Header list of 2hid.pdb file
Complete list - v 3 2 Bytes
HEADER PHOSPHOTRANSFERASE 17-MAY-96 2HID
TITLE REFINED NMR STRUCTURE OF PHOSPHOCARRIER HISTIDINE CONTAINING PROTEIN
TITLE 2 FROM BACILLUS SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTIDINE CONTAINING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HPR;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HISTIDINE CONTAINING PROTEIN, PHOSPHOTRANSFERASE, PTS
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR B.E.JONES,P.RAJAGOPAL,R.E.KLEVIT
REVDAT 4 03-NOV-21 2HID 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2HID 1 VERSN
REVDAT 2 01-APR-03 2HID 1 JRNL
REVDAT 1 08-NOV-96 2HID 0
SPRSDE 08-NOV-96 2HID 1HID
JRNL AUTH B.E.JONES,P.RAJAGOPAL,R.E.KLEVIT
JRNL TITL PHOSPHORYLATION ON HISTIDINE IS ACCOMPANIED BY LOCALIZED
JRNL TITL 2 STRUCTURAL CHANGES IN THE PHOSPHOCARRIER PROTEIN, HPR FROM
JRNL TITL 3 BACILLUS SUBTILIS.
JRNL REF PROTEIN SCI. V. 6 2107 1997
JRNL REFN ISSN 0961-8368
JRNL PMID 9336834
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.WITTEKIND,P.RAJAGOPAL,B.R.BRANCHINI,J.REIZER,
REMARK 1 AUTH 2 M.H.SAIER JUNIOR,R.E.KLEVIT
REMARK 1 TITL SOLUTION STRUCTURE OF THE PHOSPHOCARRIER PROTEIN HPR FROM
REMARK 1 TITL 2 BACILLUS SUBTILIS BY TWO-DIMENSIONAL NMR SPECTROSCOPY
REMARK 1 REF PROTEIN SCI. V. 1 1363 1992
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.WITTEKIND,J.REIZER,R.E.KLEVIT
REMARK 1 TITL SEQUENCE-SPECIFIC 1H NMR RESONANCE ASSIGNMENTS OF BACILLUS
REMARK 1 TITL 2 SUBTILIS HPR: USE OF SPECTRA OBTAINED FROM MUTANTS TO
REMARK 1 TITL 3 RESOLVE SPECTRAL OVERLAP
REMARK 1 REF BIOCHEMISTRY V. 29 7191 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.WITTEKIND,J.REIZER,J.DEUTSCHER,M.H.SAIER,R.E.KLEVIT
REMARK 1 TITL COMMON STRUCTURAL CHANGES ACCOMPANY THE FUNCTIONAL
REMARK 1 TITL 2 INACTIVATION OF HPR BY SERYL PHOSPHORYLATION OR BY SERINE TO
REMARK 1 TITL 3 ASPARTATE SUBSTITUTION
REMARK 1 REF BIOCHEMISTRY V. 28 9908 1989
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HID 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_1000178195.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.9
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 : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: 50 MM PHOSPHATE BUFFER
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: 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 GLN A 3 -172.55 -173.37
REMARK 500 1 SER A 12 -34.94 169.34
REMARK 500 1 HIS A 15 -124.93 -123.35
REMARK 500 1 LYS A 45 30.20 -96.20
REMARK 500 1 ASP A 69 40.76 -101.75
REMARK 500 2 SER A 12 -34.66 169.37
REMARK 500 2 HIS A 15 -127.09 -122.23
REMARK 500 2 ALA A 31 -165.67 -67.49
REMARK 500 2 LYS A 45 40.90 -95.17
REMARK 500 2 ASP A 69 45.48 -95.74
REMARK 500 3 GLN A 3 -164.85 43.31
REMARK 500 3 ASN A 38 -87.73 59.08
REMARK 500 3 LYS A 45 44.96 -92.72
REMARK 500 3 ALA A 56 -162.74 -129.90
REMARK 500 3 ASP A 69 40.50 -100.47
REMARK 500 4 ALA A 31 -173.66 -63.82
REMARK 500 4 ASN A 38 -85.75 63.78
REMARK 500 4 LYS A 45 46.92 -92.53
REMARK 500 4 ASP A 69 37.46 -99.56
REMARK 500 5 SER A 12 -35.18 169.65
REMARK 500 5 ALA A 31 -176.36 -61.63
REMARK 500 5 ASN A 38 -85.34 64.57
REMARK 500 5 ASP A 69 41.73 -97.04
REMARK 500 6 SER A 12 -34.94 169.76
REMARK 500 6 ASP A 69 41.23 -101.63
REMARK 500 7 HIS A 15 -167.49 -121.56
REMARK 500 8 HIS A 15 -165.58 -110.13
REMARK 500 8 ALA A 31 -174.87 -62.10
REMARK 500 8 ASP A 69 38.75 -98.13
REMARK 500 9 GLN A 3 167.33 176.50
REMARK 500 9 SER A 12 -46.19 84.44
REMARK 500 9 HIS A 15 -169.54 -119.21
REMARK 500 9 LYS A 45 41.79 -95.13
REMARK 500 9 ALA A 56 -168.51 -123.31
REMARK 500 10 THR A 9 22.63 -150.02
REMARK 500 10 ALA A 10 -169.20 -63.90
REMARK 500 10 HIS A 15 -125.78 -122.24
REMARK 500 10 ASP A 69 34.68 -98.32
REMARK 500 11 THR A 9 22.63 -150.02
REMARK 500 11 ALA A 10 -169.20 -63.90
REMARK 500 11 HIS A 15 -125.78 -122.24
REMARK 500 11 ASP A 69 34.68 -98.32
REMARK 500 12 GLN A 3 -173.72 -177.05
REMARK 500 12 LYS A 4 -171.21 -173.59
REMARK 500 12 SER A 12 -51.93 84.64
REMARK 500 12 HIS A 15 -167.59 -129.70
REMARK 500 12 ALA A 31 -174.38 -64.47
REMARK 500 12 ASP A 69 41.58 -97.71
REMARK 500 13 GLN A 3 -172.46 -177.10
REMARK 500 13 LYS A 4 -178.36 -176.33
REMARK 500
REMARK 500 THIS ENTRY HAS 111 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 1 ARG A 17 0.30 SIDE CHAIN
REMARK 500 2 ARG A 17 0.32 SIDE CHAIN
REMARK 500 3 ARG A 17 0.20 SIDE CHAIN
REMARK 500 4 ARG A 17 0.23 SIDE CHAIN
REMARK 500 5 ARG A 17 0.29 SIDE CHAIN
REMARK 500 6 ARG A 17 0.31 SIDE CHAIN
REMARK 500 7 ARG A 17 0.24 SIDE CHAIN
REMARK 500 8 ARG A 17 0.31 SIDE CHAIN
REMARK 500 9 ARG A 17 0.26 SIDE CHAIN
REMARK 500 10 ARG A 17 0.32 SIDE CHAIN
REMARK 500 11 ARG A 17 0.32 SIDE CHAIN
REMARK 500 12 ARG A 17 0.31 SIDE CHAIN
REMARK 500 13 ARG A 17 0.31 SIDE CHAIN
REMARK 500 14 ARG A 17 0.31 SIDE CHAIN
REMARK 500 15 ARG A 17 0.28 SIDE CHAIN
REMARK 500 16 ARG A 17 0.32 SIDE CHAIN
REMARK 500 17 ARG A 17 0.24 SIDE CHAIN
REMARK 500 18 ARG A 17 0.26 SIDE CHAIN
REMARK 500 19 ARG A 17 0.32 SIDE CHAIN
REMARK 500 20 ARG A 17 0.30 SIDE CHAIN
REMARK 500 21 ARG A 17 0.32 SIDE CHAIN
REMARK 500 22 ARG A 17 0.28 SIDE CHAIN
REMARK 500 23 ARG A 17 0.32 SIDE CHAIN
REMARK 500 24 ARG A 17 0.23 SIDE CHAIN
REMARK 500 25 ARG A 17 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2HID A 2 88 UNP P08877 PTHP_BACSU 1 87
SEQADV 2HID VAL A 51 UNP P08877 MET 50 ENGINEERED MUTATION
SEQRES 1 A 87 ALA GLN LYS THR PHE LYS VAL THR ALA ASP SER GLY ILE
SEQRES 2 A 87 HIS ALA ARG PRO ALA THR VAL LEU VAL GLN THR ALA SER
SEQRES 3 A 87 LYS TYR ASP ALA ASP VAL ASN LEU GLU TYR ASN GLY LYS
SEQRES 4 A 87 THR VAL ASN LEU LYS SER ILE MET GLY VAL VAL SER LEU
SEQRES 5 A 87 GLY ILE ALA LYS GLY ALA GLU ILE THR ILE SER ALA SER
SEQRES 6 A 87 GLY ALA ASP GLU ASN ASP ALA LEU ASN ALA LEU GLU GLU
SEQRES 7 A 87 THR MET LYS SER GLU GLY LEU GLY GLU
HELIX 1 1 ALA A 16 LYS A 28 1 13
HELIX 2 2 ILE A 47 LEU A 53 1 7
HELIX 3 3 GLU A 70 GLU A 84 1 15
SHEET 1 A 4 GLN A 3 VAL A 8 0
SHEET 2 A 4 ALA A 59 SER A 66 -1 N ILE A 63 O LYS A 4
SHEET 3 A 4 ASP A 32 TYR A 37 -1 N GLU A 36 O THR A 62
SHEET 4 A 4 LYS A 40 ASN A 43 -1 N VAL A 42 O 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 - v 3 2 Bytes