Instructions: Enter a protein record in PDBSTR format or select from samples below. When done, click on the SUBMIT button. The script will extract individual data elements from your input. You can also use the CLEAR button to blank out the PROTEIN ENTRY input box.

PROTEIN ENTRY:

Sample Input (hypothetical entry designed to test all sections of PDBSTR):

MEMBER 1YIC_01 108 PROTEIN 1YIC 97/02/18 97/07/23 DEFINITION THE OXIDIZED SACCHAROMYCES CEREVISIAE ISO-1-CYTOCHROME C, NMR, 20 STRUCTURES MOL_ID: 1; MOLECULE: CYTOCHROME C, ISO-1; CHAIN: NULL; SYNONYM: FERRICYTOCHROME C; ENGINEERED: YES; MUTATION: C102S; OTHER_DETAILS: OXIDIZED FORM SOURCE MOL_ID: 1; ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; ORGANISM_COMMON: BAKER'S YEAST; EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE; EXPRESSION_SYSTEM_GENE: YEAST ISO-1-CYTOCHROME C MODEL 1 of 20 (TOTAL 20 MODELS) DEPOSITOR L.BANCI,I.BERTINI,K.L.BREN,H.B.GRAY,P.SOMPORNPISUT,P.TURANO RESOLUTION NOT APPLICABLE. FEATURES FROM TO DESCRIPTION HELIX 5 4 13 1 HELIX 1 50 55 2 HELIX 1 61 69 3 HELIX 5 71 75 4 HELIX 1 90 101 5 SEQUENCE TEFKAGSAKK GATLFKTRCL QCHTVEKGGP HKVGPNLHGI FGRHSGQAEG YSYTDANIKK NVLWDENNMS EYLTNPXKYI PGTKMAFGGL KKEKDRNDLI TYLKKASE STRUCTURE X-CA Y-CA Z-CA PHI PSI X-CB Y-CB Z-CB THR -5 11.30 14.96 6.14 -999 173 11.12 13.51 5.65 GLU -4 7.69 15.85 7.02 -999 112 7.44 17.37 7.03 PHE -3 4.81 13.42 6.58 -69 -70 4.59 12.15 7.43 LYS -2 2.08 15.51 8.25 60 143 2.08 16.96 7.76 ALA -1 -1.50 14.20 8.33 -66 -92 -2.40 14.20 9.57 GLY 1 -3.72 16.52 6.24 106 -133 -999.00 -999.00 -999.00 SER 2 -7.20 15.44 5.11 -143 103 -7.87 16.73 4.59 ALA 3 -8.05 11.87 3.94 -41 -78 -8.70 10.83 4.86 LYS 4 -11.22 12.66 1.86 30 -95 -11.51 14.17 1.85 LYS 5 -9.77 12.54 -1.71 -45 -46 -8.88 13.65 -2.29 GLY 6 -7.48 9.76 -0.40 -36 -40 -999.00 -999.00 -999.00 ALA 7 -10.64 7.57 -0.40 -57 -61 -11.98 7.91 0.26 THR 8 -11.44 7.99 -4.10 -60 -45 -12.13 9.17 -4.82 LEU 9 -7.68 8.04 -4.80 -45 -59 -6.72 8.92 -4.00 PHE 10 -7.35 4.59 -3.17 -52 -51 -7.68 4.21 -1.72 LYS 11 -10.54 3.48 -4.95 -60 -26 -11.93 4.03 -4.60 THR 12 -9.09 4.70 -8.31 -107 -5 -9.46 6.13 -8.72 ARG 13 -5.39 3.80 -7.58 -121 -68 -4.61 4.84 -6.77 CYS 14 -4.76 1.05 -5.04 -85 -51 -4.53 1.38 -3.60 LEU 15 -8.16 -0.70 -4.80 -49 -22 -9.39 0.19 -4.65 GLN 16 -7.72 -1.51 -8.49 -57 -39 -6.91 -0.60 -9.42 CYS 17 -5.31 -4.22 -7.30 -111 -25 -3.86 -3.93 -7.54 HIS 18 -5.95 -4.03 -3.50 -115 -171 -5.07 -2.98 -2.82 THR 19 -8.53 -3.32 -0.83 -160 168 -9.87 -4.08 -0.92 VAL 20 -8.26 -2.30 2.87 -117 39 -7.95 -0.82 3.13 GLU 21 -11.19 -4.58 3.84 -111 150 -12.29 -4.65 2.79 LYS 22 -11.40 -7.29 6.52 -60 -65 -12.41 -7.30 7.68 GLY 23 -12.46 -10.37 4.52 -84 38 -999.00 -999.00 -999.00 GLY 24 -10.81 -8.73 1.52 -74 143 -999.00 -999.00 -999.00 PRO 25 -9.59 -10.77 -1.48 -73 -166 -10.44 -10.85 -2.76 HIS 26 -6.11 -10.54 -3.02 -131 22 -5.29 -11.76 -2.56 LYS 27 -7.08 -9.61 -6.65 -4 -93 -7.79 -8.27 -6.90 VAL 28 -3.67 -8.58 -8.02 -93 -56 -3.37 -7.42 -8.98 GLY 29 -2.29 -7.22 -4.72 -105 155 -999.00 -999.00 -999.00 PRO 30 -2.94 -8.38 -1.15 -70 147 -1.77 -8.84 -0.29 ASN 31 -5.48 -6.73 1.14 -54 134 -6.63 -7.47 1.81 LEU 32 -3.82 -4.05 3.29 -107 29 -3.21 -2.82 2.58 HIS 33 -6.42 -4.26 6.12 -58 101 -7.51 -5.34 6.19 GLY 34 -4.44 -2.68 8.97 68 32 -999.00 -999.00 -999.00 ILE 35 -1.16 -3.08 7.01 -53 -43 -0.95 -2.78 5.51 PHE 36 0.12 -0.20 9.15 -49 99 -0.70 1.08 9.32 GLY 37 1.69 -2.17 12.02 136 -36 -999.00 -999.00 -999.00 ARG 38 3.03 -5.26 10.23 -92 -172 2.18 -6.33 9.53 HIS 39 6.09 -5.69 7.97 -112 172 7.27 -6.50 8.52 SER 40 6.46 -6.18 4.23 -73 85 7.39 -5.38 3.34 GLY 41 5.05 -9.58 3.61 133 76 -999.00 -999.00 -999.00 GLN 42 2.50 -10.76 6.16 -116 -71 2.15 -9.64 7.14 ALA 43 -1.07 -11.47 4.87 24 -139 -1.22 -11.63 3.35 GLU 44 -2.05 -15.12 5.47 -152 9 -3.16 -15.25 6.51 GLY 45 -2.50 -16.34 1.87 -147 -56 -999.00 -999.00 -999.00 TYR 46 -0.85 -14.09 -0.71 -43 -49 -0.66 -12.60 -0.46 SER 47 2.74 -15.26 -0.07 73 -15 2.83 -16.65 -0.71 TYR 48 4.12 -12.12 -1.87 61 -172 4.64 -11.38 -0.63 THR 49 7.46 -11.88 -3.79 -94 152 7.80 -10.73 -4.75 ASP 50 10.82 -12.96 -2.29 -53 -41 11.93 -13.79 -2.94 ALA 51 11.79 -9.29 -2.71 -55 -62 11.69 -8.47 -4.00 ASN 52 8.87 -7.79 -0.69 -55 -48 7.37 -7.75 -1.05 ILE 53 9.21 -10.56 1.95 -51 -66 9.11 -12.06 1.67 LYS 54 12.99 -10.38 2.30 -60 -25 13.98 -10.99 1.30 LYS 55 12.68 -6.56 2.36 -53 -40 11.71 -5.74 1.50 ASN 56 10.96 -6.84 5.81 40 46 11.75 -7.72 6.80 VAL 57 10.11 -3.10 5.59 -85 135 10.04 -2.39 4.23 LEU 58 7.73 -1.69 8.24 -77 145 8.23 -1.07 9.54 TRP 59 4.49 0.02 7.14 -99 102 3.36 -0.82 6.52 ASP 60 4.24 3.49 8.80 -127 158 5.45 4.01 9.58 GLU 61 2.77 6.78 7.46 -49 -31 2.04 7.83 8.30 ASN 62 6.39 7.86 6.86 -75 -67 7.43 8.08 7.96 ASN 63 7.92 4.73 5.27 -55 -50 8.25 3.44 6.04 MET 64 4.75 3.84 3.33 -46 -41 3.37 3.77 4.00 SER 65 4.98 7.33 1.79 -52 -65 5.17 8.67 2.52 GLU 66 8.34 6.85 -0.03 -51 -48 9.69 6.62 0.68 TYR 67 7.29 3.33 -0.92 -49 -54 6.82 2.28 0.07 LEU 68 4.11 4.66 -2.57 -67 -33 2.84 5.21 -1.92 THR 69 6.00 7.58 -4.11 -51 -39 7.02 8.58 -3.53 ASN 70 7.81 4.95 -6.12 -165 84 9.06 5.72 -6.56 PRO 71 7.32 1.34 -4.98 -74 -999 5.90 0.79 -4.92 LYS 73 12.25 1.43 -7.07 -999 -47 12.54 2.92 -7.31 TYR 74 11.91 1.03 -3.27 -56 -45 10.74 1.54 -2.40 ILE 75 11.31 -2.73 -3.66 -115 85 10.02 -3.30 -3.03 PRO 76 13.21 -3.88 -6.81 -68 87 14.70 -3.58 -7.00 GLY 77 11.12 -7.05 -7.32 141 -12 -999.00 -999.00 -999.00 THR 78 7.67 -6.19 -5.87 -57 152 7.23 -4.92 -5.13 LYS 79 4.84 -6.75 -8.38 -99 28 4.21 -8.10 -8.77 MET 80 3.49 -3.36 -7.43 -54 83 4.16 -2.41 -6.45 ALA 81 2.72 -2.57 -11.06 -79 46 2.06 -3.55 -12.05 PHE 82 1.63 0.83 -9.73 -104 144 1.38 0.88 -8.21 GLY 83 1.67 4.45 -10.80 -49 -50 -999.00 -999.00 -999.00 GLY 84 2.85 5.50 -7.33 97 171 -999.00 -999.00 -999.00 LEU 85 2.17 8.81 -5.51 -129 52 1.47 8.57 -4.17 LYS 86 4.92 11.22 -6.61 -71 61 5.92 10.92 -7.74 LYS 87 2.86 14.25 -5.56 -116 -122 1.33 14.20 -5.58 GLU 88 2.94 15.87 -2.07 -172 -49 3.38 17.29 -2.44 LYS 89 -0.73 16.27 -1.09 -93 -58 -1.54 17.52 -1.48 ASP 90 -2.48 13.34 -2.93 -44 -49 -2.32 13.02 -4.44 ARG 91 0.05 10.99 -1.31 -52 -56 1.57 11.13 -1.50 ASN 92 -0.60 12.33 2.22 -60 -49 -0.24 13.74 2.69 ASP 93 -4.38 12.32 1.60 -45 -47 -5.07 12.98 0.39 LEU 94 -3.95 8.60 0.76 -64 -55 -3.22 8.01 -0.44 ILE 95 -1.68 7.68 3.72 -50 -46 -0.29 8.26 4.04 THR 96 -4.15 9.42 6.07 -66 -45 -4.39 10.94 6.11 TYR 97 -7.12 7.82 4.25 -48 -52 -7.34 7.85 2.74 LEU 98 -5.60 4.38 4.87 -55 -49 -4.22 3.87 4.43 LYS 99 -5.15 5.31 8.53 -55 -37 -4.23 6.43 9.02 LYS 100 -8.85 6.33 8.61 -69 -49 -9.48 7.46 7.77 ALA 101 -10.07 3.26 6.68 -58 -45 -9.60 2.96 5.26 SER 102 -8.21 0.97 9.12 -165 97 -8.34 -0.49 8.69 GLU 103 -5.48 2.50 11.31 -43 -999 -5.85 3.21 12.63 //

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