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Database: PDB
Entry: 3GP3
LinkDB: 3GP3
Original site: 3GP3 
HEADER    ISOMERASE                               20-MAR-09   3GP3              
TITLE     CRYSTAL STRUCTURE OF PHOSPHOGLYCEROMUTASE FROM BURKHOLDERIA           
TITLE    2 PSEUDOMALLEI WITH 2-PHOSPHOSERINE                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2,3-BISPHOSPHOGLYCERATE-DEPENDENT PHOSPHOGLYCERATE MUTASE; 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: PHOSPHOGLYCEROMUTASE, PGAM, BPG-DEPENDENT PGAM, DPGM;       
COMPND   5 EC: 5.4.2.1;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI;                      
SOURCE   3 ORGANISM_COMMON: PSEUDOMONAS PSEUDOMALLEI;                           
SOURCE   4 ORGANISM_TAXID: 28450;                                               
SOURCE   5 STRAIN: 1710B;                                                       
SOURCE   6 GENE: GPMA, BPSL0443;                                                
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: BG1861                                    
KEYWDS    PHOSPHOGLYCEROMUTASE, DECODE, SBRI, NIAID, UWPPG, GLYCOLYSIS,         
KEYWDS   2 ISOMERASE, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER   
KEYWDS   3 FOR INFECTIOUS DISEASE, SSGCID                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)    
REVDAT   3   05-OCT-11 3GP3    1       JRNL   VERSN                             
REVDAT   2   07-APR-09 3GP3    1       REMARK                                   
REVDAT   1   31-MAR-09 3GP3    0                                                
JRNL        AUTH   D.R.DAVIES,B.L.STAKER,J.A.ABENDROTH,T.E.EDWARDS,R.HARTLEY,   
JRNL        AUTH 2 J.LEONARD,H.KIM,A.L.RYCHEL,S.N.HEWITT,P.J.MYLER,L.J.STEWART  
JRNL        TITL   AN ENSEMBLE OF STRUCTURES OF BURKHOLDERIA PSEUDOMALLEI       
JRNL        TITL 2 2,3-BISPHOSPHOGLYCERATE-DEPENDENT PHOSPHOGLYCERATE MUTASE.   
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  67  1044 2011              
JRNL        REFN                   ESSN 1744-3091                               
JRNL        PMID   21904048                                                     
JRNL        DOI    10.1107/S1744309111030405                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 148953                         
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) : 0.238                           
REMARK   3   R VALUE            (WORKING SET) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7460                            
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) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8972                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.72                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 474                          
REMARK   3   BIN FREE R VALUE                    : 0.4250                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7298                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 138                                     
REMARK   3   SOLVENT ATOMS            : 712                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.76000                                             
REMARK   3    B22 (A**2) : 0.03000                                              
REMARK   3    B33 (A**2) : 1.02000                                              
REMARK   3    B12 (A**2) : -0.12000                                             
REMARK   3    B13 (A**2) : 0.21000                                              
REMARK   3    B23 (A**2) : 0.53000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.102         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.100         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.070         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.939         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7747 ; 0.027 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  5279 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10554 ; 2.114 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 12812 ; 1.099 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   944 ; 6.571 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   358 ;36.284 ;23.184       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1246 ;14.056 ;15.048       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    68 ;16.972 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1146 ; 0.139 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8590 ; 0.013 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1574 ; 0.001 ; 0.020       
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):  4692 ; 1.401 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1870 ; 0.468 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7576 ; 2.266 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3055 ; 3.465 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2978 ; 5.334 ; 4.500       
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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   3   U VALUES      : REFINED INDIVIDUALLY                               
REMARK   4                                                                      
REMARK   4 3GP3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052138.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 149575                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.0620                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: EMERALD CRYO B-4: 100MM MES PH 7.5, 5%   
REMARK 280  PEG 1000, 10% GLYCEROL, 30% PEG 600, 11.7 MG/ML PROTEIN, VAPOR      
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 289K                           
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, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    -7                                                      
REMARK 465     ALA A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     ASP A   230                                                      
REMARK 465     GLN A   231                                                      
REMARK 465     GLU A   232                                                      
REMARK 465     ALA A   233                                                      
REMARK 465     ILE A   234                                                      
REMARK 465     ALA A   235                                                      
REMARK 465     LYS A   236                                                      
REMARK 465     ALA A   237                                                      
REMARK 465     GLN A   238                                                      
REMARK 465     ALA A   239                                                      
REMARK 465     ALA A   240                                                      
REMARK 465     VAL A   241                                                      
REMARK 465     ALA A   242                                                      
REMARK 465     GLN A   243                                                      
REMARK 465     GLN A   244                                                      
REMARK 465     GLY A   245                                                      
REMARK 465     LYS A   246                                                      
REMARK 465     SER A   247                                                      
REMARK 465     ALA A   248                                                      
REMARK 465     ALA A   249                                                      
REMARK 465     MET B    -7                                                      
REMARK 465     ALA B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     ASP B   230                                                      
REMARK 465     GLN B   231                                                      
REMARK 465     GLU B   232                                                      
REMARK 465     ALA B   233                                                      
REMARK 465     ILE B   234                                                      
REMARK 465     ALA B   235                                                      
REMARK 465     LYS B   236                                                      
REMARK 465     ALA B   237                                                      
REMARK 465     GLN B   238                                                      
REMARK 465     ALA B   239                                                      
REMARK 465     ALA B   240                                                      
REMARK 465     VAL B   241                                                      
REMARK 465     ALA B   242                                                      
REMARK 465     GLN B   243                                                      
REMARK 465     GLN B   244                                                      
REMARK 465     GLY B   245                                                      
REMARK 465     LYS B   246                                                      
REMARK 465     SER B   247                                                      
REMARK 465     ALA B   248                                                      
REMARK 465     ALA B   249                                                      
REMARK 465     MET C    -7                                                      
REMARK 465     ALA C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     HIS C    -3                                                      
REMARK 465     HIS C    -2                                                      
REMARK 465     HIS C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     GLN C   231                                                      
REMARK 465     GLU C   232                                                      
REMARK 465     ALA C   233                                                      
REMARK 465     ILE C   234                                                      
REMARK 465     ALA C   235                                                      
REMARK 465     LYS C   236                                                      
REMARK 465     ALA C   237                                                      
REMARK 465     GLN C   238                                                      
REMARK 465     ALA C   239                                                      
REMARK 465     ALA C   240                                                      
REMARK 465     VAL C   241                                                      
REMARK 465     ALA C   242                                                      
REMARK 465     GLN C   243                                                      
REMARK 465     GLN C   244                                                      
REMARK 465     GLY C   245                                                      
REMARK 465     LYS C   246                                                      
REMARK 465     SER C   247                                                      
REMARK 465     ALA C   248                                                      
REMARK 465     ALA C   249                                                      
REMARK 465     MET D    -7                                                      
REMARK 465     ALA D    -6                                                      
REMARK 465     HIS D    -5                                                      
REMARK 465     HIS D    -4                                                      
REMARK 465     HIS D    -3                                                      
REMARK 465     HIS D    -2                                                      
REMARK 465     HIS D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     GLN D   231                                                      
REMARK 465     GLU D   232                                                      
REMARK 465     ALA D   233                                                      
REMARK 465     ILE D   234                                                      
REMARK 465     ALA D   235                                                      
REMARK 465     LYS D   236                                                      
REMARK 465     ALA D   237                                                      
REMARK 465     GLN D   238                                                      
REMARK 465     ALA D   239                                                      
REMARK 465     ALA D   240                                                      
REMARK 465     VAL D   241                                                      
REMARK 465     ALA D   242                                                      
REMARK 465     GLN D   243                                                      
REMARK 465     GLN D   244                                                      
REMARK 465     GLY D   245                                                      
REMARK 465     LYS D   246                                                      
REMARK 465     SER D   247                                                      
REMARK 465     ALA D   248                                                      
REMARK 465     ALA D   249                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A 118    CG   OD1  OD2                                       
REMARK 470     GLU A 129    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 140    CG   CD   CE   NZ                                   
REMARK 470     GLU A 218    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 118    CG   OD1  OD2                                       
REMARK 470     GLU B 129    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 140    CG   CD   CE   NZ                                   
REMARK 470     GLU B 218    CG   CD   OE1  OE2                                  
REMARK 470     GLN C  38    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 129    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 140    CG   CD   CE   NZ                                   
REMARK 470     GLN D  38    CG   CD   OE1  NE2                                  
REMARK 470     GLU D 129    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 140    CG   CD   CE   NZ                                   
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   NE2  GLN A    31     O    HOH A   602              1.78            
REMARK 500   O    HOH B   541     O    HOH C   501              1.95            
REMARK 500   NE2  HIS D     9     P    PO3 D   252              2.00            
REMARK 500   NE2  HIS C     9     P    PO3 C   252              2.00            
REMARK 500   NE2  HIS B     9     P    PO3 B   251              2.00            
REMARK 500   NE2  HIS A     9     P    PO3 A   251              2.01            
REMARK 500   OH   TYR B   117     O    HOH B   650              2.03            
REMARK 500   OH   TYR B   192     O    HOH B   421              2.09            
REMARK 500   OE1  GLU C    30     O    HOH C   534              2.10            
REMARK 500   O    HOH D   321     O    HOH D   400              2.11            
REMARK 500   O    THR D   149     O    HOH D   691              2.16            
REMARK 500   OE1  GLN A    31     NH1  ARG A    34              2.18            
REMARK 500   O    HOH B   281     O    HOH B   434              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TRP A  66   CZ3   TRP A  66   CH2    -0.098                       
REMARK 500    GLU A  87   CD    GLU A  87   OE2    -0.070                       
REMARK 500    GLU B  30   CD    GLU B  30   OE2     0.069                       
REMARK 500    PRO C  78   CG    PRO C  78   CD     -0.216                       
REMARK 500    CYS C 151   CB    CYS C 151   SG     -0.215                       
REMARK 500    VAL D  77   CB    VAL D  77   CG1     0.178                       
REMARK 500    GLU D 150   CA    GLU D 150   CB      0.180                       
REMARK 500    CYS D 151   CB    CYS D 151   SG     -0.107                       
REMARK 500    ASP D 194   CB    ASP D 194   CG      0.127                       
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    ARG A  84   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ASP A 198   CB  -  CG  -  OD1 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    ASP B 128   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG B 143   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG B 187   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ASP B 217   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    LEU C  42   CA  -  CB  -  CG  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    TYR C 138   CD1 -  CE1 -  CZ  ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG C 158   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG C 158   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG C 187   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG D  60   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    GLU D 150   N   -  CA  -  CB  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    ARG D 187   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ASP D 194   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 166      -51.45   -138.71                                   
REMARK 500    ALA A 181     -140.57   -147.01                                   
REMARK 500    ALA B 181     -139.29   -148.11                                   
REMARK 500    SER C 166      -53.08   -132.11                                   
REMARK 500    ALA C 181     -141.34   -145.32                                   
REMARK 500    ASN D  86      151.83    -47.48                                   
REMARK 500    SER D 166      -53.58   -133.34                                   
REMARK 500    ALA D 181     -143.23   -151.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO3 A 251                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SEP A 252                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO3 B 251                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SEP B 252                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 C 250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 C 251                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO3 C 252                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SEP C 253                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 D 250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 D 251                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO3 D 252                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SEP D 253                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3EZN   RELATED DB: PDB                                   
REMARK 900 APO STRUCTURE                                                        
REMARK 900 RELATED ID: 3FDZ   RELATED DB: PDB                                   
REMARK 900 STRUCTURE WITH 2,3-DIPHOSPHOGLYCERIC ACID IN ONE MOLECULE            
REMARK 900 AND 3-PHOSPHOGLYCERIC ACID IN THE OTHER                              
REMARK 900 RELATED ID: BUPSA.00114.A   RELATED DB: TARGETDB                     
REMARK 900 RELATED ID: 3GP5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3GW8   RELATED DB: PDB                                   
DBREF  3GP3 A    1   249  UNP    Q63XU7   GPMA_BURPS       1    249             
DBREF  3GP3 B    1   249  UNP    Q63XU7   GPMA_BURPS       1    249             
DBREF  3GP3 C    1   249  UNP    Q63XU7   GPMA_BURPS       1    249             
DBREF  3GP3 D    1   249  UNP    Q63XU7   GPMA_BURPS       1    249             
SEQADV 3GP3 MET A   -7  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 ALA A   -6  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS A   -5  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS A   -4  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS A   -3  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS A   -2  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS A   -1  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS A    0  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 MET B   -7  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 ALA B   -6  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS B   -5  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS B   -4  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS B   -3  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS B   -2  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS B   -1  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS B    0  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 MET C   -7  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 ALA C   -6  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS C   -5  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS C   -4  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS C   -3  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS C   -2  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS C   -1  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS C    0  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 MET D   -7  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 ALA D   -6  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS D   -5  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS D   -4  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS D   -3  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS D   -2  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS D   -1  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GP3 HIS D    0  UNP  Q63XU7              EXPRESSION TAG                 
SEQRES   1 A  257  MET ALA HIS HIS HIS HIS HIS HIS MET TYR LYS LEU VAL          
SEQRES   2 A  257  LEU ILE ARG HIS GLY GLU SER THR TRP ASN LYS GLU ASN          
SEQRES   3 A  257  ARG PHE THR GLY TRP VAL ASP VAL ASP LEU THR GLU GLN          
SEQRES   4 A  257  GLY ASN ARG GLU ALA ARG GLN ALA GLY GLN LEU LEU LYS          
SEQRES   5 A  257  GLU ALA GLY TYR THR PHE ASP ILE ALA TYR THR SER VAL          
SEQRES   6 A  257  LEU LYS ARG ALA ILE ARG THR LEU TRP HIS VAL GLN ASP          
SEQRES   7 A  257  GLN MET ASP LEU MET TYR VAL PRO VAL VAL HIS SER TRP          
SEQRES   8 A  257  ARG LEU ASN GLU ARG HIS TYR GLY ALA LEU SER GLY LEU          
SEQRES   9 A  257  ASN LYS ALA GLU THR ALA ALA LYS TYR GLY ASP GLU GLN          
SEQRES  10 A  257  VAL LEU VAL TRP ARG ARG SER TYR ASP THR PRO PRO PRO          
SEQRES  11 A  257  ALA LEU GLU PRO GLY ASP GLU ARG ALA PRO TYR ALA ASP          
SEQRES  12 A  257  PRO ARG TYR ALA LYS VAL PRO ARG GLU GLN LEU PRO LEU          
SEQRES  13 A  257  THR GLU CYS LEU LYS ASP THR VAL ALA ARG VAL LEU PRO          
SEQRES  14 A  257  LEU TRP ASN GLU SER ILE ALA PRO ALA VAL LYS ALA GLY          
SEQRES  15 A  257  LYS GLN VAL LEU ILE ALA ALA HIS GLY ASN SER LEU ARG          
SEQRES  16 A  257  ALA LEU ILE LYS TYR LEU ASP GLY ILE SER ASP ALA ASP          
SEQRES  17 A  257  ILE VAL GLY LEU ASN ILE PRO ASN GLY VAL PRO LEU VAL          
SEQRES  18 A  257  TYR GLU LEU ASP GLU SER LEU THR PRO ILE ARG HIS TYR          
SEQRES  19 A  257  TYR LEU GLY ASP GLN GLU ALA ILE ALA LYS ALA GLN ALA          
SEQRES  20 A  257  ALA VAL ALA GLN GLN GLY LYS SER ALA ALA                      
SEQRES   1 B  257  MET ALA HIS HIS HIS HIS HIS HIS MET TYR LYS LEU VAL          
SEQRES   2 B  257  LEU ILE ARG HIS GLY GLU SER THR TRP ASN LYS GLU ASN          
SEQRES   3 B  257  ARG PHE THR GLY TRP VAL ASP VAL ASP LEU THR GLU GLN          
SEQRES   4 B  257  GLY ASN ARG GLU ALA ARG GLN ALA GLY GLN LEU LEU LYS          
SEQRES   5 B  257  GLU ALA GLY TYR THR PHE ASP ILE ALA TYR THR SER VAL          
SEQRES   6 B  257  LEU LYS ARG ALA ILE ARG THR LEU TRP HIS VAL GLN ASP          
SEQRES   7 B  257  GLN MET ASP LEU MET TYR VAL PRO VAL VAL HIS SER TRP          
SEQRES   8 B  257  ARG LEU ASN GLU ARG HIS TYR GLY ALA LEU SER GLY LEU          
SEQRES   9 B  257  ASN LYS ALA GLU THR ALA ALA LYS TYR GLY ASP GLU GLN          
SEQRES  10 B  257  VAL LEU VAL TRP ARG ARG SER TYR ASP THR PRO PRO PRO          
SEQRES  11 B  257  ALA LEU GLU PRO GLY ASP GLU ARG ALA PRO TYR ALA ASP          
SEQRES  12 B  257  PRO ARG TYR ALA LYS VAL PRO ARG GLU GLN LEU PRO LEU          
SEQRES  13 B  257  THR GLU CYS LEU LYS ASP THR VAL ALA ARG VAL LEU PRO          
SEQRES  14 B  257  LEU TRP ASN GLU SER ILE ALA PRO ALA VAL LYS ALA GLY          
SEQRES  15 B  257  LYS GLN VAL LEU ILE ALA ALA HIS GLY ASN SER LEU ARG          
SEQRES  16 B  257  ALA LEU ILE LYS TYR LEU ASP GLY ILE SER ASP ALA ASP          
SEQRES  17 B  257  ILE VAL GLY LEU ASN ILE PRO ASN GLY VAL PRO LEU VAL          
SEQRES  18 B  257  TYR GLU LEU ASP GLU SER LEU THR PRO ILE ARG HIS TYR          
SEQRES  19 B  257  TYR LEU GLY ASP GLN GLU ALA ILE ALA LYS ALA GLN ALA          
SEQRES  20 B  257  ALA VAL ALA GLN GLN GLY LYS SER ALA ALA                      
SEQRES   1 C  257  MET ALA HIS HIS HIS HIS HIS HIS MET TYR LYS LEU VAL          
SEQRES   2 C  257  LEU ILE ARG HIS GLY GLU SER THR TRP ASN LYS GLU ASN          
SEQRES   3 C  257  ARG PHE THR GLY TRP VAL ASP VAL ASP LEU THR GLU GLN          
SEQRES   4 C  257  GLY ASN ARG GLU ALA ARG GLN ALA GLY GLN LEU LEU LYS          
SEQRES   5 C  257  GLU ALA GLY TYR THR PHE ASP ILE ALA TYR THR SER VAL          
SEQRES   6 C  257  LEU LYS ARG ALA ILE ARG THR LEU TRP HIS VAL GLN ASP          
SEQRES   7 C  257  GLN MET ASP LEU MET TYR VAL PRO VAL VAL HIS SER TRP          
SEQRES   8 C  257  ARG LEU ASN GLU ARG HIS TYR GLY ALA LEU SER GLY LEU          
SEQRES   9 C  257  ASN LYS ALA GLU THR ALA ALA LYS TYR GLY ASP GLU GLN          
SEQRES  10 C  257  VAL LEU VAL TRP ARG ARG SER TYR ASP THR PRO PRO PRO          
SEQRES  11 C  257  ALA LEU GLU PRO GLY ASP GLU ARG ALA PRO TYR ALA ASP          
SEQRES  12 C  257  PRO ARG TYR ALA LYS VAL PRO ARG GLU GLN LEU PRO LEU          
SEQRES  13 C  257  THR GLU CYS LEU LYS ASP THR VAL ALA ARG VAL LEU PRO          
SEQRES  14 C  257  LEU TRP ASN GLU SER ILE ALA PRO ALA VAL LYS ALA GLY          
SEQRES  15 C  257  LYS GLN VAL LEU ILE ALA ALA HIS GLY ASN SER LEU ARG          
SEQRES  16 C  257  ALA LEU ILE LYS TYR LEU ASP GLY ILE SER ASP ALA ASP          
SEQRES  17 C  257  ILE VAL GLY LEU ASN ILE PRO ASN GLY VAL PRO LEU VAL          
SEQRES  18 C  257  TYR GLU LEU ASP GLU SER LEU THR PRO ILE ARG HIS TYR          
SEQRES  19 C  257  TYR LEU GLY ASP GLN GLU ALA ILE ALA LYS ALA GLN ALA          
SEQRES  20 C  257  ALA VAL ALA GLN GLN GLY LYS SER ALA ALA                      
SEQRES   1 D  257  MET ALA HIS HIS HIS HIS HIS HIS MET TYR LYS LEU VAL          
SEQRES   2 D  257  LEU ILE ARG HIS GLY GLU SER THR TRP ASN LYS GLU ASN          
SEQRES   3 D  257  ARG PHE THR GLY TRP VAL ASP VAL ASP LEU THR GLU GLN          
SEQRES   4 D  257  GLY ASN ARG GLU ALA ARG GLN ALA GLY GLN LEU LEU LYS          
SEQRES   5 D  257  GLU ALA GLY TYR THR PHE ASP ILE ALA TYR THR SER VAL          
SEQRES   6 D  257  LEU LYS ARG ALA ILE ARG THR LEU TRP HIS VAL GLN ASP          
SEQRES   7 D  257  GLN MET ASP LEU MET TYR VAL PRO VAL VAL HIS SER TRP          
SEQRES   8 D  257  ARG LEU ASN GLU ARG HIS TYR GLY ALA LEU SER GLY LEU          
SEQRES   9 D  257  ASN LYS ALA GLU THR ALA ALA LYS TYR GLY ASP GLU GLN          
SEQRES  10 D  257  VAL LEU VAL TRP ARG ARG SER TYR ASP THR PRO PRO PRO          
SEQRES  11 D  257  ALA LEU GLU PRO GLY ASP GLU ARG ALA PRO TYR ALA ASP          
SEQRES  12 D  257  PRO ARG TYR ALA LYS VAL PRO ARG GLU GLN LEU PRO LEU          
SEQRES  13 D  257  THR GLU CYS LEU LYS ASP THR VAL ALA ARG VAL LEU PRO          
SEQRES  14 D  257  LEU TRP ASN GLU SER ILE ALA PRO ALA VAL LYS ALA GLY          
SEQRES  15 D  257  LYS GLN VAL LEU ILE ALA ALA HIS GLY ASN SER LEU ARG          
SEQRES  16 D  257  ALA LEU ILE LYS TYR LEU ASP GLY ILE SER ASP ALA ASP          
SEQRES  17 D  257  ILE VAL GLY LEU ASN ILE PRO ASN GLY VAL PRO LEU VAL          
SEQRES  18 D  257  TYR GLU LEU ASP GLU SER LEU THR PRO ILE ARG HIS TYR          
SEQRES  19 D  257  TYR LEU GLY ASP GLN GLU ALA ILE ALA LYS ALA GLN ALA          
SEQRES  20 D  257  ALA VAL ALA GLN GLN GLY LYS SER ALA ALA                      
HET    PG4  A 250      13                                                       
HET    PO3  A 251       4                                                       
HET    SEP  A 252      11                                                       
HET    PG4  B 250      13                                                       
HET    PO3  B 251       4                                                       
HET    SEP  B 252      11                                                       
HET    PG4  C 250      13                                                       
HET    PG4  C 251      13                                                       
HET    PO3  C 252       4                                                       
HET    SEP  C 253      11                                                       
HET    PG4  D 250      13                                                       
HET    PG4  D 251      13                                                       
HET    PO3  D 252       4                                                       
HET    SEP  D 253      11                                                       
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     PO3 PHOSPHITE ION                                                    
HETNAM     SEP PHOSPHOSERINE                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   5  PG4    6(C8 H18 O5)                                                 
FORMUL   6  PO3    4(O3 P 3-)                                                   
FORMUL   7  SEP    4(C3 H8 N O6 P)                                              
FORMUL  19  HOH   *712(H2 O)                                                    
HELIX    1   1 SER A   12  GLU A   17  1                                   6    
HELIX    2   2 THR A   29  ALA A   46  1                                  18    
HELIX    3   3 LEU A   58  ASP A   73  1                                  16    
HELIX    4   4 TRP A   83  ASN A   86  5                                   4    
HELIX    5   5 TYR A   90  SER A   94  5                                   5    
HELIX    6   6 ASN A   97  GLY A  106  1                                  10    
HELIX    7   7 GLY A  106  SER A  116  1                                  11    
HELIX    8   8 ASP A  135  ALA A  139  5                                   5    
HELIX    9   9 PRO A  142  LEU A  146  5                                   5    
HELIX   10  10 CYS A  151  SER A  166  1                                  16    
HELIX   11  11 SER A  166  ALA A  173  1                                   8    
HELIX   12  12 HIS A  182  ASP A  194  1                                  13    
HELIX   13  13 ALA A  199  LEU A  204  5                                   6    
HELIX   14  14 SER B   12  GLU B   17  1                                   6    
HELIX   15  15 THR B   29  ALA B   46  1                                  18    
HELIX   16  16 LEU B   58  ASP B   73  1                                  16    
HELIX   17  17 TRP B   83  ASN B   86  5                                   4    
HELIX   18  18 TYR B   90  SER B   94  5                                   5    
HELIX   19  19 ASN B   97  GLY B  106  1                                  10    
HELIX   20  20 GLY B  106  SER B  116  1                                  11    
HELIX   21  21 ASP B  135  ALA B  139  5                                   5    
HELIX   22  22 PRO B  142  LEU B  146  5                                   5    
HELIX   23  23 CYS B  151  SER B  166  1                                  16    
HELIX   24  24 SER B  166  ALA B  173  1                                   8    
HELIX   25  25 HIS B  182  ASP B  194  1                                  13    
HELIX   26  26 ALA B  199  LEU B  204  5                                   6    
HELIX   27  27 SER C   12  GLU C   17  1                                   6    
HELIX   28  28 THR C   29  ALA C   46  1                                  18    
HELIX   29  29 LEU C   58  ASP C   73  1                                  16    
HELIX   30  30 TRP C   83  ASN C   86  5                                   4    
HELIX   31  31 TYR C   90  SER C   94  5                                   5    
HELIX   32  32 ASN C   97  GLY C  106  1                                  10    
HELIX   33  33 GLY C  106  SER C  116  1                                  11    
HELIX   34  34 ASP C  135  ALA C  139  5                                   5    
HELIX   35  35 PRO C  142  LEU C  146  5                                   5    
HELIX   36  36 CYS C  151  SER C  166  1                                  16    
HELIX   37  37 SER C  166  ALA C  173  1                                   8    
HELIX   38  38 HIS C  182  GLY C  195  1                                  14    
HELIX   39  39 SER C  197  VAL C  202  1                                   6    
HELIX   40  40 SER D   12  GLU D   17  1                                   6    
HELIX   41  41 THR D   29  ALA D   46  1                                  18    
HELIX   42  42 LEU D   58  ASP D   73  1                                  16    
HELIX   43  43 TRP D   83  ASN D   86  5                                   4    
HELIX   44  44 TYR D   90  SER D   94  5                                   5    
HELIX   45  45 ASN D   97  GLY D  106  1                                  10    
HELIX   46  46 GLY D  106  SER D  116  1                                  11    
HELIX   47  47 ASP D  135  ALA D  139  5                                   5    
HELIX   48  48 PRO D  142  LEU D  146  5                                   5    
HELIX   49  49 CYS D  151  SER D  166  1                                  16    
HELIX   50  50 SER D  166  ALA D  173  1                                   8    
HELIX   51  51 HIS D  182  GLY D  195  1                                  14    
HELIX   52  52 ASP D  200  LEU D  204  5                                   5    
SHEET    1   A 6 VAL A  79  HIS A  81  0                                        
SHEET    2   A 6 ILE A  52  THR A  55  1  N  THR A  55   O  VAL A  80           
SHEET    3   A 6 VAL A 177  ALA A 181  1  O  ALA A 180   N  TYR A  54           
SHEET    4   A 6 TYR A   2  ARG A   8  1  N  ILE A   7   O  ALA A 181           
SHEET    5   A 6 LEU A 212  LEU A 216 -1  O  LEU A 216   N  TYR A   2           
SHEET    6   A 6 PRO A 222  TYR A 227 -1  O  TYR A 226   N  VAL A 213           
SHEET    1   B 6 VAL B  79  HIS B  81  0                                        
SHEET    2   B 6 ILE B  52  THR B  55  1  N  ALA B  53   O  VAL B  80           
SHEET    3   B 6 VAL B 177  ALA B 181  1  O  ALA B 180   N  TYR B  54           
SHEET    4   B 6 TYR B   2  ARG B   8  1  N  VAL B   5   O  ILE B 179           
SHEET    5   B 6 LEU B 212  LEU B 216 -1  O  TYR B 214   N  LEU B   4           
SHEET    6   B 6 PRO B 222  TYR B 227 -1  O  ILE B 223   N  GLU B 215           
SHEET    1   C 6 VAL C  79  HIS C  81  0                                        
SHEET    2   C 6 ILE C  52  THR C  55  1  N  THR C  55   O  VAL C  80           
SHEET    3   C 6 VAL C 177  ALA C 181  1  O  ALA C 180   N  TYR C  54           
SHEET    4   C 6 TYR C   2  ARG C   8  1  N  ILE C   7   O  ALA C 181           
SHEET    5   C 6 LEU C 212  LEU C 216 -1  O  LEU C 212   N  LEU C   6           
SHEET    6   C 6 PRO C 222  TYR C 227 -1  O  TYR C 226   N  VAL C 213           
SHEET    1   D 6 VAL D  79  HIS D  81  0                                        
SHEET    2   D 6 ILE D  52  THR D  55  1  N  THR D  55   O  VAL D  80           
SHEET    3   D 6 VAL D 177  ALA D 181  1  O  ALA D 180   N  TYR D  54           
SHEET    4   D 6 TYR D   2  ARG D   8  1  N  ILE D   7   O  ALA D 181           
SHEET    5   D 6 LEU D 212  LEU D 216 -1  O  LEU D 216   N  TYR D   2           
SHEET    6   D 6 PRO D 222  TYR D 227 -1  O  TYR D 226   N  VAL D 213           
SITE     1 AC1  3 ASP A  51  ALA A 173  LYS A 175                               
SITE     1 AC2  9 ARG A   8  HIS A   9  ASN A  15  ARG A  60                    
SITE     2 AC2  9 GLU A  87  HIS A 182  GLY A 183  SEP A 252                    
SITE     3 AC2  9 HOH A 274                                                     
SITE     1 AC3 14 ARG A   8  ASN A  15  ARG A  19  THR A  21                    
SITE     2 AC3 14 GLY A  22  GLU A  87  ARG A  88  TYR A  90                    
SITE     3 AC3 14 LYS A  98  ARG A 114  ARG A 115  ASN A 184                    
SITE     4 AC3 14 PO3 A 251  HOH A 278                                          
SITE     1 AC4  3 ASP B  51  ALA B 173  LYS B 175                               
SITE     1 AC5  9 ARG B   8  HIS B   9  ASN B  15  ARG B  60                    
SITE     2 AC5  9 GLU B  87  HIS B 182  GLY B 183  SEP B 252                    
SITE     3 AC5  9 HOH B 279                                                     
SITE     1 AC6 13 ARG B   8  ASN B  15  ARG B  19  THR B  21                    
SITE     2 AC6 13 GLY B  22  GLU B  87  TYR B  90  LYS B  98                    
SITE     3 AC6 13 ARG B 114  ARG B 115  ASN B 184  PO3 B 251                    
SITE     4 AC6 13 HOH B 299                                                     
SITE     1 AC7  4 ASP C  51  ALA C 173  LYS C 175  HOH C 552                    
SITE     1 AC8  5 ILE C 196  LEU C 204  HIS C 225  HOH C 332                    
SITE     2 AC8  5 HOH C 556                                                     
SITE     1 AC9  8 ARG C   8  HIS C   9  ASN C  15  ARG C  60                    
SITE     2 AC9  8 GLU C  87  HIS C 182  GLY C 183  SEP C 253                    
SITE     1 BC1 14 ARG C   8  ASN C  15  ARG C  19  PHE C  20                    
SITE     2 BC1 14 THR C  21  GLY C  22  GLU C  87  TYR C  90                    
SITE     3 BC1 14 LYS C  98  ARG C 114  ARG C 115  ASN C 184                    
SITE     4 BC1 14 PO3 C 252  HOH C 305                                          
SITE     1 BC2  4 ASP D  51  ALA D 173  LYS D 175  HOH D 601                    
SITE     1 BC3  8 ILE D 190  ILE D 196  TYR D 214  HIS D 225                    
SITE     2 BC3  8 TYR D 227  HOH D 282  HOH D 374  HOH D 706                    
SITE     1 BC4  9 ARG D   8  HIS D   9  ASN D  15  ARG D  60                    
SITE     2 BC4  9 GLU D  87  HIS D 182  GLY D 183  SEP D 253                    
SITE     3 BC4  9 HOH D 290                                                     
SITE     1 BC5 14 ARG D   8  ASN D  15  ARG D  19  PHE D  20                    
SITE     2 BC5 14 THR D  21  GLY D  22  GLU D  87  TYR D  90                    
SITE     3 BC5 14 LYS D  98  ARG D 114  ARG D 115  ASN D 184                    
SITE     4 BC5 14 PO3 D 252  HOH D 295                                          
CRYST1   49.263   72.045   78.036 107.96  93.00 104.20 P 1           4          
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      0.020299  0.005137  0.002935        0.00000                         
SCALE2      0.000000  0.014318  0.005035        0.00000                         
SCALE3      0.000000  0.000000  0.013603        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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