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Database: PDB
Entry: 3B8U
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Original site: 3B8U 
HEADER    ISOMERASE                               02-NOV-07   3B8U              
TITLE     CRYSTAL STRUCTURE OF ESCHERICHIA COLI ALAINE RACEMASE MUTANT E221A    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALANINE RACEMASE;                                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 5.1.1.1;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: JM109;                                                       
SOURCE   5 GENE: ALR;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    ALPHA/BETA BARREL, CELL SHAPE, CELL WALL BIOGENESIS/DEGRADATION,      
KEYWDS   2 ISOMERASE, PEPTIDOGLYCAN SYNTHESIS, PYRIDOXAL PHOSPHATE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.WU,T.HU,L.ZHANG,H.JIANG,X.SHEN                                      
REVDAT   3   13-JUL-11 3B8U    1       VERSN                                    
REVDAT   2   24-FEB-09 3B8U    1       VERSN                                    
REVDAT   1   08-JUL-08 3B8U    0                                                
JRNL        AUTH   D.WU,T.HU,L.ZHANG,J.CHEN,J.DU,J.DING,H.JIANG,X.SHEN          
JRNL        TITL   RESIDUES ASP164 AND GLU165 AT THE SUBSTRATE ENTRYWAY         
JRNL        TITL 2 FUNCTION POTENTLY IN SUBSTRATE ORIENTATION OF ALANINE        
JRNL        TITL 3 RACEMASE FROM E. COLI: ENZYMATIC CHARACTERIZATION WITH       
JRNL        TITL 4 CRYSTAL STRUCTURE ANALYSIS                                   
JRNL        REF    PROTEIN SCI.                  V.  17  1066 2008              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   18434499                                                     
JRNL        DOI    10.1110/PS.083495908                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 38.000                         
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 39281                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3736                            
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            : 10853                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 120                                     
REMARK   3   SOLVENT ATOMS            : 354                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.00900                                             
REMARK   3    B22 (A**2) : -1.00900                                             
REMARK   3    B33 (A**2) : 2.01800                                              
REMARK   3    B12 (A**2) : -5.88300                                             
REMARK   3    B13 (A**2) : 0.00000                                              
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 : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.960 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.628 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.402 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.212 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 32.07                                                
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_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NEW_PLP.PARAM                                  
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THIS IS A TWINNED STRUCTURE, THE DETWIN   
REMARK   3  FRACTION IS 0.400, AND OPERATOR IS 'H, -H-K, -L'.                   
REMARK   4                                                                      
REMARK   4 3B8U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-NOV-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB045223.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-SEP-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39617                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 164.399                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.16400                            
REMARK 200  R SYM                      (I) : 0.16400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.39100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 2RJG                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 1.6M AMMONIUM SULFATE,       
REMARK 280  PH7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z                                                
REMARK 290       6555   X-Y,X,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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.6 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     MET C   -19                                                      
REMARK 465     GLY C   -18                                                      
REMARK 465     SER C   -17                                                      
REMARK 465     SER C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     GLY C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     VAL C    -5                                                      
REMARK 465     PRO C    -4                                                      
REMARK 465     ARG C    -3                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLN C     2                                                      
REMARK 465     GLY C   326                                                      
REMARK 465     GLU C   327                                                      
REMARK 465     GLY C   328                                                      
REMARK 465     ALA C   335                                                      
REMARK 465     GLU C   336                                                      
REMARK 465     MET C   337                                                      
REMARK 465     THR C   338                                                      
REMARK 465     MET D   -19                                                      
REMARK 465     GLY D   -18                                                      
REMARK 465     SER D   -17                                                      
REMARK 465     SER D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     GLY D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     VAL D    -5                                                      
REMARK 465     PRO D    -4                                                      
REMARK 465     ARG D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLN D     2                                                      
REMARK 465     SER D   112                                                      
REMARK 465     ALA D   221                                                      
REMARK 465     ASP D   222                                                      
REMARK 465     ARG D   223                                                      
REMARK 465     ALA D   335                                                      
REMARK 465     GLU D   336                                                      
REMARK 465     MET D   337                                                      
REMARK 465     THR D   338                                                      
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   CE   LYS A    34     C4A  PLP A  1001              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS B 147   CB    CYS B 147   SG     -0.130                       
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    ARG A  11   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG A  11   NE  -  CZ  -  NH2 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG A 129   CD  -  NE  -  CZ  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ARG A 129   NE  -  CZ  -  NH1 ANGL. DEV. =  -9.9 DEGREES          
REMARK 500    ARG A 129   NE  -  CZ  -  NH2 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    PRO A 233   C   -  N   -  CD  ANGL. DEV. = -13.0 DEGREES          
REMARK 500    GLN A 315   N   -  CA  -  CB  ANGL. DEV. = -11.8 DEGREES          
REMARK 500    ARG B  11   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG B  11   NE  -  CZ  -  NH2 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG B  59   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG B  65   CD  -  NE  -  CZ  ANGL. DEV. =  10.4 DEGREES          
REMARK 500    ARG B  65   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    ARG B  65   NE  -  CZ  -  NH2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG B 129   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    PRO B 287   C   -  N   -  CD  ANGL. DEV. = -15.8 DEGREES          
REMARK 500    LEU B 289   CA  -  CB  -  CG  ANGL. DEV. =  13.8 DEGREES          
REMARK 500    ARG C  65   CD  -  NE  -  CZ  ANGL. DEV. =  10.6 DEGREES          
REMARK 500    ARG C  65   NE  -  CZ  -  NH1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG C  65   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ARG C  85   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG C  85   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG C 129   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ALA C 314   CB  -  CA  -  C   ANGL. DEV. = -13.7 DEGREES          
REMARK 500    GLN C 315   N   -  CA  -  CB  ANGL. DEV. = -19.6 DEGREES          
REMARK 500    ARG C 333   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG D  59   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG D  85   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG D  85   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG D 129   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG D 333   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG D 333   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 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    ALA A   3     -140.74    -85.84                                   
REMARK 500    LEU A  13      -72.79    -55.69                                   
REMARK 500    ARG A  14      -36.92    -14.93                                   
REMARK 500    LEU A  49       40.88   -157.56                                   
REMARK 500    PRO A  50       14.13    -52.14                                   
REMARK 500    GLU A  61      -25.10    -26.80                                   
REMARK 500    LEU A  66      -76.36    -70.02                                   
REMARK 500    ARG A  67      -50.05    -23.68                                   
REMARK 500    GLU A 102       49.01   -102.07                                   
REMARK 500    GLU A 103      -30.04   -146.21                                   
REMARK 500    ARG A 129      -73.56   -113.55                                   
REMARK 500    ARG A 162       45.93   -144.73                                   
REMARK 500    ILE A 191      -18.80   -159.80                                   
REMARK 500    ALA A 193     -154.82   -113.20                                   
REMARK 500    PHE A 205     -136.62     47.48                                   
REMARK 500    LEU A 214      -37.23    -36.61                                   
REMARK 500    ALA A 221       37.32    -84.32                                   
REMARK 500    ASP A 222     -157.28   -158.48                                   
REMARK 500    PRO A 233      101.20    -19.29                                   
REMARK 500    SER A 239     -157.83   -166.09                                   
REMARK 500    ALA A 243      145.12   -174.82                                   
REMARK 500    ASP A 304       23.49   -140.19                                   
REMARK 500    GLN A 313       42.55   -144.54                                   
REMARK 500    TRP A 325      148.85   -172.64                                   
REMARK 500    LYS A 339        9.66     88.19                                   
REMARK 500    ALA B   3     -154.07   -139.08                                   
REMARK 500    ALA B  54      170.10    179.09                                   
REMARK 500    GLU B  61      -31.70    -30.22                                   
REMARK 500    PRO B  74      143.30    -32.16                                   
REMARK 500    ARG B  85       16.39    -61.91                                   
REMARK 500    HIS B  94       41.19     72.56                                   
REMARK 500    ARG B 129      -72.38   -113.27                                   
REMARK 500    ALA B 139      -72.44    -91.07                                   
REMARK 500    PHE B 140      -57.86    -19.06                                   
REMARK 500    ARG B 162       58.49   -157.01                                   
REMARK 500    GLU B 183      111.49    -33.54                                   
REMARK 500    ILE B 191      -20.14   -140.43                                   
REMARK 500    ALA B 193     -155.13   -112.73                                   
REMARK 500    GLN B 202       33.29    -96.87                                   
REMARK 500    SER B 203       -7.63   -159.42                                   
REMARK 500    PHE B 205     -137.50     47.21                                   
REMARK 500    ALA B 221       41.02    -92.71                                   
REMARK 500    ARG B 223        5.24    101.64                                   
REMARK 500    SER B 239     -157.92   -164.97                                   
REMARK 500    ALA B 243      144.46   -175.03                                   
REMARK 500    THR B 286      151.55    -47.51                                   
REMARK 500    ASN B 291       40.10     76.88                                   
REMARK 500    GLN B 315       44.08   -107.80                                   
REMARK 500    ALA B 318      144.56    -34.82                                   
REMARK 500    LEU B 329       83.98   -177.38                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      73 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLN A    2     ALA A    3                  140.95                    
REMARK 500 ALA A    3     ALA A    4                 -134.74                    
REMARK 500 ILE A   71     THR A   72                 -146.22                    
REMARK 500 GLY A  187     GLN A  188                 -132.25                    
REMARK 500 SER A  190     ILE A  191                  149.95                    
REMARK 500 VAL A  253     GLY A  254                  141.03                    
REMARK 500 GLY B   39     HIS B   40                 -146.57                    
REMARK 500 ALA B   52     ASP B   53                 -142.75                    
REMARK 500 GLU B   61     GLU B   62                 -147.86                    
REMARK 500 ALA B  111     SER B  112                  149.95                    
REMARK 500 LYS B  173     GLN B  174                 -139.95                    
REMARK 500 ARG B  352     VAL B  353                  143.19                    
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    ASN A 101        23.7      L          L   OUTSIDE RANGE           
REMARK 500    THR B  72        24.7      L          L   OUTSIDE RANGE           
REMARK 500    MET B 305        24.8      L          L   OUTSIDE RANGE           
REMARK 500    GLN C 202        24.8      L          L   OUTSIDE RANGE           
REMARK 500    GLN C 315        46.8      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 A1088        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH A1092        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH B1009        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH B1058        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH B1085        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH B1104        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH B1105        DISTANCE =  6.72 ANGSTROMS                       
REMARK 525    HOH C1052        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH C1056        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH C1061        DISTANCE =  5.26 ANGSTROMS                       
REMARK 525    HOH D1002        DISTANCE =  6.74 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 360                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 361                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 360                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 361                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 362                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 360                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 361                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 360                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 361                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP C 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP D 1001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2RJG   RELATED DB: PDB                                   
REMARK 900 THE WILD-TYPE PROTEIN                                                
REMARK 900 RELATED ID: 2RJH   RELATED DB: PDB                                   
REMARK 900 THE WILD-TYPE PROTEIN COMPLEXED WITH D-CYCLOSERINE                   
REMARK 900 RELATED ID: 3B8T   RELATED DB: PDB                                   
REMARK 900 MUTANT P219A                                                         
REMARK 900 RELATED ID: 3B8V   RELATED DB: PDB                                   
REMARK 900 MUTANT E221K                                                         
REMARK 900 RELATED ID: 3B8W   RELATED DB: PDB                                   
REMARK 900 MUTANT E221P                                                         
DBREF  3B8U A    1   359  UNP    P0A6B4   ALR1_ECOLI       1    359             
DBREF  3B8U B    1   359  UNP    P0A6B4   ALR1_ECOLI       1    359             
DBREF  3B8U C    1   359  UNP    P0A6B4   ALR1_ECOLI       1    359             
DBREF  3B8U D    1   359  UNP    P0A6B4   ALR1_ECOLI       1    359             
SEQADV 3B8U MET A  -19  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U GLY A  -18  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER A  -17  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER A  -16  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS A  -15  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS A  -14  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS A  -13  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS A  -12  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS A  -11  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS A  -10  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER A   -9  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER A   -8  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U GLY A   -7  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U LEU A   -6  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U VAL A   -5  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U PRO A   -4  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U ARG A   -3  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U GLY A   -2  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER A   -1  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS A    0  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U ALA A  221  UNP  P0A6B4    GLU   221 ENGINEERED                     
SEQADV 3B8U MET B  -19  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U GLY B  -18  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER B  -17  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER B  -16  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS B  -15  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS B  -14  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS B  -13  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS B  -12  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS B  -11  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS B  -10  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER B   -9  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER B   -8  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U GLY B   -7  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U LEU B   -6  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U VAL B   -5  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U PRO B   -4  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U ARG B   -3  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U GLY B   -2  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER B   -1  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS B    0  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U ALA B  221  UNP  P0A6B4    GLU   221 ENGINEERED                     
SEQADV 3B8U MET C  -19  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U GLY C  -18  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER C  -17  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER C  -16  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS C  -15  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS C  -14  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS C  -13  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS C  -12  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS C  -11  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS C  -10  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER C   -9  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER C   -8  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U GLY C   -7  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U LEU C   -6  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U VAL C   -5  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U PRO C   -4  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U ARG C   -3  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U GLY C   -2  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER C   -1  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS C    0  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U ALA C  221  UNP  P0A6B4    GLU   221 ENGINEERED                     
SEQADV 3B8U MET D  -19  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U GLY D  -18  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER D  -17  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER D  -16  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS D  -15  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS D  -14  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS D  -13  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS D  -12  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS D  -11  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS D  -10  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER D   -9  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER D   -8  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U GLY D   -7  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U LEU D   -6  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U VAL D   -5  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U PRO D   -4  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U ARG D   -3  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U GLY D   -2  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U SER D   -1  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U HIS D    0  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 3B8U ALA D  221  UNP  P0A6B4    GLU   221 ENGINEERED                     
SEQRES   1 A  379  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  379  LEU VAL PRO ARG GLY SER HIS MET GLN ALA ALA THR VAL          
SEQRES   3 A  379  VAL ILE ASN ARG ARG ALA LEU ARG HIS ASN LEU GLN ARG          
SEQRES   4 A  379  LEU ARG GLU LEU ALA PRO ALA SER LYS MET VAL ALA VAL          
SEQRES   5 A  379  VAL LYS ALA ASN ALA TYR GLY HIS GLY LEU LEU GLU THR          
SEQRES   6 A  379  ALA ARG THR LEU PRO ASP ALA ASP ALA PHE GLY VAL ALA          
SEQRES   7 A  379  ARG LEU GLU GLU ALA LEU ARG LEU ARG ALA GLY GLY ILE          
SEQRES   8 A  379  THR LYS PRO VAL LEU LEU LEU GLU GLY PHE PHE ASP ALA          
SEQRES   9 A  379  ARG ASP LEU PRO THR ILE SER ALA GLN HIS PHE HIS THR          
SEQRES  10 A  379  ALA VAL HIS ASN GLU GLU GLN LEU ALA ALA LEU GLU GLU          
SEQRES  11 A  379  ALA SER LEU ASP GLU PRO VAL THR VAL TRP MET KCX LEU          
SEQRES  12 A  379  ASP THR GLY MET HIS ARG LEU GLY VAL ARG PRO GLU GLN          
SEQRES  13 A  379  ALA GLU ALA PHE TYR HIS ARG LEU THR GLN CYS LYS ASN          
SEQRES  14 A  379  VAL ARG GLN PRO VAL ASN ILE VAL SER HIS PHE ALA ARG          
SEQRES  15 A  379  ALA ASP GLU PRO LYS CYS GLY ALA THR GLU LYS GLN LEU          
SEQRES  16 A  379  ALA ILE PHE ASN THR PHE CYS GLU GLY LYS PRO GLY GLN          
SEQRES  17 A  379  ARG SER ILE ALA ALA SER GLY GLY ILE LEU LEU TRP PRO          
SEQRES  18 A  379  GLN SER HIS PHE ASP TRP VAL ARG PRO GLY ILE ILE LEU          
SEQRES  19 A  379  TYR GLY VAL SER PRO LEU ALA ASP ARG SER THR GLY ALA          
SEQRES  20 A  379  ASP PHE GLY CYS GLN PRO VAL MET SER LEU THR SER SER          
SEQRES  21 A  379  LEU ILE ALA VAL ARG GLU HIS LYS ALA GLY GLU PRO VAL          
SEQRES  22 A  379  GLY TYR GLY GLY THR TRP VAL SER GLU ARG ASP THR ARG          
SEQRES  23 A  379  LEU GLY VAL VAL ALA MET GLY TYR GLY ASP GLY TYR PRO          
SEQRES  24 A  379  ARG ALA ALA PRO SER GLY THR PRO VAL LEU VAL ASN GLY          
SEQRES  25 A  379  ARG GLU VAL PRO ILE VAL GLY ARG VAL ALA MET ASP MET          
SEQRES  26 A  379  ILE CYS VAL ASP LEU GLY PRO GLN ALA GLN ASP LYS ALA          
SEQRES  27 A  379  GLY ASP PRO VAL ILE LEU TRP GLY GLU GLY LEU PRO VAL          
SEQRES  28 A  379  GLU ARG ILE ALA GLU MET THR LYS VAL SER ALA TYR GLU          
SEQRES  29 A  379  LEU ILE THR ARG LEU THR SER ARG VAL ALA MET LYS TYR          
SEQRES  30 A  379  VAL ASP                                                      
SEQRES   1 B  379  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  379  LEU VAL PRO ARG GLY SER HIS MET GLN ALA ALA THR VAL          
SEQRES   3 B  379  VAL ILE ASN ARG ARG ALA LEU ARG HIS ASN LEU GLN ARG          
SEQRES   4 B  379  LEU ARG GLU LEU ALA PRO ALA SER LYS MET VAL ALA VAL          
SEQRES   5 B  379  VAL LYS ALA ASN ALA TYR GLY HIS GLY LEU LEU GLU THR          
SEQRES   6 B  379  ALA ARG THR LEU PRO ASP ALA ASP ALA PHE GLY VAL ALA          
SEQRES   7 B  379  ARG LEU GLU GLU ALA LEU ARG LEU ARG ALA GLY GLY ILE          
SEQRES   8 B  379  THR LYS PRO VAL LEU LEU LEU GLU GLY PHE PHE ASP ALA          
SEQRES   9 B  379  ARG ASP LEU PRO THR ILE SER ALA GLN HIS PHE HIS THR          
SEQRES  10 B  379  ALA VAL HIS ASN GLU GLU GLN LEU ALA ALA LEU GLU GLU          
SEQRES  11 B  379  ALA SER LEU ASP GLU PRO VAL THR VAL TRP MET KCX LEU          
SEQRES  12 B  379  ASP THR GLY MET HIS ARG LEU GLY VAL ARG PRO GLU GLN          
SEQRES  13 B  379  ALA GLU ALA PHE TYR HIS ARG LEU THR GLN CYS LYS ASN          
SEQRES  14 B  379  VAL ARG GLN PRO VAL ASN ILE VAL SER HIS PHE ALA ARG          
SEQRES  15 B  379  ALA ASP GLU PRO LYS CYS GLY ALA THR GLU LYS GLN LEU          
SEQRES  16 B  379  ALA ILE PHE ASN THR PHE CYS GLU GLY LYS PRO GLY GLN          
SEQRES  17 B  379  ARG SER ILE ALA ALA SER GLY GLY ILE LEU LEU TRP PRO          
SEQRES  18 B  379  GLN SER HIS PHE ASP TRP VAL ARG PRO GLY ILE ILE LEU          
SEQRES  19 B  379  TYR GLY VAL SER PRO LEU ALA ASP ARG SER THR GLY ALA          
SEQRES  20 B  379  ASP PHE GLY CYS GLN PRO VAL MET SER LEU THR SER SER          
SEQRES  21 B  379  LEU ILE ALA VAL ARG GLU HIS LYS ALA GLY GLU PRO VAL          
SEQRES  22 B  379  GLY TYR GLY GLY THR TRP VAL SER GLU ARG ASP THR ARG          
SEQRES  23 B  379  LEU GLY VAL VAL ALA MET GLY TYR GLY ASP GLY TYR PRO          
SEQRES  24 B  379  ARG ALA ALA PRO SER GLY THR PRO VAL LEU VAL ASN GLY          
SEQRES  25 B  379  ARG GLU VAL PRO ILE VAL GLY ARG VAL ALA MET ASP MET          
SEQRES  26 B  379  ILE CYS VAL ASP LEU GLY PRO GLN ALA GLN ASP LYS ALA          
SEQRES  27 B  379  GLY ASP PRO VAL ILE LEU TRP GLY GLU GLY LEU PRO VAL          
SEQRES  28 B  379  GLU ARG ILE ALA GLU MET THR LYS VAL SER ALA TYR GLU          
SEQRES  29 B  379  LEU ILE THR ARG LEU THR SER ARG VAL ALA MET LYS TYR          
SEQRES  30 B  379  VAL ASP                                                      
SEQRES   1 C  379  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  379  LEU VAL PRO ARG GLY SER HIS MET GLN ALA ALA THR VAL          
SEQRES   3 C  379  VAL ILE ASN ARG ARG ALA LEU ARG HIS ASN LEU GLN ARG          
SEQRES   4 C  379  LEU ARG GLU LEU ALA PRO ALA SER LYS MET VAL ALA VAL          
SEQRES   5 C  379  VAL LYS ALA ASN ALA TYR GLY HIS GLY LEU LEU GLU THR          
SEQRES   6 C  379  ALA ARG THR LEU PRO ASP ALA ASP ALA PHE GLY VAL ALA          
SEQRES   7 C  379  ARG LEU GLU GLU ALA LEU ARG LEU ARG ALA GLY GLY ILE          
SEQRES   8 C  379  THR LYS PRO VAL LEU LEU LEU GLU GLY PHE PHE ASP ALA          
SEQRES   9 C  379  ARG ASP LEU PRO THR ILE SER ALA GLN HIS PHE HIS THR          
SEQRES  10 C  379  ALA VAL HIS ASN GLU GLU GLN LEU ALA ALA LEU GLU GLU          
SEQRES  11 C  379  ALA SER LEU ASP GLU PRO VAL THR VAL TRP MET KCX LEU          
SEQRES  12 C  379  ASP THR GLY MET HIS ARG LEU GLY VAL ARG PRO GLU GLN          
SEQRES  13 C  379  ALA GLU ALA PHE TYR HIS ARG LEU THR GLN CYS LYS ASN          
SEQRES  14 C  379  VAL ARG GLN PRO VAL ASN ILE VAL SER HIS PHE ALA ARG          
SEQRES  15 C  379  ALA ASP GLU PRO LYS CYS GLY ALA THR GLU LYS GLN LEU          
SEQRES  16 C  379  ALA ILE PHE ASN THR PHE CYS GLU GLY LYS PRO GLY GLN          
SEQRES  17 C  379  ARG SER ILE ALA ALA SER GLY GLY ILE LEU LEU TRP PRO          
SEQRES  18 C  379  GLN SER HIS PHE ASP TRP VAL ARG PRO GLY ILE ILE LEU          
SEQRES  19 C  379  TYR GLY VAL SER PRO LEU ALA ASP ARG SER THR GLY ALA          
SEQRES  20 C  379  ASP PHE GLY CYS GLN PRO VAL MET SER LEU THR SER SER          
SEQRES  21 C  379  LEU ILE ALA VAL ARG GLU HIS LYS ALA GLY GLU PRO VAL          
SEQRES  22 C  379  GLY TYR GLY GLY THR TRP VAL SER GLU ARG ASP THR ARG          
SEQRES  23 C  379  LEU GLY VAL VAL ALA MET GLY TYR GLY ASP GLY TYR PRO          
SEQRES  24 C  379  ARG ALA ALA PRO SER GLY THR PRO VAL LEU VAL ASN GLY          
SEQRES  25 C  379  ARG GLU VAL PRO ILE VAL GLY ARG VAL ALA MET ASP MET          
SEQRES  26 C  379  ILE CYS VAL ASP LEU GLY PRO GLN ALA GLN ASP LYS ALA          
SEQRES  27 C  379  GLY ASP PRO VAL ILE LEU TRP GLY GLU GLY LEU PRO VAL          
SEQRES  28 C  379  GLU ARG ILE ALA GLU MET THR LYS VAL SER ALA TYR GLU          
SEQRES  29 C  379  LEU ILE THR ARG LEU THR SER ARG VAL ALA MET LYS TYR          
SEQRES  30 C  379  VAL ASP                                                      
SEQRES   1 D  379  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  379  LEU VAL PRO ARG GLY SER HIS MET GLN ALA ALA THR VAL          
SEQRES   3 D  379  VAL ILE ASN ARG ARG ALA LEU ARG HIS ASN LEU GLN ARG          
SEQRES   4 D  379  LEU ARG GLU LEU ALA PRO ALA SER LYS MET VAL ALA VAL          
SEQRES   5 D  379  VAL LYS ALA ASN ALA TYR GLY HIS GLY LEU LEU GLU THR          
SEQRES   6 D  379  ALA ARG THR LEU PRO ASP ALA ASP ALA PHE GLY VAL ALA          
SEQRES   7 D  379  ARG LEU GLU GLU ALA LEU ARG LEU ARG ALA GLY GLY ILE          
SEQRES   8 D  379  THR LYS PRO VAL LEU LEU LEU GLU GLY PHE PHE ASP ALA          
SEQRES   9 D  379  ARG ASP LEU PRO THR ILE SER ALA GLN HIS PHE HIS THR          
SEQRES  10 D  379  ALA VAL HIS ASN GLU GLU GLN LEU ALA ALA LEU GLU GLU          
SEQRES  11 D  379  ALA SER LEU ASP GLU PRO VAL THR VAL TRP MET KCX LEU          
SEQRES  12 D  379  ASP THR GLY MET HIS ARG LEU GLY VAL ARG PRO GLU GLN          
SEQRES  13 D  379  ALA GLU ALA PHE TYR HIS ARG LEU THR GLN CYS LYS ASN          
SEQRES  14 D  379  VAL ARG GLN PRO VAL ASN ILE VAL SER HIS PHE ALA ARG          
SEQRES  15 D  379  ALA ASP GLU PRO LYS CYS GLY ALA THR GLU LYS GLN LEU          
SEQRES  16 D  379  ALA ILE PHE ASN THR PHE CYS GLU GLY LYS PRO GLY GLN          
SEQRES  17 D  379  ARG SER ILE ALA ALA SER GLY GLY ILE LEU LEU TRP PRO          
SEQRES  18 D  379  GLN SER HIS PHE ASP TRP VAL ARG PRO GLY ILE ILE LEU          
SEQRES  19 D  379  TYR GLY VAL SER PRO LEU ALA ASP ARG SER THR GLY ALA          
SEQRES  20 D  379  ASP PHE GLY CYS GLN PRO VAL MET SER LEU THR SER SER          
SEQRES  21 D  379  LEU ILE ALA VAL ARG GLU HIS LYS ALA GLY GLU PRO VAL          
SEQRES  22 D  379  GLY TYR GLY GLY THR TRP VAL SER GLU ARG ASP THR ARG          
SEQRES  23 D  379  LEU GLY VAL VAL ALA MET GLY TYR GLY ASP GLY TYR PRO          
SEQRES  24 D  379  ARG ALA ALA PRO SER GLY THR PRO VAL LEU VAL ASN GLY          
SEQRES  25 D  379  ARG GLU VAL PRO ILE VAL GLY ARG VAL ALA MET ASP MET          
SEQRES  26 D  379  ILE CYS VAL ASP LEU GLY PRO GLN ALA GLN ASP LYS ALA          
SEQRES  27 D  379  GLY ASP PRO VAL ILE LEU TRP GLY GLU GLY LEU PRO VAL          
SEQRES  28 D  379  GLU ARG ILE ALA GLU MET THR LYS VAL SER ALA TYR GLU          
SEQRES  29 D  379  LEU ILE THR ARG LEU THR SER ARG VAL ALA MET LYS TYR          
SEQRES  30 D  379  VAL ASP                                                      
MODRES 3B8U KCX A  122  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3B8U KCX B  122  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3B8U KCX C  122  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3B8U KCX D  122  LYS  LYSINE NZ-CARBOXYLIC ACID                          
HET    KCX  A 122      12                                                       
HET    KCX  B 122      12                                                       
HET    KCX  C 122      12                                                       
HET    KCX  D 122      12                                                       
HET    SO4  A 360       5                                                       
HET    SO4  A 361       5                                                       
HET    SO4  A 362       5                                                       
HET    SO4  B 360       5                                                       
HET    SO4  B 361       5                                                       
HET    SO4  B 362       5                                                       
HET    SO4  C 360       5                                                       
HET    SO4  C 361       5                                                       
HET    SO4  C 362       5                                                       
HET    SO4  D 360       5                                                       
HET    SO4  D 361       5                                                       
HET    SO4  D 362       5                                                       
HET    PLP  A1001      15                                                       
HET    PLP  B1001      15                                                       
HET    PLP  C1001      15                                                       
HET    PLP  D1001      15                                                       
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   1  KCX    4(C7 H14 N2 O4)                                              
FORMUL   5  SO4    12(O4 S 2-)                                                  
FORMUL  17  PLP    4(C8 H10 N O6 P)                                             
FORMUL  21  HOH   *354(H2 O)                                                    
HELIX    1   1 ARG A   10  ALA A   24  1                                  15    
HELIX    2   2 VAL A   33  GLY A   39  1                                   7    
HELIX    3   3 GLY A   41  THR A   48  1                                   8    
HELIX    4   4 ARG A   59  GLY A   69  1                                  11    
HELIX    5   5 ASP A   83  ARG A   85  5                                   3    
HELIX    6   6 ASP A   86  GLN A   93  1                                   8    
HELIX    7   7 GLN A  104  GLU A  109  1                                   6    
HELIX    8   8 ARG A  133  GLU A  135  5                                   3    
HELIX    9   9 GLN A  136  THR A  145  1                                  10    
HELIX   10  10 GLY A  169  CYS A  182  1                                  14    
HELIX   11  11 ALA A  193  TRP A  200  1                                   8    
HELIX   12  12 PRO A  201  HIS A  204  5                                   4    
HELIX   13  13 GLY A  211  GLY A  216  5                                   6    
HELIX   14  14 THR A  225  GLY A  230  5                                   6    
HELIX   15  15 GLY A  254  THR A  258  5                                   5    
HELIX   16  16 PRO A  330  LYS A  339  1                                  10    
HELIX   17  17 SER A  341  ARG A  348  1                                   8    
HELIX   18  18 ARG B   10  ALA B   24  1                                  15    
HELIX   19  19 VAL B   33  HIS B   40  1                                   8    
HELIX   20  20 ARG B   59  GLY B   69  1                                  11    
HELIX   21  21 ASP B   83  ARG B   85  5                                   3    
HELIX   22  22 ASP B   86  HIS B   94  1                                   9    
HELIX   23  23 ASN B  101  ALA B  111  1                                  11    
HELIX   24  24 ARG B  133  GLU B  135  5                                   3    
HELIX   25  25 GLN B  136  THR B  145  1                                  10    
HELIX   26  26 ALA B  170  GLU B  172  5                                   3    
HELIX   27  27 LYS B  173  GLU B  183  1                                  11    
HELIX   28  28 ALA B  193  TRP B  200  1                                   8    
HELIX   29  29 PRO B  201  HIS B  204  5                                   4    
HELIX   30  30 GLY B  211  GLY B  216  5                                   6    
HELIX   31  31 GLY B  226  GLY B  230  5                                   5    
HELIX   32  32 PRO B  330  LYS B  339  1                                  10    
HELIX   33  33 SER B  341  ARG B  348  1                                   8    
HELIX   34  34 ARG C   10  ALA C   24  1                                  15    
HELIX   35  35 VAL C   33  HIS C   40  1                                   8    
HELIX   36  36 GLY C   41  THR C   48  1                                   8    
HELIX   37  37 ARG C   59  GLY C   69  1                                  11    
HELIX   38  38 ASP C   83  ARG C   85  5                                   3    
HELIX   39  39 ASP C   86  GLN C   93  1                                   8    
HELIX   40  40 ASN C  101  ALA C  111  1                                  11    
HELIX   41  41 ARG C  133  GLN C  146  1                                  14    
HELIX   42  42 GLY C  169  GLU C  183  1                                  15    
HELIX   43  43 ALA C  193  TRP C  200  1                                   8    
HELIX   44  44 PRO C  201  HIS C  204  5                                   4    
HELIX   45  45 GLY C  211  GLY C  216  5                                   6    
HELIX   46  46 THR C  225  PHE C  229  5                                   5    
HELIX   47  47 GLY C  254  THR C  258  5                                   5    
HELIX   48  48 SER C  341  ARG C  348  1                                   8    
HELIX   49  49 ARG D   10  ALA D   24  1                                  15    
HELIX   50  50 VAL D   33  HIS D   40  1                                   8    
HELIX   51  51 GLY D   41  LEU D   49  1                                   9    
HELIX   52  52 ARG D   59  GLY D   69  1                                  11    
HELIX   53  53 ASP D   83  ARG D   85  5                                   3    
HELIX   54  54 ASP D   86  GLN D   93  1                                   8    
HELIX   55  55 ASN D  101  ALA D  111  1                                  11    
HELIX   56  56 ARG D  133  THR D  145  1                                  13    
HELIX   57  57 GLY D  169  GLU D  183  1                                  15    
HELIX   58  58 ALA D  193  TRP D  200  1                                   8    
HELIX   59  59 PRO D  201  HIS D  204  5                                   4    
HELIX   60  60 GLY D  211  GLY D  216  5                                   6    
HELIX   61  61 THR D  225  GLY D  230  5                                   6    
HELIX   62  62 GLY D  254  THR D  258  5                                   5    
HELIX   63  63 SER D  341  ARG D  348  1                                   8    
SHEET    1   A 6 ARG A 293  PRO A 296  0                                        
SHEET    2   A 6 PRO A 287  VAL A 290 -1  N  VAL A 288   O  VAL A 295           
SHEET    3   A 6 PRO A 321  TRP A 325 -1  O  ILE A 323   N  LEU A 289           
SHEET    4   A 6 MET A 235  HIS A 247 -1  N  LEU A 237   O  LEU A 324           
SHEET    5   A 6 THR A 265  VAL A 270 -1  O  VAL A 269   N  ILE A 242           
SHEET    6   A 6 ILE A 306  ASP A 309 -1  O  ILE A 306   N  VAL A 270           
SHEET    1   B 6 ARG A 293  PRO A 296  0                                        
SHEET    2   B 6 PRO A 287  VAL A 290 -1  N  VAL A 288   O  VAL A 295           
SHEET    3   B 6 PRO A 321  TRP A 325 -1  O  ILE A 323   N  LEU A 289           
SHEET    4   B 6 MET A 235  HIS A 247 -1  N  LEU A 237   O  LEU A 324           
SHEET    5   B 6 THR A   5  ASN A   9 -1  N  THR A   5   O  THR A 238           
SHEET    6   B 6 ALA A 354  VAL A 358  1  O  LYS A 356   N  ILE A   8           
SHEET    1   C 7 VAL A 150  VAL A 157  0                                        
SHEET    2   C 7 VAL A 117  KCX A 122  1  N  VAL A 117   O  ARG A 151           
SHEET    3   C 7 PHE A  95  VAL A  99  1  N  THR A  97   O  TRP A 120           
SHEET    4   C 7 VAL A  75  LEU A  77  1  N  LEU A  77   O  HIS A  96           
SHEET    5   C 7 ALA A  54  VAL A  57  1  N  PHE A  55   O  LEU A  76           
SHEET    6   C 7 LYS A  28  VAL A  32  1  N  ALA A  31   O  GLY A  56           
SHEET    7   C 7 TRP A 207  VAL A 208  1  O  VAL A 208   N  LYS A  28           
SHEET    1   D 6 GLU B 294  PRO B 296  0                                        
SHEET    2   D 6 PRO B 287  VAL B 290 -1  N  VAL B 288   O  VAL B 295           
SHEET    3   D 6 PRO B 321  TRP B 325 -1  O  ILE B 323   N  LEU B 289           
SHEET    4   D 6 MET B 235  HIS B 247 -1  N  LEU B 237   O  LEU B 324           
SHEET    5   D 6 THR B 265  VAL B 270 -1  O  VAL B 269   N  ILE B 242           
SHEET    6   D 6 ILE B 306  ASP B 309 -1  O  ILE B 306   N  VAL B 270           
SHEET    1   E 6 GLU B 294  PRO B 296  0                                        
SHEET    2   E 6 PRO B 287  VAL B 290 -1  N  VAL B 288   O  VAL B 295           
SHEET    3   E 6 PRO B 321  TRP B 325 -1  O  ILE B 323   N  LEU B 289           
SHEET    4   E 6 MET B 235  HIS B 247 -1  N  LEU B 237   O  LEU B 324           
SHEET    5   E 6 THR B   5  ASN B   9 -1  N  THR B   5   O  THR B 238           
SHEET    6   E 6 ALA B 354  VAL B 358  1  O  LYS B 356   N  ILE B   8           
SHEET    1   F 8 ARG B 189  SER B 190  0                                        
SHEET    2   F 8 ASN B 155  VAL B 157  1  N  ILE B 156   O  SER B 190           
SHEET    3   F 8 VAL B 119  KCX B 122  1  N  MET B 121   O  ASN B 155           
SHEET    4   F 8 PHE B  95  VAL B  99  1  N  THR B  97   O  TRP B 120           
SHEET    5   F 8 VAL B  75  LEU B  77  1  N  VAL B  75   O  HIS B  96           
SHEET    6   F 8 ALA B  54  VAL B  57  1  N  PHE B  55   O  LEU B  76           
SHEET    7   F 8 LYS B  28  VAL B  32  1  N  ALA B  31   O  GLY B  56           
SHEET    8   F 8 TRP B 207  VAL B 208  1  O  VAL B 208   N  LYS B  28           
SHEET    1   G 2 PRO B 252  VAL B 253  0                                        
SHEET    2   G 2 TRP B 259  VAL B 260 -1  N  TRP B 259   O  VAL B 253           
SHEET    1   H 6 ARG C 293  PRO C 296  0                                        
SHEET    2   H 6 PRO C 287  VAL C 290 -1  N  VAL C 288   O  VAL C 295           
SHEET    3   H 6 PRO C 321  TRP C 325 -1  O  ILE C 323   N  LEU C 289           
SHEET    4   H 6 MET C 235  HIS C 247 -1  N  SER C 239   O  VAL C 322           
SHEET    5   H 6 THR C 265  VAL C 270 -1  O  VAL C 269   N  ILE C 242           
SHEET    6   H 6 ILE C 306  ASP C 309 -1  O  ILE C 306   N  VAL C 270           
SHEET    1   I 6 ARG C 293  PRO C 296  0                                        
SHEET    2   I 6 PRO C 287  VAL C 290 -1  N  VAL C 288   O  VAL C 295           
SHEET    3   I 6 PRO C 321  TRP C 325 -1  O  ILE C 323   N  LEU C 289           
SHEET    4   I 6 MET C 235  HIS C 247 -1  N  SER C 239   O  VAL C 322           
SHEET    5   I 6 THR C   5  ASN C   9 -1  N  THR C   5   O  THR C 238           
SHEET    6   I 6 ALA C 354  VAL C 358  1  O  LYS C 356   N  ILE C   8           
SHEET    1   J 8 ARG C 189  SER C 190  0                                        
SHEET    2   J 8 ASN C 155  VAL C 157  1  N  ILE C 156   O  SER C 190           
SHEET    3   J 8 VAL C 119  KCX C 122  1  N  MET C 121   O  ASN C 155           
SHEET    4   J 8 PHE C  95  VAL C  99  1  N  THR C  97   O  TRP C 120           
SHEET    5   J 8 VAL C  75  LEU C  77  1  N  LEU C  77   O  HIS C  96           
SHEET    6   J 8 ALA C  54  VAL C  57  1  N  PHE C  55   O  LEU C  76           
SHEET    7   J 8 LYS C  28  VAL C  32  1  N  ALA C  31   O  ALA C  54           
SHEET    8   J 8 TRP C 207  VAL C 208  1  O  VAL C 208   N  LYS C  28           
SHEET    1   K 2 PRO C 252  VAL C 253  0                                        
SHEET    2   K 2 TRP C 259  VAL C 260 -1  O  TRP C 259   N  VAL C 253           
SHEET    1   L 6 ARG D 293  PRO D 296  0                                        
SHEET    2   L 6 PRO D 287  VAL D 290 -1  N  VAL D 290   O  ARG D 293           
SHEET    3   L 6 PRO D 321  TRP D 325 -1  O  ILE D 323   N  LEU D 289           
SHEET    4   L 6 MET D 235  HIS D 247 -1  N  LEU D 237   O  LEU D 324           
SHEET    5   L 6 THR D 265  VAL D 270 -1  O  VAL D 269   N  ILE D 242           
SHEET    6   L 6 ILE D 306  ASP D 309 -1  O  ILE D 306   N  VAL D 270           
SHEET    1   M 6 ARG D 293  PRO D 296  0                                        
SHEET    2   M 6 PRO D 287  VAL D 290 -1  N  VAL D 290   O  ARG D 293           
SHEET    3   M 6 PRO D 321  TRP D 325 -1  O  ILE D 323   N  LEU D 289           
SHEET    4   M 6 MET D 235  HIS D 247 -1  N  LEU D 237   O  LEU D 324           
SHEET    5   M 6 THR D   5  ASN D   9 -1  N  THR D   5   O  THR D 238           
SHEET    6   M 6 ALA D 354  VAL D 358  1  O  LYS D 356   N  VAL D   6           
SHEET    1   N 8 ARG D 189  SER D 190  0                                        
SHEET    2   N 8 ASN D 155  VAL D 157  1  N  ILE D 156   O  SER D 190           
SHEET    3   N 8 VAL D 119  KCX D 122  1  N  MET D 121   O  ASN D 155           
SHEET    4   N 8 PHE D  95  VAL D  99  1  N  THR D  97   O  TRP D 120           
SHEET    5   N 8 VAL D  75  LEU D  77  1  N  LEU D  77   O  HIS D  96           
SHEET    6   N 8 ALA D  54  VAL D  57  1  N  PHE D  55   O  LEU D  76           
SHEET    7   N 8 LYS D  28  VAL D  32  1  N  ALA D  31   O  GLY D  56           
SHEET    8   N 8 TRP D 207  VAL D 208  1  O  VAL D 208   N  LYS D  28           
SHEET    1   O 2 PRO D 252  VAL D 253  0                                        
SHEET    2   O 2 TRP D 259  VAL D 260 -1  O  TRP D 259   N  VAL D 253           
LINK         C4A PLP A1001                 NZ  LYS A  34     1555   1555  1.27  
LINK         C4A PLP B1001                 NZ  LYS B  34     1555   1555  1.29  
LINK         C4A PLP C1001                 NZ  LYS C  34     1555   1555  1.29  
LINK         C4A PLP D1001                 NZ  LYS D  34     1555   1555  1.30  
LINK         C   MET A 121                 N   KCX A 122     1555   1555  1.33  
LINK         C   KCX A 122                 N   LEU A 123     1555   1555  1.32  
LINK         C   MET B 121                 N   KCX B 122     1555   1555  1.33  
LINK         C   KCX B 122                 N   LEU B 123     1555   1555  1.33  
LINK         C   MET C 121                 N   KCX C 122     1555   1555  1.33  
LINK         C   KCX C 122                 N   LEU C 123     1555   1555  1.33  
LINK         C   MET D 121                 N   KCX D 122     1555   1555  1.33  
LINK         C   KCX D 122                 N   LEU D 123     1555   1555  1.33  
CISPEP   1 GLN A  152    PRO A  153          0        10.85                     
CISPEP   2 GLN B  152    PRO B  153          0         0.00                     
CISPEP   3 GLN C  152    PRO C  153          0         0.13                     
CISPEP   4 GLN D  152    PRO D  153          0         0.12                     
SITE     1 AC1  3 TYR A 255  TYR A 274  ARG A 280                               
SITE     1 AC2  3 ARG A  19  ARG B 266  GLN B 315                               
SITE     1 AC3  3 TYR B 255  TYR B 274  ARG B 280                               
SITE     1 AC4  2 ARG A 266  ARG B  19                                          
SITE     1 AC5  1 ARG B 162                                                     
SITE     1 AC6  4 TYR C 255  TYR C 274  ARG C 280  ALA C 302                    
SITE     1 AC7  2 ARG C  19  ARG D 266                                          
SITE     1 AC8  4 TYR C 343  TYR D 255  TYR D 274  ARG D 280                    
SITE     1 AC9  2 ARG C 266  ARG D  19                                          
SITE     1 BC1  9 LYS A  34  TYR A  38  HIS A 159  ALA A 193                    
SITE     2 BC1  9 SER A 194  ARG A 209  GLY A 211  ILE A 212                    
SITE     3 BC1  9 TYR A 343                                                     
SITE     1 BC2  9 LYS B  34  TYR B  38  HIS B 159  ALA B 193                    
SITE     2 BC2  9 SER B 194  ARG B 209  GLY B 211  ILE B 212                    
SITE     3 BC2  9 TYR B 343                                                     
SITE     1 BC3 10 LYS C  34  TYR C  38  LEU C  78  HIS C 159                    
SITE     2 BC3 10 ALA C 193  SER C 194  ARG C 209  GLY C 211                    
SITE     3 BC3 10 ILE C 212  TYR C 343                                          
SITE     1 BC4  9 LYS D  34  TYR D  38  HIS D 159  ALA D 193                    
SITE     2 BC4  9 SER D 194  ARG D 209  GLY D 211  ILE D 212                    
SITE     3 BC4  9 TYR D 343                                                     
CRYST1  147.952  147.952  163.438  90.00  90.00 120.00 P 6          24          
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      0.006759  0.003902  0.000000        0.00000                         
SCALE2      0.000000  0.007805  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006119        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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