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Database: PDB
Entry: 2FSS
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Original site: 2FSS 
HEADER    OXIDOREDUCTASE                          23-JAN-06   2FSS              
TITLE     CANDIDA BOIDINII FORMATE DEHYDROGENASE (FDH) K47E MUTANT              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FORMATE DEHYDROGENASE;                                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 1.2.1.2;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CANDIDA BOIDINII;                               
SOURCE   3 ORGANISM_TAXID: 5477;                                                
SOURCE   4 GENE: CBFDH;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYSS;                         
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTRCHIS2A, PVLKS3                         
KEYWDS    ROSSMANN FOLD, PROTEIN HOMO DIMER, NAD BINDING SITE, FORMATE BINDING  
KEYWDS   2 SITE, OXIDOREDUCTASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.SCHIRWITZ,A.SCHMIDT,V.S.LAMZIN                                      
REVDAT   4   18-OCT-17 2FSS    1       REMARK                                   
REVDAT   3   28-APR-09 2FSS    1       JRNL                                     
REVDAT   2   24-FEB-09 2FSS    1       VERSN                                    
REVDAT   1   13-FEB-07 2FSS    0                                                
JRNL        AUTH   K.SCHIRWITZ,A.SCHMIDT,V.S.LAMZIN                             
JRNL        TITL   HIGH-RESOLUTION STRUCTURES OF FORMATE DEHYDROGENASE FROM     
JRNL        TITL 2 CANDIDA BOIDINII.                                            
JRNL        REF    PROTEIN SCI.                  V.  16  1146 2007              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   17525463                                                     
JRNL        DOI    10.1110/PS.062741707                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.42                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 150929                         
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7992                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10546                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.54                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3150                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 565                          
REMARK   3   BIN FREE R VALUE                    : 0.3720                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10830                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 25                                      
REMARK   3   SOLVENT ATOMS            : 947                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.121         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.122         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.100         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.056         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11144 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15144 ; 1.410 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1402 ; 6.328 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   503 ;37.917 ;24.851       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1895 ;15.236 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    52 ;10.791 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1705 ; 0.098 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8406 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  5633 ; 0.205 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  7743 ; 0.309 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   900 ; 0.136 ; 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):    79 ; 0.195 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    26 ; 0.152 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  7087 ; 0.815 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11150 ; 1.340 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4594 ; 2.148 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3986 ; 3.228 ; 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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2FSS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JAN-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000036267.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUL-04                          
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                       : BW7B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.84140                            
REMARK 200  MONOCHROMATOR                  : TRIANGULAR MONOCHROMATOR           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 158925                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA-CACODYLATE PH 6.5, 30% PEG       
REMARK 280  8000, 0.15M AMMONIUMSULFATE, VAPOR DIFFUSION, SITTING DROP,         
REMARK 280  TEMPERATURE 292K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: 6190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14060 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 52330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -115.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       43.13262            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -67.60931            
REMARK 350   BIOMT3   2  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     0                                                      
REMARK 465     VAL A   354                                                      
REMARK 465     THR A   355                                                      
REMARK 465     LYS A   356                                                      
REMARK 465     ALA A   357                                                      
REMARK 465     TYR A   358                                                      
REMARK 465     GLY A   359                                                      
REMARK 465     LYS A   360                                                      
REMARK 465     HIS A   361                                                      
REMARK 465     ASP A   362                                                      
REMARK 465     LYS A   363                                                      
REMARK 465     LYS A   364                                                      
REMARK 465     MET B     0                                                      
REMARK 465     LYS B    12                                                      
REMARK 465     HIS B    13                                                      
REMARK 465     ALA B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     ASP B    16                                                      
REMARK 465     GLU B    17                                                      
REMARK 465     GLU B    18                                                      
REMARK 465     VAL B   354                                                      
REMARK 465     THR B   355                                                      
REMARK 465     LYS B   356                                                      
REMARK 465     ALA B   357                                                      
REMARK 465     TYR B   358                                                      
REMARK 465     GLY B   359                                                      
REMARK 465     LYS B   360                                                      
REMARK 465     HIS B   361                                                      
REMARK 465     ASP B   362                                                      
REMARK 465     LYS B   363                                                      
REMARK 465     LYS B   364                                                      
REMARK 465     MET C     0                                                      
REMARK 465     VAL C   354                                                      
REMARK 465     THR C   355                                                      
REMARK 465     LYS C   356                                                      
REMARK 465     ALA C   357                                                      
REMARK 465     TYR C   358                                                      
REMARK 465     GLY C   359                                                      
REMARK 465     LYS C   360                                                      
REMARK 465     HIS C   361                                                      
REMARK 465     ASP C   362                                                      
REMARK 465     LYS C   363                                                      
REMARK 465     LYS C   364                                                      
REMARK 465     MET D     0                                                      
REMARK 465     ASP D     9                                                      
REMARK 465     ALA D    10                                                      
REMARK 465     GLY D    11                                                      
REMARK 465     LYS D    12                                                      
REMARK 465     HIS D    13                                                      
REMARK 465     ALA D    14                                                      
REMARK 465     ALA D    15                                                      
REMARK 465     ASP D    16                                                      
REMARK 465     GLU D    17                                                      
REMARK 465     ASP D    46                                                      
REMARK 465     GLU D    47                                                      
REMARK 465     GLU D    48                                                      
REMARK 465     GLY D    49                                                      
REMARK 465     GLY D    50                                                      
REMARK 465     ASN D    51                                                      
REMARK 465     SER D    52                                                      
REMARK 465     VAL D   354                                                      
REMARK 465     THR D   355                                                      
REMARK 465     LYS D   356                                                      
REMARK 465     ALA D   357                                                      
REMARK 465     TYR D   358                                                      
REMARK 465     GLY D   359                                                      
REMARK 465     LYS D   360                                                      
REMARK 465     HIS D   361                                                      
REMARK 465     ASP D   362                                                      
REMARK 465     LYS D   363                                                      
REMARK 465     LYS D   364                                                      
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    HIS A  70       63.67   -176.52                                   
REMARK 500    TRP A 150      103.21   -160.77                                   
REMARK 500    ALA A 257      -86.55    -98.88                                   
REMARK 500    ALA A 304     -150.05   -137.31                                   
REMARK 500    TYR A 312       -6.75   -142.43                                   
REMARK 500    ILE A 347      -62.34    -90.93                                   
REMARK 500    ALA B  10     -126.73   -106.08                                   
REMARK 500    LEU B  28       17.78     51.01                                   
REMARK 500    ASN B  51      -53.18     77.48                                   
REMARK 500    HIS B  70       68.06   -161.82                                   
REMARK 500    VAL B 115       78.16   -100.09                                   
REMARK 500    TRP B 150      104.03   -163.55                                   
REMARK 500    ASP B 195     -167.36   -161.25                                   
REMARK 500    LEU B 199       86.81     39.49                                   
REMARK 500    ALA B 257      -84.91    -91.47                                   
REMARK 500    ALA B 304     -148.64   -134.48                                   
REMARK 500    TYR B 312       -4.07   -140.30                                   
REMARK 500    LEU C  28       16.04     59.85                                   
REMARK 500    ASN C  51        4.38     93.56                                   
REMARK 500    ALA C  72       43.09    113.25                                   
REMARK 500    TRP C 150      102.97   -161.12                                   
REMARK 500    ALA C 257      -85.69    -93.41                                   
REMARK 500    ALA C 304     -148.46   -132.88                                   
REMARK 500    LEU D   7     -154.16   -137.70                                   
REMARK 500    TYR D  21      -35.33   -135.86                                   
REMARK 500    LEU D  28       14.30     51.67                                   
REMARK 500    GLU D 151       84.89   -152.44                                   
REMARK 500    ALA D 257      -84.08    -91.95                                   
REMARK 500    ALA D 304     -148.44   -134.55                                   
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 B   21     GLY B   22                  126.13                    
REMARK 500 GLY B   22     CYS B   23                 -141.71                    
REMARK 500 ALA B  198     LEU B  199                   49.62                    
REMARK 500 LYS D   19     LEU D   20                  145.63                    
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 D 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2005                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2A1Z   RELATED DB: PDB                                   
REMARK 900 CBFDH K328V MUTANT                                                   
DBREF  2FSS A    2   364  GB     7657869  CAA09466         2    364             
DBREF  2FSS B    2   364  GB     7657869  CAA09466         2    364             
DBREF  2FSS C    2   364  GB     7657869  CAA09466         2    364             
DBREF  2FSS D    2   364  GB     7657869  CAA09466         2    364             
SEQADV 2FSS MET A    0  GB   7657869             CLONING ARTIFACT               
SEQADV 2FSS ALA A    1  GB   7657869             CLONING ARTIFACT               
SEQADV 2FSS GLU A   47  GB   7657869   LYS    47 ENGINEERED                     
SEQADV 2FSS MET B    0  GB   7657869             CLONING ARTIFACT               
SEQADV 2FSS ALA B    1  GB   7657869             CLONING ARTIFACT               
SEQADV 2FSS GLU B   47  GB   7657869   LYS    47 ENGINEERED                     
SEQADV 2FSS MET C    0  GB   7657869             CLONING ARTIFACT               
SEQADV 2FSS ALA C    1  GB   7657869             CLONING ARTIFACT               
SEQADV 2FSS GLU C   47  GB   7657869   LYS    47 ENGINEERED                     
SEQADV 2FSS MET D    0  GB   7657869             CLONING ARTIFACT               
SEQADV 2FSS ALA D    1  GB   7657869             CLONING ARTIFACT               
SEQADV 2FSS GLU D   47  GB   7657869   LYS    47 ENGINEERED                     
SEQRES   1 A  365  MET ALA LYS ILE VAL LEU VAL LEU TYR ASP ALA GLY LYS          
SEQRES   2 A  365  HIS ALA ALA ASP GLU GLU LYS LEU TYR GLY CYS THR GLU          
SEQRES   3 A  365  ASN LYS LEU GLY ILE ALA ASN TRP LEU LYS ASP GLN GLY          
SEQRES   4 A  365  HIS GLU LEU ILE THR THR SER ASP GLU GLU GLY GLY ASN          
SEQRES   5 A  365  SER VAL LEU ASP GLN HIS ILE PRO ASP ALA ASP ILE ILE          
SEQRES   6 A  365  ILE THR THR PRO PHE HIS PRO ALA TYR ILE THR LYS GLU          
SEQRES   7 A  365  ARG ILE ASP LYS ALA LYS LYS LEU LYS LEU VAL VAL VAL          
SEQRES   8 A  365  ALA GLY VAL GLY SER ASP HIS ILE ASP LEU ASP TYR ILE          
SEQRES   9 A  365  ASN GLN THR GLY LYS LYS ILE SER VAL LEU GLU VAL THR          
SEQRES  10 A  365  GLY SER ASN VAL VAL SER VAL ALA GLU HIS VAL VAL MET          
SEQRES  11 A  365  THR MET LEU VAL LEU VAL ARG ASN PHE VAL PRO ALA HIS          
SEQRES  12 A  365  GLU GLN ILE ILE ASN HIS ASP TRP GLU VAL ALA ALA ILE          
SEQRES  13 A  365  ALA LYS ASP ALA TYR ASP ILE GLU GLY LYS THR ILE ALA          
SEQRES  14 A  365  THR ILE GLY ALA GLY ARG ILE GLY TYR ARG VAL LEU GLU          
SEQRES  15 A  365  ARG LEU VAL PRO PHE ASN PRO LYS GLU LEU LEU TYR TYR          
SEQRES  16 A  365  ASP TYR GLN ALA LEU PRO LYS ASP ALA GLU GLU LYS VAL          
SEQRES  17 A  365  GLY ALA ARG ARG VAL GLU ASN ILE GLU GLU LEU VAL ALA          
SEQRES  18 A  365  GLN ALA ASP ILE VAL THR VAL ASN ALA PRO LEU HIS ALA          
SEQRES  19 A  365  GLY THR LYS GLY LEU ILE ASN LYS GLU LEU LEU SER LYS          
SEQRES  20 A  365  PHE LYS LYS GLY ALA TRP LEU VAL ASN THR ALA ARG GLY          
SEQRES  21 A  365  ALA ILE CYS VAL ALA GLU ASP VAL ALA ALA ALA LEU GLU          
SEQRES  22 A  365  SER GLY GLN LEU ARG GLY TYR GLY GLY ASP VAL TRP PHE          
SEQRES  23 A  365  PRO GLN PRO ALA PRO LYS ASP HIS PRO TRP ARG ASP MET          
SEQRES  24 A  365  ARG ASN LYS TYR GLY ALA GLY ASN ALA MET THR PRO HIS          
SEQRES  25 A  365  TYR SER GLY THR THR LEU ASP ALA GLN THR ARG TYR ALA          
SEQRES  26 A  365  GLN GLY THR LYS ASN ILE LEU GLU SER PHE PHE THR GLY          
SEQRES  27 A  365  LYS PHE ASP TYR ARG PRO GLN ASP ILE ILE LEU LEU ASN          
SEQRES  28 A  365  GLY GLU TYR VAL THR LYS ALA TYR GLY LYS HIS ASP LYS          
SEQRES  29 A  365  LYS                                                          
SEQRES   1 B  365  MET ALA LYS ILE VAL LEU VAL LEU TYR ASP ALA GLY LYS          
SEQRES   2 B  365  HIS ALA ALA ASP GLU GLU LYS LEU TYR GLY CYS THR GLU          
SEQRES   3 B  365  ASN LYS LEU GLY ILE ALA ASN TRP LEU LYS ASP GLN GLY          
SEQRES   4 B  365  HIS GLU LEU ILE THR THR SER ASP GLU GLU GLY GLY ASN          
SEQRES   5 B  365  SER VAL LEU ASP GLN HIS ILE PRO ASP ALA ASP ILE ILE          
SEQRES   6 B  365  ILE THR THR PRO PHE HIS PRO ALA TYR ILE THR LYS GLU          
SEQRES   7 B  365  ARG ILE ASP LYS ALA LYS LYS LEU LYS LEU VAL VAL VAL          
SEQRES   8 B  365  ALA GLY VAL GLY SER ASP HIS ILE ASP LEU ASP TYR ILE          
SEQRES   9 B  365  ASN GLN THR GLY LYS LYS ILE SER VAL LEU GLU VAL THR          
SEQRES  10 B  365  GLY SER ASN VAL VAL SER VAL ALA GLU HIS VAL VAL MET          
SEQRES  11 B  365  THR MET LEU VAL LEU VAL ARG ASN PHE VAL PRO ALA HIS          
SEQRES  12 B  365  GLU GLN ILE ILE ASN HIS ASP TRP GLU VAL ALA ALA ILE          
SEQRES  13 B  365  ALA LYS ASP ALA TYR ASP ILE GLU GLY LYS THR ILE ALA          
SEQRES  14 B  365  THR ILE GLY ALA GLY ARG ILE GLY TYR ARG VAL LEU GLU          
SEQRES  15 B  365  ARG LEU VAL PRO PHE ASN PRO LYS GLU LEU LEU TYR TYR          
SEQRES  16 B  365  ASP TYR GLN ALA LEU PRO LYS ASP ALA GLU GLU LYS VAL          
SEQRES  17 B  365  GLY ALA ARG ARG VAL GLU ASN ILE GLU GLU LEU VAL ALA          
SEQRES  18 B  365  GLN ALA ASP ILE VAL THR VAL ASN ALA PRO LEU HIS ALA          
SEQRES  19 B  365  GLY THR LYS GLY LEU ILE ASN LYS GLU LEU LEU SER LYS          
SEQRES  20 B  365  PHE LYS LYS GLY ALA TRP LEU VAL ASN THR ALA ARG GLY          
SEQRES  21 B  365  ALA ILE CYS VAL ALA GLU ASP VAL ALA ALA ALA LEU GLU          
SEQRES  22 B  365  SER GLY GLN LEU ARG GLY TYR GLY GLY ASP VAL TRP PHE          
SEQRES  23 B  365  PRO GLN PRO ALA PRO LYS ASP HIS PRO TRP ARG ASP MET          
SEQRES  24 B  365  ARG ASN LYS TYR GLY ALA GLY ASN ALA MET THR PRO HIS          
SEQRES  25 B  365  TYR SER GLY THR THR LEU ASP ALA GLN THR ARG TYR ALA          
SEQRES  26 B  365  GLN GLY THR LYS ASN ILE LEU GLU SER PHE PHE THR GLY          
SEQRES  27 B  365  LYS PHE ASP TYR ARG PRO GLN ASP ILE ILE LEU LEU ASN          
SEQRES  28 B  365  GLY GLU TYR VAL THR LYS ALA TYR GLY LYS HIS ASP LYS          
SEQRES  29 B  365  LYS                                                          
SEQRES   1 C  365  MET ALA LYS ILE VAL LEU VAL LEU TYR ASP ALA GLY LYS          
SEQRES   2 C  365  HIS ALA ALA ASP GLU GLU LYS LEU TYR GLY CYS THR GLU          
SEQRES   3 C  365  ASN LYS LEU GLY ILE ALA ASN TRP LEU LYS ASP GLN GLY          
SEQRES   4 C  365  HIS GLU LEU ILE THR THR SER ASP GLU GLU GLY GLY ASN          
SEQRES   5 C  365  SER VAL LEU ASP GLN HIS ILE PRO ASP ALA ASP ILE ILE          
SEQRES   6 C  365  ILE THR THR PRO PHE HIS PRO ALA TYR ILE THR LYS GLU          
SEQRES   7 C  365  ARG ILE ASP LYS ALA LYS LYS LEU LYS LEU VAL VAL VAL          
SEQRES   8 C  365  ALA GLY VAL GLY SER ASP HIS ILE ASP LEU ASP TYR ILE          
SEQRES   9 C  365  ASN GLN THR GLY LYS LYS ILE SER VAL LEU GLU VAL THR          
SEQRES  10 C  365  GLY SER ASN VAL VAL SER VAL ALA GLU HIS VAL VAL MET          
SEQRES  11 C  365  THR MET LEU VAL LEU VAL ARG ASN PHE VAL PRO ALA HIS          
SEQRES  12 C  365  GLU GLN ILE ILE ASN HIS ASP TRP GLU VAL ALA ALA ILE          
SEQRES  13 C  365  ALA LYS ASP ALA TYR ASP ILE GLU GLY LYS THR ILE ALA          
SEQRES  14 C  365  THR ILE GLY ALA GLY ARG ILE GLY TYR ARG VAL LEU GLU          
SEQRES  15 C  365  ARG LEU VAL PRO PHE ASN PRO LYS GLU LEU LEU TYR TYR          
SEQRES  16 C  365  ASP TYR GLN ALA LEU PRO LYS ASP ALA GLU GLU LYS VAL          
SEQRES  17 C  365  GLY ALA ARG ARG VAL GLU ASN ILE GLU GLU LEU VAL ALA          
SEQRES  18 C  365  GLN ALA ASP ILE VAL THR VAL ASN ALA PRO LEU HIS ALA          
SEQRES  19 C  365  GLY THR LYS GLY LEU ILE ASN LYS GLU LEU LEU SER LYS          
SEQRES  20 C  365  PHE LYS LYS GLY ALA TRP LEU VAL ASN THR ALA ARG GLY          
SEQRES  21 C  365  ALA ILE CYS VAL ALA GLU ASP VAL ALA ALA ALA LEU GLU          
SEQRES  22 C  365  SER GLY GLN LEU ARG GLY TYR GLY GLY ASP VAL TRP PHE          
SEQRES  23 C  365  PRO GLN PRO ALA PRO LYS ASP HIS PRO TRP ARG ASP MET          
SEQRES  24 C  365  ARG ASN LYS TYR GLY ALA GLY ASN ALA MET THR PRO HIS          
SEQRES  25 C  365  TYR SER GLY THR THR LEU ASP ALA GLN THR ARG TYR ALA          
SEQRES  26 C  365  GLN GLY THR LYS ASN ILE LEU GLU SER PHE PHE THR GLY          
SEQRES  27 C  365  LYS PHE ASP TYR ARG PRO GLN ASP ILE ILE LEU LEU ASN          
SEQRES  28 C  365  GLY GLU TYR VAL THR LYS ALA TYR GLY LYS HIS ASP LYS          
SEQRES  29 C  365  LYS                                                          
SEQRES   1 D  365  MET ALA LYS ILE VAL LEU VAL LEU TYR ASP ALA GLY LYS          
SEQRES   2 D  365  HIS ALA ALA ASP GLU GLU LYS LEU TYR GLY CYS THR GLU          
SEQRES   3 D  365  ASN LYS LEU GLY ILE ALA ASN TRP LEU LYS ASP GLN GLY          
SEQRES   4 D  365  HIS GLU LEU ILE THR THR SER ASP GLU GLU GLY GLY ASN          
SEQRES   5 D  365  SER VAL LEU ASP GLN HIS ILE PRO ASP ALA ASP ILE ILE          
SEQRES   6 D  365  ILE THR THR PRO PHE HIS PRO ALA TYR ILE THR LYS GLU          
SEQRES   7 D  365  ARG ILE ASP LYS ALA LYS LYS LEU LYS LEU VAL VAL VAL          
SEQRES   8 D  365  ALA GLY VAL GLY SER ASP HIS ILE ASP LEU ASP TYR ILE          
SEQRES   9 D  365  ASN GLN THR GLY LYS LYS ILE SER VAL LEU GLU VAL THR          
SEQRES  10 D  365  GLY SER ASN VAL VAL SER VAL ALA GLU HIS VAL VAL MET          
SEQRES  11 D  365  THR MET LEU VAL LEU VAL ARG ASN PHE VAL PRO ALA HIS          
SEQRES  12 D  365  GLU GLN ILE ILE ASN HIS ASP TRP GLU VAL ALA ALA ILE          
SEQRES  13 D  365  ALA LYS ASP ALA TYR ASP ILE GLU GLY LYS THR ILE ALA          
SEQRES  14 D  365  THR ILE GLY ALA GLY ARG ILE GLY TYR ARG VAL LEU GLU          
SEQRES  15 D  365  ARG LEU VAL PRO PHE ASN PRO LYS GLU LEU LEU TYR TYR          
SEQRES  16 D  365  ASP TYR GLN ALA LEU PRO LYS ASP ALA GLU GLU LYS VAL          
SEQRES  17 D  365  GLY ALA ARG ARG VAL GLU ASN ILE GLU GLU LEU VAL ALA          
SEQRES  18 D  365  GLN ALA ASP ILE VAL THR VAL ASN ALA PRO LEU HIS ALA          
SEQRES  19 D  365  GLY THR LYS GLY LEU ILE ASN LYS GLU LEU LEU SER LYS          
SEQRES  20 D  365  PHE LYS LYS GLY ALA TRP LEU VAL ASN THR ALA ARG GLY          
SEQRES  21 D  365  ALA ILE CYS VAL ALA GLU ASP VAL ALA ALA ALA LEU GLU          
SEQRES  22 D  365  SER GLY GLN LEU ARG GLY TYR GLY GLY ASP VAL TRP PHE          
SEQRES  23 D  365  PRO GLN PRO ALA PRO LYS ASP HIS PRO TRP ARG ASP MET          
SEQRES  24 D  365  ARG ASN LYS TYR GLY ALA GLY ASN ALA MET THR PRO HIS          
SEQRES  25 D  365  TYR SER GLY THR THR LEU ASP ALA GLN THR ARG TYR ALA          
SEQRES  26 D  365  GLN GLY THR LYS ASN ILE LEU GLU SER PHE PHE THR GLY          
SEQRES  27 D  365  LYS PHE ASP TYR ARG PRO GLN ASP ILE ILE LEU LEU ASN          
SEQRES  28 D  365  GLY GLU TYR VAL THR LYS ALA TYR GLY LYS HIS ASP LYS          
SEQRES  29 D  365  LYS                                                          
HET    SO4  A2003       5                                                       
HET    SO4  A2005       5                                                       
HET    SO4  C2002       5                                                       
HET    SO4  C2004       5                                                       
HET    SO4  D2001       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  SO4    5(O4 S 2-)                                                   
FORMUL  10  HOH   *947(H2 O)                                                    
HELIX    1   1 GLY A   11  GLU A   17  1                                   7    
HELIX    2   2 ASN A   26  GLY A   29  5                                   4    
HELIX    3   3 ILE A   30  GLN A   37  1                                   8    
HELIX    4   4 SER A   52  ILE A   58  1                                   7    
HELIX    5   5 PRO A   59  ALA A   61  5                                   3    
HELIX    6   6 THR A   75  ALA A   82  1                                   8    
HELIX    7   7 ASP A   99  GLY A  107  1                                   9    
HELIX    8   8 ASN A  119  ARG A  136  1                                  18    
HELIX    9   9 ASN A  137  ASN A  147  1                                  11    
HELIX   10  10 GLU A  151  LYS A  157  1                                   7    
HELIX   11  11 GLY A  173  VAL A  184  1                                  12    
HELIX   12  12 PRO A  185  ASN A  187  5                                   3    
HELIX   13  13 PRO A  200  VAL A  207  1                                   8    
HELIX   14  14 ASN A  214  ALA A  220  1                                   7    
HELIX   15  15 ASN A  240  LYS A  246  1                                   7    
HELIX   16  16 ARG A  258  CYS A  262  5                                   5    
HELIX   17  17 VAL A  263  SER A  273  1                                  11    
HELIX   18  18 HIS A  293  MET A  298  1                                   6    
HELIX   19  19 TYR A  312  THR A  315  5                                   4    
HELIX   20  20 THR A  316  THR A  336  1                                  21    
HELIX   21  21 ARG A  342  GLN A  344  5                                   3    
HELIX   22  22 ASN B   26  GLY B   29  5                                   4    
HELIX   23  23 ILE B   30  ASP B   36  1                                   7    
HELIX   24  24 SER B   52  ILE B   58  1                                   7    
HELIX   25  25 PRO B   59  ALA B   61  5                                   3    
HELIX   26  26 THR B   75  ALA B   82  1                                   8    
HELIX   27  27 ASP B   99  GLY B  107  1                                   9    
HELIX   28  28 ASN B  119  ARG B  136  1                                  18    
HELIX   29  29 ASN B  137  ASN B  147  1                                  11    
HELIX   30  30 GLU B  151  LYS B  157  1                                   7    
HELIX   31  31 GLY B  173  VAL B  184  1                                  12    
HELIX   32  32 PRO B  185  ASN B  187  5                                   3    
HELIX   33  33 PRO B  200  GLY B  208  1                                   9    
HELIX   34  34 ASN B  214  GLN B  221  1                                   8    
HELIX   35  35 HIS B  232  LYS B  236  5                                   5    
HELIX   36  36 ASN B  240  PHE B  247  1                                   8    
HELIX   37  37 ARG B  258  CYS B  262  5                                   5    
HELIX   38  38 VAL B  263  GLY B  274  1                                  12    
HELIX   39  39 HIS B  293  MET B  298  1                                   6    
HELIX   40  40 TYR B  312  THR B  315  5                                   4    
HELIX   41  41 THR B  316  THR B  336  1                                  21    
HELIX   42  42 ARG B  342  GLN B  344  5                                   3    
HELIX   43  43 GLY C   11  GLU C   17  1                                   7    
HELIX   44  44 ASN C   26  GLY C   29  5                                   4    
HELIX   45  45 ILE C   30  ASP C   36  1                                   7    
HELIX   46  46 SER C   52  ILE C   58  1                                   7    
HELIX   47  47 PRO C   59  ALA C   61  5                                   3    
HELIX   48  48 THR C   75  ALA C   82  1                                   8    
HELIX   49  49 ASP C   99  GLY C  107  1                                   9    
HELIX   50  50 ASN C  119  ARG C  136  1                                  18    
HELIX   51  51 ASN C  137  ASN C  147  1                                  11    
HELIX   52  52 GLU C  151  LYS C  157  1                                   7    
HELIX   53  53 GLY C  173  VAL C  184  1                                  12    
HELIX   54  54 PRO C  185  ASN C  187  5                                   3    
HELIX   55  55 PRO C  200  VAL C  207  1                                   8    
HELIX   56  56 ASN C  214  ALA C  222  1                                   9    
HELIX   57  57 ASN C  240  SER C  245  1                                   6    
HELIX   58  58 ARG C  258  CYS C  262  5                                   5    
HELIX   59  59 VAL C  263  SER C  273  1                                  11    
HELIX   60  60 HIS C  293  MET C  298  1                                   6    
HELIX   61  61 TYR C  312  THR C  315  5                                   4    
HELIX   62  62 THR C  316  THR C  336  1                                  21    
HELIX   63  63 ARG C  342  GLN C  344  5                                   3    
HELIX   64  64 ASN D   26  GLY D   29  5                                   4    
HELIX   65  65 ILE D   30  ASP D   36  1                                   7    
HELIX   66  66 VAL D   53  ILE D   58  1                                   6    
HELIX   67  67 PRO D   59  ALA D   61  5                                   3    
HELIX   68  68 THR D   75  ALA D   82  1                                   8    
HELIX   69  69 ASP D   99  GLY D  107  1                                   9    
HELIX   70  70 ASN D  119  ARG D  136  1                                  18    
HELIX   71  71 ASN D  137  ASN D  147  1                                  11    
HELIX   72  72 GLU D  151  LYS D  157  1                                   7    
HELIX   73  73 GLY D  173  VAL D  184  1                                  12    
HELIX   74  74 PRO D  185  ASN D  187  5                                   3    
HELIX   75  75 PRO D  200  GLY D  208  1                                   9    
HELIX   76  76 ASN D  214  GLN D  221  1                                   8    
HELIX   77  77 ASN D  240  SER D  245  1                                   6    
HELIX   78  78 ARG D  258  CYS D  262  5                                   5    
HELIX   79  79 VAL D  263  SER D  273  1                                  11    
HELIX   80  80 HIS D  293  MET D  298  1                                   6    
HELIX   81  81 TYR D  312  THR D  315  5                                   4    
HELIX   82  82 THR D  316  THR D  336  1                                  21    
HELIX   83  83 ARG D  342  GLN D  344  5                                   3    
SHEET    1   A 7 GLU A  40  THR A  44  0                                        
SHEET    2   A 7 LYS A   2  VAL A   6  1  N  LEU A   5   O  ILE A  42           
SHEET    3   A 7 ILE A  63  THR A  66  1  O  ILE A  65   N  VAL A   4           
SHEET    4   A 7 LEU A  87  VAL A  90  1  O  VAL A  89   N  THR A  66           
SHEET    5   A 7 SER A 111  GLU A 114  1  O  LEU A 113   N  VAL A  90           
SHEET    6   A 7 ILE A 346  LEU A 349 -1  O  LEU A 348   N  VAL A 112           
SHEET    7   A 7 GLU A 352  TYR A 353 -1  O  GLU A 352   N  LEU A 349           
SHEET    1   B 7 ALA A 209  ARG A 211  0                                        
SHEET    2   B 7 GLU A 190  TYR A 194  1  N  TYR A 193   O  ARG A 210           
SHEET    3   B 7 THR A 166  ILE A 170  1  N  ILE A 167   O  GLU A 190           
SHEET    4   B 7 ILE A 224  VAL A 227  1  O  ILE A 224   N  ALA A 168           
SHEET    5   B 7 ALA A 251  ASN A 255  1  O  VAL A 254   N  VAL A 225           
SHEET    6   B 7 LEU A 276  GLY A 281  1  O  GLY A 280   N  ASN A 255           
SHEET    7   B 7 ASN A 306  MET A 308  1  O  ALA A 307   N  TYR A 279           
SHEET    1   C 7 GLU B  40  THR B  44  0                                        
SHEET    2   C 7 LYS B   2  VAL B   6  1  N  ILE B   3   O  GLU B  40           
SHEET    3   C 7 ILE B  63  THR B  66  1  O  ILE B  65   N  VAL B   4           
SHEET    4   C 7 LEU B  87  VAL B  90  1  O  VAL B  89   N  THR B  66           
SHEET    5   C 7 SER B 111  GLU B 114  1  O  LEU B 113   N  VAL B  90           
SHEET    6   C 7 ILE B 346  LEU B 349 -1  O  ILE B 347   N  VAL B 112           
SHEET    7   C 7 GLU B 352  TYR B 353 -1  O  GLU B 352   N  LEU B 349           
SHEET    1   D 7 ALA B 209  ARG B 211  0                                        
SHEET    2   D 7 GLU B 190  TYR B 194  1  N  TYR B 193   O  ARG B 210           
SHEET    3   D 7 THR B 166  ILE B 170  1  N  ILE B 167   O  LEU B 192           
SHEET    4   D 7 ILE B 224  VAL B 227  1  O  THR B 226   N  ILE B 170           
SHEET    5   D 7 ALA B 251  ASN B 255  1  O  VAL B 254   N  VAL B 225           
SHEET    6   D 7 LEU B 276  GLY B 281  1  O  ARG B 277   N  ALA B 251           
SHEET    7   D 7 ASN B 306  MET B 308  1  O  ALA B 307   N  TYR B 279           
SHEET    1   E 6 GLU C  40  THR C  44  0                                        
SHEET    2   E 6 LYS C   2  VAL C   6  1  N  LEU C   5   O  ILE C  42           
SHEET    3   E 6 ILE C  63  THR C  66  1  O  ILE C  65   N  VAL C   4           
SHEET    4   E 6 LEU C  87  VAL C  90  1  O  VAL C  89   N  THR C  66           
SHEET    5   E 6 SER C 111  GLU C 114  1  O  LEU C 113   N  VAL C  88           
SHEET    6   E 6 ILE C 346  LEU C 348 -1  O  LEU C 348   N  VAL C 112           
SHEET    1   F 7 ALA C 209  ARG C 211  0                                        
SHEET    2   F 7 GLU C 190  TYR C 194  1  N  LEU C 191   O  ARG C 210           
SHEET    3   F 7 THR C 166  ILE C 170  1  N  ILE C 167   O  LEU C 192           
SHEET    4   F 7 ILE C 224  VAL C 227  1  O  ILE C 224   N  ALA C 168           
SHEET    5   F 7 ALA C 251  ASN C 255  1  O  TRP C 252   N  VAL C 225           
SHEET    6   F 7 LEU C 276  GLY C 281  1  O  ARG C 277   N  ALA C 251           
SHEET    7   F 7 ASN C 306  MET C 308  1  O  ALA C 307   N  TYR C 279           
SHEET    1   G 6 GLU D  40  THR D  44  0                                        
SHEET    2   G 6 LYS D   2  VAL D   6  1  N  LEU D   5   O  ILE D  42           
SHEET    3   G 6 ILE D  63  THR D  66  1  O  ILE D  65   N  VAL D   4           
SHEET    4   G 6 LEU D  87  VAL D  90  1  O  VAL D  89   N  ILE D  64           
SHEET    5   G 6 SER D 111  GLU D 114  1  O  LEU D 113   N  VAL D  90           
SHEET    6   G 6 ILE D 346  LEU D 348 -1  O  ILE D 347   N  VAL D 112           
SHEET    1   H 7 ALA D 209  ARG D 211  0                                        
SHEET    2   H 7 GLU D 190  TYR D 194  1  N  LEU D 191   O  ARG D 210           
SHEET    3   H 7 THR D 166  ILE D 170  1  N  ILE D 167   O  GLU D 190           
SHEET    4   H 7 ILE D 224  VAL D 227  1  O  THR D 226   N  ILE D 170           
SHEET    5   H 7 ALA D 251  ASN D 255  1  O  TRP D 252   N  VAL D 225           
SHEET    6   H 7 LEU D 276  GLY D 281  1  O  ARG D 277   N  ALA D 251           
SHEET    7   H 7 ASN D 306  MET D 308  1  O  ALA D 307   N  TYR D 279           
CISPEP   1 GLU A   48    GLY A   49          0        -7.58                     
CISPEP   2 PHE A  285    PRO A  286          0        17.55                     
CISPEP   3 GLN A  287    PRO A  288          0        17.74                     
CISPEP   4 GLU B   48    GLY B   49          0        10.15                     
CISPEP   5 GLY B   49    GLY B   50          0        -1.68                     
CISPEP   6 GLY B   50    ASN B   51          0         9.31                     
CISPEP   7 PHE B  285    PRO B  286          0        -7.67                     
CISPEP   8 GLN B  287    PRO B  288          0         2.23                     
CISPEP   9 GLU C   48    GLY C   49          0        -2.98                     
CISPEP  10 PRO C   71    ALA C   72          0       -10.61                     
CISPEP  11 PHE C  285    PRO C  286          0        -6.79                     
CISPEP  12 GLN C  287    PRO C  288          0        -3.55                     
CISPEP  13 PHE D  285    PRO D  286          0        -4.78                     
CISPEP  14 GLN D  287    PRO D  288          0        -4.29                     
SITE     1 AC1  3 GLY D 173  ARG D 174  HOH D2018                               
SITE     1 AC2  6 LYS A 109  GLN C 197  ALA C 198  ARG C 211                    
SITE     2 AC2  6 HOH C2034  HOH C2192                                          
SITE     1 AC3  4 ALA A 198  ARG A 211  HOH A2021  LYS C 109                    
SITE     1 AC4  3 GLY C 173  ARG C 174  HOH C2047                               
SITE     1 AC5  4 GLY A 173  ARG A 174  HOH A2056  HOH A2199                    
CRYST1   53.430   68.389  109.369  77.93  89.33  81.34 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018716 -0.002851  0.000388        0.00000                         
SCALE2      0.000000  0.014791 -0.003173        0.00000                         
SCALE3      0.000000  0.000000  0.009352        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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