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Database: PDB
Entry: 1XTL
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Original site: 1XTL 
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   22-OCT-04   1XTL              
TITLE     CRYSTAL STRUCTURE OF P104H MUTANT OF SOD-LIKE PROTEIN FROM BACILLUS   
TITLE    2 SUBTILIS.                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYPOTHETICAL SUPEROXIDE DISMUTASE-LIKE PROTEIN YOJM;       
COMPND   3 CHAIN: B, A, C, D;                                                   
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,M.S.VIEZZOLI,     
AUTHOR   2 A.FANTONI                                                            
REVDAT   3   13-JUL-11 1XTL    1       VERSN                                    
REVDAT   2   24-FEB-09 1XTL    1       VERSN                                    
REVDAT   1   04-OCT-05 1XTL    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.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 38482                          
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) : 0.237                           
REMARK   3   R VALUE            (WORKING SET) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.299                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3477                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2759                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 252                          
REMARK   3   BIN FREE R VALUE                    : 0.4490                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4544                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 14                                      
REMARK   3   SOLVENT ATOMS            : 307                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.73                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.75                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.39000                                             
REMARK   3    B22 (A**2) : 3.01000                                              
REMARK   3    B33 (A**2) : -2.31000                                             
REMARK   3    B12 (A**2) : 0.02000                                              
REMARK   3    B13 (A**2) : -0.96000                                             
REMARK   3    B23 (A**2) : -0.76000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.241         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.219         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.168         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.115         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.893                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4627 ; 0.030 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6242 ; 2.725 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   602 ;10.658 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   223 ;40.144 ;25.605       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   729 ;20.703 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;19.316 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   659 ; 0.213 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3617 ; 0.012 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2043 ; 0.232 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2810 ; 0.304 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   277 ; 0.202 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     9 ; 0.124 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    82 ; 0.285 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.286 ; 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):  3142 ; 1.407 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4719 ; 2.062 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1718 ; 3.592 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1523 ; 4.975 ; 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):    14 ;11.200 ; 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 1XTL 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 RCSB030753.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JAN-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) : 1.37110                            
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   : 41966                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.958                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : 0.06700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.24400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
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   (%): 47.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA ACETATE, 20% PEG4000, 0.1M       
REMARK 280  AMMONIUM SULPHATE, 10MM 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 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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 FOUR          
REMARK 300 MOLECULES IN THE ASYMMETRIC UNIT                                     
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 APPLY THE FOLLOWING TO CHAINS: B, A, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -115.0 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: C                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.09286            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       12.07939            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000       57.87070            
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: 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: 4                                                       
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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     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     SER B    39                                                      
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 465     LYS C    22                                                      
REMARK 465     PRO C    23                                                      
REMARK 465     PRO C    24                                                      
REMARK 465     ASP C    25                                                      
REMARK 465     PRO C    26                                                      
REMARK 465     PRO C    27                                                      
REMARK 465     ASN C    28                                                      
REMARK 465     ARG C    29                                                      
REMARK 465     VAL C    30                                                      
REMARK 465     PRO C    31                                                      
REMARK 465     GLU C    32                                                      
REMARK 465     LYS C    33                                                      
REMARK 465     LYS C    34                                                      
REMARK 465     VAL C    35                                                      
REMARK 465     VAL C    36                                                      
REMARK 465     GLU C    37                                                      
REMARK 465     THR C    38                                                      
REMARK 465     SER C    39                                                      
REMARK 465     ASN C   192                                                      
REMARK 465     ASN C   193                                                      
REMARK 465     GLU C   194                                                      
REMARK 465     LYS C   195                                                      
REMARK 465     GLN C   196                                                      
REMARK 465     LYS D    22                                                      
REMARK 465     PRO D    23                                                      
REMARK 465     PRO D    24                                                      
REMARK 465     ASP D    25                                                      
REMARK 465     PRO D    26                                                      
REMARK 465     PRO D    27                                                      
REMARK 465     ASN D    28                                                      
REMARK 465     ARG D    29                                                      
REMARK 465     VAL D    30                                                      
REMARK 465     PRO D    31                                                      
REMARK 465     GLU D    32                                                      
REMARK 465     LYS D    33                                                      
REMARK 465     LYS D    34                                                      
REMARK 465     VAL D    35                                                      
REMARK 465     VAL D    36                                                      
REMARK 465     GLU D    37                                                      
REMARK 465     THR D    38                                                      
REMARK 465     SER D    39                                                      
REMARK 465     ASN D   192                                                      
REMARK 465     ASN D   193                                                      
REMARK 465     GLU D   194                                                      
REMARK 465     LYS D   195                                                      
REMARK 465     GLN D   196                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG B   50   NH2                                                 
REMARK 480     GLU A   51   OE1                                                 
REMARK 480     LYS A  148   NZ                                                  
REMARK 480     ARG C   95   NE                                                  
REMARK 480     ARG D   78   NH2                                                 
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    VAL B  45   CA    VAL B  45   CB      0.127                       
REMARK 500    VAL B  45   CB    VAL B  45   CG1     0.132                       
REMARK 500    ARG B  50   CZ    ARG B  50   NH2    -0.120                       
REMARK 500    PHE B  85   CE1   PHE B  85   CZ      0.117                       
REMARK 500    SER B 100   CB    SER B 100   OG      0.101                       
REMARK 500    ALA B 101   CA    ALA B 101   C       0.161                       
REMARK 500    GLY B 102   N     GLY B 102   CA      0.096                       
REMARK 500    GLU A  51   CD    GLU A  51   OE1    -0.114                       
REMARK 500    ASP A  65   C     ASP A  65   O      -0.174                       
REMARK 500    SER A 100   CA    SER A 100   CB      0.091                       
REMARK 500    GLY A 102   N     GLY A 102   CA      0.094                       
REMARK 500    ARG C  95   CD    ARG C  95   NE      0.217                       
REMARK 500    ARG C  95   NE    ARG C  95   CZ      0.213                       
REMARK 500    SER C 100   CB    SER C 100   OG      0.083                       
REMARK 500    ALA C 101   CA    ALA C 101   CB     -0.163                       
REMARK 500    ALA C 101   CA    ALA C 101   C       0.168                       
REMARK 500    GLY C 102   N     GLY C 102   CA      0.156                       
REMARK 500    GLY C 102   CA    GLY C 102   C       0.117                       
REMARK 500    ILE D  72   CA    ILE D  72   CB      0.140                       
REMARK 500    TYR D  88   CE1   TYR D  88   CZ     -0.079                       
REMARK 500    ALA D 101   CA    ALA D 101   CB     -0.178                       
REMARK 500    ALA D 101   CA    ALA D 101   C       0.172                       
REMARK 500    GLY D 102   N     GLY D 102   CA      0.131                       
REMARK 500    GLY D 150   C     GLY D 150   O       0.312                       
REMARK 500    ASP D 159   CB    ASP D 159   CG     -0.138                       
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    ARG B  50   NH1 -  CZ  -  NH2 ANGL. DEV. = -19.4 DEGREES          
REMARK 500    ARG B  50   NE  -  CZ  -  NH2 ANGL. DEV. =  14.7 DEGREES          
REMARK 500    CYS B  93   CA  -  CB  -  SG  ANGL. DEV. =   6.6 DEGREES          
REMARK 500    GLY B 103   N   -  CA  -  C   ANGL. DEV. =  16.0 DEGREES          
REMARK 500    GLY B 102   CA  -  C   -  N   ANGL. DEV. =  14.2 DEGREES          
REMARK 500    GLY B 102   O   -  C   -  N   ANGL. DEV. = -10.9 DEGREES          
REMARK 500    GLY B 103   C   -  N   -  CA  ANGL. DEV. =  16.1 DEGREES          
REMARK 500    HIS B 120   CA  -  CB  -  CG  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    HIS B 120   C   -  N   -  CA  ANGL. DEV. =  32.4 DEGREES          
REMARK 500    ASP B 159   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP B 159   CB  -  CG  -  OD2 ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    ASP B 170   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    LEU B 190   CA  -  CB  -  CG  ANGL. DEV. =  16.2 DEGREES          
REMARK 500    ASP A  65   CA  -  C   -  O   ANGL. DEV. = -13.2 DEGREES          
REMARK 500    ASP A  64   O   -  C   -  N   ANGL. DEV. = -14.2 DEGREES          
REMARK 500    ASP A  65   C   -  N   -  CA  ANGL. DEV. = -16.3 DEGREES          
REMARK 500    SER A 100   N   -  CA  -  CB  ANGL. DEV. =  13.1 DEGREES          
REMARK 500    SER A 100   N   -  CA  -  C   ANGL. DEV. = -22.6 DEGREES          
REMARK 500    SER A 100   C   -  N   -  CA  ANGL. DEV. =  19.9 DEGREES          
REMARK 500    ALA A 101   C   -  N   -  CA  ANGL. DEV. =  17.8 DEGREES          
REMARK 500    GLY A 103   C   -  N   -  CA  ANGL. DEV. =  14.8 DEGREES          
REMARK 500    LYS A 148   CD  -  CE  -  NZ  ANGL. DEV. = -16.2 DEGREES          
REMARK 500    ARG C  78   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG C  95   CD  -  NE  -  CZ  ANGL. DEV. =  23.9 DEGREES          
REMARK 500    ARG C  95   NE  -  CZ  -  NH1 ANGL. DEV. = -18.2 DEGREES          
REMARK 500    ARG C  95   NE  -  CZ  -  NH2 ANGL. DEV. =  15.5 DEGREES          
REMARK 500    SER C 100   N   -  CA  -  CB  ANGL. DEV. = -10.7 DEGREES          
REMARK 500    ALA C 101   N   -  CA  -  CB  ANGL. DEV. = -11.2 DEGREES          
REMARK 500    ALA C 101   CA  -  C   -  N   ANGL. DEV. =  12.7 DEGREES          
REMARK 500    GLY C 102   CA  -  C   -  N   ANGL. DEV. =  16.5 DEGREES          
REMARK 500    GLY C 102   O   -  C   -  N   ANGL. DEV. = -13.2 DEGREES          
REMARK 500    GLY C 103   C   -  N   -  CA  ANGL. DEV. =  20.4 DEGREES          
REMARK 500    ASP C 159   CB  -  CG  -  OD2 ANGL. DEV. =  -8.0 DEGREES          
REMARK 500    ASP C 171   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG D  78   NH1 -  CZ  -  NH2 ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ARG D  78   NE  -  CZ  -  NH2 ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ALA D 101   N   -  CA  -  CB  ANGL. DEV. = -12.9 DEGREES          
REMARK 500    ALA D 101   C   -  N   -  CA  ANGL. DEV. =  16.0 DEGREES          
REMARK 500    GLY D 102   CA  -  C   -  N   ANGL. DEV. =  15.5 DEGREES          
REMARK 500    GLY D 102   O   -  C   -  N   ANGL. DEV. = -11.5 DEGREES          
REMARK 500    GLY D 103   C   -  N   -  CA  ANGL. DEV. =  18.7 DEGREES          
REMARK 500    HIS D 120   C   -  N   -  CA  ANGL. DEV. =  33.7 DEGREES          
REMARK 500    ASP D 133   CB  -  CG  -  OD1 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ASP D 133   CB  -  CG  -  OD2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    GLY D 150   CA  -  C   -  O   ANGL. DEV. = -17.1 DEGREES          
REMARK 500    GLY D 150   O   -  C   -  N   ANGL. DEV. = -28.8 DEGREES          
REMARK 500    ASP D 159   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP D 159   CB  -  CG  -  OD2 ANGL. DEV. =  -9.6 DEGREES          
REMARK 500    LEU D 173   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    LEU D 189   CA  -  CB  -  CG  ANGL. DEV. =  14.6 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    GLU B  66     -158.77   -127.15                                   
REMARK 500    ASN B 106       53.35   -146.20                                   
REMARK 500    HIS B 120      112.14     77.84                                   
REMARK 500    ASP B 137       84.23   -155.21                                   
REMARK 500    LEU B 156       56.41    -99.81                                   
REMARK 500    LEU B 173      -53.24   -153.74                                   
REMARK 500    LEU B 190     -129.90   -105.73                                   
REMARK 500    PHE A  85      118.46   -160.36                                   
REMARK 500    SER A 100       26.88    170.79                                   
REMARK 500    ASN A 106       52.80   -143.19                                   
REMARK 500    ASP A 133      -27.47    -37.44                                   
REMARK 500    LEU A 156       59.73   -105.87                                   
REMARK 500    LEU A 173      -61.81   -141.28                                   
REMARK 500    GLU C  66     -163.25   -111.23                                   
REMARK 500    ASN C 106       58.29   -147.79                                   
REMARK 500    ASN C 109       73.59     39.00                                   
REMARK 500    ASP C 144       48.15   -102.52                                   
REMARK 500    LEU C 156       53.10   -102.42                                   
REMARK 500    LEU C 173      -44.30   -148.98                                   
REMARK 500    SER C 177       31.31   -143.63                                   
REMARK 500    GLU D  62       82.46    -57.67                                   
REMARK 500    GLU D  66     -164.83   -119.57                                   
REMARK 500    CYS D  93       75.29   -117.61                                   
REMARK 500    HIS D 120      133.60    155.80                                   
REMARK 500    ASP D 133      -53.97    -28.23                                   
REMARK 500    LEU D 156       50.67    -97.86                                   
REMARK 500    LEU D 173      -44.91   -136.69                                   
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 SER B   63     ASP B   64                  147.88                    
REMARK 500 ALA B  101     GLY B  102                  -35.90                    
REMARK 500 GLY B  102     GLY B  103                   37.04                    
REMARK 500 ASP A   64     ASP A   65                  -45.38                    
REMARK 500 GLU A   99     SER A  100                  -42.90                    
REMARK 500 GLY A  102     GLY A  103                   35.64                    
REMARK 500 ASP C   64     ASP C   65                  -31.51                    
REMARK 500 ALA C  101     GLY C  102                  -39.24                    
REMARK 500 GLY C  102     GLY C  103                   31.73                    
REMARK 500 GLU D   99     SER D  100                 -148.56                    
REMARK 500 ALA D  101     GLY D  102                  -43.18                    
REMARK 500 GLY D  102     GLY D  103                   35.83                    
REMARK 500 GLY D  119     HIS D  120                   72.03                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    HIS B 120         0.07    SIDE CHAIN                              
REMARK 500    ARG C  95         0.09    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ASP A  64         12.25                                           
REMARK 500    GLY D 150        -51.35                                           
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    HIS B 120        24.1      L          L   OUTSIDE RANGE           
REMARK 500    LEU B 173        24.6      L          L   OUTSIDE RANGE           
REMARK 500    GLU A  99        24.9      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 173        25.0      L          L   OUTSIDE RANGE           
REMARK 500    GLU D  66        21.5      L          L   OUTSIDE RANGE           
REMARK 500    HIS D 120        15.6      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 B1377        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH B1397        DISTANCE =  5.90 ANGSTROMS                       
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C SSEQI                                                      
REMARK 615     HOH B 1403                                                       
REMARK 615     HOH C 1335                                                       
REMARK 615     HOH D 1348                                                       
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 A1173  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A  88   OH                                                     
REMARK 620 2 HIS A 166   NE2  77.6                                              
REMARK 620 3 HIS A  86   ND1 157.9  98.2                                        
REMARK 620 4 HIS A 104   NE2  99.7 165.6  89.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1174  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 104   ND1                                                    
REMARK 620 2 HIS A 112   ND1 111.1                                              
REMARK 620 3 HIS A 121   ND1 110.1 117.8                                        
REMARK 620 4 ASP A 124   OD1 107.9  94.8 114.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1327  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  71   NE2                                                    
REMARK 620 2 ASP A 137   OD1 104.2                                              
REMARK 620 3 ASP A 137   OD2 133.4  53.6                                        
REMARK 620 4 ASP D 137   OD1  89.8 135.5  86.1                                  
REMARK 620 5 HIS D  71   NE2 118.0 105.0 107.8 104.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1331  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 157   OD1                                                    
REMARK 620 2 ASP A 159   OD1  92.3                                              
REMARK 620 3 ASP A 157   OD2  55.3 102.2                                        
REMARK 620 4 GLU A  89   O   152.9  84.8 151.6                                  
REMARK 620 5 GLY A 160   O    78.9  87.5 133.1  74.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B1171  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 166   NE2                                                    
REMARK 620 2 HIS B 104   NE2 167.4                                              
REMARK 620 3 TYR B  88   OH   80.7  93.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1172  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 112   ND1                                                    
REMARK 620 2 HIS B 104   ND1  98.4                                              
REMARK 620 3 HIS B 121   ND1 118.0 120.5                                        
REMARK 620 4 ASP B 124   OD1 102.2 105.7 109.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1326  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  71   NE2                                                    
REMARK 620 2 ASP B 137   OD1 108.3                                              
REMARK 620 3 ASP C 137   OD1  99.4 134.5                                        
REMARK 620 4 HIS C  71   NE2 108.2  97.9 106.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1329  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY B 160   O                                                      
REMARK 620 2 GLU B  89   O    86.6                                              
REMARK 620 3 ASP B 157   OD1  70.4 157.0                                        
REMARK 620 4 HOH B1396   O    88.2  83.1  95.2                                  
REMARK 620 5 HOH B1378   O   164.9  78.5 124.5  87.5                            
REMARK 620 6 ASP B 157   OD2 123.1 149.7  53.0  91.2  71.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C1175  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 104   NE2                                                    
REMARK 620 2 TYR C  88   OH   92.1                                              
REMARK 620 3 HIS C  86   ND1  92.3 143.2                                        
REMARK 620 4 HIS C 166   NE2 170.6  80.3  97.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1176  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 121   ND1                                                    
REMARK 620 2 ASP C 124   OD1 105.7                                              
REMARK 620 3 HIS C 112   ND1 109.7  98.0                                        
REMARK 620 4 HIS C 104   ND1 129.4 105.9 103.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1328  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 157   OD1                                                    
REMARK 620 2 ASP C 157   OD2  51.2                                              
REMARK 620 3 GLU C  89   O   161.8 147.0                                        
REMARK 620 4 GLY C 160   O    83.7 130.1  79.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D1177  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR D  88   OH                                                     
REMARK 620 2 HIS D 166   NE2  84.4                                              
REMARK 620 3 HIS D  86   ND1 144.6 119.0                                        
REMARK 620 4 HIS D 104   NE2  95.0 177.7  62.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D1178  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 121   ND1                                                    
REMARK 620 2 ASP D 124   OD1 119.9                                              
REMARK 620 3 HIS D 104   ND1 133.1  97.8                                        
REMARK 620 4 HIS D 112   ND1 111.5  86.6  96.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D1330  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D  89   O                                                      
REMARK 620 2 ASP D 157   OD1 165.6                                              
REMARK 620 3 ASP D 157   OD2 139.3  52.0                                        
REMARK 620 4 GLY D 160   O    77.0  89.4 138.5                                  
REMARK 620 5 HOH D1392   O    75.0 100.1  85.5  87.9                            
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 1171                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1172                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 1173                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1174                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 1175                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1176                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU D 1177                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1178                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1326                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1327                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1328                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1329                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1330                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1331                 
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: 1XTM   RELATED DB: PDB                                   
REMARK 900 Y88H, P104H MUTANTS                                                  
DBREF  1XTL B   22   196  UNP    O31851   YOJM_BACSU      22    196             
DBREF  1XTL A   22   196  UNP    O31851   YOJM_BACSU      22    196             
DBREF  1XTL C   22   196  UNP    O31851   YOJM_BACSU      22    196             
DBREF  1XTL D   22   196  UNP    O31851   YOJM_BACSU      22    196             
SEQADV 1XTL HIS B  104  UNP  O31851    PRO   104 ENGINEERED                     
SEQADV 1XTL HIS A  104  UNP  O31851    PRO   104 ENGINEERED                     
SEQADV 1XTL HIS C  104  UNP  O31851    PRO   104 ENGINEERED                     
SEQADV 1XTL HIS D  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 TYR 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 TYR 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                                      
SEQRES   1 C  175  LYS PRO PRO ASP PRO PRO ASN ARG VAL PRO GLU LYS LYS          
SEQRES   2 C  175  VAL VAL GLU THR SER ALA PHE GLY HIS HIS VAL GLN LEU          
SEQRES   3 C  175  VAL ASN ARG GLU GLY LYS ALA VAL GLY PHE ILE GLU ILE          
SEQRES   4 C  175  LYS GLU SER ASP ASP GLU GLY LEU ASP ILE HIS ILE SER          
SEQRES   5 C  175  ALA ASN SER LEU ARG PRO GLY ALA SER LEU GLY PHE HIS          
SEQRES   6 C  175  ILE TYR GLU LYS GLY SER CYS VAL ARG PRO ASP PHE GLU          
SEQRES   7 C  175  SER ALA GLY GLY HIS PHE ASN PRO LEU ASN LYS GLU HIS          
SEQRES   8 C  175  GLY PHE ASN ASN PRO MET GLY HIS HIS ALA GLY ASP LEU          
SEQRES   9 C  175  PRO ASN LEU GLU VAL GLY ALA ASP GLY LYS VAL ASP VAL          
SEQRES  10 C  175  ILE MET ASN ALA PRO ASP THR SER LEU LYS LYS GLY SER          
SEQRES  11 C  175  LYS LEU ASN ILE LEU ASP GLU ASP GLY SER ALA PHE ILE          
SEQRES  12 C  175  ILE HIS GLU GLN ALA ASP ASP TYR LEU THR ASN PRO SER          
SEQRES  13 C  175  GLY ASN SER GLY ALA ARG ILE VAL CYS GLY ALA LEU LEU          
SEQRES  14 C  175  GLY ASN ASN GLU LYS GLN                                      
SEQRES   1 D  175  LYS PRO PRO ASP PRO PRO ASN ARG VAL PRO GLU LYS LYS          
SEQRES   2 D  175  VAL VAL GLU THR SER ALA PHE GLY HIS HIS VAL GLN LEU          
SEQRES   3 D  175  VAL ASN ARG GLU GLY LYS ALA VAL GLY PHE ILE GLU ILE          
SEQRES   4 D  175  LYS GLU SER ASP ASP GLU GLY LEU ASP ILE HIS ILE SER          
SEQRES   5 D  175  ALA ASN SER LEU ARG PRO GLY ALA SER LEU GLY PHE HIS          
SEQRES   6 D  175  ILE TYR GLU LYS GLY SER CYS VAL ARG PRO ASP PHE GLU          
SEQRES   7 D  175  SER ALA GLY GLY HIS PHE ASN PRO LEU ASN LYS GLU HIS          
SEQRES   8 D  175  GLY PHE ASN ASN PRO MET GLY HIS HIS ALA GLY ASP LEU          
SEQRES   9 D  175  PRO ASN LEU GLU VAL GLY ALA ASP GLY LYS VAL ASP VAL          
SEQRES  10 D  175  ILE MET ASN ALA PRO ASP THR SER LEU LYS LYS GLY SER          
SEQRES  11 D  175  LYS LEU ASN ILE LEU ASP GLU ASP GLY SER ALA PHE ILE          
SEQRES  12 D  175  ILE HIS GLU GLN ALA ASP ASP TYR LEU THR ASN PRO SER          
SEQRES  13 D  175  GLY ASN SER GLY ALA ARG ILE VAL CYS GLY ALA LEU LEU          
SEQRES  14 D  175  GLY ASN ASN GLU LYS GLN                                      
HET     CU  B1171       1                                                       
HET     ZN  B1172       1                                                       
HET     CU  A1173       1                                                       
HET     ZN  A1174       1                                                       
HET     CU  C1175       1                                                       
HET     ZN  C1176       1                                                       
HET     CU  D1177       1                                                       
HET     ZN  D1178       1                                                       
HET     ZN  B1326       1                                                       
HET     ZN  A1327       1                                                       
HET     ZN  C1328       1                                                       
HET     ZN  B1329       1                                                       
HET     ZN  D1330       1                                                       
HET     ZN  A1331       1                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
FORMUL   5   CU    4(CU 2+)                                                     
FORMUL   6   ZN    10(ZN 2+)                                                    
FORMUL  19  HOH   *307(H2 O)                                                    
SHEET    1   A 8 ASP B 124  GLU B 129  0                                        
SHEET    2   A 8 SER B  82  TYR B  88 -1  N  LEU B  83   O  LEU B 128           
SHEET    3   A 8 SER B 161  HIS B 166 -1  O  ALA B 162   N  TYR B  88           
SHEET    4   A 8 ARG B 183  LEU B 189 -1  O  LEU B 189   N  SER B 161           
SHEET    5   A 8 GLY B  42  ASN B  49 -1  N  VAL B  48   O  CYS B 186           
SHEET    6   A 8 ALA B  54  GLU B  62 -1  O  VAL B  55   N  LEU B  47           
SHEET    7   A 8 LEU B  68  ALA B  74 -1  O  SER B  73   N  PHE B  57           
SHEET    8   A 8 VAL B 136  ALA B 142 -1  O  ALA B 142   N  LEU B  68           
SHEET    1   B 8 ASP A 124  GLU A 129  0                                        
SHEET    2   B 8 SER A  82  TYR A  88 -1  N  LEU A  83   O  LEU A 128           
SHEET    3   B 8 SER A 161  HIS A 166 -1  O  ALA A 162   N  TYR A  88           
SHEET    4   B 8 ARG A 183  LEU A 189 -1  O  LEU A 189   N  SER A 161           
SHEET    5   B 8 GLY A  42  ASN A  49 -1  N  VAL A  48   O  CYS A 186           
SHEET    6   B 8 ALA A  54  GLU A  62 -1  O  ILE A  60   N  GLY A  42           
SHEET    7   B 8 LEU A  68  ALA A  74 -1  O  HIS A  71   N  GLU A  59           
SHEET    8   B 8 VAL A 136  ALA A 142 -1  O  ALA A 142   N  LEU A  68           
SHEET    1   C 7 PHE C  85  TYR C  88  0                                        
SHEET    2   C 7 SER C 161  HIS C 166 -1  O  ALA C 162   N  TYR C  88           
SHEET    3   C 7 ARG C 183  LEU C 189 -1  O  GLY C 187   N  PHE C 163           
SHEET    4   C 7 GLY C  42  ASN C  49 -1  N  VAL C  48   O  CYS C 186           
SHEET    5   C 7 ALA C  54  GLU C  62 -1  O  ILE C  60   N  GLY C  42           
SHEET    6   C 7 LEU C  68  ALA C  74 -1  O  ASP C  69   N  LYS C  61           
SHEET    7   C 7 VAL C 136  ALA C 142 -1  O  MET C 140   N  ILE C  70           
SHEET    1   D 2 SER C  82  LEU C  83  0                                        
SHEET    2   D 2 LEU C 128  GLU C 129 -1  O  LEU C 128   N  LEU C  83           
SHEET    1   E 7 PHE D  85  TYR D  88  0                                        
SHEET    2   E 7 SER D 161  HIS D 166 -1  O  ILE D 164   N  HIS D  86           
SHEET    3   E 7 ARG D 183  LEU D 189 -1  O  LEU D 189   N  SER D 161           
SHEET    4   E 7 GLY D  42  ASN D  49 -1  N  VAL D  48   O  CYS D 186           
SHEET    5   E 7 ALA D  54  LYS D  61 -1  O  VAL D  55   N  LEU D  47           
SHEET    6   E 7 LEU D  68  ALA D  74 -1  O  SER D  73   N  PHE D  57           
SHEET    7   E 7 VAL D 136  ALA D 142 -1  O  MET D 140   N  ILE D  70           
SHEET    1   F 2 SER D  82  LEU D  83  0                                        
SHEET    2   F 2 LEU D 128  GLU D 129 -1  O  LEU D 128   N  LEU D  83           
SSBOND   1 CYS B   93    CYS B  186                          1555   1555  2.01  
SSBOND   2 CYS A   93    CYS A  186                          1555   1555  2.01  
SSBOND   3 CYS C   93    CYS C  186                          1555   1555  2.03  
SSBOND   4 CYS D   93    CYS D  186                          1555   1555  2.02  
LINK        CU    CU A1173                 OH  TYR A  88     1555   1555  2.74  
LINK        CU    CU A1173                 NE2 HIS A 166     1555   1555  2.06  
LINK        CU    CU A1173                 ND1 HIS A  86     1555   1555  2.23  
LINK        CU    CU A1173                 NE2 HIS A 104     1555   1555  2.13  
LINK        ZN    ZN A1174                 ND1 HIS A 104     1555   1555  1.76  
LINK        ZN    ZN A1174                 ND1 HIS A 112     1555   1555  2.33  
LINK        ZN    ZN A1174                 ND1 HIS A 121     1555   1555  2.09  
LINK        ZN    ZN A1174                 OD1 ASP A 124     1555   1555  1.99  
LINK        ZN    ZN A1327                 NE2 HIS A  71     1555   1555  2.19  
LINK        ZN    ZN A1327                 OD1 ASP A 137     1555   1555  2.05  
LINK        ZN    ZN A1327                 OD2 ASP A 137     1555   1555  2.65  
LINK        ZN    ZN A1331                 OD1 ASP A 157     1555   1555  2.45  
LINK        ZN    ZN A1331                 OD1 ASP A 159     1555   1555  2.34  
LINK        ZN    ZN A1331                 OD2 ASP A 157     1555   1555  2.52  
LINK        ZN    ZN A1331                 O   GLU A  89     1555   1555  2.76  
LINK        ZN    ZN A1331                 O   GLY A 160     1555   1555  2.55  
LINK        CU    CU B1171                 NE2 HIS B 166     1555   1555  2.22  
LINK        CU    CU B1171                 NE2 HIS B 104     1555   1555  2.01  
LINK        CU    CU B1171                 OH  TYR B  88     1555   1555  2.71  
LINK        ZN    ZN B1172                 ND1 HIS B 112     1555   1555  2.34  
LINK        ZN    ZN B1172                 ND1 HIS B 104     1555   1555  2.18  
LINK        ZN    ZN B1172                 ND1 HIS B 121     1555   1555  2.04  
LINK        ZN    ZN B1172                 OD1 ASP B 124     1555   1555  2.11  
LINK        ZN    ZN B1326                 NE2 HIS B  71     1555   1555  2.28  
LINK        ZN    ZN B1326                 OD1 ASP B 137     1555   1555  2.02  
LINK        ZN    ZN B1329                 O   GLY B 160     1555   1555  2.40  
LINK        ZN    ZN B1329                 O   GLU B  89     1555   1555  2.59  
LINK        ZN    ZN B1329                 OD1 ASP B 157     1555   1555  2.53  
LINK        ZN    ZN B1329                 O   HOH B1396     1555   1555  2.48  
LINK        ZN    ZN B1329                 O   HOH B1378     1555   1555  2.43  
LINK        ZN    ZN B1329                 OD2 ASP B 157     1555   1555  2.44  
LINK        CU    CU C1175                 NE2 HIS C 104     1555   1555  1.89  
LINK        CU    CU C1175                 OH  TYR C  88     1555   1555  2.32  
LINK        CU    CU C1175                 ND1 HIS C  86     1555   1555  2.51  
LINK        CU    CU C1175                 NE2 HIS C 166     1555   1555  2.16  
LINK        ZN    ZN C1176                 ND1 HIS C 121     1555   1555  2.32  
LINK        ZN    ZN C1176                 OD1 ASP C 124     1555   1555  2.17  
LINK        ZN    ZN C1176                 ND1 HIS C 112     1555   1555  1.97  
LINK        ZN    ZN C1176                 ND1 HIS C 104     1555   1555  2.11  
LINK        ZN    ZN C1328                 OD1 ASP C 157     1555   1555  2.53  
LINK        ZN    ZN C1328                 OD2 ASP C 157     1555   1555  2.56  
LINK        ZN    ZN C1328                 O   GLU C  89     1555   1555  2.57  
LINK        ZN    ZN C1328                 O   GLY C 160     1555   1555  2.37  
LINK        CU    CU D1177                 OH  TYR D  88     1555   1555  2.19  
LINK        CU    CU D1177                 NE2 HIS D 166     1555   1555  2.06  
LINK        CU    CU D1177                 ND1 HIS D  86     1555   1555  2.45  
LINK        CU    CU D1177                 NE2 HIS D 104     1555   1555  2.00  
LINK        ZN    ZN D1178                 ND1 HIS D 121     1555   1555  2.01  
LINK        ZN    ZN D1178                 OD1 ASP D 124     1555   1555  2.07  
LINK        ZN    ZN D1178                 ND1 HIS D 104     1555   1555  2.27  
LINK        ZN    ZN D1178                 ND1 HIS D 112     1555   1555  1.93  
LINK        ZN    ZN D1330                 O   GLU D  89     1555   1555  2.49  
LINK        ZN    ZN D1330                 OD1 ASP D 157     1555   1555  2.43  
LINK        ZN    ZN D1330                 OD2 ASP D 157     1555   1555  2.62  
LINK        ZN    ZN D1330                 O   GLY D 160     1555   1555  2.53  
LINK        ZN    ZN D1330                 O   HOH D1392     1555   1555  2.72  
LINK        ZN    ZN A1327                 OD1 ASP D 137     1555   1554  1.99  
LINK        ZN    ZN A1327                 NE2 HIS D  71     1555   1554  2.03  
LINK        ZN    ZN B1326                 OD1 ASP C 137     1555   1556  1.96  
LINK        ZN    ZN B1326                 NE2 HIS C  71     1555   1556  2.14  
CISPEP   1 ASP B   64    ASP B   65          0        -5.27                     
CISPEP   2 ASP B   65    GLU B   66          0       -11.75                     
CISPEP   3 ARG B   95    PRO B   96          0         2.64                     
CISPEP   4 SER B  100    ALA B  101          0        -5.72                     
CISPEP   5 ASN B  175    PRO B  176          0        -2.09                     
CISPEP   6 ARG A   95    PRO A   96          0         6.57                     
CISPEP   7 SER A  100    ALA A  101          0        -9.77                     
CISPEP   8 ALA A  101    GLY A  102          0       -26.45                     
CISPEP   9 GLY A  119    HIS A  120          0        -1.51                     
CISPEP  10 ASN A  175    PRO A  176          0         0.24                     
CISPEP  11 ASP C   65    GLU C   66          0       -19.09                     
CISPEP  12 ARG C   95    PRO C   96          0        -1.10                     
CISPEP  13 SER C  100    ALA C  101          0       -21.51                     
CISPEP  14 GLY C  119    HIS C  120          0         2.06                     
CISPEP  15 ASN C  175    PRO C  176          0        -6.77                     
CISPEP  16 ASP D   64    ASP D   65          0       -26.15                     
CISPEP  17 ASP D   65    GLU D   66          0       -14.53                     
CISPEP  18 ARG D   95    PRO D   96          0        -1.86                     
CISPEP  19 SER D  100    ALA D  101          0       -15.89                     
CISPEP  20 ASN D  175    PRO D  176          0        -7.86                     
SITE     1 AC1  4 HIS B  86  TYR B  88  HIS B 104  HIS B 166                    
SITE     1 AC2  4 HIS B 104  HIS B 112  HIS B 121  ASP B 124                    
SITE     1 AC3  4 HIS A  86  TYR A  88  HIS A 104  HIS A 166                    
SITE     1 AC4  4 HIS A 104  HIS A 112  HIS A 121  ASP A 124                    
SITE     1 AC5  4 HIS C  86  TYR C  88  HIS C 104  HIS C 166                    
SITE     1 AC6  5 HIS C 104  HIS C 112  HIS C 121  ASP C 124                    
SITE     2 AC6  5 PRO C 176                                                     
SITE     1 AC7  4 HIS D  86  TYR D  88  HIS D 104  HIS D 166                    
SITE     1 AC8  5 HIS D 104  HIS D 112  HIS D 121  ASP D 124                    
SITE     2 AC8  5 PRO D 176                                                     
SITE     1 AC9  4 HIS B  71  ASP B 137  HIS C  71  ASP C 137                    
SITE     1 BC1  4 HIS A  71  ASP A 137  HIS D  71  ASP D 137                    
SITE     1 BC2  4 GLU C  89  ASP C 157  ASP C 159  GLY C 160                    
SITE     1 BC3  6 GLU B  89  ASP B 157  ASP B 159  GLY B 160                    
SITE     2 BC3  6 HOH B1378  HOH B1396                                          
SITE     1 BC4  5 GLU D  89  ASP D 157  ASP D 159  GLY D 160                    
SITE     2 BC4  5 HOH D1392                                                     
SITE     1 BC5  4 GLU A  89  ASP A 157  ASP A 159  GLY A 160                    
CRYST1   52.147   56.586   59.118  78.24  89.91  85.47 P 1           4          
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      0.019177 -0.001518  0.000285        0.00000                         
SCALE2      0.000000  0.017728 -0.003700        0.00000                         
SCALE3      0.000000  0.000000  0.017280        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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