Header list of 1pfh.pdb file
Complete list - v 29 2 Bytes
HEADER TRANSPORT PROTEIN 18-AUG-95 1PFH
TITLE THE PHOSPHORYLATED FORM OF THE HISTIDINE-CONTAINING PHOSPHOCARRIER
TITLE 2 PROTEIN HPR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHO-HPR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: P-HPR;
COMPND 5 OTHER_DETAILS: PH 7.5, 20 DEGREES C, 50 MM KPI BUFFER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: HB2154
KEYWDS PHOSPHOCARRIER PROTEIN, TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.A.J.VAN NULAND,R.M.SCHEEK,G.T.ROBILLARD
REVDAT 6 29-NOV-17 1PFH 1 REMARK HELIX
REVDAT 5 12-MAY-09 1PFH 1 ATOM MODEL
REVDAT 4 14-APR-09 1PFH 1 SEQRES
REVDAT 3 24-FEB-09 1PFH 1 VERSN
REVDAT 2 01-APR-03 1PFH 1 JRNL
REVDAT 1 14-NOV-95 1PFH 0
JRNL AUTH N.A.VAN NULAND,R.BOELENS,R.M.SCHEEK,G.T.ROBILLARD
JRNL TITL HIGH-RESOLUTION STRUCTURE OF THE PHOSPHORYLATED FORM OF THE
JRNL TITL 2 HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM
JRNL TITL 3 ESCHERICHIA COLI DETERMINED BY RESTRAINED MOLECULAR DYNAMICS
JRNL TITL 4 FROM NMR-NOE DATA.
JRNL REF J.MOL.BIOL. V. 246 180 1995
JRNL REFN ISSN 0022-2836
JRNL PMID 7853396
JRNL DOI 10.1006/JMBI.1994.0075
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.A.J.VAN NULAND,I.W.HANGYI,R.C.VAN SCHAIK,H.J.C.BERENDSEN,
REMARK 1 AUTH 2 W.F.VAN GUNSTEREN,R.M.SCHEEK,G.T.ROBILLARD
REMARK 1 TITL THE HIGH-RESOLUTION STRUCTURE OF THE HISTIDINE-CONTAINING
REMARK 1 TITL 2 PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI DETERMINED
REMARK 1 TITL 3 BY RESTRAINED MOLECULAR DYNAMICS FROM NUCLEAR MAGNETIC
REMARK 1 TITL 4 RESONANCE NUCLEAR OVERHAUSER EFFECT DATA
REMARK 1 REF J.MOL.BIOL. V. 237 544 1994
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH Z.JIA,M.VANDONSELAAR,J.W.QUAIL,L.T.J.DELBAERE
REMARK 1 TITL ACTIVE-CENTRE TORSION-ANGLE STRAIN REVEALED IN 1.6
REMARK 1 TITL 2 ANGSTROMS-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 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : GROMOS
REMARK 3 AUTHORS : VAN GUNSTEREN,BERENDSEN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PFH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175640.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 OE2 GLU A 32 HG SER A 43 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 HIP A 15 -121.43 51.01
REMARK 500 1 ASN A 38 64.44 37.94
REMARK 500 1 LYS A 40 88.69 -68.51
REMARK 500 1 SER A 43 103.85 -58.98
REMARK 500 1 LEU A 47 -73.35 -32.54
REMARK 500 1 ASP A 69 31.59 -83.56
REMARK 500 2 HIP A 15 -117.05 49.57
REMARK 500 2 THR A 16 -62.67 -100.20
REMARK 500 3 HIP A 15 -124.17 42.47
REMARK 500 3 THR A 52 54.01 -100.54
REMARK 500 4 HIP A 15 -115.84 47.58
REMARK 500 4 ASN A 38 51.31 39.94
REMARK 500 4 THR A 52 75.31 -118.12
REMARK 500 4 THR A 59 113.19 -30.79
REMARK 500 4 THR A 62 99.11 -65.99
REMARK 500 5 HIP A 15 -109.09 44.18
REMARK 500 5 THR A 16 -68.05 -101.22
REMARK 500 5 THR A 52 50.66 -100.06
REMARK 500 6 HIP A 15 -124.74 57.22
REMARK 500 6 LEU A 84 -150.03 -76.85
REMARK 500 7 HIP A 15 -125.89 60.39
REMARK 500 8 HIP A 15 -117.76 42.20
REMARK 500 8 ASN A 38 83.34 35.43
REMARK 500 8 LEU A 55 77.22 -115.29
REMARK 500 8 GLN A 57 106.71 -57.54
REMARK 500 9 HIP A 15 -124.92 33.06
REMARK 500 9 ASN A 38 70.13 43.26
REMARK 500 9 GLU A 70 -72.85 -46.05
REMARK 500 10 ALA A 10 133.44 -28.77
REMARK 500 10 HIP A 15 -123.33 50.80
REMARK 500 10 ASN A 38 71.25 43.94
REMARK 500 10 LEU A 53 -51.00 -149.58
REMARK 500 10 VAL A 61 78.85 -110.54
REMARK 500 10 GLU A 83 35.68 -82.98
REMARK 500 11 HIP A 15 -128.08 56.20
REMARK 500 11 ASN A 38 75.00 47.57
REMARK 500 11 THR A 52 60.61 -108.41
REMARK 500 12 HIP A 15 -119.57 48.09
REMARK 500 12 ASN A 38 90.25 33.77
REMARK 500 12 THR A 52 67.85 -116.31
REMARK 500 12 ASP A 69 39.26 -91.64
REMARK 500 13 HIP A 15 -123.02 47.63
REMARK 500 14 HIP A 15 -118.10 48.49
REMARK 500 15 HIP A 15 -114.46 47.76
REMARK 500 15 ASN A 38 72.43 43.63
REMARK 500 15 THR A 59 104.62 -54.96
REMARK 500 15 ASP A 69 36.49 -82.38
REMARK 500 15 GLU A 70 -72.53 -45.83
REMARK 500 16 HIP A 15 -132.09 48.67
REMARK 500 16 THR A 16 -61.42 -99.28
REMARK 500
REMARK 500 THIS ENTRY HAS 70 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 2 PHE A 22 0.10 SIDE CHAIN
REMARK 500 3 PHE A 22 0.08 SIDE CHAIN
REMARK 500 4 PHE A 22 0.09 SIDE CHAIN
REMARK 500 9 PHE A 22 0.07 SIDE CHAIN
REMARK 500 11 PHE A 48 0.08 SIDE CHAIN
REMARK 500 12 PHE A 22 0.09 SIDE CHAIN
REMARK 500 13 PHE A 22 0.09 SIDE CHAIN
REMARK 500 20 PHE A 22 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 1 HIP A 15 22.89
REMARK 500 2 HIP A 15 22.70
REMARK 500 2 ASP A 69 -11.65
REMARK 500 3 HIP A 15 22.91
REMARK 500 3 ASP A 69 -10.67
REMARK 500 4 HIP A 15 23.30
REMARK 500 4 ASP A 69 -10.24
REMARK 500 5 HIP A 15 23.47
REMARK 500 6 HIP A 15 22.72
REMARK 500 7 HIP A 15 22.31
REMARK 500 8 HIP A 15 22.52
REMARK 500 8 GLN A 71 -10.21
REMARK 500 9 HIP A 15 22.76
REMARK 500 9 VAL A 60 11.14
REMARK 500 9 GLN A 71 -10.29
REMARK 500 10 HIP A 15 22.79
REMARK 500 11 HIP A 15 22.51
REMARK 500 12 HIP A 15 22.60
REMARK 500 13 HIP A 15 22.89
REMARK 500 13 SER A 31 10.13
REMARK 500 13 ASP A 69 -11.26
REMARK 500 13 GLN A 71 -10.04
REMARK 500 14 MET A 1 12.51
REMARK 500 14 HIP A 15 22.22
REMARK 500 14 GLN A 71 -11.02
REMARK 500 15 HIP A 15 22.17
REMARK 500 16 HIP A 15 21.91
REMARK 500 16 PHE A 48 -10.14
REMARK 500 17 HIP A 15 22.07
REMARK 500 17 ASP A 69 -11.73
REMARK 500 18 HIP A 15 22.48
REMARK 500 18 SER A 37 10.66
REMARK 500 19 HIP A 15 22.60
REMARK 500 19 ASP A 69 -10.50
REMARK 500 19 LYS A 79 -11.37
REMARK 500 20 HIP A 15 22.52
REMARK 500 20 LEU A 47 -10.80
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1PFH A 1 85 UNP P0AA04 PTHP_ECOLI 1 85
SEQRES 1 A 85 MET PHE GLN GLN GLU VAL THR ILE THR ALA PRO ASN GLY
SEQRES 2 A 85 LEU HIP THR ARG PRO ALA ALA GLN PHE VAL LYS GLU ALA
SEQRES 3 A 85 LYS GLY PHE THR SER GLU ILE THR VAL THR SER ASN GLY
SEQRES 4 A 85 LYS SER ALA SER ALA LYS SER LEU PHE LYS LEU GLN THR
SEQRES 5 A 85 LEU GLY LEU THR GLN GLY THR VAL VAL THR ILE SER ALA
SEQRES 6 A 85 GLU GLY GLU ASP GLU GLN LYS ALA VAL GLU HIS LEU VAL
SEQRES 7 A 85 LYS LEU MET ALA GLU LEU GLU
MODRES 1PFH HIP A 15 HIS ND1-PHOSPHONOHISTIDINE
HET HIP A 15 16
HETNAM HIP ND1-PHOSPHONOHISTIDINE
FORMUL 1 HIP C6 H11 N3 O5 P 1+
HELIX 1 1 THR A 16 LYS A 27 1 12
HELIX 2 2 SER A 46 THR A 52 1 7
HELIX 3 3 ASP A 69 LEU A 84 1 16
SHEET 1 A 4 PHE A 2 THR A 7 0
SHEET 2 A 4 VAL A 60 ALA A 65 -1 O VAL A 61 N VAL A 6
SHEET 3 A 4 THR A 34 SER A 37 -1 N THR A 36 O THR A 62
SHEET 4 A 4 LYS A 40 SER A 43 -1 O ALA A 42 N VAL A 35
LINK C LEU A 14 N HIP A 15 1555 1555 1.33
LINK C HIP A 15 N THR A 16 1555 1555 1.33
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 29 2 Bytes