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Database: PDB
Entry: 4H3E
LinkDB: 4H3E
Original site: 4H3E 
HEADER    OXIDOREDUCTASE                          13-SEP-12   4H3E              
TITLE     CRYSTAL STRUCTURE OF A PUTATIVE IRON SUPEROXIDE DISMUTASE FROM        
TITLE    2 TRYPANOSOMA CRUZI BOUND TO IRON                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: FESOD;                                                      
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CRUZI;                              
SOURCE   3 ORGANISM_TAXID: 353153;                                              
SOURCE   4 STRAIN: CL BRENER;                                                   
SOURCE   5 GENE: TC00.1047053509775.40;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PAVA0421                                  
KEYWDS    STRUCTURAL GENOMICS, NIAID, NATIONAL INSTITUTE OF ALLERGY AND         
KEYWDS   2 INFECTIOUS DISEASES, SEATTLE STRUCTURAL GENOMICS CENTER FOR          
KEYWDS   3 INFECTIOUS DISEASE, SSGCID, RADICAL OXYGEN SPECIES, TRYPANOSOMIASIS, 
KEYWDS   4 PARASITIC EUGLENOID TRYPANOSOME, CHAGAS DISEASE, RADICAL SCAVENGER,  
KEYWDS   5 HYDROGEN PEROXIDE, ANTIOXIDANT, OXIDOREDUCTASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)    
REVDAT   1   26-SEP-12 4H3E    0                                                
JRNL        AUTH   T.E.EDWARDS,M.C.CLIFTON,                                     
JRNL        AUTH 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE    
JRNL        AUTH 3 (SSGCID)                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF A PUTATIVE IRON SUPEROXIDE DISMUTASE    
JRNL        TITL 2 FROM TRYPANOSOMA CRUZI BOUND TO IRON                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 19189                          
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) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1038                            
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) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.31                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1368                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.38                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1700                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 59                           
REMARK   3   BIN FREE R VALUE                    : 0.2660                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3350                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 348                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.81                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.54000                                             
REMARK   3    B22 (A**2) : 0.19000                                              
REMARK   3    B33 (A**2) : 0.35000                                              
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): 0.364         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.216         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.132         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.698         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.911                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3456 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3150 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4712 ; 1.407 ; 1.927       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7242 ; 1.008 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   428 ; 6.073 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   161 ;38.245 ;24.534       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   517 ;12.935 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;11.965 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   499 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3993 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   841 ; 0.004 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1      A    20   233       B    20    233    12529                
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    20        A   233                          
REMARK   3    RESIDUE RANGE :   A   301        A   301                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.2983   1.0483   6.1511              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0531 T22:   0.0108                                     
REMARK   3      T33:   0.0024 T12:   0.0000                                     
REMARK   3      T13:  -0.0076 T23:   0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6030 L22:   0.2751                                     
REMARK   3      L33:   0.1527 L12:  -0.0847                                     
REMARK   3      L13:   0.0463 L23:  -0.0099                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0286 S12:   0.0231 S13:  -0.0274                       
REMARK   3      S21:  -0.0343 S22:  -0.0256 S23:   0.0054                       
REMARK   3      S31:  -0.0137 S32:  -0.0050 S33:  -0.0031                       
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    20        B   233                          
REMARK   3    RESIDUE RANGE :   B   301        B   301                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.5696  11.2692  31.6990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0306 T22:   0.0120                                     
REMARK   3      T33:   0.0273 T12:   0.0022                                     
REMARK   3      T13:  -0.0133 T23:  -0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4817 L22:   0.2454                                     
REMARK   3      L33:   0.2134 L12:  -0.1651                                     
REMARK   3      L13:  -0.1367 L23:  -0.0257                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0113 S12:  -0.0289 S13:   0.0100                       
REMARK   3      S21:   0.0047 S22:   0.0275 S23:  -0.0346                       
REMARK   3      S31:  -0.0024 S32:  -0.0133 S33:  -0.0162                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  U VALUES      : WITH TLS ADDED                                      
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   4                                                                      
REMARK   4 4H3E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB074968.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-SEP-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
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 FR-E+ SUPERBRIGHT           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : VARIMAX                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20226                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.13700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.990                              
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 ENTRY 4F2N                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRCRA.00198.B.B1 PS01521 AT 23.05 MG/    
REMARK 280  ML AGAINST JCSG+ SCREEN CONDITION G1: 0.1 M HEPES, PH 7.0, 30%      
REMARK 280  JEFFAMINE ED-2001, CRYSTAL TRACKING ID 235439G1, UNIQUE PUCK ID     
REMARK 280  GVR7-6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K             
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       23.82500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.72500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.84000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.72500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.82500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.84000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    -7                                                      
REMARK 465     ALA A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     ASN A     7                                                      
REMARK 465     ILE A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     ILE A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     ARG A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     ARG A    14                                                      
REMARK 465     MET A    15                                                      
REMARK 465     ALA A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     MET A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     MET B    -7                                                      
REMARK 465     ALA B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LEU B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     ARG B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     VAL B     6                                                      
REMARK 465     ASN B     7                                                      
REMARK 465     ILE B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     ILE B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     ARG B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     ARG B    14                                                      
REMARK 465     MET B    15                                                      
REMARK 465     ALA B    16                                                      
REMARK 465     LEU B    17                                                      
REMARK 465     MET B    18                                                      
REMARK 465     SER B    19                                                      
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     LYS A  38    CG   CD   CE   NZ                                   
REMARK 470     LYS A 126    CG   CD   CE   NZ                                   
REMARK 470     GLN A 170    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 233    CG   CD   CE   NZ                                   
REMARK 470     GLU B  96    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  97    CG   CD   CE   NZ                                   
REMARK 470     LYS B  98    CG   CD   CE   NZ                                   
REMARK 470     LYS B 126    CG   CD   CE   NZ                                   
REMARK 470     GLN B 148    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 170    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 226    CG   CD   CE   NZ                                   
REMARK 470     GLN B 230    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 233    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 207   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  62      -63.95   -107.86                                   
REMARK 500    ASN A 178     -112.52     62.88                                   
REMARK 500    GLU A 205     -130.73     51.71                                   
REMARK 500    LYS B  62      -63.21   -109.52                                   
REMARK 500    ASN B 178     -111.63     59.51                                   
REMARK 500    GLU B 205     -131.12     50.69                                   
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                             FE2 B 301  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 194   OD2                                                    
REMARK 620 2 HIS B 110   NE2 118.1                                              
REMARK 620 3 HIS B 198   NE2 122.0 119.8                                        
REMARK 620 4 HOH B 402   O    90.3  89.8  87.4                                  
REMARK 620 5 HIS B  59   NE2  81.1  95.9  95.6 171.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A 301  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 194   OD2                                                    
REMARK 620 2 HIS A 198   NE2 123.0                                              
REMARK 620 3 HIS A 110   NE2 116.0 120.3                                        
REMARK 620 4 HIS A  59   NE2  79.9  99.4  98.6                                  
REMARK 620 5 HOH A 402   O    86.3  86.3  89.5 166.0                            
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 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 B 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4F2N   RELATED DB: PDB                                   
REMARK 900 FESOD FROM L. MAJOR                                                  
REMARK 900 RELATED ID: SSGCID-TRCRA.00198.B   RELATED DB: TARGETTRACK           
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 L128F IS A NATURAL VARIANT.                                          
DBREF  4H3E A    1   233  UNP    Q4DCQ3   Q4DCQ3_TRYCC     1    233             
DBREF  4H3E B    1   233  UNP    Q4DCQ3   Q4DCQ3_TRYCC     1    233             
SEQADV 4H3E MET A   -7  UNP  Q4DCQ3              EXPRESSION TAG                 
SEQADV 4H3E ALA A   -6  UNP  Q4DCQ3              EXPRESSION TAG                 
SEQADV 4H3E HIS A   -5  UNP  Q4DCQ3              EXPRESSION TAG                 
SEQADV 4H3E HIS A   -4  UNP  Q4DCQ3              EXPRESSION TAG                 
SEQADV 4H3E HIS A   -3  UNP  Q4DCQ3              EXPRESSION TAG                 
SEQADV 4H3E HIS A   -2  UNP  Q4DCQ3              EXPRESSION TAG                 
SEQADV 4H3E HIS A   -1  UNP  Q4DCQ3              EXPRESSION TAG                 
SEQADV 4H3E HIS A    0  UNP  Q4DCQ3              EXPRESSION TAG                 
SEQADV 4H3E PHE A  128  UNP  Q4DCQ3    LEU   128 SEE REMARK 999                 
SEQADV 4H3E MET B   -7  UNP  Q4DCQ3              EXPRESSION TAG                 
SEQADV 4H3E ALA B   -6  UNP  Q4DCQ3              EXPRESSION TAG                 
SEQADV 4H3E HIS B   -5  UNP  Q4DCQ3              EXPRESSION TAG                 
SEQADV 4H3E HIS B   -4  UNP  Q4DCQ3              EXPRESSION TAG                 
SEQADV 4H3E HIS B   -3  UNP  Q4DCQ3              EXPRESSION TAG                 
SEQADV 4H3E HIS B   -2  UNP  Q4DCQ3              EXPRESSION TAG                 
SEQADV 4H3E HIS B   -1  UNP  Q4DCQ3              EXPRESSION TAG                 
SEQADV 4H3E HIS B    0  UNP  Q4DCQ3              EXPRESSION TAG                 
SEQADV 4H3E PHE B  128  UNP  Q4DCQ3    LEU   128 SEE REMARK 999                 
SEQRES   1 A  241  MET ALA HIS HIS HIS HIS HIS HIS MET LEU ARG ARG ALA          
SEQRES   2 A  241  VAL ASN ILE SER ILE ALA ARG GLY ARG MET ALA LEU MET          
SEQRES   3 A  241  SER TYR ALA THR LEU PRO ASP LEU LEU LYS PRO SER GLY          
SEQRES   4 A  241  ALA PRO ALA GLU LEU PRO LYS LEU GLY PHE ASN TRP LYS          
SEQRES   5 A  241  ASP GLY CYS ALA PRO VAL PHE SER PRO ARG GLN MET GLU          
SEQRES   6 A  241  LEU HIS TYR THR LYS HIS HIS LYS ALA TYR VAL ASP LYS          
SEQRES   7 A  241  LEU ASN ALA LEU ALA GLY THR THR TYR ASP GLY LYS SER          
SEQRES   8 A  241  ILE GLU GLU ILE ILE LEU ALA VAL ALA ASN ASP ALA GLU          
SEQRES   9 A  241  LYS LYS GLY LEU PHE ASN GLN ALA ALA GLN HIS PHE ASN          
SEQRES  10 A  241  HIS THR PHE TYR PHE ARG CYS ILE THR PRO ASN GLY LYS          
SEQRES  11 A  241  ALA MET PRO LYS SER PHE GLU SER ALA VAL THR ALA GLN          
SEQRES  12 A  241  PHE GLY SER VAL GLU GLN PHE LYS ASP ALA PHE VAL GLN          
SEQRES  13 A  241  ALA GLY VAL ASN ASN PHE GLY SER GLY TRP THR TRP LEU          
SEQRES  14 A  241  CYS VAL ASP PRO SER ASN LYS ASN GLN LEU VAL ILE ASP          
SEQRES  15 A  241  ASN THR SER ASN ALA GLY CYS PRO LEU THR LYS GLY LEU          
SEQRES  16 A  241  ARG PRO VAL LEU ALA VAL ASP VAL TRP GLU HIS ALA TYR          
SEQRES  17 A  241  TYR LYS ASP PHE GLU ASN ARG ARG PRO ASP TYR LEU LYS          
SEQRES  18 A  241  GLU ILE TRP SER VAL ILE ASP TRP GLU PHE VAL ALA LYS          
SEQRES  19 A  241  MET HIS ALA GLN ALA ILE LYS                                  
SEQRES   1 B  241  MET ALA HIS HIS HIS HIS HIS HIS MET LEU ARG ARG ALA          
SEQRES   2 B  241  VAL ASN ILE SER ILE ALA ARG GLY ARG MET ALA LEU MET          
SEQRES   3 B  241  SER TYR ALA THR LEU PRO ASP LEU LEU LYS PRO SER GLY          
SEQRES   4 B  241  ALA PRO ALA GLU LEU PRO LYS LEU GLY PHE ASN TRP LYS          
SEQRES   5 B  241  ASP GLY CYS ALA PRO VAL PHE SER PRO ARG GLN MET GLU          
SEQRES   6 B  241  LEU HIS TYR THR LYS HIS HIS LYS ALA TYR VAL ASP LYS          
SEQRES   7 B  241  LEU ASN ALA LEU ALA GLY THR THR TYR ASP GLY LYS SER          
SEQRES   8 B  241  ILE GLU GLU ILE ILE LEU ALA VAL ALA ASN ASP ALA GLU          
SEQRES   9 B  241  LYS LYS GLY LEU PHE ASN GLN ALA ALA GLN HIS PHE ASN          
SEQRES  10 B  241  HIS THR PHE TYR PHE ARG CYS ILE THR PRO ASN GLY LYS          
SEQRES  11 B  241  ALA MET PRO LYS SER PHE GLU SER ALA VAL THR ALA GLN          
SEQRES  12 B  241  PHE GLY SER VAL GLU GLN PHE LYS ASP ALA PHE VAL GLN          
SEQRES  13 B  241  ALA GLY VAL ASN ASN PHE GLY SER GLY TRP THR TRP LEU          
SEQRES  14 B  241  CYS VAL ASP PRO SER ASN LYS ASN GLN LEU VAL ILE ASP          
SEQRES  15 B  241  ASN THR SER ASN ALA GLY CYS PRO LEU THR LYS GLY LEU          
SEQRES  16 B  241  ARG PRO VAL LEU ALA VAL ASP VAL TRP GLU HIS ALA TYR          
SEQRES  17 B  241  TYR LYS ASP PHE GLU ASN ARG ARG PRO ASP TYR LEU LYS          
SEQRES  18 B  241  GLU ILE TRP SER VAL ILE ASP TRP GLU PHE VAL ALA LYS          
SEQRES  19 B  241  MET HIS ALA GLN ALA ILE LYS                                  
HET    FE2  A 301       1                                                       
HET    FE2  B 301       1                                                       
HETNAM     FE2 FE (II) ION                                                      
FORMUL   3  FE2    2(FE 2+)                                                     
FORMUL   5  HOH   *348(H2 O)                                                    
HELIX    1   1 ASN A   42  GLY A   46  5                                   5    
HELIX    2   2 SER A   52  LYS A   62  1                                  11    
HELIX    3   3 LYS A   62  GLY A   76  1                                  15    
HELIX    4   4 SER A   83  ALA A   92  1                                  10    
HELIX    5   5 ASP A   94  GLU A   96  5                                   3    
HELIX    6   6 LYS A   97  CYS A  116  1                                  20    
HELIX    7   7 PRO A  125  GLY A  137  1                                  13    
HELIX    8   8 SER A  138  ASN A  152  1                                  15    
HELIX    9   9 PRO A  165  LYS A  168  5                                   4    
HELIX   10  10 CYS A  181  GLY A  186  5                                   6    
HELIX   11  11 TRP A  196  ALA A  199  5                                   4    
HELIX   12  12 TYR A  200  GLU A  205  1                                   6    
HELIX   13  13 ARG A  207  ILE A  215  1                                   9    
HELIX   14  14 TRP A  216  ILE A  219  5                                   4    
HELIX   15  15 ASP A  220  LYS A  233  1                                  14    
HELIX   16  16 ASN B   42  GLY B   46  5                                   5    
HELIX   17  17 SER B   52  LYS B   62  1                                  11    
HELIX   18  18 LYS B   62  GLY B   76  1                                  15    
HELIX   19  19 SER B   83  ALA B   92  1                                  10    
HELIX   20  20 ASP B   94  GLU B   96  5                                   3    
HELIX   21  21 LYS B   97  CYS B  116  1                                  20    
HELIX   22  22 PRO B  125  GLY B  137  1                                  13    
HELIX   23  23 SER B  138  ASN B  152  1                                  15    
HELIX   24  24 PRO B  165  LYS B  168  5                                   4    
HELIX   25  25 CYS B  181  GLY B  186  5                                   6    
HELIX   26  26 TRP B  196  ALA B  199  5                                   4    
HELIX   27  27 TYR B  200  GLU B  205  1                                   6    
HELIX   28  28 ARG B  207  ILE B  215  1                                   9    
HELIX   29  29 TRP B  216  ILE B  219  5                                   4    
HELIX   30  30 ASP B  220  LYS B  233  1                                  14    
SHEET    1   A 3 LEU A 171  SER A 177  0                                        
SHEET    2   A 3 GLY A 157  VAL A 163 -1  N  CYS A 162   O  VAL A 172           
SHEET    3   A 3 ARG A 188  ASP A 194 -1  O  VAL A 190   N  LEU A 161           
SHEET    1   B 3 LEU B 171  SER B 177  0                                        
SHEET    2   B 3 GLY B 157  VAL B 163 -1  N  CYS B 162   O  VAL B 172           
SHEET    3   B 3 ARG B 188  ASP B 194 -1  O  VAL B 190   N  LEU B 161           
LINK         OD2 ASP B 194                FE   FE2 B 301     1555   1555  1.94  
LINK         OD2 ASP A 194                FE   FE2 A 301     1555   1555  2.01  
LINK         NE2 HIS B 110                FE   FE2 B 301     1555   1555  2.14  
LINK         NE2 HIS B 198                FE   FE2 B 301     1555   1555  2.15  
LINK         NE2 HIS A 198                FE   FE2 A 301     1555   1555  2.15  
LINK         NE2 HIS A 110                FE   FE2 A 301     1555   1555  2.16  
LINK         NE2 HIS A  59                FE   FE2 A 301     1555   1555  2.26  
LINK        FE   FE2 B 301                 O   HOH B 402     1555   1555  2.30  
LINK        FE   FE2 A 301                 O   HOH A 402     1555   1555  2.32  
LINK         NE2 HIS B  59                FE   FE2 B 301     1555   1555  2.33  
CISPEP   1 ALA A   48    PRO A   49          0         4.54                     
CISPEP   2 ALA B   48    PRO B   49          0         2.10                     
SITE     1 AC1  5 HIS A  59  HIS A 110  ASP A 194  HIS A 198                    
SITE     2 AC1  5 HOH A 402                                                     
SITE     1 AC2  5 HIS B  59  HIS B 110  ASP B 194  HIS B 198                    
SITE     2 AC2  5 HOH B 402                                                     
CRYST1   47.650   75.680  117.450  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      0.020986  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013214  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008514        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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