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Database: PDB
Entry: 2XE7
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Original site: 2XE7 
HEADER    TRANSFERASE                             11-MAY-10   2XE7              
TITLE     THE COMPLETE REACTION CYCLE OF HUMAN PHOSPHOGLYCERATE KINASE: THE OPEN
TITLE    2 TERNARY COMPLEX WITH 3PG AND ADP                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHOGLYCERATE KINASE 1;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PRIMER RECOGNITION PROTEIN 2, PRP 2, CELL MIGRATION-INDUCING
COMPND   5 GENE 10 PROTEIN;                                                     
COMPND   6 EC: 2.7.2.3;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET;                                       
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET22A                                    
KEYWDS    TRANSITION STATE ANALOGUE, HEREDITARY HEMOLYTIC ANEMIA,               
KEYWDS   2 PHOSPHOPROTEIN, GLYCOLYSIS, TRANSFERASE, PHOSPHORYL TRANSFER,        
KEYWDS   3 NUCLEOTIDE-BINDING, DOMAIN MOTIONS                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.J.CLIFF,N.J.BAXTER,G.M.BLACKBURN,A.MERLI,M.VAS,J.P.WALTHO,          
AUTHOR   2 M.W.BOWLER                                                           
REVDAT   4   20-DEC-23 2XE7    1       REMARK                                   
REVDAT   3   26-OCT-11 2XE7    1       JRNL   REMARK VERSN                      
REVDAT   2   27-APR-11 2XE7    1       JRNL   REMARK                            
REVDAT   1   19-JAN-11 2XE7    0                                                
JRNL        AUTH   L.ZERRAD,A.MERLI,G.F.SCHRODER,A.VARGA,E.GRACZER,P.PERNOT,    
JRNL        AUTH 2 A.ROUND,M.VAS,M.W.BOWLER                                     
JRNL        TITL   A SPRING LOADED RELEASE MECHANISM REGULATES DOMAIN MOVEMENT  
JRNL        TITL 2 AND CATALYSIS IN PHOSPHOGLYCERATE KINASE.                    
JRNL        REF    J.BIOL.CHEM.                  V. 286 14040 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21349853                                                     
JRNL        DOI    10.1074/JBC.M110.206813                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 19766                          
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) : 0.228                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1050                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1441                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.87                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 88                           
REMARK   3   BIN FREE R VALUE                    : 0.3750                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3096                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 38                                      
REMARK   3   SOLVENT ATOMS            : 64                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.51000                                              
REMARK   3    B22 (A**2) : 0.99000                                              
REMARK   3    B33 (A**2) : -2.51000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.347         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.262         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.231         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.949        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.886                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3216 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2190 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4337 ; 1.621 ; 1.992       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5405 ; 0.915 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   415 ; 6.690 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   121 ;42.565 ;25.785       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   586 ;17.940 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;20.393 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   495 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3525 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   573 ; 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):  2060 ; 0.673 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   857 ; 0.162 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3293 ; 1.217 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1156 ; 2.081 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1043 ; 3.259 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     4        A   186                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.5880 -20.1510 -33.6130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0925 T22:   0.3252                                     
REMARK   3      T33:   0.0029 T12:  -0.1807                                     
REMARK   3      T13:  -0.0301 T23:   0.0462                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1756 L22:   3.3453                                     
REMARK   3      L33:   4.7110 L12:   0.3730                                     
REMARK   3      L13:   0.9744 L23:   0.1785                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0825 S12:   0.6285 S13:   0.1308                       
REMARK   3      S21:  -0.0960 S22:   0.1399 S23:   0.0098                       
REMARK   3      S31:  -0.5616 S32:   0.6635 S33:  -0.0574                       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS   
REMARK   4                                                                      
REMARK   4 2XE7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAY-10.                  
REMARK 100 THE DEPOSITION ID IS D_1290043895.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JUN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : DIAMOND 110                        
REMARK 200  OPTICS                         : GE 221                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20841                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.000                              
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: PDB ENTRY 3C39                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG4000, 100MM TRIS PH 8.0           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       29.31000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.72500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.31000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.72500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LYS A    55     O    ALA A   111              1.94            
REMARK 500   OE2  GLU A   343     O2'  ADP A  1418              2.13            
REMARK 500   ND2  ASN A   137     O    HOH A  2020              2.18            
REMARK 500   O    VAL A    13     CG   LYS A    16              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CB   ALA A   308     CB   ALA A   308     2445     1.63            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLN A  32   N     GLN A  32   CA     -0.134                       
REMARK 500    TYR A  75   CD1   TYR A  75   CE1    -0.104                       
REMARK 500    TYR A  75   CE2   TYR A  75   CD2    -0.107                       
REMARK 500    CYS A  98   CB    CYS A  98   SG     -0.103                       
REMARK 500    ASP A 218   N     ASP A 218   CA     -0.173                       
REMARK 500    ASP A 218   N     ASP A 218   CA     -0.277                       
REMARK 500    CYS A 315   CB    CYS A 315   SG     -0.128                       
REMARK 500    CYS A 378   CB    CYS A 378   SG     -0.145                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 110   C   -  N   -  CD  ANGL. DEV. = -14.7 DEGREES          
REMARK 500    GLY A 212   CA  -  C   -  N   ANGL. DEV. =  12.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 109       79.90   -153.24                                   
REMARK 500    PRO A 110     -166.47    -68.25                                   
REMARK 500    ALA A 214      -73.78    -89.30                                   
REMARK 500    LYS A 215       52.61    106.69                                   
REMARK 500    ILE A 220      -63.76   -137.66                                   
REMARK 500    PRO A 307      164.37    -44.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3PG A 1417                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 1418                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2X15   RELATED DB: PDB                                   
REMARK 900 THE CATALYTICALLY ACTIVE FULLY CLOSED CONFORMATION OF HUMAN          
REMARK 900 PHOSPHOGLYCERATE KINASE IN COMPLEX WITH ADP AND 1,3-                 
REMARK 900 BISPHOSPHOGLYCERATE                                                  
REMARK 900 RELATED ID: 2WZD   RELATED DB: PDB                                   
REMARK 900 THE CATALYTICALLY ACTIVE FULLY CLOSED CONFORMATION OF HUMAN          
REMARK 900 PHOSPHOGLYCERATE KINASE K219A MUTANT IN COMPLEX WITH ADP, 3PG AND    
REMARK 900 ALUMINIUM TRIFLUORIDE                                                
REMARK 900 RELATED ID: 2X14   RELATED DB: PDB                                   
REMARK 900 THE CATALYTICALLY ACTIVE FULLY CLOSED CONFORMATION OF HUMAN          
REMARK 900 PHOSPHOGLYCERATE KINASE K219A MUTANT IN COMPLEX WITH AMP-PCP AND 3PG 
REMARK 900 RELATED ID: 2X13   RELATED DB: PDB                                   
REMARK 900 THE CATALYTICALLY ACTIVE FULLY CLOSED CONFORMATION OF HUMAN          
REMARK 900 PHOSPHOGLYCERATE KINASE IN COMPLEX WITH ADP AND 3PHOSPHOGLYCERATE    
REMARK 900 RELATED ID: 2WZB   RELATED DB: PDB                                   
REMARK 900 THE CATALYTICALLY ACTIVE FULLY CLOSED CONFORMATION OF HUMAN          
REMARK 900 PHOSPHOGLYCERATE KINASE IN COMPLEX WITH ADP, 3PG AND MAGNESIUM       
REMARK 900 TRIFLUORIDE                                                          
REMARK 900 RELATED ID: 2WZC   RELATED DB: PDB                                   
REMARK 900 THE CATALYTICALLY ACTIVE FULLY CLOSED CONFORMATION OF HUMAN          
REMARK 900 PHOSPHOGLYCERATE KINASE IN COMPLEX WITH ADP, 3PG AND ALUMINIUM       
REMARK 900 TETRAFLUORIDE                                                        
REMARK 900 RELATED ID: 2XE6   RELATED DB: PDB                                   
REMARK 900 THE COMPLETE REACTION CYCLE OF HUMAN PHOSPHOGLYCERATE KINASE: THE    
REMARK 900 OPEN BINARY COMPLEX WITH 3PG                                         
REMARK 900 RELATED ID: 2XE8   RELATED DB: PDB                                   
REMARK 900 THE COMPLETE REACTION CYCLE OF HUMAN PHOSPHOGLYCERATE KINASE: THE    
REMARK 900 OPEN TERNARY COMPLEX WITH 3PG AND AMP-PNP                            
DBREF  2XE7 A    0   416  UNP    P00558   PGK1_HUMAN       1    417             
SEQRES   1 A  417  MET SER LEU SER ASN LYS LEU THR LEU ASP LYS LEU ASP          
SEQRES   2 A  417  VAL LYS GLY LYS ARG VAL VAL MET ARG VAL ASP PHE ASN          
SEQRES   3 A  417  VAL PRO MET LYS ASN ASN GLN ILE THR ASN ASN GLN ARG          
SEQRES   4 A  417  ILE LYS ALA ALA VAL PRO SER ILE LYS PHE CYS LEU ASP          
SEQRES   5 A  417  ASN GLY ALA LYS SER VAL VAL LEU MET SER HIS LEU GLY          
SEQRES   6 A  417  ARG PRO ASP GLY VAL PRO MET PRO ASP LYS TYR SER LEU          
SEQRES   7 A  417  GLU PRO VAL ALA VAL GLU LEU LYS SER LEU LEU GLY LYS          
SEQRES   8 A  417  ASP VAL LEU PHE LEU LYS ASP CYS VAL GLY PRO GLU VAL          
SEQRES   9 A  417  GLU LYS ALA CYS ALA ASN PRO ALA ALA GLY SER VAL ILE          
SEQRES  10 A  417  LEU LEU GLU ASN LEU ARG PHE HIS VAL GLU GLU GLU GLY          
SEQRES  11 A  417  LYS GLY LYS ASP ALA SER GLY ASN LYS VAL LYS ALA GLU          
SEQRES  12 A  417  PRO ALA LYS ILE GLU ALA PHE ARG ALA SER LEU SER LYS          
SEQRES  13 A  417  LEU GLY ASP VAL TYR VAL ASN ASP ALA PHE GLY THR ALA          
SEQRES  14 A  417  HIS ARG ALA HIS SER SER MET VAL GLY VAL ASN LEU PRO          
SEQRES  15 A  417  GLN LYS ALA GLY GLY PHE LEU MET LYS LYS GLU LEU ASN          
SEQRES  16 A  417  TYR PHE ALA LYS ALA LEU GLU SER PRO GLU ARG PRO PHE          
SEQRES  17 A  417  LEU ALA ILE LEU GLY GLY ALA LYS VAL ALA ASP LYS ILE          
SEQRES  18 A  417  GLN LEU ILE ASN ASN MET LEU ASP LYS VAL ASN GLU MET          
SEQRES  19 A  417  ILE ILE GLY GLY GLY MET ALA PHE THR PHE LEU LYS VAL          
SEQRES  20 A  417  LEU ASN ASN MET GLU ILE GLY THR SER LEU PHE ASP GLU          
SEQRES  21 A  417  GLU GLY ALA LYS ILE VAL LYS ASP LEU MET SER LYS ALA          
SEQRES  22 A  417  GLU LYS ASN GLY VAL LYS ILE THR LEU PRO VAL ASP PHE          
SEQRES  23 A  417  VAL THR ALA ASP LYS PHE ASP GLU ASN ALA LYS THR GLY          
SEQRES  24 A  417  GLN ALA THR VAL ALA SER GLY ILE PRO ALA GLY TRP MET          
SEQRES  25 A  417  GLY LEU ASP CYS GLY PRO GLU SER SER LYS LYS TYR ALA          
SEQRES  26 A  417  GLU ALA VAL THR ARG ALA LYS GLN ILE VAL TRP ASN GLY          
SEQRES  27 A  417  PRO VAL GLY VAL PHE GLU TRP GLU ALA PHE ALA ARG GLY          
SEQRES  28 A  417  THR LYS ALA LEU MET ASP GLU VAL VAL LYS ALA THR SER          
SEQRES  29 A  417  ARG GLY CYS ILE THR ILE ILE GLY GLY GLY ASP THR ALA          
SEQRES  30 A  417  THR CYS CYS ALA LYS TRP ASN THR GLU ASP LYS VAL SER          
SEQRES  31 A  417  HIS VAL SER THR GLY GLY GLY ALA SER LEU GLU LEU LEU          
SEQRES  32 A  417  GLU GLY LYS VAL LEU PRO GLY VAL ASP ALA LEU SER ASN          
SEQRES  33 A  417  ILE                                                          
HET    3PG  A1417      11                                                       
HET    ADP  A1418      27                                                       
HETNAM     3PG 3-PHOSPHOGLYCERIC ACID                                           
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   2  3PG    C3 H7 O7 P                                                   
FORMUL   3  ADP    C10 H15 N5 O10 P2                                            
FORMUL   4  HOH   *64(H2 O)                                                     
HELIX    1   1 LEU A    8  LEU A   11  5                                   4    
HELIX    2   2 ASN A   36  ALA A   41  1                                   6    
HELIX    3   3 ALA A   42  ASN A   52  1                                  11    
HELIX    4   4 LEU A   77  GLY A   89  1                                  13    
HELIX    5   5 GLY A  100  ALA A  108  1                                   9    
HELIX    6   6 ASN A  120  HIS A  124  5                                   5    
HELIX    7   7 GLU A  142  LYS A  155  1                                  14    
HELIX    8   8 ALA A  164  ALA A  168  5                                   5    
HELIX    9   9 HIS A  172  GLY A  177  1                                   6    
HELIX   10  10 GLY A  186  SER A  202  1                                  17    
HELIX   11  11 ILE A  220  LEU A  227  1                                   8    
HELIX   12  12 MET A  239  ASN A  249  1                                  11    
HELIX   13  13 ASP A  258  LYS A  263  1                                   6    
HELIX   14  14 ILE A  264  ASN A  275  1                                  12    
HELIX   15  15 GLY A  316  ALA A  330  1                                  15    
HELIX   16  16 TRP A  344  PHE A  347  5                                   4    
HELIX   17  17 ALA A  348  ARG A  364  1                                  17    
HELIX   18  18 GLY A  372  TRP A  382  1                                  11    
HELIX   19  19 GLY A  394  GLU A  403  1                                  10    
HELIX   20  20 LEU A  407  ALA A  412  1                                   6    
SHEET    1  AA 6 VAL A  92  PHE A  94  0                                        
SHEET    2  AA 6 SER A 114  LEU A 117  1  O  VAL A 115   N  LEU A  93           
SHEET    3  AA 6 SER A  56  MET A  60  1  O  VAL A  57   N  ILE A 116           
SHEET    4  AA 6 ARG A  17  ARG A  21  1  O  VAL A  18   N  VAL A  58           
SHEET    5  AA 6 VAL A 159  ASN A 162  1  O  VAL A 159   N  VAL A  19           
SHEET    6  AA 6 LYS A 183  GLY A 185  1  O  ALA A 184   N  ASN A 162           
SHEET    1  AB 2 MET A  28  LYS A  29  0                                        
SHEET    2  AB 2 GLN A  32  ILE A  33 -1  O  GLN A  32   N  LYS A  29           
SHEET    1  AC 2 LYS A 130  LYS A 132  0                                        
SHEET    2  AC 2 LYS A 138  LYS A 140 -1  O  VAL A 139   N  GLY A 131           
SHEET    1  AD 6 LYS A 278  THR A 280  0                                        
SHEET    2  AD 6 GLU A 232  ILE A 235  1  O  MET A 233   N  THR A 280           
SHEET    3  AD 6 PHE A 207  LEU A 211  1  O  ALA A 209   N  ILE A 234           
SHEET    4  AD 6 GLN A 332  ASN A 336  1  O  GLN A 332   N  LEU A 208           
SHEET    5  AD 6 ILE A 367  ILE A 370  1  O  ILE A 367   N  ILE A 333           
SHEET    6  AD 6 HIS A 390  VAL A 391  1  O  HIS A 390   N  ILE A 370           
SHEET    1  AE 3 THR A 297  THR A 301  0                                        
SHEET    2  AE 3 ASP A 284  ALA A 288 -1  O  PHE A 285   N  ALA A 300           
SHEET    3  AE 3 MET A 311  CYS A 315 -1  O  MET A 311   N  ALA A 288           
CISPEP   1 ARG A  205    PRO A  206          0         5.00                     
CISPEP   2 ALA A  308    GLY A  309          0         0.17                     
SITE     1 AC1 11 ASP A  23  ASN A  25  ARG A  38  HIS A  62                    
SITE     2 AC1 11 ARG A  65  ARG A 122  GLY A 166  THR A 167                    
SITE     3 AC1 11 ARG A 170  HOH A2024  HOH A2063                               
SITE     1 AC2 20 GLY A 213  ALA A 214  LYS A 215  LYS A 219                    
SITE     2 AC2 20 GLY A 237  GLY A 238  LEU A 256  GLY A 312                    
SITE     3 AC2 20 LEU A 313  ASN A 336  GLY A 337  PRO A 338                    
SITE     4 AC2 20 GLY A 340  VAL A 341  GLU A 343  GLY A 372                    
SITE     5 AC2 20 GLY A 373  ASP A 374  THR A 375  HOH A2064                    
CRYST1   58.620   73.450   93.440  90.00  90.00  90.00 P 21 21 2     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017059  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013615  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010702        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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