Header list of 1qr5.pdb file
Complete list - v 29 2 Bytes
HEADER SIGNALING PROTEIN 19-MAY-99 1QR5
TITLE SOLUTION STRUCTURE OF HISTIDINE CONTAINING PROTEIN (HPR) FROM
TITLE 2 STAPHYLOCOCCUS CARNOSUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOCARRIER PROTEIN HPR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HISTIDINE-CONTAINING PROTEIN, HPR;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS CARNOSUS;
SOURCE 3 ORGANISM_TAXID: 1281;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PT7-5
KEYWDS PHOSPHOTRANSFERASE, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR H.R.KALBITZER,A.GORLER,H.LI,P.V.DUBOVSKII,W.HENGSTENBERG,C.KOWOLIK,
AUTHOR 2 H.YAMADA,K.AKASAKA
REVDAT 3 29-NOV-17 1QR5 1 REMARK HELIX
REVDAT 2 24-FEB-09 1QR5 1 VERSN
REVDAT 1 21-JUN-00 1QR5 0
JRNL AUTH H.R.KALBITZER,A.GORLER,H.LI,P.V.DUBOVSKII,W.HENGSTENBERG,
JRNL AUTH 2 C.KOWOLIK,H.YAMADA,K.AKASAKA
JRNL TITL 15N AND 1H NMR STUDY OF HISTIDINE CONTAINING PROTEIN (HPR)
JRNL TITL 2 FROM STAPHYLOCOCCUS CARNOSUS AT HIGH PRESSURE.
JRNL REF PROTEIN SCI. V. 9 693 2000
JRNL REFN ISSN 0961-8368
JRNL PMID 10794411
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.GORLER,W.HENGSTENBERG,M.KRAVANJA,W.BENEICKE,T.MAURER,
REMARK 1 AUTH 2 H.R.KALBITZER
REMARK 1 TITL SOLUTION STRUCTURE OF THE HISTIDINE-CONTAINING
REMARK 1 TITL 2 PHOSPHOCARRIER PROTEIN FROM STAPHYLOCOCCUS AUREUS
REMARK 1 REF APPL.MAGN.RESON. V. 17 465 1999
REMARK 1 REFN ISSN 0937-9347
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.51
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESTRAINED SIMULATED ANEALING PROTOCOL.
REMARK 3 CONSTRAINTS: 1301 NOES, 523 INTRARESIDUAL (I,I), 382
REMARK 3 INTERMEDIATE RANGE (I,I+2), 56 INTERMEDIATE RANGE (I,I+3), 31
REMARK 3 INTERMEDIATE RANGE (I,I+4), 224 LONG RANGE (I,J; J > I+4), 78 J-
REMARK 3 COUPLINGS (3JNH-HA). STRUCTURAL STATISTICS FOR THE 30 LOWEST-
REMARK 3 ENERGY STRUCTURES (REFERENCE 1): ENERGIES: TOTAL, 190.8 +-8.4 KJ/
REMARK 3 MOL; NOE, 57.6 +- 4.6 KJ/MOL; DIHEDRAL, 35.6 +- 6.1 KJ/MOL; BOND,
REMARK 3 8.4 +- 0.4 KJ/MOL; ANGLE, 64.0 +-2.6 KJ/MOL; VDW, 16.7 +- 2.3
REMARK 3 KJ/MOL; IMPROPER, 8.6 +- 1.2 KJ/MOL; ELECTRIC, 35.6 +- 6.1 KJ/
REMARK 3 MOL. RMSDS: AMINO ACID 1-88 (WHOLE PROTEIN), BACKBONE ATOMS
REMARK 3 0.093 NM, ALL NON-HYDROGEN ATOMS 0.13 NM. RMSDS: AMINO ACID 8-19
REMARK 3 (ACTIVE CENTER), BACKBONE ATOMS 0.091 NM, ALL NON-HYDROGEN ATOMS
REMARK 3 0.13 NM.
REMARK 4
REMARK 4 1QR5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUN-99.
REMARK 100 THE DEPOSITION ID IS D_1000001203.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.00
REMARK 210 PH : 7.14
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 90% H2O/10 % D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY; TOCSY; NOESY
REMARK 210 -HSQC; TOCSY-HSQC; 15N-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AMX-500; DMX-800
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : RESTRAINED MD
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 2300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST CONFORMATIONAL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 15N-LABELED PROTEIN.
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 78 H SER A 82 1.50
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 GLN A 4 118.95 -163.15
REMARK 500 1 ILE A 9 15.86 -145.86
REMARK 500 1 ILE A 14 81.70 -69.42
REMARK 500 1 HIS A 15 -162.16 -70.78
REMARK 500 1 ASP A 30 -20.26 84.07
REMARK 500 1 LYS A 41 109.65 -160.29
REMARK 500 1 LEU A 44 58.08 -68.81
REMARK 500 1 SER A 46 -49.01 69.30
REMARK 500 1 MET A 48 -39.50 -170.81
REMARK 500 1 VAL A 55 56.84 -100.79
REMARK 500 1 SER A 68 -68.74 -143.52
REMARK 500 1 THR A 87 -96.17 -96.88
REMARK 500 2 ASP A 10 87.59 -68.09
REMARK 500 2 HIS A 15 -153.53 -170.54
REMARK 500 2 ASP A 30 -7.28 74.80
REMARK 500 2 LYS A 40 -177.71 -177.84
REMARK 500 2 LEU A 44 57.53 -69.25
REMARK 500 2 SER A 46 -50.49 70.90
REMARK 500 2 MET A 48 -39.27 -166.64
REMARK 500 2 VAL A 55 63.37 35.90
REMARK 500 2 ASP A 58 11.19 86.45
REMARK 500 2 ASP A 69 36.59 -93.47
REMARK 500 2 GLN A 75 -71.72 -58.40
REMARK 500 2 THR A 87 -94.26 -94.46
REMARK 500 3 ASP A 10 78.04 -69.48
REMARK 500 3 HIS A 15 -156.23 -69.78
REMARK 500 3 ASP A 30 -20.84 82.50
REMARK 500 3 ASN A 38 -59.50 49.93
REMARK 500 3 LEU A 44 56.81 -67.66
REMARK 500 3 SER A 46 -47.64 72.95
REMARK 500 3 MET A 48 -37.93 -167.79
REMARK 500 3 VAL A 55 79.36 36.49
REMARK 500 3 ASP A 69 42.92 -91.48
REMARK 500 3 GLN A 75 -70.96 -55.52
REMARK 500 3 GLU A 84 37.29 -174.89
REMARK 500 3 THR A 87 -116.99 -123.72
REMARK 500 4 ASP A 10 73.97 -68.58
REMARK 500 4 ILE A 14 127.89 71.82
REMARK 500 4 HIS A 15 -119.30 -166.76
REMARK 500 4 ALA A 16 -167.13 -69.32
REMARK 500 4 ARG A 17 -73.03 12.29
REMARK 500 4 ASP A 30 -14.21 76.50
REMARK 500 4 LYS A 40 -179.70 -175.86
REMARK 500 4 LEU A 44 59.09 -68.81
REMARK 500 4 SER A 46 -52.28 69.59
REMARK 500 4 MET A 48 -39.19 -167.56
REMARK 500 4 ASP A 69 41.22 -91.52
REMARK 500 4 LYS A 83 -70.40 -55.96
REMARK 500 4 GLU A 84 39.80 -176.93
REMARK 500 4 THR A 87 139.08 65.03
REMARK 500
REMARK 500 THIS ENTRY HAS 131 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ND1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: THE ND1 ATOM OF RESIDUE HIS 15 OF HPR IS
REMARK 800 PHOSPHORYLATED BY ENZYME I. PHOSPHO-HPR DONATES ITS PHOSPHORYL
REMARK 800 GROUP TO ONE OF SEVERAL SUGAR SPECIFIC ENZYME II'S IN THE
REMARK 800 PHOSPHOENOLPYRUVATE DEPENDENT PHOSPHOTRANSFERASE SYSTEM (PTS) OF
REMARK 800 STAPHYLOCOCCUS CARNOSUS.
DBREF 1QR5 A 1 88 UNP P23534 PTHP_STACA 1 88
SEQRES 1 A 88 MET GLU GLN GLN SER TYR THR 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 ALA ASP ALA ILE GLN ALA ILE THR
SEQRES 7 A 88 ASP VAL LEU SER LYS GLU GLY LEU THR GLU
HELIX 1 A ALA A 16 PHE A 29 1 14
HELIX 2 B MET A 48 LEU A 53 1 6
HELIX 3 C ASP A 72 LEU A 86 1 15
SHEET 1 A 1 GLU A 2 ILE A 8 0
SHEET 1 D 1 ALA A 59 ASP A 66 0
SHEET 1 B 1 ASP A 32 TYR A 37 0
SHEET 1 C 1 LYS A 40 ASN A 43 0
SITE 1 ND1 1 HIS A 15
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