REMARK SOURCE hebe.pdb HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 22-JAN-09 3FYB COMPND PROTEIN OF UNKNOWN FUNCTION (DUF1244); COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ALCANIVORAX BORKUMENSIS SK2; SOURCE 3 ORGANISM_TAXID: 393595; SOURCE 4 STRAIN: SK2 / ATCC 700651 / DSM 11573; SOURCE 5 GENE: ABO_0290; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODONPLUS RIPL; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: P15TVLIC; SOURCE 11 OTHER_DETAILS: DIGESTED WITH TEV TO REMOVE THE N-TERMINAL HIS TAG AUTHOR A.U.SINGER,E.EVDOKIMOVA,O.KAGAN,A.M.EDWARDS,A.JOACHIMIAK,A.SAVCHENKO, AUTHOR 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG) HET MSE A 1 8 HET MSE A 12 8 HET MSE A 36 8 HET MSE A 51 8 HET MSE A 73 8 HET MSE B 1 8 HET MSE B 12 8 HET MSE B 36 8 HET MSE B 51 8 HET MSE B 73 8 HET CL A 104 1 HET CL A 105 1 HET CA A 106 1 HET PEG A 107 14 HET EDO A 108 4 HET CL B 104 1 HET CA B 105 1 HET PEG B 106 7 SITE 1 AC1 3 ASN A 32 TRP A 78 GLN A 83 SITE 1 AC2 3 ASN A 32 ASN A 44 GLN A 83 SITE 1 AC3 1 VAL A 70 SITE 1 AC4 5 ALA A 15 ARG A 18 ARG A 22 HOH A 241 SITE 1 AC5 6 GLY A 65 TYR A 69 HOH A 192 HOH A 236 SITE 1 AC6 4 GLN B 31 ASN B 32 TRP B 78 GLN B 83 SITE 1 AC7 6 GLN A 57 LYS A 84 SER B 8 THR B 55 >GLY~A 0 28.44 40.08 5.19 28.38 40.24 4.37 28.41 40.16 4.78 1 0 11.31 -999 ? C4 PEG B 106 >MET?A 1 30.23 43.41 4.76 29.36 46.65 5.43 29.79 45.03 5.09 2 0 11.76 -999 ? CA CA B 105 >ALA~A 2 32.87 41.80 2.55 33.67 40.54 2.92 33.27 41.17 2.73 2 0 12.98 -999 ? CA CA B 105 >ASP~A 3 29.05 39.93 0.35 29.88 38.24 1.26 29.46 39.08 0.81 2 0 12.65 -999 ? C4 PEG B 106 >ILE~A 4 28.20 45.30 0.98 27.21 45.79 1.83 27.71 45.55 1.40 3 0 10.77 -999 ? O2 PEG B 106 >ASP~A 5 28.98 47.31 -4.27 27.37 48.61 -3.73 28.17 47.96 -4.00 2 0 13.38 -999 ? O2 PEG B 106 >GLN~A 6 34.54 50.29 -1.39 35.84 51.82 -2.02 35.19 51.05 -1.70 2 0 16.85 -999 ? CA CA B 105 >ALA~A 7 29.84 52.56 -2.93 29.24 52.90 -4.32 29.54 52.73 -3.62 2 0 14.54 -999 ? O4 APEG A 107 >SER~A 8 27.04 51.08 -0.74 25.57 49.74 -2.15 26.30 50.41 -1.45 2 0 11.74 -999 ? C1 PEG B 106 >LYS~A 9 29.47 50.37 2.14 34.67 49.24 4.77 32.07 49.81 3.46 2 0 9.94 -999 ? CA CA B 105 >THR~A 10 30.68 53.98 2.14 32.20 55.07 1.05 31.44 54.53 1.59 2 0 12.92 -999 ? O4 APEG A 107 >GLU~A 11 26.42 55.82 -0.25 26.01 57.91 -0.15 26.21 56.87 -0.20 2 0 8.20 -999 ? O4 APEG A 107 >MET?A 12 26.22 52.90 5.02 25.79 48.88 3.63 26.01 50.89 4.33 2 0 9.61 -999 ? C1 PEG B 106 >GLU~A 13 31.13 52.18 6.65 33.03 51.90 5.78 32.08 52.04 6.22 2 0 10.77 -999 ? CA CA B 105 >ALA~A 14 28.42 57.59 6.40 28.32 58.19 4.99 28.37 57.89 5.70 2 0 7.14 -999 ? C4 BPEG A 107 >ALA~A 15 24.70 57.02 7.34 23.72 56.08 6.61 24.21 56.55 6.97 2 0 -3.72 -999 ? O4 APEG A 107s >ALA~A 16 25.77 55.22 10.58 26.56 53.92 10.69 26.16 54.57 10.63 2 0 6.73 -999 ? O4 BPEG A 107 >PHE~A 17 29.96 59.81 11.36 31.31 61.88 12.69 30.64 60.84 12.03 3 0 9.61 -999 ? CA CA A 106 >ARG~A 18 24.66 62.08 7.25 24.48 59.88 5.10 24.57 60.98 6.18 2 0 -3.90 -999 ? C4 BPEG A 107s >HIS~A 19 21.56 56.40 13.64 19.93 55.53 14.61 20.74 55.96 14.13 3 0 5.70 -999 ? O4 BPEG A 107 >LEU~A 20 27.04 58.24 15.76 28.37 58.12 17.54 27.71 58.18 16.65 3 0 9.76 -999 ? O4 BPEG A 107 >LEU~A 21 25.87 63.35 14.26 28.02 63.78 13.91 26.95 63.57 14.08 3 0 4.73 -999 ? CA CA A 106 >ARG~A 22 19.37 62.11 12.80 20.46 59.83 11.03 19.92 60.97 11.91 2 0 -2.88 -999 ? O4 BPEG A 107s >HIS~A 23 22.70 58.20 20.25 22.50 57.31 22.14 22.60 57.75 21.20 3 0 11.38 -999 ? CA CA A 106 >LEU~A 24 25.93 62.66 20.30 27.54 61.26 20.92 26.74 61.96 20.61 3 0 8.34 -999 ? CA CA A 106 >ASP~A 25 22.07 65.98 18.36 20.99 67.79 18.28 21.53 66.89 18.32 2 0 4.61 -999 ? CA CA A 106 >GLU~A 26 18.00 63.01 19.38 17.50 61.43 18.07 17.75 62.22 18.72 2 0 9.04 -999 ? CA CA A 106 >HIS.A 27 21.01 60.62 24.41 19.62 59.12 23.94 20.31 59.87 24.18 3 0 12.37 -999 ? CA CA A 106 >LYS.A 28 22.82 66.57 25.33 20.01 69.01 21.34 21.41 67.79 23.34 2 0 7.90 -999 ? CA CA A 106 >ASP.A 29 21.72 64.78 29.73 21.21 62.86 28.87 21.47 63.82 29.30 2 0 10.25 -999 ? CL CL A 104 >VAL.A 30 25.67 63.01 27.95 25.79 61.11 26.80 25.73 62.06 27.38 3 0 7.50 -999 ? CL CL A 104 >GLN~A 31 28.09 66.21 31.01 28.75 66.82 32.94 28.42 66.52 31.98 2 0 5.80 -999 ? CL CL A 104 >ASN~A 32 32.69 66.29 26.10 31.70 66.88 24.30 32.20 66.59 25.20 2 0 4.03 -999 ? CL CL A 104s >ILE~A 33 34.35 65.55 31.21 34.69 65.95 32.44 34.52 65.75 31.82 3 0 7.03 -999 ? CL CL A 104 >ASP~A 34 30.73 61.29 31.19 30.31 62.16 33.07 30.52 61.72 32.13 2 0 8.43 -999 ? CL CL A 104 >LEU~A 35 32.24 60.84 25.95 30.23 60.75 25.09 31.23 60.80 25.52 3 0 8.00 -999 ? CL CL A 104 >MET?A 36 36.42 60.82 27.69 37.93 62.43 25.19 37.18 61.62 26.44 2 0 8.60 -999 ? CL CL A 105 >ILE~A 37 35.85 59.57 32.39 35.74 60.08 33.67 35.80 59.83 33.03 3 0 11.91 -999 ? CL CL A 104 >GLN~A 38 32.29 56.35 31.13 32.74 55.15 32.84 32.52 55.75 31.98 2 0 12.45 -999 ? CL CL B 104 >ALA~A 39 35.39 55.63 26.30 34.11 55.81 25.50 34.75 55.72 25.90 2 0 11.66 -999 ? CL CL B 104 >ASP~A 40 39.52 56.80 25.28 41.45 57.61 25.29 40.49 57.21 25.29 2 0 14.50 -999 ? CL CL A 105 >PHE.A 41 34.85 58.66 21.53 32.18 57.79 21.32 33.52 58.23 21.43 3 0 12.43 -999 ? CL CL A 104 >CYH~A 42 33.90 62.65 22.93 35.28 65.00 23.64 34.59 63.83 23.28 2 0 5.65 -999 ? CL CL A 105 >ARG~A 43 28.62 66.33 21.76 27.11 65.15 24.18 27.86 65.74 22.97 2 0 5.30 -999 ? CL CL A 104 >ASN~A 44 36.10 67.73 21.07 35.00 69.21 22.16 35.55 68.47 21.62 2 0 -3.79 -999 ? CL CL A 105s >CYH~A 45 37.19 63.94 18.87 38.05 62.89 21.28 37.62 63.42 20.08 2 0 9.35 -999 ? CL CL A 105 >LEU~A 46 33.05 63.04 16.38 32.08 61.30 17.23 32.57 62.17 16.80 3 0 10.27 -999 ? CA CA A 106 >ALA~A 47 35.11 66.74 14.93 34.82 68.05 15.68 34.97 67.39 15.30 2 0 9.30 -999 ? C1 EDO A 108 >LYS~A 48 38.92 66.17 14.89 43.06 63.66 18.48 40.99 64.92 16.69 2 0 13.19 -999 ? CL CL A 105 >TRP~A 49 39.53 61.49 15.34 37.37 58.85 17.29 38.45 60.17 16.31 3 0 14.04 -999 ? CA CA B 105 >LEU~A 50 35.06 65.54 10.59 33.01 64.68 10.46 34.04 65.11 10.53 3 0 8.73 -999 ? C1 EDO A 108 >MET?A 51 39.21 67.21 9.86 39.94 69.86 13.06 39.58 68.54 11.46 2 0 10.63 -999 ? O1 EDO A 108 >GLU~A 52 42.57 63.59 11.69 42.77 62.00 13.11 42.67 62.80 12.40 2 0 16.49 -999 ? CA CA B 105 >ALA~A 53 39.26 62.80 6.83 37.87 62.24 7.13 38.57 62.52 6.98 2 0 13.31 -999 ? O1 EDO A 108 >ALA~A 54 38.99 66.19 5.08 38.69 67.56 5.72 38.84 66.88 5.40 2 0 10.38 -999 ? O1 EDO A 108 >THR~A 55 42.83 65.99 4.55 44.59 66.55 5.69 43.71 66.27 5.12 2 0 15.80 -999 ? O1 EDO A 108 >GLU~A 56 42.75 60.85 5.09 41.91 59.19 6.07 42.33 60.02 5.58 2 0 15.60 -999 ? CA CA B 105 >GLN~A 57 37.77 62.67 1.67 38.16 60.92 0.52 37.97 61.80 1.10 2 0 -16.79 -999 ? O1 EDO A 108s >GLY~A 58 41.94 66.88 -0.33 41.21 66.89 0.08 41.58 66.88 -0.12 1 0 16.00 -999 ? O1 EDO A 108 >VAL.A 59 39.27 69.25 1.03 37.35 68.05 0.83 38.31 68.65 0.93 3 0 12.07 -999 ? O1 EDO A 108 >GLU.A 60 40.67 73.63 2.20 42.57 72.89 2.82 41.62 73.26 2.51 2 0 13.42 -999 ? O1 EDO A 108 >LEU.A 61 36.82 70.47 7.33 34.87 70.21 8.39 35.85 70.34 7.86 3 0 6.05 -999 ? O1 EDO A 108 >ASP~A 62 39.08 75.21 10.19 37.38 76.47 10.42 38.23 75.84 10.30 2 0 7.51 -999 ? O1 EDO A 108 >TYR~A 63 38.56 72.18 16.24 38.07 70.78 18.60 38.32 71.48 17.42 3 0 9.40 -999 ? CL CL A 105 >ASP~A 64 35.27 76.87 14.10 36.46 77.75 15.65 35.86 77.31 14.88 2 0 9.81 -999 ? O1 EDO A 108 >GLY~A 65 33.49 74.11 11.02 33.77 73.66 11.67 33.63 73.88 11.34 1 0 -3.49 -999 ? O1 EDO A 108s >ALA~A 66 33.88 70.47 12.10 35.19 69.75 12.35 34.54 70.11 12.23 2 0 6.58 -999 ? O1 EDO A 108 >ARG~A 67 34.50 71.49 18.71 35.67 73.37 20.79 35.09 72.43 19.75 2 0 6.11 -999 ? CL CL A 105 >GLU~A 68 28.22 75.06 12.85 28.28 76.96 11.95 28.25 76.01 12.40 2 0 4.43 -999 ? C2 EDO A 108 >TYR~A 69 28.96 68.30 10.27 27.93 65.93 9.26 28.44 67.12 9.76 3 0 -5.28 -999 ? O2 EDO A 108s >VAL~A 70 29.03 67.68 14.92 30.70 66.53 15.81 29.87 67.11 15.36 3 0 -6.15 -999 ? CA CA A 106s >TYR~A 71 28.89 70.42 19.19 30.86 69.48 20.99 29.88 69.95 20.09 3 0 7.07 -999 ? CL CL A 105 >GLY~A 72 24.49 71.16 15.02 25.01 71.64 15.43 24.75 71.40 15.23 1 0 4.23 -999 ? CA CA A 106 >MET?A 73 25.40 74.76 15.91 23.61 75.08 19.81 24.51 74.92 17.86 2 0 9.57 -999 ? CA CA A 106 >PRO~A 74 27.57 78.64 15.71 27.92 76.57 16.52 27.75 77.60 16.12 3 0 7.93 -999 ? C2 EDO A 108 >PHE~A 75 32.24 74.02 21.12 32.79 73.08 23.71 32.51 73.55 22.42 3 0 5.03 -999 ? CL CL A 105 >ALA~A 76 30.40 78.43 21.55 30.90 79.79 21.03 30.65 79.11 21.29 2 0 11.22 -999 ? CL CL A 105 >GLU~A 77 24.24 78.81 20.47 23.14 79.21 18.68 23.69 79.01 19.58 2 0 12.07 -999 ? C2 EDO A 108 >TRP~A 78 25.28 71.60 21.50 27.11 69.83 24.49 26.20 70.71 22.99 3 0 -6.12 -999 ? CL CL A 104s >LYS~A 79 28.69 75.41 25.42 34.26 77.27 27.78 31.47 76.34 26.60 2 0 7.44 -999 ? CL CL A 105 >THR~A 80 26.66 78.41 26.65 26.54 80.54 26.13 26.60 79.47 26.39 2 0 12.60 -999 ? CL CL A 104 >LEU~A 81 22.60 76.49 24.98 21.57 78.07 23.87 22.08 77.28 24.43 3 0 12.08 -999 ? CL CL A 104 >TYR~A 82 22.80 72.40 25.30 20.53 72.92 23.73 21.67 72.66 24.51 3 0 9.56 -999 ? CL CL A 104 >GLN~A 83 29.94 71.79 28.71 31.71 71.99 27.56 30.83 71.89 28.13 2 0 3.56 -999 ? CL CL A 105s >LYS.A 84 28.22 72.20 32.65 23.83 74.00 35.43 26.02 73.10 34.04 2 0 -11.38 -999 ? CL CL A 104s >PRO.A 85 31.27 74.20 35.22 31.13 72.53 33.70 31.20 73.36 34.46 3 0 8.71 -999 ? CL CL A 104 >ALA.A 86 33.43 69.18 35.23 34.79 68.68 34.89 34.11 68.93 35.06 2 0 9.01 -999 ? CL CL A 104 >SER~A 87 32.89 68.23 38.90 32.27 65.89 38.88 32.58 67.06 38.89 2 0 11.98 -999 ? CL CL A 104 >GLU~A 88 35.97 69.30 43.10 35.71 69.60 45.19 35.84 69.45 44.14 2 0 18.76 -999 ? CL CL A 104 >ALA~A 89 35.15 63.83 40.79 33.89 63.14 41.27 34.52 63.48 41.03 2 0 15.37 -999 ? CL CL A 104 >GLN~A 90 32.69 64.20 36.12 31.24 65.46 35.19 31.96 64.83 35.66 2 0 8.43 -999 ? CL CL A 104 >LEU~A 91 38.74 67.33 37.56 38.68 69.32 36.61 38.71 68.33 37.09 3 0 12.38 -999 ? CL CL A 105 >ALA~A 92 39.99 63.39 39.26 39.48 63.09 40.67 39.74 63.24 39.96 2 0 17.28 -999 ? CL CL A 104 >ALA~A 93 38.58 60.49 37.21 37.11 60.07 37.14 37.84 60.28 37.17 2 0 14.77 -999 ? CL CL A 104 >PHE~A 94 39.97 63.85 32.10 40.94 64.54 29.55 40.45 64.20 30.83 3 0 10.05 -999 ? CL CL A 105 >GLU~A 95 43.45 65.02 36.56 44.79 65.59 35.01 44.12 65.31 35.78 2 0 14.84 -999 ? CL CL A 105 >ALA~A 96 42.99 58.94 36.68 41.85 58.34 37.51 42.42 58.64 37.09 2 0 18.36 -999 ? CL CL A 105 >LYS~A 97 42.63 57.78 33.06 37.22 54.46 33.25 39.92 56.12 33.16 2 0 13.38 -999 ? CL CL B 104 >GLY~B 0 32.40 74.48 6.46 32.32 74.44 5.68 32.36 74.46 6.07 1 0 -3.34 -999 ? O1 EDO A 108s >MET?B 1 30.73 71.14 5.95 31.58 67.96 6.16 31.16 69.55 6.05 2 0 -5.99 -999 ? C1 EDO A 108s >ALA~B 2 27.96 72.62 3.78 26.90 73.62 4.20 27.43 73.12 3.99 2 0 5.24 -999 ? O2 EDO A 108 >ASP~B 3 31.65 75.00 1.84 30.61 76.53 2.82 31.13 75.76 2.33 2 0 7.05 -999 ? O1 EDO A 108 >ILE~B 4 32.81 69.61 1.89 33.93 68.95 2.62 33.37 69.28 2.25 3 0 8.35 -999 ? O1 EDO A 108 >ASP~B 5 31.92 68.12 -3.61 33.29 66.57 -3.20 32.60 67.35 -3.40 2 0 14.23 -999 ? O1 EDO A 108 >GLN~B 6 26.44 64.31 -1.44 25.99 64.76 0.59 26.22 64.54 -0.43 2 0 6.37 -999 ? O1 APEG A 107 >ALA~B 7 30.93 62.82 -2.43 31.49 62.50 -3.82 31.21 62.66 -3.12 2 0 13.21 -999 ? O1 APEG A 107 >SER~B 8 33.84 64.12 -0.26 35.44 65.42 -1.63 34.64 64.77 -0.94 2 0 -14.11 -999 ? O1 EDO A 108s >LYS~B 9 31.41 64.81 2.64 26.47 65.69 5.18 28.94 65.25 3.91 2 0 5.44 -999 ? C1 APEG A 107 >THR~B 10 30.06 61.24 2.44 28.60 60.21 1.28 29.33 60.72 1.86 2 0 8.46 -999 ? O1 APEG A 107 >GLU~B 11 34.39 59.57 -0.11 34.72 57.47 -0.18 34.55 58.52 -0.15 2 0 15.23 -999 ? O1 APEG A 107 >MET?B 12 34.52 61.98 5.41 35.16 65.97 4.29 34.84 63.98 4.85 2 0 9.82 -999 ? O1 EDO A 108 >GLU~B 13 29.67 62.43 7.07 27.83 62.87 6.12 28.75 62.65 6.60 2 0 6.40 -999 ? C1 APEG A 107 >ALA~B 14 32.36 57.13 6.47 32.35 56.55 5.06 32.36 56.84 5.77 2 0 11.17 -999 ? C4 BPEG A 107 >ALA~B 15 36.02 57.65 7.41 36.98 58.65 6.80 36.50 58.15 7.11 2 0 14.16 -999 ? CA CA B 105 >ALA~B 16 35.01 59.08 10.78 34.28 60.38 11.04 34.64 59.73 10.91 2 0 12.85 -999 ? C4 BPEG A 107 >PHE~B 17 30.78 54.48 11.20 29.43 52.33 12.32 30.11 53.40 11.76 3 0 10.10 -999 ? O4 BPEG A 107 >ARG~B 18 36.12 52.60 6.78 36.30 55.03 4.88 36.21 53.81 5.83 2 0 12.52 -999 ? CA CA B 105 >HIS~B 19 39.39 57.74 13.42 41.03 58.50 14.50 40.21 58.12 13.96 3 0 12.04 -999 ? CA CA B 105 >LEU~B 20 33.90 55.74 15.82 32.60 55.83 17.64 33.25 55.78 16.73 3 0 10.75 -999 ? CA CA B 105 >LEU~B 21 34.93 50.67 13.78 32.82 50.34 13.32 33.87 50.50 13.55 3 0 5.55 -999 ? CA CA B 105 >ARG~B 22 41.34 51.97 12.18 40.38 54.39 10.57 40.86 53.18 11.37 2 0 9.10 -999 ? CA CA B 105 >HIS~B 23 38.54 55.43 19.88 38.78 56.12 21.84 38.66 55.78 20.86 3 0 11.78 -999 ? CA CA B 105 >LEU~B 24 35.15 50.87 19.77 33.59 52.27 20.56 34.37 51.57 20.17 3 0 8.79 -999 ? CA CA B 105 >ASP~B 25 38.90 47.72 17.49 40.00 45.96 17.30 39.45 46.84 17.40 2 0 4.25 -999 ? CA CA B 105 >GLU~B 26 43.31 50.69 18.89 43.45 52.22 17.41 43.38 51.46 18.15 2 0 9.03 -999 ? CA CA B 105 >HIS.B 27 39.96 52.54 23.98 41.31 54.12 23.69 40.63 53.33 23.84 3 0 12.56 -999 ? CA CA B 105 >LYS.B 28 38.36 46.52 24.29 41.19 44.51 20.23 39.78 45.52 22.26 2 0 7.58 -999 ? CA CA B 105 >ASP.B 29 39.59 47.98 28.82 41.32 46.80 28.94 40.45 47.39 28.88 2 0 10.56 -999 ? CL CL B 104 >VAL.B 30 35.57 49.71 27.51 35.54 51.77 26.69 35.55 50.74 27.10 3 0 7.54 -999 ? CL CL B 104 >GLN~B 31 33.18 46.42 30.44 32.85 46.50 32.53 33.01 46.46 31.48 2 0 -6.54 -999 ? CL CL B 104s >ASN~B 32 28.58 46.71 25.41 29.40 46.30 23.48 28.99 46.51 24.44 2 0 -3.97 -999 ? CL CL B 104s >ILE~B 33 27.40 47.32 30.80 27.17 46.99 32.08 27.28 47.15 31.44 3 0 6.90 -999 ? CL CL B 104 >ASP~B 34 31.09 51.34 30.67 31.55 50.35 32.47 31.32 50.85 31.57 2 0 8.35 -999 ? CL CL B 104 >LEU~B 35 29.26 52.18 25.62 31.16 52.38 24.56 30.21 52.28 25.09 3 0 7.94 -999 ? CL CL B 104 >MET?B 36 25.15 52.18 27.54 23.37 50.83 25.01 24.26 51.51 26.28 2 0 10.24 -999 ? CL CL B 104 >ILE~B 37 26.21 53.24 32.17 26.45 52.68 33.41 26.33 52.96 32.79 3 0 11.64 -999 ? CL CL B 104 >GLN~B 38 29.48 56.48 31.31 28.88 57.77 32.90 29.18 57.13 32.11 2 0 11.98 -999 ? CL CL A 104 >ALA~B 39 26.34 57.37 26.30 27.53 57.04 25.41 26.93 57.21 25.85 2 0 11.76 -999 ? CL CL A 104 >ASP~B 40 22.00 56.49 25.68 20.06 55.70 25.97 21.03 56.09 25.82 2 0 15.85 -999 ? CL CL B 104 >PHE.B 41 26.27 54.80 21.43 28.92 55.79 21.16 27.59 55.30 21.29 3 0 12.51 -999 ? CL CL B 104 >CYH~B 42 27.25 50.67 22.51 25.89 48.27 23.09 26.57 49.47 22.80 2 0 7.40 -999 ? CL CL B 104 >ARG~B 43 32.34 47.06 20.90 33.92 48.08 23.41 33.13 47.57 22.16 2 0 5.37 -999 ? CL CL B 104 >ASN~B 44 24.86 45.75 20.31 25.95 44.15 21.19 25.41 44.95 20.75 2 0 7.54 -999 ? CL CL B 104 >CYH~B 45 23.90 49.88 18.56 23.05 50.65 21.04 23.48 50.26 19.80 2 0 11.62 -999 ? CL CL B 104 >LEU~B 46 28.01 50.89 16.14 29.01 52.67 16.98 28.51 51.78 16.56 3 0 10.89 -999 ? CA CA B 105 >ALA~B 47 25.83 47.38 14.30 26.12 46.02 14.96 25.98 46.70 14.63 2 0 11.51 -999 ? CA CA B 105 >LYS~B 48 22.02 47.96 14.36 21.02 46.08 19.39 21.52 47.02 16.88 2 0 12.59 -999 ? CL CL B 104 >TRP~B 49 21.50 52.62 15.26 23.77 55.04 17.40 22.64 53.83 16.33 3 0 8.62 -999 ? O4 BPEG A 107 >LEU~B 50 25.91 48.95 10.20 27.90 49.61 9.79 26.91 49.28 9.99 3 0 10.41 -999 ? O4 BPEG A 107 >MET?B 51 21.79 47.26 9.48 20.68 44.31 12.28 21.24 45.79 10.88 2 0 8.58 -999 ? C2 PEG B 106 >GLU~B 52 18.40 50.69 11.41 18.34 52.07 13.03 18.37 51.38 12.22 2 0 8.08 -999 ? O4 BPEG A 107 >ALA~B 53 21.80 51.88 6.63 23.20 52.32 7.01 22.50 52.10 6.82 2 0 6.40 -999 ? O4 BPEG A 107 >ALA~B 54 22.08 48.66 4.56 22.41 47.25 5.11 22.24 47.96 4.84 2 0 5.89 -999 ? C1 PEG B 106 >THR~B 55 18.21 48.76 4.11 16.50 48.26 5.37 17.36 48.51 4.74 2 0 -3.35 -999 ? O1 PEG B 106s >GLU~B 56 18.44 54.08 4.88 19.44 55.56 6.05 18.94 54.82 5.47 2 0 -3.15 -999 ? O4 APEG A 107s >GLN~B 57 23.07 52.40 1.41 23.06 54.07 0.05 23.07 53.23 0.73 2 0 7.84 -999 ? O4 APEG A 107 >GLY.B 58 19.04 48.33 -1.06 19.74 48.24 -0.61 19.39 48.28 -0.83 1 0 6.70 -999 ? C1 PEG B 106 >VAL.B 59 21.44 45.68 0.33 23.37 46.71 -0.01 22.41 46.19 0.16 3 0 6.69 -999 ? O2 PEG B 106 >GLU.B 60 20.98 40.43 3.94 19.45 40.77 5.37 20.21 40.60 4.65 2 0 -3.51 -999 ? C2 PEG B 106s >LEU.B 61 24.21 44.40 6.45 26.15 44.45 7.43 25.18 44.42 6.94 3 0 8.35 -999 ? C2 PEG B 106 >ASP~B 62 21.77 39.40 8.82 23.48 38.12 8.96 22.63 38.76 8.89 2 0 8.84 -999 ? O4 PEG B 106 >TYR~B 63 22.26 41.76 15.13 22.83 42.94 17.61 22.54 42.35 16.37 3 0 13.07 -999 ? C2 PEG B 106 >ASP~B 64 25.60 37.35 12.70 24.31 36.38 14.06 24.96 36.87 13.38 2 0 13.60 -999 ? O4 PEG B 106 >GLY~B 65 27.18 40.34 9.70 26.96 40.71 10.45 27.07 40.53 10.08 1 0 11.61 -999 ? C2 PEG B 106 >ALA~B 66 26.92 43.86 11.15 25.64 44.63 11.46 26.28 44.24 11.31 2 0 10.98 -999 ? C2 PEG B 106 >ARG~B 67 26.46 42.12 17.61 25.16 40.10 19.50 25.81 41.11 18.55 2 0 10.31 -999 ? CL CL B 104 >GLU~B 68 32.67 39.18 11.48 32.64 37.38 10.38 32.65 38.28 10.93 2 0 10.83 -999 ? CA CA B 105 >TYR~B 69 31.89 46.13 9.43 32.84 48.64 8.70 32.36 47.38 9.06 3 0 7.14 -999 ? CA CA B 105 >VAL~B 70 31.90 46.42 14.04 30.20 47.44 15.09 31.05 46.93 14.57 3 0 6.59 -999 ? CA CA B 105 >TYR~B 71 31.98 43.30 18.09 30.01 44.05 19.95 30.99 43.68 19.02 3 0 7.52 -999 ? CL CL B 104 >GLY~B 72 36.32 42.81 13.85 35.81 42.35 14.23 36.06 42.58 14.04 1 0 3.78 -999 ? CA CA B 105 >MET?B 73 35.45 39.17 14.54 37.30 38.64 18.35 36.37 38.91 16.45 2 0 8.96 -999 ? CA CA B 105 >PRO~B 74 33.27 35.38 13.95 32.94 37.34 14.95 33.10 36.36 14.45 3 0 10.98 -999 ? CA CA B 105 >PHE~B 75 28.68 39.47 19.75 28.02 40.20 22.37 28.35 39.84 21.06 3 0 7.76 -999 ? CL CL B 104 >ALA~B 76 30.43 34.97 19.85 30.08 33.67 19.14 30.25 34.32 19.50 2 0 13.18 -999 ? CL CL B 104 >GLU~B 77 36.56 35.01 18.65 37.70 34.05 17.13 37.13 34.53 17.89 2 0 12.76 -999 ? CA CA B 105 >TRP~B 78 35.51 41.82 20.26 33.69 43.41 23.36 34.60 42.62 21.81 3 0 -6.03 -999 ? CL CL B 104s >LYS~B 79 32.08 37.77 23.94 26.45 36.23 26.08 29.26 37.00 25.01 2 0 9.64 -999 ? CL CL B 104 >THR~B 80 34.21 34.79 25.11 34.24 33.20 23.59 34.22 34.00 24.35 2 0 12.06 -999 ? CL CL B 104 >LEU~B 81 38.28 36.89 23.50 39.33 35.37 22.29 38.81 36.13 22.90 3 0 11.83 -999 ? CL CL B 104 >TYR~B 82 37.89 41.09 23.97 40.17 40.66 22.40 39.03 40.87 23.19 3 0 9.17 -999 ? CL CL B 104 >GLN~B 83 30.76 41.08 27.58 29.07 41.12 26.29 29.92 41.10 26.93 2 0 -4.09 -999 ? CL CL B 104s >PRO.B 85 30.97 38.00 34.57 30.67 39.98 33.47 30.82 38.99 34.02 3 0 9.37 -999 ? CL CL B 104 >ALA.B 86 28.74 43.54 34.97 27.45 44.21 34.53 28.09 43.88 34.75 2 0 8.93 -999 ? CL CL B 104 >SER.B 87 29.93 44.54 38.47 30.83 46.80 38.35 30.38 45.67 38.41 2 0 12.09 -999 ? CL CL B 104