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Дата изменения: Tue Jan 18 16:08:22 2011
Дата индексирования: Fri Feb 11 17:49:57 2011
Кодировка:

Поисковые слова: m 13
REM -------------------------------------------------------------------- 1QFQ
REM 1QFQ
REM STRIDE: Knowledge-based secondary structure assignment 1QFQ
REM Please cite: D.Frishman & P.Argos, Proteins 23, 566-579, 1995 1QFQ
REM 1QFQ
REM Residue accessible surface area calculation 1QFQ
REM Please cite: F.Eisenhaber & P.Argos, J.Comp.Chem. 14, 1272-1280, 1993 1QFQ
REM F.Eisenhaber et al., J.Comp.Chem., 1994, submitted 1QFQ
REM 1QFQ
REM ------------------------ General information ----------------------- 1QFQ
REM 1QFQ
HDR TRANSCRIPTION/RNA 12-APR-99 1QFQ 1QFQ
CMP MOL_ID: 1; 1QFQ
CMP MOLECULE: 36-MER N-TERMINAL PEPTIDE OF THE N PROTEIN; 1QFQ
CMP CHAIN: B; 1QFQ
CMP FRAGMENT: N-TERMINAL BINDING-DOMAIN, RESIDUES 2-36; 1QFQ
CMP SYNONYM: N36; 1QFQ
CMP ENGINEERED: YES; 1QFQ
CMP MOL_ID: 2; 1QFQ
CMP MOLECULE: 15-MER NUTRBOXB RNA HAIRPIN; 1QFQ
CMP CHAIN: A; 1QFQ
CMP FRAGMENT: BACTERIOPHAGE LAMBDA NUT BOXB-RNA; 1QFQ
CMP ENGINEERED: YES; 1QFQ
CMP OTHER_DETAILS: NUTBOXB FROM THE NUTR-SEQUENCE 1QFQ
SRC MOL_ID: 1; 1QFQ
SRC ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE LAMBDA; 1QFQ
SRC ORGANISM_TAXID: 10710; 1QFQ
SRC EXPRESSION_SYSTEM: ESCHERICHIA COLI; 1QFQ
SRC EXPRESSION_SYSTEM_TAXID: 562; 1QFQ
SRC MOL_ID: 2; 1QFQ
SRC SYNTHETIC: YES; 1QFQ
SRC OTHER_DETAILS: SEQUENCE FROM BACTERIOPHAGE LAMBDA. RNA WAS 1QFQ
SRC UNIFORMLY LABELLED WITH (13)C AND (15)N 1QFQ
AUT M.SCHAERPF,H.STICHT,P.ROESCH 1QFQ
REM 1QFQ
REM -------------------- Secondary structure summary ------------------- 1QFQ
REM 1QFQ
CHN /data/npidb/pdb/pdb_new/all/pdb1qfq.pdb B 1QFQ
REM 1QFQ
REM . . . 1QFQ
SEQ 1 DAQTRRRERRAEKQAQWKAANPLLVGVSAKPVNRP 35 1QFQ
STR HHHHHHHHHHHHHHHHHHH GGG TTTT 1QFQ
REM 1QFQ
REM 1QFQ
REM 1QFQ
LOC AlphaHelix ALA 3 B ALA 21 B 1QFQ
LOC 310Helix PRO 23 B LEU 25 B 1QFQ
LOC TurnIV GLY 27 B ALA 30 B 1QFQ
REM 1QFQ
REM --------------- Detailed secondary structure assignment------------- 1QFQ
REM 1QFQ
REM |---Residue---| |--Structure--| |-Phi-| |-Psi-| |-Area-| 1QFQ
ASG ASP B 2 1 C Coil 360.00 -160.79 169.8 1QFQ
ASG ALA B 3 2 H AlphaHelix -114.12 -27.03 70.9 1QFQ
ASG GLN B 4 3 H AlphaHelix -71.13 -57.39 117.2 1QFQ
ASG THR B 5 4 H AlphaHelix -47.88 -35.64 80.8 1QFQ
ASG ARG B 6 5 H AlphaHelix -71.43 -46.69 147.7 1QFQ
ASG ARG B 7 6 H AlphaHelix -56.76 -32.70 66.4 1QFQ
ASG ARG B 8 7 H AlphaHelix -55.53 -39.15 96.2 1QFQ
ASG GLU B 9 8 H AlphaHelix -62.06 -32.31 156.8 1QFQ
ASG ARG B 10 9 H AlphaHelix -75.60 -15.43 172.7 1QFQ
ASG ARG B 11 10 H AlphaHelix -89.14 -0.88 92.8 1QFQ
ASG ALA B 12 11 H AlphaHelix -52.70 -26.94 51.7 1QFQ
ASG GLU B 13 12 H AlphaHelix -76.49 -33.19 144.4 1QFQ
ASG LYS B 14 13 H AlphaHelix -79.94 -33.85 142.8 1QFQ
ASG GLN B 15 14 H AlphaHelix -72.63 -49.56 68.2 1QFQ
ASG ALA B 16 15 H AlphaHelix -67.33 -26.11 56.9 1QFQ
ASG GLN B 17 16 H AlphaHelix -79.89 -36.35 136.2 1QFQ
ASG TRP B 18 17 H AlphaHelix -75.41 -47.98 100.5 1QFQ
ASG LYS B 19 18 H AlphaHelix -59.10 -35.33 107.6 1QFQ
ASG ALA B 20 19 H AlphaHelix -62.50 -29.60 76.4 1QFQ
ASG ALA B 21 20 H AlphaHelix -118.88 28.49 69.7 1QFQ
ASG ASN B 22 21 C Coil -153.46 49.83 38.1 1QFQ
ASG PRO B 23 22 G 310Helix -71.16 -26.13 31.1 1QFQ
ASG LEU B 24 23 G 310Helix -58.04 -35.15 112.5 1QFQ
ASG LEU B 25 24 G 310Helix -102.12 35.64 120.7 1QFQ
ASG VAL B 26 25 C Coil -148.05 109.72 42.6 1QFQ
ASG GLY B 27 26 T Turn 42.59 97.53 58.2 1QFQ
ASG VAL B 28 27 T Turn -46.29 148.04 129.4 1QFQ
ASG SER B 29 28 T Turn 60.02 45.84 103.1 1QFQ
ASG ALA B 30 29 T Turn -139.68 51.42 47.0 1QFQ
ASG LYS B 31 30 C Coil -117.09 123.41 127.4 1QFQ
ASG PRO B 32 31 C Coil -73.59 165.19 114.3 1QFQ
ASG VAL B 33 32 C Coil -137.43 -172.30 105.4 1QFQ
ASG ASN B 34 33 C Coil -143.85 62.78 165.7 1QFQ
ASG ARG B 35 34 C Coil -153.10 70.69 207.0 1QFQ
ASG PRO B 36 35 C Coil -72.24 360.00 198.6 1QFQ