Header list of 1txe.pdb file
Complete list - v 10 2 Bytes
HEADER TRANSPORT PROTEIN 04-JUL-04 1TXE
TITLE SOLUTION STRUCTURE OF THE ACTIVE-CENTRE MUTANT ILE14ALA OF THE
TITLE 2 HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN (HPR) FROM STAPHYLOCOCCUS
TITLE 3 CARNOSUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOCARRIER PROTEIN HPR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HISTIDINE-CONTAINING PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS CARNOSUS;
SOURCE 3 ORGANISM_TAXID: 1281;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET11
KEYWDS OPEN-FACED BETA-SANDWICH, STRUCTURAL PROTEOMICS IN EUROPE, SPINE,
KEYWDS 2 STRUCTURAL GENOMICS, TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR A.MOEGLICH,B.KOCH,W.HENGSTENBERG,E.BRUNNER,H.R.KALBITZER,STRUCTURAL
AUTHOR 2 PROTEOMICS IN EUROPE (SPINE)
REVDAT 3 10-NOV-21 1TXE 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1TXE 1 VERSN
REVDAT 1 08-MAR-05 1TXE 0
JRNL AUTH A.MOEGLICH,B.KOCH,W.GRONWALD,W.HENGSTENBERG,E.BRUNNER,
JRNL AUTH 2 H.R.KALBITZER
JRNL TITL SOLUTION STRUCTURE OF THE ACTIVE-CENTRE MUTANT I14A OF THE
JRNL TITL 2 HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN FROM
JRNL TITL 3 STAPHYLOCOCCUS CARNOSUS
JRNL REF EUR.J.BIOCHEM. V. 271 4815 2004
JRNL REFN ISSN 0014-2956
JRNL PMID 15606769
JRNL DOI 10.1111/J.1432-1033.2004.04447.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.R.KALBITZER,A.GOERLER,H.LI,P.V.DUBOVSKII,W.HENGSTENBERG,
REMARK 1 AUTH 2 C.KOWOLIK,H.YAMADA,K.AKASAKA
REMARK 1 TITL 15N AND 1H NMR STUDY OF HISTIDINE CONTAINING PROTEIN (HPR)
REMARK 1 TITL 2 FROM STAPHYLOCOCCUS CARNOSUS AT HIGH PRESSURE
REMARK 1 REF PROTEIN SCI. V. 9 693 2000
REMARK 1 REFN ISSN 0961-8368
REMARK 1 PMID 10794411
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.GOERLER,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 CARNOSUS
REMARK 1 REF APPL.MAGN.RESON. V. 17 465 1999
REMARK 1 REFN ISSN 0937-9347
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.GROEGER,A.MOEGLICH,M.PONS,B.KOCH,W.HENGSTENBERG,
REMARK 1 AUTH 2 H.R.KALBITZER,E.BRUNNER
REMARK 1 TITL NMR-SPECTROSCOPIC MAPPING OF AN ENGINEERED CAVITY IN THE
REMARK 1 TITL 2 I14A MUTANT OF HPR FROM STAPHYLOCOCCUS CARNOSUS USING XENON
REMARK 1 REF J.AM.CHEM.SOC. V. 125 8726 2003
REMARK 1 REFN ISSN 0002-7863
REMARK 1 PMID 12862458
REMARK 1 DOI 10.1021/JA030113T
REMARK 1 REFERENCE 4
REMARK 1 AUTH S.B.NABUURS,A.J.NEDERVEEN,W.VRANKEN,J.F.DORELEIJERS,
REMARK 1 AUTH 2 A.M.J.J.BONVIN,G.W.VUISTER,G.VRIEND,C.A.E.M.SPRONK
REMARK 1 TITL DRESS: A DATABASE OF REFINED SOLUTION NMR STRUCTURES
REMARK 1 REF PROTEINS V. 55 483 2004
REMARK 1 REFN ISSN 0887-3585
REMARK 1 PMID 15103611
REMARK 1 DOI 10.1002/PROT.20118
REMARK 1 REFERENCE 5
REMARK 1 AUTH J.P.LINGE,M.A.WILLIAMS,C.A.E.M.SPRONK,A.M.J.J.BONVIN,
REMARK 1 AUTH 2 M.NILGES
REMARK 1 TITL REFINEMENT OF PROTEIN STRUCTURES IN EXPLICIT SOLVENT
REMARK 1 REF PROTEINS V. 50 496 2003
REMARK 1 REFN ISSN 0887-3585
REMARK 1 PMID 12557191
REMARK 1 DOI 10.1002/PROT.10299
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AUREMOL 1.0, CNS 1.0
REMARK 3 AUTHORS : GRONWALD, NEIDIG, KALBITZER (AUREMOL),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 TOTAL NUMBER OF NOES USED FOR THE CALCULATION: 1268,
REMARK 3 NUMBER OF INTRA-RESIDUE NOES USED FOR THE CALCULATION: 637,
REMARK 3 NUMBER OF SHORT RANGE NOES (I,J, I < J < I+5) USED FOR THE
REMARK 3 CALCULATION: 365,
REMARK 3 NUMBER OF LONG RANGE (I,J, J > I+4) NOES USED FOR THE
REMARK 3 CALCULATION: 266, NUMBER OF DIHEDRAL ANGLES RESTRAINTS USED
REMARK 3 FOR THE CALCULATION: 44, NUMBER OF HYDROGEN BOND RESTRAINTS
REMARK 3 USED FOR THE CALCULATION: 20,
REMARK 3 NUMBER OF 1HN/15NH RESIDUAL DIPOLAR COUPLINGS USED FOR THE
REMARK 3 CALCULATION: 49, NUMBER OF 1HN/1HA RESIDUAL DIPOLAR COUPLINGS
REMARK 3 USED FOR THE CALCULATION: 25
REMARK 4
REMARK 4 1TXE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000022999.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.14
REMARK 210 IONIC STRENGTH : 0.12
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.4MM HPRI14A, 20MM POTASSIUM
REMARK 210 PHOSPHATE PH 7.14, 100MM KCL;
REMARK 210 1.7MM HPRI14A U-15N, 20MM
REMARK 210 POTASSIUM PHOSPHATE PH 7.14,
REMARK 210 100MM KCL; 1.5MM HPRI14A U-15N,
REMARK 210 13C, 20MM POTASSIUM PHOSPHATE PH
REMARK 210 7.14, 100MM KCL; 0.9MM HPRI14A U-
REMARK 210 15N, 20MM POTASSIUM PHOSPHATE PH
REMARK 210 7.14, 100MM KCL, 7.5% DIODPC/
REMARK 210 CHAPSO (4.3:1)
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, CNS 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: RESIDUAL DIPOLAR COUPLINGS FOR THE AMIDE BOND (HN-N) AS
REMARK 210 WELL AS BETWEEN THE ATOMS HA AND HN HAVE ALSO BEEN USED AS
REMARK 210 RESTRAINTS FOR STRUCTURE DETERMINATION.
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
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 ALA A 14 -53.81 87.89
REMARK 500 1 HIS A 15 111.90 59.57
REMARK 500 1 LYS A 57 -64.28 20.12
REMARK 500 2 ALA A 14 111.12 79.48
REMARK 500 2 ASN A 38 77.91 42.02
REMARK 500 2 MET A 48 78.08 -105.59
REMARK 500 3 ALA A 14 -67.21 93.37
REMARK 500 3 HIS A 15 107.11 49.02
REMARK 500 3 ARG A 17 -51.21 -137.77
REMARK 500 3 THR A 25 -66.79 -91.26
REMARK 500 3 ASP A 30 -36.82 68.78
REMARK 500 3 TYR A 37 79.83 -110.30
REMARK 500 3 ASN A 38 79.95 34.81
REMARK 500 3 MET A 48 91.91 -68.19
REMARK 500 3 LYS A 57 -13.80 43.16
REMARK 500 3 GLU A 84 -82.80 -104.53
REMARK 500 4 ALA A 14 -34.26 89.43
REMARK 500 4 HIS A 15 135.95 67.42
REMARK 500 4 LYS A 57 -57.89 28.08
REMARK 500 5 THR A 12 11.05 57.41
REMARK 500 5 ALA A 14 10.21 -65.65
REMARK 500 5 ALA A 16 -76.33 -122.95
REMARK 500 5 TYR A 37 104.50 -165.24
REMARK 500 5 ASN A 38 74.84 48.07
REMARK 500 5 ASP A 58 -7.10 84.31
REMARK 500 6 ALA A 14 79.03 72.28
REMARK 500 6 ASN A 38 90.20 60.56
REMARK 500 6 MET A 48 81.53 -64.21
REMARK 500 6 ASP A 58 -5.40 79.88
REMARK 500 7 ALA A 14 78.19 -68.81
REMARK 500 7 ARG A 17 -47.47 -162.66
REMARK 500 7 ASN A 38 77.70 46.12
REMARK 500 7 LYS A 57 154.29 49.14
REMARK 500 7 ASP A 58 -16.65 68.82
REMARK 500 8 ALA A 14 -53.55 89.67
REMARK 500 8 HIS A 15 99.26 53.02
REMARK 500 8 TYR A 37 -25.96 -154.92
REMARK 500 8 ASN A 38 77.75 172.85
REMARK 500 8 LYS A 57 111.37 21.06
REMARK 500 8 ASP A 58 -0.79 74.80
REMARK 500 9 ASP A 10 97.28 -26.91
REMARK 500 9 ALA A 14 72.05 90.75
REMARK 500 9 ASP A 30 17.12 54.29
REMARK 500 9 LEU A 86 39.16 -140.56
REMARK 500 9 THR A 87 -155.03 -139.87
REMARK 500 10 ALA A 14 92.73 91.80
REMARK 500 10 HIS A 15 95.81 -69.99
REMARK 500 10 LYS A 28 -145.77 -114.09
REMARK 500 10 LYS A 57 -43.90 39.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6254 RELATED DB: BMRB
REMARK 900 1H, 13C, 15N CHEMICAL SHIFTS OF ILE14ALA MUTANT OF HPR FROM S.
REMARK 900 CARNOSUS
REMARK 900 RELATED ID: 1QR5 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF WILD-TYPE HPR FROM S. CARNOSUS
REMARK 900 RELATED ID: REGEN_HPR_SC RELATED DB: TARGETDB
DBREF 1TXE A 1 88 UNP P23534 PTHP_STACA 1 88
SEQADV 1TXE ALA A 14 UNP P23534 ILE 14 ENGINEERED MUTATION
SEQRES 1 A 88 MET GLU GLN GLN SER TYR THR ILE ILE ASP GLU THR GLY
SEQRES 2 A 88 ALA 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 1 HIS A 15 LYS A 28 1 14
HELIX 2 2 SER A 46 MET A 51 1 6
HELIX 3 3 ASP A 69 GLU A 84 1 16
SHEET 1 A 4 GLU A 2 THR 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 GLU A 36 O THR A 62
SHEET 4 A 4 LYS A 40 ASN A 43 -1 O LYS A 40 N TYR A 37
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 10 2 Bytes