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Database: PDB
Entry: 1FXO
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Original site: 1FXO 
HEADER    TRANSFERASE                             26-SEP-00   1FXO              
TITLE     THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND                   
TITLE    2 REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE              
TITLE    3 (RMLA). TMP COMPLEX.                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE;                 
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA);           
COMPND   5 EC: 2.7.7.24;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 287;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET23A(+)                                 
KEYWDS    RHAMNOSE, NUCLEOTIDYLTRANSFERASE, PYROPHOSPHORYLASE,                  
KEYWDS   2 THYMIDYLYLTRANSFERASE, ALLOSTERY                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.BLANKENFELDT,J.S.LAM,J.H.NAISMITH                                   
REVDAT   3   24-FEB-09 1FXO    1       VERSN                                    
REVDAT   2   01-APR-03 1FXO    1       JRNL                                     
REVDAT   1   27-DEC-00 1FXO    0                                                
JRNL        AUTH   W.BLANKENFELDT,M.ASUNCION,J.S.LAM,J.H.NAISMITH               
JRNL        TITL   THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM              
JRNL        TITL 2 AND REGULATION OF GLUCOSE-1-PHOSPHATE                        
JRNL        TITL 3 THYMIDYLYLTRANSFERASE (RMLA).                                
JRNL        REF    EMBO J.                       V.  19  6652 2000              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   11118200                                                     
JRNL        DOI    10.1093/EMBOJ/19.24.6652                                     
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   W.BLANKENFELDT,M.F.GIRAUD,G.LEONARD,R.RAHIM,                 
REMARK   1  AUTH 2 J.S.LAM,J.H.NAISMITH                                         
REMARK   1  TITL   THE PURIFICATION, CRYSTALLISATION AND PRELIMINARY            
REMARK   1  TITL 2 STRUCTURAL CHARACTERISATION OF GLUCOSE-1-PHOSPHATE           
REMARK   1  TITL 3 THYMIDYLYLTRANSFERASE (RMLA), THE FIRST ENZYME OF            
REMARK   1  TITL 4 THE DTDP-L-RHAMNOSE SYNTHESIS PATHWAY FROM                   
REMARK   1  TITL 5 PSEUDOMONAS AERUGINOSA                                       
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.MELO,L.GLASER                                              
REMARK   1  TITL   THE NUCLEOTIDE SPECIFICITY AND FEEDBACK CONTROL OF           
REMARK   1  TITL 2 THYMIDINE DIPHOSPHATE D-GLUCOSE PYROPHOSPHORYLASE            
REMARK   1  REF    J.BIOL.CHEM.                  V. 240   398 1965              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.66 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 73.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 281394                         
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) : 0.145                           
REMARK   3   R VALUE            (WORKING SET) : 0.142                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 14902                           
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 18858                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 548                                     
REMARK   3   SOLVENT ATOMS            : 3365                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.12000                                              
REMARK   3    B22 (A**2) : 0.09000                                              
REMARK   3    B33 (A**2) : -0.25000                                             
REMARK   3    B12 (A**2) : 0.04000                                              
REMARK   3    B13 (A**2) : 0.10000                                              
REMARK   3    B23 (A**2) : -0.01000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.688         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.128         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.093         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.396         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.016 ; 0.021               
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.009 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.129 ; 0.200               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.039 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.946 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 5.694 ; 3.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.874 ; 4.500                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: USED TLS-OPTION IN REFMAC5.               
REMARK   3  ANISOTROPIC B-FACTORS WERE CALCULATED BUT NOT REFINED (NCYCLE       
REMARK   3  0).                                                                 
REMARK   4                                                                      
REMARK   4 1FXO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011990.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 1141819                            
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.660                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.120                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.05300                            
REMARK 200  R SYM                      (I) : 0.05200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.33200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: PHASE EXTENSION IN DM        
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: MAD STRUCTURE (1G23)                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 % PEG 6000, 0.1 M SODIUM              
REMARK 280  CITRATE, 0.5 M LITHIUM SULFATE, 4 MICROLITRE PROTEIN, 4             
REMARK 280  MICROLITRE PRECIPITANT, 1 MICROLITRE 50 MM TMP, PH 4.6, VAPOR       
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 292K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER CONSISTING OF          
REMARK 300 CHAINS A,B,C AND D OR E,F,G AND H, RESPECTIVELY.                     
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 19240 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -159.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 19020 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -144.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 RmlA in complex with thymidine-5'-phosphate                          
REMARK 400 (TMP). TMP binds the active centre in two                            
REMARK 400 alternative conformations.                                           
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     MET C     1                                                      
REMARK 465     MET D     1                                                      
REMARK 465     MET H     1                                                      
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   OE1  GLN G   180     O    HOH G  9964              1.76            
REMARK 500   NE2  GLN F    78     O    HOH F  9901              1.78            
REMARK 500   O    HOH F  9709     O    HOH F  9893              1.83            
REMARK 500   O    HOH B  9745     O    HOH B  9844              1.85            
REMARK 500   O    HOH H  9790     O    HOH H  9839              1.88            
REMARK 500   O    HOH A  9574     O    HOH A  9906              1.90            
REMARK 500   O3   SO4 E  5700     O    HOH E  9813              1.90            
REMARK 500   OD1  ASP B   141     O    HOH B  9608              1.91            
REMARK 500   OG   SER C    71     O    HOH C  9894              1.91            
REMARK 500   O    HOH E  9542     O    HOH E  9787              1.91            
REMARK 500   O    HOH B  9690     O    HOH B  9974              1.93            
REMARK 500   O    HOH E  9757     O    HOH H  9688              1.93            
REMARK 500   O    HOH A  9927     O    HOH A  9931              1.93            
REMARK 500   OE1  GLU F   215     O    HOH F  9884              1.94            
REMARK 500   OG   SER F   124     O    HOH F  9883              1.94            
REMARK 500   O    HOH B  9987     O    HOH B  9988              1.94            
REMARK 500   O    HOH A  9658     O    HOH A  9833              1.94            
REMARK 500   O    HOH A  9672     O    HOH A  9765              1.94            
REMARK 500   O    HOH H  9680     O    HOH H  9773              1.94            
REMARK 500   O4   SO4 D  3900     O    HOH D  9713              1.95            
REMARK 500   O    HOH D  9746     O    HOH D  9829              1.96            
REMARK 500   O    HOH A  9608     O    HOH A  9642              1.96            
REMARK 500   O    HOH B  9594     O    HOH D  9710              1.96            
REMARK 500   O    HOH H  9870     O    HOH H  9874              1.97            
REMARK 500   O    HOH F  9828     O    HOH F  9854              1.97            
REMARK 500   OE1  GLN C    78     O    HOH C  9532              1.98            
REMARK 500   OG   SER D   124     O    HOH D  9834              1.98            
REMARK 500   O    HOH E  9705     O    HOH E  9820              1.98            
REMARK 500   O    HOH G  9740     O    HOH G  9753              1.99            
REMARK 500   O    HOH C  9657     O    HOH C  9729              1.99            
REMARK 500   O    HOH D  9630     O    HOH D  9880              1.99            
REMARK 500   O    HOH C  9596     O    HOH C  9709              1.99            
REMARK 500   O    HOH E  9782     O    HOH E  9784              1.99            
REMARK 500   O    HOH F  9656     O    HOH F  9803              2.00            
REMARK 500   O    HOH E  9716     O    HOH E  9837              2.00            
REMARK 500   O    HOH E  9692     O    HOH E  9776              2.00            
REMARK 500   OG   SER B    55     O    HOH B  9981              2.01            
REMARK 500   O    HOH D  9563     O    HOH D  9569              2.02            
REMARK 500   O    HOH F  9741     O    HOH F  9868              2.02            
REMARK 500   O    HOH E  9832     O    HOH E  9849              2.02            
REMARK 500   OD1  ASP G   141     O    HOH G  9634              2.02            
REMARK 500   O    HOH H  9660     O    HOH H  9761              2.02            
REMARK 500   O    HOH G  9912     O    HOH G  9916              2.03            
REMARK 500   O    HOH A  9855     O    HOH A  9946              2.03            
REMARK 500   O    HOH G  9626     O    HOH G  9808              2.03            
REMARK 500   O    HOH H  9806     O    HOH H  9850              2.04            
REMARK 500   O    HOH F  9629     O    HOH F  9842              2.04            
REMARK 500   O    HOH B  9711     O    HOH B  9737              2.04            
REMARK 500   O    HOH C  9625     O    HOH D  9594              2.04            
REMARK 500   O    HOH G  9776     O    HOH G  9888              2.05            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     142 CLOSE CONTACTS.                               
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH D  9860     O    HOH E  9857     1655     1.93            
REMARK 500   O    HOH D  9569     O    HOH H  9651     1565     2.01            
REMARK 500   O    HOH D  9563     O    HOH H  9651     1565     2.15            
REMARK 500   O    HOH A  9763     O    HOH F  9762     1566     2.15            
REMARK 500   O2   SO4 D  3900     O    HOH B  9956     1655     2.16            
REMARK 500   O    HOH F  9619     O    HOH G  9811     1455     2.17            
REMARK 500   O    HOH B  9978     O    HOH D  9669     1455     2.18            
REMARK 500   O    HOH D  9775     O    HOH H  9697     1565     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A 128   CZ    ARG A 128   NH2    -0.085                       
REMARK 500    TYR A 293   CE1   TYR A 293   CZ     -0.079                       
REMARK 500    TYR B  31   CE2   TYR B  31   CD2    -0.102                       
REMARK 500    PHE D 238   CZ    PHE D 238   CE2    -0.122                       
REMARK 500    TYR E 114   CE2   TYR E 114   CD2     0.099                       
REMARK 500    ARG G 128   CZ    ARG G 128   NH2    -0.098                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 259   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP B 141   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG B 194   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG B 194   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ASP D 110   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP D 141   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    SER F  12   N   -  CA  -  C   ANGL. DEV. = -18.9 DEGREES          
REMARK 500    ARG G 128   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG G 194   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG G 194   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP H 225   N   -  CA  -  CB  ANGL. DEV. = -11.4 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    TYR A  31      -78.76     66.48                                   
REMARK 500    ASP A 141       68.68   -119.80                                   
REMARK 500    THR A 226       34.51    -82.38                                   
REMARK 500    TYR B  31      -76.18     67.64                                   
REMARK 500    ASN B 101       45.78   -109.25                                   
REMARK 500    TYR C  31      -94.35     62.10                                   
REMARK 500    ARG C 194       -9.87    -55.22                                   
REMARK 500    THR C 226       35.17    -92.40                                   
REMARK 500    TYR D  31      -79.53     67.86                                   
REMARK 500    TYR E  31      -78.43     67.22                                   
REMARK 500    ARG E 194      -31.14    -29.57                                   
REMARK 500    THR E 226       31.74    -92.74                                   
REMARK 500    SER F  12      -58.20    131.69                                   
REMARK 500    TYR F  31      -84.12     69.30                                   
REMARK 500    TYR G  31      -79.20     66.94                                   
REMARK 500    PRO G 274        2.82    -69.18                                   
REMARK 500    TYR H  31      -93.05     65.96                                   
REMARK 500    THR H 226       35.75    -89.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    HIS A  17         0.09    SIDE_CHAIN                              
REMARK 500    HIS D  17         0.10    SIDE_CHAIN                              
REMARK 500    HIS D 119         0.09    SIDE_CHAIN                              
REMARK 500    HIS E  17         0.07    SIDE_CHAIN                              
REMARK 500    HIS E 229         0.09    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D9563        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH H9638        DISTANCE =  6.96 ANGSTROMS                       
REMARK 525    HOH G9682        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH C9727        DISTANCE =  5.76 ANGSTROMS                       
REMARK 525    HOH D9734        DISTANCE =  5.63 ANGSTROMS                       
REMARK 525    HOH H9748        DISTANCE =  7.74 ANGSTROMS                       
REMARK 525    HOH B9750        DISTANCE =  6.90 ANGSTROMS                       
REMARK 525    HOH D9767        DISTANCE =  5.39 ANGSTROMS                       
REMARK 525    HOH G9775        DISTANCE =  7.38 ANGSTROMS                       
REMARK 525    HOH H9781        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH C9779        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH E9786        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH F9789        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH C9791        DISTANCE =  7.01 ANGSTROMS                       
REMARK 525    HOH D9794        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH H9816        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH E9817        DISTANCE =  5.68 ANGSTROMS                       
REMARK 525    HOH A9821        DISTANCE =  6.42 ANGSTROMS                       
REMARK 525    HOH F9846        DISTANCE =  8.01 ANGSTROMS                       
REMARK 525    HOH F9848        DISTANCE =  9.68 ANGSTROMS                       
REMARK 525    HOH E9848        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH A9850        DISTANCE =  5.58 ANGSTROMS                       
REMARK 525    HOH D9856        DISTANCE =  6.46 ANGSTROMS                       
REMARK 525    HOH A9857        DISTANCE =  8.83 ANGSTROMS                       
REMARK 525    HOH B9862        DISTANCE =  6.46 ANGSTROMS                       
REMARK 525    HOH A9865        DISTANCE =  5.17 ANGSTROMS                       
REMARK 525    HOH F9875        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH E9876        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH H9879        DISTANCE =  6.03 ANGSTROMS                       
REMARK 525    HOH E9879        DISTANCE =  5.34 ANGSTROMS                       
REMARK 525    HOH C9882        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH C9883        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH H9890        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH A9902        DISTANCE =  6.39 ANGSTROMS                       
REMARK 525    HOH B9913        DISTANCE =  7.07 ANGSTROMS                       
REMARK 525    HOH G9920        DISTANCE =  6.97 ANGSTROMS                       
REMARK 525    HOH A9916        DISTANCE =  8.36 ANGSTROMS                       
REMARK 525    HOH H9928        DISTANCE =  5.68 ANGSTROMS                       
REMARK 525    HOH B9925        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH B9928        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH A9940        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH A9950        DISTANCE =  5.72 ANGSTROMS                       
REMARK 525    HOH G9963        DISTANCE =  6.51 ANGSTROMS                       
REMARK 525    HOH G9965        DISTANCE =  7.49 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3700                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 4700                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 3800                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3900                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 4000                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 4800                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 5000                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 5100                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 5200                
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 5700                
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 5800                
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 6700                
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 7700                
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP A 8500                
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP B 9500                
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP C 9501                
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP D 9502                
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP E 9503                
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP F 9504                
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP G 9505                
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP H 9506                
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP A 9507                
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP B 9508                
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP C 9509                
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP D 9510                
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP E 9511                
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP F 9512                
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP G 9513                
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP H 9514                
DBREF  1FXO A    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1FXO B    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1FXO C    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1FXO D    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1FXO E    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1FXO F    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1FXO G    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1FXO H    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
SEQRES   1 A  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 A  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 A  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 A  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 A  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 A  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 A  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 A  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 A  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 A  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 A  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 A  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 A  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 A  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 A  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 A  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 A  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 A  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 A  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 A  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 A  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 A  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 A  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 B  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 B  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 B  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 B  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 B  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 B  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 B  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 B  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 B  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 B  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 B  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 B  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 B  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 B  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 B  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 B  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 B  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 B  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 B  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 B  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 B  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 B  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 B  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 C  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 C  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 C  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 C  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 C  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 C  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 C  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 C  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 C  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 C  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 C  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 C  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 C  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 C  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 C  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 C  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 C  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 C  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 C  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 C  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 C  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 C  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 C  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 D  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 D  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 D  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 D  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 D  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 D  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 D  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 D  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 D  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 D  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 D  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 D  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 D  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 D  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 D  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 D  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 D  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 D  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 D  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 D  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 D  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 D  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 D  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 E  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 E  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 E  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 E  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 E  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 E  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 E  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 E  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 E  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 E  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 E  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 E  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 E  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 E  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 E  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 E  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 E  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 E  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 E  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 E  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 E  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 E  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 E  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 F  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 F  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 F  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 F  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 F  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 F  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 F  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 F  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 F  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 F  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 F  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 F  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 F  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 F  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 F  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 F  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 F  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 F  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 F  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 F  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 F  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 F  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 F  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 G  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 G  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 G  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 G  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 G  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 G  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 G  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 G  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 G  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 G  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 G  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 G  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 G  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 G  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 G  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 G  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 G  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 G  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 G  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 G  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 G  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 G  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 G  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 H  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 H  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 H  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 H  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 H  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 H  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 H  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 H  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 H  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 H  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 H  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 H  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 H  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 H  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 H  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 H  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 H  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 H  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 H  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 H  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 H  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 H  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 H  293  LEU LEU THR GLU THR VAL TYR                                  
HET    SO4  A3700       5                                                       
HET    SO4  E4700       5                                                       
HET    SO4  C3800       5                                                       
HET    SO4  D3900       5                                                       
HET    SO4  C4000       5                                                       
HET    SO4  D4800       5                                                       
HET    SO4  D5000       5                                                       
HET    SO4  D5100       5                                                       
HET    SO4  D5200       5                                                       
HET    SO4  E5700       5                                                       
HET    SO4  E5800       5                                                       
HET    SO4  F6700       5                                                       
HET    SO4  G7700       5                                                       
HET    TMP  A8500      42                                                       
HET    TMP  B9500      42                                                       
HET    TMP  C9501      42                                                       
HET    TMP  D9502      42                                                       
HET    TMP  E9503      21                                                       
HET    TMP  F9504      42                                                       
HET    TMP  G9505      42                                                       
HET    TMP  H9506      42                                                       
HET    TMP  A9507      21                                                       
HET    TMP  B9508      21                                                       
HET    TMP  C9509      21                                                       
HET    TMP  D9510      21                                                       
HET    TMP  E9511      21                                                       
HET    TMP  F9512      21                                                       
HET    TMP  G9513      21                                                       
HET    TMP  H9514      21                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     TMP THYMIDINE-5'-PHOSPHATE                                           
FORMUL   9  SO4    13(O4 S 2-)                                                  
FORMUL  22  TMP    16(C10 H15 N2 O8 P)                                          
FORMUL  38  HOH   *3365(H2 O)                                                   
HELIX    1   1 PRO A   18  ILE A   23  1                                   6    
HELIX    2   2 SER A   24  LEU A   27  5                                   4    
HELIX    3   3 ILE A   36  ALA A   46  1                                  11    
HELIX    4   4 ASP A   59  GLY A   68  1                                  10    
HELIX    5   5 GLY A   70  GLY A   74  5                                   5    
HELIX    6   6 GLY A   87  ALA A   89  5                                   3    
HELIX    7   7 GLN A   90  GLY A   95  1                                   6    
HELIX    8   8 GLY A   95  GLY A  100  1                                   6    
HELIX    9   9 ASP A  117  GLN A  127  1                                  11    
HELIX   10  10 ASP A  141  ARG A  144  5                                   4    
HELIX   11  11 GLN A  181  LEU A  189  1                                   9    
HELIX   12  12 GLU A  198  ARG A  209  1                                  12    
HELIX   13  13 THR A  228  GLY A  247  1                                  20    
HELIX   14  14 CYS A  252  GLN A  260  1                                   9    
HELIX   15  15 ASP A  264  ALA A  273  1                                  10    
HELIX   16  16 PRO A  274  ALA A  276  5                                   3    
HELIX   17  17 ASN A  278  LEU A  287  1                                  10    
HELIX   18  18 GLY B   13  HIS B   17  5                                   5    
HELIX   19  19 PRO B   18  ILE B   23  1                                   6    
HELIX   20  20 SER B   24  LEU B   27  5                                   4    
HELIX   21  21 ILE B   36  ALA B   46  1                                  11    
HELIX   22  22 ASP B   59  GLY B   68  1                                  10    
HELIX   23  23 GLY B   70  GLY B   74  5                                   5    
HELIX   24  24 ALA B   89  GLY B   95  1                                   7    
HELIX   25  25 GLY B   95  GLY B  100  1                                   6    
HELIX   26  26 ASP B  117  GLN B  127  1                                  11    
HELIX   27  27 ASP B  141  ARG B  144  5                                   4    
HELIX   28  28 GLN B  181  LEU B  189  1                                   9    
HELIX   29  29 GLU B  198  ARG B  209  1                                  12    
HELIX   30  30 THR B  228  GLY B  247  1                                  20    
HELIX   31  31 CYS B  252  GLN B  260  1                                   9    
HELIX   32  32 ASP B  264  ALA B  273  1                                  10    
HELIX   33  33 PRO B  274  ALA B  276  5                                   3    
HELIX   34  34 ASN B  278  LEU B  287  1                                  10    
HELIX   35  35 GLY C   13  HIS C   17  5                                   5    
HELIX   36  36 PRO C   18  ILE C   23  1                                   6    
HELIX   37  37 SER C   24  LEU C   28  5                                   5    
HELIX   38  38 ILE C   36  ALA C   46  1                                  11    
HELIX   39  39 ASP C   59  GLY C   68  1                                  10    
HELIX   40  40 GLY C   70  GLY C   74  5                                   5    
HELIX   41  41 GLY C   87  ALA C   89  5                                   3    
HELIX   42  42 GLN C   90  GLY C   95  1                                   6    
HELIX   43  43 GLY C   95  GLY C  100  1                                   6    
HELIX   44  44 ASP C  117  ARG C  128  1                                  12    
HELIX   45  45 ASP C  141  ARG C  144  5                                   4    
HELIX   46  46 GLN C  181  LEU C  189  1                                   9    
HELIX   47  47 GLU C  198  GLU C  208  1                                  11    
HELIX   48  48 THR C  228  GLY C  247  1                                  20    
HELIX   49  49 CYS C  252  GLN C  260  1                                   9    
HELIX   50  50 ASP C  264  ALA C  273  1                                  10    
HELIX   51  51 PRO C  274  ALA C  276  5                                   3    
HELIX   52  52 ASN C  278  LEU C  287  1                                  10    
HELIX   53  53 GLY D   13  HIS D   17  5                                   5    
HELIX   54  54 SER D   24  LEU D   27  5                                   4    
HELIX   55  55 ILE D   36  ALA D   46  1                                  11    
HELIX   56  56 ASP D   59  GLY D   68  1                                  10    
HELIX   57  57 GLY D   70  GLY D   74  5                                   5    
HELIX   58  58 GLY D   87  ALA D   89  5                                   3    
HELIX   59  59 GLN D   90  GLY D   95  1                                   6    
HELIX   60  60 GLY D   95  GLY D  100  1                                   6    
HELIX   61  61 ASP D  117  GLN D  127  1                                  11    
HELIX   62  62 ASP D  141  ARG D  144  5                                   4    
HELIX   63  63 GLN D  181  ASP D  188  1                                   8    
HELIX   64  64 GLU D  198  GLU D  208  1                                  11    
HELIX   65  65 THR D  228  GLY D  247  1                                  20    
HELIX   66  66 CYS D  252  GLN D  260  1                                   9    
HELIX   67  67 ASP D  264  ALA D  273  1                                  10    
HELIX   68  68 PRO D  274  ALA D  276  5                                   3    
HELIX   69  69 ASN D  278  LEU D  287  1                                  10    
HELIX   70  70 GLY E   13  HIS E   17  5                                   5    
HELIX   71  71 SER E   24  LEU E   27  5                                   4    
HELIX   72  72 ILE E   36  ALA E   46  1                                  11    
HELIX   73  73 ASP E   59  GLY E   68  1                                  10    
HELIX   74  74 GLY E   70  GLY E   74  5                                   5    
HELIX   75  75 ALA E   89  GLY E   95  1                                   7    
HELIX   76  76 GLY E   95  GLY E  100  1                                   6    
HELIX   77  77 ASP E  117  ARG E  128  1                                  12    
HELIX   78  78 ASP E  141  ARG E  144  5                                   4    
HELIX   79  79 GLN E  181  ASP E  188  1                                   8    
HELIX   80  80 GLU E  198  GLU E  208  1                                  11    
HELIX   81  81 THR E  228  GLY E  247  1                                  20    
HELIX   82  82 CYS E  252  GLN E  260  1                                   9    
HELIX   83  83 ASP E  264  ALA E  273  1                                  10    
HELIX   84  84 PRO E  274  ALA E  276  5                                   3    
HELIX   85  85 ASN E  278  LEU E  287  1                                  10    
HELIX   86  86 GLY F   13  HIS F   17  5                                   5    
HELIX   87  87 SER F   24  LEU F   27  5                                   4    
HELIX   88  88 ILE F   36  ALA F   46  1                                  11    
HELIX   89  89 THR F   56  GLN F   58  5                                   3    
HELIX   90  90 ASP F   59  GLY F   68  1                                  10    
HELIX   91  91 GLY F   70  GLY F   74  5                                   5    
HELIX   92  92 GLY F   87  ALA F   89  5                                   3    
HELIX   93  93 GLN F   90  GLY F   95  1                                   6    
HELIX   94  94 GLY F   95  GLY F  100  1                                   6    
HELIX   95  95 ASP F  117  ARG F  128  1                                  12    
HELIX   96  96 ASP F  141  ARG F  144  5                                   4    
HELIX   97  97 GLN F  181  LEU F  189  1                                   9    
HELIX   98  98 GLU F  198  GLU F  208  1                                  11    
HELIX   99  99 THR F  228  GLY F  247  1                                  20    
HELIX  100 100 CYS F  252  GLN F  260  1                                   9    
HELIX  101 101 ASP F  264  ALA F  273  1                                  10    
HELIX  102 102 PRO F  274  ALA F  276  5                                   3    
HELIX  103 103 ASN F  278  LEU F  287  1                                  10    
HELIX  104 104 GLY G   13  HIS G   17  5                                   5    
HELIX  105 105 PRO G   18  ILE G   23  1                                   6    
HELIX  106 106 SER G   24  LEU G   27  5                                   4    
HELIX  107 107 ILE G   36  ALA G   46  1                                  11    
HELIX  108 108 ASP G   59  GLY G   68  1                                  10    
HELIX  109 109 GLY G   70  GLY G   74  5                                   5    
HELIX  110 110 ALA G   89  GLY G   95  1                                   7    
HELIX  111 111 GLY G   95  GLY G  100  1                                   6    
HELIX  112 112 ASP G  117  GLN G  127  1                                  11    
HELIX  113 113 ASP G  141  ARG G  144  5                                   4    
HELIX  114 114 GLN G  181  LEU G  189  1                                   9    
HELIX  115 115 GLU G  198  ARG G  209  1                                  12    
HELIX  116 116 THR G  228  GLY G  247  1                                  20    
HELIX  117 117 CYS G  252  GLN G  260  1                                   9    
HELIX  118 118 ASP G  264  ALA G  273  1                                  10    
HELIX  119 119 PRO G  274  ALA G  276  5                                   3    
HELIX  120 120 ASN G  278  LEU G  287  1                                  10    
HELIX  121 121 GLY H   13  HIS H   17  5                                   5    
HELIX  122 122 PRO H   18  ILE H   23  1                                   6    
HELIX  123 123 SER H   24  LEU H   27  5                                   4    
HELIX  124 124 ILE H   36  ALA H   46  1                                  11    
HELIX  125 125 ASP H   59  GLY H   68  1                                  10    
HELIX  126 126 GLY H   70  GLY H   74  5                                   5    
HELIX  127 127 GLY H   87  ALA H   89  5                                   3    
HELIX  128 128 GLN H   90  GLY H   95  1                                   6    
HELIX  129 129 GLY H   95  GLY H  100  1                                   6    
HELIX  130 130 ASP H  117  ARG H  128  1                                  12    
HELIX  131 131 ASP H  141  ARG H  144  5                                   4    
HELIX  132 132 GLN H  181  LEU H  189  1                                   9    
HELIX  133 133 GLU H  198  ARG H  209  1                                  12    
HELIX  134 134 THR H  228  GLY H  247  1                                  20    
HELIX  135 135 CYS H  252  GLN H  260  1                                   9    
HELIX  136 136 ASP H  264  ALA H  273  1                                  10    
HELIX  137 137 PRO H  274  ALA H  276  5                                   3    
HELIX  138 138 ASN H  278  LEU H  288  1                                  11    
SHEET    1   A 7 ASP A  76  VAL A  81  0                                        
SHEET    2   A 7 GLU A  50  SER A  55  1  O  ILE A  51   N  GLN A  78           
SHEET    3   A 7 ARG A   3  LEU A   8  1  O  GLY A   5   N  LEU A  52           
SHEET    4   A 7 LEU A 103  LEU A 108  1  O  LEU A 103   N  LYS A   4           
SHEET    5   A 7 TYR A 170  TYR A 178 -1  O  GLY A 174   N  LEU A 108           
SHEET    6   A 7 ALA A 132  HIS A 138 -1  N  SER A 133   O  PHE A 177           
SHEET    7   A 7 LEU A 212  ILE A 216  1  N  SER A 213   O  ALA A 132           
SHEET    1   B 2 PRO A  29  VAL A  30  0                                        
SHEET    2   B 2 LYS A  33  PRO A  34 -1  O  LYS A  33   N  VAL A  30           
SHEET    1   C 2 ASN A 111  TYR A 114  0                                        
SHEET    2   C 2 ALA A 222  ASP A 225 -1  N  ALA A 222   O  TYR A 114           
SHEET    1   D 2 GLY A 146  PHE A 150  0                                        
SHEET    2   D 2 ALA A 156  GLU A 161 -1  N  ILE A 157   O  GLU A 149           
SHEET    1   E 7 ASP B  76  VAL B  81  0                                        
SHEET    2   E 7 GLU B  50  SER B  55  1  O  ILE B  51   N  GLN B  78           
SHEET    3   E 7 ARG B   3  LEU B   8  1  O  GLY B   5   N  LEU B  52           
SHEET    4   E 7 LEU B 103  LEU B 108  1  O  LEU B 103   N  LYS B   4           
SHEET    5   E 7 TYR B 170  TYR B 178 -1  O  GLY B 174   N  LEU B 108           
SHEET    6   E 7 ALA B 132  HIS B 138 -1  N  SER B 133   O  PHE B 177           
SHEET    7   E 7 LEU B 212  ILE B 216  1  N  SER B 213   O  ALA B 132           
SHEET    1   F 2 PRO B  29  VAL B  30  0                                        
SHEET    2   F 2 LYS B  33  PRO B  34 -1  O  LYS B  33   N  VAL B  30           
SHEET    1   G 2 ASN B 111  TYR B 114  0                                        
SHEET    2   G 2 ALA B 222  ASP B 225 -1  N  ALA B 222   O  TYR B 114           
SHEET    1   H 2 GLY B 146  PHE B 150  0                                        
SHEET    2   H 2 ALA B 156  GLU B 161 -1  N  ILE B 157   O  GLU B 149           
SHEET    1   I 3 LEU C 212  ILE C 216  0                                        
SHEET    2   I 3 ALA C 132  HIS C 138  1  O  ALA C 132   N  SER C 213           
SHEET    3   I 3 TYR C 170  VAL C 172 -1  N  ALA C 171   O  TYR C 137           
SHEET    1   J 7 LEU C 212  ILE C 216  0                                        
SHEET    2   J 7 ALA C 132  HIS C 138  1  O  ALA C 132   N  SER C 213           
SHEET    3   J 7 LEU C 175  TYR C 178 -1  N  PHE C 177   O  SER C 133           
SHEET    4   J 7 LEU C 103  LEU C 108 -1  O  SER C 104   N  TYR C 178           
SHEET    5   J 7 ARG C   3  LEU C   8  1  N  LYS C   4   O  LEU C 103           
SHEET    6   J 7 GLU C  50  SER C  55  1  O  GLU C  50   N  GLY C   5           
SHEET    7   J 7 ASP C  76  VAL C  81  1  O  ASP C  76   N  ILE C  51           
SHEET    1   K 2 ASN C 111  TYR C 114  0                                        
SHEET    2   K 2 ALA C 222  ASP C 225 -1  N  ALA C 222   O  TYR C 114           
SHEET    1   L 2 GLY C 146  PHE C 150  0                                        
SHEET    2   L 2 ALA C 156  GLU C 161 -1  N  ILE C 157   O  GLU C 149           
SHEET    1   M 3 LEU D 212  ILE D 216  0                                        
SHEET    2   M 3 ALA D 132  HIS D 138  1  O  ALA D 132   N  SER D 213           
SHEET    3   M 3 TYR D 170  VAL D 172 -1  N  ALA D 171   O  TYR D 137           
SHEET    1   N 7 LEU D 212  ILE D 216  0                                        
SHEET    2   N 7 ALA D 132  HIS D 138  1  O  ALA D 132   N  SER D 213           
SHEET    3   N 7 LEU D 175  TYR D 178 -1  N  PHE D 177   O  SER D 133           
SHEET    4   N 7 LEU D 103  LEU D 108 -1  N  SER D 104   O  TYR D 178           
SHEET    5   N 7 ARG D   3  LEU D   8  1  N  LYS D   4   O  LEU D 103           
SHEET    6   N 7 GLU D  50  SER D  55  1  O  GLU D  50   N  GLY D   5           
SHEET    7   N 7 ASP D  76  VAL D  81  1  O  ASP D  76   N  ILE D  51           
SHEET    1   O 2 PRO D  29  VAL D  30  0                                        
SHEET    2   O 2 LYS D  33  PRO D  34 -1  O  LYS D  33   N  VAL D  30           
SHEET    1   P 2 ASN D 111  TYR D 114  0                                        
SHEET    2   P 2 ALA D 222  ASP D 225 -1  N  ALA D 222   O  TYR D 114           
SHEET    1   Q 2 GLY D 146  PHE D 150  0                                        
SHEET    2   Q 2 ALA D 156  GLU D 161 -1  N  ILE D 157   O  GLU D 149           
SHEET    1   R 7 ASP E  76  VAL E  81  0                                        
SHEET    2   R 7 GLU E  50  SER E  55  1  O  ILE E  51   N  GLN E  78           
SHEET    3   R 7 ARG E   3  LEU E   8  1  O  GLY E   5   N  LEU E  52           
SHEET    4   R 7 LEU E 103  LEU E 108  1  O  LEU E 103   N  LYS E   4           
SHEET    5   R 7 TYR E 170  TYR E 178 -1  O  GLY E 174   N  LEU E 108           
SHEET    6   R 7 ALA E 132  HIS E 138 -1  O  SER E 133   N  PHE E 177           
SHEET    7   R 7 LEU E 212  ILE E 216  1  N  SER E 213   O  ALA E 132           
SHEET    1   S 2 PRO E  29  VAL E  30  0                                        
SHEET    2   S 2 LYS E  33  PRO E  34 -1  O  LYS E  33   N  VAL E  30           
SHEET    1   T 2 ASN E 111  TYR E 114  0                                        
SHEET    2   T 2 ALA E 222  ASP E 225 -1  N  ALA E 222   O  TYR E 114           
SHEET    1   U 2 GLY E 146  PHE E 150  0                                        
SHEET    2   U 2 ALA E 156  GLU E 161 -1  N  ILE E 157   O  GLU E 149           
SHEET    1   V 7 ASP F  76  VAL F  81  0                                        
SHEET    2   V 7 GLU F  50  SER F  55  1  O  ILE F  51   N  GLN F  78           
SHEET    3   V 7 ARG F   3  LEU F   8  1  O  GLY F   5   N  LEU F  52           
SHEET    4   V 7 LEU F 103  LEU F 108  1  O  LEU F 103   N  LYS F   4           
SHEET    5   V 7 TYR F 170  TYR F 178 -1  O  GLY F 174   N  LEU F 108           
SHEET    6   V 7 ALA F 132  HIS F 138 -1  O  SER F 133   N  PHE F 177           
SHEET    7   V 7 LEU F 212  ILE F 216  1  N  SER F 213   O  ALA F 132           
SHEET    1   W 2 PRO F  29  VAL F  30  0                                        
SHEET    2   W 2 LYS F  33  PRO F  34 -1  O  LYS F  33   N  VAL F  30           
SHEET    1   X 2 ASN F 111  TYR F 114  0                                        
SHEET    2   X 2 ALA F 222  ASP F 225 -1  N  ALA F 222   O  TYR F 114           
SHEET    1   Y 2 GLY F 146  PHE F 150  0                                        
SHEET    2   Y 2 ALA F 156  GLU F 161 -1  N  ILE F 157   O  GLU F 149           
SHEET    1   Z 3 LEU G 212  ILE G 216  0                                        
SHEET    2   Z 3 ALA G 132  HIS G 138  1  O  ALA G 132   N  SER G 213           
SHEET    3   Z 3 TYR G 170  VAL G 172 -1  O  ALA G 171   N  TYR G 137           
SHEET    1  AA 7 LEU G 212  ILE G 216  0                                        
SHEET    2  AA 7 ALA G 132  HIS G 138  1  O  ALA G 132   N  SER G 213           
SHEET    3  AA 7 LEU G 175  TYR G 178 -1  N  PHE G 177   O  SER G 133           
SHEET    4  AA 7 LEU G 103  LEU G 108 -1  O  SER G 104   N  TYR G 178           
SHEET    5  AA 7 ARG G   3  LEU G   8  1  N  LYS G   4   O  LEU G 103           
SHEET    6  AA 7 GLU G  50  SER G  55  1  O  GLU G  50   N  GLY G   5           
SHEET    7  AA 7 ASP G  76  VAL G  81  1  O  ASP G  76   N  ILE G  51           
SHEET    1  AB 2 PRO G  29  VAL G  30  0                                        
SHEET    2  AB 2 LYS G  33  PRO G  34 -1  O  LYS G  33   N  VAL G  30           
SHEET    1  AC 2 ASN G 111  TYR G 114  0                                        
SHEET    2  AC 2 ALA G 222  ASP G 225 -1  N  ALA G 222   O  TYR G 114           
SHEET    1  AD 2 GLY G 146  PHE G 150  0                                        
SHEET    2  AD 2 ALA G 156  GLU G 161 -1  N  ILE G 157   O  GLU G 149           
SHEET    1  AE 3 LEU H 212  ILE H 216  0                                        
SHEET    2  AE 3 ALA H 132  HIS H 138  1  O  ALA H 132   N  SER H 213           
SHEET    3  AE 3 TYR H 170  VAL H 172 -1  N  ALA H 171   O  TYR H 137           
SHEET    1  AF 7 LEU H 212  ILE H 216  0                                        
SHEET    2  AF 7 ALA H 132  HIS H 138  1  O  ALA H 132   N  SER H 213           
SHEET    3  AF 7 LEU H 175  TYR H 178 -1  N  PHE H 177   O  SER H 133           
SHEET    4  AF 7 LEU H 103  LEU H 108 -1  O  SER H 104   N  TYR H 178           
SHEET    5  AF 7 ARG H   3  LEU H   8  1  N  LYS H   4   O  LEU H 103           
SHEET    6  AF 7 GLU H  50  SER H  55  1  O  GLU H  50   N  GLY H   5           
SHEET    7  AF 7 ASP H  76  VAL H  81  1  O  ASP H  76   N  ILE H  51           
SHEET    1  AG 2 PRO H  29  VAL H  30  0                                        
SHEET    2  AG 2 LYS H  33  PRO H  34 -1  O  LYS H  33   N  VAL H  30           
SHEET    1  AH 2 ASN H 111  TYR H 114  0                                        
SHEET    2  AH 2 ALA H 222  ASP H 225 -1  N  ALA H 222   O  TYR H 114           
SHEET    1  AI 2 GLY H 146  PHE H 150  0                                        
SHEET    2  AI 2 ALA H 156  GLU H 161 -1  N  ILE H 157   O  GLU H 149           
CISPEP   1 HIS A   17    PRO A   18          0         7.64                     
CISPEP   2 HIS B   17    PRO B   18          0         5.19                     
CISPEP   3 HIS C   17    PRO C   18          0         1.50                     
CISPEP   4 HIS D   17    PRO D   18          0         2.90                     
CISPEP   5 HIS E   17    PRO E   18          0        -2.09                     
CISPEP   6 HIS F   17    PRO F   18          0         4.14                     
CISPEP   7 HIS G   17    PRO G   18          0         6.63                     
CISPEP   8 HIS H   17    PRO H   18          0         4.48                     
SITE     1 AC1  8 ARG A 128  GLU A 215  HOH A9591  HOH A9892                    
SITE     2 AC1  8 ASP F 151  GLN F 152  HOH F9678  HOH F9874                    
SITE     1 AC2  8 ARG B 128  GLU B 215  HOH B9568  ASP E 151                    
SITE     2 AC2  8 GLN E 152  HOH E9617  HOH E9790  HOH E9874                    
SITE     1 AC3  4 GLN C 127  ARG C 128  GLN C 129  THR C 130                    
SITE     1 AC4  7 HOH B9956  ARG C  62  ARG D  62  HOH D9632                    
SITE     2 AC4  7 HOH D9713  HOH D9757  HOH D9818                               
SITE     1 AC5  9 ASP C 151  GLN C 152  HOH C9673  HOH C9814                    
SITE     2 AC5  9 HOH C9886  ARG G 128  GLU G 215  HOH G9679                    
SITE     3 AC5  9 HOH G9733                                                     
SITE     1 AC6  5 GLN D 127  ARG D 128  GLN D 129  THR D 130                    
SITE     2 AC6  5 HOH D9859                                                     
SITE     1 AC7  7 ARG B 245  ARG D 144  SER D 231  HOH D9564                    
SITE     2 AC7  7 HOH D9720  HOH D9728  HOH D9887                               
SITE     1 AC8  6 ASP D 151  GLN D 152  HOH D9651  ARG H 128                    
SITE     2 AC8  6 GLU H 215  HOH H9633                                          
SITE     1 AC9  5 ARG D  49  HOH D9634  HOH D9693  ARG E 187                    
SITE     2 AC9  5 HOH E9666                                                     
SITE     1 BC1  4 ARG E  62  GLN E  65  HOH E9813  ARG F  62                    
SITE     1 BC2  5 GLN E 127  ARG E 128  GLN E 129  THR E 130                    
SITE     2 BC2  5 HOH E9850                                                     
SITE     1 BC3  2 GLN F 129  THR F 130                                          
SITE     1 BC4  6 ARG G  62  HOH G9672  HOH G9770  HOH G9833                    
SITE     2 BC4  6 HOH G9857  ARG H  62                                          
SITE     1 BC5 17 LEU A   8  GLY A  10  GLY A  11  LYS A  25                    
SITE     2 BC5 17 GLN A  26  GLN A  82  PRO A  85  ASP A  86                    
SITE     3 BC5 17 GLY A  87  LEU A  88  GLY A 109  ASP A 110                    
SITE     4 BC5 17 ARG A 194  GLU A 196  HOH A9651  HOH A9663                    
SITE     5 BC5 17 HOH A9852                                                     
SITE     1 BC6 19 LEU B   8  GLY B  10  GLY B  11  LYS B  25                    
SITE     2 BC6 19 GLN B  26  GLN B  82  PRO B  85  ASP B  86                    
SITE     3 BC6 19 GLY B  87  LEU B  88  GLY B 109  ASP B 110                    
SITE     4 BC6 19 LYS B 162  GLU B 196  HOH B9642  HOH B9667                    
SITE     5 BC6 19 HOH B9669  HOH B9702  HOH B9868                               
SITE     1 BC7 15 LEU C   8  GLY C  10  GLY C  11  LYS C  25                    
SITE     2 BC7 15 GLN C  26  GLN C  82  PRO C  85  ASP C  86                    
SITE     3 BC7 15 GLY C  87  LEU C  88  GLY C 109  ASP C 110                    
SITE     4 BC7 15 GLU C 196  HOH C9622  HOH C9760                               
SITE     1 BC8 18 LEU D   8  GLY D  10  GLY D  11  LYS D  25                    
SITE     2 BC8 18 GLN D  26  GLN D  82  PRO D  85  ASP D  86                    
SITE     3 BC8 18 GLY D  87  LEU D  88  GLY D 109  ASP D 110                    
SITE     4 BC8 18 GLU D 196  HOH D9644  HOH D9672  HOH D9698                    
SITE     5 BC8 18 HOH D9744  HOH D9781                                          
SITE     1 BC9 14 LEU E   8  GLY E  10  GLY E  11  LYS E  25                    
SITE     2 BC9 14 GLN E  26  GLN E  82  PRO E  85  ASP E  86                    
SITE     3 BC9 14 GLY E  87  LEU E  88  ASP E 110  HOH E9747                    
SITE     4 BC9 14 HOH E9752  HOH E9886                                          
SITE     1 CC1 15 LEU F   8  GLY F  10  LYS F  25  GLN F  26                    
SITE     2 CC1 15 GLN F  82  PRO F  85  ASP F  86  GLY F  87                    
SITE     3 CC1 15 LEU F  88  ASP F 110  GLU F 196  HOH F9623                    
SITE     4 CC1 15 HOH F9646  HOH F9649  HOH F9748                               
SITE     1 CC2 18 LEU G   8  GLY G  10  GLY G  11  LYS G  25                    
SITE     2 CC2 18 GLN G  26  GLN G  82  PRO G  85  ASP G  86                    
SITE     3 CC2 18 GLY G  87  LEU G  88  GLY G 109  ASP G 110                    
SITE     4 CC2 18 GLU G 196  HOH G9601  HOH G9795  HOH G9807                    
SITE     5 CC2 18 HOH G9850  HOH G9882                                          
SITE     1 CC3 21 LEU H   8  GLY H  10  GLY H  11  LYS H  25                    
SITE     2 CC3 21 GLN H  26  GLN H  82  PRO H  85  ASP H  86                    
SITE     3 CC3 21 GLY H  87  LEU H  88  GLY H 109  ASP H 110                    
SITE     4 CC3 21 HOH H9614  HOH H9673  HOH H9692  HOH H9768                    
SITE     5 CC3 21 HOH H9830  HOH H9861  HOH H9867  HOH H9882                    
SITE     6 CC3 21 HOH H9939                                                     
SITE     1 CC4 20 LEU A  45  TYR A 114  GLY A 115  HIS A 116                    
SITE     2 CC4 20 ASP A 117  VAL A 250  ALA A 251  GLU A 255                    
SITE     3 CC4 20 ILE A 256  ARG A 259  HOH A9520  HOH A9527                    
SITE     4 CC4 20 HOH A9530  HOH A9534  HOH A9535  HOH A9547                    
SITE     5 CC4 20 HOH A9947  GLY C 218  ARG C 219  GLY C 220                    
SITE     1 CC5 20 LEU B  45  TYR B 114  GLY B 115  HIS B 116                    
SITE     2 CC5 20 ASP B 117  VAL B 250  ALA B 251  GLU B 255                    
SITE     3 CC5 20 ILE B 256  HOH B9517  HOH B9521  HOH B9529                    
SITE     4 CC5 20 HOH B9536  HOH B9560  HOH B9693  HOH B9969                    
SITE     5 CC5 20 HOH B9970  GLY D 218  ARG D 219  GLY D 220                    
SITE     1 CC6 20 GLY A 218  ARG A 219  GLY A 220  LEU C  45                    
SITE     2 CC6 20 TYR C 114  GLY C 115  HIS C 116  ASP C 117                    
SITE     3 CC6 20 VAL C 250  ALA C 251  GLU C 255  ILE C 256                    
SITE     4 CC6 20 ARG C 259  HOH C9522  HOH C9547  HOH C9548                    
SITE     5 CC6 20 HOH C9575  HOH C9630  HOH C9884  HOH C9891                    
SITE     1 CC7 20 GLY B 218  ARG B 219  GLY B 220  LEU D  45                    
SITE     2 CC7 20 TYR D 114  GLY D 115  HIS D 116  ASP D 117                    
SITE     3 CC7 20 VAL D 250  ALA D 251  GLU D 255  ILE D 256                    
SITE     4 CC7 20 ARG D 259  HOH D9526  HOH D9529  HOH D9537                    
SITE     5 CC7 20 HOH D9546  HOH D9548  HOH D9571  HOH D9874                    
SITE     1 CC8 18 TYR E 114  GLY E 115  HIS E 116  ASP E 117                    
SITE     2 CC8 18 VAL E 250  ALA E 251  GLU E 255  ILE E 256                    
SITE     3 CC8 18 HOH E9517  HOH E9524  HOH E9539  HOH E9554                    
SITE     4 CC8 18 HOH E9556  HOH E9591  HOH E9598  GLY H 218                    
SITE     5 CC8 18 ARG H 219  GLY H 220                                          
SITE     1 CC9 19 LEU F  45  TYR F 114  GLY F 115  HIS F 116                    
SITE     2 CC9 19 ASP F 117  VAL F 250  ALA F 251  GLU F 255                    
SITE     3 CC9 19 ILE F 256  HOH F9514  HOH F9530  HOH F9531                    
SITE     4 CC9 19 HOH F9545  HOH F9568  HOH F9576  HOH F9602                    
SITE     5 CC9 19 GLY G 218  ARG G 219  GLY G 220                               
SITE     1 DC1 18 GLY F 218  ARG F 219  GLY F 220  TYR G 114                    
SITE     2 DC1 18 GLY G 115  HIS G 116  ASP G 117  VAL G 250                    
SITE     3 DC1 18 ALA G 251  GLU G 255  ILE G 256  HOH G9518                    
SITE     4 DC1 18 HOH G9527  HOH G9538  HOH G9542  HOH G9546                    
SITE     5 DC1 18 HOH G9588  HOH G9600                                          
SITE     1 DC2 19 GLY E 218  ARG E 219  GLY E 220  LEU H  45                    
SITE     2 DC2 19 TYR H 114  GLY H 115  HIS H 116  ASP H 117                    
SITE     3 DC2 19 VAL H 250  ALA H 251  GLU H 255  ILE H 256                    
SITE     4 DC2 19 HOH H9523  HOH H9524  HOH H9527  HOH H9533                    
SITE     5 DC2 19 HOH H9537  HOH H9541  HOH H9552                               
CRYST1   71.494   73.064  134.738  89.93  80.92  81.11 P 1           8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013987 -0.002188 -0.002288        0.00000                         
SCALE2      0.000000  0.013853  0.000329        0.00000                         
SCALE3      0.000000  0.000000  0.007518        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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