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Database: PDB
Entry: 2AQN
LinkDB: 2AQN
Original site: 2AQN 
HEADER    OXIDOREDUCTASE                          18-AUG-05   2AQN              
TITLE     CU/ZN SUPEROXIDE DISMUTASE FROM NEISSERIA MENINGITIDIS                
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                                                      
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    SUPEROXIDE DISMUTASE, NEISSERIA MENINGITIDIS.,                        
KEYWDS   2 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 2AQN    1       VERSN                                    
REVDAT   1   31-OCT-06 2AQN    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                                                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.7                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.128                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.129                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.190                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 4009                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 80120                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.118                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.119                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.179                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 3325                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 66643                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 3482                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 13                                            
REMARK   3   SOLVENT ATOMS      : 530                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 3994.32                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 3303.00                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 9                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 36222                   
REMARK   3   NUMBER OF RESTRAINTS                     : 43967                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.011                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.028                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.030                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.058                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.064                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.022                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.003                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.051                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.079                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT DECREASED R        
REMARK   3  BY 5.24 %                                                           
REMARK   4                                                                      
REMARK   4 2AQN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-AUG-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB034199.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-FEB-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 96                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08                               
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 80120                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.04500                            
REMARK 200  R SYM                      (I) : 0.04500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.25200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
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: PDB ENTRY 2APS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMSO4, PH 7.5, 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       49.89550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.29600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       49.89550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       32.29600            
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: 2050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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       51.24533            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       66.98934            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11320 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 35830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -118.0 KCAL/MOL                       
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       64.59200            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       51.24533            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       64.59200            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       66.98934            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000       51.24533            
REMARK 350   BIOMT2   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000       66.98934            
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 301  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 850  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 831  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 874  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 948  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 825  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: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ALA A  32   CA  -  C   -  O   ANGL. DEV. = -15.6 DEGREES          
REMARK 500    ALA A  32   CA  -  C   -  N   ANGL. DEV. =  17.7 DEGREES          
REMARK 500    ARG A 145   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG B 145   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG B 145   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG B 153   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG B 153   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG C 145   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG C 179   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG C 179   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  33      130.34   -171.62                                   
REMARK 500    ASP C 106       58.03   -148.03                                   
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 817        DISTANCE =  5.94 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 143.8                                              
REMARK 620 3 HIS A 160   NE2  99.4 116.7                                        
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 103.8                                              
REMARK 620 3 HIS A 122   ND1 103.1 124.6                                        
REMARK 620 4 ASP A 125   OD1 108.7  98.7 116.8                                  
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 142.6                                              
REMARK 620 3 HIS B 160   NE2  98.3 119.1                                        
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 102.3                                              
REMARK 620 3 HIS B 122   ND1 105.8 120.7                                        
REMARK 620 4 ASP B 125   OD1 109.3 100.0 117.6                                  
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 142.2                                              
REMARK 620 3 HIS C 160   NE2  98.4 119.4                                        
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 107.6                                              
REMARK 620 3 HIS C 122   ND1 102.4 124.2                                        
REMARK 620 4 ASP C 125   OD1 108.7  98.8 114.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 300  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  73   OE1                                                    
REMARK 620 2 HIS A 133   ND1 110.6                                              
REMARK 620 3 GLU B  73   OE1  75.9 117.4                                        
REMARK 620 4 HIS B 133   ND1 123.1 113.8 111.2                                  
REMARK 620 5 GLU A  73   OE2  51.8  87.0 127.6  97.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 301  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  73   OE1                                                    
REMARK 620 2 HIS C 133   ND1 101.3                                              
REMARK 620 3 GLU C  73   OE2  52.1  86.2                                        
REMARK 620 4 GLU C  73   OE1  85.1 125.5 132.8                                  
REMARK 620 5 GLU C  73   OE2 132.9  91.1 174.9  52.1                            
REMARK 620 6 HIS C 133   ND1 125.5 116.3  91.0 101.4  86.3                      
REMARK 620 N                    1     2     3     4     5                       
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 ZN A 201                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 B 200                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 201                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 C 200                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 201                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 300                  
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 301                  
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 400                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2AQM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2AQP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2AQQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2AQR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2AQS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2AQT   RELATED DB: PDB                                   
DBREF  2AQN A   23   186  UNP    Q59623   SODC_NEIMB      23    186             
DBREF  2AQN B   23   186  UNP    Q59623   SODC_NEIMB      23    186             
DBREF  2AQN C   23   186  UNP    Q59623   SODC_NEIMB      23    186             
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 LYS 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 LYS 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 LYS 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     ZN  A 201       1                                                       
HET    CU1  B 200       1                                                       
HET     ZN  B 201       1                                                       
HET    CU1  C 200       1                                                       
HET     ZN  C 201       1                                                       
HET     CU  A 300       1                                                       
HET     CU  C 301       1                                                       
HET    SO4  B 400       5                                                       
HETNAM     CU1 COPPER (I) ION                                                   
HETNAM      ZN ZINC ION                                                         
HETNAM      CU COPPER (II) ION                                                  
HETNAM     SO4 SULFATE ION                                                      
FORMUL   4  CU1    3(CU 1+)                                                     
FORMUL   5   ZN    3(ZN 2+)                                                     
FORMUL  10   CU    2(CU 2+)                                                     
FORMUL  12  SO4    O4 S 2-                                                      
FORMUL  13  HOH   *530(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  VAL B  152  5                                   5    
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  GLY A 183   N  ILE A 157           
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  VAL A  53   N  VAL A  36           
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  LYS A  91  0                                        
SHEET    2   C 2 LYS A  94  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 ILE B  34  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  LYS B  91  0                                        
SHEET    2   F 2 LYS B  94  THR B  96 -1  O  LYS B  94   N  LYS B  91           
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  GLY C 183   N  ILE C 157           
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  VAL C  53   N  VAL C  36           
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  LYS C  91  0                                        
SHEET    2   I 2 LYS C  94  THR C  96 -1  O  THR C  96   N  LYS C  89           
SSBOND   1 CYS A   86    CYS A  182                          1555   1555  2.06  
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  1.99  
LINK        CU   CU1 A 200                 NE2 HIS A  81     1555   1555  1.95  
LINK        CU   CU1 A 200                 NE2 HIS A 160     1555   1555  2.05  
LINK        ZN    ZN A 201                 ND1 HIS A 104     1555   1555  2.03  
LINK        ZN    ZN A 201                 ND1 HIS A 113     1555   1555  2.05  
LINK        ZN    ZN A 201                 ND1 HIS A 122     1555   1555  2.03  
LINK        ZN    ZN A 201                 OD1 ASP A 125     1555   1555  1.92  
LINK        CU   CU1 B 200                 ND1 HIS B  79     1555   1555  1.98  
LINK        CU   CU1 B 200                 NE2 HIS B  81     1555   1555  1.98  
LINK        CU   CU1 B 200                 NE2 HIS B 160     1555   1555  2.03  
LINK        ZN    ZN B 201                 ND1 HIS B 104     1555   1555  2.09  
LINK        ZN    ZN B 201                 ND1 HIS B 113     1555   1555  2.09  
LINK        ZN    ZN B 201                 ND1 HIS B 122     1555   1555  2.02  
LINK        ZN    ZN B 201                 OD1 ASP B 125     1555   1555  1.89  
LINK        CU   CU1 C 200                 ND1 HIS C  79     1555   1555  2.02  
LINK        CU   CU1 C 200                 NE2 HIS C  81     1555   1555  1.97  
LINK        CU   CU1 C 200                 NE2 HIS C 160     1555   1555  1.94  
LINK        ZN    ZN C 201                 ND1 HIS C 104     1555   1555  1.96  
LINK        ZN    ZN C 201                 ND1 HIS C 113     1555   1555  1.97  
LINK        ZN    ZN C 201                 ND1 HIS C 122     1555   1555  2.08  
LINK        ZN    ZN C 201                 OD1 ASP C 125     1555   1555  1.91  
LINK        CU    CU A 300                 OE1 GLU A  73     1555   1555  1.94  
LINK        CU    CU A 300                 ND1 HIS A 133     1555   1555  2.01  
LINK        CU    CU A 300                 OE1 GLU B  73     1555   1555  2.02  
LINK        CU    CU A 300                 ND1 HIS B 133     1555   1555  1.95  
LINK        CU    CU C 301                 OE1 GLU C  73     1555   1555  2.13  
LINK        CU    CU C 301                 ND1 HIS C 133     1555   1555  2.07  
LINK        CU    CU A 300                 OE2 GLU A  73     1555   1555  2.76  
LINK        CU    CU C 301                 OE2 GLU C  73     1555   1555  2.67  
LINK        CU    CU C 301                 OE1 GLU C  73     1555   2656  2.13  
LINK        CU    CU C 301                 OE2 GLU C  73     1555   2656  2.67  
LINK        CU    CU C 301                 ND1 HIS C 133     1555   2656  2.07  
CISPEP   1 HIS A  169    PRO A  170          0         4.54                     
CISPEP   2 HIS B  169    PRO B  170          0         2.46                     
CISPEP   3 HIS C  169    PRO C  170          0         0.40                     
SITE     1 AC1  4 HIS A  79  HIS A  81  HIS A 104  HIS A 160                    
SITE     1 AC2  4 HIS A 104  HIS A 113  HIS A 122  ASP A 125                    
SITE     1 AC3  4 HIS B  79  HIS B  81  HIS B 104  HIS B 160                    
SITE     1 AC4  4 HIS B 104  HIS B 113  HIS B 122  ASP B 125                    
SITE     1 AC5  4 HIS C  79  HIS C  81  HIS C 104  HIS C 160                    
SITE     1 AC6  4 HIS C 104  HIS C 113  HIS C 122  ASP C 125                    
SITE     1 AC7  4 GLU A  73  HIS A 133  GLU B  73  HIS B 133                    
SITE     1 AC8  2 GLU C  73  HIS C 133                                          
SITE     1 AC9  6 ASN A  59  LYS A 111  GLN B 118  ASP B 119                    
SITE     2 AC9  6 ASP B 120  HOH B 527                                          
CRYST1   99.791   64.592   82.730  90.00 125.93  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      0.010021  0.000000  0.007262        0.00000                         
SCALE2      0.000000  0.015482  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014928        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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