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Database: PDB
Entry: 1XTM
LinkDB: 1XTM
Original site: 1XTM 
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   22-OCT-04   1XTM              
TITLE     CRYSTAL STRUCTURE OF THE DOUBLE MUTANT Y88H-P104H OF A SOD-LIKE       
TITLE    2 PROTEIN FROM BACILLUS SUBTILIS.                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYPOTHETICAL SUPEROXIDE DISMUTASE-LIKE PROTEIN YOJM;       
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: TOP1                                       
KEYWDS    SOD, CU-ZN SOD, SOD-LIKE, SUPEROXIDE DISMUTASE MUTANTS, STRUCTURAL    
KEYWDS   2 GENOMICS, UNKNOWN FUNCTION                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.CALDERONE,S.MANGANI,L.BANCI,M.BENVENUTI,I.BERTINI,A.FANTONI,        
AUTHOR   2 M.S.VIEZZOLI                                                         
REVDAT   3   13-JUL-11 1XTM    1       VERSN                                    
REVDAT   2   24-FEB-09 1XTM    1       VERSN                                    
REVDAT   1   04-OCT-05 1XTM    0                                                
JRNL        AUTH   L.BANCI,M.BENVENUTI,I.BERTINI,D.E.CABELLI,V.CALDERONE,       
JRNL        AUTH 2 A.FANTONI,S.MANGANI,M.MIGLIARDI,M.S.VIEZZOLI                 
JRNL        TITL   FROM AN INACTIVE PROKARYOTIC SOD HOMOLOGUE TO AN ACTIVE      
JRNL        TITL 2 PROTEIN THROUGH SITE-DIRECTED MUTAGENESIS.                   
JRNL        REF    J.AM.CHEM.SOC.                V. 127 13287 2005              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   16173759                                                     
JRNL        DOI    10.1021/JA052790O                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   L.BANCI,I.BERTINI,V.CALDERONE,F.CRAMARO,R.DEL CONTE,         
REMARK   1  AUTH 2 A.FANTONI,S.MANGANI,A.QUATTRONE,M.S.VIEZZOLI                 
REMARK   1  TITL   A PROKARYOTIC SUPEROXIDE DISMUTASE PARALOG LACKING TWO CU    
REMARK   1  TITL 2 LIGANDS: FROM LARGELY UNSTRUCTURED IN SOLUTION TO ORDERED IN 
REMARK   1  TITL 3 THE CRYSTAL.                                                 
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V. 102  7541 2005              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1  PMID   15897454                                                     
REMARK   1  DOI    10.1073/PNAS.0502450102                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0003                                      
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) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.60                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 39853                          
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) : 0.254                           
REMARK   3   R VALUE            (WORKING SET) : 0.253                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3320                            
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) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2927                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4160                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 243                          
REMARK   3   BIN FREE R VALUE                    : 0.4740                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2274                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 7                                       
REMARK   3   SOLVENT ATOMS            : 226                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.91                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.87                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.36000                                             
REMARK   3    B22 (A**2) : 2.06000                                              
REMARK   3    B33 (A**2) : -0.70000                                             
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): 0.121         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.110         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.084         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.430         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.919                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2324 ; 0.015 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3138 ; 1.802 ; 1.931       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   303 ;17.208 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   114 ;41.982 ;25.439       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   369 ;18.564 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;22.000 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   331 ; 0.131 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1822 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1081 ; 0.230 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1502 ; 0.304 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   164 ; 0.235 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    11 ; 0.121 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.253 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.144 ; 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):  1544 ; 1.183 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2372 ; 1.662 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   850 ; 2.346 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   766 ; 3.512 ; 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):     7 ;22.781 ; 3.000       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 1XTM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-OCT-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030754.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAY-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.27680                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL FOCUSSING MONO      
REMARK 200                                   CHROMATOR                          
REMARK 200  OPTICS                         : DOUBLE CRYSTAL FOCUSSING MONO      
REMARK 200                                   CHROMATOR                          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43173                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : 0.05700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.47800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
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: 1S4I                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA ACETATE, 30% PEG4000, 0.2M       
REMARK 280  AMMONIUM SULPHATE, 1MM ZNCL2, PH 4.6, VAPOR DIFFUSION, SITTING      
REMARK 280  DROP, TEMPERATURE 298K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       26.23100            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.17500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.23100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.17500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE PROTEIN IS A MONOMER IN VIVO BUT THERE ARE TWO           
REMARK 300 MOLECULES.                                                           
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -125.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       26.23100            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -52.17500            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      117.51200            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     LYS B    22                                                      
REMARK 465     PRO B    23                                                      
REMARK 465     PRO B    24                                                      
REMARK 465     ASP B    25                                                      
REMARK 465     PRO B    26                                                      
REMARK 465     PRO B    27                                                      
REMARK 465     ASN B    28                                                      
REMARK 465     ARG B    29                                                      
REMARK 465     VAL B    30                                                      
REMARK 465     PRO B    31                                                      
REMARK 465     GLU B    32                                                      
REMARK 465     LYS B    33                                                      
REMARK 465     LYS B    34                                                      
REMARK 465     VAL B    35                                                      
REMARK 465     VAL B    36                                                      
REMARK 465     GLU B    37                                                      
REMARK 465     THR B    38                                                      
REMARK 465     ASN B   192                                                      
REMARK 465     ASN B   193                                                      
REMARK 465     GLU B   194                                                      
REMARK 465     LYS B   195                                                      
REMARK 465     GLN B   196                                                      
REMARK 465     LYS A    22                                                      
REMARK 465     PRO A    23                                                      
REMARK 465     PRO A    24                                                      
REMARK 465     ASP A    25                                                      
REMARK 465     PRO A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     ASN A    28                                                      
REMARK 465     ARG A    29                                                      
REMARK 465     VAL A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     GLU A    32                                                      
REMARK 465     LYS A    33                                                      
REMARK 465     LYS A    34                                                      
REMARK 465     VAL A    35                                                      
REMARK 465     VAL A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     THR A    38                                                      
REMARK 465     SER A    39                                                      
REMARK 465     ASN A   192                                                      
REMARK 465     ASN A   193                                                      
REMARK 465     GLU A   194                                                      
REMARK 465     LYS A   195                                                      
REMARK 465     GLN A   196                                                      
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    GLY A   119     N    HIS A   120              1.57            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASP B 144   C     THR B 145   N       0.165                       
REMARK 500    GLY A 119   C     HIS A 120   N      -0.578                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ALA B 101   N   -  CA  -  C   ANGL. DEV. =  18.4 DEGREES          
REMARK 500    GLY B 102   N   -  CA  -  C   ANGL. DEV. = -22.2 DEGREES          
REMARK 500    GLY B 103   N   -  CA  -  C   ANGL. DEV. = -17.6 DEGREES          
REMARK 500    ASP B 157   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A  65   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    HIS A 120   CA  -  C   -  O   ANGL. DEV. =  19.7 DEGREES          
REMARK 500    GLY A 119   CA  -  C   -  N   ANGL. DEV. =  19.4 DEGREES          
REMARK 500    GLY A 119   O   -  C   -  N   ANGL. DEV. = -18.9 DEGREES          
REMARK 500    HIS A 120   C   -  N   -  CA  ANGL. DEV. =  26.0 DEGREES          
REMARK 500    ASP A 124   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    LEU A 190   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA B  40      -18.83     93.30                                   
REMARK 500    ASN B 106       58.39   -145.42                                   
REMARK 500    LEU B 156       49.11    -97.47                                   
REMARK 500    LEU B 173      -45.75   -148.01                                   
REMARK 500    PHE A  85      115.20   -160.36                                   
REMARK 500    SER A 100       72.15   -107.94                                   
REMARK 500    ALA A 101     -147.65   -116.21                                   
REMARK 500    ASN A 106       57.79   -141.48                                   
REMARK 500    ASP A 133      -62.05     14.40                                   
REMARK 500    LEU A 173      -52.99   -143.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA B  101     GLY B  102                  147.36                    
REMARK 500 GLY B  102     GLY B  103                 -134.04                    
REMARK 500 LEU B  190     GLY B  191                  138.31                    
REMARK 500 GLY A  119     HIS A  120                  -90.64                    
REMARK 500 ALA A  132     ASP A  133                  141.59                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ALA B 101        21.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 614        DISTANCE =  6.47 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 503  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  86   ND1                                                    
REMARK 620 2 HIS A  88   NE2 130.9                                              
REMARK 620 3 HIS A 104   NE2  93.5  95.5                                        
REMARK 620 4 HIS A 166   NE2  91.1 115.6 133.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 124   OD2                                                    
REMARK 620 2 HIS A 112   ND1  90.0                                              
REMARK 620 3 HIS A 121   ND1 115.2 123.5                                        
REMARK 620 4 HIS A 104   ND1 107.2 112.7 106.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 500  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  86   ND1                                                    
REMARK 620 2 HIS B 166   NE2 101.0                                              
REMARK 620 3 HIS B  88   NE2 126.7 127.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 124   OD2                                                    
REMARK 620 2 HIS B 121   ND1 111.5                                              
REMARK 620 3 HIS B 104   ND1 107.9 104.4                                        
REMARK 620 4 HIS B 112   ND1 100.7 120.2 111.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 137   OD1                                                    
REMARK 620 2 HIS B  71   NE2 108.3                                              
REMARK 620 3 HIS A  71   NE2  99.1 104.8                                        
REMARK 620 4 ASP A 137   OD1 134.0  97.9 110.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 505  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 642   O                                                      
REMARK 620 2 HOH B 553   O   136.2                                              
REMARK 620 3 HIS B 120   NE2 108.1  81.0                                        
REMARK 620 4 ASP B 144   OD2  80.2 123.3 136.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 506  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 628   O                                                      
REMARK 620 2 GLY B 160   O    84.1                                              
REMARK 620 3 GLU B  89   O    84.4  71.5                                        
REMARK 620 4 ASP B 157   OD2  95.5 135.1 153.3                                  
REMARK 620 5 ASP B 157   OD1  94.1  81.3 152.7  53.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 506                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1S4I   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A SOD-LIKE PROTEIN FROM BACILLUS                
REMARK 900 SUBTILIS CRYSTALLISED IN THE PRESENCE OF ZINC                        
REMARK 900 RELATED ID: 1XTL   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF P104H MUTANT OF SOD-LIKE PROTEIN                
DBREF  1XTM B   22   196  UNP    O31851   YOJM_BACSU      22    196             
DBREF  1XTM A   22   196  UNP    O31851   YOJM_BACSU      22    196             
SEQADV 1XTM HIS B   88  UNP  O31851    TYR    88 ENGINEERED                     
SEQADV 1XTM HIS B  104  UNP  O31851    PRO   104 ENGINEERED                     
SEQADV 1XTM HIS A   88  UNP  O31851    TYR    88 ENGINEERED                     
SEQADV 1XTM HIS A  104  UNP  O31851    PRO   104 ENGINEERED                     
SEQRES   1 B  175  LYS PRO PRO ASP PRO PRO ASN ARG VAL PRO GLU LYS LYS          
SEQRES   2 B  175  VAL VAL GLU THR SER ALA PHE GLY HIS HIS VAL GLN LEU          
SEQRES   3 B  175  VAL ASN ARG GLU GLY LYS ALA VAL GLY PHE ILE GLU ILE          
SEQRES   4 B  175  LYS GLU SER ASP ASP GLU GLY LEU ASP ILE HIS ILE SER          
SEQRES   5 B  175  ALA ASN SER LEU ARG PRO GLY ALA SER LEU GLY PHE HIS          
SEQRES   6 B  175  ILE HIS GLU LYS GLY SER CYS VAL ARG PRO ASP PHE GLU          
SEQRES   7 B  175  SER ALA GLY GLY HIS PHE ASN PRO LEU ASN LYS GLU HIS          
SEQRES   8 B  175  GLY PHE ASN ASN PRO MET GLY HIS HIS ALA GLY ASP LEU          
SEQRES   9 B  175  PRO ASN LEU GLU VAL GLY ALA ASP GLY LYS VAL ASP VAL          
SEQRES  10 B  175  ILE MET ASN ALA PRO ASP THR SER LEU LYS LYS GLY SER          
SEQRES  11 B  175  LYS LEU ASN ILE LEU ASP GLU ASP GLY SER ALA PHE ILE          
SEQRES  12 B  175  ILE HIS GLU GLN ALA ASP ASP TYR LEU THR ASN PRO SER          
SEQRES  13 B  175  GLY ASN SER GLY ALA ARG ILE VAL CYS GLY ALA LEU LEU          
SEQRES  14 B  175  GLY ASN ASN GLU LYS GLN                                      
SEQRES   1 A  175  LYS PRO PRO ASP PRO PRO ASN ARG VAL PRO GLU LYS LYS          
SEQRES   2 A  175  VAL VAL GLU THR SER ALA PHE GLY HIS HIS VAL GLN LEU          
SEQRES   3 A  175  VAL ASN ARG GLU GLY LYS ALA VAL GLY PHE ILE GLU ILE          
SEQRES   4 A  175  LYS GLU SER ASP ASP GLU GLY LEU ASP ILE HIS ILE SER          
SEQRES   5 A  175  ALA ASN SER LEU ARG PRO GLY ALA SER LEU GLY PHE HIS          
SEQRES   6 A  175  ILE HIS GLU LYS GLY SER CYS VAL ARG PRO ASP PHE GLU          
SEQRES   7 A  175  SER ALA GLY GLY HIS PHE ASN PRO LEU ASN LYS GLU HIS          
SEQRES   8 A  175  GLY PHE ASN ASN PRO MET GLY HIS HIS ALA GLY ASP LEU          
SEQRES   9 A  175  PRO ASN LEU GLU VAL GLY ALA ASP GLY LYS VAL ASP VAL          
SEQRES  10 A  175  ILE MET ASN ALA PRO ASP THR SER LEU LYS LYS GLY SER          
SEQRES  11 A  175  LYS LEU ASN ILE LEU ASP GLU ASP GLY SER ALA PHE ILE          
SEQRES  12 A  175  ILE HIS GLU GLN ALA ASP ASP TYR LEU THR ASN PRO SER          
SEQRES  13 A  175  GLY ASN SER GLY ALA ARG ILE VAL CYS GLY ALA LEU LEU          
SEQRES  14 A  175  GLY ASN ASN GLU LYS GLN                                      
HET     CU  B 500       1                                                       
HET     ZN  B 501       1                                                       
HET     ZN  B 502       1                                                       
HET     CU  A 503       1                                                       
HET     ZN  A 504       1                                                       
HET     ZN  B 505       1                                                       
HET     ZN  B 506       1                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
FORMUL   3   CU    2(CU 2+)                                                     
FORMUL   4   ZN    5(ZN 2+)                                                     
FORMUL  10  HOH   *226(H2 O)                                                    
HELIX    1   1 PHE B   98  GLY B  102  5                                   5    
SHEET    1   A 7 PHE B  85  HIS B  88  0                                        
SHEET    2   A 7 SER B 161  HIS B 166 -1  O  ALA B 162   N  HIS B  88           
SHEET    3   A 7 ARG B 183  LEU B 189 -1  O  LEU B 189   N  SER B 161           
SHEET    4   A 7 GLY B  42  ASN B  49 -1  N  VAL B  48   O  CYS B 186           
SHEET    5   A 7 ALA B  54  GLU B  62 -1  O  ILE B  60   N  GLY B  42           
SHEET    6   A 7 LEU B  68  ALA B  74 -1  O  HIS B  71   N  GLU B  59           
SHEET    7   A 7 VAL B 136  ALA B 142 -1  O  ALA B 142   N  LEU B  68           
SHEET    1   B 2 SER B  82  LEU B  83  0                                        
SHEET    2   B 2 LEU B 128  GLU B 129 -1  O  LEU B 128   N  LEU B  83           
SHEET    1   C 7 PHE A  85  HIS A  88  0                                        
SHEET    2   C 7 SER A 161  HIS A 166 -1  O  ALA A 162   N  HIS A  88           
SHEET    3   C 7 ARG A 183  LEU A 189 -1  O  LEU A 189   N  SER A 161           
SHEET    4   C 7 GLY A  42  ASN A  49 -1  N  VAL A  48   O  CYS A 186           
SHEET    5   C 7 ALA A  54  GLU A  62 -1  O  ILE A  60   N  GLY A  42           
SHEET    6   C 7 LEU A  68  ALA A  74 -1  O  HIS A  71   N  GLU A  59           
SHEET    7   C 7 VAL A 136  ALA A 142 -1  O  MET A 140   N  ILE A  70           
SHEET    1   D 2 SER A  82  LEU A  83  0                                        
SHEET    2   D 2 LEU A 128  GLU A 129 -1  O  LEU A 128   N  LEU A  83           
SSBOND   1 CYS B   93    CYS B  186                          1555   1555  2.04  
SSBOND   2 CYS A   93    CYS A  186                          1555   1555  2.05  
LINK        CU    CU A 503                 ND1 HIS A  86     1555   1555  2.41  
LINK        CU    CU A 503                 NE2 HIS A  88     1555   1555  2.24  
LINK        CU    CU A 503                 NE2 HIS A 104     1555   1555  2.49  
LINK        CU    CU A 503                 NE2 HIS A 166     1555   1555  1.89  
LINK        ZN    ZN A 504                 OD2 ASP A 124     1555   1555  2.03  
LINK        ZN    ZN A 504                 ND1 HIS A 112     1555   1555  2.14  
LINK        ZN    ZN A 504                 ND1 HIS A 121     1555   1555  1.87  
LINK        ZN    ZN A 504                 ND1 HIS A 104     1555   1555  2.08  
LINK        CU    CU B 500                 ND1 HIS B  86     1555   1555  2.05  
LINK        CU    CU B 500                 NE2 HIS B 166     1555   1555  2.00  
LINK        CU    CU B 500                 NE2 HIS B  88     1555   1555  2.07  
LINK        ZN    ZN B 501                 OD2 ASP B 124     1555   1555  1.97  
LINK        ZN    ZN B 501                 ND1 HIS B 121     1555   1555  2.03  
LINK        ZN    ZN B 501                 ND1 HIS B 104     1555   1555  1.97  
LINK        ZN    ZN B 501                 ND1 HIS B 112     1555   1555  2.06  
LINK        ZN    ZN B 502                 OD1 ASP B 137     1555   1555  1.92  
LINK        ZN    ZN B 502                 NE2 HIS B  71     1555   1555  2.17  
LINK        ZN    ZN B 505                 O   HOH B 642     1555   1555  2.01  
LINK        ZN    ZN B 505                 O   HOH B 553     1555   1555  2.00  
LINK        ZN    ZN B 505                 NE2 HIS B 120     1555   1555  2.32  
LINK        ZN    ZN B 505                 OD2 ASP B 144     1555   1555  2.24  
LINK        ZN    ZN B 506                 O   HOH B 628     1555   1555  2.47  
LINK        ZN    ZN B 506                 O   GLY B 160     1555   1555  2.50  
LINK        ZN    ZN B 506                 O   GLU B  89     1555   1555  2.52  
LINK        ZN    ZN B 506                 OD2 ASP B 157     1555   1555  2.30  
LINK        ZN    ZN B 506                 OD1 ASP B 157     1555   1555  2.45  
LINK        ZN    ZN B 502                 NE2 HIS A  71     1555   3547  2.19  
LINK        ZN    ZN B 502                 OD1 ASP A 137     1555   3547  1.96  
CISPEP   1 ASP B   64    ASP B   65          0         8.99                     
CISPEP   2 ASP B   65    GLU B   66          0       -12.00                     
CISPEP   3 ARG B   95    PRO B   96          0        -5.16                     
CISPEP   4 GLY B  119    HIS B  120          0         2.63                     
CISPEP   5 ASN B  175    PRO B  176          0       -10.09                     
CISPEP   6 ASP A   64    ASP A   65          0         2.31                     
CISPEP   7 ASP A   65    GLU A   66          0       -19.80                     
CISPEP   8 ARG A   95    PRO A   96          0         2.02                     
CISPEP   9 SER A  100    ALA A  101          0       -16.36                     
CISPEP  10 ALA A  101    GLY A  102          0       -26.77                     
CISPEP  11 GLY A  102    GLY A  103          0        17.75                     
CISPEP  12 ASN A  175    PRO A  176          0       -11.91                     
SITE     1 AC1  5 HIS B  86  HIS B  88  HIS B 104  HIS B 166                    
SITE     2 AC1  5 HOH B 508                                                     
SITE     1 AC2  4 HIS B 104  HIS B 112  HIS B 121  ASP B 124                    
SITE     1 AC3  4 HIS A  71  ASP A 137  HIS B  71  ASP B 137                    
SITE     1 AC4  4 HIS A  86  HIS A  88  HIS A 104  HIS A 166                    
SITE     1 AC5  4 HIS A 104  HIS A 112  HIS A 121  ASP A 124                    
SITE     1 AC6  4 HIS B 120  ASP B 144  HOH B 553  HOH B 642                    
SITE     1 AC7  5 GLU B  89  ASP B 157  ASP B 159  GLY B 160                    
SITE     2 AC7  5 HOH B 628                                                     
CRYST1   52.462  104.350   58.756  90.00  90.00  90.00 P 21 21 2     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      0.019061  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009583  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017020        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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