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Database: PDB
Entry: 2OEE
LinkDB: 2OEE
Original site: 2OEE 
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   29-DEC-06   2OEE              
TITLE     YHEA FROM BACILLUS SUBTILIS                                           
CAVEAT     2OEE    CHIRALITY ERRORS AT RESIDUES A50, A71, A72                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UPF0342 PROTEIN YHEA;                                      
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 STRAIN: 168;                                                         
SOURCE   5 GENE: YHEA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    YHEA, MCSG, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, 
KEYWDS   2 MIDWEST CENTER FOR STRUCTURAL GENOMICS, UNKNOWN FUNCTION             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.A.BINKOWSKI,M.BOROVILOS,J.ABDULLAH,A.JOACHIMIAK,MIDWEST CENTER FOR  
AUTHOR   2 STRUCTURAL GENOMICS (MCSG)                                           
REVDAT   3   13-JUL-11 2OEE    1       VERSN                                    
REVDAT   2   24-FEB-09 2OEE    1       VERSN                                    
REVDAT   1   30-JAN-07 2OEE    0                                                
JRNL        AUTH   T.A.BINKOWSKI,M.BOROVILOS,J.ABDULLAH,A.JOACHIMIAK            
JRNL        TITL   YHEA FROM BACILLUS SUBTILIS                                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.96 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.13                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 19402                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1046                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.96                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.01                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1388                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.18                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2230                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 66                           
REMARK   3   BIN FREE R VALUE                    : 0.3000                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1531                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 271                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.50000                                              
REMARK   3    B22 (A**2) : 0.50000                                              
REMARK   3    B33 (A**2) : -0.75000                                             
REMARK   3    B12 (A**2) : 0.25000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.168         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.153         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.919                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1551 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2078 ; 1.345 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   183 ;13.560 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    89 ;34.538 ;25.506       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   311 ;15.131 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;14.012 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   229 ; 0.323 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1163 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   778 ; 0.231 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1115 ; 0.301 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   242 ; 0.136 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     6 ; 0.124 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   158 ; 0.450 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    35 ; 0.151 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):     3 ; 0.063 ; 0.200       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   922 ; 2.223 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1479 ; 2.850 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   629 ; 2.516 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   598 ; 3.943 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2OEE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041030.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-DEC-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 150                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97944                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SBC                                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19402                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.960                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0, VAPOR DIFFUSION, SITTING DROP,   
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      110.89867            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       55.44933            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       55.44933            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      110.89867            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). AUTHORS STATE THAT THE                 
REMARK 300 BIOLOGICAL UNIT OF THIS PROTEIN IS UNKNOWN.                          
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,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 3490 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 3480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       92.22478            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       55.44933            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MSE A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ARG A    51                                                      
REMARK 465     LEU A    52                                                      
REMARK 465     GLN A    53                                                      
REMARK 465     GLN A    54                                                      
REMARK 465     LYS A    55                                                      
REMARK 465     GLN A    56                                                      
REMARK 465     MSE A    57                                                      
REMARK 465     ALA A    58                                                      
REMARK 465     GLY A    59                                                      
REMARK 465     GLU A    60                                                      
REMARK 465     GLU A    61                                                      
REMARK 465     ILE A    62                                                      
REMARK 465     THR A    63                                                      
REMARK 465     GLN A    64                                                      
REMARK 465     GLU A    65                                                      
REMARK 465     GLU A    66                                                      
REMARK 465     VAL A    67                                                      
REMARK 465     THR A    68                                                      
REMARK 465     GLY A   113                                                      
REMARK 465     SER A   114                                                      
REMARK 465     VAL A   115                                                      
REMARK 465     GLU A   116                                                      
REMARK 465     GLY A   117                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     LEU B    52                                                      
REMARK 465     GLN B    53                                                      
REMARK 465     GLN B    54                                                      
REMARK 465     LYS B    55                                                      
REMARK 465     GLN B    56                                                      
REMARK 465     MSE B    57                                                      
REMARK 465     ALA B    58                                                      
REMARK 465     GLY B    59                                                      
REMARK 465     GLU B    60                                                      
REMARK 465     GLU B    61                                                      
REMARK 465     ILE B    62                                                      
REMARK 465     THR B    63                                                      
REMARK 465     GLN B    64                                                      
REMARK 465     GLU B    65                                                      
REMARK 465     GLU B    66                                                      
REMARK 465     VAL B    67                                                      
REMARK 465     THR B    68                                                      
REMARK 465     GLY B   113                                                      
REMARK 465     SER B   114                                                      
REMARK 465     VAL B   115                                                      
REMARK 465     GLU B   116                                                      
REMARK 465     GLY B   117                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CZ   PHE A     5     CD1  LEU A   100     4555     1.82            
REMARK 500   CE2  PHE A     5     CD1  LEU A   100     4555     1.85            
REMARK 500   CZ   PHE B     5     CD1  LEU B   100     5675     1.96            
REMARK 500   CE2  PHE B     5     CD1  LEU B   100     5675     2.01            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  46   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
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    ALA A  70      -72.54    -31.40                                   
REMARK 500    LYS A  72     -122.76    152.23                                   
REMARK 500    THR A  73      -35.31    -35.91                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLN A   49     LEU A   50                  110.59                    
REMARK 500 ALA A   70     GLN A   71                 -106.61                    
REMARK 500 LYS A   72     THR A   73                  131.39                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LEU A  50       -27.0      L          D   WRONG HAND              
REMARK 500    GLN A  71       -25.6      L          D   WRONG HAND              
REMARK 500    LYS A  72       -27.5      L          D   WRONG HAND              
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 B 181        DISTANCE =  6.31 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 118  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 120   O                                                      
REMARK 620 2 GLU A  81   OE1 107.1                                              
REMARK 620 3 GLU A  81   OE2  76.7  52.6                                        
REMARK 620 4 HOH A 155   O    78.9 171.2 136.1                                  
REMARK 620 5 HOH A 151   O    88.3  77.4 118.4  96.6                            
REMARK 620 6 GLU B  13   OE2 163.1  89.4 117.8  84.3  91.6                      
REMARK 620 7 GLU B  13   OE1 123.5  99.5  82.0  81.8 146.6  55.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 118  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  81   OE1                                                    
REMARK 620 2 GLU B  81   OE2  52.4                                              
REMARK 620 3 HOH B 123   O   107.8  81.0                                        
REMARK 620 4 GLU A  13   OE2  88.7 118.2 160.4                                  
REMARK 620 5 GLU A  13   OE1 100.4  83.3 128.3  55.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 118                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 118                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: APC1174   RELATED DB: TARGETDB                           
DBREF  2OEE A    1   117  UNP    O07542   YHEA_BACSU       1    117             
DBREF  2OEE B    1   117  UNP    O07542   YHEA_BACSU       1    117             
SEQADV 2OEE MSE A    1  UNP  O07542    MET     1 MODIFIED RESIDUE               
SEQADV 2OEE MSE A   41  UNP  O07542    MET    41 MODIFIED RESIDUE               
SEQADV 2OEE MSE A   57  UNP  O07542    MET    57 MODIFIED RESIDUE               
SEQADV 2OEE MSE A   87  UNP  O07542    MET    87 MODIFIED RESIDUE               
SEQADV 2OEE MSE A   93  UNP  O07542    MET    93 MODIFIED RESIDUE               
SEQADV 2OEE MSE A   95  UNP  O07542    MET    95 MODIFIED RESIDUE               
SEQADV 2OEE MSE A  105  UNP  O07542    MET   105 MODIFIED RESIDUE               
SEQADV 2OEE MSE B    1  UNP  O07542    MET     1 MODIFIED RESIDUE               
SEQADV 2OEE MSE B   41  UNP  O07542    MET    41 MODIFIED RESIDUE               
SEQADV 2OEE MSE B   57  UNP  O07542    MET    57 MODIFIED RESIDUE               
SEQADV 2OEE MSE B   87  UNP  O07542    MET    87 MODIFIED RESIDUE               
SEQADV 2OEE MSE B   93  UNP  O07542    MET    93 MODIFIED RESIDUE               
SEQADV 2OEE MSE B   95  UNP  O07542    MET    95 MODIFIED RESIDUE               
SEQADV 2OEE MSE B  105  UNP  O07542    MET   105 MODIFIED RESIDUE               
SEQRES   1 A  117  MSE ALA VAL ASN PHE TYR ASP VAL ALA TYR ASP LEU GLU          
SEQRES   2 A  117  ASN ALA LEU ARG GLY SER GLU GLU PHE THR ARG LEU LYS          
SEQRES   3 A  117  ASN LEU TYR ASP GLU VAL ASN ALA ASP GLU SER ALA LYS          
SEQRES   4 A  117  ARG MSE PHE GLU ASN PHE ARG ASP VAL GLN LEU ARG LEU          
SEQRES   5 A  117  GLN GLN LYS GLN MSE ALA GLY GLU GLU ILE THR GLN GLU          
SEQRES   6 A  117  GLU VAL THR GLN ALA GLN LYS THR VAL ALA LEU VAL GLN          
SEQRES   7 A  117  GLN HIS GLU LYS ILE SER GLN LEU MSE GLU ALA GLU GLN          
SEQRES   8 A  117  ARG MSE SER MSE LEU ILE GLY GLU LEU ASN LYS ILE ILE          
SEQRES   9 A  117  MSE LYS PRO LEU GLU GLU LEU TYR GLY SER VAL GLU GLY          
SEQRES   1 B  117  MSE ALA VAL ASN PHE TYR ASP VAL ALA TYR ASP LEU GLU          
SEQRES   2 B  117  ASN ALA LEU ARG GLY SER GLU GLU PHE THR ARG LEU LYS          
SEQRES   3 B  117  ASN LEU TYR ASP GLU VAL ASN ALA ASP GLU SER ALA LYS          
SEQRES   4 B  117  ARG MSE PHE GLU ASN PHE ARG ASP VAL GLN LEU ARG LEU          
SEQRES   5 B  117  GLN GLN LYS GLN MSE ALA GLY GLU GLU ILE THR GLN GLU          
SEQRES   6 B  117  GLU VAL THR GLN ALA GLN LYS THR VAL ALA LEU VAL GLN          
SEQRES   7 B  117  GLN HIS GLU LYS ILE SER GLN LEU MSE GLU ALA GLU GLN          
SEQRES   8 B  117  ARG MSE SER MSE LEU ILE GLY GLU LEU ASN LYS ILE ILE          
SEQRES   9 B  117  MSE LYS PRO LEU GLU GLU LEU TYR GLY SER VAL GLU GLY          
MODRES 2OEE MSE A   41  MET  SELENOMETHIONINE                                   
MODRES 2OEE MSE A   87  MET  SELENOMETHIONINE                                   
MODRES 2OEE MSE A   93  MET  SELENOMETHIONINE                                   
MODRES 2OEE MSE A   95  MET  SELENOMETHIONINE                                   
MODRES 2OEE MSE A  105  MET  SELENOMETHIONINE                                   
MODRES 2OEE MSE B   41  MET  SELENOMETHIONINE                                   
MODRES 2OEE MSE B   87  MET  SELENOMETHIONINE                                   
MODRES 2OEE MSE B   93  MET  SELENOMETHIONINE                                   
MODRES 2OEE MSE B   95  MET  SELENOMETHIONINE                                   
MODRES 2OEE MSE B  105  MET  SELENOMETHIONINE                                   
HET    MSE  A  41       8                                                       
HET    MSE  A  87       8                                                       
HET    MSE  A  93       8                                                       
HET    MSE  A  95      13                                                       
HET    MSE  A 105       8                                                       
HET    MSE  B  41       8                                                       
HET    MSE  B  87       8                                                       
HET    MSE  B  93       8                                                       
HET    MSE  B  95       8                                                       
HET    MSE  B 105       8                                                       
HET     CA  A 118       1                                                       
HET     CA  B 118       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CA CALCIUM ION                                                      
FORMUL   1  MSE    10(C5 H11 N O2 SE)                                           
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   5  HOH   *271(H2 O)                                                    
HELIX    1   1 ASN A    4  GLY A   18  1                                  15    
HELIX    2   2 SER A   19  ASP A   35  1                                  17    
HELIX    3   3 ASP A   35  GLN A   49  1                                  15    
HELIX    4   4 GLN A   69  GLN A   79  1                                  11    
HELIX    5   5 HIS A   80  MSE A  105  1                                  26    
HELIX    6   6 MSE A  105  TYR A  112  1                                   8    
HELIX    7   7 ASN B    4  GLY B   18  1                                  15    
HELIX    8   8 SER B   19  ASP B   35  1                                  17    
HELIX    9   9 ASP B   35  ARG B   51  1                                  17    
HELIX   10  10 GLN B   69  GLN B   79  1                                  11    
HELIX   11  11 HIS B   80  TYR B  112  1                                  33    
LINK         C   ARG A  40                 N   MSE A  41     1555   1555  1.33  
LINK         C   MSE A  41                 N   PHE A  42     1555   1555  1.33  
LINK         C   LEU A  86                 N   MSE A  87     1555   1555  1.33  
LINK         C   MSE A  87                 N   GLU A  88     1555   1555  1.33  
LINK         C   ARG A  92                 N   MSE A  93     1555   1555  1.33  
LINK         C   MSE A  93                 N   SER A  94     1555   1555  1.33  
LINK         C   SER A  94                 N   MSE A  95     1555   1555  1.33  
LINK         C   MSE A  95                 N   LEU A  96     1555   1555  1.33  
LINK         C   ILE A 104                 N   MSE A 105     1555   1555  1.33  
LINK         C   MSE A 105                 N   LYS A 106     1555   1555  1.33  
LINK        CA    CA A 118                 O   HOH A 120     1555   1555  2.50  
LINK        CA    CA A 118                 OE1 GLU A  81     1555   1555  2.41  
LINK        CA    CA A 118                 OE2 GLU A  81     1555   1555  2.52  
LINK        CA    CA A 118                 O   HOH A 155     1555   1555  2.33  
LINK        CA    CA A 118                 O   HOH A 151     1555   1555  2.35  
LINK         C   ARG B  40                 N   MSE B  41     1555   1555  1.33  
LINK         C   MSE B  41                 N   PHE B  42     1555   1555  1.32  
LINK         C   LEU B  86                 N   MSE B  87     1555   1555  1.33  
LINK         C   MSE B  87                 N   GLU B  88     1555   1555  1.33  
LINK         C   ARG B  92                 N   MSE B  93     1555   1555  1.33  
LINK         C   MSE B  93                 N   SER B  94     1555   1555  1.33  
LINK         C   SER B  94                 N   MSE B  95     1555   1555  1.33  
LINK         C   MSE B  95                 N   LEU B  96     1555   1555  1.33  
LINK         C   ILE B 104                 N   MSE B 105     1555   1555  1.33  
LINK         C   MSE B 105                 N   LYS B 106     1555   1555  1.34  
LINK        CA    CA B 118                 OE1 GLU B  81     1555   1555  2.42  
LINK        CA    CA B 118                 OE2 GLU B  81     1555   1555  2.55  
LINK        CA    CA B 118                 O   HOH B 123     1555   1555  2.42  
LINK        CA    CA A 118                 OE2 GLU B  13     1555   5675  2.34  
LINK        CA    CA A 118                 OE1 GLU B  13     1555   5675  2.45  
LINK        CA    CA B 118                 OE2 GLU A  13     1555   4555  2.35  
LINK        CA    CA B 118                 OE1 GLU A  13     1555   4555  2.38  
CISPEP   1 GLN A   71    LYS A   72          0        -1.86                     
SITE     1 AC1  5 GLU A  81  HOH A 120  HOH A 151  HOH A 155                    
SITE     2 AC1  5 GLU B  13                                                     
SITE     1 AC2  3 GLU A  13  GLU B  81  HOH B 123                               
CRYST1   53.246   53.246  166.348  90.00  90.00 120.00 P 32 2 1     12          
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      0.018781  0.010843  0.000000        0.00000                         
SCALE2      0.000000  0.021686  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006011        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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