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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
Complete list - b 16 2 Bytes