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Database: PDB
Entry: 4Y4M
LinkDB: 4Y4M
Original site: 4Y4M 
HEADER    BIOSYNTHETIC PROTEIN                    10-FEB-15   4Y4M              
TITLE     THIAZOLE SYNTHASE THI4 FROM METHANOCALDOCOCCUS JANNASCHII             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE RIBOSE 1,5-BISPHOSPHATE ISOMERASE;                
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: RIBULOSE 1,5-BISPHOSPHATE SYNTHASE,RUBP SYNTHASE;           
COMPND   5 EC: 5.3.1.29;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: METHANOCALDOCOCCUS JANNASCHII;                  
SOURCE   3 ORGANISM_TAXID: 243232;                                              
SOURCE   4 STRAIN: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;     
SOURCE   5 GENE: MJ0601;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    THIAZOLE SYNTHASE, ISOMERASE, BIOSYNTHETIC PROTEIN                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.ZHANG,S.E.EALICK                                                    
REVDAT   2   04-MAY-16 4Y4M    1       JRNL                                     
REVDAT   1   09-MAR-16 4Y4M    0                                                
JRNL        AUTH   X.ZHANG,B.E.ESER,P.K.CHANANI,T.P.BEGLEY,S.E.EALICK           
JRNL        TITL   STRUCTURAL BASIS FOR IRON-MEDIATED SULFUR TRANSFER IN        
JRNL        TITL 2 ARCHAEL AND YEAST THIAZOLE SYNTHASES.                        
JRNL        REF    BIOCHEMISTRY                  V.  55  1826 2016              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   26919468                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.6B00030                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.71 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
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) : 2.71                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 68627                          
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) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3646                            
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) : 2.71                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.78                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4862                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.84                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 257                          
REMARK   3   BIN FREE R VALUE                    : 0.3360                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15270                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 353                                     
REMARK   3   SOLVENT ATOMS            : 21                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.81000                                              
REMARK   3    B22 (A**2) : 0.81000                                              
REMARK   3    B33 (A**2) : -2.62000                                             
REMARK   3    B12 (A**2) : 0.40000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.787         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.268         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15879 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 15492 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 21553 ; 1.361 ; 1.999       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 35590 ; 3.659 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2057 ; 6.054 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   567 ;41.608 ;24.497       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2606 ;16.322 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    72 ;20.202 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2536 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 17662 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  3250 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  8252 ; 2.963 ; 5.267       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  8251 ; 2.962 ; 5.267       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10301 ; 4.525 ; 7.895       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 10302 ; 4.525 ; 7.895       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7627 ; 4.143 ; 5.836       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  7628 ; 4.143 ; 5.836       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 11252 ; 6.613 ; 8.568       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 17265 ; 9.971 ;43.305       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 17264 ; 9.971 ;43.304       
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 : 1                                 
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      3       A     300      1                      
REMARK   3           1     B      3       B     300      1                      
REMARK   3           1     C      3       C     300      1                      
REMARK   3           1     D      3       D     300      1                      
REMARK   3           1     E      3       E     300      1                      
REMARK   3           1     F      3       F     300      1                      
REMARK   3           1     G      3       G     300      1                      
REMARK   3           1     H      3       H     300      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      1    A (A**2):   3747 ;  5.59 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):   3747 ;  5.93 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):   3747 ;  7.08 ;  0.50           
REMARK   3   TIGHT THERMAL      1    D (A**2):   3747 ;  7.14 ;  0.50           
REMARK   3   TIGHT THERMAL      1    E (A**2):   3747 ;  5.88 ;  0.50           
REMARK   3   TIGHT THERMAL      1    F (A**2):   3747 ;  4.35 ;  0.50           
REMARK   3   TIGHT THERMAL      1    G (A**2):   3747 ;  4.29 ;  0.50           
REMARK   3   TIGHT THERMAL      1    H (A**2):   3747 ;  5.85 ;  0.50           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4Y4M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206837.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 72800                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : 0.07200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 1RP0                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.05 M POTASSIUM/SODIUM TARTRATE, 0.1    
REMARK 280  M CHES/ SODIUM HYDROXIDE PH 9.5, 0.2 M LITHIUM SULFATE,             
REMARK 280  EVAPORATION, TEMPERATURE 295K                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.88533            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       24.44267            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H                
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   -22                                                      
REMARK 465     GLY A   -21                                                      
REMARK 465     SER A   -20                                                      
REMARK 465     ASP A   -19                                                      
REMARK 465     LYS A   -18                                                      
REMARK 465     ILE A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     GLU A    -7                                                      
REMARK 465     ASN A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     TYR A    -4                                                      
REMARK 465     PHE A    -3                                                      
REMARK 465     GLN A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     ASN A   265                                                      
REMARK 465     LYS A   266                                                      
REMARK 465     GLU A   267                                                      
REMARK 465     MET B   -22                                                      
REMARK 465     GLY B   -21                                                      
REMARK 465     SER B   -20                                                      
REMARK 465     ASP B   -19                                                      
REMARK 465     LYS B   -18                                                      
REMARK 465     ILE B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     GLU B    -7                                                      
REMARK 465     ASN B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     TYR B    -4                                                      
REMARK 465     PHE B    -3                                                      
REMARK 465     GLN B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     MET B     5                                                      
REMARK 465     ASN B     6                                                      
REMARK 465     ILE B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     ASP B     9                                                      
REMARK 465     LYS B   266                                                      
REMARK 465     GLU B   267                                                      
REMARK 465     MET C   -22                                                      
REMARK 465     GLY C   -21                                                      
REMARK 465     SER C   -20                                                      
REMARK 465     ASP C   -19                                                      
REMARK 465     LYS C   -18                                                      
REMARK 465     ILE C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     SER C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     GLY C    -8                                                      
REMARK 465     GLU C    -7                                                      
REMARK 465     ASN C    -6                                                      
REMARK 465     LEU C    -5                                                      
REMARK 465     TYR C    -4                                                      
REMARK 465     PHE C    -3                                                      
REMARK 465     GLN C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     ASN C     3                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     MET C     5                                                      
REMARK 465     ASN C     6                                                      
REMARK 465     ILE C     7                                                      
REMARK 465     LYS C     8                                                      
REMARK 465     ASP C     9                                                      
REMARK 465     ASN C   265                                                      
REMARK 465     LYS C   266                                                      
REMARK 465     GLU C   267                                                      
REMARK 465     MET D   -22                                                      
REMARK 465     GLY D   -21                                                      
REMARK 465     SER D   -20                                                      
REMARK 465     ASP D   -19                                                      
REMARK 465     LYS D   -18                                                      
REMARK 465     ILE D   -17                                                      
REMARK 465     HIS D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     SER D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     GLY D    -8                                                      
REMARK 465     GLU D    -7                                                      
REMARK 465     ASN D    -6                                                      
REMARK 465     LEU D    -5                                                      
REMARK 465     TYR D    -4                                                      
REMARK 465     PHE D    -3                                                      
REMARK 465     GLN D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 465     ASN D     3                                                      
REMARK 465     LEU D     4                                                      
REMARK 465     MET D     5                                                      
REMARK 465     ASN D     6                                                      
REMARK 465     ILE D     7                                                      
REMARK 465     LYS D     8                                                      
REMARK 465     ASP D     9                                                      
REMARK 465     ASN D   265                                                      
REMARK 465     LYS D   266                                                      
REMARK 465     GLU D   267                                                      
REMARK 465     MET E   -22                                                      
REMARK 465     GLY E   -21                                                      
REMARK 465     SER E   -20                                                      
REMARK 465     ASP E   -19                                                      
REMARK 465     LYS E   -18                                                      
REMARK 465     ILE E   -17                                                      
REMARK 465     HIS E   -16                                                      
REMARK 465     HIS E   -15                                                      
REMARK 465     HIS E   -14                                                      
REMARK 465     HIS E   -13                                                      
REMARK 465     HIS E   -12                                                      
REMARK 465     HIS E   -11                                                      
REMARK 465     SER E   -10                                                      
REMARK 465     SER E    -9                                                      
REMARK 465     GLY E    -8                                                      
REMARK 465     GLU E    -7                                                      
REMARK 465     ASN E    -6                                                      
REMARK 465     LEU E    -5                                                      
REMARK 465     TYR E    -4                                                      
REMARK 465     PHE E    -3                                                      
REMARK 465     GLN E    -2                                                      
REMARK 465     GLY E    -1                                                      
REMARK 465     HIS E     0                                                      
REMARK 465     MET E     1                                                      
REMARK 465     VAL E     2                                                      
REMARK 465     ASN E     3                                                      
REMARK 465     LEU E     4                                                      
REMARK 465     MET E     5                                                      
REMARK 465     ASN E     6                                                      
REMARK 465     ILE E     7                                                      
REMARK 465     LYS E     8                                                      
REMARK 465     ASP E     9                                                      
REMARK 465     LYS E   266                                                      
REMARK 465     GLU E   267                                                      
REMARK 465     MET F   -22                                                      
REMARK 465     GLY F   -21                                                      
REMARK 465     SER F   -20                                                      
REMARK 465     ASP F   -19                                                      
REMARK 465     LYS F   -18                                                      
REMARK 465     ILE F   -17                                                      
REMARK 465     HIS F   -16                                                      
REMARK 465     HIS F   -15                                                      
REMARK 465     HIS F   -14                                                      
REMARK 465     HIS F   -13                                                      
REMARK 465     HIS F   -12                                                      
REMARK 465     HIS F   -11                                                      
REMARK 465     SER F   -10                                                      
REMARK 465     SER F    -9                                                      
REMARK 465     GLY F    -8                                                      
REMARK 465     GLU F    -7                                                      
REMARK 465     ASN F    -6                                                      
REMARK 465     LEU F    -5                                                      
REMARK 465     TYR F    -4                                                      
REMARK 465     PHE F    -3                                                      
REMARK 465     GLN F    -2                                                      
REMARK 465     GLY F    -1                                                      
REMARK 465     HIS F     0                                                      
REMARK 465     MET F     1                                                      
REMARK 465     VAL F     2                                                      
REMARK 465     ASN F     3                                                      
REMARK 465     LYS F   266                                                      
REMARK 465     GLU F   267                                                      
REMARK 465     MET G   -22                                                      
REMARK 465     GLY G   -21                                                      
REMARK 465     SER G   -20                                                      
REMARK 465     ASP G   -19                                                      
REMARK 465     LYS G   -18                                                      
REMARK 465     ILE G   -17                                                      
REMARK 465     HIS G   -16                                                      
REMARK 465     HIS G   -15                                                      
REMARK 465     HIS G   -14                                                      
REMARK 465     HIS G   -13                                                      
REMARK 465     HIS G   -12                                                      
REMARK 465     HIS G   -11                                                      
REMARK 465     SER G   -10                                                      
REMARK 465     SER G    -9                                                      
REMARK 465     GLY G    -8                                                      
REMARK 465     GLU G    -7                                                      
REMARK 465     ASN G    -6                                                      
REMARK 465     LEU G    -5                                                      
REMARK 465     TYR G    -4                                                      
REMARK 465     PHE G    -3                                                      
REMARK 465     GLN G    -2                                                      
REMARK 465     GLY G    -1                                                      
REMARK 465     HIS G     0                                                      
REMARK 465     MET G     1                                                      
REMARK 465     VAL G     2                                                      
REMARK 465     ASN G     3                                                      
REMARK 465     LYS G   266                                                      
REMARK 465     GLU G   267                                                      
REMARK 465     MET H   -22                                                      
REMARK 465     GLY H   -21                                                      
REMARK 465     SER H   -20                                                      
REMARK 465     ASP H   -19                                                      
REMARK 465     LYS H   -18                                                      
REMARK 465     ILE H   -17                                                      
REMARK 465     HIS H   -16                                                      
REMARK 465     HIS H   -15                                                      
REMARK 465     HIS H   -14                                                      
REMARK 465     HIS H   -13                                                      
REMARK 465     HIS H   -12                                                      
REMARK 465     HIS H   -11                                                      
REMARK 465     SER H   -10                                                      
REMARK 465     SER H    -9                                                      
REMARK 465     GLY H    -8                                                      
REMARK 465     GLU H    -7                                                      
REMARK 465     ASN H    -6                                                      
REMARK 465     LEU H    -5                                                      
REMARK 465     TYR H    -4                                                      
REMARK 465     PHE H    -3                                                      
REMARK 465     GLN H    -2                                                      
REMARK 465     GLY H    -1                                                      
REMARK 465     HIS H     0                                                      
REMARK 465     MET H     1                                                      
REMARK 465     VAL H     2                                                      
REMARK 465     ASN H     3                                                      
REMARK 465     LEU H     4                                                      
REMARK 465     MET H     5                                                      
REMARK 465     ASN H   265                                                      
REMARK 465     LYS H   266                                                      
REMARK 465     GLU H   267                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   8    CG   CD   CE   NZ                                   
REMARK 470     LYS A  11    CG   CD   CE   NZ                                   
REMARK 470     LYS A  57    CG   CD   CE   NZ                                   
REMARK 470     GLU A  89    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 196    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 198    CG   OD1  OD2                                       
REMARK 470     LYS A 264    CG   CD   CE   NZ                                   
REMARK 470     LYS B  11    CG   CD   CE   NZ                                   
REMARK 470     ASN B  13    CG   OD1  ND2                                       
REMARK 470     LYS B  57    CG   CD   CE   NZ                                   
REMARK 470     GLU B  89    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 191    CG   CD   CE   NZ                                   
REMARK 470     LYS B 194    CG   CD   CE   NZ                                   
REMARK 470     GLU B 196    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 198    CG   OD1  OD2                                       
REMARK 470     LYS C  11    CG   CD   CE   NZ                                   
REMARK 470     LYS C  57    CG   CD   CE   NZ                                   
REMARK 470     GLU C  89    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 191    CG   CD   CE   NZ                                   
REMARK 470     ASP C 198    CG   OD1  OD2                                       
REMARK 470     LYS C 264    CG   CD   CE   NZ                                   
REMARK 470     LYS D  11    CG   CD   CE   NZ                                   
REMARK 470     LYS D  57    CG   CD   CE   NZ                                   
REMARK 470     GLU D  89    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 191    CG   CD   CE   NZ                                   
REMARK 470     ASP D 198    CG   OD1  OD2                                       
REMARK 470     LYS D 264    CG   CD   CE   NZ                                   
REMARK 470     LYS E  11    CG   CD   CE   NZ                                   
REMARK 470     ASN E  13    CG   OD1  ND2                                       
REMARK 470     LYS E  57    CG   CD   CE   NZ                                   
REMARK 470     GLU E  89    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 191    CG   CD   CE   NZ                                   
REMARK 470     GLU E 196    CG   CD   OE1  OE2                                  
REMARK 470     LEU F   4    CG   CD1  CD2                                       
REMARK 470     LYS F   8    CG   CD   CE   NZ                                   
REMARK 470     LYS F  11    CG   CD   CE   NZ                                   
REMARK 470     LYS F  57    CG   CD   CE   NZ                                   
REMARK 470     GLU F  89    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 191    CG   CD   CE   NZ                                   
REMARK 470     ASP F 198    CG   OD1  OD2                                       
REMARK 470     LYS G   8    CG   CD   CE   NZ                                   
REMARK 470     LYS G  11    CG   CD   CE   NZ                                   
REMARK 470     LYS G  57    CG   CD   CE   NZ                                   
REMARK 470     GLU G  89    CG   CD   OE1  OE2                                  
REMARK 470     LYS G 191    CG   CD   CE   NZ                                   
REMARK 470     LYS G 194    CG   CD   CE   NZ                                   
REMARK 470     ASP G 198    CG   OD1  OD2                                       
REMARK 470     LYS H   8    CG   CD   CE   NZ                                   
REMARK 470     LYS H  11    CG   CD   CE   NZ                                   
REMARK 470     LYS H  57    CG   CD   CE   NZ                                   
REMARK 470     GLU H  89    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 191    CG   CD   CE   NZ                                   
REMARK 470     LYS H 194    CG   CD   CE   NZ                                   
REMARK 470     GLU H 196    CG   CD   OE1  OE2                                  
REMARK 470     ASP H 198    CG   OD1  OD2                                       
REMARK 470     LYS H 264    CG   CD   CE   NZ                                   
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   CD2  PHE A    28     CD1  PHE B    28              1.91            
REMARK 500   CD2  PHE C    28     CD1  PHE D    28              1.96            
REMARK 500   CZ   PHE A    28     CA   PHE B    28              1.97            
REMARK 500   CE1  PHE A    28     CB   PHE B    28              2.02            
REMARK 500   CZ   PHE A    28     CB   PHE B    28              2.10            
REMARK 500   CD2  PHE C    28     CG   PHE D    28              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B 240   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A   9       40.30   -105.44                                   
REMARK 500    ALA A  44       42.21    -92.65                                   
REMARK 500    ALA A 197      145.98   -173.10                                   
REMARK 500    SER A 204     -174.75    -69.95                                   
REMARK 500    TRP A 206       86.62   -150.29                                   
REMARK 500    ALA A 243       37.25    -82.10                                   
REMARK 500    ALA B  44       43.68    -94.01                                   
REMARK 500    ALA B 197      146.82   -173.86                                   
REMARK 500    TRP B 206       86.13   -151.08                                   
REMARK 500    ALA B 243       37.27    -84.47                                   
REMARK 500    ALA C  44       42.49    -94.77                                   
REMARK 500    ALA C 197      146.19   -172.69                                   
REMARK 500    TRP C 206       85.37   -150.78                                   
REMARK 500    ALA C 243       37.23    -84.02                                   
REMARK 500    ALA D  44       42.27    -94.91                                   
REMARK 500    ALA D 197      145.53   -172.32                                   
REMARK 500    TRP D 206       85.91   -150.80                                   
REMARK 500    ALA D 243       36.40    -82.61                                   
REMARK 500    ALA E  44       44.23    -93.32                                   
REMARK 500    ALA E 197      146.57   -173.93                                   
REMARK 500    TRP E 206       86.51   -150.68                                   
REMARK 500    ALA E 243       37.24    -83.55                                   
REMARK 500    LYS F   8      -19.01    -49.79                                   
REMARK 500    ALA F  44       40.52    -93.62                                   
REMARK 500    ASP F 146      -38.30    -39.26                                   
REMARK 500    ALA F 197      145.47   -173.53                                   
REMARK 500    ALA F 243       36.54    -82.12                                   
REMARK 500    LYS G   8      -19.62    -49.87                                   
REMARK 500    ALA G  44       42.53    -94.96                                   
REMARK 500    ALA G 197      145.96   -173.47                                   
REMARK 500    ALA G 243       36.74    -82.63                                   
REMARK 500    ASP H   9       48.79   -109.72                                   
REMARK 500    ALA H  44       42.13    -93.16                                   
REMARK 500    ASP H 146      -38.70    -39.66                                   
REMARK 500    ALA H 197      146.07   -173.18                                   
REMARK 500    ALA H 243       37.99    -82.89                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 48F A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NHE A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 48F B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 48F C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NHE C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 48F D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 48F E 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 48F F 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NHE F 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 48F G 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NHE G 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 48F H 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NHE H 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4Y4L   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Y4N   RELATED DB: PDB                                   
DBREF  4Y4M A    1   267  UNP    Q58018   RUBPS_METJA      1    267             
DBREF  4Y4M B    1   267  UNP    Q58018   RUBPS_METJA      1    267             
DBREF  4Y4M C    1   267  UNP    Q58018   RUBPS_METJA      1    267             
DBREF  4Y4M D    1   267  UNP    Q58018   RUBPS_METJA      1    267             
DBREF  4Y4M E    1   267  UNP    Q58018   RUBPS_METJA      1    267             
DBREF  4Y4M F    1   267  UNP    Q58018   RUBPS_METJA      1    267             
DBREF  4Y4M G    1   267  UNP    Q58018   RUBPS_METJA      1    267             
DBREF  4Y4M H    1   267  UNP    Q58018   RUBPS_METJA      1    267             
SEQADV 4Y4M MET A  -22  UNP  Q58018              INITIATING METHIONINE          
SEQADV 4Y4M GLY A  -21  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER A  -20  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ASP A  -19  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M LYS A  -18  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ILE A  -17  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS A  -16  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS A  -15  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS A  -14  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS A  -13  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS A  -12  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS A  -11  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER A  -10  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER A   -9  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLY A   -8  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLU A   -7  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ASN A   -6  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M LEU A   -5  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M TYR A   -4  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M PHE A   -3  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLN A   -2  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLY A   -1  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS A    0  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M MET B  -22  UNP  Q58018              INITIATING METHIONINE          
SEQADV 4Y4M GLY B  -21  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER B  -20  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ASP B  -19  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M LYS B  -18  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ILE B  -17  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS B  -16  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS B  -15  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS B  -14  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS B  -13  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS B  -12  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS B  -11  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER B  -10  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER B   -9  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLY B   -8  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLU B   -7  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ASN B   -6  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M LEU B   -5  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M TYR B   -4  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M PHE B   -3  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLN B   -2  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLY B   -1  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS B    0  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M MET C  -22  UNP  Q58018              INITIATING METHIONINE          
SEQADV 4Y4M GLY C  -21  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER C  -20  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ASP C  -19  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M LYS C  -18  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ILE C  -17  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS C  -16  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS C  -15  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS C  -14  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS C  -13  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS C  -12  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS C  -11  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER C  -10  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER C   -9  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLY C   -8  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLU C   -7  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ASN C   -6  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M LEU C   -5  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M TYR C   -4  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M PHE C   -3  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLN C   -2  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLY C   -1  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS C    0  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M MET D  -22  UNP  Q58018              INITIATING METHIONINE          
SEQADV 4Y4M GLY D  -21  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER D  -20  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ASP D  -19  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M LYS D  -18  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ILE D  -17  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS D  -16  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS D  -15  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS D  -14  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS D  -13  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS D  -12  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS D  -11  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER D  -10  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER D   -9  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLY D   -8  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLU D   -7  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ASN D   -6  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M LEU D   -5  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M TYR D   -4  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M PHE D   -3  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLN D   -2  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLY D   -1  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS D    0  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M MET E  -22  UNP  Q58018              INITIATING METHIONINE          
SEQADV 4Y4M GLY E  -21  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER E  -20  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ASP E  -19  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M LYS E  -18  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ILE E  -17  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS E  -16  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS E  -15  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS E  -14  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS E  -13  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS E  -12  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS E  -11  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER E  -10  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER E   -9  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLY E   -8  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLU E   -7  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ASN E   -6  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M LEU E   -5  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M TYR E   -4  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M PHE E   -3  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLN E   -2  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLY E   -1  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS E    0  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M MET F  -22  UNP  Q58018              INITIATING METHIONINE          
SEQADV 4Y4M GLY F  -21  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER F  -20  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ASP F  -19  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M LYS F  -18  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ILE F  -17  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS F  -16  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS F  -15  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS F  -14  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS F  -13  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS F  -12  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS F  -11  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER F  -10  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER F   -9  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLY F   -8  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLU F   -7  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ASN F   -6  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M LEU F   -5  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M TYR F   -4  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M PHE F   -3  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLN F   -2  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLY F   -1  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS F    0  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M MET G  -22  UNP  Q58018              INITIATING METHIONINE          
SEQADV 4Y4M GLY G  -21  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER G  -20  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ASP G  -19  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M LYS G  -18  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ILE G  -17  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS G  -16  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS G  -15  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS G  -14  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS G  -13  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS G  -12  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS G  -11  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER G  -10  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER G   -9  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLY G   -8  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLU G   -7  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ASN G   -6  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M LEU G   -5  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M TYR G   -4  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M PHE G   -3  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLN G   -2  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLY G   -1  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS G    0  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M MET H  -22  UNP  Q58018              INITIATING METHIONINE          
SEQADV 4Y4M GLY H  -21  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER H  -20  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ASP H  -19  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M LYS H  -18  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ILE H  -17  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS H  -16  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS H  -15  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS H  -14  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS H  -13  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS H  -12  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS H  -11  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER H  -10  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M SER H   -9  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLY H   -8  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLU H   -7  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M ASN H   -6  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M LEU H   -5  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M TYR H   -4  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M PHE H   -3  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLN H   -2  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M GLY H   -1  UNP  Q58018              EXPRESSION TAG                 
SEQADV 4Y4M HIS H    0  UNP  Q58018              EXPRESSION TAG                 
SEQRES   1 A  290  MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 A  290  SER GLY GLU ASN LEU TYR PHE GLN GLY HIS MET VAL ASN          
SEQRES   3 A  290  LEU MET ASN ILE LYS ASP ILE LYS LEU ASN ALA ASP GLU          
SEQRES   4 A  290  THR LYS THR THR LYS ALA ILE LEU LYS ALA SER PHE ASP          
SEQRES   5 A  290  MET TRP LEU ASP ILE VAL GLU ALA ASP VAL VAL ILE VAL          
SEQRES   6 A  290  GLY ALA GLY PRO SER GLY LEU THR CYS ALA ARG TYR LEU          
SEQRES   7 A  290  ALA LYS GLU GLY PHE LYS VAL VAL VAL LEU GLU ARG HIS          
SEQRES   8 A  290  LEU ALA PHE GLY GLY GLY THR TRP GLY GLY GLY MET GLY          
SEQRES   9 A  290  PHE PRO TYR ILE VAL VAL GLU GLU PRO ALA ASP GLU LEU          
SEQRES  10 A  290  LEU ARG GLU VAL GLY ILE LYS LEU ILE ASP MET GLY ASP          
SEQRES  11 A  290  GLY TYR TYR VAL ALA ASP SER VAL GLU VAL PRO ALA LYS          
SEQRES  12 A  290  LEU ALA VAL ALA ALA MET ASP ALA GLY ALA LYS ILE LEU          
SEQRES  13 A  290  THR GLY ILE VAL VAL GLU ASP LEU ILE LEU ARG GLU ASP          
SEQRES  14 A  290  GLY VAL ALA GLY VAL VAL ILE ASN SER TYR ALA ILE GLU          
SEQRES  15 A  290  ARG ALA GLY LEU HIS ILE ASP PRO LEU THR ILE ARG SER          
SEQRES  16 A  290  LYS VAL VAL VAL ASP ALA THR GLY HIS GLU ALA SER ILE          
SEQRES  17 A  290  VAL ASN ILE LEU VAL LYS LYS ASN LYS LEU GLU ALA ASP          
SEQRES  18 A  290  VAL PRO GLY GLU LYS SER MET TRP ALA GLU LYS GLY GLU          
SEQRES  19 A  290  ASN ALA LEU LEU ARG ASN THR ARG GLU VAL TYR PRO ASN          
SEQRES  20 A  290  LEU PHE VAL CYS GLY MET ALA ALA ASN ALA SER HIS GLY          
SEQRES  21 A  290  GLY TYR ARG MET GLY ALA ILE PHE GLY GLY MET TYR LEU          
SEQRES  22 A  290  SER GLY LYS LEU CYS ALA GLU LEU ILE THR GLU LYS LEU          
SEQRES  23 A  290  LYS ASN LYS GLU                                              
SEQRES   1 B  290  MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 B  290  SER GLY GLU ASN LEU TYR PHE GLN GLY HIS MET VAL ASN          
SEQRES   3 B  290  LEU MET ASN ILE LYS ASP ILE LYS LEU ASN ALA ASP GLU          
SEQRES   4 B  290  THR LYS THR THR LYS ALA ILE LEU LYS ALA SER PHE ASP          
SEQRES   5 B  290  MET TRP LEU ASP ILE VAL GLU ALA ASP VAL VAL ILE VAL          
SEQRES   6 B  290  GLY ALA GLY PRO SER GLY LEU THR CYS ALA ARG TYR LEU          
SEQRES   7 B  290  ALA LYS GLU GLY PHE LYS VAL VAL VAL LEU GLU ARG HIS          
SEQRES   8 B  290  LEU ALA PHE GLY GLY GLY THR TRP GLY GLY GLY MET GLY          
SEQRES   9 B  290  PHE PRO TYR ILE VAL VAL GLU GLU PRO ALA ASP GLU LEU          
SEQRES  10 B  290  LEU ARG GLU VAL GLY ILE LYS LEU ILE ASP MET GLY ASP          
SEQRES  11 B  290  GLY TYR TYR VAL ALA ASP SER VAL GLU VAL PRO ALA LYS          
SEQRES  12 B  290  LEU ALA VAL ALA ALA MET ASP ALA GLY ALA LYS ILE LEU          
SEQRES  13 B  290  THR GLY ILE VAL VAL GLU ASP LEU ILE LEU ARG GLU ASP          
SEQRES  14 B  290  GLY VAL ALA GLY VAL VAL ILE ASN SER TYR ALA ILE GLU          
SEQRES  15 B  290  ARG ALA GLY LEU HIS ILE ASP PRO LEU THR ILE ARG SER          
SEQRES  16 B  290  LYS VAL VAL VAL ASP ALA THR GLY HIS GLU ALA SER ILE          
SEQRES  17 B  290  VAL ASN ILE LEU VAL LYS LYS ASN LYS LEU GLU ALA ASP          
SEQRES  18 B  290  VAL PRO GLY GLU LYS SER MET TRP ALA GLU LYS GLY GLU          
SEQRES  19 B  290  ASN ALA LEU LEU ARG ASN THR ARG GLU VAL TYR PRO ASN          
SEQRES  20 B  290  LEU PHE VAL CYS GLY MET ALA ALA ASN ALA SER HIS GLY          
SEQRES  21 B  290  GLY TYR ARG MET GLY ALA ILE PHE GLY GLY MET TYR LEU          
SEQRES  22 B  290  SER GLY LYS LEU CYS ALA GLU LEU ILE THR GLU LYS LEU          
SEQRES  23 B  290  LYS ASN LYS GLU                                              
SEQRES   1 C  290  MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 C  290  SER GLY GLU ASN LEU TYR PHE GLN GLY HIS MET VAL ASN          
SEQRES   3 C  290  LEU MET ASN ILE LYS ASP ILE LYS LEU ASN ALA ASP GLU          
SEQRES   4 C  290  THR LYS THR THR LYS ALA ILE LEU LYS ALA SER PHE ASP          
SEQRES   5 C  290  MET TRP LEU ASP ILE VAL GLU ALA ASP VAL VAL ILE VAL          
SEQRES   6 C  290  GLY ALA GLY PRO SER GLY LEU THR CYS ALA ARG TYR LEU          
SEQRES   7 C  290  ALA LYS GLU GLY PHE LYS VAL VAL VAL LEU GLU ARG HIS          
SEQRES   8 C  290  LEU ALA PHE GLY GLY GLY THR TRP GLY GLY GLY MET GLY          
SEQRES   9 C  290  PHE PRO TYR ILE VAL VAL GLU GLU PRO ALA ASP GLU LEU          
SEQRES  10 C  290  LEU ARG GLU VAL GLY ILE LYS LEU ILE ASP MET GLY ASP          
SEQRES  11 C  290  GLY TYR TYR VAL ALA ASP SER VAL GLU VAL PRO ALA LYS          
SEQRES  12 C  290  LEU ALA VAL ALA ALA MET ASP ALA GLY ALA LYS ILE LEU          
SEQRES  13 C  290  THR GLY ILE VAL VAL GLU ASP LEU ILE LEU ARG GLU ASP          
SEQRES  14 C  290  GLY VAL ALA GLY VAL VAL ILE ASN SER TYR ALA ILE GLU          
SEQRES  15 C  290  ARG ALA GLY LEU HIS ILE ASP PRO LEU THR ILE ARG SER          
SEQRES  16 C  290  LYS VAL VAL VAL ASP ALA THR GLY HIS GLU ALA SER ILE          
SEQRES  17 C  290  VAL ASN ILE LEU VAL LYS LYS ASN LYS LEU GLU ALA ASP          
SEQRES  18 C  290  VAL PRO GLY GLU LYS SER MET TRP ALA GLU LYS GLY GLU          
SEQRES  19 C  290  ASN ALA LEU LEU ARG ASN THR ARG GLU VAL TYR PRO ASN          
SEQRES  20 C  290  LEU PHE VAL CYS GLY MET ALA ALA ASN ALA SER HIS GLY          
SEQRES  21 C  290  GLY TYR ARG MET GLY ALA ILE PHE GLY GLY MET TYR LEU          
SEQRES  22 C  290  SER GLY LYS LEU CYS ALA GLU LEU ILE THR GLU LYS LEU          
SEQRES  23 C  290  LYS ASN LYS GLU                                              
SEQRES   1 D  290  MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 D  290  SER GLY GLU ASN LEU TYR PHE GLN GLY HIS MET VAL ASN          
SEQRES   3 D  290  LEU MET ASN ILE LYS ASP ILE LYS LEU ASN ALA ASP GLU          
SEQRES   4 D  290  THR LYS THR THR LYS ALA ILE LEU LYS ALA SER PHE ASP          
SEQRES   5 D  290  MET TRP LEU ASP ILE VAL GLU ALA ASP VAL VAL ILE VAL          
SEQRES   6 D  290  GLY ALA GLY PRO SER GLY LEU THR CYS ALA ARG TYR LEU          
SEQRES   7 D  290  ALA LYS GLU GLY PHE LYS VAL VAL VAL LEU GLU ARG HIS          
SEQRES   8 D  290  LEU ALA PHE GLY GLY GLY THR TRP GLY GLY GLY MET GLY          
SEQRES   9 D  290  PHE PRO TYR ILE VAL VAL GLU GLU PRO ALA ASP GLU LEU          
SEQRES  10 D  290  LEU ARG GLU VAL GLY ILE LYS LEU ILE ASP MET GLY ASP          
SEQRES  11 D  290  GLY TYR TYR VAL ALA ASP SER VAL GLU VAL PRO ALA LYS          
SEQRES  12 D  290  LEU ALA VAL ALA ALA MET ASP ALA GLY ALA LYS ILE LEU          
SEQRES  13 D  290  THR GLY ILE VAL VAL GLU ASP LEU ILE LEU ARG GLU ASP          
SEQRES  14 D  290  GLY VAL ALA GLY VAL VAL ILE ASN SER TYR ALA ILE GLU          
SEQRES  15 D  290  ARG ALA GLY LEU HIS ILE ASP PRO LEU THR ILE ARG SER          
SEQRES  16 D  290  LYS VAL VAL VAL ASP ALA THR GLY HIS GLU ALA SER ILE          
SEQRES  17 D  290  VAL ASN ILE LEU VAL LYS LYS ASN LYS LEU GLU ALA ASP          
SEQRES  18 D  290  VAL PRO GLY GLU LYS SER MET TRP ALA GLU LYS GLY GLU          
SEQRES  19 D  290  ASN ALA LEU LEU ARG ASN THR ARG GLU VAL TYR PRO ASN          
SEQRES  20 D  290  LEU PHE VAL CYS GLY MET ALA ALA ASN ALA SER HIS GLY          
SEQRES  21 D  290  GLY TYR ARG MET GLY ALA ILE PHE GLY GLY MET TYR LEU          
SEQRES  22 D  290  SER GLY LYS LEU CYS ALA GLU LEU ILE THR GLU LYS LEU          
SEQRES  23 D  290  LYS ASN LYS GLU                                              
SEQRES   1 E  290  MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 E  290  SER GLY GLU ASN LEU TYR PHE GLN GLY HIS MET VAL ASN          
SEQRES   3 E  290  LEU MET ASN ILE LYS ASP ILE LYS LEU ASN ALA ASP GLU          
SEQRES   4 E  290  THR LYS THR THR LYS ALA ILE LEU LYS ALA SER PHE ASP          
SEQRES   5 E  290  MET TRP LEU ASP ILE VAL GLU ALA ASP VAL VAL ILE VAL          
SEQRES   6 E  290  GLY ALA GLY PRO SER GLY LEU THR CYS ALA ARG TYR LEU          
SEQRES   7 E  290  ALA LYS GLU GLY PHE LYS VAL VAL VAL LEU GLU ARG HIS          
SEQRES   8 E  290  LEU ALA PHE GLY GLY GLY THR TRP GLY GLY GLY MET GLY          
SEQRES   9 E  290  PHE PRO TYR ILE VAL VAL GLU GLU PRO ALA ASP GLU LEU          
SEQRES  10 E  290  LEU ARG GLU VAL GLY ILE LYS LEU ILE ASP MET GLY ASP          
SEQRES  11 E  290  GLY TYR TYR VAL ALA ASP SER VAL GLU VAL PRO ALA LYS          
SEQRES  12 E  290  LEU ALA VAL ALA ALA MET ASP ALA GLY ALA LYS ILE LEU          
SEQRES  13 E  290  THR GLY ILE VAL VAL GLU ASP LEU ILE LEU ARG GLU ASP          
SEQRES  14 E  290  GLY VAL ALA GLY VAL VAL ILE ASN SER TYR ALA ILE GLU          
SEQRES  15 E  290  ARG ALA GLY LEU HIS ILE ASP PRO LEU THR ILE ARG SER          
SEQRES  16 E  290  LYS VAL VAL VAL ASP ALA THR GLY HIS GLU ALA SER ILE          
SEQRES  17 E  290  VAL ASN ILE LEU VAL LYS LYS ASN LYS LEU GLU ALA ASP          
SEQRES  18 E  290  VAL PRO GLY GLU LYS SER MET TRP ALA GLU LYS GLY GLU          
SEQRES  19 E  290  ASN ALA LEU LEU ARG ASN THR ARG GLU VAL TYR PRO ASN          
SEQRES  20 E  290  LEU PHE VAL CYS GLY MET ALA ALA ASN ALA SER HIS GLY          
SEQRES  21 E  290  GLY TYR ARG MET GLY ALA ILE PHE GLY GLY MET TYR LEU          
SEQRES  22 E  290  SER GLY LYS LEU CYS ALA GLU LEU ILE THR GLU LYS LEU          
SEQRES  23 E  290  LYS ASN LYS GLU                                              
SEQRES   1 F  290  MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 F  290  SER GLY GLU ASN LEU TYR PHE GLN GLY HIS MET VAL ASN          
SEQRES   3 F  290  LEU MET ASN ILE LYS ASP ILE LYS LEU ASN ALA ASP GLU          
SEQRES   4 F  290  THR LYS THR THR LYS ALA ILE LEU LYS ALA SER PHE ASP          
SEQRES   5 F  290  MET TRP LEU ASP ILE VAL GLU ALA ASP VAL VAL ILE VAL          
SEQRES   6 F  290  GLY ALA GLY PRO SER GLY LEU THR CYS ALA ARG TYR LEU          
SEQRES   7 F  290  ALA LYS GLU GLY PHE LYS VAL VAL VAL LEU GLU ARG HIS          
SEQRES   8 F  290  LEU ALA PHE GLY GLY GLY THR TRP GLY GLY GLY MET GLY          
SEQRES   9 F  290  PHE PRO TYR ILE VAL VAL GLU GLU PRO ALA ASP GLU LEU          
SEQRES  10 F  290  LEU ARG GLU VAL GLY ILE LYS LEU ILE ASP MET GLY ASP          
SEQRES  11 F  290  GLY TYR TYR VAL ALA ASP SER VAL GLU VAL PRO ALA LYS          
SEQRES  12 F  290  LEU ALA VAL ALA ALA MET ASP ALA GLY ALA LYS ILE LEU          
SEQRES  13 F  290  THR GLY ILE VAL VAL GLU ASP LEU ILE LEU ARG GLU ASP          
SEQRES  14 F  290  GLY VAL ALA GLY VAL VAL ILE ASN SER TYR ALA ILE GLU          
SEQRES  15 F  290  ARG ALA GLY LEU HIS ILE ASP PRO LEU THR ILE ARG SER          
SEQRES  16 F  290  LYS VAL VAL VAL ASP ALA THR GLY HIS GLU ALA SER ILE          
SEQRES  17 F  290  VAL ASN ILE LEU VAL LYS LYS ASN LYS LEU GLU ALA ASP          
SEQRES  18 F  290  VAL PRO GLY GLU LYS SER MET TRP ALA GLU LYS GLY GLU          
SEQRES  19 F  290  ASN ALA LEU LEU ARG ASN THR ARG GLU VAL TYR PRO ASN          
SEQRES  20 F  290  LEU PHE VAL CYS GLY MET ALA ALA ASN ALA SER HIS GLY          
SEQRES  21 F  290  GLY TYR ARG MET GLY ALA ILE PHE GLY GLY MET TYR LEU          
SEQRES  22 F  290  SER GLY LYS LEU CYS ALA GLU LEU ILE THR GLU LYS LEU          
SEQRES  23 F  290  LYS ASN LYS GLU                                              
SEQRES   1 G  290  MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 G  290  SER GLY GLU ASN LEU TYR PHE GLN GLY HIS MET VAL ASN          
SEQRES   3 G  290  LEU MET ASN ILE LYS ASP ILE LYS LEU ASN ALA ASP GLU          
SEQRES   4 G  290  THR LYS THR THR LYS ALA ILE LEU LYS ALA SER PHE ASP          
SEQRES   5 G  290  MET TRP LEU ASP ILE VAL GLU ALA ASP VAL VAL ILE VAL          
SEQRES   6 G  290  GLY ALA GLY PRO SER GLY LEU THR CYS ALA ARG TYR LEU          
SEQRES   7 G  290  ALA LYS GLU GLY PHE LYS VAL VAL VAL LEU GLU ARG HIS          
SEQRES   8 G  290  LEU ALA PHE GLY GLY GLY THR TRP GLY GLY GLY MET GLY          
SEQRES   9 G  290  PHE PRO TYR ILE VAL VAL GLU GLU PRO ALA ASP GLU LEU          
SEQRES  10 G  290  LEU ARG GLU VAL GLY ILE LYS LEU ILE ASP MET GLY ASP          
SEQRES  11 G  290  GLY TYR TYR VAL ALA ASP SER VAL GLU VAL PRO ALA LYS          
SEQRES  12 G  290  LEU ALA VAL ALA ALA MET ASP ALA GLY ALA LYS ILE LEU          
SEQRES  13 G  290  THR GLY ILE VAL VAL GLU ASP LEU ILE LEU ARG GLU ASP          
SEQRES  14 G  290  GLY VAL ALA GLY VAL VAL ILE ASN SER TYR ALA ILE GLU          
SEQRES  15 G  290  ARG ALA GLY LEU HIS ILE ASP PRO LEU THR ILE ARG SER          
SEQRES  16 G  290  LYS VAL VAL VAL ASP ALA THR GLY HIS GLU ALA SER ILE          
SEQRES  17 G  290  VAL ASN ILE LEU VAL LYS LYS ASN LYS LEU GLU ALA ASP          
SEQRES  18 G  290  VAL PRO GLY GLU LYS SER MET TRP ALA GLU LYS GLY GLU          
SEQRES  19 G  290  ASN ALA LEU LEU ARG ASN THR ARG GLU VAL TYR PRO ASN          
SEQRES  20 G  290  LEU PHE VAL CYS GLY MET ALA ALA ASN ALA SER HIS GLY          
SEQRES  21 G  290  GLY TYR ARG MET GLY ALA ILE PHE GLY GLY MET TYR LEU          
SEQRES  22 G  290  SER GLY LYS LEU CYS ALA GLU LEU ILE THR GLU LYS LEU          
SEQRES  23 G  290  LYS ASN LYS GLU                                              
SEQRES   1 H  290  MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 H  290  SER GLY GLU ASN LEU TYR PHE GLN GLY HIS MET VAL ASN          
SEQRES   3 H  290  LEU MET ASN ILE LYS ASP ILE LYS LEU ASN ALA ASP GLU          
SEQRES   4 H  290  THR LYS THR THR LYS ALA ILE LEU LYS ALA SER PHE ASP          
SEQRES   5 H  290  MET TRP LEU ASP ILE VAL GLU ALA ASP VAL VAL ILE VAL          
SEQRES   6 H  290  GLY ALA GLY PRO SER GLY LEU THR CYS ALA ARG TYR LEU          
SEQRES   7 H  290  ALA LYS GLU GLY PHE LYS VAL VAL VAL LEU GLU ARG HIS          
SEQRES   8 H  290  LEU ALA PHE GLY GLY GLY THR TRP GLY GLY GLY MET GLY          
SEQRES   9 H  290  PHE PRO TYR ILE VAL VAL GLU GLU PRO ALA ASP GLU LEU          
SEQRES  10 H  290  LEU ARG GLU VAL GLY ILE LYS LEU ILE ASP MET GLY ASP          
SEQRES  11 H  290  GLY TYR TYR VAL ALA ASP SER VAL GLU VAL PRO ALA LYS          
SEQRES  12 H  290  LEU ALA VAL ALA ALA MET ASP ALA GLY ALA LYS ILE LEU          
SEQRES  13 H  290  THR GLY ILE VAL VAL GLU ASP LEU ILE LEU ARG GLU ASP          
SEQRES  14 H  290  GLY VAL ALA GLY VAL VAL ILE ASN SER TYR ALA ILE GLU          
SEQRES  15 H  290  ARG ALA GLY LEU HIS ILE ASP PRO LEU THR ILE ARG SER          
SEQRES  16 H  290  LYS VAL VAL VAL ASP ALA THR GLY HIS GLU ALA SER ILE          
SEQRES  17 H  290  VAL ASN ILE LEU VAL LYS LYS ASN LYS LEU GLU ALA ASP          
SEQRES  18 H  290  VAL PRO GLY GLU LYS SER MET TRP ALA GLU LYS GLY GLU          
SEQRES  19 H  290  ASN ALA LEU LEU ARG ASN THR ARG GLU VAL TYR PRO ASN          
SEQRES  20 H  290  LEU PHE VAL CYS GLY MET ALA ALA ASN ALA SER HIS GLY          
SEQRES  21 H  290  GLY TYR ARG MET GLY ALA ILE PHE GLY GLY MET TYR LEU          
SEQRES  22 H  290  SER GLY LYS LEU CYS ALA GLU LEU ILE THR GLU LYS LEU          
SEQRES  23 H  290  LYS ASN LYS GLU                                              
HET    48F  A 301      36                                                       
HET    NHE  A 302      13                                                       
HET    48F  B 301      36                                                       
HET    48F  C 301      36                                                       
HET    NHE  C 302      13                                                       
HET    48F  D 301      36                                                       
HET    48F  E 301      36                                                       
HET    48F  F 301      36                                                       
HET    NHE  F 302      13                                                       
HET    48F  G 301      36                                                       
HET    NHE  G 302      13                                                       
HET    48F  H 301      36                                                       
HET    NHE  H 302      13                                                       
HETNAM     48F [[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-                       
HETNAM   2 48F  BIS(OXIDANYL)OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]           
HETNAM   3 48F  [(2R,3R)-2,3,5-TRIS(OXIDANYL)-4-OXIDANYLIDENE-PENTYL]           
HETNAM   4 48F  HYDROGEN PHOSPHATE                                              
HETNAM     NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID                        
HETSYN     NHE N-CYCLOHEXYLTAURINE; CHES                                        
FORMUL   9  48F    8(C15 H23 N5 O14 P2)                                         
FORMUL  10  NHE    5(C8 H17 N O3 S)                                             
FORMUL  22  HOH   *21(H2 O)                                                     
HELIX    1 AA1 ASP A   15  VAL A   35  1                                  21    
HELIX    2 AA2 GLY A   45  GLU A   58  1                                  14    
HELIX    3 AA3 ASP A   92  GLU A   97  1                                   6    
HELIX    4 AA4 VAL A  115  ALA A  128  1                                  14    
HELIX    5 AA5 TYR A  156  GLY A  162  1                                   7    
HELIX    6 AA6 THR A  179  GLU A  182  5                                   4    
HELIX    7 AA7 ALA A  183  ASN A  193  1                                  11    
HELIX    8 AA8 TRP A  206  THR A  218  1                                  13    
HELIX    9 AA9 GLY A  229  HIS A  236  1                                   8    
HELIX   10 AB1 PHE A  245  LYS A  264  1                                  20    
HELIX   11 AB2 ASP B   15  VAL B   35  1                                  21    
HELIX   12 AB3 GLY B   45  GLU B   58  1                                  14    
HELIX   13 AB4 ASP B   92  GLU B   97  1                                   6    
HELIX   14 AB5 VAL B  115  ALA B  128  1                                  14    
HELIX   15 AB6 TYR B  156  GLY B  162  1                                   7    
HELIX   16 AB7 THR B  179  GLU B  182  5                                   4    
HELIX   17 AB8 ALA B  183  ASN B  193  1                                  11    
HELIX   18 AB9 TRP B  206  THR B  218  1                                  13    
HELIX   19 AC1 GLY B  229  GLY B  237  1                                   9    
HELIX   20 AC2 PHE B  245  LYS B  264  1                                  20    
HELIX   21 AC3 ASP C   15  VAL C   35  1                                  21    
HELIX   22 AC4 GLY C   45  GLU C   58  1                                  14    
HELIX   23 AC5 ASP C   92  GLU C   97  1                                   6    
HELIX   24 AC6 VAL C  115  ALA C  128  1                                  14    
HELIX   25 AC7 TYR C  156  GLY C  162  1                                   7    
HELIX   26 AC8 THR C  179  GLU C  182  5                                   4    
HELIX   27 AC9 ALA C  183  ASN C  193  1                                  11    
HELIX   28 AD1 TRP C  206  THR C  218  1                                  13    
HELIX   29 AD2 GLY C  229  HIS C  236  1                                   8    
HELIX   30 AD3 PHE C  245  LYS C  264  1                                  20    
HELIX   31 AD4 ASP D   15  VAL D   35  1                                  21    
HELIX   32 AD5 GLY D   45  GLU D   58  1                                  14    
HELIX   33 AD6 ALA D   91  GLU D   97  1                                   7    
HELIX   34 AD7 VAL D  115  ALA D  128  1                                  14    
HELIX   35 AD8 TYR D  156  GLY D  162  1                                   7    
HELIX   36 AD9 THR D  179  GLU D  182  5                                   4    
HELIX   37 AE1 ALA D  183  ASN D  193  1                                  11    
HELIX   38 AE2 TRP D  206  THR D  218  1                                  13    
HELIX   39 AE3 GLY D  229  HIS D  236  1                                   8    
HELIX   40 AE4 PHE D  245  LYS D  264  1                                  20    
HELIX   41 AE5 ASP E   15  VAL E   35  1                                  21    
HELIX   42 AE6 GLY E   45  GLU E   58  1                                  14    
HELIX   43 AE7 ASP E   92  GLU E   97  1                                   6    
HELIX   44 AE8 VAL E  115  ALA E  128  1                                  14    
HELIX   45 AE9 TYR E  156  GLY E  162  1                                   7    
HELIX   46 AF1 THR E  179  GLU E  182  5                                   4    
HELIX   47 AF2 ALA E  183  ASN E  193  1                                  11    
HELIX   48 AF3 TRP E  206  THR E  218  1                                  13    
HELIX   49 AF4 GLY E  229  HIS E  236  1                                   8    
HELIX   50 AF5 PHE E  245  LYS E  264  1                                  20    
HELIX   51 AF6 ASN F    6  ILE F   10  5                                   5    
HELIX   52 AF7 ASP F   15  VAL F   35  1                                  21    
HELIX   53 AF8 GLY F   45  GLU F   58  1                                  14    
HELIX   54 AF9 ASP F   92  GLU F   97  1                                   6    
HELIX   55 AG1 VAL F  115  ALA F  128  1                                  14    
HELIX   56 AG2 TYR F  156  GLY F  162  1                                   7    
HELIX   57 AG3 THR F  179  GLU F  182  5                                   4    
HELIX   58 AG4 ALA F  183  ASN F  193  1                                  11    
HELIX   59 AG5 TRP F  206  THR F  218  1                                  13    
HELIX   60 AG6 GLY F  229  HIS F  236  1                                   8    
HELIX   61 AG7 PHE F  245  LYS F  264  1                                  20    
HELIX   62 AG8 ASN G    6  ILE G   10  5                                   5    
HELIX   63 AG9 ASP G   15  VAL G   35  1                                  21    
HELIX   64 AH1 GLY G   45  GLU G   58  1                                  14    
HELIX   65 AH2 ASP G   92  GLU G   97  1                                   6    
HELIX   66 AH3 VAL G  115  ALA G  128  1                                  14    
HELIX   67 AH4 TYR G  156  GLY G  162  1                                   7    
HELIX   68 AH5 THR G  179  GLU G  182  5                                   4    
HELIX   69 AH6 ALA G  183  ASN G  193  1                                  11    
HELIX   70 AH7 TRP G  206  THR G  218  1                                  13    
HELIX   71 AH8 GLY G  229  HIS G  236  1                                   8    
HELIX   72 AH9 PHE G  245  LYS G  264  1                                  20    
HELIX   73 AI1 ASN H    6  ILE H   10  5                                   5    
HELIX   74 AI2 ASP H   15  VAL H   35  1                                  21    
HELIX   75 AI3 GLY H   45  GLU H   58  1                                  14    
HELIX   76 AI4 ASP H   92  GLU H   97  1                                   6    
HELIX   77 AI5 VAL H  115  ALA H  128  1                                  14    
HELIX   78 AI6 TYR H  156  GLY H  162  1                                   7    
HELIX   79 AI7 THR H  179  GLU H  182  5                                   4    
HELIX   80 AI8 ALA H  183  ASN H  193  1                                  11    
HELIX   81 AI9 TRP H  206  THR H  218  1                                  13    
HELIX   82 AJ1 GLY H  229  HIS H  236  1                                   8    
HELIX   83 AJ2 PHE H  245  LYS H  264  1                                  20    
SHEET    1 AA1 6 LYS A 131  THR A 134  0                                        
SHEET    2 AA1 6 VAL A  62  GLU A  66  1  N  VAL A  64   O  LEU A 133           
SHEET    3 AA1 6 GLU A  36  VAL A  42  1  N  ILE A  41   O  VAL A  63           
SHEET    4 AA1 6 LEU A 168  ASP A 177  1  O  VAL A 176   N  VAL A  42           
SHEET    5 AA1 6 GLY A 147  SER A 155 -1  N  VAL A 151   O  ILE A 170           
SHEET    6 AA1 6 ILE A 136  ARG A 144 -1  N  ILE A 142   O  ALA A 149           
SHEET    1 AA2 6 LYS A 131  THR A 134  0                                        
SHEET    2 AA2 6 VAL A  62  GLU A  66  1  N  VAL A  64   O  LEU A 133           
SHEET    3 AA2 6 GLU A  36  VAL A  42  1  N  ILE A  41   O  VAL A  63           
SHEET    4 AA2 6 LEU A 168  ASP A 177  1  O  VAL A 176   N  VAL A  42           
SHEET    5 AA2 6 LEU A 225  VAL A 227  1  O  PHE A 226   N  ASP A 177           
SHEET    6 AA2 6 GLU A 220  TYR A 222 -1  N  TYR A 222   O  LEU A 225           
SHEET    1 AA3 3 TYR A  84  GLU A  88  0                                        
SHEET    2 AA3 3 TYR A 109  ASP A 113 -1  O  TYR A 110   N  VAL A  87           
SHEET    3 AA3 3 ILE A 103  GLY A 106 -1  N  MET A 105   O  TYR A 109           
SHEET    1 AA4 6 LYS B 131  LEU B 133  0                                        
SHEET    2 AA4 6 VAL B  62  LEU B  65  1  N  VAL B  64   O  LYS B 131           
SHEET    3 AA4 6 GLU B  36  VAL B  42  1  N  ILE B  41   O  VAL B  63           
SHEET    4 AA4 6 LEU B 168  ASP B 177  1  O  VAL B 176   N  VAL B  42           
SHEET    5 AA4 6 GLY B 147  SER B 155 -1  N  ILE B 153   O  LEU B 168           
SHEET    6 AA4 6 ILE B 136  ARG B 144 -1  N  ILE B 142   O  ALA B 149           
SHEET    1 AA5 6 LYS B 131  LEU B 133  0                                        
SHEET    2 AA5 6 VAL B  62  LEU B  65  1  N  VAL B  64   O  LYS B 131           
SHEET    3 AA5 6 GLU B  36  VAL B  42  1  N  ILE B  41   O  VAL B  63           
SHEET    4 AA5 6 LEU B 168  ASP B 177  1  O  VAL B 176   N  VAL B  42           
SHEET    5 AA5 6 LEU B 225  VAL B 227  1  O  PHE B 226   N  ASP B 177           
SHEET    6 AA5 6 GLU B 220  TYR B 222 -1  N  TYR B 222   O  LEU B 225           
SHEET    1 AA6 3 TYR B  84  GLU B  88  0                                        
SHEET    2 AA6 3 TYR B 109  ASP B 113 -1  O  TYR B 110   N  VAL B  87           
SHEET    3 AA6 3 ILE B 103  GLY B 106 -1  N  MET B 105   O  TYR B 109           
SHEET    1 AA7 6 LYS C 131  THR C 134  0                                        
SHEET    2 AA7 6 VAL C  62  GLU C  66  1  N  VAL C  64   O  LEU C 133           
SHEET    3 AA7 6 GLU C  36  VAL C  42  1  N  ILE C  41   O  VAL C  63           
SHEET    4 AA7 6 LEU C 168  ASP C 177  1  O  VAL C 176   N  VAL C  42           
SHEET    5 AA7 6 GLY C 147  SER C 155 -1  N  ILE C 153   O  LEU C 168           
SHEET    6 AA7 6 ILE C 136  ARG C 144 -1  N  ILE C 142   O  ALA C 149           
SHEET    1 AA8 6 LYS C 131  THR C 134  0                                        
SHEET    2 AA8 6 VAL C  62  GLU C  66  1  N  VAL C  64   O  LEU C 133           
SHEET    3 AA8 6 GLU C  36  VAL C  42  1  N  ILE C  41   O  VAL C  63           
SHEET    4 AA8 6 LEU C 168  ASP C 177  1  O  VAL C 176   N  VAL C  42           
SHEET    5 AA8 6 LEU C 225  VAL C 227  1  O  PHE C 226   N  ASP C 177           
SHEET    6 AA8 6 GLU C 220  TYR C 222 -1  N  TYR C 222   O  LEU C 225           
SHEET    1 AA9 3 TYR C  84  GLU C  88  0                                        
SHEET    2 AA9 3 TYR C 109  ASP C 113 -1  O  TYR C 110   N  VAL C  87           
SHEET    3 AA9 3 ILE C 103  GLY C 106 -1  N  MET C 105   O  TYR C 109           
SHEET    1 AB1 6 LYS D 131  THR D 134  0                                        
SHEET    2 AB1 6 VAL D  62  GLU D  66  1  N  VAL D  64   O  LEU D 133           
SHEET    3 AB1 6 GLU D  36  VAL D  42  1  N  ILE D  41   O  VAL D  63           
SHEET    4 AB1 6 LEU D 168  ASP D 177  1  O  VAL D 176   N  VAL D  42           
SHEET    5 AB1 6 GLY D 147  SER D 155 -1  N  VAL D 151   O  ILE D 170           
SHEET    6 AB1 6 ILE D 136  ARG D 144 -1  N  VAL D 137   O  ASN D 154           
SHEET    1 AB2 6 LYS D 131  THR D 134  0                                        
SHEET    2 AB2 6 VAL D  62  GLU D  66  1  N  VAL D  64   O  LEU D 133           
SHEET    3 AB2 6 GLU D  36  VAL D  42  1  N  ILE D  41   O  VAL D  63           
SHEET    4 AB2 6 LEU D 168  ASP D 177  1  O  VAL D 176   N  VAL D  42           
SHEET    5 AB2 6 LEU D 225  VAL D 227  1  O  PHE D 226   N  ASP D 177           
SHEET    6 AB2 6 GLU D 220  TYR D 222 -1  N  TYR D 222   O  LEU D 225           
SHEET    1 AB3 3 TYR D  84  GLU D  88  0                                        
SHEET    2 AB3 3 TYR D 109  ASP D 113 -1  O  TYR D 110   N  VAL D  87           
SHEET    3 AB3 3 ILE D 103  GLY D 106 -1  N  MET D 105   O  TYR D 109           
SHEET    1 AB4 6 LYS E 131  THR E 134  0                                        
SHEET    2 AB4 6 VAL E  62  GLU E  66  1  N  VAL E  64   O  LYS E 131           
SHEET    3 AB4 6 GLU E  36  VAL E  42  1  N  ILE E  41   O  VAL E  63           
SHEET    4 AB4 6 LEU E 168  ASP E 177  1  O  VAL E 176   N  VAL E  42           
SHEET    5 AB4 6 GLY E 147  SER E 155 -1  N  ILE E 153   O  LEU E 168           
SHEET    6 AB4 6 ILE E 136  ARG E 144 -1  N  ILE E 142   O  ALA E 149           
SHEET    1 AB5 6 LYS E 131  THR E 134  0                                        
SHEET    2 AB5 6 VAL E  62  GLU E  66  1  N  VAL E  64   O  LYS E 131           
SHEET    3 AB5 6 GLU E  36  VAL E  42  1  N  ILE E  41   O  VAL E  63           
SHEET    4 AB5 6 LEU E 168  ASP E 177  1  O  VAL E 176   N  VAL E  42           
SHEET    5 AB5 6 LEU E 225  VAL E 227  1  O  PHE E 226   N  ASP E 177           
SHEET    6 AB5 6 GLU E 220  TYR E 222 -1  N  TYR E 222   O  LEU E 225           
SHEET    1 AB6 3 TYR E  84  GLU E  88  0                                        
SHEET    2 AB6 3 TYR E 109  ASP E 113 -1  O  TYR E 110   N  VAL E  87           
SHEET    3 AB6 3 ILE E 103  GLY E 106 -1  N  MET E 105   O  TYR E 109           
SHEET    1 AB7 6 LYS F 131  THR F 134  0                                        
SHEET    2 AB7 6 VAL F  62  GLU F  66  1  N  VAL F  64   O  LYS F 131           
SHEET    3 AB7 6 GLU F  36  VAL F  42  1  N  ILE F  41   O  VAL F  63           
SHEET    4 AB7 6 LEU F 168  ASP F 177  1  O  VAL F 176   N  VAL F  42           
SHEET    5 AB7 6 GLY F 147  SER F 155 -1  N  VAL F 151   O  ILE F 170           
SHEET    6 AB7 6 ILE F 136  ARG F 144 -1  N  ILE F 142   O  ALA F 149           
SHEET    1 AB8 6 LYS F 131  THR F 134  0                                        
SHEET    2 AB8 6 VAL F  62  GLU F  66  1  N  VAL F  64   O  LYS F 131           
SHEET    3 AB8 6 GLU F  36  VAL F  42  1  N  ILE F  41   O  VAL F  63           
SHEET    4 AB8 6 LEU F 168  ASP F 177  1  O  VAL F 176   N  VAL F  42           
SHEET    5 AB8 6 LEU F 225  VAL F 227  1  O  PHE F 226   N  ASP F 177           
SHEET    6 AB8 6 GLU F 220  TYR F 222 -1  N  TYR F 222   O  LEU F 225           
SHEET    1 AB9 3 TYR F  84  GLU F  88  0                                        
SHEET    2 AB9 3 TYR F 109  ASP F 113 -1  O  TYR F 110   N  VAL F  87           
SHEET    3 AB9 3 ILE F 103  GLY F 106 -1  N  MET F 105   O  TYR F 109           
SHEET    1 AC1 6 LYS G 131  THR G 134  0                                        
SHEET    2 AC1 6 VAL G  62  GLU G  66  1  N  VAL G  64   O  LYS G 131           
SHEET    3 AC1 6 GLU G  36  VAL G  42  1  N  ILE G  41   O  VAL G  63           
SHEET    4 AC1 6 LEU G 168  ASP G 177  1  O  VAL G 176   N  VAL G  42           
SHEET    5 AC1 6 GLY G 147  SER G 155 -1  N  ILE G 153   O  LEU G 168           
SHEET    6 AC1 6 ILE G 136  ARG G 144 -1  N  ILE G 142   O  ALA G 149           
SHEET    1 AC2 6 LYS G 131  THR G 134  0                                        
SHEET    2 AC2 6 VAL G  62  GLU G  66  1  N  VAL G  64   O  LYS G 131           
SHEET    3 AC2 6 GLU G  36  VAL G  42  1  N  ILE G  41   O  VAL G  63           
SHEET    4 AC2 6 LEU G 168  ASP G 177  1  O  VAL G 176   N  VAL G  42           
SHEET    5 AC2 6 LEU G 225  VAL G 227  1  O  PHE G 226   N  ASP G 177           
SHEET    6 AC2 6 GLU G 220  TYR G 222 -1  N  TYR G 222   O  LEU G 225           
SHEET    1 AC3 3 TYR G  84  GLU G  88  0                                        
SHEET    2 AC3 3 TYR G 109  ASP G 113 -1  O  TYR G 110   N  VAL G  87           
SHEET    3 AC3 3 ILE G 103  GLY G 106 -1  N  MET G 105   O  TYR G 109           
SHEET    1 AC4 6 LYS H 131  THR H 134  0                                        
SHEET    2 AC4 6 VAL H  62  GLU H  66  1  N  VAL H  64   O  LYS H 131           
SHEET    3 AC4 6 GLU H  36  VAL H  42  1  N  ILE H  41   O  VAL H  63           
SHEET    4 AC4 6 LEU H 168  ASP H 177  1  O  VAL H 176   N  VAL H  42           
SHEET    5 AC4 6 GLY H 147  SER H 155 -1  N  VAL H 151   O  ILE H 170           
SHEET    6 AC4 6 ILE H 136  ARG H 144 -1  N  ILE H 142   O  ALA H 149           
SHEET    1 AC5 6 LYS H 131  THR H 134  0                                        
SHEET    2 AC5 6 VAL H  62  GLU H  66  1  N  VAL H  64   O  LYS H 131           
SHEET    3 AC5 6 GLU H  36  VAL H  42  1  N  ILE H  41   O  VAL H  63           
SHEET    4 AC5 6 LEU H 168  ASP H 177  1  O  VAL H 176   N  VAL H  42           
SHEET    5 AC5 6 LEU H 225  VAL H 227  1  O  PHE H 226   N  ASP H 177           
SHEET    6 AC5 6 GLU H 220  TYR H 222 -1  N  TYR H 222   O  LEU H 225           
SHEET    1 AC6 3 TYR H  84  GLU H  88  0                                        
SHEET    2 AC6 3 TYR H 109  ASP H 113 -1  O  TYR H 110   N  VAL H  87           
SHEET    3 AC6 3 ILE H 103  GLY H 106 -1  N  MET H 105   O  TYR H 109           
CISPEP   1 GLU A   89    PRO A   90          0        -0.40                     
CISPEP   2 GLU B   89    PRO B   90          0         0.25                     
CISPEP   3 GLU C   89    PRO C   90          0         0.40                     
CISPEP   4 GLU D   89    PRO D   90          0         1.02                     
CISPEP   5 GLU E   89    PRO E   90          0         0.46                     
CISPEP   6 GLU F   89    PRO F   90          0        -0.97                     
CISPEP   7 GLU G   89    PRO G   90          0        -0.56                     
CISPEP   8 GLU H   89    PRO H   90          0         1.23                     
SITE     1 AC1 23 VAL A  42  GLY A  43  GLY A  45  PRO A  46                    
SITE     2 AC1 23 SER A  47  GLU A  66  ARG A  67  HIS A  68                    
SITE     3 AC1 23 GLY A  73  GLY A  74  ILE A 136  VAL A 138                    
SITE     4 AC1 23 ALA A 178  THR A 179  GLY A 180  SER A 184                    
SITE     5 AC1 23 GLY A 229  MET A 230  GLY A 242  PHE A 245                    
SITE     6 AC1 23 MET A 248  HIS D 164  ASP D 166                               
SITE     1 AC2  6 ASP A 198  PRO A 200  VAL A 221  SER A 235                    
SITE     2 AC2  6 HIS A 236  GLU C 196                                          
SITE     1 AC3 23 VAL B  42  GLY B  43  GLY B  45  PRO B  46                    
SITE     2 AC3 23 SER B  47  GLU B  66  ARG B  67  HIS B  68                    
SITE     3 AC3 23 GLY B  73  GLY B  74  ILE B 136  VAL B 137                    
SITE     4 AC3 23 VAL B 138  ALA B 178  THR B 179  GLY B 180                    
SITE     5 AC3 23 SER B 184  GLY B 229  MET B 230  GLY B 242                    
SITE     6 AC3 23 MET B 248  HIS F 164  ASP F 166                               
SITE     1 AC4 23 HIS B 164  ASP B 166  VAL C  42  GLY C  43                    
SITE     2 AC4 23 GLY C  45  PRO C  46  SER C  47  GLU C  66                    
SITE     3 AC4 23 ARG C  67  HIS C  68  GLY C  73  GLY C  74                    
SITE     4 AC4 23 ILE C 136  VAL C 138  ALA C 178  THR C 179                    
SITE     5 AC4 23 GLY C 180  SER C 184  GLY C 229  MET C 230                    
SITE     6 AC4 23 GLY C 242  PHE C 245  MET C 248                               
SITE     1 AC5  4 ALA C 197  ASP C 198  SER C 235  HIS C 236                    
SITE     1 AC6 22 VAL D  42  GLY D  43  GLY D  45  PRO D  46                    
SITE     2 AC6 22 SER D  47  GLU D  66  ARG D  67  HIS D  68                    
SITE     3 AC6 22 GLY D  73  GLY D  74  ILE D 136  VAL D 138                    
SITE     4 AC6 22 ALA D 178  THR D 179  GLY D 180  SER D 184                    
SITE     5 AC6 22 GLY D 229  MET D 230  GLY D 242  MET D 248                    
SITE     6 AC6 22 HIS E 164  ASP E 166                                          
SITE     1 AC7 23 VAL E  42  GLY E  43  GLY E  45  PRO E  46                    
SITE     2 AC7 23 SER E  47  GLU E  66  ARG E  67  HIS E  68                    
SITE     3 AC7 23 GLY E  73  GLY E  74  ILE E 136  VAL E 138                    
SITE     4 AC7 23 ALA E 178  THR E 179  GLY E 180  SER E 184                    
SITE     5 AC7 23 GLY E 229  MET E 230  MET E 241  GLY E 242                    
SITE     6 AC7 23 MET E 248  HIS G 164  ASP G 166                               
SITE     1 AC8 25 VAL F  42  GLY F  43  GLY F  45  PRO F  46                    
SITE     2 AC8 25 SER F  47  GLU F  66  ARG F  67  HIS F  68                    
SITE     3 AC8 25 GLY F  73  GLY F  74  ILE F 136  VAL F 138                    
SITE     4 AC8 25 ALA F 178  THR F 179  GLY F 180  SER F 184                    
SITE     5 AC8 25 GLY F 229  MET F 230  GLY F 242  PHE F 245                    
SITE     6 AC8 25 MET F 248  HOH F 401  HOH F 402  HIS H 164                    
SITE     7 AC8 25 ASP H 166                                                     
SITE     1 AC9  4 ALA F 197  ASP F 198  SER F 235  GLU G 196                    
SITE     1 AD1 25 HIS A 164  ASP A 166  VAL G  42  GLY G  43                    
SITE     2 AD1 25 GLY G  45  PRO G  46  SER G  47  GLU G  66                    
SITE     3 AD1 25 ARG G  67  HIS G  68  GLY G  73  GLY G  74                    
SITE     4 AD1 25 ILE G 136  VAL G 138  ALA G 178  THR G 179                    
SITE     5 AD1 25 GLY G 180  SER G 184  GLY G 229  MET G 230                    
SITE     6 AD1 25 GLY G 242  PHE G 245  MET G 248  HOH G 401                    
SITE     7 AD1 25 HOH G 402                                                     
SITE     1 AD2  6 GLU F 196  ALA G 197  ASP G 198  PRO G 200                    
SITE     2 AD2  6 SER G 235  HIS G 236                                          
SITE     1 AD3 24 HIS C 164  ASP C 166  VAL H  42  GLY H  43                    
SITE     2 AD3 24 GLY H  45  PRO H  46  SER H  47  GLU H  66                    
SITE     3 AD3 24 ARG H  67  HIS H  68  GLY H  73  GLY H  74                    
SITE     4 AD3 24 ILE H 136  VAL H 137  VAL H 138  ALA H 178                    
SITE     5 AD3 24 THR H 179  GLY H 180  SER H 184  GLY H 229                    
SITE     6 AD3 24 MET H 230  GLY H 242  PHE H 245  MET H 248                    
SITE     1 AD4  7 GLU D 196  ALA H 197  ASP H 198  PRO H 200                    
SITE     2 AD4  7 VAL H 221  SER H 235  HIS H 236                               
CRYST1  180.760  180.760   73.328  90.00  90.00 120.00 P 32         24          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005532  0.003194  0.000000        0.00000                         
SCALE2      0.000000  0.006388  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013637        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2  0.453442 -0.839324  0.299876       10.01166    1                    
MTRIX2   2 -0.838538 -0.515764 -0.175620        2.73902    1                    
MTRIX3   2  0.302067 -0.171824 -0.937674      -40.71800    1                    
MTRIX1   3  0.834989  0.494301  0.241784       21.73484    1                    
MTRIX2   3  0.493803 -0.866980  0.067120      -64.55105    1                    
MTRIX3   3  0.242800  0.063349 -0.968006      -33.15097    1                    
MTRIX1   4  0.011075  0.970249 -0.241856       65.69120    1                    
MTRIX2   4 -0.997698 -0.005461 -0.067594       23.73042    1                    
MTRIX3   4 -0.066903  0.242048  0.967955        8.29738    1                    
MTRIX1   5 -0.953241 -0.025878 -0.301100       87.74722    1                    
MTRIX2   5 -0.028675 -0.984087  0.175360      -41.97642    1                    
MTRIX3   5 -0.300846  0.175794  0.937330       17.66459    1                    
MTRIX1   6 -0.880500 -0.470580  0.057222       78.18453    1                    
MTRIX2   6 -0.469581  0.849297 -0.241223       16.24388    1                    
MTRIX3   6  0.064916 -0.239267 -0.968781      -31.66574    1                    
MTRIX1   7  0.032760 -0.997810 -0.057456       21.80578    1                    
MTRIX2   7  0.970227  0.017947  0.241531      -64.80766    1                    
MTRIX3   7 -0.239972 -0.063658  0.968691        9.51802    1                    
MTRIX1   8 -0.499293  0.866433  0.000071       90.33633    1                    
MTRIX2   8  0.866433  0.499292  0.000958      -52.17899    1                    
MTRIX3   8  0.000795  0.000540 -1.000000      -23.58238    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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