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Database: PDB
Entry: 1G1L
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HEADER    TRANSFERASE                             12-OCT-00   1G1L              
TITLE     THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF     
TITLE    2 GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). TDP-GLUCOSE        
TITLE    3 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    L-RHAMNOSE, NUCLEOTIDYLTRANSFERASE, PYROPHOSPHORYLASE,                
KEYWDS   2 THYMIDYLYLTRANSFERASE, ALLOSTERY, TRANSFERASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.BLANKENFELDT,M.ASUNCION,J.S.LAM,J.H.NAIMSMITH                       
REVDAT   5   31-JAN-18 1G1L    1       JRNL   REMARK                            
REVDAT   4   23-MAY-12 1G1L    1       HETATM REMARK VERSN                      
REVDAT   3   24-FEB-09 1G1L    1       VERSN                                    
REVDAT   2   01-APR-03 1G1L    1       JRNL                                     
REVDAT   1   27-DEC-00 1G1L    0                                                
JRNL        AUTH   W.BLANKENFELDT,M.ASUNCION,J.S.LAM,J.H.NAISMITH               
JRNL        TITL   THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND          
JRNL        TITL 2 REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE      
JRNL        TITL 3 (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,C.CREUZENET,     
REMARK   1  AUTH 2 J.S.LAM,J.H.NAISMITH                                         
REMARK   1  TITL   THE PURIFICATION, CRYSTALLISATION AND PRELIMINARY STRUCTURAL 
REMARK   1  TITL 2 CHARACTERIZATION OF GLUCOSE-1-PHOSPHATE                      
REMARK   1  TITL 3 THYMIDYLYLTRANSFERASE (RMLA), THE FIRST ENZYME OF THE        
REMARK   1  TITL 4 DTDP-L-RHAMNOSE SYNTHESIS PATHWAY FROM PSEUDOMONAS           
REMARK   1  TITL 5 AERUGINOSA                                                   
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  56  1501 2000              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  DOI    10.1107/S0907444900010040                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.MELO,L.GLASER                                              
REMARK   1  TITL   THE NUCLEOTIDE SPECIFICITY AND FEEDBACK CONTROL OF THYMIDINE 
REMARK   1  TITL 2 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.    1.77 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) : 1.77                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 230146                         
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) : 0.159                           
REMARK   3   R VALUE            (WORKING SET) : 0.156                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 12192                           
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 18296                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 717                                     
REMARK   3   SOLVENT ATOMS            : 2971                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.45                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.45000                                              
REMARK   3    B22 (A**2) : -0.16000                                             
REMARK   3    B33 (A**2) : -0.28000                                             
REMARK   3    B12 (A**2) : 0.02000                                              
REMARK   3    B13 (A**2) : -0.03000                                             
REMARK   3    B23 (A**2) : -0.26000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.254         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.123         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.129         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.973         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.022 ; 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) : 0.010 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.126 ; 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) : 4.270 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.708 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 6.138 ; 3.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 7.678 ; 4.500                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: TLS REFINEMENT IN REFMAC5. ANISOTROPIC    
REMARK   3  B-FACTORS CALCULATED BUT NOT REFINED                                
REMARK   4                                                                      
REMARK   4 1G1L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000012119.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-FEB-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                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
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   : 202988                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.770                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.640                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 9-11 % (W/V) PEG 6000, 0.5 M LITHIUM     
REMARK 280  SULFATE, 0.1 M CITRATE. 4 + 4 MIKROLITRE. SUBSTRATE ADDED IN 1      
REMARK 280  MIKROLITRE 50 MM., PH 4.6, VAPOR DIFFUSION, SITTING DROP,           
REMARK 280  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 BEST DESCRIBED AS A    
REMARK 300 DIMER OF DIMERS.                                                     
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: 23790 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -285.0 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: 22890 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -264.0 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 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 E     1                                                      
REMARK 465     MET G     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   O3P  DAU F  3510     O    HOH F  4118              1.90            
REMARK 500   O2   SO4 A  3818     O    HOH A  3921              1.95            
REMARK 500   O    HOH G  4041     O    HOH G  4150              1.95            
REMARK 500   OD1  ASN H   101     O    HOH H  4130              1.96            
REMARK 500   O3   SO4 B  3701     O    HOH B  4205              2.02            
REMARK 500   O    HOH A  4176     O    HOH C  3961              2.02            
REMARK 500   O    HOH E  4043     O    HOH E  4074              2.03            
REMARK 500   O3   CIT A  3801     O    HOH A  4216              2.04            
REMARK 500   O1   SO4 E  3810     O    HOH E  3990              2.05            
REMARK 500   O2   SO4 E  3820     O    HOH E  4034              2.05            
REMARK 500   O    HOH G  3952     O    HOH G  4124              2.05            
REMARK 500   OE1  GLN G   237     NE2  GLN H   237              2.07            
REMARK 500   OE1  GLN E   282     O    HOH E  4036              2.08            
REMARK 500   OE1  GLU E   269     CD1  LEU E   288              2.08            
REMARK 500   OG1  THR H   289     O    HOH H  4230              2.09            
REMARK 500   O    HOH C  4002     O    HOH C  4103              2.09            
REMARK 500   O    HOH A  4213     O    HOH A  4224              2.09            
REMARK 500   OD2  ASP C    86     O    HOH C  4159              2.09            
REMARK 500   NE2  HIS G   119     O    HOH G  4077              2.09            
REMARK 500   OG1  THR G   289     O    HOH G  4203              2.10            
REMARK 500   O1   SO4 A  3818     O4   DAU A  3501              2.11            
REMARK 500   NZ   LYS A     2     OE1  GLU A    50              2.12            
REMARK 500   O    HOH B  4050     O    HOH B  4060              2.12            
REMARK 500   O2P  DAU C  3504     O    HOH C  4149              2.13            
REMARK 500   O    HOH H  4174     O    HOH H  4205              2.13            
REMARK 500   O2   CIT A  3801     O    HOH A  4215              2.13            
REMARK 500   O    GLU D   161     NH2  ARG D   194              2.13            
REMARK 500   O    HOH D  3883     O    HOH D  4008              2.13            
REMARK 500   OD1  ASP H   184     NH1  ARG H   187              2.14            
REMARK 500   O    HOH D  3939     O    HOH D  4047              2.14            
REMARK 500   O    HOH A  4036     O    HOH A  4148              2.14            
REMARK 500   OE2  GLU E   234     O    HOH E  4074              2.14            
REMARK 500   NZ   LYS F     2     OE1  GLU F    50              2.14            
REMARK 500   O    HOH E  3856     O    HOH E  3904              2.14            
REMARK 500   O    HOH G  4146     O    HOH G  4165              2.15            
REMARK 500   O    LYS D     2     O    HOH D  4119              2.16            
REMARK 500   NH1  ARG G    15     O4   SO4 G  3702              2.16            
REMARK 500   OG1  THR C   289     O    HOH C  4163              2.16            
REMARK 500   O    HOH G  4205     O    HOH H  4199              2.16            
REMARK 500   O    HOH A  3969     O    HOH A  4027              2.17            
REMARK 500   O    HOH A  3924     O    HOH A  4145              2.17            
REMARK 500   O    HOH G  4057     O    HOH G  4112              2.17            
REMARK 500   O    HOH E  4019     O    HOH E  4041              2.17            
REMARK 500   O2P  DAU E  3508     O    HOH E  4128              2.17            
REMARK 500   O7   CIT A  3800     O    HOH A  4206              2.17            
REMARK 500   OE1  GLN E   282     O    HOH E  4140              2.17            
REMARK 500   O6   DAU F  3510     O    HOH F  4119              2.17            
REMARK 500   O    HOH B  3879     O    HOH B  4215              2.17            
REMARK 500   NE   ARG A    62     O4   SO4 A  3802              2.18            
REMARK 500   O    HOH A  4059     O    HOH A  4085              2.18            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      60 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  3941     O    HOH H  4205     1565     2.12            
REMARK 500   O    HOH D  4087     O    HOH E  4106     1655     2.14            
REMARK 500   O    HOH A  4001     O    HOH B  4113     1565     2.19            
REMARK 500   OE1  GLN F    64     O    HOH G  4216     1455     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    TYR H  37   CD1   TYR H  37   CE1     0.094                       
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    ASP A  59   CB  -  CG  -  OD2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ARG A 128   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 209   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    LEU B  88   CB  -  CG  -  CD2 ANGL. DEV. =  10.4 DEGREES          
REMARK 500    ARG B 209   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG B 209   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    ASP C  76   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG D 259   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG D 259   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG D 259   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG D 259   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ARG F  62   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ASP F  86   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP F 110   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP F 230   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP G  86   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG G 128   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG G 209   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG G 209   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ASP H  76   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG H 194   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG H 194   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG H 286   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 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      -76.72     68.83                                   
REMARK 500    ARG A 194       -7.09    -57.68                                   
REMARK 500    THR A 226       30.91    -87.45                                   
REMARK 500    TYR B  31      -78.06     71.47                                   
REMARK 500    ASN B 101       44.98   -109.26                                   
REMARK 500    THR B 226       35.62    -90.91                                   
REMARK 500    TYR C  31      -80.80     65.79                                   
REMARK 500    THR C 226       30.71    -95.31                                   
REMARK 500    THR D  20       34.53    -92.70                                   
REMARK 500    TYR D  31      -83.51     68.05                                   
REMARK 500    THR E  14      -44.66    -28.76                                   
REMARK 500    TYR E  31      -84.90     66.73                                   
REMARK 500    TYR F  31      -83.26     67.66                                   
REMARK 500    TYR G  31      -82.14     69.57                                   
REMARK 500    THR G 226       32.31    -97.52                                   
REMARK 500    TYR H  31      -77.15     71.12                                   
REMARK 500    ASN H 101       31.06    -99.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     HOH B  3913                                                      
REMARK 615     HOH H  3907                                                      
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                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 3701                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 3702                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 3703                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3802                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3803                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 3804                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 3805                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 3806                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3807                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 3808                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 3809                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 3810                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 3811                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 3812                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 3813                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 3814                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 3815                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 3816                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3817                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3818                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3819                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 3820                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAU A 3500                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAU A 3501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAU B 3502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAU B 3503                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAU C 3504                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAU C 3505                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAU D 3506                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAU D 3507                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAU E 3508                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAU E 3509                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAU F 3510                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAU F 3511                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAU H 3512                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAU H 3513                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAU G 3514                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAU G 3515                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 3800                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 3801                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FXO   RELATED DB: PDB                                   
REMARK 900 1FXO IS RMLA IN COMPLEX WITH DTMP                                    
REMARK 900 RELATED ID: 1FZW   RELATED DB: PDB                                   
REMARK 900 1FZW IS RMLA APO-ENZYME                                              
REMARK 900 RELATED ID: 1G0R   RELATED DB: PDB                                   
REMARK 900 1G0R IS RMLA IN COMPLEX WITH THYMIDINE AND GLUCOSE-1-PHOSPHATE       
REMARK 900 RELATED ID: 1G23   RELATED DB: PDB                                   
REMARK 900 1G23 IS RMLA IN COMPLEX WITH ALPHA-D-GLUCOSE-1-PHOSPHATE (G1P)       
REMARK 900 RELATED ID: 1G2V   RELATED DB: PDB                                   
REMARK 900 1G2V IS RMLA IN COMPLEX WITH 2'-DEOXY-THYMIDINE-5'-TRIPHOSPHATE      
REMARK 900 (TTP)                                                                
REMARK 900 RELATED ID: 1G31   RELATED DB: PDB                                   
REMARK 900 1G31 IS RMLA IN COMPLEX WITH 2'-DEOXY-THYMIDINE-BETA-L-RHAMNOSE      
REMARK 900 (TDR)                                                                
DBREF  1G1L A    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G1L B    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G1L C    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G1L D    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G1L E    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G1L F    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G1L G    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G1L 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  A3802       5                                                       
HET    SO4  A3803       5                                                       
HET    SO4  A3817       5                                                       
HET    SO4  A3818       5                                                       
HET    DAU  A3500      36                                                       
HET    DAU  A3501      36                                                       
HET    CIT  A3800      13                                                       
HET    CIT  A3801      13                                                       
HET    SO4  B3701       5                                                       
HET    SO4  B3804       5                                                       
HET    DAU  B3502      36                                                       
HET    DAU  B3503      36                                                       
HET    SO4  C3805       5                                                       
HET    SO4  C3806       5                                                       
HET    DAU  C3504      36                                                       
HET    DAU  C3505      36                                                       
HET    SO4  D3807       5                                                       
HET    SO4  D3819       5                                                       
HET    DAU  D3506      36                                                       
HET    DAU  D3507      36                                                       
HET    SO4  E3808       5                                                       
HET    SO4  E3809       5                                                       
HET    SO4  E3810       5                                                       
HET    SO4  E3820       5                                                       
HET    DAU  E3508      36                                                       
HET    DAU  E3509      36                                                       
HET    SO4  F3811       5                                                       
HET    DAU  F3510      36                                                       
HET    DAU  F3511      36                                                       
HET    SO4  G3702       5                                                       
HET    SO4  G3812       5                                                       
HET    SO4  G3813       5                                                       
HET    DAU  G3514      36                                                       
HET    DAU  G3515      36                                                       
HET    SO4  H3703       5                                                       
HET    SO4  H3814       5                                                       
HET    SO4  H3815       5                                                       
HET    SO4  H3816       5                                                       
HET    DAU  H3512      36                                                       
HET    DAU  H3513      36                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     DAU 2'DEOXY-THYMIDINE-5'-DIPHOSPHO-ALPHA-D-GLUCOSE                   
HETNAM     CIT CITRIC ACID                                                      
FORMUL   9  SO4    23(O4 S 2-)                                                  
FORMUL  14  DAU    16(C16 H26 N2 O16 P2)                                        
FORMUL  16  CIT    2(C6 H8 O7)                                                  
FORMUL  50  HOH   *2971(H2 O)                                                   
HELIX    1   1 GLY A   13  HIS A   17  5                                   5    
HELIX    2   2 PRO A   18  ILE A   23  1                                   6    
HELIX    3   3 SER A   24  LEU A   27  5                                   4    
HELIX    4   4 ILE A   36  ALA A   46  1                                  11    
HELIX    5   5 ASP A   59  GLY A   68  1                                  10    
HELIX    6   6 GLY A   70  GLY A   74  5                                   5    
HELIX    7   7 GLY A   87  ALA A   89  5                                   3    
HELIX    8   8 GLN A   90  GLY A   95  1                                   6    
HELIX    9   9 GLY A   95  GLY A  100  1                                   6    
HELIX   10  10 ASP A  117  GLN A  127  1                                  11    
HELIX   11  11 ASP A  141  ARG A  144  5                                   4    
HELIX   12  12 GLN A  181  ASP A  188  1                                   8    
HELIX   13  13 GLU A  198  ARG A  209  1                                  12    
HELIX   14  14 THR A  228  GLY A  247  1                                  20    
HELIX   15  15 CYS A  252  GLN A  260  1                                   9    
HELIX   16  16 ASP A  264  ALA A  273  1                                  10    
HELIX   17  17 PRO A  274  ALA A  276  5                                   3    
HELIX   18  18 ASN A  278  LEU A  287  1                                  10    
HELIX   19  19 GLY B   13  HIS B   17  5                                   5    
HELIX   20  20 PRO B   18  ILE B   23  1                                   6    
HELIX   21  21 SER B   24  LEU B   27  5                                   4    
HELIX   22  22 ILE B   36  ALA B   46  1                                  11    
HELIX   23  23 ASP B   59  GLY B   68  1                                  10    
HELIX   24  24 GLY B   70  GLY B   74  5                                   5    
HELIX   25  25 GLY B   87  ALA B   89  5                                   3    
HELIX   26  26 GLN B   90  GLY B   95  1                                   6    
HELIX   27  27 GLY B   95  GLY B  100  1                                   6    
HELIX   28  28 ASP B  117  ARG B  128  1                                  12    
HELIX   29  29 ASP B  141  ARG B  144  5                                   4    
HELIX   30  30 GLN B  181  LEU B  189  1                                   9    
HELIX   31  31 GLU B  198  ARG B  209  1                                  12    
HELIX   32  32 THR B  228  GLY B  247  1                                  20    
HELIX   33  33 CYS B  252  GLN B  260  1                                   9    
HELIX   34  34 ASP B  264  ALA B  273  1                                  10    
HELIX   35  35 PRO B  274  ALA B  276  5                                   3    
HELIX   36  36 ASN B  278  THR B  289  1                                  12    
HELIX   37  37 PRO C   18  ALA C   22  5                                   5    
HELIX   38  38 SER C   24  LEU C   27  5                                   4    
HELIX   39  39 ILE C   36  ALA C   46  1                                  11    
HELIX   40  40 ASP C   59  GLY C   68  1                                  10    
HELIX   41  41 GLY C   70  GLY C   74  5                                   5    
HELIX   42  42 GLY C   87  ALA C   89  5                                   3    
HELIX   43  43 GLN C   90  GLY C   95  1                                   6    
HELIX   44  44 GLY C   95  GLY C  100  1                                   6    
HELIX   45  45 ASP C  117  ARG C  128  1                                  12    
HELIX   46  46 ASP C  141  ARG C  144  5                                   4    
HELIX   47  47 GLN C  181  ASP C  188  1                                   8    
HELIX   48  48 GLU C  198  GLU C  208  1                                  11    
HELIX   49  49 THR C  228  GLY C  247  1                                  20    
HELIX   50  50 CYS C  252  GLN C  260  1                                   9    
HELIX   51  51 ASP C  264  ALA C  273  1                                  10    
HELIX   52  52 PRO C  274  ALA C  276  5                                   3    
HELIX   53  53 ASN C  278  GLU C  290  1                                  13    
HELIX   54  54 GLY D   13  HIS D   17  5                                   5    
HELIX   55  55 PRO D   18  ALA D   22  5                                   5    
HELIX   56  56 SER D   24  LEU D   27  5                                   4    
HELIX   57  57 ILE D   36  ALA D   46  1                                  11    
HELIX   58  58 ASP D   59  GLY D   68  1                                  10    
HELIX   59  59 GLY D   70  GLY D   74  5                                   5    
HELIX   60  60 GLY D   87  ALA D   89  5                                   3    
HELIX   61  61 GLN D   90  GLY D   95  1                                   6    
HELIX   62  62 GLY D   95  GLY D  100  1                                   6    
HELIX   63  63 ASP D  117  GLN D  127  1                                  11    
HELIX   64  64 ASP D  141  ARG D  144  5                                   4    
HELIX   65  65 GLN D  181  LEU D  189  1                                   9    
HELIX   66  66 GLU D  198  GLU D  208  1                                  11    
HELIX   67  67 THR D  228  GLY D  247  1                                  20    
HELIX   68  68 CYS D  252  GLN D  260  1                                   9    
HELIX   69  69 ASP D  264  ALA D  273  1                                  10    
HELIX   70  70 PRO D  274  ALA D  276  5                                   3    
HELIX   71  71 ASN D  278  LEU D  287  1                                  10    
HELIX   72  72 GLY E   13  HIS E   17  5                                   5    
HELIX   73  73 SER E   24  LEU E   27  5                                   4    
HELIX   74  74 ILE E   36  ALA E   46  1                                  11    
HELIX   75  75 ASP E   59  GLY E   68  1                                  10    
HELIX   76  76 GLY E   70  GLY E   74  5                                   5    
HELIX   77  77 ALA E   89  GLY E   95  1                                   7    
HELIX   78  78 GLY E   95  GLY E  100  1                                   6    
HELIX   79  79 ASP E  117  GLN E  127  1                                  11    
HELIX   80  80 ASP E  141  ARG E  144  5                                   4    
HELIX   81  81 GLN E  181  LEU E  189  1                                   9    
HELIX   82  82 GLU E  198  GLU E  208  1                                  11    
HELIX   83  83 THR E  228  GLY E  247  1                                  20    
HELIX   84  84 CYS E  252  GLN E  260  1                                   9    
HELIX   85  85 ASP E  264  ALA E  273  1                                  10    
HELIX   86  86 PRO E  274  ALA E  276  5                                   3    
HELIX   87  87 ASN E  278  LEU E  288  1                                  11    
HELIX   88  88 GLY F   13  HIS F   17  5                                   5    
HELIX   89  89 PRO F   18  ALA F   22  5                                   5    
HELIX   90  90 SER F   24  LEU F   27  5                                   4    
HELIX   91  91 ILE F   36  ALA F   46  1                                  11    
HELIX   92  92 THR F   56  GLN F   58  5                                   3    
HELIX   93  93 ASP F   59  GLY F   68  1                                  10    
HELIX   94  94 GLY F   70  GLY F   74  5                                   5    
HELIX   95  95 ALA F   89  GLY F   95  1                                   7    
HELIX   96  96 GLY F   95  GLY F  100  1                                   6    
HELIX   97  97 ASP F  117  ARG F  128  1                                  12    
HELIX   98  98 ASP F  141  ARG F  144  5                                   4    
HELIX   99  99 GLN F  181  LEU F  189  1                                   9    
HELIX  100 100 GLU F  198  GLU F  208  1                                  11    
HELIX  101 101 THR F  228  GLY F  247  1                                  20    
HELIX  102 102 CYS F  252  GLN F  260  1                                   9    
HELIX  103 103 ASP F  264  ALA F  273  1                                  10    
HELIX  104 104 PRO F  274  ALA F  276  5                                   3    
HELIX  105 105 ASN F  278  LEU F  288  1                                  11    
HELIX  106 106 GLY G   13  HIS G   17  5                                   5    
HELIX  107 107 PRO G   18  ILE G   23  1                                   6    
HELIX  108 108 ILE G   36  ALA G   46  1                                  11    
HELIX  109 109 ASP G   59  GLY G   68  1                                  10    
HELIX  110 110 GLY G   70  GLY G   74  5                                   5    
HELIX  111 111 GLY G   87  ALA G   89  5                                   3    
HELIX  112 112 GLN G   90  GLY G   95  1                                   6    
HELIX  113 113 GLY G   95  GLY G  100  1                                   6    
HELIX  114 114 ASP G  117  GLN G  127  1                                  11    
HELIX  115 115 ASP G  141  ARG G  144  5                                   4    
HELIX  116 116 GLN G  181  ASP G  188  1                                   8    
HELIX  117 117 GLU G  198  ARG G  209  1                                  12    
HELIX  118 118 THR G  228  GLY G  247  1                                  20    
HELIX  119 119 CYS G  252  GLN G  260  1                                   9    
HELIX  120 120 ASP G  264  ALA G  273  1                                  10    
HELIX  121 121 PRO G  274  ALA G  276  5                                   3    
HELIX  122 122 ASN G  278  LEU G  288  1                                  11    
HELIX  123 123 GLY H   13  HIS H   17  5                                   5    
HELIX  124 124 SER H   24  LEU H   27  5                                   4    
HELIX  125 125 ILE H   36  ALA H   46  1                                  11    
HELIX  126 126 ASP H   59  GLY H   68  1                                  10    
HELIX  127 127 GLY H   70  GLY H   74  5                                   5    
HELIX  128 128 GLY H   87  ALA H   89  5                                   3    
HELIX  129 129 GLN H   90  GLY H   95  1                                   6    
HELIX  130 130 GLY H   95  GLY H  100  1                                   6    
HELIX  131 131 ASP H  117  GLN H  127  1                                  11    
HELIX  132 132 ASP H  141  ARG H  144  5                                   4    
HELIX  133 133 GLN H  181  LEU H  189  1                                   9    
HELIX  134 134 GLU H  198  ARG H  209  1                                  12    
HELIX  135 135 THR H  228  GLY H  247  1                                  20    
HELIX  136 136 CYS H  252  GLN H  260  1                                   9    
HELIX  137 137 ASP H  264  ALA H  273  1                                  10    
HELIX  138 138 PRO H  274  ALA H  276  5                                   3    
HELIX  139 139 ASN H  278  LEU H  288  1                                  11    
SHEET    1   A 7 LEU A 212  ILE A 216  0                                        
SHEET    2   A 7 ALA A 132  HIS A 138  1  O  ALA A 132   N  SER A 213           
SHEET    3   A 7 TYR A 170  TYR A 178 -1  N  ALA A 171   O  TYR A 137           
SHEET    4   A 7 LEU A 103  LEU A 108 -1  O  SER A 104   N  TYR A 178           
SHEET    5   A 7 ARG A   3  LEU A   8  1  N  LYS A   4   O  LEU A 103           
SHEET    6   A 7 GLU A  50  SER A  55  1  O  GLU A  50   N  GLY A   5           
SHEET    7   A 7 ASP A  76  VAL A  81  1  O  ASP A  76   N  ILE A  51           
SHEET    1   B 5 LEU A 212  ILE A 216  0                                        
SHEET    2   B 5 ALA A 132  HIS A 138  1  O  ALA A 132   N  SER A 213           
SHEET    3   B 5 TYR A 170  TYR A 178 -1  N  ALA A 171   O  TYR A 137           
SHEET    4   B 5 GLY A 146  PHE A 150 -1  O  GLY A 146   N  VAL A 172           
SHEET    5   B 5 ALA A 156  GLU A 161 -1  N  ILE A 157   O  GLU A 149           
SHEET    1   C 2 PRO A  29  VAL A  30  0                                        
SHEET    2   C 2 LYS A  33  PRO A  34 -1  O  LYS A  33   N  VAL A  30           
SHEET    1   D 2 ASN A 111  TYR A 114  0                                        
SHEET    2   D 2 ALA A 222  ASP A 225 -1  N  ALA A 222   O  TYR A 114           
SHEET    1   E 7 LEU B 212  ILE B 216  0                                        
SHEET    2   E 7 ALA B 132  HIS B 138  1  O  ALA B 132   N  SER B 213           
SHEET    3   E 7 TYR B 170  TYR B 178 -1  N  ALA B 171   O  TYR B 137           
SHEET    4   E 7 LEU B 103  LEU B 108 -1  O  SER B 104   N  TYR B 178           
SHEET    5   E 7 ARG B   3  LEU B   8  1  N  LYS B   4   O  LEU B 103           
SHEET    6   E 7 GLU B  50  SER B  55  1  O  GLU B  50   N  GLY B   5           
SHEET    7   E 7 ASP B  76  VAL B  81  1  O  ASP B  76   N  ILE B  51           
SHEET    1   F 5 LEU B 212  ILE B 216  0                                        
SHEET    2   F 5 ALA B 132  HIS B 138  1  O  ALA B 132   N  SER B 213           
SHEET    3   F 5 TYR B 170  TYR B 178 -1  N  ALA B 171   O  TYR B 137           
SHEET    4   F 5 GLY B 146  PHE B 150 -1  O  GLY B 146   N  VAL B 172           
SHEET    5   F 5 ALA B 156  GLU B 161 -1  N  ILE B 157   O  GLU B 149           
SHEET    1   G 2 PRO B  29  VAL B  30  0                                        
SHEET    2   G 2 LYS B  33  PRO B  34 -1  O  LYS B  33   N  VAL B  30           
SHEET    1   H 2 ASN B 111  TYR B 114  0                                        
SHEET    2   H 2 ALA B 222  ASP B 225 -1  N  ALA B 222   O  TYR B 114           
SHEET    1   I 7 LEU C 212  ILE C 216  0                                        
SHEET    2   I 7 ALA C 132  HIS C 138  1  O  ALA C 132   N  SER C 213           
SHEET    3   I 7 TYR C 170  TYR C 178 -1  N  ALA C 171   O  TYR C 137           
SHEET    4   I 7 LEU C 103  LEU C 108 -1  N  SER C 104   O  TYR C 178           
SHEET    5   I 7 ARG C   3  LEU C   8  1  N  LYS C   4   O  LEU C 103           
SHEET    6   I 7 GLU C  50  SER C  55  1  O  GLU C  50   N  GLY C   5           
SHEET    7   I 7 ASP C  76  VAL C  81  1  O  ASP C  76   N  ILE C  51           
SHEET    1   J 5 LEU C 212  ILE C 216  0                                        
SHEET    2   J 5 ALA C 132  HIS C 138  1  O  ALA C 132   N  SER C 213           
SHEET    3   J 5 TYR C 170  TYR C 178 -1  N  ALA C 171   O  TYR C 137           
SHEET    4   J 5 GLY C 146  PHE C 150 -1  O  GLY C 146   N  VAL C 172           
SHEET    5   J 5 ALA C 156  GLU C 161 -1  N  ILE C 157   O  GLU C 149           
SHEET    1   K 2 PRO C  29  VAL C  30  0                                        
SHEET    2   K 2 LYS C  33  PRO C  34 -1  O  LYS C  33   N  VAL C  30           
SHEET    1   L 2 ASN C 111  TYR C 114  0                                        
SHEET    2   L 2 ALA C 222  ASP C 225 -1  N  ALA C 222   O  TYR C 114           
SHEET    1   M 7 LEU D 212  ILE D 216  0                                        
SHEET    2   M 7 ALA D 132  HIS D 138  1  O  ALA D 132   N  SER D 213           
SHEET    3   M 7 TYR D 170  TYR D 178 -1  N  ALA D 171   O  TYR D 137           
SHEET    4   M 7 LEU D 103  LEU D 108 -1  N  SER D 104   O  TYR D 178           
SHEET    5   M 7 ARG D   3  LEU D   8  1  N  LYS D   4   O  LEU D 103           
SHEET    6   M 7 GLU D  50  SER D  55  1  O  GLU D  50   N  GLY D   5           
SHEET    7   M 7 ASP D  76  VAL D  81  1  O  ASP D  76   N  ILE D  51           
SHEET    1   N 5 LEU D 212  ILE D 216  0                                        
SHEET    2   N 5 ALA D 132  HIS D 138  1  O  ALA D 132   N  SER D 213           
SHEET    3   N 5 TYR D 170  TYR D 178 -1  N  ALA D 171   O  TYR D 137           
SHEET    4   N 5 GLY D 146  PHE D 150 -1  O  GLY D 146   N  VAL D 172           
SHEET    5   N 5 ALA D 156  GLU D 161 -1  N  ILE D 157   O  GLU D 149           
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 3 LEU E 212  ILE E 216  0                                        
SHEET    2   Q 3 ALA E 132  HIS E 138  1  O  ALA E 132   N  SER E 213           
SHEET    3   Q 3 TYR E 170  VAL E 172 -1  N  ALA E 171   O  TYR E 137           
SHEET    1   R 7 LEU E 212  ILE E 216  0                                        
SHEET    2   R 7 ALA E 132  HIS E 138  1  O  ALA E 132   N  SER E 213           
SHEET    3   R 7 LEU E 175  TYR E 178 -1  N  PHE E 177   O  SER E 133           
SHEET    4   R 7 LEU E 103  LEU E 108 -1  N  SER E 104   O  TYR E 178           
SHEET    5   R 7 ARG E   3  LEU E   8  1  N  LYS E   4   O  LEU E 103           
SHEET    6   R 7 GLU E  50  SER E  55  1  O  GLU E  50   N  GLY E   5           
SHEET    7   R 7 ASP E  76  VAL E  81  1  O  ASP E  76   N  ILE E  51           
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 LEU F 212  ILE F 216  0                                        
SHEET    2   V 7 ALA F 132  HIS F 138  1  O  ALA F 132   N  SER F 213           
SHEET    3   V 7 TYR F 170  TYR F 178 -1  N  ALA F 171   O  TYR F 137           
SHEET    4   V 7 LEU F 103  LEU F 108 -1  O  SER F 104   N  TYR F 178           
SHEET    5   V 7 ARG F   3  LEU F   8  1  N  LYS F   4   O  LEU F 103           
SHEET    6   V 7 GLU F  50  SER F  55  1  O  GLU F  50   N  GLY F   5           
SHEET    7   V 7 ASP F  76  VAL F  81  1  O  ASP F  76   N  ILE F  51           
SHEET    1   W 5 LEU F 212  ILE F 216  0                                        
SHEET    2   W 5 ALA F 132  HIS F 138  1  O  ALA F 132   N  SER F 213           
SHEET    3   W 5 TYR F 170  TYR F 178 -1  N  ALA F 171   O  TYR F 137           
SHEET    4   W 5 GLY F 146  PHE F 150 -1  O  GLY F 146   N  VAL F 172           
SHEET    5   W 5 ALA F 156  GLU F 161 -1  N  ILE F 157   O  GLU F 149           
SHEET    1   X 2 PRO F  29  VAL F  30  0                                        
SHEET    2   X 2 LYS F  33  PRO F  34 -1  O  LYS F  33   N  VAL F  30           
SHEET    1   Y 2 ASN F 111  TYR F 114  0                                        
SHEET    2   Y 2 ALA F 222  ASP F 225 -1  N  ALA F 222   O  TYR F 114           
SHEET    1   Z 5 LEU G 212  ILE G 216  0                                        
SHEET    2   Z 5 ALA G 132  HIS G 138  1  O  ALA G 132   N  SER G 213           
SHEET    3   Z 5 TYR G 170  VAL G 172 -1  N  ALA G 171   O  TYR G 137           
SHEET    4   Z 5 GLY G 146  PHE G 150 -1  O  GLY G 146   N  VAL G 172           
SHEET    5   Z 5 ALA G 156  GLU G 161 -1  N  ILE G 157   O  GLU G 149           
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 5 LEU H 212  ILE H 216  0                                        
SHEET    2  AD 5 ALA H 132  HIS H 138  1  O  ALA H 132   N  SER H 213           
SHEET    3  AD 5 TYR H 170  VAL H 172 -1  N  ALA H 171   O  TYR H 137           
SHEET    4  AD 5 GLY H 146  PHE H 150 -1  O  GLY H 146   N  VAL H 172           
SHEET    5  AD 5 ALA H 156  GLU H 161 -1  N  ILE H 157   O  GLU H 149           
SHEET    1  AE 7 LEU H 212  ILE H 216  0                                        
SHEET    2  AE 7 ALA H 132  HIS H 138  1  O  ALA H 132   N  SER H 213           
SHEET    3  AE 7 LEU H 175  TYR H 178 -1  N  PHE H 177   O  SER H 133           
SHEET    4  AE 7 LEU H 103  LEU H 108 -1  O  SER H 104   N  TYR H 178           
SHEET    5  AE 7 ARG H   3  LEU H   8  1  N  LYS H   4   O  LEU H 103           
SHEET    6  AE 7 GLU H  50  SER H  55  1  O  GLU H  50   N  GLY H   5           
SHEET    7  AE 7 ASP H  76  VAL H  81  1  O  ASP H  76   N  ILE H  51           
SHEET    1  AF 2 PRO H  29  VAL H  30  0                                        
SHEET    2  AF 2 LYS H  33  PRO H  34 -1  O  LYS H  33   N  VAL H  30           
SHEET    1  AG 2 ASN H 111  TYR H 114  0                                        
SHEET    2  AG 2 ALA H 222  ASP H 225 -1  N  ALA H 222   O  TYR H 114           
LINK         NE  ARG H  62                 O3  SO4 H3814     1555   1555  1.96  
CISPEP   1 HIS A   17    PRO A   18          0         1.72                     
CISPEP   2 HIS B   17    PRO B   18          0        -2.11                     
CISPEP   3 HIS C   17    PRO C   18          0         5.73                     
CISPEP   4 HIS D   17    PRO D   18          0         1.29                     
CISPEP   5 HIS E   17    PRO E   18          0        -2.71                     
CISPEP   6 HIS F   17    PRO F   18          0        -1.50                     
CISPEP   7 HIS G   17    PRO G   18          0        -1.50                     
CISPEP   8 HIS H   17    PRO H   18          0        -1.61                     
SITE     1 AC1  6 SER A  12  GLY A  13  THR A  14  ARG A  15                    
SITE     2 AC1  6 LYS A  25  HOH A4062                                          
SITE     1 AC2 10 SER B  12  GLY B  13  THR B  14  ARG B  15                    
SITE     2 AC2 10 LYS B  25  HOH B3986  HOH B4080  HOH B4153                    
SITE     3 AC2 10 HOH B4203  HOH B4205                                          
SITE     1 AC3 10 SER G  12  GLY G  13  THR G  14  ARG G  15                    
SITE     2 AC3 10 LYS G  25  HOH G3946  HOH G4117  HOH G4139                    
SITE     3 AC3 10 HOH G4157  HOH G4204                                          
SITE     1 AC4  4 SER H  12  GLY H  13  THR H  14  ARG H  15                    
SITE     1 AC5  4 ARG A  62  HOH A3985  ARG B  62  HOH C4051                    
SITE     1 AC6  7 ARG A 128  GLU A 215  HOH A4030  HOH A4084                    
SITE     2 AC6  7 ASP F 151  GLN F 152  HOH F4059                               
SITE     1 AC7  7 GLU B 160  GLU B 161  ARG B 194  ARG B 204                    
SITE     2 AC7  7 HOH B3899  HOH B3925  HOH B4108                               
SITE     1 AC8  6 HOH B4118  ARG C  62  HOH C3935  HOH C4021                    
SITE     2 AC8  6 ARG D  62  HOH D3955                                          
SITE     1 AC9  4 GLN C 127  ARG C 128  GLN C 129  THR C 130                    
SITE     1 BC1  4 GLN D 127  ARG D 128  GLN D 129  THR D 130                    
SITE     1 BC2  3 ARG E  62  HOH E3885  ARG F  62                               
SITE     1 BC3  5 GLN E 127  ARG E 128  GLN E 129  THR E 130                    
SITE     2 BC3  5 HOH E3980                                                     
SITE     1 BC4  6 ARG B 128  GLU B 215  ASP E 151  GLN E 152                    
SITE     2 BC4  6 HOH E3989  HOH E3990                                          
SITE     1 BC5  2 GLN F 129  THR F 130                                          
SITE     1 BC6  8 ASP C 151  GLN C 152  HOH C4014  HOH C4093                    
SITE     2 BC6  8 ARG G 128  GLU G 215  HOH G3951  HOH G4101                    
SITE     1 BC7  7 GLU G 160  GLU G 161  ARG G 194  ARG G 204                    
SITE     2 BC7  7 HOH G3880  HOH G3941  HOH G4134                               
SITE     1 BC8  2 ARG G  62  ARG H  62                                          
SITE     1 BC9  8 ASP D 151  GLN D 152  HOH D3943  HOH D3949                    
SITE     2 BC9  8 HOH D4074  ARG H 128  GLU H 215  HOH H3892                    
SITE     1 CC1  5 GLU H 160  GLU H 161  ARG H 204  HOH H3919                    
SITE     2 CC1  5 HOH H4149                                                     
SITE     1 CC2  9 GLU A 160  GLU A 161  ARG A 194  ARG A 204                    
SITE     2 CC2  9 HOH A3908  HOH A3914  HOH A3992  HOH A4201                    
SITE     3 CC2  9 HOH B4183                                                     
SITE     1 CC3  9 HIS A 116  DAU A3501  HOH A3829  HOH A3921                    
SITE     2 CC3  9 HOH A3927  HOH A3997  LEU C 121  TYR C 221                    
SITE     3 CC3  9 HOH C3905                                                     
SITE     1 CC4  7 LEU B 121  TYR B 221  HOH B3816  HIS D 116                    
SITE     2 CC4  7 DAU D3507  HOH D3892  HOH D3933                               
SITE     1 CC5  8 HIS E 116  DAU E3509  HOH E3831  HOH E3894                    
SITE     2 CC5  8 HOH E4034  LEU H 121  TYR H 221  HOH H3871                    
SITE     1 CC6 25 LEU A   8  GLY A  10  GLY A  11  GLN A  26                    
SITE     2 CC6 25 GLN A  82  PRO A  85  ASP A  86  GLY A  87                    
SITE     3 CC6 25 LEU A  88  LEU A 108  GLY A 109  ASP A 110                    
SITE     4 CC6 25 ASN A 111  TYR A 145  GLY A 146  GLU A 161                    
SITE     5 CC6 25 LYS A 162  VAL A 172  GLU A 196  THR A 200                    
SITE     6 CC6 25 HOH A3819  HOH A3904  HOH A4168  HOH A4203                    
SITE     7 CC6 25 HOH A4224                                                     
SITE     1 CC7 28 LEU A  45  TYR A 114  GLY A 115  HIS A 116                    
SITE     2 CC7 28 ASP A 117  PHE A 118  HIS A 119  GLU A 120                    
SITE     3 CC7 28 VAL A 250  ALA A 251  GLU A 255  ILE A 256                    
SITE     4 CC7 28 ARG A 259  TYR A 293  SO4 A3818  HOH A3839                    
SITE     5 CC7 28 HOH A3847  HOH A3850  HOH A3862  HOH A3900                    
SITE     6 CC7 28 HOH A3927  HOH A4023  HOH A4049  HOH A4184                    
SITE     7 CC7 28 ILE C 216  GLY C 218  ARG C 219  GLY C 220                    
SITE     1 CC8 27 LEU B   8  GLY B  10  GLY B  11  ARG B  15                    
SITE     2 CC8 27 GLN B  26  GLN B  82  PRO B  85  ASP B  86                    
SITE     3 CC8 27 GLY B  87  LEU B  88  LEU B 108  GLY B 109                    
SITE     4 CC8 27 ASP B 110  ASN B 111  TYR B 145  GLY B 146                    
SITE     5 CC8 27 GLU B 161  LYS B 162  VAL B 172  THR B 200                    
SITE     6 CC8 27 HOH B3832  HOH B3856  HOH B3915  HOH B3969                    
SITE     7 CC8 27 HOH B4199  HOH B4200  HOH B4201                               
SITE     1 CC9 25 LEU B  45  TYR B 114  GLY B 115  HIS B 116                    
SITE     2 CC9 25 ASP B 117  PHE B 118  HIS B 119  GLU B 120                    
SITE     3 CC9 25 VAL B 250  ALA B 251  GLU B 255  ILE B 256                    
SITE     4 CC9 25 TYR B 293  HOH B3817  HOH B3826  HOH B3835                    
SITE     5 CC9 25 HOH B3863  HOH B3876  HOH B3887  HOH B3971                    
SITE     6 CC9 25 HOH B4112  ILE D 216  GLY D 218  ARG D 219                    
SITE     7 CC9 25 GLY D 220                                                     
SITE     1 DC1 28 LEU C   8  GLY C  10  GLY C  11  LYS C  25                    
SITE     2 DC1 28 GLN C  26  GLN C  82  PRO C  85  ASP C  86                    
SITE     3 DC1 28 GLY C  87  LEU C  88  LEU C 108  GLY C 109                    
SITE     4 DC1 28 ASP C 110  ASN C 111  TYR C 145  GLY C 146                    
SITE     5 DC1 28 GLU C 161  LYS C 162  VAL C 172  THR C 200                    
SITE     6 DC1 28 HOH C3814  HOH C3852  HOH C3977  HOH C4121                    
SITE     7 DC1 28 HOH C4146  HOH C4147  HOH C4149  HOH C4154                    
SITE     1 DC2 24 ILE A 216  GLY A 218  ARG A 219  GLY A 220                    
SITE     2 DC2 24 LEU C  45  TYR C 114  GLY C 115  HIS C 116                    
SITE     3 DC2 24 ASP C 117  PHE C 118  HIS C 119  GLU C 120                    
SITE     4 DC2 24 VAL C 250  ALA C 251  GLU C 255  ILE C 256                    
SITE     5 DC2 24 ARG C 259  TYR C 293  HOH C3810  HOH C3826                    
SITE     6 DC2 24 HOH C3832  HOH C3850  HOH C3880  HOH C3979                    
SITE     1 DC3 25 LEU D   8  GLY D  10  GLY D  11  LYS D  25                    
SITE     2 DC3 25 GLN D  26  GLN D  82  PRO D  85  ASP D  86                    
SITE     3 DC3 25 GLY D  87  LEU D  88  LEU D 108  ASP D 110                    
SITE     4 DC3 25 ASN D 111  TYR D 145  GLY D 146  GLU D 161                    
SITE     5 DC3 25 LYS D 162  VAL D 172  GLU D 196  THR D 200                    
SITE     6 DC3 25 HOH D3820  HOH D3958  HOH D3988  HOH D4107                    
SITE     7 DC3 25 HOH D4108                                                     
SITE     1 DC4 26 ILE B 216  GLY B 218  ARG B 219  GLY B 220                    
SITE     2 DC4 26 LEU D  45  TYR D 114  GLY D 115  HIS D 116                    
SITE     3 DC4 26 ASP D 117  PHE D 118  HIS D 119  GLU D 120                    
SITE     4 DC4 26 VAL D 250  ALA D 251  GLU D 255  ILE D 256                    
SITE     5 DC4 26 ARG D 259  TYR D 293  SO4 D3819  HOH D3827                    
SITE     6 DC4 26 HOH D3833  HOH D3840  HOH D3857  HOH D3886                    
SITE     7 DC4 26 HOH D3892  HOH D3940                                          
SITE     1 DC5 24 LEU E   8  GLY E  10  GLY E  11  LYS E  25                    
SITE     2 DC5 24 GLN E  26  GLN E  82  PRO E  85  ASP E  86                    
SITE     3 DC5 24 GLY E  87  LEU E  88  LEU E 108  ASP E 110                    
SITE     4 DC5 24 ASN E 111  TYR E 145  GLY E 146  GLU E 161                    
SITE     5 DC5 24 LYS E 162  VAL E 172  GLU E 196  THR E 200                    
SITE     6 DC5 24 HOH E3825  HOH E4126  HOH E4127  HOH E4128                    
SITE     1 DC6 24 LEU E  45  TYR E 114  GLY E 115  HIS E 116                    
SITE     2 DC6 24 ASP E 117  PHE E 118  HIS E 119  GLU E 120                    
SITE     3 DC6 24 VAL E 250  ALA E 251  GLU E 255  ILE E 256                    
SITE     4 DC6 24 TYR E 293  SO4 E3820  HOH E3827  HOH E3832                    
SITE     5 DC6 24 HOH E3833  HOH E3873  HOH E3894  HOH E3937                    
SITE     6 DC6 24 ILE H 216  GLY H 218  ARG H 219  GLY H 220                    
SITE     1 DC7 28 LEU F   8  GLY F  10  GLY F  11  LYS F  25                    
SITE     2 DC7 28 GLN F  26  GLN F  82  PRO F  85  ASP F  86                    
SITE     3 DC7 28 GLY F  87  LEU F  88  LEU F 108  ASP F 110                    
SITE     4 DC7 28 ASN F 111  TYR F 145  GLY F 146  GLU F 161                    
SITE     5 DC7 28 LYS F 162  VAL F 172  ARG F 194  GLU F 196                    
SITE     6 DC7 28 THR F 200  TRP F 223  HOH F3828  HOH F3922                    
SITE     7 DC7 28 HOH F3990  HOH F4001  HOH F4118  HOH F4119                    
SITE     1 DC8 23 LEU F  45  TYR F 114  GLY F 115  HIS F 116                    
SITE     2 DC8 23 ASP F 117  PHE F 118  HIS F 119  GLU F 120                    
SITE     3 DC8 23 VAL F 250  ALA F 251  GLU F 255  ILE F 256                    
SITE     4 DC8 23 TYR F 293  HOH F3818  HOH F3826  HOH F3832                    
SITE     5 DC8 23 HOH F3876  HOH F3878  HOH F3926  ILE G 216                    
SITE     6 DC8 23 GLY G 218  ARG G 219  GLY G 220                               
SITE     1 DC9 24 LEU H   8  GLY H  10  GLY H  11  GLN H  26                    
SITE     2 DC9 24 GLN H  82  PRO H  85  ASP H  86  GLY H  87                    
SITE     3 DC9 24 LEU H  88  LEU H 108  ASP H 110  ASN H 111                    
SITE     4 DC9 24 TYR H 145  GLY H 146  GLU H 161  LYS H 162                    
SITE     5 DC9 24 VAL H 172  THR H 200  HOH H3825  HOH H3884                    
SITE     6 DC9 24 HOH H4002  HOH H4068  HOH H4139  HOH H4193                    
SITE     1 EC1 27 ILE E 216  GLY E 218  ARG E 219  GLY E 220                    
SITE     2 EC1 27 LEU H  45  TYR H 114  GLY H 115  HIS H 116                    
SITE     3 EC1 27 ASP H 117  PHE H 118  HIS H 119  GLU H 120                    
SITE     4 EC1 27 VAL H 250  ALA H 251  GLU H 255  ILE H 256                    
SITE     5 EC1 27 ARG H 259  TYR H 293  HOH H3832  HOH H3835                    
SITE     6 EC1 27 HOH H3851  HOH H3905  HOH H3908  HOH H3914                    
SITE     7 EC1 27 HOH H3949  HOH H3952  HOH H4076                               
SITE     1 EC2 28 LEU G   8  GLY G  10  GLY G  11  GLN G  26                    
SITE     2 EC2 28 GLN G  82  PRO G  85  ASP G  86  GLY G  87                    
SITE     3 EC2 28 LEU G  88  LEU G 108  GLY G 109  ASP G 110                    
SITE     4 EC2 28 ASN G 111  TYR G 145  GLY G 146  GLU G 161                    
SITE     5 EC2 28 LYS G 162  VAL G 172  THR G 200  HOH G3827                    
SITE     6 EC2 28 HOH G3895  HOH G3902  HOH G3965  HOH G3990                    
SITE     7 EC2 28 HOH G4052  HOH G4117  HOH G4126  HOH G4157                    
SITE     1 EC3 26 ILE F 216  GLY F 218  ARG F 219  GLY F 220                    
SITE     2 EC3 26 LEU G  45  TYR G 114  GLY G 115  HIS G 116                    
SITE     3 EC3 26 ASP G 117  PHE G 118  HIS G 119  GLU G 120                    
SITE     4 EC3 26 VAL G 250  ALA G 251  GLU G 255  ILE G 256                    
SITE     5 EC3 26 ARG G 259  TYR G 293  HOH G3823  HOH G3829                    
SITE     6 EC3 26 HOH G3856  HOH G3879  HOH G3891  HOH G3907                    
SITE     7 EC3 26 HOH G3997  HOH G4142                                          
SITE     1 EC4  9 TYR A  31  LYS A 249  GLY A 279  HOH A3955                    
SITE     2 EC4  9 HOH A4205  HOH A4206  HOH A4221  ARG B  15                    
SITE     3 EC4  9 HIS B 229                                                     
SITE     1 EC5 12 HIS A 229  HOH A3905  HOH A3912  HOH A4063                    
SITE     2 EC5 12 HOH A4214  HOH A4215  HOH A4216  HOH A4217                    
SITE     3 EC5 12 TYR B  31  ASP B  32  LYS B 249  GLY B 279                    
CRYST1   71.575   73.410  134.290  89.94  80.61  80.93 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      0.013971 -0.002230 -0.002367        0.00000                         
SCALE2      0.000000  0.013795  0.000350        0.00000                         
SCALE3      0.000000  0.000000  0.007550        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system