Документ взят из кэша поисковой машины. Адрес оригинального документа : http://mouse.belozersky.msu.ru/npidb/data/pdb_new/stride/3vxv.std.txt Дата изменения: Wed Jan 23 17:38:17 2013 Дата индексирования: Sun Feb 3 22:25:05 2013 Кодировка:

REM -------------------------------------------------------------------- 3VXV
REM 3VXV
REM STRIDE: Knowledge-based secondary structure assignment 3VXV
REM Please cite: D.Frishman & P.Argos, Proteins 23, 566-579, 1995 3VXV
REM 3VXV
REM Residue accessible surface area calculation 3VXV
REM Please cite: F.Eisenhaber & P.Argos, J.Comp.Chem. 14, 1272-1280, 1993 3VXV
REM F.Eisenhaber et al., J.Comp.Chem., 1994, submitted 3VXV
REM 3VXV
REM ------------------------ General information ----------------------- 3VXV
REM 3VXV
HDR HYDROLASE/DNA 21-SEP-12 3VXV 3VXV
CMP MOL_ID: 1; 3VXV
CMP MOLECULE: METHYL-CPG-BINDING DOMAIN PROTEIN 4; 3VXV
CMP CHAIN: A; 3VXV
CMP FRAGMENT: METHYL CPG BINDING DOMAIN, UNP RESIDUES 69-136; 3VXV
CMP SYNONYM: METHYL-CPG-BINDING PROTEIN MBD4, MISMATCH-SPECIFIC 3VXV
CMP GLYCOSYLASE; 3VXV
CMP EC: 3.2.2.-; 3VXV
CMP ENGINEERED: YES; 3VXV
CMP MOL_ID: 2; 3VXV
CMP MOLECULE: DNA (5'-D(*GP*TP*CP*AP*CP*TP*AP*CP*(5CM)P*GP*GP*AP 3VXV
CMP 3'); 3VXV
CMP CHAIN: B; 3VXV
CMP ENGINEERED: YES; 3VXV
CMP MOL_ID: 3; 3VXV
CMP MOLECULE: DNA (5'-D(*GP*TP*CP*TP*GP*GP*TP*AP*GP*TP*GP*AP*CP* 3VXV
CMP CHAIN: C; 3VXV
CMP ENGINEERED: YES 3VXV
SRC MOL_ID: 1; 3VXV
SRC ORGANISM_SCIENTIFIC: MUS MUSCULUS; 3VXV
SRC ORGANISM_COMMON: MOUSE; 3VXV
SRC ORGANISM_TAXID: 10090; 3VXV
SRC GENE: MBD4; 3VXV
SRC EXPRESSION_SYSTEM: ESCHERICHIA COLI; 3VXV
SRC EXPRESSION_SYSTEM_TAXID: 562; 3VXV
SRC EXPRESSION_SYSTEM_STRAIN: BL21(DE3); 3VXV
SRC EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; 3VXV
SRC MOL_ID: 2; 3VXV
SRC SYNTHETIC: YES; 3VXV
SRC MOL_ID: 3; 3VXV
SRC SYNTHETIC: YES 3VXV
AUT J.OTANI,K.ARITA,T.KATO,M.KINOSHITA,M.ARIYOSHI,M.SHIRAKAWA 3VXV
REM 3VXV
REM -------------------- Secondary structure summary ------------------- 3VXV
REM 3VXV
CHN /data/npidb/pdb/pdb_new/all/pdb3vxv.pdb A 3VXV
REM 3VXV
REM . . . . . 3VXV
SEQ 1 KPVPCGWERVVKQRLSGKTAGKFDVYFISPQGLKFRSKRSLANYLLKNGE 50 3VXV
STR TTTTTTTEEEEEEE TTTTTTEEEEEEETTTT EE HHHHHHHHHHHH 3VXV
REM 3VXV
REM . 3VXV
SEQ 51 TFLKPEDFNFTVLPK 65 3VXV
STR GGG 3VXV
REM 3VXV
REM 3VXV
REM 3VXV
LOC AlphaHelix LYS 108 A GLY 119 A 3VXV
LOC 310Helix PRO 125 A ASP 127 A 3VXV
LOC Strand GLU 78 A ARG 84 A 3VXV
LOC Strand LYS 92 A ILE 98 A 3VXV
LOC Strand LYS 104 A PHE 105 A 3VXV
LOC TurnVIII LYS 71 A PRO 74 A 3VXV
LOC TurnII PRO 74 A TRP 77 A 3VXV
LOC TurnIV SER 86 A THR 89 A 3VXV
LOC TurnI GLY 87 A ALA 90 A 3VXV
LOC TurnII THR 89 A LYS 92 A 3VXV
LOC TurnI SER 99 A GLY 102 A 3VXV
LOC Disulfide CYS 75 A CYS 75 A PDB 3VXV
REM 3VXV
REM --------------- Detailed secondary structure assignment------------- 3VXV
REM 3VXV
REM |---Residue---| |--Structure--| |-Phi-| |-Psi-| |-Area-| 3VXV
ASG LYS A 71 1 T Turn 360.00 -64.29 118.7 3VXV
ASG PRO A 72 2 T Turn -48.24 -50.26 134.8 3VXV
ASG VAL A 73 3 T Turn -100.41 117.98 52.4 3VXV
ASG PRO A 74 4 T Turn -48.18 145.62 70.1 3VXV
ASG CYS A 75 5 T Turn -53.47 127.70 130.5 3VXV
ASG GLY A 76 6 T Turn 86.20 -11.08 57.0 3VXV
ASG TRP A 77 7 T Turn -89.02 161.90 52.2 3VXV
ASG GLU A 78 8 E Strand -127.78 144.09 113.4 3VXV
ASG ARG A 79 9 E Strand -116.72 139.57 130.5 3VXV
ASG VAL A 80 10 E Strand -121.82 132.82 25.2 3VXV
ASG VAL A 81 11 E Strand -116.33 131.15 72.9 3VXV
ASG LYS A 82 12 E Strand -134.75 152.53 125.1 3VXV
ASG GLN A 83 13 E Strand -113.74 123.12 97.1 3VXV
ASG ARG A 84 14 E Strand -63.69 143.05 98.0 3VXV
ASG LEU A 85 15 C Coil -116.16 -9.57 149.3 3VXV
ASG SER A 86 16 T Turn -149.00 169.59 92.9 3VXV
ASG GLY A 87 17 T Turn 70.90 -170.46 64.7 3VXV
ASG LYS A 88 18 T Turn -64.49 -25.81 220.5 3VXV
ASG THR A 89 19 T Turn -97.73 12.40 59.8 3VXV
ASG ALA A 90 20 T Turn -44.47 133.41 52.3 3VXV
ASG GLY A 91 21 T Turn 95.15 -25.39 34.4 3VXV
ASG LYS A 92 22 E Strand -70.54 147.56 144.2 3VXV
ASG PHE A 93 23 E Strand -98.87 149.20 131.4 3VXV
ASG ASP A 94 24 E Strand -127.20 136.75 53.7 3VXV
ASG VAL A 95 25 E Strand -129.14 131.57 57.1 3VXV
ASG TYR A 96 26 E Strand -143.91 164.70 42.5 3VXV
ASG PHE A 97 27 E Strand -123.98 150.37 52.5 3VXV
ASG ILE A 98 28 E Strand -120.35 124.87 44.7 3VXV
ASG SER A 99 29 T Turn -75.49 168.85 5.1 3VXV
ASG PRO A 100 30 T Turn -62.32 -22.64 70.9 3VXV
ASG GLN A 101 31 T Turn -89.15 4.31 122.7 3VXV
ASG GLY A 102 32 T Turn 90.03 10.23 52.0 3VXV
ASG LEU A 103 33 C Coil -81.76 132.55 78.2 3VXV
ASG LYS A 104 34 E Strand -100.32 125.89 114.0 3VXV
ASG PHE A 105 35 E Strand -116.77 117.36 21.8 3VXV
ASG ARG A 106 36 C Coil -93.12 3.53 187.5 3VXV
ASG SER A 107 37 C Coil -152.03 154.81 55.1 3VXV
ASG LYS A 108 38 H AlphaHelix -70.58 -37.82 190.6 3VXV
ASG ARG A 109 39 H AlphaHelix -56.85 -48.04 220.9 3VXV
ASG SER A 110 40 H AlphaHelix -71.42 -41.56 45.3 3VXV
ASG LEU A 111 41 H AlphaHelix -60.19 -47.28 31.1 3VXV
ASG ALA A 112 42 H AlphaHelix -54.23 -48.21 50.7 3VXV
ASG ASN A 113 43 H AlphaHelix -57.90 -45.82 116.0 3VXV
ASG TYR A 114 44 H AlphaHelix -62.00 -40.99 40.4 3VXV
ASG LEU A 115 45 H AlphaHelix -64.66 -25.15 78.8 3VXV
ASG LEU A 116 46 H AlphaHelix -49.37 -49.12 140.8 3VXV
ASG LYS A 117 47 H AlphaHelix -105.77 -20.33 179.9 3VXV
ASG ASN A 118 48 H AlphaHelix -117.74 12.32 87.8 3VXV
ASG GLY A 119 49 H AlphaHelix -84.58 -15.54 43.4 3VXV
ASG GLU A 120 50 C Coil -74.84 141.39 140.4 3VXV
ASG THR A 121 51 C Coil -121.53 144.60 125.3 3VXV
ASG PHE A 122 52 C Coil -128.09 154.20 151.0 3VXV
ASG LEU A 123 53 C Coil -122.94 140.83 123.2 3VXV
ASG LYS A 124 54 C Coil -124.11 155.94 126.3 3VXV
ASG PRO A 125 55 G 310Helix -52.20 -37.07 118.6 3VXV
ASG GLU A 126 56 G 310Helix -67.09 -11.18 152.2 3VXV
ASG ASP A 127 57 G 310Helix -77.97 -11.21 85.1 3VXV
ASG PHE A 128 58 C Coil -115.39 121.59 117.3 3VXV
ASG ASN A 129 59 C Coil -92.41 103.69 127.7 3VXV
ASG PHE A 130 60 C Coil -87.70 16.70 190.9 3VXV
ASG THR A 131 61 C Coil -121.73 154.11 98.3 3VXV
ASG VAL A 132 62 C Coil -107.70 127.26 142.9 3VXV
ASG LEU A 133 63 C Coil -71.57 150.51 151.1 3VXV
ASG PRO A 134 64 C Coil -84.04 174.29 106.2 3VXV
ASG LYS A 135 65 C Coil 132.87 360.00 244.6 3VXV