Header list of 1npq.pdb file
Complete list - t 27 2 Bytes
HEADER STRUCTURAL PROTEIN 18-JAN-03 1NPQ TITLE STRUCTURE OF A RHODAMINE-LABELED N-DOMAIN TROPONIN C MUTANT (CA2+ TITLE 2 SATURATED) IN COMPLEX WITH SKELETAL TROPONIN I 115-131 COMPND MOL_ID: 1; COMPND 2 MOLECULE: TROPONIN C; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: TNC, RESIDUES 1-90; COMPND 5 SYNONYM: TROPONIN C, SKELETAL MUSCLE; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: TROPONIN I; COMPND 10 CHAIN: B; COMPND 11 FRAGMENT: SWITCH PEPTIDE, RESIDUES 115-131; COMPND 12 SYNONYM: TROPONIN I, FAST SKELETAL MUSCLE; TROPONIN I, FAST-TWITCH COMPND 13 ISOFORM; COMPND 14 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: TNNC2; 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: PET3A; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3ASNTNC; SOURCE 11 MOL_ID: 2; SOURCE 12 SYNTHETIC: YES; SOURCE 13 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN ORYCTOLAGUS SOURCE 14 CUNICULUS (RABIT) KEYWDS TROPONIN C- TROPONIN I COMPLEX, BIFUNCTIONAL RHODAMINE LABELED KEYWDS 2 TOPONIN C, STRUCTURAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 21 MDLTYP MINIMIZED AVERAGE AUTHOR P.MERCIER,R.E.FERGUSON,M.IRVING,J.E.T.CORRIE,D.R.TRENTHAM,B.D.SYKES REVDAT 3 27-OCT-21 1NPQ 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1NPQ 1 VERSN REVDAT 1 29-APR-03 1NPQ 0 JRNL AUTH P.MERCIER,R.E.FERGUSON,M.IRVING,J.E.T.CORRIE,D.R.TRENTHAM, JRNL AUTH 2 B.D.SYKES JRNL TITL NMR STRUCTURE OF A BIFUNCTIONAL RHODAMINE LABELED N-DOMAIN JRNL TITL 2 OF TROPONIN C COMPLEXED WITH THE REGULATORY "SWITCH" PEPTIDE JRNL TITL 3 FROM TROPONIN I: IMPLICATIONS FOR IN SITU FLUORESCENCE JRNL TITL 4 STUDIES IN MUSCLE FIBERS JRNL REF BIOCHEMISTRY V. 42 4333 2003 JRNL REFN ISSN 0006-2960 JRNL PMID 12693929 JRNL DOI 10.1021/BI027041N REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1, CNS 1.1 REMARK 3 AUTHORS : A.T.BRUNGER (CNS), A.T.BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 CALCIUM RESTRAINTS WERE INTRODUCED ONLY DURING THE 2ND COOLING REMARK 3 STAGE REMARK 3 USING CARTESIAN DYNAMICS. SEE TABLE 3 OF THE REFERENCE PAPER FOR A REMARK 3 DETAILED DESCRIPTION OF THE DISTANCE AND DIHEDRAL RESTRAINTS. REMARK 4 REMARK 4 1NPQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-03. REMARK 100 THE DEPOSITION ID IS D_1000018087. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 320 MM KCL REMARK 210 PRESSURE : AMBIANT REMARK 210 SAMPLE CONTENTS : 320 MM KCL, 10 MM IMIDAZOLE, REMARK 210 1.3% NAN3, PH 6.5, ~1MM REMARK 210 SNTNC.2CA2+.TNI115-131.BR56-63 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; REMARK 210 3D_15N/13C-NOESY; HNHA; 2D_13C/ REMARK 210 15N-EDITED-NOESY; 2D_13C/15N- REMARK 210 FILTERED/EDITED-NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA; UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE FEB 2002, NMRVIEW 5.0.4, REMARK 210 PROCHECK 3.5.4 REMARK 210 METHOD USED : SIMULATED ANNEALING USING REMARK 210 TORSION ANGLE DYNAMICS AND REMARK 210 CARTESIAN DYNAMICS WITH THE REMARK 210 PROGRAM CNS 1.1 REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: REMARK 210 THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE SPECTROSCOPY. REMARK 210 THE REMARK 210 CHEMICAL SHIFTS FOR TNI115-131 WERE OBTAINED FROM A REMARK 210 2D_15N/13C_FILTERED-DIPSI EXPERIMENT. INTRAMOLECULAR NOES FOR REMARK 210 TNI115-131 WERE OBTAINED FROM A 2D_15N/13C_FILTERED-NOESY REMARK 210 EXPERIMENT. 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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: 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 MET A 3 -47.14 -139.34 REMARK 500 1 THR A 4 117.26 -161.86 REMARK 500 1 ALA A 24 -78.05 -58.10 REMARK 500 1 PHE A 29 -70.30 -55.45 REMARK 500 1 SER A 38 -166.18 -115.01 REMARK 500 1 THR A 44 -76.97 -59.57 REMARK 500 1 MET A 48 35.63 -97.79 REMARK 500 1 LEU A 49 -47.98 -146.39 REMARK 500 1 ASN A 52 53.15 -149.70 REMARK 500 1 THR A 54 -178.52 -57.27 REMARK 500 1 ASP A 74 -169.40 -75.93 REMARK 500 1 PHE A 75 -75.78 -60.23 REMARK 500 1 MET A 86 -75.97 -63.06 REMARK 500 1 GLU A 88 103.57 -54.51 REMARK 500 1 ASP A 89 86.51 -178.04 REMARK 500 1 MET B 116 -72.31 -67.16 REMARK 500 1 ALA B 124 -73.00 -50.85 REMARK 500 1 LEU B 126 158.84 60.50 REMARK 500 1 HIS B 130 -65.72 68.31 REMARK 500 2 MET A 3 -46.15 -157.16 REMARK 500 2 ALA A 24 -73.32 -46.01 REMARK 500 2 PHE A 29 -73.87 -57.74 REMARK 500 2 ASP A 36 -177.56 52.28 REMARK 500 2 SER A 38 -163.00 -102.02 REMARK 500 2 THR A 44 -78.67 -58.83 REMARK 500 2 ASN A 52 48.78 -144.21 REMARK 500 2 ASP A 74 -174.00 -66.91 REMARK 500 2 PHE A 75 -78.15 -59.89 REMARK 500 2 ASP A 89 -175.71 60.37 REMARK 500 2 MET B 116 -65.06 -101.87 REMARK 500 2 ALA B 124 -75.02 -78.51 REMARK 500 2 LEU B 126 170.45 56.68 REMARK 500 2 HIS B 130 -67.44 -163.71 REMARK 500 3 SER A 2 175.79 60.32 REMARK 500 3 MET A 3 -39.95 -176.99 REMARK 500 3 ALA A 24 -74.27 -47.54 REMARK 500 3 PHE A 29 -75.05 -58.71 REMARK 500 3 ASP A 36 -175.21 55.82 REMARK 500 3 SER A 38 -164.13 -106.78 REMARK 500 3 THR A 44 -75.95 -59.29 REMARK 500 3 ASN A 52 51.08 -144.24 REMARK 500 3 THR A 54 -178.31 -56.36 REMARK 500 3 ASP A 66 97.50 -68.91 REMARK 500 3 ASP A 74 -168.86 -71.47 REMARK 500 3 PHE A 75 -73.59 -61.12 REMARK 500 3 MET B 116 -76.89 63.88 REMARK 500 3 LEU B 126 159.73 59.64 REMARK 500 4 MET A 3 -50.76 -125.91 REMARK 500 4 THR A 4 109.70 -177.19 REMARK 500 4 ALA A 24 -77.22 -44.70 REMARK 500 REMARK 500 THIS ENTRY HAS 295 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 133 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 30 OD1 REMARK 620 2 ALA A 31 N 108.8 REMARK 620 3 ASP A 32 OD1 121.1 81.7 REMARK 620 4 ASP A 36 O 86.1 148.0 115.4 REMARK 620 5 GLU A 41 OE1 89.0 79.4 148.4 72.5 REMARK 620 6 GLU A 41 OE2 132.6 88.6 104.5 61.7 50.1 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 132 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 66 OD2 REMARK 620 2 ASP A 68 OD1 96.8 REMARK 620 3 SER A 70 OG 62.3 62.4 REMARK 620 4 THR A 72 O 55.2 151.8 96.9 REMARK 620 5 GLU A 77 OE1 113.9 139.5 155.7 65.7 REMARK 620 6 GLU A 77 OE2 128.0 96.0 158.2 104.4 44.4 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 132 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 133 DBREF 1NPQ A 1 90 UNP P02588 TNNC2_CHICK 1 90 DBREF 1NPQ B 115 131 UNP P02643 TNNI2_RABIT 115 131 SEQADV 1NPQ CYS A 56 UNP P02588 GLU 56 ENGINEERED MUTATION SEQADV 1NPQ CYS A 63 UNP P02588 GLU 63 ENGINEERED MUTATION 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 CYS GLU LEU ASP ALA ILE ILE CYS 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 SEQRES 1 B 17 ARG MET SER ALA ASP ALA MET LEU ARG ALA LEU LEU GLY SEQRES 2 B 17 SER LYS HIS LYS HET CA A 132 1 HET CA A 133 1 HETNAM CA CALCIUM ION FORMUL 3 CA 2(CA 2+) HELIX 1 1 ASP A 5 LEU A 14 1 10 HELIX 2 2 SER A 15 LYS A 23 1 9 HELIX 3 3 ALA A 25 ASP A 30 1 6 HELIX 4 4 SER A 38 MET A 48 1 11 HELIX 5 5 THR A 54 ASP A 66 1 13 HELIX 6 6 GLU A 76 LYS A 87 1 12 HELIX 7 7 ALA B 118 LEU B 126 1 9 LINK OD1 ASP A 30 CA CA A 133 1555 1555 2.58 LINK N ALA A 31 CA CA A 133 1555 1555 3.18 LINK OD1 ASP A 32 CA CA A 133 1555 1555 2.82 LINK O ASP A 36 CA CA A 133 1555 1555 2.78 LINK OE1 GLU A 41 CA CA A 133 1555 1555 2.83 LINK OE2 GLU A 41 CA CA A 133 1555 1555 2.16 LINK OD2 ASP A 66 CA CA A 132 1555 1555 2.50 LINK OD1 ASP A 68 CA CA A 132 1555 1555 2.95 LINK OG SER A 70 CA CA A 132 1555 1555 2.98 LINK O THR A 72 CA CA A 132 1555 1555 2.87 LINK OE1 GLU A 77 CA CA A 132 1555 1555 2.97 LINK OE2 GLU A 77 CA CA A 132 1555 1555 2.84 SITE 1 AC1 5 ASP A 66 ASP A 68 SER A 70 THR A 72 SITE 2 AC1 5 GLU A 77 SITE 1 AC2 5 ASP A 30 ALA A 31 ASP A 32 ASP A 36 SITE 2 AC2 5 GLU A 41 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 - t 27 2 Bytes