Header list of 1tmz.pdb file
Complete list - r 2 2 Bytes
HEADER TROPOMYOSIN 20-APR-98 1TMZ
TITLE TMZIP: A CHIMERIC PEPTIDE MODEL OF THE N-TERMINUS OF ALPHA
TITLE 2 TROPOMYOSIN, NMR, 15 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TMZIP;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: SYNTHETIC CHIMERIC PEPTIDE OF THE N-TERMINUS OF RAT
COMPND 6 ALPHA-TROPOMYOSIN AND THE C-TERMINUS OF THE YEAST TRANSCRIPTION
COMPND 7 FACTOR GCN4
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS RATTUS, SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BLACK RAT, BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 10117,4932;
SOURCE 5 STRAIN: ,
KEYWDS TROPOMYOSIN, ACTIN-BINDING, THIN-FILAMENT-REGULATION, MUSCLE, ALPHA-
KEYWDS 2 HELIX COILED-COIL DIMER, GCN4, CHIMERIC-PEPTIDE-MODEL, DIMERIC TW0-
KEYWDS 3 CHAINED COILED-COIL
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR N.J.GREENFIELD,G.T.MONTELIONE,S.E.HITCHCOCK-DEGREGORI,R.S.FARID
REVDAT 4 02-MAR-22 1TMZ 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1TMZ 1 VERSN
REVDAT 2 01-APR-03 1TMZ 1 JRNL
REVDAT 1 17-JUN-98 1TMZ 0
JRNL AUTH N.J.GREENFIELD,G.T.MONTELIONE,R.S.FARID,
JRNL AUTH 2 S.E.HITCHCOCK-DEGREGORI
JRNL TITL THE STRUCTURE OF THE N-TERMINUS OF STRIATED MUSCLE
JRNL TITL 2 ALPHA-TROPOMYOSIN IN A CHIMERIC PEPTIDE: NUCLEAR MAGNETIC
JRNL TITL 3 RESONANCE STRUCTURE AND CIRCULAR DICHROISM STUDIES.
JRNL REF BIOCHEMISTRY V. 37 7834 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9601044
JRNL DOI 10.1021/BI973167M
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA
REMARK 3 AUTHORS : GUNTERT,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1TMZ 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_1000176740.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 6.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; 2QF-COSY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY 500
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VARIAN VNMR VNMR, DIANA
REMARK 210 METHOD USED : CONSTRAINED MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST VALUE OF TARGET FUNCTION
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: 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
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 VAL A 29 -62.99 -106.39
REMARK 500 1 VAL B 29 -63.58 -106.66
REMARK 500 2 VAL A 29 -61.01 -108.26
REMARK 500 2 GLU A 31 157.77 -43.53
REMARK 500 2 VAL B 29 -63.91 -109.45
REMARK 500 3 GLU A 31 157.37 -43.49
REMARK 500 3 VAL B 29 -63.18 -109.35
REMARK 500 4 VAL B 29 -66.51 -104.31
REMARK 500 5 VAL A 29 -62.17 -106.90
REMARK 500 5 VAL B 29 -64.91 -107.92
REMARK 500 6 VAL A 29 -67.43 -107.41
REMARK 500 6 VAL B 29 -60.18 -107.80
REMARK 500 7 VAL A 29 -62.12 -109.27
REMARK 500 7 VAL B 29 -64.80 -108.23
REMARK 500 8 GLU B 31 25.95 -73.49
REMARK 500 9 VAL B 29 -64.30 -109.82
REMARK 500 9 GLU B 31 95.61 -59.32
REMARK 500 10 VAL B 29 -68.63 -105.33
REMARK 500 11 VAL A 29 -67.35 -105.00
REMARK 500 11 GLU A 31 96.26 -54.97
REMARK 500 11 VAL B 29 -65.47 -107.53
REMARK 500 12 VAL A 29 -62.98 -108.87
REMARK 500 12 VAL B 29 -62.97 -109.69
REMARK 500 12 GLU B 31 157.36 -43.45
REMARK 500 13 VAL A 29 -64.41 -102.57
REMARK 500 13 GLU A 31 153.64 -43.01
REMARK 500 13 VAL B 29 -64.84 -105.10
REMARK 500 14 VAL A 29 -63.28 -104.56
REMARK 500 14 VAL B 29 -65.76 -106.23
REMARK 500 14 GLU B 31 101.90 -41.27
REMARK 500 15 VAL A 29 -60.48 -109.86
REMARK 500 15 GLU A 31 156.66 -42.81
REMARK 500 15 VAL B 29 -61.80 -109.88
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1TMZ A 1 32 UNP P03069 GCN4_YEAST 250 281
DBREF 1TMZ B 1 32 UNP P03069 GCN4_YEAST 250 281
SEQADV 1TMZ ASP A 2 UNP P03069 LYS 251 CONFLICT
SEQADV 1TMZ ALA A 3 UNP P03069 GLN 252 CONFLICT
SEQADV 1TMZ ILE A 4 UNP P03069 LEU 253 CONFLICT
SEQADV 1TMZ LYS A 5 UNP P03069 GLU 254 CONFLICT
SEQADV 1TMZ LYS A 6 UNP P03069 ASP 255 CONFLICT
SEQADV 1TMZ MET A 8 UNP P03069 VAL 257 CONFLICT
SEQADV 1TMZ GLN A 9 UNP P03069 GLU 258 CONFLICT
SEQADV 1TMZ MET A 10 UNP P03069 GLU 259 CONFLICT
SEQADV 1TMZ LYS A 12 UNP P03069 LEU 261 CONFLICT
SEQADV 1TMZ LEU A 13 UNP P03069 SER 262 CONFLICT
SEQADV 1TMZ ASP A 14 UNP P03069 LYS 263 CONFLICT
SEQADV 1TMZ ASP B 2 UNP P03069 LYS 251 CONFLICT
SEQADV 1TMZ ALA B 3 UNP P03069 GLN 252 CONFLICT
SEQADV 1TMZ ILE B 4 UNP P03069 LEU 253 CONFLICT
SEQADV 1TMZ LYS B 5 UNP P03069 GLU 254 CONFLICT
SEQADV 1TMZ LYS B 6 UNP P03069 ASP 255 CONFLICT
SEQADV 1TMZ MET B 8 UNP P03069 VAL 257 CONFLICT
SEQADV 1TMZ GLN B 9 UNP P03069 GLU 258 CONFLICT
SEQADV 1TMZ MET B 10 UNP P03069 GLU 259 CONFLICT
SEQADV 1TMZ LYS B 12 UNP P03069 LEU 261 CONFLICT
SEQADV 1TMZ LEU B 13 UNP P03069 SER 262 CONFLICT
SEQADV 1TMZ ASP B 14 UNP P03069 LYS 263 CONFLICT
SEQRES 1 A 32 MET ASP ALA ILE LYS LYS LYS MET GLN MET LEU LYS LEU
SEQRES 2 A 32 ASP ASN TYR HIS LEU GLU ASN GLU VAL ALA ARG LEU LYS
SEQRES 3 A 32 LYS LEU VAL GLY GLU ARG
SEQRES 1 B 32 MET ASP ALA ILE LYS LYS LYS MET GLN MET LEU LYS LEU
SEQRES 2 B 32 ASP ASN TYR HIS LEU GLU ASN GLU VAL ALA ARG LEU LYS
SEQRES 3 B 32 LYS LEU VAL GLY GLU ARG
HELIX 1 1 ILE A 4 LYS A 26 1 23
HELIX 2 2 ILE B 4 LEU B 25 1 22
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 - r 2 2 Bytes