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Database: PDB
Entry: 1G3L
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HEADER    TRANSFERASE                             24-OCT-00   1G3L              
TITLE     THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF     
TITLE    2 GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). TDP-L-RHAMNOSE     
TITLE    3 COMPLEX.                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE;                 
COMPND   3 CHAIN: A, B, C, D;                                                   
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 1G3L    1       REMARK                                   
REVDAT   3   24-FEB-09 1G3L    1       VERSN                                    
REVDAT   2   01-APR-03 1G3L    1       JRNL                                     
REVDAT   1   27-DEC-00 1G3L    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.    2.70 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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 34462                          
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) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1815                            
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            : 9148                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 305                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 37.11                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.07000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -1.08000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.470         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.410         
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 1G3L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000012190.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.0                                
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   : 36311                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 70.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
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   (%): 45.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 % (W/V) PEG 6000, 0.2 M LI-SULFATE,   
REMARK 280  0.1 M NA-CITRATE PH 4.0; PROTEIN INCUBATED WITH 10 MM DTDP-L-       
REMARK 280  RHAMNOSE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       35.54350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.83800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       69.27850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.83800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.54350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       69.27850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER CONSISTING OF TWO      
REMARK 300 DIMERS.                                                              
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 21980 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -146.0 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 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 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   OD1  ASP D    69     OG   SER D    71              2.06            
REMARK 500   OD1  ASP A    69     OG   SER A    71              2.15            
REMARK 500   OD2  ASP A   110     O3'  TRH A   500              2.16            
REMARK 500   OE1  GLN A   237     NE2  GLN B   237              2.17            
REMARK 500   OG   SER D    24     OD2  ASP D    59              2.17            
REMARK 500   OD1  ASP B    69     OG   SER B    71              2.18            
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 184   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP A 201   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 225   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP B  59   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP B 102   CB  -  CG  -  OD2 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    GLN B 152   CA  -  CB  -  CG  ANGL. DEV. = -13.3 DEGREES          
REMARK 500    ARG B 209   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B 209   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ASP C  59   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP C 110   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    GLN C 152   CA  -  CB  -  CG  ANGL. DEV. = -14.9 DEGREES          
REMARK 500    ASP C 184   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP D  59   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP D 117   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 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    LEU A  16       12.89    -67.74                                   
REMARK 500    TYR A  31      -80.73     69.99                                   
REMARK 500    THR A 289       25.89   -144.01                                   
REMARK 500    LEU B  16       13.82    -65.74                                   
REMARK 500    TYR B  31      -85.85     59.58                                   
REMARK 500    THR B 226       64.96   -100.57                                   
REMARK 500    ALA C   9       51.55   -118.16                                   
REMARK 500    SER C  12     -154.54    -75.15                                   
REMARK 500    ARG C  15      -89.46    -38.55                                   
REMARK 500    LEU C  16        0.95    -51.88                                   
REMARK 500    HIS C  17      151.55    -49.70                                   
REMARK 500    ILE C  23      136.84   -174.48                                   
REMARK 500    TYR C  31      -85.43     67.92                                   
REMARK 500    THR C 226       62.31   -105.44                                   
REMARK 500    ARG D  15      -72.18    -44.92                                   
REMARK 500    HIS D  17      150.56    -49.66                                   
REMARK 500    TYR D  31      -81.30     71.48                                   
REMARK 500    ARG D 219       -7.63    -58.72                                   
REMARK 500    LYS D 277        0.73    -66.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    HIS A  17         0.10    SIDE CHAIN                              
REMARK 500    HIS A 119         0.09    SIDE CHAIN                              
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 SO4 B 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRH A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRH A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRH B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRH B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRH C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRH C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRH D 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRH D 507                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1G23   RELATED DB: PDB                                   
REMARK 900 1G23 IS RMLA IN COMPLEX WITH GLUCOSE-1-PHOSPHATE                     
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: 1G2V   RELATED DB: PDB                                   
REMARK 900 1G2V IS RMLA IN COMPLEX WITH DTTP                                    
REMARK 900 RELATED ID: 1G0R   RELATED DB: PDB                                   
REMARK 900 1G0R IS RMLA IN COMPLEX WITH GLUCOSE-1-PHOSPHATE AND THYMIDINE       
REMARK 900 RELATED ID: 1G1L   RELATED DB: PDB                                   
REMARK 900 1G1L IS RMLA IN COMPLEX WITH DTDP-D-GLUCOSE                          
DBREF  1G3L A    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G3L B    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G3L C    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1G3L D    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                                  
HET    SO4  A 701       5                                                       
HET    TRH  A 500      35                                                       
HET    TRH  A 501      35                                                       
HET    SO4  B 700       5                                                       
HET    SO4  B 702       5                                                       
HET    TRH  B 502      35                                                       
HET    TRH  B 503      35                                                       
HET    SO4  C 703       5                                                       
HET    TRH  C 504      35                                                       
HET    TRH  C 505      35                                                       
HET    SO4  D 704       5                                                       
HET    TRH  D 506      35                                                       
HET    TRH  D 507      35                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     TRH 2'-DEOXY-THYMIDINE-BETA-L-RHAMNOSE                               
FORMUL   5  SO4    5(O4 S 2-)                                                   
FORMUL   6  TRH    8(C16 H26 N2 O15 P2)                                         
HELIX    1   1 SER A   24  LEU A   27  5                                   4    
HELIX    2   2 ILE A   36  ALA A   46  1                                  11    
HELIX    3   3 ASP A   59  GLY A   68  1                                  10    
HELIX    4   4 GLY A   70  GLY A   74  5                                   5    
HELIX    5   5 ALA A   89  GLY A   95  1                                   7    
HELIX    6   6 GLY A   95  GLY A  100  1                                   6    
HELIX    7   7 ASP A  117  ARG A  128  1                                  12    
HELIX    8   8 ASP A  141  ARG A  144  5                                   4    
HELIX    9   9 GLN A  181  ASP A  188  1                                   8    
HELIX   10  10 GLU A  198  ARG A  209  1                                  12    
HELIX   11  11 THR A  228  GLY A  247  1                                  20    
HELIX   12  12 CYS A  252  GLN A  260  1                                   9    
HELIX   13  13 ASP A  264  ALA A  273  1                                  10    
HELIX   14  14 PRO A  274  ALA A  276  5                                   3    
HELIX   15  15 ASN A  278  LEU A  288  1                                  11    
HELIX   16  16 SER B   24  LEU B   27  5                                   4    
HELIX   17  17 ILE B   36  ALA B   46  1                                  11    
HELIX   18  18 ASP B   59  GLY B   68  1                                  10    
HELIX   19  19 GLY B   70  GLY B   74  5                                   5    
HELIX   20  20 ALA B   89  GLY B   95  1                                   7    
HELIX   21  21 GLY B   95  GLY B  100  1                                   6    
HELIX   22  22 ASP B  117  ARG B  128  1                                  12    
HELIX   23  23 ASP B  141  ARG B  144  5                                   4    
HELIX   24  24 GLN B  181  ASP B  188  1                                   8    
HELIX   25  25 GLU B  198  ARG B  209  1                                  12    
HELIX   26  26 THR B  228  GLY B  247  1                                  20    
HELIX   27  27 CYS B  252  GLN B  260  1                                   9    
HELIX   28  28 ASP B  264  ALA B  273  1                                  10    
HELIX   29  29 PRO B  274  ALA B  276  5                                   3    
HELIX   30  30 ASN B  278  LEU B  288  1                                  11    
HELIX   31  31 SER C   24  LEU C   27  5                                   4    
HELIX   32  32 ILE C   36  ALA C   46  1                                  11    
HELIX   33  33 ASP C   59  GLY C   68  1                                  10    
HELIX   34  34 GLY C   70  GLY C   74  5                                   5    
HELIX   35  35 ALA C   89  GLY C   95  1                                   7    
HELIX   36  36 GLY C   95  GLY C  100  1                                   6    
HELIX   37  37 ASP C  117  GLN C  127  1                                  11    
HELIX   38  38 ASP C  141  ARG C  144  5                                   4    
HELIX   39  39 GLN C  181  ASP C  188  1                                   8    
HELIX   40  40 GLU C  198  GLU C  208  1                                  11    
HELIX   41  41 THR C  228  GLY C  247  1                                  20    
HELIX   42  42 CYS C  252  GLN C  260  1                                   9    
HELIX   43  43 ASP C  264  ALA C  273  1                                  10    
HELIX   44  44 PRO C  274  ALA C  276  5                                   3    
HELIX   45  45 ASN C  278  LEU C  288  1                                  11    
HELIX   46  46 PRO D   18  ALA D   22  5                                   5    
HELIX   47  47 SER D   24  LEU D   27  5                                   4    
HELIX   48  48 ILE D   36  ALA D   46  1                                  11    
HELIX   49  49 ASP D   59  GLY D   68  1                                  10    
HELIX   50  50 GLY D   70  GLY D   74  5                                   5    
HELIX   51  51 ALA D   89  GLY D   95  1                                   7    
HELIX   52  52 GLY D   95  GLY D  100  1                                   6    
HELIX   53  53 ASP D  117  ARG D  128  1                                  12    
HELIX   54  54 ASP D  141  ARG D  144  5                                   4    
HELIX   55  55 GLN D  181  ASP D  188  1                                   8    
HELIX   56  56 GLU D  198  GLU D  208  1                                  11    
HELIX   57  57 THR D  228  GLY D  247  1                                  20    
HELIX   58  58 CYS D  252  GLN D  260  1                                   9    
HELIX   59  59 ASP D  264  ALA D  273  1                                  10    
HELIX   60  60 PRO D  274  ALA D  276  5                                   3    
HELIX   61  61 ASN D  278  LEU D  288  1                                  11    
SHEET    1   A 5 ASP A  76  VAL A  81  0                                        
SHEET    2   A 5 GLU A  50  SER A  55  1  O  ILE A  51   N  GLN A  78           
SHEET    3   A 5 ARG A   3  LEU A   8  1  O  GLY A   5   N  LEU A  52           
SHEET    4   A 5 LEU A 103  LEU A 108  1  O  LEU A 103   N  LYS A   4           
SHEET    5   A 5 LEU A 175  TYR A 178 -1  O  TYR A 176   N  LEU A 106           
SHEET    1   B 2 PRO A  29  VAL A  30  0                                        
SHEET    2   B 2 LYS A  33  PRO A  34 -1  O  LYS A  33   N  VAL A  30           
SHEET    1   C 2 ASN A 111  TYR A 114  0                                        
SHEET    2   C 2 ALA A 222  ASP A 225 -1  N  ALA A 222   O  TYR A 114           
SHEET    1   D 3 TYR A 170  VAL A 172  0                                        
SHEET    2   D 3 ALA A 132  HIS A 138 -1  O  TYR A 137   N  ALA A 171           
SHEET    3   D 3 LEU A 212  ILE A 216  1  N  SER A 213   O  ALA A 132           
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  ALA B   9  1  O  GLY B   5   N  LEU B  52           
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  N  SER B 133   O  PHE B 177           
SHEET    7   F 7 LEU B 212  ILE B 216  1  O  SER B 213   N  VAL B 134           
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 5 ASP C  76  VAL C  81  0                                        
SHEET    2   J 5 GLU C  50  SER C  55  1  O  ILE C  51   N  GLN C  78           
SHEET    3   J 5 ARG C   3  ALA C   9  1  O  GLY C   5   N  LEU C  52           
SHEET    4   J 5 LEU C 103  LEU C 108  1  O  LEU C 103   N  LYS C   4           
SHEET    5   J 5 LEU C 175  TYR C 178 -1  N  TYR C 176   O  LEU C 106           
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 3 TYR C 170  VAL C 172  0                                        
SHEET    2   M 3 ALA C 132  HIS C 138 -1  N  TYR C 137   O  ALA C 171           
SHEET    3   M 3 LEU C 212  ILE C 216  1  O  SER C 213   N  VAL C 134           
SHEET    1   N 2 GLY C 146  PHE C 150  0                                        
SHEET    2   N 2 ALA C 156  GLU C 161 -1  N  ILE C 157   O  GLU C 149           
SHEET    1   O 5 ASP D  76  VAL D  81  0                                        
SHEET    2   O 5 GLU D  50  SER D  55  1  O  ILE D  51   N  GLN D  78           
SHEET    3   O 5 ARG D   3  LEU D   8  1  O  GLY D   5   N  LEU D  52           
SHEET    4   O 5 LEU D 103  LEU D 108  1  O  LEU D 103   N  LYS D   4           
SHEET    5   O 5 LEU D 175  TYR D 178 -1  N  TYR D 176   O  LEU D 106           
SHEET    1   P 2 PRO D  29  VAL D  30  0                                        
SHEET    2   P 2 LYS D  33  PRO D  34 -1  O  LYS D  33   N  VAL D  30           
SHEET    1   Q 2 ASN D 111  TYR D 114  0                                        
SHEET    2   Q 2 ALA D 222  ASP D 225 -1  N  ALA D 222   O  TYR D 114           
SHEET    1   R 3 TYR D 170  VAL D 172  0                                        
SHEET    2   R 3 ALA D 132  HIS D 138 -1  N  TYR D 137   O  ALA D 171           
SHEET    3   R 3 LEU D 212  ILE D 216  1  O  SER D 213   N  VAL D 134           
SHEET    1   S 2 GLY D 146  PHE D 150  0                                        
SHEET    2   S 2 ALA D 156  GLU D 161 -1  N  ILE D 157   O  GLU D 149           
CISPEP   1 HIS A   17    PRO A   18          0        -3.94                     
CISPEP   2 HIS B   17    PRO B   18          0        -6.58                     
CISPEP   3 HIS C   17    PRO C   18          0         0.73                     
CISPEP   4 HIS D   17    PRO D   18          0        -3.51                     
SITE     1 AC1  3 ARG A  62  PRO B  61  ARG B  62                               
SITE     1 AC2  4 ARG A 128  GLU A 215  ASP D 151  GLN D 152                    
SITE     1 AC3  4 ARG B 128  GLU B 215  ASP C 151  GLN C 152                    
SITE     1 AC4  3 ARG C 128  GLN C 129  THR C 130                               
SITE     1 AC5  3 ARG D 128  GLN D 129  THR D 130                               
SITE     1 AC6 20 LEU A   8  ALA A   9  GLY A  10  GLY A  11                    
SITE     2 AC6 20 GLN A  82  PRO A  85  ASP A  86  GLY A  87                    
SITE     3 AC6 20 ASP A 110  TYR A 145  GLY A 146  GLU A 161                    
SITE     4 AC6 20 LYS A 162  VAL A 172  THR A 173  GLY A 174                    
SITE     5 AC6 20 TYR A 176  ARG A 194  GLU A 196  THR A 200                    
SITE     1 AC7 16 TYR A 114  GLY A 115  HIS A 116  ASP A 117                    
SITE     2 AC7 16 PHE A 118  HIS A 119  GLU A 120  VAL A 250                    
SITE     3 AC7 16 ALA A 251  GLU A 255  ILE A 256  ARG A 259                    
SITE     4 AC7 16 TYR A 293  GLY C 218  ARG C 219  GLY C 220                    
SITE     1 AC8 18 LEU B   8  GLY B  10  GLY B  11  GLN B  82                    
SITE     2 AC8 18 PRO B  85  ASP B  86  GLY B  87  ASP B 110                    
SITE     3 AC8 18 TYR B 145  GLY B 146  GLU B 161  LYS B 162                    
SITE     4 AC8 18 VAL B 172  THR B 173  TYR B 176  ARG B 194                    
SITE     5 AC8 18 GLU B 196  THR B 200                                          
SITE     1 AC9 15 LEU B  45  TYR B 114  GLY B 115  HIS B 116                    
SITE     2 AC9 15 ASP B 117  PHE B 118  HIS B 119  GLU B 120                    
SITE     3 AC9 15 ALA B 251  GLU B 255  ILE B 256  ARG B 259                    
SITE     4 AC9 15 GLY D 218  ARG D 219  GLY D 220                               
SITE     1 BC1 18 LEU C   8  GLY C  10  GLY C  11  GLN C  82                    
SITE     2 BC1 18 PRO C  85  ASP C  86  GLY C  87  LEU C 108                    
SITE     3 BC1 18 ASP C 110  TYR C 145  GLY C 146  GLU C 161                    
SITE     4 BC1 18 LYS C 162  VAL C 172  TYR C 176  ARG C 194                    
SITE     5 BC1 18 GLU C 196  THR C 200                                          
SITE     1 BC2 16 GLY A 218  ARG A 219  GLY A 220  LEU C  45                    
SITE     2 BC2 16 TYR C 114  GLY C 115  HIS C 116  ASP C 117                    
SITE     3 BC2 16 PHE C 118  HIS C 119  GLU C 120  VAL C 250                    
SITE     4 BC2 16 ALA C 251  GLU C 255  ARG C 259  TYR C 293                    
SITE     1 BC3 18 LEU D   8  GLY D  10  GLY D  11  GLN D  26                    
SITE     2 BC3 18 GLN D  82  PRO D  85  ASP D  86  GLY D  87                    
SITE     3 BC3 18 ASP D 110  GLY D 146  GLU D 161  LYS D 162                    
SITE     4 BC3 18 VAL D 172  THR D 173  TYR D 176  ARG D 194                    
SITE     5 BC3 18 GLU D 196  THR D 200                                          
SITE     1 BC4 16 ILE B 216  GLY B 218  ARG B 219  GLY B 220                    
SITE     2 BC4 16 LEU D  45  TYR D 114  GLY D 115  HIS D 116                    
SITE     3 BC4 16 ASP D 117  PHE D 118  HIS D 119  ALA D 251                    
SITE     4 BC4 16 GLU D 255  ILE D 256  ARG D 259  TYR D 293                    
CRYST1   71.087  138.557  139.676  90.00  90.00  90.00 P 21 21 21   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      0.014067  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007217  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007159        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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