HEADER TRANSFERASE 30-MAR-00 1EQ0
TITLE SOLUTION STRUCTURE OF 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN
TITLE 2 PYROPHOSPHOKINASE COMPLEXED WITH MGAMPPCP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HPPK;
COMPND 5 EC: 2.7.6.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-17B
KEYWDS FOLATE PTERIN, PYROPHOSPHOKINASE, PYROPHOSPHORYL TRANSFER, INDUCED
KEYWDS 2 CONFORMATIONAL CHANGE, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
MDLTYP MINIMIZED AVERAGE
AUTHOR G.SHI,H.YAN
REVDAT 3 16-FEB-22 1EQ0 1 REMARK
REVDAT 2 24-FEB-09 1EQ0 1 VERSN
REVDAT 1 07-NOV-01 1EQ0 0
JRNL AUTH B.XIAO,G.SHI,J.GAO,J.BLASZCZYK,Q.LIU,X.JI,H.YAN
JRNL TITL UNUSUAL CONFORMATIONAL CHANGES IN
JRNL TITL 2 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE AS
JRNL TITL 3 REVEALED BY X-RAY CRYSTALLOGRAPHY AND NMR.
JRNL REF J.BIOL.CHEM. V. 276 40274 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11546767
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.SHI,J.GAO,H.YAN
REMARK 1 TITL 1H, 13C AND 15N RESONANCE ASSIGNMENTS OF ESCHERICHIA COLI
REMARK 1 TITL 2 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE AND ITS
REMARK 1 TITL 3 COMPLEX WITH MGAMPPCP
REMARK 1 REF J.BIOMOL.NMR V. 14 189 1999
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1008309801414
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.XIAO,G.SHI,X.CHEN,H.YAN,X.JI
REMARK 1 TITL CRYSTAL STRUCTURE OF 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN
REMARK 1 TITL 2 PYROPHOSPHOKINASE, A POTENTIAL TARGET FOR THE DEVELOPMENT OF
REMARK 1 TITL 3 NOVEL ANTIMICROBIAL AGENTS.
REMARK 1 REF STRUCTURE V. 7 489 1999
REMARK 1 REFN ISSN 0969-2126
REMARK 1 DOI 10.1016/S0969-2126(99)80065-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1EQ0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010804.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.5MM HPPK U-15N,13C; 20MM
REMARK 210 PHOSPHATE BUFFER A; 90% H2O, 10%
REMARK 210 D2O N
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, VNMR 6.1, NMRVIEW 4.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM,
REMARK 210 STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 ARG A 75 H GLN A 79 1.56
REMARK 500 O GLU A 68 H HIS A 72 1.59
REMARK 500 O VAL A 113 H HIS A 115 1.59
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 1 VAL A 2 123.97 -174.95
REMARK 500 1 PRO A 14 76.10 -61.80
REMARK 500 1 HIS A 32 143.40 -179.58
REMARK 500 1 SER A 37 -169.79 -60.72
REMARK 500 1 ARG A 41 82.86 -156.11
REMARK 500 1 PRO A 44 -164.13 -60.22
REMARK 500 1 GLN A 48 -106.81 -81.12
REMARK 500 1 ASP A 49 88.07 176.43
REMARK 500 1 ASP A 52 88.96 -63.38
REMARK 500 1 TYR A 53 86.08 -60.49
REMARK 500 1 GLU A 61 62.86 -104.48
REMARK 500 1 LEU A 64 -167.41 -67.53
REMARK 500 1 PRO A 66 -33.96 -34.95
REMARK 500 1 LYS A 85 83.73 -154.91
REMARK 500 1 ALA A 86 -133.40 64.10
REMARK 500 1 TRP A 89 169.12 -46.46
REMARK 500 1 PRO A 91 -167.96 -73.64
REMARK 500 1 ILE A 98 95.57 -69.74
REMARK 500 1 ASN A 103 43.78 -143.58
REMARK 500 1 ILE A 106 -75.74 -117.25
REMARK 500 1 THR A 112 69.58 -173.37
REMARK 500 1 PRO A 114 67.64 -64.02
REMARK 500 1 HIS A 115 89.83 -14.39
REMARK 500 1 TYR A 116 -19.88 -44.95
REMARK 500 1 ASN A 120 25.67 -156.31
REMARK 500 1 ALA A 132 53.48 -143.31
REMARK 500 1 PRO A 133 -18.30 -49.64
REMARK 500 1 GLU A 141 162.86 -49.06
REMARK 500 2 VAL A 2 120.89 -170.57
REMARK 500 2 PRO A 14 62.98 -66.83
REMARK 500 2 HIS A 32 139.43 178.41
REMARK 500 2 ILE A 33 97.99 -47.52
REMARK 500 2 PRO A 43 172.54 -54.31
REMARK 500 2 PRO A 44 -165.02 -56.34
REMARK 500 2 GLN A 48 -100.28 -84.02
REMARK 500 2 ASP A 49 88.25 169.75
REMARK 500 2 ASP A 52 86.61 -60.43
REMARK 500 2 TYR A 53 77.77 -66.01
REMARK 500 2 GLU A 61 55.12 -97.64
REMARK 500 2 LEU A 64 -168.39 -63.26
REMARK 500 2 PRO A 66 -39.00 -33.02
REMARK 500 2 GLN A 79 -79.39 -60.29
REMARK 500 2 LYS A 85 84.71 -154.82
REMARK 500 2 ALA A 86 -133.05 66.26
REMARK 500 2 PRO A 91 -167.89 -74.73
REMARK 500 2 ASN A 103 43.53 -143.89
REMARK 500 2 ILE A 106 -77.23 -100.66
REMARK 500 2 PRO A 114 60.63 -68.15
REMARK 500 2 HIS A 115 82.35 -4.28
REMARK 500 2 TYR A 116 -31.07 -36.14
REMARK 500
REMARK 500 THIS ENTRY HAS 504 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HKA RELATED DB: PDB
REMARK 900 1HKA CONTAINS THE SAME PROTEIN.
REMARK 900 RELATED ID: 4299 RELATED DB: BMRB
REMARK 900 4299 CONTAINS THE SAME PROTEIN.
REMARK 900 RELATED ID: 4300 RELATED DB: BMRB
REMARK 900 4300 CONTAINS THE SAME PROTEIN COMPLEXED WITH AMPPCP.
DBREF 1EQ0 A 1 158 UNP P26281 HPPK_ECOLI 1 158
SEQRES 1 A 158 THR VAL ALA TYR ILE ALA ILE GLY SER ASN LEU ALA SER
SEQRES 2 A 158 PRO LEU GLU GLN VAL ASN ALA ALA LEU LYS ALA LEU GLY
SEQRES 3 A 158 ASP ILE PRO GLU SER HIS ILE LEU THR VAL SER SER PHE
SEQRES 4 A 158 TYR ARG THR PRO PRO LEU GLY PRO GLN ASP GLN PRO ASP
SEQRES 5 A 158 TYR LEU ASN ALA ALA VAL ALA LEU GLU THR SER LEU ALA
SEQRES 6 A 158 PRO GLU GLU LEU LEU ASN HIS THR GLN ARG ILE GLU LEU
SEQRES 7 A 158 GLN GLN GLY ARG VAL ARG LYS ALA GLU ARG TRP GLY PRO
SEQRES 8 A 158 ARG THR LEU ASP LEU ASP ILE MET LEU PHE GLY ASN GLU
SEQRES 9 A 158 VAL ILE ASN THR GLU ARG LEU THR VAL PRO HIS TYR ASP
SEQRES 10 A 158 MET LYS ASN ARG GLY PHE MET LEU TRP PRO LEU PHE GLU
SEQRES 11 A 158 ILE ALA PRO GLU LEU VAL PHE PRO ASP GLY GLU MET LEU
SEQRES 12 A 158 ARG GLN ILE LEU HIS THR ARG ALA PHE ASP LYS LEU ASN
SEQRES 13 A 158 LYS TRP
HELIX 1 1 GLN A 17 GLY A 26 1 10
HELIX 2 2 ALA A 65 GLN A 79 1 15
HELIX 3 3 MET A 124 GLU A 130 1 7
HELIX 4 4 MET A 142 ALA A 151 1 10
SHEET 1 A 2 ALA A 6 SER A 9 0
SHEET 2 A 2 LEU A 54 ALA A 57 -1 N LEU A 54 O SER A 9
SHEET 1 B 2 TYR A 40 ARG A 41 0
SHEET 2 B 2 ASN A 156 LYS A 157 -1 O ASN A 156 N ARG A 41
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
