Документ взят из кэша поисковой машины. Адрес оригинального документа : http://mouse.belozersky.msu.ru/npidb/data/pdb_new/stride/1t2s.std.txt Дата изменения: Sat May 19 00:32:56 2012 Дата индексирования: Tue Oct 2 11:58:18 2012 Кодировка:

REM -------------------------------------------------------------------- 1T2S
REM 1T2S
REM STRIDE: Knowledge-based secondary structure assignment 1T2S
REM Please cite: D.Frishman & P.Argos, Proteins 23, 566-579, 1995 1T2S
REM 1T2S
REM Residue accessible surface area calculation 1T2S
REM Please cite: F.Eisenhaber & P.Argos, J.Comp.Chem. 14, 1272-1280, 1993 1T2S
REM F.Eisenhaber et al., J.Comp.Chem., 1994, submitted 1T2S
REM 1T2S
REM ------------------------ General information ----------------------- 1T2S
REM 1T2S
HDR NUCLEIC ACID BINDING PROTEIN/DNA 22-APR-04 1T2S 1T2S
CMP MOL_ID: 1; 1T2S
CMP MOLECULE: ARGONAUTE 2; 1T2S
CMP CHAIN: A; 1T2S
CMP FRAGMENT: PAZ DOMAIN, RESIDUES 605-723; 1T2S
CMP SYNONYM: CG7439 PROTEIN; 1T2S
CMP ENGINEERED: YES; 1T2S
CMP MOL_ID: 2; 1T2S
CMP MOLECULE: 5'-D(*CP*TP*CP*AP*C)-3'; 1T2S
CMP CHAIN: B; 1T2S
CMP ENGINEERED: YES 1T2S
SRC MOL_ID: 1; 1T2S
SRC ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER; 1T2S
SRC ORGANISM_COMMON: FRUIT FLY; 1T2S
SRC ORGANISM_TAXID: 7227; 1T2S
SRC EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); 1T2S
SRC EXPRESSION_SYSTEM_TAXID: 469008; 1T2S
SRC EXPRESSION_SYSTEM_STRAIN: BL21(DE3); 1T2S
SRC EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; 1T2S
SRC EXPRESSION_SYSTEM_PLASMID: PETM60; 1T2S
SRC MOL_ID: 2; 1T2S
SRC SYNTHETIC: YES 1T2S
AUT A.LINGEL,B.SIMON,E.IZAURRALDE,M.SATTLER 1T2S
REM 1T2S
REM -------------------- Secondary structure summary ------------------- 1T2S
REM 1T2S
CHN /data/npidb/pdb/pdb_new/all/pdb1t2s.pdb A 1T2S
REM 1T2S
REM . . . . . 1T2S
SEQ 1 GAMAMPMIEYLERFSLKAKINNTTNLDYSRRFLEPFLRGINVVYTPPQSF 50 1T2S
STR EEHHHHHHHHHH TTTTTTTTHHHHHHHHHTTEEEEE TTTT 1T2S
REM 1T2S
REM . . . . . 1T2S
SEQ 51 QSAPRVYRVNGLSRAPASSETFEHDGKKVTIASYFHSRNYPLKFPQLHCL 100 1T2S
STR T EEEEEEEEEEEETTTTEEEETTEEEEHHHHHHHH TTTTTTEEE 1T2S
REM 1T2S
REM . . 1T2S
SEQ 101 NVGSSIKSILLPIELCSIEEGQA 123 1T2S
STR EEETTTTEEEE GGGEEETTTT 1T2S
REM 1T2S
REM 1T2S
REM 1T2S
LOC AlphaHelix MET 7 A LEU 16 A 1T2S
LOC AlphaHelix SER 29 A LEU 37 A 1T2S
LOC AlphaHelix ILE 81 A ARG 88 A 1T2S
LOC 310Helix ILE 113 A LEU 115 A 1T2S
LOC Strand MET 5 A PRO 6 A 1T2S
LOC Strand ILE 40 A TYR 44 A 1T2S
LOC Strand ARG 55 A PRO 66 A 1T2S
LOC Strand THR 71 A HIS 74 A 1T2S
LOC Strand LYS 77 A THR 80 A 1T2S
LOC Strand HIS 98 A GLY 103 A 1T2S
LOC Strand SER 108 A LEU 111 A 1T2S
LOC Strand CYS 116 A ILE 118 A 1T2S
LOC TurnI ASN 21 A THR 24 A 1T2S
LOC TurnIV THR 24 A ASP 27 A 1T2S
LOC TurnIV ASN 25 A TYR 28 A 1T2S
LOC TurnI LEU 26 A SER 29 A 1T2S
LOC TurnII LEU 37 A ILE 40 A 1T2S
LOC TurnI PRO 47 A PHE 50 A 1T2S
LOC TurnI GLN 48 A GLN 51 A 1T2S
LOC TurnI PRO 66 A SER 69 A 1T2S
LOC TurnIV ALA 67 A GLU 70 A 1T2S
LOC TurnIV GLU 73 A GLY 76 A 1T2S
LOC TurnI' HIS 74 A LYS 77 A 1T2S
LOC TurnIV LEU 92 A PRO 95 A 1T2S
LOC TurnI PHE 94 A LEU 97 A 1T2S
LOC TurnI SER 104 A LYS 107 A 1T2S
LOC TurnIV SER 105 A SER 108 A 1T2S
LOC TurnI GLU 119 A GLN 122 A 1T2S
REM 1T2S
REM --------------- Detailed secondary structure assignment------------- 1T2S
REM 1T2S
REM |---Residue---| |--Structure--| |-Phi-| |-Psi-| |-Area-| 1T2S
ASG GLY A 1 1 C Coil 360.00 -151.19 101.1 1T2S
ASG ALA A 2 2 C Coil 58.38 45.44 100.0 1T2S
ASG MET A 3 3 C Coil -113.98 61.12 95.0 1T2S
ASG ALA A 4 4 C Coil -77.84 96.82 62.9 1T2S
ASG MET A 5 5 E Strand -91.14 119.50 12.5 1T2S
ASG PRO A 6 6 E Strand -53.63 135.00 63.0 1T2S
ASG MET A 7 7 H AlphaHelix -59.21 -30.11 0.6 1T2S
ASG ILE A 8 8 H AlphaHelix -67.71 -47.81 10.4 1T2S
ASG GLU A 9 9 H AlphaHelix -61.12 -41.91 59.6 1T2S
ASG TYR A 10 10 H AlphaHelix -61.18 -44.30 28.9 1T2S
ASG LEU A 11 11 H AlphaHelix -60.02 -45.18 1.2 1T2S
ASG GLU A 12 12 H AlphaHelix -59.89 -55.77 17.3 1T2S
ASG ARG A 13 13 H AlphaHelix -69.96 -43.19 136.4 1T2S
ASG PHE A 14 14 H AlphaHelix -100.08 -47.18 104.5 1T2S
ASG SER A 15 15 H AlphaHelix -85.86 -33.01 49.8 1T2S
ASG LEU A 16 16 H AlphaHelix -114.68 -33.80 53.1 1T2S
ASG LYS A 17 17 C Coil 65.01 18.78 164.9 1T2S
ASG ALA A 18 18 C Coil -132.60 -170.57 58.9 1T2S
ASG LYS A 19 19 C Coil -102.24 129.23 128.6 1T2S
ASG ILE A 20 20 C Coil -89.97 113.90 10.9 1T2S
ASG ASN A 21 21 T Turn -153.95 -154.52 57.5 1T2S
ASG ASN A 22 22 T Turn -64.38 -6.82 145.1 1T2S
ASG THR A 23 23 T Turn -98.17 15.50 90.9 1T2S
ASG THR A 24 24 T Turn -60.04 131.07 19.6 1T2S
ASG ASN A 25 25 T Turn -105.61 0.84 131.2 1T2S
ASG LEU A 26 26 T Turn -80.45 -0.67 28.1 1T2S
ASG ASP A 27 27 T Turn -57.55 -61.74 17.6 1T2S
ASG TYR A 28 28 T Turn -79.72 -6.84 169.6 1T2S
ASG SER A 29 29 H AlphaHelix -87.67 -7.11 32.5 1T2S
ASG ARG A 30 30 H AlphaHelix -55.20 -33.87 0.4 1T2S
ASG ARG A 31 31 H AlphaHelix -63.00 -33.17 148.4 1T2S
ASG PHE A 32 32 H AlphaHelix -95.77 -5.61 143.3 1T2S
ASG LEU A 33 33 H AlphaHelix -87.20 -21.18 26.9 1T2S
ASG GLU A 34 34 H AlphaHelix -46.29 -53.21 13.8 1T2S
ASG PRO A 35 35 H AlphaHelix -54.52 -29.99 85.9 1T2S
ASG PHE A 36 36 H AlphaHelix -85.71 -27.54 113.8 1T2S
ASG LEU A 37 37 H AlphaHelix -91.51 -17.25 1.6 1T2S
ASG ARG A 38 38 T Turn -62.25 127.44 167.9 1T2S
ASG GLY A 39 39 T Turn 79.72 39.90 43.7 1T2S
ASG ILE A 40 40 E Strand -114.82 165.44 15.4 1T2S
ASG ASN A 41 41 E Strand -115.76 122.86 14.6 1T2S
ASG VAL A 42 42 E Strand -118.26 134.19 1.0 1T2S
ASG VAL A 43 43 E Strand -84.60 111.09 32.5 1T2S
ASG TYR A 44 44 E Strand -79.18 113.25 26.1 1T2S
ASG THR A 45 45 C Coil -100.33 105.82 62.3 1T2S
ASG PRO A 46 46 C Coil -62.81 128.55 20.6 1T2S
ASG PRO A 47 47 T Turn -50.40 155.43 9.8 1T2S
ASG GLN A 48 48 T Turn -56.10 -23.59 177.0 1T2S
ASG SER A 49 49 T Turn -81.02 -10.01 40.9 1T2S
ASG PHE A 50 50 T Turn -91.38 -40.37 24.3 1T2S
ASG GLN A 51 51 T Turn 56.16 43.95 184.5 1T2S
ASG SER A 52 52 C Coil -112.55 152.00 57.9 1T2S
ASG ALA A 53 53 C Coil -72.60 130.94 85.3 1T2S
ASG PRO A 54 54 C Coil -69.07 136.30 80.6 1T2S
ASG ARG A 55 55 E Strand -131.84 138.29 153.9 1T2S
ASG VAL A 56 56 E Strand -85.66 138.85 69.4 1T2S
ASG TYR A 57 57 E Strand -127.41 139.39 47.4 1T2S
ASG ARG A 58 58 E Strand -78.03 113.60 133.1 1T2S
ASG VAL A 59 59 E Strand -73.92 116.42 0.2 1T2S
ASG ASN A 60 60 E Strand -86.30 -26.84 76.3 1T2S
ASG GLY A 61 61 E Strand 165.10 -138.88 6.1 1T2S
ASG LEU A 62 62 E Strand -125.93 149.45 7.3 1T2S
ASG SER A 63 63 E Strand -85.03 149.69 10.3 1T2S
ASG ARG A 64 64 E Strand -74.58 -5.53 152.6 1T2S
ASG ALA A 65 65 E Strand -128.94 135.23 17.4 1T2S
ASG PRO A 66 66 E Strand -66.59 169.64 12.4 1T2S
ASG ALA A 67 67 T Turn -69.08 -22.97 1.0 1T2S
ASG SER A 68 68 T Turn -88.64 -1.52 45.0 1T2S
ASG SER A 69 69 T Turn -104.69 -52.40 57.2 1T2S
ASG GLU A 70 70 T Turn -69.41 141.29 83.6 1T2S
ASG THR A 71 71 E Strand -128.62 145.92 68.4 1T2S
ASG PHE A 72 72 E Strand -130.52 149.32 70.2 1T2S
ASG GLU A 73 73 E Strand -86.15 113.66 145.6 1T2S
ASG HIS A 74 74 E Strand -138.07 126.96 104.9 1T2S
ASG ASP A 75 75 T Turn 69.63 17.81 126.6 1T2S
ASG GLY A 76 76 T Turn 82.56 -3.25 52.9 1T2S
ASG LYS A 77 77 E Strand -101.29 132.66 114.8 1T2S
ASG LYS A 78 78 E Strand -86.41 95.76 142.8 1T2S
ASG VAL A 79 79 E Strand -97.90 146.46 41.9 1T2S
ASG THR A 80 80 E Strand -77.88 154.85 28.6 1T2S
ASG ILE A 81 81 H AlphaHelix -52.81 -47.45 18.2 1T2S
ASG ALA A 82 82 H AlphaHelix -59.25 -40.50 14.2 1T2S
ASG SER A 83 83 H AlphaHelix -68.50 -36.42 59.3 1T2S
ASG TYR A 84 84 H AlphaHelix -63.82 -43.48 60.4 1T2S
ASG PHE A 85 85 H AlphaHelix -66.43 -39.04 11.8 1T2S
ASG HIS A 86 86 H AlphaHelix -64.30 -37.29 119.7 1T2S
ASG SER A 87 87 H AlphaHelix -69.66 -30.59 104.2 1T2S
ASG ARG A 88 88 H AlphaHelix -74.93 4.02 99.4 1T2S
ASG ASN A 89 89 C Coil 72.80 50.21 124.5 1T2S
ASG TYR A 90 90 C Coil -150.25 100.59 49.5 1T2S
ASG PRO A 91 91 C Coil -75.00 120.93 77.9 1T2S
ASG LEU A 92 92 T Turn -70.00 129.07 22.1 1T2S
ASG LYS A 93 93 T Turn -75.49 -27.71 126.0 1T2S
ASG PHE A 94 94 T Turn -142.79 68.33 14.2 1T2S
ASG PRO A 95 95 T Turn -72.18 -7.91 36.6 1T2S
ASG GLN A 96 96 T Turn -82.69 -5.57 71.9 1T2S
ASG LEU A 97 97 T Turn -70.57 128.10 7.0 1T2S
ASG HIS A 98 98 E Strand -51.80 128.61 27.9 1T2S
ASG CYS A 99 99 E Strand -63.88 146.88 0.0 1T2S
ASG LEU A 100 100 E Strand -73.75 125.57 0.4 1T2S
ASG ASN A 101 101 E Strand -90.62 96.94 29.9 1T2S
ASG VAL A 102 102 E Strand -133.68 -167.60 0.2 1T2S
ASG GLY A 103 103 E Strand 89.73 -77.90 38.7 1T2S
ASG SER A 104 104 T Turn -154.32 158.31 37.5 1T2S
ASG SER A 105 105 T Turn -79.55 -24.48 95.4 1T2S
ASG ILE A 106 106 T Turn -96.57 -22.25 161.8 1T2S
ASG LYS A 107 107 T Turn -127.82 85.18 139.3 1T2S
ASG SER A 108 108 E Strand -83.41 134.98 54.7 1T2S
ASG ILE A 109 109 E Strand -116.77 137.08 36.6 1T2S
ASG LEU A 110 110 E Strand -100.39 120.84 36.0 1T2S
ASG LEU A 111 111 E Strand -128.81 137.96 21.4 1T2S
ASG PRO A 112 112 C Coil -60.44 111.96 9.0 1T2S
ASG ILE A 113 113 G 310Helix -56.78 -21.45 1.7 1T2S
ASG GLU A 114 114 G 310Helix -52.04 -37.45 23.6 1T2S
ASG LEU A 115 115 G 310Helix -98.26 5.06 10.8 1T2S
ASG CYS A 116 116 E Strand -99.87 144.20 0.5 1T2S
ASG SER A 117 117 E Strand -134.15 135.54 5.6 1T2S
ASG ILE A 118 118 E Strand -77.01 127.91 8.5 1T2S
ASG GLU A 119 119 T Turn -76.48 138.23 75.4 1T2S
ASG GLU A 120 120 T Turn -59.06 -21.51 75.6 1T2S
ASG GLY A 121 121 T Turn -82.92 -9.33 61.6 1T2S
ASG GLN A 122 122 T Turn -83.85 -34.15 61.6 1T2S
ASG ALA A 123 123 C Coil -82.60 360.00 120.7 1T2S