Header list of 1smg.pdb file
Complete list - v 3 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 04-FEB-97 1SMG
TITLE CALCIUM-BOUND E41A MUTANT OF THE N-DOMAIN OF CHICKEN TROPONIN C, NMR,
TITLE 2 40 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPONIN C;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-DOMAIN;
COMPND 5 SYNONYM: TNC;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: 2 CALCIUM IONS BOUND IN SOLUTION
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 ORGAN: SKELETAL;
SOURCE 7 TISSUE: MUSCLE;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYS S;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PET3A;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: BL21
KEYWDS CALCIUM-BINDING PROTEIN, MUSCLE PROTEIN, TROPONIN C
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR S.M.GAGNE,M.X.LI,B.D.SYKES
REVDAT 3 03-NOV-21 1SMG 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1SMG 1 VERSN
REVDAT 1 12-AUG-97 1SMG 0
JRNL AUTH S.M.GAGNE,M.X.LI,B.D.SYKES
JRNL TITL MECHANISM OF DIRECT COUPLING BETWEEN BINDING AND INDUCED
JRNL TITL 2 STRUCTURAL CHANGE IN REGULATORY CALCIUM BINDING PROTEINS.
JRNL REF BIOCHEMISTRY V. 36 4386 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9109645
JRNL DOI 10.1021/BI963076+
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
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 1SMG 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_1000176430.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303.15
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-HSQC; 13C-CT-HSQC; HNCACB;
REMARK 210 CBCA(CO)NNH; 15N-EDITED-NOESY;
REMARK 210 13C-EDITED-NOESY; 2D-NOESY; 15N-
REMARK 210 EDITED TOCSY; HCCHTOCSY; 2D-COSY;
REMARK 210 HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY-600
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : SA.INP
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TOTAL ENERGY
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: 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 91.06 -160.87
REMARK 500 1 MET A 46 -72.93 -59.46
REMARK 500 1 ASP A 89 52.03 -146.85
REMARK 500 2 PHE A 29 43.43 -103.75
REMARK 500 2 ASP A 30 53.21 -114.71
REMARK 500 2 MET A 82 -74.02 -55.39
REMARK 500 2 LYS A 87 -93.55 -51.97
REMARK 500 2 GLU A 88 135.40 -179.38
REMARK 500 3 LYS A 87 -81.37 -47.09
REMARK 500 3 GLU A 88 49.45 169.16
REMARK 500 3 ASP A 89 77.31 46.27
REMARK 500 4 SER A 2 -164.56 175.04
REMARK 500 4 PHE A 26 -71.45 -59.09
REMARK 500 4 ASP A 30 46.85 -104.67
REMARK 500 4 ASP A 89 93.62 46.22
REMARK 500 5 SER A 2 -88.88 -136.53
REMARK 500 5 MET A 46 -72.00 -62.46
REMARK 500 5 MET A 48 -76.52 -61.56
REMARK 500 5 LEU A 49 -71.01 -43.99
REMARK 500 5 MET A 82 -71.22 -63.83
REMARK 500 5 LYS A 87 -74.23 -43.62
REMARK 500 6 SER A 2 -43.95 -174.90
REMARK 500 6 MET A 3 33.74 -154.50
REMARK 500 6 THR A 4 143.35 59.32
REMARK 500 6 ASP A 30 43.81 -87.66
REMARK 500 6 GLN A 85 19.03 -147.67
REMARK 500 7 SER A 2 -163.59 46.59
REMARK 500 7 PHE A 26 -71.79 -59.07
REMARK 500 7 ASP A 89 56.03 -104.91
REMARK 500 8 SER A 2 172.32 177.17
REMARK 500 8 THR A 4 155.66 -47.51
REMARK 500 8 ALA A 8 -72.17 -71.01
REMARK 500 8 ASN A 52 63.48 -151.56
REMARK 500 8 PRO A 53 -169.91 -78.53
REMARK 500 8 MET A 82 -74.70 -65.60
REMARK 500 8 LYS A 87 -68.60 -96.00
REMARK 500 9 PHE A 26 -71.33 -50.71
REMARK 500 9 GLN A 51 130.80 175.58
REMARK 500 9 MET A 82 -75.17 -58.09
REMARK 500 9 LYS A 87 55.86 -95.32
REMARK 500 9 GLU A 88 -148.80 45.86
REMARK 500 9 ASP A 89 44.24 -155.14
REMARK 500 10 THR A 4 156.39 -48.41
REMARK 500 10 MET A 86 -81.84 -43.87
REMARK 500 10 GLU A 88 -156.38 53.62
REMARK 500 11 SER A 2 -159.32 -69.34
REMARK 500 11 MET A 3 81.10 -174.57
REMARK 500 11 ASP A 30 73.86 -112.35
REMARK 500 11 ALA A 31 -75.83 -48.00
REMARK 500 11 ASP A 32 -91.87 -90.19
REMARK 500
REMARK 500 THIS ENTRY HAS 183 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 0.31 SIDE CHAIN
REMARK 500 1 ARG A 84 0.15 SIDE CHAIN
REMARK 500 2 ARG A 11 0.30 SIDE CHAIN
REMARK 500 2 ARG A 47 0.28 SIDE CHAIN
REMARK 500 2 ARG A 84 0.27 SIDE CHAIN
REMARK 500 3 ARG A 47 0.32 SIDE CHAIN
REMARK 500 3 ARG A 84 0.19 SIDE CHAIN
REMARK 500 4 ARG A 11 0.29 SIDE CHAIN
REMARK 500 4 ARG A 47 0.32 SIDE CHAIN
REMARK 500 4 ARG A 84 0.26 SIDE CHAIN
REMARK 500 5 ARG A 11 0.26 SIDE CHAIN
REMARK 500 5 ARG A 47 0.27 SIDE CHAIN
REMARK 500 5 ARG A 84 0.32 SIDE CHAIN
REMARK 500 6 ARG A 11 0.32 SIDE CHAIN
REMARK 500 6 ARG A 47 0.29 SIDE CHAIN
REMARK 500 6 ARG A 84 0.30 SIDE CHAIN
REMARK 500 7 ARG A 11 0.24 SIDE CHAIN
REMARK 500 7 ARG A 47 0.28 SIDE CHAIN
REMARK 500 7 ARG A 84 0.24 SIDE CHAIN
REMARK 500 8 ARG A 11 0.26 SIDE CHAIN
REMARK 500 8 ARG A 47 0.26 SIDE CHAIN
REMARK 500 8 ARG A 84 0.31 SIDE CHAIN
REMARK 500 9 ARG A 11 0.23 SIDE CHAIN
REMARK 500 9 ARG A 47 0.14 SIDE CHAIN
REMARK 500 9 ARG A 84 0.32 SIDE CHAIN
REMARK 500 10 ARG A 11 0.32 SIDE CHAIN
REMARK 500 10 ARG A 47 0.21 SIDE CHAIN
REMARK 500 10 ARG A 84 0.31 SIDE CHAIN
REMARK 500 11 ARG A 11 0.32 SIDE CHAIN
REMARK 500 11 ARG A 47 0.29 SIDE CHAIN
REMARK 500 11 ARG A 84 0.31 SIDE CHAIN
REMARK 500 12 ARG A 11 0.28 SIDE CHAIN
REMARK 500 12 ARG A 47 0.16 SIDE CHAIN
REMARK 500 12 ARG A 84 0.29 SIDE CHAIN
REMARK 500 13 ARG A 11 0.30 SIDE CHAIN
REMARK 500 13 ARG A 47 0.27 SIDE CHAIN
REMARK 500 13 ARG A 84 0.29 SIDE CHAIN
REMARK 500 14 ARG A 11 0.26 SIDE CHAIN
REMARK 500 14 ARG A 47 0.27 SIDE CHAIN
REMARK 500 14 ARG A 84 0.20 SIDE CHAIN
REMARK 500 15 ARG A 11 0.32 SIDE CHAIN
REMARK 500 15 ARG A 47 0.32 SIDE CHAIN
REMARK 500 16 ARG A 11 0.32 SIDE CHAIN
REMARK 500 16 ARG A 47 0.19 SIDE CHAIN
REMARK 500 16 ARG A 84 0.31 SIDE CHAIN
REMARK 500 17 ARG A 11 0.32 SIDE CHAIN
REMARK 500 17 ARG A 47 0.27 SIDE CHAIN
REMARK 500 17 ARG A 84 0.29 SIDE CHAIN
REMARK 500 18 ARG A 11 0.23 SIDE CHAIN
REMARK 500 18 ARG A 47 0.28 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 114 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 91 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 66 OD1
REMARK 620 2 ASP A 68 OD1 87.5
REMARK 620 3 ASP A 68 OD2 90.1 41.9
REMARK 620 4 SER A 70 OG 99.7 108.3 66.6
REMARK 620 5 THR A 72 O 83.4 168.7 144.5 80.1
REMARK 620 6 GLU A 77 OE1 73.9 89.8 130.3 160.8 81.2
REMARK 620 7 GLU A 77 OE2 111.0 58.9 96.5 145.1 118.5 50.8
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 91
DBREF 1SMG A 1 90 UNP P02588 TNNC2_CHICK 1 90
SEQADV 1SMG ALA A 41 UNP P02588 GLU 41 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 ALA 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
HET CA A 91 1
HETNAM CA CALCIUM ION
FORMUL 2 CA CA 2+
HELIX 1 N ASP A 5 PHE A 13 1 9
HELIX 2 A GLU A 16 MET A 28 1 13
HELIX 3 B LEU A 42 LEU A 49 1 8
HELIX 4 C LYS A 55 GLU A 64 1 10
HELIX 5 D PHE A 75 ARG A 84 1 10
SHEET 1 S1 2 ASP A 36 SER A 38 0
SHEET 2 S1 2 THR A 72 ASP A 74 -1
LINK OD1 ASP A 66 CA CA A 91 1555 1555 2.39
LINK OD1 ASP A 68 CA CA A 91 1555 1555 3.22
LINK OD2 ASP A 68 CA CA A 91 1555 1555 2.57
LINK OG SER A 70 CA CA A 91 1555 1555 2.76
LINK O THR A 72 CA CA A 91 1555 1555 2.40
LINK OE1 GLU A 77 CA CA A 91 1555 1555 2.73
LINK OE2 GLU A 77 CA CA A 91 1555 1555 2.14
SITE 1 AC1 5 ASP A 66 ASP A 68 SER A 70 THR A 72
SITE 2 AC1 5 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 - v 3 2 Bytes