Header list of 1sbj.pdb file
Complete list - r 2 2 Bytes
HEADER CONTRACTILE PROTEIN, STRUCTURAL PROTEIN 10-FEB-04 1SBJ
TITLE NMR STRUCTURE OF THE MG2+-LOADED C TERMINAL DOMAIN OF CARDIAC TROPONIN
TITLE 2 C BOUND TO THE N TERMINAL DOMAIN OF CARDIAC TROPONIN I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPONIN C, SLOW SKELETAL AND CARDIAC MUSCLES;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (RESIDUES 81 - 161);
COMPND 5 SYNONYM: TN-C;
COMPND 6 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: CTNC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-23D+
KEYWDS TROPONIN C-TROPONIN I INTERACTION, CARDIAC, MUSCLE PROTEIN, 2
KEYWDS 2 MAGNESIUM BINDING PROTEIN, CONTRACTILE PROTEIN, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.L.FINLEY,J.W.HOWARTH,P.R.ROSEVEAR
REVDAT 5 02-MAR-22 1SBJ 1 REMARK LINK
REVDAT 4 24-FEB-09 1SBJ 1 VERSN
REVDAT 3 14-DEC-04 1SBJ 1 JRNL
REVDAT 2 30-NOV-04 1SBJ 1 HELIX SHEET REMARK
REVDAT 1 23-NOV-04 1SBJ 0
JRNL AUTH N.L.FINLEY,J.W.HOWARTH,P.R.ROSEVEAR
JRNL TITL STRUCTURE OF THE MG2+-LOADED C-LOBE OF CARDIAC TROPONIN C
JRNL TITL 2 BOUND TO THE N-DOMAIN OF CARDIAC TROPONIN I: COMPARISON WITH
JRNL TITL 3 THE CA2+-LOADED STRUCTURE.
JRNL REF BIOCHEMISTRY V. 43 11371 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15350124
JRNL DOI 10.1021/BI049672I
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 2000, CNX 1.0
REMARK 3 AUTHORS : ACCELRYS (FELIX), ACCELRYS (CNX)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 958 RESTRAINTS, 818 ARE NOE-DERIVED DISTANCE RESTRAINTS, 78
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 4 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS AND 58 DIPOLAR COUPLING RESTRAINTS
REMARK 4
REMARK 4 1SBJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-04.
REMARK 100 THE DEPOSITION ID IS D_1000021578.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 318.00
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 100 MM CACL2, 20 MM MGCL2
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM [13C,15]CTNC(81-161)/CTNI(33
REMARK 210 -80), 20MM TRIS(D11), 10MM DTT,
REMARK 210 20MM BETA-MERCAPTOETHANOL, 2MM
REMARK 210 EGTA, 100MM KCL, 20MM MGCL2, 90%
REMARK 210 H20, 10% D2O; 1MM [15N]CTNC(81-
REMARK 210 161)/CTNI(33-80), 20MM TRIS(D11),
REMARK 210 10MM DTT, 20MM BETA-
REMARK 210 MERCAPTOETHANOL, 2MM EGTA, 100MM
REMARK 210 KCL, 20MM MGCL2, 90% H20, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HSQC; HNHA, HNHB, CN-NOESY-HSQC;
REMARK 210 (HB)CBCA(CO)NH, HNCACB; H(CCO)NH,
REMARK 210 C(CO)NH; (HB)CB(CGCD)HD, (HB)
REMARK 210 CB(CGCDCE)HE; NOESY-HSQC, AB-
REMARK 210 TROSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.0, CNX 1.0
REMARK 210 METHOD USED : DGSA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
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 : 11
REMARK 210
REMARK 210 REMARK:
REMARK 210 BEST 20 STRUCTURES. THESE STRUCTURES WERE DETERMINED USING TRIPLE-
REMARK 210 RESONANCE
REMARK 210 NMR SPECTROSCOPY ON MG2+-SATURATED 15N,13C-CTNC(81-161) BOUND TO
REMARK 210 CTNI(33-80).
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 ARG A 83 -48.68 -141.26
REMARK 500 1 LYS A 86 -174.38 60.76
REMARK 500 1 LYS A 90 -178.32 -63.92
REMARK 500 1 THR A 93 -168.31 -111.65
REMARK 500 1 THR A 124 172.26 -59.63
REMARK 500 1 LYS A 158 41.65 -98.75
REMARK 500 2 LYS A 86 -62.25 -146.69
REMARK 500 2 SER A 89 -71.02 -106.98
REMARK 500 2 THR A 93 -92.56 -85.25
REMARK 500 2 ALA A 108 70.15 46.96
REMARK 500 2 THR A 124 174.32 -58.33
REMARK 500 2 LYS A 158 35.21 -99.31
REMARK 500 3 VAL A 82 -67.57 68.96
REMARK 500 3 MET A 85 108.27 -169.73
REMARK 500 3 ASP A 88 -77.42 -70.21
REMARK 500 3 LYS A 90 -171.23 -60.82
REMARK 500 3 THR A 93 -156.53 -113.94
REMARK 500 3 ALA A 108 71.19 47.16
REMARK 500 4 ARG A 83 101.57 60.19
REMARK 500 4 CYS A 84 -46.32 -152.07
REMARK 500 4 LYS A 86 -47.03 -152.89
REMARK 500 4 ASP A 88 -79.14 -132.37
REMARK 500 4 ALA A 108 75.36 44.80
REMARK 500 4 MET A 157 -72.71 -78.54
REMARK 500 4 LYS A 158 69.36 -61.81
REMARK 500 4 VAL A 160 41.00 -95.99
REMARK 500 5 VAL A 82 -65.63 69.17
REMARK 500 5 CYS A 84 114.43 59.83
REMARK 500 5 LYS A 86 -66.89 -127.32
REMARK 500 6 VAL A 82 -64.65 69.80
REMARK 500 6 ARG A 83 101.07 66.45
REMARK 500 6 LYS A 86 -167.80 58.72
REMARK 500 6 ASP A 88 177.22 -50.96
REMARK 500 6 THR A 93 -148.95 -113.41
REMARK 500 6 ALA A 108 75.30 46.34
REMARK 500 6 LYS A 158 39.94 -99.55
REMARK 500 7 VAL A 82 -46.37 -133.36
REMARK 500 7 ARG A 83 -66.21 -144.64
REMARK 500 7 CYS A 84 -55.41 -147.46
REMARK 500 7 SER A 89 -150.39 -105.96
REMARK 500 7 THR A 93 -158.21 -113.06
REMARK 500 7 THR A 124 -169.28 -63.81
REMARK 500 7 ASP A 141 83.21 -69.01
REMARK 500 8 CYS A 84 -64.65 -105.11
REMARK 500 8 ASP A 88 44.29 -103.45
REMARK 500 8 SER A 89 -88.20 -125.25
REMARK 500 8 LYS A 92 61.31 -119.32
REMARK 500 8 ALA A 108 96.01 40.65
REMARK 500 8 ASP A 109 -40.90 -141.11
REMARK 500 8 LYS A 158 66.34 -62.74
REMARK 500
REMARK 500 THIS ENTRY HAS 134 RAMACHANDRAN OUTLIERS.
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 MG A 162 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 105 OD2
REMARK 620 2 ASP A 105 OD1 19.8
REMARK 620 3 ASN A 107 OD1 95.3 103.4
REMARK 620 4 ASP A 109 OD1 54.9 74.2 62.6
REMARK 620 5 TYR A 111 O 62.3 73.7 121.6 60.7
REMARK 620 6 GLU A 116 OE2 169.4 170.5 78.5 114.5 113.4
REMARK 620 7 GLU A 116 OE1 136.4 128.8 127.3 132.5 84.6 48.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 163 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 141 OD1
REMARK 620 2 ASP A 141 OD2 43.1
REMARK 620 3 ASN A 143 OD1 64.7 107.8
REMARK 620 4 ASN A 143 ND2 107.1 141.5 50.6
REMARK 620 5 ASP A 145 OD2 97.0 86.2 103.8 72.4
REMARK 620 6 ASP A 145 OD1 70.3 77.2 78.8 68.1 30.6
REMARK 620 7 ARG A 147 O 100.5 58.6 159.7 129.3 62.6 83.1
REMARK 620 8 GLU A 152 OE1 96.6 104.1 81.6 103.0 166.5 159.8 115.2
REMARK 620 9 GLU A 152 OE2 145.1 123.2 115.4 95.1 115.6 144.3 84.8 51.4
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOR: AUTHOR
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOR: AUTHOR
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 163
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FI5 RELATED DB: PDB
REMARK 900 SAME COMPLEX WITH CA2+ BOUND
DBREF 1SBJ A 81 161 UNP P09860 TNNC1_CHICK 81 161
SEQRES 1 A 81 MET VAL ARG CYS MET LYS ASP ASP SER LYS GLY LYS THR
SEQRES 2 A 81 GLU GLU GLU LEU SER ASP LEU PHE ARG MET PHE ASP LYS
SEQRES 3 A 81 ASN ALA ASP GLY TYR ILE ASP LEU GLU GLU LEU LYS ILE
SEQRES 4 A 81 MET LEU GLN ALA THR GLY GLU THR ILE THR GLU ASP ASP
SEQRES 5 A 81 ILE GLU GLU LEU MET LYS ASP GLY ASP LYS ASN ASN ASP
SEQRES 6 A 81 GLY ARG ILE ASP TYR ASP GLU PHE LEU GLU PHE MET LYS
SEQRES 7 A 81 GLY VAL GLU
HET MG A 162 1
HET MG A 163 1
HETNAM MG MAGNESIUM ION
FORMUL 2 MG 2(MG 2+)
HELIX 1 1 THR A 93 MET A 103 5 11
HELIX 2 2 LEU A 114 ALA A 123 1 10
HELIX 3 3 GLU A 130 ASP A 139 1 10
HELIX 4 4 TYR A 150 PHE A 156 1 7
SHEET 1 A 2 TYR A 111 ASP A 113 0
SHEET 2 A 2 ARG A 147 ASP A 149 -1 O ILE A 148 N ILE A 112
LINK OD2 ASP A 105 MG MG A 162 1555 1555 4.15
LINK OD1 ASP A 105 MG MG A 162 1555 1555 2.21
LINK OD1 ASN A 107 MG MG A 162 1555 1555 2.62
LINK OD1 ASP A 109 MG MG A 162 1555 1555 2.64
LINK O TYR A 111 MG MG A 162 1555 1555 2.70
LINK OE2 GLU A 116 MG MG A 162 1555 1555 2.89
LINK OE1 GLU A 116 MG MG A 162 1555 1555 2.23
LINK OD1 ASP A 141 MG MG A 163 1555 1555 2.85
LINK OD2 ASP A 141 MG MG A 163 1555 1555 3.11
LINK OD1 ASN A 143 MG MG A 163 1555 1555 1.91
LINK ND2 ASN A 143 MG MG A 163 1555 1555 2.91
LINK OD2 ASP A 145 MG MG A 163 1555 1555 3.67
LINK OD1 ASP A 145 MG MG A 163 1555 1555 2.00
LINK O ARG A 147 MG MG A 163 1555 1555 2.23
LINK OE1 GLU A 152 MG MG A 163 1555 1555 2.78
LINK OE2 GLU A 152 MG MG A 163 1555 1555 2.06
SITE 1 AC1 5 ASP A 105 ASN A 107 ASP A 109 TYR A 111
SITE 2 AC1 5 GLU A 116
SITE 1 AC2 5 ASP A 141 ASN A 143 ASP A 145 ARG A 147
SITE 2 AC2 5 GLU A 152
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