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Database: PDB
Entry: 1SC6
LinkDB: 1SC6
Original site: 1SC6 
HEADER    OXIDOREDUCTASE                          11-FEB-04   1SC6              
TITLE     CRYSTAL STRUCTURE OF W139G D-3-PHOSPHOGLYCERATE                       
TITLE    2 DEHYDROGENASE COMPLEXED WITH NAD+                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-3-PHOSPHOGLYCERATE DEHYDROGENASE;                        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: PGDH;                                                       
COMPND   5 EC: 1.1.1.95;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: SERA, B2913, C3494, Z4251, ECS3784, SF2898, S3098;             
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PTRC99A                                   
KEYWDS    ALLOSTERIC REGULATION PHOSPHOGLYCERATE DEHYDROGENASE PGDH,            
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.K.BELL,G.A.GRANT,L.J.BANASZAK                                       
REVDAT   2   24-FEB-09 1SC6    1       VERSN                                    
REVDAT   1   22-FEB-05 1SC6    0                                                
JRNL        AUTH   J.K.BELL,G.A.GRANT,L.J.BANASZAK                              
JRNL        TITL   MULTICONFORMATIONAL STATES IN PHOSPHOGLYCERATE               
JRNL        TITL 2 DEHYDROGENASE                                                
JRNL        REF    BIOCHEMISTRY                  V.  43  3450 2004              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   15035616                                                     
JRNL        DOI    10.1021/BI035462E                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   D.J.SCHULLER,G.A.GRANT,L.J.BANASZAK                          
REMARK   1  TITL   THE ALLOSTERIC LIGAND SITE IN THE VMAX-TYPE                  
REMARK   1  TITL 2 COOPERATIVE ENZYME PHOSPHOGLYCERATE DEHYDROGENASE            
REMARK   1  REF    NAT.STRUCT.MOL.BIOL.          V.   2    69 1995              
REMARK   1  REFN                   ISSN 1545-9993                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.09 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 104630                         
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 SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 17250                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11663                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 176                                     
REMARK   3   SOLVENT ATOMS            : 463                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.61500                                             
REMARK   3    B22 (A**2) : -1.06900                                             
REMARK   3    B33 (A**2) : 2.68400                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -5.05200                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ANISOTROPIC                               
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.589 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.609 ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.312 ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.314 ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1SC6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB021593.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-MAR-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934, 0.97951, 0.95373          
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK DOUBLE-CRYSTAL      
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ANL-ECT                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 104640                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.090                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : 0.06300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.43600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE, DM, CNS                                        
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CITRATE, PEG 4K, NAD, ALPHA-             
REMARK 280  KETOGLUTARATE, PH 5.2, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       35.42100            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 18410 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 58300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A   141                                                      
REMARK 465     LEU A   142                                                      
REMARK 465     ALA A   143                                                      
REMARK 465     ALA A   144                                                      
REMARK 465     GLY A   145                                                      
REMARK 465     PHE A   266                                                      
REMARK 465     PRO A   267                                                      
REMARK 465     THR A   268                                                      
REMARK 465     GLU A   269                                                      
REMARK 465     PRO A   270                                                      
REMARK 465     ALA A   271                                                      
REMARK 465     THR A   272                                                      
REMARK 465     ASN A   273                                                      
REMARK 465     SER A   274                                                      
REMARK 465     LYS B   141                                                      
REMARK 465     LEU B   142                                                      
REMARK 465     ALA B   143                                                      
REMARK 465     ALA B   144                                                      
REMARK 465     GLY B   145                                                      
REMARK 465     VAL B   265                                                      
REMARK 465     PHE B   266                                                      
REMARK 465     PRO B   267                                                      
REMARK 465     THR B   268                                                      
REMARK 465     GLU B   269                                                      
REMARK 465     PRO B   270                                                      
REMARK 465     ALA B   271                                                      
REMARK 465     THR B   272                                                      
REMARK 465     ASN B   273                                                      
REMARK 465     SER B   274                                                      
REMARK 465     ASP B   275                                                      
REMARK 465     PRO B   276                                                      
REMARK 465     PHE B   277                                                      
REMARK 465     THR B   278                                                      
REMARK 465     GLU C     7                                                      
REMARK 465     LYS C     8                                                      
REMARK 465     LYS C   141                                                      
REMARK 465     LEU C   142                                                      
REMARK 465     ALA C   143                                                      
REMARK 465     ALA C   144                                                      
REMARK 465     PHE C   266                                                      
REMARK 465     PRO C   267                                                      
REMARK 465     THR C   268                                                      
REMARK 465     GLU C   269                                                      
REMARK 465     PRO C   270                                                      
REMARK 465     ALA C   271                                                      
REMARK 465     THR C   272                                                      
REMARK 465     ASN C   273                                                      
REMARK 465     SER C   274                                                      
REMARK 465     ASP C   275                                                      
REMARK 465     PRO C   276                                                      
REMARK 465     PHE C   277                                                      
REMARK 465     THR C   278                                                      
REMARK 465     HIS C   292                                                      
REMARK 465     ILE C   293                                                      
REMARK 465     GLY C   294                                                      
REMARK 465     GLY C   295                                                      
REMARK 465     SER C   296                                                      
REMARK 465     THR C   297                                                      
REMARK 465     GLN C   298                                                      
REMARK 465     ASN D   140                                                      
REMARK 465     LYS D   141                                                      
REMARK 465     LEU D   142                                                      
REMARK 465     ALA D   143                                                      
REMARK 465     ALA D   144                                                      
REMARK 465     GLY D   145                                                      
REMARK 465     PHE D   266                                                      
REMARK 465     PRO D   267                                                      
REMARK 465     THR D   268                                                      
REMARK 465     GLU D   269                                                      
REMARK 465     PRO D   270                                                      
REMARK 465     ALA D   271                                                      
REMARK 465     THR D   272                                                      
REMARK 465     ASN D   273                                                      
REMARK 465     SER D   274                                                      
REMARK 465     ASP D   275                                                      
REMARK 465     HIS D   292                                                      
REMARK 465     ILE D   293                                                      
REMARK 465     GLY D   294                                                      
REMARK 465     GLY D   295                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     ILE B  293                                                       
REMARK 475     GLY B  294                                                       
REMARK 475     LYS C   10                                                       
REMARK 475     GLY C   31                                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A   10   C     O     CB    CG    CD    CE    NZ              
REMARK 480     LYS A   39   CG    CD                                            
REMARK 480     GLU A   45   CB    CG    CD    OE1   OE2                         
REMARK 480     ARG A   62   CB    CG    CD    NE    CZ    NH1   NH2             
REMARK 480     ASP A   68   CB    CG    OD1   OD2                               
REMARK 480     ASN A   71   CB    CG                                            
REMARK 480     GLU A   74   CB    CG                                            
REMARK 480     ILE A   84   CB    CG1   CG2   CD1                               
REMARK 480     ASN A   87   CB    CG    ND2                                     
REMARK 480     LYS A   96   CD    CE    NZ                                      
REMARK 480     GLY A  137   O                                                   
REMARK 480     VAL A  138   CB    CG1   CG2                                     
REMARK 480     PHE A  147   CG    CD1   CD2   CE1   CE2   CZ                    
REMARK 480     GLU A  183   CD    OE1   OE2                                     
REMARK 480     LYS A  218   CB    CG    CD    CE    NZ                          
REMARK 480     LYS A  224   CE    NZ                                            
REMARK 480     THR A  242   OG1   CG2                                           
REMARK 480     LYS A  256   CE    NZ                                            
REMARK 480     VAL A  265   CG1   CG2                                           
REMARK 480     HIS A  292   CG    ND1   CD2   CE1   NE2                         
REMARK 480     ILE A  293   CB    CG2                                           
REMARK 480     GLY A  294   CA    C     O                                       
REMARK 480     GLY A  295   C     O                                             
REMARK 480     SER A  296   N     CA    C     CB                                
REMARK 480     THR A  297   N     CA    CB    OG1   CG2                         
REMARK 480     GLN A  298   CG    CD    OE1   NE2                               
REMARK 480     LYS A  356   CD    NZ                                            
REMARK 480     GLN A  361   CB    CG    CD    OE1   NE2                         
REMARK 480     GLN A  375   CB    CG    CD    OE1   NE2                         
REMARK 480     GLU A  384   OE1                                                 
REMARK 480     ASP A  386   CB    OD1                                           
REMARK 480     GLU A  387   OE1                                                 
REMARK 480     ASP A  388   CB    CG    OD1   OD2                               
REMARK 480     LYS A  392   CG    CD    CE    NZ                                
REMARK 480     LYS B    8   CE    NZ                                            
REMARK 480     LYS B   10   CB    CG    CD    CE    NZ                          
REMARK 480     LYS B   22   CE    NZ                                            
REMARK 480     GLU B   45   CB    CG                                            
REMARK 480     LYS B   48   CG    CE    NZ                                      
REMARK 480     GLU B   49   CG    CD    OE1   OE2                               
REMARK 480     ASP B   92   OD1   OD2                                           
REMARK 480     ASN B  140   CB    CG    OD1   ND2                               
REMARK 480     LEU B  186   CD2                                                 
REMARK 480     LYS B  218   CG    CD    CE    NZ                                
REMARK 480     LYS B  224   CE    NZ                                            
REMARK 480     ARG B  240   CA    CB    CG    CD    NE    CZ    NH1             
REMARK 480     ARG B  240   NH2                                                 
REMARK 480     HIS B  292   CA    C     O     CB    CG    ND1   CD2             
REMARK 480     HIS B  292   CE1   NE2                                           
REMARK 480     GLY B  295   N     CA                                            
REMARK 480     LEU B  334   CD1   CD2                                           
REMARK 480     LYS B  356   CD    CE    NZ                                      
REMARK 480     GLU B  384   CG    CD    OE1   OE2                               
REMARK 480     ASP B  388   CB    CG    OD1   OD2                               
REMARK 480     LYS B  392   CE    NZ                                            
REMARK 480     ARG B  407   CD    NE    CZ                                      
REMARK 480     GLN C   21   CB    CG    CD    OE1                               
REMARK 480     LYS C   22   CB    CG    NZ                                      
REMARK 480     ARG C   28   CB    CG    CD    NE    NH1   NH2                   
REMARK 480     ASN C   34   CA                                                  
REMARK 480     ASP C   44   OD1   OD2                                           
REMARK 480     GLU C   45   N     CB    CG    CD    OE1   OE2                   
REMARK 480     LYS C   48   CD    CE    NZ                                      
REMARK 480     GLU C   49   CB    CG    CD    OE1   OE2                         
REMARK 480     ARG C   52   CB    CG    CD    NE    CZ    NH1   NH2             
REMARK 480     LEU C   59   CD1   CD2                                           
REMARK 480     HIS C   64   ND1   CD2   CE1                                     
REMARK 480     GLU C   67   OE1   OE2                                           
REMARK 480     ASP C   68   CB    CG    OD2                                     
REMARK 480     ASN C   71   CB    CG    OD1   ND2                               
REMARK 480     LYS C   75   CG    CD    CE    NZ                                
REMARK 480     GLY C   85   N     CA    C                                       
REMARK 480     ASN C   87   CB    CG    OD1   ND2                               
REMARK 480     GLN C   88   CB    CG    CD    OE1   NE2                         
REMARK 480     LYS C   96   CE    NZ                                            
REMARK 480     ASN C  140   C     O     CG    OD1   ND2                         
REMARK 480     GLY C  145   N     CA                                            
REMARK 480     GLU C  213   CB    CG    CD    OE1   OE2                         
REMARK 480     LYS C  218   CB    CG    CD    CE    NZ                          
REMARK 480     LYS C  224   CG    CD    CE    NZ                                
REMARK 480     ARG C  240   CB    CG    CD    NE    CZ    NH1   NH2             
REMARK 480     VAL C  265   C     O     CB    CG1   CG2                         
REMARK 480     SER C  279   N                                                   
REMARK 480     PRO C  291   CA    C     O     CB    CG    CD                    
REMARK 480     GLU C  299   N     CB    CG    CD    OE1   OE2                   
REMARK 480     LEU C  306   CG    CD1   CD2                                     
REMARK 480     LYS C  314   CG    CD    CE    NZ                                
REMARK 480     GLN C  375   CB    CG    CD    OE1   NE2                         
REMARK 480     GLU C  384   CB    CG    CD    OE1   OE2                         
REMARK 480     ASP C  386   OD1   OD2                                           
REMARK 480     GLU C  387   CG    CD    OE1   OE2                               
REMARK 480     ASP C  388   CB    CG    OD1   OD2                               
REMARK 480     VAL C  389   CB    CG1   CG2                                     
REMARK 480     LYS C  392   CB    CD    CE    NZ                                
REMARK 480     GLU D    7   N     O     CG    CD    OE1   OE2                   
REMARK 480     LYS D   39   CG    CD    CE    NZ                                
REMARK 480     ASP D   43   CB    CG    OD1   OD2                               
REMARK 480     GLU D   45   CB    CG    CD                                      
REMARK 480     ARG D   62   NE    CZ    NH1   NH2                               
REMARK 480     LYS D   75   CE    NZ                                            
REMARK 480     LYS D   96   CE    NZ                                            
REMARK 480     GLY D  139   O                                                   
REMARK 480     LYS D  218   CB    CG    CD    CE    NZ                          
REMARK 480     ARG D  240   CG    CD                                            
REMARK 480     PRO D  276   N     CA    CB    CG    CD                          
REMARK 480     SER D  279   CB    OG                                            
REMARK 480     SER D  296   N     CA    CB    OG                                
REMARK 480     THR D  297   OG1   CG2                                           
REMARK 480     GLU D  360   CG                                                  
REMARK 480     GLN D  375   CB    CG    CD    NE2                               
REMARK 480     ASP D  386   CB    CG    OD1   OD2                               
REMARK 480     GLU D  387   CB    CG    CD    OE1   OE2                         
REMARK 480     ASP D  388   CB    CG    OD1   OD2                               
REMARK 480     LYS D  392   CD    CE    NZ                                      
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    ASN B 214   C     PRO B 215   N       0.126                       
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    GLU A   7   CA  -  C   -  N   ANGL. DEV. =  13.7 DEGREES          
REMARK 500    GLU A   7   O   -  C   -  N   ANGL. DEV. = -14.5 DEGREES          
REMARK 500    LYS A   8   C   -  N   -  CA  ANGL. DEV. =  26.7 DEGREES          
REMARK 500    PRO A 291   O   -  C   -  N   ANGL. DEV. = -11.9 DEGREES          
REMARK 500    PRO A 348   CA  -  N   -  CD  ANGL. DEV. = -14.8 DEGREES          
REMARK 500    PRO A 401   CA  -  N   -  CD  ANGL. DEV. = -11.1 DEGREES          
REMARK 500    PRO D 276   CA  -  N   -  CD  ANGL. DEV. = -11.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A   8      163.75    -26.24                                   
REMARK 500    ASN A  34       82.27    -62.69                                   
REMARK 500    ARG A  60     -134.53   -125.19                                   
REMARK 500    ARG A  62       40.91    -84.02                                   
REMARK 500    ALA A  83     -178.94    179.17                                   
REMARK 500    THR A  86       29.87   -144.13                                   
REMARK 500    ARG A 240     -161.76     78.18                                   
REMARK 500    PRO A 291     -115.67    -65.85                                   
REMARK 500    HIS A 292      122.68    -30.22                                   
REMARK 500    ILE A 293       88.83   -159.02                                   
REMARK 500    SER A 296     -130.50    -71.12                                   
REMARK 500    THR A 297     -157.11   -113.39                                   
REMARK 500    GLN A 298      -37.01    -32.55                                   
REMARK 500    SER A 323        2.15     80.35                                   
REMARK 500    SER A 373     -135.26   -144.06                                   
REMARK 500    ALA A 374      -85.10    -51.17                                   
REMARK 500    ARG B  60     -145.05   -127.61                                   
REMARK 500    ALA B  83     -175.16    179.42                                   
REMARK 500    ASN B 103     -166.46   -122.63                                   
REMARK 500    ALA B 104       78.10   -109.73                                   
REMARK 500    ASN B 214      150.29    177.58                                   
REMARK 500    PRO B 215      -28.54    -33.80                                   
REMARK 500    SER B 239       81.63   -166.63                                   
REMARK 500    ARG B 240     -130.96   -137.75                                   
REMARK 500    THR B 290       71.84   -116.00                                   
REMARK 500    PRO B 291      114.97    -36.40                                   
REMARK 500    HIS B 292      118.41     45.34                                   
REMARK 500    SER B 323       -4.41     78.08                                   
REMARK 500    ASN B 326       28.55   -141.60                                   
REMARK 500    SER B 331      118.82   -160.10                                   
REMARK 500    ALA B 374     -130.34     70.31                                   
REMARK 500    ARG B 405      155.17    179.63                                   
REMARK 500    LYS C  10       30.84    -98.61                                   
REMARK 500    TYR C  32       91.06    -44.99                                   
REMARK 500    ASN C  34       85.17     73.71                                   
REMARK 500    ARG C  60     -151.68   -118.52                                   
REMARK 500    GLU C  74       -8.27   -140.76                                   
REMARK 500    ALA C  83     -169.61   -168.68                                   
REMARK 500    ILE C  84      -11.68    -47.79                                   
REMARK 500    ASN C  87      -92.57   -133.98                                   
REMARK 500    ASN C 103     -167.37   -117.24                                   
REMARK 500    ASN C 108       33.72    -98.78                                   
REMARK 500    SER C 146      104.25     56.09                                   
REMARK 500    SER C 216        3.60    -69.09                                   
REMARK 500    THR C 242       57.65   -109.36                                   
REMARK 500    ALA C 300        0.76    -65.05                                   
REMARK 500    GLN C 301      -17.83    -48.66                                   
REMARK 500    ASN C 326       29.41   -144.85                                   
REMARK 500    ALA C 390      -72.57    -57.98                                   
REMARK 500    LYS D   8      120.76    177.54                                   
REMARK 500    ARG D  60     -140.78   -121.96                                   
REMARK 500    ALA D  83     -177.63    179.62                                   
REMARK 500    ASN D 103     -164.72   -127.03                                   
REMARK 500    HIS D 210       58.26   -146.20                                   
REMARK 500    PHE D 277      -22.84    175.85                                   
REMARK 500    THR D 297       15.44   -160.43                                   
REMARK 500    GLN D 298     -140.86   -135.11                                   
REMARK 500    GLU D 360       -2.18    -57.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    PRO A 291         21.76                                           
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 NAD A 2101                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 2102                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 2103                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 2104                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1PSD   RELATED DB: PDB                                   
REMARK 900 THE ALLOSTERIC LIGAND SITE IN THE VMAX-TYPE COOPERATIVE              
REMARK 900 ENZYME PHOSPHOGLYCERATE DEHYDROGENASE                                
DBREF  1SC6 A    7   410  UNP    P0A9T0   SERA_ECOLI       6    409             
DBREF  1SC6 B    7   410  UNP    P0A9T0   SERA_ECOLI       6    409             
DBREF  1SC6 C    7   410  UNP    P0A9T0   SERA_ECOLI       6    409             
DBREF  1SC6 D    7   410  UNP    P0A9T0   SERA_ECOLI       6    409             
SEQADV 1SC6 ALA A   81  UNP  P0A9T0    CYS    80 ENGINEERED                     
SEQADV 1SC6 ALA A   83  UNP  P0A9T0    CYS    82 ENGINEERED                     
SEQADV 1SC6 GLY A  139  UNP  P0A9T0    TRP   138 ENGINEERED                     
SEQADV 1SC6 MSE A  175  UNP  P0A9T0    MET   174 MODIFIED RESIDUE               
SEQADV 1SC6 MSE A  203  UNP  P0A9T0    MET   202 MODIFIED RESIDUE               
SEQADV 1SC6 MSE A  220  UNP  P0A9T0    MET   219 MODIFIED RESIDUE               
SEQADV 1SC6 MSE A  221  UNP  P0A9T0    MET   220 MODIFIED RESIDUE               
SEQADV 1SC6 MSE A  229  UNP  P0A9T0    MET   228 MODIFIED RESIDUE               
SEQADV 1SC6 ALA A  250  UNP  P0A9T0    CYS   249 ENGINEERED                     
SEQADV 1SC6 ALA A  282  UNP  P0A9T0    CYS   281 ENGINEERED                     
SEQADV 1SC6 MSE A  341  UNP  P0A9T0    MET   340 MODIFIED RESIDUE               
SEQADV 1SC6 MSE A  376  UNP  P0A9T0    MET   375 MODIFIED RESIDUE               
SEQADV 1SC6 MSE A  397  UNP  P0A9T0    MET   396 MODIFIED RESIDUE               
SEQADV 1SC6 ALA B   81  UNP  P0A9T0    CYS    80 ENGINEERED                     
SEQADV 1SC6 ALA B   83  UNP  P0A9T0    CYS    82 ENGINEERED                     
SEQADV 1SC6 GLY B  139  UNP  P0A9T0    TRP   138 ENGINEERED                     
SEQADV 1SC6 MSE B  175  UNP  P0A9T0    MET   174 MODIFIED RESIDUE               
SEQADV 1SC6 MSE B  203  UNP  P0A9T0    MET   202 MODIFIED RESIDUE               
SEQADV 1SC6 MSE B  220  UNP  P0A9T0    MET   219 MODIFIED RESIDUE               
SEQADV 1SC6 MSE B  221  UNP  P0A9T0    MET   220 MODIFIED RESIDUE               
SEQADV 1SC6 MSE B  229  UNP  P0A9T0    MET   228 MODIFIED RESIDUE               
SEQADV 1SC6 ALA B  250  UNP  P0A9T0    CYS   249 ENGINEERED                     
SEQADV 1SC6 ALA B  282  UNP  P0A9T0    CYS   281 ENGINEERED                     
SEQADV 1SC6 MSE B  341  UNP  P0A9T0    MET   340 MODIFIED RESIDUE               
SEQADV 1SC6 MSE B  376  UNP  P0A9T0    MET   375 MODIFIED RESIDUE               
SEQADV 1SC6 MSE B  397  UNP  P0A9T0    MET   396 MODIFIED RESIDUE               
SEQADV 1SC6 ALA C   81  UNP  P0A9T0    CYS    80 ENGINEERED                     
SEQADV 1SC6 ALA C   83  UNP  P0A9T0    CYS    82 ENGINEERED                     
SEQADV 1SC6 GLY C  139  UNP  P0A9T0    TRP   138 ENGINEERED                     
SEQADV 1SC6 MSE C  175  UNP  P0A9T0    MET   174 MODIFIED RESIDUE               
SEQADV 1SC6 MSE C  203  UNP  P0A9T0    MET   202 MODIFIED RESIDUE               
SEQADV 1SC6 MSE C  220  UNP  P0A9T0    MET   219 MODIFIED RESIDUE               
SEQADV 1SC6 MSE C  221  UNP  P0A9T0    MET   220 MODIFIED RESIDUE               
SEQADV 1SC6 MSE C  229  UNP  P0A9T0    MET   228 MODIFIED RESIDUE               
SEQADV 1SC6 ALA C  250  UNP  P0A9T0    CYS   249 ENGINEERED                     
SEQADV 1SC6 ALA C  282  UNP  P0A9T0    CYS   281 ENGINEERED                     
SEQADV 1SC6 MSE C  341  UNP  P0A9T0    MET   340 MODIFIED RESIDUE               
SEQADV 1SC6 MSE C  376  UNP  P0A9T0    MET   375 MODIFIED RESIDUE               
SEQADV 1SC6 MSE C  397  UNP  P0A9T0    MET   396 MODIFIED RESIDUE               
SEQADV 1SC6 ALA D   81  UNP  P0A9T0    CYS    80 ENGINEERED                     
SEQADV 1SC6 ALA D   83  UNP  P0A9T0    CYS    82 ENGINEERED                     
SEQADV 1SC6 GLY D  139  UNP  P0A9T0    TRP   138 ENGINEERED                     
SEQADV 1SC6 MSE D  175  UNP  P0A9T0    MET   174 MODIFIED RESIDUE               
SEQADV 1SC6 MSE D  203  UNP  P0A9T0    MET   202 MODIFIED RESIDUE               
SEQADV 1SC6 MSE D  220  UNP  P0A9T0    MET   219 MODIFIED RESIDUE               
SEQADV 1SC6 MSE D  221  UNP  P0A9T0    MET   220 MODIFIED RESIDUE               
SEQADV 1SC6 MSE D  229  UNP  P0A9T0    MET   228 MODIFIED RESIDUE               
SEQADV 1SC6 ALA D  250  UNP  P0A9T0    CYS   249 ENGINEERED                     
SEQADV 1SC6 ALA D  282  UNP  P0A9T0    CYS   281 ENGINEERED                     
SEQADV 1SC6 MSE D  341  UNP  P0A9T0    MET   340 MODIFIED RESIDUE               
SEQADV 1SC6 MSE D  376  UNP  P0A9T0    MET   375 MODIFIED RESIDUE               
SEQADV 1SC6 MSE D  397  UNP  P0A9T0    MET   396 MODIFIED RESIDUE               
SEQRES   1 A  404  GLU LYS ASP LYS ILE LYS PHE LEU LEU VAL GLU GLY VAL          
SEQRES   2 A  404  HIS GLN LYS ALA LEU GLU SER LEU ARG ALA ALA GLY TYR          
SEQRES   3 A  404  THR ASN ILE GLU PHE HIS LYS GLY ALA LEU ASP ASP GLU          
SEQRES   4 A  404  GLN LEU LYS GLU SER ILE ARG ASP ALA HIS PHE ILE GLY          
SEQRES   5 A  404  LEU ARG SER ARG THR HIS LEU THR GLU ASP VAL ILE ASN          
SEQRES   6 A  404  ALA ALA GLU LYS LEU VAL ALA ILE GLY ALA PHE ALA ILE          
SEQRES   7 A  404  GLY THR ASN GLN VAL ASP LEU ASP ALA ALA ALA LYS ARG          
SEQRES   8 A  404  GLY ILE PRO VAL PHE ASN ALA PRO PHE SER ASN THR ARG          
SEQRES   9 A  404  SER VAL ALA GLU LEU VAL ILE GLY GLU LEU LEU LEU LEU          
SEQRES  10 A  404  LEU ARG GLY VAL PRO GLU ALA ASN ALA LYS ALA HIS ARG          
SEQRES  11 A  404  GLY VAL GLY ASN LYS LEU ALA ALA GLY SER PHE GLU ALA          
SEQRES  12 A  404  ARG GLY LYS LYS LEU GLY ILE ILE GLY TYR GLY HIS ILE          
SEQRES  13 A  404  GLY THR GLN LEU GLY ILE LEU ALA GLU SER LEU GLY MSE          
SEQRES  14 A  404  TYR VAL TYR PHE TYR ASP ILE GLU ASN LYS LEU PRO LEU          
SEQRES  15 A  404  GLY ASN ALA THR GLN VAL GLN HIS LEU SER ASP LEU LEU          
SEQRES  16 A  404  ASN MSE SER ASP VAL VAL SER LEU HIS VAL PRO GLU ASN          
SEQRES  17 A  404  PRO SER THR LYS ASN MSE MSE GLY ALA LYS GLU ILE SER          
SEQRES  18 A  404  LEU MSE LYS PRO GLY SER LEU LEU ILE ASN ALA SER ARG          
SEQRES  19 A  404  GLY THR VAL VAL ASP ILE PRO ALA LEU ALA ASP ALA LEU          
SEQRES  20 A  404  ALA SER LYS HIS LEU ALA GLY ALA ALA ILE ASP VAL PHE          
SEQRES  21 A  404  PRO THR GLU PRO ALA THR ASN SER ASP PRO PHE THR SER          
SEQRES  22 A  404  PRO LEU ALA GLU PHE ASP ASN VAL LEU LEU THR PRO HIS          
SEQRES  23 A  404  ILE GLY GLY SER THR GLN GLU ALA GLN GLU ASN ILE GLY          
SEQRES  24 A  404  LEU GLU VAL ALA GLY LYS LEU ILE LYS TYR SER ASP ASN          
SEQRES  25 A  404  GLY SER THR LEU SER ALA VAL ASN PHE PRO GLU VAL SER          
SEQRES  26 A  404  LEU PRO LEU HIS GLY GLY ARG ARG LEU MSE HIS ILE HIS          
SEQRES  27 A  404  GLU ASN ARG PRO GLY VAL LEU THR ALA LEU ASN LYS ILE          
SEQRES  28 A  404  PHE ALA GLU GLN GLY VAL ASN ILE ALA ALA GLN TYR LEU          
SEQRES  29 A  404  GLN THR SER ALA GLN MSE GLY TYR VAL VAL ILE ASP ILE          
SEQRES  30 A  404  GLU ALA ASP GLU ASP VAL ALA GLU LYS ALA LEU GLN ALA          
SEQRES  31 A  404  MSE LYS ALA ILE PRO GLY THR ILE ARG ALA ARG LEU LEU          
SEQRES  32 A  404  TYR                                                          
SEQRES   1 B  404  GLU LYS ASP LYS ILE LYS PHE LEU LEU VAL GLU GLY VAL          
SEQRES   2 B  404  HIS GLN LYS ALA LEU GLU SER LEU ARG ALA ALA GLY TYR          
SEQRES   3 B  404  THR ASN ILE GLU PHE HIS LYS GLY ALA LEU ASP ASP GLU          
SEQRES   4 B  404  GLN LEU LYS GLU SER ILE ARG ASP ALA HIS PHE ILE GLY          
SEQRES   5 B  404  LEU ARG SER ARG THR HIS LEU THR GLU ASP VAL ILE ASN          
SEQRES   6 B  404  ALA ALA GLU LYS LEU VAL ALA ILE GLY ALA PHE ALA ILE          
SEQRES   7 B  404  GLY THR ASN GLN VAL ASP LEU ASP ALA ALA ALA LYS ARG          
SEQRES   8 B  404  GLY ILE PRO VAL PHE ASN ALA PRO PHE SER ASN THR ARG          
SEQRES   9 B  404  SER VAL ALA GLU LEU VAL ILE GLY GLU LEU LEU LEU LEU          
SEQRES  10 B  404  LEU ARG GLY VAL PRO GLU ALA ASN ALA LYS ALA HIS ARG          
SEQRES  11 B  404  GLY VAL GLY ASN LYS LEU ALA ALA GLY SER PHE GLU ALA          
SEQRES  12 B  404  ARG GLY LYS LYS LEU GLY ILE ILE GLY TYR GLY HIS ILE          
SEQRES  13 B  404  GLY THR GLN LEU GLY ILE LEU ALA GLU SER LEU GLY MSE          
SEQRES  14 B  404  TYR VAL TYR PHE TYR ASP ILE GLU ASN LYS LEU PRO LEU          
SEQRES  15 B  404  GLY ASN ALA THR GLN VAL GLN HIS LEU SER ASP LEU LEU          
SEQRES  16 B  404  ASN MSE SER ASP VAL VAL SER LEU HIS VAL PRO GLU ASN          
SEQRES  17 B  404  PRO SER THR LYS ASN MSE MSE GLY ALA LYS GLU ILE SER          
SEQRES  18 B  404  LEU MSE LYS PRO GLY SER LEU LEU ILE ASN ALA SER ARG          
SEQRES  19 B  404  GLY THR VAL VAL ASP ILE PRO ALA LEU ALA ASP ALA LEU          
SEQRES  20 B  404  ALA SER LYS HIS LEU ALA GLY ALA ALA ILE ASP VAL PHE          
SEQRES  21 B  404  PRO THR GLU PRO ALA THR ASN SER ASP PRO PHE THR SER          
SEQRES  22 B  404  PRO LEU ALA GLU PHE ASP ASN VAL LEU LEU THR PRO HIS          
SEQRES  23 B  404  ILE GLY GLY SER THR GLN GLU ALA GLN GLU ASN ILE GLY          
SEQRES  24 B  404  LEU GLU VAL ALA GLY LYS LEU ILE LYS TYR SER ASP ASN          
SEQRES  25 B  404  GLY SER THR LEU SER ALA VAL ASN PHE PRO GLU VAL SER          
SEQRES  26 B  404  LEU PRO LEU HIS GLY GLY ARG ARG LEU MSE HIS ILE HIS          
SEQRES  27 B  404  GLU ASN ARG PRO GLY VAL LEU THR ALA LEU ASN LYS ILE          
SEQRES  28 B  404  PHE ALA GLU GLN GLY VAL ASN ILE ALA ALA GLN TYR LEU          
SEQRES  29 B  404  GLN THR SER ALA GLN MSE GLY TYR VAL VAL ILE ASP ILE          
SEQRES  30 B  404  GLU ALA ASP GLU ASP VAL ALA GLU LYS ALA LEU GLN ALA          
SEQRES  31 B  404  MSE LYS ALA ILE PRO GLY THR ILE ARG ALA ARG LEU LEU          
SEQRES  32 B  404  TYR                                                          
SEQRES   1 C  404  GLU LYS ASP LYS ILE LYS PHE LEU LEU VAL GLU GLY VAL          
SEQRES   2 C  404  HIS GLN LYS ALA LEU GLU SER LEU ARG ALA ALA GLY TYR          
SEQRES   3 C  404  THR ASN ILE GLU PHE HIS LYS GLY ALA LEU ASP ASP GLU          
SEQRES   4 C  404  GLN LEU LYS GLU SER ILE ARG ASP ALA HIS PHE ILE GLY          
SEQRES   5 C  404  LEU ARG SER ARG THR HIS LEU THR GLU ASP VAL ILE ASN          
SEQRES   6 C  404  ALA ALA GLU LYS LEU VAL ALA ILE GLY ALA PHE ALA ILE          
SEQRES   7 C  404  GLY THR ASN GLN VAL ASP LEU ASP ALA ALA ALA LYS ARG          
SEQRES   8 C  404  GLY ILE PRO VAL PHE ASN ALA PRO PHE SER ASN THR ARG          
SEQRES   9 C  404  SER VAL ALA GLU LEU VAL ILE GLY GLU LEU LEU LEU LEU          
SEQRES  10 C  404  LEU ARG GLY VAL PRO GLU ALA ASN ALA LYS ALA HIS ARG          
SEQRES  11 C  404  GLY VAL GLY ASN LYS LEU ALA ALA GLY SER PHE GLU ALA          
SEQRES  12 C  404  ARG GLY LYS LYS LEU GLY ILE ILE GLY TYR GLY HIS ILE          
SEQRES  13 C  404  GLY THR GLN LEU GLY ILE LEU ALA GLU SER LEU GLY MSE          
SEQRES  14 C  404  TYR VAL TYR PHE TYR ASP ILE GLU ASN LYS LEU PRO LEU          
SEQRES  15 C  404  GLY ASN ALA THR GLN VAL GLN HIS LEU SER ASP LEU LEU          
SEQRES  16 C  404  ASN MSE SER ASP VAL VAL SER LEU HIS VAL PRO GLU ASN          
SEQRES  17 C  404  PRO SER THR LYS ASN MSE MSE GLY ALA LYS GLU ILE SER          
SEQRES  18 C  404  LEU MSE LYS PRO GLY SER LEU LEU ILE ASN ALA SER ARG          
SEQRES  19 C  404  GLY THR VAL VAL ASP ILE PRO ALA LEU ALA ASP ALA LEU          
SEQRES  20 C  404  ALA SER LYS HIS LEU ALA GLY ALA ALA ILE ASP VAL PHE          
SEQRES  21 C  404  PRO THR GLU PRO ALA THR ASN SER ASP PRO PHE THR SER          
SEQRES  22 C  404  PRO LEU ALA GLU PHE ASP ASN VAL LEU LEU THR PRO HIS          
SEQRES  23 C  404  ILE GLY GLY SER THR GLN GLU ALA GLN GLU ASN ILE GLY          
SEQRES  24 C  404  LEU GLU VAL ALA GLY LYS LEU ILE LYS TYR SER ASP ASN          
SEQRES  25 C  404  GLY SER THR LEU SER ALA VAL ASN PHE PRO GLU VAL SER          
SEQRES  26 C  404  LEU PRO LEU HIS GLY GLY ARG ARG LEU MSE HIS ILE HIS          
SEQRES  27 C  404  GLU ASN ARG PRO GLY VAL LEU THR ALA LEU ASN LYS ILE          
SEQRES  28 C  404  PHE ALA GLU GLN GLY VAL ASN ILE ALA ALA GLN TYR LEU          
SEQRES  29 C  404  GLN THR SER ALA GLN MSE GLY TYR VAL VAL ILE ASP ILE          
SEQRES  30 C  404  GLU ALA ASP GLU ASP VAL ALA GLU LYS ALA LEU GLN ALA          
SEQRES  31 C  404  MSE LYS ALA ILE PRO GLY THR ILE ARG ALA ARG LEU LEU          
SEQRES  32 C  404  TYR                                                          
SEQRES   1 D  404  GLU LYS ASP LYS ILE LYS PHE LEU LEU VAL GLU GLY VAL          
SEQRES   2 D  404  HIS GLN LYS ALA LEU GLU SER LEU ARG ALA ALA GLY TYR          
SEQRES   3 D  404  THR ASN ILE GLU PHE HIS LYS GLY ALA LEU ASP ASP GLU          
SEQRES   4 D  404  GLN LEU LYS GLU SER ILE ARG ASP ALA HIS PHE ILE GLY          
SEQRES   5 D  404  LEU ARG SER ARG THR HIS LEU THR GLU ASP VAL ILE ASN          
SEQRES   6 D  404  ALA ALA GLU LYS LEU VAL ALA ILE GLY ALA PHE ALA ILE          
SEQRES   7 D  404  GLY THR ASN GLN VAL ASP LEU ASP ALA ALA ALA LYS ARG          
SEQRES   8 D  404  GLY ILE PRO VAL PHE ASN ALA PRO PHE SER ASN THR ARG          
SEQRES   9 D  404  SER VAL ALA GLU LEU VAL ILE GLY GLU LEU LEU LEU LEU          
SEQRES  10 D  404  LEU ARG GLY VAL PRO GLU ALA ASN ALA LYS ALA HIS ARG          
SEQRES  11 D  404  GLY VAL GLY ASN LYS LEU ALA ALA GLY SER PHE GLU ALA          
SEQRES  12 D  404  ARG GLY LYS LYS LEU GLY ILE ILE GLY TYR GLY HIS ILE          
SEQRES  13 D  404  GLY THR GLN LEU GLY ILE LEU ALA GLU SER LEU GLY MSE          
SEQRES  14 D  404  TYR VAL TYR PHE TYR ASP ILE GLU ASN LYS LEU PRO LEU          
SEQRES  15 D  404  GLY ASN ALA THR GLN VAL GLN HIS LEU SER ASP LEU LEU          
SEQRES  16 D  404  ASN MSE SER ASP VAL VAL SER LEU HIS VAL PRO GLU ASN          
SEQRES  17 D  404  PRO SER THR LYS ASN MSE MSE GLY ALA LYS GLU ILE SER          
SEQRES  18 D  404  LEU MSE LYS PRO GLY SER LEU LEU ILE ASN ALA SER ARG          
SEQRES  19 D  404  GLY THR VAL VAL ASP ILE PRO ALA LEU ALA ASP ALA LEU          
SEQRES  20 D  404  ALA SER LYS HIS LEU ALA GLY ALA ALA ILE ASP VAL PHE          
SEQRES  21 D  404  PRO THR GLU PRO ALA THR ASN SER ASP PRO PHE THR SER          
SEQRES  22 D  404  PRO LEU ALA GLU PHE ASP ASN VAL LEU LEU THR PRO HIS          
SEQRES  23 D  404  ILE GLY GLY SER THR GLN GLU ALA GLN GLU ASN ILE GLY          
SEQRES  24 D  404  LEU GLU VAL ALA GLY LYS LEU ILE LYS TYR SER ASP ASN          
SEQRES  25 D  404  GLY SER THR LEU SER ALA VAL ASN PHE PRO GLU VAL SER          
SEQRES  26 D  404  LEU PRO LEU HIS GLY GLY ARG ARG LEU MSE HIS ILE HIS          
SEQRES  27 D  404  GLU ASN ARG PRO GLY VAL LEU THR ALA LEU ASN LYS ILE          
SEQRES  28 D  404  PHE ALA GLU GLN GLY VAL ASN ILE ALA ALA GLN TYR LEU          
SEQRES  29 D  404  GLN THR SER ALA GLN MSE GLY TYR VAL VAL ILE ASP ILE          
SEQRES  30 D  404  GLU ALA ASP GLU ASP VAL ALA GLU LYS ALA LEU GLN ALA          
SEQRES  31 D  404  MSE LYS ALA ILE PRO GLY THR ILE ARG ALA ARG LEU LEU          
SEQRES  32 D  404  TYR                                                          
MODRES 1SC6 MSE A  175  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE A  203  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE A  220  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE A  221  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE A  229  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE A  341  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE A  376  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE A  397  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE B  175  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE B  203  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE B  220  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE B  221  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE B  229  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE B  341  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE B  376  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE B  397  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE C  175  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE C  203  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE C  220  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE C  221  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE C  229  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE C  341  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE C  376  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE C  397  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE D  175  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE D  203  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE D  220  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE D  221  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE D  229  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE D  341  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE D  376  MET  SELENOMETHIONINE                                   
MODRES 1SC6 MSE D  397  MET  SELENOMETHIONINE                                   
HET    MSE  A 175       8                                                       
HET    MSE  A 203       8                                                       
HET    MSE  A 220       8                                                       
HET    MSE  A 221       8                                                       
HET    MSE  A 229       8                                                       
HET    MSE  A 341       8                                                       
HET    MSE  A 376       8                                                       
HET    MSE  A 397       8                                                       
HET    MSE  B 175       8                                                       
HET    MSE  B 203       8                                                       
HET    MSE  B 220       8                                                       
HET    MSE  B 221       8                                                       
HET    MSE  B 229       8                                                       
HET    MSE  B 341       8                                                       
HET    MSE  B 376       8                                                       
HET    MSE  B 397       8                                                       
HET    MSE  C 175       8                                                       
HET    MSE  C 203       8                                                       
HET    MSE  C 220       8                                                       
HET    MSE  C 221       8                                                       
HET    MSE  C 229       8                                                       
HET    MSE  C 341       8                                                       
HET    MSE  C 376       8                                                       
HET    MSE  C 397       8                                                       
HET    MSE  D 175       8                                                       
HET    MSE  D 203       8                                                       
HET    MSE  D 220       8                                                       
HET    MSE  D 221       8                                                       
HET    MSE  D 229       8                                                       
HET    MSE  D 341       8                                                       
HET    MSE  D 376       8                                                       
HET    MSE  D 397       8                                                       
HET    NAD  A2101      44                                                       
HET    NAD  B2102      44                                                       
HET    NAD  C2103      44                                                       
HET    NAD  D2104      44                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
FORMUL   1  MSE    32(C5 H11 N O2 SE)                                           
FORMUL   5  NAD    4(C21 H27 N7 O14 P2)                                         
FORMUL   9  HOH   *463(H2 O)                                                    
HELIX    1   1 HIS A   20  ALA A   30  1                                  11    
HELIX    2   2 ASP A   43  ILE A   51  1                                   9    
HELIX    3   3 THR A   66  ALA A   73  1                                   8    
HELIX    4   4 ASP A   90  ARG A   97  1                                   8    
HELIX    5   5 ASN A  108  GLY A  126  1                                  19    
HELIX    6   6 GLY A  126  GLY A  137  1                                  12    
HELIX    7   7 GLY A  160  LEU A  173  1                                  14    
HELIX    8   8 HIS A  196  SER A  204  1                                   9    
HELIX    9   9 GLY A  222  MSE A  229  1                                   8    
HELIX   10  10 ASP A  245  SER A  255  1                                  11    
HELIX   11  11 THR A  278  ALA A  282  5                                   5    
HELIX   12  12 THR A  297  GLY A  319  1                                  23    
HELIX   13  13 GLY A  349  GLN A  361  1                                  13    
HELIX   14  14 ASP A  386  ALA A  399  1                                  14    
HELIX   15  15 HIS B   20  ALA B   30  1                                  11    
HELIX   16  16 ASP B   43  ARG B   52  1                                  10    
HELIX   17  17 THR B   66  ALA B   73  1                                   8    
HELIX   18  18 ASP B   90  ARG B   97  1                                   8    
HELIX   19  19 ASN B  108  GLY B  126  1                                  19    
HELIX   20  20 GLY B  126  ARG B  136  1                                  11    
HELIX   21  21 GLY B  160  LEU B  173  1                                  14    
HELIX   22  22 HIS B  196  SER B  204  1                                   9    
HELIX   23  23 GLY B  222  MSE B  229  1                                   8    
HELIX   24  24 ASP B  245  SER B  255  1                                  11    
HELIX   25  25 ALA B  300  GLY B  319  1                                  20    
HELIX   26  26 GLY B  349  GLN B  361  1                                  13    
HELIX   27  27 ASP B  386  ALA B  399  1                                  14    
HELIX   28  28 HIS C   20  ALA C   30  1                                  11    
HELIX   29  29 ASP C   43  ARG C   52  1                                  10    
HELIX   30  30 THR C   66  ALA C   73  1                                   8    
HELIX   31  31 ASP C   90  ARG C   97  1                                   8    
HELIX   32  32 ASN C  108  ARG C  125  1                                  18    
HELIX   33  33 GLY C  126  ARG C  136  1                                  11    
HELIX   34  34 GLY C  160  LEU C  173  1                                  14    
HELIX   35  35 HIS C  196  SER C  204  1                                   9    
HELIX   36  36 GLY C  222  MSE C  229  1                                   8    
HELIX   37  37 ASP C  245  SER C  255  1                                  11    
HELIX   38  38 ALA C  300  GLY C  319  1                                  20    
HELIX   39  39 GLY C  349  GLN C  361  1                                  13    
HELIX   40  40 ASP C  386  ALA C  399  1                                  14    
HELIX   41  41 HIS D   20  ALA D   30  1                                  11    
HELIX   42  42 ASP D   43  ARG D   52  1                                  10    
HELIX   43  43 THR D   66  ALA D   73  1                                   8    
HELIX   44  44 ASP D   90  ARG D   97  1                                   8    
HELIX   45  45 ASN D  108  ARG D  125  1                                  18    
HELIX   46  46 GLY D  126  HIS D  135  1                                  10    
HELIX   47  47 GLY D  160  LEU D  173  1                                  14    
HELIX   48  48 HIS D  196  SER D  204  1                                   9    
HELIX   49  49 GLY D  222  MSE D  229  1                                   8    
HELIX   50  50 ASP D  245  SER D  255  1                                  11    
HELIX   51  51 THR D  278  ALA D  282  5                                   5    
HELIX   52  52 GLU D  299  GLY D  319  1                                  21    
HELIX   53  53 GLY D  349  GLU D  360  1                                  12    
HELIX   54  54 ASP D  386  ILE D  400  1                                  15    
SHEET    1   A 5 ILE A  35  PHE A  37  0                                        
SHEET    2   A 5 PHE A  13  LEU A  15  1  N  PHE A  13   O  GLU A  36           
SHEET    3   A 5 PHE A  56  LEU A  59  1  O  GLY A  58   N  LEU A  14           
SHEET    4   A 5 ALA A  78  ALA A  81  1  O  GLY A  80   N  ILE A  57           
SHEET    5   A 5 VAL A 101  PHE A 102  1  O  PHE A 102   N  ALA A  81           
SHEET    1   B 7 THR A 192  GLN A 193  0                                        
SHEET    2   B 7 TYR A 176  TYR A 180  1  N  PHE A 179   O  THR A 192           
SHEET    3   B 7 LYS A 153  ILE A 157  1  N  LEU A 154   O  TYR A 176           
SHEET    4   B 7 VAL A 206  LEU A 209  1  O  VAL A 206   N  GLY A 155           
SHEET    5   B 7 SER A 233  ASN A 237  1  O  ILE A 236   N  VAL A 207           
SHEET    6   B 7 LEU A 258  ASP A 264  1  O  ALA A 262   N  ASN A 237           
SHEET    7   B 7 VAL A 287  THR A 290  1  O  LEU A 288   N  ILE A 263           
SHEET    1   C 8 THR A 403  TYR A 410  0                                        
SHEET    2   C 8 ARG A 338  GLU A 345 -1  N  ILE A 343   O  ARG A 405           
SHEET    3   C 8 MSE A 376  GLU A 384 -1  O  ILE A 381   N  LEU A 340           
SHEET    4   C 8 ASN A 364  THR A 372 -1  N  ALA A 367   O  ASP A 382           
SHEET    5   C 8 ILE C 365  THR C 372 -1  O  LEU C 370   N  GLN A 368           
SHEET    6   C 8 MSE C 376  ILE C 383 -1  O  TYR C 378   N  GLN C 371           
SHEET    7   C 8 ARG C 338  GLU C 345 -1  N  ARG C 338   O  ILE C 383           
SHEET    8   C 8 THR C 403  TYR C 410 -1  O  ARG C 405   N  ILE C 343           
SHEET    1   D 5 ILE B  35  PHE B  37  0                                        
SHEET    2   D 5 PHE B  13  LEU B  15  1  N  LEU B  15   O  GLU B  36           
SHEET    3   D 5 PHE B  56  LEU B  59  1  O  GLY B  58   N  LEU B  14           
SHEET    4   D 5 ALA B  78  ALA B  81  1  O  GLY B  80   N  ILE B  57           
SHEET    5   D 5 VAL B 101  PHE B 102  1  O  PHE B 102   N  ALA B  81           
SHEET    1   E 7 THR B 192  GLN B 193  0                                        
SHEET    2   E 7 TYR B 176  TYR B 180  1  N  PHE B 179   O  THR B 192           
SHEET    3   E 7 LYS B 153  ILE B 157  1  N  LEU B 154   O  TYR B 176           
SHEET    4   E 7 VAL B 206  LEU B 209  1  O  VAL B 206   N  GLY B 155           
SHEET    5   E 7 SER B 233  ASN B 237  1  O  ILE B 236   N  VAL B 207           
SHEET    6   E 7 LEU B 258  ILE B 263  1  O  ALA B 262   N  ASN B 237           
SHEET    7   E 7 VAL B 287  LEU B 289  1  O  LEU B 288   N  ALA B 261           
SHEET    1   F 8 THR B 403  TYR B 410  0                                        
SHEET    2   F 8 ARG B 338  GLU B 345 -1  N  ILE B 343   O  ARG B 405           
SHEET    3   F 8 MSE B 376  ILE B 383 -1  O  ILE B 381   N  LEU B 340           
SHEET    4   F 8 ILE B 365  SER B 373 -1  N  ALA B 367   O  ASP B 382           
SHEET    5   F 8 ASN D 364  THR D 372 -1  O  GLN D 368   N  LEU B 370           
SHEET    6   F 8 MSE D 376  GLU D 384 -1  O  ASP D 382   N  ALA D 367           
SHEET    7   F 8 ARG D 338  GLU D 345 -1  N  LEU D 340   O  ILE D 381           
SHEET    8   F 8 THR D 403  TYR D 410 -1  O  ARG D 405   N  ILE D 343           
SHEET    1   G 5 ILE C  35  PHE C  37  0                                        
SHEET    2   G 5 PHE C  13  LEU C  15  1  N  LEU C  15   O  GLU C  36           
SHEET    3   G 5 PHE C  56  LEU C  59  1  O  GLY C  58   N  LEU C  14           
SHEET    4   G 5 ALA C  78  ALA C  81  1  O  GLY C  80   N  ILE C  57           
SHEET    5   G 5 VAL C 101  PHE C 102  1  O  PHE C 102   N  ALA C  81           
SHEET    1   H 7 THR C 192  GLN C 193  0                                        
SHEET    2   H 7 TYR C 176  TYR C 180  1  N  PHE C 179   O  THR C 192           
SHEET    3   H 7 LYS C 153  ILE C 157  1  N  ILE C 156   O  TYR C 178           
SHEET    4   H 7 VAL C 206  LEU C 209  1  O  VAL C 206   N  GLY C 155           
SHEET    5   H 7 SER C 233  ASN C 237  1  O  ILE C 236   N  VAL C 207           
SHEET    6   H 7 LEU C 258  ASP C 264  1  O  ALA C 262   N  ASN C 237           
SHEET    7   H 7 VAL C 287  THR C 290  1  O  LEU C 288   N  ILE C 263           
SHEET    1   I 5 ILE D  35  PHE D  37  0                                        
SHEET    2   I 5 PHE D  13  LEU D  15  1  N  PHE D  13   O  GLU D  36           
SHEET    3   I 5 PHE D  56  LEU D  59  1  O  PHE D  56   N  LEU D  14           
SHEET    4   I 5 ALA D  78  ALA D  81  1  O  GLY D  80   N  ILE D  57           
SHEET    5   I 5 VAL D 101  PHE D 102  1  O  PHE D 102   N  ALA D  81           
SHEET    1   J 7 THR D 192  GLN D 193  0                                        
SHEET    2   J 7 TYR D 176  TYR D 180  1  N  PHE D 179   O  THR D 192           
SHEET    3   J 7 LYS D 153  ILE D 157  1  N  ILE D 156   O  TYR D 178           
SHEET    4   J 7 VAL D 206  LEU D 209  1  O  VAL D 206   N  GLY D 155           
SHEET    5   J 7 SER D 233  ASN D 237  1  O  ILE D 236   N  VAL D 207           
SHEET    6   J 7 LEU D 258  ASP D 264  1  O  ALA D 262   N  ASN D 237           
SHEET    7   J 7 VAL D 287  THR D 290  1  O  LEU D 288   N  ALA D 261           
LINK         C   GLY A 174                 N   MSE A 175     1555   1555  1.33  
LINK         C   MSE A 175                 N   TYR A 176     1555   1555  1.33  
LINK         C   ASN A 202                 N   MSE A 203     1555   1555  1.33  
LINK         C   MSE A 203                 N   SER A 204     1555   1555  1.33  
LINK         C   ASN A 219                 N   MSE A 220     1555   1555  1.33  
LINK         C   MSE A 220                 N   MSE A 221     1555   1555  1.33  
LINK         C   MSE A 221                 N   GLY A 222     1555   1555  1.33  
LINK         C   LEU A 228                 N   MSE A 229     1555   1555  1.33  
LINK         C   MSE A 229                 N   LYS A 230     1555   1555  1.33  
LINK         C   LEU A 340                 N   MSE A 341     1555   1555  1.33  
LINK         C   MSE A 341                 N   HIS A 342     1555   1555  1.33  
LINK         C   GLN A 375                 N   MSE A 376     1555   1555  1.33  
LINK         C   MSE A 376                 N   GLY A 377     1555   1555  1.33  
LINK         C   ALA A 396                 N   MSE A 397     1555   1555  1.33  
LINK         C   MSE A 397                 N   LYS A 398     1555   1555  1.33  
LINK         C   GLY B 174                 N   MSE B 175     1555   1555  1.33  
LINK         C   MSE B 175                 N   TYR B 176     1555   1555  1.33  
LINK         C   ASN B 202                 N   MSE B 203     1555   1555  1.33  
LINK         C   MSE B 203                 N   SER B 204     1555   1555  1.33  
LINK         C   ASN B 219                 N   MSE B 220     1555   1555  1.34  
LINK         C   MSE B 220                 N   MSE B 221     1555   1555  1.33  
LINK         C   MSE B 221                 N   GLY B 222     1555   1555  1.33  
LINK         C   LEU B 228                 N   MSE B 229     1555   1555  1.33  
LINK         C   MSE B 229                 N   LYS B 230     1555   1555  1.33  
LINK         C   LEU B 340                 N   MSE B 341     1555   1555  1.33  
LINK         C   MSE B 341                 N   HIS B 342     1555   1555  1.33  
LINK         C   GLN B 375                 N   MSE B 376     1555   1555  1.33  
LINK         C   MSE B 376                 N   GLY B 377     1555   1555  1.33  
LINK         C   ALA B 396                 N   MSE B 397     1555   1555  1.33  
LINK         C   MSE B 397                 N   LYS B 398     1555   1555  1.33  
LINK         C   GLY C 174                 N   MSE C 175     1555   1555  1.33  
LINK         C   MSE C 175                 N   TYR C 176     1555   1555  1.33  
LINK         C   ASN C 202                 N   MSE C 203     1555   1555  1.33  
LINK         C   MSE C 203                 N   SER C 204     1555   1555  1.32  
LINK         C   ASN C 219                 N   MSE C 220     1555   1555  1.33  
LINK         C   MSE C 220                 N   MSE C 221     1555   1555  1.33  
LINK         C   MSE C 221                 N   GLY C 222     1555   1555  1.33  
LINK         C   LEU C 228                 N   MSE C 229     1555   1555  1.33  
LINK         C   MSE C 229                 N   LYS C 230     1555   1555  1.33  
LINK         C   LEU C 340                 N   MSE C 341     1555   1555  1.33  
LINK         C   MSE C 341                 N   HIS C 342     1555   1555  1.33  
LINK         C   GLN C 375                 N   MSE C 376     1555   1555  1.33  
LINK         C   MSE C 376                 N   GLY C 377     1555   1555  1.33  
LINK         C   ALA C 396                 N   MSE C 397     1555   1555  1.33  
LINK         C   MSE C 397                 N   LYS C 398     1555   1555  1.33  
LINK         C   GLY D 174                 N   MSE D 175     1555   1555  1.33  
LINK         C   MSE D 175                 N   TYR D 176     1555   1555  1.33  
LINK         C   ASN D 202                 N   MSE D 203     1555   1555  1.34  
LINK         C   MSE D 203                 N   SER D 204     1555   1555  1.33  
LINK         C   ASN D 219                 N   MSE D 220     1555   1555  1.33  
LINK         C   MSE D 220                 N   MSE D 221     1555   1555  1.33  
LINK         C   MSE D 221                 N   GLY D 222     1555   1555  1.33  
LINK         C   LEU D 228                 N   MSE D 229     1555   1555  1.33  
LINK         C   MSE D 229                 N   LYS D 230     1555   1555  1.33  
LINK         C   LEU D 340                 N   MSE D 341     1555   1555  1.33  
LINK         C   MSE D 341                 N   HIS D 342     1555   1555  1.33  
LINK         C   GLN D 375                 N   MSE D 376     1555   1555  1.33  
LINK         C   MSE D 376                 N   GLY D 377     1555   1555  1.33  
LINK         C   ALA D 396                 N   MSE D 397     1555   1555  1.33  
LINK         C   MSE D 397                 N   LYS D 398     1555   1555  1.33  
SITE     1 AC1 20 PRO A 105  PHE A 106  ASN A 108  THR A 109                    
SITE     2 AC1 20 GLY A 158  TYR A 159  GLY A 160  HIS A 161                    
SITE     3 AC1 20 ILE A 162  ASP A 181  ILE A 182  LYS A 185                    
SITE     4 AC1 20 HIS A 210  VAL A 211  PRO A 212  SER A 216                    
SITE     5 AC1 20 THR A 217  ARG A 240  HOH A1616  HOH A1894                    
SITE     1 AC2 25 ILE B  84  PRO B 105  PHE B 106  ASN B 108                    
SITE     2 AC2 25 THR B 109  GLY B 158  TYR B 159  GLY B 160                    
SITE     3 AC2 25 HIS B 161  ILE B 162  ASP B 181  ILE B 182                    
SITE     4 AC2 25 LYS B 185  HIS B 210  VAL B 211  PRO B 212                    
SITE     5 AC2 25 SER B 216  THR B 217  SER B 239  HOH B1601                    
SITE     6 AC2 25 HOH B1671  HOH B1717  HOH B1871  HOH B1893                    
SITE     7 AC2 25 HOH B1958                                                     
SITE     1 AC3 22 PRO C 105  PHE C 106  ASN C 108  THR C 109                    
SITE     2 AC3 22 GLY C 158  TYR C 159  GLY C 160  HIS C 161                    
SITE     3 AC3 22 ILE C 162  ASP C 181  ILE C 182  LYS C 185                    
SITE     4 AC3 22 HIS C 210  VAL C 211  PRO C 212  SER C 216                    
SITE     5 AC3 22 THR C 217  HOH C1611  HOH C1637  HOH C1869                    
SITE     6 AC3 22 HOH C1900  HOH C1942                                          
SITE     1 AC4 22 PRO D 105  PHE D 106  ASN D 108  THR D 109                    
SITE     2 AC4 22 GLY D 158  TYR D 159  GLY D 160  HIS D 161                    
SITE     3 AC4 22 ILE D 162  TYR D 180  ASP D 181  ILE D 182                    
SITE     4 AC4 22 LYS D 185  HIS D 210  VAL D 211  PRO D 212                    
SITE     5 AC4 22 SER D 216  THR D 217  SER D 239  HOH D1600                    
SITE     6 AC4 22 HOH D1732  HOH D1943                                          
CRYST1   74.487   70.842  149.468  90.00  95.39  90.00 P 1 21 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      0.013425  0.000000  0.001266        0.00000                         
SCALE2      0.000000  0.014116  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006720        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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