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Database: PDB
Entry: 1S4I
LinkDB: 1S4I
Original site: 1S4I 
HEADER    OXIDOREDUCTASE                          16-JAN-04   1S4I              
TITLE     CRYSTAL STRUCTURE OF A SOD-LIKE PROTEIN FROM BACILLUS SUBTILIS        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE-LIKE PROTEIN YOJM;                    
COMPND   3 CHAIN: B, A, C, D;                                                   
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: YOJM, BSU19400;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SOD, CU-ZN SOD, SOD-LIKE, SUPEROXIDE DISMUTASE, OXIDOREDUCTASE        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.BANCI,I.BERTINI,V.CALDERONE,F.CRAMARO,R.DEL CONTE,A.FANTONI,        
AUTHOR   2 S.MANGANI,A.QUATTRONE,M.S.VIEZZOLI                                   
REVDAT   4   13-JUL-11 1S4I    1       VERSN                                    
REVDAT   3   24-FEB-09 1S4I    1       VERSN                                    
REVDAT   2   21-JUN-05 1S4I    1       JRNL                                     
REVDAT   1   26-APR-05 1S4I    0                                                
JRNL        AUTH   L.BANCI,I.BERTINI,V.CALDERONE,F.CRAMARO,R.DEL CONTE,         
JRNL        AUTH 2 A.FANTONI,S.MANGANI,A.QUATTRONE,M.S.VIEZZOLI                 
JRNL        TITL   A PROKARYOTIC SUPEROXIDE DISMUTASE PARALOG LACKING TWO CU    
JRNL        TITL 2 LIGANDS: FROM LARGELY UNSTRUCTURED IN SOLUTION TO ORDERED IN 
JRNL        TITL 3 THE CRYSTAL.                                                 
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 102  7541 2005              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   15897454                                                     
JRNL        DOI    10.1073/PNAS.0502450102                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 45524                          
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) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4150                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3227                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3240                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 300                          
REMARK   3   BIN FREE R VALUE                    : 0.3700                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4520                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 390                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.17                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.87                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.11000                                             
REMARK   3    B22 (A**2) : -1.98000                                             
REMARK   3    B33 (A**2) : 1.15000                                              
REMARK   3    B12 (A**2) : -1.25000                                             
REMARK   3    B13 (A**2) : 2.52000                                              
REMARK   3    B23 (A**2) : -1.48000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.179         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.157         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.125         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.270         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4620 ; 0.026 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6245 ; 2.775 ; 1.951       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   601 ;17.076 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   660 ; 0.220 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3624 ; 0.012 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2333 ; 0.286 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   352 ; 0.209 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    19 ; 0.182 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    64 ; 0.298 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.157 ; 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):  2976 ; 1.575 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4725 ; 2.584 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1644 ; 3.771 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1520 ; 5.571 ; 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):    10 ;14.179 ; 2.000       
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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 1S4I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB021356.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-OCT-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.281                              
REMARK 200  MONOCHROMATOR                  : DOUBLE-CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
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   : 49677                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.070                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.03400                            
REMARK 200  R SYM                      (I) : 0.03400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.23000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, AMMONIUM SULPHATE, PEG4000,        
REMARK 280  LICL, PH 8.5, VAPOR DIFFUSION, SITTING 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                                              
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR                     
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 300 THE AUTHORS STATE THE BIOLOGICAL UNIT APPEARS TO BE                  
REMARK 300 A MONOMER.                                                           
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: MONOMERIC                         
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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -145.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -143.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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     GLY A   191                                                      
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     GLY C   191                                                      
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     GLY D   191                                                      
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 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    PRO B  96   C     PRO B  96   O       0.134                       
REMARK 500    ASP B  97   C     ASP B  97   O       0.147                       
REMARK 500    PRO B  96   C     ASP B  97   N      -0.217                       
REMARK 500    ASP B  97   C     PHE B  98   N      -0.217                       
REMARK 500    GLY A 119   N     GLY A 119   CA     -0.092                       
REMARK 500    HIS A 120   C     HIS A 121   N       0.251                       
REMARK 500    GLU D  59   CD    GLU D  59   OE2     0.070                       
REMARK 500    ASP D  65   C     ASP D  65   O       0.163                       
REMARK 500    ASP D  65   C     GLU D  66   N      -0.196                       
REMARK 500    PRO D  96   CD    PRO D  96   N       0.150                       
REMARK 500    ASP D  97   C     PHE D  98   N       0.158                       
REMARK 500    GLY D 102   C     GLY D 103   N      -0.163                       
REMARK 500    PRO D 104   CD    PRO D 104   N       0.095                       
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    PHE B  41   N   -  CA  -  C   ANGL. DEV. = -17.5 DEGREES          
REMARK 500    PRO B  96   CA  -  C   -  O   ANGL. DEV. = -20.3 DEGREES          
REMARK 500    ASP B  97   CA  -  C   -  O   ANGL. DEV. = -16.8 DEGREES          
REMARK 500    PRO B  96   CA  -  C   -  N   ANGL. DEV. =  19.3 DEGREES          
REMARK 500    ASP B  97   C   -  N   -  CA  ANGL. DEV. =  47.9 DEGREES          
REMARK 500    ASP B  97   CA  -  C   -  N   ANGL. DEV. =  18.1 DEGREES          
REMARK 500    ASP B  97   O   -  C   -  N   ANGL. DEV. = -29.3 DEGREES          
REMARK 500    GLU B 129   CG  -  CD  -  OE1 ANGL. DEV. = -12.3 DEGREES          
REMARK 500    ASP B 133   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP B 137   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP B 144   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    LEU B 173   CB  -  CG  -  CD1 ANGL. DEV. = -14.5 DEGREES          
REMARK 500    ASP A  64   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A  65   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    HIS A 120   CB  -  CA  -  C   ANGL. DEV. =  12.8 DEGREES          
REMARK 500    HIS A 120   CA  -  C   -  N   ANGL. DEV. = -18.1 DEGREES          
REMARK 500    ARG A 183   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    PHE C  41   CA  -  C   -  N   ANGL. DEV. =  16.4 DEGREES          
REMARK 500    PHE C  41   O   -  C   -  N   ANGL. DEV. = -14.4 DEGREES          
REMARK 500    ASP C  64   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASN C  75   CB  -  CA  -  C   ANGL. DEV. = -14.5 DEGREES          
REMARK 500    ASP C  97   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    GLY C 103   CA  -  C   -  O   ANGL. DEV. = -13.1 DEGREES          
REMARK 500    GLY C 102   CA  -  C   -  N   ANGL. DEV. =  12.2 DEGREES          
REMARK 500    ASP C 124   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP C 133   CB  -  CG  -  OD2 ANGL. DEV. =   8.3 DEGREES          
REMARK 500    ASP C 137   CB  -  CG  -  OD1 ANGL. DEV. =  11.5 DEGREES          
REMARK 500    ASP C 144   CB  -  CG  -  OD2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ASP C 157   CB  -  CG  -  OD2 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    GLN C 168   CB  -  CA  -  C   ANGL. DEV. = -12.9 DEGREES          
REMARK 500    GLY D  42   N   -  CA  -  C   ANGL. DEV. =  15.5 DEGREES          
REMARK 500    ASP D  65   CA  -  C   -  O   ANGL. DEV. = -21.1 DEGREES          
REMARK 500    ASP D  65   CA  -  C   -  N   ANGL. DEV. =  15.2 DEGREES          
REMARK 500    HIS D  71   N   -  CA  -  C   ANGL. DEV. = -16.5 DEGREES          
REMARK 500    ARG D  95   N   -  CA  -  CB  ANGL. DEV. =  12.9 DEGREES          
REMARK 500    ARG D  95   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    PRO D  96   CA  -  N   -  CD  ANGL. DEV. = -13.8 DEGREES          
REMARK 500    ARG D  95   CA  -  C   -  N   ANGL. DEV. =  20.7 DEGREES          
REMARK 500    ARG D  95   O   -  C   -  N   ANGL. DEV. = -14.5 DEGREES          
REMARK 500    PRO D  96   C   -  N   -  CD  ANGL. DEV. =  15.6 DEGREES          
REMARK 500    PRO D  96   CA  -  C   -  N   ANGL. DEV. =  14.4 DEGREES          
REMARK 500    ASP D  97   CA  -  C   -  N   ANGL. DEV. = -14.8 DEGREES          
REMARK 500    PHE D  98   O   -  C   -  N   ANGL. DEV. = -10.7 DEGREES          
REMARK 500    SER D 100   C   -  N   -  CA  ANGL. DEV. =  24.6 DEGREES          
REMARK 500    ALA D 101   CB  -  CA  -  C   ANGL. DEV. =  12.1 DEGREES          
REMARK 500    ALA D 101   N   -  CA  -  CB  ANGL. DEV. =   8.7 DEGREES          
REMARK 500    GLY D 102   CA  -  C   -  O   ANGL. DEV. =  11.5 DEGREES          
REMARK 500    GLY D 102   C   -  N   -  CA  ANGL. DEV. = -14.8 DEGREES          
REMARK 500    GLY D 102   O   -  C   -  N   ANGL. DEV. = -13.0 DEGREES          
REMARK 500    PRO D 104   CA  -  N   -  CD  ANGL. DEV. = -14.5 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      55 ANGLE DEVIATIONS.                             
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    ASP B  65      162.04    175.34                                   
REMARK 500    ARG B  95      143.39    -38.22                                   
REMARK 500    ASP B  97       46.45    -42.80                                   
REMARK 500    PHE B  98       30.08     26.60                                   
REMARK 500    SER B 100       61.52   -117.90                                   
REMARK 500    ALA B 101     -159.78   -161.31                                   
REMARK 500    ASN B 106       58.58   -149.94                                   
REMARK 500    ASN B 109       65.76     34.27                                   
REMARK 500    HIS B 120       98.66    169.52                                   
REMARK 500    ASP B 133      -40.42    -23.13                                   
REMARK 500    ASP B 137       86.59   -155.21                                   
REMARK 500    ASP B 144       42.33   -104.93                                   
REMARK 500    LEU B 156       68.68   -111.57                                   
REMARK 500    LEU B 173      -49.17   -140.45                                   
REMARK 500    ASN A  49     -163.60   -101.02                                   
REMARK 500    ASP A  64       77.66   -105.51                                   
REMARK 500    ASP A  97      -24.38     64.21                                   
REMARK 500    PHE A  98       28.63     47.59                                   
REMARK 500    HIS A 120       73.26    104.40                                   
REMARK 500    HIS A 121      125.92    -33.24                                   
REMARK 500    ASP A 137       83.74   -158.80                                   
REMARK 500    ASP A 144       50.57   -108.97                                   
REMARK 500    LEU A 156       65.97   -119.79                                   
REMARK 500    LEU A 173      -47.75   -143.98                                   
REMARK 500    SER A 177       32.24   -143.49                                   
REMARK 500    ARG C  50       57.75    -69.35                                   
REMARK 500    GLU C  51       -7.87   -174.14                                   
REMARK 500    LYS C  53       95.54    -59.03                                   
REMARK 500    ASP C  64       80.32   -167.82                                   
REMARK 500    SER C  76       13.77     55.57                                   
REMARK 500    ASP C  97      -22.83    -36.64                                   
REMARK 500    PHE C  98        7.86     57.05                                   
REMARK 500    SER C 100       79.60   -100.54                                   
REMARK 500    ALA C 101      158.80    176.64                                   
REMARK 500    ASN C 106       57.06   -144.93                                   
REMARK 500    HIS C 120      103.16     89.84                                   
REMARK 500    ASP C 133      -44.36    -24.14                                   
REMARK 500    ASP C 137       89.91   -153.48                                   
REMARK 500    LEU C 156       47.44   -108.75                                   
REMARK 500    GLU C 158      -68.07    -13.43                                   
REMARK 500    LEU C 173      -51.19   -143.76                                   
REMARK 500    SER C 177       32.48   -149.58                                   
REMARK 500    ARG D  95      164.71    -47.07                                   
REMARK 500    PHE D  98       30.52     38.05                                   
REMARK 500    ASN D 106       73.61   -155.94                                   
REMARK 500    ASN D 109       66.78     30.43                                   
REMARK 500    HIS D 120       44.25    158.69                                   
REMARK 500    ASP D 133      -43.17    -12.99                                   
REMARK 500    ASP D 144       46.47   -100.41                                   
REMARK 500    LEU D 156       60.95   -111.00                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      52 RAMACHANDRAN OUTLIERS.                        
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   40     PHE B   41                 -131.58                    
REMARK 500 PRO B   96     ASP B   97                  100.69                    
REMARK 500 ASP B   97     PHE B   98                  124.65                    
REMARK 500 GLY B  102     GLY B  103                   68.07                    
REMARK 500 GLY B  103     PRO B  104                   98.63                    
REMARK 500 GLY B  119     HIS B  120                  108.70                    
REMARK 500 ALA A   40     PHE A   41                  -95.79                    
REMARK 500 GLY A   42     HIS A   43                 -141.16                    
REMARK 500 TYR A   88     GLU A   89                 -149.92                    
REMARK 500 SER A  100     ALA A  101                   32.09                    
REMARK 500 GLY A  102     GLY A  103                   77.76                    
REMARK 500 GLY A  103     PRO A  104                  -87.13                    
REMARK 500 ALA C   40     PHE C   41                 -132.82                    
REMARK 500 GLY C  102     GLY C  103                   61.03                    
REMARK 500 GLY C  103     PRO C  104                  128.67                    
REMARK 500 ALA D   40     PHE D   41                 -122.19                    
REMARK 500 ASP D   64     ASP D   65                  -55.07                    
REMARK 500 ARG D   95     PRO D   96                  -40.63                    
REMARK 500 PRO D   96     ASP D   97                 -136.55                    
REMARK 500 ALA D  101     GLY D  102                  127.50                    
REMARK 500 ALA D  132     ASP D  133                  147.26                    
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 B  97        -51.56                                           
REMARK 500    GLY A 119        -10.80                                           
REMARK 500    GLY C 103        -13.22                                           
REMARK 500    ARG D  95        -20.03                                           
REMARK 500    ASP D  97        -28.62                                           
REMARK 500    ALA D 101        -27.54                                           
REMARK 500    GLY D 103        -13.83                                           
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    GLU B  66        24.8      L          L   OUTSIDE RANGE           
REMARK 500    ASP A  97        24.5      L          L   OUTSIDE RANGE           
REMARK 500    ASN A 109        24.4      L          L   OUTSIDE RANGE           
REMARK 500    HIS A 120         9.6      L          L   EXPECTING SP3           
REMARK 500    GLU C  51        23.9      L          L   OUTSIDE RANGE           
REMARK 500    HIS C 120        13.1      L          L   OUTSIDE RANGE           
REMARK 500    LEU C 190        23.1      L          L   OUTSIDE RANGE           
REMARK 500    ARG D  95        13.7      L          L   OUTSIDE RANGE           
REMARK 500    PRO D  96        20.9      L          L   OUTSIDE RANGE           
REMARK 500    ALA D 101         4.2      L          L   EXPECTING SP3           
REMARK 500    ASN D 109        24.5      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 C 672        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH D 756        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH D 764        DISTANCE =  5.36 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                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 124   OD2                                                    
REMARK 620 2 HIS A 112   ND1 105.3                                              
REMARK 620 3 HIS A 121   ND1 104.4 110.4                                        
REMARK 620 4  CL A 502  CL   109.9 113.0 113.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 802  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  71   NE2                                                    
REMARK 620 2 ASP C 137   OD1 113.9                                              
REMARK 620 3 HIS A  71   NE2 106.1  90.0                                        
REMARK 620 4 ASP A 137   OD1 109.2 123.0 112.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 112   ND1                                                    
REMARK 620 2  CL B 402  CL   103.3                                              
REMARK 620 3 HIS B 121   ND1 118.5 118.7                                        
REMARK 620 4 ASP B 124   OD2 101.2 104.1 109.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 801  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  71   NE2                                                    
REMARK 620 2 ASP D 137   OD1 105.7                                              
REMARK 620 3 HIS D  71   NE2 102.0 106.3                                        
REMARK 620 4 ASP B 137   OD1 104.0 133.3 101.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 112   ND1                                                    
REMARK 620 2 ASP C 124   OD2  95.7                                              
REMARK 620 3  CL C 602  CL   110.6 102.2                                        
REMARK 620 4 HIS C 121   ND1 122.3 110.9 112.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 121   ND1                                                    
REMARK 620 2 ASP D 124   OD2 114.0                                              
REMARK 620 3  CL D 702  CL   120.2 101.4                                        
REMARK 620 4 HIS D 112   ND1 119.4  95.5 102.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 802                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE AUTHORS STATE THE SEQUENCE IN THE SEQRES CORRESPONDS             
REMARK 999 TO THE ONE CLONED BUT THEY STATE IT IS LIKELY                        
REMARK 999 THAT SOME RESIDUES AT THE N-TERMINUS ARE CLEAVED OFF DURING          
REMARK 999 CRYSTALLISATION.                                                     
DBREF  1S4I A   22   196  UNP    O31851   YOJM_BACSU      22    196             
DBREF  1S4I B   22   196  UNP    O31851   YOJM_BACSU      22    196             
DBREF  1S4I C   22   196  UNP    O31851   YOJM_BACSU      22    196             
DBREF  1S4I D   22   196  UNP    O31851   YOJM_BACSU      22    196             
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 PRO 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 PRO 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 PRO 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 PRO 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     ZN  B 401       1                                                       
HET     CL  B 402       1                                                       
HET     ZN  A 501       1                                                       
HET     CL  A 502       1                                                       
HET     ZN  C 601       1                                                       
HET     CL  C 602       1                                                       
HET     ZN  D 701       1                                                       
HET     CL  D 702       1                                                       
HET     ZN  B 801       1                                                       
HET     ZN  A 802       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
FORMUL   5   ZN    6(ZN 2+)                                                     
FORMUL   6   CL    4(CL 1-)                                                     
FORMUL  15  HOH   *390(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  ILE B  58   N  VAL B  45           
SHEET    7   A 8 LEU B  68  ALA B  74 -1  O  ASP B  69   N  LYS B  61           
SHEET    8   A 8 VAL B 136  ALA B 142 -1  O  MET B 140   N  ILE B  70           
SHEET    1   B 4 VAL A  45  VAL A  48  0                                        
SHEET    2   B 4 ALA A  54  GLU A  62 -1  O  ILE A  58   N  VAL A  45           
SHEET    3   B 4 LEU A  68  ALA A  74 -1  O  HIS A  71   N  GLU A  59           
SHEET    4   B 4 VAL A 136  ALA A 142 -1  O  ALA A 142   N  LEU A  68           
SHEET    1   C 4 ASP A 124  GLU A 129  0                                        
SHEET    2   C 4 SER A  82  TYR A  88 -1  N  LEU A  83   O  LEU A 128           
SHEET    3   C 4 SER A 161  HIS A 166 -1  O  ALA A 162   N  TYR A  88           
SHEET    4   C 4 ARG A 183  LEU A 189 -1  O  LEU A 189   N  SER A 161           
SHEET    1   D 4 VAL C  45  VAL C  48  0                                        
SHEET    2   D 4 ALA C  54  GLU C  62 -1  O  VAL C  55   N  LEU C  47           
SHEET    3   D 4 LEU C  68  ALA C  74 -1  O  HIS C  71   N  GLU C  59           
SHEET    4   D 4 VAL C 136  ALA C 142 -1  O  ALA C 142   N  LEU C  68           
SHEET    1   E 4 ASP C 124  GLU C 129  0                                        
SHEET    2   E 4 SER C  82  TYR C  88 -1  N  LEU C  83   O  LEU C 128           
SHEET    3   E 4 SER C 161  HIS C 166 -1  O  ALA C 162   N  TYR C  88           
SHEET    4   E 4 ARG C 183  LEU C 189 -1  O  LEU C 189   N  SER C 161           
SHEET    1   F 7 PHE D  85  TYR D  88  0                                        
SHEET    2   F 7 SER D 161  HIS D 166 -1  O  ALA D 162   N  TYR D  88           
SHEET    3   F 7 ARG D 183  LEU D 189 -1  O  LEU D 189   N  SER D 161           
SHEET    4   F 7 VAL D  45  ASN D  49 -1  N  VAL D  48   O  CYS D 186           
SHEET    5   F 7 ALA D  54  GLU D  62 -1  O  GLY D  56   N  LEU D  47           
SHEET    6   F 7 LEU D  68  ALA D  74 -1  O  HIS D  71   N  GLU D  59           
SHEET    7   F 7 VAL D 136  ALA D 142 -1  O  MET D 140   N  ILE D  70           
SHEET    1   G 2 SER D  82  LEU D  83  0                                        
SHEET    2   G 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  2.03  
SSBOND   2 CYS A   93    CYS A  186                          1555   1555  2.02  
SSBOND   3 CYS C   93    CYS C  186                          1555   1555  2.04  
SSBOND   4 CYS D   93    CYS D  186                          1555   1555  2.05  
LINK        ZN    ZN A 501                 OD2 ASP A 124     1555   1555  1.88  
LINK        ZN    ZN A 501                 ND1 HIS A 112     1555   1555  2.03  
LINK        ZN    ZN A 501                 ND1 HIS A 121     1555   1555  1.84  
LINK        ZN    ZN A 501                CL    CL A 502     1555   1555  2.07  
LINK        ZN    ZN A 802                 NE2 HIS C  71     1555   1555  1.99  
LINK        ZN    ZN A 802                 OD1 ASP C 137     1555   1555  1.82  
LINK        ZN    ZN A 802                 NE2 HIS A  71     1555   1555  2.09  
LINK        ZN    ZN A 802                 OD1 ASP A 137     1555   1555  1.81  
LINK        ZN    ZN B 401                 ND1 HIS B 112     1555   1555  2.20  
LINK        ZN    ZN B 401                CL    CL B 402     1555   1555  2.07  
LINK        ZN    ZN B 401                 ND1 HIS B 121     1555   1555  2.15  
LINK        ZN    ZN B 401                 OD2 ASP B 124     1555   1555  1.93  
LINK        ZN    ZN B 801                 NE2 HIS B  71     1555   1555  1.99  
LINK        ZN    ZN B 801                 OD1 ASP D 137     1555   1555  1.78  
LINK        ZN    ZN B 801                 NE2 HIS D  71     1555   1555  2.13  
LINK        ZN    ZN B 801                 OD1 ASP B 137     1555   1555  1.88  
LINK        ZN    ZN C 601                 ND1 HIS C 112     1555   1555  1.96  
LINK        ZN    ZN C 601                 OD2 ASP C 124     1555   1555  1.98  
LINK        ZN    ZN C 601                CL    CL C 602     1555   1555  2.20  
LINK        ZN    ZN C 601                 ND1 HIS C 121     1555   1555  1.94  
LINK        ZN    ZN D 701                 ND1 HIS D 121     1555   1555  1.89  
LINK        ZN    ZN D 701                 OD2 ASP D 124     1555   1555  1.93  
LINK        ZN    ZN D 701                CL    CL D 702     1555   1555  2.17  
LINK        ZN    ZN D 701                 ND1 HIS D 112     1555   1555  2.03  
CISPEP   1 ASP B   64    ASP B   65          0        -1.56                     
CISPEP   2 ASP B   65    GLU B   66          0        12.29                     
CISPEP   3 ARG B   95    PRO B   96          0        16.44                     
CISPEP   4 SER B  100    ALA B  101          0        11.29                     
CISPEP   5 ALA B  101    GLY B  102          0       -24.18                     
CISPEP   6 ASN B  175    PRO B  176          0        -7.91                     
CISPEP   7 ASP A   64    ASP A   65          0       -28.06                     
CISPEP   8 ASP A   65    GLU A   66          0        17.97                     
CISPEP   9 ARG A   95    PRO A   96          0       -11.35                     
CISPEP  10 ALA A  101    GLY A  102          0       -14.52                     
CISPEP  11 ASN A  175    PRO A  176          0        -6.08                     
CISPEP  12 ASP C   64    ASP C   65          0         0.67                     
CISPEP  13 ASP C   65    GLU C   66          0        11.05                     
CISPEP  14 ARG C   95    PRO C   96          0       -12.05                     
CISPEP  15 SER C  100    ALA C  101          0        28.72                     
CISPEP  16 ALA C  101    GLY C  102          0        -4.09                     
CISPEP  17 ASN C  175    PRO C  176          0         2.72                     
CISPEP  18 ASP D   65    GLU D   66          0       -14.41                     
CISPEP  19 SER D  100    ALA D  101          0        15.01                     
CISPEP  20 ASN D  175    PRO D  176          0        -6.72                     
SITE     1 AC1  5 HIS B 112  HIS B 121  ASP B 124  PRO B 176                    
SITE     2 AC1  5  CL B 402                                                     
SITE     1 AC2  7 HIS B  86  HIS B 112  HIS B 121  ASP B 124                    
SITE     2 AC2  7 PRO B 176   ZN B 401  HOH B 830                               
SITE     1 AC3  4 HIS A 112  HIS A 121  ASP A 124   CL A 502                    
SITE     1 AC4  6 HIS A  86  HIS A 112  HIS A 121  ASP A 124                    
SITE     2 AC4  6 SER A 177   ZN A 501                                          
SITE     1 AC5  5 HIS C 112  HIS C 121  ASP C 124  PRO C 176                    
SITE     2 AC5  5  CL C 602                                                     
SITE     1 AC6  7 HIS C  86  PRO C 104  HIS C 112  HIS C 121                    
SITE     2 AC6  7 ASP C 124  SER C 177   ZN C 601                               
SITE     1 AC7  5 HIS D 112  HIS D 121  ASP D 124  PRO D 176                    
SITE     2 AC7  5  CL D 702                                                     
SITE     1 AC8  6 HIS D  86  HIS D 112  HIS D 121  ASP D 124                    
SITE     2 AC8  6 PRO D 176   ZN D 701                                          
SITE     1 AC9  4 HIS B  71  ASP B 137  HIS D  71  ASP D 137                    
SITE     1 BC1  4 HIS A  71  ASP A 137  HIS C  71  ASP C 137                    
CRYST1   38.225   61.108   64.915  84.35  76.02  90.42 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      0.026161  0.000192 -0.006568        0.00000                         
SCALE2      0.000000  0.016365 -0.001699        0.00000                         
SCALE3      0.000000  0.000000  0.015960        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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