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Database: PDB
Entry: 3GNT
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Original site: 3GNT 
HEADER    OXIDOREDUCTASE                          18-MAR-09   3GNT              
TITLE     CRYSTAL STRUCTURE OF THE STAPHYLOCOCCUS AUREUS ENOYL-ACYL CARRIER     
TITLE    2 PROTEIN REDUCTASE (FABI) IN APO FORM (TWO MOLECULES IN AU)           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH];             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.3.1.9;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 STRAIN: MRSA252;                                                     
SOURCE   5 GENE: FABI;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    ENOYL REDUCTASE, ROSSMANN FOLD, OXIDOREDUCTASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.PRIYADARSHI,K.Y.HWANG                                               
REVDAT   2   12-FEB-14 3GNT    1       JRNL   VERSN                             
REVDAT   1   20-OCT-09 3GNT    0                                                
JRNL        AUTH   A.PRIYADARSHI,E.E.KIM,K.Y.HWANG                              
JRNL        TITL   STRUCTURAL INSIGHTS INTO STAPHYLOCOCCUS AUREUS ENOYL-ACP     
JRNL        TITL 2 REDUCTASE (FABI), IN COMPLEX WITH NADP AND TRICLOSAN.        
JRNL        REF    PROTEINS                      V.  78   480 2010              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   19768684                                                     
JRNL        DOI    10.1002/PROT.22581                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 10886                          
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) : 0.243                           
REMARK   3   R VALUE            (WORKING SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 548                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 434                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 45.21                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 14                           
REMARK   3   BIN FREE R VALUE                    : 0.4030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3157                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.12000                                              
REMARK   3    B22 (A**2) : -0.14000                                             
REMARK   3    B33 (A**2) : 0.05000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.03000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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): 0.444         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.278         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.349        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.879                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.869                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3194 ; 0.046 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4302 ; 4.260 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   399 ;22.748 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   142 ;45.602 ;25.282       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   594 ;29.959 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;27.305 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   503 ; 0.736 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2335 ; 0.016 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2217 ; 0.435 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2228 ; 0.398 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   194 ; 0.297 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    23 ; 0.464 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  2075 ; 2.224 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3224 ; 3.073 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1272 ; 5.057 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1078 ; 7.129 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3GNT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052092.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-MAY-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 6C1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10886                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : 0.17000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 47.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.18000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.17000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 2PD3                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 400, 0.1M TRIS PH 8.0, 4%        
REMARK 280  GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       57.54950            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.23100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       57.54950            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       37.23100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 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   BIOMT1   2 -1.000000  0.000000  0.000000      -80.49047            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -61.54576            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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 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     ALA A    95                                                      
REMARK 465     PHE A    96                                                      
REMARK 465     ALA A    97                                                      
REMARK 465     ASN A    98                                                      
REMARK 465     MET A    99                                                      
REMARK 465     GLU A   100                                                      
REMARK 465     ASP A   101                                                      
REMARK 465     LEU A   102                                                      
REMARK 465     ARG A   103                                                      
REMARK 465     GLY A   104                                                      
REMARK 465     ARG A   105                                                      
REMARK 465     PHE A   106                                                      
REMARK 465     SER A   107                                                      
REMARK 465     GLU A   108                                                      
REMARK 465     THR A   109                                                      
REMARK 465     SER A   110                                                      
REMARK 465     ARG A   111                                                      
REMARK 465     GLU A   112                                                      
REMARK 465     GLY A   113                                                      
REMARK 465     PHE A   114                                                      
REMARK 465     LEU A   115                                                      
REMARK 465     LEU A   116                                                      
REMARK 465     ALA A   117                                                      
REMARK 465     GLN A   118                                                      
REMARK 465     ASP A   119                                                      
REMARK 465     LEU A   148                                                      
REMARK 465     GLY A   149                                                      
REMARK 465     GLY A   150                                                      
REMARK 465     GLU A   151                                                      
REMARK 465     PHE A   152                                                      
REMARK 465     ALA A   153                                                      
REMARK 465     VAL A   154                                                      
REMARK 465     GLN A   155                                                      
REMARK 465     ASN A   156                                                      
REMARK 465     TYR A   157                                                      
REMARK 465     ASN A   158                                                      
REMARK 465     VAL A   159                                                      
REMARK 465     MET A   160                                                      
REMARK 465     GLY A   161                                                      
REMARK 465     VAL A   162                                                      
REMARK 465     ALA A   163                                                      
REMARK 465     LEU A   196                                                      
REMARK 465     SER A   197                                                      
REMARK 465     ALA A   198                                                      
REMARK 465     LYS A   199                                                      
REMARK 465     GLY A   200                                                      
REMARK 465     VAL A   201                                                      
REMARK 465     GLY A   202                                                      
REMARK 465     GLY A   203                                                      
REMARK 465     ILE B    94                                                      
REMARK 465     ALA B    95                                                      
REMARK 465     PHE B    96                                                      
REMARK 465     ALA B    97                                                      
REMARK 465     ASN B    98                                                      
REMARK 465     MET B    99                                                      
REMARK 465     GLU B   100                                                      
REMARK 465     ASP B   101                                                      
REMARK 465     LEU B   102                                                      
REMARK 465     ARG B   103                                                      
REMARK 465     GLY B   104                                                      
REMARK 465     ARG B   105                                                      
REMARK 465     PHE B   106                                                      
REMARK 465     SER B   107                                                      
REMARK 465     GLU B   108                                                      
REMARK 465     THR B   109                                                      
REMARK 465     SER B   110                                                      
REMARK 465     ARG B   111                                                      
REMARK 465     GLU B   112                                                      
REMARK 465     GLY B   113                                                      
REMARK 465     PHE B   114                                                      
REMARK 465     LEU B   115                                                      
REMARK 465     LEU B   116                                                      
REMARK 465     ALA B   117                                                      
REMARK 465     GLN B   118                                                      
REMARK 465     ASP B   119                                                      
REMARK 465     LEU B   148                                                      
REMARK 465     GLY B   149                                                      
REMARK 465     GLY B   150                                                      
REMARK 465     GLU B   151                                                      
REMARK 465     PHE B   152                                                      
REMARK 465     ALA B   153                                                      
REMARK 465     VAL B   154                                                      
REMARK 465     GLN B   155                                                      
REMARK 465     ASN B   156                                                      
REMARK 465     TYR B   157                                                      
REMARK 465     ASN B   158                                                      
REMARK 465     VAL B   159                                                      
REMARK 465     MET B   160                                                      
REMARK 465     GLY B   161                                                      
REMARK 465     VAL B   162                                                      
REMARK 465     ALA B   163                                                      
REMARK 465     THR B   195                                                      
REMARK 465     LEU B   196                                                      
REMARK 465     SER B   197                                                      
REMARK 465     ALA B   198                                                      
REMARK 465     LYS B   199                                                      
REMARK 465     GLY B   200                                                      
REMARK 465     VAL B   201                                                      
REMARK 465     GLY B   202                                                      
REMARK 465     GLY B   203                                                      
REMARK 465     PHE B   204                                                      
REMARK 465     ASN B   205                                                      
REMARK 465     THR B   206                                                      
REMARK 465     ILE B   207                                                      
REMARK 465     LYS B   256                                                      
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    MET A   1   CG    MET A   1   SD      0.176                       
REMARK 500    VAL A  10   CB    VAL A  10   CG2    -0.135                       
REMARK 500    ILE A  11   CA    ILE A  11   CB     -0.201                       
REMARK 500    ILE A  20   CB    ILE A  20   CG2    -0.203                       
REMARK 500    PHE A  37   CE1   PHE A  37   CZ      0.125                       
REMARK 500    GLU A  72   CG    GLU A  72   CD      0.105                       
REMARK 500    GLU A  78   CG    GLU A  78   CD      0.117                       
REMARK 500    GLU A 138   CG    GLU A 138   CD     -0.110                       
REMARK 500    TYR A 147   CG    TYR A 147   CD1     0.090                       
REMARK 500    TYR A 147   CE1   TYR A 147   CZ      0.091                       
REMARK 500    TYR A 173   CB    TYR A 173   CG     -0.104                       
REMARK 500    SER A 235   CA    SER A 235   CB      0.092                       
REMARK 500    SER B  19   C     SER B  19   O       0.121                       
REMARK 500    LEU B  35   N     LEU B  35   CA     -0.121                       
REMARK 500    TYR B  39   CD1   TYR B  39   CE1     0.111                       
REMARK 500    TYR B  39   CE2   TYR B  39   CD2     0.105                       
REMARK 500    GLU B 131   CG    GLU B 131   CD      0.105                       
REMARK 500    TYR B 147   CG    TYR B 147   CD1     0.088                       
REMARK 500    TYR B 147   CZ    TYR B 147   CE2     0.099                       
REMARK 500    LYS B 164   CE    LYS B 164   NZ      0.168                       
REMARK 500    PRO B 180   N     PRO B 180   CA     -0.119                       
REMARK 500    ASP B 222   CB    ASP B 222   CG     -0.202                       
REMARK 500    ALA B 230   CA    ALA B 230   CB     -0.143                       
REMARK 500    TYR B 232   CZ    TYR B 232   CE2    -0.081                       
REMARK 500    VAL B 241   CA    VAL B 241   CB     -0.145                       
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    MET A   1   CA  -  CB  -  CG  ANGL. DEV. = -14.2 DEGREES          
REMARK 500    MET A   1   CG  -  SD  -  CE  ANGL. DEV. =  13.8 DEGREES          
REMARK 500    LEU A   2   CA  -  CB  -  CG  ANGL. DEV. = -19.7 DEGREES          
REMARK 500    LEU A   2   CB  -  CG  -  CD1 ANGL. DEV. = -14.2 DEGREES          
REMARK 500    LEU A   2   CB  -  CG  -  CD2 ANGL. DEV. =  12.1 DEGREES          
REMARK 500    ASN A   6   CB  -  CA  -  C   ANGL. DEV. = -12.1 DEGREES          
REMARK 500    ILE A  11   CB  -  CA  -  C   ANGL. DEV. = -19.3 DEGREES          
REMARK 500    MET A  12   CA  -  CB  -  CG  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    MET A  12   CB  -  CG  -  SD  ANGL. DEV. = -20.0 DEGREES          
REMARK 500    ARG A  18   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A  18   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    SER A  19   N   -  CA  -  C   ANGL. DEV. = -16.9 DEGREES          
REMARK 500    LEU A  28   CA  -  CB  -  CG  ANGL. DEV. = -22.5 DEGREES          
REMARK 500    THR A  38   CB  -  CA  -  C   ANGL. DEV. = -16.7 DEGREES          
REMARK 500    THR A  38   CA  -  CB  -  OG1 ANGL. DEV. =  13.8 DEGREES          
REMARK 500    TYR A  39   CB  -  CG  -  CD2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A  45   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG A  45   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    GLU A  49   CB  -  CA  -  C   ANGL. DEV. = -26.1 DEGREES          
REMARK 500    LEU A  51   N   -  CA  -  C   ANGL. DEV. = -17.2 DEGREES          
REMARK 500    PRO A  58   C   -  N   -  CA  ANGL. DEV. = -16.7 DEGREES          
REMARK 500    PRO A  58   C   -  N   -  CD  ANGL. DEV. =  16.1 DEGREES          
REMARK 500    LEU A  62   CB  -  CG  -  CD1 ANGL. DEV. =  12.9 DEGREES          
REMARK 500    ASP A  83   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASN A  86   N   -  CA  -  C   ANGL. DEV. =  16.4 DEGREES          
REMARK 500    ASP A  88   CB  -  CG  -  OD1 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    ASP A  88   CB  -  CG  -  OD2 ANGL. DEV. =  10.0 DEGREES          
REMARK 500    MET A 136   CG  -  SD  -  CE  ANGL. DEV. = -13.1 DEGREES          
REMARK 500    VAL A 143   CB  -  CA  -  C   ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ASN A 170   C   -  N   -  CA  ANGL. DEV. = -17.2 DEGREES          
REMARK 500    LEU A 174   CA  -  CB  -  CG  ANGL. DEV. =  19.1 DEGREES          
REMARK 500    ILE A 188   CB  -  CA  -  C   ANGL. DEV. = -12.5 DEGREES          
REMARK 500    ARG A 194   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ASP A 222   CB  -  CG  -  OD1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    LEU A 233   CB  -  CG  -  CD1 ANGL. DEV. =  11.9 DEGREES          
REMARK 500    GLU A 244   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.8 DEGREES          
REMARK 500    MET B   1   CB  -  CA  -  C   ANGL. DEV. =  14.1 DEGREES          
REMARK 500    LEU B   4   CB  -  CA  -  C   ANGL. DEV. = -18.2 DEGREES          
REMARK 500    LEU B   4   N   -  CA  -  C   ANGL. DEV. =  29.8 DEGREES          
REMARK 500    MET B  12   CA  -  CB  -  CG  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    MET B  12   CB  -  CG  -  SD  ANGL. DEV. = -30.3 DEGREES          
REMARK 500    ASP B  29   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ASN B  56   N   -  CA  -  C   ANGL. DEV. = -23.6 DEGREES          
REMARK 500    TYR B  63   N   -  CA  -  C   ANGL. DEV. = -18.6 DEGREES          
REMARK 500    GLN B  64   CB  -  CA  -  C   ANGL. DEV. = -12.8 DEGREES          
REMARK 500    ASP B  66   CB  -  CA  -  C   ANGL. DEV. = -15.4 DEGREES          
REMARK 500    VAL B  67   O   -  C   -  N   ANGL. DEV. =  -9.6 DEGREES          
REMARK 500    ILE B  80   CB  -  CA  -  C   ANGL. DEV. = -19.4 DEGREES          
REMARK 500    SER B 122   N   -  CA  -  C   ANGL. DEV. =  16.5 DEGREES          
REMARK 500    ILE B 142   CG1 -  CB  -  CG2 ANGL. DEV. = -13.9 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      60 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    LEU A   2     -132.04   -155.02                                   
REMARK 500    ASN A   3     -112.07    -80.32                                   
REMARK 500    GLU A   5     -179.68    -58.15                                   
REMARK 500    ASN A   6        1.34    100.02                                   
REMARK 500    ASN A  16     -155.79   -139.82                                   
REMARK 500    LYS A  17        3.82    -56.84                                   
REMARK 500    ARG A  18       15.63   -147.89                                   
REMARK 500    LEU A  31       11.69    -68.64                                   
REMARK 500    TYR A  39      134.93   -176.04                                   
REMARK 500    ARG A  40      -60.14   -106.60                                   
REMARK 500    LEU A  52      106.87     47.07                                   
REMARK 500    GLN A  54     -167.59    -78.61                                   
REMARK 500    GLU A  59      -59.47   -141.10                                   
REMARK 500    HIS A  61       63.85     69.36                                   
REMARK 500    ASP A  83      -71.24    -74.83                                   
REMARK 500    ALA A 165       82.07    -69.45                                   
REMARK 500    ARG A 214       10.89   -153.38                                   
REMARK 500    PRO A 216      -60.37    -22.94                                   
REMARK 500    ASP A 249       12.72   -144.96                                   
REMARK 500    HIS A 253        6.75    -64.01                                   
REMARK 500    ALA A 254       48.42   -141.34                                   
REMARK 500    ASN B   3       54.85     95.84                                   
REMARK 500    LEU B   4      -59.82   -138.32                                   
REMARK 500    ASN B   6      -12.20     84.21                                   
REMARK 500    ASN B  16     -159.49   -148.55                                   
REMARK 500    ARG B  43      -26.53   -144.69                                   
REMARK 500    LYS B  50      -19.63    -46.61                                   
REMARK 500    LEU B  52     -155.05    152.82                                   
REMARK 500    GLU B  53      123.96    -19.65                                   
REMARK 500    GLN B  54       19.33    102.06                                   
REMARK 500    LEU B  55       -5.87     72.59                                   
REMARK 500    PRO B  58     -169.36   -129.96                                   
REMARK 500    SER B  69       83.68   -163.19                                   
REMARK 500    SER B 121       55.81   -159.40                                   
REMARK 500    SER B 124       22.27   -141.03                                   
REMARK 500    VAL B 128      -28.74    -33.05                                   
REMARK 500    LYS B 134       28.19    -78.03                                   
REMARK 500    ALA B 165       14.32   -164.57                                   
REMARK 500    LEU B 167      112.65    177.40                                   
REMARK 500    GLU B 168       45.80    102.31                                   
REMARK 500    ALA B 169       -7.01    174.69                                   
REMARK 500    LEU B 176      -33.99    -35.48                                   
REMARK 500    GLU B 212      -31.40    -34.62                                   
REMARK 500    HIS B 253       -9.40    -54.64                                   
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 LEU A    2     ASN A    3                 -128.28                    
REMARK 500 ASN A    6     LYS A    7                 -145.39                    
REMARK 500 ILE A   11     MET A   12                 -145.37                    
REMARK 500 THR A   38     TYR A   39                 -128.06                    
REMARK 500 GLU A   42     ARG A   43                  149.34                    
REMARK 500 GLU A   49     LYS A   50                  130.84                    
REMARK 500 LYS A   50     LEU A   51                  -56.96                    
REMARK 500 LEU A   51     LEU A   52                 -108.89                    
REMARK 500 GLN A   57     PRO A   58                  146.04                    
REMARK 500 GLU A   59     ALA A   60                   54.77                    
REMARK 500 ALA A   60     HIS A   61                 -122.50                    
REMARK 500 ASN A   86     ILE A   87                 -145.14                    
REMARK 500 ILE A  127     VAL A  128                  135.01                    
REMARK 500 THR A  146     TYR A  147                 -140.43                    
REMARK 500 LYS A  164     ALA A  165                  137.69                    
REMARK 500 ALA A  165     SER A  166                  109.28                    
REMARK 500 SER A  166     LEU A  167                  129.12                    
REMARK 500 VAL A  185     ASN A  186                 -149.06                    
REMARK 500 MET B    1     LEU B    2                 -109.27                    
REMARK 500 LEU B    2     ASN B    3                  146.47                    
REMARK 500 ASN B    3     LEU B    4                 -147.25                    
REMARK 500 VAL B   24     ALA B   25                  146.33                    
REMARK 500 LYS B   34     LEU B   35                 -133.75                    
REMARK 500 THR B   38     TYR B   39                 -144.88                    
REMARK 500 LYS B   41     GLU B   42                 -147.12                    
REMARK 500 GLU B   42     ARG B   43                 -122.13                    
REMARK 500 LEU B   51     LEU B   52                 -140.82                    
REMARK 500 LEU B   52     GLU B   53                 -110.93                    
REMARK 500 GLU B   53     GLN B   54                  -81.99                    
REMARK 500 GLN B   54     LEU B   55                  101.27                    
REMARK 500 VAL B   67     GLN B   68                  131.39                    
REMARK 500 SER B  121     SER B  122                  -88.38                    
REMARK 500 SER B  122     TYR B  123                  139.29                    
REMARK 500 ALA B  165     SER B  166                  140.56                    
REMARK 500 LEU B  167     GLU B  168                   39.26                    
REMARK 500 ALA B  169     ASN B  170                  142.30                    
REMARK 500 LEU B  176     ASP B  177                 -138.89                    
REMARK 500 ILE B  193     ARG B  194                  129.74                    
REMARK 500 LEU B  208     LYS B  209                 -149.50                    
REMARK 500 VAL B  221     ASP B  222                  142.48                    
REMARK 500 ALA B  254     ILE B  255                 -138.85                    
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    GLU A  71        -10.31                                           
REMARK 500    VAL B 224        -13.00                                           
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    MET A   1        19.1      L          L   OUTSIDE RANGE           
REMARK 500    LEU A   2        19.3      L          L   OUTSIDE RANGE           
REMARK 500    SER A  19        46.9      L          L   OUTSIDE RANGE           
REMARK 500    PHE A  37        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE A  65        20.3      L          L   OUTSIDE RANGE           
REMARK 500    SER A  69        24.3      L          L   OUTSIDE RANGE           
REMARK 500    GLU A  72        24.6      L          L   OUTSIDE RANGE           
REMARK 500    ASN A  86        20.5      L          L   OUTSIDE RANGE           
REMARK 500    ILE A  87        24.5      L          L   OUTSIDE RANGE           
REMARK 500    LYS A 218        23.8      L          L   OUTSIDE RANGE           
REMARK 500    ASN A 220        14.1      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 224        21.7      L          L   OUTSIDE RANGE           
REMARK 500    LEU B   4        21.9      L          L   OUTSIDE RANGE           
REMARK 500    LYS B  17        23.9      L          L   OUTSIDE RANGE           
REMARK 500    ASN B  56        48.3      L          L   OUTSIDE RANGE           
REMARK 500    GLN B  57        23.0      L          L   OUTSIDE RANGE           
REMARK 500    ILE B  74        23.6      L          L   OUTSIDE RANGE           
REMARK 500    SER B 122        17.1      L          L   OUTSIDE RANGE           
REMARK 500    LEU B 135        24.9      L          L   OUTSIDE RANGE           
REMARK 500    THR B 146        47.1      L          L   OUTSIDE RANGE           
REMARK 500    SER B 166        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ARG B 184        22.5      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 185        19.2      L          L   OUTSIDE RANGE           
REMARK 500    LEU B 217        20.0      L          L   OUTSIDE RANGE           
REMARK 500    ASN B 220        23.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3GNS   RELATED DB: PDB                                   
REMARK 900 ANOTHER SPACE GROUP                                                  
DBREF  3GNT A    1   256  UNP    Q6GI75   Q6GI75_STAAR     1    256             
DBREF  3GNT B    1   256  UNP    Q6GI75   Q6GI75_STAAR     1    256             
SEQRES   1 A  256  MET LEU ASN LEU GLU ASN LYS THR TYR VAL ILE MET GLY          
SEQRES   2 A  256  ILE ALA ASN LYS ARG SER ILE ALA PHE GLY VAL ALA LYS          
SEQRES   3 A  256  VAL LEU ASP GLN LEU GLY ALA LYS LEU VAL PHE THR TYR          
SEQRES   4 A  256  ARG LYS GLU ARG SER ARG LYS GLU LEU GLU LYS LEU LEU          
SEQRES   5 A  256  GLU GLN LEU ASN GLN PRO GLU ALA HIS LEU TYR GLN ILE          
SEQRES   6 A  256  ASP VAL GLN SER ASP GLU GLU VAL ILE ASN GLY PHE GLU          
SEQRES   7 A  256  GLN ILE GLY LYS ASP VAL GLY ASN ILE ASP GLY VAL TYR          
SEQRES   8 A  256  HIS SER ILE ALA PHE ALA ASN MET GLU ASP LEU ARG GLY          
SEQRES   9 A  256  ARG PHE SER GLU THR SER ARG GLU GLY PHE LEU LEU ALA          
SEQRES  10 A  256  GLN ASP ILE SER SER TYR SER LEU THR ILE VAL ALA HIS          
SEQRES  11 A  256  GLU ALA LYS LYS LEU MET PRO GLU GLY GLY SER ILE VAL          
SEQRES  12 A  256  ALA THR THR TYR LEU GLY GLY GLU PHE ALA VAL GLN ASN          
SEQRES  13 A  256  TYR ASN VAL MET GLY VAL ALA LYS ALA SER LEU GLU ALA          
SEQRES  14 A  256  ASN VAL LYS TYR LEU ALA LEU ASP LEU GLY PRO ASP ASN          
SEQRES  15 A  256  ILE ARG VAL ASN ALA ILE SER ALA GLY PRO ILE ARG THR          
SEQRES  16 A  256  LEU SER ALA LYS GLY VAL GLY GLY PHE ASN THR ILE LEU          
SEQRES  17 A  256  LYS GLU ILE GLU GLU ARG ALA PRO LEU LYS ARG ASN VAL          
SEQRES  18 A  256  ASP GLN VAL GLU VAL GLY LYS THR ALA ALA TYR LEU LEU          
SEQRES  19 A  256  SER ASP LEU SER SER GLY VAL THR GLY GLU ASN ILE HIS          
SEQRES  20 A  256  VAL ASP SER GLY PHE HIS ALA ILE LYS                          
SEQRES   1 B  256  MET LEU ASN LEU GLU ASN LYS THR TYR VAL ILE MET GLY          
SEQRES   2 B  256  ILE ALA ASN LYS ARG SER ILE ALA PHE GLY VAL ALA LYS          
SEQRES   3 B  256  VAL LEU ASP GLN LEU GLY ALA LYS LEU VAL PHE THR TYR          
SEQRES   4 B  256  ARG LYS GLU ARG SER ARG LYS GLU LEU GLU LYS LEU LEU          
SEQRES   5 B  256  GLU GLN LEU ASN GLN PRO GLU ALA HIS LEU TYR GLN ILE          
SEQRES   6 B  256  ASP VAL GLN SER ASP GLU GLU VAL ILE ASN GLY PHE GLU          
SEQRES   7 B  256  GLN ILE GLY LYS ASP VAL GLY ASN ILE ASP GLY VAL TYR          
SEQRES   8 B  256  HIS SER ILE ALA PHE ALA ASN MET GLU ASP LEU ARG GLY          
SEQRES   9 B  256  ARG PHE SER GLU THR SER ARG GLU GLY PHE LEU LEU ALA          
SEQRES  10 B  256  GLN ASP ILE SER SER TYR SER LEU THR ILE VAL ALA HIS          
SEQRES  11 B  256  GLU ALA LYS LYS LEU MET PRO GLU GLY GLY SER ILE VAL          
SEQRES  12 B  256  ALA THR THR TYR LEU GLY GLY GLU PHE ALA VAL GLN ASN          
SEQRES  13 B  256  TYR ASN VAL MET GLY VAL ALA LYS ALA SER LEU GLU ALA          
SEQRES  14 B  256  ASN VAL LYS TYR LEU ALA LEU ASP LEU GLY PRO ASP ASN          
SEQRES  15 B  256  ILE ARG VAL ASN ALA ILE SER ALA GLY PRO ILE ARG THR          
SEQRES  16 B  256  LEU SER ALA LYS GLY VAL GLY GLY PHE ASN THR ILE LEU          
SEQRES  17 B  256  LYS GLU ILE GLU GLU ARG ALA PRO LEU LYS ARG ASN VAL          
SEQRES  18 B  256  ASP GLN VAL GLU VAL GLY LYS THR ALA ALA TYR LEU LEU          
SEQRES  19 B  256  SER ASP LEU SER SER GLY VAL THR GLY GLU ASN ILE HIS          
SEQRES  20 B  256  VAL ASP SER GLY PHE HIS ALA ILE LYS                          
HELIX    1   1 SER A   19  LEU A   31  1                                  13    
HELIX    2   2 GLU A   42  GLU A   49  1                                   8    
HELIX    3   3 SER A   69  VAL A   84  1                                  16    
HELIX    4   4 SER A  122  LYS A  133  1                                  12    
HELIX    5   5 LYS A  134  MET A  136  5                                   3    
HELIX    6   6 SER A  166  LEU A  178  1                                  13    
HELIX    7   7 GLY A  179  ASP A  181  5                                   3    
HELIX    8   8 ASN A  205  ALA A  215  1                                  11    
HELIX    9   9 ASP A  222  SER A  235  1                                  14    
HELIX   10  10 ASP A  236  SER A  239  5                                   4    
HELIX   11  11 SER B   19  LEU B   31  1                                  13    
HELIX   12  12 ARG B   43  LEU B   51  1                                   9    
HELIX   13  13 SER B   69  GLY B   85  1                                  17    
HELIX   14  14 SER B  124  LYS B  133  1                                  10    
HELIX   15  15 ALA B  169  GLY B  179  1                                  11    
HELIX   16  16 GLU B  210  ALA B  215  1                                   6    
HELIX   17  17 ASP B  222  SER B  235  1                                  14    
HELIX   18  18 ASP B  236  SER B  239  5                                   4    
HELIX   19  19 GLY B  251  ILE B  255  5                                   5    
SHEET    1   A 7 LEU A  62  GLN A  64  0                                        
SHEET    2   A 7 LYS A  34  TYR A  39  1  N  PHE A  37   O  TYR A  63           
SHEET    3   A 7 THR A   8  MET A  12  1  N  TYR A   9   O  LYS A  34           
SHEET    4   A 7 GLY A  89  SER A  93  1  O  TYR A  91   N  VAL A  10           
SHEET    5   A 7 GLY A 140  THR A 146  1  O  VAL A 143   N  HIS A  92           
SHEET    6   A 7 ILE A 183  ALA A 190  1  O  ARG A 184   N  GLY A 140           
SHEET    7   A 7 ASN A 245  VAL A 248  1  O  ILE A 246   N  SER A 189           
SHEET    1   B 6 LYS B  34  PHE B  37  0                                        
SHEET    2   B 6 THR B   8  ILE B  11  1  N  TYR B   9   O  VAL B  36           
SHEET    3   B 6 GLY B  89  HIS B  92  1  N  TYR B  91   O  VAL B  10           
SHEET    4   B 6 GLY B 140  THR B 146  1  O  VAL B 143   N  HIS B  92           
SHEET    5   B 6 ILE B 183  ALA B 190  1  O  ARG B 184   N  GLY B 140           
SHEET    6   B 6 ASN B 245  VAL B 248  1  O  ILE B 246   N  ALA B 187           
CISPEP   1 PRO A   58    GLU A   59          0       -24.33                     
CISPEP   2 PRO B   58    GLU B   59          0       -24.26                     
CISPEP   3 GLU B   59    ALA B   60          0        22.68                     
CISPEP   4 ILE B  120    SER B  121          0       -27.92                     
CISPEP   5 LYS B  164    ALA B  165          0       -25.84                     
CRYST1  115.099   74.462   70.609  90.00 119.35  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008688  0.000000  0.004886        0.00000                         
SCALE2      0.000000  0.013430  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016248        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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