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Database: PDB
Entry: 3AK1
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Original site: 3AK1 
HEADER    OXIDOREDUCTASE                          30-JUN-10   3AK1              
TITLE     SUPEROXIDE DISMUTASE FROM AEROPYRUM PERNIX K1, APO-FORM               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN/FE];                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AEROPYRUM PERNIX;                               
SOURCE   3 ORGANISM_TAXID: 272557;                                              
SOURCE   4 STRAIN: K1;                                                          
SOURCE   5 GENE: APE0741;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET11                                     
KEYWDS    SUPEROXIDE DISMUTASE, CAMBIALISTIC, OXIDOREDUCTASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.NAKAMURA,K.UEGAKI                                                   
REVDAT   2   23-FEB-11 3AK1    1       JRNL                                     
REVDAT   1   02-FEB-11 3AK1    0                                                
JRNL        AUTH   T.NAKAMURA,K.TORIKAI,K.UEGAKI,J.MORITA,K.MACHIDA,A.SUZUKI,   
JRNL        AUTH 2 Y.KAWATA                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF THE CAMBIALISTIC SUPEROXIDE DISMUTASE   
JRNL        TITL 2 FROM AEROPYRUM PERNIX K1 - INSIGHTS INTO THE ENZYME          
JRNL        TITL 3 MECHANISM AND STABILITY                                      
JRNL        REF    FEBS J.                       V. 278   598 2011              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   21182595                                                     
JRNL        DOI    10.1111/J.1742-4658.2010.07977.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.57 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.57                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.13                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 98731                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5190                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.57                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.61                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6589                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3370                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 342                          
REMARK   3   BIN FREE R VALUE                    : 0.3590                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6910                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 104                                     
REMARK   3   SOLVENT ATOMS            : 630                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.75                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.106         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.106         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.087         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.519         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7282 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9854 ; 1.136 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   873 ; 5.738 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   349 ;36.567 ;24.327       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1220 ;13.093 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;18.342 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1031 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5549 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4013 ; 0.200 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4951 ; 0.305 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   604 ; 0.128 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    51 ; 0.194 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    23 ; 0.100 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4417 ; 0.814 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6894 ; 0.844 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3351 ; 1.487 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2946 ; 2.246 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3AK1 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-JUL-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB029347.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL44XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAC SCIENCE DIP-2040               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 103949                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.560                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.62                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1WB8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES, 10% PEG 6000, 8% ETHYLENE   
REMARK 280  GLYCOL, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       36.12550            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16220 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 27390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     PRO A   213                                                      
REMARK 465     GLN A   214                                                      
REMARK 465     GLN B   214                                                      
REMARK 465     GLN C   214                                                      
REMARK 465     PRO D   213                                                      
REMARK 465     GLN D   214                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH D   227     O    HOH D   355              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  34      -61.10   -101.62                                   
REMARK 500    LYS A 149     -126.58     50.04                                   
REMARK 500    ASN A 151       32.28   -146.44                                   
REMARK 500    LEU A 153      -15.02     79.97                                   
REMARK 500    TYR A 171      -20.22   -145.31                                   
REMARK 500    LYS A 176     -132.55     48.32                                   
REMARK 500    SER B   3     -123.94     89.49                                   
REMARK 500    LYS B  34      -63.95   -102.19                                   
REMARK 500    LYS B 149     -124.66     48.73                                   
REMARK 500    ASN B 151       30.52   -145.90                                   
REMARK 500    LEU B 153      -12.62     81.96                                   
REMARK 500    TYR B 171      -20.62   -146.48                                   
REMARK 500    LYS B 176     -136.22     50.44                                   
REMARK 500    LYS C  34      -62.25   -100.85                                   
REMARK 500    LYS C 149     -124.84     50.86                                   
REMARK 500    ASN C 151       31.32   -143.67                                   
REMARK 500    LEU C 153      -16.60     85.10                                   
REMARK 500    TYR C 171      -23.67   -144.64                                   
REMARK 500    LYS C 176     -131.65     55.26                                   
REMARK 500    PRO C 208        9.09    -65.14                                   
REMARK 500    LEU C 211      -81.28    -65.91                                   
REMARK 500    LEU C 212       78.20     54.57                                   
REMARK 500    LYS D  34      -60.42   -104.75                                   
REMARK 500    LYS D 149     -125.07     46.58                                   
REMARK 500    ASN D 151       30.10   -145.82                                   
REMARK 500    LEU D 153      -15.70     85.67                                   
REMARK 500    TYR D 171      -19.57   -148.88                                   
REMARK 500    LYS D 176     -134.48     52.52                                   
REMARK 500    PRO D 208       47.40    -76.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C 419        DISTANCE =  5.44 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 215                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 216                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 217                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 218                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 219                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 220                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 221                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 222                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 223                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 215                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 216                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 217                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 218                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 219                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 220                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 215                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 216                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 217                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 218                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 219                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 215                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 216                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 217                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 218                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 219                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 220                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3AK2   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN, MN-BOUND FORM                                          
REMARK 900 RELATED ID: 3AK3   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN, FE-BOUND FORM                                          
DBREF  3AK1 A    1   214  UNP    Q9Y8H8   SODF_AERPE       1    214             
DBREF  3AK1 B    1   214  UNP    Q9Y8H8   SODF_AERPE       1    214             
DBREF  3AK1 C    1   214  UNP    Q9Y8H8   SODF_AERPE       1    214             
DBREF  3AK1 D    1   214  UNP    Q9Y8H8   SODF_AERPE       1    214             
SEQRES   1 A  214  MET VAL SER PHE LYS ARG TYR GLU LEU PRO PRO LEU PRO          
SEQRES   2 A  214  TYR ASN TYR ASN ALA LEU GLU PRO TYR ILE ILE GLU GLU          
SEQRES   3 A  214  ILE MET LYS LEU HIS HIS GLN LYS HIS HIS ASN THR TYR          
SEQRES   4 A  214  VAL LYS GLY ALA ASN ALA ALA LEU GLU LYS ILE GLU LYS          
SEQRES   5 A  214  HIS LEU LYS GLY GLU ILE GLN ILE ASP VAL ARG ALA VAL          
SEQRES   6 A  214  MET ARG ASP PHE SER PHE ASN TYR ALA GLY HIS ILE MET          
SEQRES   7 A  214  HIS THR ILE PHE TRP PRO ASN MET ALA PRO PRO GLY LYS          
SEQRES   8 A  214  GLY GLY GLY THR PRO GLY GLY ARG VAL ALA ASP LEU ILE          
SEQRES   9 A  214  GLU LYS GLN PHE GLY GLY PHE GLU LYS PHE LYS ALA LEU          
SEQRES  10 A  214  PHE SER ALA ALA ALA LYS THR VAL GLU GLY VAL GLY TRP          
SEQRES  11 A  214  GLY VAL LEU ALA PHE ASP PRO LEU THR GLU GLU LEU ARG          
SEQRES  12 A  214  ILE LEU GLN VAL GLU LYS HIS ASN VAL LEU MET THR ALA          
SEQRES  13 A  214  GLY LEU VAL PRO ILE LEU VAL ILE ASP VAL TRP GLU HIS          
SEQRES  14 A  214  ALA TYR TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR          
SEQRES  15 A  214  VAL GLU ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL          
SEQRES  16 A  214  GLU LYS ARG LEU GLU GLN ALA LEU ASN ASN ALA LYS PRO          
SEQRES  17 A  214  LEU TYR LEU LEU PRO GLN                                      
SEQRES   1 B  214  MET VAL SER PHE LYS ARG TYR GLU LEU PRO PRO LEU PRO          
SEQRES   2 B  214  TYR ASN TYR ASN ALA LEU GLU PRO TYR ILE ILE GLU GLU          
SEQRES   3 B  214  ILE MET LYS LEU HIS HIS GLN LYS HIS HIS ASN THR TYR          
SEQRES   4 B  214  VAL LYS GLY ALA ASN ALA ALA LEU GLU LYS ILE GLU LYS          
SEQRES   5 B  214  HIS LEU LYS GLY GLU ILE GLN ILE ASP VAL ARG ALA VAL          
SEQRES   6 B  214  MET ARG ASP PHE SER PHE ASN TYR ALA GLY HIS ILE MET          
SEQRES   7 B  214  HIS THR ILE PHE TRP PRO ASN MET ALA PRO PRO GLY LYS          
SEQRES   8 B  214  GLY GLY GLY THR PRO GLY GLY ARG VAL ALA ASP LEU ILE          
SEQRES   9 B  214  GLU LYS GLN PHE GLY GLY PHE GLU LYS PHE LYS ALA LEU          
SEQRES  10 B  214  PHE SER ALA ALA ALA LYS THR VAL GLU GLY VAL GLY TRP          
SEQRES  11 B  214  GLY VAL LEU ALA PHE ASP PRO LEU THR GLU GLU LEU ARG          
SEQRES  12 B  214  ILE LEU GLN VAL GLU LYS HIS ASN VAL LEU MET THR ALA          
SEQRES  13 B  214  GLY LEU VAL PRO ILE LEU VAL ILE ASP VAL TRP GLU HIS          
SEQRES  14 B  214  ALA TYR TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR          
SEQRES  15 B  214  VAL GLU ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL          
SEQRES  16 B  214  GLU LYS ARG LEU GLU GLN ALA LEU ASN ASN ALA LYS PRO          
SEQRES  17 B  214  LEU TYR LEU LEU PRO GLN                                      
SEQRES   1 C  214  MET VAL SER PHE LYS ARG TYR GLU LEU PRO PRO LEU PRO          
SEQRES   2 C  214  TYR ASN TYR ASN ALA LEU GLU PRO TYR ILE ILE GLU GLU          
SEQRES   3 C  214  ILE MET LYS LEU HIS HIS GLN LYS HIS HIS ASN THR TYR          
SEQRES   4 C  214  VAL LYS GLY ALA ASN ALA ALA LEU GLU LYS ILE GLU LYS          
SEQRES   5 C  214  HIS LEU LYS GLY GLU ILE GLN ILE ASP VAL ARG ALA VAL          
SEQRES   6 C  214  MET ARG ASP PHE SER PHE ASN TYR ALA GLY HIS ILE MET          
SEQRES   7 C  214  HIS THR ILE PHE TRP PRO ASN MET ALA PRO PRO GLY LYS          
SEQRES   8 C  214  GLY GLY GLY THR PRO GLY GLY ARG VAL ALA ASP LEU ILE          
SEQRES   9 C  214  GLU LYS GLN PHE GLY GLY PHE GLU LYS PHE LYS ALA LEU          
SEQRES  10 C  214  PHE SER ALA ALA ALA LYS THR VAL GLU GLY VAL GLY TRP          
SEQRES  11 C  214  GLY VAL LEU ALA PHE ASP PRO LEU THR GLU GLU LEU ARG          
SEQRES  12 C  214  ILE LEU GLN VAL GLU LYS HIS ASN VAL LEU MET THR ALA          
SEQRES  13 C  214  GLY LEU VAL PRO ILE LEU VAL ILE ASP VAL TRP GLU HIS          
SEQRES  14 C  214  ALA TYR TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR          
SEQRES  15 C  214  VAL GLU ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL          
SEQRES  16 C  214  GLU LYS ARG LEU GLU GLN ALA LEU ASN ASN ALA LYS PRO          
SEQRES  17 C  214  LEU TYR LEU LEU PRO GLN                                      
SEQRES   1 D  214  MET VAL SER PHE LYS ARG TYR GLU LEU PRO PRO LEU PRO          
SEQRES   2 D  214  TYR ASN TYR ASN ALA LEU GLU PRO TYR ILE ILE GLU GLU          
SEQRES   3 D  214  ILE MET LYS LEU HIS HIS GLN LYS HIS HIS ASN THR TYR          
SEQRES   4 D  214  VAL LYS GLY ALA ASN ALA ALA LEU GLU LYS ILE GLU LYS          
SEQRES   5 D  214  HIS LEU LYS GLY GLU ILE GLN ILE ASP VAL ARG ALA VAL          
SEQRES   6 D  214  MET ARG ASP PHE SER PHE ASN TYR ALA GLY HIS ILE MET          
SEQRES   7 D  214  HIS THR ILE PHE TRP PRO ASN MET ALA PRO PRO GLY LYS          
SEQRES   8 D  214  GLY GLY GLY THR PRO GLY GLY ARG VAL ALA ASP LEU ILE          
SEQRES   9 D  214  GLU LYS GLN PHE GLY GLY PHE GLU LYS PHE LYS ALA LEU          
SEQRES  10 D  214  PHE SER ALA ALA ALA LYS THR VAL GLU GLY VAL GLY TRP          
SEQRES  11 D  214  GLY VAL LEU ALA PHE ASP PRO LEU THR GLU GLU LEU ARG          
SEQRES  12 D  214  ILE LEU GLN VAL GLU LYS HIS ASN VAL LEU MET THR ALA          
SEQRES  13 D  214  GLY LEU VAL PRO ILE LEU VAL ILE ASP VAL TRP GLU HIS          
SEQRES  14 D  214  ALA TYR TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR          
SEQRES  15 D  214  VAL GLU ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL          
SEQRES  16 D  214  GLU LYS ARG LEU GLU GLN ALA LEU ASN ASN ALA LYS PRO          
SEQRES  17 D  214  LEU TYR LEU LEU PRO GLN                                      
HET    EDO  A 215       4                                                       
HET    EDO  A 216       4                                                       
HET    EDO  A 217       4                                                       
HET    EDO  A 218       4                                                       
HET    EDO  A 219       4                                                       
HET    EDO  A 220       4                                                       
HET    EDO  A 221       4                                                       
HET    EDO  A 222       4                                                       
HET    EDO  A 223       4                                                       
HET    EDO  B 215       4                                                       
HET    EDO  B 216       4                                                       
HET    EDO  B 217       4                                                       
HET    EDO  B 218       4                                                       
HET    EDO  B 219       4                                                       
HET    EDO  B 220       4                                                       
HET    EDO  C 215       4                                                       
HET    EDO  C 216       4                                                       
HET    EDO  C 217       4                                                       
HET    EDO  C 218       4                                                       
HET    EDO  C 219       4                                                       
HET    EDO  D 215       4                                                       
HET    EDO  D 216       4                                                       
HET    EDO  D 217       4                                                       
HET    EDO  D 218       4                                                       
HET    EDO  D 219       4                                                       
HET    EDO  D 220       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5  EDO    26(C2 H6 O2)                                                 
FORMUL  31  HOH   *630(H2 O)                                                    
HELIX    1   1 ILE A   24  LYS A   34  1                                  11    
HELIX    2   2 LYS A   34  LYS A   55  1                                  22    
HELIX    3   3 ASP A   61  TRP A   83  1                                  23    
HELIX    4   4 GLY A   97  GLY A  109  1                                  13    
HELIX    5   5 GLY A  110  THR A  124  1                                  15    
HELIX    6   6 TRP A  167  ALA A  170  5                                   4    
HELIX    7   7 TYR A  171  LYS A  176  1                                   6    
HELIX    8   8 ASP A  178  TRP A  187  1                                  10    
HELIX    9   9 ASN A  188  VAL A  190  5                                   3    
HELIX   10  10 ASN A  191  LEU A  212  1                                  22    
HELIX   11  11 ILE B   24  LYS B   34  1                                  11    
HELIX   12  12 LYS B   34  LYS B   55  1                                  22    
HELIX   13  13 ASP B   61  TRP B   83  1                                  23    
HELIX   14  14 GLY B   97  GLY B  109  1                                  13    
HELIX   15  15 GLY B  110  THR B  124  1                                  15    
HELIX   16  16 TRP B  167  ALA B  170  5                                   4    
HELIX   17  17 TYR B  171  LYS B  176  1                                   6    
HELIX   18  18 ASP B  178  TRP B  187  1                                  10    
HELIX   19  19 ASN B  188  VAL B  190  5                                   3    
HELIX   20  20 ASN B  191  ALA B  206  1                                  16    
HELIX   21  21 LYS B  207  TYR B  210  5                                   4    
HELIX   22  22 ILE C   24  LYS C   34  1                                  11    
HELIX   23  23 LYS C   34  LYS C   55  1                                  22    
HELIX   24  24 ASP C   61  TRP C   83  1                                  23    
HELIX   25  25 GLY C   97  GLY C  109  1                                  13    
HELIX   26  26 GLY C  110  THR C  124  1                                  15    
HELIX   27  27 TRP C  167  ALA C  170  5                                   4    
HELIX   28  28 TYR C  171  LYS C  176  1                                   6    
HELIX   29  29 ASP C  178  TRP C  187  1                                  10    
HELIX   30  30 ASN C  188  VAL C  190  5                                   3    
HELIX   31  31 ASN C  191  ALA C  206  1                                  16    
HELIX   32  32 ALA C  206  LEU C  211  1                                   6    
HELIX   33  33 ILE D   24  LYS D   34  1                                  11    
HELIX   34  34 LYS D   34  LYS D   55  1                                  22    
HELIX   35  35 ASP D   61  TRP D   83  1                                  23    
HELIX   36  36 GLY D   97  GLY D  109  1                                  13    
HELIX   37  37 GLY D  110  THR D  124  1                                  15    
HELIX   38  38 TRP D  167  ALA D  170  5                                   4    
HELIX   39  39 TYR D  171  LYS D  176  1                                   6    
HELIX   40  40 ASP D  178  TRP D  187  1                                  10    
HELIX   41  41 ASN D  188  VAL D  190  5                                   3    
HELIX   42  42 ASN D  191  ALA D  206  1                                  16    
SHEET    1   A 3 GLU A 141  GLU A 148  0                                        
SHEET    2   A 3 GLY A 129  ASP A 136 -1  N  ALA A 134   O  ARG A 143           
SHEET    3   A 3 VAL A 159  ASP A 165 -1  O  LEU A 162   N  LEU A 133           
SHEET    1   B 3 GLU B 141  GLU B 148  0                                        
SHEET    2   B 3 GLY B 129  ASP B 136 -1  N  ALA B 134   O  ARG B 143           
SHEET    3   B 3 VAL B 159  ASP B 165 -1  O  ILE B 161   N  LEU B 133           
SHEET    1   C 3 GLU C 141  GLU C 148  0                                        
SHEET    2   C 3 GLY C 129  ASP C 136 -1  N  ASP C 136   O  GLU C 141           
SHEET    3   C 3 VAL C 159  ASP C 165 -1  O  LEU C 162   N  LEU C 133           
SHEET    1   D 3 LEU D 142  GLU D 148  0                                        
SHEET    2   D 3 GLY D 129  PHE D 135 -1  N  ALA D 134   O  ARG D 143           
SHEET    3   D 3 VAL D 159  ASP D 165 -1  O  LEU D 162   N  LEU D 133           
CISPEP   1 GLU A   20    PRO A   21          0         8.92                     
CISPEP   2 GLU B   20    PRO B   21          0         5.43                     
CISPEP   3 GLU C   20    PRO C   21          0         4.38                     
CISPEP   4 GLU D   20    PRO D   21          0         5.14                     
SITE     1 AC1  5 PRO A  11  LEU A  12  TYR A  14  TYR A  16                    
SITE     2 AC1  5 HOH A 311                                                     
SITE     1 AC2  6 GLU A  20  ILE B  24  LEU B 173  GLN B 174                    
SITE     2 AC2  6 EDO B 217  HOH B 424                                          
SITE     1 AC3  4 ASN A  15  ASN A  17  EDO B 216  EDO B 217                    
SITE     1 AC4  6 ILE A  23  MET A  28  HIS A  31  PHE A  82                    
SITE     2 AC4  6 ALA A 170  TYR A 182                                          
SITE     1 AC5  6 HIS A  35  THR A  38  HOH A 259  HOH A 290                    
SITE     2 AC5  6 HOH A 447  ASN C 177                                          
SITE     1 AC6  6 LEU A  47  GLU A  51  HOH A 396  HOH A 601                    
SITE     2 AC6  6 GLN B 107  ARG B 143                                          
SITE     1 AC7  6 HIS A  53  HOH A 271  HOH A 538  ALA B 116                    
SITE     2 AC7  6 LEU B 117  ALA B 120                                          
SITE     1 AC8  5 ARG A 143  ILE A 144  HOH A 508  LEU B  47                    
SITE     2 AC8  5 PHE B  69                                                     
SITE     1 AC9  5 GLY A 127  GLU A 168  ARG A 179  HOH A 567                    
SITE     2 AC9  5 TRP C 167                                                     
SITE     1 BC1  6 PRO B  11  LEU B  12  TYR B  14  TYR B  16                    
SITE     2 BC1  6 HIS B  32  HOH B 272                                          
SITE     1 BC2  5 EDO A 217  PRO B  21  ASN B 185  EDO B 217                    
SITE     2 BC2  5 HOH B 221                                                     
SITE     1 BC3  8 ASN A  17  GLU A  20  EDO A 216  EDO A 217                    
SITE     2 BC3  8 HOH A 300  GLN B 174  EDO B 216  HOH B 464                    
SITE     1 BC4  5 ALA B  64  ASP B  68  HOH B 225  HOH B 257                    
SITE     2 BC4  5 ASP C  61                                                     
SITE     1 BC5  4 GLU B 148  LYS B 149  GLU D 148  LYS D 149                    
SITE     1 BC6  9 VAL B 125  GLY B 127  GLU B 168  ARG B 179                    
SITE     2 BC6  9 HOH B 336  HOH B 513  TRP D 167  HOH D 293                    
SITE     3 BC6  9 HOH D 586                                                     
SITE     1 BC7  3 GLU A 148  GLU C 148  EDO C 218                               
SITE     1 BC8  8 ALA B  64  ARG B  67  ASP B  68  HOH B 248                    
SITE     2 BC8  8 ALA C  64  ARG C  67  ASP C  68  HOH C 263                    
SITE     1 BC9  7 GLN C 107  PHE C 108  LEU C 142  ARG C 143                    
SITE     2 BC9  7 HOH C 284  HOH C 289  HOH C 374                               
SITE     1 CC1  9 VAL A 128  LYS A 149  GLU C 126  GLY C 127                    
SITE     2 CC1  9 VAL C 128  GLU C 148  LYS C 149  EDO C 215                    
SITE     3 CC1  9 HOH C 400                                                     
SITE     1 CC2  4 TYR C   7  GLU C   8  HIS C  76  HOH C 477                    
SITE     1 CC3  4 PRO D  11  LEU D  12  TYR D  14  TYR D  16                    
SITE     1 CC4  8 ASN B 177  LYS D  34  HIS D  35  THR D  38                    
SITE     2 CC4  8 HOH D 266  HOH D 293  HOH D 569  HOH D 611                    
SITE     1 CC5  2 LYS D  55  GLU D  57                                          
SITE     1 CC6  6 PRO D  96  GLY D  97  GLY D  98  TRP D 192                    
SITE     2 CC6  6 ASP D 193  GLU D 196                                          
SITE     1 CC7  7 HIS B  35  GLU D 168  TYR D 171  TYR D 172                    
SITE     2 CC7  7 ASN D 177  HOH D 270  HOH D 387                               
SITE     1 CC8  4 GLY D  56  ILE D  58  GLN D  59  HOH D 239                    
CRYST1   69.260   72.251   76.652  90.00  90.99  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014438  0.000000  0.000250        0.00000                         
SCALE2      0.000000  0.013841  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013048        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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