Header list of 1hdn.pdb file
Complete list - v 29 2 Bytes
HEADER PHOSPHOTRANSFERASE 10-FEB-94 1HDN
TITLE THE HIGH-RESOLUTION STRUCTURE OF THE HISTIDINE-CONTAINING
TITLE 2 PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI DETERMINED BY
TITLE 3 RESTRAINED MOLECULAR DYNAMICS FROM NMR NUCLEAR OVERHAUSER EFFECT DATA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS PHOSPHOTRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR N.A.J.VAN NULAND,R.M.SCHEEK,G.T.ROBILLARD
REVDAT 4 29-NOV-17 1HDN 1 REMARK HELIX
REVDAT 3 24-FEB-09 1HDN 1 VERSN
REVDAT 2 01-APR-03 1HDN 1 JRNL
REVDAT 1 22-JUN-94 1HDN 0
JRNL AUTH N.A.VAN NULAND,I.W.HANGYI,R.C.VAN SCHAIK,H.J.BERENDSEN,
JRNL AUTH 2 W.F.VAN GUNSTEREN,R.M.SCHEEK,G.T.ROBILLARD
JRNL TITL THE HIGH-RESOLUTION STRUCTURE OF THE HISTIDINE-CONTAINING
JRNL TITL 2 PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI DETERMINED
JRNL TITL 3 BY RESTRAINED MOLECULAR DYNAMICS FROM NUCLEAR MAGNETIC
JRNL TITL 4 RESONANCE NUCLEAR OVERHAUSER EFFECT DATA.
JRNL REF J.MOL.BIOL. V. 237 544 1994
JRNL REFN ISSN 0022-2836
JRNL PMID 8158637
JRNL DOI 10.1006/JMBI.1994.1254
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.A.J.VAN NULAND,J.GROETZINGER,K.DIJKSTRA,R.M.SCHEEK,
REMARK 1 AUTH 2 G.T.ROBILLARD
REMARK 1 TITL DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF THE
REMARK 1 TITL 2 HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM
REMARK 1 TITL 3 ESCHERICHIA COLI USING MULTIDIMENSIONAL NMR SPECTROSCOPY
REMARK 1 REF EUR.J.BIOCHEM. V. 210 881 1992
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.E.TORDA,R.M.SCHEEK,W.F.VAN GUNSTEREN
REMARK 1 TITL TIME-AVERAGED NUCLEAR OVERHAUSER EFFECT DISTANCE RESTRAINTS
REMARK 1 TITL 2 APPLIED TO TENDAMISTAT
REMARK 1 REF BIOCHEMISTRY V. 29 8164 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : GROMOS
REMARK 3 AUTHORS : FUJINAGA,GROS,VAN GUNSTEREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HDN 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_1000173797.
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 : 30
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 1.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 2 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 11 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 12 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 13 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 14 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 15 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 17 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 18 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 19 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 20 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 21 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 22 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 23 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 30 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
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 LEU A 14 57.45 -92.88
REMARK 500 1 THR A 16 -68.89 1.26
REMARK 500 1 ASN A 38 76.97 48.52
REMARK 500 1 LYS A 45 35.61 -95.24
REMARK 500 1 LEU A 55 76.78 -107.93
REMARK 500 1 GLN A 57 125.56 -35.90
REMARK 500 1 THR A 59 123.63 24.55
REMARK 500 2 HIS A 15 -147.46 -70.19
REMARK 500 2 ASN A 38 90.12 -19.32
REMARK 500 2 LYS A 45 31.17 -82.14
REMARK 500 2 SER A 46 113.32 -160.23
REMARK 500 2 LEU A 55 48.45 -100.38
REMARK 500 3 LEU A 14 69.35 -115.61
REMARK 500 3 ASN A 38 101.34 2.67
REMARK 500 3 GLN A 57 104.70 -49.01
REMARK 500 3 GLU A 70 -70.90 -8.00
REMARK 500 4 HIS A 15 -167.03 -67.41
REMARK 500 4 ASN A 38 87.51 -0.55
REMARK 500 4 THR A 56 -132.37 -135.30
REMARK 500 4 THR A 59 114.96 -3.09
REMARK 500 4 ASP A 69 33.73 -81.30
REMARK 500 4 LEU A 84 47.96 -108.64
REMARK 500 5 THR A 9 53.79 -118.48
REMARK 500 5 LEU A 14 58.18 -99.64
REMARK 500 5 HIS A 15 -169.60 -62.86
REMARK 500 5 ASN A 38 89.70 2.56
REMARK 500 5 LEU A 47 -71.00 -53.37
REMARK 500 5 LEU A 55 56.75 -103.82
REMARK 500 5 ASP A 69 47.05 -82.12
REMARK 500 6 ILE A 33 92.06 -64.57
REMARK 500 6 ASN A 38 67.47 32.81
REMARK 500 6 LYS A 40 93.69 -68.15
REMARK 500 6 SER A 41 106.41 -58.44
REMARK 500 6 SER A 43 106.09 -47.65
REMARK 500 6 GLN A 57 109.78 -18.12
REMARK 500 6 ASP A 69 40.52 -80.71
REMARK 500 6 GLU A 70 -73.25 -47.78
REMARK 500 7 PRO A 11 -76.64 -42.08
REMARK 500 7 HIS A 15 -155.52 -66.49
REMARK 500 7 ASN A 38 88.47 47.47
REMARK 500 7 ASP A 69 36.52 -83.28
REMARK 500 8 HIS A 15 -169.51 -72.34
REMARK 500 8 ASN A 38 61.97 35.12
REMARK 500 8 ASP A 69 33.49 -83.05
REMARK 500 9 ASN A 38 63.98 24.98
REMARK 500 10 HIS A 15 -154.93 -109.20
REMARK 500 10 ASN A 38 81.40 21.12
REMARK 500 10 THR A 52 33.71 -85.03
REMARK 500 10 LEU A 55 57.86 -94.96
REMARK 500 10 ASP A 69 42.71 -85.62
REMARK 500
REMARK 500 THIS ENTRY HAS 144 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 0.08 SIDE CHAIN
REMARK 500 3 HIS A 15 0.10 SIDE CHAIN
REMARK 500 5 PHE A 22 0.12 SIDE CHAIN
REMARK 500 6 HIS A 15 0.10 SIDE CHAIN
REMARK 500 8 PHE A 2 0.08 SIDE CHAIN
REMARK 500 8 HIS A 76 0.09 SIDE CHAIN
REMARK 500 16 PHE A 48 0.09 SIDE CHAIN
REMARK 500 17 PHE A 48 0.09 SIDE CHAIN
REMARK 500 22 PHE A 22 0.09 SIDE CHAIN
REMARK 500 23 PHE A 22 0.09 SIDE CHAIN
REMARK 500 24 PHE A 2 0.09 SIDE CHAIN
REMARK 500 26 PHE A 22 0.09 SIDE CHAIN
REMARK 500 30 PHE A 2 0.07 SIDE CHAIN
REMARK 500 30 PHE A 22 0.13 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 GLY A 13 -10.58
REMARK 500 2 MET A 1 10.21
REMARK 500 2 THR A 30 -10.10
REMARK 500 4 THR A 9 -12.95
REMARK 500 4 ASP A 69 -10.26
REMARK 500 5 GLU A 66 10.71
REMARK 500 5 ASP A 69 -10.54
REMARK 500 5 GLN A 71 -10.39
REMARK 500 6 ASP A 69 -10.33
REMARK 500 7 GLY A 13 -11.05
REMARK 500 8 LEU A 47 -10.93
REMARK 500 9 SER A 37 12.58
REMARK 500 9 THR A 59 10.64
REMARK 500 10 ASP A 69 -10.71
REMARK 500 11 SER A 37 10.69
REMARK 500 11 LEU A 47 -12.00
REMARK 500 14 LYS A 79 -10.59
REMARK 500 17 LEU A 14 -13.46
REMARK 500 17 SER A 37 10.35
REMARK 500 20 VAL A 60 12.17
REMARK 500 21 THR A 30 -11.06
REMARK 500 21 VAL A 60 10.40
REMARK 500 22 GLU A 32 11.79
REMARK 500 23 THR A 30 -10.11
REMARK 500 24 GLU A 32 11.71
REMARK 500 26 THR A 30 -10.22
REMARK 500 26 ASP A 69 -10.50
REMARK 500 27 LYS A 79 -10.26
REMARK 500 30 GLU A 32 10.26
REMARK 500 30 LYS A 49 -10.34
REMARK 500 30 LYS A 79 -10.04
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1HDN 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 HIS 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
HELIX 1 THR A 16 LYS A 27 1 12
HELIX 2 LEU A 47 THR A 52 1 6
HELIX 3 GLU A 70 GLU A 83 1 14
SHEET 1 S1 4 MET A 1 ILE A 8 0
SHEET 2 S1 4 VAL A 60 GLU A 66 -1
SHEET 3 S1 4 GLU A 32 SER A 37 -1
SHEET 4 S1 4 LYS A 40 SER A 43 -1
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