Header list of 1mv4.pdb file
Complete list - 23 20 Bytes
HEADER DE NOVO PROTEIN 24-SEP-02 1MV4
TITLE TM9A251-284: A PEPTIDE MODEL OF THE C-TERMINUS OF A RAT STRIATED ALPHA
TITLE 2 TROPOMYOSIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPOMYOSIN 1 ALPHA CHAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL (RESIDUES 251-284);
COMPND 5 SYNONYM: ALPHA-TROPOMYOSIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 TISSUE: SKELETAL MUSCLE;
SOURCE 6 GENE: TPM1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: DH5;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PPROEX HTA
KEYWDS TROPOMYOSIN, EXON 9A, ACTIN-BINDING, TROPONIN BINDING, MUSCLE, ALPHA-
KEYWDS 2 HELIX, COILED-COIL, DIMER, PEPTIDE-MODEL, TWO-CHAINED, DISULFIDE
KEYWDS 3 CROSS-LINKED, DE NOVO PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR N.J.GREENFIELD,G.V.T.SWAPNA,Y.HUANG,T.PALM,S.GRABOSKI,G.T.MONTELIONE,
AUTHOR 2 S.E.HITCHCOCK-DEGREGORI
REVDAT 3 23-FEB-22 1MV4 1 REMARK
REVDAT 2 24-FEB-09 1MV4 1 VERSN
REVDAT 1 18-FEB-03 1MV4 0
JRNL AUTH N.J.GREENFIELD,G.V.T.SWAPNA,Y.HUANG,T.PALM,S.GRABOSKI,
JRNL AUTH 2 G.T.MONTELIONE,S.E.HITCHCOCK-DEGREGORI
JRNL TITL THE STRUCTURE OF THE CARBOXYL TERMINUS OF STRIATED
JRNL TITL 2 ALPHA-TROPOMYOSIN IN SOLUTION REVEALS AN UNUSUAL PARALLEL
JRNL TITL 3 ARRANGEMENT OF INTERACTING ALPHA-HELICES
JRNL REF BIOCHEMISTRY V. 42 614 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12534273
JRNL DOI 10.1021/BI026989E
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
REMARK 3 REFERENCE CITED ABOVE
REMARK 4
REMARK 4 1MV4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017208.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283.00
REMARK 210 PH : 6.40
REMARK 210 IONIC STRENGTH : 0.12 N
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1-2 MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-X-
REMARK 210 FILTERED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 5.3B, DYANA 1.5, AUTOASSIGN
REMARK 210 1.0, AUTOSTRUCTURE 1.0, SPARKY
REMARK 210 3.74
REMARK 210 METHOD USED : 1648 CONFORMATIONALLY-
REMARK 210 RESTRICTING NOE CONSTRAINTS (OUT
REMARK 210 OF A TOTAL OF 2036 NOE DERIVED
REMARK 210 DISTANCES) 52 LOOSE DIHEDRAL
REMARK 210 ANGLE CONSTRAINTS AND 48
REMARK 210 BACKBONE INTRA- HELICAL HYDROGEN
REMARK 210 BOND CONSTRAINTS WERE UTILILIZED.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH COVALENT
REMARK 210 GEOMETRY, STRUCTURES WITH THE
REMARK 210 LEAST RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE RESONANCE ASSIGNMENTS WERE MADE USING THROUGH BOND
REMARK 210 TRIPLE RESONANCE EXPERIMENTS INCLUDING HN(CA)CO, HNCO, H(CA)(C0)
REMARK 210 NH, H(CA)NH, CA(CO)NH, CANH, CBCA(CO)NH, CBCANH, HCCH-COSY AND
REMARK 210 CCH-COSY
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 278 H THR A 282 1.54
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 249 -154.92 47.35
REMARK 500 1 LYS A 251 -81.12 -141.51
REMARK 500 1 SER A 252 37.22 -151.04
REMARK 500 1 LEU A 260 -73.92 -64.91
REMARK 500 1 THR A 282 160.02 55.11
REMARK 500 1 SER A 283 91.21 -54.19
REMARK 500 1 CYS B 249 -77.45 -117.41
REMARK 500 1 LYS B 251 -90.25 -151.91
REMARK 500 1 THR B 282 164.91 55.01
REMARK 500 2 LYS A 251 -83.82 172.65
REMARK 500 2 SER A 252 22.05 -142.65
REMARK 500 2 LEU A 256 -76.07 -52.78
REMARK 500 2 LEU A 260 -77.00 -65.54
REMARK 500 2 SER A 283 98.79 3.72
REMARK 500 2 CYS B 249 -55.45 87.55
REMARK 500 2 LYS B 251 -96.92 -163.02
REMARK 500 2 SER B 252 42.13 -160.07
REMARK 500 2 ASP B 258 -71.85 -69.49
REMARK 500 2 LEU B 260 -72.26 -64.87
REMARK 500 2 THR B 282 -178.41 47.63
REMARK 500 3 CYS A 249 -151.72 173.91
REMARK 500 3 LYS A 251 -61.73 -154.81
REMARK 500 3 THR A 282 -154.74 33.34
REMARK 500 3 LYS B 251 -54.60 -171.29
REMARK 500 3 LEU B 260 -75.99 -67.73
REMARK 500 3 SER B 283 96.95 8.58
REMARK 500 4 CYS A 249 -65.68 72.18
REMARK 500 4 LYS A 251 -72.40 165.42
REMARK 500 4 LEU A 256 -76.55 -56.78
REMARK 500 4 ASP A 258 -71.18 -50.57
REMARK 500 4 LEU A 260 -76.94 -64.54
REMARK 500 4 THR A 282 -135.23 27.04
REMARK 500 4 CYS B 249 99.73 -172.87
REMARK 500 4 LYS B 251 -71.82 -158.68
REMARK 500 4 ASP B 258 -72.12 -66.32
REMARK 500 4 THR B 282 179.10 49.29
REMARK 500 5 LYS A 251 -84.42 176.16
REMARK 500 5 THR A 282 -174.95 46.47
REMARK 500 5 CYS B 249 -107.33 65.47
REMARK 500 5 LYS B 251 -73.98 175.65
REMARK 500 5 LEU B 256 -72.30 -56.11
REMARK 500 5 ASP B 258 -72.03 -50.54
REMARK 500 5 LEU B 260 -75.37 -70.45
REMARK 500 5 TYR B 261 -37.33 -37.57
REMARK 500 5 THR B 282 165.78 52.98
REMARK 500 6 CYS A 249 -42.87 89.06
REMARK 500 6 LYS A 251 -73.16 163.25
REMARK 500 6 LEU A 256 -70.60 -60.67
REMARK 500 6 LEU A 260 -78.50 -67.80
REMARK 500 6 THR A 282 -173.70 46.58
REMARK 500
REMARK 500 THIS ENTRY HAS 96 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IHQ RELATED DB: PDB
REMARK 900 1IHQ IS GLYTM1BZIP: A CHIMERIC PEPTIDE MODEL OF THE N-TERMINUS OF A
REMARK 900 RAT SHORT ALPHA TROPOMYOSIN WITH THE N-TERMINUS ENCODED BY EXON 1B
REMARK 900 RELATED ID: 1TMZ RELATED DB: PDB
REMARK 900 1TMZ IS TMZIP: A CHIMERIC PEPTIDE MODEL OF THE N-TERMINUS OF ALPHA
REMARK 900 TROPOMYOSIN, NMR, 15 STRUCTURES
REMARK 900 RELATED ID: 1IC2 RELATED DB: PDB
REMARK 900 1IC2 IS DECIPHERING THE DESIGN OF THE TROPOMYOSIN MOLECULE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS SEQUENCE HAS A SYNTHETIC GCG AT N-TERMINUS
REMARK 999 AND CONTAINS THE MUTATION N279K. THE SEQUENCE
REMARK 999 DATABASE MATCH, HOWEVER, ERRONEOUSLY HAS A K AT
REMARK 999 THIS POSITION AS WELL. THE SEQUENCE IN THE DATABASE SHOULD
REMARK 999 HAVE AN ASN AT POSITION 279, WHICH HAS BEEN ENGINEERED
REMARK 999 TO LYS IN THIS ENTRY.
DBREF 1MV4 A 251 284 UNP P04692 TPM1_RAT 251 284
DBREF 1MV4 B 251 284 UNP P04692 TPM1_RAT 251 284
SEQADV 1MV4 GLY A 248 UNP P04692 SEE REMARK 999
SEQADV 1MV4 CYS A 249 UNP P04692 SEE REMARK 999
SEQADV 1MV4 GLY A 250 UNP P04692 SEE REMARK 999
SEQADV 1MV4 GLY B 248 UNP P04692 SEE REMARK 999
SEQADV 1MV4 CYS B 249 UNP P04692 SEE REMARK 999
SEQADV 1MV4 GLY B 250 UNP P04692 SEE REMARK 999
SEQRES 1 A 37 GLY CYS GLY LYS SER ILE ASP ASP LEU GLU ASP GLU LEU
SEQRES 2 A 37 TYR ALA GLN LYS LEU LYS TYR LYS ALA ILE SER GLU GLU
SEQRES 3 A 37 LEU ASP HIS ALA LEU LYS ASP MET THR SER ILE
SEQRES 1 B 37 GLY CYS GLY LYS SER ILE ASP ASP LEU GLU ASP GLU LEU
SEQRES 2 B 37 TYR ALA GLN LYS LEU LYS TYR LYS ALA ILE SER GLU GLU
SEQRES 3 B 37 LEU ASP HIS ALA LEU LYS ASP MET THR SER ILE
HELIX 1 1 ILE A 253 THR A 282 1 30
HELIX 2 2 ILE B 253 ASP B 280 1 28
SSBOND 1 CYS A 249 CYS B 249 1555 1555 2.03
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 - 23 20 Bytes