODIFIED RESIDUE               
SEQADV 1ZMB MSE B   41  UNP  Q97LM8    MET    41 MODIFIED RESIDUE               
SEQADV 1ZMB MSE B  106  UNP  Q97LM8    MET   106 MODIFIED RESIDUE               
SEQADV 1ZMB MSE B  260  UNP  Q97LM8    MET   260 MODIFIED RESIDUE               
SEQADV 1ZMB MSE B  277  UNP  Q97LM8    MET   277 MODIFIED RESIDUE               
SEQADV 1ZMB LEU B  283  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB GLU B  284  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS B  285  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS B  286  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS B  287  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS B  288  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS B  289  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS B  290  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB MSE C    1  UNP  Q97LM8    MET     1 MODIFIED RESIDUE               
SEQADV 1ZMB MSE C    7  UNP  Q97LM8    MET     7 MODIFIED RESIDUE               
SEQADV 1ZMB MSE C   13  UNP  Q97LM8    MET    13 MODIFIED RESIDUE               
SEQADV 1ZMB MSE C   24  UNP  Q97LM8    MET    24 MODIFIED RESIDUE               
SEQADV 1ZMB MSE C   32  UNP  Q97LM8    MET    32 MODIFIED RESIDUE               
SEQADV 1ZMB MSE C   40  UNP  Q97LM8    MET    40 MODIFIED RESIDUE               
SEQADV 1ZMB MSE C   41  UNP  Q97LM8    MET    41 MODIFIED RESIDUE               
SEQADV 1ZMB MSE C  106  UNP  Q97LM8    MET   106 MODIFIED RESIDUE               
SEQADV 1ZMB MSE C  260  UNP  Q97LM8    MET   260 MODIFIED RESIDUE               
SEQADV 1ZMB MSE C  277  UNP  Q97LM8    MET   277 MODIFIED RESIDUE               
SEQADV 1ZMB LEU C  283  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB GLU C  284  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS C  285  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS C  286  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS C  287  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS C  288  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS C  289  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS C  290  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB MSE D    1  UNP  Q97LM8    MET     1 MODIFIED RESIDUE               
SEQADV 1ZMB MSE D    7  UNP  Q97LM8    MET     7 MODIFIED RESIDUE               
SEQADV 1ZMB MSE D   13  UNP  Q97LM8    MET    13 MODIFIED RESIDUE               
SEQADV 1ZMB MSE D   24  UNP  Q97LM8    MET    24 MODIFIED RESIDUE               
SEQADV 1ZMB MSE D   32  UNP  Q97LM8    MET    32 MODIFIED RESIDUE               
SEQADV 1ZMB MSE D   40  UNP  Q97LM8    MET    40 MODIFIED RESIDUE               
SEQADV 1ZMB MSE D   41  UNP  Q97LM8    MET    41 MODIFIED RESIDUE               
SEQADV 1ZMB MSE D  106  UNP  Q97LM8    MET   106 MODIFIED RESIDUE               
SEQADV 1ZMB MSE D  260  UNP  Q97LM8    MET   260 MODIFIED RESIDUE               
SEQADV 1ZMB MSE D  277  UNP  Q97LM8    MET   277 MODIFIED RESIDUE               
SEQADV 1ZMB LEU D  283  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB GLU D  284  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS D  285  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS D  286  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS D  287  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS D  288  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS D  289  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS D  290  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB MSE E    1  UNP  Q97LM8    MET     1 MODIFIED RESIDUE               
SEQADV 1ZMB MSE E    7  UNP  Q97LM8    MET     7 MODIFIED RESIDUE               
SEQADV 1ZMB MSE E   13  UNP  Q97LM8    MET    13 MODIFIED RESIDUE               
SEQADV 1ZMB MSE E   24  UNP  Q97LM8    MET    24 MODIFIED RESIDUE               
SEQADV 1ZMB MSE E   32  UNP  Q97LM8    MET    32 MODIFIED RESIDUE               
SEQADV 1ZMB MSE E   40  UNP  Q97LM8    MET    40 MODIFIED RESIDUE               
SEQADV 1ZMB MSE E   41  UNP  Q97LM8    MET    41 MODIFIED RESIDUE               
SEQADV 1ZMB MSE E  106  UNP  Q97LM8    MET   106 MODIFIED RESIDUE               
SEQADV 1ZMB MSE E  260  UNP  Q97LM8    MET   260 MODIFIED RESIDUE               
SEQADV 1ZMB MSE E  277  UNP  Q97LM8    MET   277 MODIFIED RESIDUE               
SEQADV 1ZMB LEU E  283  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB GLU E  284  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS E  285  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS E  286  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS E  287  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS E  288  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS E  289  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS E  290  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB MSE F    1  UNP  Q97LM8    MET     1 MODIFIED RESIDUE               
SEQADV 1ZMB MSE F    7  UNP  Q97LM8    MET     7 MODIFIED RESIDUE               
SEQADV 1ZMB MSE F   13  UNP  Q97LM8    MET    13 MODIFIED RESIDUE               
SEQADV 1ZMB MSE F   24  UNP  Q97LM8    MET    24 MODIFIED RESIDUE               
SEQADV 1ZMB MSE F   32  UNP  Q97LM8    MET    32 MODIFIED RESIDUE               
SEQADV 1ZMB MSE F   40  UNP  Q97LM8    MET    40 MODIFIED RESIDUE               
SEQADV 1ZMB MSE F   41  UNP  Q97LM8    MET    41 MODIFIED RESIDUE               
SEQADV 1ZMB MSE F  106  UNP  Q97LM8    MET   106 MODIFIED RESIDUE               
SEQADV 1ZMB MSE F  260  UNP  Q97LM8    MET   260 MODIFIED RESIDUE               
SEQADV 1ZMB MSE F  277  UNP  Q97LM8    MET   277 MODIFIED RESIDUE               
SEQADV 1ZMB LEU F  283  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB GLU F  284  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS F  285  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS F  286  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS F  287  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS F  288  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS F  289  UNP  Q97LM8              CLONING ARTIFACT               
SEQADV 1ZMB HIS F  290  UNP  Q97LM8              CLONING ARTIFACT               
SEQRES   1 A  290  MSE VAL LYS SER PHE LEU MSE LEU GLY GLN SER ASN MSE          
SEQRES   2 A  290  ALA GLY ARG GLY PHE ILE ASN GLU VAL PRO MSE ILE TYR          
SEQRES   3 A  290  ASN GLU ARG ILE GLN MSE LEU ARG ASN GLY ARG TRP GLN          
SEQRES   4 A  290  MSE MSE THR GLU PRO ILE ASN TYR ASP ARG PRO VAL SER          
SEQRES   5 A  290  GLY ILE SER LEU ALA GLY SER PHE ALA ASP ALA TRP SER          
SEQRES   6 A  290  GLN LYS ASN GLN GLU ASP ILE ILE GLY LEU ILE PRO CYS          
SEQRES   7 A  290  ALA GLU GLY GLY SER SER ILE ASP GLU TRP ALA LEU ASP          
SEQRES   8 A  290  GLY VAL LEU PHE ARG HIS ALA LEU THR GLU ALA LYS PHE          
SEQRES   9 A  290  ALA MSE GLU SER SER GLU LEU THR GLY ILE LEU TRP HIS          
SEQRES  10 A  290  GLN GLY GLU SER ASP SER LEU ASN GLY ASN TYR LYS VAL          
SEQRES  11 A  290  TYR TYR LYS LYS LEU LEU LEU ILE ILE GLU ALA LEU ARG          
SEQRES  12 A  290  LYS GLU LEU ASN VAL PRO ASP ILE PRO ILE ILE ILE GLY          
SEQRES  13 A  290  GLY LEU GLY ASP PHE LEU GLY LYS GLU ARG PHE GLY LYS          
SEQRES  14 A  290  GLY CYS THR GLU TYR ASN PHE ILE ASN LYS GLU LEU GLN          
SEQRES  15 A  290  LYS PHE ALA PHE GLU GLN ASP ASN CYS TYR PHE VAL THR          
SEQRES  16 A  290  ALA SER GLY LEU THR CYS ASN PRO ASP GLY ILE HIS ILE          
SEQRES  17 A  290  ASP ALA ILE SER GLN ARG LYS PHE GLY LEU ARG TYR PHE          
SEQRES  18 A  290  GLU ALA PHE PHE ASN ARG LYS HIS VAL LEU GLU PRO LEU          
SEQRES  19 A  290  ILE ASN GLU ASN GLU LEU LEU ASN LEU ASN TYR ALA ARG          
SEQRES  20 A  290  THR HIS THR LYS ALA GLU LYS ILE TYR ILE LYS SER MSE          
SEQRES  21 A  290  ASP PHE ALA LEU GLY LYS ILE SER TYR ASP GLU PHE THR          
SEQRES  22 A  290  SER GLU LEU MSE LYS ILE ASN ASN ASP LEU GLU HIS HIS          
SEQRES  23 A  290  HIS HIS HIS HIS                                              
SEQRES   1 B  290  MSE VAL LYS SER PHE LEU MSE LEU GLY GLN SER ASN MSE          
SEQRES   2 B  290  ALA GLY ARG GLY PHE ILE ASN GLU VAL PRO MSE ILE TYR          
SEQRES   3 B  290  ASN GLU ARG ILE GLN MSE LEU ARG ASN GLY ARG TRP GLN          
SEQRES   4 B  290  MSE MSE THR GLU PRO ILE ASN TYR ASP ARG PRO VAL SER          
SEQRES   5 B  290  GLY ILE SER LEU ALA GLY SER PHE ALA ASP ALA TRP SER          
SEQRES   6 B  290  GLN LYS ASN GLN GLU ASP ILE ILE GLY LEU ILE PRO CYS          
SEQRES   7 B  290  ALA GLU GLY GLY SER SER ILE ASP GLU TRP ALA LEU ASP          
SEQRES   8 B  290  GLY VAL LEU PHE ARG HIS ALA LEU THR GLU ALA LYS PHE          
SEQRES   9 B  290  ALA MSE GLU SER SER GLU LEU THR GLY ILE LEU TRP HIS          
SEQRES  10 B  290  GLN GLY GLU SER ASP SER LEU ASN GLY ASN TYR LYS VAL          
SEQRES  11 B  290  TYR TYR LYS LYS LEU LEU LEU ILE ILE GLU ALA LEU ARG          
SEQRES  12 B  290  LYS GLU LEU ASN VAL PRO ASP ILE PRO ILE ILE ILE GLY          
SEQRES  13 B  290  GLY LEU GLY ASP PHE LEU GLY LYS GLU ARG PHE GLY LYS          
SEQRES  14 B  290  GLY CYS THR GLU TYR ASN PHE ILE ASN LYS GLU LEU GLN          
SEQRES  15 B  290  LYS PHE ALA PHE GLU GLN ASP ASN CYS TYR PHE VAL THR          
SEQRES  16 B  290  ALA SER GLY LEU THR CYS ASN PRO ASP GLY ILE HIS ILE          
SEQRES  17 B  290  ASP ALA ILE SER GLN ARG LYS PHE GLY LEU ARG TYR PHE          
SEQRES  18 B  290  GLU ALA PHE PHE ASN ARG LYS HIS VAL LEU GLU PRO LEU          
SEQRES  19 B  290  ILE ASN GLU ASN GLU LEU LEU ASN LEU ASN TYR ALA ARG          
SEQRES  20 B  290  THR HIS THR LYS ALA GLU LYS ILE TYR ILE LYS SER MSE          
SEQRES  21 B  290  ASP PHE ALA LEU GLY LYS ILE SER TYR ASP GLU PHE THR          
SEQRES  22 B  290  SER GLU LEU MSE LYS ILE ASN ASN ASP LEU GLU HIS HIS          
SEQRES  23 B  290  HIS HIS HIS HIS                                              
SEQRES   1 C  290  MSE VAL LYS SER PHE LEU MSE LEU GLY GLN SER ASN MSE          
SEQRES   2 C  290  ALA GLY ARG GLY PHE ILE ASN GLU VAL PRO MSE ILE TYR          
SEQRES   3 C  290  ASN GLU ARG ILE GLN MSE LEU ARG ASN GLY ARG TRP GLN          
SEQRES   4 C  290  MSE MSE THR GLU PRO ILE ASN TYR ASP ARG PRO VAL SER          
SEQRES   5 C  290  GLY ILE SER LEU ALA GLY SER PHE ALA ASP ALA TRP SER          
SEQRES   6 C  290  GLN LYS ASN GLN GLU ASP ILE ILE GLY LEU ILE PRO CYS          
SEQRES   7 C  290  ALA GLU GLY GLY SER SER ILE ASP GLU TRP ALA LEU ASP          
SEQRES   8 C  290  GLY VAL LEU PHE ARG HIS ALA LEU THR GLU ALA LYS PHE          
SEQRES   9 C  290  ALA MSE GLU SER SER GLU LEU THR GLY ILE LEU TRP HIS          
SEQRES  10 C  290  GLN GLY GLU SER ASP SER LEU ASN GLY ASN TYR LYS VAL          
SEQRES  11 C  290  TYR TYR LYS LYS LEU LEU LEU ILE ILE GLU ALA LEU ARG          
SEQRES  12 C  290  LYS GLU LEU ASN VAL PRO ASP ILE PRO ILE ILE ILE GLY          
SEQRES  13 C  290  GLY LEU GLY ASP PHE LEU GLY LYS GLU ARG PHE GLY LYS          
SEQRES  14 C  290  GLY CYS THR GLU TYR ASN PHE ILE ASN LYS GLU LEU GLN          
SEQRES  15 C  290  LYS PHE ALA PHE GLU GLN ASP ASN CYS TYR PHE VAL THR          
SEQRES  16 C  290  ALA SER GLY LEU THR CYS ASN PRO ASP GLY ILE HIS ILE          
SEQRES  17 C  290  ASP ALA ILE SER GLN ARG LYS PHE GLY LEU ARG TYR PHE          
SEQRES  18 C  290  GLU ALA PHE PHE ASN ARG LYS HIS VAL LEU GLU PRO LEU          
SEQRES  19 C  290  ILE ASN GLU ASN GLU LEU LEU ASN LEU ASN TYR ALA ARG          
SEQRES  20 C  290  THR HIS THR LYS ALA GLU LYS ILE TYR ILE LYS SER MSE          
SEQRES  21 C  290  ASP PHE ALA LEU GLY LYS ILE SER TYR ASP GLU PHE THR          
SEQRES  22 C  290  SER GLU LEU MSE LYS ILE ASN ASN ASP LEU GLU HIS HIS          
SEQRES  23 C  290  HIS HIS HIS HIS                                              
SEQRES   1 D  290  MSE VAL LYS SER PHE LEU MSE LEU GLY GLN SER ASN MSE          
SEQRES   2 D  290  ALA GLY ARG GLY PHE ILE ASN GLU VAL PRO MSE ILE TYR          
SEQRES   3 D  290  ASN GLU ARG ILE GLN MSE LEU ARG ASN GLY ARG TRP GLN          
SEQRES   4 D  290  MSE MSE THR GLU PRO ILE ASN TYR ASP ARG PRO VAL SER          
SEQRES   5 D  290  GLY ILE SER LEU ALA GLY SER PHE ALA ASP ALA TRP SER          
SEQRES   6 D  290  GLN LYS ASN GLN GLU ASP ILE ILE GLY LEU ILE PRO CYS          
SEQRES   7 D  290  ALA GLU GLY GLY SER SER ILE ASP GLU TRP ALA LEU ASP          
SEQRES   8 D  290  GLY VAL LEU PHE ARG HIS ALA LEU THR GLU ALA LYS PHE          
SEQRES   9 D  290  ALA MSE GLU SER SER GLU LEU THR GLY ILE LEU TRP HIS          
SEQRES  10 D  290  GLN GLY GLU SER ASP SER LEU ASN GLY ASN TYR LYS VAL          
SEQRES  11 D  290  TYR TYR LYS LYS LEU LEU LEU ILE ILE GLU ALA LEU ARG          
SEQRES  12 D  290  LYS GLU LEU ASN VAL PRO ASP ILE PRO ILE ILE ILE GLY          
SEQRES  13 D  290  GLY LEU GLY ASP PHE LEU GLY LYS GLU ARG PHE GLY LYS          
SEQRES  14 D  290  GLY CYS THR GLU TYR ASN PHE ILE ASN LYS GLU LEU GLN          
SEQRES  15 D  290  LYS PHE ALA PHE GLU GLN ASP ASN CYS TYR PHE VAL THR          
SEQRES  16 D  290  ALA SER GLY LEU THR CYS ASN PRO ASP GLY ILE HIS ILE          
SEQRES  17 D  290  ASP ALA ILE SER GLN ARG LYS PHE GLY LEU ARG TYR PHE          
SEQRES  18 D  290  GLU ALA PHE PHE ASN ARG LYS HIS VAL LEU GLU PRO LEU          
SEQRES  19 D  290  ILE ASN GLU ASN GLU LEU LEU ASN LEU ASN TYR ALA ARG          
SEQRES  20 D  290  THR HIS THR LYS ALA GLU LYS ILE TYR ILE LYS SER MSE          
SEQRES  21 D  290  ASP PHE ALA LEU GLY LYS ILE SER TYR ASP GLU PHE THR          
SEQRES  22 D  290  SER GLU LEU MSE LYS ILE ASN ASN ASP LEU GLU HIS HIS          
SEQRES  23 D  290  HIS HIS HIS HIS                                              
SEQRES   1 E  290  MSE VAL LYS SER PHE LEU MSE LEU GLY GLN SER ASN MSE          
SEQRES   2 E  290  ALA GLY ARG GLY PHE ILE ASN GLU VAL PRO MSE ILE TYR          
SEQRES   3 E  290  ASN GLU ARG ILE GLN MSE LEU ARG ASN GLY ARG TRP GLN          
SEQRES   4 E  290  MSE MSE THR GLU PRO ILE ASN TYR ASP ARG PRO VAL SER          
SEQRES   5 E  290  GLY ILE SER LEU ALA GLY SER PHE ALA ASP ALA TRP SER          
SEQRES   6 E  290  GLN LYS ASN GLN GLU ASP ILE ILE GLY LEU ILE PRO CYS          
SEQRES   7 E  290  ALA GLU GLY GLY SER SER ILE ASP GLU TRP ALA LEU ASP          
SEQRES   8 E  290  GLY VAL LEU PHE ARG HIS ALA LEU THR GLU ALA LYS PHE          
SEQRES   9 E  290  ALA MSE GLU SER SER GLU LEU THR GLY ILE LEU TRP HIS          
SEQRES  10 E  290  GLN GLY GLU SER ASP SER LEU ASN GLY ASN TYR LYS VAL          
SEQRES  11 E  290  TYR TYR LYS LYS LEU LEU LEU ILE ILE GLU ALA LEU ARG          
SEQRES  12 E  290  LYS GLU LEU ASN VAL PRO ASP ILE PRO ILE ILE ILE GLY          
SEQRES  13 E  290  GLY LEU GLY ASP PHE LEU GLY LYS GLU ARG PHE GLY LYS          
SEQRES  14 E  290  GLY CYS THR GLU TYR ASN PHE ILE ASN LYS GLU LEU GLN          
SEQRES  15 E  290  LYS PHE ALA PHE GLU GLN ASP ASN CYS TYR PHE VAL THR          
SEQRES  16 E  290  ALA SER GLY LEU THR CYS ASN PRO ASP GLY ILE HIS ILE          
SEQRES  17 E  290  ASP ALA ILE SER GLN ARG LYS PHE GLY LEU ARG TYR PHE          
SEQRES  18 E  290  GLU ALA PHE PHE ASN ARG LYS HIS VAL LEU GLU PRO LEU          
SEQRES  19 E  290  ILE ASN GLU ASN GLU LEU LEU ASN LEU ASN TYR ALA ARG          
SEQRES  20 E  290  THR HIS THR LYS ALA GLU LYS ILE TYR ILE LYS SER MSE          
SEQRES  21 E  290  ASP PHE ALA LEU GLY LYS ILE SER TYR ASP GLU PHE THR          
SEQRES  22 E  290  SER GLU LEU MSE LYS ILE ASN ASN ASP LEU GLU HIS HIS          
SEQRES  23 E  290  HIS HIS HIS HIS                                              
SEQRES   1 F  290  MSE VAL LYS SER PHE LEU MSE LEU GLY GLN SER ASN MSE          
SEQRES   2 F  290  ALA GLY ARG GLY PHE ILE ASN GLU VAL PRO MSE ILE TYR          
SEQRES   3 F  290  ASN GLU ARG ILE GLN MSE LEU ARG ASN GLY ARG TRP GLN          
SEQRES   4 F  290  MSE MSE THR GLU PRO ILE ASN TYR ASP ARG PRO VAL SER          
SEQRES   5 F  290  GLY ILE SER LEU ALA GLY SER PHE ALA ASP ALA TRP SER          
SEQRES   6 F  290  GLN LYS ASN GLN GLU ASP ILE ILE GLY LEU ILE PRO CYS          
SEQRES   7 F  290  ALA GLU GLY GLY SER SER ILE ASP GLU TRP ALA LEU ASP          
SEQRES   8 F  290  GLY VAL LEU PHE ARG HIS ALA LEU THR GLU ALA LYS PHE          
SEQRES   9 F  290  ALA MSE GLU SER SER GLU LEU THR GLY ILE LEU TRP HIS          
SEQRES  10 F  290  GLN GLY GLU SER ASP SER LEU ASN GLY ASN TYR LYS VAL          
SEQRES  11 F  290  TYR TYR LYS LYS LEU LEU LEU ILE ILE GLU ALA LEU ARG          
SEQRES  12 F  290  LYS GLU LEU ASN VAL PRO ASP ILE PRO ILE ILE ILE GLY          
SEQRES  13 F  290  GLY LEU GLY ASP PHE LEU GLY LYS GLU ARG PHE GLY LYS          
SEQRES  14 F  290  GLY CYS THR GLU TYR ASN PHE ILE ASN LYS GLU LEU GLN          
SEQRES  15 F  290  LYS PHE ALA PHE GLU GLN ASP ASN CYS TYR PHE VAL THR          
SEQRES  16 F  290  ALA SER GLY LEU THR CYS ASN PRO ASP GLY ILE HIS ILE          
SEQRES  17 F  290  ASP ALA ILE SER GLN ARG LYS PHE GLY LEU ARG TYR PHE          
SEQRES  18 F  290  GLU ALA PHE PHE ASN ARG LYS HIS VAL LEU GLU PRO LEU          
SEQRES  19 F  290  ILE ASN GLU ASN GLU LEU LEU ASN LEU ASN TYR ALA ARG          
SEQRES  20 F  290  THR HIS THR LYS ALA GLU LYS ILE TYR ILE LYS SER MSE          
SEQRES  21 F  290  ASP PHE ALA LEU GLY LYS ILE SER TYR ASP GLU PHE THR          
SEQRES  22 F  290  SER GLU LEU MSE LYS ILE ASN ASN ASP LEU GLU HIS HIS          
SEQRES  23 F  290  HIS HIS HIS HIS                                              
MODRES 1ZMB MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE A    7  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE A   13  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE A   24  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE A   32  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE A   40  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE A   41  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE A  106  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE A  260  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE A  277  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE B    7  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE B   13  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE B   24  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE B   32  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE B   40  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE B   41  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE B  106  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE B  260  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE B  277  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE C    1  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE C    7  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE C   13  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE C   24  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE C   32  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE C   40  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE C   41  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE C  106  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE C  260  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE C  277  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE D    1  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE D    7  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE D   13  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE D   24  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE D   32  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE D   40  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE D   41  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE D  106  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE D  260  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE D  277  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE E    1  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE E    7  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE E   13  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE E   24  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE E   32  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE E   40  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE E   41  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE E  106  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE E  260  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE E  277  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE F    1  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE F    7  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE F   13  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE F   24  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE F   32  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE F   40  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE F   41  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE F  106  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE F  260  MET  SELENOMETHIONINE                                   
MODRES 1ZMB MSE F  277  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A   7       8                                                       
HET    MSE  A  13       8                                                       
HET    MSE  A  24       8                                                       
HET    MSE  A  32       8                                                       
HET    MSE  A  40       8                                                       
HET    MSE  A  41       8                                                       
HET    MSE  A 106       8                                                       
HET    MSE  A 260       8                                                       
HET    MSE  A 277       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B   7       8                                                       
HET    MSE  B  13       8                                                       
HET    MSE  B  24       8                                                       
HET    MSE  B  32       8                                                       
HET    MSE  B  40       8                                                       
HET    MSE  B  41       8                                                       
HET    MSE  B 106       8                                                       
HET    MSE  B 260       8                                                       
HET    MSE  B 277       8                                                       
HET    MSE  C   1       8                                                       
HET    MSE  C   7       8                                                       
HET    MSE  C  13       8                                                       
HET    MSE  C  24       8                                                       
HET    MSE  C  32       8                                                       
HET    MSE  C  40       8                                                       
HET    MSE  C  41       8                                                       
HET    MSE  C 106       8                                                       
HET    MSE  C 260       8                                                       
HET    MSE  C 277       8                                                       
HET    MSE  D   1       8                                                       
HET    MSE  D   7       8                                                       
HET    MSE  D  13       8                                                       
HET    MSE  D  24       8                                                       
HET    MSE  D  32       8                                                       
HET    MSE  D  40       8                                                       
HET    MSE  D  41       8                                                       
HET    MSE  D 106       8                                                       
HET    MSE  D 260       8                                                       
HET    MSE  D 277       8                                                       
HET    MSE  E   1       8                                                       
HET    MSE  E   7       8                                                       
HET    MSE  E  13       8                                                       
HET    MSE  E  24       8                                                       
HET    MSE  E  32       8                                                       
HET    MSE  E  40       8                                                       
HET    MSE  E  41       8                                                       
HET    MSE  E 106       8                                                       
HET    MSE  E 260       8                                                       
HET    MSE  E 277       8                                                       
HET    MSE  F   1       8                                                       
HET    MSE  F   7       8                                                       
HET    MSE  F  13       8                                                       
HET    MSE  F  24       8                                                       
HET    MSE  F  32       8                                                       
HET    MSE  F  40       8                                                       
HET    MSE  F  41       8                                                       
HET    MSE  F 106       8                                                       
HET    MSE  F 260       8                                                       
HET    MSE  F 277       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    60(C5 H11 N O2 SE)                                           
FORMUL   7  HOH   *123(H2 O)                                                    
HELIX    1   1 GLN A   10  GLY A   15  1                                   6    
HELIX    2   2 LEU A   56  LYS A   67  1                                  12    
HELIX    3   3 SER A   84  ALA A   89  5                                   6    
HELIX    4   4 GLY A   92  GLU A  107  1                                  16    
HELIX    5   5 GLY A  119  SER A  123  5                                   5    
HELIX    6   6 VAL A  130  LEU A  146  1                                  17    
HELIX    7   7 GLU A  165  LYS A  169  5                                   5    
HELIX    8   8 GLU A  173  GLN A  188  1                                  16    
HELIX    9   9 ASP A  209  ARG A  227  1                                  19    
HELIX   10  10 ASN A  236  ARG A  247  1                                  12    
HELIX   11  11 THR A  250  LEU A  264  1                                  15    
HELIX   12  12 SER A  268  ASP A  282  1                                  15    
HELIX   13  13 GLN B   10  GLY B   15  1                                   6    
HELIX   14  14 LEU B   56  LYS B   67  1                                  12    
HELIX   15  15 SER B   84  ALA B   89  5                                   6    
HELIX   16  16 GLY B   92  GLU B  107  1                                  16    
HELIX   17  17 GLY B  119  SER B  123  5                                   5    
HELIX   18  18 VAL B  130  LEU B  146  1                                  17    
HELIX   19  19 GLU B  165  LYS B  169  5                                   5    
HELIX   20  20 GLU B  173  GLN B  188  1                                  16    
HELIX   21  21 ASP B  209  ARG B  227  1                                  19    
HELIX   22  22 ASN B  236  ARG B  247  1                                  12    
HELIX   23  23 THR B  250  LEU B  264  1                                  15    
HELIX   24  24 SER B  268  ASP B  282  1                                  15    
HELIX   25  25 GLN C   10  GLY C   15  1                                   6    
HELIX   26  26 PHE C   18  VAL C   22  5                                   5    
HELIX   27  27 LEU C   56  LYS C   67  1                                  12    
HELIX   28  28 SER C   84  ALA C   89  5                                   6    
HELIX   29  29 GLY C   92  GLU C  107  1                                  16    
HELIX   30  30 GLY C  119  SER C  123  5                                   5    
HELIX   31  31 VAL C  130  LEU C  146  1                                  17    
HELIX   32  32 GLU C  165  LYS C  169  5                                   5    
HELIX   33  33 GLU C  173  GLN C  188  1                                  16    
HELIX   34  34 ASP C  209  ARG C  227  1                                  19    
HELIX   35  35 ASN C  236  ARG C  247  1                                  12    
HELIX   36  36 THR C  250  LEU C  264  1                                  15    
HELIX   37  37 SER C  268  ASP C  282  1                                  15    
HELIX   38  38 GLN D   10  GLY D   15  1                                   6    
HELIX   39  39 LEU D   56  LYS D   67  1                                  12    
HELIX   40  40 SER D   84  ALA D   89  5                                   6    
HELIX   41  41 GLY D   92  GLU D  107  1                                  16    
HELIX   42  42 GLY D  119  SER D  123  5                                   5    
HELIX   43  43 VAL D  130  LEU D  146  1                                  17    
HELIX   44  44 GLU D  165  LYS D  169  5                                   5    
HELIX   45  45 GLU D  173  GLN D  188  1                                  16    
HELIX   46  46 ASP D  209  ARG D  227  1                                  19    
HELIX   47  47 ASN D  236  ARG D  247  1                                  12    
HELIX   48  48 THR D  250  LEU D  264  1                                  15    
HELIX   49  49 SER D  268  ASP D  282  1                                  15    
HELIX   50  50 GLN E   10  GLY E   15  1                                   6    
HELIX   51  51 LEU E   56  LYS E   67  1                                  12    
HELIX   52  52 SER E   84  ALA E   89  5                                   6    
HELIX   53  53 GLY E   92  GLU E  107  1                                  16    
HELIX   54  54 GLY E  119  SER E  123  5                                   5    
HELIX   55  55 VAL E  130  LEU E  146  1                                  17    
HELIX   56  56 GLU E  165  LYS E  169  5                                   5    
HELIX   57  57 GLU E  173  GLN E  188  1                                  16    
HELIX   58  58 ASP E  209  ARG E  227  1                                  19    
HELIX   59  59 ASN E  236  ARG E  247  1                                  12    
HELIX   60  60 THR E  250  LEU E  264  1                                  15    
HELIX   61  61 SER E  268  ASP E  282  1                                  15    
HELIX   62  62 GLN F   10  GLY F   15  1                                   6    
HELIX   63  63 PHE F   18  VAL F   22  5                                   5    
HELIX   64  64 LEU F   56  LYS F   67  1                                  12    
HELIX   65  65 SER F   84  ALA F   89  5                                   6    
HELIX   66  66 GLY F   92  GLU F  107  1                                  16    
HELIX   67  67 GLY F  119  SER F  123  5                                   5    
HELIX   68  68 VAL F  130  LEU F  146  1                                  17    
HELIX   69  69 GLU F  165  LYS F  169  5                                   5    
HELIX   70  70 GLU F  173  GLN F  188  1                                  16    
HELIX   71  71 ASP F  209  ARG F  227  1                                  19    
HELIX   72  72 ASN F  236  ARG F  247  1                                  12    
HELIX   73  73 THR F  250  LEU F  264  1                                  15    
HELIX   74  74 SER F  268  ASP F  282  1                                  15    
SHEET    1   A 7 ARG A  37  MSE A  40  0                                        
SHEET    2   A 7 ILE A  30  ARG A  34 -1  N  MSE A  32   O  GLN A  39           
SHEET    3   A 7 ILE A  72  PRO A  77  1  O  ILE A  73   N  GLN A  31           
SHEET    4   A 7 VAL A   2  GLY A   9  1  N  MSE A   7   O  ILE A  76           
SHEET    5   A 7 GLU A 110  HIS A 117  1  O  LEU A 115   N  LEU A   8           
SHEET    6   A 7 ILE A 153  GLY A 156  1  O  ILE A 154   N  TRP A 116           
SHEET    7   A 7 CYS A 191  VAL A 194  1  O  TYR A 192   N  ILE A 155           
SHEET    1   B 7 ARG B  37  MSE B  40  0                                        
SHEET    2   B 7 ILE B  30  ARG B  34 -1  N  ARG B  34   O  ARG B  37           
SHEET    3   B 7 ILE B  72  PRO B  77  1  O  LEU B  75   N  GLN B  31           
SHEET    4   B 7 VAL B   2  GLY B   9  1  N  LYS B   3   O  GLY B  74           
SHEET    5   B 7 GLU B 110  HIS B 117  1  O  LEU B 115   N  LEU B   8           
SHEET    6   B 7 ILE B 153  GLY B 156  1  O  ILE B 154   N  TRP B 116           
SHEET    7   B 7 CYS B 191  VAL B 194  1  O  TYR B 192   N  ILE B 155           
SHEET    1   C 7 ARG C  37  MSE C  40  0                                        
SHEET    2   C 7 ILE C  30  ARG C  34 -1  N  ARG C  34   O  ARG C  37           
SHEET    3   C 7 ILE C  72  PRO C  77  1  O  LEU C  75   N  GLN C  31           
SHEET    4   C 7 VAL C   2  GLY C   9  1  N  LYS C   3   O  GLY C  74           
SHEET    5   C 7 GLU C 110  HIS C 117  1  O  LEU C 115   N  LEU C   8           
SHEET    6   C 7 ILE C 153  GLY C 156  1  O  ILE C 154   N  TRP C 116           
SHEET    7   C 7 CYS C 191  VAL C 194  1  O  TYR C 192   N  ILE C 155           
SHEET    1   D 7 ARG D  37  MSE D  40  0                                        
SHEET    2   D 7 ILE D  30  ARG D  34 -1  N  ARG D  34   O  ARG D  37           
SHEET    3   D 7 ILE D  72  PRO D  77  1  O  LEU D  75   N  GLN D  31           
SHEET    4   D 7 VAL D   2  GLY D   9  1  N  MSE D   7   O  ILE D  76           
SHEET    5   D 7 GLU D 110  HIS D 117  1  O  LEU D 115   N  LEU D   8           
SHEET    6   D 7 ILE D 153  GLY D 156  1  O  ILE D 154   N  TRP D 116           
SHEET    7   D 7 CYS D 191  VAL D 194  1  O  TYR D 192   N  ILE D 155           
SHEET    1   E 7 ARG E  37  MSE E  40  0                                        
SHEET    2   E 7 ILE E  30  ARG E  34 -1  N  ARG E  34   O  ARG E  37           
SHEET    3   E 7 ILE E  72  PRO E  77  1  O  LEU E  75   N  GLN E  31           
SHEET    4   E 7 VAL E   2  GLY E   9  1  N  MSE E   7   O  ILE E  76           
SHEET    5   E 7 GLU E 110  HIS E 117  1  O  LEU E 115   N  LEU E   8           
SHEET    6   E 7 ILE E 153  GLY E 156  1  O  ILE E 154   N  TRP E 116           
SHEET    7   E 7 CYS E 191  VAL E 194  1  O  TYR E 192   N  ILE E 155           
SHEET    1   F 7 ARG F  37  MSE F  40  0                                        
SHEET    2   F 7 ILE F  30  ARG F  34 -1  N  ARG F  34   O  ARG F  37           
SHEET    3   F 7 ILE F  72  PRO F  77  1  O  LEU F  75   N  GLN F  31           
SHEET    4   F 7 VAL F   2  GLY F   9  1  N  LYS F   3   O  GLY F  74           
SHEET    5   F 7 GLU F 110  HIS F 117  1  O  LEU F 115   N  LEU F   8           
SHEET    6   F 7 ILE F 153  GLY F 156  1  O  ILE F 154   N  TRP F 116           
SHEET    7   F 7 CYS F 191  VAL F 194  1  O  TYR F 192   N  ILE F 155           
LINK         C   MSE A   1                 N   VAL A   2     1555   1555  1.33  
LINK         C   LEU A   6                 N   MSE A   7     1555   1555  1.33  
LINK         C   MSE A   7                 N   LEU A   8     1555   1555  1.33  
LINK         C   ASN A  12                 N   MSE A  13     1555   1555  1.33  
LINK         C   MSE A  13                 N   ALA A  14     1555   1555  1.33  
LINK         C   PRO A  23                 N   MSE A  24     1555   1555  1.33  
LINK         C   MSE A  24                 N   ILE A  25     1555   1555  1.33  
LINK         C   GLN A  31                 N   MSE A  32     1555   1555  1.33  
LINK         C   MSE A  32                 N   LEU A  33     1555   1555  1.33  
LINK         C   GLN A  39                 N   MSE A  40     1555   1555  1.33  
LINK         C   MSE A  40                 N   MSE A  41     1555   1555  1.33  
LINK         C   MSE A  41                 N   THR A  42     1555   1555  1.33  
LINK         C   ALA A 105                 N   MSE A 106     1555   1555  1.33  
LINK         C   MSE A 106                 N   GLU A 107     1555   1555  1.32  
LINK         C   SER A 259                 N   MSE A 260     1555   1555  1.32  
LINK         C   MSE A 260                 N   ASP A 261     1555   1555  1.33  
LINK         C   LEU A 276                 N   MSE A 277     1555   1555  1.33  
LINK         C   MSE A 277                 N   LYS A 278     1555   1555  1.34  
LINK         C   MSE B   1                 N   VAL B   2     1555   1555  1.33  
LINK         C   LEU B   6                 N   MSE B   7     1555   1555  1.33  
LINK         C   MSE B   7                 N   LEU B   8     1555   1555  1.33  
LINK         C   ASN B  12                 N   MSE B  13     1555   1555  1.33  
LINK         C   MSE B  13                 N   ALA B  14     1555   1555  1.34  
LINK         C   PRO B  23                 N   MSE B  24     1555   1555  1.33  
LINK         C   MSE B  24                 N   ILE B  25     1555   1555  1.33  
LINK         C   GLN B  31                 N   MSE B  32     1555   1555  1.33  
LINK         C   MSE B  32                 N   LEU B  33     1555   1555  1.32  
LINK         C   GLN B  39                 N   MSE B  40     1555   1555  1.32  
LINK         C   MSE B  40                 N   MSE B  41     1555   1555  1.33  
LINK         C   MSE B  41                 N   THR B  42     1555   1555  1.33  
LINK         C   ALA B 105                 N   MSE B 106     1555   1555  1.33  
LINK         C   MSE B 106                 N   GLU B 107     1555   1555  1.32  
LINK         C   SER B 259                 N   MSE B 260     1555   1555  1.32  
LINK         C   MSE B 260                 N   ASP B 261     1555   1555  1.33  
LINK         C   LEU B 276                 N   MSE B 277     1555   1555  1.33  
LINK         C   MSE B 277                 N   LYS B 278     1555   1555  1.33  
LINK         C   MSE C   1                 N   VAL C   2     1555   1555  1.33  
LINK         C   LEU C   6                 N   MSE C   7     1555   1555  1.33  
LINK         C   MSE C   7                 N   LEU C   8     1555   1555  1.33  
LINK         C   ASN C  12                 N   MSE C  13     1555   1555  1.33  
LINK         C   MSE C  13                 N   ALA C  14     1555   1555  1.33  
LINK         C   PRO C  23                 N   MSE C  24     1555   1555  1.33  
LINK         C   MSE C  24                 N   ILE C  25     1555   1555  1.33  
LINK         C   GLN C  31                 N   MSE C  32     1555   1555  1.33  
LINK         C   MSE C  32                 N   LEU C  33     1555   1555  1.33  
LINK         C   GLN C  39                 N   MSE C  40     1555   1555  1.32  
LINK         C   MSE C  40                 N   MSE C  41     1555   1555  1.33  
LINK         C   MSE C  41                 N   THR C  42     1555   1555  1.33  
LINK         C   ALA C 105                 N   MSE C 106     1555   1555  1.33  
LINK         C   MSE C 106                 N   GLU C 107     1555   1555  1.32  
LINK         C   SER C 259                 N   MSE C 260     1555   1555  1.32  
LINK         C   MSE C 260                 N   ASP C 261     1555   1555  1.33  
LINK         C   LEU C 276                 N   MSE C 277     1555   1555  1.33  
LINK         C   MSE C 277                 N   LYS C 278     1555   1555  1.33  
LINK         C   MSE D   1                 N   VAL D   2     1555   1555  1.33  
LINK         C   LEU D   6                 N   MSE D   7     1555   1555  1.34  
LINK         C   MSE D   7                 N   LEU D   8     1555   1555  1.33  
LINK         C   ASN D  12                 N   MSE D  13     1555   1555  1.33  
LINK         C   MSE D  13                 N   ALA D  14     1555   1555  1.33  
LINK         C   PRO D  23                 N   MSE D  24     1555   1555  1.33  
LINK         C   MSE D  24                 N   ILE D  25     1555   1555  1.33  
LINK         C   GLN D  31                 N   MSE D  32     1555   1555  1.33  
LINK         C   MSE D  32                 N   LEU D  33     1555   1555  1.32  
LINK         C   GLN D  39                 N   MSE D  40     1555   1555  1.33  
LINK         C   MSE D  40                 N   MSE D  41     1555   1555  1.33  
LINK         C   MSE D  41                 N   THR D  42     1555   1555  1.33  
LINK         C   ALA D 105                 N   MSE D 106     1555   1555  1.33  
LINK         C   MSE D 106                 N   GLU D 107     1555   1555  1.32  
LINK         C   SER D 259                 N   MSE D 260     1555   1555  1.32  
LINK         C   MSE D 260                 N   ASP D 261     1555   1555  1.33  
LINK         C   LEU D 276                 N   MSE D 277     1555   1555  1.33  
LINK         C   MSE D 277                 N   LYS D 278     1555   1555  1.33  
LINK         C   MSE E   1                 N   VAL E   2     1555   1555  1.33  
LINK         C   LEU E   6                 N   MSE E   7     1555   1555  1.34  
LINK         C   MSE E   7                 N   LEU E   8     1555   1555  1.33  
LINK         C   ASN E  12                 N   MSE E  13     1555   1555  1.33  
LINK         C   MSE E  13                 N   ALA E  14     1555   1555  1.33  
LINK         C   PRO E  23                 N   MSE E  24     1555   1555  1.33  
LINK         C   MSE E  24                 N   ILE E  25     1555   1555  1.33  
LINK         C   GLN E  31                 N   MSE E  32     1555   1555  1.33  
LINK         C   MSE E  32                 N   LEU E  33     1555   1555  1.33  
LINK         C   GLN E  39                 N   MSE E  40     1555   1555  1.33  
LINK         C   MSE E  40                 N   MSE E  41     1555   1555  1.33  
LINK         C   MSE E  41                 N   THR E  42     1555   1555  1.33  
LINK         C   ALA E 105                 N   MSE E 106     1555   1555  1.33  
LINK         C   MSE E 106                 N   GLU E 107     1555   1555  1.32  
LINK         C   SER E 259                 N   MSE E 260     1555   1555  1.32  
LINK         C   MSE E 260                 N   ASP E 261     1555   1555  1.33  
LINK         C   LEU E 276                 N   MSE E 277     1555   1555  1.33  
LINK         C   MSE E 277                 N   LYS E 278     1555   1555  1.34  
LINK         C   MSE F   1                 N   VAL F   2     1555   1555  1.33  
LINK         C   LEU F   6                 N   MSE F   7     1555   1555  1.33  
LINK         C   MSE F   7                 N   LEU F   8     1555   1555  1.33  
LINK         C   ASN F  12                 N   MSE F  13     1555   1555  1.33  
LINK         C   MSE F  13                 N   ALA F  14     1555   1555  1.34  
LINK         C   PRO F  23                 N   MSE F  24     1555   1555  1.33  
LINK         C   MSE F  24                 N   ILE F  25     1555   1555  1.33  
LINK         C   GLN F  31                 N   MSE F  32     1555   1555  1.33  
LINK         C   MSE F  32                 N   LEU F  33     1555   1555  1.33  
LINK         C   GLN F  39                 N   MSE F  40     1555   1555  1.33  
LINK         C   MSE F  40                 N   MSE F  41     1555   1555  1.33  
LINK         C   MSE F  41                 N   THR F  42     1555   1555  1.33  
LINK         C   ALA F 105                 N   MSE F 106     1555   1555  1.33  
LINK         C   MSE F 106                 N   GLU F 107     1555   1555  1.33  
LINK         C   SER F 259                 N   MSE F 260     1555   1555  1.32  
LINK         C   MSE F 260                 N   ASP F 261     1555   1555  1.33  
LINK         C   LEU F 276                 N   MSE F 277     1555   1555  1.33  
LINK         C   MSE F 277                 N   LYS F 278     1555   1555  1.34  
CISPEP   1 GLU A   43    PRO A   44          0        -0.22                     
CISPEP   2 GLU B   43    PRO B   44          0        -0.83                     
CISPEP   3 GLU C   43    PRO C   44          0        -1.82                     
CISPEP   4 GLU D   43    PRO D   44          0        -0.61                     
CISPEP   5 GLU E   43    PRO E   44          0        -1.84                     
CISPEP   6 GLU F   43    PRO F   44          0         0.38                     
CRYST1   70.999   87.936  103.510 106.50 100.22 113.80 P 1           6          
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      0.014085  0.006213  0.005438        0.00000                         
SCALE2      0.000000  0.012429  0.005346        0.00000                         
SCALE3      0.000000  0.000000  0.010686        0.00000                         
HETATM    1  N   MSE A   1      36.358 -26.713  43.446  1.00 60.87           N  
HETATM    2  CA  MSE A   1      36.788 -26.209  44.782  1.00 60.52           C  
HETATM    3  C   MSE A   1      35.746 -25.243  45.347  1.00 55.61           C  
HETATM    4  O   MSE A   1      34.603 -25.185  44.874  1.00 55.50           O  
HETATM    5  CB  MSE A   1      38.156 -25.500  44.688  1.00 68.32           C  
HETATM    6  CG  MSE A   1      38.161 -24.177  43.889  1.00 78.54           C  
HETATM    7 SE   MSE A   1      39.811 -23.059  43.986  1.00 94.81          SE  
HETATM    8  CE  MSE A   1      40.708 -23.593  42.310  1.00 89.76           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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