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Database: PDB
Entry: 2AQP
LinkDB: 2AQP
Original site: 2AQP 
HEADER    OXIDOREDUCTASE                          18-AUG-05   2AQP              
TITLE     CU/ZN SUPEROXIDE DISMUTASE FROM NEISSERIA MENINGITIDIS E73A MUTANT    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B;                                                         
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    SUPEROXIDE DISMUTASE, ELECTROSTATIC GUIDANCE, NEISSERIA MENINGITIDIS, 
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.DIDONATO,C.J.KASSMANN,C.K.BRUNS,D.E.CABELLI,Z.CAO,L.B.TABATABAI,    
AUTHOR   2 J.S.KROLL,E.D.GETZOFF                                                
REVDAT   3   13-JUL-11 2AQP    1       VERSN                                    
REVDAT   2   24-FEB-09 2AQP    1       VERSN                                    
REVDAT   1   31-OCT-06 2AQP    0                                                
JRNL        AUTH   M.DIDONATO,C.J.KASSMANN,C.K.BRUNS,D.E.CABELLI,Z.CAO,         
JRNL        AUTH 2 L.B.TABATABAI,J.S.KROLL,E.D.GETZOFF                          
JRNL        TITL   CU/ZN SUPEROXIDE DISMUTASE FROM NEISSERIA MENINGITIDIS E73A  
JRNL        TITL 2 MUTANT                                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 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) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.0                           
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) : 0.135                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.135                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.183                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.300                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 3772                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 75512                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.129                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.175                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.300                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 3304                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 62810                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 2296                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 41                                            
REMARK   3   SOLVENT ATOMS      : 381                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 2717.40                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 2212.00                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 11                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 24855                   
REMARK   3   NUMBER OF RESTRAINTS                     : 30239                   
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) : 0.031                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.065                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.068                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.028                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.004                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.052                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.092                   
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 BY     
REMARK   3  9.26 %                                                              
REMARK   4                                                                      
REMARK   4 2AQP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB034201.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-JAN-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                       : 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   : 75512                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY                : 4.030                              
REMARK 200  R MERGE                    (I) : 0.04500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.57                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.540                              
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   (%): 48.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, PH 8.0, VAPOR DIFFUSION, HANGING    
REMARK 280  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       72.93700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.34850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       72.93700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.34850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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   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      HOH A 622  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 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    TYR A  60   CB  -  CG  -  CD1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ASP A 106   OD1 -  CG  -  OD2 ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ASP A 106   CB  -  CG  -  OD1 ANGL. DEV. =  10.0 DEGREES          
REMARK 500    ARG A 145   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG B 145   CD  -  NE  -  CZ  ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ASP B 150   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 A 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  79   ND1                                                    
REMARK 620 2 HIS A  81   NE2 143.2                                              
REMARK 620 3 HIS A 160   NE2 100.1 116.6                                        
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 102.6                                              
REMARK 620 3 HIS A 122   ND1 106.1 122.5                                        
REMARK 620 4 ASP A 125   OD1 110.1  98.7 115.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 A 250  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 148   ND1                                                    
REMARK 620 2 HOH A 779   O   124.0                                              
REMARK 620 3 HIS B 148   ND1 105.2 130.8                                        
REMARK 620 N                    1     2                                         
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 145.6                                              
REMARK 620 3 HIS B 160   NE2  98.2 116.1                                        
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 109.0 122.5                                        
REMARK 620 4 ASP B 125   OD1 108.7  97.9 115.0                                  
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                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 B 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 309                 
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: 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  2AQP A   23   186  UNP    Q59623   SODC_NEIMB      23    186             
DBREF  2AQP B   23   186  UNP    Q59623   SODC_NEIMB      23    186             
SEQADV 2AQP ALA A   73  UNP  Q59623    GLU    73 ENGINEERED                     
SEQADV 2AQP ALA B   73  UNP  Q59623    GLU    73 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 ALA 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 ALA 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                              
HET    CU1  A 200       1                                                       
HET     ZN  A 201       1                                                       
HET    CU1  A 250       1                                                       
HET    CU1  B 200       1                                                       
HET     ZN  B 201       1                                                       
HET    EDO  A 300       4                                                       
HET    EDO  A 301       4                                                       
HET    EDO  A 302       4                                                       
HET    EDO  B 303       4                                                       
HET    EDO  A 304       4                                                       
HET    EDO  A 305       4                                                       
HET    EDO  A 306       4                                                       
HET    EDO  B 307       6                                                       
HET    EDO  B 309       7                                                       
HETNAM     CU1 COPPER (I) ION                                                   
HETNAM      ZN ZINC ION                                                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  CU1    3(CU 1+)                                                     
FORMUL   4   ZN    2(ZN 2+)                                                     
FORMUL   8  EDO    9(C2 H6 O2)                                                  
FORMUL  17  HOH   *381(H2 O)                                                    
HELIX    1   1 GLY A   98  GLY A  102  5                                   5    
HELIX    2   2 HIS A  148  ARG A  153  5                                   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    
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  ALA A 181   N  ILE A 159           
SHEET    4   A 7 SER A  33  GLN A  40 -1  N  GLN A  39   O  CYS A 182           
SHEET    5   A 7 LYS A  48  SER A  58 -1  O  GLY A  51   N  VAL A  38           
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  ALA A 143   N  LEU A  62           
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 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  ILE B  55   N  ILE B  34           
SHEET    6   D 7 GLY B  61  LEU B  68 -1  O  ASP B  67   N  THR B  52           
SHEET    7   D 7 VAL B 141  ALA B 143 -1  O  ALA B 143   N  LEU B  62           
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  THR B  96   N  LYS B  89           
SSBOND   1 CYS A   86    CYS A  182                          1555   1555  2.05  
SSBOND   2 CYS B   86    CYS B  182                          1555   1555  2.04  
LINK        CU   CU1 A 200                 ND1 HIS A  79     1555   1555  1.94  
LINK        CU   CU1 A 200                 NE2 HIS A  81     1555   1555  1.93  
LINK        CU   CU1 A 200                 NE2 HIS A 160     1555   1555  2.03  
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  1.91  
LINK        CU   CU1 A 250                 ND1 HIS A 148     1555   1555  2.24  
LINK        CU   CU1 B 200                 ND1 HIS B  79     1555   1555  1.97  
LINK        CU   CU1 B 200                 NE2 HIS B  81     1555   1555  1.91  
LINK        CU   CU1 B 200                 NE2 HIS B 160     1555   1555  2.05  
LINK        ZN    ZN B 201                 ND1 HIS B 104     1555   1555  2.04  
LINK        ZN    ZN B 201                 ND1 HIS B 113     1555   1555  2.04  
LINK        ZN    ZN B 201                 ND1 HIS B 122     1555   1555  2.02  
LINK        ZN    ZN B 201                 OD1 ASP B 125     1555   1555  1.96  
LINK        CU   CU1 A 250                 O   HOH A 779     1555   1555  2.01  
LINK        CU   CU1 A 250                 ND1 HIS B 148     1555   2555  2.15  
CISPEP   1 HIS A  169    PRO A  170          0         3.17                     
CISPEP   2 HIS B  169    PRO B  170          0         5.40                     
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  5 GLU A  57  HIS A 148  HOH A 779  GLU B  57                    
SITE     2 AC3  5 HIS B 148                                                     
SITE     1 AC4  4 HIS B  79  HIS B  81  HIS B 104  HIS B 160                    
SITE     1 AC5  4 HIS B 104  HIS B 113  HIS B 122  ASP B 125                    
SITE     1 AC6  9 LEU A  41  THR A 161  PRO A 178  ARG A 179                    
SITE     2 AC6  9 MET A 180  HOH A 535  HOH A 633  HOH A 715                    
SITE     3 AC6  9 HOH A 741                                                     
SITE     1 AC7 12 GLY A  74  THR A 130  VAL A 131  HIS A 133                    
SITE     2 AC7 12 HOH A 430  HOH A 436  HOH A 510  GLY B  74                    
SITE     3 AC7 12 THR B 130  VAL B 131  HIS B 133  HOH B 512                    
SITE     1 AC8  7 THR A 138  HOH A 472  HOH A 492  HOH A 757                    
SITE     2 AC8  7 ASP B 164  ASN B 165  HOH B 494                               
SITE     1 AC9  4 ASP B 134  THR B 136  HOH B 441  HOH B 646                    
SITE     1 BC1  6 ASN A 165  HOH A 455  HOH A 504  HOH A 693                    
SITE     2 BC1  6 THR B 138  HOH B 429                                          
SITE     1 BC2  7 TYR A 115  GLN A 118  HIS A 166  SER A 167                    
SITE     2 BC2  7 HOH A 532  HOH A 547  HOH A 590                               
SITE     1 BC3  5 ASP A 134  THR A 136  HOH A 438  HOH A 658                    
SITE     2 BC3  5 HOH A 741                                                     
SITE     1 BC4  4 ASP B  67  HOH B 499  HOH B 648  HOH B 649                    
SITE     1 BC5  2 TYR B 115  HOH B 630                                          
CRYST1  145.874   48.697   49.042  90.00 109.57  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006855  0.000000  0.002437        0.00000                         
SCALE2      0.000000  0.020535  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021641        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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