Header list of 1ihq.pdb file
Complete list - b 23 2 Bytes
HEADER DE NOVO PROTEIN 19-APR-01 1IHQ
TITLE GLYTM1BZIP: A CHIMERIC PEPTIDE MODEL OF THE N-TERMINUS OF A RAT SHORT
TITLE 2 ALPHA TROPOMYOSIN WITH THE N-TERMINUS ENCODED BY EXON 1B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHIMERIC PEPTIDE GLYTM1BZIP: TROPOMYOSIN ALPHA CHAIN,
COMPND 3 BRAIN-3 AND GENERAL CONTROL PROTEIN GCN4;
COMPND 4 CHAIN: A, B;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: THE CHIMERA CONSISTS OF AN INITIAL GLY, RESIDUES 2-20
COMPND 7 OF TROPOMYOSIN ALPHA CHAIN, BRAIN-3 AND RESIDUES 21-38 OF GENERAL
COMPND 8 CONTROL PROTEIN GCN4.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS, SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT, BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 10116,4932;
SOURCE 5 STRAIN: ,;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPROEX HTA
KEYWDS TROPOMYOSIN, EXON 1B, ACTIN-BINDING, THIN-FILAMENT-REGULATION, NON-
KEYWDS 2 MUSCLE, ALPHA-HELIX, COILED-COIL, DIMER, GCN4, CHIMERIC-PEPTIDE-
KEYWDS 3 MODEL, TW0-CHAINED, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE
KEYWDS 4 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, DE NOVO
KEYWDS 5 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR N.J.GREENFIELD,Y.J.YUANG,T.PALM,G.V.SWAPNA,D.MONLEON,G.T.MONTELIONE,
AUTHOR 2 S.E.HITCHCOCK-DEGREGORI,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 3 (NESG)
REVDAT 5 23-FEB-22 1IHQ 1 REMARK
REVDAT 4 24-FEB-09 1IHQ 1 VERSN
REVDAT 3 25-JAN-05 1IHQ 1 JRNL AUTHOR KEYWDS REMARK
REVDAT 2 21-NOV-01 1IHQ 1 DBREF
REVDAT 1 03-OCT-01 1IHQ 0
JRNL AUTH N.J.GREENFIELD,Y.J.HUANG,T.PALM,G.V.SWAPNA,D.MONLEON,
JRNL AUTH 2 G.T.MONTELIONE,S.E.HITCHCOCK-DEGREGORI
JRNL TITL SOLUTION NMR STRUCTURE AND FOLDING DYNAMICS OF THE N
JRNL TITL 2 TERMINUS OF A RAT NON-MUSCLE ALPHA-TROPOMYOSIN IN AN
JRNL TITL 3 ENGINEERED CHIMERIC PROTEIN.
JRNL REF J.MOL.BIOL. V. 312 833 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11575936
JRNL DOI 10.1006/JMBI.2001.4982
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : GUNTERT,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JOURNAL CITATION ABOVE.
REMARK 4
REMARK 4 1IHQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013278.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 281
REMARK 210 PH : 6.4
REMARK 210 IONIC STRENGTH : 0.12 N
REMARK 210 PRESSURE : ATMOSPHERIC ATM
REMARK 210 SAMPLE CONTENTS : 1-2 MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TRIPLE RESONANCE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA 500
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 5.3B, DYANA 1.5, AUTOASSIGN
REMARK 210 1.5, AUTOSTRUCTURE 1.0, SPARKY
REMARK 210 3.74
REMARK 210 METHOD USED : 1156 CONFORMATIONALLY
REMARK 210 -RESTRICTING NOE CONSTRAINTS
REMARK 210 (OUT OF A TOTAL OF 1746 NOE
REMARK 210 DERIVED DISTANCES) 112 LOOSE
REMARK 210 DIHEDRAL ANGLE CONSTRAINTS AND
REMARK 210 FORTY-EIGHT BACKBONE INTRA-
REMARK 210 HELICAL HYDROGEN BOND
REMARK 210 CONSTRAINTS WERE UTILILIZED.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS,TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURE WAS DETERMINE USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
REMARK 210 INTER-CHAIN INTERACTIONS WERE DETERMINED USING X-FILTERED NOESY
REMARK 210 EXPERIMENTS
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: 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 O LEU A 31 H VAL A 35 1.44
REMARK 500 O LEU B 17 HD21 ASN B 21 1.48
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 ALA A 2 168.26 56.86
REMARK 500 1 SER A 4 73.61 85.80
REMARK 500 1 SER A 5 108.24 179.09
REMARK 500 1 GLU A 37 -168.53 -71.21
REMARK 500 1 ALA B 2 58.36 -100.33
REMARK 500 1 SER B 4 136.16 79.35
REMARK 500 1 SER B 5 37.21 -145.02
REMARK 500 1 SER B 6 104.33 54.25
REMARK 500 1 VAL B 35 -81.91 -80.03
REMARK 500 1 GLU B 37 -166.95 -65.99
REMARK 500 2 ALA A 2 -75.87 -152.57
REMARK 500 2 SER A 4 81.02 73.23
REMARK 500 2 SER A 5 122.83 74.94
REMARK 500 2 SER A 6 110.42 172.16
REMARK 500 2 GLU A 37 -173.93 -61.04
REMARK 500 2 ALA B 2 156.43 -44.32
REMARK 500 2 SER B 4 -73.60 -145.44
REMARK 500 2 SER B 5 -94.66 -142.94
REMARK 500 2 LEU B 7 -35.10 -39.39
REMARK 500 2 GLU B 37 -163.30 -71.08
REMARK 500 3 ALA A 2 -177.61 -178.71
REMARK 500 3 SER A 4 143.50 172.81
REMARK 500 3 SER A 5 -100.03 -53.49
REMARK 500 3 SER A 6 121.91 66.56
REMARK 500 3 GLU A 37 -168.31 -55.94
REMARK 500 3 ALA B 2 170.93 63.49
REMARK 500 3 SER B 4 -176.49 54.45
REMARK 500 3 VAL B 35 -73.79 -48.29
REMARK 500 4 SER A 5 -61.52 -144.33
REMARK 500 4 SER A 6 138.53 84.58
REMARK 500 4 ALA B 2 161.35 58.63
REMARK 500 4 SER B 5 110.25 67.04
REMARK 500 4 SER B 6 105.57 -170.35
REMARK 500 4 GLU B 37 -167.84 -127.42
REMARK 500 5 SER A 6 117.62 172.44
REMARK 500 5 GLU A 37 -169.81 -78.54
REMARK 500 5 SER B 4 172.12 -46.56
REMARK 500 5 SER B 5 -76.54 -131.17
REMARK 500 5 SER B 6 114.49 77.51
REMARK 500 5 VAL B 35 -80.76 -78.73
REMARK 500 5 GLU B 37 -169.04 -66.71
REMARK 500 6 ALA A 2 175.38 -54.94
REMARK 500 6 SER A 4 173.46 72.67
REMARK 500 6 SER A 5 -106.10 -89.77
REMARK 500 6 SER A 6 114.23 163.53
REMARK 500 6 LEU A 31 -71.48 -64.66
REMARK 500 6 GLU A 37 -152.87 39.13
REMARK 500 6 ALA B 2 98.12 177.81
REMARK 500 6 SER B 4 -82.84 64.01
REMARK 500 6 SER B 5 -74.40 -162.45
REMARK 500
REMARK 500 THIS ENTRY HAS 82 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TMZ RELATED DB: PDB
REMARK 900 A CHIMERIC PEPTIDE MODEL OF THE N-TERMINUS OF A RAT LONG ALPHA
REMARK 900 TROPOMYOSIN WITH THE N-TERMINUS ENCODED BY EXON 1A
REMARK 900 RELATED ID: OR1 RELATED DB: TARGETDB
DBREF 1IHQ A 2 20 UNP P18344 TPMZ_RAT 2 20
DBREF 1IHQ B 2 20 UNP P18344 TPMZ_RAT 2 20
DBREF 1IHQ A 21 38 UNP P03069 GCN4_YEAST 264 281
DBREF 1IHQ B 21 38 UNP P03069 GCN4_YEAST 264 281
SEQADV 1IHQ GLY A 1 UNP P18344 SEE REMARK 999
SEQADV 1IHQ GLY B 1 UNP P18344 SEE REMARK 999
SEQRES 1 A 38 GLY ALA GLY SER SER SER LEU GLU ALA VAL ARG ARG LYS
SEQRES 2 A 38 ILE ARG SER LEU GLN GLU GLN ASN TYR HIS LEU GLU ASN
SEQRES 3 A 38 GLU VAL ALA ARG LEU LYS LYS LEU VAL GLY GLU ARG
SEQRES 1 B 38 GLY ALA GLY SER SER SER LEU GLU ALA VAL ARG ARG LYS
SEQRES 2 B 38 ILE ARG SER LEU GLN GLU GLN ASN TYR HIS LEU GLU ASN
SEQRES 3 B 38 GLU VAL ALA ARG LEU LYS LYS LEU VAL GLY GLU ARG
HELIX 1 1 SER A 6 GLY A 36 1 31
HELIX 2 2 SER B 6 GLY B 36 1 31
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