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Database: PDB
Entry: 4M7S
LinkDB: 4M7S
Original site: 4M7S 
HEADER    METAL BINDING PROTEIN                   12-AUG-13   4M7S              
TITLE     CRYSTAL STRUCTURE OF SEMET BTRN IN AN OPEN CONFORMATION               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BTRN;                                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: BTRN PROTEIN;                                               
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS CIRCULANS;                             
SOURCE   3 ORGANISM_TAXID: 1397;                                                
SOURCE   4 GENE: BTRN;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ADOMET RADICAL FOLD, METAL BINDING PROTEIN                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.J.GOLDMAN,C.L.DRENNAN                                               
REVDAT   2   05-FEB-14 4M7S    1       JRNL                                     
REVDAT   1   02-OCT-13 4M7S    0                                                
JRNL        AUTH   P.J.GOLDMAN,T.L.GROVE,S.J.BOOKER,C.L.DRENNAN                 
JRNL        TITL   X-RAY ANALYSIS OF BUTIROSIN BIOSYNTHETIC ENZYME BTRN         
JRNL        TITL 2 REDEFINES STRUCTURAL MOTIFS FOR ADOMET RADICAL CHEMISTRY.    
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 110 15949 2013              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   24048029                                                     
JRNL        DOI    10.1073/PNAS.1312228110                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.02 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.51                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 13343                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1291                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.5197 -  4.2035    1.00     2728   149  0.1729 0.2044        
REMARK   3     2  4.2035 -  3.3370    1.00     2758   142  0.1526 0.2007        
REMARK   3     3  3.3370 -  2.9154    1.00     2746   147  0.1684 0.2331        
REMARK   3     4  2.9154 -  2.6489    1.00     2736   145  0.1653 0.2115        
REMARK   3     5  2.6489 -  2.4591    1.00     2740   143  0.1661 0.2024        
REMARK   3     6  2.4591 -  2.3141    1.00     2757   145  0.1660 0.2161        
REMARK   3     7  2.3141 -  2.1982    1.00     2727   148  0.1760 0.2482        
REMARK   3     8  2.1982 -  2.1025    0.99     2730   145  0.2046 0.2646        
REMARK   3     9  2.1025 -  2.0216    0.88     2436   127  0.2313 0.2960        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.610           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.51                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.38                          
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           1777                                  
REMARK   3   ANGLE     :  1.129           2410                                  
REMARK   3   CHIRALITY :  0.084            268                                  
REMARK   3   PLANARITY :  0.004            304                                  
REMARK   3   DIHEDRAL  : 17.208            657                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 1:37)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 114.7691 -20.8513  10.8999              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3553 T22:   0.2477                                     
REMARK   3      T33:   0.2313 T12:   0.0480                                     
REMARK   3      T13:  -0.0416 T23:  -0.0475                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5697 L22:   4.0611                                     
REMARK   3      L33:   1.0437 L12:   1.2777                                     
REMARK   3      L13:  -0.6079 L23:  -0.2259                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0457 S12:   0.0539 S13:  -0.2294                       
REMARK   3      S21:  -0.0507 S22:   0.0186 S23:  -0.1664                       
REMARK   3      S31:   0.2841 S32:   0.0511 S33:  -0.0564                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 38:107)                          
REMARK   3    ORIGIN FOR THE GROUP (A): 110.2061 -13.1676  19.2500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1607 T22:   0.1565                                     
REMARK   3      T33:   0.1510 T12:   0.0329                                     
REMARK   3      T13:  -0.0274 T23:  -0.0247                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8303 L22:   4.6268                                     
REMARK   3      L33:   4.1628 L12:   2.0284                                     
REMARK   3      L13:  -0.7585 L23:  -2.8084                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0632 S12:  -0.1013 S13:   0.0558                       
REMARK   3      S21:   0.1226 S22:   0.0073 S23:   0.1179                       
REMARK   3      S31:  -0.1957 S32:  -0.0539 S33:  -0.0835                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 108:120)                         
REMARK   3    ORIGIN FOR THE GROUP (A): 103.5411 -24.7226  17.3760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2203 T22:   0.2707                                     
REMARK   3      T33:   0.3261 T12:  -0.0636                                     
REMARK   3      T13:  -0.0410 T23:  -0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2012 L22:   7.6632                                     
REMARK   3      L33:   6.2910 L12:  -5.7857                                     
REMARK   3      L13:   0.2781 L23:   1.1281                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3218 S12:   0.3171 S13:  -0.9409                       
REMARK   3      S21:  -0.4571 S22:  -0.3493 S23:   0.6950                       
REMARK   3      S31:   0.3841 S32:  -0.6183 S33:   0.0799                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 135:170)                         
REMARK   3    ORIGIN FOR THE GROUP (A): 101.4104 -23.6189   4.9544              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3301 T22:   0.4858                                     
REMARK   3      T33:   0.3886 T12:  -0.1431                                     
REMARK   3      T13:  -0.1275 T23:  -0.0695                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9877 L22:   4.5833                                     
REMARK   3      L33:   3.6293 L12:   1.5369                                     
REMARK   3      L13:  -3.6379 L23:  -2.4288                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3716 S12:   0.2305 S13:  -0.2610                       
REMARK   3      S21:  -0.1203 S22:   0.2290 S23:   0.0614                       
REMARK   3      S31:   0.5725 S32:  -0.9001 S33:   0.4106                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 171:228)                         
REMARK   3    ORIGIN FOR THE GROUP (A): 116.1808 -12.3211  -0.8513              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2690 T22:   0.2849                                     
REMARK   3      T33:   0.1714 T12:  -0.0397                                     
REMARK   3      T13:   0.0145 T23:   0.0164                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8297 L22:   4.1494                                     
REMARK   3      L33:   5.3141 L12:   0.0844                                     
REMARK   3      L13:   1.4991 L23:   0.7443                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1476 S12:   0.4940 S13:   0.0104                       
REMARK   3      S21:  -0.6814 S22:   0.1750 S23:  -0.0604                       
REMARK   3      S31:  -0.2491 S32:   0.4140 S33:  -0.0233                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 229:249)                         
REMARK   3    ORIGIN FOR THE GROUP (A): 104.6389 -21.8535  -6.3811              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3948 T22:   0.3212                                     
REMARK   3      T33:   0.4995 T12:  -0.0463                                     
REMARK   3      T13:  -0.0808 T23:  -0.0836                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4767 L22:   4.6004                                     
REMARK   3      L33:   8.0651 L12:   0.5048                                     
REMARK   3      L13:  -3.6959 L23:  -1.7561                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2163 S12:   0.2497 S13:  -0.7085                       
REMARK   3      S21:  -0.0143 S22:   0.1691 S23:   1.0383                       
REMARK   3      S31:   0.1015 S32:  -0.7190 S33:   0.0412                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4M7S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-AUG-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB081573.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : DEC-11                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
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                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25638                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.020                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
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) : 2.02                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.0                               
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         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13-18 % JEFFAMINE ED-2001 PH 7.0         
REMARK 280  (HAMPTON RESEARCH) AND 100 MM IMIDAZOLE PH 7.0, VAPOR DIFFUSION,    
REMARK 280  SITTING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       49.70400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       21.02900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       49.70400            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       21.02900            
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 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 654  LIES ON A SPECIAL POSITION.                          
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    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     ARG A    30                                                      
REMARK 465     LYS A    31                                                      
REMARK 465     GLU A    32                                                      
REMARK 465     LYS A   121                                                      
REMARK 465     HIS A   122                                                      
REMARK 465     LYS A   123                                                      
REMARK 465     PHE A   124                                                      
REMARK 465     ARG A   125                                                      
REMARK 465     GLY A   126                                                      
REMARK 465     VAL A   127                                                      
REMARK 465     TYR A   128                                                      
REMARK 465     ASP A   129                                                      
REMARK 465     GLN A   130                                                      
REMARK 465     LEU A   131                                                      
REMARK 465     ALA A   132                                                      
REMARK 465     GLY A   133                                                      
REMARK 465     ALA A   134                                                      
REMARK 465     ASP A   146                                                      
REMARK 465     LEU A   147                                                      
REMARK 465     VAL A   148                                                      
REMARK 465     LEU A   149                                                      
REMARK 465     SER A   150                                                      
REMARK 465     ASN A   151                                                      
REMARK 465     ARG A   152                                                      
REMARK 465     GLY A   153                                                      
REMARK 465     GLY A   154                                                      
REMARK 465     ILE A   155                                                      
REMARK 465     LEU A   156                                                      
REMARK 465     ASP A   157                                                      
REMARK 465     ASN A   158                                                      
REMARK 465     ILE A   159                                                      
REMARK 465     PRO A   160                                                      
REMARK 465     GLN A   161                                                      
REMARK 465     LEU A   250                                                      
REMARK 465     ASN A   251                                                      
REMARK 465     SER A   252                                                      
REMARK 465     SER A   253                                                      
REMARK 465     SER A   254                                                      
REMARK 465     VAL A   255                                                      
REMARK 465     ASP A   256                                                      
REMARK 465     LYS A   257                                                      
REMARK 465     LEU A   258                                                      
REMARK 465     ALA A   259                                                      
REMARK 465     ALA A   260                                                      
REMARK 465     ALA A   261                                                      
REMARK 465     LEU A   262                                                      
REMARK 465     GLU A   263                                                      
REMARK 465     HIS A   264                                                      
REMARK 465     HIS A   265                                                      
REMARK 465     HIS A   266                                                      
REMARK 465     HIS A   267                                                      
REMARK 465     HIS A   268                                                      
REMARK 465     HIS A   269                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     MSE A   1    CG  SE    CE                                        
REMARK 470     SER A  26    OG                                                  
REMARK 470     VAL A  27    CG1  CG2                                            
REMARK 470     ASP A 135    CG   OD1  OD2                                       
REMARK 470     LYS A 164    CG   CD   CE   NZ                                   
REMARK 470     TYR A 248    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL A 249    CG1  CG2                                            
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    PHE A  61      -75.31   -140.17                                   
REMARK 500    HIS A 225       52.93    -95.47                                   
REMARK 500    TYR A 248     -143.75   -119.89                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                             SF4 A 501  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 232   SG                                                     
REMARK 620 2 SF4 A 501   S1  111.2                                              
REMARK 620 3 SF4 A 501   S3  111.0 107.8                                        
REMARK 620 4 SF4 A 501   S4  115.7 105.1 105.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 502  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  20   SG                                                     
REMARK 620 2 SF4 A 502   S1  110.2                                              
REMARK 620 3 SF4 A 502   S3  118.6 103.9                                        
REMARK 620 4 SF4 A 502   S4  109.5 107.1 106.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 502  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  16   SG                                                     
REMARK 620 2 SF4 A 502   S2  117.7                                              
REMARK 620 3 SF4 A 502   S3  102.9 105.9                                        
REMARK 620 4 SF4 A 502   S4  117.2 105.7 106.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 502  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  23   SG                                                     
REMARK 620 2 SF4 A 502   S1  107.7                                              
REMARK 620 3 SF4 A 502   S2  117.5 104.7                                        
REMARK 620 4 SF4 A 502   S4  113.5 107.2 105.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 501  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 169   SG                                                     
REMARK 620 2 SF4 A 501   S1  112.6                                              
REMARK 620 3 SF4 A 501   S2  108.2 106.6                                        
REMARK 620 4 SF4 A 501   S3  117.0 107.6 104.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 501  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 235   SG                                                     
REMARK 620 2 SF4 A 501   S2  116.0                                              
REMARK 620 3 SF4 A 501   S3  115.2 104.3                                        
REMARK 620 4 SF4 A 501   S4  107.6 107.2 106.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 501  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 187   SG                                                     
REMARK 620 2 SF4 A 501   S1  115.0                                              
REMARK 620 3 SF4 A 501   S2  102.6 106.4                                        
REMARK 620 4 SF4 A 501   S4  119.0 105.9 107.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 505                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4M7T   RELATED DB: PDB                                   
DBREF  4M7S A    1   250  UNP    Q8G907   Q8G907_BACCI     1    250             
SEQADV 4M7S ASN A  251  UNP  Q8G907              EXPRESSION TAG                 
SEQADV 4M7S SER A  252  UNP  Q8G907              EXPRESSION TAG                 
SEQADV 4M7S SER A  253  UNP  Q8G907              EXPRESSION TAG                 
SEQADV 4M7S SER A  254  UNP  Q8G907              EXPRESSION TAG                 
SEQADV 4M7S VAL A  255  UNP  Q8G907              EXPRESSION TAG                 
SEQADV 4M7S ASP A  256  UNP  Q8G907              EXPRESSION TAG                 
SEQADV 4M7S LYS A  257  UNP  Q8G907              EXPRESSION TAG                 
SEQADV 4M7S LEU A  258  UNP  Q8G907              EXPRESSION TAG                 
SEQADV 4M7S ALA A  259  UNP  Q8G907              EXPRESSION TAG                 
SEQADV 4M7S ALA A  260  UNP  Q8G907              EXPRESSION TAG                 
SEQADV 4M7S ALA A  261  UNP  Q8G907              EXPRESSION TAG                 
SEQADV 4M7S LEU A  262  UNP  Q8G907              EXPRESSION TAG                 
SEQADV 4M7S GLU A  263  UNP  Q8G907              EXPRESSION TAG                 
SEQADV 4M7S HIS A  264  UNP  Q8G907              EXPRESSION TAG                 
SEQADV 4M7S HIS A  265  UNP  Q8G907              EXPRESSION TAG                 
SEQADV 4M7S HIS A  266  UNP  Q8G907              EXPRESSION TAG                 
SEQADV 4M7S HIS A  267  UNP  Q8G907              EXPRESSION TAG                 
SEQADV 4M7S HIS A  268  UNP  Q8G907              EXPRESSION TAG                 
SEQADV 4M7S HIS A  269  UNP  Q8G907              EXPRESSION TAG                 
SEQRES   1 A  269  MSE ASP LYS LEU PHE SER MSE ILE GLU VAL GLU VAL ASN          
SEQRES   2 A  269  SER GLN CYS ASN ARG THR CYS TRP TYR CYS PRO ASN SER          
SEQRES   3 A  269  VAL SER LYS ARG LYS GLU THR GLY GLU MSE ASP PRO ALA          
SEQRES   4 A  269  LEU TYR LYS THR LEU MSE GLU GLN LEU SER SER LEU ASP          
SEQRES   5 A  269  PHE ALA GLY ARG ILE SER PHE HIS PHE TYR GLY GLU PRO          
SEQRES   6 A  269  LEU LEU CYS LYS ASN LEU ASP LEU PHE VAL GLY MSE THR          
SEQRES   7 A  269  THR GLU TYR ILE PRO ARG ALA ARG PRO ILE ILE TYR THR          
SEQRES   8 A  269  ASN GLY ASP PHE LEU THR GLU LYS ARG LEU GLN THR LEU          
SEQRES   9 A  269  THR GLU LEU GLY ILE GLN LYS PHE ILE VAL THR GLN HIS          
SEQRES  10 A  269  ALA GLY ALA LYS HIS LYS PHE ARG GLY VAL TYR ASP GLN          
SEQRES  11 A  269  LEU ALA GLY ALA ASP LYS GLU LYS VAL VAL TYR LEU ASP          
SEQRES  12 A  269  HIS SER ASP LEU VAL LEU SER ASN ARG GLY GLY ILE LEU          
SEQRES  13 A  269  ASP ASN ILE PRO GLN ALA SER LYS ALA ASN MSE SER CYS          
SEQRES  14 A  269  MSE VAL PRO SER ASN LEU ALA VAL VAL THR VAL LEU GLY          
SEQRES  15 A  269  ASN VAL LEU PRO CYS PHE GLU ASP PHE ASN GLN LYS MSE          
SEQRES  16 A  269  VAL MSE GLY ASN ILE GLY GLU GLN HIS ILE SER ASP ILE          
SEQRES  17 A  269  TRP HIS ASN ASP LYS PHE THR SER PHE ARG LYS MSE LEU          
SEQRES  18 A  269  LYS GLU GLY HIS ARG GLY LYS SER ASP LEU CYS LYS ASN          
SEQRES  19 A  269  CYS ASN ASN VAL SER VAL GLN THR GLU GLU GLN TYR ASP          
SEQRES  20 A  269  TYR VAL LEU ASN SER SER SER VAL ASP LYS LEU ALA ALA          
SEQRES  21 A  269  ALA LEU GLU HIS HIS HIS HIS HIS HIS                          
MODRES 4M7S MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 4M7S MSE A    7  MET  SELENOMETHIONINE                                   
MODRES 4M7S MSE A   36  MET  SELENOMETHIONINE                                   
MODRES 4M7S MSE A   45  MET  SELENOMETHIONINE                                   
MODRES 4M7S MSE A   77  MET  SELENOMETHIONINE                                   
MODRES 4M7S MSE A  167  MET  SELENOMETHIONINE                                   
MODRES 4M7S MSE A  170  MET  SELENOMETHIONINE                                   
MODRES 4M7S MSE A  195  MET  SELENOMETHIONINE                                   
MODRES 4M7S MSE A  197  MET  SELENOMETHIONINE                                   
MODRES 4M7S MSE A  220  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       5                                                       
HET    MSE  A   7       8                                                       
HET    MSE  A  36       8                                                       
HET    MSE  A  45       8                                                       
HET    MSE  A  77       8                                                       
HET    MSE  A 167       8                                                       
HET    MSE  A 170       8                                                       
HET    MSE  A 195       8                                                       
HET    MSE  A 197       8                                                       
HET    MSE  A 220       8                                                       
HET    SF4  A 501       8                                                       
HET    SF4  A 502       8                                                       
HET    GOL  A 503       6                                                       
HET    GOL  A 504       6                                                       
HET    IMD  A 505       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     GOL GLYCEROL                                                         
HETNAM     IMD IMIDAZOLE                                                        
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MSE    10(C5 H11 N O2 SE)                                           
FORMUL   2  SF4    2(FE4 S4)                                                    
FORMUL   4  GOL    2(C3 H8 O3)                                                  
FORMUL   6  IMD    C3 H5 N2 1+                                                  
FORMUL   7  HOH   *57(H2 O)                                                     
HELIX    1   1 ASP A   37  LEU A   51  1                                  15    
HELIX    2   2 GLU A   64  CYS A   68  5                                   5    
HELIX    3   3 ASN A   70  ILE A   82  1                                  13    
HELIX    4   4 THR A   97  GLY A  108  1                                  12    
HELIX    5   5 ALA A  162  MSE A  167  5                                   6    
HELIX    6   6 MSE A  170  ASN A  174  1                                   5    
HELIX    7   7 HIS A  204  HIS A  210  1                                   7    
HELIX    8   8 ASN A  211  GLU A  223  1                                  13    
HELIX    9   9 HIS A  225  SER A  229  5                                   5    
HELIX   10  10 THR A  242  ASP A  247  5                                   6    
SHEET    1   A 8 VAL A 139  ASP A 143  0                                        
SHEET    2   A 8 LYS A 111  GLN A 116  1  N  VAL A 114   O  LEU A 142           
SHEET    3   A 8 ARG A  86  THR A  91  1  N  ILE A  89   O  ILE A 113           
SHEET    4   A 8 ARG A  56  SER A  58  1  N  ILE A  57   O  ILE A  88           
SHEET    5   A 8 MSE A   7  VAL A  10  1  N  VAL A  10   O  SER A  58           
SHEET    6   A 8 LEU A 175  VAL A 178  1  O  VAL A 178   N  GLU A   9           
SHEET    7   A 8 ASN A 183  LEU A 185 -1  O  LEU A 185   N  VAL A 177           
SHEET    8   A 8 GLY A 198  ASN A 199 -1  O  GLY A 198   N  VAL A 184           
LINK         C   MSE A   1                 N   ASP A   2     1555   1555  1.33  
LINK         C   SER A   6                 N   MSE A   7     1555   1555  1.33  
LINK         C   MSE A   7                 N   ILE A   8     1555   1555  1.33  
LINK         C   GLU A  35                 N   MSE A  36     1555   1555  1.33  
LINK         C   MSE A  36                 N   ASP A  37     1555   1555  1.33  
LINK         C   LEU A  44                 N   MSE A  45     1555   1555  1.33  
LINK         C   MSE A  45                 N   GLU A  46     1555   1555  1.33  
LINK         C   GLY A  76                 N   MSE A  77     1555   1555  1.33  
LINK         C   MSE A  77                 N   THR A  78     1555   1555  1.33  
LINK         C   ASN A 166                 N   MSE A 167     1555   1555  1.33  
LINK         C   MSE A 167                 N   SER A 168     1555   1555  1.32  
LINK         C   CYS A 169                 N   MSE A 170     1555   1555  1.33  
LINK         C   MSE A 170                 N   VAL A 171     1555   1555  1.33  
LINK         C   LYS A 194                 N   MSE A 195     1555   1555  1.33  
LINK         C   MSE A 195                 N   VAL A 196     1555   1555  1.33  
LINK         C   VAL A 196                 N   MSE A 197     1555   1555  1.33  
LINK         C   MSE A 197                 N   GLY A 198     1555   1555  1.32  
LINK         C   LYS A 219                 N   MSE A 220     1555   1555  1.33  
LINK         C   MSE A 220                 N   LEU A 221     1555   1555  1.33  
LINK         SG  CYS A 232                FE2  SF4 A 501     1555   1555  2.26  
LINK         SG  CYS A  20                FE2  SF4 A 502     1555   1555  2.35  
LINK         SG  CYS A  16                FE1  SF4 A 502     1555   1555  2.41  
LINK         SG  CYS A  23                FE3  SF4 A 502     1555   1555  2.42  
LINK         SG  CYS A 169                FE4  SF4 A 501     1555   1555  2.45  
LINK         SG  CYS A 235                FE1  SF4 A 501     1555   1555  2.47  
LINK         SG  CYS A 187                FE3  SF4 A 501     1555   1555  2.49  
CISPEP   1 SER A   26    VAL A   27          0         5.23                     
CISPEP   2 GLY A  119    ALA A  120          0        -2.63                     
CISPEP   3 ASP A  247    TYR A  248          0        -1.77                     
SITE     1 AC1  7 CYS A 169  PRO A 172  CYS A 187  ARG A 226                    
SITE     2 AC1  7 CYS A 232  CYS A 235  ASN A 237                               
SITE     1 AC2  9 CYS A  16  ARG A  18  CYS A  20  CYS A  23                    
SITE     2 AC2  9 ASN A  25  TYR A  62  ASN A  92  HIS A 117                    
SITE     3 AC2  9 HOH A 638                                                     
SITE     1 AC3  5 MSE A 170  SER A 173  LYS A 222  GOL A 504                    
SITE     2 AC3  5 HOH A 641                                                     
SITE     1 AC4  4 LYS A   3  MSE A 170  ASN A 174  GOL A 503                    
SITE     1 AC5  3 ASP A  37  ASP A  94  LEU A  96                               
CRYST1   99.408   42.058   50.925  90.00 105.40  90.00 C 1 2 1       4          
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      0.010060  0.000000  0.002771        0.00000                         
SCALE2      0.000000  0.023777  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020368        0.00000                         
HETATM    1  N   MSE A   1     108.506  -3.443  -6.506  1.00 55.38           N  
ANISOU    1  N   MSE A   1     8015   7178   5847   -250  -1524   2108       N  
HETATM    2  CA  MSE A   1     109.256  -3.913  -5.348  1.00 52.19           C  
ANISOU    2  CA  MSE A   1     7529   6748   5554   -150  -1252   1811       C  
HETATM    3  C   MSE A   1     109.252  -2.886  -4.227  1.00 59.05           C  
ANISOU    3  C   MSE A   1     8131   7469   6838    -12  -1105   1825       C  
HETATM    4  O   MSE A   1     110.041  -2.985  -3.289  1.00 61.70           O  
ANISOU    4  O   MSE A   1     8408   7774   7260     61   -871   1611       O  
HETATM    5  CB  MSE A   1     110.696  -4.218  -5.740  1.00 45.99           C  
ANISOU    5  CB  MSE A   1     6962   6029   4484   -188  -1007   1642       C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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