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Database: PDB
Entry: 1ORU
LinkDB: 1ORU
Original site: 1ORU 
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   15-MAR-03   1ORU              
TITLE     CRYSTAL STRUCTURE OF APC1665, YUAD PROTEIN FROM BACILLUS              
TITLE    2 SUBTILIS                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: YUAD PROTEIN;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_PLASMID: PMCSG7                                    
KEYWDS    STRUCTURAL GENOMICS, YUAD PROTEIN, CYTOSOLIC HYPOTHETICAL             
KEYWDS   2 PROTEIN, PSI, PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER           
KEYWDS   3 FOR STRUCTURAL GENOMICS, MCSG, UNKNOWN FUNCTION                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.KIM,A.JOACHIMIAK,A.EDWARDS,T.SKARINA,A.SAVCHENKO,MIDWEST            
AUTHOR   2 CENTER FOR STRUCTURAL GENOMICS (MCSG)                                
REVDAT   3   24-FEB-09 1ORU    1       VERSN                                    
REVDAT   2   18-JAN-05 1ORU    1       AUTHOR KEYWDS REMARK                     
REVDAT   1   23-SEP-03 1ORU    0                                                
JRNL        AUTH   Y.KIM,A.JOACHIMIAK,A.EDWARDS,T.SKARINA,A.SAVCHENKO           
JRNL        TITL   CRYSTAL STRUCTURE OF APC1665, YUAD PROTEIN FROM              
JRNL        TITL 2 BACILLUS SUBTILIS                                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
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) : 41.07                          
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)   (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 41997                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4203                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.88                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5820                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2930                       
REMARK   3   BIN FREE R VALUE                    : 0.3270                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.40                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 895                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2929                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 18                                      
REMARK   3   SOLVENT ATOMS            : 365                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.92000                                              
REMARK   3    B22 (A**2) : -5.86000                                             
REMARK   3    B33 (A**2) : -1.06000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.19                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.16                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.22                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.17                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.74                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.330 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.040 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.480 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.830 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 49.61                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ORU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018604.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-FEB-03                          
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               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97943, 0.97962, 0.961            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SBC-3                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK, HKL-2000                   
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43357                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 8.700                              
REMARK 200  R MERGE                    (I) : 0.09100                            
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) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
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: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, PEG 400, AMMONIUM SULFATE,        
REMARK 280  PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
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       21.32600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.12450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.60100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.12450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.32600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.60100            
REMARK 290   SMTRY3   4  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 300 REMARK: ALTHOUGH THERE IS NO EVICDENCE, IT APPEARS TO BE A DIMER     
REMARK 300 AS THE ASYMMETRIC CONTENT.                                           
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     ARG A   183                                                      
REMARK 465     LYS A   184                                                      
REMARK 465     VAL A   185                                                      
REMARK 465     LYS A   186                                                      
REMARK 465     ARG A   187                                                      
REMARK 465     LYS A   188                                                      
REMARK 465     ALA A   189                                                      
REMARK 465     GLU A   190                                                      
REMARK 465     ARG A   191                                                      
REMARK 465     VAL A   192                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     ARG B   183                                                      
REMARK 465     LYS B   184                                                      
REMARK 465     VAL B   185                                                      
REMARK 465     LYS B   186                                                      
REMARK 465     ARG B   187                                                      
REMARK 465     LYS B   188                                                      
REMARK 465     ALA B   189                                                      
REMARK 465     GLU B   190                                                      
REMARK 465     ARG B   191                                                      
REMARK 465     VAL B   192                                                      
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  17     -166.83   -129.37                                   
REMARK 500    ILE A 157       29.80   -143.77                                   
REMARK 500    THR B  17     -169.00   -123.98                                   
REMARK 500    ARG B  64       58.44   -109.53                                   
REMARK 500    ILE B 157       30.69   -141.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 663        DISTANCE =  5.81 ANGSTROMS                       
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 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 502                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 503                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 505                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 506                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: APC1665   RELATED DB: TARGETDB                           
DBREF  1ORU A   -2   192  UNP    O32079   O32079_BACSU     1    192             
DBREF  1ORU B   -2   192  UNP    O32079   O32079_BACSU     1    192             
SEQADV 1ORU SER A   -2  UNP  O32079              CLONING ARTIFACT               
SEQADV 1ORU ASN A   -1  UNP  O32079              CLONING ARTIFACT               
SEQADV 1ORU ALA A    0  UNP  O32079              CLONING ARTIFACT               
SEQADV 1ORU MSE A    1  UNP  O32079    MET     1 MODIFIED RESIDUE               
SEQADV 1ORU MSE A    5  UNP  O32079    MET     5 MODIFIED RESIDUE               
SEQADV 1ORU MSE A   25  UNP  O32079    MET    25 MODIFIED RESIDUE               
SEQADV 1ORU MSE A   53  UNP  O32079    MET    53 MODIFIED RESIDUE               
SEQADV 1ORU MSE A   81  UNP  O32079    MET    81 MODIFIED RESIDUE               
SEQADV 1ORU MSE A  100  UNP  O32079    MET   100 MODIFIED RESIDUE               
SEQADV 1ORU SER B   -2  UNP  O32079              CLONING ARTIFACT               
SEQADV 1ORU ASN B   -1  UNP  O32079              CLONING ARTIFACT               
SEQADV 1ORU ALA B    0  UNP  O32079              CLONING ARTIFACT               
SEQADV 1ORU MSE B    1  UNP  O32079    MET     1 MODIFIED RESIDUE               
SEQADV 1ORU MSE B    5  UNP  O32079    MET     5 MODIFIED RESIDUE               
SEQADV 1ORU MSE B   25  UNP  O32079    MET    25 MODIFIED RESIDUE               
SEQADV 1ORU MSE B   53  UNP  O32079    MET    53 MODIFIED RESIDUE               
SEQADV 1ORU MSE B   81  UNP  O32079    MET    81 MODIFIED RESIDUE               
SEQADV 1ORU MSE B  100  UNP  O32079    MET   100 MODIFIED RESIDUE               
SEQRES   1 A  195  SER ASN ALA MSE TRP LYS ARG MSE THR ALA LYS ALA GLU          
SEQRES   2 A  195  GLY LEU TYR ILE ALA ASP THR LYS SER PHE VAL THR LYS          
SEQRES   3 A  195  GLN MSE ASP LYS LEU ASP PHE ASP TYR GLY GLY ILE PRO          
SEQRES   4 A  195  GLY ASP LEU HIS PHE GLY LEU THR LYS LYS ALA GLY ALA          
SEQRES   5 A  195  ARG GLU PRO MSE PHE SER ARG GLY THR GLU ILE PHE ASN          
SEQRES   6 A  195  ARG ARG GLN ILE SER ILE VAL SER ILE GLU GLU CYS ASN          
SEQRES   7 A  195  GLU ILE ALA LEU LYS MSE GLY VAL PRO ARG ILE LEU PRO          
SEQRES   8 A  195  GLU TRP LEU GLY ALA ASN VAL ALA VAL SER GLY MSE PRO          
SEQRES   9 A  195  ASP LEU THR SER LEU LYS GLU GLY SER ARG ILE ILE PHE          
SEQRES  10 A  195  PRO SER GLY ALA ALA LEU LEU CYS GLU GLY GLU ASN ASP          
SEQRES  11 A  195  PRO CYS ILE GLN PRO GLY GLU VAL ILE GLN SER TYR TYR          
SEQRES  12 A  195  PRO ASP GLN PRO LYS LEU ALA SER ALA PHE VAL ARG HIS          
SEQRES  13 A  195  ALA LEU GLY ILE ARG GLY ILE VAL CYS ILE VAL GLU ARG          
SEQRES  14 A  195  PRO GLY ALA VAL TYR THR GLY ASP GLU ILE GLU VAL HIS          
SEQRES  15 A  195  SER TYR GLN ARG LYS VAL LYS ARG LYS ALA GLU ARG VAL          
SEQRES   1 B  195  SER ASN ALA MSE TRP LYS ARG MSE THR ALA LYS ALA GLU          
SEQRES   2 B  195  GLY LEU TYR ILE ALA ASP THR LYS SER PHE VAL THR LYS          
SEQRES   3 B  195  GLN MSE ASP LYS LEU ASP PHE ASP TYR GLY GLY ILE PRO          
SEQRES   4 B  195  GLY ASP LEU HIS PHE GLY LEU THR LYS LYS ALA GLY ALA          
SEQRES   5 B  195  ARG GLU PRO MSE PHE SER ARG GLY THR GLU ILE PHE ASN          
SEQRES   6 B  195  ARG ARG GLN ILE SER ILE VAL SER ILE GLU GLU CYS ASN          
SEQRES   7 B  195  GLU ILE ALA LEU LYS MSE GLY VAL PRO ARG ILE LEU PRO          
SEQRES   8 B  195  GLU TRP LEU GLY ALA ASN VAL ALA VAL SER GLY MSE PRO          
SEQRES   9 B  195  ASP LEU THR SER LEU LYS GLU GLY SER ARG ILE ILE PHE          
SEQRES  10 B  195  PRO SER GLY ALA ALA LEU LEU CYS GLU GLY GLU ASN ASP          
SEQRES  11 B  195  PRO CYS ILE GLN PRO GLY GLU VAL ILE GLN SER TYR TYR          
SEQRES  12 B  195  PRO ASP GLN PRO LYS LEU ALA SER ALA PHE VAL ARG HIS          
SEQRES  13 B  195  ALA LEU GLY ILE ARG GLY ILE VAL CYS ILE VAL GLU ARG          
SEQRES  14 B  195  PRO GLY ALA VAL TYR THR GLY ASP GLU ILE GLU VAL HIS          
SEQRES  15 B  195  SER TYR GLN ARG LYS VAL LYS ARG LYS ALA GLU ARG VAL          
MODRES 1ORU MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 1ORU MSE A    5  MET  SELENOMETHIONINE                                   
MODRES 1ORU MSE A   25  MET  SELENOMETHIONINE                                   
MODRES 1ORU MSE A   53  MET  SELENOMETHIONINE                                   
MODRES 1ORU MSE A   81  MET  SELENOMETHIONINE                                   
MODRES 1ORU MSE A  100  MET  SELENOMETHIONINE                                   
MODRES 1ORU MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 1ORU MSE B    5  MET  SELENOMETHIONINE                                   
MODRES 1ORU MSE B   25  MET  SELENOMETHIONINE                                   
MODRES 1ORU MSE B   53  MET  SELENOMETHIONINE                                   
MODRES 1ORU MSE B   81  MET  SELENOMETHIONINE                                   
MODRES 1ORU MSE B  100  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A   5      16                                                       
HET    MSE  A  25       8                                                       
HET    MSE  A  53       8                                                       
HET    MSE  A  81       8                                                       
HET    MSE  A 100      16                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B   5       8                                                       
HET    MSE  B  25       8                                                       
HET    MSE  B  53       8                                                       
HET    MSE  B  81       8                                                       
HET    MSE  B 100       8                                                       
HET    SO4  A 501       5                                                       
HET    SO4  B 502       5                                                       
HET    SO4  B 503       5                                                       
HET     CL  A 504       1                                                       
HET     CL  B 505       1                                                       
HET     CL  A 506       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   1  MSE    12(C5 H11 N O2 SE)                                           
FORMUL   3  SO4    3(O4 S 2-)                                                   
FORMUL   6   CL    3(CL 1-)                                                     
FORMUL   9  HOH   *365(H2 O)                                                    
HELIX    1   1 ILE A   71  GLY A   82  1                                  12    
HELIX    2   2 LEU A   87  GLY A   92  5                                   6    
HELIX    3   3 ASP A  102  LEU A  106  5                                   5    
HELIX    4   4 CYS A  129  TYR A  140  1                                  12    
HELIX    5   5 LYS A  145  ALA A  154  1                                  10    
HELIX    6   6 ILE B   71  GLY B   82  1                                  12    
HELIX    7   7 LEU B   87  GLY B   92  5                                   6    
HELIX    8   8 ASP B  102  LEU B  106  5                                   5    
HELIX    9   9 CYS B  129  TYR B  140  1                                  12    
HELIX   10  10 LYS B  145  LEU B  155  1                                  11    
SHEET    1   A 9 LYS A  23  MSE A  25  0                                        
SHEET    2   A 9 TRP A   2  ILE A  14 -1  O  LEU A  12   N  MSE A  25           
SHEET    3   A 9 GLU A 175  TYR A 181 -1  N  ILE A 176   O  ALA A   7           
SHEET    4   A 9 ARG A 111  ILE A 113 -1  O  ARG A 111   N  HIS A 179           
SHEET    5   A 9 ALA A 119  GLU A 125 -1  N  LEU A 120   O  ILE A 112           
SHEET    6   A 9 ILE A 160  ARG A 166 -1  O  VAL A 161   N  GLU A 123           
SHEET    7   A 9 ILE A  66  SER A  70 -1  O  ILE A  66   N  CYS A 162           
SHEET    8   A 9 VAL A  95  SER A  98  1  O  VAL A  95   N  VAL A  69           
SHEET    9   A 9 TRP A   2  ILE A  14 -1  O  LYS A   8   N  SER A  98           
SHEET    1   B 2 LYS A  27  PHE A  30  0                                        
SHEET    2   B 2 GLY A 168  TYR A 171 -1  O  GLY A 168   N  PHE A  30           
SHEET    1   C 2 THR A  44  LYS A  46  0                                        
SHEET    2   C 2 GLU A  59  PHE A  61 -1  N  ILE A  60   O  LYS A  45           
SHEET    1   D 9 LYS B  23  GLN B  24  0                                        
SHEET    2   D 9 TRP B   2  ILE B  14 -1  O  ILE B  14   N  LYS B  23           
SHEET    3   D 9 GLU B 175  TYR B 181 -1  N  ILE B 176   O  ALA B   7           
SHEET    4   D 9 ARG B 111  ILE B 113 -1  O  ARG B 111   N  HIS B 179           
SHEET    5   D 9 ALA B 119  GLU B 125 -1  N  LEU B 120   O  ILE B 112           
SHEET    6   D 9 ILE B 160  ARG B 166 -1  O  VAL B 161   N  GLU B 123           
SHEET    7   D 9 ILE B  66  SER B  70 -1  O  ILE B  66   N  CYS B 162           
SHEET    8   D 9 VAL B  95  SER B  98  1  O  VAL B  95   N  VAL B  69           
SHEET    9   D 9 TRP B   2  ILE B  14 -1  N  LYS B   8   O  SER B  98           
SHEET    1   E 2 LYS B  27  PHE B  30  0                                        
SHEET    2   E 2 GLY B 168  TYR B 171 -1  O  GLY B 168   N  PHE B  30           
SHEET    1   F 2 THR B  44  LYS B  46  0                                        
SHEET    2   F 2 GLU B  59  PHE B  61 -1  N  ILE B  60   O  LYS B  45           
LINK         C   MSE A   1                 N   TRP A   2     1555   1555  1.33  
LINK         C   ARG A   4                 N  BMSE A   5     1555   1555  1.33  
LINK         C   ARG A   4                 N  AMSE A   5     1555   1555  1.33  
LINK         C  BMSE A   5                 N   THR A   6     1555   1555  1.33  
LINK         C  AMSE A   5                 N   THR A   6     1555   1555  1.33  
LINK         C   GLN A  24                 N   MSE A  25     1555   1555  1.33  
LINK         C   MSE A  25                 N  AASP A  26     1555   1555  1.33  
LINK         C   MSE A  25                 N  BASP A  26     1555   1555  1.33  
LINK         C   PRO A  52                 N   MSE A  53     1555   1555  1.33  
LINK         C   MSE A  53                 N   PHE A  54     1555   1555  1.33  
LINK         C   LYS A  80                 N   MSE A  81     1555   1555  1.33  
LINK         C   MSE A  81                 N   GLY A  82     1555   1555  1.33  
LINK         C   GLY A  99                 N  AMSE A 100     1555   1555  1.33  
LINK         C   GLY A  99                 N  BMSE A 100     1555   1555  1.33  
LINK         C  BMSE A 100                 N   PRO A 101     1555   1555  1.35  
LINK         C  AMSE A 100                 N   PRO A 101     1555   1555  1.34  
LINK         C   MSE B   1                 N   TRP B   2     1555   1555  1.33  
LINK         C   ARG B   4                 N   MSE B   5     1555   1555  1.33  
LINK         C   MSE B   5                 N   THR B   6     1555   1555  1.33  
LINK         C  BGLN B  24                 N   MSE B  25     1555   1555  1.33  
LINK         C  AGLN B  24                 N   MSE B  25     1555   1555  1.33  
LINK         C   MSE B  25                 N   ASP B  26     1555   1555  1.33  
LINK         C   PRO B  52                 N   MSE B  53     1555   1555  1.33  
LINK         C   MSE B  53                 N   PHE B  54     1555   1555  1.33  
LINK         C   LYS B  80                 N   MSE B  81     1555   1555  1.33  
LINK         C   MSE B  81                 N   GLY B  82     1555   1555  1.33  
LINK         C   GLY B  99                 N   MSE B 100     1555   1555  1.33  
LINK         C   MSE B 100                 N   PRO B 101     1555   1555  1.34  
SITE     1 AC1  4 HIS A  40  LYS A  45  ARG A  50  HOH A 623                    
SITE     1 AC2  5 ARG A 166  LYS B   8  THR B  58  GLU B  59                    
SITE     2 AC2  5 GLY B 173                                                     
SITE     1 AC3  6 LYS B  45  ARG B  50  ARG B  64  HOH B 565                    
SITE     2 AC3  6 HOH B 593  HOH B 674                                          
SITE     1 AC4  5 ARG B  50  ASP B 127  CYS B 129  PRO B 132                    
SITE     2 AC4  5 ARG B 158                                                     
SITE     1 AC5  4 ARG A  50  CYS A 129  PRO A 132  ARG A 158                    
CRYST1   42.652   87.202  122.249  90.00  90.00  90.00 P 21 21 21    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      0.023446  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011468  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008180        0.00000                         
HETATM    1  N   MSE A   1      19.243  53.500  40.831  1.00 61.98           N  
HETATM    2  CA  MSE A   1      19.362  52.783  39.527  1.00 64.78           C  
HETATM    3  C   MSE A   1      19.021  53.727  38.379  1.00 58.91           C  
HETATM    4  O   MSE A   1      18.932  53.312  37.220  1.00 57.23           O  
HETATM    5  CB  MSE A   1      18.413  51.588  39.496  1.00 73.05           C  
HETATM    6  CG  MSE A   1      16.970  51.962  39.768  1.00 80.90           C  
HETATM    7 SE   MSE A   1      15.782  50.448  39.729  0.53 91.66          SE  
HETATM    8  CE  MSE A   1      14.980  50.727  37.996  1.00 94.66           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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