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Database: PDB
Entry: 4J7C
LinkDB: 4J7C
Original site: 4J7C 
HEADER    TRANSPORT PROTEIN                       13-FEB-13   4J7C              
TITLE     KTRAB POTASSIUM TRANSPORTER FROM BACILLUS SUBTILIS                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KTR SYSTEM POTASSIUM UPTAKE PROTEIN A;                     
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: K(+)-UPTAKE PROTEIN KTRA;                                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: KTR SYSTEM POTASSIUM UPTAKE PROTEIN B;                     
COMPND   9 CHAIN: I, J, K, L;                                                   
COMPND  10 SYNONYM: K(+)-UPTAKE PROTEIN KTRB;                                   
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: KTRA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  11 ORGANISM_TAXID: 224308;                                              
SOURCE  12 STRAIN: 168;                                                         
SOURCE  13 GENE: KTRB;                                                          
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    KTRB PORE-FORMING MEMBRANE PROTEIN, KTRA REGULATORY CYTOSOLIC RING,   
KEYWDS   2 POTASSIUM ION TRANSPORT, POTASSIUM, CELL MEMBRANE, CYTOSOL,          
KEYWDS   3 TRANSPORT PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.S.VIEIRA-PIRES,J.H.MORAIS-CABRAL                                    
REVDAT   2   07-AUG-13 4J7C    1       JRNL                                     
REVDAT   1   17-APR-13 4J7C    0                                                
JRNL        AUTH   R.S.VIEIRA-PIRES,A.SZOLLOSI,J.H.MORAIS-CABRAL                
JRNL        TITL   THE STRUCTURE OF THE KTRAB POTASSIUM TRANSPORTER             
JRNL        REF    NATURE                        V. 496   323 2013              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   23598340                                                     
JRNL        DOI    10.1038/NATURE12055                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 147.44                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 79.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 60372                          
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) : 0.259                           
REMARK   3   R VALUE            (WORKING SET) : 0.258                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3061                            
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) : 3.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1014                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 19.36                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 55                           
REMARK   3   BIN FREE R VALUE                    : 0.3180                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 26744                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 252                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.88000                                             
REMARK   3    B22 (A**2) : -2.82000                                             
REMARK   3    B33 (A**2) : 3.52000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.32000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.715         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.521         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.155        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.832                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.834                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 27048 ; 0.008 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 36781 ; 1.385 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3432 ; 5.361 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1003 ;33.762 ;24.357       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  4579 ;15.213 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    97 ; 9.637 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4490 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 19505 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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   NUMBER OF DIFFERENT NCS GROUPS : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D E F G H                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      7       A     222      1                      
REMARK   3           1     B      7       B     222      1                      
REMARK   3           1     C      7       C     222      1                      
REMARK   3           1     D      7       D     222      1                      
REMARK   3           1     E      7       E     222      1                      
REMARK   3           1     F      7       F     222      1                      
REMARK   3           1     G      7       G     222      1                      
REMARK   3           1     H      7       H     222      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      1    A (A**2):   1591 ; 9.310 ; 0.500           
REMARK   3   TIGHT THERMAL      1    B (A**2):   1591 ;11.100 ; 0.500           
REMARK   3   TIGHT THERMAL      1    C (A**2):   1591 ;18.950 ; 0.500           
REMARK   3   TIGHT THERMAL      1    D (A**2):   1591 ;14.580 ; 0.500           
REMARK   3   TIGHT THERMAL      1    E (A**2):   1591 ;14.120 ; 0.500           
REMARK   3   TIGHT THERMAL      1    F (A**2):   1591 ; 8.910 ; 0.500           
REMARK   3   TIGHT THERMAL      1    G (A**2):   1591 ;15.390 ; 0.500           
REMARK   3   TIGHT THERMAL      1    H (A**2):   1591 ;13.250 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : I J K L                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     I     16       I     445      1                      
REMARK   3           1     J     16       J     445      1                      
REMARK   3           1     K     16       K     445      1                      
REMARK   3           1     L     16       L     445      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      2    I (A**2):   3220 ; 6.940 ; 0.500           
REMARK   3   TIGHT THERMAL      2    J (A**2):   3220 ; 7.330 ; 0.500           
REMARK   3   TIGHT THERMAL      2    K (A**2):   3220 ; 8.520 ; 0.500           
REMARK   3   TIGHT THERMAL      2    L (A**2):   3220 ; 7.020 ; 0.500           
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 USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES: REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 4J7C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-FEB-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB077687.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933400                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 87633                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 148.186                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.16300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.01300                            
REMARK 200  R SYM FOR SHELL            (I) : 1.34700                            
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: PHASER                                                
REMARK 200 STARTING MODEL: 3PJZ, 2HMW                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M (N-(2-ACETAMIDO)-IMINODIACETIC      
REMARK 280  ACID) BUFFER, 20% POLYETHYLENE GLYCOL 400, 0.2M AMMONIUM SULFATE,   
REMARK 280  PH 6.5, VAPOR DIFFUSION, SITTING DROP, 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       70.09500            
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, 3                                                 
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 300 REMARK: THE KNOWN BIOLOGICAL RELEVANT ASSEMBLY IS ONE OCTAMER BOUND  
REMARK 300 TO ONE DIMER, THEREFORE EITHER "CHAINS: A, B, C, D, E, F, G, H, AND  
REMARK 300 CHAINS: I,J" OR "CHAINS: A, B, C, D, E, F, G, H, AND CHAINS: K,L".   
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: DECAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J          
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: DECAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, K, L          
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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 53580 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 136910 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -318.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,            
REMARK 350                    AND CHAINS: J, K, L                               
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     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     ASN A     6                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     ARG C     3                                                      
REMARK 465     ILE C     4                                                      
REMARK 465     LYS C     5                                                      
REMARK 465     ASN C     6                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     ARG D     3                                                      
REMARK 465     ILE D     4                                                      
REMARK 465     LYS D     5                                                      
REMARK 465     MET E     1                                                      
REMARK 465     GLY E     2                                                      
REMARK 465     ARG E     3                                                      
REMARK 465     ILE E     4                                                      
REMARK 465     LYS E     5                                                      
REMARK 465     ASN E     6                                                      
REMARK 465     MET F     1                                                      
REMARK 465     GLY F     2                                                      
REMARK 465     ARG F     3                                                      
REMARK 465     ILE F     4                                                      
REMARK 465     LYS F     5                                                      
REMARK 465     MET G     1                                                      
REMARK 465     GLY G     2                                                      
REMARK 465     ARG G     3                                                      
REMARK 465     ILE G     4                                                      
REMARK 465     LYS G     5                                                      
REMARK 465     ASN G     6                                                      
REMARK 465     MET H     1                                                      
REMARK 465     GLY H     2                                                      
REMARK 465     ARG H     3                                                      
REMARK 465     ILE H     4                                                      
REMARK 465     LYS H     5                                                      
REMARK 465     MET I   -19                                                      
REMARK 465     GLY I   -18                                                      
REMARK 465     SER I   -17                                                      
REMARK 465     SER I   -16                                                      
REMARK 465     HIS I   -15                                                      
REMARK 465     HIS I   -14                                                      
REMARK 465     HIS I   -13                                                      
REMARK 465     HIS I   -12                                                      
REMARK 465     HIS I   -11                                                      
REMARK 465     HIS I   -10                                                      
REMARK 465     SER I    -9                                                      
REMARK 465     SER I    -8                                                      
REMARK 465     GLY I    -7                                                      
REMARK 465     LEU I    -6                                                      
REMARK 465     VAL I    -5                                                      
REMARK 465     PRO I    -4                                                      
REMARK 465     ARG I    -3                                                      
REMARK 465     GLY I    -2                                                      
REMARK 465     SER I    -1                                                      
REMARK 465     HIS I     0                                                      
REMARK 465     MET I     1                                                      
REMARK 465     THR I     2                                                      
REMARK 465     LEU I     3                                                      
REMARK 465     GLN I     4                                                      
REMARK 465     LYS I     5                                                      
REMARK 465     ASP I     6                                                      
REMARK 465     LYS I     7                                                      
REMARK 465     VAL I     8                                                      
REMARK 465     ILE I     9                                                      
REMARK 465     LYS I    10                                                      
REMARK 465     TRP I    11                                                      
REMARK 465     VAL I    12                                                      
REMARK 465     ARG I    13                                                      
REMARK 465     PHE I    14                                                      
REMARK 465     GLY I   103                                                      
REMARK 465     LYS I   104                                                      
REMARK 465     MET J   -19                                                      
REMARK 465     GLY J   -18                                                      
REMARK 465     SER J   -17                                                      
REMARK 465     SER J   -16                                                      
REMARK 465     HIS J   -15                                                      
REMARK 465     HIS J   -14                                                      
REMARK 465     HIS J   -13                                                      
REMARK 465     HIS J   -12                                                      
REMARK 465     HIS J   -11                                                      
REMARK 465     HIS J   -10                                                      
REMARK 465     SER J    -9                                                      
REMARK 465     SER J    -8                                                      
REMARK 465     GLY J    -7                                                      
REMARK 465     LEU J    -6                                                      
REMARK 465     VAL J    -5                                                      
REMARK 465     PRO J    -4                                                      
REMARK 465     ARG J    -3                                                      
REMARK 465     GLY J    -2                                                      
REMARK 465     SER J    -1                                                      
REMARK 465     HIS J     0                                                      
REMARK 465     MET J     1                                                      
REMARK 465     THR J     2                                                      
REMARK 465     LEU J     3                                                      
REMARK 465     GLN J     4                                                      
REMARK 465     LYS J     5                                                      
REMARK 465     ASP J     6                                                      
REMARK 465     LYS J     7                                                      
REMARK 465     VAL J     8                                                      
REMARK 465     ILE J     9                                                      
REMARK 465     LYS J    10                                                      
REMARK 465     TRP J    11                                                      
REMARK 465     VAL J    12                                                      
REMARK 465     ARG J    13                                                      
REMARK 465     PHE J    14                                                      
REMARK 465     GLY J   103                                                      
REMARK 465     LYS J   104                                                      
REMARK 465     MET K   -19                                                      
REMARK 465     GLY K   -18                                                      
REMARK 465     SER K   -17                                                      
REMARK 465     SER K   -16                                                      
REMARK 465     HIS K   -15                                                      
REMARK 465     HIS K   -14                                                      
REMARK 465     HIS K   -13                                                      
REMARK 465     HIS K   -12                                                      
REMARK 465     HIS K   -11                                                      
REMARK 465     HIS K   -10                                                      
REMARK 465     SER K    -9                                                      
REMARK 465     SER K    -8                                                      
REMARK 465     GLY K    -7                                                      
REMARK 465     LEU K    -6                                                      
REMARK 465     VAL K    -5                                                      
REMARK 465     PRO K    -4                                                      
REMARK 465     ARG K    -3                                                      
REMARK 465     GLY K    -2                                                      
REMARK 465     SER K    -1                                                      
REMARK 465     HIS K     0                                                      
REMARK 465     MET K     1                                                      
REMARK 465     THR K     2                                                      
REMARK 465     LEU K     3                                                      
REMARK 465     GLN K     4                                                      
REMARK 465     LYS K     5                                                      
REMARK 465     ASP K     6                                                      
REMARK 465     LYS K     7                                                      
REMARK 465     VAL K     8                                                      
REMARK 465     ILE K     9                                                      
REMARK 465     LYS K    10                                                      
REMARK 465     TRP K    11                                                      
REMARK 465     VAL K    12                                                      
REMARK 465     ARG K    13                                                      
REMARK 465     PHE K    14                                                      
REMARK 465     GLY K   103                                                      
REMARK 465     LYS K   104                                                      
REMARK 465     MET L   -19                                                      
REMARK 465     GLY L   -18                                                      
REMARK 465     SER L   -17                                                      
REMARK 465     SER L   -16                                                      
REMARK 465     HIS L   -15                                                      
REMARK 465     HIS L   -14                                                      
REMARK 465     HIS L   -13                                                      
REMARK 465     HIS L   -12                                                      
REMARK 465     HIS L   -11                                                      
REMARK 465     HIS L   -10                                                      
REMARK 465     SER L    -9                                                      
REMARK 465     SER L    -8                                                      
REMARK 465     GLY L    -7                                                      
REMARK 465     LEU L    -6                                                      
REMARK 465     VAL L    -5                                                      
REMARK 465     PRO L    -4                                                      
REMARK 465     ARG L    -3                                                      
REMARK 465     GLY L    -2                                                      
REMARK 465     SER L    -1                                                      
REMARK 465     HIS L     0                                                      
REMARK 465     MET L     1                                                      
REMARK 465     THR L     2                                                      
REMARK 465     LEU L     3                                                      
REMARK 465     GLN L     4                                                      
REMARK 465     LYS L     5                                                      
REMARK 465     ASP L     6                                                      
REMARK 465     LYS L     7                                                      
REMARK 465     VAL L     8                                                      
REMARK 465     ILE L     9                                                      
REMARK 465     LYS L    10                                                      
REMARK 465     TRP L    11                                                      
REMARK 465     VAL L    12                                                      
REMARK 465     ARG L    13                                                      
REMARK 465     PHE L    14                                                      
REMARK 465     GLY L   103                                                      
REMARK 465     LYS L   104                                                      
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   CD1  ILE I   150     CD2  LEU I   162              1.70            
REMARK 500   CD1  ILE K   150     CD2  LEU K   162              2.06            
REMARK 500   CD   LYS E   161     O    MET E   222              2.16            
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   NH2  ARG E   160     CA   ASP G   163     2646     1.13            
REMARK 500   NH2  ARG E   160     CB   ASP G   163     2646     1.34            
REMARK 500   O    ARG E   160     NZ   LYS G   165     2646     1.40            
REMARK 500   NH1  ARG E   160     N    ASP G   163     2646     1.52            
REMARK 500   NH2  ARG E   160     C    ASP G   163     2646     1.61            
REMARK 500   CD   ARG E   160     O    ARG G   160     2646     1.69            
REMARK 500   CD   ARG F   160     CD1  ILE I    39     2545     1.75            
REMARK 500   CZ   ARG E   160     N    ASP G   163     2646     1.81            
REMARK 500   NH2  ARG E   160     N    ASP G   163     2646     1.81            
REMARK 500   CA   LYS E   161     NZ   LYS G   165     2646     1.82            
REMARK 500   NH2  ARG E   160     O    ASP G   163     2646     1.89            
REMARK 500   C    ARG E   160     NZ   LYS G   165     2646     1.92            
REMARK 500   O    ARG E   160     CE   LYS G   165     2646     1.94            
REMARK 500   OD2  ASP E   163     NZ   LYS G   161     2646     1.94            
REMARK 500   NH1  ARG A   173     ND2  ASN G   171     2656     1.94            
REMARK 500   NE   ARG E   160     O    ARG G   160     2646     1.96            
REMARK 500   NH1  ARG E   160     C    LEU G   162     2646     1.96            
REMARK 500   C    LYS E   161     NZ   LYS G   165     2646     2.06            
REMARK 500   N    LYS E   161     NZ   LYS G   165     2646     2.07            
REMARK 500   CZ   ARG E   160     CA   ASP G   163     2646     2.15            
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    HIS A  51   CG    HIS A  51   ND1    -0.125                       
REMARK 500    HIS A  51   CE1   HIS A  51   NE2    -0.099                       
REMARK 500    HIS D  51   CE1   HIS D  51   NE2    -0.088                       
REMARK 500    HIS E  51   CG    HIS E  51   ND1    -0.137                       
REMARK 500    HIS E  51   CE1   HIS E  51   NE2    -0.099                       
REMARK 500    HIS H  51   CG    HIS H  51   CD2    -0.142                       
REMARK 500    HIS I 259   CG    HIS I 259   CD2     0.057                       
REMARK 500    GLN J 155   CB    GLN J 155   CG      0.257                       
REMARK 500    GLN J 155   CD    GLN J 155   NE2     0.187                       
REMARK 500    HIS J 259   CG    HIS J 259   CD2     0.060                       
REMARK 500    HIS L 259   CG    HIS L 259   CD2     0.054                       
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    HIS A  51   CB  -  CA  -  C   ANGL. DEV. = -13.9 DEGREES          
REMARK 500    HIS D  51   CB  -  CA  -  C   ANGL. DEV. = -12.6 DEGREES          
REMARK 500    HIS E  51   CB  -  CA  -  C   ANGL. DEV. = -14.1 DEGREES          
REMARK 500    HIS H  51   CB  -  CA  -  C   ANGL. DEV. = -14.6 DEGREES          
REMARK 500    HIS H  51   CG  -  ND1 -  CE1 ANGL. DEV. =   9.9 DEGREES          
REMARK 500    HIS H  51   ND1 -  CE1 -  NE2 ANGL. DEV. = -12.8 DEGREES          
REMARK 500    HIS H  51   CE1 -  NE2 -  CD2 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    LEU I 249   CA  -  CB  -  CG  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    ILE I 314   CG1 -  CB  -  CG2 ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ARG I 331   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    PRO J 154   CA  -  N   -  CD  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    MET J 395   N   -  CA  -  C   ANGL. DEV. = -16.5 DEGREES          
REMARK 500    ARG K 151   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    PRO L 182   C   -  N   -  CA  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    MET L 395   N   -  CA  -  C   ANGL. DEV. = -16.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  77       43.77    -95.64                                   
REMARK 500    HIS A 123       78.73   -112.04                                   
REMARK 500    SER A 192       70.37     39.77                                   
REMARK 500    HIS B  51      135.64   -174.87                                   
REMARK 500    ALA B  77       43.81    -96.42                                   
REMARK 500    HIS B 123       79.83   -112.80                                   
REMARK 500    HIS C  51      135.22   -174.59                                   
REMARK 500    ALA C  77       44.42    -95.27                                   
REMARK 500    HIS C 123       79.67   -112.59                                   
REMARK 500    ALA D  77       43.29    -95.67                                   
REMARK 500    HIS D 123       79.77   -113.49                                   
REMARK 500    ALA E  77       45.31    -95.58                                   
REMARK 500    HIS E 123       79.55   -112.88                                   
REMARK 500    SER E 192       73.61     38.21                                   
REMARK 500    HIS F  51      135.47   -176.01                                   
REMARK 500    ALA F  77       45.30    -95.39                                   
REMARK 500    SER F 192       53.39     35.12                                   
REMARK 500    HIS G  51      135.20   -175.26                                   
REMARK 500    ALA G  77       44.46    -95.28                                   
REMARK 500    HIS G 123       78.77   -113.68                                   
REMARK 500    ALA H  77       45.20    -94.94                                   
REMARK 500    HIS H 123       79.96   -112.86                                   
REMARK 500    PRO I  44      136.45    -39.87                                   
REMARK 500    THR I  61      -70.28    -66.88                                   
REMARK 500    ASN I 119       66.36     34.69                                   
REMARK 500    SER I 137      -72.27    -58.66                                   
REMARK 500    ALA I 176      -73.03    -52.45                                   
REMARK 500    LEU I 185       15.99     80.98                                   
REMARK 500    SER I 187      -39.03    -37.21                                   
REMARK 500    ASN I 253      113.76    -39.09                                   
REMARK 500    LEU I 257      -11.04     81.67                                   
REMARK 500    HIS I 259       50.42   -104.81                                   
REMARK 500    SER I 288       59.39   -107.54                                   
REMARK 500    SER I 309     -156.98   -153.98                                   
REMARK 500    PHE I 339       19.82     50.89                                   
REMARK 500    GLN I 432       78.92   -112.81                                   
REMARK 500    PRO J  44      136.73    -39.94                                   
REMARK 500    THR J  61      -70.00    -66.17                                   
REMARK 500    ASN J 119       66.76     34.41                                   
REMARK 500    SER J 137      -72.17    -59.80                                   
REMARK 500    VAL J 153       38.37   -141.64                                   
REMARK 500    PRO J 154       43.50   -108.04                                   
REMARK 500    ALA J 176      -72.23    -52.16                                   
REMARK 500    THR J 223       28.09    -79.98                                   
REMARK 500    ASN J 253      114.20    -38.85                                   
REMARK 500    LEU J 257       -8.29     82.76                                   
REMARK 500    HIS J 259       43.66   -104.91                                   
REMARK 500    SER J 288       59.16   -106.09                                   
REMARK 500    SER J 309     -157.32   -153.01                                   
REMARK 500    PHE J 339       19.56     50.82                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      79 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR I  394     MET I  395                  139.05                    
REMARK 500 THR J  394     MET J  395                  143.67                    
REMARK 500 MET J  395     GLY J  396                 -148.56                    
REMARK 500 THR K  394     MET K  395                  136.09                    
REMARK 500 ILE L  314     LYS L  315                 -148.56                    
REMARK 500 THR L  394     MET L  395                  144.86                    
REMARK 500 MET L  395     GLY L  396                 -148.69                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                               K I 501   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL I 391   O                                                      
REMARK 620 2 ALA I 176   O   111.7                                              
REMARK 620 3 THR I  61   O    70.7  74.1                                        
REMARK 620 4 THR I 278   O    73.7 139.7 139.0                                  
REMARK 620 5 ASN I 175   O   141.2  73.5 141.9  79.1                            
REMARK 620 6 THR I 390   O    80.0 136.7  71.1  83.4 123.9                      
REMARK 620 7 ALA I 279   O    76.0  70.0 116.1  73.1  69.9 150.2                
REMARK 620 8 VAL I  60   O   140.1  74.6  73.8 128.0  78.7  71.5 137.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K L 501   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL L 391   O                                                      
REMARK 620 2 ALA L 176   O   109.3                                              
REMARK 620 3 ASN L 175   O   142.9  76.1                                        
REMARK 620 4 THR L  61   O    67.4  72.5 143.4                                  
REMARK 620 5 THR L 278   O    74.9 142.2  79.5 137.0                            
REMARK 620 6 THR L 390   O    76.7 135.4 126.1  69.6  82.4                      
REMARK 620 7 ALA L 279   O    77.3  70.2  70.1 114.9  74.5 148.8                
REMARK 620 8 VAL L  60   O   134.5  77.0  82.6  72.4 127.9  69.9 141.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K K 501   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL K 391   O                                                      
REMARK 620 2 THR K  61   O    69.2                                              
REMARK 620 3 ALA K 176   O   109.1  72.7                                        
REMARK 620 4 ASN K 175   O   139.7 142.7  74.3                                  
REMARK 620 5 THR K 278   O    74.4 138.9 139.2  78.4                            
REMARK 620 6 THR K 390   O    78.8  70.3 136.0 127.7  84.7                      
REMARK 620 7 ALA K 279   O    75.4 114.4  69.4  68.3  72.7 149.4                
REMARK 620 8 VAL K  60   O   138.6  73.4  75.2  81.7 129.9  72.3 138.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K J 501   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA J 176   O                                                      
REMARK 620 2 THR J  61   O    74.0                                              
REMARK 620 3 ASN J 175   O    75.8 147.3                                        
REMARK 620 4 VAL J 391   O   107.1  67.2 135.1                                  
REMARK 620 5 THR J 390   O   140.9  72.0 129.5  76.7                            
REMARK 620 6 THR J 278   O   136.8 134.5  77.4  70.9  81.9                      
REMARK 620 7 VAL J  60   O    78.3  76.2  85.7 139.2  75.3 132.4                
REMARK 620 8 ALA J 279   O    68.4 112.3  66.7  73.0 144.0  70.1 140.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP F 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP G 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP H 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K I 501                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K J 501                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K K 501                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K L 501                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4J90   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4J91   RELATED DB: PDB                                   
DBREF  4J7C A    1   222  UNP    O32080   KTRA_BACSU       1    222             
DBREF  4J7C B    1   222  UNP    O32080   KTRA_BACSU       1    222             
DBREF  4J7C C    1   222  UNP    O32080   KTRA_BACSU       1    222             
DBREF  4J7C D    1   222  UNP    O32080   KTRA_BACSU       1    222             
DBREF  4J7C E    1   222  UNP    O32080   KTRA_BACSU       1    222             
DBREF  4J7C F    1   222  UNP    O32080   KTRA_BACSU       1    222             
DBREF  4J7C G    1   222  UNP    O32080   KTRA_BACSU       1    222             
DBREF  4J7C H    1   222  UNP    O32080   KTRA_BACSU       1    222             
DBREF  4J7C I    1   445  UNP    O32081   KTRB_BACSU       1    445             
DBREF  4J7C J    1   445  UNP    O32081   KTRB_BACSU       1    445             
DBREF  4J7C K    1   445  UNP    O32081   KTRB_BACSU       1    445             
DBREF  4J7C L    1   445  UNP    O32081   KTRB_BACSU       1    445             
SEQADV 4J7C VAL A   22  UNP  O32080    CYS    22 ENGINEERED MUTATION            
SEQADV 4J7C VAL B   22  UNP  O32080    CYS    22 ENGINEERED MUTATION            
SEQADV 4J7C VAL C   22  UNP  O32080    CYS    22 ENGINEERED MUTATION            
SEQADV 4J7C VAL D   22  UNP  O32080    CYS    22 ENGINEERED MUTATION            
SEQADV 4J7C VAL E   22  UNP  O32080    CYS    22 ENGINEERED MUTATION            
SEQADV 4J7C VAL F   22  UNP  O32080    CYS    22 ENGINEERED MUTATION            
SEQADV 4J7C VAL G   22  UNP  O32080    CYS    22 ENGINEERED MUTATION            
SEQADV 4J7C VAL H   22  UNP  O32080    CYS    22 ENGINEERED MUTATION            
SEQADV 4J7C MET I  -19  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C GLY I  -18  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER I  -17  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER I  -16  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS I  -15  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS I  -14  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS I  -13  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS I  -12  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS I  -11  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS I  -10  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER I   -9  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER I   -8  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C GLY I   -7  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C LEU I   -6  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C VAL I   -5  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C PRO I   -4  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C ARG I   -3  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C GLY I   -2  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER I   -1  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS I    0  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C MET J  -19  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C GLY J  -18  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER J  -17  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER J  -16  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS J  -15  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS J  -14  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS J  -13  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS J  -12  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS J  -11  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS J  -10  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER J   -9  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER J   -8  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C GLY J   -7  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C LEU J   -6  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C VAL J   -5  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C PRO J   -4  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C ARG J   -3  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C GLY J   -2  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER J   -1  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS J    0  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C MET K  -19  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C GLY K  -18  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER K  -17  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER K  -16  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS K  -15  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS K  -14  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS K  -13  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS K  -12  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS K  -11  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS K  -10  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER K   -9  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER K   -8  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C GLY K   -7  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C LEU K   -6  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C VAL K   -5  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C PRO K   -4  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C ARG K   -3  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C GLY K   -2  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER K   -1  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS K    0  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C MET L  -19  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C GLY L  -18  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER L  -17  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER L  -16  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS L  -15  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS L  -14  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS L  -13  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS L  -12  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS L  -11  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS L  -10  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER L   -9  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER L   -8  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C GLY L   -7  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C LEU L   -6  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C VAL L   -5  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C PRO L   -4  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C ARG L   -3  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C GLY L   -2  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C SER L   -1  UNP  O32081              EXPRESSION TAG                 
SEQADV 4J7C HIS L    0  UNP  O32081              EXPRESSION TAG                 
SEQRES   1 A  222  MET GLY ARG ILE LYS ASN LYS GLN PHE ALA VAL ILE GLY          
SEQRES   2 A  222  LEU GLY ARG PHE GLY GLY SER ILE VAL LYS GLU LEU HIS          
SEQRES   3 A  222  ARG MET GLY HIS GLU VAL LEU ALA VAL ASP ILE ASN GLU          
SEQRES   4 A  222  GLU LYS VAL ASN ALA TYR ALA SER TYR ALA THR HIS ALA          
SEQRES   5 A  222  VAL ILE ALA ASN ALA THR GLU GLU ASN GLU LEU LEU SER          
SEQRES   6 A  222  LEU GLY ILE ARG ASN PHE GLU TYR VAL ILE VAL ALA ILE          
SEQRES   7 A  222  GLY ALA ASN ILE GLN ALA SER THR LEU THR THR LEU LEU          
SEQRES   8 A  222  LEU LYS GLU LEU ASP ILE PRO ASN ILE TRP VAL LYS ALA          
SEQRES   9 A  222  GLN ASN TYR TYR HIS HIS LYS VAL LEU GLU LYS ILE GLY          
SEQRES  10 A  222  ALA ASP ARG ILE ILE HIS PRO GLU LYS ASP MET GLY VAL          
SEQRES  11 A  222  LYS ILE ALA GLN SER LEU SER ASP GLU ASN VAL LEU ASN          
SEQRES  12 A  222  TYR ILE ASP LEU SER ASP GLU TYR SER ILE VAL GLU LEU          
SEQRES  13 A  222  LEU ALA THR ARG LYS LEU ASP SER LYS SER ILE ILE ASP          
SEQRES  14 A  222  LEU ASN VAL ARG ALA LYS TYR GLY CYS THR ILE LEU ALA          
SEQRES  15 A  222  ILE LYS HIS HIS GLY ASP ILE CYS LEU SER PRO ALA PRO          
SEQRES  16 A  222  GLU ASP ILE ILE ARG GLU GLN ASP CYS LEU VAL ILE MET          
SEQRES  17 A  222  GLY HIS LYS LYS ASP ILE LYS ARG PHE GLU ASN GLU GLY          
SEQRES  18 A  222  MET                                                          
SEQRES   1 B  222  MET GLY ARG ILE LYS ASN LYS GLN PHE ALA VAL ILE GLY          
SEQRES   2 B  222  LEU GLY ARG PHE GLY GLY SER ILE VAL LYS GLU LEU HIS          
SEQRES   3 B  222  ARG MET GLY HIS GLU VAL LEU ALA VAL ASP ILE ASN GLU          
SEQRES   4 B  222  GLU LYS VAL ASN ALA TYR ALA SER TYR ALA THR HIS ALA          
SEQRES   5 B  222  VAL ILE ALA ASN ALA THR GLU GLU ASN GLU LEU LEU SER          
SEQRES   6 B  222  LEU GLY ILE ARG ASN PHE GLU TYR VAL ILE VAL ALA ILE          
SEQRES   7 B  222  GLY ALA ASN ILE GLN ALA SER THR LEU THR THR LEU LEU          
SEQRES   8 B  222  LEU LYS GLU LEU ASP ILE PRO ASN ILE TRP VAL LYS ALA          
SEQRES   9 B  222  GLN ASN TYR TYR HIS HIS LYS VAL LEU GLU LYS ILE GLY          
SEQRES  10 B  222  ALA ASP ARG ILE ILE HIS PRO GLU LYS ASP MET GLY VAL          
SEQRES  11 B  222  LYS ILE ALA GLN SER LEU SER ASP GLU ASN VAL LEU ASN          
SEQRES  12 B  222  TYR ILE ASP LEU SER ASP GLU TYR SER ILE VAL GLU LEU          
SEQRES  13 B  222  LEU ALA THR ARG LYS LEU ASP SER LYS SER ILE ILE ASP          
SEQRES  14 B  222  LEU ASN VAL ARG ALA LYS TYR GLY CYS THR ILE LEU ALA          
SEQRES  15 B  222  ILE LYS HIS HIS GLY ASP ILE CYS LEU SER PRO ALA PRO          
SEQRES  16 B  222  GLU ASP ILE ILE ARG GLU GLN ASP CYS LEU VAL ILE MET          
SEQRES  17 B  222  GLY HIS LYS LYS ASP ILE LYS ARG PHE GLU ASN GLU GLY          
SEQRES  18 B  222  MET                                                          
SEQRES   1 C  222  MET GLY ARG ILE LYS ASN LYS GLN PHE ALA VAL ILE GLY          
SEQRES   2 C  222  LEU GLY ARG PHE GLY GLY SER ILE VAL LYS GLU LEU HIS          
SEQRES   3 C  222  ARG MET GLY HIS GLU VAL LEU ALA VAL ASP ILE ASN GLU          
SEQRES   4 C  222  GLU LYS VAL ASN ALA TYR ALA SER TYR ALA THR HIS ALA          
SEQRES   5 C  222  VAL ILE ALA ASN ALA THR GLU GLU ASN GLU LEU LEU SER          
SEQRES   6 C  222  LEU GLY ILE ARG ASN PHE GLU TYR VAL ILE VAL ALA ILE          
SEQRES   7 C  222  GLY ALA ASN ILE GLN ALA SER THR LEU THR THR LEU LEU          
SEQRES   8 C  222  LEU LYS GLU LEU ASP ILE PRO ASN ILE TRP VAL LYS ALA          
SEQRES   9 C  222  GLN ASN TYR TYR HIS HIS LYS VAL LEU GLU LYS ILE GLY          
SEQRES  10 C  222  ALA ASP ARG ILE ILE HIS PRO GLU LYS ASP MET GLY VAL          
SEQRES  11 C  222  LYS ILE ALA GLN SER LEU SER ASP GLU ASN VAL LEU ASN          
SEQRES  12 C  222  TYR ILE ASP LEU SER ASP GLU TYR SER ILE VAL GLU LEU          
SEQRES  13 C  222  LEU ALA THR ARG LYS LEU ASP SER LYS SER ILE ILE ASP          
SEQRES  14 C  222  LEU ASN VAL ARG ALA LYS TYR GLY CYS THR ILE LEU ALA          
SEQRES  15 C  222  ILE LYS HIS HIS GLY ASP ILE CYS LEU SER PRO ALA PRO          
SEQRES  16 C  222  GLU ASP ILE ILE ARG GLU GLN ASP CYS LEU VAL ILE MET          
SEQRES  17 C  222  GLY HIS LYS LYS ASP ILE LYS ARG PHE GLU ASN GLU GLY          
SEQRES  18 C  222  MET                                                          
SEQRES   1 D  222  MET GLY ARG ILE LYS ASN LYS GLN PHE ALA VAL ILE GLY          
SEQRES   2 D  222  LEU GLY ARG PHE GLY GLY SER ILE VAL LYS GLU LEU HIS          
SEQRES   3 D  222  ARG MET GLY HIS GLU VAL LEU ALA VAL ASP ILE ASN GLU          
SEQRES   4 D  222  GLU LYS VAL ASN ALA TYR ALA SER TYR ALA THR HIS ALA          
SEQRES   5 D  222  VAL ILE ALA ASN ALA THR GLU GLU ASN GLU LEU LEU SER          
SEQRES   6 D  222  LEU GLY ILE ARG ASN PHE GLU TYR VAL ILE VAL ALA ILE          
SEQRES   7 D  222  GLY ALA ASN ILE GLN ALA SER THR LEU THR THR LEU LEU          
SEQRES   8 D  222  LEU LYS GLU LEU ASP ILE PRO ASN ILE TRP VAL LYS ALA          
SEQRES   9 D  222  GLN ASN TYR TYR HIS HIS LYS VAL LEU GLU LYS ILE GLY          
SEQRES  10 D  222  ALA ASP ARG ILE ILE HIS PRO GLU LYS ASP MET GLY VAL          
SEQRES  11 D  222  LYS ILE ALA GLN SER LEU SER ASP GLU ASN VAL LEU ASN          
SEQRES  12 D  222  TYR ILE ASP LEU SER ASP GLU TYR SER ILE VAL GLU LEU          
SEQRES  13 D  222  LEU ALA THR ARG LYS LEU ASP SER LYS SER ILE ILE ASP          
SEQRES  14 D  222  LEU ASN VAL ARG ALA LYS TYR GLY CYS THR ILE LEU ALA          
SEQRES  15 D  222  ILE LYS HIS HIS GLY ASP ILE CYS LEU SER PRO ALA PRO          
SEQRES  16 D  222  GLU ASP ILE ILE ARG GLU GLN ASP CYS LEU VAL ILE MET          
SEQRES  17 D  222  GLY HIS LYS LYS ASP ILE LYS ARG PHE GLU ASN GLU GLY          
SEQRES  18 D  222  MET                                                          
SEQRES   1 E  222  MET GLY ARG ILE LYS ASN LYS GLN PHE ALA VAL ILE GLY          
SEQRES   2 E  222  LEU GLY ARG PHE GLY GLY SER ILE VAL LYS GLU LEU HIS          
SEQRES   3 E  222  ARG MET GLY HIS GLU VAL LEU ALA VAL ASP ILE ASN GLU          
SEQRES   4 E  222  GLU LYS VAL ASN ALA TYR ALA SER TYR ALA THR HIS ALA          
SEQRES   5 E  222  VAL ILE ALA ASN ALA THR GLU GLU ASN GLU LEU LEU SER          
SEQRES   6 E  222  LEU GLY ILE ARG ASN PHE GLU TYR VAL ILE VAL ALA ILE          
SEQRES   7 E  222  GLY ALA ASN ILE GLN ALA SER THR LEU THR THR LEU LEU          
SEQRES   8 E  222  LEU LYS GLU LEU ASP ILE PRO ASN ILE TRP VAL LYS ALA          
SEQRES   9 E  222  GLN ASN TYR TYR HIS HIS LYS VAL LEU GLU LYS ILE GLY          
SEQRES  10 E  222  ALA ASP ARG ILE ILE HIS PRO GLU LYS ASP MET GLY VAL          
SEQRES  11 E  222  LYS ILE ALA GLN SER LEU SER ASP GLU ASN VAL LEU ASN          
SEQRES  12 E  222  TYR ILE ASP LEU SER ASP GLU TYR SER ILE VAL GLU LEU          
SEQRES  13 E  222  LEU ALA THR ARG LYS LEU ASP SER LYS SER ILE ILE ASP          
SEQRES  14 E  222  LEU ASN VAL ARG ALA LYS TYR GLY CYS THR ILE LEU ALA          
SEQRES  15 E  222  ILE LYS HIS HIS GLY ASP ILE CYS LEU SER PRO ALA PRO          
SEQRES  16 E  222  GLU ASP ILE ILE ARG GLU GLN ASP CYS LEU VAL ILE MET          
SEQRES  17 E  222  GLY HIS LYS LYS ASP ILE LYS ARG PHE GLU ASN GLU GLY          
SEQRES  18 E  222  MET                                                          
SEQRES   1 F  222  MET GLY ARG ILE LYS ASN LYS GLN PHE ALA VAL ILE GLY          
SEQRES   2 F  222  LEU GLY ARG PHE GLY GLY SER ILE VAL LYS GLU LEU HIS          
SEQRES   3 F  222  ARG MET GLY HIS GLU VAL LEU ALA VAL ASP ILE ASN GLU          
SEQRES   4 F  222  GLU LYS VAL ASN ALA TYR ALA SER TYR ALA THR HIS ALA          
SEQRES   5 F  222  VAL ILE ALA ASN ALA THR GLU GLU ASN GLU LEU LEU SER          
SEQRES   6 F  222  LEU GLY ILE ARG ASN PHE GLU TYR VAL ILE VAL ALA ILE          
SEQRES   7 F  222  GLY ALA ASN ILE GLN ALA SER THR LEU THR THR LEU LEU          
SEQRES   8 F  222  LEU LYS GLU LEU ASP ILE PRO ASN ILE TRP VAL LYS ALA          
SEQRES   9 F  222  GLN ASN TYR TYR HIS HIS LYS VAL LEU GLU LYS ILE GLY          
SEQRES  10 F  222  ALA ASP ARG ILE ILE HIS PRO GLU LYS ASP MET GLY VAL          
SEQRES  11 F  222  LYS ILE ALA GLN SER LEU SER ASP GLU ASN VAL LEU ASN          
SEQRES  12 F  222  TYR ILE ASP LEU SER ASP GLU TYR SER ILE VAL GLU LEU          
SEQRES  13 F  222  LEU ALA THR ARG LYS LEU ASP SER LYS SER ILE ILE ASP          
SEQRES  14 F  222  LEU ASN VAL ARG ALA LYS TYR GLY CYS THR ILE LEU ALA          
SEQRES  15 F  222  ILE LYS HIS HIS GLY ASP ILE CYS LEU SER PRO ALA PRO          
SEQRES  16 F  222  GLU ASP ILE ILE ARG GLU GLN ASP CYS LEU VAL ILE MET          
SEQRES  17 F  222  GLY HIS LYS LYS ASP ILE LYS ARG PHE GLU ASN GLU GLY          
SEQRES  18 F  222  MET                                                          
SEQRES   1 G  222  MET GLY ARG ILE LYS ASN LYS GLN PHE ALA VAL ILE GLY          
SEQRES   2 G  222  LEU GLY ARG PHE GLY GLY SER ILE VAL LYS GLU LEU HIS          
SEQRES   3 G  222  ARG MET GLY HIS GLU VAL LEU ALA VAL ASP ILE ASN GLU          
SEQRES   4 G  222  GLU LYS VAL ASN ALA TYR ALA SER TYR ALA THR HIS ALA          
SEQRES   5 G  222  VAL ILE ALA ASN ALA THR GLU GLU ASN GLU LEU LEU SER          
SEQRES   6 G  222  LEU GLY ILE ARG ASN PHE GLU TYR VAL ILE VAL ALA ILE          
SEQRES   7 G  222  GLY ALA ASN ILE GLN ALA SER THR LEU THR THR LEU LEU          
SEQRES   8 G  222  LEU LYS GLU LEU ASP ILE PRO ASN ILE TRP VAL LYS ALA          
SEQRES   9 G  222  GLN ASN TYR TYR HIS HIS LYS VAL LEU GLU LYS ILE GLY          
SEQRES  10 G  222  ALA ASP ARG ILE ILE HIS PRO GLU LYS ASP MET GLY VAL          
SEQRES  11 G  222  LYS ILE ALA GLN SER LEU SER ASP GLU ASN VAL LEU ASN          
SEQRES  12 G  222  TYR ILE ASP LEU SER ASP GLU TYR SER ILE VAL GLU LEU          
SEQRES  13 G  222  LEU ALA THR ARG LYS LEU ASP SER LYS SER ILE ILE ASP          
SEQRES  14 G  222  LEU ASN VAL ARG ALA LYS TYR GLY CYS THR ILE LEU ALA          
SEQRES  15 G  222  ILE LYS HIS HIS GLY ASP ILE CYS LEU SER PRO ALA PRO          
SEQRES  16 G  222  GLU ASP ILE ILE ARG GLU GLN ASP CYS LEU VAL ILE MET          
SEQRES  17 G  222  GLY HIS LYS LYS ASP ILE LYS ARG PHE GLU ASN GLU GLY          
SEQRES  18 G  222  MET                                                          
SEQRES   1 H  222  MET GLY ARG ILE LYS ASN LYS GLN PHE ALA VAL ILE GLY          
SEQRES   2 H  222  LEU GLY ARG PHE GLY GLY SER ILE VAL LYS GLU LEU HIS          
SEQRES   3 H  222  ARG MET GLY HIS GLU VAL LEU ALA VAL ASP ILE ASN GLU          
SEQRES   4 H  222  GLU LYS VAL ASN ALA TYR ALA SER TYR ALA THR HIS ALA          
SEQRES   5 H  222  VAL ILE ALA ASN ALA THR GLU GLU ASN GLU LEU LEU SER          
SEQRES   6 H  222  LEU GLY ILE ARG ASN PHE GLU TYR VAL ILE VAL ALA ILE          
SEQRES   7 H  222  GLY ALA ASN ILE GLN ALA SER THR LEU THR THR LEU LEU          
SEQRES   8 H  222  LEU LYS GLU LEU ASP ILE PRO ASN ILE TRP VAL LYS ALA          
SEQRES   9 H  222  GLN ASN TYR TYR HIS HIS LYS VAL LEU GLU LYS ILE GLY          
SEQRES  10 H  222  ALA ASP ARG ILE ILE HIS PRO GLU LYS ASP MET GLY VAL          
SEQRES  11 H  222  LYS ILE ALA GLN SER LEU SER ASP GLU ASN VAL LEU ASN          
SEQRES  12 H  222  TYR ILE ASP LEU SER ASP GLU TYR SER ILE VAL GLU LEU          
SEQRES  13 H  222  LEU ALA THR ARG LYS LEU ASP SER LYS SER ILE ILE ASP          
SEQRES  14 H  222  LEU ASN VAL ARG ALA LYS TYR GLY CYS THR ILE LEU ALA          
SEQRES  15 H  222  ILE LYS HIS HIS GLY ASP ILE CYS LEU SER PRO ALA PRO          
SEQRES  16 H  222  GLU ASP ILE ILE ARG GLU GLN ASP CYS LEU VAL ILE MET          
SEQRES  17 H  222  GLY HIS LYS LYS ASP ILE LYS ARG PHE GLU ASN GLU GLY          
SEQRES  18 H  222  MET                                                          
SEQRES   1 I  465  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 I  465  LEU VAL PRO ARG GLY SER HIS MET THR LEU GLN LYS ASP          
SEQRES   3 I  465  LYS VAL ILE LYS TRP VAL ARG PHE THR PRO PRO GLN VAL          
SEQRES   4 I  465  LEU ALA ILE GLY PHE PHE LEU THR ILE ILE ILE GLY ALA          
SEQRES   5 I  465  VAL LEU LEU MET LEU PRO ILE SER THR THR LYS PRO LEU          
SEQRES   6 I  465  SER TRP ILE ASP ALA LEU PHE THR ALA ALA SER ALA THR          
SEQRES   7 I  465  THR VAL THR GLY LEU ALA VAL VAL ASP THR GLY THR GLN          
SEQRES   8 I  465  PHE THR VAL PHE GLY GLN THR VAL ILE MET GLY LEU ILE          
SEQRES   9 I  465  GLN ILE GLY GLY LEU GLY PHE MET THR PHE ALA VAL LEU          
SEQRES  10 I  465  ILE VAL MET ILE LEU GLY LYS LYS ILE GLY LEU LYS GLU          
SEQRES  11 I  465  ARG MET LEU VAL GLN GLU ALA LEU ASN GLN PRO THR ILE          
SEQRES  12 I  465  GLY GLY VAL ILE GLY LEU VAL LYS VAL LEU PHE LEU PHE          
SEQRES  13 I  465  SER ILE SER ILE GLU LEU ILE ALA ALA LEU ILE LEU SER          
SEQRES  14 I  465  ILE ARG LEU VAL PRO GLN TYR GLY TRP SER SER GLY LEU          
SEQRES  15 I  465  PHE ALA SER LEU PHE HIS ALA ILE SER ALA PHE ASN ASN          
SEQRES  16 I  465  ALA GLY PHE SER LEU TRP PRO ASP ASN LEU MET SER TYR          
SEQRES  17 I  465  VAL GLY ASP PRO THR VAL ASN LEU VAL ILE THR PHE LEU          
SEQRES  18 I  465  PHE ILE THR GLY GLY ILE GLY PHE THR VAL LEU PHE ASP          
SEQRES  19 I  465  VAL MET LYS ASN ARG ARG PHE LYS THR PHE SER LEU HIS          
SEQRES  20 I  465  THR LYS LEU MET LEU THR GLY THR LEU MET LEU ASN ALA          
SEQRES  21 I  465  ILE ALA MET LEU THR VAL PHE ILE LEU GLU TYR SER ASN          
SEQRES  22 I  465  PRO GLY THR LEU GLY HIS LEU HIS ILE VAL ASP LYS LEU          
SEQRES  23 I  465  TRP ALA SER TYR PHE GLN ALA VAL THR PRO ARG THR ALA          
SEQRES  24 I  465  GLY PHE ASN SER LEU ASP PHE GLY SER MET ARG GLU GLY          
SEQRES  25 I  465  THR ILE VAL PHE THR LEU LEU LEU MET PHE ILE GLY ALA          
SEQRES  26 I  465  GLY SER ALA SER THR ALA SER GLY ILE LYS LEU THR THR          
SEQRES  27 I  465  PHE ILE VAL ILE LEU THR SER VAL ILE ALA TYR LEU ARG          
SEQRES  28 I  465  GLY LYS LYS GLU THR VAL ILE PHE ARG ARG SER ILE LYS          
SEQRES  29 I  465  TYR PRO ILE ILE ILE LYS ALA LEU ALA VAL SER VAL THR          
SEQRES  30 I  465  SER LEU PHE ILE VAL PHE LEU GLY ILE PHE ALA LEU THR          
SEQRES  31 I  465  ILE THR GLU GLN ALA PRO PHE LEU GLN ILE VAL PHE GLU          
SEQRES  32 I  465  THR PHE SER ALA PHE GLY THR VAL GLY LEU THR MET GLY          
SEQRES  33 I  465  LEU THR PRO GLU LEU THR THR ALA GLY LYS CYS ILE ILE          
SEQRES  34 I  465  ILE VAL ILE MET PHE ILE GLY ARG ILE GLY PRO LEU THR          
SEQRES  35 I  465  PHE VAL PHE SER PHE ALA LYS THR GLU GLN SER ASN ILE          
SEQRES  36 I  465  ARG TYR PRO ASP GLY GLU VAL PHE THR GLY                      
SEQRES   1 J  465  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 J  465  LEU VAL PRO ARG GLY SER HIS MET THR LEU GLN LYS ASP          
SEQRES   3 J  465  LYS VAL ILE LYS TRP VAL ARG PHE THR PRO PRO GLN VAL          
SEQRES   4 J  465  LEU ALA ILE GLY PHE PHE LEU THR ILE ILE ILE GLY ALA          
SEQRES   5 J  465  VAL LEU LEU MET LEU PRO ILE SER THR THR LYS PRO LEU          
SEQRES   6 J  465  SER TRP ILE ASP ALA LEU PHE THR ALA ALA SER ALA THR          
SEQRES   7 J  465  THR VAL THR GLY LEU ALA VAL VAL ASP THR GLY THR GLN          
SEQRES   8 J  465  PHE THR VAL PHE GLY GLN THR VAL ILE MET GLY LEU ILE          
SEQRES   9 J  465  GLN ILE GLY GLY LEU GLY PHE MET THR PHE ALA VAL LEU          
SEQRES  10 J  465  ILE VAL MET ILE LEU GLY LYS LYS ILE GLY LEU LYS GLU          
SEQRES  11 J  465  ARG MET LEU VAL GLN GLU ALA LEU ASN GLN PRO THR ILE          
SEQRES  12 J  465  GLY GLY VAL ILE GLY LEU VAL LYS VAL LEU PHE LEU PHE          
SEQRES  13 J  465  SER ILE SER ILE GLU LEU ILE ALA ALA LEU ILE LEU SER          
SEQRES  14 J  465  ILE ARG LEU VAL PRO GLN TYR GLY TRP SER SER GLY LEU          
SEQRES  15 J  465  PHE ALA SER LEU PHE HIS ALA ILE SER ALA PHE ASN ASN          
SEQRES  16 J  465  ALA GLY PHE SER LEU TRP PRO ASP ASN LEU MET SER TYR          
SEQRES  17 J  465  VAL GLY ASP PRO THR VAL ASN LEU VAL ILE THR PHE LEU          
SEQRES  18 J  465  PHE ILE THR GLY GLY ILE GLY PHE THR VAL LEU PHE ASP          
SEQRES  19 J  465  VAL MET LYS ASN ARG ARG PHE LYS THR PHE SER LEU HIS          
SEQRES  20 J  465  THR LYS LEU MET LEU THR GLY THR LEU MET LEU ASN ALA          
SEQRES  21 J  465  ILE ALA MET LEU THR VAL PHE ILE LEU GLU TYR SER ASN          
SEQRES  22 J  465  PRO GLY THR LEU GLY HIS LEU HIS ILE VAL ASP LYS LEU          
SEQRES  23 J  465  TRP ALA SER TYR PHE GLN ALA VAL THR PRO ARG THR ALA          
SEQRES  24 J  465  GLY PHE ASN SER LEU ASP PHE GLY SER MET ARG GLU GLY          
SEQRES  25 J  465  THR ILE VAL PHE THR LEU LEU LEU MET PHE ILE GLY ALA          
SEQRES  26 J  465  GLY SER ALA SER THR ALA SER GLY ILE LYS LEU THR THR          
SEQRES  27 J  465  PHE ILE VAL ILE LEU THR SER VAL ILE ALA TYR LEU ARG          
SEQRES  28 J  465  GLY LYS LYS GLU THR VAL ILE PHE ARG ARG SER ILE LYS          
SEQRES  29 J  465  TYR PRO ILE ILE ILE LYS ALA LEU ALA VAL SER VAL THR          
SEQRES  30 J  465  SER LEU PHE ILE VAL PHE LEU GLY ILE PHE ALA LEU THR          
SEQRES  31 J  465  ILE THR GLU GLN ALA PRO PHE LEU GLN ILE VAL PHE GLU          
SEQRES  32 J  465  THR PHE SER ALA PHE GLY THR VAL GLY LEU THR MET GLY          
SEQRES  33 J  465  LEU THR PRO GLU LEU THR THR ALA GLY LYS CYS ILE ILE          
SEQRES  34 J  465  ILE VAL ILE MET PHE ILE GLY ARG ILE GLY PRO LEU THR          
SEQRES  35 J  465  PHE VAL PHE SER PHE ALA LYS THR GLU GLN SER ASN ILE          
SEQRES  36 J  465  ARG TYR PRO ASP GLY GLU VAL PHE THR GLY                      
SEQRES   1 K  465  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 K  465  LEU VAL PRO ARG GLY SER HIS MET THR LEU GLN LYS ASP          
SEQRES   3 K  465  LYS VAL ILE LYS TRP VAL ARG PHE THR PRO PRO GLN VAL          
SEQRES   4 K  465  LEU ALA ILE GLY PHE PHE LEU THR ILE ILE ILE GLY ALA          
SEQRES   5 K  465  VAL LEU LEU MET LEU PRO ILE SER THR THR LYS PRO LEU          
SEQRES   6 K  465  SER TRP ILE ASP ALA LEU PHE THR ALA ALA SER ALA THR          
SEQRES   7 K  465  THR VAL THR GLY LEU ALA VAL VAL ASP THR GLY THR GLN          
SEQRES   8 K  465  PHE THR VAL PHE GLY GLN THR VAL ILE MET GLY LEU ILE          
SEQRES   9 K  465  GLN ILE GLY GLY LEU GLY PHE MET THR PHE ALA VAL LEU          
SEQRES  10 K  465  ILE VAL MET ILE LEU GLY LYS LYS ILE GLY LEU LYS GLU          
SEQRES  11 K  465  ARG MET LEU VAL GLN GLU ALA LEU ASN GLN PRO THR ILE          
SEQRES  12 K  465  GLY GLY VAL ILE GLY LEU VAL LYS VAL LEU PHE LEU PHE          
SEQRES  13 K  465  SER ILE SER ILE GLU LEU ILE ALA ALA LEU ILE LEU SER          
SEQRES  14 K  465  ILE ARG LEU VAL PRO GLN TYR GLY TRP SER SER GLY LEU          
SEQRES  15 K  465  PHE ALA SER LEU PHE HIS ALA ILE SER ALA PHE ASN ASN          
SEQRES  16 K  465  ALA GLY PHE SER LEU TRP PRO ASP ASN LEU MET SER TYR          
SEQRES  17 K  465  VAL GLY ASP PRO THR VAL ASN LEU VAL ILE THR PHE LEU          
SEQRES  18 K  465  PHE ILE THR GLY GLY ILE GLY PHE THR VAL LEU PHE ASP          
SEQRES  19 K  465  VAL MET LYS ASN ARG ARG PHE LYS THR PHE SER LEU HIS          
SEQRES  20 K  465  THR LYS LEU MET LEU THR GLY THR LEU MET LEU ASN ALA          
SEQRES  21 K  465  ILE ALA MET LEU THR VAL PHE ILE LEU GLU TYR SER ASN          
SEQRES  22 K  465  PRO GLY THR LEU GLY HIS LEU HIS ILE VAL ASP LYS LEU          
SEQRES  23 K  465  TRP ALA SER TYR PHE GLN ALA VAL THR PRO ARG THR ALA          
SEQRES  24 K  465  GLY PHE ASN SER LEU ASP PHE GLY SER MET ARG GLU GLY          
SEQRES  25 K  465  THR ILE VAL PHE THR LEU LEU LEU MET PHE ILE GLY ALA          
SEQRES  26 K  465  GLY SER ALA SER THR ALA SER GLY ILE LYS LEU THR THR          
SEQRES  27 K  465  PHE ILE VAL ILE LEU THR SER VAL ILE ALA TYR LEU ARG          
SEQRES  28 K  465  GLY LYS LYS GLU THR VAL ILE PHE ARG ARG SER ILE LYS          
SEQRES  29 K  465  TYR PRO ILE ILE ILE LYS ALA LEU ALA VAL SER VAL THR          
SEQRES  30 K  465  SER LEU PHE ILE VAL PHE LEU GLY ILE PHE ALA LEU THR          
SEQRES  31 K  465  ILE THR GLU GLN ALA PRO PHE LEU GLN ILE VAL PHE GLU          
SEQRES  32 K  465  THR PHE SER ALA PHE GLY THR VAL GLY LEU THR MET GLY          
SEQRES  33 K  465  LEU THR PRO GLU LEU THR THR ALA GLY LYS CYS ILE ILE          
SEQRES  34 K  465  ILE VAL ILE MET PHE ILE GLY ARG ILE GLY PRO LEU THR          
SEQRES  35 K  465  PHE VAL PHE SER PHE ALA LYS THR GLU GLN SER ASN ILE          
SEQRES  36 K  465  ARG TYR PRO ASP GLY GLU VAL PHE THR GLY                      
SEQRES   1 L  465  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 L  465  LEU VAL PRO ARG GLY SER HIS MET THR LEU GLN LYS ASP          
SEQRES   3 L  465  LYS VAL ILE LYS TRP VAL ARG PHE THR PRO PRO GLN VAL          
SEQRES   4 L  465  LEU ALA ILE GLY PHE PHE LEU THR ILE ILE ILE GLY ALA          
SEQRES   5 L  465  VAL LEU LEU MET LEU PRO ILE SER THR THR LYS PRO LEU          
SEQRES   6 L  465  SER TRP ILE ASP ALA LEU PHE THR ALA ALA SER ALA THR          
SEQRES   7 L  465  THR VAL THR GLY LEU ALA VAL VAL ASP THR GLY THR GLN          
SEQRES   8 L  465  PHE THR VAL PHE GLY GLN THR VAL ILE MET GLY LEU ILE          
SEQRES   9 L  465  GLN ILE GLY GLY LEU GLY PHE MET THR PHE ALA VAL LEU          
SEQRES  10 L  465  ILE VAL MET ILE LEU GLY LYS LYS ILE GLY LEU LYS GLU          
SEQRES  11 L  465  ARG MET LEU VAL GLN GLU ALA LEU ASN GLN PRO THR ILE          
SEQRES  12 L  465  GLY GLY VAL ILE GLY LEU VAL LYS VAL LEU PHE LEU PHE          
SEQRES  13 L  465  SER ILE SER ILE GLU LEU ILE ALA ALA LEU ILE LEU SER          
SEQRES  14 L  465  ILE ARG LEU VAL PRO GLN TYR GLY TRP SER SER GLY LEU          
SEQRES  15 L  465  PHE ALA SER LEU PHE HIS ALA ILE SER ALA PHE ASN ASN          
SEQRES  16 L  465  ALA GLY PHE SER LEU TRP PRO ASP ASN LEU MET SER TYR          
SEQRES  17 L  465  VAL GLY ASP PRO THR VAL ASN LEU VAL ILE THR PHE LEU          
SEQRES  18 L  465  PHE ILE THR GLY GLY ILE GLY PHE THR VAL LEU PHE ASP          
SEQRES  19 L  465  VAL MET LYS ASN ARG ARG PHE LYS THR PHE SER LEU HIS          
SEQRES  20 L  465  THR LYS LEU MET LEU THR GLY THR LEU MET LEU ASN ALA          
SEQRES  21 L  465  ILE ALA MET LEU THR VAL PHE ILE LEU GLU TYR SER ASN          
SEQRES  22 L  465  PRO GLY THR LEU GLY HIS LEU HIS ILE VAL ASP LYS LEU          
SEQRES  23 L  465  TRP ALA SER TYR PHE GLN ALA VAL THR PRO ARG THR ALA          
SEQRES  24 L  465  GLY PHE ASN SER LEU ASP PHE GLY SER MET ARG GLU GLY          
SEQRES  25 L  465  THR ILE VAL PHE THR LEU LEU LEU MET PHE ILE GLY ALA          
SEQRES  26 L  465  GLY SER ALA SER THR ALA SER GLY ILE LYS LEU THR THR          
SEQRES  27 L  465  PHE ILE VAL ILE LEU THR SER VAL ILE ALA TYR LEU ARG          
SEQRES  28 L  465  GLY LYS LYS GLU THR VAL ILE PHE ARG ARG SER ILE LYS          
SEQRES  29 L  465  TYR PRO ILE ILE ILE LYS ALA LEU ALA VAL SER VAL THR          
SEQRES  30 L  465  SER LEU PHE ILE VAL PHE LEU GLY ILE PHE ALA LEU THR          
SEQRES  31 L  465  ILE THR GLU GLN ALA PRO PHE LEU GLN ILE VAL PHE GLU          
SEQRES  32 L  465  THR PHE SER ALA PHE GLY THR VAL GLY LEU THR MET GLY          
SEQRES  33 L  465  LEU THR PRO GLU LEU THR THR ALA GLY LYS CYS ILE ILE          
SEQRES  34 L  465  ILE VAL ILE MET PHE ILE GLY ARG ILE GLY PRO LEU THR          
SEQRES  35 L  465  PHE VAL PHE SER PHE ALA LYS THR GLU GLN SER ASN ILE          
SEQRES  36 L  465  ARG TYR PRO ASP GLY GLU VAL PHE THR GLY                      
HET    ATP  A 601      31                                                       
HET    ATP  B 301      31                                                       
HET    ATP  C 601      31                                                       
HET    ATP  D 301      31                                                       
HET    ATP  E 601      31                                                       
HET    ATP  F 301      31                                                       
HET    ATP  G 601      31                                                       
HET    ATP  H 301      31                                                       
HET      K  I 501       1                                                       
HET      K  J 501       1                                                       
HET      K  K 501       1                                                       
HET      K  L 501       1                                                       
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM       K POTASSIUM ION                                                    
FORMUL  13  ATP    8(C10 H16 N5 O13 P3)                                         
FORMUL  21    K    4(K 1+)                                                      
HELIX    1   1 PHE A   17  MET A   28  1                                  12    
HELIX    2   2 ASN A   38  ALA A   46  1                                   9    
HELIX    3   3 GLU A   59  LEU A   66  1                                   8    
HELIX    4   4 GLY A   67  PHE A   71  5                                   5    
HELIX    5   5 ASN A   81  LEU A   95  1                                  15    
HELIX    6   6 ASN A  106  ILE A  116  1                                  11    
HELIX    7   7 HIS A  123  ASP A  138  1                                  16    
HELIX    8   8 THR A  159  ASP A  163  5                                   5    
HELIX    9   9 VAL A  172  GLY A  177  1                                   6    
HELIX   10  10 LYS A  211  MET A  222  1                                  12    
HELIX   11  11 PHE B   17  MET B   28  1                                  12    
HELIX   12  12 ASN B   38  ALA B   46  1                                   9    
HELIX   13  13 GLU B   59  LEU B   66  1                                   8    
HELIX   14  14 GLY B   67  PHE B   71  5                                   5    
HELIX   15  15 ASN B   81  LEU B   95  1                                  15    
HELIX   16  16 ASN B  106  ILE B  116  1                                  11    
HELIX   17  17 HIS B  123  ASP B  138  1                                  16    
HELIX   18  18 THR B  159  ASP B  163  5                                   5    
HELIX   19  19 LYS B  211  MET B  222  1                                  12    
HELIX   20  20 PHE C   17  MET C   28  1                                  12    
HELIX   21  21 ASN C   38  ALA C   46  1                                   9    
HELIX   22  22 GLU C   59  LEU C   66  1                                   8    
HELIX   23  23 GLY C   67  PHE C   71  5                                   5    
HELIX   24  24 ASN C   81  LEU C   95  1                                  15    
HELIX   25  25 ASN C  106  ILE C  116  1                                  11    
HELIX   26  26 HIS C  123  ASP C  138  1                                  16    
HELIX   27  27 THR C  159  ASP C  163  5                                   5    
HELIX   28  28 LYS C  211  MET C  222  1                                  12    
HELIX   29  29 PHE D   17  MET D   28  1                                  12    
HELIX   30  30 ASN D   38  ALA D   46  1                                   9    
HELIX   31  31 GLU D   59  LEU D   66  1                                   8    
HELIX   32  32 GLY D   67  PHE D   71  5                                   5    
HELIX   33  33 ASN D   81  LEU D   95  1                                  15    
HELIX   34  34 ASN D  106  ILE D  116  1                                  11    
HELIX   35  35 HIS D  123  ASP D  138  1                                  16    
HELIX   36  36 THR D  159  ASP D  163  5                                   5    
HELIX   37  37 LYS D  211  MET D  222  1                                  12    
HELIX   38  38 PHE E   17  MET E   28  1                                  12    
HELIX   39  39 ASN E   38  ALA E   46  1                                   9    
HELIX   40  40 SER E   47  ALA E   49  5                                   3    
HELIX   41  41 GLU E   59  LEU E   66  1                                   8    
HELIX   42  42 GLY E   67  PHE E   71  5                                   5    
HELIX   43  43 ASN E   81  LEU E   95  1                                  15    
HELIX   44  44 ASN E  106  ILE E  116  1                                  11    
HELIX   45  45 HIS E  123  ASP E  138  1                                  16    
HELIX   46  46 THR E  159  ASP E  163  5                                   5    
HELIX   47  47 LYS E  211  MET E  222  1                                  12    
HELIX   48  48 GLY F   15  MET F   28  1                                  14    
HELIX   49  49 ASN F   38  ALA F   46  1                                   9    
HELIX   50  50 GLU F   59  LEU F   66  1                                   8    
HELIX   51  51 GLY F   67  PHE F   71  5                                   5    
HELIX   52  52 ASN F   81  LEU F   95  1                                  15    
HELIX   53  53 ASN F  106  ILE F  116  1                                  11    
HELIX   54  54 HIS F  123  ASP F  138  1                                  16    
HELIX   55  55 THR F  159  ASP F  163  5                                   5    
HELIX   56  56 LYS F  211  MET F  222  1                                  12    
HELIX   57  57 PHE G   17  MET G   28  1                                  12    
HELIX   58  58 ASN G   38  ALA G   46  1                                   9    
HELIX   59  59 GLU G   59  LEU G   66  1                                   8    
HELIX   60  60 GLY G   67  PHE G   71  5                                   5    
HELIX   61  61 ASN G   81  LEU G   95  1                                  15    
HELIX   62  62 ASN G  106  ILE G  116  1                                  11    
HELIX   63  63 HIS G  123  ASP G  138  1                                  16    
HELIX   64  64 THR G  159  ASP G  163  5                                   5    
HELIX   65  65 LYS G  211  MET G  222  1                                  12    
HELIX   66  66 PHE H   17  MET H   28  1                                  12    
HELIX   67  67 ASN H   38  ALA H   46  1                                   9    
HELIX   68  68 GLU H   59  LEU H   66  1                                   8    
HELIX   69  69 GLY H   67  PHE H   71  5                                   5    
HELIX   70  70 ASN H   81  LEU H   95  1                                  15    
HELIX   71  71 ASN H  106  ILE H  116  1                                  11    
HELIX   72  72 HIS H  123  ASP H  138  1                                  16    
HELIX   73  73 THR H  159  ASP H  163  5                                   5    
HELIX   74  74 LYS H  211  MET H  222  1                                  12    
HELIX   75  75 PRO I   16  LEU I   37  1                                  22    
HELIX   76  76 PRO I   38  THR I   41  5                                   4    
HELIX   77  77 SER I   46  THR I   59  1                                  14    
HELIX   78  78 ASP I   67  PHE I   72  1                                   6    
HELIX   79  79 THR I   73  GLY I   90  1                                  18    
HELIX   80  80 GLY I   90  LEU I  102  1                                  13    
HELIX   81  81 GLY I  107  LEU I  118  1                                  12    
HELIX   82  82 GLY I  125  LEU I  146  1                                  22    
HELIX   83  83 ILE I  147  LEU I  152  1                                   6    
HELIX   84  84 SER I  160  ASN I  174  1                                  15    
HELIX   85  85 LEU I  185  VAL I  189  5                                   5    
HELIX   86  86 ASP I  191  ILE I  207  1                                  17    
HELIX   87  87 GLY I  208  ARG I  219  1                                  12    
HELIX   88  88 SER I  225  TYR I  251  1                                  27    
HELIX   89  89 VAL I  263  THR I  275  1                                  13    
HELIX   90  90 ARG I  290  ILE I  303  1                                  14    
HELIX   91  91 LYS I  315  ARG I  331  1                                  17    
HELIX   92  92 LYS I  344  GLU I  373  1                                  30    
HELIX   93  93 PRO I  376  GLY I  389  1                                  14    
HELIX   94  94 LEU I  397  LEU I  401  5                                   5    
HELIX   95  95 THR I  402  GLY I  419  1                                  18    
HELIX   96  96 GLY I  419  PHE I  425  1                                   7    
HELIX   97  97 PRO J   16  LEU J   37  1                                  22    
HELIX   98  98 PRO J   38  THR J   41  5                                   4    
HELIX   99  99 SER J   46  THR J   59  1                                  14    
HELIX  100 100 ASP J   67  PHE J   72  1                                   6    
HELIX  101 101 THR J   73  GLY J   90  1                                  18    
HELIX  102 102 GLY J   90  LEU J  102  1                                  13    
HELIX  103 103 GLY J  107  LEU J  118  1                                  12    
HELIX  104 104 GLY J  125  LEU J  146  1                                  22    
HELIX  105 105 ILE J  147  LEU J  152  1                                   6    
HELIX  106 106 SER J  160  ASN J  174  1                                  15    
HELIX  107 107 ASP J  191  ILE J  207  1                                  17    
HELIX  108 108 GLY J  208  ARG J  219  1                                  12    
HELIX  109 109 SER J  225  TYR J  251  1                                  27    
HELIX  110 110 VAL J  263  THR J  275  1                                  13    
HELIX  111 111 ARG J  290  ILE J  303  1                                  14    
HELIX  112 112 LYS J  315  ARG J  331  1                                  17    
HELIX  113 113 LYS J  344  GLU J  373  1                                  30    
HELIX  114 114 PRO J  376  GLY J  389  1                                  14    
HELIX  115 115 LEU J  397  LEU J  401  5                                   5    
HELIX  116 116 THR J  402  GLY J  419  1                                  18    
HELIX  117 117 GLY J  419  ALA J  428  1                                  10    
HELIX  118 118 PRO K   16  LEU K   37  1                                  22    
HELIX  119 119 PRO K   38  THR K   41  5                                   4    
HELIX  120 120 SER K   46  THR K   59  1                                  14    
HELIX  121 121 ASP K   67  PHE K   72  1                                   6    
HELIX  122 122 THR K   73  GLY K   90  1                                  18    
HELIX  123 123 GLY K   90  LEU K  102  1                                  13    
HELIX  124 124 GLY K  107  LEU K  118  1                                  12    
HELIX  125 125 GLY K  125  LEU K  152  1                                  28    
HELIX  126 126 SER K  160  ASN K  174  1                                  15    
HELIX  127 127 LEU K  185  VAL K  189  5                                   5    
HELIX  128 128 ASP K  191  ILE K  207  1                                  17    
HELIX  129 129 GLY K  208  ARG K  219  1                                  12    
HELIX  130 130 SER K  225  TYR K  251  1                                  27    
HELIX  131 131 VAL K  263  THR K  275  1                                  13    
HELIX  132 132 ASP K  285  MET K  289  5                                   5    
HELIX  133 133 ARG K  290  ILE K  303  1                                  14    
HELIX  134 134 LYS K  315  ARG K  331  1                                  17    
HELIX  135 135 LYS K  344  GLU K  373  1                                  30    
HELIX  136 136 PRO K  376  GLY K  389  1                                  14    
HELIX  137 137 LEU K  397  LEU K  401  5                                   5    
HELIX  138 138 THR K  402  GLY K  419  1                                  18    
HELIX  139 139 GLY K  419  ALA K  428  1                                  10    
HELIX  140 140 PRO L   16  LEU L   37  1                                  22    
HELIX  141 141 PRO L   38  THR L   41  5                                   4    
HELIX  142 142 SER L   46  THR L   59  1                                  14    
HELIX  143 143 ASP L   67  PHE L   72  1                                   6    
HELIX  144 144 THR L   73  GLY L   90  1                                  18    
HELIX  145 145 GLY L   90  LEU L  102  1                                  13    
HELIX  146 146 GLY L  107  LEU L  118  1                                  12    
HELIX  147 147 GLY L  125  LEU L  152  1                                  28    
HELIX  148 148 SER L  160  ASN L  174  1                                  15    
HELIX  149 149 LEU L  185  VAL L  189  5                                   5    
HELIX  150 150 ASP L  191  ILE L  207  1                                  17    
HELIX  151 151 GLY L  208  ARG L  219  1                                  12    
HELIX  152 152 SER L  225  TYR L  251  1                                  27    
HELIX  153 153 VAL L  263  THR L  275  1                                  13    
HELIX  154 154 ASP L  285  MET L  289  5                                   5    
HELIX  155 155 ARG L  290  ILE L  303  1                                  14    
HELIX  156 156 LYS L  315  ARG L  331  1                                  17    
HELIX  157 157 LYS L  344  GLU L  373  1                                  30    
HELIX  158 158 PRO L  376  GLY L  389  1                                  14    
HELIX  159 159 THR L  402  GLY L  419  1                                  18    
HELIX  160 160 GLY L  419  ALA L  428  1                                  10    
SHEET    1   A 6 HIS A  51  ILE A  54  0                                        
SHEET    2   A 6 GLU A  31  ASP A  36  1  N  ALA A  34   O  HIS A  51           
SHEET    3   A 6 GLN A   8  ILE A  12  1  N  PHE A   9   O  GLU A  31           
SHEET    4   A 6 TYR A  73  VAL A  76  1  O  ILE A  75   N  ALA A  10           
SHEET    5   A 6 ASN A  99  LYS A 103  1  O  LYS A 103   N  VAL A  76           
SHEET    6   A 6 ARG A 120  ILE A 122  1  O  ILE A 122   N  VAL A 102           
SHEET    1   B 5 VAL A 141  ASP A 146  0                                        
SHEET    2   B 5 TYR A 151  LEU A 157 -1  O  GLU A 155   N  ASN A 143           
SHEET    3   B 5 CYS A 204  HIS A 210 -1  O  LEU A 205   N  LEU A 156           
SHEET    4   B 5 THR A 179  HIS A 185 -1  N  LEU A 181   O  VAL A 206           
SHEET    5   B 5 ASP A 188  LEU A 191 -1  O  CYS A 190   N  ILE A 183           
SHEET    1   C 2 LYS A 165  SER A 166  0                                        
SHEET    2   C 2 ILE A 198  ILE A 199 -1  O  ILE A 199   N  LYS A 165           
SHEET    1   D 6 HIS B  51  ILE B  54  0                                        
SHEET    2   D 6 GLU B  31  ASP B  36  1  N  ALA B  34   O  HIS B  51           
SHEET    3   D 6 GLN B   8  ILE B  12  1  N  PHE B   9   O  GLU B  31           
SHEET    4   D 6 TYR B  73  VAL B  76  1  O  ILE B  75   N  ALA B  10           
SHEET    5   D 6 ASN B  99  LYS B 103  1  O  LYS B 103   N  VAL B  76           
SHEET    6   D 6 ARG B 120  ILE B 122  1  O  ILE B 122   N  VAL B 102           
SHEET    1   E 5 VAL B 141  ASP B 146  0                                        
SHEET    2   E 5 TYR B 151  LEU B 157 -1  O  GLU B 155   N  ASN B 143           
SHEET    3   E 5 CYS B 204  HIS B 210 -1  O  LEU B 205   N  LEU B 156           
SHEET    4   E 5 THR B 179  HIS B 185 -1  N  LEU B 181   O  VAL B 206           
SHEET    5   E 5 ASP B 188  LEU B 191 -1  O  CYS B 190   N  ILE B 183           
SHEET    1   F 6 HIS C  51  ILE C  54  0                                        
SHEET    2   F 6 GLU C  31  ASP C  36  1  N  ALA C  34   O  HIS C  51           
SHEET    3   F 6 GLN C   8  ILE C  12  1  N  PHE C   9   O  GLU C  31           
SHEET    4   F 6 TYR C  73  VAL C  76  1  O  ILE C  75   N  ALA C  10           
SHEET    5   F 6 ASN C  99  LYS C 103  1  O  LYS C 103   N  VAL C  76           
SHEET    6   F 6 ARG C 120  ILE C 122  1  O  ILE C 122   N  VAL C 102           
SHEET    1   G 5 VAL C 141  ASP C 146  0                                        
SHEET    2   G 5 TYR C 151  LEU C 157 -1  O  GLU C 155   N  ASN C 143           
SHEET    3   G 5 CYS C 204  HIS C 210 -1  O  LEU C 205   N  LEU C 156           
SHEET    4   G 5 THR C 179  HIS C 185 -1  N  LEU C 181   O  VAL C 206           
SHEET    5   G 5 ASP C 188  LEU C 191 -1  O  CYS C 190   N  ILE C 183           
SHEET    1   H 2 LYS C 165  SER C 166  0                                        
SHEET    2   H 2 ILE C 198  ILE C 199 -1  O  ILE C 199   N  LYS C 165           
SHEET    1   I 6 HIS D  51  ILE D  54  0                                        
SHEET    2   I 6 GLU D  31  ASP D  36  1  N  ALA D  34   O  HIS D  51           
SHEET    3   I 6 GLN D   8  ILE D  12  1  N  PHE D   9   O  GLU D  31           
SHEET    4   I 6 TYR D  73  VAL D  76  1  O  ILE D  75   N  ALA D  10           
SHEET    5   I 6 ASN D  99  LYS D 103  1  O  LYS D 103   N  VAL D  76           
SHEET    6   I 6 ARG D 120  ILE D 122  1  O  ILE D 122   N  VAL D 102           
SHEET    1   J 5 VAL D 141  ASP D 146  0                                        
SHEET    2   J 5 TYR D 151  LEU D 157 -1  O  GLU D 155   N  ASN D 143           
SHEET    3   J 5 CYS D 204  HIS D 210 -1  O  LEU D 205   N  LEU D 156           
SHEET    4   J 5 THR D 179  HIS D 185 -1  N  LEU D 181   O  VAL D 206           
SHEET    5   J 5 ASP D 188  LEU D 191 -1  O  CYS D 190   N  ILE D 183           
SHEET    1   K 6 HIS E  51  ILE E  54  0                                        
SHEET    2   K 6 GLU E  31  ASP E  36  1  N  ALA E  34   O  HIS E  51           
SHEET    3   K 6 GLN E   8  ILE E  12  1  N  PHE E   9   O  GLU E  31           
SHEET    4   K 6 TYR E  73  VAL E  76  1  O  ILE E  75   N  ALA E  10           
SHEET    5   K 6 ASN E  99  LYS E 103  1  O  LYS E 103   N  VAL E  76           
SHEET    6   K 6 ARG E 120  ILE E 122  1  O  ILE E 122   N  VAL E 102           
SHEET    1   L 5 VAL E 141  ASP E 146  0                                        
SHEET    2   L 5 TYR E 151  LEU E 157 -1  O  GLU E 155   N  ASN E 143           
SHEET    3   L 5 CYS E 204  HIS E 210 -1  O  LEU E 205   N  LEU E 156           
SHEET    4   L 5 THR E 179  HIS E 185 -1  N  LEU E 181   O  VAL E 206           
SHEET    5   L 5 ASP E 188  LEU E 191 -1  O  CYS E 190   N  ILE E 183           
SHEET    1   M 2 LYS E 165  SER E 166  0                                        
SHEET    2   M 2 ILE E 198  ILE E 199 -1  O  ILE E 199   N  LYS E 165           
SHEET    1   N 6 HIS F  51  ILE F  54  0                                        
SHEET    2   N 6 GLU F  31  ASP F  36  1  N  ALA F  34   O  HIS F  51           
SHEET    3   N 6 GLN F   8  ILE F  12  1  N  PHE F   9   O  GLU F  31           
SHEET    4   N 6 TYR F  73  VAL F  76  1  O  ILE F  75   N  ALA F  10           
SHEET    5   N 6 ASN F  99  LYS F 103  1  O  LYS F 103   N  VAL F  76           
SHEET    6   N 6 ARG F 120  ILE F 122  1  O  ILE F 122   N  VAL F 102           
SHEET    1   O 5 VAL F 141  ASP F 146  0                                        
SHEET    2   O 5 TYR F 151  LEU F 157 -1  O  GLU F 155   N  ASN F 143           
SHEET    3   O 5 CYS F 204  HIS F 210 -1  O  LEU F 205   N  LEU F 156           
SHEET    4   O 5 THR F 179  HIS F 185 -1  N  LEU F 181   O  VAL F 206           
SHEET    5   O 5 ASP F 188  LEU F 191 -1  O  CYS F 190   N  ILE F 183           
SHEET    1   P 6 HIS G  51  ILE G  54  0                                        
SHEET    2   P 6 GLU G  31  ASP G  36  1  N  ALA G  34   O  HIS G  51           
SHEET    3   P 6 GLN G   8  ILE G  12  1  N  PHE G   9   O  GLU G  31           
SHEET    4   P 6 TYR G  73  VAL G  76  1  O  ILE G  75   N  ALA G  10           
SHEET    5   P 6 ASN G  99  LYS G 103  1  O  LYS G 103   N  VAL G  76           
SHEET    6   P 6 ARG G 120  ILE G 122  1  O  ILE G 122   N  VAL G 102           
SHEET    1   Q 5 VAL G 141  ASP G 146  0                                        
SHEET    2   Q 5 TYR G 151  LEU G 157 -1  O  GLU G 155   N  ASN G 143           
SHEET    3   Q 5 CYS G 204  HIS G 210 -1  O  LEU G 205   N  LEU G 156           
SHEET    4   Q 5 THR G 179  HIS G 185 -1  N  LEU G 181   O  VAL G 206           
SHEET    5   Q 5 ASP G 188  LEU G 191 -1  O  CYS G 190   N  ILE G 183           
SHEET    1   R 2 LYS G 165  SER G 166  0                                        
SHEET    2   R 2 ILE G 198  ILE G 199 -1  O  ILE G 199   N  LYS G 165           
SHEET    1   S 6 HIS H  51  ILE H  54  0                                        
SHEET    2   S 6 GLU H  31  ASP H  36  1  N  ALA H  34   O  HIS H  51           
SHEET    3   S 6 GLN H   8  ILE H  12  1  N  PHE H   9   O  GLU H  31           
SHEET    4   S 6 TYR H  73  VAL H  76  1  O  ILE H  75   N  ALA H  10           
SHEET    5   S 6 ASN H  99  LYS H 103  1  O  LYS H 103   N  VAL H  76           
SHEET    6   S 6 ARG H 120  ILE H 122  1  O  ILE H 122   N  VAL H 102           
SHEET    1   T 5 VAL H 141  ASP H 146  0                                        
SHEET    2   T 5 TYR H 151  LEU H 157 -1  O  GLU H 155   N  ASN H 143           
SHEET    3   T 5 CYS H 204  HIS H 210 -1  O  LEU H 205   N  LEU H 156           
SHEET    4   T 5 THR H 179  HIS H 185 -1  N  LEU H 181   O  VAL H 206           
SHEET    5   T 5 ASP H 188  LEU H 191 -1  O  CYS H 190   N  ILE H 183           
SHEET    1   U 2 VAL I 337  ILE I 338  0                                        
SHEET    2   U 2 ARG I 341  SER I 342 -1  O  ARG I 341   N  ILE I 338           
SHEET    1   V 2 VAL J 337  ILE J 338  0                                        
SHEET    2   V 2 ARG J 341  SER J 342 -1  O  ARG J 341   N  ILE J 338           
SHEET    1   W 2 VAL K 337  ILE K 338  0                                        
SHEET    2   W 2 ARG K 341  SER K 342 -1  O  ARG K 341   N  ILE K 338           
SHEET    1   X 2 VAL L 337  ILE L 338  0                                        
SHEET    2   X 2 ARG L 341  SER L 342 -1  O  ARG L 341   N  ILE L 338           
LINK         O   VAL I 391                 K     K I 501     1555   1555  2.22  
LINK         O   VAL L 391                 K     K L 501     1555   1555  2.25  
LINK         O   VAL K 391                 K     K K 501     1555   1555  2.26  
LINK         O   ALA L 176                 K     K L 501     1555   1555  2.27  
LINK         O   ALA J 176                 K     K J 501     1555   1555  2.28  
LINK         O   ASN L 175                 K     K L 501     1555   1555  2.30  
LINK         O   ALA I 176                 K     K I 501     1555   1555  2.31  
LINK         O   THR J  61                 K     K J 501     1555   1555  2.31  
LINK         O   THR I  61                 K     K I 501     1555   1555  2.32  
LINK         O   ASN J 175                 K     K J 501     1555   1555  2.33  
LINK         O   THR K  61                 K     K K 501     1555   1555  2.35  
LINK         O   ALA K 176                 K     K K 501     1555   1555  2.35  
LINK         O   VAL J 391                 K     K J 501     1555   1555  2.36  
LINK         O   ASN K 175                 K     K K 501     1555   1555  2.37  
LINK         O   THR L  61                 K     K L 501     1555   1555  2.38  
LINK         O   THR K 278                 K     K K 501     1555   1555  2.39  
LINK         O   THR L 278                 K     K L 501     1555   1555  2.40  
LINK         O   THR I 278                 K     K I 501     1555   1555  2.40  
LINK         O   ASN I 175                 K     K I 501     1555   1555  2.41  
LINK         O   THR J 390                 K     K J 501     1555   1555  2.45  
LINK         O   THR K 390                 K     K K 501     1555   1555  2.47  
LINK         O   THR I 390                 K     K I 501     1555   1555  2.50  
LINK         O   THR J 278                 K     K J 501     1555   1555  2.50  
LINK         O   THR L 390                 K     K L 501     1555   1555  2.53  
LINK         O   VAL J  60                 K     K J 501     1555   1555  2.66  
LINK         O   ALA L 279                 K     K L 501     1555   1555  2.71  
LINK         O   ALA I 279                 K     K I 501     1555   1555  2.74  
LINK         O   ALA K 279                 K     K K 501     1555   1555  2.76  
LINK         O   VAL K  60                 K     K K 501     1555   1555  2.81  
LINK         O   VAL L  60                 K     K L 501     1555   1555  2.84  
LINK         O   VAL I  60                 K     K I 501     1555   1555  2.85  
LINK         O   ALA J 279                 K     K J 501     1555   1555  2.87  
CISPEP   1 PRO A  195    GLU A  196          0         3.40                     
CISPEP   2 PRO B  195    GLU B  196          0         3.68                     
CISPEP   3 PRO C  195    GLU C  196          0         3.30                     
CISPEP   4 PRO D  195    GLU D  196          0         3.76                     
CISPEP   5 PRO E  195    GLU E  196          0         3.60                     
CISPEP   6 PRO F  195    GLU F  196          0         3.85                     
CISPEP   7 PRO G  195    GLU G  196          0         3.27                     
CISPEP   8 PRO H  195    GLU H  196          0         3.26                     
CISPEP   9 LYS I  105    ILE I  106          0        -4.42                     
CISPEP  10 ARG I  277    THR I  278          0       -12.91                     
CISPEP  11 ALA I  308    SER I  309          0       -10.38                     
CISPEP  12 ARG I  331    GLY I  332          0        -9.33                     
CISPEP  13 LYS J  105    ILE J  106          0        -4.42                     
CISPEP  14 ARG J  277    THR J  278          0       -12.79                     
CISPEP  15 ALA J  308    SER J  309          0       -11.63                     
CISPEP  16 ARG J  331    GLY J  332          0       -11.00                     
CISPEP  17 LYS K  105    ILE K  106          0        -4.99                     
CISPEP  18 ARG K  277    THR K  278          0       -12.90                     
CISPEP  19 ALA K  308    SER K  309          0       -11.41                     
CISPEP  20 ARG K  331    GLY K  332          0       -11.61                     
CISPEP  21 LYS L  105    ILE L  106          0         0.19                     
CISPEP  22 ARG L  277    THR L  278          0       -12.49                     
CISPEP  23 ALA L  308    SER L  309          0       -11.21                     
CISPEP  24 ARG L  331    GLY L  332          0       -10.13                     
SITE     1 AC1 17 GLY A  13  LEU A  14  GLY A  15  ARG A  16                    
SITE     2 AC1 17 PHE A  17  ASP A  36  ILE A  37  LYS A  41                    
SITE     3 AC1 17 ASN A  56  ALA A  57  ALA A  77  ILE A  78                    
SITE     4 AC1 17 GLY A  79  ALA A  80  LYS A 103  GLU A 125                    
SITE     5 AC1 17 ARG B  16                                                     
SITE     1 AC2 19 ARG A  16  ILE B  12  GLY B  13  LEU B  14                    
SITE     2 AC2 19 GLY B  15  ARG B  16  PHE B  17  ASP B  36                    
SITE     3 AC2 19 ILE B  37  LYS B  41  ALA B  55  ASN B  56                    
SITE     4 AC2 19 ALA B  57  ALA B  77  ILE B  78  GLY B  79                    
SITE     5 AC2 19 ALA B  80  LYS B 103  GLU B 125                               
SITE     1 AC3 17 GLY C  13  GLY C  15  ARG C  16  PHE C  17                    
SITE     2 AC3 17 ASP C  36  ILE C  37  LYS C  41  ALA C  55                    
SITE     3 AC3 17 ASN C  56  ALA C  57  ALA C  77  ILE C  78                    
SITE     4 AC3 17 GLY C  79  ALA C  80  LYS C 103  ARG D  16                    
SITE     5 AC3 17 GLU D 125                                                     
SITE     1 AC4 18 ARG C  16  GLY D  13  GLY D  15  ARG D  16                    
SITE     2 AC4 18 PHE D  17  ASP D  36  ILE D  37  LYS D  41                    
SITE     3 AC4 18 ALA D  55  ASN D  56  ALA D  57  ALA D  77                    
SITE     4 AC4 18 ILE D  78  GLY D  79  ALA D  80  ALA D  84                    
SITE     5 AC4 18 LYS D 103  GLU D 125                                          
SITE     1 AC5 19 GLY E  13  LEU E  14  GLY E  15  ARG E  16                    
SITE     2 AC5 19 PHE E  17  ASP E  36  ILE E  37  LYS E  41                    
SITE     3 AC5 19 ALA E  55  ASN E  56  ALA E  57  ALA E  77                    
SITE     4 AC5 19 ILE E  78  GLY E  79  ALA E  80  ALA E  84                    
SITE     5 AC5 19 LYS E 103  GLU E 125  ARG F  16                               
SITE     1 AC6 17 ARG E  16  GLU E 125  GLY F  13  GLY F  15                    
SITE     2 AC6 17 ARG F  16  PHE F  17  ASP F  36  ILE F  37                    
SITE     3 AC6 17 LYS F  41  ALA F  55  ASN F  56  ALA F  57                    
SITE     4 AC6 17 ILE F  78  GLY F  79  ALA F  80  LYS F 103                    
SITE     5 AC6 17 GLU F 125                                                     
SITE     1 AC7 18 GLY G  13  LEU G  14  GLY G  15  ARG G  16                    
SITE     2 AC7 18 PHE G  17  ASP G  36  ILE G  37  LYS G  41                    
SITE     3 AC7 18 ALA G  55  ASN G  56  ALA G  57  ALA G  77                    
SITE     4 AC7 18 ILE G  78  GLY G  79  ALA G  80  LYS G 103                    
SITE     5 AC7 18 GLU G 125  ARG H  16                                          
SITE     1 AC8 18 ARG G  16  GLU G 125  GLY H  13  GLY H  15                    
SITE     2 AC8 18 ARG H  16  PHE H  17  ASP H  36  ILE H  37                    
SITE     3 AC8 18 LYS H  41  ALA H  55  ASN H  56  ALA H  57                    
SITE     4 AC8 18 ALA H  77  ILE H  78  GLY H  79  ALA H  80                    
SITE     5 AC8 18 ALA H  84  LYS H 103                                          
SITE     1 AC9  8 VAL I  60  THR I  61  ASN I 175  ALA I 176                    
SITE     2 AC9  8 THR I 278  ALA I 279  THR I 390  VAL I 391                    
SITE     1 BC1  8 VAL J  60  THR J  61  ASN J 175  ALA J 176                    
SITE     2 BC1  8 THR J 278  ALA J 279  THR J 390  VAL J 391                    
SITE     1 BC2  8 VAL K  60  THR K  61  ASN K 175  ALA K 176                    
SITE     2 BC2  8 THR K 278  ALA K 279  THR K 390  VAL K 391                    
SITE     1 BC3  8 VAL L  60  THR L  61  ASN L 175  ALA L 176                    
SITE     2 BC3  8 THR L 278  ALA L 279  THR L 390  VAL L 391                    
CRYST1  146.520  140.190  153.930  90.00 105.69  90.00 P 1 21 1     16          
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      0.006825  0.000000  0.001917        0.00000                         
SCALE2      0.000000  0.007133  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006748        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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