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Database: PDB
Entry: 2NYB
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Original site: 2NYB 
HEADER    OXIDOREDUCTASE                          20-NOV-06   2NYB              
TITLE     CRYSTAL STRUCTURE OF E.COLI IRON SUPEROXIDE DISMUTASE Q69E            
TITLE    2 AT 1.1 ANGSTROM RESOLUTION                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [FE];                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: IRON SUPEROXIDE DISMUTASE;                                  
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: SODB, B1656, JW1648;                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    IRON SUPEROXIDE DISMUTASE Q69E, FESOD, OXIDOREDUCTASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.C.PORTA,A.VAHEDI-FARIDI,G.E.O.BORGSTAHL                             
REVDAT   3   24-FEB-09 2NYB    1       VERSN                                    
REVDAT   2   04-SEP-07 2NYB    1       JRNL                                     
REVDAT   1   05-DEC-06 2NYB    0                                                
JRNL        AUTH   E.YIKILMAZ,J.PORTA,L.E.GROVE,A.VAHEDI-FARIDI,                
JRNL        AUTH 2 Y.BRONSHTEYN,T.C.BRUNOLD,G.E.BORGSTAHL,A.F.MILLER            
JRNL        TITL   HOW CAN A SINGLE SECOND SPHERE AMINO ACID                    
JRNL        TITL 2 SUBSTITUTION CAUSE REDUCTION MIDPOINT POTENTIAL              
JRNL        TITL 3 CHANGES OF HUNDREDS OF MILLIVOLTS?                           
JRNL        REF    J.AM.CHEM.SOC.                V. 129  9927 2007              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   17628062                                                     
JRNL        DOI    10.1021/JA069224T                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.29                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 269833                         
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) : 0.160                           
REMARK   3   R VALUE            (WORKING SET) : 0.160                           
REMARK   3   FREE R VALUE                     : 0.174                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 14104                           
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) : 1.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.13                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 17777                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2130                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 961                          
REMARK   3   BIN FREE R VALUE                    : 0.2340                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6661                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 1144                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.75                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.75                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.07000                                              
REMARK   3    B22 (A**2) : 0.04000                                              
REMARK   3    B33 (A**2) : -0.14000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.13000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.035         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.033         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.020         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.902         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.973                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.968                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6937 ; 0.007 ; 0.023       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9540 ; 1.067 ; 1.922       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   911 ; 5.176 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   319 ;33.901 ;24.859       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1034 ;11.187 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;14.258 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   998 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5606 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3624 ; 0.195 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4977 ; 0.306 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   852 ; 0.076 ; 0.200       
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):    65 ; 0.155 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    70 ; 0.085 ; 0.200       
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):  4376 ; 0.548 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6942 ; 0.868 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3002 ; 1.287 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2598 ; 1.707 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  7378 ; 0.854 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  1148 ; 2.114 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  6661 ; 1.907 ; 3.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2NYB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB040453.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.88557                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 283939                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.290                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 1.050                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.02700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM AMMONIUM ACETATE PH 5.7, 10       
REMARK 280  MM SODIUM CITRATE, 22.5% PEG 4000, VAPOR DIFFUSION, HANGING         
REMARK 280  DROP, TEMPERATURE 298K                                              
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       53.79800            
REMARK 290   SMTRY3   2  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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HOMOTETRAMER GENERATED BY       
REMARK 300 THE TWO-FOLD AXIS: -X, Y+1/2, -Z.                                    
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: 1840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16440 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 1840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A  184   CG    CD    OE1   OE2                               
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    PRO A   8        1.12    -69.85                                   
REMARK 500    ALA A  84     -137.90   -127.00                                   
REMARK 500    ASN A 140     -116.80     59.73                                   
REMARK 500    ARG A 167     -132.12     52.55                                   
REMARK 500    LYS B  29      -62.08   -107.70                                   
REMARK 500    ALA B  84     -138.60   -126.45                                   
REMARK 500    ASN B 140     -114.83     58.68                                   
REMARK 500    ARG B 167     -131.73     51.32                                   
REMARK 500    ALA C  84     -136.49   -130.32                                   
REMARK 500    ASN C 140     -114.09     57.43                                   
REMARK 500    ARG C 167     -130.61     51.09                                   
REMARK 500    LYS D  29      -54.08   -120.69                                   
REMARK 500    SER D  58       20.15   -145.01                                   
REMARK 500    ALA D  84     -138.92   -130.96                                   
REMARK 500    ASN D 140     -117.38     60.65                                   
REMARK 500    ARG D 167     -130.57     51.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C 304        DISTANCE =  6.62 ANGSTROMS                       
REMARK 525    HOH B 466        DISTANCE =  6.44 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A 193  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  26   NE2                                                    
REMARK 620 2 HIS A  73   NE2  89.6                                              
REMARK 620 3 ASP A 156   OD2  85.1 112.8                                        
REMARK 620 4 HIS A 160   NE2  89.8 125.8 121.1                                  
REMARK 620 5   O A 194   O   179.5  89.9  94.8  90.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 B 193  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  26   NE2                                                    
REMARK 620 2 HIS B  73   NE2  91.0                                              
REMARK 620 3 ASP B 156   OD2  85.5 113.4                                        
REMARK 620 4 HIS B 160   NE2  89.4 127.9 118.6                                  
REMARK 620 5   O B 194   O   179.3  89.7  94.3  90.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 C 193  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  26   NE2                                                    
REMARK 620 2 HIS C  73   NE2  89.9                                              
REMARK 620 3 ASP C 156   OD2  86.4 111.6                                        
REMARK 620 4 HIS C 160   NE2  89.8 128.1 120.2                                  
REMARK 620 5   O C 194   O   178.7  89.0  93.3  91.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 D 193  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  26   NE2                                                    
REMARK 620 2 HIS D  73   NE2  91.7                                              
REMARK 620 3 ASP D 156   OD2  85.7 112.3                                        
REMARK 620 4 HIS D 160   NE2  90.4 127.0 120.7                                  
REMARK 620 5   O D 194   O   179.1  89.2  93.7  89.3                            
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 193                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 B 193                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 C 193                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 D 193                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE O A 194                   
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE O B 194                   
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE O C 194                   
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE O D 194                   
DBREF  2NYB A    1   192  UNP    P0AGD3   SODF_ECOLI       1    192             
DBREF  2NYB B    1   192  UNP    P0AGD3   SODF_ECOLI       1    192             
DBREF  2NYB C    1   192  UNP    P0AGD3   SODF_ECOLI       1    192             
DBREF  2NYB D    1   192  UNP    P0AGD3   SODF_ECOLI       1    192             
SEQADV 2NYB GLU A   69  UNP  P0AGD3    GLN    69 ENGINEERED                     
SEQADV 2NYB GLU B   69  UNP  P0AGD3    GLN    69 ENGINEERED                     
SEQADV 2NYB GLU C   69  UNP  P0AGD3    GLN    69 ENGINEERED                     
SEQADV 2NYB GLU D   69  UNP  P0AGD3    GLN    69 ENGINEERED                     
SEQRES   1 A  192  SER PHE GLU LEU PRO ALA LEU PRO TYR ALA LYS ASP ALA          
SEQRES   2 A  192  LEU ALA PRO HIS ILE SER ALA GLU THR ILE GLU TYR HIS          
SEQRES   3 A  192  TYR GLY LYS HIS HIS GLN THR TYR VAL THR ASN LEU ASN          
SEQRES   4 A  192  ASN LEU ILE LYS GLY THR ALA PHE GLU GLY LYS SER LEU          
SEQRES   5 A  192  GLU GLU ILE ILE ARG SER SER GLU GLY GLY VAL PHE ASN          
SEQRES   6 A  192  ASN ALA ALA GLU VAL TRP ASN HIS THR PHE TYR TRP ASN          
SEQRES   7 A  192  CYS LEU ALA PRO ASN ALA GLY GLY GLU PRO THR GLY LYS          
SEQRES   8 A  192  VAL ALA GLU ALA ILE ALA ALA SER PHE GLY SER PHE ALA          
SEQRES   9 A  192  ASP PHE LYS ALA GLN PHE THR ASP ALA ALA ILE LYS ASN          
SEQRES  10 A  192  PHE GLY SER GLY TRP THR TRP LEU VAL LYS ASN SER ASP          
SEQRES  11 A  192  GLY LYS LEU ALA ILE VAL SER THR SER ASN ALA GLY THR          
SEQRES  12 A  192  PRO LEU THR THR ASP ALA THR PRO LEU LEU THR VAL ASP          
SEQRES  13 A  192  VAL TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN ALA          
SEQRES  14 A  192  ARG PRO GLY TYR LEU GLU HIS PHE TRP ALA LEU VAL ASN          
SEQRES  15 A  192  TRP GLU PHE VAL ALA LYS ASN LEU ALA ALA                      
SEQRES   1 B  192  SER PHE GLU LEU PRO ALA LEU PRO TYR ALA LYS ASP ALA          
SEQRES   2 B  192  LEU ALA PRO HIS ILE SER ALA GLU THR ILE GLU TYR HIS          
SEQRES   3 B  192  TYR GLY LYS HIS HIS GLN THR TYR VAL THR ASN LEU ASN          
SEQRES   4 B  192  ASN LEU ILE LYS GLY THR ALA PHE GLU GLY LYS SER LEU          
SEQRES   5 B  192  GLU GLU ILE ILE ARG SER SER GLU GLY GLY VAL PHE ASN          
SEQRES   6 B  192  ASN ALA ALA GLU VAL TRP ASN HIS THR PHE TYR TRP ASN          
SEQRES   7 B  192  CYS LEU ALA PRO ASN ALA GLY GLY GLU PRO THR GLY LYS          
SEQRES   8 B  192  VAL ALA GLU ALA ILE ALA ALA SER PHE GLY SER PHE ALA          
SEQRES   9 B  192  ASP PHE LYS ALA GLN PHE THR ASP ALA ALA ILE LYS ASN          
SEQRES  10 B  192  PHE GLY SER GLY TRP THR TRP LEU VAL LYS ASN SER ASP          
SEQRES  11 B  192  GLY LYS LEU ALA ILE VAL SER THR SER ASN ALA GLY THR          
SEQRES  12 B  192  PRO LEU THR THR ASP ALA THR PRO LEU LEU THR VAL ASP          
SEQRES  13 B  192  VAL TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN ALA          
SEQRES  14 B  192  ARG PRO GLY TYR LEU GLU HIS PHE TRP ALA LEU VAL ASN          
SEQRES  15 B  192  TRP GLU PHE VAL ALA LYS ASN LEU ALA ALA                      
SEQRES   1 C  192  SER PHE GLU LEU PRO ALA LEU PRO TYR ALA LYS ASP ALA          
SEQRES   2 C  192  LEU ALA PRO HIS ILE SER ALA GLU THR ILE GLU TYR HIS          
SEQRES   3 C  192  TYR GLY LYS HIS HIS GLN THR TYR VAL THR ASN LEU ASN          
SEQRES   4 C  192  ASN LEU ILE LYS GLY THR ALA PHE GLU GLY LYS SER LEU          
SEQRES   5 C  192  GLU GLU ILE ILE ARG SER SER GLU GLY GLY VAL PHE ASN          
SEQRES   6 C  192  ASN ALA ALA GLU VAL TRP ASN HIS THR PHE TYR TRP ASN          
SEQRES   7 C  192  CYS LEU ALA PRO ASN ALA GLY GLY GLU PRO THR GLY LYS          
SEQRES   8 C  192  VAL ALA GLU ALA ILE ALA ALA SER PHE GLY SER PHE ALA          
SEQRES   9 C  192  ASP PHE LYS ALA GLN PHE THR ASP ALA ALA ILE LYS ASN          
SEQRES  10 C  192  PHE GLY SER GLY TRP THR TRP LEU VAL LYS ASN SER ASP          
SEQRES  11 C  192  GLY LYS LEU ALA ILE VAL SER THR SER ASN ALA GLY THR          
SEQRES  12 C  192  PRO LEU THR THR ASP ALA THR PRO LEU LEU THR VAL ASP          
SEQRES  13 C  192  VAL TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN ALA          
SEQRES  14 C  192  ARG PRO GLY TYR LEU GLU HIS PHE TRP ALA LEU VAL ASN          
SEQRES  15 C  192  TRP GLU PHE VAL ALA LYS ASN LEU ALA ALA                      
SEQRES   1 D  192  SER PHE GLU LEU PRO ALA LEU PRO TYR ALA LYS ASP ALA          
SEQRES   2 D  192  LEU ALA PRO HIS ILE SER ALA GLU THR ILE GLU TYR HIS          
SEQRES   3 D  192  TYR GLY LYS HIS HIS GLN THR TYR VAL THR ASN LEU ASN          
SEQRES   4 D  192  ASN LEU ILE LYS GLY THR ALA PHE GLU GLY LYS SER LEU          
SEQRES   5 D  192  GLU GLU ILE ILE ARG SER SER GLU GLY GLY VAL PHE ASN          
SEQRES   6 D  192  ASN ALA ALA GLU VAL TRP ASN HIS THR PHE TYR TRP ASN          
SEQRES   7 D  192  CYS LEU ALA PRO ASN ALA GLY GLY GLU PRO THR GLY LYS          
SEQRES   8 D  192  VAL ALA GLU ALA ILE ALA ALA SER PHE GLY SER PHE ALA          
SEQRES   9 D  192  ASP PHE LYS ALA GLN PHE THR ASP ALA ALA ILE LYS ASN          
SEQRES  10 D  192  PHE GLY SER GLY TRP THR TRP LEU VAL LYS ASN SER ASP          
SEQRES  11 D  192  GLY LYS LEU ALA ILE VAL SER THR SER ASN ALA GLY THR          
SEQRES  12 D  192  PRO LEU THR THR ASP ALA THR PRO LEU LEU THR VAL ASP          
SEQRES  13 D  192  VAL TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN ALA          
SEQRES  14 D  192  ARG PRO GLY TYR LEU GLU HIS PHE TRP ALA LEU VAL ASN          
SEQRES  15 D  192  TRP GLU PHE VAL ALA LYS ASN LEU ALA ALA                      
HET    FE2  A 193       1                                                       
HET    FE2  B 193       1                                                       
HET    FE2  C 193       1                                                       
HET    FE2  D 193       1                                                       
HET      O  A 194       1                                                       
HET      O  B 194       1                                                       
HET      O  C 194       1                                                       
HET      O  D 194       1                                                       
HETNAM     FE2 FE (II) ION                                                      
HETNAM       O OXYGEN ATOM                                                      
FORMUL   5  FE2    4(FE 2+)                                                     
FORMUL   9    O    4(O)                                                         
FORMUL  13  HOH   *1144(H2 O)                                                   
HELIX    1   1 SER A   19  LYS A   29  1                                  11    
HELIX    2   2 LYS A   29  LYS A   43  1                                  15    
HELIX    3   3 SER A   51  ARG A   57  1                                   7    
HELIX    4   4 GLU A   60  CYS A   79  1                                  20    
HELIX    5   5 THR A   89  GLY A  101  1                                  13    
HELIX    6   6 SER A  102  ASN A  117  1                                  16    
HELIX    7   7 THR A  143  THR A  147  5                                   5    
HELIX    8   8 TRP A  158  ALA A  161  5                                   4    
HELIX    9   9 TYR A  162  ARG A  167  1                                   6    
HELIX   10  10 ALA A  169  ALA A  179  1                                  11    
HELIX   11  11 ASN A  182  ALA A  192  1                                  11    
HELIX   12  12 SER B   19  TYR B   27  1                                   9    
HELIX   13  13 LYS B   29  LYS B   43  1                                  15    
HELIX   14  14 SER B   51  ARG B   57  1                                   7    
HELIX   15  15 GLU B   60  CYS B   79  1                                  20    
HELIX   16  16 THR B   89  GLY B  101  1                                  13    
HELIX   17  17 SER B  102  ASN B  117  1                                  16    
HELIX   18  18 THR B  143  THR B  147  5                                   5    
HELIX   19  19 TRP B  158  ALA B  161  5                                   4    
HELIX   20  20 TYR B  162  ARG B  167  1                                   6    
HELIX   21  21 ALA B  169  TRP B  178  1                                  10    
HELIX   22  22 ASN B  182  ALA B  192  1                                  11    
HELIX   23  23 SER C   19  TYR C   27  1                                   9    
HELIX   24  24 LYS C   29  LYS C   43  1                                  15    
HELIX   25  25 SER C   51  ARG C   57  1                                   7    
HELIX   26  26 GLU C   60  CYS C   79  1                                  20    
HELIX   27  27 THR C   89  GLY C  101  1                                  13    
HELIX   28  28 SER C  102  LYS C  116  1                                  15    
HELIX   29  29 THR C  143  THR C  147  5                                   5    
HELIX   30  30 TRP C  158  ALA C  161  5                                   4    
HELIX   31  31 TYR C  162  ARG C  167  1                                   6    
HELIX   32  32 ALA C  169  TRP C  178  1                                  10    
HELIX   33  33 ASN C  182  ALA C  192  1                                  11    
HELIX   34  34 SER D   19  TYR D   27  1                                   9    
HELIX   35  35 LYS D   29  LYS D   43  1                                  15    
HELIX   36  36 SER D   51  ARG D   57  1                                   7    
HELIX   37  37 GLU D   60  CYS D   79  1                                  20    
HELIX   38  38 THR D   89  GLY D  101  1                                  13    
HELIX   39  39 SER D  102  ASN D  117  1                                  16    
HELIX   40  40 THR D  143  THR D  147  5                                   5    
HELIX   41  41 TRP D  158  ALA D  161  5                                   4    
HELIX   42  42 TYR D  162  ARG D  167  1                                   6    
HELIX   43  43 ALA D  169  TRP D  178  1                                  10    
HELIX   44  44 ASN D  182  ALA D  192  1                                  11    
SHEET    1   A 3 LEU A 133  SER A 139  0                                        
SHEET    2   A 3 GLY A 121  LYS A 127 -1  N  TRP A 124   O  VAL A 136           
SHEET    3   A 3 THR A 150  ASP A 156 -1  O  LEU A 152   N  LEU A 125           
SHEET    1   B 3 LEU B 133  SER B 139  0                                        
SHEET    2   B 3 GLY B 121  LYS B 127 -1  N  TRP B 124   O  VAL B 136           
SHEET    3   B 3 THR B 150  ASP B 156 -1  O  LEU B 152   N  LEU B 125           
SHEET    1   C 3 LEU C 133  SER C 139  0                                        
SHEET    2   C 3 GLY C 121  LYS C 127 -1  N  TRP C 124   O  VAL C 136           
SHEET    3   C 3 THR C 150  ASP C 156 -1  O  LEU C 152   N  LEU C 125           
SHEET    1   D 3 LEU D 133  SER D 139  0                                        
SHEET    2   D 3 GLY D 121  LYS D 127 -1  N  TRP D 124   O  VAL D 136           
SHEET    3   D 3 THR D 150  ASP D 156 -1  O  LEU D 152   N  LEU D 125           
LINK         NE2 HIS A  26                FE   FE2 A 193     1555   1555  2.21  
LINK         NE2 HIS A  73                FE   FE2 A 193     1555   1555  2.13  
LINK         OD2 ASP A 156                FE   FE2 A 193     1555   1555  1.96  
LINK         NE2 HIS A 160                FE   FE2 A 193     1555   1555  2.12  
LINK         O     O A 194                FE   FE2 A 193     1555   1555  2.16  
LINK         NE2 HIS B  26                FE   FE2 B 193     1555   1555  2.22  
LINK         NE2 HIS B  73                FE   FE2 B 193     1555   1555  2.10  
LINK         OD2 ASP B 156                FE   FE2 B 193     1555   1555  1.95  
LINK         NE2 HIS B 160                FE   FE2 B 193     1555   1555  2.14  
LINK         O     O B 194                FE   FE2 B 193     1555   1555  2.15  
LINK         NE2 HIS C  26                FE   FE2 C 193     1555   1555  2.20  
LINK         NE2 HIS C  73                FE   FE2 C 193     1555   1555  2.12  
LINK         OD2 ASP C 156                FE   FE2 C 193     1555   1555  1.94  
LINK         NE2 HIS C 160                FE   FE2 C 193     1555   1555  2.12  
LINK         O     O C 194                FE   FE2 C 193     1555   1555  2.14  
LINK         NE2 HIS D  26                FE   FE2 D 193     1555   1555  2.19  
LINK         NE2 HIS D  73                FE   FE2 D 193     1555   1555  2.10  
LINK         OD2 ASP D 156                FE   FE2 D 193     1555   1555  1.94  
LINK         NE2 HIS D 160                FE   FE2 D 193     1555   1555  2.13  
LINK         O     O D 194                FE   FE2 D 193     1555   1555  2.19  
CISPEP   1 ALA A   15    PRO A   16          0         1.98                     
CISPEP   2 ALA B   15    PRO B   16          0         0.60                     
CISPEP   3 ALA C   15    PRO C   16          0         1.74                     
CISPEP   4 ALA D   15    PRO D   16          0         0.53                     
SITE     1 AC1  5 HIS A  26  HIS A  73  ASP A 156  HIS A 160                    
SITE     2 AC1  5   O A 194                                                     
SITE     1 AC2  5 HIS B  26  HIS B  73  ASP B 156  HIS B 160                    
SITE     2 AC2  5   O B 194                                                     
SITE     1 AC3  5 HIS C  26  HIS C  73  ASP C 156  HIS C 160                    
SITE     2 AC3  5   O C 194                                                     
SITE     1 AC4  5 HIS D  26  HIS D  73  ASP D 156  HIS D 160                    
SITE     2 AC4  5   O D 194                                                     
SITE     1 AC5  7 GLU A  69  HIS A  73  TRP A 122  ASP A 156                    
SITE     2 AC5  7 TRP A 158  HIS A 160  FE2 A 193                               
SITE     1 AC6  7 GLU B  69  HIS B  73  TRP B 122  ASP B 156                    
SITE     2 AC6  7 TRP B 158  HIS B 160  FE2 B 193                               
SITE     1 AC7  7 GLU C  69  HIS C  73  TRP C 122  ASP C 156                    
SITE     2 AC7  7 TRP C 158  HIS C 160  FE2 C 193                               
SITE     1 AC8  7 GLU D  69  HIS D  73  TRP D 122  ASP D 156                    
SITE     2 AC8  7 TRP D 158  HIS D 160  FE2 D 193                               
CRYST1   43.508  107.596   84.120  90.00  94.89  90.00 P 1 21 1      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      0.022984  0.000000  0.001965        0.00000                         
SCALE2      0.000000  0.009294  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011931        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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