Header list of 1ka5.pdb file
Complete list - b 23 2 Bytes
HEADER LIGAND TRANSPORT 31-OCT-01 1KA5 TITLE REFINED SOLUTION STRUCTURE OF HISTIDINE CONTAINING PHOSPHOCARRIER TITLE 2 PROTEIN FROM STAPHYLOCCOCUS AUREUS COMPND MOL_ID: 1; COMPND 2 MOLECULE: PHOSPHOCARRIER PROTEIN HPR; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: HISTIDINE-CONTAINING PROTEIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS; SOURCE 3 ORGANISM_TAXID: 1280 KEYWDS OPEN FACED BETA-SANDWICH, STRUCTURAL PROTEOMICS IN EUROPE, SPINE, KEYWDS 2 STRUCTURAL GENOMICS, LIGAND TRANSPORT EXPDTA SOLUTION NMR NUMMDL 16 AUTHOR T.MAURER,S.MEIER,W.HENGSTENBERG,H.R.KALBITZER,STRUCTURAL PROTEOMICS AUTHOR 2 IN EUROPE (SPINE) REVDAT 4 23-FEB-22 1KA5 1 REMARK REVDAT 3 24-FEB-09 1KA5 1 VERSN REVDAT 2 12-OCT-04 1KA5 1 JRNL REVDAT 1 03-JUN-03 1KA5 0 SPRSDE 03-JUN-03 1KA5 1ZER JRNL AUTH T.MAURER,S.MEIER,N.KACHEL,C.E.MUNTE,S.HASENBEIN,B.KOCH, JRNL AUTH 2 W.HENGSTENBERG,H.R.KALBITZER JRNL TITL HIGH-RESOLUTION STRUCTURE OF THE HISTIDINE-CONTAINING JRNL TITL 2 PHOSPHOCARRIER PROTEIN (HPR) FROM STAPHYLOCOCCUS AUREUS AND JRNL TITL 3 CHARACTERIZATION OF ITS INTERACTION WITH THE BIFUNCTIONAL JRNL TITL 4 HPR KINASE/PHOSPHORYLASE JRNL REF J.BACTERIOL. V. 186 5906 2004 JRNL REFN ISSN 0021-9193 JRNL PMID 15317796 JRNL DOI 10.1128/JB.186.17.5906-5918.2004 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH H.R.KALBITZER,W.HENGSTENBERG REMARK 1 TITL THE SOLUTION STRUCTURE OF THE HISTIDINE CONTAINING REMARK 1 TITL 2 PHOSPHOCARRIER PROTEIN (HPR) FROM STAPHYLOCOCCUS AUREUS AS REMARK 1 TITL 3 DETERMINED BY TWO-DIMENSIONAL 1H-NMR SPECTROSCOPY REMARK 1 REF EUR.J.BIOCHEM. V. 216 205 1993 REMARK 1 REFN ISSN 0014-2956 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.6, DYANA 1.6 REMARK 3 AUTHORS : GUENTERT, P., MUMENTHALER, C. AND WUETHRICH, K. REMARK 3 (DYANA), GUENTERT, P., MUMENTHALER, C. AND REMARK 3 WUETHRICH, K. (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 1883 DISTANCE AND ANGLE RESTRAINTS AND REMARK 3 HYDROGEN BONDING PATTERNS REMARK 4 REMARK 4 1KA5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-01. REMARK 100 THE DEPOSITION ID IS D_1000014751. 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 : 0 REMARK 210 PRESSURE : AMBINET REMARK 210 SAMPLE CONTENTS : 2MM HPR REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY; HNHA; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 440 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION 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 GLN A 34 H TYR A 64 1.33 REMARK 500 O ASP A 69 H ALA A 73 1.43 REMARK 500 O LEU A 35 H VAL A 42 1.46 REMARK 500 H GLU A 36 O THR A 62 1.48 REMARK 500 O GLN A 3 HD21 ASN A 4 1.49 REMARK 500 O ILE A 47 H MET A 51 1.49 REMARK 500 O GLY A 54 H GLY A 56 1.50 REMARK 500 O GLN A 24 H LYS A 28 1.51 REMARK 500 O GLU A 36 H THR A 62 1.51 REMARK 500 H ILE A 9 O LEU A 86 1.51 REMARK 500 O THR A 20 H GLN A 24 1.54 REMARK 500 OD2 ASP A 10 H THR A 12 1.54 REMARK 500 H ILE A 8 O ALA A 59 1.54 REMARK 500 OG SER A 27 HZ2 LYS A 45 1.55 REMARK 500 O ASP A 79 H LYS A 83 1.58 REMARK 500 O MET A 21 H THR A 25 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 ILE A 14 111.21 -22.24 REMARK 500 1 HIS A 15 -166.68 -108.85 REMARK 500 1 LYS A 28 -34.93 -33.85 REMARK 500 1 PHE A 29 -81.23 -72.07 REMARK 500 1 ASP A 30 -60.66 169.57 REMARK 500 1 SER A 31 157.71 -36.30 REMARK 500 1 LEU A 44 22.37 -78.25 REMARK 500 1 MET A 48 -31.55 -37.23 REMARK 500 1 VAL A 55 62.56 -63.88 REMARK 500 1 ILE A 77 -70.30 -57.07 REMARK 500 2 ILE A 14 110.67 -20.47 REMARK 500 2 HIS A 15 -167.69 -109.26 REMARK 500 2 LYS A 28 -35.88 -32.42 REMARK 500 2 PHE A 29 -82.74 -70.02 REMARK 500 2 ASP A 30 -60.16 170.12 REMARK 500 2 SER A 31 158.16 -37.12 REMARK 500 2 MET A 48 -57.53 -17.90 REMARK 500 2 VAL A 55 62.51 -62.35 REMARK 500 2 ILE A 77 -70.41 -56.32 REMARK 500 3 ILE A 14 109.43 -20.00 REMARK 500 3 HIS A 15 -167.29 -108.37 REMARK 500 3 LYS A 28 -36.59 -33.88 REMARK 500 3 PHE A 29 -96.46 -75.31 REMARK 500 3 ASP A 30 -47.52 175.55 REMARK 500 3 SER A 31 151.29 -38.20 REMARK 500 3 MET A 48 -30.86 -37.47 REMARK 500 3 VAL A 55 62.81 -63.22 REMARK 500 3 ILE A 77 -70.84 -55.39 REMARK 500 4 ILE A 14 109.43 -20.00 REMARK 500 4 HIS A 15 -167.29 -108.37 REMARK 500 4 LYS A 28 -36.59 -33.88 REMARK 500 4 PHE A 29 -96.46 -75.31 REMARK 500 4 ASP A 30 -47.52 175.55 REMARK 500 4 SER A 31 151.29 -38.20 REMARK 500 4 MET A 48 -30.86 -37.47 REMARK 500 4 VAL A 55 62.81 -63.22 REMARK 500 4 ILE A 77 -70.84 -55.39 REMARK 500 5 ILE A 14 108.86 -20.18 REMARK 500 5 HIS A 15 -167.28 -107.80 REMARK 500 5 LYS A 28 -36.40 -36.11 REMARK 500 5 PHE A 29 -157.72 -79.36 REMARK 500 5 SER A 31 152.17 -37.76 REMARK 500 5 MET A 48 -30.10 -37.36 REMARK 500 5 VAL A 55 62.42 -64.04 REMARK 500 5 ILE A 77 -73.22 -53.78 REMARK 500 5 SER A 78 -34.17 -39.19 REMARK 500 6 ILE A 14 108.63 -21.33 REMARK 500 6 HIS A 15 -167.40 -107.79 REMARK 500 6 LYS A 28 -35.81 -33.69 REMARK 500 6 PHE A 29 -96.61 -76.24 REMARK 500 REMARK 500 THIS ENTRY HAS 147 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1ZER RELATED DB: PDB REMARK 900 THIS ENTRY REPLACES ENTRY 1ZER REMARK 900 RELATED ID: REGEN_HPR_SA RELATED DB: TARGETDB DBREF 1KA5 A 1 88 UNP P0A0E3 PTHP_STAAU 1 88 SEQRES 1 A 88 MET GLU GLN ASN SER TYR VAL ILE ILE ASP GLU THR GLY SEQRES 2 A 88 ILE HIS ALA ARG PRO ALA THR MET LEU VAL GLN THR ALA SEQRES 3 A 88 SER LYS PHE ASP SER ASP ILE GLN LEU GLU TYR ASN GLY SEQRES 4 A 88 LYS LYS VAL ASN LEU LYS SER ILE MET GLY VAL MET SER SEQRES 5 A 88 LEU GLY VAL GLY LYS ASP ALA GLU ILE THR ILE TYR ALA SEQRES 6 A 88 ASP GLY SER ASP GLU SER ASP ALA ILE GLN ALA ILE SER SEQRES 7 A 88 ASP VAL LEU SER LYS GLU GLY LEU THR LYS HELIX 1 1 HIS A 15 ASP A 30 1 16 HELIX 2 2 SER A 46 SER A 52 1 7 HELIX 3 3 ASP A 69 GLY A 85 1 17 SHEET 1 A 4 GLU A 2 VAL A 7 0 SHEET 2 A 4 GLU A 60 ASP A 66 -1 O ILE A 61 N TYR A 6 SHEET 3 A 4 ASP A 32 TYR A 37 -1 N GLN A 34 O TYR A 64 SHEET 4 A 4 LYS A 40 ASN A 43 -1 O VAL A 42 N LEU A 35 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 23 2 Bytes