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Database: PDB
Entry: 1G2V
LinkDB: 1G2V
Original site: 1G2V 
HEADER    TRANSFERASE                             21-OCT-00   1G2V              
TITLE     THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF     
TITLE    2 GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). TTP 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_STRAIN: BL21(LAMBDA DE3);                          
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 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.NAISMITH                        
REVDAT   4   07-MAR-18 1G2V    1       REMARK                                   
REVDAT   3   24-FEB-09 1G2V    1       VERSN                                    
REVDAT   2   01-APR-03 1G2V    1       JRNL                                     
REVDAT   1   27-DEC-00 1G2V    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.    2.60 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 71748                          
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) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3797                            
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            : 18280                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 464                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.30000                                             
REMARK   3    B22 (A**2) : -0.03000                                             
REMARK   3    B33 (A**2) : 1.36000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.08000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.370         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.350         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 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: NULL                                      
REMARK   4                                                                      
REMARK   4 1G2V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000012165.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-JUL-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7557                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.5                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 60.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1G1L                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% (W/V) PEG 6000, 0.1 M NA-CITRATE PH   
REMARK 280  4.0; PROTEIN INCUBATED WITH 10 MM DTTP, PH 4.00, VAPOR DIFFUSION,   
REMARK 280  SITTING DROP, TEMPERATURE 292K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       67.18050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 18910 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 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: 18940 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 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 B     1                                                      
REMARK 465     MET C     1                                                      
REMARK 465     MET D     1                                                      
REMARK 465     MET E     1                                                      
REMARK 465     MET F     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   NZ   LYS D     2     OE1  GLU D    50              2.12            
REMARK 500   OE1  GLU F   255     OH   TYR F   283              2.14            
REMARK 500   OD1  ASP E    69     OG   SER E    71              2.18            
REMARK 500   OH   TYR E    31     OD1  ASP F   230              2.18            
REMARK 500   NZ   LYS D     4     OD2  ASP D   102              2.19            
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   OE1  GLN E   127     NZ   LYS H   167     2647     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    ALA A  89   CA    ALA A  89   CB     -0.148                       
REMARK 500    TYR A 170   CE2   TYR A 170   CD2    -0.106                       
REMARK 500    CYS A 252   CB    CYS A 252   SG     -0.101                       
REMARK 500    TYR B 170   CE2   TYR B 170   CD2    -0.093                       
REMARK 500    TYR B 206   CD1   TYR B 206   CE1    -0.096                       
REMARK 500    TYR B 206   CE2   TYR B 206   CD2    -0.113                       
REMARK 500    TYR C 206   CD1   TYR C 206   CE1    -0.095                       
REMARK 500    TYR D  37   CE2   TYR D  37   CD2    -0.108                       
REMARK 500    VAL D 148   CB    VAL D 148   CG1    -0.127                       
REMARK 500    ALA D 186   CA    ALA D 186   CB     -0.131                       
REMARK 500    TYR D 206   CE2   TYR D 206   CD2    -0.091                       
REMARK 500    CYS E 252   CB    CYS E 252   SG     -0.098                       
REMARK 500    MET F  35   CG    MET F  35   SD     -0.199                       
REMARK 500    MET F  35   SD    MET F  35   CE     -0.829                       
REMARK 500    GLU F  96   CD    GLU F  96   OE2     0.067                       
REMARK 500    ALA F 235   CA    ALA F 235   CB     -0.143                       
REMARK 500    GLU G 120   CG    GLU G 120   CD      0.091                       
REMARK 500    TYR H 280   CE2   TYR H 280   CD2    -0.113                       
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 102   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG A 128   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ASP A 151   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 184   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP B  59   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP B 102   CB  -  CG  -  OD2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    HIS B 119   CB  -  CA  -  C   ANGL. DEV. =  12.3 DEGREES          
REMARK 500    ARG B 128   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ASP B 230   CB  -  CG  -  OD2 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ARG B 259   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP C  86   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP C 110   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    LEU C 112   CB  -  CG  -  CD2 ANGL. DEV. = -10.5 DEGREES          
REMARK 500    ASP C 117   CB  -  CG  -  OD1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP C 141   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP C 188   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP C 201   CB  -  CG  -  OD2 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ASP D  86   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP D 102   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP D 110   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP D 225   CB  -  CG  -  OD2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ASP D 230   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP E  59   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP E 102   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG E 128   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG F  15   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG F 128   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP F 141   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP F 184   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    LEU G 112   CB  -  CG  -  CD2 ANGL. DEV. = -10.5 DEGREES          
REMARK 500    ASP G 117   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP G 141   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP G 201   CB  -  CG  -  OD2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ASP G 230   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP H  86   CB  -  CG  -  OD2 ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ASP H 110   CB  -  CG  -  OD2 ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ASP H 117   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP H 201   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP H 230   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP H 264   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  31      -86.78     66.96                                   
REMARK 500    ASP A 141       64.02   -118.66                                   
REMARK 500    ASP A 179     -156.52    -98.26                                   
REMARK 500    THR A 226       39.14    -92.67                                   
REMARK 500    TYR B  31      -84.87     64.74                                   
REMARK 500    ASP B 141       60.19   -115.02                                   
REMARK 500    LYS B 162       58.20     36.35                                   
REMARK 500    ASP B 179     -159.82    -93.93                                   
REMARK 500    THR B 226       33.62    -90.00                                   
REMARK 500    TYR C  31      -82.93     62.32                                   
REMARK 500    ASP C 141       67.20   -117.47                                   
REMARK 500    ASP C 179     -158.66    -98.28                                   
REMARK 500    THR C 226       36.85    -96.89                                   
REMARK 500    ILE D  23      170.97    170.40                                   
REMARK 500    TYR D  31      -81.95     63.32                                   
REMARK 500    ASP D 141       63.93   -116.86                                   
REMARK 500    LYS D 162       57.09     38.84                                   
REMARK 500    ASP D 179     -159.38    -97.25                                   
REMARK 500    THR D 226       38.63    -92.89                                   
REMARK 500    GLN E  26        1.09    -69.86                                   
REMARK 500    TYR E  31      -86.74     66.59                                   
REMARK 500    ASP E 179     -163.66   -102.31                                   
REMARK 500    THR E 226       39.51    -92.58                                   
REMARK 500    TYR F  31      -89.41     66.09                                   
REMARK 500    ASP F 141       60.64   -118.18                                   
REMARK 500    ASP F 179     -156.95    -94.78                                   
REMARK 500    THR F 226       35.22    -90.62                                   
REMARK 500    TYR G  31      -83.34     64.41                                   
REMARK 500    ASP G 141       68.88   -115.77                                   
REMARK 500    THR G 226       34.72    -95.21                                   
REMARK 500    TYR H  31      -79.19     65.32                                   
REMARK 500    LYS H 162       59.26     37.71                                   
REMARK 500    THR H 226       35.53    -95.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP A 3500                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP A 3501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP B 3502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP B 3503                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP C 3504                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP C 3505                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP D 3506                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP D 3507                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP E 3508                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP E 3509                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP F 3510                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP F 3511                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP G 3512                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP G 3513                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP H 3514                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP H 3515                
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: 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: 1G31   RELATED DB: PDB                                   
REMARK 900 1G31 IS RMLA IN COMPLEX WITH 2'-DEOXY-THYMIDINE-BETA-L-RHAMNOSE      
REMARK 900 (TDR)                                                                
DBREF  1G2V A    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G2V B    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G2V C    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G2V D    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G2V E    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G2V F    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G2V G    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G2V 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    TTP  A3500      29                                                       
HET    TTP  A3501      29                                                       
HET    TTP  B3502      29                                                       
HET    TTP  B3503      29                                                       
HET    TTP  C3504      29                                                       
HET    TTP  C3505      29                                                       
HET    TTP  D3506      29                                                       
HET    TTP  D3507      29                                                       
HET    TTP  E3508      29                                                       
HET    TTP  E3509      29                                                       
HET    TTP  F3510      29                                                       
HET    TTP  F3511      29                                                       
HET    TTP  G3512      29                                                       
HET    TTP  G3513      29                                                       
HET    TTP  H3514      29                                                       
HET    TTP  H3515      29                                                       
HETNAM     TTP THYMIDINE-5'-TRIPHOSPHATE                                        
FORMUL   9  TTP    16(C10 H17 N2 O14 P3)                                        
HELIX    1   1 GLY A   13  HIS A   17  5                                   5    
HELIX    2   2 SER A   24  LEU A   27  5                                   4    
HELIX    3   3 ILE A   36  ALA A   46  1                                  11    
HELIX    4   4 ASP A   59  GLY A   68  1                                  10    
HELIX    5   5 GLY A   70  GLY A   74  5                                   5    
HELIX    6   6 ALA A   89  GLY A   95  1                                   7    
HELIX    7   7 GLY A   95  GLY A  100  1                                   6    
HELIX    8   8 ASP A  117  ARG A  128  1                                  12    
HELIX    9   9 ASP A  141  ARG A  144  5                                   4    
HELIX   10  10 GLN A  181  ASP A  188  1                                   8    
HELIX   11  11 GLU A  198  ARG A  209  1                                  12    
HELIX   12  12 THR A  228  GLY A  247  1                                  20    
HELIX   13  13 CYS A  252  GLN A  260  1                                   9    
HELIX   14  14 ASP A  264  ALA A  273  1                                  10    
HELIX   15  15 PRO A  274  ALA A  276  5                                   3    
HELIX   16  16 ASN A  278  LEU A  287  1                                  10    
HELIX   17  17 LEU A  288  GLU A  290  5                                   3    
HELIX   18  18 GLY B   13  HIS B   17  5                                   5    
HELIX   19  19 PRO B   18  ILE B   23  1                                   6    
HELIX   20  20 SER B   24  LEU B   27  5                                   4    
HELIX   21  21 ILE B   36  ALA B   46  1                                  11    
HELIX   22  22 ASP B   59  GLY B   68  1                                  10    
HELIX   23  23 GLY B   70  GLY B   74  5                                   5    
HELIX   24  24 ALA B   89  GLY B   95  1                                   7    
HELIX   25  25 GLY B   95  GLY B  100  1                                   6    
HELIX   26  26 ASP B  117  ARG B  128  1                                  12    
HELIX   27  27 ASP B  141  ARG B  144  5                                   4    
HELIX   28  28 GLN B  181  ASP B  188  1                                   8    
HELIX   29  29 GLU B  198  ARG B  209  1                                  12    
HELIX   30  30 THR B  228  GLY B  247  1                                  20    
HELIX   31  31 CYS B  252  GLN B  260  1                                   9    
HELIX   32  32 ASP B  264  ALA B  273  1                                  10    
HELIX   33  33 PRO B  274  ALA B  276  5                                   3    
HELIX   34  34 ASN B  278  LEU B  287  1                                  10    
HELIX   35  35 GLY C   13  HIS C   17  5                                   5    
HELIX   36  36 PRO C   18  ILE C   23  1                                   6    
HELIX   37  37 SER C   24  LEU C   27  5                                   4    
HELIX   38  38 ILE C   36  ALA C   46  1                                  11    
HELIX   39  39 ASP C   59  GLY C   68  1                                  10    
HELIX   40  40 GLY C   70  GLY C   74  5                                   5    
HELIX   41  41 ALA C   89  GLY C   95  1                                   7    
HELIX   42  42 GLY C   95  GLY C  100  1                                   6    
HELIX   43  43 ASP C  117  ARG C  128  1                                  12    
HELIX   44  44 ASP C  141  ARG C  144  5                                   4    
HELIX   45  45 GLN C  181  ASP C  188  1                                   8    
HELIX   46  46 GLU C  198  ARG C  209  1                                  12    
HELIX   47  47 THR C  228  GLY C  247  1                                  20    
HELIX   48  48 CYS C  252  LYS C  261  1                                  10    
HELIX   49  49 ASP C  264  ALA C  273  1                                  10    
HELIX   50  50 PRO C  274  ALA C  276  5                                   3    
HELIX   51  51 ASN C  278  LEU C  288  1                                  11    
HELIX   52  52 GLY D   13  HIS D   17  5                                   5    
HELIX   53  53 PRO D   18  ALA D   22  5                                   5    
HELIX   54  54 SER D   24  LEU D   27  5                                   4    
HELIX   55  55 ILE D   36  ALA D   46  1                                  11    
HELIX   56  56 ASP D   59  GLY D   68  1                                  10    
HELIX   57  57 GLY D   70  GLY D   74  5                                   5    
HELIX   58  58 ALA D   89  GLY D   95  1                                   7    
HELIX   59  59 GLY D   95  GLY D  100  1                                   6    
HELIX   60  60 ASP D  117  GLN D  127  1                                  11    
HELIX   61  61 ASP D  141  ARG D  144  5                                   4    
HELIX   62  62 GLN D  181  ASP D  188  1                                   8    
HELIX   63  63 GLU D  198  ARG D  209  1                                  12    
HELIX   64  64 THR D  228  GLY D  247  1                                  20    
HELIX   65  65 CYS D  252  GLN D  260  1                                   9    
HELIX   66  66 ASP D  264  ALA D  273  1                                  10    
HELIX   67  67 PRO D  274  ALA D  276  5                                   3    
HELIX   68  68 ASN D  278  LEU D  287  1                                  10    
HELIX   69  69 GLY E   13  HIS E   17  5                                   5    
HELIX   70  70 SER E   24  LEU E   27  5                                   4    
HELIX   71  71 ILE E   36  ALA E   46  1                                  11    
HELIX   72  72 ASP E   59  GLY E   68  1                                  10    
HELIX   73  73 GLY E   70  GLY E   74  5                                   5    
HELIX   74  74 ALA E   89  GLY E   95  1                                   7    
HELIX   75  75 GLY E   95  GLY E  100  1                                   6    
HELIX   76  76 ASP E  117  ARG E  128  1                                  12    
HELIX   77  77 ASP E  141  ARG E  144  5                                   4    
HELIX   78  78 GLN E  181  ASP E  188  1                                   8    
HELIX   79  79 GLU E  198  ARG E  209  1                                  12    
HELIX   80  80 THR E  228  GLY E  247  1                                  20    
HELIX   81  81 CYS E  252  GLN E  260  1                                   9    
HELIX   82  82 ASP E  264  ALA E  273  1                                  10    
HELIX   83  83 PRO E  274  ALA E  276  5                                   3    
HELIX   84  84 ASN E  278  LEU E  287  1                                  10    
HELIX   85  85 GLY F   13  HIS F   17  5                                   5    
HELIX   86  86 PRO F   18  ILE F   23  1                                   6    
HELIX   87  87 SER F   24  LEU F   27  5                                   4    
HELIX   88  88 ILE F   36  ALA F   46  1                                  11    
HELIX   89  89 ASP F   59  GLY F   68  1                                  10    
HELIX   90  90 GLY F   70  GLY F   74  5                                   5    
HELIX   91  91 ALA F   89  GLY F   95  1                                   7    
HELIX   92  92 GLY F   95  GLY F  100  1                                   6    
HELIX   93  93 ASP F  117  ARG F  128  1                                  12    
HELIX   94  94 ASP F  141  ARG F  144  5                                   4    
HELIX   95  95 GLN F  181  ASP F  188  1                                   8    
HELIX   96  96 GLU F  198  ARG F  209  1                                  12    
HELIX   97  97 THR F  228  GLY F  247  1                                  20    
HELIX   98  98 CYS F  252  GLN F  260  1                                   9    
HELIX   99  99 ASP F  264  ALA F  273  1                                  10    
HELIX  100 100 PRO F  274  ALA F  276  5                                   3    
HELIX  101 101 ASN F  278  LEU F  287  1                                  10    
HELIX  102 102 GLY G   13  HIS G   17  5                                   5    
HELIX  103 103 PRO G   18  ILE G   23  1                                   6    
HELIX  104 104 SER G   24  LEU G   27  5                                   4    
HELIX  105 105 ILE G   36  ALA G   46  1                                  11    
HELIX  106 106 ASP G   59  GLY G   68  1                                  10    
HELIX  107 107 GLY G   70  GLY G   74  5                                   5    
HELIX  108 108 ALA G   89  GLY G   95  1                                   7    
HELIX  109 109 GLY G   95  GLY G  100  1                                   6    
HELIX  110 110 ASP G  117  GLN G  127  1                                  11    
HELIX  111 111 ASP G  141  ARG G  144  5                                   4    
HELIX  112 112 GLN G  181  ASP G  188  1                                   8    
HELIX  113 113 GLU G  198  ARG G  209  1                                  12    
HELIX  114 114 THR G  228  GLY G  247  1                                  20    
HELIX  115 115 CYS G  252  LYS G  261  1                                  10    
HELIX  116 116 ASP G  264  ALA G  273  1                                  10    
HELIX  117 117 PRO G  274  ALA G  276  5                                   3    
HELIX  118 118 ASN G  278  LEU G  288  1                                  11    
HELIX  119 119 GLY H   13  HIS H   17  5                                   5    
HELIX  120 120 SER H   24  LEU H   27  5                                   4    
HELIX  121 121 ILE H   36  ALA H   46  1                                  11    
HELIX  122 122 ASP H   59  GLY H   68  1                                  10    
HELIX  123 123 GLY H   70  GLY H   74  5                                   5    
HELIX  124 124 ALA H   89  GLY H   95  1                                   7    
HELIX  125 125 GLY H   95  GLY H  100  1                                   6    
HELIX  126 126 ASP H  117  GLN H  127  1                                  11    
HELIX  127 127 ASP H  141  ARG H  144  5                                   4    
HELIX  128 128 GLN H  181  ASP H  188  1                                   8    
HELIX  129 129 GLU H  198  ARG H  209  1                                  12    
HELIX  130 130 THR H  228  GLY H  247  1                                  20    
HELIX  131 131 CYS H  252  GLN H  260  1                                   9    
HELIX  132 132 ASP H  264  ALA H  273  1                                  10    
HELIX  133 133 PRO H  274  ALA H  276  5                                   3    
HELIX  134 134 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  O  ALA A 171   N  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  O  SER A 104   N  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 3 LEU B 212  ILE B 216  0                                        
SHEET    2   F 3 ALA B 132  HIS B 138  1  O  ALA B 132   N  SER B 213           
SHEET    3   F 3 TYR B 170  VAL B 172 -1  N  ALA B 171   O  TYR B 137           
SHEET    1   G 7 LEU B 212  ILE B 216  0                                        
SHEET    2   G 7 ALA B 132  HIS B 138  1  O  ALA B 132   N  SER B 213           
SHEET    3   G 7 LEU B 175  TYR B 178 -1  O  PHE B 177   N  SER B 133           
SHEET    4   G 7 LEU B 103  LEU B 108 -1  O  SER B 104   N  TYR B 178           
SHEET    5   G 7 ARG B   3  LEU B   8  1  N  LYS B   4   O  LEU B 103           
SHEET    6   G 7 GLU B  50  SER B  55  1  O  GLU B  50   N  GLY B   5           
SHEET    7   G 7 ASP B  76  VAL B  81  1  O  ASP B  76   N  ILE B  51           
SHEET    1   H 2 PRO B  29  VAL B  30  0                                        
SHEET    2   H 2 LYS B  33  PRO B  34 -1  O  LYS B  33   N  VAL B  30           
SHEET    1   I 2 ASN B 111  TYR B 114  0                                        
SHEET    2   I 2 ALA B 222  ASP B 225 -1  N  ALA B 222   O  TYR B 114           
SHEET    1   J 2 GLY B 146  PHE B 150  0                                        
SHEET    2   J 2 ALA B 156  GLU B 161 -1  N  ILE B 157   O  GLU B 149           
SHEET    1   K 5 ASP C  76  VAL C  81  0                                        
SHEET    2   K 5 GLU C  50  SER C  55  1  O  ILE C  51   N  GLN C  78           
SHEET    3   K 5 ARG C   3  LEU C   8  1  O  GLY C   5   N  LEU C  52           
SHEET    4   K 5 LEU C 103  LEU C 108  1  O  LEU C 103   N  LYS C   4           
SHEET    5   K 5 LEU C 175  TYR C 178 -1  O  TYR C 176   N  LEU C 106           
SHEET    1   L 2 PRO C  29  VAL C  30  0                                        
SHEET    2   L 2 LYS C  33  PRO C  34 -1  O  LYS C  33   N  VAL C  30           
SHEET    1   M 2 ASN C 111  TYR C 114  0                                        
SHEET    2   M 2 ALA C 222  ASP C 225 -1  N  ALA C 222   O  TYR C 114           
SHEET    1   N 3 TYR C 170  VAL C 172  0                                        
SHEET    2   N 3 ALA C 132  HIS C 138 -1  N  TYR C 137   O  ALA C 171           
SHEET    3   N 3 LEU C 212  ILE C 216  1  N  SER C 213   O  ALA C 132           
SHEET    1   O 2 GLY C 146  PHE C 150  0                                        
SHEET    2   O 2 ALA C 156  GLU C 161 -1  N  ILE C 157   O  GLU C 149           
SHEET    1   P 5 ASP D  76  VAL D  81  0                                        
SHEET    2   P 5 GLU D  50  SER D  55  1  O  ILE D  51   N  GLN D  78           
SHEET    3   P 5 ARG D   3  LEU D   8  1  O  GLY D   5   N  LEU D  52           
SHEET    4   P 5 LEU D 103  LEU D 108  1  O  LEU D 103   N  LYS D   4           
SHEET    5   P 5 LEU D 175  TYR D 178 -1  N  TYR D 176   O  LEU D 106           
SHEET    1   Q 2 PRO D  29  VAL D  30  0                                        
SHEET    2   Q 2 LYS D  33  PRO D  34 -1  O  LYS D  33   N  VAL D  30           
SHEET    1   R 2 ASN D 111  TYR D 114  0                                        
SHEET    2   R 2 ALA D 222  ASP D 225 -1  N  ALA D 222   O  TYR D 114           
SHEET    1   S 3 TYR D 170  VAL D 172  0                                        
SHEET    2   S 3 ALA D 132  HIS D 138 -1  N  TYR D 137   O  ALA D 171           
SHEET    3   S 3 LEU D 212  ILE D 216  1  N  SER D 213   O  ALA D 132           
SHEET    1   T 2 GLY D 146  PHE D 150  0                                        
SHEET    2   T 2 ALA D 156  GLU D 161 -1  N  ILE D 157   O  GLU D 149           
SHEET    1   U 5 ASP E  76  VAL E  81  0                                        
SHEET    2   U 5 GLU E  50  SER E  55  1  O  ILE E  51   N  GLN E  78           
SHEET    3   U 5 ARG E   3  LEU E   8  1  O  GLY E   5   N  LEU E  52           
SHEET    4   U 5 LEU E 103  LEU E 108  1  O  LEU E 103   N  LYS E   4           
SHEET    5   U 5 LEU E 175  TYR E 178 -1  N  TYR E 176   O  LEU E 106           
SHEET    1   V 2 PRO E  29  VAL E  30  0                                        
SHEET    2   V 2 LYS E  33  PRO E  34 -1  O  LYS E  33   N  VAL E  30           
SHEET    1   W 2 ASN E 111  TYR E 114  0                                        
SHEET    2   W 2 ALA E 222  ASP E 225 -1  N  ALA E 222   O  TYR E 114           
SHEET    1   X 3 TYR E 170  VAL E 172  0                                        
SHEET    2   X 3 ALA E 132  HIS E 138 -1  N  TYR E 137   O  ALA E 171           
SHEET    3   X 3 LEU E 212  ILE E 216  1  N  SER E 213   O  ALA E 132           
SHEET    1   Y 2 GLY E 146  PHE E 150  0                                        
SHEET    2   Y 2 ALA E 156  GLU E 161 -1  N  ILE E 157   O  GLU E 149           
SHEET    1   Z 3 LEU F 212  ILE F 216  0                                        
SHEET    2   Z 3 ALA F 132  HIS F 138  1  O  ALA F 132   N  SER F 213           
SHEET    3   Z 3 TYR F 170  VAL F 172 -1  O  ALA F 171   N  TYR F 137           
SHEET    1  AA 7 LEU F 212  ILE F 216  0                                        
SHEET    2  AA 7 ALA F 132  HIS F 138  1  O  ALA F 132   N  SER F 213           
SHEET    3  AA 7 LEU F 175  TYR F 178 -1  N  PHE F 177   O  SER F 133           
SHEET    4  AA 7 LEU F 103  LEU F 108 -1  O  SER F 104   N  TYR F 178           
SHEET    5  AA 7 ARG F   3  LEU F   8  1  N  LYS F   4   O  LEU F 103           
SHEET    6  AA 7 GLU F  50  SER F  55  1  O  GLU F  50   N  GLY F   5           
SHEET    7  AA 7 ASP F  76  VAL F  81  1  O  ASP F  76   N  ILE F  51           
SHEET    1  AB 2 PRO F  29  VAL F  30  0                                        
SHEET    2  AB 2 LYS F  33  PRO F  34 -1  O  LYS F  33   N  VAL F  30           
SHEET    1  AC 2 ASN F 111  TYR F 114  0                                        
SHEET    2  AC 2 ALA F 222  ASP F 225 -1  N  ALA F 222   O  TYR F 114           
SHEET    1  AD 2 GLY F 146  PHE F 150  0                                        
SHEET    2  AD 2 ALA F 156  GLU F 161 -1  N  ILE F 157   O  GLU F 149           
SHEET    1  AE 5 ASP G  76  VAL G  81  0                                        
SHEET    2  AE 5 GLU G  50  SER G  55  1  O  ILE G  51   N  GLN G  78           
SHEET    3  AE 5 ARG G   3  LEU G   8  1  O  GLY G   5   N  LEU G  52           
SHEET    4  AE 5 LEU G 103  LEU G 108  1  O  LEU G 103   N  LYS G   4           
SHEET    5  AE 5 LEU G 175  TYR G 178 -1  O  TYR G 176   N  LEU G 106           
SHEET    1  AF 2 PRO G  29  VAL G  30  0                                        
SHEET    2  AF 2 LYS G  33  PRO G  34 -1  O  LYS G  33   N  VAL G  30           
SHEET    1  AG 2 ASN G 111  TYR G 114  0                                        
SHEET    2  AG 2 ALA G 222  ASP G 225 -1  N  ALA G 222   O  TYR G 114           
SHEET    1  AH 3 TYR G 170  VAL G 172  0                                        
SHEET    2  AH 3 ALA G 132  HIS G 138 -1  N  TYR G 137   O  ALA G 171           
SHEET    3  AH 3 LEU G 212  ILE G 216  1  N  SER G 213   O  ALA G 132           
SHEET    1  AI 2 GLY G 146  PHE G 150  0                                        
SHEET    2  AI 2 ALA G 156  GLU G 161 -1  N  ILE G 157   O  GLU G 149           
SHEET    1  AJ 3 LEU H 212  ILE H 216  0                                        
SHEET    2  AJ 3 ALA H 132  HIS H 138  1  O  ALA H 132   N  SER H 213           
SHEET    3  AJ 3 TYR H 170  VAL H 172 -1  N  ALA H 171   O  TYR H 137           
SHEET    1  AK 7 LEU H 212  ILE H 216  0                                        
SHEET    2  AK 7 ALA H 132  HIS H 138  1  O  ALA H 132   N  SER H 213           
SHEET    3  AK 7 LEU H 175  TYR H 178 -1  N  PHE H 177   O  SER H 133           
SHEET    4  AK 7 LEU H 103  LEU H 108 -1  O  SER H 104   N  TYR H 178           
SHEET    5  AK 7 ARG H   3  LEU H   8  1  N  LYS H   4   O  LEU H 103           
SHEET    6  AK 7 GLU H  50  SER H  55  1  O  GLU H  50   N  GLY H   5           
SHEET    7  AK 7 ASP H  76  VAL H  81  1  O  ASP H  76   N  ILE H  51           
SHEET    1  AL 2 PRO H  29  VAL H  30  0                                        
SHEET    2  AL 2 LYS H  33  PRO H  34 -1  O  LYS H  33   N  VAL H  30           
SHEET    1  AM 2 ASN H 111  TYR H 114  0                                        
SHEET    2  AM 2 ALA H 222  ASP H 225 -1  N  ALA H 222   O  TYR H 114           
SHEET    1  AN 2 GLY H 146  PHE H 150  0                                        
SHEET    2  AN 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        -2.71                     
CISPEP   2 HIS B   17    PRO B   18          0        -7.73                     
CISPEP   3 HIS C   17    PRO C   18          0        -5.15                     
CISPEP   4 HIS D   17    PRO D   18          0        -3.43                     
CISPEP   5 HIS E   17    PRO E   18          0        -3.45                     
CISPEP   6 HIS F   17    PRO F   18          0        -7.14                     
CISPEP   7 HIS G   17    PRO G   18          0        -4.14                     
CISPEP   8 HIS H   17    PRO H   18          0         1.06                     
SITE     1 AC1 15 LEU A   8  ALA A   9  GLY A  10  GLY A  11                    
SITE     2 AC1 15 GLY A  13  THR A  14  ARG A  15  LYS A  25                    
SITE     3 AC1 15 GLN A  26  GLN A  82  PRO A  85  ASP A  86                    
SITE     4 AC1 15 GLY A  87  LEU A  88  ASP A 110                               
SITE     1 AC2 16 LEU A  45  TYR A 114  GLY A 115  HIS A 116                    
SITE     2 AC2 16 ASP A 117  PHE A 118  HIS A 119  VAL A 250                    
SITE     3 AC2 16 ALA A 251  GLU A 255  ILE A 256  ARG A 259                    
SITE     4 AC2 16 TYR A 293  GLY C 218  ARG C 219  GLY C 220                    
SITE     1 AC3 15 LEU B   8  ALA B   9  GLY B  10  GLY B  11                    
SITE     2 AC3 15 SER B  12  GLY B  13  THR B  14  ARG B  15                    
SITE     3 AC3 15 LYS B  25  GLN B  26  GLN B  82  PRO B  85                    
SITE     4 AC3 15 GLY B  87  LEU B  88  ASP B 110                               
SITE     1 AC4 14 TYR B 114  GLY B 115  HIS B 116  ASP B 117                    
SITE     2 AC4 14 PHE B 118  HIS B 119  VAL B 250  ALA B 251                    
SITE     3 AC4 14 GLU B 255  ILE B 256  ARG B 259  GLY D 218                    
SITE     4 AC4 14 ARG D 219  GLY D 220                                          
SITE     1 AC5 14 LEU C   8  ALA C   9  GLY C  10  GLY C  13                    
SITE     2 AC5 14 THR C  14  ARG C  15  LYS C  25  GLN C  26                    
SITE     3 AC5 14 GLN C  82  PRO C  85  ASP C  86  GLY C  87                    
SITE     4 AC5 14 LEU C  88  ASP C 110                                          
SITE     1 AC6 14 GLY A 218  ARG A 219  GLY A 220  LEU C  45                    
SITE     2 AC6 14 TYR C 114  GLY C 115  HIS C 116  ASP C 117                    
SITE     3 AC6 14 PHE C 118  HIS C 119  ALA C 251  GLU C 255                    
SITE     4 AC6 14 ILE C 256  ARG C 259                                          
SITE     1 AC7 16 LEU D   8  ALA D   9  GLY D  10  GLY D  11                    
SITE     2 AC7 16 SER D  12  GLY D  13  THR D  14  ARG D  15                    
SITE     3 AC7 16 LYS D  25  GLN D  26  GLN D  82  PRO D  85                    
SITE     4 AC7 16 ASP D  86  GLY D  87  LEU D  88  ASP D 110                    
SITE     1 AC8 15 GLY B 218  ARG B 219  GLY B 220  LEU D  45                    
SITE     2 AC8 15 TYR D 114  GLY D 115  HIS D 116  ASP D 117                    
SITE     3 AC8 15 PHE D 118  HIS D 119  VAL D 250  ALA D 251                    
SITE     4 AC8 15 GLU D 255  ILE D 256  ARG D 259                               
SITE     1 AC9 15 LEU E   8  ALA E   9  GLY E  10  GLY E  11                    
SITE     2 AC9 15 GLY E  13  THR E  14  ARG E  15  LYS E  25                    
SITE     3 AC9 15 GLN E  26  GLN E  82  PRO E  85  ASP E  86                    
SITE     4 AC9 15 GLY E  87  LEU E  88  ASP E 110                               
SITE     1 BC1 15 LEU E  45  TYR E 114  GLY E 115  HIS E 116                    
SITE     2 BC1 15 ASP E 117  PHE E 118  HIS E 119  ALA E 251                    
SITE     3 BC1 15 GLU E 255  ILE E 256  ARG E 259  TYR E 293                    
SITE     4 BC1 15 GLY G 218  ARG G 219  GLY G 220                               
SITE     1 BC2 16 LEU F   8  ALA F   9  GLY F  10  GLY F  11                    
SITE     2 BC2 16 SER F  12  GLY F  13  THR F  14  ARG F  15                    
SITE     3 BC2 16 LYS F  25  GLN F  26  GLN F  82  PRO F  85                    
SITE     4 BC2 16 ASP F  86  GLY F  87  LEU F  88  ASP F 110                    
SITE     1 BC3 15 LEU F  45  TYR F 114  GLY F 115  HIS F 116                    
SITE     2 BC3 15 ASP F 117  PHE F 118  HIS F 119  VAL F 250                    
SITE     3 BC3 15 ALA F 251  GLU F 255  ILE F 256  ARG F 259                    
SITE     4 BC3 15 GLY H 218  ARG H 219  GLY H 220                               
SITE     1 BC4 14 LEU G   8  GLY G  10  GLY G  11  GLY G  13                    
SITE     2 BC4 14 THR G  14  ARG G  15  LYS G  25  GLN G  26                    
SITE     3 BC4 14 GLN G  82  PRO G  85  ASP G  86  GLY G  87                    
SITE     4 BC4 14 LEU G  88  ASP G 110                                          
SITE     1 BC5 16 GLY E 218  ARG E 219  GLY E 220  LEU G  45                    
SITE     2 BC5 16 TYR G 114  GLY G 115  HIS G 116  ASP G 117                    
SITE     3 BC5 16 PHE G 118  HIS G 119  VAL G 250  ALA G 251                    
SITE     4 BC5 16 GLU G 255  ILE G 256  ARG G 259  TYR G 293                    
SITE     1 BC6 16 LEU H   8  ALA H   9  GLY H  10  GLY H  11                    
SITE     2 BC6 16 SER H  12  GLY H  13  THR H  14  ARG H  15                    
SITE     3 BC6 16 LYS H  25  GLN H  26  GLN H  82  PRO H  85                    
SITE     4 BC6 16 ASP H  86  GLY H  87  LEU H  88  ASP H 110                    
SITE     1 BC7 15 GLY F 218  ARG F 219  GLY F 220  TYR H 114                    
SITE     2 BC7 15 GLY H 115  HIS H 116  ASP H 117  PHE H 118                    
SITE     3 BC7 15 HIS H 119  VAL H 250  ALA H 251  GLU H 255                    
SITE     4 BC7 15 ILE H 256  ARG H 259  TYR H 293                               
CRYST1   73.017  134.361  140.901  90.00  98.22  90.00 P 1 21 1     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013695  0.000000  0.001979        0.00000                         
SCALE2      0.000000  0.007443  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007171        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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