Header list of 1p82.pdb file
Complete list - 23 20 Bytes
HEADER CHAPERONE 06-MAY-03 1P82
TITLE NMR STRUCTURE OF 1-25 FRAGMENT OF MYCOBACTERIUM TUBERCULOSIS CPN10
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 10 KDA CHAPERONIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 1-25;
COMPND 5 SYNONYM: PROTEIN CPN10, GROES PROTEIN, BCG-A HEAT SHOCK PROTEIN, 10
COMPND 6 KDA ANTIGEN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SOLID PHASE SYNTHESIS
KEYWDS CPN10, MYCOBACTERIUM TUBERCULOSIS, HELIX FORMATION, CHAPERONE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.CIUTTI,O.SPIGA,E.GIANNOZZI,M.SCARSELLI,D.DI MARO,D.CALAMANDREI,
AUTHOR 2 N.NICCOLAI,A.BERNINI
REVDAT 3 23-FEB-22 1P82 1 REMARK
REVDAT 2 24-FEB-09 1P82 1 VERSN
REVDAT 1 27-MAY-03 1P82 0
JRNL AUTH A.CIUTTI,O.SPIGA,E.GIANNOZZI,M.SCARSELLI,D.DI MARO,
JRNL AUTH 2 D.CALAMANDREI,N.NICCOLAI,A.BERNINI
JRNL TITL SOLUTION STRUCTURE OF 1-25 FRAGMENT OF CPN10 FROM
JRNL TITL 2 MYCOBACTERIUM TUBERCULOSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.FOSSATI,G.IZZO,E.RIZZI,E.GANCIA,D.MODENA,M.L.MORAS,
REMARK 1 AUTH 2 N.NICCOLAI,E.GIANNOZZI,O.SPIGA,L.BONO,P.MARONE,E.LEONE,
REMARK 1 AUTH 3 F.MANGILI,S.HARDING,N.ERRINGTON,C.WALTER,B.HENDERSON,
REMARK 1 AUTH 4 M.M.ROBERTS,A.R.M.COATES,B.CASETTA,P.MASCAGNI
REMARK 1 TITL MYCOBACTERIUM TUBERCULOSIS CHAPERONIN 10 IS SECRETED IN THE
REMARK 1 TITL 2 MACROPHAGE PHAGOLYSOSOME: IS SECRETION DUE TO DISSOCIATION
REMARK 1 TITL 3 AND THE ADOPTION OF PARTIALLY HELICAL STRUCTURE AT THE
REMARK 1 TITL 4 MEMBRANE?
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, AMBER 5.1
REMARK 3 AUTHORS : BRUKER SPECTROSPIN (XWINNMR), CASE, PEARLMAN
REMARK 3 (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1P82 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019124.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM 1-25 FRAGMENT OF CPN10
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.1, NMRVIEW 4.1, DYANA
REMARK 210 1.5
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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 ASP A 10 H VAL A 14 1.38
REMARK 500 O VAL A 14 H GLU A 18 1.46
REMARK 500 O ILE A 5 H GLU A 9 1.54
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 ASN A 4 71.96 -103.62
REMARK 500 1 GLU A 20 -71.04 -77.85
REMARK 500 1 THR A 21 149.08 -36.24
REMARK 500 1 THR A 23 160.13 -39.84
REMARK 500 1 ALA A 24 82.11 -62.54
REMARK 500 2 ASN A 4 71.96 -103.82
REMARK 500 2 GLU A 20 -70.95 -77.46
REMARK 500 2 THR A 21 130.45 -36.23
REMARK 500 2 THR A 22 161.36 -46.94
REMARK 500 2 THR A 23 157.50 -38.47
REMARK 500 2 ALA A 24 83.59 -60.86
REMARK 500 3 ASN A 4 72.08 -103.70
REMARK 500 3 GLU A 20 -71.03 -77.84
REMARK 500 3 THR A 21 147.91 -36.24
REMARK 500 3 THR A 22 -85.01 -40.45
REMARK 500 3 THR A 23 36.46 -179.44
REMARK 500 4 ASN A 4 72.00 -103.62
REMARK 500 4 GLU A 20 -70.84 -77.71
REMARK 500 4 THR A 21 149.05 -36.31
REMARK 500 4 THR A 22 -178.05 -52.08
REMARK 500 4 THR A 23 34.84 -175.48
REMARK 500 5 ASN A 4 72.13 -103.71
REMARK 500 5 GLU A 20 -70.80 -77.65
REMARK 500 5 THR A 21 100.07 -36.32
REMARK 500 5 THR A 23 64.36 -67.88
REMARK 500 6 ASN A 4 72.10 -103.66
REMARK 500 6 GLU A 20 -70.94 -77.84
REMARK 500 6 THR A 21 153.53 -36.26
REMARK 500 6 THR A 22 107.24 -45.10
REMARK 500 6 THR A 23 67.36 -67.01
REMARK 500 7 ASN A 4 72.06 -103.70
REMARK 500 7 GLU A 20 -70.82 -77.60
REMARK 500 7 THR A 21 106.63 -36.30
REMARK 500 7 THR A 23 33.37 39.01
REMARK 500 8 ASN A 4 71.98 -103.70
REMARK 500 8 GLU A 20 -70.92 -77.88
REMARK 500 8 THR A 21 153.28 -36.40
REMARK 500 8 THR A 23 -157.87 38.78
REMARK 500 9 ASN A 4 72.03 -103.66
REMARK 500 9 GLU A 20 -71.08 -77.87
REMARK 500 9 THR A 21 153.05 -36.26
REMARK 500 9 THR A 23 66.98 -67.19
REMARK 500 9 ALA A 24 -70.72 -115.09
REMARK 500 10 ASN A 4 72.08 -103.72
REMARK 500 10 GLU A 20 -71.08 -77.88
REMARK 500 10 THR A 21 153.17 -36.27
REMARK 500 10 THR A 23 67.35 -66.95
REMARK 500 11 ASN A 4 72.85 -103.71
REMARK 500 11 ILE A 5 15.33 49.98
REMARK 500 11 GLU A 20 -70.95 -77.83
REMARK 500
REMARK 500 THIS ENTRY HAS 92 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HX5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ALL M. TUBERCULOSIS CHAPERONIN-10
DBREF 1P82 A 1 25 UNP P09621 CH10_MYCTU 1 25
SEQRES 1 A 25 ALA LYS VAL ASN ILE LYS PRO LEU GLU ASP LYS ILE LEU
SEQRES 2 A 25 VAL GLN ALA ASN GLU ALA GLU THR THR THR ALA SER
HELIX 1 1 ILE A 5 ALA A 19 1 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 - 23 20 Bytes