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Database: PDB
Entry: 4FGD
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Original site: 4FGD 
HEADER    HYDROLASE                               04-JUN-12   4FGD              
TITLE     STRUCTURE OF THE EFFECTOR PROTEIN TSE1 FROM PSEUDOMONAS AERUGINOSA,   
TITLE    2 SELENOMETHIONINE VARIANT                                             
CAVEAT     4FGD    S-C-N BOND ANGLE IN SCN C 202 LIGAND IS OUTSIDE ACCEPTED     
CAVEAT   2 4FGD     RANGE                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TSE1;                                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 208964;                                              
SOURCE   4 STRAIN: PAO1;                                                        
SOURCE   5 GENE: PA1844;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIL;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET21D                                
KEYWDS    N1PC/P60 SUPERFAMILY, PEPTIDOGLYCAN HYDROLASE, CYTOSOL, HYDROLASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.BENZ,C.SENDLMEIER,T.R.M.BARENDS,A.MEINHART                          
REVDAT   3   25-JUL-12 4FGD    1       JRNL                                     
REVDAT   2   18-JUL-12 4FGD    1       JRNL                                     
REVDAT   1   20-JUN-12 4FGD    0                                                
JRNL        AUTH   J.BENZ,C.SENDLMEIER,T.R.BARENDS,A.MEINHART                   
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE EFFECTOR - IMMUNITY SYSTEM      
JRNL        TITL 2 TSE1/TSI1 FROM PSEUDOMONAS AERUGINOSA.                       
JRNL        REF    PLOS ONE                      V.   7 40453 2012              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   22792331                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0040453                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 20367                          
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 + TEST SET) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1072                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1408                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 74                           
REMARK   3   BIN FREE R VALUE                    : 0.3020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4392                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 128                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.43000                                              
REMARK   3    B22 (A**2) : -1.27000                                             
REMARK   3    B33 (A**2) : -1.19000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.22000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.772         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.313         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.221         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.222        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.922                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.892                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4490 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6081 ; 1.103 ; 1.940       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   584 ; 5.301 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   184 ;35.678 ;24.348       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   714 ;15.437 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;17.282 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   654 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3416 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1930 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3076 ; 0.292 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   157 ; 0.115 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    59 ; 0.322 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.098 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2898 ; 0.418 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4579 ; 0.815 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1592 ; 1.298 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1502 ; 2.036 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4FGD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072867.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21546                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 9.300                              
REMARK 200  R MERGE                    (I) : 0.09200                            
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) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXD AND SHELXE                                     
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM KSCN, 1% (V/V) MPD, AND 15% (W/   
REMARK 280  V) PEG 3350, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       54.20000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5                                                       
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: 1830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MSE A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     PRO A   151                                                      
REMARK 465     ARG A   152                                                      
REMARK 465     ALA A   153                                                      
REMARK 465     SER A   154                                                      
REMARK 465     ALA A   155                                                      
REMARK 465     ALA A   156                                                      
REMARK 465     ALA A   157                                                      
REMARK 465     LEU A   158                                                      
REMARK 465     GLU A   159                                                      
REMARK 465     HIS A   160                                                      
REMARK 465     HIS A   161                                                      
REMARK 465     HIS A   162                                                      
REMARK 465     HIS A   163                                                      
REMARK 465     HIS A   164                                                      
REMARK 465     HIS A   165                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     LEU B   150                                                      
REMARK 465     PRO B   151                                                      
REMARK 465     ARG B   152                                                      
REMARK 465     ALA B   153                                                      
REMARK 465     SER B   154                                                      
REMARK 465     ALA B   155                                                      
REMARK 465     ALA B   156                                                      
REMARK 465     ALA B   157                                                      
REMARK 465     LEU B   158                                                      
REMARK 465     GLU B   159                                                      
REMARK 465     HIS B   160                                                      
REMARK 465     HIS B   161                                                      
REMARK 465     HIS B   162                                                      
REMARK 465     HIS B   163                                                      
REMARK 465     HIS B   164                                                      
REMARK 465     HIS B   165                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     ASP C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     PRO C   151                                                      
REMARK 465     ARG C   152                                                      
REMARK 465     ALA C   153                                                      
REMARK 465     SER C   154                                                      
REMARK 465     ALA C   155                                                      
REMARK 465     ALA C   156                                                      
REMARK 465     ALA C   157                                                      
REMARK 465     LEU C   158                                                      
REMARK 465     GLU C   159                                                      
REMARK 465     HIS C   160                                                      
REMARK 465     HIS C   161                                                      
REMARK 465     HIS C   162                                                      
REMARK 465     HIS C   163                                                      
REMARK 465     HIS C   164                                                      
REMARK 465     HIS C   165                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     ASP D     2                                                      
REMARK 465     LEU D   150                                                      
REMARK 465     PRO D   151                                                      
REMARK 465     ARG D   152                                                      
REMARK 465     ALA D   153                                                      
REMARK 465     SER D   154                                                      
REMARK 465     ALA D   155                                                      
REMARK 465     ALA D   156                                                      
REMARK 465     ALA D   157                                                      
REMARK 465     LEU D   158                                                      
REMARK 465     GLU D   159                                                      
REMARK 465     HIS D   160                                                      
REMARK 465     HIS D   161                                                      
REMARK 465     HIS D   162                                                      
REMARK 465     HIS D   163                                                      
REMARK 465     HIS D   164                                                      
REMARK 465     HIS D   165                                                      
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    THR A  88      -63.54    -99.46                                   
REMARK 500    GLN A 103       14.63     59.29                                   
REMARK 500    LYS A 104      -46.02   -134.91                                   
REMARK 500    SER B  60      -15.33   -140.58                                   
REMARK 500    GLN B 103       18.51     52.77                                   
REMARK 500    LYS B 104      -45.51   -139.21                                   
REMARK 500    THR C  88      -65.43    -98.71                                   
REMARK 500    GLN C 103       15.96     53.64                                   
REMARK 500    LYS C 104      -35.10   -130.13                                   
REMARK 500    ASN D  29       92.05   -164.59                                   
REMARK 500    LYS D 104      -45.16   -137.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN D 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4FGE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FGI   RELATED DB: PDB                                   
DBREF  4FGD A    1   154  UNP    Q9I2Q1   Q9I2Q1_PSEAE     1    154             
DBREF  4FGD B    1   154  UNP    Q9I2Q1   Q9I2Q1_PSEAE     1    154             
DBREF  4FGD C    1   154  UNP    Q9I2Q1   Q9I2Q1_PSEAE     1    154             
DBREF  4FGD D    1   154  UNP    Q9I2Q1   Q9I2Q1_PSEAE     1    154             
SEQADV 4FGD ALA A  155  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD ALA A  156  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD ALA A  157  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD LEU A  158  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD GLU A  159  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS A  160  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS A  161  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS A  162  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS A  163  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS A  164  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS A  165  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD ALA B  155  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD ALA B  156  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD ALA B  157  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD LEU B  158  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD GLU B  159  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS B  160  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS B  161  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS B  162  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS B  163  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS B  164  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS B  165  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD ALA C  155  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD ALA C  156  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD ALA C  157  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD LEU C  158  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD GLU C  159  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS C  160  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS C  161  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS C  162  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS C  163  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS C  164  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS C  165  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD ALA D  155  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD ALA D  156  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD ALA D  157  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD LEU D  158  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD GLU D  159  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS D  160  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS D  161  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS D  162  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS D  163  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS D  164  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FGD HIS D  165  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQRES   1 A  165  MSE ASP SER LEU ASP GLN CYS ILE VAL ASN ALA CYS LYS          
SEQRES   2 A  165  ASN SER TRP ASP LYS SER TYR LEU ALA GLY THR PRO ASN          
SEQRES   3 A  165  LYS ASP ASN CYS SER GLY PHE VAL GLN SER VAL ALA ALA          
SEQRES   4 A  165  GLU LEU GLY VAL PRO MSE PRO ARG GLY ASN ALA ASN ALA          
SEQRES   5 A  165  MSE VAL ASP GLY LEU GLU GLN SER TRP THR LYS LEU ALA          
SEQRES   6 A  165  SER GLY ALA GLU ALA ALA GLN LYS ALA ALA GLN GLY PHE          
SEQRES   7 A  165  LEU VAL ILE ALA GLY LEU LYS GLY ARG THR TYR GLY HIS          
SEQRES   8 A  165  VAL ALA VAL VAL ILE SER GLY PRO LEU TYR ARG GLN LYS          
SEQRES   9 A  165  TYR PRO MSE CYS TRP CYS GLY SER ILE ALA GLY ALA VAL          
SEQRES  10 A  165  GLY GLN SER GLN GLY LEU LYS SER VAL GLY GLN VAL TRP          
SEQRES  11 A  165  ASN ARG THR ASP ARG ASP ARG LEU ASN TYR TYR VAL TYR          
SEQRES  12 A  165  SER LEU ALA SER CYS SER LEU PRO ARG ALA SER ALA ALA          
SEQRES  13 A  165  ALA LEU GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 B  165  MSE ASP SER LEU ASP GLN CYS ILE VAL ASN ALA CYS LYS          
SEQRES   2 B  165  ASN SER TRP ASP LYS SER TYR LEU ALA GLY THR PRO ASN          
SEQRES   3 B  165  LYS ASP ASN CYS SER GLY PHE VAL GLN SER VAL ALA ALA          
SEQRES   4 B  165  GLU LEU GLY VAL PRO MSE PRO ARG GLY ASN ALA ASN ALA          
SEQRES   5 B  165  MSE VAL ASP GLY LEU GLU GLN SER TRP THR LYS LEU ALA          
SEQRES   6 B  165  SER GLY ALA GLU ALA ALA GLN LYS ALA ALA GLN GLY PHE          
SEQRES   7 B  165  LEU VAL ILE ALA GLY LEU LYS GLY ARG THR TYR GLY HIS          
SEQRES   8 B  165  VAL ALA VAL VAL ILE SER GLY PRO LEU TYR ARG GLN LYS          
SEQRES   9 B  165  TYR PRO MSE CYS TRP CYS GLY SER ILE ALA GLY ALA VAL          
SEQRES  10 B  165  GLY GLN SER GLN GLY LEU LYS SER VAL GLY GLN VAL TRP          
SEQRES  11 B  165  ASN ARG THR ASP ARG ASP ARG LEU ASN TYR TYR VAL TYR          
SEQRES  12 B  165  SER LEU ALA SER CYS SER LEU PRO ARG ALA SER ALA ALA          
SEQRES  13 B  165  ALA LEU GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 C  165  MSE ASP SER LEU ASP GLN CYS ILE VAL ASN ALA CYS LYS          
SEQRES   2 C  165  ASN SER TRP ASP LYS SER TYR LEU ALA GLY THR PRO ASN          
SEQRES   3 C  165  LYS ASP ASN CYS SER GLY PHE VAL GLN SER VAL ALA ALA          
SEQRES   4 C  165  GLU LEU GLY VAL PRO MSE PRO ARG GLY ASN ALA ASN ALA          
SEQRES   5 C  165  MSE VAL ASP GLY LEU GLU GLN SER TRP THR LYS LEU ALA          
SEQRES   6 C  165  SER GLY ALA GLU ALA ALA GLN LYS ALA ALA GLN GLY PHE          
SEQRES   7 C  165  LEU VAL ILE ALA GLY LEU LYS GLY ARG THR TYR GLY HIS          
SEQRES   8 C  165  VAL ALA VAL VAL ILE SER GLY PRO LEU TYR ARG GLN LYS          
SEQRES   9 C  165  TYR PRO MSE CYS TRP CYS GLY SER ILE ALA GLY ALA VAL          
SEQRES  10 C  165  GLY GLN SER GLN GLY LEU LYS SER VAL GLY GLN VAL TRP          
SEQRES  11 C  165  ASN ARG THR ASP ARG ASP ARG LEU ASN TYR TYR VAL TYR          
SEQRES  12 C  165  SER LEU ALA SER CYS SER LEU PRO ARG ALA SER ALA ALA          
SEQRES  13 C  165  ALA LEU GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 D  165  MSE ASP SER LEU ASP GLN CYS ILE VAL ASN ALA CYS LYS          
SEQRES   2 D  165  ASN SER TRP ASP LYS SER TYR LEU ALA GLY THR PRO ASN          
SEQRES   3 D  165  LYS ASP ASN CYS SER GLY PHE VAL GLN SER VAL ALA ALA          
SEQRES   4 D  165  GLU LEU GLY VAL PRO MSE PRO ARG GLY ASN ALA ASN ALA          
SEQRES   5 D  165  MSE VAL ASP GLY LEU GLU GLN SER TRP THR LYS LEU ALA          
SEQRES   6 D  165  SER GLY ALA GLU ALA ALA GLN LYS ALA ALA GLN GLY PHE          
SEQRES   7 D  165  LEU VAL ILE ALA GLY LEU LYS GLY ARG THR TYR GLY HIS          
SEQRES   8 D  165  VAL ALA VAL VAL ILE SER GLY PRO LEU TYR ARG GLN LYS          
SEQRES   9 D  165  TYR PRO MSE CYS TRP CYS GLY SER ILE ALA GLY ALA VAL          
SEQRES  10 D  165  GLY GLN SER GLN GLY LEU LYS SER VAL GLY GLN VAL TRP          
SEQRES  11 D  165  ASN ARG THR ASP ARG ASP ARG LEU ASN TYR TYR VAL TYR          
SEQRES  12 D  165  SER LEU ALA SER CYS SER LEU PRO ARG ALA SER ALA ALA          
SEQRES  13 D  165  ALA LEU GLU HIS HIS HIS HIS HIS HIS                          
MODRES 4FGD MSE A   45  MET  SELENOMETHIONINE                                   
MODRES 4FGD MSE A   53  MET  SELENOMETHIONINE                                   
MODRES 4FGD MSE A  107  MET  SELENOMETHIONINE                                   
MODRES 4FGD MSE B   45  MET  SELENOMETHIONINE                                   
MODRES 4FGD MSE B   53  MET  SELENOMETHIONINE                                   
MODRES 4FGD MSE B  107  MET  SELENOMETHIONINE                                   
MODRES 4FGD MSE C   45  MET  SELENOMETHIONINE                                   
MODRES 4FGD MSE C   53  MET  SELENOMETHIONINE                                   
MODRES 4FGD MSE C  107  MET  SELENOMETHIONINE                                   
MODRES 4FGD MSE D   45  MET  SELENOMETHIONINE                                   
MODRES 4FGD MSE D   53  MET  SELENOMETHIONINE                                   
MODRES 4FGD MSE D  107  MET  SELENOMETHIONINE                                   
HET    MSE  A  45       8                                                       
HET    MSE  A  53       8                                                       
HET    MSE  A 107       8                                                       
HET    MSE  B  45       8                                                       
HET    MSE  B  53       8                                                       
HET    MSE  B 107       8                                                       
HET    MSE  C  45       8                                                       
HET    MSE  C  53       8                                                       
HET    MSE  C 107       8                                                       
HET    MSE  D  45       8                                                       
HET    MSE  D  53       8                                                       
HET    MSE  D 107       8                                                       
HET    SCN  C 201       3                                                       
HET    SCN  C 202       3                                                       
HET    SCN  D 201       3                                                       
HET     CL  D 202       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SCN THIOCYANATE ION                                                  
HETNAM      CL CHLORIDE ION                                                     
FORMUL   1  MSE    12(C5 H11 N O2 SE)                                           
FORMUL   5  SCN    3(C N S 1-)                                                  
FORMUL   8   CL    CL 1-                                                        
FORMUL   9  HOH   *128(H2 O)                                                    
HELIX    1   1 ASP A    5  TRP A   16  1                                  12    
HELIX    2   2 PRO A   25  ASP A   28  5                                   4    
HELIX    3   3 ASN A   29  GLY A   42  1                                  14    
HELIX    4   4 ASN A   49  TRP A   61  1                                  13    
HELIX    5   5 SER A   66  GLN A   76  1                                  11    
HELIX    6   6 LEU A  100  LYS A  104  5                                   5    
HELIX    7   7 GLY A  127  VAL A  129  5                                   3    
HELIX    8   8 ASP B    5  ASP B   17  1                                  13    
HELIX    9   9 PRO B   25  ASP B   28  5                                   4    
HELIX   10  10 ASN B   29  GLY B   42  1                                  14    
HELIX   11  11 ASN B   49  TRP B   61  1                                  13    
HELIX   12  12 SER B   66  GLN B   76  1                                  11    
HELIX   13  13 LEU B  100  LYS B  104  5                                   5    
HELIX   14  14 GLY B  115  GLN B  119  5                                   5    
HELIX   15  15 VAL B  126  TRP B  130  1                                   5    
HELIX   16  16 THR B  133  LEU B  138  5                                   6    
HELIX   17  17 ASP C    5  TRP C   16  1                                  12    
HELIX   18  18 PRO C   25  ASP C   28  5                                   4    
HELIX   19  19 ASN C   29  LEU C   41  1                                  13    
HELIX   20  20 ASN C   49  TRP C   61  1                                  13    
HELIX   21  21 SER C   66  GLN C   76  1                                  11    
HELIX   22  22 LEU C  100  LYS C  104  5                                   5    
HELIX   23  23 GLY C  115  GLN C  119  5                                   5    
HELIX   24  24 VAL C  126  TRP C  130  1                                   5    
HELIX   25  25 ASN C  131  ASP C  136  1                                   6    
HELIX   26  26 ASP D    5  TRP D   16  1                                  12    
HELIX   27  27 PRO D   25  ASP D   28  5                                   4    
HELIX   28  28 ASN D   29  LEU D   41  1                                  13    
HELIX   29  29 ASN D   49  TRP D   61  1                                  13    
HELIX   30  30 SER D   66  GLN D   76  1                                  11    
HELIX   31  31 ARG D  102  LYS D  104  5                                   3    
HELIX   32  32 GLY D  115  GLN D  119  5                                   5    
HELIX   33  33 VAL D  126  TRP D  130  1                                   5    
HELIX   34  34 THR D  133  LEU D  138  5                                   6    
SHEET    1   A 6 THR A  62  LYS A  63  0                                        
SHEET    2   A 6 ASN A 139  VAL A 142 -1  O  VAL A 142   N  THR A  62           
SHEET    3   A 6 VAL A  80  LEU A  84 -1  N  ILE A  81   O  TYR A 141           
SHEET    4   A 6 HIS A  91  VAL A  95 -1  O  ALA A  93   N  ALA A  82           
SHEET    5   A 6 MSE A 107  CYS A 110 -1  O  TRP A 109   N  VAL A  94           
SHEET    6   A 6 SER A 120  SER A 125 -1  O  SER A 120   N  CYS A 110           
SHEET    1   B 6 THR B  62  LYS B  63  0                                        
SHEET    2   B 6 ASN B 139  VAL B 142 -1  O  VAL B 142   N  THR B  62           
SHEET    3   B 6 VAL B  80  LEU B  84 -1  N  ILE B  81   O  TYR B 141           
SHEET    4   B 6 HIS B  91  VAL B  95 -1  O  ALA B  93   N  ALA B  82           
SHEET    5   B 6 MSE B 107  CYS B 110 -1  O  TRP B 109   N  VAL B  94           
SHEET    6   B 6 SER B 120  SER B 125 -1  O  SER B 120   N  CYS B 110           
SHEET    1   C 6 THR C  62  LYS C  63  0                                        
SHEET    2   C 6 ASN C 139  VAL C 142 -1  O  VAL C 142   N  THR C  62           
SHEET    3   C 6 VAL C  80  LEU C  84 -1  N  ILE C  81   O  TYR C 141           
SHEET    4   C 6 HIS C  91  VAL C  95 -1  O  ALA C  93   N  ALA C  82           
SHEET    5   C 6 MSE C 107  CYS C 110 -1  O  TRP C 109   N  VAL C  94           
SHEET    6   C 6 SER C 120  SER C 125 -1  O  SER C 120   N  CYS C 110           
SHEET    1   D 6 THR D  62  LYS D  63  0                                        
SHEET    2   D 6 ASN D 139  VAL D 142 -1  O  VAL D 142   N  THR D  62           
SHEET    3   D 6 VAL D  80  LEU D  84 -1  N  GLY D  83   O  ASN D 139           
SHEET    4   D 6 HIS D  91  TYR D 101 -1  O  ALA D  93   N  ALA D  82           
SHEET    5   D 6 TYR D 105  CYS D 110 -1  O  TRP D 109   N  VAL D  94           
SHEET    6   D 6 SER D 120  SER D 125 -1  O  SER D 120   N  CYS D 110           
SSBOND   1 CYS A    7    CYS A  148                          1555   1555  2.04  
SSBOND   2 CYS B    7    CYS B  148                          1555   1555  2.04  
SSBOND   3 CYS C    7    CYS C  148                          1555   1555  2.04  
SSBOND   4 CYS D    7    CYS D  148                          1555   1555  2.03  
LINK         C   PRO A  44                 N   MSE A  45     1555   1555  1.32  
LINK         C   MSE A  45                 N   PRO A  46     1555   1555  1.34  
LINK         C   ALA A  52                 N   MSE A  53     1555   1555  1.33  
LINK         C   MSE A  53                 N   VAL A  54     1555   1555  1.33  
LINK         C   PRO A 106                 N   MSE A 107     1555   1555  1.33  
LINK         C   MSE A 107                 N   CYS A 108     1555   1555  1.33  
LINK         C   PRO B  44                 N   MSE B  45     1555   1555  1.32  
LINK         C   MSE B  45                 N   PRO B  46     1555   1555  1.35  
LINK         C   ALA B  52                 N   MSE B  53     1555   1555  1.33  
LINK         C   MSE B  53                 N   VAL B  54     1555   1555  1.33  
LINK         C   PRO B 106                 N   MSE B 107     1555   1555  1.33  
LINK         C   MSE B 107                 N   CYS B 108     1555   1555  1.34  
LINK         C   PRO C  44                 N   MSE C  45     1555   1555  1.33  
LINK         C   MSE C  45                 N   PRO C  46     1555   1555  1.35  
LINK         C   ALA C  52                 N   MSE C  53     1555   1555  1.33  
LINK         C   MSE C  53                 N   VAL C  54     1555   1555  1.33  
LINK         C   PRO C 106                 N   MSE C 107     1555   1555  1.33  
LINK         C   MSE C 107                 N   CYS C 108     1555   1555  1.33  
LINK         C   PRO D  44                 N   MSE D  45     1555   1555  1.33  
LINK         C   MSE D  45                 N   PRO D  46     1555   1555  1.35  
LINK         C   ALA D  52                 N   MSE D  53     1555   1555  1.33  
LINK         C   MSE D  53                 N   VAL D  54     1555   1555  1.33  
LINK         C   PRO D 106                 N   MSE D 107     1555   1555  1.33  
LINK         C   MSE D 107                 N   CYS D 108     1555   1555  1.33  
SITE     1 AC1  4 SER C 120  GLN C 121  LEU C 123  LYS C 124                    
SITE     1 AC2  4 ALA A  22  ASN C  29  SER C  31  ASN C  49                    
SITE     1 AC3  3 SER D 120  GLN D 121  LYS D 124                               
CRYST1   39.210  108.400   83.760  90.00  93.80  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.025504  0.000000  0.001694        0.00000                         
SCALE2      0.000000  0.009225  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011965        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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