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Database: PDB
Entry: 3QY6
LinkDB: 3QY6
Original site: 3QY6 
HEADER    HYDROLASE                               03-MAR-11   3QY6              
TITLE     CRYSTAL STRUCTURES OF YWQE FROM BACILLUS SUBTILIS AND CPSB FROM       
TITLE    2 STREPTOCOCCUS PNEUMONIAE, UNIQUE METAL-DEPENDENT TYROSINE            
TITLE    3 PHOSPHATASES                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE YWQE;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.3.48;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: BSU36240, YWQE;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET21A(+)                                 
KEYWDS    TIM BARREL, POLYMERASE AND HISTINDINOL PHOSPHATASE(PHP)-LIKE          
KEYWDS   2 PHOSPHATASE, PHOSPHATASE, HYDROLASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.S.KIM,S.J.LEE,H.J.YOON,D.R.AN,D.J.KIM,S.-J.KIM,S.W.SUH              
REVDAT   2   17-AUG-11 3QY6    1       JRNL   VERSN                             
REVDAT   1   08-JUN-11 3QY6    0                                                
JRNL        AUTH   H.S.KIM,S.J.LEE,H.J.YOON,D.R.AN,D.J.KIM,S.J.KIM,S.W.SUH      
JRNL        TITL   CRYSTAL STRUCTURES OF YWQE FROM BACILLUS SUBTILIS AND CPSB   
JRNL        TITL 2 FROM STREPTOCOCCUS PNEUMONIAE, UNIQUE METAL-DEPENDENT        
JRNL        TITL 3 TYROSINE PHOSPHATASES.                                       
JRNL        REF    J.STRUCT.BIOL.                V. 175   442 2011              
JRNL        REFN                   ISSN 1047-8477                               
JRNL        PMID   21605684                                                     
JRNL        DOI    10.1016/J.JSB.2011.05.007                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 21414                          
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) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1153                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.84                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1495                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.80                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2710                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 79                           
REMARK   3   BIN FREE R VALUE                    : 0.2990                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1980                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 3                                       
REMARK   3   SOLVENT ATOMS            : 154                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.86                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.97000                                             
REMARK   3    B22 (A**2) : 0.81000                                              
REMARK   3    B33 (A**2) : 0.08000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.83000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.148         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.120         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.834         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2031 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2753 ; 1.211 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   248 ; 5.371 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   103 ;32.356 ;24.078       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   356 ;15.205 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;15.380 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   305 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1561 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1242 ; 0.762 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2008 ; 1.388 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   789 ; 1.948 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   745 ; 3.318 ; 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   : 1.40                                          
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 3QY6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB064251.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-OCT-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 4A                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97952                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22595                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 55.300                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 42.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.450                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, 8% (W/V) PEG 8000, PH   
REMARK 280  8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 273K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       29.82050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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     ARG A   248                                                      
REMARK 465     LYS A   249                                                      
REMARK 465     LEU A   250                                                      
REMARK 465     PHE A   251                                                      
REMARK 465     GLY A   252                                                      
REMARK 465     PHE A   253                                                      
REMARK 465     PHE A   254                                                      
REMARK 465     LEU A   255                                                      
REMARK 465     GLU A   256                                                      
REMARK 465     HIS A   257                                                      
REMARK 465     HIS A   258                                                      
REMARK 465     HIS A   259                                                      
REMARK 465     HIS A   260                                                      
REMARK 465     HIS A   261                                                      
REMARK 465     HIS A   262                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500  FE     FE A   264     O    HOH A   348              1.29            
REMARK 500  MG     MG A   265     O    HOH A   405              1.62            
REMARK 500   CE1  HIS A    42     O    HOH A   349              1.64            
REMARK 500   O    HOH A   376     O    HOH A   405              2.03            
REMARK 500   O    HOH A   276     O    HOH A   416              2.13            
REMARK 500   O    HOH A   367     O    HOH A   414              2.18            
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    HIS A   7       54.79   -105.83                                   
REMARK 500    ASP A  13     -147.47   -147.11                                   
REMARK 500    HIS A 136       60.81     36.69                                   
REMARK 500    ALA A 185        2.14    -69.08                                   
REMARK 500    LYS A 199      -69.03    -93.69                                   
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                              FE A 263  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 349   O                                                      
REMARK 620 2 HIS A 136   NE2 170.9                                              
REMARK 620 3 GLU A  80   OE1  93.8  94.8                                        
REMARK 620 4 GLU A 108   OE1  83.4  93.5  90.4                                  
REMARK 620 5 HOH A 347   O    73.9  97.3 166.2  82.1                            
REMARK 620 6 HOH A 348   O    89.1  95.9  75.8 163.9 109.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 264  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A   7   NE2                                                    
REMARK 620 2 GLU A  80   OE2  89.4                                              
REMARK 620 3 ASP A 194   OD1  91.0 172.9                                        
REMARK 620 4 HIS A   5   NE2 112.3  89.8  83.5                                  
REMARK 620 5 HOH A 376   O    79.7  94.4  92.6 167.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 265  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  14   OD2                                                    
REMARK 620 2 HOH A 376   O   163.1                                              
REMARK 620 3 ASP A  14   OD1  51.7 144.5                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 263                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 264                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 265                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3QY7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3QY8   RELATED DB: PDB                                   
DBREF  3QY6 A    1   254  UNP    P96717   YWQE_BACSU       1    254             
SEQADV 3QY6 LEU A  255  UNP  P96717              EXPRESSION TAG                 
SEQADV 3QY6 GLU A  256  UNP  P96717              EXPRESSION TAG                 
SEQADV 3QY6 HIS A  257  UNP  P96717              EXPRESSION TAG                 
SEQADV 3QY6 HIS A  258  UNP  P96717              EXPRESSION TAG                 
SEQADV 3QY6 HIS A  259  UNP  P96717              EXPRESSION TAG                 
SEQADV 3QY6 HIS A  260  UNP  P96717              EXPRESSION TAG                 
SEQADV 3QY6 HIS A  261  UNP  P96717              EXPRESSION TAG                 
SEQADV 3QY6 HIS A  262  UNP  P96717              EXPRESSION TAG                 
SEQRES   1 A  262  MET ILE ASP ILE HIS CYS HIS ILE LEU PRO ALA MET ASP          
SEQRES   2 A  262  ASP GLY ALA GLY ASP SER ALA ASP SER ILE GLU MET ALA          
SEQRES   3 A  262  ARG ALA ALA VAL ARG GLN GLY ILE ARG THR ILE ILE ALA          
SEQRES   4 A  262  THR PRO HIS HIS ASN ASN GLY VAL TYR LYS ASN GLU PRO          
SEQRES   5 A  262  ALA ALA VAL ARG GLU ALA ALA ASP GLN LEU ASN LYS ARG          
SEQRES   6 A  262  LEU ILE LYS GLU ASP ILE PRO LEU HIS VAL LEU PRO GLY          
SEQRES   7 A  262  GLN GLU ILE ARG ILE TYR GLY GLU VAL GLU GLN ASP LEU          
SEQRES   8 A  262  ALA LYS ARG GLN LEU LEU SER LEU ASN ASP THR LYS TYR          
SEQRES   9 A  262  ILE LEU ILE GLU PHE PRO PHE ASP HIS VAL PRO ARG TYR          
SEQRES  10 A  262  ALA GLU GLN LEU PHE TYR ASP LEU GLN LEU LYS GLY TYR          
SEQRES  11 A  262  ILE PRO VAL ILE ALA HIS PRO GLU ARG ASN ARG GLU ILE          
SEQRES  12 A  262  ARG GLU ASN PRO SER LEU LEU TYR HIS LEU VAL GLU LYS          
SEQRES  13 A  262  GLY ALA ALA SER GLN ILE THR SER GLY SER LEU ALA GLY          
SEQRES  14 A  262  ILE PHE GLY LYS GLN LEU LYS ALA PHE SER LEU ARG LEU          
SEQRES  15 A  262  VAL GLU ALA ASN LEU ILE HIS PHE VAL ALA SER ASP ALA          
SEQRES  16 A  262  HIS ASN VAL LYS THR ARG ASN PHE HIS THR GLN GLU ALA          
SEQRES  17 A  262  LEU TYR VAL LEU GLU LYS GLU PHE GLY SER GLU LEU PRO          
SEQRES  18 A  262  TYR MET LEU THR GLU ASN ALA GLU LEU LEU LEU ARG ASN          
SEQRES  19 A  262  GLN THR ILE PHE ARG GLN PRO PRO GLN PRO VAL LYS ARG          
SEQRES  20 A  262  ARG LYS LEU PHE GLY PHE PHE LEU GLU HIS HIS HIS HIS          
SEQRES  21 A  262  HIS HIS                                                      
HET     FE  A 263       1                                                       
HET     FE  A 264       1                                                       
HET     MG  A 265       1                                                       
HETNAM      FE FE (III) ION                                                     
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   2   FE    2(FE 3+)                                                     
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  HOH   *154(H2 O)                                                    
HELIX    1   1 ASP A   18  GLN A   32  1                                  15    
HELIX    2   2 GLU A   51  GLU A   69  1                                  19    
HELIX    3   3 GLU A   86  LYS A   93  1                                   8    
HELIX    4   4 SER A   98  THR A  102  5                                   5    
HELIX    5   5 TYR A  117  LYS A  128  1                                  12    
HELIX    6   6 PRO A  137  ARG A  139  5                                   3    
HELIX    7   7 ASN A  140  ASN A  146  1                                   7    
HELIX    8   8 PRO A  147  LYS A  156  1                                  10    
HELIX    9   9 SER A  164  ALA A  168  1                                   5    
HELIX   10  10 GLY A  172  ALA A  185  1                                  14    
HELIX   11  11 HIS A  204  GLY A  217  1                                  14    
HELIX   12  12 SER A  218  ARG A  233  1                                  16    
SHEET    1   A 3 ILE A   2  ASP A   3  0                                        
SHEET    2   A 3 THR A  36  ILE A  38  1  O  ILE A  38   N  ASP A   3           
SHEET    3   A 3 HIS A  74  LEU A  76  1  O  LEU A  76   N  ILE A  37           
SHEET    1   B 6 HIS A  42  HIS A  43  0                                        
SHEET    2   B 6 GLU A  80  ARG A  82  1  O  GLU A  80   N  HIS A  43           
SHEET    3   B 6 TYR A 104  GLU A 108  1  O  GLU A 108   N  ILE A  81           
SHEET    4   B 6 ILE A 131  ALA A 135  1  O  VAL A 133   N  ILE A 105           
SHEET    5   B 6 ALA A 159  THR A 163  1  O  ALA A 159   N  ILE A 134           
SHEET    6   B 6 PHE A 190  ALA A 192  1  O  PHE A 190   N  ILE A 162           
LINK        FE    FE A 263                 O   HOH A 349     1555   1555  1.78  
LINK         NE2 HIS A   7                FE    FE A 264     1555   1555  2.00  
LINK         NE2 HIS A 136                FE    FE A 263     1555   1555  2.04  
LINK         OE1 GLU A  80                FE    FE A 263     1555   1555  2.12  
LINK         OE2 GLU A  80                FE    FE A 264     1555   1555  2.15  
LINK         OD1 ASP A 194                FE    FE A 264     1555   1555  2.18  
LINK         OD2BASP A  14                MG    MG A 265     1555   1555  2.20  
LINK         OE1 GLU A 108                FE    FE A 263     1555   1555  2.20  
LINK         NE2 HIS A   5                FE    FE A 264     1555   1555  2.21  
LINK        FE    FE A 263                 O   HOH A 347     1555   1555  2.21  
LINK        FE    FE A 264                 O   HOH A 376     1555   1555  2.23  
LINK        MG    MG A 265                 O   HOH A 376     1555   1555  2.23  
LINK        FE    FE A 263                 O   HOH A 348     1555   1555  2.42  
LINK         OD1BASP A  14                MG    MG A 265     1555   1555  2.72  
SITE     1 AC1  8 HIS A  42  GLU A  80  GLU A 108  HIS A 136                    
SITE     2 AC1  8  FE A 264  HOH A 347  HOH A 348  HOH A 349                    
SITE     1 AC2  7 HIS A   5  HIS A   7  GLU A  80  ASP A 194                    
SITE     2 AC2  7  FE A 263  HOH A 348  HOH A 376                               
SITE     1 AC3  5 ASP A  14  HIS A  42  HIS A 196  HOH A 376                    
SITE     2 AC3  5 HOH A 405                                                     
CRYST1   36.624   59.641   57.530  90.00 101.08  90.00 P 1 21 1      2          
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      0.027304  0.000000  0.005346        0.00000                         
SCALE2      0.000000  0.016767  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017712        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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