GenomeNet

Database: PDB
Entry: 2RJH
LinkDB: 2RJH
Original site: 2RJH 
HEADER    ISOMERASE                               15-OCT-07   2RJH              
TITLE     CRYSTAL STRUCTURE OF BIOSYNTHETIC ALAINE RACEMASE IN D-               
TITLE    2 CYCLOSERINE-BOUND FORM FROM ESCHERICHIA COLI                         
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                                                      
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;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    ALPHA/BETA BARREL, CELL SHAPE, CELL WALL                              
KEYWDS   2 BIOGENESIS/DEGRADATION, ISOMERASE, PEPTIDOGLYCAN SYNTHESIS,          
KEYWDS   3 PYRIDOXAL PHOSPHATE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.WU,T.HU,L.ZHANG,H.JIANG,X.SHEN                                      
REVDAT   2   24-FEB-09 2RJH    1       VERSN                                    
REVDAT   1   08-JUL-08 2RJH    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                  
JRNL        TITL 2 ENTRYWAY FUNCTION POTENTLY IN SUBSTRATE                      
JRNL        TITL 3 ORIENTATION OF ALANINE RACEMASE FROM E. COLI:                
JRNL        TITL 4 ENZYMATIC CHARACTERIZATION WITH CRYSTAL STRUCTURE            
JRNL        TITL 5 ANALYSIS                                                     
JRNL        REF    PROTEIN SCI.                  V.  17  1066 2008              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   18434499                                                     
JRNL        DOI    10.1110/PS.083495908                                         
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 31.000                         
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 78640                          
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) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7605                            
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            : 10949                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 118                                     
REMARK   3   SOLVENT ATOMS            : 566                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.24600                                             
REMARK   3    B22 (A**2) : -2.24600                                             
REMARK   3    B33 (A**2) : 4.49200                                              
REMARK   3    B12 (A**2) : -3.52900                                             
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) : 1.108 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.819 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.742 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.574 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 37.12                                                
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  : KCX.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          
REMARK   3  DETWIN FRACTION IS 0.400, AND OPERATOR IS 'H, -H-K, -L'.            
REMARK   4                                                                      
REMARK   4 2RJH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-OCT-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB044933.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-NOV-06                          
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   : 78993                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 9.700                              
REMARK 200  R MERGE                    (I) : 0.12100                            
REMARK 200  R SYM                      (I) : 0.12100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.39500                            
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: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1RCQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11                     
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: 7640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.3 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: 7160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.7 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 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     ARG C   333                                                      
REMARK 465     ILE C   334                                                      
REMARK 465     ALA C   335                                                      
REMARK 465     GLU C   336                                                      
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 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   OD2  ASP C   222     O    HOH C   498              1.79            
REMARK 500   O    HOH B   540     O    HOH B   596              1.95            
REMARK 500   NH1  ARG C    11     O    ASP C   359              1.97            
REMARK 500   O    CYS A   168     O    HOH A   516              2.10            
REMARK 500   NZ   LYS A    73     O    HOH A   458              2.16            
REMARK 500   O    HOH C   430     O    HOH C   442              2.16            
REMARK 500   O    HOH B   471     O    HOH B   653              2.18            
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   CD  -  NE  -  CZ  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    ARG A  11   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ARG A  11   NE  -  CZ  -  NH2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG A  65   CD  -  NE  -  CZ  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    ARG A  65   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    ARG A  65   NE  -  CZ  -  NH2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ARG A 129   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ARG A 129   NE  -  CZ  -  NH2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG A 223   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A 333   CD  -  NE  -  CZ  ANGL. DEV. =  12.0 DEGREES          
REMARK 500    ARG A 333   NE  -  CZ  -  NH1 ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    ARG A 333   NE  -  CZ  -  NH2 ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ARG B  59   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG B  65   CD  -  NE  -  CZ  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ARG B  65   NE  -  CZ  -  NH1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG B  65   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ARG B  85   CD  -  NE  -  CZ  ANGL. DEV. =  10.8 DEGREES          
REMARK 500    ARG B  85   NE  -  CZ  -  NH1 ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    ARG B  85   NE  -  CZ  -  NH2 ANGL. DEV. =   8.6 DEGREES          
REMARK 500    ARG B 129   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ARG B 129   NE  -  CZ  -  NH2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG B 151   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG B 151   NE  -  CZ  -  NH2 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG B 333   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG B 333   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG C  11   CD  -  NE  -  CZ  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ARG C  11   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    ARG C  11   NE  -  CZ  -  NH2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG C  65   CD  -  NE  -  CZ  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ARG C  65   NE  -  CZ  -  NH1 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ARG C  65   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    ARG C  85   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG C 129   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG C 129   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ARG C 151   CD  -  NE  -  CZ  ANGL. DEV. =  15.4 DEGREES          
REMARK 500    ARG C 151   NE  -  CZ  -  NH1 ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ARG C 151   NE  -  CZ  -  NH2 ANGL. DEV. = -10.6 DEGREES          
REMARK 500    ARG C 223   CD  -  NE  -  CZ  ANGL. DEV. =  14.4 DEGREES          
REMARK 500    ARG C 223   NE  -  CZ  -  NH1 ANGL. DEV. =  10.3 DEGREES          
REMARK 500    ARG C 223   NE  -  CZ  -  NH2 ANGL. DEV. = -10.4 DEGREES          
REMARK 500    ARG D  11   CD  -  NE  -  CZ  ANGL. DEV. =  11.4 DEGREES          
REMARK 500    ARG D  11   NE  -  CZ  -  NH1 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    ARG D  11   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    ARG D  65   CD  -  NE  -  CZ  ANGL. DEV. =  11.1 DEGREES          
REMARK 500    ARG D  65   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    ARG D  65   NE  -  CZ  -  NH2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG D 129   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG D 129   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG D 151   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG D 151   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A   3     -162.08   -108.11                                   
REMARK 500    ALA A   4      106.44    -35.58                                   
REMARK 500    ARG A 129      -78.04   -110.80                                   
REMARK 500    ARG A 162       41.17   -145.86                                   
REMARK 500    GLU A 165       79.09   -118.84                                   
REMARK 500    ALA A 193     -156.87   -116.99                                   
REMARK 500    PHE A 205     -136.16     47.56                                   
REMARK 500    GLU A 221       43.71   -106.76                                   
REMARK 500    SER A 239     -156.65   -165.18                                   
REMARK 500    ALA A 243      144.46   -170.66                                   
REMARK 500    GLN A 315       -6.57     78.19                                   
REMARK 500    TRP A 325      139.13   -173.19                                   
REMARK 500    LEU A 329       86.34   -154.39                                   
REMARK 500    GLN B   2       34.86    -72.92                                   
REMARK 500    ALA B   3     -150.26   -105.92                                   
REMARK 500    ALA B   4      106.27    -42.75                                   
REMARK 500    ARG B 129      -77.09   -110.78                                   
REMARK 500    ARG B 162       40.83   -145.35                                   
REMARK 500    GLU B 165       79.35   -118.27                                   
REMARK 500    ALA B 193     -156.36   -115.82                                   
REMARK 500    PHE B 205     -135.53     47.04                                   
REMARK 500    GLU B 221       43.67   -106.53                                   
REMARK 500    SER B 239     -156.58   -164.53                                   
REMARK 500    ALA B 243      142.95   -170.46                                   
REMARK 500    TRP B 325      141.78   -171.27                                   
REMARK 500    LEU B 329       86.78   -156.08                                   
REMARK 500    ALA C   4      109.10    -45.31                                   
REMARK 500    ARG C 129      -77.38   -110.08                                   
REMARK 500    ARG C 162       40.19   -146.30                                   
REMARK 500    GLU C 165       79.90   -118.26                                   
REMARK 500    ALA C 193     -155.60   -117.41                                   
REMARK 500    PHE C 205     -136.37     47.25                                   
REMARK 500    GLU C 221       43.83   -107.69                                   
REMARK 500    SER C 239     -156.78   -165.19                                   
REMARK 500    ALA C 243      143.49   -171.78                                   
REMARK 500    GLN C 315       -6.34     78.76                                   
REMARK 500    TRP C 325      142.14   -173.21                                   
REMARK 500    LEU C 329       86.55   -155.33                                   
REMARK 500    ALA D   4      107.49    -58.65                                   
REMARK 500    ARG D 129      -77.59   -108.43                                   
REMARK 500    ARG D 162       40.74   -146.80                                   
REMARK 500    GLU D 165       79.90   -118.02                                   
REMARK 500    ALA D 193     -156.17   -117.01                                   
REMARK 500    PHE D 205     -135.88     48.42                                   
REMARK 500    ARG D 209       76.34   -119.94                                   
REMARK 500    GLU D 221       43.95   -108.33                                   
REMARK 500    ARG D 223       19.33     58.66                                   
REMARK 500    SER D 239     -157.13   -165.76                                   
REMARK 500    ALA D 243      143.54   -171.78                                   
REMARK 500    GLN D 315       -6.78     77.55                                   
REMARK 500    TRP D 325      140.60   -173.57                                   
REMARK 500    LEU D 329       86.59   -154.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    VAL D 358        -10.09                                           
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 D 388        DISTANCE =  6.79 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 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 360                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 360                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 361                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 361                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCS A 362                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCS B 362                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCS C 362                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCS D 360                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2RJG   RELATED DB: PDB                                   
REMARK 900 NATIVE PROTEIN                                                       
DBREF  2RJH A    1   359  UNP    P0A6B4   ALR1_ECOLI       1    359             
DBREF  2RJH B    1   359  UNP    P0A6B4   ALR1_ECOLI       1    359             
DBREF  2RJH C    1   359  UNP    P0A6B4   ALR1_ECOLI       1    359             
DBREF  2RJH D    1   359  UNP    P0A6B4   ALR1_ECOLI       1    359             
SEQADV 2RJH MET A  -19  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH GLY A  -18  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER A  -17  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER A  -16  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS A  -15  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS A  -14  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS A  -13  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS A  -12  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS A  -11  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS A  -10  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER A   -9  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER A   -8  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH GLY A   -7  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH LEU A   -6  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH VAL A   -5  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH PRO A   -4  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH ARG A   -3  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH GLY A   -2  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER A   -1  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS A    0  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH MET B  -19  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH GLY B  -18  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER B  -17  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER B  -16  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS B  -15  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS B  -14  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS B  -13  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS B  -12  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS B  -11  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS B  -10  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER B   -9  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER B   -8  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH GLY B   -7  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH LEU B   -6  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH VAL B   -5  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH PRO B   -4  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH ARG B   -3  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH GLY B   -2  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER B   -1  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS B    0  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH MET C  -19  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH GLY C  -18  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER C  -17  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER C  -16  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS C  -15  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS C  -14  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS C  -13  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS C  -12  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS C  -11  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS C  -10  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER C   -9  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER C   -8  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH GLY C   -7  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH LEU C   -6  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH VAL C   -5  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH PRO C   -4  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH ARG C   -3  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH GLY C   -2  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER C   -1  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS C    0  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH MET D  -19  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH GLY D  -18  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER D  -17  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER D  -16  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS D  -15  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS D  -14  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS D  -13  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS D  -12  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS D  -11  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS D  -10  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER D   -9  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER D   -8  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH GLY D   -7  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH LEU D   -6  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH VAL D   -5  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH PRO D   -4  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH ARG D   -3  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH GLY D   -2  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH SER D   -1  UNP  P0A6B4              EXPRESSION TAG                 
SEQADV 2RJH HIS D    0  UNP  P0A6B4              EXPRESSION TAG                 
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 GLU 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 GLU 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 GLU 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 GLU 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 2RJH KCX A  122  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 2RJH KCX B  122  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 2RJH KCX C  122  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 2RJH 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  B 360       5                                                       
HET    SO4  B 361       5                                                       
HET    SO4  C 360       5                                                       
HET    SO4  C 361       5                                                       
HET    DCS  A 362      22                                                       
HET    DCS  B 362      22                                                       
HET    DCS  C 362      22                                                       
HET    DCS  D 360      22                                                       
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM     SO4 SULFATE ION                                                      
HETNAM     DCS D-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-            
HETNAM   2 DCS  YLMETHYL]-N,O-CYCLOSERYLAMIDE                                   
HETSYN     DCS D-PYRIDOXYL-N,O-CYCLOSERYLAMIDE-5-MONOPHOSPHATE                  
FORMUL   1  KCX    4(C7 H14 N2 O4)                                              
FORMUL   5  SO4    6(O4 S 2-)                                                   
FORMUL  11  DCS    4(C11 H16 N3 O7 P)                                           
FORMUL  15  HOH   *566(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  LEU A   49  1                                   9    
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 ASN A  101  ALA A  111  1                                  11    
HELIX    8   8 ARG A  133  GLN A  146  1                                  14    
HELIX    9   9 GLY A  169  GLU A  183  1                                  15    
HELIX   10  10 ALA A  193  TRP A  200  1                                   8    
HELIX   11  11 PRO A  201  HIS A  204  5                                   4    
HELIX   12  12 GLY A  211  GLY A  216  5                                   6    
HELIX   13  13 THR A  225  GLY A  230  5                                   6    
HELIX   14  14 GLY A  254  THR A  258  5                                   5    
HELIX   15  15 PRO A  330  LYS A  339  1                                  10    
HELIX   16  16 SER A  341  ARG A  348  1                                   8    
HELIX   17  17 ARG B   10  ALA B   24  1                                  15    
HELIX   18  18 VAL B   33  GLY B   39  1                                   7    
HELIX   19  19 GLY B   41  THR B   48  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  GLN B   93  1                                   8    
HELIX   23  23 ASN B  101  ALA B  111  1                                  11    
HELIX   24  24 ARG B  133  GLN B  146  1                                  14    
HELIX   25  25 GLY B  169  GLU B  183  1                                  15    
HELIX   26  26 ALA B  193  TRP B  200  1                                   8    
HELIX   27  27 PRO B  201  HIS B  204  5                                   4    
HELIX   28  28 GLY B  211  GLY B  216  5                                   6    
HELIX   29  29 THR B  225  GLY B  230  5                                   6    
HELIX   30  30 GLY B  254  THR B  258  5                                   5    
HELIX   31  31 PRO B  330  LYS B  339  1                                  10    
HELIX   32  32 SER B  341  ARG B  348  1                                   8    
HELIX   33  33 ARG C   10  ALA C   24  1                                  15    
HELIX   34  34 VAL C   33  GLY C   39  1                                   7    
HELIX   35  35 GLY C   41  THR C   48  1                                   8    
HELIX   36  36 ARG C   59  GLY C   69  1                                  11    
HELIX   37  37 ASP C   83  ARG C   85  5                                   3    
HELIX   38  38 ASP C   86  GLN C   93  1                                   8    
HELIX   39  39 ASN C  101  ALA C  111  1                                  11    
HELIX   40  40 ARG C  133  GLN C  146  1                                  14    
HELIX   41  41 GLY C  169  GLU C  183  1                                  15    
HELIX   42  42 ALA C  193  TRP C  200  1                                   8    
HELIX   43  43 PRO C  201  HIS C  204  5                                   4    
HELIX   44  44 GLY C  211  GLY C  216  5                                   6    
HELIX   45  45 THR C  225  GLY C  230  5                                   6    
HELIX   46  46 GLY C  254  THR C  258  5                                   5    
HELIX   47  47 SER C  341  ARG C  348  1                                   8    
HELIX   48  48 ARG D   10  ALA D   24  1                                  15    
HELIX   49  49 VAL D   33  GLY D   39  1                                   7    
HELIX   50  50 GLY D   41  THR D   48  1                                   8    
HELIX   51  51 ARG D   59  GLY D   69  1                                  11    
HELIX   52  52 ASP D   83  ARG D   85  5                                   3    
HELIX   53  53 ASP D   86  GLN D   93  1                                   8    
HELIX   54  54 ASN D  101  ALA D  111  1                                  11    
HELIX   55  55 ARG D  133  GLN D  146  1                                  14    
HELIX   56  56 GLY D  169  GLU D  183  1                                  15    
HELIX   57  57 ALA D  193  TRP D  200  1                                   8    
HELIX   58  58 PRO D  201  HIS D  204  5                                   4    
HELIX   59  59 GLY D  211  GLY D  216  5                                   6    
HELIX   60  60 THR D  225  GLY D  230  5                                   6    
HELIX   61  61 GLY D  254  THR D  258  5                                   5    
HELIX   62  62 PRO D  330  LYS D  339  1                                  10    
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  TRP A 325           
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  TRP A 325           
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 8 ARG A 189  SER A 190  0                                        
SHEET    2   C 8 ASN A 155  VAL A 157  1  N  ILE A 156   O  SER A 190           
SHEET    3   C 8 VAL A 119  KCX A 122  1  N  MET A 121   O  ASN A 155           
SHEET    4   C 8 PHE A  95  VAL A  99  1  N  THR A  97   O  TRP A 120           
SHEET    5   C 8 VAL A  75  LEU A  77  1  N  VAL A  75   O  HIS A  96           
SHEET    6   C 8 ALA A  54  VAL A  57  1  N  PHE A  55   O  LEU A  76           
SHEET    7   C 8 LYS A  28  VAL A  32  1  N  ALA A  31   O  ALA A  54           
SHEET    8   C 8 TRP A 207  VAL A 208  1  O  VAL A 208   N  LYS A  28           
SHEET    1   D 2 PRO A 252  VAL A 253  0                                        
SHEET    2   D 2 TRP A 259  VAL A 260 -1  O  TRP A 259   N  VAL A 253           
SHEET    1   E 6 ARG B 293  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  TRP B 325           
SHEET    5   E 6 THR B 265  VAL B 270 -1  O  VAL B 269   N  ILE B 242           
SHEET    6   E 6 ILE B 306  ASP B 309 -1  O  ILE B 306   N  VAL B 270           
SHEET    1   F 6 ARG B 293  PRO B 296  0                                        
SHEET    2   F 6 PRO B 287  VAL B 290 -1  N  VAL B 288   O  VAL B 295           
SHEET    3   F 6 PRO B 321  TRP B 325 -1  O  ILE B 323   N  LEU B 289           
SHEET    4   F 6 MET B 235  HIS B 247 -1  N  LEU B 237   O  TRP B 325           
SHEET    5   F 6 THR B   5  ASN B   9 -1  N  THR B   5   O  THR B 238           
SHEET    6   F 6 ALA B 354  VAL B 358  1  O  LYS B 356   N  ILE B   8           
SHEET    1   G 8 ARG B 189  SER B 190  0                                        
SHEET    2   G 8 VAL B 150  VAL B 157  1  N  ILE B 156   O  SER B 190           
SHEET    3   G 8 VAL B 117  KCX B 122  1  N  MET B 121   O  VAL B 157           
SHEET    4   G 8 PHE B  95  VAL B  99  1  N  THR B  97   O  TRP B 120           
SHEET    5   G 8 VAL B  75  LEU B  77  1  N  LEU B  77   O  HIS B  96           
SHEET    6   G 8 ALA B  54  VAL B  57  1  N  PHE B  55   O  LEU B  76           
SHEET    7   G 8 LYS B  28  VAL B  32  1  N  ALA B  31   O  ALA B  54           
SHEET    8   G 8 TRP B 207  VAL B 208  1  O  VAL B 208   N  LYS B  28           
SHEET    1   H 2 PRO B 252  VAL B 253  0                                        
SHEET    2   H 2 TRP B 259  VAL B 260 -1  O  TRP B 259   N  VAL B 253           
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  LEU C 237   O  TRP C 325           
SHEET    5   I 6 THR C 265  VAL C 270 -1  O  VAL C 269   N  ILE C 242           
SHEET    6   I 6 ILE C 306  ASP C 309 -1  O  ILE C 306   N  VAL C 270           
SHEET    1   J 6 ARG C 293  PRO C 296  0                                        
SHEET    2   J 6 PRO C 287  VAL C 290 -1  N  VAL C 288   O  VAL C 295           
SHEET    3   J 6 PRO C 321  TRP C 325 -1  O  ILE C 323   N  LEU C 289           
SHEET    4   J 6 MET C 235  HIS C 247 -1  N  LEU C 237   O  TRP C 325           
SHEET    5   J 6 THR C   5  ASN C   9 -1  N  THR C   5   O  THR C 238           
SHEET    6   J 6 ALA C 354  VAL C 358  1  O  LYS C 356   N  ILE C   8           
SHEET    1   K 8 ARG C 189  SER C 190  0                                        
SHEET    2   K 8 VAL C 150  VAL C 157  1  N  ILE C 156   O  SER C 190           
SHEET    3   K 8 VAL C 117  KCX C 122  1  N  MET C 121   O  ASN C 155           
SHEET    4   K 8 PHE C  95  VAL C  99  1  N  THR C  97   O  TRP C 120           
SHEET    5   K 8 VAL C  75  LEU C  77  1  N  LEU C  77   O  HIS C  96           
SHEET    6   K 8 ALA C  54  VAL C  57  1  N  PHE C  55   O  LEU C  76           
SHEET    7   K 8 LYS C  28  VAL C  32  1  N  ALA C  31   O  ALA C  54           
SHEET    8   K 8 TRP C 207  VAL C 208  1  O  VAL C 208   N  LYS C  28           
SHEET    1   L 2 PRO C 252  VAL C 253  0                                        
SHEET    2   L 2 TRP C 259  VAL C 260 -1  O  TRP C 259   N  VAL C 253           
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 288   O  VAL D 295           
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  TRP D 325           
SHEET    5   M 6 THR D 265  VAL D 270 -1  O  VAL D 269   N  ILE D 242           
SHEET    6   M 6 ILE D 306  ASP D 309 -1  O  ILE D 306   N  VAL D 270           
SHEET    1   N 6 ARG D 293  PRO D 296  0                                        
SHEET    2   N 6 PRO D 287  VAL D 290 -1  N  VAL D 288   O  VAL D 295           
SHEET    3   N 6 PRO D 321  TRP D 325 -1  O  ILE D 323   N  LEU D 289           
SHEET    4   N 6 MET D 235  HIS D 247 -1  N  LEU D 237   O  TRP D 325           
SHEET    5   N 6 THR D   5  ASN D   9 -1  N  THR D   5   O  THR D 238           
SHEET    6   N 6 ALA D 354  VAL D 358  1  O  LYS D 356   N  ILE D   8           
SHEET    1   O 8 ARG D 189  SER D 190  0                                        
SHEET    2   O 8 VAL D 150  VAL D 157  1  N  ILE D 156   O  SER D 190           
SHEET    3   O 8 VAL D 117  KCX D 122  1  N  MET D 121   O  ASN D 155           
SHEET    4   O 8 PHE D  95  VAL D  99  1  N  THR D  97   O  TRP D 120           
SHEET    5   O 8 VAL D  75  LEU D  77  1  N  LEU D  77   O  HIS D  96           
SHEET    6   O 8 ALA D  54  VAL D  57  1  N  PHE D  55   O  LEU D  76           
SHEET    7   O 8 LYS D  28  VAL D  32  1  N  ALA D  31   O  ALA D  54           
SHEET    8   O 8 TRP D 207  VAL D 208  1  O  VAL D 208   N  LYS D  28           
SHEET    1   P 2 PRO D 252  VAL D 253  0                                        
SHEET    2   P 2 TRP D 259  VAL D 260 -1  O  TRP D 259   N  VAL D 253           
LINK         C   MET A 121                 N   KCX A 122     1555   1555  1.33  
LINK         C   KCX A 122                 N   LEU A 123     1555   1555  1.31  
LINK         C   MET B 121                 N   KCX B 122     1555   1555  1.31  
LINK         C   KCX B 122                 N   LEU B 123     1555   1555  1.34  
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        -0.08                     
CISPEP   2 GLN B  152    PRO B  153          0        -0.05                     
CISPEP   3 GLN C  152    PRO C  153          0         0.04                     
CISPEP   4 GLN D  152    PRO D  153          0        -0.01                     
SITE     1 AC1  2 ARG A  19  ARG B 266                                          
SITE     1 AC2  2 ARG A 266  ARG B  19                                          
SITE     1 AC3  3 ARG C  19  ARG D 266  GLN D 315                               
SITE     1 AC4  2 ARG A 162  CYS A 168                                          
SITE     1 AC5  2 ARG B 162  CYS B 168                                          
SITE     1 AC6 14 LYS A  34  TYR A  38  ARG A 129  HIS A 159                    
SITE     2 AC6 14 ALA A 193  SER A 194  ARG A 209  GLY A 211                    
SITE     3 AC6 14 ILE A 212  TYR A 343  TYR B 255  TYR B 274                    
SITE     4 AC6 14 ALA B 302  MET B 303                                          
SITE     1 AC7 14 TYR A 255  TYR A 274  ALA A 302  MET A 303                    
SITE     2 AC7 14 LYS B  34  TYR B  38  ARG B 129  HIS B 159                    
SITE     3 AC7 14 ALA B 193  SER B 194  ARG B 209  GLY B 211                    
SITE     4 AC7 14 ILE B 212  TYR B 343                                          
SITE     1 AC8 14 LYS C  34  TYR C  38  ARG C 129  HIS C 159                    
SITE     2 AC8 14 ALA C 193  SER C 194  ARG C 209  GLY C 211                    
SITE     3 AC8 14 ILE C 212  TYR C 343  TYR D 255  TYR D 274                    
SITE     4 AC8 14 ALA D 302  MET D 303                                          
SITE     1 AC9 14 TYR C 255  TYR C 274  MET C 303  LYS D  34                    
SITE     2 AC9 14 TYR D  38  LEU D  78  ARG D 129  HIS D 159                    
SITE     3 AC9 14 ALA D 193  SER D 194  ARG D 209  GLY D 211                    
SITE     4 AC9 14 ILE D 212  TYR D 343                                          
CRYST1  147.713  147.713  163.724  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      0.006770  0.003909  0.000000        0.00000                         
SCALE2      0.000000  0.007817  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006108        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system