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Database: PDB
Entry: 3CO8
LinkDB: 3CO8
Original site: 3CO8 
HEADER    ISOMERASE                               27-MAR-08   3CO8              
TITLE     CRYSTAL STRUCTURE OF ALANINE RACEMASE FROM OENOCOCCUS OENI            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALANINE RACEMASE;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 5.1.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: OENOCOCCUS OENI;                                
SOURCE   3 ORGANISM_TAXID: 203123;                                              
SOURCE   4 STRAIN: PSU-1;                                                       
SOURCE   5 ATCC: BAA-331;                                                       
SOURCE   6 GENE: OEOE_0162;                                                     
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: BC-PSGX(BC)                               
KEYWDS    ALANINE RACEMASE, PROTEIN STRUCTURE INITIATIVE II, PSI-II, NYSGXRC,   
KEYWDS   2 11082I, PLP, TIM BARREL, STRUCTURAL GENOMICS, NEW YORK SGX RESEARCH  
KEYWDS   3 CENTER FOR STRUCTURAL GENOMICS, ISOMERASE, PYRIDOXAL PHOSPHATE       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.PALANI,S.K.BURLEY,S.SWAMINATHAN,NEW YORK SGX RESEARCH CENTER FOR    
AUTHOR   2 STRUCTURAL GENOMICS (NYSGXRC)                                        
REVDAT   7   06-FEB-13 3CO8    1       JRNL                                     
REVDAT   6   09-JAN-13 3CO8    1       JRNL                                     
REVDAT   5   13-JUL-11 3CO8    1       VERSN                                    
REVDAT   4   09-JUN-09 3CO8    1       REVDAT                                   
REVDAT   3   24-FEB-09 3CO8    1       VERSN                                    
REVDAT   2   23-DEC-08 3CO8    1       AUTHOR KEYWDS                            
REVDAT   1   08-APR-08 3CO8    0                                                
JRNL        AUTH   K.PALANI,S.K.BURLEY,S.SWAMINATHAN                            
JRNL        TITL   STRUCTURE OF ALANINE RACEMASE FROM OENOCOCCUS OENI WITH      
JRNL        TITL 2 BOUND PYRIDOXAL 5'-PHOSPHATE.                                
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  69    15 2013              
JRNL        REFN                   ESSN 1744-3091                               
JRNL        PMID   23295479                                                     
JRNL        DOI    10.1107/S1744309112047276                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.08                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 197480.700                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 80948                          
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) : 0.247                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4092                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.81                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 11468                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2910                       
REMARK   3   BIN FREE R VALUE                    : 0.3040                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 615                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5548                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 626                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.38000                                             
REMARK   3    B22 (A**2) : 2.49000                                              
REMARK   3    B33 (A**2) : -2.12000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.80000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.15                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.26                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.18                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.48                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.39                                                 
REMARK   3   BSOL        : 10.00                                                
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  : PROTEIN.PARAM                                  
REMARK   3  PARAMETER FILE  2  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUES LISTED AS MISSING IN REMARK      
REMARK   3  465 ARE DUE TO LACK OF ELECTRON DENSITY. RESIDUES WITH MISSING      
REMARK   3  ATOMS LISTED IN REMARK 470 ARE DUE TO LACK OF ELECTRON DENSITY      
REMARK   3  FOR SIDE CHAINS AND MODELED AS ALANINES.                            
REMARK   4                                                                      
REMARK   4 3CO8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-APR-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB047014.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-MAR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97900                            
REMARK 200  MONOCHROMATOR                  : SI(III)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 80948                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.7000                            
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) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXD, SHARP, ARP/WARP                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM CHLORIDE, 0.1M BIS-TRIS,     
REMARK 280  25% PEG 3350, PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE    
REMARK 280  298.0K                                                              
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       49.81950            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MSE A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     SER A   169                                                      
REMARK 465     SER A   170                                                      
REMARK 465     ASP A   171                                                      
REMARK 465     ASN A   172                                                      
REMARK 465     PRO A   173                                                      
REMARK 465     ASP A   174                                                      
REMARK 465     ASP A   175                                                      
REMARK 465     HIS A   176                                                      
REMARK 465     TYR A   177                                                      
REMARK 465     ASP A   371                                                      
REMARK 465     GLU A   372                                                      
REMARK 465     GLY A   373                                                      
REMARK 465     HIS A   374                                                      
REMARK 465     HIS A   375                                                      
REMARK 465     HIS A   376                                                      
REMARK 465     HIS A   377                                                      
REMARK 465     HIS A   378                                                      
REMARK 465     HIS A   379                                                      
REMARK 465     MSE B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     LEU B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     ILE B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     ILE B   258                                                      
REMARK 465     PRO B   259                                                      
REMARK 465     ALA B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     GLU B   262                                                      
REMARK 465     GLY B   263                                                      
REMARK 465     ILE B   264                                                      
REMARK 465     SER B   265                                                      
REMARK 465     TYR B   266                                                      
REMARK 465     GLY B   267                                                      
REMARK 465     SER B   268                                                      
REMARK 465     LYS B   269                                                      
REMARK 465     PHE B   270                                                      
REMARK 465     VAL B   271                                                      
REMARK 465     THR B   272                                                      
REMARK 465     SER B   273                                                      
REMARK 465     ARG B   274                                                      
REMARK 465     ASP B   275                                                      
REMARK 465     THR B   276                                                      
REMARK 465     ASP B   371                                                      
REMARK 465     GLU B   372                                                      
REMARK 465     GLY B   373                                                      
REMARK 465     HIS B   374                                                      
REMARK 465     HIS B   375                                                      
REMARK 465     HIS B   376                                                      
REMARK 465     HIS B   377                                                      
REMARK 465     HIS B   378                                                      
REMARK 465     HIS B   379                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   448     O    HOH A   715              2.17            
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    LEU A 118   N   -  CA  -  C   ANGL. DEV. =  16.3 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    VAL A 200      -19.26   -142.44                                   
REMARK 500    LEU A 213       60.05   -118.81                                   
REMARK 500    SER A 265     -171.80     67.79                                   
REMARK 500    ASP A 295        4.39     80.08                                   
REMARK 500    SER A 336      112.74   -161.48                                   
REMARK 500    ARG B 135      -75.48   -104.26                                   
REMARK 500    SER B 169       51.77   -153.55                                   
REMARK 500    VAL B 200      -20.10   -142.91                                   
REMARK 500    CYS B 216       32.56   -141.32                                   
REMARK 500    ASP B 295        4.53     83.97                                   
REMARK 500    ASP B 314       16.16   -141.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LEU A 118        23.0      L          L   OUTSIDE RANGE           
REMARK 500    MSE B 201        25.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 677        DISTANCE =  5.81 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-11082I   RELATED DB: TARGETDB                    
DBREF  3CO8 A    3   371  UNP    Q04HB7   Q04HB7_OENOB     3    371             
DBREF  3CO8 B    3   371  UNP    Q04HB7   Q04HB7_OENOB     3    371             
SEQADV 3CO8 MSE A    0  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 SER A    1  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 LEU A    2  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 GLU A  372  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 GLY A  373  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 HIS A  374  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 HIS A  375  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 HIS A  376  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 HIS A  377  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 HIS A  378  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 HIS A  379  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 MSE B    0  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 SER B    1  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 LEU B    2  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 GLU B  372  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 GLY B  373  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 HIS B  374  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 HIS B  375  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 HIS B  376  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 HIS B  377  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 HIS B  378  UNP  Q04HB7              EXPRESSION TAG                 
SEQADV 3CO8 HIS B  379  UNP  Q04HB7              EXPRESSION TAG                 
SEQRES   1 A  380  MSE SER LEU GLU ALA ILE HIS ARG SER THR ARG ILE GLU          
SEQRES   2 A  380  PHE SER LYS SER SER LEU ALA TYR ASN VAL GLN TYR THR          
SEQRES   3 A  380  LYS GLN VAL SER GLY ALA LYS THR LEU TRP LEU ALA VAL          
SEQRES   4 A  380  LYS SER ASN ALA TYR GLY HIS GLY LEU LEU GLN VAL SER          
SEQRES   5 A  380  LYS ILE ALA ARG GLU CYS GLY VAL ASP GLY LEU ALA VAL          
SEQRES   6 A  380  SER VAL LEU ASP GLU GLY ILE ALA ILE ARG GLN ALA GLY          
SEQRES   7 A  380  ILE ASP ASP PHE ILE LEU ILE LEU GLY PRO ILE ASP VAL          
SEQRES   8 A  380  LYS TYR ALA PRO ILE ALA SER LYS TYR HIS PHE LEU THR          
SEQRES   9 A  380  THR VAL SER SER LEU ASP TRP LEU LYS SER ALA ASP LYS          
SEQRES  10 A  380  ILE LEU GLY LYS GLU LYS LEU SER VAL ASN LEU ALA VAL          
SEQRES  11 A  380  ASP THR GLY MSE ASN ARG ILE GLY VAL ARG SER LYS LYS          
SEQRES  12 A  380  ASP LEU LYS ASP GLU ILE GLU PHE LEU GLN GLU HIS SER          
SEQRES  13 A  380  ASP HIS PHE SER TYR ASP GLY ILE PHE THR HIS PHE ALA          
SEQRES  14 A  380  SER SER ASP ASN PRO ASP ASP HIS TYR PHE GLN ARG GLN          
SEQRES  15 A  380  LYS ASN ARG TRP TYR GLU LEU ILE ASP GLY LEU ILE MSE          
SEQRES  16 A  380  PRO ARG TYR VAL HIS VAL MSE ASN SER GLY ALA ALA MSE          
SEQRES  17 A  380  TYR HIS SER LYS GLU LEU PRO GLY CYS ASN SER ILE ALA          
SEQRES  18 A  380  ARG VAL GLY THR VAL VAL TYR GLY VAL GLU PRO SER GLU          
SEQRES  19 A  380  GLY VAL LEU GLY PRO ILE ASP LYS LEU LYS PRO VAL PHE          
SEQRES  20 A  380  GLU LEU LYS SER ALA LEU THR PHE VAL LYS LYS ILE PRO          
SEQRES  21 A  380  ALA GLY GLU GLY ILE SER TYR GLY SER LYS PHE VAL THR          
SEQRES  22 A  380  SER ARG ASP THR TRP ILE GLY THR LEU PRO ILE GLY TYR          
SEQRES  23 A  380  GLY ASP GLY TRP LEU ALA GLU TYR GLN ASP PHE GLN LEU          
SEQRES  24 A  380  LEU ILE ASP GLY GLN LYS CYS ARG GLN VAL GLY GLN ILE          
SEQRES  25 A  380  ALA MSE ASP GLN MSE MSE VAL ALA LEU PRO HIS GLU TYR          
SEQRES  26 A  380  PRO ILE GLY THR GLU VAL THR LEU ILE GLY LYS SER GLY          
SEQRES  27 A  380  LYS TYR GLU ASN THR LEU TYR ASP LEU HIS LYS HIS SER          
SEQRES  28 A  380  GLY VAL PRO PRO TRP LYS ILE THR VAL ALA PHE SER ASP          
SEQRES  29 A  380  ARG LEU LYS ARG MSE VAL VAL ASP GLU GLY HIS HIS HIS          
SEQRES  30 A  380  HIS HIS HIS                                                  
SEQRES   1 B  380  MSE SER LEU GLU ALA ILE HIS ARG SER THR ARG ILE GLU          
SEQRES   2 B  380  PHE SER LYS SER SER LEU ALA TYR ASN VAL GLN TYR THR          
SEQRES   3 B  380  LYS GLN VAL SER GLY ALA LYS THR LEU TRP LEU ALA VAL          
SEQRES   4 B  380  LYS SER ASN ALA TYR GLY HIS GLY LEU LEU GLN VAL SER          
SEQRES   5 B  380  LYS ILE ALA ARG GLU CYS GLY VAL ASP GLY LEU ALA VAL          
SEQRES   6 B  380  SER VAL LEU ASP GLU GLY ILE ALA ILE ARG GLN ALA GLY          
SEQRES   7 B  380  ILE ASP ASP PHE ILE LEU ILE LEU GLY PRO ILE ASP VAL          
SEQRES   8 B  380  LYS TYR ALA PRO ILE ALA SER LYS TYR HIS PHE LEU THR          
SEQRES   9 B  380  THR VAL SER SER LEU ASP TRP LEU LYS SER ALA ASP LYS          
SEQRES  10 B  380  ILE LEU GLY LYS GLU LYS LEU SER VAL ASN LEU ALA VAL          
SEQRES  11 B  380  ASP THR GLY MSE ASN ARG ILE GLY VAL ARG SER LYS LYS          
SEQRES  12 B  380  ASP LEU LYS ASP GLU ILE GLU PHE LEU GLN GLU HIS SER          
SEQRES  13 B  380  ASP HIS PHE SER TYR ASP GLY ILE PHE THR HIS PHE ALA          
SEQRES  14 B  380  SER SER ASP ASN PRO ASP ASP HIS TYR PHE GLN ARG GLN          
SEQRES  15 B  380  LYS ASN ARG TRP TYR GLU LEU ILE ASP GLY LEU ILE MSE          
SEQRES  16 B  380  PRO ARG TYR VAL HIS VAL MSE ASN SER GLY ALA ALA MSE          
SEQRES  17 B  380  TYR HIS SER LYS GLU LEU PRO GLY CYS ASN SER ILE ALA          
SEQRES  18 B  380  ARG VAL GLY THR VAL VAL TYR GLY VAL GLU PRO SER GLU          
SEQRES  19 B  380  GLY VAL LEU GLY PRO ILE ASP LYS LEU LYS PRO VAL PHE          
SEQRES  20 B  380  GLU LEU LYS SER ALA LEU THR PHE VAL LYS LYS ILE PRO          
SEQRES  21 B  380  ALA GLY GLU GLY ILE SER TYR GLY SER LYS PHE VAL THR          
SEQRES  22 B  380  SER ARG ASP THR TRP ILE GLY THR LEU PRO ILE GLY TYR          
SEQRES  23 B  380  GLY ASP GLY TRP LEU ALA GLU TYR GLN ASP PHE GLN LEU          
SEQRES  24 B  380  LEU ILE ASP GLY GLN LYS CYS ARG GLN VAL GLY GLN ILE          
SEQRES  25 B  380  ALA MSE ASP GLN MSE MSE VAL ALA LEU PRO HIS GLU TYR          
SEQRES  26 B  380  PRO ILE GLY THR GLU VAL THR LEU ILE GLY LYS SER GLY          
SEQRES  27 B  380  LYS TYR GLU ASN THR LEU TYR ASP LEU HIS LYS HIS SER          
SEQRES  28 B  380  GLY VAL PRO PRO TRP LYS ILE THR VAL ALA PHE SER ASP          
SEQRES  29 B  380  ARG LEU LYS ARG MSE VAL VAL ASP GLU GLY HIS HIS HIS          
SEQRES  30 B  380  HIS HIS HIS                                                  
MODRES 3CO8 MSE A  133  MET  SELENOMETHIONINE                                   
MODRES 3CO8 MSE A  194  MET  SELENOMETHIONINE                                   
MODRES 3CO8 MSE A  201  MET  SELENOMETHIONINE                                   
MODRES 3CO8 MSE A  207  MET  SELENOMETHIONINE                                   
MODRES 3CO8 MSE A  313  MET  SELENOMETHIONINE                                   
MODRES 3CO8 MSE A  316  MET  SELENOMETHIONINE                                   
MODRES 3CO8 MSE A  317  MET  SELENOMETHIONINE                                   
MODRES 3CO8 MSE A  368  MET  SELENOMETHIONINE                                   
MODRES 3CO8 MSE B  133  MET  SELENOMETHIONINE                                   
MODRES 3CO8 MSE B  194  MET  SELENOMETHIONINE                                   
MODRES 3CO8 MSE B  201  MET  SELENOMETHIONINE                                   
MODRES 3CO8 MSE B  207  MET  SELENOMETHIONINE                                   
MODRES 3CO8 MSE B  313  MET  SELENOMETHIONINE                                   
MODRES 3CO8 MSE B  316  MET  SELENOMETHIONINE                                   
MODRES 3CO8 MSE B  317  MET  SELENOMETHIONINE                                   
MODRES 3CO8 MSE B  368  MET  SELENOMETHIONINE                                   
HET    MSE  A 133       8                                                       
HET    MSE  A 194       8                                                       
HET    MSE  A 201       8                                                       
HET    MSE  A 207       8                                                       
HET    MSE  A 313       8                                                       
HET    MSE  A 316       8                                                       
HET    MSE  A 317       8                                                       
HET    MSE  A 368       8                                                       
HET    MSE  B 133       8                                                       
HET    MSE  B 194       8                                                       
HET    MSE  B 201       8                                                       
HET    MSE  B 207       8                                                       
HET    MSE  B 313       8                                                       
HET    MSE  B 316       8                                                       
HET    MSE  B 317       8                                                       
HET    MSE  B 368       8                                                       
HET    PLP  A 401      15                                                       
HET    PLP  B 401      15                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   1  MSE    16(C5 H11 N O2 SE)                                           
FORMUL   3  PLP    2(C8 H10 N O6 P)                                             
FORMUL   5  HOH   *626(H2 O)                                                    
HELIX    1   1 LYS A   15  GLY A   30  1                                  16    
HELIX    2   2 VAL A   38  GLY A   44  1                                   7    
HELIX    3   3 GLY A   46  ARG A   55  1                                  10    
HELIX    4   4 GLU A   56  GLY A   58  5                                   3    
HELIX    5   5 VAL A   66  ALA A   76  1                                  11    
HELIX    6   6 ASP A   89  LYS A   91  5                                   3    
HELIX    7   7 TYR A   92  TYR A   99  1                                   8    
HELIX    8   8 SER A  107  LEU A  118  1                                  12    
HELIX    9   9 SER A  140  HIS A  154  1                                  15    
HELIX   10  10 PHE A  178  ASP A  190  1                                  13    
HELIX   11  11 ASN A  202  HIS A  209  1                                   8    
HELIX   12  12 SER A  210  LEU A  213  5                                   4    
HELIX   13  13 PRO A  238  LEU A  242  5                                   5    
HELIX   14  14 SER A  265  LYS A  269  5                                   5    
HELIX   15  15 GLY A  284  GLY A  288  5                                   5    
HELIX   16  16 LEU A  290  GLN A  294  5                                   5    
HELIX   17  17 THR A  342  GLY A  351  1                                  10    
HELIX   18  18 PRO A  353  ALA A  360  1                                   8    
HELIX   19  19 LYS B   15  GLY B   30  1                                  16    
HELIX   20  20 VAL B   38  GLY B   44  1                                   7    
HELIX   21  21 GLY B   46  ALA B   54  1                                   9    
HELIX   22  22 VAL B   66  ALA B   76  1                                  11    
HELIX   23  23 ASP B   89  LYS B   91  5                                   3    
HELIX   24  24 TYR B   92  TYR B   99  1                                   8    
HELIX   25  25 SER B  107  LYS B  116  1                                  10    
HELIX   26  26 SER B  140  HIS B  154  1                                  15    
HELIX   27  27 ASP B  175  ASP B  190  1                                  16    
HELIX   28  28 ASN B  202  HIS B  209  1                                   8    
HELIX   29  29 SER B  210  LEU B  213  5                                   4    
HELIX   30  30 GLY B  284  GLY B  288  5                                   5    
HELIX   31  31 LEU B  290  GLN B  294  5                                   5    
HELIX   32  32 THR B  342  GLY B  351  1                                  10    
HELIX   33  33 PRO B  353  ALA B  360  1                                   8    
SHEET    1   A 5 TYR A 339  ASN A 341  0                                        
SHEET    2   A 5 GLU A 329  SER A 336 -1  N  GLY A 334   O  ASN A 341           
SHEET    3   A 5 PHE A 246  ALA A 251 -1  N  LEU A 248   O  LEU A 332           
SHEET    4   A 5 ARG A  10  SER A  14 -1  N  GLU A  12   O  GLU A 247           
SHEET    5   A 5 LYS A 366  VAL A 370  1  O  VAL A 370   N  PHE A  13           
SHEET    1   B 8 TYR A 197  HIS A 199  0                                        
SHEET    2   B 8 PHE A 158  PHE A 164  1  N  ASP A 161   O  TYR A 197           
SHEET    3   B 8 LEU A 123  ALA A 128  1  N  VAL A 125   O  SER A 159           
SHEET    4   B 8 LEU A 102  VAL A 105  1  N  THR A 103   O  SER A 124           
SHEET    5   B 8 ILE A  82  ILE A  84  1  N  ILE A  82   O  LEU A 102           
SHEET    6   B 8 GLY A  61  VAL A  64  1  N  VAL A  64   O  LEU A  83           
SHEET    7   B 8 THR A  33  ALA A  37  1  N  LEU A  36   O  ALA A  63           
SHEET    8   B 8 ILE A 219  VAL A 222  1  O  ALA A 220   N  TRP A  35           
SHEET    1   C 5 PHE A 254  ILE A 258  0                                        
SHEET    2   C 5 THR A 276  LEU A 281 -1  O  ILE A 278   N  LYS A 256           
SHEET    3   C 5 MSE A 316  LEU A 320 -1  O  MSE A 316   N  LEU A 281           
SHEET    4   C 5 GLN A 303  VAL A 308 -1  N  ARG A 306   O  ALA A 319           
SHEET    5   C 5 GLN A 297  ILE A 300 -1  N  LEU A 298   O  CYS A 305           
SHEET    1   D 2 GLY A 263  ILE A 264  0                                        
SHEET    2   D 2 PHE A 270  VAL A 271 -1  O  PHE A 270   N  ILE A 264           
SHEET    1   E 5 TYR B 339  ASN B 341  0                                        
SHEET    2   E 5 GLU B 329  SER B 336 -1  N  GLY B 334   O  ASN B 341           
SHEET    3   E 5 PHE B 246  ALA B 251 -1  N  LEU B 248   O  LEU B 332           
SHEET    4   E 5 ARG B  10  SER B  14 -1  N  ARG B  10   O  LYS B 249           
SHEET    5   E 5 LYS B 366  VAL B 370  1  O  VAL B 370   N  PHE B  13           
SHEET    1   F 8 TYR B 197  HIS B 199  0                                        
SHEET    2   F 8 PHE B 158  PHE B 164  1  N  ILE B 163   O  HIS B 199           
SHEET    3   F 8 LEU B 123  ALA B 128  1  N  VAL B 125   O  SER B 159           
SHEET    4   F 8 PHE B 101  VAL B 105  1  N  THR B 103   O  SER B 124           
SHEET    5   F 8 ILE B  82  ILE B  84  1  N  ILE B  82   O  LEU B 102           
SHEET    6   F 8 GLY B  61  VAL B  64  1  N  VAL B  64   O  LEU B  83           
SHEET    7   F 8 THR B  33  ALA B  37  1  N  LEU B  36   O  ALA B  63           
SHEET    8   F 8 ILE B 219  VAL B 222  1  O  ALA B 220   N  TRP B  35           
SHEET    1   G 4 PHE B 254  LYS B 256  0                                        
SHEET    2   G 4 ILE B 278  LEU B 281 -1  O  THR B 280   N  PHE B 254           
SHEET    3   G 4 MSE B 316  ALA B 319 -1  O  VAL B 318   N  GLY B 279           
SHEET    4   G 4 GLN B 307  VAL B 308 -1  N  VAL B 308   O  MSE B 317           
SHEET    1   H 2 LEU B 298  ILE B 300  0                                        
SHEET    2   H 2 GLN B 303  CYS B 305 -1  O  CYS B 305   N  LEU B 298           
LINK         C   GLY A 132                 N   MSE A 133     1555   1555  1.33  
LINK         C   MSE A 133                 N   ASN A 134     1555   1555  1.34  
LINK         C   ILE A 193                 N   MSE A 194     1555   1555  1.33  
LINK         C   MSE A 194                 N   PRO A 195     1555   1555  1.35  
LINK         C   VAL A 200                 N   MSE A 201     1555   1555  1.33  
LINK         C   MSE A 201                 N   ASN A 202     1555   1555  1.34  
LINK         C   ALA A 206                 N   MSE A 207     1555   1555  1.33  
LINK         C   MSE A 207                 N   TYR A 208     1555   1555  1.34  
LINK         C   ALA A 312                 N   MSE A 313     1555   1555  1.33  
LINK         C   MSE A 313                 N   ASP A 314     1555   1555  1.33  
LINK         C   GLN A 315                 N   MSE A 316     1555   1555  1.33  
LINK         C   MSE A 316                 N   MSE A 317     1555   1555  1.33  
LINK         C   MSE A 317                 N   VAL A 318     1555   1555  1.33  
LINK         C   ARG A 367                 N   MSE A 368     1555   1555  1.33  
LINK         C   MSE A 368                 N   VAL A 369     1555   1555  1.33  
LINK         C   GLY B 132                 N   MSE B 133     1555   1555  1.34  
LINK         C   MSE B 133                 N   ASN B 134     1555   1555  1.34  
LINK         C   ILE B 193                 N   MSE B 194     1555   1555  1.33  
LINK         C   MSE B 194                 N   PRO B 195     1555   1555  1.35  
LINK         C   VAL B 200                 N   MSE B 201     1555   1555  1.33  
LINK         C   MSE B 201                 N   ASN B 202     1555   1555  1.34  
LINK         C   ALA B 206                 N   MSE B 207     1555   1555  1.33  
LINK         C   MSE B 207                 N   TYR B 208     1555   1555  1.33  
LINK         C   ALA B 312                 N   MSE B 313     1555   1555  1.33  
LINK         C   MSE B 313                 N   ASP B 314     1555   1555  1.33  
LINK         C   GLN B 315                 N   MSE B 316     1555   1555  1.33  
LINK         C   MSE B 316                 N   MSE B 317     1555   1555  1.33  
LINK         C   MSE B 317                 N   VAL B 318     1555   1555  1.33  
LINK         C   ARG B 367                 N   MSE B 368     1555   1555  1.33  
LINK         C   MSE B 368                 N   VAL B 369     1555   1555  1.33  
LINK         NZ  LYS A  39                 C4A PLP A 401     1555   1555  1.34  
LINK         NZ  LYS B  39                 C4A PLP B 401     1555   1555  1.35  
SITE     1 AC1  8 LYS A  39  TYR A  43  LEU A  85  HIS A 166                    
SITE     2 AC1  8 SER A 203  ARG A 221  GLY A 223  THR A 224                    
SITE     1 AC2  8 LYS B  39  TYR B  43  ARG B 135  HIS B 166                    
SITE     2 AC2  8 SER B 203  ARG B 221  GLY B 223  THR B 224                    
CRYST1   47.397   99.639   84.670  90.00 103.26  90.00 P 1 21 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      0.021098  0.000000  0.004972        0.00000                         
SCALE2      0.000000  0.010036  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012134        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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