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Database: PDB
Entry: 1J4A
LinkDB: 1J4A
Original site: 1J4A 
HEADER    OXIDOREDUCTASE                          18-AUG-01   1J4A              
TITLE     INSIGHTS INTO DOMAIN CLOSURE, SUBSTRATE SPECIFICITY AND               
TITLE    2 CATALYSIS OF D-LACTATE DEHYDROGENASE FROM LACTOBACILLUS              
TITLE    3 BULGARICUS                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-LACTATE DEHYDROGENASE;                                   
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: D-LDH;                                                      
COMPND   5 EC: 1.1.1.28;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LACTOBACILLUS DELBRUECKII SUBSP.                
SOURCE   3 BULGARICUS;                                                          
SOURCE   4 ORGANISM_TAXID: 1585;                                                
SOURCE   5 STRAIN: N42;                                                         
SOURCE   6 ATCC: NESTLE' CULTURE COLLECTION;                                    
SOURCE   7 COLLECTION: NESTLE' CULTURE COLLECTION;                              
SOURCE   8 CELLULAR_LOCATION: CYTOPLASM;                                        
SOURCE   9 GENE: LDHD;                                                          
SOURCE  10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  12 EXPRESSION_SYSTEM_STRAIN: SURE;                                      
SOURCE  13 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;                      
SOURCE  14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  15 EXPRESSION_SYSTEM_PLASMID: PMD19;                                    
SOURCE  16 EXPRESSION_SYSTEM_GENE: LDHD                                         
KEYWDS    NAD-DEPENDENT DEHYDROGENASE, REVERSIBLE INTERCONVERSION OF            
KEYWDS   2 PYRUVATE INTO D-LACTATE, OXIDOREDUCTASE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.RAZETO,S.KOCHHAR,H.HOTTINGER,M.DAUTER,K.S.WILSON,                   
AUTHOR   2 V.S.LAMZIN                                                           
REVDAT   2   24-FEB-09 1J4A    1       VERSN                                    
REVDAT   1   29-MAY-02 1J4A    0                                                
JRNL        AUTH   A.RAZETO,S.KOCHHAR,H.HOTTINGER,M.DAUTER,K.S.WILSON,          
JRNL        AUTH 2 V.S.LAMZIN                                                   
JRNL        TITL   DOMAIN CLOSURE, SUBSTRATE SPECIFICITY AND                    
JRNL        TITL 2 CATALYSIS OF D-LACTATE DEHYDROGENASE FROM                    
JRNL        TITL 3 LACTOBACILLUS BULGARICUS.                                    
JRNL        REF    J.MOL.BIOL.                   V. 318   109 2002              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   12054772                                                     
JRNL        DOI    10.1016/S0022-2836(02)00086-4                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.RAZETO                                                     
REMARK   1  TITL   LYSINE REPLACING HISTIDINE IN THE ACID-BASE                  
REMARK   1  TITL 2 CATALYSIS OF D-LACTATE DEHYDROGENASE: STRUCTURAL             
REMARK   1  TITL 3 INVESTIGATION ON ENZYMATIC STEREOSELECTIVITY.                
REMARK   1  REF    THESIS                                 124 1999              
REMARK   1  PUBL   UNIVERSITY OF YORK, DEPARTMENT OF CHEMISTRY                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 132346                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT APART FROM THE       
REMARK   3                                      LAST 3 CYCLES                   
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6647                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10473                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 55                                      
REMARK   3   SOLVENT ATOMS            : 900                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 0.21                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 0.33                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.150         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.440         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.013 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.031 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.035 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.023 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.130 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.190 ; 0.300               
REMARK   3    MULTIPLE TORSION                (A) : 0.250 ; 0.300               
REMARK   3    H-BOND (X...Y)                  (A) : 0.197 ; 0.300               
REMARK   3    H-BOND (X-H...Y)                (A) : 0.197 ; 0.300               
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : 0.000 ; 15.000              
REMARK   3    PLANAR                    (DEGREES) : 3.900 ; 7.000               
REMARK   3    STAGGERED                 (DEGREES) : 15.000; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : 36.100; 20.000              
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.900 ; 2.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.500 ; 3.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.500 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.200 ; 3.000                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE DENSITY OF THE CATALYTIC DOMAIN       
REMARK   3  OF SUBUNIT C IS VERY POOR: 49 RESIDUES WERE ASSIGNED ZERO           
REMARK   3  OCCUPANCY. IN ALL SUBUNITS THERE IS NO DENSITY FOR THE              
REMARK   3  METHIONINE AT THE N-TERMINUS AND IN SUBUNITS A,B,C FOR GLY-333      
REMARK   3  AT THE C-TERMINUS.                                                  
REMARK   4                                                                      
REMARK   4 1J4A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB001594.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
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                       : X11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.906                              
REMARK 200  MONOCHROMATOR                  : SILICON CRYSTAL                    
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 132348                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.04700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: MODEL OF NATIVE D-LDH WHICH IS CURRENTLY BEING       
REMARK 200  DEPOSITED IN THE PDB                                                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: ORTHORHOMBIC CRYSTALS  WERE GROWN        
REMARK 280  BY VAPOUR DIFFUSION FROM SOLUTIONS OF 20 % PEG 6K, 0.2 M            
REMARK 280  AMMONIUM SULPHATE IN 0.1 M CACODYLATE BUFFER PH 6.5.                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       96.70000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       96.70000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       47.15000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       94.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       47.15000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       94.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       96.70000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       47.15000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       94.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       96.70000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       47.15000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       94.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -150.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLY A   333                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B   333                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLY C   333                                                      
REMARK 465     MET D     1                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     ASP C   22                                                       
REMARK 475     ALA C   23                                                       
REMARK 475     HIS C   24                                                       
REMARK 475     LYS C   25                                                       
REMARK 475     ASP C   26                                                       
REMARK 475     VAL C   27                                                       
REMARK 475     GLU C   28                                                       
REMARK 475     LEU C   36                                                       
REMARK 475     THR C   37                                                       
REMARK 475     PRO C   38                                                       
REMARK 475     LEU C   43                                                       
REMARK 475     ALA C   44                                                       
REMARK 475     LYS C   45                                                       
REMARK 475     GLY C   46                                                       
REMARK 475     ALA C   47                                                       
REMARK 475     LEU C   56                                                       
REMARK 475     GLU C   61                                                       
REMARK 475     GLN C   64                                                       
REMARK 475     ALA C   65                                                       
REMARK 475     LEU C   66                                                       
REMARK 475     ALA C   67                                                       
REMARK 475     ASP C   68                                                       
REMARK 475     ASN C   69                                                       
REMARK 475     LYS C   73                                                       
REMARK 475     GLY C   80                                                       
REMARK 475     VAL C   81                                                       
REMARK 475     ASP C   82                                                       
REMARK 475     ASN C   83                                                       
REMARK 475     ASP C   85                                                       
REMARK 475     MET C   86                                                       
REMARK 475     ALA C   87                                                       
REMARK 475     LYS C   88                                                       
REMARK 475     ALA C   89                                                       
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     LYS A   18   CD                                                  
REMARK 480     VAL A   41   CG1   CG2                                           
REMARK 480     MET A   86   CG                                                  
REMARK 480     GLU A   91   CG    CD    OE1   OE2                               
REMARK 480     ASP A  122   CG    OD1   OD2                                     
REMARK 480     LYS A  171   CE    NZ                                            
REMARK 480     THR A  174   OG1   CG2                                           
REMARK 480     GLU A  182   CG    CD    OE1   OE2                               
REMARK 480     GLU A  220   CD    OE1   OE2                                     
REMARK 480     ILE A  254   CD1                                                 
REMARK 480     GLU A  265   CB    CG    CD    OE1   OE2                         
REMARK 480     LYS A  324   CE    NZ                                            
REMARK 480     GLU A  325   CD    OE1   OE2                                     
REMARK 480     LYS A  331   CG    CD    CE    NZ                                
REMARK 480     ASP B  122   CG    OD1   OD2                                     
REMARK 480     THR B  174   OG1   CG2                                           
REMARK 480     LYS B  185   CD    CE    NZ                                      
REMARK 480     ILE B  268   CD1                                                 
REMARK 480     LYS B  331   CE    NZ                                            
REMARK 480     THR C    2   N                                                   
REMARK 480     LYS C    3   CB    CG    CD    CE    NZ                          
REMARK 480     ILE C    4   N     CG2                                           
REMARK 480     TYR C    7   CG    CD1   CD2   CE1   CE2   CZ    OH              
REMARK 480     LYS C   18   CD    CE    NZ                                      
REMARK 480     TRP C   20   CZ2   CZ3   CH2                                     
REMARK 480     VAL C   29   N     CA    CB    CG1   CG2                         
REMARK 480     GLU C   30   OE1   OE2                                           
REMARK 480     LYS C   34   CG    CD    CE    NZ                                
REMARK 480     GLU C   39   N     CB    CG    CD    OE1   OE2                   
REMARK 480     THR C   40   CB    OG1   CG2                                     
REMARK 480     ALA C   42   CA    C     O     CB                                
REMARK 480     ASP C   48   N     CG    OD1   OD2                               
REMARK 480     GLY C   49   N     CA                                            
REMARK 480     GLN C   54   CB    CG    CD    OE1   NE2                         
REMARK 480     GLN C   55   CB    CG    CD    OE1   NE2                         
REMARK 480     ASP C   57   N     CB    CG    OD1   OD2                         
REMARK 480     TYR C   58   C     O     CB    CG    CD1   CD2   CE1             
REMARK 480     TYR C   58   CE2   CZ    OH                                      
REMARK 480     ILE C   59   CG2   CD1                                           
REMARK 480     ALA C   60   C     O     CB                                      
REMARK 480     THR C   62   N                                                   
REMARK 480     LEU C   63   CA    C     O     CB    CG    CD1   CD2             
REMARK 480     GLY C   70   N     CA                                            
REMARK 480     ILE C   71   CB    CG1   CG2   CD1                               
REMARK 480     MET C   74   N     CA    CB    CG    SD    CE                    
REMARK 480     ILE C   84   N     CA    C     O                                 
REMARK 480     LYS C   90   N     CA    CB    CG    CD    CE    NZ              
REMARK 480     GLU C   91   O     CB    CG    CD    OE1   OE2                   
REMARK 480     LEU C   92   O     CB    CG    CD1   CD2                         
REMARK 480     GLY C   93   CA                                                  
REMARK 480     PHE C   94   N     CD1   CD2   CE1   CE2   CZ                    
REMARK 480     ILE C   96   CB    CG1   CG2   CD1                               
REMARK 480     THR C   97   N     CA    CB    OG1   CG2                         
REMARK 480     ASP C  122   CG    OD1   OD2                                     
REMARK 480     THR C  174   OG1   CG2                                           
REMARK 480     GLU C  182   CG    CD    OE1   OE2                               
REMARK 480     LYS C  185   CD    CE    NZ                                      
REMARK 480     LYS C  198   CD    CE    NZ                                      
REMARK 480     ARG C  236   NH2                                                 
REMARK 480     GLU C  265   CB    CG                                            
REMARK 480     LYS C  297   CE    NZ                                            
REMARK 480     LEU C  318   CB    CG    CD1   CD2                               
REMARK 480     VAL C  321   CB    CG1   CG2                                     
REMARK 480     GLU C  325   CA                                                  
REMARK 480     VAL C  330   CB    CG1   CG2                                     
REMARK 480     LYS C  331   CG    CD    CE    NZ                                
REMARK 480     VAL C  332   CG1   CG2                                           
REMARK 480     LYS D   45   CD    CE    NZ                                      
REMARK 480     ASP D  122   CG    OD1   OD2                                     
REMARK 480     THR D  174   OG1   CG2                                           
REMARK 480     GLU D  182   CG    CD    OE1   OE2                               
REMARK 480     LYS D  198   CD    CE    NZ                                      
REMARK 480     GLU D  265   CB    CG    CD    OE1   OE2                         
REMARK 480     ILE D  268   CD1                                                 
REMARK 480     LYS D  297   NZ                                                  
REMARK 480     LYS D  324   CG    CD    CE    NZ                                
REMARK 480     GLU D  325   CG    CD    OE1   OE2                               
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A   265     O    HOH A  1470              0.07            
REMARK 500   CD   GLU D   265     O    HOH D  4533              0.79            
REMARK 500   O    ASN C    69     O    HOH C  3526              0.80            
REMARK 500   OE1  GLU A   220     O    HOH A  1527              0.81            
REMARK 500   CG   GLU D   265     O    HOH D  4533              0.94            
REMARK 500   OG   SER B    75     OD1  ASN B   317              0.95            
REMARK 500   C    ASN C    69     O    HOH C  3526              1.03            
REMARK 500   O    THR C    40     CG   LEU C    43              1.17            
REMARK 500   OG   SER D    75     OD1  ASN D   317              1.17            
REMARK 500   CD   GLU A   265     O    HOH A  1470              1.28            
REMARK 500   OE2  GLU A   265     O    HOH A  1639              1.41            
REMARK 500   O    VAL C    41     N    ALA C    44              1.42            
REMARK 500   CB   SER B    75     OD1  ASN B   317              1.52            
REMARK 500   CB   SER D    75     OD1  ASN D   317              1.53            
REMARK 500   CD   GLU A   220     O    HOH A  1527              1.54            
REMARK 500   OE1  GLU D   265     O    HOH D  4533              1.55            
REMARK 500   OE1  GLU A   182     O    HOH A  1628              1.64            
REMARK 500   CA   ASN C    69     O    HOH C  3526              1.72            
REMARK 500   O    VAL C    41     N    LEU C    43              1.78            
REMARK 500   NZ   LYS C    90     O    VAL C   332              1.78            
REMARK 500   CD   GLU A   265     O    HOH A  1639              1.79            
REMARK 500   CD   LYS C    90     C    VAL C   332              1.80            
REMARK 500   CD   LYS C    90     O    VAL C   332              1.87            
REMARK 500   CG   GLU A   265     O    HOH A  1639              1.88            
REMARK 500   O    THR C    40     CB   LEU C    43              1.91            
REMARK 500   CG2  VAL D    51     ND2  ASN D   317              1.92            
REMARK 500   O    HOH B  2488     O    HOH B  2606              1.93            
REMARK 500   O    THR C    40     CD1  LEU C    43              1.96            
REMARK 500   O    HOH B  2491     O    HOH B  2637              1.96            
REMARK 500   OE2  GLU A   220     O    HOH A  1527              1.99            
REMARK 500   O    THR C    72     CD1  PHE C    94              2.00            
REMARK 500   OE2  GLU D   265     O    HOH D  4533              2.01            
REMARK 500   CB   ASN C    69     O    HOH C  3526              2.02            
REMARK 500   OG   SER B    75     CG   ASN B   317              2.04            
REMARK 500   CE   LYS C    90     O    VAL C   332              2.07            
REMARK 500   O    VAL C    41     C    LEU C    43              2.07            
REMARK 500   O    HOH A  1525     O    HOH A  1547              2.08            
REMARK 500   O    VAL C    41     CA   LEU C    43              2.09            
REMARK 500   O    THR C    72     CE1  PHE C    94              2.09            
REMARK 500   O3   SO4 A  1402     O    HOH A  1470              2.10            
REMARK 500   OE1  GLU A   265     O3   SO4 A  1402              2.14            
REMARK 500   CG2  VAL C    50     CG   MET C    74              2.15            
REMARK 500   CB   SER B    75     CG   ASN B   317              2.15            
REMARK 500   O    HOH C  3517     O    HOH D  4509              2.16            
REMARK 500   O    HOH C  3536     O    HOH C  3540              2.18            
REMARK 500   OE2  GLU B   277     O    HOH B  2502              2.18            
REMARK 500   OD1  ASP B    85     O    HOH B  2548              2.18            
REMARK 500   OG   SER D    75     CG   ASN D   317              2.18            
REMARK 500   O    HOH A  1535     O    HOH A  1604              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B  2531     O    HOH B  2531     3555     1.36            
REMARK 500   O    HOH D  4513     O    HOH D  4513     3655     2.01            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    VAL A  41   CB    VAL A  41   CG2    -0.139                       
REMARK 500    GLU A 220   CG    GLU A 220   CD     -0.125                       
REMARK 500    GLU A 325   CG    GLU A 325   CD      0.132                       
REMARK 500    TYR C   7   CB    TYR C   7   CG     -0.145                       
REMARK 500    GLU C  21   C     ASP C  22   N      -0.148                       
REMARK 500    LYS C  25   CA    LYS C  25   C      -0.303                       
REMARK 500    ASP C  26   N     ASP C  26   CA      0.158                       
REMARK 500    ASP C  26   CA    ASP C  26   CB     -0.173                       
REMARK 500    VAL C  27   CA    VAL C  27   CB     -0.296                       
REMARK 500    ASP C  26   C     VAL C  27   N       0.177                       
REMARK 500    GLU C  30   CD    GLU C  30   OE1     0.157                       
REMARK 500    PRO C  38   N     PRO C  38   CA      0.105                       
REMARK 500    PRO C  38   CA    PRO C  38   C       0.184                       
REMARK 500    GLU C  39   N     GLU C  39   CA      0.165                       
REMARK 500    ALA C  42   N     ALA C  42   CA     -0.162                       
REMARK 500    GLN C  55   CA    GLN C  55   CB      0.306                       
REMARK 500    TYR C  58   CA    TYR C  58   CB     -0.177                       
REMARK 500    TYR C  58   CA    TYR C  58   C       0.171                       
REMARK 500    TYR C  58   C     ILE C  59   N      -0.453                       
REMARK 500    ALA C  60   CA    ALA C  60   CB      0.184                       
REMARK 500    ALA C  60   CA    ALA C  60   C      -0.591                       
REMARK 500    GLY C  70   CA    GLY C  70   C      -0.114                       
REMARK 500    LYS C  73   N     LYS C  73   CA      0.163                       
REMARK 500    LYS C  73   CA    LYS C  73   CB      0.154                       
REMARK 500    LYS C  73   CA    LYS C  73   C       0.241                       
REMARK 500    THR C  72   C     LYS C  73   N       0.258                       
REMARK 500    MET C  74   N     MET C  74   CA      0.433                       
REMARK 500    LYS C  73   C     MET C  74   N       0.326                       
REMARK 500    ALA C  89   N     ALA C  89   CA      0.140                       
REMARK 500    LYS C  90   CA    LYS C  90   C       0.363                       
REMARK 500    GLU C  91   CA    GLU C  91   CB     -0.141                       
REMARK 500    LEU C  92   C     LEU C  92   O      -0.156                       
REMARK 500    GLY C  93   N     GLY C  93   CA     -0.193                       
REMARK 500    ILE C  96   CA    ILE C  96   CB     -0.442                       
REMARK 500    THR C  97   CA    THR C  97   C       0.186                       
REMARK 500    ILE C  96   C     THR C  97   N       0.356                       
REMARK 500    LYS C 185   CG    LYS C 185   CD      0.213                       
REMARK 500    ARG C 236   CZ    ARG C 236   NH2     0.095                       
REMARK 500    LYS C 297   CD    LYS C 297   CE     -0.221                       
REMARK 500    LEU C 318   CA    LEU C 318   CB     -0.287                       
REMARK 500    VAL C 332   CB    VAL C 332   CG1    -0.292                       
REMARK 500    LYS D  45   CG    LYS D  45   CD      0.397                       
REMARK 500    GLU D 325   CB    GLU D 325   CG      0.128                       
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    LYS A  18   CD  -  CE  -  NZ  ANGL. DEV. =  19.0 DEGREES          
REMARK 500    VAL A  41   CA  -  CB  -  CG2 ANGL. DEV. =  10.9 DEGREES          
REMARK 500    ARG A  77   CD  -  NE  -  CZ  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    MET A  86   CG  -  SD  -  CE  ANGL. DEV. =  13.8 DEGREES          
REMARK 500    ARG A 120   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 131   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A 131   NE  -  CZ  -  NH2 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG A 179   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    ASP A 191   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 280   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A 289   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ASP B 280   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    THR C   2   N   -  CA  -  CB  ANGL. DEV. = -13.0 DEGREES          
REMARK 500    ILE C   4   CG1 -  CB  -  CG2 ANGL. DEV. = -15.8 DEGREES          
REMARK 500    TYR C   7   CA  -  CB  -  CG  ANGL. DEV. =  19.9 DEGREES          
REMARK 500    TYR C   7   CB  -  CG  -  CD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    TYR C   7   CB  -  CG  -  CD1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    GLU C  21   O   -  C   -  N   ANGL. DEV. = -10.6 DEGREES          
REMARK 500    ASP C  26   CA  -  CB  -  CG  ANGL. DEV. =  17.3 DEGREES          
REMARK 500    ASP C  26   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ASP C  26   C   -  N   -  CA  ANGL. DEV. = -19.8 DEGREES          
REMARK 500    VAL C  27   N   -  CA  -  CB  ANGL. DEV. =  14.3 DEGREES          
REMARK 500    GLU C  30   OE1 -  CD  -  OE2 ANGL. DEV. = -10.6 DEGREES          
REMARK 500    LEU C  35   O   -  C   -  N   ANGL. DEV. = -11.7 DEGREES          
REMARK 500    PRO C  38   N   -  CA  -  C   ANGL. DEV. =  16.0 DEGREES          
REMARK 500    PRO C  38   O   -  C   -  N   ANGL. DEV. = -10.3 DEGREES          
REMARK 500    ALA C  42   N   -  CA  -  CB  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    ALA C  42   N   -  CA  -  C   ANGL. DEV. = -16.7 DEGREES          
REMARK 500    ALA C  42   C   -  N   -  CA  ANGL. DEV. =  17.9 DEGREES          
REMARK 500    ASP C  48   N   -  CA  -  CB  ANGL. DEV. = -20.2 DEGREES          
REMARK 500    ASP C  48   N   -  CA  -  C   ANGL. DEV. =  18.3 DEGREES          
REMARK 500    GLN C  55   O   -  C   -  N   ANGL. DEV. = -68.7 DEGREES          
REMARK 500    LEU C  56   O   -  C   -  N   ANGL. DEV. =  11.5 DEGREES          
REMARK 500    TYR C  58   N   -  CA  -  CB  ANGL. DEV. =  13.7 DEGREES          
REMARK 500    TYR C  58   CB  -  CG  -  CD1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    TYR C  58   N   -  CA  -  C   ANGL. DEV. = -16.6 DEGREES          
REMARK 500    ILE C  59   CG1 -  CB  -  CG2 ANGL. DEV. = -20.2 DEGREES          
REMARK 500    TYR C  58   CA  -  C   -  N   ANGL. DEV. =  19.7 DEGREES          
REMARK 500    TYR C  58   O   -  C   -  N   ANGL. DEV. = -20.2 DEGREES          
REMARK 500    ILE C  59   C   -  N   -  CA  ANGL. DEV. =  38.3 DEGREES          
REMARK 500    ALA C  60   CB  -  CA  -  C   ANGL. DEV. = -18.5 DEGREES          
REMARK 500    ALA C  60   N   -  CA  -  CB  ANGL. DEV. =  -9.0 DEGREES          
REMARK 500    ALA C  60   N   -  CA  -  C   ANGL. DEV. =  38.0 DEGREES          
REMARK 500    LEU C  63   C   -  N   -  CA  ANGL. DEV. = -16.2 DEGREES          
REMARK 500    MET C  74   CB  -  CA  -  C   ANGL. DEV. = -15.9 DEGREES          
REMARK 500    MET C  74   CA  -  C   -  O   ANGL. DEV. = -27.7 DEGREES          
REMARK 500    LYS C  73   CA  -  C   -  N   ANGL. DEV. =  15.9 DEGREES          
REMARK 500    LYS C  73   O   -  C   -  N   ANGL. DEV. = -12.8 DEGREES          
REMARK 500    ILE C  84   CA  -  CB  -  CG2 ANGL. DEV. =  15.7 DEGREES          
REMARK 500    MET C  86   CG  -  SD  -  CE  ANGL. DEV. =   9.8 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      77 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    TYR A  53      111.68   -173.69                                   
REMARK 500    ASP A  85       95.26    -66.99                                   
REMARK 500    TYR A 102      -23.91   -146.33                                   
REMARK 500    SER A 103       92.34    174.56                                   
REMARK 500    SER A 235      -75.06    -98.29                                   
REMARK 500    ILE A 268      -57.27   -120.31                                   
REMARK 500    PRO A 296       57.88    -90.07                                   
REMARK 500    TYR B  53      105.48   -168.75                                   
REMARK 500    TYR B 102      -28.25   -142.61                                   
REMARK 500    SER B 103       96.28    176.81                                   
REMARK 500    HIS B 132       17.66     80.29                                   
REMARK 500    ASP B 209       38.03    -75.13                                   
REMARK 500    SER B 235      -77.90    -97.16                                   
REMARK 500    GLU C  21        3.33    -52.82                                   
REMARK 500    HIS C  24       39.45   -162.85                                   
REMARK 500    LYS C  25       -6.81    -34.80                                   
REMARK 500    LEU C  35     -146.21    -57.83                                   
REMARK 500    LEU C  36       51.46   -151.25                                   
REMARK 500    PRO C  38       59.60    -67.38                                   
REMARK 500    GLU C  39      -19.45   -159.06                                   
REMARK 500    VAL C  41      -89.48    -31.66                                   
REMARK 500    ALA C  42      -36.26      7.12                                   
REMARK 500    LYS C  45       81.50    -45.01                                   
REMARK 500    TYR C  53      121.11   -174.71                                   
REMARK 500    GLN C  54      164.12    171.58                                   
REMARK 500    ASP C  57      131.96    -21.72                                   
REMARK 500    TYR C  58       63.53   -103.20                                   
REMARK 500    THR C  72      -53.14   -123.63                                   
REMARK 500    SER C  75      113.41   -162.79                                   
REMARK 500    ASP C  82      -61.17   -122.26                                   
REMARK 500    ASN C  83       30.55    -69.08                                   
REMARK 500    ASP C  85       92.33    -43.91                                   
REMARK 500    MET C  86     -132.44    -59.60                                   
REMARK 500    ALA C  87      -63.47     18.45                                   
REMARK 500    LYS C  88      -39.65    -39.07                                   
REMARK 500    TYR C 102      -30.05   -131.21                                   
REMARK 500    SER C 103       96.33    177.04                                   
REMARK 500    SER C 235      -77.96    -99.07                                   
REMARK 500    TYR D  53      106.67   -167.80                                   
REMARK 500    TYR D 102      -33.21   -135.59                                   
REMARK 500    SER D 103       99.40   -177.10                                   
REMARK 500    HIS D 132       20.60     80.54                                   
REMARK 500    SER D 235      -72.94    -94.13                                   
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 TYR C   58     ILE C   59                  144.30                    
REMARK 500 ALA C   60     GLU C   61                  149.76                    
REMARK 500 LYS C   90     GLU C   91                  147.84                    
REMARK 500 GLU C   91     LEU C   92                 -149.34                    
REMARK 500 LEU C   92     GLY C   93                 -111.98                    
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    GLU C  30         0.12    SIDE_CHAIN                              
REMARK 500    PHE C  94         0.06    SIDE_CHAIN                              
REMARK 500    GLU C 265         0.08    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, 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    LYS C   3        -12.29                                           
REMARK 500    GLU C  21        -13.47                                           
REMARK 500    LEU C  35        -24.56                                           
REMARK 500    VAL C  41         11.05                                           
REMARK 500    GLY C  49        -12.81                                           
REMARK 500    GLN C  55         48.35                                           
REMARK 500    ALA C  60        -14.72                                           
REMARK 500    GLY C  70         17.07                                           
REMARK 500    MET C  74         35.30                                           
REMARK 500    MET C  86         28.37                                           
REMARK 500    LYS C  90        -28.39                                           
REMARK 500    GLY C  93         26.15                                           
REMARK 500    ILE C  96        -28.75                                           
REMARK 500    THR C  97         11.30                                           
REMARK 500    VAL D 152         10.88                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1400                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1401                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1402                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1403                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2400                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2401                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2402                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2403                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 3400                
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 4400                
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 4401                
DBREF  1J4A A    1   333  UNP    P26297   LDHD_LACDE       1    333             
DBREF  1J4A B    1   333  UNP    P26297   LDHD_LACDE       1    333             
DBREF  1J4A C    1   333  UNP    P26297   LDHD_LACDE       1    333             
DBREF  1J4A D    1   333  UNP    P26297   LDHD_LACDE       1    333             
SEQADV 1J4A ILE A   59  UNP  P26297    THR    59 SEE REMARK 999                 
SEQADV 1J4A ARG A  117  UNP  P26297    ALA   117 SEE REMARK 999                 
SEQADV 1J4A VAL A  152  UNP  P26297    ILE   152 SEE REMARK 999                 
SEQADV 1J4A LYS A  297  UNP  P26297    HIS   297 ENGINEERED                     
SEQADV 1J4A ILE B   59  UNP  P26297    THR    59 SEE REMARK 999                 
SEQADV 1J4A ARG B  117  UNP  P26297    ALA   117 SEE REMARK 999                 
SEQADV 1J4A VAL B  152  UNP  P26297    ILE   152 SEE REMARK 999                 
SEQADV 1J4A LYS B  297  UNP  P26297    HIS   297 ENGINEERED                     
SEQADV 1J4A ILE C   59  UNP  P26297    THR    59 SEE REMARK 999                 
SEQADV 1J4A ARG C  117  UNP  P26297    ALA   117 SEE REMARK 999                 
SEQADV 1J4A VAL C  152  UNP  P26297    ILE   152 SEE REMARK 999                 
SEQADV 1J4A LYS C  297  UNP  P26297    HIS   297 ENGINEERED                     
SEQADV 1J4A ILE D   59  UNP  P26297    THR    59 SEE REMARK 999                 
SEQADV 1J4A ARG D  117  UNP  P26297    ALA   117 SEE REMARK 999                 
SEQADV 1J4A VAL D  152  UNP  P26297    ILE   152 SEE REMARK 999                 
SEQADV 1J4A LYS D  297  UNP  P26297    HIS   297 ENGINEERED                     
SEQRES   1 A  333  MET THR LYS ILE PHE ALA TYR ALA ILE ARG GLU ASP GLU          
SEQRES   2 A  333  LYS PRO PHE LEU LYS GLU TRP GLU ASP ALA HIS LYS ASP          
SEQRES   3 A  333  VAL GLU VAL GLU TYR THR ASP LYS LEU LEU THR PRO GLU          
SEQRES   4 A  333  THR VAL ALA LEU ALA LYS GLY ALA ASP GLY VAL VAL VAL          
SEQRES   5 A  333  TYR GLN GLN LEU ASP TYR ILE ALA GLU THR LEU GLN ALA          
SEQRES   6 A  333  LEU ALA ASP ASN GLY ILE THR LYS MET SER LEU ARG ASN          
SEQRES   7 A  333  VAL GLY VAL ASP ASN ILE ASP MET ALA LYS ALA LYS GLU          
SEQRES   8 A  333  LEU GLY PHE GLN ILE THR ASN VAL PRO VAL TYR SER PRO          
SEQRES   9 A  333  ASN ALA ILE ALA GLU HIS ALA ALA ILE GLN ALA ALA ARG          
SEQRES  10 A  333  ILE LEU ARG GLN ASP LYS ALA MET ASP GLU LYS VAL ALA          
SEQRES  11 A  333  ARG HIS ASP LEU ARG TRP ALA PRO THR ILE GLY ARG GLU          
SEQRES  12 A  333  VAL ARG ASP GLN VAL VAL GLY VAL VAL GLY THR GLY HIS          
SEQRES  13 A  333  ILE GLY GLN VAL PHE MET GLN ILE MET GLU GLY PHE GLY          
SEQRES  14 A  333  ALA LYS VAL ILE THR TYR ASP ILE PHE ARG ASN PRO GLU          
SEQRES  15 A  333  LEU GLU LYS LYS GLY TYR TYR VAL ASP SER LEU ASP ASP          
SEQRES  16 A  333  LEU TYR LYS GLN ALA ASP VAL ILE SER LEU HIS VAL PRO          
SEQRES  17 A  333  ASP VAL PRO ALA ASN VAL HIS MET ILE ASN ASP GLU SER          
SEQRES  18 A  333  ILE ALA LYS MET LYS GLN ASP VAL VAL ILE VAL ASN VAL          
SEQRES  19 A  333  SER ARG GLY PRO LEU VAL ASP THR ASP ALA VAL ILE ARG          
SEQRES  20 A  333  GLY LEU ASP SER GLY LYS ILE PHE GLY TYR ALA MET ASP          
SEQRES  21 A  333  VAL TYR GLU GLY GLU VAL GLY ILE PHE ASN GLU ASP TRP          
SEQRES  22 A  333  GLU GLY LYS GLU PHE PRO ASP ALA ARG LEU ALA ASP LEU          
SEQRES  23 A  333  ILE ALA ARG PRO ASN VAL LEU VAL THR PRO LYS THR ALA          
SEQRES  24 A  333  PHE TYR THR THR HIS ALA VAL ARG ASN MET VAL VAL LYS          
SEQRES  25 A  333  ALA PHE ASP ASN ASN LEU GLU LEU VAL GLU GLY LYS GLU          
SEQRES  26 A  333  ALA GLU THR PRO VAL LYS VAL GLY                              
SEQRES   1 B  333  MET THR LYS ILE PHE ALA TYR ALA ILE ARG GLU ASP GLU          
SEQRES   2 B  333  LYS PRO PHE LEU LYS GLU TRP GLU ASP ALA HIS LYS ASP          
SEQRES   3 B  333  VAL GLU VAL GLU TYR THR ASP LYS LEU LEU THR PRO GLU          
SEQRES   4 B  333  THR VAL ALA LEU ALA LYS GLY ALA ASP GLY VAL VAL VAL          
SEQRES   5 B  333  TYR GLN GLN LEU ASP TYR ILE ALA GLU THR LEU GLN ALA          
SEQRES   6 B  333  LEU ALA ASP ASN GLY ILE THR LYS MET SER LEU ARG ASN          
SEQRES   7 B  333  VAL GLY VAL ASP ASN ILE ASP MET ALA LYS ALA LYS GLU          
SEQRES   8 B  333  LEU GLY PHE GLN ILE THR ASN VAL PRO VAL TYR SER PRO          
SEQRES   9 B  333  ASN ALA ILE ALA GLU HIS ALA ALA ILE GLN ALA ALA ARG          
SEQRES  10 B  333  ILE LEU ARG GLN ASP LYS ALA MET ASP GLU LYS VAL ALA          
SEQRES  11 B  333  ARG HIS ASP LEU ARG TRP ALA PRO THR ILE GLY ARG GLU          
SEQRES  12 B  333  VAL ARG ASP GLN VAL VAL GLY VAL VAL GLY THR GLY HIS          
SEQRES  13 B  333  ILE GLY GLN VAL PHE MET GLN ILE MET GLU GLY PHE GLY          
SEQRES  14 B  333  ALA LYS VAL ILE THR TYR ASP ILE PHE ARG ASN PRO GLU          
SEQRES  15 B  333  LEU GLU LYS LYS GLY TYR TYR VAL ASP SER LEU ASP ASP          
SEQRES  16 B  333  LEU TYR LYS GLN ALA ASP VAL ILE SER LEU HIS VAL PRO          
SEQRES  17 B  333  ASP VAL PRO ALA ASN VAL HIS MET ILE ASN ASP GLU SER          
SEQRES  18 B  333  ILE ALA LYS MET LYS GLN ASP VAL VAL ILE VAL ASN VAL          
SEQRES  19 B  333  SER ARG GLY PRO LEU VAL ASP THR ASP ALA VAL ILE ARG          
SEQRES  20 B  333  GLY LEU ASP SER GLY LYS ILE PHE GLY TYR ALA MET ASP          
SEQRES  21 B  333  VAL TYR GLU GLY GLU VAL GLY ILE PHE ASN GLU ASP TRP          
SEQRES  22 B  333  GLU GLY LYS GLU PHE PRO ASP ALA ARG LEU ALA ASP LEU          
SEQRES  23 B  333  ILE ALA ARG PRO ASN VAL LEU VAL THR PRO LYS THR ALA          
SEQRES  24 B  333  PHE TYR THR THR HIS ALA VAL ARG ASN MET VAL VAL LYS          
SEQRES  25 B  333  ALA PHE ASP ASN ASN LEU GLU LEU VAL GLU GLY LYS GLU          
SEQRES  26 B  333  ALA GLU THR PRO VAL LYS VAL GLY                              
SEQRES   1 C  333  MET THR LYS ILE PHE ALA TYR ALA ILE ARG GLU ASP GLU          
SEQRES   2 C  333  LYS PRO PHE LEU LYS GLU TRP GLU ASP ALA HIS LYS ASP          
SEQRES   3 C  333  VAL GLU VAL GLU TYR THR ASP LYS LEU LEU THR PRO GLU          
SEQRES   4 C  333  THR VAL ALA LEU ALA LYS GLY ALA ASP GLY VAL VAL VAL          
SEQRES   5 C  333  TYR GLN GLN LEU ASP TYR ILE ALA GLU THR LEU GLN ALA          
SEQRES   6 C  333  LEU ALA ASP ASN GLY ILE THR LYS MET SER LEU ARG ASN          
SEQRES   7 C  333  VAL GLY VAL ASP ASN ILE ASP MET ALA LYS ALA LYS GLU          
SEQRES   8 C  333  LEU GLY PHE GLN ILE THR ASN VAL PRO VAL TYR SER PRO          
SEQRES   9 C  333  ASN ALA ILE ALA GLU HIS ALA ALA ILE GLN ALA ALA ARG          
SEQRES  10 C  333  ILE LEU ARG GLN ASP LYS ALA MET ASP GLU LYS VAL ALA          
SEQRES  11 C  333  ARG HIS ASP LEU ARG TRP ALA PRO THR ILE GLY ARG GLU          
SEQRES  12 C  333  VAL ARG ASP GLN VAL VAL GLY VAL VAL GLY THR GLY HIS          
SEQRES  13 C  333  ILE GLY GLN VAL PHE MET GLN ILE MET GLU GLY PHE GLY          
SEQRES  14 C  333  ALA LYS VAL ILE THR TYR ASP ILE PHE ARG ASN PRO GLU          
SEQRES  15 C  333  LEU GLU LYS LYS GLY TYR TYR VAL ASP SER LEU ASP ASP          
SEQRES  16 C  333  LEU TYR LYS GLN ALA ASP VAL ILE SER LEU HIS VAL PRO          
SEQRES  17 C  333  ASP VAL PRO ALA ASN VAL HIS MET ILE ASN ASP GLU SER          
SEQRES  18 C  333  ILE ALA LYS MET LYS GLN ASP VAL VAL ILE VAL ASN VAL          
SEQRES  19 C  333  SER ARG GLY PRO LEU VAL ASP THR ASP ALA VAL ILE ARG          
SEQRES  20 C  333  GLY LEU ASP SER GLY LYS ILE PHE GLY TYR ALA MET ASP          
SEQRES  21 C  333  VAL TYR GLU GLY GLU VAL GLY ILE PHE ASN GLU ASP TRP          
SEQRES  22 C  333  GLU GLY LYS GLU PHE PRO ASP ALA ARG LEU ALA ASP LEU          
SEQRES  23 C  333  ILE ALA ARG PRO ASN VAL LEU VAL THR PRO LYS THR ALA          
SEQRES  24 C  333  PHE TYR THR THR HIS ALA VAL ARG ASN MET VAL VAL LYS          
SEQRES  25 C  333  ALA PHE ASP ASN ASN LEU GLU LEU VAL GLU GLY LYS GLU          
SEQRES  26 C  333  ALA GLU THR PRO VAL LYS VAL GLY                              
SEQRES   1 D  333  MET THR LYS ILE PHE ALA TYR ALA ILE ARG GLU ASP GLU          
SEQRES   2 D  333  LYS PRO PHE LEU LYS GLU TRP GLU ASP ALA HIS LYS ASP          
SEQRES   3 D  333  VAL GLU VAL GLU TYR THR ASP LYS LEU LEU THR PRO GLU          
SEQRES   4 D  333  THR VAL ALA LEU ALA LYS GLY ALA ASP GLY VAL VAL VAL          
SEQRES   5 D  333  TYR GLN GLN LEU ASP TYR ILE ALA GLU THR LEU GLN ALA          
SEQRES   6 D  333  LEU ALA ASP ASN GLY ILE THR LYS MET SER LEU ARG ASN          
SEQRES   7 D  333  VAL GLY VAL ASP ASN ILE ASP MET ALA LYS ALA LYS GLU          
SEQRES   8 D  333  LEU GLY PHE GLN ILE THR ASN VAL PRO VAL TYR SER PRO          
SEQRES   9 D  333  ASN ALA ILE ALA GLU HIS ALA ALA ILE GLN ALA ALA ARG          
SEQRES  10 D  333  ILE LEU ARG GLN ASP LYS ALA MET ASP GLU LYS VAL ALA          
SEQRES  11 D  333  ARG HIS ASP LEU ARG TRP ALA PRO THR ILE GLY ARG GLU          
SEQRES  12 D  333  VAL ARG ASP GLN VAL VAL GLY VAL VAL GLY THR GLY HIS          
SEQRES  13 D  333  ILE GLY GLN VAL PHE MET GLN ILE MET GLU GLY PHE GLY          
SEQRES  14 D  333  ALA LYS VAL ILE THR TYR ASP ILE PHE ARG ASN PRO GLU          
SEQRES  15 D  333  LEU GLU LYS LYS GLY TYR TYR VAL ASP SER LEU ASP ASP          
SEQRES  16 D  333  LEU TYR LYS GLN ALA ASP VAL ILE SER LEU HIS VAL PRO          
SEQRES  17 D  333  ASP VAL PRO ALA ASN VAL HIS MET ILE ASN ASP GLU SER          
SEQRES  18 D  333  ILE ALA LYS MET LYS GLN ASP VAL VAL ILE VAL ASN VAL          
SEQRES  19 D  333  SER ARG GLY PRO LEU VAL ASP THR ASP ALA VAL ILE ARG          
SEQRES  20 D  333  GLY LEU ASP SER GLY LYS ILE PHE GLY TYR ALA MET ASP          
SEQRES  21 D  333  VAL TYR GLU GLY GLU VAL GLY ILE PHE ASN GLU ASP TRP          
SEQRES  22 D  333  GLU GLY LYS GLU PHE PRO ASP ALA ARG LEU ALA ASP LEU          
SEQRES  23 D  333  ILE ALA ARG PRO ASN VAL LEU VAL THR PRO LYS THR ALA          
SEQRES  24 D  333  PHE TYR THR THR HIS ALA VAL ARG ASN MET VAL VAL LYS          
SEQRES  25 D  333  ALA PHE ASP ASN ASN LEU GLU LEU VAL GLU GLY LYS GLU          
SEQRES  26 D  333  ALA GLU THR PRO VAL LYS VAL GLY                              
HET    SO4  A1400       5                                                       
HET    SO4  A1401       5                                                       
HET    SO4  A1402       5                                                       
HET    SO4  A1403       5                                                       
HET    SO4  B2400       5                                                       
HET    SO4  B2401       5                                                       
HET    SO4  B2402       5                                                       
HET    SO4  B2403       5                                                       
HET    SO4  C3400       5                                                       
HET    SO4  D4400       5                                                       
HET    SO4  D4401       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  SO4    11(O4 S 2-)                                                  
FORMUL  16  HOH   *900(H2 O)                                                    
HELIX    1   1 ARG A   10  ASP A   12  5                                   3    
HELIX    2   2 GLU A   13  ALA A   23  1                                  11    
HELIX    3   3 THR A   40  LYS A   45  5                                   6    
HELIX    4   4 ILE A   59  ASN A   69  1                                  11    
HELIX    5   5 ASP A   85  LEU A   92  1                                   8    
HELIX    6   6 SER A  103  GLN A  121  1                                  19    
HELIX    7   7 GLN A  121  ARG A  131  1                                  11    
HELIX    8   8 GLU A  143  ASP A  146  5                                   4    
HELIX    9   9 GLY A  155  PHE A  168  1                                  14    
HELIX   10  10 ASN A  180  LYS A  186  1                                   7    
HELIX   11  11 SER A  192  ALA A  200  1                                   9    
HELIX   12  12 VAL A  210  VAL A  214  5                                   5    
HELIX   13  13 ASN A  218  MET A  225  1                                   8    
HELIX   14  14 ARG A  236  VAL A  240  5                                   5    
HELIX   15  15 ASP A  241  SER A  251  1                                  11    
HELIX   16  16 ASP A  280  ARG A  289  1                                  10    
HELIX   17  17 THR A  302  GLU A  322  1                                  21    
HELIX   18  18 ARG B   10  ASP B   12  5                                   3    
HELIX   19  19 GLU B   13  ALA B   23  1                                  11    
HELIX   20  20 GLU B   39  LYS B   45  5                                   7    
HELIX   21  21 ILE B   59  ASN B   69  1                                  11    
HELIX   22  22 ASP B   85  LEU B   92  1                                   8    
HELIX   23  23 SER B  103  GLN B  121  1                                  19    
HELIX   24  24 GLN B  121  ARG B  131  1                                  11    
HELIX   25  25 GLU B  143  ASP B  146  5                                   4    
HELIX   26  26 GLY B  155  GLY B  169  1                                  15    
HELIX   27  27 ASN B  180  LYS B  186  1                                   7    
HELIX   28  28 SER B  192  ALA B  200  1                                   9    
HELIX   29  29 VAL B  210  VAL B  214  5                                   5    
HELIX   30  30 ASN B  218  MET B  225  1                                   8    
HELIX   31  31 ARG B  236  VAL B  240  5                                   5    
HELIX   32  32 ASP B  241  SER B  251  1                                  11    
HELIX   33  33 ASP B  280  ARG B  289  1                                  10    
HELIX   34  34 THR B  302  GLU B  322  1                                  21    
HELIX   35  35 ARG C   10  ASP C   12  5                                   3    
HELIX   36  36 GLU C   13  ASP C   22  1                                  10    
HELIX   37  37 THR C   40  ALA C   44  5                                   5    
HELIX   38  38 ILE C   59  ASN C   69  1                                  11    
HELIX   39  39 ASP C   85  LEU C   92  1                                   8    
HELIX   40  40 SER C  103  GLN C  121  1                                  19    
HELIX   41  41 GLN C  121  ARG C  131  1                                  11    
HELIX   42  42 GLU C  143  ASP C  146  5                                   4    
HELIX   43  43 GLY C  155  PHE C  168  1                                  14    
HELIX   44  44 ASN C  180  LYS C  186  1                                   7    
HELIX   45  45 SER C  192  ALA C  200  1                                   9    
HELIX   46  46 VAL C  210  VAL C  214  5                                   5    
HELIX   47  47 ASN C  218  MET C  225  1                                   8    
HELIX   48  48 ARG C  236  VAL C  240  5                                   5    
HELIX   49  49 ASP C  241  SER C  251  1                                  11    
HELIX   50  50 ASP C  280  ARG C  289  1                                  10    
HELIX   51  51 THR C  302  GLU C  322  1                                  21    
HELIX   52  52 ARG D   10  ASP D   12  5                                   3    
HELIX   53  53 GLU D   13  ALA D   23  1                                  11    
HELIX   54  54 THR D   40  LYS D   45  5                                   6    
HELIX   55  55 ILE D   59  ASN D   69  1                                  11    
HELIX   56  56 ASP D   85  LEU D   92  1                                   8    
HELIX   57  57 SER D  103  GLN D  121  1                                  19    
HELIX   58  58 GLN D  121  ARG D  131  1                                  11    
HELIX   59  59 GLU D  143  ASP D  146  5                                   4    
HELIX   60  60 GLY D  155  PHE D  168  1                                  14    
HELIX   61  61 ASN D  180  LYS D  186  1                                   7    
HELIX   62  62 SER D  192  ALA D  200  1                                   9    
HELIX   63  63 VAL D  210  VAL D  214  5                                   5    
HELIX   64  64 ASN D  218  MET D  225  1                                   8    
HELIX   65  65 ARG D  236  VAL D  240  5                                   5    
HELIX   66  66 ASP D  241  SER D  251  1                                  11    
HELIX   67  67 ASP D  280  ARG D  289  1                                  10    
HELIX   68  68 THR D  302  GLU D  322  1                                  21    
SHEET    1   A 5 GLU A  28  TYR A  31  0                                        
SHEET    2   A 5 LYS A   3  ALA A   6  1  N  ILE A   4   O  GLU A  28           
SHEET    3   A 5 GLY A  49  VAL A  52  1  O  GLY A  49   N  PHE A   5           
SHEET    4   A 5 LYS A  73  LEU A  76  1  O  SER A  75   N  VAL A  50           
SHEET    5   A 5 GLN A  95  THR A  97  1  O  GLN A  95   N  MET A  74           
SHEET    1   B 6 LYS A 171  TYR A 175  0                                        
SHEET    2   B 6 VAL A 148  VAL A 152  1  N  VAL A 149   O  LYS A 171           
SHEET    3   B 6 VAL A 202  LEU A 205  1  O  VAL A 202   N  GLY A 150           
SHEET    4   B 6 VAL A 229  ASN A 233  1  O  VAL A 232   N  ILE A 203           
SHEET    5   B 6 ILE A 254  MET A 259  1  O  ALA A 258   N  ASN A 233           
SHEET    6   B 6 VAL A 292  VAL A 294  1  O  LEU A 293   N  MET A 259           
SHEET    1   C 6 GLU B  28  TYR B  31  0                                        
SHEET    2   C 6 LYS B   3  ALA B   6  1  N  ILE B   4   O  GLU B  28           
SHEET    3   C 6 GLY B  49  VAL B  52  1  O  VAL B  51   N  PHE B   5           
SHEET    4   C 6 LYS B  73  LEU B  76  1  O  LYS B  73   N  VAL B  50           
SHEET    5   C 6 GLN B  95  THR B  97  1  O  GLN B  95   N  MET B  74           
SHEET    6   C 6 PRO B 329  VAL B 330 -1  O  VAL B 330   N  ILE B  96           
SHEET    1   D 6 LYS B 171  TYR B 175  0                                        
SHEET    2   D 6 VAL B 148  VAL B 152  1  N  VAL B 149   O  LYS B 171           
SHEET    3   D 6 VAL B 202  LEU B 205  1  O  VAL B 202   N  GLY B 150           
SHEET    4   D 6 VAL B 229  ASN B 233  1  O  VAL B 230   N  ILE B 203           
SHEET    5   D 6 ILE B 254  MET B 259  1  O  ALA B 258   N  ILE B 231           
SHEET    6   D 6 VAL B 292  VAL B 294  1  O  LEU B 293   N  MET B 259           
SHEET    1   E 3 GLU C  28  TYR C  31  0                                        
SHEET    2   E 3 LYS C   3  ALA C   6  1  N  ILE C   4   O  GLU C  28           
SHEET    3   E 3 VAL C  50  VAL C  51  1  O  VAL C  51   N  PHE C   5           
SHEET    1   F 6 LYS C 171  TYR C 175  0                                        
SHEET    2   F 6 VAL C 148  VAL C 152  1  N  VAL C 151   O  ILE C 173           
SHEET    3   F 6 VAL C 202  LEU C 205  1  O  VAL C 202   N  GLY C 150           
SHEET    4   F 6 VAL C 229  ASN C 233  1  O  VAL C 232   N  ILE C 203           
SHEET    5   F 6 ILE C 254  MET C 259  1  O  ALA C 258   N  ASN C 233           
SHEET    6   F 6 VAL C 292  VAL C 294  1  O  LEU C 293   N  MET C 259           
SHEET    1   G 6 GLU D  28  TYR D  31  0                                        
SHEET    2   G 6 LYS D   3  ALA D   6  1  N  ILE D   4   O  GLU D  28           
SHEET    3   G 6 GLY D  49  VAL D  52  1  O  GLY D  49   N  PHE D   5           
SHEET    4   G 6 LYS D  73  LEU D  76  1  O  SER D  75   N  VAL D  52           
SHEET    5   G 6 GLN D  95  THR D  97  1  O  GLN D  95   N  MET D  74           
SHEET    6   G 6 PRO D 329  VAL D 330 -1  O  VAL D 330   N  ILE D  96           
SHEET    1   H 6 LYS D 171  TYR D 175  0                                        
SHEET    2   H 6 VAL D 148  VAL D 152  1  N  VAL D 149   O  ILE D 173           
SHEET    3   H 6 VAL D 202  LEU D 205  1  O  VAL D 202   N  GLY D 150           
SHEET    4   H 6 VAL D 229  ASN D 233  1  O  VAL D 230   N  ILE D 203           
SHEET    5   H 6 ILE D 254  MET D 259  1  O  ALA D 258   N  ASN D 233           
SHEET    6   H 6 VAL D 292  VAL D 294  1  O  LEU D 293   N  MET D 259           
CISPEP   1 ALA A  137    PRO A  138          0         4.81                     
CISPEP   2 ALA B  137    PRO B  138          0        -0.26                     
CISPEP   3 ALA C  137    PRO C  138          0         4.76                     
CISPEP   4 ALA D  137    PRO D  138          0        -2.04                     
SITE     1 AC1  7 GLY A 155  HIS A 156  ILE A 157  HOH A1423                    
SITE     2 AC1  7 HOH A1444  HOH A1479  HOH A1642                               
SITE     1 AC2  5 GLN A  55  ASN A  78  VAL A  79  GLY A  80                    
SITE     2 AC2  5 HOH A1611                                                     
SITE     1 AC3  7 ARG A 236  GLY A 237  VAL A 261  LYS A 297                    
SITE     2 AC3  7 HOH A1470  HOH A1554  HOH A1638                               
SITE     1 AC4  3 LYS A  18  GLU A  21  TYR A  31                               
SITE     1 AC5  7 GLY B 155  HIS B 156  ILE B 157  HOH B2416                    
SITE     2 AC5  7 HOH B2488  HOH B2585  HOH B2656                               
SITE     1 AC6  4 ASN B  78  VAL B  79  GLY B  80  SO4 B2403                    
SITE     1 AC7  3 HIS B 304  ASN B 308  HOH B2511                               
SITE     1 AC8  5 TYR B  53  PHE B 300  SO4 B2401  HOH B2495                    
SITE     2 AC8  5 HOH B2572                                                     
SITE     1 AC9  7 GLY C 155  HIS C 156  ILE C 157  HOH C3415                    
SITE     2 AC9  7 HOH C3467  HOH C3530  HOH C3554                               
SITE     1 BC1  5 GLY D 155  HIS D 156  ILE D 157  HOH D4418                    
SITE     2 BC1  5 HOH D4449                                                     
SITE     1 BC2  6 GLN D  55  ASN D  78  VAL D  79  GLY D  80                    
SITE     2 BC2  6 HOH D4535  HOH D4626                                          
CRYST1   94.300  188.000  193.400  90.00  90.00  90.00 C 2 2 21     32          
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      0.010604  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005319  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005171        0.00000                         
MTRIX1   1 -0.894000 -0.096000  0.437000      -21.43531    1                    
MTRIX2   1 -0.082000 -0.925000 -0.372000      168.97028    1                    
MTRIX3   1  0.440000 -0.368000  0.819000       39.45271    1                    
MTRIX1   2  0.676000 -0.557000 -0.482000      100.49666    1                    
MTRIX2   2 -0.553000 -0.816000  0.167000      226.24240    1                    
MTRIX3   2 -0.487000  0.154000 -0.860000       88.51561    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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