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Database: PDB
Entry: 5FAJ
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Original site: 5FAJ 
HEADER    ISOMERASE                               11-DEC-15   5FAJ              
TITLE     ALANINE RACEMASE FROM STREPTOMYCES COELICOLOR A3(2) IN COMPLEX WITH D-
TITLE    2 CYCLOSERINE                                                          
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: STREPTOMYCES COELICOLOR A3(2);                  
SOURCE   3 ORGANISM_TAXID: 100226;                                              
SOURCE   4 GENE: ALR, SCO4745, SC6G4.23;                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: STAR;                                     
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET-15B                                   
KEYWDS    ISOMERASE, PLP, ALANINE RACEMASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.TASSONI,N.S.PANNU                                                   
REVDAT   3   01-FEB-17 5FAJ    1       JRNL                                     
REVDAT   2   25-JAN-17 5FAJ    1       JRNL                                     
REVDAT   1   21-DEC-16 5FAJ    0                                                
JRNL        AUTH   R.TASSONI,L.T.VAN DER AART,M.UBBINK,G.P.VAN WEZEL,N.S.PANNU  
JRNL        TITL   STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF THE ALANINE    
JRNL        TITL 2 RACEMASE FROM STREPTOMYCES COELICOLOR A3(2).                 
JRNL        REF    BIOCHEM. BIOPHYS. RES.        V. 483   122 2017              
JRNL        REF  2 COMMUN.                                                      
JRNL        REFN                   ESSN 1090-2104                               
JRNL        PMID   28042035                                                     
JRNL        DOI    10.1016/J.BBRC.2016.12.183                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.64 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.64                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 106.60                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 77.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 133358                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6996                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.64                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.68                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1081                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 8.56                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5470                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 65                           
REMARK   3   BIN FREE R VALUE                    : 0.4130                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11350                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 99                                      
REMARK   3   SOLVENT ATOMS            : 760                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.03000                                             
REMARK   3    B22 (A**2) : 0.13000                                              
REMARK   3    B33 (A**2) : -0.11000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.03000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.145         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.133         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.108         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.414         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11845 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 11271 ; 0.009 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 16192 ; 1.843 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 25812 ; 1.598 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1557 ; 6.193 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   488 ;32.758 ;21.557       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1691 ;13.918 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   142 ;18.071 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1770 ; 0.109 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 13664 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2710 ; 0.007 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  6162 ; 3.112 ; 3.092       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  6162 ; 3.111 ; 3.093       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7696 ; 4.305 ; 4.625       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  7697 ; 4.305 ; 4.626       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5683 ; 3.580 ; 3.450       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  5679 ; 3.579 ; 3.450       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  8476 ; 5.281 ; 5.046       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 13798 ; 6.982 ;25.530       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 13497 ; 6.973 ;25.413       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 6                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A    10    390       B    10    390   45654  0.06  0.05     
REMARK   3    2     A    10    390       C    10    390   45626  0.07  0.05     
REMARK   3    3     A    10    390       D    10    390   45618  0.07  0.05     
REMARK   3    4     B    10    391       C    10    391   46064  0.06  0.05     
REMARK   3    5     B    10    391       D    10    391   45668  0.07  0.05     
REMARK   3    6     C    10    391       D    10    391   45858  0.06  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5FAJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-DEC-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000216275.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-MAY-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.968622                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 177142                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.640                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.130                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.13000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 5FAC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PROPANE PH 8.5, 0.2 M     
REMARK 280  NABR, 20% (W/V) PEG3350, VAPOR DIFFUSION, SITTING DROP,             
REMARK 280  TEMPERATURE 293.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       44.35500            
REMARK 290   SMTRY3   2  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: 8240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 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: 8230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 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   -18                                                      
REMARK 465     GLY 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 A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     MET B   -18                                                      
REMARK 465     GLY 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     SER B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     ARG B     7                                                      
REMARK 465     ARG B     8                                                      
REMARK 465     ASP B     9                                                      
REMARK 465     MET C   -18                                                      
REMARK 465     GLY 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     SER C     2                                                      
REMARK 465     GLU C     3                                                      
REMARK 465     THR C     4                                                      
REMARK 465     THR C     5                                                      
REMARK 465     ALA C     6                                                      
REMARK 465     ARG C     7                                                      
REMARK 465     ARG C     8                                                      
REMARK 465     ASP C     9                                                      
REMARK 465     MET D   -18                                                      
REMARK 465     GLY 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     SER D     2                                                      
REMARK 465     GLU D     3                                                      
REMARK 465     THR D     4                                                      
REMARK 465     THR D     5                                                      
REMARK 465     ALA D     6                                                      
REMARK 465     ARG D     7                                                      
REMARK 465     ARG D     8                                                      
REMARK 465     ASP D     9                                                      
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   C    GLU B   391     O    HOH B   501              1.41            
REMARK 500   O    HOH B   555     O    HOH B   699              1.65            
REMARK 500   O    HOH B   509     O    HOH B   699              1.66            
REMARK 500   NH2  ARG A   166     O    HOH A   501              1.71            
REMARK 500   CG   ARG D   199     O    HOH D   543              1.79            
REMARK 500   SD   MET D    94     O    HOH D   583              1.87            
REMARK 500   NH1  ARG A   148     O    HOH A   502              1.95            
REMARK 500   OQ2  KCX A   141     NH2  ARG A   148              2.01            
REMARK 500   NH2  ARG A   217     O    HOH A   503              2.02            
REMARK 500   OG1  THR D   293     O    GLY D   339              2.05            
REMARK 500   O    GLU B   391     O    HOH B   501              2.06            
REMARK 500   NH2  ARG C    17     OE2  GLU C   348              2.08            
REMARK 500   SD   MET D   203     O    HOH D   543              2.08            
REMARK 500   NH2  ARG B    17     OE2  GLU B   348              2.09            
REMARK 500   OG   DCS B   401     O    HOH B   502              2.12            
REMARK 500   O    VAL C   272     O    HOH C   501              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NE   ARG A   166     OE1  GLU B   123     1455     2.14            
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    ARG B  30   CZ    ARG B  30   NH1    -0.198                       
REMARK 500    ARG B  30   CZ    ARG B  30   NH2    -0.084                       
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  30   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ARG A  30   NE  -  CZ  -  NH2 ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ARG A 111   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A 148   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG A 148   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A 201   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 217   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 217   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG B  17   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG B  30   CB  -  CG  -  CD  ANGL. DEV. =  17.3 DEGREES          
REMARK 500    ARG B  30   NE  -  CZ  -  NH1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG B  30   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B  35   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG B  35   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG B  81   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG B 111   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG B 159   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG B 210   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG B 328   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ASP C  11   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG C 328   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG D  35   CG  -  CD  -  NE  ANGL. DEV. = -16.8 DEGREES          
REMARK 500    ARG D 328   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    GLY D 339   N   -  CA  -  C   ANGL. DEV. = -15.3 DEGREES          
REMARK 500    ARG D 357   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG D 383   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG D 383   NE  -  CZ  -  NH2 ANGL. DEV. =   4.9 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    ARG A 148     -110.36   -118.10                                   
REMARK 500    ARG A 148     -110.49   -118.10                                   
REMARK 500    PHE A 233     -132.71     47.13                                   
REMARK 500    SER A 282      178.89     66.06                                   
REMARK 500    SER A 312        3.45     59.58                                   
REMARK 500    THR A 371     -158.96   -139.04                                   
REMARK 500    ARG B 148     -109.17   -118.73                                   
REMARK 500    PHE B 233     -130.86     47.24                                   
REMARK 500    SER B 282     -179.79     67.89                                   
REMARK 500    ARG C 148     -110.28   -118.88                                   
REMARK 500    PHE C 233     -131.10     44.76                                   
REMARK 500    SER C 282     -179.51     66.01                                   
REMARK 500    ARG D 148     -110.06   -119.37                                   
REMARK 500    PHE D 233     -132.39     46.50                                   
REMARK 500    SER D 282      177.25     65.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 720        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH A 721        DISTANCE =  6.38 ANGSTROMS                       
REMARK 525    HOH B 731        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH C 665        DISTANCE =  6.72 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 180   OG                                                     
REMARK 620 2 HIS A 181   O    77.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 180   OG                                                     
REMARK 620 2 HIS B 181   O    77.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER C 180   OG                                                     
REMARK 620 2 HIS C 181   O    76.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 403  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA C 231   O                                                      
REMARK 620 2 HIS C 232   O    83.0                                              
REMARK 620 3 LEU C 235   O   144.3  65.4                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DCS A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DCS B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DCS C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DCS D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 403                  
DBREF  5FAJ A    1   391  UNP    O86786   ALR_STRCO        1    391             
DBREF  5FAJ B    1   391  UNP    O86786   ALR_STRCO        1    391             
DBREF  5FAJ C    1   391  UNP    O86786   ALR_STRCO        1    391             
DBREF  5FAJ D    1   391  UNP    O86786   ALR_STRCO        1    391             
SEQADV 5FAJ MET A  -18  UNP  O86786              INITIATING METHIONINE          
SEQADV 5FAJ GLY A  -17  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ SER A  -16  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS A  -15  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS A  -14  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS A  -13  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS A  -12  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS A  -11  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS A  -10  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ SER A   -9  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ SER A   -8  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ GLY A   -7  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ LEU A   -6  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ VAL A   -5  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ PRO A   -4  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ ARG A   -3  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ GLY A   -2  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ SER A   -1  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS A    0  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ MET B  -18  UNP  O86786              INITIATING METHIONINE          
SEQADV 5FAJ GLY B  -17  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ SER B  -16  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS B  -15  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS B  -14  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS B  -13  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS B  -12  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS B  -11  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS B  -10  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ SER B   -9  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ SER B   -8  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ GLY B   -7  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ LEU B   -6  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ VAL B   -5  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ PRO B   -4  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ ARG B   -3  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ GLY B   -2  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ SER B   -1  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS B    0  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ MET C  -18  UNP  O86786              INITIATING METHIONINE          
SEQADV 5FAJ GLY C  -17  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ SER C  -16  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS C  -15  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS C  -14  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS C  -13  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS C  -12  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS C  -11  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS C  -10  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ SER C   -9  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ SER C   -8  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ GLY C   -7  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ LEU C   -6  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ VAL C   -5  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ PRO C   -4  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ ARG C   -3  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ GLY C   -2  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ SER C   -1  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS C    0  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ MET D  -18  UNP  O86786              INITIATING METHIONINE          
SEQADV 5FAJ GLY D  -17  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ SER D  -16  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS D  -15  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS D  -14  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS D  -13  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS D  -12  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS D  -11  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS D  -10  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ SER D   -9  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ SER D   -8  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ GLY D   -7  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ LEU D   -6  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ VAL D   -5  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ PRO D   -4  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ ARG D   -3  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ GLY D   -2  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ SER D   -1  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAJ HIS D    0  UNP  O86786              EXPRESSION TAG                 
SEQRES   1 A  410  MET GLY SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 A  410  VAL PRO ARG GLY SER HIS MET SER GLU THR THR ALA ARG          
SEQRES   3 A  410  ARG ASP ALA ASP ALA VAL LEU ARG ALA ARG ALA GLU ILE          
SEQRES   4 A  410  ASP LEU ALA ALA LEU ARG ALA ASN VAL ARG ALA LEU ARG          
SEQRES   5 A  410  GLU ARG ALA PRO GLY ALA ALA LEU MET ALA VAL VAL LYS          
SEQRES   6 A  410  ALA ASP ALA TYR GLY HIS GLY ALA ILE PRO CYS ALA ARG          
SEQRES   7 A  410  ALA ALA VAL ALA ALA GLY ALA THR TRP LEU GLY THR ALA          
SEQRES   8 A  410  THR PRO GLN GLU ALA LEU ALA LEU ARG ALA ALA GLU PRO          
SEQRES   9 A  410  GLY LEU PRO ASP ASP VAL ARG ILE MET CYS TRP LEU TRP          
SEQRES  10 A  410  THR PRO GLY GLY PRO TRP ARG GLU ALA VAL GLU ALA ARG          
SEQRES  11 A  410  LEU ASP VAL SER VAL SER ALA MET TRP ALA MET GLU GLU          
SEQRES  12 A  410  VAL THR GLY ALA ALA ARG ALA ALA GLY VAL PRO ALA ARG          
SEQRES  13 A  410  VAL GLN LEU KCX ALA ASP THR GLY LEU GLY ARG GLY GLY          
SEQRES  14 A  410  CYS GLN PRO GLY ALA ASP TRP GLU ARG LEU VAL GLY ALA          
SEQRES  15 A  410  ALA LEU ARG ALA GLU GLU GLU GLY LEU LEU ARG VAL THR          
SEQRES  16 A  410  GLY LEU TRP SER HIS PHE ALA CYS ALA ASP GLU PRO GLY          
SEQRES  17 A  410  HIS PRO SER ILE ALA ALA GLN LEU THR ARG PHE ARG GLU          
SEQRES  18 A  410  MET THR ALA TYR ALA GLU GLN ARG GLY LEU ARG PRO GLU          
SEQRES  19 A  410  VAL ARG HIS ILE ALA ASN SER PRO ALA THR LEU THR LEU          
SEQRES  20 A  410  PRO ASP ALA HIS PHE ASP LEU VAL ARG PRO GLY ILE ALA          
SEQRES  21 A  410  MET TYR GLY VAL SER PRO SER PRO GLU ILE GLY THR PRO          
SEQRES  22 A  410  ALA ASP PHE GLY LEU ARG PRO VAL MET THR LEU ALA ALA          
SEQRES  23 A  410  SER LEU ALA LEU VAL LYS GLN VAL PRO GLY GLY HIS GLY          
SEQRES  24 A  410  VAL SER TYR GLY HIS HIS TYR THR THR PRO GLY GLU THR          
SEQRES  25 A  410  THR LEU GLY LEU VAL PRO LEU GLY TYR ALA ASP GLY ILE          
SEQRES  26 A  410  PRO ARG HIS ALA SER SER SER GLY PRO VAL LEU VAL ASP          
SEQRES  27 A  410  GLY LYS TRP ARG THR VAL ALA GLY ARG ILE ALA MET ASP          
SEQRES  28 A  410  GLN PHE VAL VAL ASP LEU GLY GLY ASP ARG PRO GLU PRO          
SEQRES  29 A  410  GLY ALA GLU ALA VAL LEU PHE GLY PRO GLY ASP ARG GLY          
SEQRES  30 A  410  GLU PRO THR ALA GLU ASP TRP ALA GLN ALA ALA GLY THR          
SEQRES  31 A  410  ILE ALA TYR GLU ILE VAL THR ARG ILE GLY SER ARG VAL          
SEQRES  32 A  410  PRO ARG VAL TYR VAL ASN GLU                                  
SEQRES   1 B  410  MET GLY SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 B  410  VAL PRO ARG GLY SER HIS MET SER GLU THR THR ALA ARG          
SEQRES   3 B  410  ARG ASP ALA ASP ALA VAL LEU ARG ALA ARG ALA GLU ILE          
SEQRES   4 B  410  ASP LEU ALA ALA LEU ARG ALA ASN VAL ARG ALA LEU ARG          
SEQRES   5 B  410  GLU ARG ALA PRO GLY ALA ALA LEU MET ALA VAL VAL LYS          
SEQRES   6 B  410  ALA ASP ALA TYR GLY HIS GLY ALA ILE PRO CYS ALA ARG          
SEQRES   7 B  410  ALA ALA VAL ALA ALA GLY ALA THR TRP LEU GLY THR ALA          
SEQRES   8 B  410  THR PRO GLN GLU ALA LEU ALA LEU ARG ALA ALA GLU PRO          
SEQRES   9 B  410  GLY LEU PRO ASP ASP VAL ARG ILE MET CYS TRP LEU TRP          
SEQRES  10 B  410  THR PRO GLY GLY PRO TRP ARG GLU ALA VAL GLU ALA ARG          
SEQRES  11 B  410  LEU ASP VAL SER VAL SER ALA MET TRP ALA MET GLU GLU          
SEQRES  12 B  410  VAL THR GLY ALA ALA ARG ALA ALA GLY VAL PRO ALA ARG          
SEQRES  13 B  410  VAL GLN LEU KCX ALA ASP THR GLY LEU GLY ARG GLY GLY          
SEQRES  14 B  410  CYS GLN PRO GLY ALA ASP TRP GLU ARG LEU VAL GLY ALA          
SEQRES  15 B  410  ALA LEU ARG ALA GLU GLU GLU GLY LEU LEU ARG VAL THR          
SEQRES  16 B  410  GLY LEU TRP SER HIS PHE ALA CYS ALA ASP GLU PRO GLY          
SEQRES  17 B  410  HIS PRO SER ILE ALA ALA GLN LEU THR ARG PHE ARG GLU          
SEQRES  18 B  410  MET THR ALA TYR ALA GLU GLN ARG GLY LEU ARG PRO GLU          
SEQRES  19 B  410  VAL ARG HIS ILE ALA ASN SER PRO ALA THR LEU THR LEU          
SEQRES  20 B  410  PRO ASP ALA HIS PHE ASP LEU VAL ARG PRO GLY ILE ALA          
SEQRES  21 B  410  MET TYR GLY VAL SER PRO SER PRO GLU ILE GLY THR PRO          
SEQRES  22 B  410  ALA ASP PHE GLY LEU ARG PRO VAL MET THR LEU ALA ALA          
SEQRES  23 B  410  SER LEU ALA LEU VAL LYS GLN VAL PRO GLY GLY HIS GLY          
SEQRES  24 B  410  VAL SER TYR GLY HIS HIS TYR THR THR PRO GLY GLU THR          
SEQRES  25 B  410  THR LEU GLY LEU VAL PRO LEU GLY TYR ALA ASP GLY ILE          
SEQRES  26 B  410  PRO ARG HIS ALA SER SER SER GLY PRO VAL LEU VAL ASP          
SEQRES  27 B  410  GLY LYS TRP ARG THR VAL ALA GLY ARG ILE ALA MET ASP          
SEQRES  28 B  410  GLN PHE VAL VAL ASP LEU GLY GLY ASP ARG PRO GLU PRO          
SEQRES  29 B  410  GLY ALA GLU ALA VAL LEU PHE GLY PRO GLY ASP ARG GLY          
SEQRES  30 B  410  GLU PRO THR ALA GLU ASP TRP ALA GLN ALA ALA GLY THR          
SEQRES  31 B  410  ILE ALA TYR GLU ILE VAL THR ARG ILE GLY SER ARG VAL          
SEQRES  32 B  410  PRO ARG VAL TYR VAL ASN GLU                                  
SEQRES   1 C  410  MET GLY SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 C  410  VAL PRO ARG GLY SER HIS MET SER GLU THR THR ALA ARG          
SEQRES   3 C  410  ARG ASP ALA ASP ALA VAL LEU ARG ALA ARG ALA GLU ILE          
SEQRES   4 C  410  ASP LEU ALA ALA LEU ARG ALA ASN VAL ARG ALA LEU ARG          
SEQRES   5 C  410  GLU ARG ALA PRO GLY ALA ALA LEU MET ALA VAL VAL LYS          
SEQRES   6 C  410  ALA ASP ALA TYR GLY HIS GLY ALA ILE PRO CYS ALA ARG          
SEQRES   7 C  410  ALA ALA VAL ALA ALA GLY ALA THR TRP LEU GLY THR ALA          
SEQRES   8 C  410  THR PRO GLN GLU ALA LEU ALA LEU ARG ALA ALA GLU PRO          
SEQRES   9 C  410  GLY LEU PRO ASP ASP VAL ARG ILE MET CYS TRP LEU TRP          
SEQRES  10 C  410  THR PRO GLY GLY PRO TRP ARG GLU ALA VAL GLU ALA ARG          
SEQRES  11 C  410  LEU ASP VAL SER VAL SER ALA MET TRP ALA MET GLU GLU          
SEQRES  12 C  410  VAL THR GLY ALA ALA ARG ALA ALA GLY VAL PRO ALA ARG          
SEQRES  13 C  410  VAL GLN LEU KCX ALA ASP THR GLY LEU GLY ARG GLY GLY          
SEQRES  14 C  410  CYS GLN PRO GLY ALA ASP TRP GLU ARG LEU VAL GLY ALA          
SEQRES  15 C  410  ALA LEU ARG ALA GLU GLU GLU GLY LEU LEU ARG VAL THR          
SEQRES  16 C  410  GLY LEU TRP SER HIS PHE ALA CYS ALA ASP GLU PRO GLY          
SEQRES  17 C  410  HIS PRO SER ILE ALA ALA GLN LEU THR ARG PHE ARG GLU          
SEQRES  18 C  410  MET THR ALA TYR ALA GLU GLN ARG GLY LEU ARG PRO GLU          
SEQRES  19 C  410  VAL ARG HIS ILE ALA ASN SER PRO ALA THR LEU THR LEU          
SEQRES  20 C  410  PRO ASP ALA HIS PHE ASP LEU VAL ARG PRO GLY ILE ALA          
SEQRES  21 C  410  MET TYR GLY VAL SER PRO SER PRO GLU ILE GLY THR PRO          
SEQRES  22 C  410  ALA ASP PHE GLY LEU ARG PRO VAL MET THR LEU ALA ALA          
SEQRES  23 C  410  SER LEU ALA LEU VAL LYS GLN VAL PRO GLY GLY HIS GLY          
SEQRES  24 C  410  VAL SER TYR GLY HIS HIS TYR THR THR PRO GLY GLU THR          
SEQRES  25 C  410  THR LEU GLY LEU VAL PRO LEU GLY TYR ALA ASP GLY ILE          
SEQRES  26 C  410  PRO ARG HIS ALA SER SER SER GLY PRO VAL LEU VAL ASP          
SEQRES  27 C  410  GLY LYS TRP ARG THR VAL ALA GLY ARG ILE ALA MET ASP          
SEQRES  28 C  410  GLN PHE VAL VAL ASP LEU GLY GLY ASP ARG PRO GLU PRO          
SEQRES  29 C  410  GLY ALA GLU ALA VAL LEU PHE GLY PRO GLY ASP ARG GLY          
SEQRES  30 C  410  GLU PRO THR ALA GLU ASP TRP ALA GLN ALA ALA GLY THR          
SEQRES  31 C  410  ILE ALA TYR GLU ILE VAL THR ARG ILE GLY SER ARG VAL          
SEQRES  32 C  410  PRO ARG VAL TYR VAL ASN GLU                                  
SEQRES   1 D  410  MET GLY SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 D  410  VAL PRO ARG GLY SER HIS MET SER GLU THR THR ALA ARG          
SEQRES   3 D  410  ARG ASP ALA ASP ALA VAL LEU ARG ALA ARG ALA GLU ILE          
SEQRES   4 D  410  ASP LEU ALA ALA LEU ARG ALA ASN VAL ARG ALA LEU ARG          
SEQRES   5 D  410  GLU ARG ALA PRO GLY ALA ALA LEU MET ALA VAL VAL LYS          
SEQRES   6 D  410  ALA ASP ALA TYR GLY HIS GLY ALA ILE PRO CYS ALA ARG          
SEQRES   7 D  410  ALA ALA VAL ALA ALA GLY ALA THR TRP LEU GLY THR ALA          
SEQRES   8 D  410  THR PRO GLN GLU ALA LEU ALA LEU ARG ALA ALA GLU PRO          
SEQRES   9 D  410  GLY LEU PRO ASP ASP VAL ARG ILE MET CYS TRP LEU TRP          
SEQRES  10 D  410  THR PRO GLY GLY PRO TRP ARG GLU ALA VAL GLU ALA ARG          
SEQRES  11 D  410  LEU ASP VAL SER VAL SER ALA MET TRP ALA MET GLU GLU          
SEQRES  12 D  410  VAL THR GLY ALA ALA ARG ALA ALA GLY VAL PRO ALA ARG          
SEQRES  13 D  410  VAL GLN LEU KCX ALA ASP THR GLY LEU GLY ARG GLY GLY          
SEQRES  14 D  410  CYS GLN PRO GLY ALA ASP TRP GLU ARG LEU VAL GLY ALA          
SEQRES  15 D  410  ALA LEU ARG ALA GLU GLU GLU GLY LEU LEU ARG VAL THR          
SEQRES  16 D  410  GLY LEU TRP SER HIS PHE ALA CYS ALA ASP GLU PRO GLY          
SEQRES  17 D  410  HIS PRO SER ILE ALA ALA GLN LEU THR ARG PHE ARG GLU          
SEQRES  18 D  410  MET THR ALA TYR ALA GLU GLN ARG GLY LEU ARG PRO GLU          
SEQRES  19 D  410  VAL ARG HIS ILE ALA ASN SER PRO ALA THR LEU THR LEU          
SEQRES  20 D  410  PRO ASP ALA HIS PHE ASP LEU VAL ARG PRO GLY ILE ALA          
SEQRES  21 D  410  MET TYR GLY VAL SER PRO SER PRO GLU ILE GLY THR PRO          
SEQRES  22 D  410  ALA ASP PHE GLY LEU ARG PRO VAL MET THR LEU ALA ALA          
SEQRES  23 D  410  SER LEU ALA LEU VAL LYS GLN VAL PRO GLY GLY HIS GLY          
SEQRES  24 D  410  VAL SER TYR GLY HIS HIS TYR THR THR PRO GLY GLU THR          
SEQRES  25 D  410  THR LEU GLY LEU VAL PRO LEU GLY TYR ALA ASP GLY ILE          
SEQRES  26 D  410  PRO ARG HIS ALA SER SER SER GLY PRO VAL LEU VAL ASP          
SEQRES  27 D  410  GLY LYS TRP ARG THR VAL ALA GLY ARG ILE ALA MET ASP          
SEQRES  28 D  410  GLN PHE VAL VAL ASP LEU GLY GLY ASP ARG PRO GLU PRO          
SEQRES  29 D  410  GLY ALA GLU ALA VAL LEU PHE GLY PRO GLY ASP ARG GLY          
SEQRES  30 D  410  GLU PRO THR ALA GLU ASP TRP ALA GLN ALA ALA GLY THR          
SEQRES  31 D  410  ILE ALA TYR GLU ILE VAL THR ARG ILE GLY SER ARG VAL          
SEQRES  32 D  410  PRO ARG VAL TYR VAL ASN GLU                                  
MODRES 5FAJ KCX A  141  LYS  MODIFIED RESIDUE                                   
MODRES 5FAJ KCX B  141  LYS  MODIFIED RESIDUE                                   
MODRES 5FAJ KCX C  141  LYS  MODIFIED RESIDUE                                   
MODRES 5FAJ KCX D  141  LYS  MODIFIED RESIDUE                                   
HET    KCX  A 141      12                                                       
HET    KCX  B 141      12                                                       
HET    KCX  C 141      12                                                       
HET    KCX  D 141      12                                                       
HET    DCS  A 401      22                                                       
HET     NA  A 402       1                                                       
HET     CL  A 403       1                                                       
HET    DCS  B 401      22                                                       
HET     NA  B 402       1                                                       
HET     CL  B 403       1                                                       
HET     CL  B 404       1                                                       
HET    DCS  C 401      22                                                       
HET     NA  C 402       1                                                       
HET     NA  C 403       1                                                       
HET     NA  C 404       1                                                       
HET     CL  C 405       1                                                       
HET    DCS  D 401      22                                                       
HET     NA  D 402       1                                                       
HET     CL  D 403       1                                                       
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM     DCS D-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-            
HETNAM   2 DCS  YLMETHYL]-N,O-CYCLOSERYLAMIDE                                   
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETSYN     DCS D-PYRIDOXYL-N,O-CYCLOSERYLAMIDE-5-MONOPHOSPHATE                  
FORMUL   1  KCX    4(C7 H14 N2 O4)                                              
FORMUL   5  DCS    4(C11 H16 N3 O7 P)                                           
FORMUL   6   NA    6(NA 1+)                                                     
FORMUL   7   CL    5(CL 1-)                                                     
FORMUL  20  HOH   *760(H2 O)                                                    
HELIX    1 AA1 ARG A    7  VAL A   13  1                                   7    
HELIX    2 AA2 LEU A   22  ALA A   36  1                                  15    
HELIX    3 AA3 VAL A   45  GLY A   51  1                                   7    
HELIX    4 AA4 GLY A   53  ALA A   64  1                                  12    
HELIX    5 AA5 THR A   73  ALA A   82  1                                  10    
HELIX    6 AA6 PRO A  103  ALA A  110  1                                   8    
HELIX    7 AA7 ALA A  118  GLY A  133  1                                  16    
HELIX    8 AA8 GLY A  154  GLU A  170  1                                  17    
HELIX    9 AA9 HIS A  190  ARG A  210  1                                  21    
HELIX   10 AB1 ASN A  221  LEU A  228  1                                   8    
HELIX   11 AB2 PRO A  229  HIS A  232  5                                   4    
HELIX   12 AB3 PRO A  238  TYR A  243  1                                   6    
HELIX   13 AB4 PRO A  254  GLY A  258  5                                   5    
HELIX   14 AB5 SER A  282  HIS A  286  5                                   5    
HELIX   15 AB6 GLY A  301  GLY A  305  5                                   5    
HELIX   16 AB7 PRO A  307  SER A  311  5                                   5    
HELIX   17 AB8 THR A  361  ALA A  369  1                                   9    
HELIX   18 AB9 ILE A  372  ARG A  379  1                                   8    
HELIX   19 AC1 ALA B   10  LEU B   14  5                                   5    
HELIX   20 AC2 LEU B   22  ALA B   36  1                                  15    
HELIX   21 AC3 VAL B   45  GLY B   51  1                                   7    
HELIX   22 AC4 GLY B   53  ALA B   64  1                                  12    
HELIX   23 AC5 THR B   73  ALA B   82  1                                  10    
HELIX   24 AC6 PRO B  103  ALA B  110  1                                   8    
HELIX   25 AC7 ALA B  118  GLY B  133  1                                  16    
HELIX   26 AC8 GLY B  154  GLU B  170  1                                  17    
HELIX   27 AC9 HIS B  190  ARG B  210  1                                  21    
HELIX   28 AD1 ASN B  221  LEU B  228  1                                   8    
HELIX   29 AD2 PRO B  229  HIS B  232  5                                   4    
HELIX   30 AD3 PRO B  238  TYR B  243  1                                   6    
HELIX   31 AD4 PRO B  254  GLY B  258  5                                   5    
HELIX   32 AD5 SER B  282  HIS B  286  5                                   5    
HELIX   33 AD6 GLY B  301  GLY B  305  5                                   5    
HELIX   34 AD7 PRO B  307  SER B  311  5                                   5    
HELIX   35 AD8 THR B  361  ALA B  369  1                                   9    
HELIX   36 AD9 ILE B  372  ARG B  379  1                                   8    
HELIX   37 AE1 ASP C   11  LEU C   14  5                                   4    
HELIX   38 AE2 LEU C   22  ALA C   36  1                                  15    
HELIX   39 AE3 VAL C   45  GLY C   51  1                                   7    
HELIX   40 AE4 GLY C   53  ALA C   64  1                                  12    
HELIX   41 AE5 THR C   73  ALA C   82  1                                  10    
HELIX   42 AE6 PRO C  103  ALA C  110  1                                   8    
HELIX   43 AE7 ALA C  118  GLY C  133  1                                  16    
HELIX   44 AE8 GLY C  154  GLU C  170  1                                  17    
HELIX   45 AE9 HIS C  190  ARG C  210  1                                  21    
HELIX   46 AF1 ASN C  221  LEU C  228  1                                   8    
HELIX   47 AF2 PRO C  229  HIS C  232  5                                   4    
HELIX   48 AF3 PRO C  238  TYR C  243  1                                   6    
HELIX   49 AF4 PRO C  254  GLY C  258  5                                   5    
HELIX   50 AF5 SER C  282  HIS C  286  5                                   5    
HELIX   51 AF6 GLY C  301  GLY C  305  5                                   5    
HELIX   52 AF7 PRO C  307  SER C  311  5                                   5    
HELIX   53 AF8 THR C  361  ALA C  369  1                                   9    
HELIX   54 AF9 ILE C  372  ARG C  379  1                                   8    
HELIX   55 AG1 ASP D   11  LEU D   14  5                                   4    
HELIX   56 AG2 LEU D   22  ALA D   36  1                                  15    
HELIX   57 AG3 VAL D   45  GLY D   51  1                                   7    
HELIX   58 AG4 GLY D   53  ALA D   64  1                                  12    
HELIX   59 AG5 THR D   73  ALA D   82  1                                  10    
HELIX   60 AG6 PRO D  103  ALA D  110  1                                   8    
HELIX   61 AG7 ALA D  118  GLY D  133  1                                  16    
HELIX   62 AG8 GLY D  154  GLU D  170  1                                  17    
HELIX   63 AG9 HIS D  190  ARG D  210  1                                  21    
HELIX   64 AH1 ASN D  221  LEU D  228  1                                   8    
HELIX   65 AH2 PRO D  229  HIS D  232  5                                   4    
HELIX   66 AH3 PRO D  238  TYR D  243  1                                   6    
HELIX   67 AH4 PRO D  254  GLY D  258  5                                   5    
HELIX   68 AH5 SER D  282  HIS D  286  5                                   5    
HELIX   69 AH6 GLY D  301  GLY D  305  5                                   5    
HELIX   70 AH7 PRO D  307  SER D  311  5                                   5    
HELIX   71 AH8 THR D  361  ALA D  369  1                                   9    
HELIX   72 AH9 ILE D  372  ARG D  379  1                                   8    
SHEET    1 AA1 6 LYS A 321  THR A 324  0                                        
SHEET    2 AA1 6 PRO A 315  VAL A 318 -1  N  VAL A 316   O  ARG A 323           
SHEET    3 AA1 6 GLU A 348  PHE A 352 -1  O  VAL A 350   N  LEU A 317           
SHEET    4 AA1 6 MET A 263  SER A 268 -1  N  ALA A 267   O  ALA A 349           
SHEET    5 AA1 6 ALA A  16  ASP A  21 -1  N  GLU A  19   O  THR A 264           
SHEET    6 AA1 6 ARG A 386  VAL A 389  1  O  VAL A 387   N  ILE A  20           
SHEET    1 AA2 8 VAL A 216  HIS A 218  0                                        
SHEET    2 AA2 8 LEU A 173  TRP A 179  1  N  THR A 176   O  VAL A 216           
SHEET    3 AA2 8 ALA A 136  KCX A 141  1  N  LEU A 140   O  GLY A 177           
SHEET    4 AA2 8 ASP A 113  VAL A 116  1  N  VAL A 114   O  GLN A 139           
SHEET    5 AA2 8 ARG A  92  CYS A  95  1  N  ILE A  93   O  ASP A 113           
SHEET    6 AA2 8 TRP A  68  THR A  71  1  N  LEU A  69   O  MET A  94           
SHEET    7 AA2 8 ALA A  40  VAL A  44  1  N  ALA A  43   O  TRP A  68           
SHEET    8 AA2 8 LEU A 235  VAL A 236  1  O  VAL A 236   N  MET A  42           
SHEET    1 AA3 3 LEU A 271  VAL A 275  0                                        
SHEET    2 AA3 3 THR A 293  VAL A 298 -1  O  LEU A 295   N  LYS A 273           
SHEET    3 AA3 3 PHE A 334  ASP A 337 -1  O  PHE A 334   N  VAL A 298           
SHEET    1 AA4 2 GLY A 280  VAL A 281  0                                        
SHEET    2 AA4 2 TYR A 287  THR A 288 -1  O  TYR A 287   N  VAL A 281           
SHEET    1 AA5 6 LYS B 321  THR B 324  0                                        
SHEET    2 AA5 6 PRO B 315  VAL B 318 -1  N  VAL B 316   O  ARG B 323           
SHEET    3 AA5 6 GLU B 348  PHE B 352 -1  O  VAL B 350   N  LEU B 317           
SHEET    4 AA5 6 MET B 263  SER B 268 -1  N  ALA B 267   O  ALA B 349           
SHEET    5 AA5 6 ALA B  16  ASP B  21 -1  N  GLU B  19   O  THR B 264           
SHEET    6 AA5 6 ARG B 386  VAL B 389  1  O  VAL B 387   N  ILE B  20           
SHEET    1 AA6 8 VAL B 216  HIS B 218  0                                        
SHEET    2 AA6 8 LEU B 173  TRP B 179  1  N  THR B 176   O  VAL B 216           
SHEET    3 AA6 8 ALA B 136  KCX B 141  1  N  LEU B 140   O  GLY B 177           
SHEET    4 AA6 8 ASP B 113  VAL B 116  1  N  VAL B 114   O  ARG B 137           
SHEET    5 AA6 8 ARG B  92  CYS B  95  1  N  ILE B  93   O  ASP B 113           
SHEET    6 AA6 8 TRP B  68  THR B  71  1  N  LEU B  69   O  MET B  94           
SHEET    7 AA6 8 ALA B  40  VAL B  44  1  N  ALA B  43   O  TRP B  68           
SHEET    8 AA6 8 LEU B 235  VAL B 236  1  O  VAL B 236   N  MET B  42           
SHEET    1 AA7 3 LEU B 271  VAL B 275  0                                        
SHEET    2 AA7 3 THR B 293  VAL B 298 -1  O  LEU B 295   N  LYS B 273           
SHEET    3 AA7 3 PHE B 334  ASP B 337 -1  O  PHE B 334   N  VAL B 298           
SHEET    1 AA8 2 GLY B 280  VAL B 281  0                                        
SHEET    2 AA8 2 TYR B 287  THR B 288 -1  O  TYR B 287   N  VAL B 281           
SHEET    1 AA9 6 LYS C 321  THR C 324  0                                        
SHEET    2 AA9 6 PRO C 315  VAL C 318 -1  N  VAL C 316   O  ARG C 323           
SHEET    3 AA9 6 GLU C 348  PHE C 352 -1  O  VAL C 350   N  LEU C 317           
SHEET    4 AA9 6 MET C 263  SER C 268 -1  N  ALA C 267   O  ALA C 349           
SHEET    5 AA9 6 ALA C  16  ASP C  21 -1  N  GLU C  19   O  THR C 264           
SHEET    6 AA9 6 ARG C 386  VAL C 389  1  O  VAL C 387   N  ILE C  20           
SHEET    1 AB1 8 VAL C 216  HIS C 218  0                                        
SHEET    2 AB1 8 LEU C 173  TRP C 179  1  N  THR C 176   O  VAL C 216           
SHEET    3 AB1 8 ALA C 136  KCX C 141  1  N  VAL C 138   O  ARG C 174           
SHEET    4 AB1 8 ASP C 113  VAL C 116  1  N  VAL C 114   O  ARG C 137           
SHEET    5 AB1 8 ARG C  92  CYS C  95  1  N  ILE C  93   O  ASP C 113           
SHEET    6 AB1 8 TRP C  68  THR C  71  1  N  LEU C  69   O  MET C  94           
SHEET    7 AB1 8 ALA C  40  VAL C  44  1  N  ALA C  43   O  TRP C  68           
SHEET    8 AB1 8 LEU C 235  VAL C 236  1  O  VAL C 236   N  MET C  42           
SHEET    1 AB2 3 LEU C 271  VAL C 275  0                                        
SHEET    2 AB2 3 THR C 293  VAL C 298 -1  O  THR C 293   N  VAL C 275           
SHEET    3 AB2 3 PHE C 334  ASP C 337 -1  O  PHE C 334   N  VAL C 298           
SHEET    1 AB3 2 GLY C 280  VAL C 281  0                                        
SHEET    2 AB3 2 TYR C 287  THR C 288 -1  O  TYR C 287   N  VAL C 281           
SHEET    1 AB4 6 LYS D 321  THR D 324  0                                        
SHEET    2 AB4 6 PRO D 315  VAL D 318 -1  N  VAL D 316   O  ARG D 323           
SHEET    3 AB4 6 GLU D 348  PHE D 352 -1  O  VAL D 350   N  LEU D 317           
SHEET    4 AB4 6 MET D 263  SER D 268 -1  N  ALA D 267   O  ALA D 349           
SHEET    5 AB4 6 ALA D  16  ASP D  21 -1  N  GLU D  19   O  THR D 264           
SHEET    6 AB4 6 ARG D 386  VAL D 389  1  O  VAL D 387   N  ILE D  20           
SHEET    1 AB5 8 VAL D 216  HIS D 218  0                                        
SHEET    2 AB5 8 LEU D 173  TRP D 179  1  N  LEU D 178   O  VAL D 216           
SHEET    3 AB5 8 ALA D 136  KCX D 141  1  N  VAL D 138   O  ARG D 174           
SHEET    4 AB5 8 ASP D 113  VAL D 116  1  N  VAL D 114   O  ARG D 137           
SHEET    5 AB5 8 ARG D  92  CYS D  95  1  N  ILE D  93   O  ASP D 113           
SHEET    6 AB5 8 TRP D  68  THR D  71  1  N  LEU D  69   O  MET D  94           
SHEET    7 AB5 8 ALA D  40  VAL D  44  1  N  ALA D  43   O  TRP D  68           
SHEET    8 AB5 8 LEU D 235  VAL D 236  1  O  VAL D 236   N  MET D  42           
SHEET    1 AB6 3 LEU D 271  VAL D 275  0                                        
SHEET    2 AB6 3 THR D 293  VAL D 298 -1  O  LEU D 295   N  LYS D 273           
SHEET    3 AB6 3 PHE D 334  GLY D 339 -1  O  PHE D 334   N  VAL D 298           
SHEET    1 AB7 2 GLY D 280  VAL D 281  0                                        
SHEET    2 AB7 2 TYR D 287  THR D 288 -1  O  TYR D 287   N  VAL D 281           
LINK         C   LEU A 140                 N   KCX A 141     1555   1555  1.33  
LINK         C   KCX A 141                 N   ALA A 142     1555   1555  1.35  
LINK         OG  SER A 180                NA    NA A 402     1555   1555  2.92  
LINK         O   HIS A 181                NA    NA A 402     1555   1555  3.12  
LINK         C   LEU B 140                 N   KCX B 141     1555   1555  1.33  
LINK         C   KCX B 141                 N   ALA B 142     1555   1555  1.34  
LINK         OG  SER B 180                NA    NA B 402     1555   1555  3.09  
LINK         O   HIS B 181                NA    NA B 402     1555   1555  3.00  
LINK         C   LEU C 140                 N   KCX C 141     1555   1555  1.33  
LINK         C   KCX C 141                 N   ALA C 142     1555   1555  1.34  
LINK         OG  SER C 180                NA    NA C 402     1555   1555  2.98  
LINK         O   HIS C 181                NA    NA C 402     1555   1555  3.11  
LINK         O   ALA C 231                NA    NA C 403     1555   1555  2.63  
LINK         O   HIS C 232                NA    NA C 403     1555   1555  2.98  
LINK         O   LEU C 235                NA    NA C 403     1555   1555  2.64  
LINK         OG  SER C 312                NA    NA C 404     1555   1555  2.87  
LINK         C   LEU D 140                 N   KCX D 141     1555   1555  1.33  
LINK         C   KCX D 141                 N   ALA D 142     1555   1555  1.34  
LINK         OG  SER D 312                NA    NA D 402     1555   1555  2.85  
CISPEP   1 GLU A   84    PRO A   85          0         0.81                     
CISPEP   2 GLU B   84    PRO B   85          0        -1.08                     
CISPEP   3 GLU C   84    PRO C   85          0         0.37                     
CISPEP   4 GLU D   84    PRO D   85          0        -1.58                     
SITE     1 AC1 22 LYS A  46  TYR A  50  TRP A  96  ARG A 148                    
SITE     2 AC1 22 TRP A 179  HIS A 181  ASN A 221  SER A 222                    
SITE     3 AC1 22 ARG A 237  PRO A 238  GLY A 239  ILE A 240                    
SITE     4 AC1 22 TYR A 374  HOH A 502  HOH A 505  HOH A 615                    
SITE     5 AC1 22 TYR B 283  TYR B 302  ALA B 330  MET B 331                    
SITE     6 AC1 22 HOH B 534  HOH B 545                                          
SITE     1 AC2  8 ALA A 142  ASP A 143  THR A 144  LEU A 146                    
SITE     2 AC2  8 SER A 180  HIS A 181  GLN A 196   CL A 403                    
SITE     1 AC3  6 KCX A 141  ASP A 143  ARG A 148  GLY A 149                    
SITE     2 AC3  6 GLY A 150   NA A 402                                          
SITE     1 AC4 20 TYR A 283  TYR A 302  ALA A 330  MET A 331                    
SITE     2 AC4 20 HOH A 530  HOH A 533  LYS B  46  TYR B  50                    
SITE     3 AC4 20 ARG B 148  TRP B 179  HIS B 181  ASN B 221                    
SITE     4 AC4 20 SER B 222  ARG B 237  PRO B 238  GLY B 239                    
SITE     5 AC4 20 ILE B 240  TYR B 374  HOH B 502  HOH B 556                    
SITE     1 AC5  8 ASP B 143  THR B 144  GLY B 145  LEU B 146                    
SITE     2 AC5  8 SER B 180  HIS B 181  GLN B 196   CL B 403                    
SITE     1 AC6  7 KCX B 141  ASP B 143  LEU B 146  ARG B 148                    
SITE     2 AC6  7 GLY B 149  GLY B 150   NA B 402                               
SITE     1 AC7  3 HIS B 286  SER B 311  SER B 312                               
SITE     1 AC8 20 LYS C  46  TYR C  50  TRP C  96  ARG C 148                    
SITE     2 AC8 20 TRP C 179  HIS C 181  ASN C 221  SER C 222                    
SITE     3 AC8 20 ARG C 237  PRO C 238  GLY C 239  ILE C 240                    
SITE     4 AC8 20 TYR C 374  HOH C 513  HOH C 577  TYR D 283                    
SITE     5 AC8 20 TYR D 302  ALA D 330  MET D 331  HOH D 504                    
SITE     1 AC9  8 ASP C 143  THR C 144  GLY C 145  LEU C 146                    
SITE     2 AC9  8 SER C 180  HIS C 181  GLN C 196   CL C 405                    
SITE     1 AD1  6 HIS C 218  ILE C 219  ALA C 220  ALA C 231                    
SITE     2 AD1  6 HIS C 232  LEU C 235                                          
SITE     1 AD2  2 HIS C 286  SER C 312                                          
SITE     1 AD3  6 KCX C 141  ASP C 143  ARG C 148  GLY C 149                    
SITE     2 AD3  6 GLY C 150   NA C 402                                          
SITE     1 AD4 18 TYR C 283  TYR C 302  ALA C 330  MET C 331                    
SITE     2 AD4 18 LYS D  46  TYR D  50  TRP D  96  ARG D 148                    
SITE     3 AD4 18 TRP D 179  HIS D 181  ASN D 221  SER D 222                    
SITE     4 AD4 18 ARG D 237  PRO D 238  GLY D 239  ILE D 240                    
SITE     5 AD4 18 TYR D 374  HOH D 501                                          
SITE     1 AD5  3 HIS D 286  SER D 311  SER D 312                               
SITE     1 AD6  4 KCX D 141  ARG D 148  GLY D 149  GLY D 150                    
CRYST1   79.740   88.710  109.140  90.00 102.25  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012541  0.000000  0.002723        0.00000                         
SCALE2      0.000000  0.011273  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009376        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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