S 3
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200 400 600 800 1000 1200 1400 0 5 10 15 20 25 30 35 40 45 50 55 60 65 70 75 80 85 90 95 100 R elative abundance m/z y4 y5 y7 y11++ y8 y9 y10 y11 b3 b4 b5 b8 b10 b11 # b b* b 0 Seq. y y* y 0 # 1 70.03 52.02 S@ 14 2 183.11 165.1 L 1474.74 1457.71 1456.73 13 3 311.21 294.18 293.2 K 1361.65 1344.63 1343.64 12 4 408.26 391.23 390.25 P 1233.56 1216.53 1215.55 11 5 523.29 506.26 505.28 D 1136.51 1119.48 1118.5 10 6 624.34 607.31 606.32 T 1021.48 1004.45 1003.47 9 7 753.38 736.35 735.37 E 920.43 903.41 902.42 8 8 867.42 850.39 849.41 N 791.39 774.36 773.38 7 9 995.48 978.45 977.47 Q 677.35 660.32 659.34 6 10 1124.52 1107.5 1106.51 E 549.29 532.26 531.28 5 11 1211.55 1194.53 1193.54 S 420.25 403.22 402.23 4 12 1298.59 1281.56 1280.58 S 333.21 316.19 315.2 3 13 1397.65 1380.63 1379.64 V 246.18 229.15 2 14 K 147.11 130.09 1 S 3.1 Positive ionization low energy CID fragmentation spectrum of the singly phosphorylated peptide pSLKPDTENQESSVK of Rec 10 MS 3 spectrum of the doubly charged peptide at 772.38 Da. The position of the dehydro-alanine generated by the loss of phosphoric acid from the phosphorylated serine residue (S503) was labeled with “@”. Identified b and y fragment ions detected in the measurement are colored in the fragmentation table and labeled respectively blue and red in the spectrum. Identified satellite ions originating from the loss of water (b0 or y0 ions) or ammonia (b* or y* ions) are also labeled in the table. 400 600 800 1000 1200 1400 1600 0 5 10 15 20 25 30 35 40 45 50 55 60 65 70 75 80 85 90 95 100 1513.77 R elative abundance y6 y7 y8 y9 y2 y11 y12 y11++ y11-98++ y11-98 b3 b5 b8 b10 b11 b13 b13-98 [M+2H-H PO ] 3 4 2+ [M+2H-H PO -H O] 3 4 2 2+ m/z # b b* b 0 Seq. y y* y 0 # 1 88.04 70.03 S 14 2 201.12 183.11 L 1554.7 1537.68 1536.69 13 3 329.22 312.19 311.21 K 1441.62 1424.59 1423.61 12 4 426.27 409.24 408.26 P 1313.53 1296.5 1295.52 11 5 541.3 524.27 523.29 D 1216.47 1199.45 1198.46 10 6 642.35 625.32 624.34 T 1101.45 1084.42 1083.44 9 7 771.39 754.36 753.38 E 1000.4 983.37 982.39 8 8 885.43 868.4 867.42 N 871.36 854.33 853.35 7 9 1013.49 996.46 995.48 Q 757.31 740.29 739.3 6 10 1142.53 1125.51 1124.52 E 629.25 612.23 611.24 5 11 1229.56 1212.54 1211.55 S 500.21 483.19 482.2 4 12 1396.56 1379.54 1378.55 S# 413.18 396.15 395.17 3 13 1495.63 1478.6 1477.62 V 246.18 229.15 2 14 K 147.11 130.09 1 S 3.2 Positive ionization low energy CID fragmentation spectrum of the singly phosphorylated peptide SLKPDTENQESpSVK of Rec 10 MS 2 spectrum of the doubly charged peptide at m/z 821.67 Da. The position of the phosphorylated serine residue (S513) was labeled with “#”. Identified b and y fragment ions detected in the measurement are colored in the fragmentation table and labeled respectively blue and red in the spectrum. Identified satellite ions originating from the loss of water (b0 or y0 ions) or ammonia (b* or y* ions) are also labeled in the table. Because of the low intensity of y3 and y4 fragment ions, the modification could not be unambiguously assigned toS511 or S512. The intensity of the MS 3 spectrum was low and the identified fragment ions did not provide S 3
description
S 3. S 3.1 Positive ionization low energy CID fragmentation spectrum of the singly phosphorylated peptide pSLKPDTENQESSVK of Rec 10 - PowerPoint PPT Presentation
Transcript of S 3
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# b b* b0 Seq. y y* y0 #1 70.03 52.02 S@ 142 183.11 165.1 L 1474.74 1457.71 1456.73 133 311.21 294.18 293.2 K 1361.65 1344.63 1343.64 124 408.26 391.23 390.25 P 1233.56 1216.53 1215.55 115 523.29 506.26 505.28 D 1136.51 1119.48 1118.5 106 624.34 607.31 606.32 T 1021.48 1004.45 1003.47 97 753.38 736.35 735.37 E 920.43 903.41 902.42 88 867.42 850.39 849.41 N 791.39 774.36 773.38 79 995.48 978.45 977.47 Q 677.35 660.32 659.34 6
10 1124.52 1107.5 1106.51 E 549.29 532.26 531.28 511 1211.55 1194.53 1193.54 S 420.25 403.22 402.23 412 1298.59 1281.56 1280.58 S 333.21 316.19 315.2 313 1397.65 1380.63 1379.64 V 246.18 229.15 214 K 147.11 130.09 1
S 3.1 Positive ionization low energy CID fragmentation spectrum of the singly phosphorylated peptide pSLKPDTENQESSVK of Rec 10MS3 spectrum of the doubly charged peptide at 772.38 Da. The position of the dehydro-alanine generated by the loss of phosphoric acid from the phosphorylated serine residue (S503) was labeled with “@”. Identified b and y fragment ions detected in the measurement are colored in the fragmentation table and labeled respectively blue and red in the spectrum. Identified satellite ions originating from the loss of water (b0 or y0 ions) or ammonia (b* or y* ions) are also labeled in the table.
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[M+2H-HPO ]3 42+
[M+2H-HPO -HO]3 4 22+
m/z
# b b* b0 Seq. y y* y0 #1 88.04 70.03 S 142 201.12 183.11 L 1554.7 1537.68 1536.69 133 329.22 312.19 311.21 K 1441.62 1424.59 1423.61 124 426.27 409.24 408.26 P 1313.53 1296.5 1295.52 115 541.3 524.27 523.29 D 1216.47 1199.45 1198.46 106 642.35 625.32 624.34 T 1101.45 1084.42 1083.44 97 771.39 754.36 753.38 E 1000.4 983.37 982.39 88 885.43 868.4 867.42 N 871.36 854.33 853.35 79 1013.49 996.46 995.48 Q 757.31 740.29 739.3 6
10 1142.53 1125.51 1124.52 E 629.25 612.23 611.24 511 1229.56 1212.54 1211.55 S 500.21 483.19 482.2 412 1396.56 1379.54 1378.55 S# 413.18 396.15 395.17 313 1495.63 1478.6 1477.62 V 246.18 229.15 214 K 147.11 130.09 1
S 3.2 Positive ionization low energy CID fragmentation spectrum of the singly phosphorylated peptide SLKPDTENQESpSVK of Rec 10MS2 spectrum of the doubly charged peptide at m/z 821.67 Da. The position of the phosphorylated serine residue (S513) was labeled with “#”. Identified b and y fragment ions detected in the measurement are colored in the fragmentation table and labeled respectively blue and red in the spectrum. Identified satellite ions originating from the loss of water (b0 or y0 ions) or ammonia (b* or y* ions) are also labeled in the table. Because of the low intensity of y3 and y4 fragment ions, the modification could not be unambiguously assigned toS511 or S512. The intensity of the MS3 spectrum was low and the identified fragment ions did not provide additional information.
S 3
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S 3.3 Positive ionization low energy CID fragmentation spectrum of the singly phosphorylated peptide AKSNVNLQYpSPK of Rec 10MS3 spectrum of the doubly charged peptide at m/z 665.94 Da. The position of the dehydro-alanine generated by the loss of phosphoric acid from the phosphorylated serine (S529) residue was labeled with “@”. Identified b and y fragment ions detected in the measurement are colored in the fragmentation table and labeled respectively blue and red in the spectrum. Identified satellite ions originating from the loss of water (b0 or y0 ions) or ammonia (b* or y* ions) are also labeled in the table.
# b b* b0 Seq. y y* y0 #1 72.04 A 122 200.14 183.11 K 1259.67 1242.65 1241.66 113 287.17 270.14 269.16 S 1131.58 1114.55 1113.57 104 401.21 384.19 383.2 N 1044.55 1027.52 1026.54 95 500.28 483.26 482.27 V 930.5 913.48 912.49 86 614.33 597.3 596.32 N 831.44 814.41 813.43 77 727.41 710.38 709.4 L 717.39 700.37 699.38 68 855.47 838.44 837.46 Q 604.31 587.28 586.3 59 1018.53 1001.51 1000.52 Y 476.25 459.22 458.24 4
10 1087.55 1070.53 1069.54 S@ 313.19 296.16 295.18 311 1184.61 1167.58 1166.6 P 244.17 227.14 212 K 147.11 130.09 1
S 3.4 Positive ionization low energy CID fragmentation spectrum of the singly phosphorylated peptide NRpSIIQIK of Rec 10MS3 spectrum of the doubly charged peptide at m/z 477.46 Da. The position of the dehydro-alanine generated by the loss of phosphoric acid from the phosphorylated serine (S356) residue was labeled with “@”. The MS3 spectrum showed an intensive fragment ion at m/z 468.96 Da. This can be interpreted as the loss of ammonia from the arginine residue after the loss of phosphoric acid from the phosphoserine residue. Identified b and y fragment ions detected in the measurement are colored in the fragmentation table and labeled respectively blue and red in the spectrum. Identified satellite ions originating from the loss of water (b0 or y0 ions) or ammonia (b* or y* ions) are also labeled in the table.
# b b* b0 Seq. y y* y0 #1 115.05 98.02 N 82 271.15 254.12 R 839.55 822.52 821.54 73 340.17 323.15 322.16 S@ 683.45 666.42 665.43 64 453.26 436.23 435.25 I 614.42 597.4 55 566.34 549.31 548.33 I 501.34 484.31 46 694.4 677.37 676.39 Q 388.26 371.23 37 807.48 790.46 789.47 I 260.2 243.17 28 K 147.11 130.09 1
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[M+2H-HPO -NH]3 4 32+
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S 3.5 Positive ionization low energy CID fragmentation spectrum of the singly phosphorylated peptide SNVNLQYpSPK of Rec 10MS3 spectrum of the doubly charged peptide at m/z 566.32 Da. The position of the dehydro-alanine generated by the loss of phosphoric acid from the phosphorylated serine residue (S529) was labeled with “@”. The loss of water from the unphosphorylated serine residue generated an intensive fragment ion, which is also labeled. Identified b and y fragment ions detected in the measurement are colored in the fragmentation table and labeled respectively blue and red in the spectrum. Identified satellite ions originating from the loss of water (b0 or y0 ions) or ammonia (b* or y* ions) are also labeled in the table.
# b b* b0 Seq. y y* y0 #
1 88.04 70.03 S 102 202.08 185.06 184.07 N 1044.6 1027.52 1026.54 93 301.15 284.12 283.14 V 930.5 913.48 912.49 84 415.19 398.17 397.18 N 831.44 814.41 813.43 75 528.28 511.25 510.27 L 717.39 700.37 699.38 66 656.34 639.31 638.33 Q 604.31 587.28 586.3 57 819.40 802.37 801.39 Y 476.25 459.22 458.24 48 888.42 871.39 870.41 S@ 313.19 296.16 295.18 39 985.47 968.45 967.46 P 244.17 227.14 2
10 K 147.11 130.09 1
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S 3.6 Positive ionization low energy CID fragmentation spectrum of the singly phosphorylated peptide DSLpSADDYAYDTK of Rec 10MS3 spectrum of the doubly charged peptide at m/z 723.23 Da. The position of the dehydro-alanine generated by the loss of phosphoric acid from the phosphorylated serine (S424) residue was labeled with “@”. Identified b and y fragment ions detected in the measurement are colored in the fragmentation table and labeled respectively blue and red in the spectrum. Identified satellite ions originating from the loss of water (b0 or y0 ions) or ammonia (b* or y* ions) are also labeled in the table.
# b b0 Seq. y y* y0 #
1 116.03 98.02 D 132 203.07 185.06 S 1330.58 1313.55 1312.57 123 316.15 298.14 L 1243.55 1226.52 1225.54 114 385.17 367.16 S@ 1130.46 1113.44 1112.45 105 456.21 438.20 A 1061.44 1044.42 1043.43 96 571.24 553.23 D 990.41 973.38 972.39 87 686.26 668.25 D 875.38 858.35 857.37 78 849.33 831.32 Y 760.35 743.32 742.34 69 920.36 902.35 A 597.29 580.26 579.28 5
10 1083.43 1065.42 Y 526.25 509.22 508.24 411 1198.45 1180.44 D 363.19 346.16 345.18 312 1299.50 1281.49 T 248.16 231.13 230.15 213 K 147.11 130.09 1
# b b0 Seq. y y* y0 #
1 114.09 L 102 227.18 L 1017.57 1000.55 999.56 93 324.23 P 904.49 887.46 886.48 84 395.27 A 807.44 790.41 789.43 75 508.35 I 736.40 719.37 718.39 66 621.43 I 623.32 606.29 605.31 57 720.50 V 510.23 493.21 492.22 48 887.50 869.49 S# 411.16 394.14 393.15 39 984.55 966.54 P 244.17 227.14 2
10 K 147.11 130.09 1
y2
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y6
y8
y8++
y7b2
b7b8
b5
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[M+2H-HPO ]3 42+
S 3.7 Positive ionization low energy CID fragmentation spectrum of the singly phosphorylated peptide LLPAIIVpSPK of Rec 10MS2 spectrum of the doubly charged peptide at m/z 566.12 Da. The fragment ion generated by the loss of phosphoric acid from the phosphoserine residue (S347) was labeled in the spectrum. The intensity of this fragment was not among the 3 most intensive ones due to the strong fragmentation at the proline residues, thus no MS3 spectrum was generated. Identified b and y fragment ions detected in the measurement are colored in the fragmentation table and labeled respectively blue and red in the spectrum. The position of the phosphoserine residue was labeled with “#”. Identified satellite ions originating from the loss of water (b0 or y0 ions) or ammonia (y* ions) are also labeled in the table.
# b b++ b+++ Seq. y y++ y+++ #
1 116.03 58.52 39.35 D 202 245.08 123.04 82.36 E 2146.23 1073.62 716.08 193 359.12 180.06 120.38 N 2017.19 1009.10 673.07 184 458.19 229.60 153.40 V 1903.15 952.08 635.05 175 571.27 286.14 191.10 I 1804.08 902.54 602.03 166 685.32 343.16 229.11 N 1690.99 846.00 564.34 157 813.37 407.19 271.80 Q 1576.95 788.98 526.32 148 914.42 457.71 305.48 T 1448.89 724.95 483.64 139 971.44 486.23 324.49 G 1347.84 674.43 449.95 12
10 1068.50 534.75 356.84 P 1290.82 645.91 430.95 1111 1139.53 570.27 380.52 A 1193.77 597.39 398.59 1012 1267.63 634.32 423.21 K 1122.73 561.87 374.92 913 1395.72 698.36 465.91 K 994.64 497.82 332.22 814 1478.77 739.89 493.59 T@ 866.54 433.77 289.52 715 1575.82 788.42 525.95 P 783.49 392.25 261.84 616 1674.89 837.95 558.97 V 686.44 343.72 229.49 517 1802.95 901.98 601.65 Q 587.37 294.19 196.46 418 1959.05 980.03 653.69 R 459.32 230.16 153.78 319 2115.15 1058.08 705.72 R 303.21 152.11 101.74 220 K 147.11 74.06 49.71 1
S 3.8 Positive ionization low energy CID fragmentation spectrum of the singly phosphorylated peptide DENVINQTGPAKKpTPVQRRK of Rec 10MS3 spectrum of the triply charged peptide at m/z 754.78 Da. The position of the dehydro-aminobutyric acid generated by the loss of phosphoric acid from the phosphorylated threonine (T482) residue was labeled with “@”. Identified b and y fragment ions detected in the measurement are colored in the fragmentation table and labeled respectively blue and red in the spectrum. This peptide was generated by AspN digest and contained several basic amino acids. Because of this reason several doubly or triply charged fragment ions could be detected.
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# b b* b0 Seq. y y* y0 #
1 100.08 V 72 213.16 I 865.48 848.45 847.47 63 455.30 438.27 K^ 752.39 735.37 734.38 54 584.34 567.31 566.33 E 510.26 493.23 492.25 45 731.41 714.38 713.4 F 381.21 364.19 363.20 36 818.44 801.41 800.43 S 234.14 217.12 216.13 27 K 147.11 130.09 1
S 3.9 Positive ionization low energy CID fragmentation spectrum of the ubiquitinylated peptide VIKEFSK of Rec 10MS2 spectrum of the doubly charged peptide at m/z 482.8 Da. Identified b and y fragment ions detected in the measurement are colored in the fragmentation table and labeled respectively blue and red in the spectrum. The position of the modified residue (K757) was labeled with “^”. Identified satellite ions originating from the loss of water (b0 or y0 ions) or ammonia (y* ions) are also labeled in the table.
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S 3.10 Positive ionization low energy CID fragmentation spectrum of the ubiquitinylated peptide SSVWKELLKE of Rec10MS2 spectrum of the doubly charged peptide at m/z Da. Identified b and y fragment ions detected in the measurement are colored in the fragmentation table and labeled respectively blue and red in the spectrum. The position of the modified residue (K604) was labeled with “^”. Identified satellite ions originating from the loss of water (b0 or y0 ions) or ammonia (y* ions) are also labeled in the table.
# b b* b0 Seq. y y* y0 #1 88.04 70.03 S 92 175.07 157.06 S 1116.64 1099.61 1098.63 83 274.14 256.13 V 1029.61 1012.58 1011.6 74 460.22 442.21 W 930.54 913.51 912.53 65 702.36 685.33 684.35 K^ 744.46 727.43 726.45 56 831.40 814.37 813.39 E 502.32 485.30 484.31 47 944.48 927.46 926.47 L 373.28 356.25 38 1057.6 1040.5 1039.56 L 260.20 243.17 29 K 147.11 130.09 1
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1 115.05 58.03 98.02 49.52 N 182 244.09 122.55 227.07 114.04 226.08 113.54 E 1950.95 975.98 1933.93 967.47 1932.94 966.97 173 315.13 158.07 298.10 149.56 297.12 149.06 A 1821.91 911.46 1804.88 902.94 1803.90 902.45 164 478.19 239.60 461.17 231.09 460.18 230.59 Y 1750.87 875.94 1733.85 867.43 1732.86 866.93 155 592.24 296.62 575.21 288.11 574.23 287.62 N 1587.81 794.41 1570.78 785.89 1569.80 785.40 146 689.29 345.15 672.26 336.63 671.28 336.14 P 1473.77 737.39 1456.74 728.87 1455.76 728.38 137 776.32 388.66 759.29 380.15 758.31 379.66 S 1376.71 688.86 1359.69 680.35 1358.70 679.85 128 863.35 432.18 846.33 423.67 845.34 423.17 S 1289.68 645.34 1272.65 636.83 1271.67 636.34 119 1105.49 553.25 1088.46 544.74 1087.48 544.24 K^ 1202.65 601.83 1185.62 593.31 1184.64 592.82 10
10 1192.52 596.77 1175.5 588.25 1174.51 587.76 S 960.51 480.76 943.48 472.25 942.50 471.75 911 1263.56 632.28 1246.53 623.77 1245.55 623.28 A 873.48 437.24 856.45 428.73 855.47 428.24 812 1364.61 682.81 1347.58 674.29 1346.60 673.80 T 802.44 401.72 785.42 393.21 784.43 392.72 713 1477.69 739.35 1460.67 730.84 1459.68 730.34 I 701.39 351.20 684.37 342.69 683.38 342.20 614 1592.72 796.86 1575.69 788.35 1574.71 787.86 D 588.31 294.66 571.28 286.15 570.30 285.65 515 1649.74 825.37 1632.71 816.86 1631.73 816.37 G 473.28 237.15 456.26 228.63 416 1762.82 881.92 1745.80 873.40 1744.81 872.91 L 416.26 208.63 399.24 200.12 317 1890.88 945.95 1873.86 937.43 1872.87 936.94 Q 303.18 152.09 286.15 143.58 218 R 175.12 88.06 158.09 79.55 1
S 3.11 Positive ionization low energy CID fragmentation spectrum of the ubiquitinylated peptide NEAYNPSSKSATIDGLQR of Rec 10MS2 spectrum of the triply charged peptide at m/z 689.57 Da. Identified b and y fragment ions detected in the measurement are colored in the fragmentation table and labeled respectively blue and red in the spectrum. The position of the modified residue (K712) was labeled with “^”. Identified satellite ions originating from the loss of water (b0 or y0 ions) or ammonia (y* ions) are also labeled in the table.
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b11
# b b* b0 Seq. y y* y0 #
1 114.09 L 122 227.18 I 1347.70 1330.67 1329.69 113 374.24 F 1234.62 1217.59 1216.61 104 445.28 A 1087.55 1070.52 1069.54 95 502.30 G 1016.51 999.49 998.50 86 744.44 727.41 K^ 959.49 942.46 941.48 77 872.50 855.47 Q 717.35 700.33 699.34 68 985.58 968.56 L 589.29 572.27 571.28 59 1114.63 1097.60 1096.61 E 476.21 459.18 458.20 4
10 1229.65 1212.63 1211.64 D 347.17 330.14 329.16 311 1286.67 1269.65 1268.66 G 232.14 215.11 212 R 175.12 158.09 1
S 3.12 Positive ionization low energy CID fragmentation spectrum of the ubiquitinylated peptide LIFAGKQLEDGR of Ubi2MS2 spectrum of the doubly charged peptide at m/z 731.42 Da. Identified b and y fragment ions detected in the measurement are colored in the fragmentation table and labeled respectively blue and red in the spectrum. The position of the modified residue (K48) was labeled with “^”. Identified satellite ions originating from the loss of water (b0 or y0 ions) or ammonia (y* ions) are also labeled in the table.
