Header list of 1qfr.pdb file
Complete list - v 27 2 Bytes
HEADER TRANSPORT PROTEIN 13-APR-99 1QFR TITLE NMR SOLUTION STRUCTURE OF PHOSPHOCARRIER PROTEIN HPR FROM ENTEROCOCCUS TITLE 2 FAECALIS COMPND MOL_ID: 1; COMPND 2 MOLECULE: PHOSPHOCARRIER PROTEIN HPR; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: HPR, HISTIDINE-CONTAINING PROTEIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROCOCCUS FAECALIS; SOURCE 3 ORGANISM_TAXID: 1351; SOURCE 4 STRAIN: S. FAECALIS 26487 KEYWDS HISTIDINE CONTAINING PHOSPHCARRIER PROTEIN, ENTEROCOCCUS FAECALIS, KEYWDS 2 PROTEIN, TRANSPORT PROTEIN EXPDTA SOLUTION NMR NUMMDL 16 AUTHOR T.MAURER,R.DOEKER,A.GOERLER,W.HENGSTENBERG,H.R.KALBITZER REVDAT 4 27-NOV-19 1QFR 1 JRNL REMARK SEQADV ATOM REVDAT 3 24-FEB-09 1QFR 1 VERSN REVDAT 2 01-APR-03 1QFR 1 JRNL REVDAT 1 28-FEB-01 1QFR 0 JRNL AUTH T.MAURER,R.DOKER,A.GORLER,W.HENGSTENBERG,H.R.KALBITZER JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE HISTIDINE-CONTAINING JRNL TITL 2 PHOSPHOCARRIER PROTEIN (HPR) FROM ENTEROCOCCUS FAECALIS IN JRNL TITL 3 SOLUTION. JRNL REF EUR.J.BIOCHEM. V. 268 635 2001 JRNL REFN ISSN 0014-2956 JRNL PMID 11168402 JRNL DOI 10.1046/J.1432-1327.2001.01916.X REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.HAHMANN,T.MAURER,M.LORENZ,W.HENGSTENBERG,S.GLASER, REMARK 1 AUTH 2 H.R.KALBITZER REMARK 1 TITL STRUCTURAL STUDIES OF HISTIDINE-CONTAINING PHOSPHOCARRIER REMARK 1 TITL 2 PROTEIN FROM ENTEROCOCCUS FAECALIS. REMARK 1 REF EUR.J.BIOCHEM. V. 252 51 1998 REMARK 1 REFN ISSN 0014-2956 REMARK 1 PMID 9523711 REMARK 1 DOI 10.1046/J.1432-1327.1998.2520051.X REMARK 1 REFERENCE 2 REMARK 1 AUTH Z.JIA,M.VANDONSELAAR,J.W.QUAIL,L.T.DELBAERE REMARK 1 TITL ACTIVE-CENTRE TORSION-ANGLE STRAIN REVEALED IN 1.6 REMARK 1 TITL 2 A-RESOLUTION STRUCTURE OF HISTIDINE-CONTAINING REMARK 1 TITL 3 PHOSPHOCARRIER PROTEIN. REMARK 1 REF NATURE V. 361 94 1993 REMARK 1 REFN ISSN 0028-0836 REMARK 1 PMID 8421502 REMARK 1 DOI 10.1038/361094A0 REMARK 1 REFERENCE 3 REMARK 1 AUTH J.DEUTSCHER,B.PEVEC,K.BEYREUTHER,H.H.KILTZ,W.HENGSTENBERG REMARK 1 TITL STREPTOCOCCAL PHOSPHOENOLPYRUVATE-SUGAR PHOSPHOTRANSFERASE REMARK 1 TITL 2 SYSTEM: AMINO ACID SEQUENCE AND SITE OF ATP-DEPENDENT REMARK 1 TITL 3 PHOSPHORYLATION OF HPR. REMARK 1 REF BIOCHEMISTRY V. 25 6543 1986 REMARK 1 REFN ISSN 0006-2960 REMARK 1 PMID 3098288 REMARK 1 DOI 10.1021/BI00369A031 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5 REMARK 3 AUTHORS : GUNTERT, MUMENTHALER, WUTHRICH REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: STANDARD ANGULAR SPACE SIMULATED REMARK 3 ANNEALING PROTOCOLL: CALC_ALL REMARK 4 REMARK 4 1QFR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-99. REMARK 100 THE DEPOSITION ID IS D_1000000842. 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 : 10% WATER/90% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY; NOESY-TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : AMX; DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR REMARK 210 METHOD USED : ANGULAR SPACE SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 440 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16 REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMUM PENALTY FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED BY HOMONUCLEAR NMR REMARK 210 EXPERIMENT. 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 THR A 20 H GLN A 24 1.10 REMARK 500 H ASP A 32 O ASP A 66 1.12 REMARK 500 H GLU A 36 O THR A 62 1.18 REMARK 500 O ILE A 47 H MET A 51 1.20 REMARK 500 O ASN A 43 H SER A 46 1.20 REMARK 500 O GLU A 36 H THR A 62 1.22 REMARK 500 HZ2 LYS A 40 O GLY A 49 1.23 REMARK 500 O HIS A 15 H ALA A 19 1.24 REMARK 500 O VAL A 23 H SER A 27 1.25 REMARK 500 O LEU A 81 H ALA A 87 1.33 REMARK 500 H ILE A 8 O SER A 59 1.34 REMARK 500 O THR A 80 H GLU A 84 1.35 REMARK 500 O ALA A 76 H THR A 80 1.35 REMARK 500 O ILE A 77 H LEU A 81 1.41 REMARK 500 H LYS A 4 O ILE A 63 1.46 REMARK 500 O MET A 74 H VAL A 78 1.50 REMARK 500 HA ILE A 8 O LEU A 86 1.51 REMARK 500 O SER A 46 H VAL A 50 1.51 REMARK 500 O ASP A 69 H GLY A 73 1.51 REMARK 500 HA ILE A 33 O THR A 64 1.54 REMARK 500 O LYS A 4 H ILE A 63 1.54 REMARK 500 O LEU A 22 H ALA A 26 1.55 REMARK 500 OG SER A 31 H GLU A 70 1.56 REMARK 500 H PHE A 6 O VAL A 61 1.58 REMARK 500 O ALA A 19 HG11 VAL A 23 1.58 REMARK 500 O ASN A 43 N SER A 46 1.92 REMARK 500 O PHE A 6 O VAL A 61 1.92 REMARK 500 N GLU A 36 O THR A 62 2.00 REMARK 500 O GLU A 36 N THR A 62 2.04 REMARK 500 O THR A 20 N GLN A 24 2.09 REMARK 500 N ASP A 32 O ASP A 66 2.11 REMARK 500 O ALA A 16 OG1 THR A 20 2.11 REMARK 500 O HIS A 15 N ALA A 19 2.12 REMARK 500 O ASN A 43 N LYS A 45 2.14 REMARK 500 NZ LYS A 40 O GLY A 49 2.16 REMARK 500 O ILE A 47 N MET A 51 2.16 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 GLU A 11 17.82 45.46 REMARK 500 1 ILE A 14 73.73 33.47 REMARK 500 1 ARG A 17 -73.69 -64.96 REMARK 500 1 SER A 27 45.48 -90.49 REMARK 500 1 LYS A 28 20.61 -148.55 REMARK 500 1 LYS A 38 -5.48 74.34 REMARK 500 1 ASN A 43 87.63 -42.78 REMARK 500 1 LEU A 44 -40.78 -19.97 REMARK 500 1 LEU A 53 -88.97 -92.16 REMARK 500 1 GLN A 57 87.23 -39.07 REMARK 500 1 GLU A 70 -59.79 -9.62 REMARK 500 2 GLU A 11 16.26 46.91 REMARK 500 2 ILE A 14 75.63 33.49 REMARK 500 2 ALA A 16 -35.68 -39.95 REMARK 500 2 ARG A 17 -73.55 -65.16 REMARK 500 2 SER A 27 44.98 -90.47 REMARK 500 2 LYS A 28 22.54 -149.12 REMARK 500 2 ASN A 30 0.13 -69.65 REMARK 500 2 ASN A 43 89.37 -42.02 REMARK 500 2 LEU A 44 -39.47 -21.18 REMARK 500 2 ILE A 47 -88.62 -40.31 REMARK 500 2 LEU A 53 -108.72 -75.18 REMARK 500 2 GLN A 57 84.62 -37.17 REMARK 500 2 GLU A 70 -69.11 -5.08 REMARK 500 2 ALA A 71 -72.30 -56.87 REMARK 500 3 GLU A 11 18.48 46.09 REMARK 500 3 ILE A 14 72.85 37.96 REMARK 500 3 ARG A 17 -73.34 -66.52 REMARK 500 3 SER A 27 44.63 -91.54 REMARK 500 3 LYS A 28 23.18 -149.98 REMARK 500 3 LYS A 38 -0.77 71.69 REMARK 500 3 ASN A 43 84.18 -44.38 REMARK 500 3 LEU A 44 -41.25 -11.64 REMARK 500 3 MET A 48 -76.03 -40.58 REMARK 500 3 LEU A 53 -93.42 -95.07 REMARK 500 3 GLN A 57 80.10 -35.92 REMARK 500 3 SER A 59 165.32 -42.57 REMARK 500 3 GLU A 70 -60.99 -12.30 REMARK 500 4 GLU A 11 16.02 46.69 REMARK 500 4 THR A 12 -78.28 -69.48 REMARK 500 4 ILE A 14 68.52 39.06 REMARK 500 4 ALA A 16 -35.78 -39.75 REMARK 500 4 ARG A 17 -71.89 -67.62 REMARK 500 4 SER A 27 42.46 -91.39 REMARK 500 4 LYS A 28 23.85 -148.72 REMARK 500 4 ASN A 43 88.86 -42.61 REMARK 500 4 LEU A 44 -38.62 -19.18 REMARK 500 4 LEU A 53 -92.49 -92.76 REMARK 500 4 GLN A 57 89.32 -42.16 REMARK 500 4 ALA A 68 -66.65 -98.85 REMARK 500 REMARK 500 THIS ENTRY HAS 222 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1QFR A 1 88 UNP P07515 PTHP_ENTFA 1 88 SEQADV 1QFR GLN A 89 UNP P07515 CONFLICT SEQRES 1 A 89 MET GLU LYS LYS GLU PHE HIS ILE VAL ALA GLU THR GLY SEQRES 2 A 89 ILE HIS ALA ARG PRO ALA THR LEU LEU VAL GLN THR ALA SEQRES 3 A 89 SER LYS PHE ASN SER ASP ILE ASN LEU GLU TYR LYS GLY SEQRES 4 A 89 LYS SER VAL ASN LEU LYS SER ILE MET GLY VAL MET SER SEQRES 5 A 89 LEU GLY VAL GLY GLN GLY SER ASP VAL THR ILE THR VAL SEQRES 6 A 89 ASP GLY ALA ASP GLU ALA GLU GLY MET ALA ALA ILE VAL SEQRES 7 A 89 GLU THR LEU GLN LYS GLU GLY LEU ALA GLU GLN HELIX 1 1 HIS A 15 SER A 27 1 13 HELIX 2 2 SER A 46 GLY A 54 1 9 HELIX 3 3 ASP A 69 GLU A 84 1 16 SHEET 1 A 4 GLU A 2 HIS A 7 0 SHEET 2 A 4 ASP A 60 ASP A 66 -1 O VAL A 61 N PHE A 6 SHEET 3 A 4 ASP A 32 TYR A 37 -1 N ASP A 32 O ASP A 66 SHEET 4 A 4 LYS A 40 VAL A 42 -1 O LYS A 40 N TYR A 37 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 - v 27 2 Bytes