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Database: PDB
Entry: 2AQR
LinkDB: 2AQR
Original site: 2AQR 
HEADER    OXIDOREDUCTASE                          18-AUG-05   2AQR              
TITLE     CU/ZN SUPEROXIDE DISMUTASE FROM NEISSERIA MENINGITIDIS K91Q           
TITLE    2 MUTANT                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS;                         
SOURCE   3 ORGANISM_TAXID: 487;                                                 
SOURCE   4 GENE: SODC;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CU/ZN SUPEROXIDE DISMUTASE, ELECTROSTATIC GUIDANCE,                   
KEYWDS   2 NEISSERIA MENINGITIDIS, OXIDOREDUCTASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.DIDONATO,C.J.KASSMANN,C.K.BRUNS,D.E.CABELLI,Z.CAO,                  
AUTHOR   2 L.B.TABATABAI,J.S.KROLL,E.D.GETZOFF                                  
REVDAT   2   24-FEB-09 2AQR    1       VERSN                                    
REVDAT   1   31-OCT-06 2AQR    0                                                
JRNL        AUTH   M.DIDONATO,C.J.KASSMANN,C.K.BRUNS,D.E.CABELLI,               
JRNL        AUTH 2 Z.CAO,L.B.TABATABAI,J.S.KROLL,E.D.GETZOFF                    
JRNL        TITL   CU/ZN SUPEROXIDE DISMUTASE FROM NEISSERIA                    
JRNL        TITL 2 MENINGITIDIS K91Q MUTANT                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.47                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1814717.420                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 42445                          
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 SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.197                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4282                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.81                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3783                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2240                       
REMARK   3   BIN FREE R VALUE                    : 0.2490                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.50                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 444                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3456                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 462                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.54000                                             
REMARK   3    B22 (A**2) : 3.87000                                              
REMARK   3    B33 (A**2) : -0.34000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.95000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.17                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.11                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.19                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.14                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.84                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.200 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.820 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.090 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.170 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.41                                                 
REMARK   3   BSOL        : 50.60                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2AQR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-SEP-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB034203.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JUN-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 96                                 
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42545                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.34900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.360                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: WILD-TYPE                                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMSO4, PH 8.0, VAPOR DIFFUSION,          
REMARK 280  HANGING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       49.42000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.52600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       49.42000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       32.52600            
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, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 APPLY THE FOLLOWING TO CHAINS: C                                     
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10690 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 36000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CU    CU C 251  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 772  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A    23                                                      
REMARK 465     GLU A    24                                                      
REMARK 465     HIS A    25                                                      
REMARK 465     ASN A    26                                                      
REMARK 465     THR A    27                                                      
REMARK 465     ILE A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     LYS A    30                                                      
REMARK 465     GLY A    31                                                      
REMARK 465     HIS B    23                                                      
REMARK 465     GLU B    24                                                      
REMARK 465     HIS B    25                                                      
REMARK 465     ASN B    26                                                      
REMARK 465     THR B    27                                                      
REMARK 465     ILE B    28                                                      
REMARK 465     PRO B    29                                                      
REMARK 465     LYS B    30                                                      
REMARK 465     GLY B    31                                                      
REMARK 465     HIS C    23                                                      
REMARK 465     GLU C    24                                                      
REMARK 465     HIS C    25                                                      
REMARK 465     ASN C    26                                                      
REMARK 465     THR C    27                                                      
REMARK 465     ILE C    28                                                      
REMARK 465     PRO C    29                                                      
REMARK 465     LYS C    30                                                      
REMARK 465     GLY C    31                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLU C    73     OE1  GLU C    73     2555     1.69            
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    SER A  33      138.49   -175.04                                   
REMARK 500    VAL A  44      -67.28    -98.25                                   
REMARK 500    ASP A  67       73.02   -151.80                                   
REMARK 500    ASP A 120       37.03    -98.08                                   
REMARK 500    ASP B  67       72.90   -152.18                                   
REMARK 500    VAL C  44      -60.97    -90.78                                   
REMARK 500    ASP C  67       70.98   -151.48                                   
REMARK 500    ASP C 120       43.63   -100.25                                   
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 B 591        DISTANCE =  5.45 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                             CU1 A 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  79   ND1                                                    
REMARK 620 2 HIS A  81   NE2 139.7                                              
REMARK 620 3 HIS A 160   NE2 100.6 119.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 104   ND1                                                    
REMARK 620 2 HIS A 113   ND1 102.5                                              
REMARK 620 3 HIS A 122   ND1 104.0 122.0                                        
REMARK 620 4 ASP A 125   OD1 112.9  95.8 118.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 B 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  79   ND1                                                    
REMARK 620 2 HIS B  81   NE2 140.0                                              
REMARK 620 3 HIS B 160   NE2  97.5 122.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 104   ND1                                                    
REMARK 620 2 HIS B 113   ND1 101.6                                              
REMARK 620 3 HIS B 122   ND1 102.9 124.2                                        
REMARK 620 4 ASP B 125   OD1 107.9  97.1 121.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 C 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  79   ND1                                                    
REMARK 620 2 HIS C  81   NE2 139.4                                              
REMARK 620 3 HIS C 160   NE2 101.1 119.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 104   ND1                                                    
REMARK 620 2 HIS C 113   ND1 104.5                                              
REMARK 620 3 HIS C 122   ND1 103.9 121.3                                        
REMARK 620 4 ASP C 125   OD1 109.8  97.9 118.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 250  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  73   OE1                                                    
REMARK 620 2 HIS A 133   ND1 115.6                                              
REMARK 620 3 GLU B  73   OE1  78.2 117.3                                        
REMARK 620 4 HIS B 133   ND1 112.0 120.1 105.9                                  
REMARK 620 5 GLU A  73   OE2  53.3  83.2 131.2  98.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 251  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  73   OE1                                                    
REMARK 620 2 HIS C 133   ND1 107.9                                              
REMARK 620 3 GLU C  73   OE1  55.7 118.9                                        
REMARK 620 4 HIS C 133   ND1 122.2 122.4 112.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 200                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 B 200                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 C 200                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 250                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 251                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 201                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 201                  
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 201                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2AQM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2AQN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2AQP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2AQQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2AQS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2AQT   RELATED DB: PDB                                   
DBREF  2AQR A   23   186  UNP    Q59623   SODC_NEIMB      23    186             
DBREF  2AQR B   23   186  UNP    Q59623   SODC_NEIMB      23    186             
DBREF  2AQR C   23   186  UNP    Q59623   SODC_NEIMB      23    186             
SEQADV 2AQR GLN A   91  UNP  Q59623    LYS    91 ENGINEERED                     
SEQADV 2AQR GLN B   91  UNP  Q59623    LYS    91 ENGINEERED                     
SEQADV 2AQR GLN C   91  UNP  Q59623    LYS    91 ENGINEERED                     
SEQRES   1 A  164  HIS GLU HIS ASN THR ILE PRO LYS GLY ALA SER ILE GLU          
SEQRES   2 A  164  VAL LYS VAL GLN GLN LEU ASP PRO VAL ASN GLY ASN LYS          
SEQRES   3 A  164  ASP VAL GLY THR VAL THR ILE THR GLU SER ASN TYR GLY          
SEQRES   4 A  164  LEU VAL PHE THR PRO ASP LEU GLN GLY LEU SER GLU GLY          
SEQRES   5 A  164  LEU HIS GLY PHE HIS ILE HIS GLU ASN PRO SER CYS GLU          
SEQRES   6 A  164  PRO LYS GLU GLN GLU GLY LYS LEU THR ALA GLY LEU GLY          
SEQRES   7 A  164  ALA GLY GLY HIS TRP ASP PRO LYS GLY ALA LYS GLN HIS          
SEQRES   8 A  164  GLY TYR PRO TRP GLN ASP ASP ALA HIS LEU GLY ASP LEU          
SEQRES   9 A  164  PRO ALA LEU THR VAL LEU HIS ASP GLY THR ALA THR ASN          
SEQRES  10 A  164  PRO VAL LEU ALA PRO ARG LEU LYS HIS LEU ASP ASP VAL          
SEQRES  11 A  164  ARG GLY HIS SER ILE MET ILE HIS THR GLY GLY ASP ASN          
SEQRES  12 A  164  HIS SER ASP HIS PRO ALA PRO LEU GLY GLY GLY GLY PRO          
SEQRES  13 A  164  ARG MET ALA CYS GLY VAL ILE LYS                              
SEQRES   1 B  164  HIS GLU HIS ASN THR ILE PRO LYS GLY ALA SER ILE GLU          
SEQRES   2 B  164  VAL LYS VAL GLN GLN LEU ASP PRO VAL ASN GLY ASN LYS          
SEQRES   3 B  164  ASP VAL GLY THR VAL THR ILE THR GLU SER ASN TYR GLY          
SEQRES   4 B  164  LEU VAL PHE THR PRO ASP LEU GLN GLY LEU SER GLU GLY          
SEQRES   5 B  164  LEU HIS GLY PHE HIS ILE HIS GLU ASN PRO SER CYS GLU          
SEQRES   6 B  164  PRO LYS GLU GLN GLU GLY LYS LEU THR ALA GLY LEU GLY          
SEQRES   7 B  164  ALA GLY GLY HIS TRP ASP PRO LYS GLY ALA LYS GLN HIS          
SEQRES   8 B  164  GLY TYR PRO TRP GLN ASP ASP ALA HIS LEU GLY ASP LEU          
SEQRES   9 B  164  PRO ALA LEU THR VAL LEU HIS ASP GLY THR ALA THR ASN          
SEQRES  10 B  164  PRO VAL LEU ALA PRO ARG LEU LYS HIS LEU ASP ASP VAL          
SEQRES  11 B  164  ARG GLY HIS SER ILE MET ILE HIS THR GLY GLY ASP ASN          
SEQRES  12 B  164  HIS SER ASP HIS PRO ALA PRO LEU GLY GLY GLY GLY PRO          
SEQRES  13 B  164  ARG MET ALA CYS GLY VAL ILE LYS                              
SEQRES   1 C  164  HIS GLU HIS ASN THR ILE PRO LYS GLY ALA SER ILE GLU          
SEQRES   2 C  164  VAL LYS VAL GLN GLN LEU ASP PRO VAL ASN GLY ASN LYS          
SEQRES   3 C  164  ASP VAL GLY THR VAL THR ILE THR GLU SER ASN TYR GLY          
SEQRES   4 C  164  LEU VAL PHE THR PRO ASP LEU GLN GLY LEU SER GLU GLY          
SEQRES   5 C  164  LEU HIS GLY PHE HIS ILE HIS GLU ASN PRO SER CYS GLU          
SEQRES   6 C  164  PRO LYS GLU GLN GLU GLY LYS LEU THR ALA GLY LEU GLY          
SEQRES   7 C  164  ALA GLY GLY HIS TRP ASP PRO LYS GLY ALA LYS GLN HIS          
SEQRES   8 C  164  GLY TYR PRO TRP GLN ASP ASP ALA HIS LEU GLY ASP LEU          
SEQRES   9 C  164  PRO ALA LEU THR VAL LEU HIS ASP GLY THR ALA THR ASN          
SEQRES  10 C  164  PRO VAL LEU ALA PRO ARG LEU LYS HIS LEU ASP ASP VAL          
SEQRES  11 C  164  ARG GLY HIS SER ILE MET ILE HIS THR GLY GLY ASP ASN          
SEQRES  12 C  164  HIS SER ASP HIS PRO ALA PRO LEU GLY GLY GLY GLY PRO          
SEQRES  13 C  164  ARG MET ALA CYS GLY VAL ILE LYS                              
HET    CU1  A 200       1                                                       
HET    CU1  B 200       1                                                       
HET    CU1  C 200       1                                                       
HET     CU  A 250       1                                                       
HET     CU  C 251       1                                                       
HET     ZN  A 201       1                                                       
HET     ZN  B 201       1                                                       
HET     ZN  C 201       1                                                       
HETNAM     CU1 COPPER (I) ION                                                   
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
FORMUL   4  CU1    3(CU 1+)                                                     
FORMUL   7   CU    2(CU 2+)                                                     
FORMUL   9   ZN    3(ZN 2+)                                                     
FORMUL  12  HOH   *462(H2 O)                                                    
HELIX    1   1 GLY A   98  GLY A  102  5                                   5    
HELIX    2   2 HIS A  148  ARG A  153  1                                   6    
HELIX    3   3 ALA A  171  GLY A  176  5                                   6    
HELIX    4   4 GLY B   98  GLY B  102  5                                   5    
HELIX    5   5 HIS B  148  ARG B  153  1                                   6    
HELIX    6   6 ALA B  171  GLY B  176  5                                   6    
HELIX    7   7 GLY C   98  GLY C  102  5                                   5    
HELIX    8   8 HIS C  148  ARG C  153  1                                   6    
HELIX    9   9 ALA C  171  GLY C  176  5                                   6    
SHEET    1   A 7 PHE A  78  HIS A  81  0                                        
SHEET    2   A 7 HIS A 155  HIS A 160 -1  O  MET A 158   N  HIS A  79           
SHEET    3   A 7 ARG A 179  ILE A 185 -1  O  ILE A 185   N  HIS A 155           
SHEET    4   A 7 ILE A  34  GLN A  40 -1  N  GLN A  39   O  CYS A 182           
SHEET    5   A 7 LYS A  48  SER A  58 -1  O  LYS A  48   N  GLN A  40           
SHEET    6   A 7 GLY A  61  LEU A  68 -1  O  THR A  65   N  THR A  54           
SHEET    7   A 7 VAL A 141  ALA A 143 -1  O  VAL A 141   N  PHE A  64           
SHEET    1   B 2 GLY A  74  HIS A  76  0                                        
SHEET    2   B 2 LEU A 129  VAL A 131 -1  O  VAL A 131   N  GLY A  74           
SHEET    1   C 2 LYS A  89  GLU A  90  0                                        
SHEET    2   C 2 LEU A  95  THR A  96 -1  O  THR A  96   N  LYS A  89           
SHEET    1   D 7 PHE B  78  HIS B  81  0                                        
SHEET    2   D 7 HIS B 155  HIS B 160 -1  O  MET B 158   N  HIS B  79           
SHEET    3   D 7 ARG B 179  ILE B 185 -1  O  ALA B 181   N  ILE B 159           
SHEET    4   D 7 SER B  33  GLN B  40 -1  N  GLN B  39   O  CYS B 182           
SHEET    5   D 7 LYS B  48  SER B  58 -1  O  LYS B  48   N  GLN B  40           
SHEET    6   D 7 GLY B  61  LEU B  68 -1  O  THR B  65   N  THR B  54           
SHEET    7   D 7 VAL B 141  ALA B 143 -1  O  VAL B 141   N  PHE B  64           
SHEET    1   E 2 GLY B  74  HIS B  76  0                                        
SHEET    2   E 2 LEU B 129  VAL B 131 -1  O  VAL B 131   N  GLY B  74           
SHEET    1   F 2 LYS B  89  GLN B  91  0                                        
SHEET    2   F 2 LYS B  94  THR B  96 -1  O  THR B  96   N  LYS B  89           
SHEET    1   G 7 PHE C  78  HIS C  81  0                                        
SHEET    2   G 7 HIS C 155  HIS C 160 -1  O  MET C 158   N  HIS C  79           
SHEET    3   G 7 ARG C 179  ILE C 185 -1  O  ALA C 181   N  ILE C 159           
SHEET    4   G 7 SER C  33  GLN C  40 -1  N  GLN C  39   O  CYS C 182           
SHEET    5   G 7 LYS C  48  SER C  58 -1  O  LYS C  48   N  GLN C  40           
SHEET    6   G 7 GLY C  61  LEU C  68 -1  O  THR C  65   N  THR C  54           
SHEET    7   G 7 VAL C 141  ALA C 143 -1  O  VAL C 141   N  PHE C  64           
SHEET    1   H 2 GLY C  74  HIS C  76  0                                        
SHEET    2   H 2 LEU C 129  VAL C 131 -1  O  VAL C 131   N  GLY C  74           
SHEET    1   I 2 LYS C  89  GLN C  91  0                                        
SHEET    2   I 2 LYS C  94  THR C  96 -1  O  LYS C  94   N  GLN C  91           
SSBOND   1 CYS A   86    CYS A  182                          1555   1555  2.03  
SSBOND   2 CYS B   86    CYS B  182                          1555   1555  2.04  
SSBOND   3 CYS C   86    CYS C  182                          1555   1555  2.04  
LINK        CU   CU1 A 200                 ND1 HIS A  79     1555   1555  2.10  
LINK        CU   CU1 A 200                 NE2 HIS A  81     1555   1555  2.01  
LINK        CU   CU1 A 200                 NE2 HIS A 160     1555   1555  2.05  
LINK        ZN    ZN A 201                 ND1 HIS A 104     1555   1555  2.02  
LINK        ZN    ZN A 201                 ND1 HIS A 113     1555   1555  2.07  
LINK        ZN    ZN A 201                 ND1 HIS A 122     1555   1555  2.09  
LINK        ZN    ZN A 201                 OD1 ASP A 125     1555   1555  1.93  
LINK        CU   CU1 B 200                 ND1 HIS B  79     1555   1555  2.06  
LINK        CU   CU1 B 200                 NE2 HIS B  81     1555   1555  2.03  
LINK        CU   CU1 B 200                 NE2 HIS B 160     1555   1555  2.05  
LINK        ZN    ZN B 201                 ND1 HIS B 104     1555   1555  2.06  
LINK        ZN    ZN B 201                 ND1 HIS B 113     1555   1555  2.08  
LINK        ZN    ZN B 201                 ND1 HIS B 122     1555   1555  2.11  
LINK        ZN    ZN B 201                 OD1 ASP B 125     1555   1555  1.94  
LINK        CU   CU1 C 200                 ND1 HIS C  79     1555   1555  2.08  
LINK        CU   CU1 C 200                 NE2 HIS C  81     1555   1555  2.04  
LINK        CU   CU1 C 200                 NE2 HIS C 160     1555   1555  2.10  
LINK        ZN    ZN C 201                 ND1 HIS C 104     1555   1555  2.01  
LINK        ZN    ZN C 201                 ND1 HIS C 113     1555   1555  2.09  
LINK        ZN    ZN C 201                 ND1 HIS C 122     1555   1555  2.09  
LINK        ZN    ZN C 201                 OD1 ASP C 125     1555   1555  1.95  
LINK        CU    CU A 250                 OE1 GLU A  73     1555   1555  1.91  
LINK        CU    CU A 250                 ND1 HIS A 133     1555   1555  2.05  
LINK        CU    CU A 250                 OE1 GLU B  73     1555   1555  2.05  
LINK        CU    CU A 250                 ND1 HIS B 133     1555   1555  2.09  
LINK        CU    CU C 251                 OE1 GLU C  73     1555   1555  1.82  
LINK        CU    CU C 251                 ND1 HIS C 133     1555   1555  2.05  
LINK        CU    CU A 250                 OE2 GLU A  73     1555   1555  2.71  
LINK        CU    CU C 251                 OE1 GLU C  73     1555   2555  1.80  
LINK        CU    CU C 251                 ND1 HIS C 133     1555   2555  1.96  
CISPEP   1 HIS A  169    PRO A  170          0         0.07                     
CISPEP   2 HIS B  169    PRO B  170          0        -0.05                     
CISPEP   3 HIS C  169    PRO C  170          0        -0.01                     
SITE     1 AC1  4 HIS A  79  HIS A  81  HIS A 104  HIS A 160                    
SITE     1 AC2  4 HIS B  79  HIS B  81  HIS B 104  HIS B 160                    
SITE     1 AC3  4 HIS C  79  HIS C  81  HIS C 104  HIS C 160                    
SITE     1 AC4  4 GLU A  73  HIS A 133  GLU B  73  HIS B 133                    
SITE     1 AC5  2 GLU C  73  HIS C 133                                          
SITE     1 AC6  4 HIS A 104  HIS A 113  HIS A 122  ASP A 125                    
SITE     1 AC7  4 HIS B 104  HIS B 113  HIS B 122  ASP B 125                    
SITE     1 AC8  4 HIS C 104  HIS C 113  HIS C 122  ASP C 125                    
CRYST1   98.840   65.052   77.443  90.00 121.02  90.00 C 1 2 1      12          
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      0.010117  0.000000  0.006085        0.00000                         
SCALE2      0.000000  0.015372  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015068        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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