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Database: PDB
Entry: 3GW8
LinkDB: 3GW8
Original site: 3GW8 
HEADER    ISOMERASE                               31-MAR-09   3GW8              
TITLE     CRYSTAL STRUCTURE OF PHOSPHOGLYCEROMUTASE FROM BURKHOLDERIA           
TITLE    2 PSEUDOMALLEI WITH VANADATE AND GLYCEROL                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2,3-BISPHOSPHOGLYCERATE-DEPENDENT PHOSPHOGLYCERATE MUTASE; 
COMPND   3 CHAIN: A, B;                                                         
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    SSGCID, NIAID, DECODE, UWPPG, SBRI, GLYCOLYSIS, ISOMERASE, STRUCTURAL 
KEYWDS   2 GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)    
REVDAT   3   05-OCT-11 3GW8    1       JRNL                                     
REVDAT   2   13-JUL-11 3GW8    1       VERSN                                    
REVDAT   1   07-APR-09 3GW8    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.    1.93 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) : 1.93                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 34057                          
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) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1696                            
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) : 1.93                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2017                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.28                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2600                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 92                           
REMARK   3   BIN FREE R VALUE                    : 0.3080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3666                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 82                                      
REMARK   3   SOLVENT ATOMS            : 315                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.58000                                              
REMARK   3    B22 (A**2) : -0.38000                                             
REMARK   3    B33 (A**2) : 0.07000                                              
REMARK   3    B12 (A**2) : 0.31000                                              
REMARK   3    B13 (A**2) : -0.28000                                             
REMARK   3    B23 (A**2) : 0.17000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.192         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.163         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.102         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.495         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3879 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2664 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5265 ; 1.200 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6461 ; 0.838 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   466 ; 6.004 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   181 ;34.778 ;23.370       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   617 ;12.783 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    33 ;18.038 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   567 ; 0.069 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4259 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   778 ; 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):  2320 ; 0.550 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   928 ; 0.115 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3742 ; 1.019 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1559 ; 1.511 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1523 ; 2.505 ; 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 3GW8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-APR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052384.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-OCT-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E+ SUPERBRIGHT           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34058                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.930                              
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     (%) : 92.8                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.9750                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.890                              
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: 3EZN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: EMERALD CRYO SCREEN B-4, 100 MM MES PH   
REMARK 280  6.0, 5% PEG 1000, 10% GLYCEROL, 30% PEG 600, 11.7 MG/ML PROTEIN,    
REMARK 280  VAPOR 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                                                    
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 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 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 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     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     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 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     GLU A 129    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 202    CG1  CG2                                            
REMARK 470     LYS B  44    CG   CD   CE   NZ                                   
REMARK 470     LYS B 140    CG   CD   CE   NZ                                   
REMARK 470     GLU B 218    CG   CD   OE1  OE2                                  
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      -52.63   -132.96                                   
REMARK 500    ALA A 181     -139.69   -144.48                                   
REMARK 500    ARG B 115       13.47   -147.04                                   
REMARK 500    SER B 166      -52.94   -134.91                                   
REMARK 500    ALA B 181     -133.51   -145.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     VO4 A  401                                                       
REMARK 610     VO4 B  401                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             VO4 B 401   V                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GOL B 402   O2                                                     
REMARK 620 2 VO4 B 401   O1   89.3                                              
REMARK 620 3 VO4 B 401   O2   97.8 115.6                                        
REMARK 620 4 VO4 B 401   O3   91.8 124.0 119.7                                  
REMARK 620 5 HIS B   9   NE2 174.9  89.1  87.2  85.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             VO4 A 401   V                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GOL A 402   O2                                                     
REMARK 620 2 VO4 A 401   O1  110.8                                              
REMARK 620 3 VO4 A 401   O2   99.6 114.1                                        
REMARK 620 4 VO4 A 401   O3   83.9 124.4 115.5                                  
REMARK 620 5 HIS A   9   NE2 160.2  84.0  85.4  76.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3EZN   RELATED DB: PDB                                   
REMARK 900 APO CRYSTAL STRUCTURE                                                
REMARK 900 RELATED ID: 3FDZ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE WITH 2,3-DIPHOSPHOGLYCERIC ACID IN ONE             
REMARK 900 MONOMER AND 3-PHOSPHOGLYCERIC ACID IN THE OTHER                      
REMARK 900 RELATED ID: 3GP3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE WITH 2-PHOSPHOSERINE                               
REMARK 900 RELATED ID: 3GP5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE WITH VANADATE AND 3-PHOSPHOGLYCERIC ACID           
REMARK 900 RELATED ID: BUPSA.00114.A   RELATED DB: TARGETDB                     
DBREF  3GW8 A    1   249  UNP    Q63XU7   GPMA_BURPS       1    249             
DBREF  3GW8 B    1   249  UNP    Q63XU7   GPMA_BURPS       1    249             
SEQADV 3GW8 MET A   -7  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GW8 ALA A   -6  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GW8 HIS A   -5  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GW8 HIS A   -4  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GW8 HIS A   -3  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GW8 HIS A   -2  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GW8 HIS A   -1  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GW8 HIS A    0  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GW8 MET B   -7  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GW8 ALA B   -6  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GW8 HIS B   -5  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GW8 HIS B   -4  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GW8 HIS B   -3  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GW8 HIS B   -2  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GW8 HIS B   -1  UNP  Q63XU7              EXPRESSION TAG                 
SEQADV 3GW8 HIS B    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                      
HET    VO4  A 401       4                                                       
HET    GOL  A 402      12                                                       
HET    VO4  A 403       5                                                       
HET    PG4  A 501      13                                                       
HET    PG4  A 502      13                                                       
HET    PG4  A 250      13                                                       
HET    VO4  B 401       4                                                       
HET    GOL  B 402      12                                                       
HET    VO4  B 403       5                                                       
HET    PG4  B 501      13                                                       
HETNAM     VO4 VANADATE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  VO4    4(O4 V 3-)                                                   
FORMUL   4  GOL    2(C3 H8 O3)                                                  
FORMUL   6  PG4    4(C8 H18 O5)                                                 
FORMUL  13  HOH   *315(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  GLY A  195  1                                  14    
HELIX   13  13 SER A  197  VAL A  202  1                                   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 SER B  197  VAL B  202  1                                   6    
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 212   N  LEU A   6           
SHEET    6   A 6 PRO A 222  TYR A 227 -1  O  ILE A 223   N  GLU A 215           
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           
LINK         V   VO4 B 401                 O2 BGOL B 402     1555   1555  1.92  
LINK         V   VO4 A 401                 O2 AGOL A 402     1555   1555  1.94  
LINK         V   VO4 A 401                 O2 BGOL A 402     1555   1555  1.98  
LINK         V   VO4 B 401                 O2 AGOL B 402     1555   1555  2.01  
LINK         NE2 HIS B   9                 V   VO4 B 401     1555   1555  2.23  
LINK         NE2 HIS A   9                 V   VO4 A 401     1555   1555  2.30  
SITE     1 AC1  9 ARG A   8  HIS A   9  ASN A  15  ARG A  60                    
SITE     2 AC1  9 GLU A  87  HIS A 182  GLY A 183  HOH A 313                    
SITE     3 AC1  9 GOL A 402                                                     
SITE     1 AC2 12 ARG A   8  ASN A  15  ARG A  19  PHE A  20                    
SITE     2 AC2 12 THR A  21  GLY A  22  GLU A  87  TYR A  90                    
SITE     3 AC2 12 HOH A 255  HOH A 383  VO4 A 401  VO4 A 403                    
SITE     1 AC3  6 PHE A  20  TYR A  90  LYS A  98  ASN A 184                    
SITE     2 AC3  6 HOH A 255  GOL A 402                                          
SITE     1 AC4  4 ILE A 196  LEU A 204  HIS A 225  HOH A 414                    
SITE     1 AC5  2 ALA A 173  LYS A 175                                          
SITE     1 AC6  4 LYS A 140  HOH A 317  ASP B  51  LYS B 175                    
SITE     1 AC7  9 ARG B   8  HIS B   9  ASN B  15  ARG B  60                    
SITE     2 AC7  9 GLU B  87  HIS B 182  GLY B 183  HOH B 277                    
SITE     3 AC7  9 GOL B 402                                                     
SITE     1 AC8 11 ARG B   8  ASN B  15  ARG B  19  PHE B  20                    
SITE     2 AC8 11 THR B  21  GLY B  22  GLU B  87  TYR B  90                    
SITE     3 AC8 11 HOH B 342  VO4 B 401  VO4 B 403                               
SITE     1 AC9  6 TYR B  90  LYS B  98  ARG B 114  ARG B 115                    
SITE     2 AC9  6 ASN B 184  GOL B 402                                          
SITE     1 BC1  7 ASP B 194  ILE B 196  LEU B 204  TYR B 214                    
SITE     2 BC1  7 HIS B 225  TYR B 227  HOH B 282                               
CRYST1   45.175   49.112   62.590 106.42  91.18 107.61 P 1           2          
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      0.022136  0.007026  0.002711        0.00000                         
SCALE2      0.000000  0.021363  0.006794        0.00000                         
SCALE3      0.000000  0.000000  0.016769        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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