Header list of 1nct.pdb file
Complete list - 29 20 Bytes
HEADER MUSCLE PROTEIN 13-AUG-96 1NCT
TITLE TITIN MODULE M5, N-TERMINALLY EXTENDED, NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TITIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINALLY EXTENDED MODULE M5;
COMPND 5 SYNONYM: CONNECTIN, NEXTM5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 TISSUE: CARDIAC MUSCLE;
SOURCE 7 ORGANELLE: CYTOPLASMA/SARCOMERE;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21 PLYS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET8C
KEYWDS CELL ADHESION, GLYCOPROTEIN, TRANSMEMBRANE, BRAIN, IMMUNOGLOBULIN
KEYWDS 2 FOLD, ALTERNATIVE SPLICING, MUSCLE PROTEIN
EXPDTA SOLUTION NMR
AUTHOR M.PFUHL,A.PASTORE
REVDAT 3 29-NOV-17 1NCT 1 REMARK HELIX
REVDAT 2 24-FEB-09 1NCT 1 VERSN
REVDAT 1 08-NOV-96 1NCT 0
JRNL AUTH M.PFUHL,S.IMPROTA,A.S.POLITOUS,A.PASTORE
JRNL TITL WHEN A MODULE IS ALSO A DOMAIN: THE ROLE OF THE N TERMINUS
JRNL TITL 2 IN THE STABILITY AND THE DYNAMICS OF IMMUNOGLOBULIN DOMAINS
JRNL TITL 3 FROM TITIN.
JRNL REF J.MOL.BIOL. V. 265 242 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9020985
JRNL DOI 10.1006/JMBI.1996.0725
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.IMPROTA,A.S.POLITOU,A.PASTORE
REMARK 1 TITL IMMUNOGLOBULIN-LIKE MODULES FROM TITIN I-BAND EXTENSIBLE
REMARK 1 TITL 2 COMPONENTS OF MUSCLE ELASTICITY
REMARK 1 REF STRUCTURE V. 4 323 1996
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.PFUHL,A.PASTORE
REMARK 1 TITL TERTIARY STRUCTURE OF AN IMMUNOGLOBULIN-LIKE DOMAIN FROM THE
REMARK 1 TITL 2 GIANT MUSCLE PROTEIN TITIN: A NEW MEMBER OF THE I SET
REMARK 1 REF STRUCTURE V. 3 391 1995
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.PFUHL,M.GAUTEL,A.S.POLITOU,C.JOSEPH,A.PASTORE
REMARK 1 TITL SECONDARY STRUCTURE DETERMINATION BY NMR SPECTROSCOPY OF AN
REMARK 1 TITL 2 IMMUNOGLOBULIN-LIKE DOMAIN FROM THE GIANT MUSCLE PROTEIN
REMARK 1 TITL 3 TITIN
REMARK 1 REF J.BIOMOL.NMR V. 6 48 1995
REMARK 1 REFN ISSN 0925-2738
REMARK 1 REFERENCE 4
REMARK 1 AUTH A.S.POLITOU,M.GAUTEL,C.JOSEPH,A.PASTORE
REMARK 1 TITL IMMUNOGLOBULIN-TYPE DOMAINS OF TITIN ARE STABILIZED BY
REMARK 1 TITL 2 AMINO-TERMINAL EXTENSION
REMARK 1 REF FEBS LETT. V. 352 27 1994
REMARK 1 REFN ISSN 0014-5793
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 1NCT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175237.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 4.8
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 : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: 20 MM ACETATE BUFFER, NO OTHER SALTS
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 MET A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 SER A -7
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 THR A -4 -81.59 -89.57
REMARK 500 THR A -3 28.37 -176.93
REMARK 500 LEU A -2 -153.40 -85.67
REMARK 500 ALA A -1 -114.85 -174.29
REMARK 500 ARG A 7 176.12 -56.56
REMARK 500 SER A 8 -164.61 -100.80
REMARK 500 MET A 9 -176.67 -177.79
REMARK 500 THR A 10 119.62 -163.95
REMARK 500 GLU A 13 -128.07 -155.57
REMARK 500 GLU A 15 -81.85 -53.12
REMARK 500 SER A 16 52.64 175.78
REMARK 500 SER A 20 131.52 -176.00
REMARK 500 ARG A 35 -40.72 -169.48
REMARK 500 LYS A 36 34.27 -177.16
REMARK 500 GLN A 38 85.29 52.80
REMARK 500 VAL A 39 96.67 38.23
REMARK 500 SER A 41 90.83 -33.09
REMARK 500 THR A 42 50.17 21.56
REMARK 500 ALA A 44 -32.64 174.44
REMARK 500 THR A 51 -84.47 -117.68
REMARK 500 LYS A 52 -68.07 -138.15
REMARK 500 LYS A 54 117.06 -164.06
REMARK 500 SER A 60 16.35 -163.24
REMARK 500 GLN A 63 -74.78 -110.08
REMARK 500 ALA A 64 27.32 -165.61
REMARK 500 SER A 65 17.33 -150.66
REMARK 500 GLU A 67 -167.14 52.01
REMARK 500 ASN A 69 112.50 -29.96
REMARK 500 SER A 77 -31.04 -35.18
REMARK 500 GLU A 78 -11.70 -150.45
REMARK 500 LYS A 80 74.72 -158.28
REMARK 500 PHE A 85 131.68 -177.93
REMARK 500 ILE A 89 48.68 -142.09
REMARK 500 GLN A 90 114.92 -37.77
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 ARG A 1 0.20 SIDE CHAIN
REMARK 500 ARG A 7 0.24 SIDE CHAIN
REMARK 500 ARG A 18 0.30 SIDE CHAIN
REMARK 500 ARG A 35 0.27 SIDE CHAIN
REMARK 500 ARG A 45 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NCU RELATED DB: PDB
DBREF 1NCT A -5 91 UNP Q10466 Q10466_HUMAN 26059 26155
SEQRES 1 A 106 MET HIS HIS HIS HIS HIS HIS SER SER LYS THR THR LEU
SEQRES 2 A 106 ALA ALA ARG ILE LEU THR LYS PRO ARG SER MET THR VAL
SEQRES 3 A 106 TYR GLU GLY GLU SER ALA ARG PHE SER CYS ASP THR ASP
SEQRES 4 A 106 GLY GLU PRO VAL PRO THR VAL THR TRP LEU ARG LYS GLY
SEQRES 5 A 106 GLN VAL LEU SER THR SER ALA ARG HIS GLN VAL THR THR
SEQRES 6 A 106 THR LYS TYR LYS SER THR PHE GLU ILE SER SER VAL GLN
SEQRES 7 A 106 ALA SER ASP GLU GLY ASN TYR SER VAL VAL VAL GLU ASN
SEQRES 8 A 106 SER GLU GLY LYS GLN GLU ALA GLU PHE THR LEU THR ILE
SEQRES 9 A 106 GLN LYS
SHEET 1 S1 4 ALA A -1 LYS A 5 0
SHEET 2 S1 4 ARG A 18 GLU A 26 -1 N ASP A 22 O THR A 4
SHEET 3 S1 4 LYS A 54 ILE A 59 -1 N SER A 55 O CYS A 21
SHEET 4 S1 4 HIS A 46 THR A 51 -1 O THR A 49 N THR A 56
SHEET 1 S2 3 SER A 8 TYR A 12 0
SHEET 2 S2 3 GLY A 79 GLN A 90 1 N THR A 88 O MET A 9
SHEET 3 S2 3 GLY A 68 ASN A 76 -1 N VAL A 72 O ALA A 83
CISPEP 1 GLU A 26 PRO A 27 0 -0.60
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
Complete list - 29 20 Bytes