Header list of 1fi5.pdb file
Complete list - b 23 2 Bytes
HEADER CONTRACTILE PROTEIN 03-AUG-00 1FI5 TITLE NMR STRUCTURE OF THE C TERMINAL DOMAIN OF CARDIAC TROPONIN C BOUND TO TITLE 2 THE N TERMINAL DOMAIN OF CARDIAC TROPONIN I. COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (TROPONIN C); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 81 - 161; 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 ORGAN: HEART; SOURCE 6 TISSUE: MUSCLE; SOURCE 7 CELL: MYOCYTE; SOURCE 8 CELLULAR_LOCATION: THIN FILAMENT; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 10 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET-23D+; SOURCE 13 EXPRESSION_SYSTEM_GENE: CTNC(81-161); SOURCE 14 OTHER_DETAILS: C TERMINAL DOMAIN OF CARDIAC TROPONIN C (81- 161) SOURCE 15 BOUND TO THE N TERMINAL DOMAIN OF CARDIAC TROPONIN I (33-80), SOURCE 16 CALCIUM IONS BOUND AT SITES III AND IV KEYWDS TROPONIN C-TROPONIN I INTERACTION, CARDIAC, MUSCLE PROTEIN, CALCIUM KEYWDS 2 BINDING PROTEIN, CONTRACTILE PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR G.M.GASMI-SEABROOK,J.W.HOWARTH,N.FINLEY,E.ABUSAMHADNEH,V.GAPONENKO, AUTHOR 2 R.M.BRITO,R.J.SOLARO,P.R.ROSEVEAR REVDAT 3 23-FEB-22 1FI5 1 REMARK LINK REVDAT 2 24-FEB-09 1FI5 1 VERSN REVDAT 1 23-AUG-00 1FI5 0 SPRSDE 23-AUG-00 1FI5 1GGS JRNL AUTH G.M.GASMI-SEABROOK,J.W.HOWARTH,N.FINLEY,E.ABUSAMHADNEH, JRNL AUTH 2 V.GAPONENKO,R.M.BRITO,R.J.SOLARO,P.R.ROSEVEAR JRNL TITL SOLUTION STRUCTURES OF THE C-TERMINAL DOMAIN OF CARDIAC JRNL TITL 2 TROPONIN C FREE AND BOUND TO THE N-TERMINAL DOMAIN OF JRNL TITL 3 CARDIAC TROPONIN I. JRNL REF BIOCHEMISTRY V. 38 8313 1999 JRNL REFN ISSN 0006-2960 JRNL PMID 10387077 JRNL DOI 10.1021/BI9902642 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION ABOVE REMARK 4 REMARK 4 1FI5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-AUG-00. REMARK 100 THE DEPOSITION ID IS D_1000011611. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 318.00 REMARK 210 PH : 6.80 REMARK 210 IONIC STRENGTH : 100MM KCL,15MM CACL2, 100MM REMARK 210 KCL,15MM CACL2 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM [15N,13C]CTNC(81 REMARK 210 -161)/CTNI(33-80); 20MM TRIS-D11; REMARK 210 100MM KCL; 20MM DTT; 15MM CACL2; REMARK 210 0.1MM LEUPETIN; 0.1MM PEFABLOC; REMARK 210 90% H2O/10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-HSQC; 15N-NOESY- HSQC; 15N REMARK 210 -TOCSY-HSQC; HNCO; HNCACB; (HB) REMARK 210 CBCA (CO)NNH; H(CCO)NH; C (CO)NH; REMARK 210 (HB)CB(CGCD)HD; (HB)CB(CGCDCE) REMARK 210 HE; CN- NOESY-HSQC; HNHA; HNHB. REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : INOVA600; INOVA800 REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS 1.0 REMARK 210 METHOD USED : DGSA REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 500 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : SMALLEST RMSD TO AVERAGE REMARK 210 STRUCTURE REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 5 REMARK 210 REMARK 210 REMARK: BEST 20 STRUCTURES. THESE STRUCTURES WERE DETERMINED USING REMARK 210 TRIPLE-RESONANCE NMR SPECTROSCOPY ON CA2+_SATURATED 15N, 13C- REMARK 210 CTNC(81-161) BOUND TO 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 CYS A 84 -68.88 -93.04 REMARK 500 1 LYS A 86 79.21 60.43 REMARK 500 1 SER A 89 71.00 -69.08 REMARK 500 1 LYS A 90 55.67 -109.89 REMARK 500 1 ALA A 108 64.02 63.78 REMARK 500 2 VAL A 82 135.43 -178.07 REMARK 500 2 ARG A 83 97.39 60.51 REMARK 500 3 LYS A 86 -79.19 63.79 REMARK 500 3 LYS A 90 39.75 -97.25 REMARK 500 3 THR A 124 174.29 -58.93 REMARK 500 3 THR A 127 48.50 -106.07 REMARK 500 4 MET A 85 144.72 63.04 REMARK 500 4 SER A 89 30.29 -98.92 REMARK 500 5 VAL A 82 -44.77 -161.73 REMARK 500 5 ARG A 83 -173.84 -69.08 REMARK 500 5 CYS A 84 -171.37 61.16 REMARK 500 5 MET A 85 -78.77 64.60 REMARK 500 6 ASP A 88 -167.58 -73.83 REMARK 500 6 SER A 89 50.33 -91.48 REMARK 500 6 THR A 93 -85.06 -99.95 REMARK 500 6 ALA A 108 75.33 67.73 REMARK 500 6 ASN A 144 71.87 66.81 REMARK 500 7 CYS A 84 -48.98 -149.70 REMARK 500 7 LYS A 86 78.50 -105.07 REMARK 500 7 ASP A 87 -65.65 -92.80 REMARK 500 7 ALA A 108 72.36 67.82 REMARK 500 7 THR A 127 77.55 -102.81 REMARK 500 7 VAL A 160 74.34 -102.11 REMARK 500 8 CYS A 84 -62.96 -156.06 REMARK 500 8 ASP A 87 42.08 -96.40 REMARK 500 9 VAL A 82 59.97 -171.09 REMARK 500 9 ASP A 87 -179.38 -58.91 REMARK 500 9 ALA A 108 74.90 64.27 REMARK 500 9 THR A 124 179.10 -59.84 REMARK 500 10 ARG A 83 88.58 60.10 REMARK 500 10 MET A 85 41.11 -140.15 REMARK 500 10 LYS A 86 30.28 -98.23 REMARK 500 10 ASP A 88 77.39 -101.42 REMARK 500 10 LYS A 90 39.89 -97.11 REMARK 500 10 THR A 93 -74.96 -100.72 REMARK 500 10 ASN A 144 60.22 66.11 REMARK 500 10 VAL A 160 43.38 -94.93 REMARK 500 11 VAL A 82 -53.79 -151.15 REMARK 500 11 ARG A 83 -169.11 60.60 REMARK 500 11 LYS A 86 -41.18 -172.92 REMARK 500 11 ASP A 87 36.61 -97.66 REMARK 500 11 LYS A 92 49.88 -98.04 REMARK 500 11 ALA A 108 68.29 62.86 REMARK 500 11 THR A 127 72.33 -102.99 REMARK 500 12 MET A 85 -179.01 60.29 REMARK 500 REMARK 500 THIS ENTRY HAS 82 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 CA A 162 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 105 OD1 REMARK 620 2 ASP A 105 OD2 56.5 REMARK 620 3 ASN A 107 OD1 129.7 75.3 REMARK 620 4 ASP A 109 OD1 106.2 86.9 82.8 REMARK 620 5 ASP A 109 OD2 156.2 118.0 59.1 50.3 REMARK 620 6 TYR A 111 O 69.0 118.5 159.2 82.6 100.1 REMARK 620 7 GLU A 116 OE2 129.2 116.2 58.9 124.2 74.6 119.5 REMARK 620 8 GLU A 116 OE1 117.6 149.8 96.2 121.3 79.0 78.9 40.6 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 163 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 141 OD1 REMARK 620 2 ASN A 143 N 65.0 REMARK 620 3 ASN A 143 OD1 133.5 71.0 REMARK 620 4 ASP A 145 OD1 84.2 127.3 136.9 REMARK 620 5 ARG A 147 O 83.5 145.3 131.7 58.6 REMARK 620 6 GLU A 152 OE1 76.9 100.1 97.3 113.8 56.6 REMARK 620 7 GLU A 152 OE2 129.3 140.6 78.9 92.1 53.0 58.7 REMARK 620 N 1 2 3 4 5 6 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 162 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 163 DBREF 1FI5 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 CA A 162 1 HET CA A 163 1 HETNAM CA CALCIUM ION FORMUL 2 CA 2(CA 2+) HELIX 1 E THR A 93 MET A 103 1 11 HELIX 2 F LEU A 114 ALA A 123 1 10 HELIX 3 G GLU A 130 ASP A 139 1 10 HELIX 4 H TYR A 150 LYS A 158 1 9 SHEET 1 S 2 TYR A 111 ASP A 113 0 SHEET 2 S 2 ARG A 147 ASP A 149 -1 N ILE A 148 O ILE A 112 LINK OD1 ASP A 105 CA CA A 162 1555 1555 2.43 LINK OD2 ASP A 105 CA CA A 162 1555 1555 2.20 LINK OD1 ASN A 107 CA CA A 162 1555 1555 3.13 LINK OD1 ASP A 109 CA CA A 162 1555 1555 2.01 LINK OD2 ASP A 109 CA CA A 162 1555 1555 2.84 LINK O TYR A 111 CA CA A 162 1555 1555 2.19 LINK OE2 GLU A 116 CA CA A 162 1555 1555 2.76 LINK OE1 GLU A 116 CA CA A 162 1555 1555 3.36 LINK OD1 ASP A 141 CA CA A 163 1555 1555 2.43 LINK N ASN A 143 CA CA A 163 1555 1555 2.87 LINK OD1 ASN A 143 CA CA A 163 1555 1555 3.17 LINK OD1 ASP A 145 CA CA A 163 1555 1555 1.92 LINK O ARG A 147 CA CA A 163 1555 1555 3.30 LINK OE1 GLU A 152 CA CA A 163 1555 1555 2.39 LINK OE2 GLU A 152 CA CA 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 - b 23 2 Bytes