Header list of 1jc2.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL PROTEIN 07-JUN-01 1JC2
TITLE COMPLEX OF THE C-DOMAIN OF TROPONIN C WITH RESIDUES 1-40 OF TROPONIN I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPONIN C, SKELETAL MUSCLE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 89-163 OF GB ENTRY 212778;
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 GENE: STNC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS CA2+ BINDING PROTEIN, TROPONIN C, TROPONIN I, MUSCLE CONTRACTION,
KEYWDS 2 STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR P.MERCIER,L.SPYRACOPOULOS,B.D.SYKES
REVDAT 5 23-FEB-22 1JC2 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1JC2 1 VERSN
REVDAT 3 22-MAR-05 1JC2 1 JRNL REMARK
REVDAT 2 01-APR-03 1JC2 1 JRNL
REVDAT 1 14-SEP-01 1JC2 0
JRNL AUTH P.MERCIER,L.SPYRACOPOULOS,B.D.SYKES
JRNL TITL STRUCTURE, DYNAMICS, AND THERMODYNAMICS OF THE STRUCTURAL
JRNL TITL 2 DOMAIN OF TROPONIN C IN COMPLEX WITH THE REGULATORY PEPTIDE
JRNL TITL 3 1-40 OF TROPONIN I
JRNL REF BIOCHEMISTRY V. 40 10063 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11513585
JRNL DOI 10.1021/BI010748+
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER, A.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ~880 NOE RESTRAINTS WERE USED, AS WELL
REMARK 3 AS A 86 DIHEDRAL RESTRAINTS. THE CA AND CB CHEMICAL SHIFTS OF
REMARK 3 RESIDUES LOCATED IN WELL-DEFINED REGIONS WERE ALSO USED TO
REMARK 3 REFINE THE STRUCTURES
REMARK 4
REMARK 4 1JC2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-01.
REMARK 100 THE DEPOSITION ID IS D_1000013607.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 0.1
REMARK 210 PRESSURE : AMBIANT
REMARK 210 SAMPLE CONTENTS : ~1.3 MM C-DOMAIN OF SQELETAL
REMARK 210 TROPONIN C, 1.9 MM OF TNI
REMARK 210 PEPTIDE (RESIDUES 1-40), 100 MM
REMARK 210 KCL, 10 MM IMIDAZOLE, 1 MM DSS
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA; HNHB;
REMARK 210 HNCACB; CBCACONNH
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.8 REV 2000.081.21.00,
REMARK 210 NMRVIEW 4.0.3, PIPP 4.2
REMARK 210 METHOD USED : SIMMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: PROTON-PROTON NOES BETWEEN THE TNI PEPTIDE AND THE C
REMARK 210 -DOMAIN OF TROPONIN C WERE OBSERVED BUT COULD NOT BE ASSIGNED
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 1-30
REMARK 465 RES C SSSEQI
REMARK 465 MET A 87
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 ILE A 113 H ILE A 149 1.56
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 ASP A 89 150.58 65.07
REMARK 500 1 LYS A 93 -158.89 42.13
REMARK 500 1 ASP A 106 87.04 -67.61
REMARK 500 1 ALA A 109 89.93 -51.68
REMARK 500 1 ASP A 110 -34.54 -142.29
REMARK 500 1 THR A 125 -169.33 -74.90
REMARK 500 1 SER A 141 -61.50 -102.51
REMARK 500 1 ASP A 142 93.08 -39.38
REMARK 500 2 SER A 94 147.39 61.74
REMARK 500 2 ASN A 108 -151.70 -109.35
REMARK 500 2 ASP A 142 97.45 -45.41
REMARK 500 2 MET A 158 64.07 -101.04
REMARK 500 3 ALA A 90 114.61 66.70
REMARK 500 3 ALA A 109 79.42 43.98
REMARK 500 3 GLU A 127 92.64 -52.24
REMARK 500 3 HIS A 128 76.73 -67.32
REMARK 500 3 ASP A 142 96.70 -41.89
REMARK 500 3 ASN A 144 22.57 -140.31
REMARK 500 3 ASN A 145 86.10 48.94
REMARK 500 3 MET A 158 32.91 -95.66
REMARK 500 4 ASP A 89 -77.03 -132.12
REMARK 500 4 LYS A 91 142.46 -177.62
REMARK 500 4 LEU A 118 -30.07 -38.86
REMARK 500 4 VAL A 129 166.19 -45.48
REMARK 500 4 ASP A 142 88.51 -51.99
REMARK 500 4 MET A 158 48.92 -109.06
REMARK 500 5 ALA A 90 37.14 -143.38
REMARK 500 5 LYS A 93 93.92 -168.16
REMARK 500 5 ASP A 142 92.08 -43.44
REMARK 500 5 ASP A 150 -156.32 -97.70
REMARK 500 5 MET A 158 50.93 -96.88
REMARK 500 6 ASP A 89 67.88 -150.11
REMARK 500 6 ALA A 90 81.29 -172.19
REMARK 500 6 LYS A 91 -151.16 -112.69
REMARK 500 6 LYS A 93 107.09 54.95
REMARK 500 6 ASP A 142 91.14 -46.74
REMARK 500 6 ASN A 145 87.80 53.49
REMARK 500 6 ASP A 146 13.87 -143.97
REMARK 500 6 MET A 158 -29.16 -39.06
REMARK 500 7 ALA A 90 46.81 -98.29
REMARK 500 7 HIS A 128 72.45 43.58
REMARK 500 7 ASP A 142 89.28 -46.45
REMARK 500 8 ALA A 90 96.66 58.35
REMARK 500 8 LYS A 91 -168.56 -120.30
REMARK 500 8 ASP A 142 90.27 -60.55
REMARK 500 8 LYS A 143 49.12 -100.47
REMARK 500 8 ASN A 144 -74.32 -147.61
REMARK 500 8 ASN A 145 -46.26 172.06
REMARK 500 9 ASP A 89 148.93 65.37
REMARK 500 9 ALA A 90 81.17 64.14
REMARK 500
REMARK 500 THIS ENTRY HAS 205 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 103 0.32 SIDE CHAIN
REMARK 500 1 ARG A 123 0.32 SIDE CHAIN
REMARK 500 1 ARG A 148 0.24 SIDE CHAIN
REMARK 500 2 ARG A 103 0.21 SIDE CHAIN
REMARK 500 2 ARG A 123 0.22 SIDE CHAIN
REMARK 500 2 ARG A 148 0.31 SIDE CHAIN
REMARK 500 3 ARG A 103 0.27 SIDE CHAIN
REMARK 500 3 ARG A 123 0.30 SIDE CHAIN
REMARK 500 3 ARG A 148 0.21 SIDE CHAIN
REMARK 500 4 ARG A 103 0.31 SIDE CHAIN
REMARK 500 4 ARG A 123 0.31 SIDE CHAIN
REMARK 500 4 ARG A 148 0.30 SIDE CHAIN
REMARK 500 5 ARG A 103 0.31 SIDE CHAIN
REMARK 500 5 ARG A 123 0.32 SIDE CHAIN
REMARK 500 5 ARG A 148 0.31 SIDE CHAIN
REMARK 500 6 ARG A 103 0.09 SIDE CHAIN
REMARK 500 6 ARG A 123 0.17 SIDE CHAIN
REMARK 500 6 ARG A 148 0.32 SIDE CHAIN
REMARK 500 7 ARG A 103 0.24 SIDE CHAIN
REMARK 500 7 ARG A 123 0.31 SIDE CHAIN
REMARK 500 8 ARG A 103 0.23 SIDE CHAIN
REMARK 500 8 ARG A 123 0.21 SIDE CHAIN
REMARK 500 8 ARG A 148 0.28 SIDE CHAIN
REMARK 500 9 ARG A 103 0.32 SIDE CHAIN
REMARK 500 9 ARG A 123 0.31 SIDE CHAIN
REMARK 500 9 ARG A 148 0.19 SIDE CHAIN
REMARK 500 10 ARG A 103 0.10 SIDE CHAIN
REMARK 500 10 ARG A 123 0.10 SIDE CHAIN
REMARK 500 10 ARG A 148 0.11 SIDE CHAIN
REMARK 500 11 ARG A 103 0.13 SIDE CHAIN
REMARK 500 11 ARG A 123 0.30 SIDE CHAIN
REMARK 500 11 ARG A 148 0.24 SIDE CHAIN
REMARK 500 12 ARG A 103 0.29 SIDE CHAIN
REMARK 500 12 ARG A 123 0.28 SIDE CHAIN
REMARK 500 12 ARG A 148 0.30 SIDE CHAIN
REMARK 500 13 ARG A 103 0.10 SIDE CHAIN
REMARK 500 13 ARG A 123 0.10 SIDE CHAIN
REMARK 500 13 ARG A 148 0.25 SIDE CHAIN
REMARK 500 14 ARG A 103 0.23 SIDE CHAIN
REMARK 500 14 ARG A 123 0.31 SIDE CHAIN
REMARK 500 14 ARG A 148 0.20 SIDE CHAIN
REMARK 500 15 ARG A 148 0.29 SIDE CHAIN
REMARK 500 16 ARG A 103 0.32 SIDE CHAIN
REMARK 500 16 ARG A 123 0.30 SIDE CHAIN
REMARK 500 16 ARG A 148 0.30 SIDE CHAIN
REMARK 500 17 ARG A 103 0.29 SIDE CHAIN
REMARK 500 17 ARG A 123 0.09 SIDE CHAIN
REMARK 500 17 ARG A 148 0.26 SIDE CHAIN
REMARK 500 18 ARG A 103 0.32 SIDE CHAIN
REMARK 500 18 ARG A 148 0.25 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 86 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 2 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 106 OD1
REMARK 620 2 ASN A 108 ND2 129.2
REMARK 620 3 ASP A 110 OD2 92.7 106.6
REMARK 620 4 PHE A 112 O 63.0 155.8 49.3
REMARK 620 5 GLU A 117 OE1 105.4 113.3 105.5 76.9
REMARK 620 6 GLU A 117 OE2 118.0 70.3 143.4 126.1 49.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 3 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 142 OD1
REMARK 620 2 ASP A 146 OD1 72.5
REMARK 620 3 ASP A 146 OD2 109.7 58.6
REMARK 620 4 ARG A 148 O 115.9 56.2 75.4
REMARK 620 5 GLU A 153 OE1 117.7 137.6 132.5 85.0
REMARK 620 6 GLU A 153 OE2 133.2 150.3 94.2 108.7 51.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A2X RELATED DB: PDB
REMARK 900 COMPLEX OF TROPONIN C WITH A 47 RESIDUE (1-47) FRAGMENT OF TROPONIN
REMARK 900 I
DBREF 1JC2 A 88 162 UNP P02588 TNNC2_CHICK 89 163
SEQADV 1JC2 MET A 87 UNP P02588 CLONING ARTIFACT
SEQRES 1 A 76 MET GLU ASP ALA LYS GLY LYS SER GLU GLU GLU LEU ALA
SEQRES 2 A 76 ASN CYS PHE ARG ILE PHE ASP LYS ASN ALA ASP GLY PHE
SEQRES 3 A 76 ILE ASP ILE GLU GLU LEU GLY GLU ILE LEU ARG ALA THR
SEQRES 4 A 76 GLY GLU HIS VAL ILE GLU GLU ASP ILE GLU ASP LEU MET
SEQRES 5 A 76 LYS ASP SER ASP LYS ASN ASN ASP GLY ARG ILE ASP PHE
SEQRES 6 A 76 ASP GLU PHE LEU LYS MET MET GLU GLY VAL GLN
HET CA A 2 1
HET CA A 3 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 2(CA 2+)
HELIX 1 1 SER A 94 ASP A 106 1 13
HELIX 2 2 ILE A 115 THR A 125 1 11
HELIX 3 3 ILE A 130 ASP A 142 1 13
HELIX 4 4 ASP A 150 GLY A 160 1 11
SHEET 1 A 2 ILE A 113 ASP A 114 0
SHEET 2 A 2 ARG A 148 ILE A 149 -1 N ILE A 149 O ILE A 113
LINK CA CA A 2 OD1 ASP A 106 1555 1555 2.41
LINK CA CA A 2 ND2 ASN A 108 1555 1555 2.51
LINK CA CA A 2 OD2 ASP A 110 1555 1555 2.79
LINK CA CA A 2 O PHE A 112 1555 1555 2.97
LINK CA CA A 2 OE1 GLU A 117 1555 1555 2.58
LINK CA CA A 2 OE2 GLU A 117 1555 1555 2.52
LINK CA CA A 3 OD1 ASP A 142 1555 1555 2.80
LINK CA CA A 3 OD1 ASP A 146 1555 1555 2.36
LINK CA CA A 3 OD2 ASP A 146 1555 1555 1.99
LINK CA CA A 3 O ARG A 148 1555 1555 2.81
LINK CA CA A 3 OE1 GLU A 153 1555 1555 2.09
LINK CA CA A 3 OE2 GLU A 153 1555 1555 2.68
SITE 1 AC1 5 ASP A 106 ASN A 108 ASP A 110 PHE A 112
SITE 2 AC1 5 GLU A 117
SITE 1 AC2 5 ASP A 142 LYS A 143 ASP A 146 ARG A 148
SITE 2 AC2 5 GLU A 153
CRYST1 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 - b 23 2 Bytes