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Database: PDB
Entry: 1FZW
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HEADER    TRANSFERASE                             04-OCT-00   1FZW              
TITLE     THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND                   
TITLE    2 REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE              
TITLE    3 (RMLA). APO ENZYME.                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE;                 
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA);           
COMPND   5 EC: 2.7.7.24;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 287;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET23A(+)                                 
KEYWDS    RHAMNOSE, NUCLEOTIDYLTRANSFERASE, PYROPHOSPHORYLASE,                  
KEYWDS   2 THYMIDYLYLTRANSFERASE, ALLOSTERY                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.BLANKENFELDT,M.ASUNCION,J.S.LAM,J.H.NAISMITH                        
REVDAT   3   24-FEB-09 1FZW    1       VERSN                                    
REVDAT   2   01-APR-03 1FZW    1       JRNL                                     
REVDAT   1   27-DEC-00 1FZW    0                                                
JRNL        AUTH   W.BLANKENFELDT,M.ASUNCION,J.S.LAM,J.H.NAISMITH               
JRNL        TITL   THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM              
JRNL        TITL 2 AND REGULATION OF GLUCOSE-1-PHOSPHATE                        
JRNL        TITL 3 THYMIDYLYLTRANSFERASE (RMLA).                                
JRNL        REF    EMBO J.                       V.  19  6652 2000              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   11118200                                                     
JRNL        DOI    10.1093/EMBOJ/19.24.6652                                     
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   W.BLANKENFELDT,M.F.GIRAUD,G.LEONARD,R.RAHIM,                 
REMARK   1  AUTH 2 C.CREUZENET,J.S.LAM,J.H.NAISMITH                             
REMARK   1  TITL   THE PURIFICATION, CRYSTALLISATION AND PRELIMINARY            
REMARK   1  TITL 2 STRUCTURAL CHARACTERISATION OF GLUCOSE-1-PHOSPHATE           
REMARK   1  TITL 3 THYMIDYLYLTRANSFERASE (RMLA), THE FIRST ENZYME OF            
REMARK   1  TITL 4 THE DTDP-L-RHAMNOSE SYNTHESIS PATHWAY FROM                   
REMARK   1  TITL 5 PSEUDOMONAS AERUGINOSA                                       
REMARK   1  REF    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           
REMARK   1  TITL 2 THYMIDINE DIPHOSPHATE D-GLUCOSE PYROPHOSPHORYLASE            
REMARK   1  REF    J.BIOL.CHEM.                  V. 240   398 1965              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5                                             
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 73.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 190758                         
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) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 10141                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 12512                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.80                        
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE SET COUNT          : 623                          
REMARK   3   BIN FREE R VALUE                    : 0.4500                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 18516                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 100                                     
REMARK   3   SOLVENT ATOMS            : 2478                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.53                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.28000                                              
REMARK   3    B22 (A**2) : -0.10000                                             
REMARK   3    B33 (A**2) : -0.07000                                             
REMARK   3    B12 (A**2) : -0.19000                                             
REMARK   3    B13 (A**2) : -0.13000                                             
REMARK   3    B23 (A**2) : -0.09000                                             
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): 0.220         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.180         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.570        
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   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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 1FZW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB012058.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-FEB-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 202988                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 72.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.99                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA-CITRATE,  0.5 M LI-             
REMARK 280  SULFATE, 9-11% (W/V) PEG 6000, PH 4.6, VAPOR DIFFUSION,             
REMARK 280  SITTING DROP, TEMPERATURE 292K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER THAT CAN BE            
REMARK 300 DESCRIBED AS A DIMER OF DIMERS                                       
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14130 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 43940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -179.0 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: 14640 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 43530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -213.0 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 D     1                                                      
REMARK 465     MET E     1                                                      
REMARK 465     MET G     1                                                      
REMARK 465     MET H     1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLY C    13     O    HOH C  5196              1.92            
REMARK 500   O    HOH G  4974     O    HOH G  5200              1.92            
REMARK 500   O    HOH A  3792     O    HOH A  3828              1.92            
REMARK 500   O    HOH D  3856     O    HOH D  3939              1.95            
REMARK 500   O    HOH B  3945     O    HOH B  3969              1.97            
REMARK 500   OE2  GLU F   269     O    HOH F  4984              1.97            
REMARK 500   O    HOH A  3921     O    HOH C  5044              1.99            
REMARK 500   OG   SER C    55     O    HOH C  5263              2.00            
REMARK 500   O    HOH H  6285     O    HOH H  6378              2.01            
REMARK 500   O    HOH G  5102     O    HOH G  5182              2.02            
REMARK 500   N    PHE E    98     O    HOH E  6239              2.02            
REMARK 500   O    HOH G  5090     O    HOH G  5200              2.02            
REMARK 500   O    HOH G  4968     O    HOH G  5041              2.03            
REMARK 500   O    HOH F  4745     O    HOH F  4946              2.04            
REMARK 500   N    GLY E   227     O    HOH E  6150              2.04            
REMARK 500   O    HOH C  5115     O    HOH C  5233              2.04            
REMARK 500   O    HOH C  5111     O    HOH C  5153              2.04            
REMARK 500   OD1  ASP B   141     O    HOH B  3954              2.07            
REMARK 500   O    HOH C  5146     O    HOH C  5255              2.07            
REMARK 500   O    HOH B  3781     O    HOH B  3835              2.08            
REMARK 500   OE1  GLN G   127     O    HOH G  5199              2.09            
REMARK 500   OE1  GLN G   152     O    HOH G  5042              2.09            
REMARK 500   OE2  GLU B   149     O    HOH B  3960              2.09            
REMARK 500   N    LYS H     2     O    HOH H  6268              2.09            
REMARK 500   O    HOH D  3966     O    HOH D  4034              2.09            
REMARK 500   NE2  GLN E    26     O    HOH E  6286              2.09            
REMARK 500   O    HOH C  5044     O    HOH C  5204              2.10            
REMARK 500   O    HOH G  4930     O    HOH G  5071              2.11            
REMARK 500   O    GLN E    26     O    HOH E  6299              2.11            
REMARK 500   OE2  GLU C   234     O    HOH C  5256              2.11            
REMARK 500   O    HOH E  6146     O    HOH E  6284              2.11            
REMARK 500   OD2  ASP F   141     NH2  ARG F   144              2.12            
REMARK 500   NH2  ARG F    15     O    HOH F  4951              2.12            
REMARK 500   OD1  ASP A   141     O    HOH A  3913              2.12            
REMARK 500   O    HOH G  5261     O    HOH H  6148              2.12            
REMARK 500   O    HOH D  3855     O    HOH D  3992              2.13            
REMARK 500   CD2  HIS C   119     O    HOH C  5244              2.13            
REMARK 500   O    HOH H  6257     O    HOH H  6320              2.14            
REMARK 500   O    HOH F  4803     O    HOH F  5013              2.14            
REMARK 500   O    HOH B  3798     O    HOH B  3981              2.14            
REMARK 500   NE2  HIS B    17     O    HOH B  3873              2.14            
REMARK 500   O    HOH A  3871     O    HOH A  3875              2.14            
REMARK 500   NH1  ARG B   128     O    HOH B  3973              2.15            
REMARK 500   NH2  ARG E   128     OE2  GLU E   215              2.15            
REMARK 500   O    HOH G  5178     O    HOH G  5192              2.15            
REMARK 500   NE2  GLN E   260     O    HOH E  6211              2.15            
REMARK 500   OE1  GLN A    90     O    HOH A  3877              2.15            
REMARK 500   NE2  GLN E   260     O    HOH E  6211              2.16            
REMARK 500   NH1  ARG E   128     OG   SER E   133              2.16            
REMARK 500   O    HOH C  5100     O    HOH C  5111              2.16            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      69 CLOSE CONTACTS.                               
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OG   SER G    84     O    HOH F  4852     1655     1.25            
REMARK 500   O    HOH A  3776     O    HOH F  4954     1566     1.99            
REMARK 500   O    HOH F  4955     O    HOH G  5148     1455     2.06            
REMARK 500   O    HOH G  5209     O    HOH H  6340     1565     2.09            
REMARK 500   O    HOH F  4950     O    HOH G  4974     1455     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR A  38   CE1   TYR A  38   CZ      0.085                       
REMARK 500    ARG A 128   CZ    ARG A 128   NH2    -0.131                       
REMARK 500    VAL A 148   CB    VAL A 148   CG1    -0.128                       
REMARK 500    SER A 213   CB    SER A 213   OG      0.086                       
REMARK 500    TYR A 221   CE2   TYR A 221   CD2     0.092                       
REMARK 500    LYS A 249   CE    LYS A 249   NZ      0.166                       
REMARK 500    MET B  35   CG    MET B  35   SD     -0.176                       
REMARK 500    TYR B 114   CE2   TYR B 114   CD2    -0.109                       
REMARK 500    PHE B 135   CZ    PHE B 135   CE2    -0.128                       
REMARK 500    TYR B 145   CE1   TYR B 145   CZ     -0.084                       
REMARK 500    TYR B 178   CD1   TYR B 178   CE1     0.098                       
REMARK 500    GLN B 180   CG    GLN B 180   CD      0.155                       
REMARK 500    ARG B 245   CG    ARG B 245   CD     -0.167                       
REMARK 500    PHE C  92   CE1   PHE C  92   CZ     -0.138                       
REMARK 500    TYR C 137   CZ    TYR C 137   CE2    -0.082                       
REMARK 500    TYR C 206   CG    TYR C 206   CD1    -0.097                       
REMARK 500    ALA C 222   CA    ALA C 222   CB     -0.129                       
REMARK 500    ALA C 257   CA    ALA C 257   CB     -0.136                       
REMARK 500    MET D  35   CG    MET D  35   SD     -0.248                       
REMARK 500    PHE D  92   CB    PHE D  92   CG     -0.106                       
REMARK 500    GLU D 120   CD    GLU D 120   OE1     0.078                       
REMARK 500    GLU D 120   CD    GLU D 120   OE2     0.075                       
REMARK 500    TYR D 137   CE2   TYR D 137   CD2     0.107                       
REMARK 500    TYR D 206   CE2   TYR D 206   CD2    -0.095                       
REMARK 500    TYR E  38   CG    TYR E  38   CD1     0.080                       
REMARK 500    GLU E 120   CD    GLU E 120   OE1     0.074                       
REMARK 500    TYR E 137   CE2   TYR E 137   CD2     0.103                       
REMARK 500    LYS E 249   CD    LYS E 249   CE      0.206                       
REMARK 500    TYR E 280   CD1   TYR E 280   CE1     0.104                       
REMARK 500    ILE F  51   N     ILE F  51   CA     -0.125                       
REMARK 500    TYR F  79   CE1   TYR F  79   CZ      0.094                       
REMARK 500    SER F 124   CB    SER F 124   OG      0.083                       
REMARK 500    TYR F 137   CG    TYR F 137   CD2    -0.103                       
REMARK 500    ARG F 144   CG    ARG F 144   CD      0.154                       
REMARK 500    VAL F 172   CB    VAL F 172   CG1     0.136                       
REMARK 500    LYS F 249   CD    LYS F 249   CE      0.153                       
REMARK 500    ALA F 251   CA    ALA F 251   CB      0.167                       
REMARK 500    ARG F 286   CG    ARG F 286   CD      0.166                       
REMARK 500    ALA G 105   CA    ALA G 105   CB     -0.145                       
REMARK 500    PHE G 118   CG    PHE G 118   CD1    -0.111                       
REMARK 500    PHE G 118   CE1   PHE G 118   CZ     -0.116                       
REMARK 500    PHE G 118   CZ    PHE G 118   CE2     0.117                       
REMARK 500    GLU G 120   CD    GLU G 120   OE1     0.068                       
REMARK 500    SER G 124   CB    SER G 124   OG      0.095                       
REMARK 500    ARG G 128   CB    ARG G 128   CG     -0.166                       
REMARK 500    VAL G 148   CB    VAL G 148   CG1    -0.161                       
REMARK 500    GLU G 149   CD    GLU G 149   OE2    -0.069                       
REMARK 500    TYR G 178   CZ    TYR G 178   CE2     0.081                       
REMARK 500    VAL G 214   CB    VAL G 214   CG2    -0.138                       
REMARK 500    TRP G 223   CB    TRP G 223   CG      0.124                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      63 BOND DEVIATIONS.                              
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    ASP A 117   CB  -  CG  -  OD2 ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ARG A 128   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG A 128   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ASP A 201   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG A 209   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ARG A 286   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    MET B  35   CG  -  SD  -  CE  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ASP B  69   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP B  76   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP B  86   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP B 102   CB  -  CG  -  OD2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    ASP B 117   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    LEU B 121   CB  -  CG  -  CD1 ANGL. DEV. = -12.1 DEGREES          
REMARK 500    ASP B 151   CB  -  CG  -  OD1 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ASP B 188   CB  -  CG  -  OD2 ANGL. DEV. =   8.9 DEGREES          
REMARK 500    ASP B 201   CB  -  CG  -  OD1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ARG B 209   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG B 209   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    ARG B 219   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B 245   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG B 286   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ASP C  69   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP C  86   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    PHE C 118   CB  -  CA  -  C   ANGL. DEV. =  12.9 DEGREES          
REMARK 500    ASP C 141   CB  -  CG  -  OD1 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    ARG C 144   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG C 144   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP C 151   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    GLY C 154   N   -  CA  -  C   ANGL. DEV. =  15.8 DEGREES          
REMARK 500    THR C 226   OG1 -  CB  -  CG2 ANGL. DEV. = -14.8 DEGREES          
REMARK 500    LEU C 232   CB  -  CG  -  CD1 ANGL. DEV. =  13.3 DEGREES          
REMARK 500    CYS C 252   CA  -  CB  -  SG  ANGL. DEV. =   8.2 DEGREES          
REMARK 500    ARG C 259   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG C 259   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ASP C 264   CB  -  CG  -  OD2 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    ASP D  69   CB  -  CG  -  OD1 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ASP D  76   CB  -  CG  -  OD2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ASP D  86   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP D 141   CB  -  CG  -  OD1 ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ASP D 188   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    LEU E  88   CA  -  CB  -  CG  ANGL. DEV. =  20.4 DEGREES          
REMARK 500    LEU E  88   CB  -  CG  -  CD2 ANGL. DEV. =  11.5 DEGREES          
REMARK 500    ARG E 144   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG E 144   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ASP E 151   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP E 188   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP F  59   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP F  69   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ASP F  86   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      74 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  31      -90.17     64.03                                   
REMARK 500    PRO A  85       73.90    -67.35                                   
REMARK 500    ASN A 101       48.25   -108.26                                   
REMARK 500    ASP A 179     -164.81    -79.89                                   
REMARK 500    THR A 226       41.99   -101.38                                   
REMARK 500    ALA B   9       55.46   -116.05                                   
REMARK 500    SER B  24      154.60    -45.29                                   
REMARK 500    TYR B  31      -81.03     65.35                                   
REMARK 500    ASN B 101       41.24   -106.16                                   
REMARK 500    TYR C  31      -94.22     64.48                                   
REMARK 500    SER C 192     -178.34    -60.41                                   
REMARK 500    ARG C 194       16.12    -67.46                                   
REMARK 500    THR C 226       42.43    -99.25                                   
REMARK 500    THR D  14      -58.01    -20.99                                   
REMARK 500    TYR D  31      -82.00     73.55                                   
REMARK 500    ALA D 273      -70.27    -39.72                                   
REMARK 500    THR E  14      -59.35     -7.06                                   
REMARK 500    TYR E  31      -86.38     58.41                                   
REMARK 500    PRO E 191      103.71    -47.23                                   
REMARK 500    SER E 192      162.18    -33.07                                   
REMARK 500    THR F  14      -39.21    -32.37                                   
REMARK 500    ARG F  15      -77.67    -55.43                                   
REMARK 500    LEU F  16        2.57    -62.35                                   
REMARK 500    ALA F  19      -39.98    -38.81                                   
REMARK 500    TYR F  31      -87.57     61.05                                   
REMARK 500    LEU G  16       41.49   -102.31                                   
REMARK 500    LEU G  21      -38.08    -37.13                                   
REMARK 500    TYR G  31      -82.56     67.18                                   
REMARK 500    ASP G  86       30.78    -99.65                                   
REMARK 500    ASN G 101       50.51   -107.36                                   
REMARK 500    TYR H  31      -85.19     59.81                                   
REMARK 500    THR H 226       40.27   -107.80                                   
REMARK 500    LEU H 287      -19.34    -49.76                                   
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 C 119         0.09    SIDE_CHAIN                              
REMARK 500    HIS G  17         0.07    SIDE_CHAIN                              
REMARK 500    HIS G 138         0.08    SIDE_CHAIN                              
REMARK 500    HIS H  17         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C5099        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH G5037        DISTANCE =  6.71 ANGSTROMS                       
REMARK 525    HOH D4024        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH D4026        DISTANCE =  8.46 ANGSTROMS                       
REMARK 525    HOH A3935        DISTANCE =  6.74 ANGSTROMS                       
REMARK 525    HOH A3936        DISTANCE =  6.69 ANGSTROMS                       
REMARK 525    HOH D4051        DISTANCE =  8.70 ANGSTROMS                       
REMARK 525    HOH D4052        DISTANCE =  6.53 ANGSTROMS                       
REMARK 525    HOH D4056        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH D4058        DISTANCE =  7.12 ANGSTROMS                       
REMARK 525    HOH D4059        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH H6360        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH C5260        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH F4965        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH C5271        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH E6377        DISTANCE =  6.60 ANGSTROMS                       
REMARK 525    HOH E6378        DISTANCE =  6.73 ANGSTROMS                       
REMARK 525    HOH F4978        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH E6379        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH B3985        DISTANCE =  6.91 ANGSTROMS                       
REMARK 525    HOH H6400        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH F5017        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH A4019        DISTANCE =  7.93 ANGSTROMS                       
REMARK 525    HOH B4020        DISTANCE =  6.58 ANGSTROMS                       
REMARK 525    HOH F5019        DISTANCE =  6.91 ANGSTROMS                       
REMARK 525    HOH B4021        DISTANCE =  9.18 ANGSTROMS                       
REMARK 525    HOH A4023        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH B4024        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH B4025        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH A4025        DISTANCE = 10.41 ANGSTROMS                       
REMARK 525    HOH B4028        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH B4029        DISTANCE =  5.26 ANGSTROMS                       
REMARK 525    HOH B4030        DISTANCE =  8.11 ANGSTROMS                       
REMARK 525    HOH B4034        DISTANCE = 10.45 ANGSTROMS                       
REMARK 525    HOH G5258        DISTANCE =  5.79 ANGSTROMS                       
REMARK 525    HOH G5262        DISTANCE =  5.60 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 3600                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3601                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3602                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 3603                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 3604                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 3605                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 3606                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 3607                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3700                
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 3701                
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 3702                
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3703                
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3800                
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 4700                
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 4900                
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 3704                
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 5000                
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 5001                
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 6100                
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 6101                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FXO   RELATED DB: PDB                                   
REMARK 900 1FXO IS RMLA IN COMPLEX WITH 2'-DEOXY-THYMIDINE-5'-                  
REMARK 900 MONOPHOSPHATE (TMP)                                                  
REMARK 900 RELATED ID: 1G0R   RELATED DB: PDB                                   
REMARK 900 1G0R IS RMLA IN COMPLEX WITH 2'-DEOXY-THIMIDINE (THM) AND            
REMARK 900 ALPHA-D-GLUCOSE-1-PHOSPHATE (G1P)                                    
REMARK 900 RELATED ID: 1G1L   RELATED DB: PDB                                   
REMARK 900 1G1L IS RMLA IN COMPLEX WITH 2'-DEOXY-THYMIDINE-ALPHA-D-             
REMARK 900 GLUCOSE (TDG)                                                        
REMARK 900 RELATED ID: 1G23   RELATED DB: PDB                                   
REMARK 900 1G23 IS RMLA IN COMPLEX WITH ALPHA-D-GLUCOSE-1-PHOSPHATE             
REMARK 900 (G1P)                                                                
REMARK 900 RELATED ID: 1G2V   RELATED DB: PDB                                   
REMARK 900 1G2V IS RMLA IN COMPLEX WITH 2'-DEOXY-THYMIDINE-5'-                  
REMARK 900 TRIPHOSPHATE (TTP)                                                   
REMARK 900 RELATED ID: 1G31   RELATED DB: PDB                                   
REMARK 900 1G31 IS RMLA IN COMPLEX WITH 2'-DEOXY-THYMIDINE-BETA-L-              
REMARK 900 RHAMNOSE (TDR)                                                       
DBREF  1FZW A    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1FZW B    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1FZW C    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1FZW D    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1FZW E    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1FZW F    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1FZW G    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
DBREF  1FZW H    1   293  UNP    Q9HU22   Q9HU22_PSEAE     1    293             
SEQRES   1 A  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 A  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 A  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 A  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 A  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 A  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 A  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 A  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 A  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 A  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 A  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 A  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 A  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 A  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 A  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 A  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 A  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 A  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 A  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 A  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 A  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 A  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 A  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 B  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 B  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 B  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 B  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 B  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 B  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 B  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 B  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 B  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 B  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 B  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 B  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 B  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 B  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 B  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 B  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 B  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 B  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 B  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 B  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 B  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 B  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 B  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 C  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 C  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 C  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 C  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 C  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 C  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 C  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 C  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 C  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 C  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 C  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 C  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 C  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 C  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 C  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 C  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 C  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 C  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 C  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 C  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 C  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 C  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 C  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 D  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 D  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 D  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 D  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 D  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 D  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 D  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 D  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 D  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 D  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 D  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 D  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 D  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 D  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 D  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 D  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 D  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 D  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 D  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 D  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 D  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 D  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 D  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 E  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 E  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 E  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 E  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 E  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 E  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 E  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 E  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 E  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 E  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 E  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 E  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 E  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 E  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 E  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 E  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 E  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 E  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 E  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 E  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 E  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 E  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 E  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 F  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 F  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 F  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 F  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 F  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 F  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 F  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 F  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 F  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 F  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 F  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 F  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 F  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 F  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 F  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 F  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 F  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 F  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 F  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 F  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 F  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 F  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 F  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 G  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 G  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 G  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 G  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 G  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 G  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 G  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 G  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 G  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 G  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 G  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 G  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 G  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 G  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 G  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 G  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 G  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 G  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 G  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 G  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 G  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 G  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 G  293  LEU LEU THR GLU THR VAL TYR                                  
SEQRES   1 H  293  MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY          
SEQRES   2 H  293  THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN          
SEQRES   3 H  293  LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO          
SEQRES   4 H  293  LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU          
SEQRES   5 H  293  ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN          
SEQRES   6 H  293  LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN          
SEQRES   7 H  293  TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA          
SEQRES   8 H  293  PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER          
SEQRES   9 H  293  ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP          
SEQRES  10 H  293  PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR          
SEQRES  11 H  293  GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU          
SEQRES  12 H  293  ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA          
SEQRES  13 H  293  ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN          
SEQRES  14 H  293  TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL          
SEQRES  15 H  293  VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY          
SEQRES  16 H  293  GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU          
SEQRES  17 H  293  ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR          
SEQRES  18 H  293  ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU          
SEQRES  19 H  293  ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY          
SEQRES  20 H  293  LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN          
SEQRES  21 H  293  LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA          
SEQRES  22 H  293  PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG          
SEQRES  23 H  293  LEU LEU THR GLU THR VAL TYR                                  
HET    SO4  C3600       5                                                       
HET    SO4  D3601       5                                                       
HET    SO4  A3602       5                                                       
HET    SO4  B3603       5                                                       
HET    SO4  H3604       5                                                       
HET    SO4  G3605       5                                                       
HET    SO4  F3606       5                                                       
HET    SO4  E3607       5                                                       
HET    SO4  A3700       5                                                       
HET    SO4  B3701       5                                                       
HET    SO4  C3702       5                                                       
HET    SO4  D3703       5                                                       
HET    SO4  D3800       5                                                       
HET    SO4  F4700       5                                                       
HET    SO4  G4900       5                                                       
HET    SO4  G3704       5                                                       
HET    SO4  C5000       5                                                       
HET    SO4  E5001       5                                                       
HET    SO4  E6100       5                                                       
HET    SO4  H6101       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   9  SO4    20(O4 S 2-)                                                  
FORMUL  29  HOH   *2478(H2 O)                                                   
HELIX    1   1 GLY A   13  HIS A   17  5                                   5    
HELIX    2   2 PRO A   18  ILE A   23  1                                   6    
HELIX    3   3 SER A   24  LEU A   27  5                                   4    
HELIX    4   4 ILE A   36  ALA A   46  1                                  11    
HELIX    5   5 ASP A   59  GLY A   68  1                                  10    
HELIX    6   6 GLY A   70  GLY A   74  5                                   5    
HELIX    7   7 GLY A   87  ALA A   89  5                                   3    
HELIX    8   8 GLN A   90  GLY A   95  1                                   6    
HELIX    9   9 GLY A   95  GLY A  100  1                                   6    
HELIX   10  10 ASP A  117  ARG A  128  1                                  12    
HELIX   11  11 ASP A  141  ARG A  144  5                                   4    
HELIX   12  12 GLN A  181  ASP A  188  1                                   8    
HELIX   13  13 GLU A  198  ARG A  209  1                                  12    
HELIX   14  14 THR A  228  GLY A  247  1                                  20    
HELIX   15  15 CYS A  252  GLN A  260  1                                   9    
HELIX   16  16 ASP A  264  ALA A  273  1                                  10    
HELIX   17  17 PRO A  274  ALA A  276  5                                   3    
HELIX   18  18 ASN A  278  GLU A  290  1                                  13    
HELIX   19  19 GLY B   13  HIS B   17  5                                   5    
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 GLY B   87  ALA B   89  5                                   3    
HELIX   25  25 GLN B   90  GLY B   95  1                                   6    
HELIX   26  26 GLY B   95  GLY B  100  1                                   6    
HELIX   27  27 ASP B  117  ARG B  128  1                                  12    
HELIX   28  28 ASP B  141  ARG B  144  5                                   4    
HELIX   29  29 GLN B  181  LEU B  189  1                                   9    
HELIX   30  30 GLU B  198  ARG B  209  1                                  12    
HELIX   31  31 THR B  228  GLY B  247  1                                  20    
HELIX   32  32 CYS B  252  GLN B  260  1                                   9    
HELIX   33  33 ASP B  264  ALA B  273  1                                  10    
HELIX   34  34 PRO B  274  ALA B  276  5                                   3    
HELIX   35  35 ASN B  278  GLU B  290  1                                  13    
HELIX   36  36 GLY C   13  HIS C   17  5                                   5    
HELIX   37  37 PRO C   18  ALA C   22  5                                   5    
HELIX   38  38 SER C   24  LEU C   27  5                                   4    
HELIX   39  39 ILE C   36  ALA C   46  1                                  11    
HELIX   40  40 ASP C   59  GLY C   68  1                                  10    
HELIX   41  41 GLY C   70  GLY C   74  5                                   5    
HELIX   42  42 GLY C   87  ALA C   89  5                                   3    
HELIX   43  43 GLN C   90  GLY C   95  1                                   6    
HELIX   44  44 GLY C   95  GLY C  100  1                                   6    
HELIX   45  45 ASP C  117  ARG C  128  1                                  12    
HELIX   46  46 ASP C  141  ARG C  144  5                                   4    
HELIX   47  47 GLN C  181  LEU C  189  1                                   9    
HELIX   48  48 GLU C  198  GLU C  208  1                                  11    
HELIX   49  49 THR C  228  GLY C  247  1                                  20    
HELIX   50  50 CYS C  252  GLN C  260  1                                   9    
HELIX   51  51 ASP C  264  ALA C  273  1                                  10    
HELIX   52  52 PRO C  274  ALA C  276  5                                   3    
HELIX   53  53 ASN C  278  GLU C  290  1                                  13    
HELIX   54  54 GLY D   13  HIS D   17  5                                   5    
HELIX   55  55 SER D   24  LEU D   27  5                                   4    
HELIX   56  56 ILE D   36  ALA D   46  1                                  11    
HELIX   57  57 ASP D   59  GLY D   68  1                                  10    
HELIX   58  58 GLY D   70  GLY D   74  5                                   5    
HELIX   59  59 GLY D   87  ALA D   89  5                                   3    
HELIX   60  60 GLN D   90  GLY D   95  1                                   6    
HELIX   61  61 GLY D   95  GLY D  100  1                                   6    
HELIX   62  62 ASP D  117  GLN D  127  1                                  11    
HELIX   63  63 ASP D  141  ARG D  144  5                                   4    
HELIX   64  64 GLN D  181  ASP D  188  1                                   8    
HELIX   65  65 GLU D  198  GLU D  208  1                                  11    
HELIX   66  66 THR D  228  GLY D  247  1                                  20    
HELIX   67  67 CYS D  252  GLN D  260  1                                   9    
HELIX   68  68 ASP D  264  ALA D  273  1                                  10    
HELIX   69  69 PRO D  274  ALA D  276  5                                   3    
HELIX   70  70 ASN D  278  GLU D  290  1                                  13    
HELIX   71  71 GLY E   13  HIS E   17  5                                   5    
HELIX   72  72 SER E   24  LEU E   27  5                                   4    
HELIX   73  73 ILE E   36  ALA E   46  1                                  11    
HELIX   74  74 ASP E   59  GLY E   68  1                                  10    
HELIX   75  75 GLY E   70  GLY E   74  5                                   5    
HELIX   76  76 GLY E   87  ALA E   89  5                                   3    
HELIX   77  77 GLN E   90  GLY E   95  1                                   6    
HELIX   78  78 GLY E   95  GLY E  100  1                                   6    
HELIX   79  79 ASP E  117  ARG E  128  1                                  12    
HELIX   80  80 ASP E  141  ARG E  144  5                                   4    
HELIX   81  81 GLN E  181  ASP E  188  1                                   8    
HELIX   82  82 GLU E  198  GLU E  208  1                                  11    
HELIX   83  83 THR E  228  GLY E  247  1                                  20    
HELIX   84  84 CYS E  252  GLN E  260  1                                   9    
HELIX   85  85 ASP E  264  ALA E  273  1                                  10    
HELIX   86  86 PRO E  274  ALA E  276  5                                   3    
HELIX   87  87 ASN E  278  LEU E  287  1                                  10    
HELIX   88  88 SER F   24  LEU F   27  5                                   4    
HELIX   89  89 ILE F   36  ALA F   46  1                                  11    
HELIX   90  90 ASP F   59  GLY F   68  1                                  10    
HELIX   91  91 GLY F   70  GLY F   74  5                                   5    
HELIX   92  92 ALA F   89  GLY F   95  1                                   7    
HELIX   93  93 GLY F   95  GLY F  100  1                                   6    
HELIX   94  94 ASP F  117  ARG F  128  1                                  12    
HELIX   95  95 ASP F  141  ARG F  144  5                                   4    
HELIX   96  96 GLN F  181  ASP F  188  1                                   8    
HELIX   97  97 GLU F  198  GLU F  208  1                                  11    
HELIX   98  98 THR F  228  GLY F  247  1                                  20    
HELIX   99  99 CYS F  252  GLN F  260  1                                   9    
HELIX  100 100 ASP F  264  ALA F  273  1                                  10    
HELIX  101 101 PRO F  274  ALA F  276  5                                   3    
HELIX  102 102 ASN F  278  LEU F  287  1                                  10    
HELIX  103 103 GLY G   13  HIS G   17  5                                   5    
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 GLY G   87  ALA G   89  5                                   3    
HELIX  109 109 GLN G   90  GLY G   95  1                                   6    
HELIX  110 110 GLY G   95  GLY G  100  1                                   6    
HELIX  111 111 ASP G  117  ARG G  128  1                                  12    
HELIX  112 112 ASP G  141  ARG G  144  5                                   4    
HELIX  113 113 GLN G  181  ASP G  188  1                                   8    
HELIX  114 114 GLU G  198  ARG G  209  1                                  12    
HELIX  115 115 THR G  228  GLY G  247  1                                  20    
HELIX  116 116 CYS G  252  GLN G  260  1                                   9    
HELIX  117 117 ASP G  264  ALA G  273  1                                  10    
HELIX  118 118 PRO G  274  ALA G  276  5                                   3    
HELIX  119 119 ASN G  278  THR G  289  1                                  12    
HELIX  120 120 GLY H   13  HIS H   17  5                                   5    
HELIX  121 121 SER H   24  LEU H   27  5                                   4    
HELIX  122 122 ILE H   36  ALA H   46  1                                  11    
HELIX  123 123 ASP H   59  GLY H   68  1                                  10    
HELIX  124 124 GLY H   70  GLY H   74  5                                   5    
HELIX  125 125 GLY H   87  ALA H   89  5                                   3    
HELIX  126 126 GLN H   90  GLY H   95  1                                   6    
HELIX  127 127 GLY H   95  GLY H  100  1                                   6    
HELIX  128 128 ASP H  117  ARG H  128  1                                  12    
HELIX  129 129 ASP H  141  ARG H  144  5                                   4    
HELIX  130 130 GLN H  181  LEU H  189  1                                   9    
HELIX  131 131 GLU H  198  ARG H  209  1                                  12    
HELIX  132 132 THR H  228  GLY H  247  1                                  20    
HELIX  133 133 CYS H  252  GLN H  260  1                                   9    
HELIX  134 134 ASP H  264  ALA H  273  1                                  10    
HELIX  135 135 PRO H  274  ALA H  276  5                                   3    
HELIX  136 136 ASN H  278  LEU H  287  1                                  10    
HELIX  137 137 LEU H  288  GLU H  290  5                                   3    
SHEET    1   A 7 ASP A  76  VAL A  81  0                                        
SHEET    2   A 7 GLU A  50  SER A  55  1  N  ILE A  51   O  ASP A  76           
SHEET    3   A 7 ARG A   3  LEU A   8  1  O  GLY A   5   N  LEU A  52           
SHEET    4   A 7 LEU A 103  LEU A 108  1  O  LEU A 103   N  LYS A   4           
SHEET    5   A 7 TYR A 170  TYR A 178 -1  O  GLY A 174   N  LEU A 108           
SHEET    6   A 7 ALA A 132  HIS A 138 -1  O  SER A 133   N  PHE A 177           
SHEET    7   A 7 LEU A 212  ILE A 216  1  N  SER A 213   O  ALA A 132           
SHEET    1   B 2 PRO A  29  VAL A  30  0                                        
SHEET    2   B 2 LYS A  33  PRO A  34 -1  O  LYS A  33   N  VAL A  30           
SHEET    1   C 2 ASN A 111  TYR A 114  0                                        
SHEET    2   C 2 ALA A 222  ASP A 225 -1  O  ALA A 222   N  TYR A 114           
SHEET    1   D 2 GLY A 146  PHE A 150  0                                        
SHEET    2   D 2 ALA A 156  GLU A 161 -1  N  ILE A 157   O  GLU A 149           
SHEET    1   E 7 ASP B  76  VAL B  81  0                                        
SHEET    2   E 7 GLU B  50  SER B  55  1  O  ILE B  51   N  GLN B  78           
SHEET    3   E 7 ARG B   3  LEU B   8  1  N  GLY B   5   O  GLU B  50           
SHEET    4   E 7 LEU B 103  LEU B 108  1  O  LEU B 103   N  LYS B   4           
SHEET    5   E 7 TYR B 170  TYR B 178 -1  O  GLY B 174   N  LEU B 108           
SHEET    6   E 7 ALA B 132  HIS B 138 -1  O  SER B 133   N  PHE B 177           
SHEET    7   E 7 LEU B 212  ILE B 216  1  N  SER B 213   O  ALA B 132           
SHEET    1   F 2 PRO B  29  VAL B  30  0                                        
SHEET    2   F 2 LYS B  33  PRO B  34 -1  O  LYS B  33   N  VAL B  30           
SHEET    1   G 2 ASN B 111  TYR B 114  0                                        
SHEET    2   G 2 ALA B 222  ASP B 225 -1  N  ALA B 222   O  TYR B 114           
SHEET    1   H 2 GLY B 146  PHE B 150  0                                        
SHEET    2   H 2 ALA B 156  GLU B 161 -1  N  ILE B 157   O  GLU B 149           
SHEET    1   I 7 ASP C  76  VAL C  81  0                                        
SHEET    2   I 7 GLU C  50  SER C  55  1  O  ILE C  51   N  GLN C  78           
SHEET    3   I 7 ARG C   3  LEU C   8  1  N  GLY C   5   O  GLU C  50           
SHEET    4   I 7 LEU C 103  LEU C 108  1  O  LEU C 103   N  LYS C   4           
SHEET    5   I 7 TYR C 170  TYR C 178 -1  O  GLY C 174   N  LEU C 108           
SHEET    6   I 7 ALA C 132  HIS C 138 -1  N  SER C 133   O  PHE C 177           
SHEET    7   I 7 LEU C 212  ILE C 216  1  N  SER C 213   O  ALA C 132           
SHEET    1   J 2 PRO C  29  VAL C  30  0                                        
SHEET    2   J 2 LYS C  33  PRO C  34 -1  O  LYS C  33   N  VAL C  30           
SHEET    1   K 2 ASN C 111  TYR C 114  0                                        
SHEET    2   K 2 ALA C 222  ASP C 225 -1  N  ALA C 222   O  TYR C 114           
SHEET    1   L 2 GLY C 146  PHE C 150  0                                        
SHEET    2   L 2 ALA C 156  GLU C 161 -1  N  ILE C 157   O  GLU C 149           
SHEET    1   M 7 ASP D  76  VAL D  81  0                                        
SHEET    2   M 7 GLU D  50  SER D  55  1  O  ILE D  51   N  GLN D  78           
SHEET    3   M 7 ARG D   3  LEU D   8  1  O  GLY D   5   N  LEU D  52           
SHEET    4   M 7 LEU D 103  LEU D 108  1  O  LEU D 103   N  LYS D   4           
SHEET    5   M 7 TYR D 170  TYR D 178 -1  O  GLY D 174   N  LEU D 108           
SHEET    6   M 7 ALA D 132  HIS D 138 -1  O  SER D 133   N  PHE D 177           
SHEET    7   M 7 LEU D 212  ILE D 216  1  N  SER D 213   O  ALA D 132           
SHEET    1   N 2 PRO D  29  VAL D  30  0                                        
SHEET    2   N 2 LYS D  33  PRO D  34 -1  O  LYS D  33   N  VAL D  30           
SHEET    1   O 2 ASN D 111  TYR D 114  0                                        
SHEET    2   O 2 ALA D 222  ASP D 225 -1  N  ALA D 222   O  TYR D 114           
SHEET    1   P 2 GLY D 146  PHE D 150  0                                        
SHEET    2   P 2 ALA D 156  GLU D 161 -1  N  ILE D 157   O  GLU D 149           
SHEET    1   Q 7 ASP E  76  VAL E  81  0                                        
SHEET    2   Q 7 GLU E  50  SER E  55  1  O  ILE E  51   N  GLN E  78           
SHEET    3   Q 7 ARG E   3  LEU E   8  1  O  GLY E   5   N  LEU E  52           
SHEET    4   Q 7 LEU E 103  LEU E 108  1  O  LEU E 103   N  LYS E   4           
SHEET    5   Q 7 TYR E 170  TYR E 178 -1  O  GLY E 174   N  LEU E 108           
SHEET    6   Q 7 ALA E 132  HIS E 138 -1  O  SER E 133   N  PHE E 177           
SHEET    7   Q 7 LEU E 212  ILE E 216  1  N  SER E 213   O  ALA E 132           
SHEET    1   R 2 PRO E  29  VAL E  30  0                                        
SHEET    2   R 2 LYS E  33  PRO E  34 -1  O  LYS E  33   N  VAL E  30           
SHEET    1   S 2 ASN E 111  TYR E 114  0                                        
SHEET    2   S 2 ALA E 222  ASP E 225 -1  O  ALA E 222   N  TYR E 114           
SHEET    1   T 2 GLY E 146  PHE E 150  0                                        
SHEET    2   T 2 ALA E 156  GLU E 161 -1  N  ILE E 157   O  GLU E 149           
SHEET    1   U 7 ASP F  76  VAL F  81  0                                        
SHEET    2   U 7 GLU F  50  SER F  55  1  O  ILE F  51   N  GLN F  78           
SHEET    3   U 7 ARG F   3  LEU F   8  1  N  GLY F   5   O  GLU F  50           
SHEET    4   U 7 LEU F 103  LEU F 108  1  O  LEU F 103   N  LYS F   4           
SHEET    5   U 7 TYR F 170  TYR F 178 -1  O  GLY F 174   N  LEU F 108           
SHEET    6   U 7 ALA F 132  HIS F 138 -1  O  SER F 133   N  PHE F 177           
SHEET    7   U 7 LEU F 212  ILE F 216  1  N  SER F 213   O  ALA F 132           
SHEET    1   V 2 PRO F  29  VAL F  30  0                                        
SHEET    2   V 2 LYS F  33  PRO F  34 -1  O  LYS F  33   N  VAL F  30           
SHEET    1   W 2 ASN F 111  TYR F 114  0                                        
SHEET    2   W 2 ALA F 222  ASP F 225 -1  N  ALA F 222   O  TYR F 114           
SHEET    1   X 2 GLY F 146  PHE F 150  0                                        
SHEET    2   X 2 ALA F 156  GLU F 161 -1  N  ILE F 157   O  GLU F 149           
SHEET    1   Y 3 LEU G 212  ILE G 216  0                                        
SHEET    2   Y 3 ALA G 132  HIS G 138  1  O  ALA G 132   N  SER G 213           
SHEET    3   Y 3 TYR G 170  VAL G 172 -1  O  ALA G 171   N  TYR G 137           
SHEET    1   Z 7 LEU G 212  ILE G 216  0                                        
SHEET    2   Z 7 ALA G 132  HIS G 138  1  O  ALA G 132   N  SER G 213           
SHEET    3   Z 7 LEU G 175  TYR G 178 -1  N  PHE G 177   O  SER G 133           
SHEET    4   Z 7 LEU G 103  LEU G 108 -1  O  SER G 104   N  TYR G 178           
SHEET    5   Z 7 ARG G   3  ALA G   9  1  N  LYS G   4   O  LEU G 103           
SHEET    6   Z 7 GLU G  50  SER G  55  1  O  GLU G  50   N  GLY G   5           
SHEET    7   Z 7 ASP G  76  VAL G  81  1  O  ASP G  76   N  ILE G  51           
SHEET    1  AA 2 PRO G  29  VAL G  30  0                                        
SHEET    2  AA 2 LYS G  33  PRO G  34 -1  O  LYS G  33   N  VAL G  30           
SHEET    1  AB 2 ASN G 111  TYR G 114  0                                        
SHEET    2  AB 2 ALA G 222  ASP G 225 -1  N  ALA G 222   O  TYR G 114           
SHEET    1  AC 2 GLY G 146  PHE G 150  0                                        
SHEET    2  AC 2 ALA G 156  GLU G 161 -1  N  ILE G 157   O  GLU G 149           
SHEET    1  AD 7 ASP H  76  VAL H  81  0                                        
SHEET    2  AD 7 GLU H  50  SER H  55  1  N  ILE H  51   O  ASP H  76           
SHEET    3  AD 7 ARG H   3  LEU H   8  1  O  GLY H   5   N  LEU H  52           
SHEET    4  AD 7 LEU H 103  LEU H 108  1  O  LEU H 103   N  LYS H   4           
SHEET    5  AD 7 TYR H 170  TYR H 178 -1  O  GLY H 174   N  LEU H 108           
SHEET    6  AD 7 ALA H 132  HIS H 138 -1  O  SER H 133   N  PHE H 177           
SHEET    7  AD 7 LEU H 212  ILE H 216  1  N  SER H 213   O  ALA H 132           
SHEET    1  AE 2 PRO H  29  VAL H  30  0                                        
SHEET    2  AE 2 LYS H  33  PRO H  34 -1  O  LYS H  33   N  VAL H  30           
SHEET    1  AF 2 ASN H 111  TYR H 114  0                                        
SHEET    2  AF 2 ALA H 222  ASP H 225 -1  N  ALA H 222   O  TYR H 114           
SHEET    1  AG 2 GLY H 146  PHE H 150  0                                        
SHEET    2  AG 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        -0.20                     
CISPEP   2 HIS B   17    PRO B   18          0        -1.24                     
CISPEP   3 HIS C   17    PRO C   18          0         5.67                     
CISPEP   4 HIS D   17    PRO D   18          0        -1.17                     
CISPEP   5 HIS E   17    PRO E   18          0         1.97                     
CISPEP   6 HIS F   17    PRO F   18          0        -4.95                     
CISPEP   7 HIS G   17    PRO G   18          0         1.33                     
CISPEP   8 HIS H   17    PRO H   18          0        -0.56                     
SITE     1 AC1  9 HIS A 116  ASP A 117  GLY C 218  ARG C 219                    
SITE     2 AC1  9 GLY C 220  HOH C5007  HOH C5064  HOH C5229                    
SITE     3 AC1  9 HOH C5240                                                     
SITE     1 AC2  9 HIS B 116  ASP B 117  HOH B3735  HOH B3800                    
SITE     2 AC2  9 GLY D 218  ARG D 219  GLY D 220  HOH D3923                    
SITE     3 AC2  9 HOH D3941                                                     
SITE     1 AC3 10 GLY A 218  ARG A 219  GLY A 220  HOH A3723                    
SITE     2 AC3 10 HOH A3761  HOH A3839  HIS C 116  ASP C 117                    
SITE     3 AC3 10 HOH C5022  HOH C5197                                          
SITE     1 AC4 11 GLY B 218  ARG B 219  GLY B 220  HOH B3765                    
SITE     2 AC4 11 HOH B3771  HOH B3792  HIS D 116  ASP D 117                    
SITE     3 AC4 11 HOH D3806  HOH D3895  HOH D4030                               
SITE     1 AC5 11 HIS E 116  ASP E 117  HIS E 119  HOH E6110                    
SITE     2 AC5 11 HOH E6270  GLY H 218  ARG H 219  GLY H 220                    
SITE     3 AC5 11 HOH H6106  HOH H6174  HOH H6365                               
SITE     1 AC6 11 HIS F 116  ASP F 117  HOH F4712  HOH F4898                    
SITE     2 AC6 11 HOH F4928  GLY G 218  ARG G 219  GLY G 220                    
SITE     3 AC6 11 HOH G4991  HOH G5003  HOH G5027                               
SITE     1 AC7  9 GLY F 218  ARG F 219  GLY F 220  HOH F4765                    
SITE     2 AC7  9 HOH F4867  HOH F4874  HIS G 116  ASP G 117                    
SITE     3 AC7  9 HOH G4913                                                     
SITE     1 AC8 10 GLY E 218  ARG E 219  GLY E 220  HOH E6161                    
SITE     2 AC8 10 HOH E6177  HOH E6202  HIS H 116  ASP H 117                    
SITE     3 AC8 10 HOH H6142  HOH H6222                                          
SITE     1 AC9  7 ARG A 128  GLU A 215  HOH A3801  ASP F 151                    
SITE     2 AC9  7 GLN F 152  HOH F4877  HOH F4938                               
SITE     1 BC1  6 ARG B 128  GLU B 215  HOH B3986  HOH B4011                    
SITE     2 BC1  6 ASP E 151  GLN E 152                                          
SITE     1 BC2  3 ARG C 128  GLN C 129  THR C 130                               
SITE     1 BC3  2 GLN D 129  THR D 130                                          
SITE     1 BC4  6 ASP D 151  GLN D 152  ARG H 128  GLU H 215                    
SITE     2 BC4  6 HOH H6192  HOH H6269                                          
SITE     1 BC5  3 ARG F 128  GLN F 129  THR F 130                               
SITE     1 BC6  4 ARG G  62  HOH G5186  ARG H  62  GLN H  65                    
SITE     1 BC7  6 ASP C 151  GLN C 152  ARG G 128  GLU G 215                    
SITE     2 BC7  6 HOH G5068  HOH G5204                                          
SITE     1 BC8  2 ARG C  62  ARG D  62                                          
SITE     1 BC9  3 ARG E  62  HOH E6355  ARG F  62                               
SITE     1 CC1  5 GLN E 127  ARG E 128  GLN E 129  THR E 130                    
SITE     2 CC1  5 HOH E6265                                                     
SITE     1 CC2  4 SER H  12  GLY H  13  THR H  14  ARG H  15                    
CRYST1   71.656   73.656  134.469  89.98  80.91  80.91 P 1           8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013956 -0.002233 -0.002291        0.00000                         
SCALE2      0.000000  0.013749  0.000348        0.00000                         
SCALE3      0.000000  0.000000  0.007534        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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