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Database: PDB
Entry: 1N3B
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HEADER    TRANSFERASE                             25-OCT-02   1N3B              
TITLE     CRYSTAL STRUCTURE OF DEPHOSPHOCOENZYME A KINASE FROM ESCHERICHIA COLI 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DEPHOSPHO-COA KINASE;                                      
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: DEPHOSPHOCOENZYME A KINASE;                                 
COMPND   5 EC: 2.7.1.24;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: COAE;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: DL41(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET20B DERIVATIVE                         
KEYWDS    TRIMER, P-LOOP, ALPHA/BETA, MONTREAL-KINGSTON BACTERIAL STRUCTURAL    
KEYWDS   2 GENOMICS INITIATIVE, BSGI, STRUCTURAL GENOMICS, TRANSFERASE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.O'TOOLE,J.A.R.G.BARBOSA,Y.LI,L.-W.HUNG,A.MATTE,M.CYGLER,MONTREAL-   
AUTHOR   2 KINGSTON BACTERIAL STRUCTURAL GENOMICS INITIATIVE (BSGI)             
REVDAT   4   01-FEB-17 1N3B    1       AUTHOR                                   
REVDAT   3   16-APR-14 1N3B    1       REMARK VERSN                             
REVDAT   2   24-FEB-09 1N3B    1       VERSN                                    
REVDAT   1   28-JAN-03 1N3B    0                                                
JRNL        AUTH   N.O'TOOLE,J.A.R.G.BARBOSA,Y.LI,L.-W.HUNG,A.MATTE,M.CYGLER    
JRNL        TITL   CRYSTAL STRUCTURE OF A TRIMERIC FORM OF DEPHOSPHOCOENZYME A  
JRNL        TITL 2 KINASE FROM ESCHERICHIA COLI                                 
JRNL        REF    PROTEIN SCI.                  V.  12   327 2003              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   12538896                                                     
JRNL        DOI    10.1110/PS.0227803                                           
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.OBLOMOVA,A.TEPLYAKOV,N.BONANDER,E.EISENSTEIN,A.HOWARD,     
REMARK   1  AUTH 2 G.GILLILAND                                                  
REMARK   1  TITL   CRYSTAL STRUCTURE OF DEPHOSPHO-COENZYME A KINASE FROM        
REMARK   1  TITL 2 HAEMOPHILUS INFLUENZAE                                       
REMARK   1  REF    J.STRUCT.BIOL.                V. 136   119 2001              
REMARK   1  REFN                   ISSN 1047-8477                               
REMARK   1  DOI    10.1006/JSBI.2001.4428                                       
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   P.K.MISHRA,P.K.PARK,D.G.DRUECKHAMMER                         
REMARK   1  TITL   IDENTIFICATION OF YACE (COAE) AS THE STRUCTURAL GENE FOR     
REMARK   1  TITL 2 DEPHOSPHOCOENZYME A KINASE IN ESCHERICHIA COLI K-12          
REMARK   1  REF    J.BACTERIOL.                  V. 183  2774 2001              
REMARK   1  REFN                   ISSN 0021-9193                               
REMARK   1  DOI    10.1128/JB.183.9.2774-2778.2001                              
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   C.VORHEIN,H.BONISCH,G.SCHAFER,G.E.SCHULZ                     
REMARK   1  TITL   THE STRUCTURE OF A TRIMERIC ARCHAEL ADENYLATE KINASE         
REMARK   1  REF    J.MOL.BIOL.                   V. 282   167 1998              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  DOI    10.1006/JMBI.1998.2003                                       
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   D.M.WORRAL,P.K.TUBBS                                         
REMARK   1  TITL   A BIFUNCTIONAL ENZYME COMPLEX IN COENZYME A BIOSYNTHESIS:    
REMARK   1  TITL 2 PURIFICATION OF PANTETHEINE PHOSPHATE ADENYLYLTRANSFERASE    
REMARK   1  TITL 3 AND DEPHOSPHO-COA KINASE                                     
REMARK   1  REF    BIOCHEM.J.                    V. 215   153 1983              
REMARK   1  REFN                   ISSN 0264-6021                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   S.AGHAJANIAN,D.M.WORRAL                                      
REMARK   1  TITL   IDENTIFICATION AND CHARACTERIZATION OF THE GENE ENCODING THE 
REMARK   1  TITL 2 HUMAN ADENYLYLTRANSFERASE AND DEPHOSPHOCOENZYME A KINASE     
REMARK   1  TITL 3 BIFUNCTIONAL ENZYME                                          
REMARK   1  REF    BIOCHEM.J.                    V. 365    13 2002              
REMARK   1  REFN                   ISSN 0264-6021                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 107923                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE-R                          
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5518                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4547                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 449                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.46                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.260                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  BULK SOLVENT CORRECTION EMPLOYED.                                   
REMARK   3  THE STRUCTURE WAS REFINED USING FRIEDEL'S PAIRS.                    
REMARK   4                                                                      
REMARK   4 1N3B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB017465.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUL-01                          
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                       : X8C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97957, 0.97941                   
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MONOCHROMATING CRYSTAL             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59512                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.3                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.81                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.43900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, CACODYLATE BUFFER, AMMONIUM    
REMARK 280  SULFATE, GLYCEROL, PH 6.5, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       41.20500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -165.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ILE A    50                                                      
REMARK 465     ALA A    51                                                      
REMARK 465     ASP A    52                                                      
REMARK 465     HIS A    53                                                      
REMARK 465     PHE A    54                                                      
REMARK 465     GLY A    55                                                      
REMARK 465     ALA A    56                                                      
REMARK 465     ASN A    57                                                      
REMARK 465     MSE A    58                                                      
REMARK 465     ILE A    59                                                      
REMARK 465     ALA A    60                                                      
REMARK 465     ALA A    61                                                      
REMARK 465     ASP A    62                                                      
REMARK 465     GLY A    63                                                      
REMARK 465     THR A    64                                                      
REMARK 465     LEU A    65                                                      
REMARK 465     GLN A    66                                                      
REMARK 465     ARG A    67                                                      
REMARK 465     ARG A    68                                                      
REMARK 465     ALA A    69                                                      
REMARK 465     LEU A    70                                                      
REMARK 465     ARG A    71                                                      
REMARK 465     GLU A    72                                                      
REMARK 465     ARG A    73                                                      
REMARK 465     ILE A    74                                                      
REMARK 465     PHE A    75                                                      
REMARK 465     ALA A    76                                                      
REMARK 465     ASN A    77                                                      
REMARK 465     LYS A   205                                                      
REMARK 465     PRO A   206                                                      
REMARK 465     GLY A   207                                                      
REMARK 465     SER A   208                                                      
REMARK 465     HIS A   209                                                      
REMARK 465     HIS A   210                                                      
REMARK 465     HIS A   211                                                      
REMARK 465     HIS A   212                                                      
REMARK 465     HIS A   213                                                      
REMARK 465     HIS A   214                                                      
REMARK 465     HIS A   215                                                      
REMARK 465     HIS A   216                                                      
REMARK 465     GLY B   207                                                      
REMARK 465     SER B   208                                                      
REMARK 465     HIS B   209                                                      
REMARK 465     HIS B   210                                                      
REMARK 465     HIS B   211                                                      
REMARK 465     HIS B   212                                                      
REMARK 465     HIS B   213                                                      
REMARK 465     HIS B   214                                                      
REMARK 465     HIS B   215                                                      
REMARK 465     HIS B   216                                                      
REMARK 465     GLY C   207                                                      
REMARK 465     SER C   208                                                      
REMARK 465     HIS C   209                                                      
REMARK 465     HIS C   210                                                      
REMARK 465     HIS C   211                                                      
REMARK 465     HIS C   212                                                      
REMARK 465     HIS C   213                                                      
REMARK 465     HIS C   214                                                      
REMARK 465     HIS C   215                                                      
REMARK 465     HIS C   216                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   627     O    HOH B   657              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  79      -69.14     73.83                                   
REMARK 500    ASP A 146       70.93     43.06                                   
REMARK 500    ALA B  76      -39.57     75.06                                   
REMARK 500    LEU B 114       30.19    -96.92                                   
REMARK 500    ASN C  77       70.71    168.87                                   
REMARK 500    ASP C 145     -119.83   -137.35                                   
REMARK 500    ASP C 146     -156.64   -155.50                                   
REMARK 500    VAL C 147       65.82     38.57                                   
REMARK 500    THR C 148     -135.48     11.90                                   
REMARK 500    HIS C 151      -54.99     69.94                                   
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 SO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 510                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: COAE_ECOLI   RELATED DB: TARGETDB                        
DBREF  1N3B A    1   206  UNP    P0A6I9   COAE_ECOLI       1    206             
DBREF  1N3B B    1   206  UNP    P0A6I9   COAE_ECOLI       1    206             
DBREF  1N3B C    1   206  UNP    P0A6I9   COAE_ECOLI       1    206             
SEQADV 1N3B MSE A    1  UNP  P0A6I9    MET     1 MODIFIED RESIDUE               
SEQADV 1N3B MSE A   58  UNP  P0A6I9    MET    58 MODIFIED RESIDUE               
SEQADV 1N3B MSE A  142  UNP  P0A6I9    MET   142 MODIFIED RESIDUE               
SEQADV 1N3B GLY A  207  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B SER A  208  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS A  209  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS A  210  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS A  211  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS A  212  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS A  213  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS A  214  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS A  215  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS A  216  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B MSE B    1  UNP  P0A6I9    MET     1 MODIFIED RESIDUE               
SEQADV 1N3B MSE B   58  UNP  P0A6I9    MET    58 MODIFIED RESIDUE               
SEQADV 1N3B MSE B  142  UNP  P0A6I9    MET   142 MODIFIED RESIDUE               
SEQADV 1N3B GLY B  207  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B SER B  208  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS B  209  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS B  210  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS B  211  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS B  212  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS B  213  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS B  214  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS B  215  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS B  216  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B MSE C    1  UNP  P0A6I9    MET     1 MODIFIED RESIDUE               
SEQADV 1N3B MSE C   58  UNP  P0A6I9    MET    58 MODIFIED RESIDUE               
SEQADV 1N3B MSE C  142  UNP  P0A6I9    MET   142 MODIFIED RESIDUE               
SEQADV 1N3B GLY C  207  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B SER C  208  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS C  209  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS C  210  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS C  211  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS C  212  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS C  213  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS C  214  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS C  215  UNP  P0A6I9              EXPRESSION TAG                 
SEQADV 1N3B HIS C  216  UNP  P0A6I9              EXPRESSION TAG                 
SEQRES   1 A  216  MSE ARG TYR ILE VAL ALA LEU THR GLY GLY ILE GLY SER          
SEQRES   2 A  216  GLY LYS SER THR VAL ALA ASN ALA PHE ALA ASP LEU GLY          
SEQRES   3 A  216  ILE ASN VAL ILE ASP ALA ASP ILE ILE ALA ARG GLN VAL          
SEQRES   4 A  216  VAL GLU PRO GLY ALA PRO ALA LEU HIS ALA ILE ALA ASP          
SEQRES   5 A  216  HIS PHE GLY ALA ASN MSE ILE ALA ALA ASP GLY THR LEU          
SEQRES   6 A  216  GLN ARG ARG ALA LEU ARG GLU ARG ILE PHE ALA ASN PRO          
SEQRES   7 A  216  GLU GLU LYS ASN TRP LEU ASN ALA LEU LEU HIS PRO LEU          
SEQRES   8 A  216  ILE GLN GLN GLU THR GLN HIS GLN ILE GLN GLN ALA THR          
SEQRES   9 A  216  SER PRO TYR VAL LEU TRP VAL VAL PRO LEU LEU VAL GLU          
SEQRES  10 A  216  ASN SER LEU TYR LYS LYS ALA ASN ARG VAL LEU VAL VAL          
SEQRES  11 A  216  ASP VAL SER PRO GLU THR GLN LEU LYS ARG THR MSE GLN          
SEQRES  12 A  216  ARG ASP ASP VAL THR ARG GLU HIS VAL GLU GLN ILE LEU          
SEQRES  13 A  216  ALA ALA GLN ALA THR ARG GLU ALA ARG LEU ALA VAL ALA          
SEQRES  14 A  216  ASP ASP VAL ILE ASP ASN ASN GLY ALA PRO ASP ALA ILE          
SEQRES  15 A  216  ALA SER ASP VAL ALA ARG LEU HIS ALA HIS TYR LEU GLN          
SEQRES  16 A  216  LEU ALA SER GLN PHE VAL SER GLN GLU LYS PRO GLY SER          
SEQRES  17 A  216  HIS HIS HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B  216  MSE ARG TYR ILE VAL ALA LEU THR GLY GLY ILE GLY SER          
SEQRES   2 B  216  GLY LYS SER THR VAL ALA ASN ALA PHE ALA ASP LEU GLY          
SEQRES   3 B  216  ILE ASN VAL ILE ASP ALA ASP ILE ILE ALA ARG GLN VAL          
SEQRES   4 B  216  VAL GLU PRO GLY ALA PRO ALA LEU HIS ALA ILE ALA ASP          
SEQRES   5 B  216  HIS PHE GLY ALA ASN MSE ILE ALA ALA ASP GLY THR LEU          
SEQRES   6 B  216  GLN ARG ARG ALA LEU ARG GLU ARG ILE PHE ALA ASN PRO          
SEQRES   7 B  216  GLU GLU LYS ASN TRP LEU ASN ALA LEU LEU HIS PRO LEU          
SEQRES   8 B  216  ILE GLN GLN GLU THR GLN HIS GLN ILE GLN GLN ALA THR          
SEQRES   9 B  216  SER PRO TYR VAL LEU TRP VAL VAL PRO LEU LEU VAL GLU          
SEQRES  10 B  216  ASN SER LEU TYR LYS LYS ALA ASN ARG VAL LEU VAL VAL          
SEQRES  11 B  216  ASP VAL SER PRO GLU THR GLN LEU LYS ARG THR MSE GLN          
SEQRES  12 B  216  ARG ASP ASP VAL THR ARG GLU HIS VAL GLU GLN ILE LEU          
SEQRES  13 B  216  ALA ALA GLN ALA THR ARG GLU ALA ARG LEU ALA VAL ALA          
SEQRES  14 B  216  ASP ASP VAL ILE ASP ASN ASN GLY ALA PRO ASP ALA ILE          
SEQRES  15 B  216  ALA SER ASP VAL ALA ARG LEU HIS ALA HIS TYR LEU GLN          
SEQRES  16 B  216  LEU ALA SER GLN PHE VAL SER GLN GLU LYS PRO GLY SER          
SEQRES  17 B  216  HIS HIS HIS HIS HIS HIS HIS HIS                              
SEQRES   1 C  216  MSE ARG TYR ILE VAL ALA LEU THR GLY GLY ILE GLY SER          
SEQRES   2 C  216  GLY LYS SER THR VAL ALA ASN ALA PHE ALA ASP LEU GLY          
SEQRES   3 C  216  ILE ASN VAL ILE ASP ALA ASP ILE ILE ALA ARG GLN VAL          
SEQRES   4 C  216  VAL GLU PRO GLY ALA PRO ALA LEU HIS ALA ILE ALA ASP          
SEQRES   5 C  216  HIS PHE GLY ALA ASN MSE ILE ALA ALA ASP GLY THR LEU          
SEQRES   6 C  216  GLN ARG ARG ALA LEU ARG GLU ARG ILE PHE ALA ASN PRO          
SEQRES   7 C  216  GLU GLU LYS ASN TRP LEU ASN ALA LEU LEU HIS PRO LEU          
SEQRES   8 C  216  ILE GLN GLN GLU THR GLN HIS GLN ILE GLN GLN ALA THR          
SEQRES   9 C  216  SER PRO TYR VAL LEU TRP VAL VAL PRO LEU LEU VAL GLU          
SEQRES  10 C  216  ASN SER LEU TYR LYS LYS ALA ASN ARG VAL LEU VAL VAL          
SEQRES  11 C  216  ASP VAL SER PRO GLU THR GLN LEU LYS ARG THR MSE GLN          
SEQRES  12 C  216  ARG ASP ASP VAL THR ARG GLU HIS VAL GLU GLN ILE LEU          
SEQRES  13 C  216  ALA ALA GLN ALA THR ARG GLU ALA ARG LEU ALA VAL ALA          
SEQRES  14 C  216  ASP ASP VAL ILE ASP ASN ASN GLY ALA PRO ASP ALA ILE          
SEQRES  15 C  216  ALA SER ASP VAL ALA ARG LEU HIS ALA HIS TYR LEU GLN          
SEQRES  16 C  216  LEU ALA SER GLN PHE VAL SER GLN GLU LYS PRO GLY SER          
SEQRES  17 C  216  HIS HIS HIS HIS HIS HIS HIS HIS                              
MODRES 1N3B MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 1N3B MSE A  142  MET  SELENOMETHIONINE                                   
MODRES 1N3B MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 1N3B MSE B   58  MET  SELENOMETHIONINE                                   
MODRES 1N3B MSE B  142  MET  SELENOMETHIONINE                                   
MODRES 1N3B MSE C    1  MET  SELENOMETHIONINE                                   
MODRES 1N3B MSE C   58  MET  SELENOMETHIONINE                                   
MODRES 1N3B MSE C  142  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A 142       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B  58       8                                                       
HET    MSE  B 142       8                                                       
HET    MSE  C   1       8                                                       
HET    MSE  C  58       8                                                       
HET    MSE  C 142       8                                                       
HET    SO4  A 501       5                                                       
HET    SO4  B 502       5                                                       
HET    SO4  C 503       5                                                       
HET    SO4  C 504       5                                                       
HET    SO4  A 505       5                                                       
HET    SO4  B 506       5                                                       
HET    SO4  C 507       5                                                       
HET    SO4  C 508       5                                                       
HET    SO4  B 509       5                                                       
HET    SO4  A 510       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    8(C5 H11 N O2 SE)                                            
FORMUL   4  SO4    10(O4 S 2-)                                                  
FORMUL  14  HOH   *449(H2 O)                                                    
HELIX    1   1 GLY A   14  LEU A   25  1                                  12    
HELIX    2   2 ALA A   32  VAL A   39  1                                   8    
HELIX    3   3 ALA A   44  ALA A   49  1                                   6    
HELIX    4   4 GLU A   79  ALA A  103  1                                  25    
HELIX    5   5 SER A  119  ALA A  124  5                                   6    
HELIX    6   6 SER A  133  ASP A  146  1                                  14    
HELIX    7   7 THR A  148  GLN A  159  1                                  12    
HELIX    8   8 THR A  161  ALA A  169  1                                   9    
HELIX    9   9 ALA A  178  ALA A  181  5                                   4    
HELIX   10  10 ILE A  182  PHE A  200  1                                  19    
HELIX   11  11 GLY B   14  LEU B   25  1                                  12    
HELIX   12  12 ALA B   32  VAL B   39  1                                   8    
HELIX   13  13 ALA B   44  GLY B   55  1                                  12    
HELIX   14  14 ALA B   56  ILE B   59  5                                   4    
HELIX   15  15 GLN B   66  PHE B   75  1                                  10    
HELIX   16  16 ASN B   77  ALA B  103  1                                  27    
HELIX   17  17 SER B  119  ALA B  124  5                                   6    
HELIX   18  18 SER B  133  ASP B  145  1                                  13    
HELIX   19  19 THR B  148  GLN B  159  1                                  12    
HELIX   20  20 THR B  161  ALA B  169  1                                   9    
HELIX   21  21 ALA B  178  ALA B  181  5                                   4    
HELIX   22  22 ILE B  182  PHE B  200  1                                  19    
HELIX   23  23 GLY C   14  ASP C   24  1                                  11    
HELIX   24  24 ALA C   32  VAL C   39  1                                   8    
HELIX   25  25 ALA C   44  GLY C   55  1                                  12    
HELIX   26  26 ALA C   56  ILE C   59  5                                   4    
HELIX   27  27 GLN C   66  ALA C   76  1                                  11    
HELIX   28  28 ASN C   77  ALA C  103  1                                  27    
HELIX   29  29 SER C  119  ALA C  124  5                                   6    
HELIX   30  30 SER C  133  ASP C  145  1                                  13    
HELIX   31  31 HIS C  151  GLN C  159  1                                   9    
HELIX   32  32 THR C  161  ALA C  169  1                                   9    
HELIX   33  33 ALA C  181  PHE C  200  1                                  20    
SHEET    1   A 5 ASN A  28  ASP A  31  0                                        
SHEET    2   A 5 TYR A 107  VAL A 111  1  O  LEU A 109   N  ILE A  30           
SHEET    3   A 5 TYR A   3  THR A   8  1  N  LEU A   7   O  TRP A 110           
SHEET    4   A 5 ARG A 126  ASP A 131  1  O  LEU A 128   N  ALA A   6           
SHEET    5   A 5 ASP A 171  ASP A 174  1  O  ILE A 173   N  ASP A 131           
SHEET    1   B 5 ASN B  28  ASP B  31  0                                        
SHEET    2   B 5 TYR B 107  VAL B 111  1  O  LEU B 109   N  ILE B  30           
SHEET    3   B 5 TYR B   3  THR B   8  1  N  LEU B   7   O  TRP B 110           
SHEET    4   B 5 ARG B 126  ASP B 131  1  O  LEU B 128   N  ALA B   6           
SHEET    5   B 5 ASP B 171  ASP B 174  1  O  ILE B 173   N  ASP B 131           
SHEET    1   C 5 ASN C  28  ASP C  31  0                                        
SHEET    2   C 5 TYR C 107  VAL C 111  1  O  LEU C 109   N  ILE C  30           
SHEET    3   C 5 TYR C   3  THR C   8  1  N  VAL C   5   O  TRP C 110           
SHEET    4   C 5 ARG C 126  ASP C 131  1  O  LEU C 128   N  ALA C   6           
SHEET    5   C 5 ASP C 171  ASP C 174  1  O  ILE C 173   N  VAL C 129           
LINK         C   MSE A   1                 N   ARG A   2     1555   1555  1.33  
LINK         C   THR A 141                 N   MSE A 142     1555   1555  1.33  
LINK         C   MSE A 142                 N   GLN A 143     1555   1555  1.33  
LINK         C   MSE B   1                 N   ARG B   2     1555   1555  1.33  
LINK         C   ASN B  57                 N   MSE B  58     1555   1555  1.34  
LINK         C   MSE B  58                 N   ILE B  59     1555   1555  1.33  
LINK         C   THR B 141                 N   MSE B 142     1555   1555  1.33  
LINK         C   MSE B 142                 N   GLN B 143     1555   1555  1.33  
LINK         C   MSE C   1                 N   ARG C   2     1555   1555  1.33  
LINK         C   ASN C  57                 N   MSE C  58     1555   1555  1.33  
LINK         C   MSE C  58                 N   ILE C  59     1555   1555  1.33  
LINK         C   THR C 141                 N   MSE C 142     1555   1555  1.33  
LINK         C   MSE C 142                 N   GLN C 143     1555   1555  1.33  
CISPEP   1 ALA C  178    PRO C  179          0         0.35                     
SITE     1 AC1  8 ILE A  11  GLY A  12  SER A  13  GLY A  14                    
SITE     2 AC1  8 LYS A  15  ARG A 144  HOH A 528  HOH A 604                    
SITE     1 AC2  8 ILE B  11  GLY B  12  SER B  13  GLY B  14                    
SITE     2 AC2  8 LYS B  15  ARG B 144  HOH B 563  HOH B 587                    
SITE     1 AC3  6 GLY C  12  SER C  13  GLY C  14  LYS C  15                    
SITE     2 AC3  6 ARG C 144  HOH C 596                                          
SITE     1 AC4 10 SER A 119  TYR A 121  LYS A 122  SER B 119                    
SITE     2 AC4 10 TYR B 121  LYS B 122  HOH B 554  SER C 119                    
SITE     3 AC4 10 TYR C 121  LYS C 122                                          
SITE     1 AC5  3 ARG A 126  HIS A 192  HOH A 576                               
SITE     1 AC6  2 ARG B 126  HIS B 192                                          
SITE     1 AC7  3 ARG C 126  HIS C 192  HOH C 653                               
SITE     1 AC8  5 HOH B 680  GLN C  93  THR C  96  GLN C  97                    
SITE     2 AC8  5 TRP C 110                                                     
SITE     1 AC9  4 ALA A 157  GLN B  93  GLN B  97  TRP B 110                    
SITE     1 BC1  6 GLN A  93  THR A  96  GLN A  97  TRP A 110                    
SITE     2 BC1  6 LYS A 123  HOH C 650                                          
CRYST1   55.500   82.410   76.000  90.00  94.77  90.00 P 1 21 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      0.018018  0.000000  0.001504        0.00000                         
SCALE2      0.000000  0.012134  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013204        0.00000                         
HETATM    1  N   MSE A   1      15.279  50.586  45.803  1.00 46.10           N  
HETATM    2  CA  MSE A   1      15.268  49.091  45.836  1.00 46.36           C  
HETATM    3  C   MSE A   1      14.501  48.547  44.656  1.00 42.93           C  
HETATM    4  O   MSE A   1      13.650  49.239  44.087  1.00 43.92           O  
HETATM    5  CB  MSE A   1      14.583  48.579  47.089  1.00 51.37           C  
HETATM    6  CG  MSE A   1      15.160  49.063  48.379  1.00 58.22           C  
HETATM    7 SE   MSE A   1      14.135  48.235  49.752  1.00 68.21          SE  
HETATM    8  CE  MSE A   1      15.133  46.578  49.871  1.00 63.53           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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