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Database: PDB
Entry: 3TQJ
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HEADER    OXIDOREDUCTASE                          09-SEP-11   3TQJ              
TITLE     STRUCTURE OF THE SUPEROXIDE DISMUTASE (FE) (SODB) FROM COXIELLA       
TITLE    2 BURNETII                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [FE];                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: COXIELLA BURNETII;                              
SOURCE   3 ORGANISM_TAXID: 777;                                                 
SOURCE   4 STRAIN: RSA 493 NINE MILE PHASE I;                                   
SOURCE   5 GENE: CBU_1708, SODB;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    SUPEROXIDE DISMUTASE (FE), OXIDOREDUCTASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.C.FRANKLIN,J.CHEUNG,M.CASSIDY,J.LOVE                                
REVDAT   3   20-JAN-16 3TQJ    1       JRNL                                     
REVDAT   2   24-JUN-15 3TQJ    1       JRNL                                     
REVDAT   1   21-SEP-11 3TQJ    0                                                
JRNL        AUTH   M.C.FRANKLIN,J.CHEUNG,M.J.RUDOLPH,F.BURSHTEYN,M.CASSIDY,     
JRNL        AUTH 2 E.GARY,B.HILLERICH,Z.K.YAO,P.R.CARLIER,M.TOTROV,J.D.LOVE     
JRNL        TITL   STRUCTURAL GENOMICS FOR DRUG DESIGN AGAINST THE PATHOGEN     
JRNL        TITL 2 COXIELLA BURNETII.                                           
JRNL        REF    PROTEINS                      V.  83  2124 2015              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   26033498                                                     
JRNL        DOI    10.1002/PROT.24841                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.15                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 27134                          
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) : 0.235                           
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1388                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.06                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1420                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.21                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3730                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 70                           
REMARK   3   BIN FREE R VALUE                    : 0.5240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3134                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 382                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.94000                                             
REMARK   3    B22 (A**2) : -0.80000                                             
REMARK   3    B33 (A**2) : 1.74000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.269         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.210         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.139         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.311        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3244 ; 0.006 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2190 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4390 ; 0.879 ; 1.914       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5320 ; 0.786 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   382 ; 5.180 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   170 ;33.057 ;24.706       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   524 ;12.338 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ; 9.019 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   438 ; 0.055 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3630 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   684 ; 0.001 ; 0.020       
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):  1912 ; 0.186 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   772 ; 0.035 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3074 ; 0.359 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1332 ; 0.602 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1316 ; 0.974 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   193                          
REMARK   3    RESIDUE RANGE :   A  1001        A  1001                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.7000   9.5290 -10.6433              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0221 T22:   0.0886                                     
REMARK   3      T33:   0.0581 T12:  -0.0145                                     
REMARK   3      T13:   0.0221 T23:  -0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4325 L22:   2.5942                                     
REMARK   3      L33:   1.3100 L12:  -0.0208                                     
REMARK   3      L13:   0.0589 L23:  -0.3309                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0147 S12:   0.1103 S13:   0.1508                       
REMARK   3      S21:  -0.2125 S22:   0.0180 S23:  -0.2831                       
REMARK   3      S31:  -0.0327 S32:   0.0986 S33:  -0.0034                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B   193                          
REMARK   3    RESIDUE RANGE :   B  1001        B  1001                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.5535  -9.6168 -10.5027              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0414 T22:   0.0863                                     
REMARK   3      T33:   0.0627 T12:  -0.0134                                     
REMARK   3      T13:  -0.0242 T23:   0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6441 L22:   2.8594                                     
REMARK   3      L33:   1.3938 L12:   0.1357                                     
REMARK   3      L13:  -0.0145 L23:   0.4201                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0353 S12:   0.1398 S13:  -0.1280                       
REMARK   3      S21:  -0.2963 S22:   0.0450 S23:   0.3031                       
REMARK   3      S31:   0.0378 S32:  -0.1123 S33:  -0.0097                       
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 3TQJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-SEP-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB067797.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JAN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : VARIMAX HF                         
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27752                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY                : 13.500                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 34.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.25100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB CODE 1ISA                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M IMIDAZOLE, 10% PEG 8000, PH 8.0,   
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       30.05100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.03450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.64250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.03450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.05100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.64250            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A   194                                                      
REMARK 465     ASN A   195                                                      
REMARK 465     LEU A   196                                                      
REMARK 465     TYR A   197                                                      
REMARK 465     PHE A   198                                                      
REMARK 465     GLN A   199                                                      
REMARK 465     GLY A   200                                                      
REMARK 465     HIS A   201                                                      
REMARK 465     HIS A   202                                                      
REMARK 465     HIS A   203                                                      
REMARK 465     HIS A   204                                                      
REMARK 465     HIS A   205                                                      
REMARK 465     HIS A   206                                                      
REMARK 465     HIS A   207                                                      
REMARK 465     HIS A   208                                                      
REMARK 465     HIS A   209                                                      
REMARK 465     HIS A   210                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B   194                                                      
REMARK 465     ASN B   195                                                      
REMARK 465     LEU B   196                                                      
REMARK 465     TYR B   197                                                      
REMARK 465     PHE B   198                                                      
REMARK 465     GLN B   199                                                      
REMARK 465     GLY B   200                                                      
REMARK 465     HIS B   201                                                      
REMARK 465     HIS B   202                                                      
REMARK 465     HIS B   203                                                      
REMARK 465     HIS B   204                                                      
REMARK 465     HIS B   205                                                      
REMARK 465     HIS B   206                                                      
REMARK 465     HIS B   207                                                      
REMARK 465     HIS B   208                                                      
REMARK 465     HIS B   209                                                      
REMARK 465     HIS B   210                                                      
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    LYS A  30      -55.78   -121.68                                   
REMARK 500    ASN A 141     -104.80     59.71                                   
REMARK 500    ARG A 168     -124.95     52.81                                   
REMARK 500    PRO B   9        0.13    -69.20                                   
REMARK 500    ASN B 141     -105.88     59.54                                   
REMARK 500    ARG B 168     -124.52     52.33                                   
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                             FE2 A1001  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  27   NE2                                                    
REMARK 620 2 HIS A  74   NE2  97.8                                              
REMARK 620 3 ASP A 157   OD2  86.7 116.3                                        
REMARK 620 4 HIS A 161   NE2  91.1 129.2 114.1                                  
REMARK 620 5 HOH A 404   O   173.1  85.8  86.5  91.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 B1001  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  27   NE2                                                    
REMARK 620 2 HIS B  74   NE2  91.7                                              
REMARK 620 3 ASP B 157   OD2  87.1 114.4                                        
REMARK 620 4 HIS B 161   NE2  94.3 127.7 117.9                                  
REMARK 620 5 HOH B 355   O   173.0  90.7  85.9  89.5                            
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 FE2 A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 B 1001                
DBREF  3TQJ A    1   193  UNP    P19685   SODF_COXBU       1    193             
DBREF  3TQJ B    1   193  UNP    P19685   SODF_COXBU       1    193             
SEQADV 3TQJ GLU A  194  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ ASN A  195  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ LEU A  196  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ TYR A  197  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ PHE A  198  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ GLN A  199  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ GLY A  200  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS A  201  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS A  202  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS A  203  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS A  204  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS A  205  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS A  206  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS A  207  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS A  208  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS A  209  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS A  210  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ GLU B  194  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ ASN B  195  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ LEU B  196  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ TYR B  197  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ PHE B  198  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ GLN B  199  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ GLY B  200  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS B  201  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS B  202  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS B  203  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS B  204  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS B  205  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS B  206  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS B  207  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS B  208  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS B  209  UNP  P19685              EXPRESSION TAG                 
SEQADV 3TQJ HIS B  210  UNP  P19685              EXPRESSION TAG                 
SEQRES   1 A  210  MET ALA PHE GLU LEU PRO ASP LEU PRO TYR LYS LEU ASN          
SEQRES   2 A  210  ALA LEU GLU PRO HIS ILE SER GLN GLU THR LEU GLU TYR          
SEQRES   3 A  210  HIS HIS GLY LYS HIS HIS ARG ALA TYR VAL ASN LYS LEU          
SEQRES   4 A  210  ASN LYS LEU ILE GLU GLY THR PRO PHE GLU LYS GLU PRO          
SEQRES   5 A  210  LEU GLU GLU ILE ILE ARG LYS SER ASP GLY GLY ILE PHE          
SEQRES   6 A  210  ASN ASN ALA ALA GLN HIS TRP ASN HIS THR PHE TYR TRP          
SEQRES   7 A  210  HIS CYS MET SER PRO ASP GLY GLY GLY ASP PRO SER GLY          
SEQRES   8 A  210  GLU LEU ALA SER ALA ILE ASP LYS THR PHE GLY SER LEU          
SEQRES   9 A  210  GLU LYS PHE LYS ALA LEU PHE THR ASP SER ALA ASN ASN          
SEQRES  10 A  210  HIS PHE GLY SER GLY TRP ALA TRP LEU VAL LYS ASP ASN          
SEQRES  11 A  210  ASN GLY LYS LEU GLU VAL LEU SER THR VAL ASN ALA ARG          
SEQRES  12 A  210  ASN PRO MET THR GLU GLY LYS LYS PRO LEU MET THR CYS          
SEQRES  13 A  210  ASP VAL TRP GLU HIS ALA TYR TYR ILE ASP THR ARG ASN          
SEQRES  14 A  210  ASP ARG PRO LYS TYR VAL ASN ASN PHE TRP GLN VAL VAL          
SEQRES  15 A  210  ASN TRP ASP PHE VAL MET LYS ASN PHE LYS SER GLU ASN          
SEQRES  16 A  210  LEU TYR PHE GLN GLY HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES  17 A  210  HIS HIS                                                      
SEQRES   1 B  210  MET ALA PHE GLU LEU PRO ASP LEU PRO TYR LYS LEU ASN          
SEQRES   2 B  210  ALA LEU GLU PRO HIS ILE SER GLN GLU THR LEU GLU TYR          
SEQRES   3 B  210  HIS HIS GLY LYS HIS HIS ARG ALA TYR VAL ASN LYS LEU          
SEQRES   4 B  210  ASN LYS LEU ILE GLU GLY THR PRO PHE GLU LYS GLU PRO          
SEQRES   5 B  210  LEU GLU GLU ILE ILE ARG LYS SER ASP GLY GLY ILE PHE          
SEQRES   6 B  210  ASN ASN ALA ALA GLN HIS TRP ASN HIS THR PHE TYR TRP          
SEQRES   7 B  210  HIS CYS MET SER PRO ASP GLY GLY GLY ASP PRO SER GLY          
SEQRES   8 B  210  GLU LEU ALA SER ALA ILE ASP LYS THR PHE GLY SER LEU          
SEQRES   9 B  210  GLU LYS PHE LYS ALA LEU PHE THR ASP SER ALA ASN ASN          
SEQRES  10 B  210  HIS PHE GLY SER GLY TRP ALA TRP LEU VAL LYS ASP ASN          
SEQRES  11 B  210  ASN GLY LYS LEU GLU VAL LEU SER THR VAL ASN ALA ARG          
SEQRES  12 B  210  ASN PRO MET THR GLU GLY LYS LYS PRO LEU MET THR CYS          
SEQRES  13 B  210  ASP VAL TRP GLU HIS ALA TYR TYR ILE ASP THR ARG ASN          
SEQRES  14 B  210  ASP ARG PRO LYS TYR VAL ASN ASN PHE TRP GLN VAL VAL          
SEQRES  15 B  210  ASN TRP ASP PHE VAL MET LYS ASN PHE LYS SER GLU ASN          
SEQRES  16 B  210  LEU TYR PHE GLN GLY HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES  17 B  210  HIS HIS                                                      
HET    FE2  A1001       1                                                       
HET    FE2  B1001       1                                                       
HETNAM     FE2 FE (II) ION                                                      
FORMUL   3  FE2    2(FE 2+)                                                     
FORMUL   5  HOH   *382(H2 O)                                                    
HELIX    1   1 SER A   20  LYS A   30  1                                  11    
HELIX    2   2 LYS A   30  GLU A   44  1                                  15    
HELIX    3   3 PRO A   52  SER A   60  1                                   9    
HELIX    4   4 ASP A   61  CYS A   80  1                                  20    
HELIX    5   5 SER A   90  GLY A  102  1                                  13    
HELIX    6   6 SER A  103  HIS A  118  1                                  16    
HELIX    7   7 ASN A  144  GLY A  149  5                                   6    
HELIX    8   8 TRP A  159  ALA A  162  5                                   4    
HELIX    9   9 TYR A  163  ARG A  168  1                                   6    
HELIX   10  10 ASP A  170  VAL A  182  1                                  13    
HELIX   11  11 ASN A  183  LYS A  192  1                                  10    
HELIX   12  12 SER B   20  HIS B   28  1                                   9    
HELIX   13  13 LYS B   30  GLU B   44  1                                  15    
HELIX   14  14 PRO B   52  SER B   60  1                                   9    
HELIX   15  15 ASP B   61  CYS B   80  1                                  20    
HELIX   16  16 SER B   90  GLY B  102  1                                  13    
HELIX   17  17 SER B  103  HIS B  118  1                                  16    
HELIX   18  18 ASN B  144  GLU B  148  5                                   5    
HELIX   19  19 TRP B  159  ALA B  162  5                                   4    
HELIX   20  20 TYR B  163  ARG B  168  1                                   6    
HELIX   21  21 ASP B  170  VAL B  182  1                                  13    
HELIX   22  22 ASN B  183  SER B  193  1                                  11    
SHEET    1   A 3 LEU A 134  VAL A 140  0                                        
SHEET    2   A 3 GLY A 122  LYS A 128 -1  N  TRP A 125   O  LEU A 137           
SHEET    3   A 3 LYS A 151  ASP A 157 -1  O  LEU A 153   N  LEU A 126           
SHEET    1   B 3 LEU B 134  VAL B 140  0                                        
SHEET    2   B 3 GLY B 122  ASP B 129 -1  N  TRP B 125   O  LEU B 137           
SHEET    3   B 3 LYS B 150  ASP B 157 -1  O  LEU B 153   N  LEU B 126           
LINK         NE2 HIS A  27                FE   FE2 A1001     1555   1555  2.15  
LINK         NE2 HIS B  27                FE   FE2 B1001     1555   1555  2.14  
LINK         NE2 HIS A  74                FE   FE2 A1001     1555   1555  2.15  
LINK         NE2 HIS B  74                FE   FE2 B1001     1555   1555  2.15  
LINK         OD2 ASP A 157                FE   FE2 A1001     1555   1555  1.89  
LINK         OD2 ASP B 157                FE   FE2 B1001     1555   1555  1.89  
LINK         NE2 HIS A 161                FE   FE2 A1001     1555   1555  2.14  
LINK         NE2 HIS B 161                FE   FE2 B1001     1555   1555  2.14  
LINK        FE   FE2 A1001                 O   HOH A 404     1555   1555  2.16  
LINK        FE   FE2 B1001                 O   HOH B 355     1555   1555  2.17  
CISPEP   1 GLU A   16    PRO A   17          0        -1.41                     
CISPEP   2 GLU B   16    PRO B   17          0        -1.42                     
SITE     1 AC1  5 HIS A  27  HIS A  74  ASP A 157  HIS A 161                    
SITE     2 AC1  5 HOH A 404                                                     
SITE     1 AC2  5 HIS B  27  HIS B  74  ASP B 157  HIS B 161                    
SITE     2 AC2  5 HOH B 355                                                     
CRYST1   60.102   65.285  110.069  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016638  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015317  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009085        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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