Header list of 1aq5.pdb file
Complete list - n 13 2 Bytes
HEADER COILED-COIL 07-AUG-97 1AQ5
TITLE HIGH-RESOLUTION SOLUTION NMR STRUCTURE OF THE TRIMERIC COILED-COIL
TITLE 2 DOMAIN OF CHICKEN CARTILAGE MATRIX PROTEIN, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARTILAGE MATRIX PROTEIN;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: CMPCC, COILED-COIL OLIGOMERIZATION DOMAIN, RESIDUES 451 -
COMPND 5 493;
COMPND 6 SYNONYM: MATRILIN-1, CMP;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: INTERCHAIN DISULFIDE BONDS
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 TISSUE: CARTILAGE MATRIX;
SOURCE 7 GENE: CMP;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: BL21
KEYWDS COILED-COIL, HEPTAD REPEAT, INTERCHAIN DISULFIDE BONDS,
KEYWDS 2 OLIGOMERIZATION DOMAIN, TRIMER, CARTILAGE MATRIX PROTEIN, MATRILIN-
KEYWDS 3 1, NONCOLLAGENOUS EXTRACELLULAR PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.A.DAMES,R.WILTSCHECK,R.A.KAMMERER,J.ENGEL,A.T.ALEXANDRESCU
REVDAT 4 13-JAN-21 1AQ5 1 COMPND
REVDAT 3 03-NOV-10 1AQ5 1 JRNL REMARK
REVDAT 2 24-FEB-09 1AQ5 1 VERSN
REVDAT 1 11-FEB-98 1AQ5 0
JRNL AUTH S.A.DAMES,R.A.KAMMERER,R.WILTSCHECK,J.ENGEL,A.T.ALEXANDRESCU
JRNL TITL NMR STRUCTURE OF A PARALLEL HOMOTRIMERIC COILED COIL.
JRNL REF NAT.STRUCT.BIOL. V. 5 687 1998
JRNL REFN ISSN 1072-8368
JRNL PMID 9699631
JRNL DOI 10.1038/1382
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.WILTSCHECK,R.A.KAMMERER,S.A.DAMES,T.SCHULTHESS,
REMARK 1 AUTH 2 M.J.BLOMMERS,J.ENGEL,A.T.ALEXANDRESCU
REMARK 1 TITL HETERONUCLEAR NMR ASSIGNMENTS AND SECONDARY STRUCTURE OF THE
REMARK 1 TITL 2 COILED COIL TRIMERIZATION DOMAIN FROM CARTILAGE MATRIX
REMARK 1 TITL 3 PROTEIN IN OXIDIZED AND REDUCED FORMS.
REMARK 1 REF PROTEIN SCI. V. 6 1734 1997
REMARK 1 REFN ISSN 0961-8368
REMARK 1 PMID 9260286
REMARK 1 DOI 10.1002/PRO.5560060814
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: ALL STRUCTURE CALCULATIONS WERE
REMARK 3 PERFORMED USING X-PLOR VERSION 3.1. FIRST 60 MONOMER STRUCTURES
REMARK 3 WERE CALCULATED FROM INTRACHAIN DISTANCE RESTRAINTS, TOGETHER
REMARK 3 WITH THE DIHEDRAL ANGLE RESTRAINTS FOR PHI AND CHI1 AND THE
REMARK 3 HYDROGEN BOND RESTRAINTS, USING THE HYBRID DISTANCE GEOMETRY-
REMARK 3 DYNAMICAL SIMULATED ANNEALING METHOD (NILGES, M.; CLORE, G.M.;
REMARK 3 GRONENBORN, A.M. (1988); FEBS LETT. 229, 317-324). THE 30 BEST
REMARK 3 MONOMER STRUCTURES WERE USED AS INPUT FOR THE GENERATION OF
REMARK 3 TRIMER STARTING STRUCTURES. EACH SELECTED HELIX MONOMER WAS
REMARK 3 FIRST ORIENTED SUCH THAT ITS GEOMETRIC CENTER COINCIDED WITH THE
REMARK 3 ORIGIN AND ITS LONG AXIS LAY ALONG THE X-AXIS AND SECOND
REMARK 3 TRANSLATED BY 10 ANGSTROMS ALONG THE Y-AXIS. COORDINATES FOR THE
REMARK 3 SECOND AND THIRD SUBUNIT WERE GENERATED BY A ROTATION AROUND THE
REMARK 3 X-AXIS BY 120 OR 240 DEGREES, RESPECTIVELY. THE 30 GENERATED
REMARK 3 TRIMER STARTING STRUCTURES WERE USED AS INPUT FOR A SECOND RUN
REMARK 3 OF SIMULATED ANNEALING INCLUDING THE INTERCHAIN DISTANCE
REMARK 3 RESTRAINTS. IN THE RESULTING STRUCTURES THE INTERCHAIN DISULFIDE
REMARK 3 BONDS WERE INTRODUCED AND A FINAL RUN OF SIMULATED ANNEALING AND
REMARK 3 REFINEMENT PERFORMED. THE LAST STEPS OF REFINEMENT INCLUDED
REMARK 3 ADDITIONALLY NON-CRYSTALLOGRAPHIC SYMMETRY (NCS) CONSTRAINTS AND
REMARK 3 R^(-6)-SUM AVERAGED DISTANCE RESTRAINTS FOR AMBIGUOUS NOES
REMARK 3 (NILGES, M. (1993); PROTEINS 17, 297-309).
REMARK 4
REMARK 4 1AQ5 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_1000171120.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 323
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 2D 1H-15N
REMARK 210 HSQC; 2D 1H-13C HSQC; 3D 1H-15N
REMARK 210 NOESY-HSQC; 3D 1H-15N TOCSY-HSQC;
REMARK 210 3D HCCH-TOCSY; 3D HNCA; 3D HNHA;
REMARK 210 3D HNHB; 2D VERSION OF A 4D 13C/
REMARK 210 15N HMQC-NOESY-HMQC; 3D 13C F1-
REMARK 210 EDITED; F3-FILTERED HMQC-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY/ SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY AND LEAST
REMARK 210 RESTRAINT VIOLATIONS
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 GLU A 5 -42.31 -158.48
REMARK 500 1 ASP A 7 93.35 50.73
REMARK 500 1 GLU B 5 -41.77 -157.19
REMARK 500 1 ASP B 7 91.88 49.97
REMARK 500 1 GLU C 5 -40.95 -156.26
REMARK 500 1 ASP C 7 93.01 52.71
REMARK 500 2 GLU A 5 -167.62 -126.22
REMARK 500 2 GLU A 6 99.13 -175.56
REMARK 500 2 ASP A 7 105.02 -42.81
REMARK 500 2 GLU A 10 43.15 40.00
REMARK 500 2 GLU B 6 99.94 -174.05
REMARK 500 2 ASP B 7 105.40 -43.00
REMARK 500 2 GLU B 10 41.99 39.90
REMARK 500 2 SER C 2 90.60 -68.99
REMARK 500 2 GLU C 6 99.15 -173.40
REMARK 500 2 ASP C 7 105.68 -43.11
REMARK 500 2 GLU C 10 43.44 39.40
REMARK 500 3 HIS A 3 -65.37 -107.23
REMARK 500 3 GLU A 5 66.24 60.30
REMARK 500 3 GLU A 6 178.20 56.33
REMARK 500 3 ASP A 7 107.82 -44.15
REMARK 500 3 HIS B 3 -68.56 -103.09
REMARK 500 3 GLU B 6 177.86 56.36
REMARK 500 3 ASP B 7 108.50 -44.04
REMARK 500 3 GLU B 10 52.60 39.54
REMARK 500 3 HIS C 3 -67.61 -102.91
REMARK 500 3 GLU C 6 177.35 53.71
REMARK 500 3 ASP C 7 107.77 -42.56
REMARK 500 3 GLU C 10 51.51 37.92
REMARK 500 4 MET A 4 -89.60 53.84
REMARK 500 4 GLU A 5 142.43 63.39
REMARK 500 4 MET B 4 -90.48 53.62
REMARK 500 4 GLU B 5 137.72 63.19
REMARK 500 4 GLU B 10 48.13 39.14
REMARK 500 4 MET C 4 -91.33 54.43
REMARK 500 4 GLU C 5 139.90 64.38
REMARK 500 4 GLU C 10 45.77 39.38
REMARK 500 5 SER A 2 -66.17 -149.19
REMARK 500 5 MET A 4 81.84 55.59
REMARK 500 5 ASP A 7 112.84 -179.18
REMARK 500 5 CYS A 9 43.59 -107.92
REMARK 500 5 SER B 2 -68.44 -150.14
REMARK 500 5 MET B 4 82.34 56.36
REMARK 500 5 ASP B 7 112.97 179.89
REMARK 500 5 CYS B 9 44.15 -106.97
REMARK 500 5 SER C 2 -63.30 -148.47
REMARK 500 5 MET C 4 82.89 55.98
REMARK 500 5 ASP C 7 113.82 -179.62
REMARK 500 5 CYS C 9 45.88 -106.81
REMARK 500 6 SER A 2 -61.65 -142.65
REMARK 500
REMARK 500 THIS ENTRY HAS 184 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 2 ARG A 38 0.20 SIDE CHAIN
REMARK 500 2 ARG B 38 0.22 SIDE CHAIN
REMARK 500 2 ARG C 38 0.20 SIDE CHAIN
REMARK 500 3 ARG A 38 0.27 SIDE CHAIN
REMARK 500 3 ARG B 38 0.27 SIDE CHAIN
REMARK 500 3 ARG C 38 0.27 SIDE CHAIN
REMARK 500 4 ARG A 38 0.28 SIDE CHAIN
REMARK 500 4 ARG B 38 0.27 SIDE CHAIN
REMARK 500 4 ARG C 38 0.28 SIDE CHAIN
REMARK 500 6 ARG A 38 0.28 SIDE CHAIN
REMARK 500 6 ARG B 38 0.27 SIDE CHAIN
REMARK 500 6 ARG C 38 0.28 SIDE CHAIN
REMARK 500 7 ARG A 38 0.29 SIDE CHAIN
REMARK 500 7 ARG B 38 0.28 SIDE CHAIN
REMARK 500 7 ARG C 38 0.29 SIDE CHAIN
REMARK 500 8 ARG A 38 0.24 SIDE CHAIN
REMARK 500 8 ARG B 38 0.25 SIDE CHAIN
REMARK 500 8 ARG C 38 0.24 SIDE CHAIN
REMARK 500 9 ARG A 38 0.28 SIDE CHAIN
REMARK 500 9 ARG B 38 0.28 SIDE CHAIN
REMARK 500 9 ARG C 38 0.28 SIDE CHAIN
REMARK 500 10 ARG A 38 0.30 SIDE CHAIN
REMARK 500 10 ARG B 38 0.30 SIDE CHAIN
REMARK 500 10 ARG C 38 0.30 SIDE CHAIN
REMARK 500 11 ARG A 38 0.25 SIDE CHAIN
REMARK 500 11 ARG B 38 0.27 SIDE CHAIN
REMARK 500 11 ARG C 38 0.26 SIDE CHAIN
REMARK 500 12 ARG A 38 0.32 SIDE CHAIN
REMARK 500 12 ARG B 38 0.32 SIDE CHAIN
REMARK 500 12 ARG C 38 0.32 SIDE CHAIN
REMARK 500 13 ARG A 38 0.13 SIDE CHAIN
REMARK 500 13 ARG B 38 0.12 SIDE CHAIN
REMARK 500 13 ARG C 38 0.14 SIDE CHAIN
REMARK 500 14 ARG A 38 0.10 SIDE CHAIN
REMARK 500 14 ARG B 38 0.08 SIDE CHAIN
REMARK 500 14 ARG C 38 0.10 SIDE CHAIN
REMARK 500 15 ARG A 38 0.22 SIDE CHAIN
REMARK 500 15 ARG B 38 0.23 SIDE CHAIN
REMARK 500 15 ARG C 38 0.22 SIDE CHAIN
REMARK 500 16 ARG A 38 0.23 SIDE CHAIN
REMARK 500 16 ARG B 38 0.26 SIDE CHAIN
REMARK 500 16 ARG C 38 0.23 SIDE CHAIN
REMARK 500 17 ARG A 38 0.14 SIDE CHAIN
REMARK 500 17 ARG B 38 0.12 SIDE CHAIN
REMARK 500 17 ARG C 38 0.14 SIDE CHAIN
REMARK 500 18 ARG A 38 0.20 SIDE CHAIN
REMARK 500 18 ARG B 38 0.19 SIDE CHAIN
REMARK 500 18 ARG C 38 0.19 SIDE CHAIN
REMARK 500 19 ARG A 38 0.31 SIDE CHAIN
REMARK 500 19 ARG B 38 0.31 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 54 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AQ5 A 5 47 UNP P05099 MATN1_CHICK 451 493
DBREF 1AQ5 B 5 47 UNP P05099 MATN1_CHICK 451 493
DBREF 1AQ5 C 5 47 UNP P05099 MATN1_CHICK 451 493
SEQRES 1 A 47 GLY SER HIS MET GLU GLU ASP PRO CYS GLU CYS LYS SER
SEQRES 2 A 47 ILE VAL LYS PHE GLN THR LYS VAL GLU GLU LEU ILE ASN
SEQRES 3 A 47 THR LEU GLN GLN LYS LEU GLU ALA VAL ALA LYS ARG ILE
SEQRES 4 A 47 GLU ALA LEU GLU ASN LYS ILE ILE
SEQRES 1 B 47 GLY SER HIS MET GLU GLU ASP PRO CYS GLU CYS LYS SER
SEQRES 2 B 47 ILE VAL LYS PHE GLN THR LYS VAL GLU GLU LEU ILE ASN
SEQRES 3 B 47 THR LEU GLN GLN LYS LEU GLU ALA VAL ALA LYS ARG ILE
SEQRES 4 B 47 GLU ALA LEU GLU ASN LYS ILE ILE
SEQRES 1 C 47 GLY SER HIS MET GLU GLU ASP PRO CYS GLU CYS LYS SER
SEQRES 2 C 47 ILE VAL LYS PHE GLN THR LYS VAL GLU GLU LEU ILE ASN
SEQRES 3 C 47 THR LEU GLN GLN LYS LEU GLU ALA VAL ALA LYS ARG ILE
SEQRES 4 C 47 GLU ALA LEU GLU ASN LYS ILE ILE
HELIX 1 1 SER A 13 GLU A 43 1 31
HELIX 2 2 SER B 13 GLU B 43 1 31
HELIX 3 3 SER C 13 GLU C 43 1 31
SSBOND 1 CYS A 9 CYS C 11 1555 1555 2.02
SSBOND 2 CYS A 11 CYS B 9 1555 1555 2.02
SSBOND 3 CYS B 11 CYS C 9 1555 1555 2.02
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 - n 13 2 Bytes