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Database: PDB
Entry: 1G0R
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HEADER    TRANSFERASE                             07-OCT-00   1G0R              
TITLE     THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF     
TITLE    2 GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). THYMIDINE/GLUCOSE- 
TITLE    3 1-PHOSPHATE 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: PET23(+)                                  
KEYWDS    L-RHAMNOSE, NUCLEOTIDYLTRANSFERASE, PYROPHOSPHORYLASE,                
KEYWDS   2 THYMIDYLYLTRANSFERASE, ALLOSTERY, TRANSFERASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.BLANKENFELDT,M.ASUNCION,J.S.LAM,J.H.NAISMITH                        
REVDAT   5   29-JUL-20 1G0R    1       COMPND REMARK HETNAM SITE                
REVDAT   4   13-JUL-11 1G0R    1       VERSN                                    
REVDAT   3   24-FEB-09 1G0R    1       VERSN                                    
REVDAT   2   01-APR-03 1G0R    1       JRNL                                     
REVDAT   1   27-DEC-00 1G0R    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 CHARACTERISATION 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.    1.87 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.87                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 73.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 174042                         
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) : 0.151                           
REMARK   3   R VALUE            (WORKING SET) : 0.147                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9145                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 18288                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 499                                     
REMARK   3   SOLVENT ATOMS            : 2236                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.69000                                             
REMARK   3    B22 (A**2) : 0.70000                                              
REMARK   3    B33 (A**2) : -0.22000                                             
REMARK   3    B12 (A**2) : -0.01000                                             
REMARK   3    B13 (A**2) : 0.71000                                              
REMARK   3    B23 (A**2) : 0.20000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.211         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.165         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.813        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: INITIAL TLS-REFINEMENT. ANISOTROPIC B     
REMARK   3  -VALUES CALCULATED BUT NOT REFINED                                  
REMARK   4                                                                      
REMARK   4 1G0R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000012089.                                   
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) : 100.0                              
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   : 183207                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.870                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 72.550                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.7                               
REMARK 200  DATA REDUNDANCY                : 1.800                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 66.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29100                            
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   (%): 53.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 9-11% (W/V) PEG 6000 0.5 M LITHIUM       
REMARK 280  SULFATE COCRYSTALLISATION WITH LIGANDS, PH 4.6, VAPOR DIFFUSION,    
REMARK 280  SITTING DROP, TEMPERATURE 292K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER THAT CAN BE DESCRIBED  
REMARK 300 AS A 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: PQS                                                   
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: PQS                                                   
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 B     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   O    HOH A  2720     O    HOH B  2700              2.04            
REMARK 500   O    HOH D  2774     O    HOH D  2777              2.04            
REMARK 500   O2   SO4 A  2507     O    HOH A  2824              2.05            
REMARK 500   O    HOH D  2707     O    HOH D  2717              2.07            
REMARK 500   O    HOH C  2658     O    HOH D  2649              2.08            
REMARK 500   O    HOH C  2572     O    HOH C  2700              2.09            
REMARK 500   O    HOH G  2749     O    HOH G  2795              2.10            
REMARK 500   NZ   LYS A     2     OE1  GLU A    50              2.10            
REMARK 500   O2   SO4 H  2518     O    HOH H  2671              2.11            
REMARK 500   O    HOH B  2634     O    HOH B  2797              2.11            
REMARK 500   O    HOH G  2861     O    HOH G  2865              2.12            
REMARK 500   O    HOH E  2622     O    HOH E  2734              2.12            
REMARK 500   O    HOH A  2611     O    HOH A  2757              2.13            
REMARK 500   O    PRO H    85     O    HOH H  2780              2.14            
REMARK 500   O    HOH A  2612     O    HOH B  2684              2.14            
REMARK 500   OE1  GLN E    65     O    HOH E  2742              2.15            
REMARK 500   O4   SO4 H  2526     O    HOH H  2826              2.15            
REMARK 500   O    HOH F  2706     O    HOH F  2802              2.15            
REMARK 500   O    HOH D  2747     O    HOH D  2794              2.16            
REMARK 500   O    HOH A  2734     O    HOH A  2786              2.18            
REMARK 500   OG   SER F    24     OD2  ASP F    59              2.18            
REMARK 500   CB   ASP B   141     O    HOH B  2787              2.18            
REMARK 500   OD1  ASP G   141     O    HOH G  2681              2.19            
REMARK 500   O    HOH C  2613     O    HOH C  2672              2.19            
REMARK 500   O    HOH H  2755     O    HOH H  2783              2.19            
REMARK 500   O    HOH C  2640     O    HOH C  2726              2.19            
REMARK 500   NZ   LYS C   270     O    HOH C  2679              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 A  37   CE1   TYR A  37   CZ     -0.079                       
REMARK 500    CYS A 252   CB    CYS A 252   SG     -0.109                       
REMARK 500    VAL B 183   CB    VAL B 183   CG2    -0.143                       
REMARK 500    TYR B 206   CD1   TYR B 206   CE1    -0.091                       
REMARK 500    CYS B 252   CB    CYS B 252   SG     -0.099                       
REMARK 500    TYR B 280   CZ    TYR B 280   CE2    -0.082                       
REMARK 500    SER C  55   CB    SER C  55   OG      0.107                       
REMARK 500    TYR C 137   CD1   TYR C 137   CE1    -0.127                       
REMARK 500    TRP C 223   CE3   TRP C 223   CZ3    -0.128                       
REMARK 500    TYR D 114   CG    TYR D 114   CD1    -0.131                       
REMARK 500    TYR D 114   CE1   TYR D 114   CZ     -0.095                       
REMARK 500    TYR E 178   CG    TYR E 178   CD2    -0.086                       
REMARK 500    VAL F  81   CB    VAL F  81   CG1    -0.193                       
REMARK 500    GLU F 208   CD    GLU F 208   OE1    -0.076                       
REMARK 500    PHE F 238   CE2   PHE F 238   CD2     0.124                       
REMARK 500    CYS F 252   CB    CYS F 252   SG     -0.098                       
REMARK 500    TYR F 283   CE2   TYR F 283   CD2    -0.096                       
REMARK 500    GLN G  58   CB    GLN G  58   CG     -0.162                       
REMARK 500    TYR G 113   CE2   TYR G 113   CD2    -0.094                       
REMARK 500    ARG G 128   CB    ARG G 128   CG     -0.165                       
REMARK 500    VAL G 134   CB    VAL G 134   CG1    -0.139                       
REMARK 500    TYR G 206   CE1   TYR G 206   CZ      0.097                       
REMARK 500    CYS G 252   CB    CYS G 252   SG     -0.108                       
REMARK 500    TYR G 258   CD1   TYR G 258   CE1    -0.091                       
REMARK 500    TYR H  79   CE2   TYR H  79   CD2    -0.096                       
REMARK 500    TYR H 113   CE1   TYR H 113   CZ     -0.081                       
REMARK 500    VAL H 134   CB    VAL H 134   CG2    -0.148                       
REMARK 500    TYR H 170   CD1   TYR H 170   CE1    -0.095                       
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. =   5.9 DEGREES          
REMARK 500    ASP A  86   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    GLU A 120   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    ASP A 151   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 188   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG A 209   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ASP B  59   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B  69   CB  -  CG  -  OD1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG B 128   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG B 128   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ASP B 151   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP B 184   CB  -  CG  -  OD1 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG B 209   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG C   3   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG C   3   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ASP C  69   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP C  76   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP C 110   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP C 188   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP C 201   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG C 245   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP C 264   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ASP D 102   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP D 117   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP D 188   CB  -  CG  -  OD2 ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ASP D 201   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG D 204   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ASP E  32   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP E 151   CB  -  CG  -  OD1 ANGL. DEV. =   8.6 DEGREES          
REMARK 500    SER F  24   N   -  CA  -  CB  ANGL. DEV. = -11.0 DEGREES          
REMARK 500    ASP F 102   CB  -  CG  -  OD2 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    LEU F 197   CB  -  CG  -  CD2 ANGL. DEV. =  11.2 DEGREES          
REMARK 500    ASP F 230   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG G  15   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    LEU G  27   CB  -  CG  -  CD2 ANGL. DEV. = -10.3 DEGREES          
REMARK 500    LEU G  28   CB  -  CG  -  CD2 ANGL. DEV. = -11.3 DEGREES          
REMARK 500    MET G  35   CB  -  CG  -  SD  ANGL. DEV. = -30.5 DEGREES          
REMARK 500    ASP G  86   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ASP G 110   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG G 128   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG G 128   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ASP G 141   CB  -  CG  -  OD2 ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ASP G 151   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG G 209   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG G 209   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ASP G 264   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP H 117   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG H 128   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG H 128   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ASP H 151   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      51 ANGLE DEVIATIONS.                             
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    HIS A  17      135.63    -37.91                                   
REMARK 500    TYR A  31      -75.81     73.59                                   
REMARK 500    THR A 226       36.70    -97.49                                   
REMARK 500    ILE B  23      175.22    179.91                                   
REMARK 500    TYR B  31      -82.06     65.74                                   
REMARK 500    ARG C  15      -73.34    -52.03                                   
REMARK 500    HIS C  17      146.60    -39.71                                   
REMARK 500    TYR C  31      -79.97     64.68                                   
REMARK 500    ASP C 141       70.54   -117.99                                   
REMARK 500    THR C 226       40.04    -97.76                                   
REMARK 500    THR D  14      -79.00      5.00                                   
REMARK 500    LEU D  16       -3.50    -52.80                                   
REMARK 500    HIS D  17      131.29    -22.39                                   
REMARK 500    TYR D  31      -80.83     66.51                                   
REMARK 500    ALA D  46        0.58    -68.26                                   
REMARK 500    THR D 226       31.43    -87.33                                   
REMARK 500    SER E  12      -59.38    -22.69                                   
REMARK 500    THR E  14      -38.59    -14.87                                   
REMARK 500    TYR E  31      -80.00     63.10                                   
REMARK 500    PRO E  61      -16.14    -47.58                                   
REMARK 500    LYS E 162       57.74     38.16                                   
REMARK 500    THR E 226       42.57   -100.39                                   
REMARK 500    THR F  14      -51.64    -25.18                                   
REMARK 500    ARG F  15      -71.81    -51.39                                   
REMARK 500    TYR F  31      -87.56     62.50                                   
REMARK 500    ASP F 141       67.31   -119.93                                   
REMARK 500    ARG F 194        3.53    -69.56                                   
REMARK 500    ARG F 194        2.89    -69.70                                   
REMARK 500    THR F 226       42.83    -95.36                                   
REMARK 500    TYR G  31      -81.99     64.77                                   
REMARK 500    ALA H  19      -37.93    -35.77                                   
REMARK 500    TYR H  31      -73.85     73.48                                   
REMARK 500    ASN H 101       43.17   -109.32                                   
REMARK 500    THR H 226       40.25    -86.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU D   16     HIS D   17                  145.19                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    HIS D 119         0.10    SIDE CHAIN                              
REMARK 500    HIS E 119         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FXO   RELATED DB: PDB                                   
REMARK 900 1FXO IS RMLA IN COMPLEX WITH TMP                                     
REMARK 900 RELATED ID: 1FZW   RELATED DB: PDB                                   
REMARK 900 1FZW IS RMLA APO-ENZYME                                              
REMARK 900 RELATED ID: 1G1L   RELATED DB: PDB                                   
REMARK 900 1G1L IS RMLA IN COMPLEX WITH 2'-DEOXY-THYMIDINE-ALPHA-D-GLUCOSE      
REMARK 900 (TDG)                                                                
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  1G0R A    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G0R B    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G0R C    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G0R D    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G0R E    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G0R F    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G0R G    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G0R 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    G1P  A2500      16                                                       
HET    SO4  A2507       5                                                       
HET    SO4  A2508       5                                                       
HET    THM  A2530      17                                                       
HET    THM  A2538      17                                                       
HET    G1P  B2501      16                                                       
HET    SO4  B2510       5                                                       
HET    SO4  B2511       5                                                       
HET    SO4  B2528       5                                                       
HET    THM  B2531      17                                                       
HET    THM  B2539      17                                                       
HET    G1P  C2502      16                                                       
HET    SO4  C2509       5                                                       
HET    SO4  C2513       5                                                       
HET    SO4  C2515       5                                                       
HET    THM  C2532      17                                                       
HET    THM  C2540      17                                                       
HET    G1P  D2503      16                                                       
HET    SO4  D2512       5                                                       
HET    SO4  D2514       5                                                       
HET    SO4  D2516       5                                                       
HET    SO4  D2517       5                                                       
HET    THM  D2533      17                                                       
HET    THM  D2541      17                                                       
HET    G1P  E2504      16                                                       
HET    SO4  E2520       5                                                       
HET    SO4  E2527       5                                                       
HET    THM  E2534      17                                                       
HET    THM  E2542      17                                                       
HET    SO4  F2519       5                                                       
HET    SO4  F2521       5                                                       
HET    SO4  F2522       5                                                       
HET    SO4  F2524       5                                                       
HET    THM  F2535      17                                                       
HET    THM  F2543      17                                                       
HET    G1P  G2505      16                                                       
HET    SO4  G2523       5                                                       
HET    SO4  G2525       5                                                       
HET    THM  G2536      17                                                       
HET    THM  G2544      17                                                       
HET    G1P  H2506      16                                                       
HET    SO4  H2518       5                                                       
HET    SO4  H2526       5                                                       
HET    SO4  H2529       5                                                       
HET    THM  H2537      17                                                       
HET    THM  H2545      17                                                       
HETNAM     G1P 1-O-PHOSPHONO-ALPHA-D-GLUCOPYRANOSE                              
HETNAM     SO4 SULFATE ION                                                      
HETNAM     THM THYMIDINE                                                        
HETSYN     THM DEOXYTHYMIDINE; 2'-DEOXYTHYMIDINE                                
FORMUL   9  G1P    7(C6 H13 O9 P)                                               
FORMUL  10  SO4    23(O4 S 2-)                                                  
FORMUL  12  THM    16(C10 H14 N2 O5)                                            
FORMUL  55  HOH   *2236(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 ALA A   89  GLY A   95  1                                   7    
HELIX    8   8 GLY A   95  GLY A  100  1                                   6    
HELIX    9   9 ASP A  117  ARG A  128  1                                  12    
HELIX   10  10 ASP A  141  ARG A  144  5                                   4    
HELIX   11  11 GLN A  181  ASP A  188  1                                   8    
HELIX   12  12 GLU A  198  ARG A  209  1                                  12    
HELIX   13  13 THR A  228  GLY A  247  1                                  20    
HELIX   14  14 CYS A  252  GLN A  260  1                                   9    
HELIX   15  15 ASP A  264  ALA A  273  1                                  10    
HELIX   16  16 PRO A  274  ALA A  276  5                                   3    
HELIX   17  17 ASN A  278  LEU A  287  1                                  10    
HELIX   18  18 PRO B   18  ALA B   22  5                                   5    
HELIX   19  19 ILE B   36  ALA B   46  1                                  11    
HELIX   20  20 ASP B   59  GLY B   68  1                                  10    
HELIX   21  21 GLY B   70  GLY B   74  5                                   5    
HELIX   22  22 ALA B   89  GLY B   95  1                                   7    
HELIX   23  23 GLY B   95  GLY B  100  1                                   6    
HELIX   24  24 ASP B  117  GLN B  127  1                                  11    
HELIX   25  25 ASP B  141  ARG B  144  5                                   4    
HELIX   26  26 GLN B  181  ASP B  188  1                                   8    
HELIX   27  27 GLU B  198  ARG B  209  1                                  12    
HELIX   28  28 THR B  228  GLY B  247  1                                  20    
HELIX   29  29 CYS B  252  GLN B  260  1                                   9    
HELIX   30  30 ASP B  264  ALA B  273  1                                  10    
HELIX   31  31 PRO B  274  ALA B  276  5                                   3    
HELIX   32  32 ASN B  278  LEU B  287  1                                  10    
HELIX   33  33 PRO C   18  ILE C   23  1                                   6    
HELIX   34  34 SER C   24  LEU C   27  5                                   4    
HELIX   35  35 ILE C   36  ALA C   46  1                                  11    
HELIX   36  36 ASP C   59  GLY C   68  1                                  10    
HELIX   37  37 GLY C   70  GLY C   74  5                                   5    
HELIX   38  38 GLY C   87  ALA C   89  5                                   3    
HELIX   39  39 GLN C   90  GLY C   95  1                                   6    
HELIX   40  40 GLY C   95  GLY C  100  1                                   6    
HELIX   41  41 ASP C  117  ARG C  128  1                                  12    
HELIX   42  42 ASP C  141  ARG C  144  5                                   4    
HELIX   43  43 GLN C  181  LEU C  189  1                                   9    
HELIX   44  44 GLU C  198  GLU C  208  1                                  11    
HELIX   45  45 THR C  228  GLY C  247  1                                  20    
HELIX   46  46 CYS C  252  GLN C  260  1                                   9    
HELIX   47  47 ASP C  264  ALA C  273  1                                  10    
HELIX   48  48 PRO C  274  ALA C  276  5                                   3    
HELIX   49  49 ASN C  278  LEU C  288  1                                  11    
HELIX   50  50 SER D   24  LEU D   27  5                                   4    
HELIX   51  51 ILE D   36  ALA D   46  1                                  11    
HELIX   52  52 ASP D   59  GLY D   68  1                                  10    
HELIX   53  53 GLY D   70  GLY D   74  5                                   5    
HELIX   54  54 ALA D   89  GLY D   95  1                                   7    
HELIX   55  55 GLY D   95  GLY D  100  1                                   6    
HELIX   56  56 ASP D  117  ARG D  128  1                                  12    
HELIX   57  57 ASP D  141  ARG D  144  5                                   4    
HELIX   58  58 GLN D  181  LEU D  189  1                                   9    
HELIX   59  59 GLU D  198  GLU D  208  1                                  11    
HELIX   60  60 THR D  228  GLY D  247  1                                  20    
HELIX   61  61 CYS D  252  GLN D  260  1                                   9    
HELIX   62  62 ASP D  264  ALA D  273  1                                  10    
HELIX   63  63 PRO D  274  ALA D  276  5                                   3    
HELIX   64  64 ASN D  278  GLU D  290  1                                  13    
HELIX   65  65 GLY E   13  HIS E   17  5                                   5    
HELIX   66  66 SER E   24  LEU E   27  5                                   4    
HELIX   67  67 ILE E   36  ALA E   46  1                                  11    
HELIX   68  68 ASP E   59  GLY E   68  1                                  10    
HELIX   69  69 GLY E   70  GLY E   74  5                                   5    
HELIX   70  70 GLY E   87  ALA E   89  5                                   3    
HELIX   71  71 GLN E   90  GLY E   95  1                                   6    
HELIX   72  72 GLY E   95  GLY E  100  1                                   6    
HELIX   73  73 ASP E  117  ARG E  128  1                                  12    
HELIX   74  74 ASP E  141  ARG E  144  5                                   4    
HELIX   75  75 GLN E  181  ASP E  188  1                                   8    
HELIX   76  76 GLU E  198  GLU E  208  1                                  11    
HELIX   77  77 THR E  228  GLY E  247  1                                  20    
HELIX   78  78 CYS E  252  GLN E  260  1                                   9    
HELIX   79  79 ASP E  264  ALA E  273  1                                  10    
HELIX   80  80 PRO E  274  ALA E  276  5                                   3    
HELIX   81  81 ASN E  278  LEU E  288  1                                  11    
HELIX   82  82 GLY F   13  HIS F   17  5                                   5    
HELIX   83  83 PRO F   18  ALA F   22  5                                   5    
HELIX   84  84 SER F   24  LEU F   27  5                                   4    
HELIX   85  85 ILE F   36  ALA F   46  1                                  11    
HELIX   86  86 ASP F   59  GLY F   68  1                                  10    
HELIX   87  87 GLY F   70  GLY F   74  5                                   5    
HELIX   88  88 ALA F   89  GLY F   95  1                                   7    
HELIX   89  89 GLY F   95  GLY F  100  1                                   6    
HELIX   90  90 ASP F  117  ARG F  128  1                                  12    
HELIX   91  91 ASP F  141  ARG F  144  5                                   4    
HELIX   92  92 GLN F  181  ASP F  188  1                                   8    
HELIX   93  93 GLU F  198  GLU F  208  1                                  11    
HELIX   94  94 THR F  228  GLY F  247  1                                  20    
HELIX   95  95 CYS F  252  GLN F  260  1                                   9    
HELIX   96  96 ASP F  264  ALA F  273  1                                  10    
HELIX   97  97 PRO F  274  ALA F  276  5                                   3    
HELIX   98  98 ASN F  278  LEU F  287  1                                  10    
HELIX   99  99 GLY G   13  HIS G   17  5                                   5    
HELIX  100 100 PRO G   18  ILE G   23  1                                   6    
HELIX  101 101 ILE G   36  ALA G   46  1                                  11    
HELIX  102 102 ASP G   59  GLY G   68  1                                  10    
HELIX  103 103 GLY G   70  GLY G   74  5                                   5    
HELIX  104 104 GLY G   87  ALA G   89  5                                   3    
HELIX  105 105 GLN G   90  GLY G   95  1                                   6    
HELIX  106 106 GLY G   95  GLY G  100  1                                   6    
HELIX  107 107 ASP G  117  GLN G  127  1                                  11    
HELIX  108 108 ASP G  141  ARG G  144  5                                   4    
HELIX  109 109 GLN G  181  ASP G  188  1                                   8    
HELIX  110 110 GLU G  198  ARG G  209  1                                  12    
HELIX  111 111 THR G  228  GLY G  247  1                                  20    
HELIX  112 112 CYS G  252  GLN G  260  1                                   9    
HELIX  113 113 ASP G  264  ALA G  273  1                                  10    
HELIX  114 114 PRO G  274  ALA G  276  5                                   3    
HELIX  115 115 ASN G  278  LEU G  287  1                                  10    
HELIX  116 116 LEU G  288  GLU G  290  5                                   3    
HELIX  117 117 GLY H   13  HIS H   17  5                                   5    
HELIX  118 118 SER H   24  LEU H   27  5                                   4    
HELIX  119 119 ILE H   36  ALA H   46  1                                  11    
HELIX  120 120 ASP H   59  GLY H   68  1                                  10    
HELIX  121 121 GLY H   70  GLY H   74  5                                   5    
HELIX  122 122 GLY H   87  ALA H   89  5                                   3    
HELIX  123 123 GLN H   90  GLY H   95  1                                   6    
HELIX  124 124 GLY H   95  GLY H  100  1                                   6    
HELIX  125 125 ASP H  117  ARG H  128  1                                  12    
HELIX  126 126 ASP H  141  ARG H  144  5                                   4    
HELIX  127 127 GLN H  181  ASP H  188  1                                   8    
HELIX  128 128 GLU H  198  ARG H  209  1                                  12    
HELIX  129 129 THR H  228  GLY H  247  1                                  20    
HELIX  130 130 CYS H  252  GLN H  260  1                                   9    
HELIX  131 131 ASP H  264  ALA H  273  1                                  10    
HELIX  132 132 PRO H  274  ALA H  276  5                                   3    
HELIX  133 133 ASN H  278  LEU H  287  1                                  10    
SHEET    1   A 3 LEU A 212  ILE A 216  0                                        
SHEET    2   A 3 ALA A 132  HIS A 138  1  O  ALA A 132   N  SER A 213           
SHEET    3   A 3 TYR A 170  VAL A 172 -1  N  ALA A 171   O  TYR A 137           
SHEET    1   B 7 LEU A 212  ILE A 216  0                                        
SHEET    2   B 7 ALA A 132  HIS A 138  1  O  ALA A 132   N  SER A 213           
SHEET    3   B 7 LEU A 175  TYR A 178 -1  O  PHE A 177   N  SER A 133           
SHEET    4   B 7 LEU A 103  LEU A 108 -1  N  SER A 104   O  TYR A 178           
SHEET    5   B 7 ARG A   3  LEU A   8  1  N  LYS A   4   O  LEU A 103           
SHEET    6   B 7 GLU A  50  SER A  55  1  O  GLU A  50   N  GLY A   5           
SHEET    7   B 7 ASP A  76  VAL A  81  1  O  ASP A  76   N  ILE A  51           
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 2 GLY A 146  PHE A 150  0                                        
SHEET    2   E 2 ALA A 156  GLU A 161 -1  N  ILE A 157   O  GLU A 149           
SHEET    1   F 7 ASP B  76  VAL B  81  0                                        
SHEET    2   F 7 GLU B  50  SER B  55  1  O  ILE B  51   N  GLN B  78           
SHEET    3   F 7 ARG B   3  LEU B   8  1  N  GLY B   5   O  GLU B  50           
SHEET    4   F 7 LEU B 103  LEU B 108  1  O  LEU B 103   N  LYS B   4           
SHEET    5   F 7 TYR B 170  TYR B 178 -1  O  GLY B 174   N  LEU B 108           
SHEET    6   F 7 ALA B 132  HIS B 138 -1  O  SER B 133   N  PHE B 177           
SHEET    7   F 7 LEU B 212  ILE B 216  1  N  SER B 213   O  ALA B 132           
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 2 GLY B 146  PHE B 150  0                                        
SHEET    2   I 2 ALA B 156  GLU B 161 -1  N  ILE B 157   O  GLU B 149           
SHEET    1   J 7 ASP C  76  VAL C  81  0                                        
SHEET    2   J 7 GLU C  50  SER C  55  1  N  ILE C  51   O  ASP C  76           
SHEET    3   J 7 ARG C   3  LEU C   8  1  N  GLY C   5   O  GLU C  50           
SHEET    4   J 7 LEU C 103  LEU C 108  1  O  LEU C 103   N  LYS C   4           
SHEET    5   J 7 TYR C 170  TYR C 178 -1  O  GLY C 174   N  LEU C 108           
SHEET    6   J 7 ALA C 132  HIS C 138 -1  O  SER C 133   N  PHE C 177           
SHEET    7   J 7 LEU C 212  ILE C 216  1  N  SER C 213   O  ALA C 132           
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 2 GLY C 146  PHE C 150  0                                        
SHEET    2   M 2 ALA C 156  GLU C 161 -1  N  ILE C 157   O  GLU C 149           
SHEET    1   N 7 ASP D  76  VAL D  81  0                                        
SHEET    2   N 7 GLU D  50  SER D  55  1  O  ILE D  51   N  GLN D  78           
SHEET    3   N 7 ARG D   3  LEU D   8  1  O  GLY D   5   N  LEU D  52           
SHEET    4   N 7 LEU D 103  LEU D 108  1  O  LEU D 103   N  LYS D   4           
SHEET    5   N 7 TYR D 170  TYR D 178 -1  O  GLY D 174   N  LEU D 108           
SHEET    6   N 7 ALA D 132  HIS D 138 -1  O  SER D 133   N  PHE D 177           
SHEET    7   N 7 LEU D 212  ILE D 216  1  N  SER D 213   O  ALA D 132           
SHEET    1   O 2 PRO D  29  VAL D  30  0                                        
SHEET    2   O 2 LYS D  33  PRO D  34 -1  O  LYS D  33   N  VAL D  30           
SHEET    1   P 2 ASN D 111  TYR D 114  0                                        
SHEET    2   P 2 ALA D 222  ASP D 225 -1  N  ALA D 222   O  TYR D 114           
SHEET    1   Q 2 GLY D 146  PHE D 150  0                                        
SHEET    2   Q 2 ALA D 156  GLU D 161 -1  N  ILE D 157   O  GLU D 149           
SHEET    1   R 3 LEU E 212  ILE E 216  0                                        
SHEET    2   R 3 ALA E 132  HIS E 138  1  O  ALA E 132   N  SER E 213           
SHEET    3   R 3 TYR E 170  VAL E 172 -1  N  ALA E 171   O  TYR E 137           
SHEET    1   S 7 LEU E 212  ILE E 216  0                                        
SHEET    2   S 7 ALA E 132  HIS E 138  1  O  ALA E 132   N  SER E 213           
SHEET    3   S 7 LEU E 175  TYR E 178 -1  N  PHE E 177   O  SER E 133           
SHEET    4   S 7 LEU E 103  LEU E 108 -1  O  SER E 104   N  TYR E 178           
SHEET    5   S 7 ARG E   3  LEU E   8  1  N  LYS E   4   O  LEU E 103           
SHEET    6   S 7 GLU E  50  SER E  55  1  O  GLU E  50   N  GLY E   5           
SHEET    7   S 7 ASP E  76  VAL E  81  1  O  ASP E  76   N  ILE E  51           
SHEET    1   T 2 PRO E  29  VAL E  30  0                                        
SHEET    2   T 2 LYS E  33  PRO E  34 -1  O  LYS E  33   N  VAL E  30           
SHEET    1   U 2 ASN E 111  TYR E 114  0                                        
SHEET    2   U 2 ALA E 222  ASP E 225 -1  N  ALA E 222   O  TYR E 114           
SHEET    1   V 2 GLY E 146  PHE E 150  0                                        
SHEET    2   V 2 ALA E 156  GLU E 161 -1  N  ILE E 157   O  GLU E 149           
SHEET    1   W 7 ASP F  76  VAL F  81  0                                        
SHEET    2   W 7 GLU F  50  SER F  55  1  O  ILE F  51   N  GLN F  78           
SHEET    3   W 7 ARG F   3  ALA F   9  1  N  GLY F   5   O  GLU F  50           
SHEET    4   W 7 LEU F 103  LEU F 108  1  O  LEU F 103   N  LYS F   4           
SHEET    5   W 7 TYR F 170  TYR F 178 -1  O  GLY F 174   N  LEU F 108           
SHEET    6   W 7 ALA F 132  HIS F 138 -1  O  SER F 133   N  PHE F 177           
SHEET    7   W 7 LEU F 212  ILE F 216  1  N  SER F 213   O  ALA F 132           
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 2 GLY F 146  PHE F 150  0                                        
SHEET    2   Z 2 ALA F 156  GLU F 161 -1  N  ILE F 157   O  GLU F 149           
SHEET    1  AA 3 LEU G 212  ILE G 216  0                                        
SHEET    2  AA 3 ALA G 132  HIS G 138  1  O  ALA G 132   N  SER G 213           
SHEET    3  AA 3 TYR G 170  VAL G 172 -1  N  ALA G 171   O  TYR G 137           
SHEET    1  AB 7 LEU G 212  ILE G 216  0                                        
SHEET    2  AB 7 ALA G 132  HIS G 138  1  O  ALA G 132   N  SER G 213           
SHEET    3  AB 7 LEU G 175  TYR G 178 -1  N  PHE G 177   O  SER G 133           
SHEET    4  AB 7 LEU G 103  LEU G 108 -1  O  SER G 104   N  TYR G 178           
SHEET    5  AB 7 ARG G   3  LEU G   8  1  N  LYS G   4   O  LEU G 103           
SHEET    6  AB 7 GLU G  50  SER G  55  1  O  GLU G  50   N  GLY G   5           
SHEET    7  AB 7 ASP G  76  VAL G  81  1  O  ASP G  76   N  ILE G  51           
SHEET    1  AC 2 PRO G  29  VAL G  30  0                                        
SHEET    2  AC 2 LYS G  33  PRO G  34 -1  O  LYS G  33   N  VAL G  30           
SHEET    1  AD 2 ASN G 111  TYR G 114  0                                        
SHEET    2  AD 2 ALA G 222  ASP G 225 -1  N  ALA G 222   O  TYR G 114           
SHEET    1  AE 2 GLY G 146  PHE G 150  0                                        
SHEET    2  AE 2 ALA G 156  GLU G 161 -1  N  ILE G 157   O  GLU G 149           
SHEET    1  AF 7 ASP H  76  VAL H  81  0                                        
SHEET    2  AF 7 GLU H  50  SER H  55  1  O  ILE H  51   N  GLN H  78           
SHEET    3  AF 7 ARG H   3  LEU H   8  1  O  GLY H   5   N  LEU H  52           
SHEET    4  AF 7 LEU H 103  LEU H 108  1  O  LEU H 103   N  LYS H   4           
SHEET    5  AF 7 TYR H 170  TYR H 178 -1  O  GLY H 174   N  LEU H 108           
SHEET    6  AF 7 ALA H 132  HIS H 138 -1  N  SER H 133   O  PHE H 177           
SHEET    7  AF 7 LEU H 212  ILE H 216  1  N  SER H 213   O  ALA H 132           
SHEET    1  AG 2 PRO H  29  VAL H  30  0                                        
SHEET    2  AG 2 LYS H  33  PRO H  34 -1  O  LYS H  33   N  VAL H  30           
SHEET    1  AH 2 ASN H 111  TYR H 114  0                                        
SHEET    2  AH 2 ALA H 222  ASP H 225 -1  N  ALA H 222   O  TYR H 114           
SHEET    1  AI 2 GLY H 146  PHE H 150  0                                        
SHEET    2  AI 2 ALA H 156  GLU H 161 -1  N  ILE H 157   O  GLU H 149           
CISPEP   1 HIS A   17    PRO A   18          0         4.11                     
CISPEP   2 HIS B   17    PRO B   18          0        -0.28                     
CISPEP   3 HIS C   17    PRO C   18          0        -5.08                     
CISPEP   4 HIS D   17    PRO D   18          0        -6.32                     
CISPEP   5 HIS E   17    PRO E   18          0        -4.17                     
CISPEP   6 HIS F   17    PRO F   18          0        -9.93                     
CISPEP   7 HIS G   17    PRO G   18          0        -0.79                     
CISPEP   8 HIS H   17    PRO H   18          0        -3.86                     
CRYST1   71.274   73.084  133.652  89.98  81.42  81.56 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      0.014030 -0.002082 -0.002163        0.00000                         
SCALE2      0.000000  0.013833  0.000305        0.00000                         
SCALE3      0.000000  0.000000  0.007569        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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