Header list of 1tnp.pdb file
Complete list - r 2 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 07-JUL-95 1TNP
TITLE STRUCTURES OF THE APO AND CALCIUM TROPONIN-C REGULATORY DOMAINS: THE
TITLE 2 MUSCLE CONTRACTION SWITCH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPONIN-C (APO);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NTNC APO;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 TISSUE: SKELETON;
SOURCE 6 GENE: NTNC;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 10 EXPRESSION_SYSTEM_GENE: NTNC
KEYWDS EF-HAND, CALCIUM-BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR S.M.GAGNE,B.D.SYKES
REVDAT 3 02-MAR-22 1TNP 1 REMARK
REVDAT 2 24-FEB-09 1TNP 1 VERSN
REVDAT 1 15-OCT-95 1TNP 0
JRNL AUTH S.M.GAGNE,S.TSUDA,M.X.LI,L.B.SMILLIE,B.D.SYKES
JRNL TITL STRUCTURES OF THE TROPONIN C REGULATORY DOMAINS IN THE APO
JRNL TITL 2 AND CALCIUM-SATURATED STATES.
JRNL REF NAT.STRUCT.BIOL. V. 2 784 1995
JRNL REFN ISSN 1072-8368
JRNL PMID 7552750
JRNL DOI 10.1038/NSB0995-784
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.M.GAGNE,S.TSUDA,M.X.LI,M.CHANDRA,L.B.SMILLIE,B.D.SYKES
REMARK 1 TITL QUANTIFICATION OF THE CALCIUM-INDUCED SECONDARY STRUCTURAL
REMARK 1 TITL 2 CHANGES IN THE REGULATORY DOMAIN OF TROPONIN-C
REMARK 1 REF PROTEIN SCI. V. 3 1961 1994
REMARK 1 REFN ISSN 0961-8368
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII
REMARK 3 AUTHORS : HAVEL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TNP 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_1000176758.
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 : 40
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 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 SER A 2 88.71 62.88
REMARK 500 1 ASP A 5 33.38 -156.14
REMARK 500 1 ALA A 31 -83.50 -52.27
REMARK 500 1 GLN A 51 -169.50 -114.53
REMARK 500 1 ASN A 52 50.18 -158.60
REMARK 500 1 VAL A 65 -85.06 -74.77
REMARK 500 1 GLU A 88 149.96 73.12
REMARK 500 2 SER A 2 35.10 -96.91
REMARK 500 2 MET A 3 50.72 -147.10
REMARK 500 2 ASP A 5 66.14 172.62
REMARK 500 2 PHE A 13 45.79 -99.17
REMARK 500 2 ASP A 66 37.93 -98.14
REMARK 500 2 ASP A 68 -87.51 -111.02
REMARK 500 2 SER A 70 -81.10 -77.86
REMARK 500 2 ASP A 89 174.55 72.59
REMARK 500 3 SER A 2 104.53 64.67
REMARK 500 3 MET A 3 41.66 -102.28
REMARK 500 3 ASP A 5 64.93 -168.89
REMARK 500 3 PHE A 13 35.29 -96.88
REMARK 500 3 ASN A 52 41.51 -158.84
REMARK 500 3 PRO A 53 -163.56 -64.11
REMARK 500 3 VAL A 65 36.48 -98.94
REMARK 500 3 ASP A 66 34.47 -151.69
REMARK 500 3 ASP A 68 75.55 -153.70
REMARK 500 3 ASP A 89 -87.81 -75.89
REMARK 500 4 SER A 2 106.30 74.11
REMARK 500 4 ASP A 5 70.83 -173.56
REMARK 500 4 LYS A 87 -72.51 -69.93
REMARK 500 4 ASP A 89 -81.97 -55.83
REMARK 500 5 SER A 2 -157.47 75.45
REMARK 500 5 MET A 3 75.27 78.15
REMARK 500 5 ASP A 5 50.72 82.41
REMARK 500 5 ASN A 52 57.47 -146.66
REMARK 500 5 PRO A 53 -156.97 -76.64
REMARK 500 5 ASP A 68 -50.51 -131.08
REMARK 500 5 SER A 70 91.81 56.96
REMARK 500 5 ASP A 74 -165.66 -108.50
REMARK 500 5 GLU A 88 138.68 172.39
REMARK 500 6 SER A 2 69.46 75.80
REMARK 500 6 ASP A 5 70.01 -170.10
REMARK 500 6 ALA A 31 -75.59 -59.93
REMARK 500 6 VAL A 65 -58.87 -156.16
REMARK 500 6 ASP A 66 50.51 -92.49
REMARK 500 6 ASP A 68 -154.94 -95.20
REMARK 500 6 ARG A 84 -71.63 -64.52
REMARK 500 6 ASP A 89 -75.91 -147.89
REMARK 500 7 MET A 3 36.77 -97.88
REMARK 500 7 ASP A 5 49.42 -149.33
REMARK 500 7 ASN A 52 64.77 -157.30
REMARK 500 7 GLU A 64 -71.09 -80.05
REMARK 500
REMARK 500 THIS ENTRY HAS 336 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 11 0.15 SIDE CHAIN
REMARK 500 1 ARG A 47 0.15 SIDE CHAIN
REMARK 500 1 ARG A 84 0.12 SIDE CHAIN
REMARK 500 2 ARG A 11 0.15 SIDE CHAIN
REMARK 500 2 ARG A 47 0.15 SIDE CHAIN
REMARK 500 2 ARG A 84 0.11 SIDE CHAIN
REMARK 500 3 ARG A 11 0.14 SIDE CHAIN
REMARK 500 3 ARG A 47 0.10 SIDE CHAIN
REMARK 500 3 ARG A 84 0.15 SIDE CHAIN
REMARK 500 4 ARG A 11 0.12 SIDE CHAIN
REMARK 500 4 ARG A 47 0.11 SIDE CHAIN
REMARK 500 4 ARG A 84 0.15 SIDE CHAIN
REMARK 500 5 ARG A 11 0.12 SIDE CHAIN
REMARK 500 5 ARG A 47 0.14 SIDE CHAIN
REMARK 500 5 ARG A 84 0.15 SIDE CHAIN
REMARK 500 6 ARG A 11 0.09 SIDE CHAIN
REMARK 500 6 ARG A 47 0.14 SIDE CHAIN
REMARK 500 6 ARG A 84 0.15 SIDE CHAIN
REMARK 500 7 ARG A 11 0.14 SIDE CHAIN
REMARK 500 7 ARG A 47 0.14 SIDE CHAIN
REMARK 500 7 ARG A 84 0.14 SIDE CHAIN
REMARK 500 8 ARG A 11 0.11 SIDE CHAIN
REMARK 500 8 ARG A 47 0.12 SIDE CHAIN
REMARK 500 8 ARG A 84 0.15 SIDE CHAIN
REMARK 500 9 ARG A 11 0.12 SIDE CHAIN
REMARK 500 9 ARG A 47 0.12 SIDE CHAIN
REMARK 500 9 ARG A 84 0.15 SIDE CHAIN
REMARK 500 10 ARG A 11 0.15 SIDE CHAIN
REMARK 500 10 ARG A 47 0.14 SIDE CHAIN
REMARK 500 10 ARG A 84 0.09 SIDE CHAIN
REMARK 500 11 ARG A 11 0.15 SIDE CHAIN
REMARK 500 11 ARG A 47 0.15 SIDE CHAIN
REMARK 500 11 ARG A 84 0.15 SIDE CHAIN
REMARK 500 12 ARG A 11 0.14 SIDE CHAIN
REMARK 500 12 ARG A 47 0.14 SIDE CHAIN
REMARK 500 12 ARG A 84 0.15 SIDE CHAIN
REMARK 500 13 ARG A 11 0.12 SIDE CHAIN
REMARK 500 13 ARG A 47 0.13 SIDE CHAIN
REMARK 500 13 ARG A 84 0.13 SIDE CHAIN
REMARK 500 14 ARG A 11 0.15 SIDE CHAIN
REMARK 500 14 ARG A 47 0.14 SIDE CHAIN
REMARK 500 14 ARG A 84 0.15 SIDE CHAIN
REMARK 500 15 ARG A 11 0.14 SIDE CHAIN
REMARK 500 15 ARG A 47 0.15 SIDE CHAIN
REMARK 500 15 ARG A 84 0.14 SIDE CHAIN
REMARK 500 16 ARG A 11 0.14 SIDE CHAIN
REMARK 500 16 ARG A 47 0.15 SIDE CHAIN
REMARK 500 16 ARG A 84 0.15 SIDE CHAIN
REMARK 500 17 ARG A 11 0.15 SIDE CHAIN
REMARK 500 17 ARG A 47 0.12 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 119 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: I
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: II
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
DBREF 1TNP A 1 90 UNP P02588 TNNC2_CHICK 1 90
SEQRES 1 A 90 ALA SER MET THR ASP GLN GLN ALA GLU ALA ARG ALA PHE
SEQRES 2 A 90 LEU SER GLU GLU MET ILE ALA GLU PHE LYS ALA ALA PHE
SEQRES 3 A 90 ASP MET PHE ASP ALA ASP GLY GLY GLY ASP ILE SER THR
SEQRES 4 A 90 LYS GLU LEU GLY THR VAL MET ARG MET LEU GLY GLN ASN
SEQRES 5 A 90 PRO THR LYS GLU GLU LEU ASP ALA ILE ILE GLU GLU VAL
SEQRES 6 A 90 ASP GLU ASP GLY SER GLY THR ILE ASP PHE GLU GLU PHE
SEQRES 7 A 90 LEU VAL MET MET VAL ARG GLN MET LYS GLU ASP ALA
HELIX 1 N GLN A 6 PHE A 13 1 8
HELIX 2 A GLU A 16 PHE A 29 1 14
HELIX 3 B THR A 39 MET A 48 1 10
HELIX 4 C LYS A 55 VAL A 65 1 11
HELIX 5 D PHE A 75 MET A 86 1 12
SHEET 1 A 2 ASP A 36 ILE A 37 0
SHEET 2 A 2 ILE A 73 ASP A 74 -1 O ILE A 73 N ILE A 37
SITE 1 I 12 ASP A 30 ALA A 31 ASP A 32 GLY A 33
SITE 2 I 12 GLY A 34 GLY A 35 ASP A 36 ILE A 37
SITE 3 I 12 SER A 38 THR A 39 LYS A 40 GLU A 41
SITE 1 II 12 ASP A 66 GLU A 67 ASP A 68 GLY A 69
SITE 2 II 12 SER A 70 GLY A 71 THR A 72 ILE A 73
SITE 3 II 12 ASP A 74 PHE A 75 GLU A 76 GLU A 77
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 - r 2 2 Bytes