HEADER MUSCLE PROTEIN 17-JAN-95 1TNN
TITLE TERTIARY STRUCTURE OF AN IMMUNOGLOBULIN-LIKE DOMAIN FROM THE GIANT
TITLE 2 MUSCLE PROTEIN TITIN: A NEW MEMBER OF THE I SET
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TITIN MODULE M5;
COMPND 3 CHAIN: A;
COMPND 4 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 ORGAN: CARDIAC MUSCLE;
SOURCE 7 GENE: TTN;
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 MUSCLE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR M.PFUHL,A.PASTORE
REVDAT 4 29-NOV-17 1TNN 1 REMARK HELIX
REVDAT 3 19-MAY-10 1TNN 1 SOURCE DBREF SEQADV
REVDAT 2 24-FEB-09 1TNN 1 VERSN
REVDAT 1 20-APR-95 1TNN 0
JRNL AUTH M.PFUHL,A.PASTORE
JRNL TITL TERTIARY STRUCTURE OF AN IMMUNOGLOBULIN-LIKE DOMAIN FROM THE
JRNL TITL 2 GIANT MUSCLE PROTEIN TITIN: A NEW MEMBER OF THE I SET.
JRNL REF STRUCTURE V. 3 391 1995
JRNL REFN ISSN 0969-2126
JRNL PMID 7613868
JRNL DOI 10.1016/S0969-2126(01)00170-8
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.PFUHL,M.GAUTEL,A.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 TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : GUNTERT,BRAUN,WUTHRICH (DIANA), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TNN 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_1000176757.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
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 : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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 MODELS 1-16
REMARK 465 RES C SSSEQI
REMARK 465 MET A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 SER A -1
REMARK 465 SER A 0
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 ILE A 2 76.45 55.87
REMARK 500 1 ARG A 7 -146.96 -62.66
REMARK 500 1 MET A 9 -171.41 173.72
REMARK 500 1 GLU A 13 114.35 -175.73
REMARK 500 1 SER A 16 -88.36 175.48
REMARK 500 1 ALA A 17 26.67 49.18
REMARK 500 1 GLU A 26 88.56 -169.02
REMARK 500 1 VAL A 28 137.26 57.93
REMARK 500 1 LEU A 34 157.34 179.16
REMARK 500 1 ARG A 35 66.82 179.07
REMARK 500 1 LEU A 40 28.03 42.46
REMARK 500 1 SER A 41 -149.44 39.83
REMARK 500 1 THR A 42 -32.26 -161.42
REMARK 500 1 SER A 43 -38.43 -157.73
REMARK 500 1 GLN A 47 51.19 -98.76
REMARK 500 1 SER A 61 48.91 -179.03
REMARK 500 1 GLN A 63 -149.14 -118.08
REMARK 500 1 ASP A 66 108.39 78.10
REMARK 500 1 GLU A 67 -11.49 -154.39
REMARK 500 1 ASN A 69 114.18 -37.47
REMARK 500 1 ASN A 76 58.14 -143.36
REMARK 500 1 SER A 77 22.87 45.94
REMARK 500 1 GLU A 78 -28.91 167.62
REMARK 500 1 GLU A 82 143.87 -172.68
REMARK 500 1 PHE A 85 -155.32 -145.93
REMARK 500 2 ILE A 2 84.05 55.40
REMARK 500 2 ARG A 7 -152.93 -62.57
REMARK 500 2 MET A 9 -170.88 173.71
REMARK 500 2 GLU A 13 119.88 -173.86
REMARK 500 2 GLU A 15 -152.36 -72.50
REMARK 500 2 SER A 16 -83.12 -69.72
REMARK 500 2 ALA A 17 100.48 54.45
REMARK 500 2 GLU A 26 71.64 -176.14
REMARK 500 2 VAL A 28 113.94 55.57
REMARK 500 2 ARG A 35 63.48 179.80
REMARK 500 2 SER A 41 -140.00 42.89
REMARK 500 2 THR A 42 81.24 174.52
REMARK 500 2 SER A 43 -61.54 80.06
REMARK 500 2 GLN A 47 52.88 -116.47
REMARK 500 2 SER A 61 31.92 -161.02
REMARK 500 2 ALA A 64 -88.07 55.69
REMARK 500 2 SER A 65 120.02 -175.49
REMARK 500 2 GLU A 67 -167.95 41.86
REMARK 500 2 ASN A 69 81.43 -5.82
REMARK 500 2 GLU A 78 48.24 -159.03
REMARK 500 2 GLU A 82 -176.60 -176.81
REMARK 500 2 PHE A 85 -169.66 -163.80
REMARK 500 2 GLN A 90 72.47 -116.21
REMARK 500 3 ARG A 7 -156.50 -66.29
REMARK 500 3 MET A 9 -172.86 179.00
REMARK 500
REMARK 500 THIS ENTRY HAS 420 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 1 0.26 SIDE CHAIN
REMARK 500 1 ARG A 7 0.31 SIDE CHAIN
REMARK 500 1 ARG A 18 0.24 SIDE CHAIN
REMARK 500 1 ARG A 35 0.29 SIDE CHAIN
REMARK 500 1 ARG A 45 0.31 SIDE CHAIN
REMARK 500 2 ARG A 1 0.20 SIDE CHAIN
REMARK 500 2 ARG A 7 0.28 SIDE CHAIN
REMARK 500 2 ARG A 18 0.17 SIDE CHAIN
REMARK 500 2 ARG A 35 0.14 SIDE CHAIN
REMARK 500 2 ARG A 45 0.32 SIDE CHAIN
REMARK 500 3 ARG A 1 0.27 SIDE CHAIN
REMARK 500 3 ARG A 7 0.31 SIDE CHAIN
REMARK 500 3 ARG A 18 0.27 SIDE CHAIN
REMARK 500 3 ARG A 35 0.17 SIDE CHAIN
REMARK 500 3 ARG A 45 0.27 SIDE CHAIN
REMARK 500 4 ARG A 1 0.27 SIDE CHAIN
REMARK 500 4 ARG A 7 0.25 SIDE CHAIN
REMARK 500 4 ARG A 18 0.30 SIDE CHAIN
REMARK 500 4 ARG A 35 0.23 SIDE CHAIN
REMARK 500 4 ARG A 45 0.24 SIDE CHAIN
REMARK 500 5 ARG A 1 0.20 SIDE CHAIN
REMARK 500 5 ARG A 7 0.27 SIDE CHAIN
REMARK 500 5 ARG A 18 0.24 SIDE CHAIN
REMARK 500 5 ARG A 35 0.26 SIDE CHAIN
REMARK 500 5 ARG A 45 0.30 SIDE CHAIN
REMARK 500 6 ARG A 1 0.21 SIDE CHAIN
REMARK 500 6 ARG A 7 0.32 SIDE CHAIN
REMARK 500 6 ARG A 18 0.22 SIDE CHAIN
REMARK 500 6 ARG A 35 0.30 SIDE CHAIN
REMARK 500 6 ARG A 45 0.30 SIDE CHAIN
REMARK 500 7 ARG A 1 0.24 SIDE CHAIN
REMARK 500 7 ARG A 7 0.28 SIDE CHAIN
REMARK 500 7 ARG A 18 0.32 SIDE CHAIN
REMARK 500 7 ARG A 35 0.30 SIDE CHAIN
REMARK 500 7 ARG A 45 0.31 SIDE CHAIN
REMARK 500 8 ARG A 1 0.24 SIDE CHAIN
REMARK 500 8 ARG A 7 0.30 SIDE CHAIN
REMARK 500 8 ARG A 18 0.21 SIDE CHAIN
REMARK 500 8 ARG A 35 0.22 SIDE CHAIN
REMARK 500 8 ARG A 45 0.32 SIDE CHAIN
REMARK 500 9 ARG A 1 0.31 SIDE CHAIN
REMARK 500 9 ARG A 7 0.23 SIDE CHAIN
REMARK 500 9 ARG A 18 0.27 SIDE CHAIN
REMARK 500 9 ARG A 45 0.25 SIDE CHAIN
REMARK 500 10 ARG A 1 0.32 SIDE CHAIN
REMARK 500 10 ARG A 7 0.30 SIDE CHAIN
REMARK 500 10 ARG A 18 0.27 SIDE CHAIN
REMARK 500 10 ARG A 35 0.30 SIDE CHAIN
REMARK 500 10 ARG A 45 0.29 SIDE CHAIN
REMARK 500 11 ARG A 1 0.21 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 79 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TNM RELATED DB: PDB
DBREF 1TNN A 1 91 UNP Q8WZ42 Q8WZ42_HUMAN 33489 33579
SEQADV 1TNN MET A -8 UNP Q8WZ42 EXPRESSION TAG
SEQADV 1TNN HIS A -7 UNP Q8WZ42 EXPRESSION TAG
SEQADV 1TNN HIS A -6 UNP Q8WZ42 EXPRESSION TAG
SEQADV 1TNN HIS A -5 UNP Q8WZ42 EXPRESSION TAG
SEQADV 1TNN HIS A -4 UNP Q8WZ42 EXPRESSION TAG
SEQADV 1TNN HIS A -3 UNP Q8WZ42 EXPRESSION TAG
SEQADV 1TNN HIS A -2 UNP Q8WZ42 EXPRESSION TAG
SEQADV 1TNN SER A -1 UNP Q8WZ42 EXPRESSION TAG
SEQADV 1TNN SER A 0 UNP Q8WZ42 EXPRESSION TAG
SEQRES 1 A 100 MET HIS HIS HIS HIS HIS HIS SER SER ARG ILE LEU THR
SEQRES 2 A 100 LYS PRO ARG SER MET THR VAL TYR GLU GLY GLU SER ALA
SEQRES 3 A 100 ARG PHE SER CYS ASP THR ASP GLY GLU PRO VAL PRO THR
SEQRES 4 A 100 VAL THR TRP LEU ARG LYS GLY GLN VAL LEU SER THR SER
SEQRES 5 A 100 ALA ARG HIS GLN VAL THR THR THR LYS TYR LYS SER THR
SEQRES 6 A 100 PHE GLU ILE SER SER VAL GLN ALA SER ASP GLU GLY ASN
SEQRES 7 A 100 TYR SER VAL VAL VAL GLU ASN SER GLU GLY LYS GLN GLU
SEQRES 8 A 100 ALA GLU PHE THR LEU THR ILE GLN LYS
SHEET 1 S1 4 ILE A 2 LYS A 5 0
SHEET 2 S1 4 ARG A 18 THR A 23 -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 4 SER A 8 TYR A 12 0
SHEET 2 S2 4 GLY A 79 GLN A 90 1 N THR A 88 O MET A 9
SHEET 3 S2 4 GLY A 68 ASN A 76 -1 N VAL A 72 O ALA A 83
SHEET 4 S2 4 THR A 30 ARG A 35 -1 N LEU A 34 O SER A 71
CISPEP 1 GLU A 26 PRO A 27 1 -0.49
CISPEP 2 GLU A 26 PRO A 27 2 -1.66
CISPEP 3 GLU A 26 PRO A 27 3 -0.38
CISPEP 4 GLU A 26 PRO A 27 4 -0.50
CISPEP 5 GLU A 26 PRO A 27 5 -0.40
CISPEP 6 GLU A 26 PRO A 27 6 -0.58
CISPEP 7 GLU A 26 PRO A 27 7 -0.51
CISPEP 8 GLU A 26 PRO A 27 8 -0.82
CISPEP 9 GLU A 26 PRO A 27 9 -1.25
CISPEP 10 GLU A 26 PRO A 27 10 -1.11
CISPEP 11 GLU A 26 PRO A 27 11 -0.92
CISPEP 12 GLU A 26 PRO A 27 12 -1.94
CISPEP 13 GLU A 26 PRO A 27 13 -0.96
CISPEP 14 GLU A 26 PRO A 27 14 -0.40
CISPEP 15 GLU A 26 PRO A 27 15 -1.00
CISPEP 16 GLU A 26 PRO A 27 16 -0.83
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
(ATOM LINES ARE NOT SHOWN.)
END
