GenomeNet

Database: PDB
Entry: 3FDZ
LinkDB: 3FDZ
Original site: 3FDZ 
HEADER    ISOMERASE                               26-NOV-08   3FDZ              
TITLE     CRYSTAL STRUCTURE OF PHOSPHOGLYCEROMUTASE FROM BURKHOLDERIA           
TITLE    2 PSEUDOMALLEI 1710B WITH BOUND 2,3-DIPHOSPHOGLYCERIC ACID AND 3-      
TITLE    3 PHOSPHOGLYCERIC ACID                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2,3-BISPHOSPHOGLYCERATE-DEPENDENT PHOSPHOGLYCERATE MUTASE; 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PHOSPHOGLYCEROMUTASE, PGAM, BPG-DEPENDENT PGAM, DPGM;       
COMPND   5 EC: 5.4.2.1;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: 2,3-BISPHOSPHOGLYCERATE-DEPENDENT PHOSPHOGLYCERATE MUTASE; 
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: PHOSPHOGLYCEROMUTASE, PGAM, BPG-DEPENDENT PGAM, DPGM;       
COMPND  11 EC: 5.4.2.1;                                                         
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI 1710B;                
SOURCE   3 ORGANISM_TAXID: 320372;                                              
SOURCE   4 STRAIN: 1719B;                                                       
SOURCE   5 GENE: BURPS1710B_0662, GPMA;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: AVA0421;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI 1710B;                
SOURCE  13 ORGANISM_TAXID: 320372;                                              
SOURCE  14 STRAIN: 1719B;                                                       
SOURCE  15 GENE: BURPS1710B_0662, GPMA;                                         
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: AVA0421                                   
KEYWDS    ISOMERASE, SSGCID, PHOSPHOGLYCEROMUTASE, BURKHOLDERIA PSEUDOMALLEI,   
KEYWDS   2 GLYCOLYSIS, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER  
KEYWDS   3 FOR INFECTIOUS DISEASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)    
REVDAT   4   05-OCT-11 3FDZ    1       JRNL   VERSN                             
REVDAT   3   07-APR-09 3FDZ    1       REMARK                                   
REVDAT   2   31-MAR-09 3FDZ    1       REMARK                                   
REVDAT   1   13-JAN-09 3FDZ    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.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0053                                      
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) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.75                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 20934                          
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) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1066                            
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) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.31                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1440                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.87                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 82                           
REMARK   3   BIN FREE R VALUE                    : 0.3310                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3668                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 223                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.18                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.60000                                              
REMARK   3    B22 (A**2) : -0.45000                                             
REMARK   3    B33 (A**2) : -0.17000                                             
REMARK   3    B12 (A**2) : 0.12000                                              
REMARK   3    B13 (A**2) : -1.14000                                             
REMARK   3    B23 (A**2) : -0.05000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.418         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.266         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.174         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.030         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.891                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3796 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5175 ; 1.526 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   457 ; 6.698 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   177 ;38.445 ;23.390       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   610 ;14.593 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;13.904 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   563 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2905 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2291 ; 0.585 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3693 ; 1.059 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1505 ; 1.923 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1482 ; 3.013 ; 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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   4                                                                      
REMARK   4 3FDZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-DEC-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB050471.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-SEP-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SATURN                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20934                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
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   (%): 41.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 600, 5% PEG 1000, 10%            
REMARK 280  GLYCEROL, 100 MM MES PH 6.0, CRYSTALS SOAKED OVERNIGHT WITH 20 MM   
REMARK 280  3-PHOSPHOGLYCERIC ACID, VAPOR DIFFUSION, VAPOR DIFFUSION, SITTING   
REMARK 280  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                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE ASYMMETRIC UNIT CONTAINS TWO BIOLOGICAL UNITS            
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: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 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     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 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     LYS A 140    CG   CD   CE   NZ                                   
REMARK 470     LYS B 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    41     OE1  GLN A    71              2.08            
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    ASP A  25       52.32    -95.95                                   
REMARK 500    SER A 166      -60.56   -138.38                                   
REMARK 500    ALA A 181     -137.08   -143.90                                   
REMARK 500    ASP B  25       56.83    -93.88                                   
REMARK 500    SER B 166      -59.07   -127.36                                   
REMARK 500    ALA B 181     -141.56   -141.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 323        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH B 345        DISTANCE =  5.69 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DG2 A1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3PG B1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1002                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3EZN   RELATED DB: PDB                                   
REMARK 900 SAME STRUCTURE WITHOUT LIGANDS                                       
REMARK 900 RELATED ID: BUPSA.00114.A   RELATED DB: TARGETDB                     
REMARK 900 RELATED ID: 3GP3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3GP5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3GW8   RELATED DB: PDB                                   
DBREF  3FDZ A    1   249  UNP    Q3JWH7   GPMA_BURP1       1    249             
DBREF  3FDZ B    1   249  UNP    Q3JWH7   GPMA_BURP1       1    249             
SEQADV 3FDZ MET A   -7  UNP  Q3JWH7              EXPRESSION TAG                 
SEQADV 3FDZ ALA A   -6  UNP  Q3JWH7              EXPRESSION TAG                 
SEQADV 3FDZ HIS A   -5  UNP  Q3JWH7              EXPRESSION TAG                 
SEQADV 3FDZ HIS A   -4  UNP  Q3JWH7              EXPRESSION TAG                 
SEQADV 3FDZ HIS A   -3  UNP  Q3JWH7              EXPRESSION TAG                 
SEQADV 3FDZ HIS A   -2  UNP  Q3JWH7              EXPRESSION TAG                 
SEQADV 3FDZ HIS A   -1  UNP  Q3JWH7              EXPRESSION TAG                 
SEQADV 3FDZ HIS A    0  UNP  Q3JWH7              EXPRESSION TAG                 
SEQADV 3FDZ MET B   -7  UNP  Q3JWH7              EXPRESSION TAG                 
SEQADV 3FDZ ALA B   -6  UNP  Q3JWH7              EXPRESSION TAG                 
SEQADV 3FDZ HIS B   -5  UNP  Q3JWH7              EXPRESSION TAG                 
SEQADV 3FDZ HIS B   -4  UNP  Q3JWH7              EXPRESSION TAG                 
SEQADV 3FDZ HIS B   -3  UNP  Q3JWH7              EXPRESSION TAG                 
SEQADV 3FDZ HIS B   -2  UNP  Q3JWH7              EXPRESSION TAG                 
SEQADV 3FDZ HIS B   -1  UNP  Q3JWH7              EXPRESSION TAG                 
SEQADV 3FDZ HIS B    0  UNP  Q3JWH7              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 NEP 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                      
MODRES 3FDZ NEP B    9  HIS  N1-PHOSPHONOHISTIDINE                              
HET    NEP  B   9      14                                                       
HET    DG2  A1001      15                                                       
HET    PEG  A1002       7                                                       
HET    3PG  B1001      11                                                       
HET    PEG  B1002       7                                                       
HETNAM     NEP N1-PHOSPHONOHISTIDINE                                            
HETNAM     DG2 2,3-DIPHOSPHOGLYCERIC ACID                                       
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     3PG 3-PHOSPHOGLYCERIC ACID                                           
FORMUL   2  NEP    C6 H10 N3 O5 P                                               
FORMUL   3  DG2    C3 H8 O10 P2                                                 
FORMUL   4  PEG    2(C4 H10 O3)                                                 
FORMUL   5  3PG    C3 H7 O7 P                                                   
FORMUL   7  HOH   *223(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  GLY A  174  1                                   9    
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  GLY B   47  1                                  19    
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    
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  LEU A 178   N  TYR A  54           
SHEET    4   A 6 TYR A   2  ARG A   8  1  N  VAL A   5   O  ILE A 179           
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  THR B  55   O  VAL B  80           
SHEET    3   B 6 VAL B 177  ALA B 181  1  O  LEU B 178   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 PRO B 211  LEU B 216 -1  O  LEU B 216   N  TYR B   2           
SHEET    6   B 6 PRO B 222  TYR B 227 -1  O  TYR B 226   N  VAL B 213           
LINK         C   ARG B   8                 N   NEP B   9     1555   1555  1.34  
LINK         C   NEP B   9                 N   GLY B  10     1555   1555  1.32  
SITE     1 AC1 17 ARG A   8  HIS A   9  ASN A  15  THR A  21                    
SITE     2 AC1 17 GLY A  22  ARG A  60  GLU A  87  TYR A  90                    
SITE     3 AC1 17 LYS A  98  ARG A 114  ARG A 115  HIS A 182                    
SITE     4 AC1 17 GLY A 183  ASN A 184  HOH A 349  HOH A 350                    
SITE     5 AC1 17 HOH A 355                                                     
SITE     1 AC2  6 ASP A 194  LEU A 204  TYR A 214  HIS A 225                    
SITE     2 AC2  6 TYR A 227  HOH A 259                                          
SITE     1 AC3 12 NEP B   9  ARG B  19  PHE B  20  THR B  21                    
SITE     2 AC3 12 GLY B  22  GLU B  87  TYR B  90  LYS B  98                    
SITE     3 AC3 12 ARG B 114  ARG B 115  ASN B 184  HOH B 330                    
SITE     1 AC4  6 ILE B 190  LEU B 204  TYR B 214  HIS B 225                    
SITE     2 AC4  6 TYR B 227  HOH B 366                                          
CRYST1   44.390   48.480   62.090 106.03  91.54 107.50 P 1           1          
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      0.022528  0.007103  0.002853        0.00000                         
SCALE2      0.000000  0.021628  0.006755        0.00000                         
SCALE3      0.000000  0.000000  0.016879        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system