NMR Restraints Grid
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NMR Restraints Grid |
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Result table
| image | mrblock_id | pdb_id | bmrb_id | cing | stage | position | program | type |
|
|
601714 |
2n07   |
25516 | cing | 1-original | 2 | unknown | unknown |
*** WARNING: Inconsistency in chemical shift list 1 for ILE 15: QG1 1.399, HG12 0.932, HG13 1.397
Peak 70 from 2DNOESY.peaks (7.16, 3.98 ppm; 3.73 A):
2 out of 4 assignments used, quality = 1.00:
H ILE 15 + HA ILE 15 OK 100 100 100 100 2.8-2.9 3.0=100
H ILE 15 + HA GLU 14 OK 100 100 100 100 3.5-3.6 3.5=100
H ILE 15 - HA ALA 20 far 0 82 0 - 7.1-12.4
H ILE 15 - HA ASP 11 far 0 96 0 - 7.9-8.2
Violated in 0 structures by 0.00 A.
Peak 71 from 2DNOESY.peaks (7.16, 1.71 ppm; 3.81 A):
2 out of 3 assignments used, quality = 0.99:
H ILE 15 + HB ILE 15 OK 98 98 100 100 2.6-2.6 3.8=100
H ILE 15 + HB2 GLU 14 OK 31 40 85 92 3.5-4.0 4.4=63, 159/3.7=52...(4)
H ILE 15 - HG3 PRO 13 far 0 37 0 - 5.2-5.3
Violated in 0 structures by 0.00 A.
Peak 75 from 2DNOESY.peaks (7.16, 0.60 ppm; 4.85 A):
1 out of 1 assignment used, quality = 0.99:
H ILE 15 + QD1 ILE 15 OK 99 99 100 100 3.5-3.6 4.4=100
Violated in 0 structures by 0.00 A.
Peak 79 from 2DNOESY.peaks (9.34, 2.01 ppm; 4.45 A increased from 4.18 A):
2 out of 2 assignments used, quality = 0.99:
H GLU 14 + HG2 GLU 14 OK 97 99 100 98 1.9-4.4 144/3.0=78, 5.0=70...(6)
H GLU 14 + HB3 PRO 13 OK 72 72 100 100 4.4-4.4 4.0=100
Violated in 0 structures by 0.00 A.
Peak 80 from 2DNOESY.peaks (7.69, 4.01 ppm; 3.52 A):
1 out of 4 assignments used, quality = 1.00:
H PHE 8 + HA PHE 8 OK 100 100 100 100 2.9-2.9 2.9=100
H ASP 11 - HA PHE 8 far 0 41 0 - 4.2-4.5
H PHE 8 - HA SER 4 far 0 60 0 - 7.3-7.4
H PHE 8 - HA ALA 20 far 0 53 0 - 8.7-12.4
Violated in 0 structures by 0.00 A.
Peak 81 from 2DNOESY.peaks (7.69, 3.19 ppm; 3.31 A):
1 out of 2 assignments used, quality = 0.97:
H PHE 8 + HB3 PHE 8 OK 97 99 100 98 2.3-2.4 82/1.8=75, 4.0=55...(6)
H ASP 11 - HB3 PHE 8 far 0 40 0 - 6.5-6.8
Violated in 0 structures by 0.00 A.
Peak 82 from 2DNOESY.peaks (7.69, 2.84 ppm; 3.13 A):
1 out of 2 assignments used, quality = 0.92:
H PHE 8 + HB2 PHE 8 OK 92 100 100 92 2.7-2.8 81/1.8=64, 4.0=47...(4)
H ASP 11 - HB2 PHE 8 far 0 40 0 - 6.5-6.8
Violated in 0 structures by 0.00 A.
Peak 84 from 2DNOESY.peaks (8.58, 2.56 ppm; 3.38 A):
1 out of 4 assignments used, quality = 0.85:
H ASN 9 + HB3 ASN 9 OK 85 99 100 86 2.5-2.7 4.0=61, 218/202=46, 364/386=34
H ASN 9 - HB2 CYSS 16 far 0 76 0 - 5.0-5.8
H HIS+ 2 - HB2 CYSS 16 far 0 53 0 - 7.8-8.9
H HIS+ 2 - HB3 ASN 9 far 0 69 0 - 9.5-10.5
Violated in 0 structures by 0.00 A.
Peak 85 from 2DNOESY.peaks (7.66, 3.75 ppm; 3.36 A):
1 out of 1 assignment used, quality = 1.00:
H TYR 10 + HA TYR 10 OK 100 100 100 100 2.9-2.9 3.0=100
Violated in 0 structures by 0.00 A.
Peak 86 from 2DNOESY.peaks (7.67, 2.89 ppm; 3.00 A):
1 out of 2 assignments used, quality = 0.92:
H TYR 10 + HB3 TYR 10 OK 92 100 100 92 2.7-2.8 87/1.8=65, 3.8=50...(5)
H TYR 10 - HB3 CYSS 3 far 0 46 0 - 9.4-9.7
Violated in 0 structures by 0.00 A.
Peak 87 from 2DNOESY.peaks (7.67, 2.78 ppm; 3.09 A):
1 out of 1 assignment used, quality = 0.95:
H TYR 10 + HB2 TYR 10 OK 95 100 100 95 2.3-2.5 86/1.8=71, 3.8=55...(5)
Violated in 0 structures by 0.00 A.
Peak 89 from 2DNOESY.peaks (7.71, 2.23 ppm; 3.35 A):
1 out of 3 assignments used, quality = 0.74:
H ASP 11 + HB2 ASP 11 OK 74 99 100 75 2.3-2.8 3.9=62, 214/4.5=32
H ASP 11 - HB2 HIS+ 12 far 0 49 0 - 6.1-6.2
H ASP 11 - HG3 GLU 14 far 0 52 0 - 8.2-11.9
Violated in 0 structures by 0.00 A.
Peak 90 from 2DNOESY.peaks (7.71, 1.86 ppm; 3.79 A):
0 out of 2 assignments used, quality = 0.00:
H PHE 8 - HG3 PRO 6 far 0 40 0 - 5.0-5.2
H ASP 11 - HG3 PRO 6 far 0 97 0 - 7.6-7.9
Violated in 20 structures by 1.28 A.
Peak 92 from 2DNOESY.peaks (7.29, 5.00 ppm; 4.16 A):
1 out of 2 assignments used, quality = 0.99:
H HIS+ 12 + HA HIS+ 12 OK 99 99 100 100 2.9-2.9 3.0=100
HE ARG 7 - HA HIS+ 12 far 0 87 0 - 9.0-12.2
Violated in 0 structures by 0.00 A.
Peak 93 from 2DNOESY.peaks (7.29, 2.60 ppm; 4.62 A):
1 out of 2 assignments used, quality = 1.00:
H HIS+ 12 + HB3 HIS+ 12 OK 100 100 100 100 2.5-2.7 4.0=100
HE ARG 7 - HB3 HIS+ 12 far 0 88 0 - 8.0-10.7
Violated in 0 structures by 0.00 A.
Peak 94 from 2DNOESY.peaks (7.29, 2.26 ppm; 3.87 A):
1 out of 5 assignments used, quality = 0.94:
H HIS+ 12 + HB2 HIS+ 12 OK 94 97 100 97 3.7-3.8 4.0=92, 269/4.8=32...(4)
H HIS+ 12 - HB2 ASP 11 poor 18 36 50 - 3.8-4.3
HE ARG 7 - HB2 ASP 11 far 0 30 0 - 4.6-8.2
H HIS+ 12 - HG3 GLU 14 far 0 95 0 - 6.0-9.6
HE ARG 7 - HB2 HIS+ 12 far 0 80 0 - 9.6-12.4
Violated in 0 structures by 0.00 A.
Peak 97 from 2DNOESY.peaks (7.50, 4.79 ppm; 3.78 A):
1 out of 1 assignment used, quality = 1.00:
H ASP 5 + HA ASP 5 OK 100 100 100 100 2.9-2.9 3.0=100
Violated in 0 structures by 0.00 A.
Peak 98 from 2DNOESY.peaks (7.62, 3.72 ppm; 3.82 A):
1 out of 1 assignment used, quality = 0.97:
H SER 4 + HB2 SER 4 OK 97 99 100 98 3.5-3.6 4.0=87, 99/1.8=78, 187/4.5=42
Violated in 0 structures by 0.00 A.
Peak 99 from 2DNOESY.peaks (7.62, 3.66 ppm; 3.70 A):
1 out of 4 assignments used, quality = 0.96:
H SER 4 + HB3 SER 4 OK 96 100 100 96 2.3-2.9 4.0=79, 98/1.8=70, 187/186=40
H SER 4 - HA3 GLY 22 far 5 99 5 - 3.5-7.2
H SER 4 - HA3 GLY 21 far 0 46 0 - 6.3-9.6
H SER 4 - HD2 PRO 6 far 0 99 0 - 7.4-7.5
Violated in 0 structures by 0.00 A.
Peak 101 from 2DNOESY.peaks (7.50, 2.46 ppm; 3.85 A increased from 3.43 A):
1 out of 1 assignment used, quality = 0.99:
H ASP 5 + HB2 ASP 5 OK 99 99 100 99 3.6-3.7 4.0=91, 228/1.8=87, 225/423=26
Violated in 0 structures by 0.00 A.
Peak 103 from 2DNOESY.peaks (7.90, 3.08 ppm; 3.72 A):
1 out of 1 assignment used, quality = 0.99:
H CYSS 3 + HB2 CYSS 3 OK 99 100 100 99 2.2-2.3 349/1.8=84, 3.9=84...(4)
Violated in 0 structures by 0.00 A.
Peak 108 from 2DNOESY.peaks (8.57, 4.16 ppm; 3.58 A):
2 out of 4 assignments used, quality = 1.00:
H HIS+ 2 + HA HIS+ 2 OK 99 99 100 100 2.9-2.9 3.0=100
H ASN 9 + HA ASN 9 OK 66 66 100 100 2.9-2.9 3.0=100
H ASN 9 - HA HIS+ 2 far 0 69 0 - 7.7-8.5
H HIS+ 2 - HA ASN 9 far 0 94 0 - 8.4-9.3
Violated in 0 structures by 0.00 A.
Peak 109 from 2DNOESY.peaks (7.79, 3.91 ppm; 3.71 A):
1 out of 1 assignment used, quality = 0.99:
H ARG 7 + HA ARG 7 OK 99 99 100 100 2.8-2.8 3.0=100
Violated in 0 structures by 0.00 A.
Peak 114 from 2DNOESY.peaks (8.15, 3.69 ppm; 3.78 A):
1 out of 1 assignment used, quality = 1.00:
H GLY 18 + HA2 GLY 18 OK 100 100 100 100 2.3-3.0 3.0=100
Violated in 0 structures by 0.00 A.
Peak 115 from 2DNOESY.peaks (7.78, 4.08 ppm; 3.58 A):
2 out of 3 assignments used, quality = 1.00:
H ALA 19 + HA ALA 19 OK 100 100 100 100 2.8-2.9 3.0=100
H ARG 7 + HA PRO 6 OK 66 66 100 100 3.5-3.5 3.6=100
H ALA 19 - HA PRO 6 far 0 85 0 - 8.0-13.9
Violated in 0 structures by 0.00 A.
Peak 116 from 2DNOESY.peaks (7.78, 1.19 ppm; 3.23 A):
1 out of 1 assignment used, quality = 1.00:
H ALA 19 + QB ALA 19 OK 100 100 100 100 2.2-2.9 2.9=100
Violated in 0 structures by 0.00 A.
Peak 117 from 2DNOESY.peaks (8.24, 3.99 ppm; 3.29 A):
1 out of 4 assignments used, quality = 1.00:
H ALA 20 + HA ALA 20 OK 100 100 100 100 2.3-2.9 3.0=100
H ALA 20 - HA ILE 15 far 0 82 0 - 5.6-12.0
H ALA 20 - HA SER 4 far 0 99 0 - 6.0-11.3
H ALA 20 - HA GLU 14 far 0 82 0 - 7.4-12.4
Violated in 0 structures by 0.00 A.
Peak 118 from 2DNOESY.peaks (8.24, 1.10 ppm; 3.33 A):
1 out of 1 assignment used, quality = 1.00:
H ALA 20 + QB ALA 20 OK 100 100 100 100 2.0-2.8 2.9=100
Violated in 0 structures by 0.00 A.
Peak 122 from 2DNOESY.peaks (7.79, 2.97 ppm; 4.68 A):
2 out of 2 assignments used, quality = 1.00:
H ARG 7 + HD3 ARG 7 OK 100 100 100 100 3.9-4.7 3.0/396=80, 237/3.7=74...(6)
H ARG 7 + HB3 ASP 5 OK 75 76 100 98 2.9-3.6 239/241=74, 246/3.0=58...(6)
Violated in 0 structures by 0.00 A.
Peak 123 from 2DNOESY.peaks (7.79, 2.97 ppm; 4.68 A):
2 out of 2 assignments used, quality = 1.00:
H ARG 7 + HD3 ARG 7 OK 100 100 100 100 3.9-4.7 3.0/396=80, 237/3.7=74...(6)
H ARG 7 + HB3 ASP 5 OK 75 76 100 98 2.9-3.6 239/241=74, 246/3.0=58...(6)
Violated in 0 structures by 0.00 A.
Peak 124 from 2DNOESY.peaks (7.79, 1.77 ppm; 3.51 A):
1 out of 1 assignment used, quality = 0.99:
H ARG 7 + HB3 ARG 7 OK 99 100 100 99 2.6-2.9 237/1.8=73, 3.9=71...(8)
Violated in 0 structures by 0.00 A.
Peak 126 from 2DNOESY.peaks (7.79, 1.45 ppm; 4.78 A increased from 4.50 A):
1 out of 1 assignment used, quality = 0.99:
H ARG 7 + HG3 ARG 7 OK 99 99 100 100 4.6-4.6 4.8=96, 237/2.9=88...(7)
Violated in 0 structures by 0.00 A.
Peak 127 from 2DNOESY.peaks (7.79, 1.39 ppm; 4.56 A increased from 4.29 A):
1 out of 2 assignments used, quality = 1.00:
H ARG 7 + HG2 ARG 7 OK 100 100 100 100 4.4-4.5 4.8=83, 237/2.9=83...(7)
H ALA 19 - HG13 ILE 15 far 0 76 0 - 6.8-11.4
Violated in 0 structures by 0.00 A.
Peak 135 from 2DNOESY.peaks (3.95, 4.07 ppm; 3.90 A):
1 out of 1 assignment used, quality = 0.99:
HD3 PRO 6 + HA PRO 6 OK 99 99 100 100 3.6-3.6 3.6=100
Violated in 0 structures by 0.00 A.
Peak 136 from 2DNOESY.peaks (3.95, 4.78 ppm; 3.13 A):
1 out of 1 assignment used, quality = 0.97:
HD3 PRO 6 + HA ASP 5 OK 97 97 100 100 2.3-2.3 2.5=100
Violated in 0 structures by 0.00 A.
Peak 137 from 2DNOESY.peaks (3.66, 4.79 ppm; 3.42 A):
1 out of 3 assignments used, quality = 0.99:
HD2 PRO 6 + HA ASP 5 OK 99 99 100 100 2.4-2.4 2.5=100
HB3 SER 4 - HA ASP 5 far 0 96 0 - 5.7-5.7
HA3 GLY 22 - HA ASP 5 far 0 99 0 - 8.8-12.5
Violated in 0 structures by 0.00 A.
Peak 138 from 2DNOESY.peaks (3.06, 3.23 ppm; 2.82 A):
1 out of 2 assignments used, quality = 0.96:
HD2 PRO 13 + HD3 PRO 13 OK 96 96 100 100 1.8-1.8 1.8=100
HD2 PRO 13 - HB3 CYSS 16 far 0 70 0 - 8.2-8.5
Violated in 0 structures by 0.00 A.
Peak 142 from 2DNOESY.peaks (9.34, 3.98 ppm; 3.47 A):
1 out of 4 assignments used, quality = 0.98:
H GLU 14 + HA GLU 14 OK 98 98 100 100 2.9-2.9 2.9=100
H GLU 14 - HA ILE 15 far 0 98 0 - 4.8-4.9
H GLU 14 - HA ASP 11 far 0 94 0 - 6.9-6.9
H GLU 14 - HA ALA 20 far 0 81 0 - 8.8-13.3
Violated in 0 structures by 0.00 A.
Peak 143 from 2DNOESY.peaks (9.34, 2.25 ppm; 4.38 A):
2 out of 3 assignments used, quality = 0.97:
H GLU 14 + HB2 HIS+ 12 OK 89 94 100 94 3.6-3.7 280/3.0=63, 277/4.8=46...(5)
H GLU 14 + HG3 GLU 14 OK 70 96 75 98 1.9-4.8 144/3.0=76, 5.0=67...(7)
H GLU 14 - HB2 ASP 11 far 0 70 0 - 8.4-8.6
Violated in 0 structures by 0.00 A.
Peak 144 from 2DNOESY.peaks (9.34, 1.81 ppm; 3.60 A):
1 out of 1 assignment used, quality = 0.98:
H GLU 14 + HB3 GLU 14 OK 98 100 100 98 2.4-3.1 3.7=94, 159/4.4=37...(5)
Violated in 0 structures by 0.00 A.
Peak 146 from 2DNOESY.peaks (7.16, 2.01 ppm; 4.88 A):
1 out of 2 assignments used, quality = 0.98:
H ILE 15 + HG2 GLU 14 OK 98 99 100 99 1.9-3.5 159/5.0=58, 407/416=56...(7)
H ILE 15 - HB3 PRO 13 far 0 76 0 - 6.1-6.5
Violated in 0 structures by 0.00 A.
Peak 147 from 2DNOESY.peaks (7.16, 1.81 ppm; 4.85 A):
1 out of 1 assignment used, quality = 1.00:
H ILE 15 + HB3 GLU 14 OK 100 100 100 100 2.5-4.1 4.4=100
Violated in 0 structures by 0.00 A.
Peak 148 from 2DNOESY.peaks (8.04, 4.73 ppm; 3.96 A):
1 out of 1 assignment used, quality = 0.99:
H CYSS 16 + HA CYSS 16 OK 99 99 100 100 2.9-2.9 2.9=100
Violated in 0 structures by 0.00 A.
Peak 149 from 2DNOESY.peaks (8.04, 3.25 ppm; 3.84 A):
1 out of 2 assignments used, quality = 0.99:
H CYSS 16 + HB3 CYSS 16 OK 99 100 100 99 3.5-3.6 4.0=88, 150/1.8=85, 354/4.3=45
H CYSS 16 - HD3 PRO 13 far 0 56 0 - 6.3-6.5
Violated in 0 structures by 0.00 A.
Peak 150 from 2DNOESY.peaks (8.04, 2.55 ppm; 3.39 A):
1 out of 2 assignments used, quality = 0.89:
H CYSS 16 + HB2 CYSS 16 OK 89 100 100 90 2.3-2.4 4.0=61, 149/1.8=59, 354/4.3=35
H CYSS 16 - HB3 ASN 9 far 0 85 0 - 7.0-7.3
Violated in 0 structures by 0.00 A.
Peak 151 from 2DNOESY.peaks (8.04, 1.71 ppm; 3.50 A):
1 out of 3 assignments used, quality = 0.96:
H CYSS 16 + HB ILE 15 OK 96 100 100 97 2.9-3.1 157/2.1=53, 4.5=48...(7)
H CYSS 16 - HB2 GLU 14 far 0 49 0 - 5.1-5.5
H CYSS 16 - HG3 PRO 13 far 0 46 0 - 6.2-6.3
Violated in 0 structures by 0.00 A.
Peak 152 from 2DNOESY.peaks (8.04, 1.40 ppm; 4.63 A):
1 out of 1 assignment used, quality = 1.00:
H CYSS 16 + HG13 ILE 15 OK 100 100 100 100 4.2-4.4 151/3.0=84, 157/3.2=71...(7)
Violated in 0 structures by 0.00 A.
Peak 156 from 2DNOESY.peaks (8.04, 0.93 ppm; 5.34 A increased from 4.75 A):
1 out of 1 assignment used, quality = 0.99:
H CYSS 16 + HG12 ILE 15 OK 99 99 100 100 5.0-5.1 151/3.0=95, 152/1.8=94...(7)
Violated in 0 structures by 0.00 A.
Peak 157 from 2DNOESY.peaks (8.04, 0.74 ppm; 4.07 A):
1 out of 1 assignment used, quality = 0.98:
H CYSS 16 + QG2 ILE 15 OK 98 98 100 100 3.7-4.0 4.1=97, 151/2.1=83...(7)
Violated in 0 structures by 0.00 A.
Peak 158 from 2DNOESY.peaks (8.04, 0.60 ppm; 4.95 A increased from 4.66 A):
1 out of 1 assignment used, quality = 0.97:
H CYSS 16 + QD1 ILE 15 OK 97 97 100 100 4.8-4.9 151/3.2=87, 152/2.1=83...(6)
Violated in 0 structures by 0.00 A.
Peak 159 from 2DNOESY.peaks (9.34, 7.16 ppm; 3.56 A):
1 out of 1 assignment used, quality = 0.87:
H GLU 14 + H ILE 15 OK 87 99 100 87 2.1-2.2 4.6=45, 161/160=36...(7)
Violated in 0 structures by 0.00 A.
Peak 160 from 2DNOESY.peaks (8.04, 7.16 ppm; 3.03 A):
1 out of 1 assignment used, quality = 0.83:
H CYSS 16 + H ILE 15 OK 83 96 100 86 2.4-2.8 151/3.8=31, 4.6=28...(9)
Violated in 0 structures by 0.00 A.
Peak 161 from 2DNOESY.peaks (9.34, 8.05 ppm; 4.66 A):
1 out of 1 assignment used, quality = 0.94:
H GLU 14 + H CYSS 16 OK 94 97 100 97 3.5-3.6 159/160=80, 3.6/287=64...(5)
Violated in 0 structures by 0.00 A.
Peak 162 from 2DNOESY.peaks (8.19, 4.03 ppm; 3.87 A):
1 out of 4 assignments used, quality = 1.00:
H GLY 17 + HA3 GLY 17 OK 100 100 100 100 2.3-2.9 3.0=100
HE1 HIS+ 2 - HA PHE 8 far 0 82 0 - 7.9-9.7
H GLY 17 - HA PHE 8 far 0 82 0 - 8.4-8.8
H GLY 21 - HA3 GLY 17 far 0 78 0 - 8.5-11.2
Violated in 0 structures by 0.00 A.
Peak 163 from 2DNOESY.peaks (8.19, 3.80 ppm; 3.22 A):
1 out of 2 assignments used, quality = 1.00:
H GLY 17 + HA2 GLY 17 OK 100 100 100 100 2.3-2.9 3.0=100
H GLY 21 - HA2 GLY 17 far 0 70 0 - 8.7-11.6
Violated in 0 structures by 0.00 A.
Peak 164 from 2DNOESY.peaks (8.15, 3.85 ppm; 3.36 A):
1 out of 1 assignment used, quality = 1.00:
H GLY 18 + HA3 GLY 18 OK 100 100 100 100 2.3-3.0 3.0=100
Violated in 0 structures by 0.00 A.
Peak 166 from 2DNOESY.peaks (7.78, 3.85 ppm; 3.94 A):
1 out of 1 assignment used, quality = 1.00:
H ALA 19 + HA3 GLY 18 OK 100 100 100 100 2.2-3.6 3.6=100
Violated in 0 structures by 0.00 A.
Peak 167 from 2DNOESY.peaks (8.24, 4.08 ppm; 3.51 A):
1 out of 2 assignments used, quality = 0.97:
H ALA 20 + HA ALA 19 OK 97 100 100 98 2.2-3.5 3.6=95, 170/3.0=48
H ALA 20 - HA PRO 6 far 0 85 0 - 8.3-13.5
Violated in 0 structures by 0.00 A.
Peak 169 from 2DNOESY.peaks (8.24, 1.19 ppm; 3.82 A):
1 out of 1 assignment used, quality = 1.00:
H ALA 20 + QB ALA 19 OK 100 100 100 100 2.8-3.6 3.6=100
Violated in 0 structures by 0.00 A.
Peak 170 from 2DNOESY.peaks (8.24, 7.78 ppm; 3.90 A increased from 3.67 A):
1 out of 1 assignment used, quality = 0.87:
H ALA 20 + H ALA 19 OK 87 100 100 87 2.3-3.9 167/3.0=66, 4.6=60
Violated in 0 structures by 0.00 A.
Peak 175 from 2DNOESY.peaks (8.35, 3.40 ppm; 3.42 A):
0 out of 0 assignments used, quality = 0.00:
Peak 178 from 2DNOESY.peaks (8.18, 3.48 ppm; 3.49 A):
1 out of 5 assignments used, quality = 0.96:
H GLY 21 + HA2 GLY 21 OK 96 96 100 100 2.5-3.0 3.0=100
H GLY 21 - HA2 GLY 22 far 0 73 0 - 4.1-5.1
HE1 HIS+ 2 - HA2 GLY 22 far 0 65 0 - 7.5-11.5
H GLY 17 - HA2 GLY 21 far 0 75 0 - 8.9-12.4
H GLY 17 - HA2 GLY 22 far 0 57 0 - 9.3-13.9
Violated in 0 structures by 0.00 A.
Peak 179 from 2DNOESY.peaks (7.87, 3.66 ppm; 3.01 A):
2 out of 3 assignments used, quality = 1.00:
H GLY 22 + HA3 GLY 22 OK 100 100 100 100 2.3-3.0 3.0=100
H GLY 22 + HA3 GLY 21 OK 32 53 80 76 2.2-3.6 3.6=60, 355/3.0=38
H GLY 22 - HB3 SER 4 far 0 99 0 - 4.9-8.4
Violated in 0 structures by 0.00 A.
Peak 180 from 2DNOESY.peaks (7.88, 3.48 ppm; 3.76 A):
2 out of 2 assignments used, quality = 0.97:
H GLY 22 + HA2 GLY 21 OK 92 92 100 100 2.4-3.6 3.6=100
H GLY 22 + HA2 GLY 22 OK 66 66 100 100 2.3-3.0 3.0=100
Violated in 0 structures by 0.00 A.
Peak 181 from 2DNOESY.peaks (8.35, 3.66 ppm; 3.08 A):
0 out of 0 assignments used, quality = 0.00:
Peak 183 from 2DNOESY.peaks (7.62, 4.00 ppm; 3.66 A):
1 out of 3 assignments used, quality = 0.99:
H SER 4 + HA SER 4 OK 99 99 100 100 2.8-2.8 3.0=100
H SER 4 - HA ALA 20 far 0 98 0 - 5.0-9.1
H SER 4 - HA PHE 8 far 0 59 0 - 7.5-7.7
Violated in 0 structures by 0.00 A.
Peak 184 from 2DNOESY.peaks (7.50, 3.99 ppm; 4.01 A):
1 out of 3 assignments used, quality = 0.98:
H ASP 5 + HA SER 4 OK 98 98 100 100 3.5-3.5 3.6=100
H ASP 5 - HA ALA 20 far 0 100 0 - 6.3-11.2
H ASP 5 - HA PHE 8 far 0 49 0 - 6.3-6.4
Violated in 0 structures by 0.00 A.
Peak 185 from 2DNOESY.peaks (7.50, 3.72 ppm; 4.78 A):
1 out of 2 assignments used, quality = 0.99:
H ASP 5 + HB2 SER 4 OK 99 99 100 100 3.6-4.1 4.5=100
H ASP 5 - HA2 GLY 18 far 0 43 0 - 9.6-15.3
Violated in 0 structures by 0.00 A.
Peak 186 from 2DNOESY.peaks (7.50, 3.67 ppm; 4.42 A):
1 out of 4 assignments used, quality = 0.98:
H ASP 5 + HB3 SER 4 OK 98 99 100 99 3.8-4.3 4.5=96, 187/99=68
H ASP 5 - HD2 PRO 6 far 0 98 0 - 4.8-4.8
H ASP 5 - HA3 GLY 22 far 0 98 0 - 6.1-9.7
H ASP 5 - HA3 GLY 21 far 0 42 0 - 8.5-12.2
Violated in 0 structures by 0.00 A.
Peak 187 from 2DNOESY.peaks (7.63, 7.50 ppm; 3.46 A):
1 out of 1 assignment used, quality = 0.90:
H SER 4 + H ASP 5 OK 90 99 100 91 2.7-2.8 4.5=44, 3.6/232=34...(6)
Violated in 0 structures by 0.00 A.
Peak 188 from 2DNOESY.peaks (7.63, 2.87 ppm; 4.38 A):
1 out of 1 assignment used, quality = 0.94:
H SER 4 + HB3 CYSS 3 OK 94 98 100 96 3.0-3.2 4.6=84, 325/349=73
Violated in 0 structures by 0.00 A.
Peak 189 from 2DNOESY.peaks (7.63, 3.08 ppm; 4.91 A):
1 out of 1 assignment used, quality = 0.99:
H SER 4 + HB2 CYSS 3 OK 99 99 100 100 3.8-4.0 4.6=100
Violated in 0 structures by 0.00 A.
Peak 190 from 2DNOESY.peaks (7.90, 4.26 ppm; 3.69 A):
1 out of 1 assignment used, quality = 1.00:
H CYSS 3 + HA CYSS 3 OK 100 100 100 100 2.8-2.8 3.0=100
Violated in 0 structures by 0.00 A.
Peak 191 from 2DNOESY.peaks (7.63, 4.26 ppm; 4.23 A):
1 out of 1 assignment used, quality = 1.00:
H SER 4 + HA CYSS 3 OK 100 100 100 100 3.4-3.5 3.6=100
Violated in 0 structures by 0.00 A.
Peak 192 from 2DNOESY.peaks (7.90, 4.16 ppm; 3.75 A):
1 out of 2 assignments used, quality = 0.98:
H CYSS 3 + HA HIS+ 2 OK 98 98 100 100 3.0-3.5 3.6=100
H CYSS 3 - HA ASN 9 far 0 93 0 - 7.4-7.7
Violated in 0 structures by 0.00 A.
Peak 193 from 2DNOESY.peaks (8.57, 1.94 ppm; 4.30 A):
1 out of 2 assignments used, quality = 0.99:
H HIS+ 2 + HB3 HIS+ 2 OK 99 99 100 100 3.6-3.7 3.9=100
H ASN 9 - HB3 HIS+ 2 far 0 82 0 - 6.4-6.8
Violated in 0 structures by 0.00 A.
Peak 194 from 2DNOESY.peaks (8.57, 1.74 ppm; 3.87 A):
1 out of 5 assignments used, quality = 0.97:
H HIS+ 2 + HB2 HIS+ 2 OK 97 97 100 99 2.4-2.6 3.9=99
H ASN 9 - HB3 ARG 7 far 0 34 0 - 4.6-4.7
H ASN 9 - HB2 PRO 6 far 0 70 0 - 4.8-4.9
H ASN 9 - HB2 HIS+ 2 far 0 72 0 - 7.2-7.7
H HIS+ 2 - HB3 ARG 7 far 0 46 0 - 8.6-9.2
Violated in 0 structures by 0.00 A.
Peak 195 from 2DNOESY.peaks (8.57, 7.90 ppm; 3.79 A):
1 out of 2 assignments used, quality = 0.81:
H HIS+ 2 + H CYSS 3 OK 81 100 100 81 1.9-2.4 4.6=56, 194/4.2=42, 220/327=24
H ASN 9 - H CYSS 3 far 0 70 0 - 7.3-7.5
Violated in 0 structures by 0.00 A.
Peak 196 from 2DNOESY.peaks (8.58, 4.16 ppm; 3.52 A):
2 out of 4 assignments used, quality = 0.97:
H ASN 9 + HA ASN 9 OK 88 88 100 100 2.9-2.9 3.0=100
H HIS+ 2 + HA HIS+ 2 OK 75 75 100 100 2.9-2.9 3.0=100
H ASN 9 - HA HIS+ 2 far 0 96 0 - 7.7-8.5
H HIS+ 2 - HA ASN 9 far 0 68 0 - 8.4-9.3
Violated in 0 structures by 0.00 A.
Peak 197 from 2DNOESY.peaks (8.58, 3.19 ppm; 4.39 A increased from 3.69 A):
1 out of 2 assignments used, quality = 0.98:
H ASN 9 + HB3 PHE 8 OK 98 98 100 100 4.1-4.2 4.3=100
H HIS+ 2 - HB3 PHE 8 far 0 69 0 - 4.8-5.6
Violated in 0 structures by 0.00 A.
Peak 198 from 2DNOESY.peaks (8.58, 2.84 ppm; 3.60 A increased from 3.20 A):
1 out of 4 assignments used, quality = 0.84:
H ASN 9 + HB2 PHE 8 OK 84 98 100 86 3.5-3.6 4.3=59, 221/82=57, 5.7/351=15
H HIS+ 2 - HB3 CYSS 3 far 0 28 0 - 4.4-5.2
H HIS+ 2 - HB2 PHE 8 far 0 69 0 - 4.8-5.5
H ASN 9 - HB3 CYSS 3 far 0 40 0 - 7.6-7.8
Violated in 0 structures by 0.00 A.
Peak 201 from 2DNOESY.peaks (7.66, 2.78 ppm; 3.09 A):
1 out of 1 assignment used, quality = 0.95:
H TYR 10 + HB2 TYR 10 OK 95 100 100 95 2.3-2.5 86/1.8=71, 3.8=55...(5)
Violated in 0 structures by 0.00 A.
Peak 202 from 2DNOESY.peaks (7.66, 2.56 ppm; 3.29 A):
1 out of 2 assignments used, quality = 0.66:
H TYR 10 + HB3 ASN 9 OK 66 99 100 67 3.1-3.2 218/84=42, 4.4=41
H TYR 10 - HB2 CYSS 16 far 0 76 0 - 5.7-6.5
Violated in 0 structures by 0.00 A.
Peak 203 from 2DNOESY.peaks (7.66, 2.56 ppm; 3.29 A):
1 out of 2 assignments used, quality = 0.66:
H TYR 10 + HB3 ASN 9 OK 66 99 100 67 3.1-3.2 218/84=42, 4.4=41
H TYR 10 - HB2 CYSS 16 far 0 76 0 - 5.7-6.5
Violated in 0 structures by 0.00 A.
Peak 204 from 2DNOESY.peaks (7.66, 4.15 ppm; 4.01 A):
1 out of 2 assignments used, quality = 0.97:
H TYR 10 + HA ASN 9 OK 97 97 100 100 3.4-3.4 3.6=100
H TYR 10 - HA HIS+ 2 far 0 90 0 - 9.5-10.3
Violated in 0 structures by 0.00 A.
Peak 205 from 2DNOESY.peaks (6.88, 3.75 ppm; 3.41 A):
1 out of 1 assignment used, quality = 0.96:
QD TYR 10 + HA TYR 10 OK 96 99 100 97 2.2-3.1 3.7=76, 217/3.0=40...(7)
Violated in 0 structures by 0.00 A.
Peak 206 from 2DNOESY.peaks (6.88, 2.89 ppm; 3.42 A):
1 out of 1 assignment used, quality = 0.99:
QD TYR 10 + HB3 TYR 10 OK 99 99 100 100 2.3-2.6 2.5=100
Violated in 0 structures by 0.00 A.
Peak 207 from 2DNOESY.peaks (6.88, 2.78 ppm; 3.21 A):
1 out of 1 assignment used, quality = 1.00:
QD TYR 10 + HB2 TYR 10 OK 100 100 100 100 2.3-2.7 2.5=100
Violated in 0 structures by 0.00 A.
Peak 208 from 2DNOESY.peaks (7.71, 3.99 ppm; 3.50 A):
1 out of 5 assignments used, quality = 1.00:
H ASP 11 + HA ASP 11 OK 100 100 100 100 2.9-2.9 3.0=100
H PHE 8 - HA SER 4 far 0 37 0 - 7.3-7.4
H PHE 8 - HA ASP 11 far 0 41 0 - 8.1-8.3
H PHE 8 - HA ALA 20 far 0 38 0 - 8.7-12.4
H ASP 11 - HA GLU 14 far 0 96 0 - 9.9-10.0
Violated in 0 structures by 0.00 A.
Peak 210 from 2DNOESY.peaks (7.71, 3.75 ppm; 4.18 A):
1 out of 2 assignments used, quality = 1.00:
H ASP 11 + HA TYR 10 OK 100 100 100 100 3.6-3.6 3.6=100
H PHE 8 - HA TYR 10 far 0 41 0 - 6.9-6.9
Violated in 0 structures by 0.00 A.
Peak 211 from 2DNOESY.peaks (7.71, 2.89 ppm; 3.95 A):
1 out of 1 assignment used, quality = 0.99:
H ASP 11 + HB3 TYR 10 OK 99 100 100 99 2.1-3.8 212/1.8=83, 4.4=73...(6)
Violated in 0 structures by 0.00 A.
Peak 212 from 2DNOESY.peaks (7.71, 2.78 ppm; 3.62 A):
1 out of 2 assignments used, quality = 0.97:
H ASP 11 + HB2 TYR 10 OK 97 100 100 97 2.2-3.5 211/1.8=64, 4.4=56...(6)
H PHE 8 - HB2 TYR 10 far 0 41 0 - 5.4-5.7
Violated in 0 structures by 0.00 A.
Peak 214 from 2DNOESY.peaks (7.71, 7.29 ppm; 3.38 A):
1 out of 2 assignments used, quality = 0.69:
H ASP 11 + H HIS+ 12 OK 69 99 100 69 2.4-2.5 4.6=39, 89/4.5=33, 4.6/216=23
H ASP 11 - HE ARG 7 far 0 92 0 - 4.0-7.6
Violated in 0 structures by 0.00 A.
Peak 215 from 2DNOESY.peaks (7.71, 6.88 ppm; 4.17 A):
1 out of 2 assignments used, quality = 0.97:
H ASP 11 + QD TYR 10 OK 97 97 100 100 2.7-3.8 4.4=85, 212/2.5=78...(7)
H PHE 8 - QD TYR 10 far 0 52 0 - 6.8-7.2
Violated in 0 structures by 0.00 A.
Peak 216 from 2DNOESY.peaks (7.67, 7.29 ppm; 4.65 A):
1 out of 2 assignments used, quality = 0.63:
H TYR 10 + H HIS+ 12 OK 63 100 100 63 3.4-3.5 4.6/214=61
H TYR 10 - HE ARG 7 far 14 92 15 - 4.6-7.5
Violated in 0 structures by 0.00 A.
Peak 217 from 2DNOESY.peaks (7.67, 6.88 ppm; 4.19 A increased from 3.94 A):
1 out of 1 assignment used, quality = 0.99:
H TYR 10 + QD TYR 10 OK 99 99 100 100 4.1-4.2 86/2.5=90, 87/2.5=88...(6)
Violated in 1 structures by 0.00 A.
Peak 218 from 2DNOESY.peaks (8.58, 7.67 ppm; 3.54 A):
1 out of 2 assignments used, quality = 0.73:
H ASN 9 + H TYR 10 OK 73 99 100 74 1.9-2.0 84/202=52, 4.7=44
H HIS+ 2 - H TYR 10 far 0 82 0 - 9.9-10.8
Violated in 0 structures by 0.00 A.
Peak 219 from 2DNOESY.peaks (6.76, 4.02 ppm; 3.77 A):
1 out of 4 assignments used, quality = 0.99:
QD PHE 8 + HA PHE 8 OK 99 99 100 100 2.1-2.6 3.7=100
QD PHE 8 - HA ALA 20 far 0 46 0 - 5.4-8.5
QD PHE 8 - HA SER 4 far 0 53 0 - 6.6-6.6
QD PHE 8 - HA3 GLY 17 far 0 88 0 - 8.8-9.2
Violated in 0 structures by 0.00 A.
Peak 220 from 2DNOESY.peaks (8.58, 6.76 ppm; 4.11 A):
1 out of 2 assignments used, quality = 0.65:
H HIS+ 2 + QD PHE 8 OK 65 74 95 93 3.1-4.4 3.0/289=51, 3.9/297=46...(5)
H ASN 9 - QD PHE 8 far 0 100 0 - 4.8-4.8
Violated in 3 structures by 0.01 A.
Peak 221 from 2DNOESY.peaks (8.58, 7.69 ppm; 3.31 A):
1 out of 3 assignments used, quality = 0.85:
H ASN 9 + H PHE 8 OK 85 98 100 86 2.5-2.5 198/82=45, 4.6=37...(5)
H ASN 9 - H ASP 11 far 0 66 0 - 3.9-4.1
H HIS+ 2 - H PHE 8 far 0 69 0 - 7.0-7.7
Violated in 0 structures by 0.00 A.
Peak 222 from 2DNOESY.peaks (8.58, 7.69 ppm; 3.31 A):
1 out of 3 assignments used, quality = 0.85:
H ASN 9 + H PHE 8 OK 85 98 100 86 2.5-2.5 198/82=45, 4.6=37...(5)
H ASN 9 - H ASP 11 far 0 66 0 - 3.9-4.1
H HIS+ 2 - H PHE 8 far 0 69 0 - 7.0-7.7
Violated in 0 structures by 0.00 A.
Peak 223 from 2DNOESY.peaks (8.58, 4.01 ppm; 4.21 A):
1 out of 7 assignments used, quality = 0.99:
H ASN 9 + HA PHE 8 OK 99 99 100 100 3.3-3.3 3.6=100
H HIS+ 2 - HA SER 4 far 0 46 0 - 6.4-7.3
H HIS+ 2 - HA PHE 8 far 0 82 0 - 6.4-7.6
H HIS+ 2 - HA ALA 20 far 0 40 0 - 6.8-9.5
H ASN 9 - HA SER 4 far 0 56 0 - 8.1-8.4
H ASN 9 - HA ALA 20 far 0 49 0 - 8.5-12.1
H ASN 9 - HA3 GLY 17 far 0 84 0 - 8.8-10.6
Violated in 0 structures by 0.00 A.
Peak 224 from 2DNOESY.peaks (7.69, 6.76 ppm; 4.31 A increased from 4.05 A):
1 out of 1 assignment used, quality = 0.98:
H PHE 8 + QD PHE 8 OK 98 98 100 100 4.0-4.1 82/2.5=90, 81/2.5=87...(6)
Violated in 0 structures by 0.00 A.
Peak 225 from 2DNOESY.peaks (7.50, 3.19 ppm; 4.55 A):
1 out of 1 assignment used, quality = 0.97:
H ASP 5 + HB3 PHE 8 OK 97 100 100 97 3.9-4.1 226/1.8=82, 228/452=73
Violated in 0 structures by 0.00 A.
Peak 226 from 2DNOESY.peaks (7.50, 2.84 ppm; 4.42 A):
1 out of 1 assignment used, quality = 0.76:
H ASP 5 + HB2 PHE 8 OK 76 100 100 76 3.8-4.0 225/1.8=74
Violated in 0 structures by 0.00 A.
Peak 228 from 2DNOESY.peaks (7.50, 2.98 ppm; 3.32 A):
1 out of 2 assignments used, quality = 0.86:
H ASP 5 + HB3 ASP 5 OK 86 98 100 87 2.4-2.9 4.0=58, 101/1.8=56, 225/452=28
H ASP 5 - HD3 ARG 7 far 0 82 0 - 8.5-9.4
Violated in 0 structures by 0.00 A.
Peak 229 from 2DNOESY.peaks (7.69, 2.46 ppm; 4.46 A):
1 out of 2 assignments used, quality = 0.93:
H PHE 8 + HB2 ASP 5 OK 93 97 100 95 3.6-4.4 231/1.8=91, 81/423=45
H ASP 11 - HB2 ASP 5 far 0 36 0 - 8.5-9.2
Violated in 0 structures by 0.00 A.
Peak 230 from 2DNOESY.peaks (7.69, 2.98 ppm; 3.85 A):
1 out of 4 assignments used, quality = 0.90:
H PHE 8 + HB3 ASP 5 OK 90 96 100 94 2.9-3.3 229/1.8=58, 81/452=55...(7)
H ASP 11 - HD3 ARG 7 far 0 32 0 - 4.0-6.8
H PHE 8 - HD3 ARG 7 far 0 88 0 - 5.0-5.8
H ASP 11 - HB3 ASP 5 far 0 35 0 - 8.1-8.6
Violated in 0 structures by 0.00 A.
Peak 231 from 2DNOESY.peaks (7.69, 2.98 ppm; 3.85 A):
1 out of 4 assignments used, quality = 0.90:
H PHE 8 + HB3 ASP 5 OK 90 96 100 94 2.9-3.3 229/1.8=58, 81/452=55...(7)
H ASP 11 - HD3 ARG 7 far 0 32 0 - 4.0-6.8
H PHE 8 - HD3 ARG 7 far 0 88 0 - 5.0-5.8
H ASP 11 - HB3 ASP 5 far 0 35 0 - 8.1-8.6
Violated in 0 structures by 0.00 A.
Peak 232 from 2DNOESY.peaks (7.50, 4.27 ppm; 4.43 A):
1 out of 1 assignment used, quality = 0.86:
H ASP 5 + HA CYSS 3 OK 86 98 100 87 3.6-3.7 187/3.6=71, 326/3.0=54
Violated in 0 structures by 0.00 A.
Peak 233 from 2DNOESY.peaks (7.50, 4.16 ppm; 4.67 A):
1 out of 2 assignments used, quality = 0.84:
H ASP 5 + HA HIS+ 2 OK 84 100 100 84 3.8-4.1 187/363=63, 326/3.6=54
H ASP 5 - HA ASN 9 far 0 96 0 - 7.4-7.7
Violated in 0 structures by 0.00 A.
Peak 237 from 2DNOESY.peaks (7.79, 1.65 ppm; 3.48 A):
1 out of 1 assignment used, quality = 0.98:
H ARG 7 + HB2 ARG 7 OK 98 100 100 98 2.2-2.5 124/1.8=71, 3.9=69...(8)
Violated in 0 structures by 0.00 A.
Peak 239 from 2DNOESY.peaks (7.79, 7.69 ppm; 3.24 A):
1 out of 3 assignments used, quality = 0.85:
H ARG 7 + H PHE 8 OK 85 100 100 85 2.6-2.7 124/242=38, 4.5=37...(6)
H ARG 7 - H ASP 11 far 0 59 0 - 6.1-6.4
H ALA 19 - H PHE 8 far 0 85 0 - 9.5-13.4
Violated in 0 structures by 0.00 A.
Peak 240 from 2DNOESY.peaks (7.69, 3.91 ppm; 3.99 A):
2 out of 2 assignments used, quality = 1.00:
H PHE 8 + HA ARG 7 OK 100 100 100 100 3.5-3.5 3.6=100
H ASP 11 + HA ARG 7 OK 32 40 100 79 3.7-4.0 4.4/422=44, 4.4/421=42...(4)
Violated in 0 structures by 0.00 A.
Peak 241 from 2DNOESY.peaks (7.69, 2.97 ppm; 3.92 A):
1 out of 4 assignments used, quality = 0.64:
H PHE 8 + HB3 ASP 5 OK 64 70 100 92 2.9-3.3 229/1.8=61, 81/452=49...(7)
H ASP 11 - HD3 ARG 7 far 4 37 10 - 4.0-6.8
H PHE 8 - HD3 ARG 7 far 0 100 0 - 5.0-5.8
H ASP 11 - HB3 ASP 5 far 0 26 0 - 8.1-8.6
Violated in 0 structures by 0.00 A.
Peak 242 from 2DNOESY.peaks (7.69, 1.77 ppm; 3.62 A):
1 out of 2 assignments used, quality = 0.96:
H PHE 8 + HB3 ARG 7 OK 96 100 100 96 2.6-2.8 243/1.8=61, 239/124=53...(6)
H ASP 11 - HB3 ARG 7 far 0 41 0 - 5.5-6.0
Violated in 0 structures by 0.00 A.
Peak 243 from 2DNOESY.peaks (7.69, 1.64 ppm; 4.06 A increased from 3.82 A):
1 out of 2 assignments used, quality = 0.99:
H PHE 8 + HB2 ARG 7 OK 99 100 100 100 3.6-3.9 242/1.8=86, 4.7=66...(6)
H ASP 11 - HB2 ARG 7 far 0 37 0 - 6.0-6.3
Violated in 0 structures by 0.00 A.
Peak 244 from 2DNOESY.peaks (7.69, 1.45 ppm; 4.90 A):
1 out of 2 assignments used, quality = 0.99:
H PHE 8 + HG3 ARG 7 OK 99 100 100 100 4.4-4.9 242/2.9=88, 243/2.9=81...(4)
H ASP 11 - HG3 ARG 7 far 0 37 0 - 5.7-6.2
Violated in 2 structures by 0.00 A.
Peak 245 from 2DNOESY.peaks (7.69, 1.39 ppm; 4.85 A):
1 out of 4 assignments used, quality = 0.98:
H PHE 8 + HG2 ARG 7 OK 98 99 100 100 3.9-4.5 242/2.9=87, 243/2.9=80...(4)
H ASP 11 - HG2 ARG 7 poor 10 40 100 24 4.0-4.6 240/3.9=17, 3.9/412=2
H ASP 11 - HG13 ILE 15 far 0 39 0 - 8.1-8.4
H PHE 8 - HG13 ILE 15 far 0 96 0 - 9.6-9.9
Violated in 0 structures by 0.00 A.
Peak 246 from 2DNOESY.peaks (7.79, 4.79 ppm; 5.05 A):
1 out of 2 assignments used, quality = 1.00:
H ARG 7 + HA ASP 5 OK 100 100 100 100 4.0-4.2 273/2.5=91, 274/2.5=82...(4)
H ALA 19 - HA ASP 5 far 0 82 0 - 10.0-15.6
Violated in 0 structures by 0.00 A.
Peak 247 from 2DNOESY.peaks (7.79, 1.86 ppm; 4.35 A):
1 out of 1 assignment used, quality = 0.91:
H ARG 7 + HG3 PRO 6 OK 91 94 100 97 2.4-2.6 273/2.3=79, 274/2.3=66...(4)
Violated in 0 structures by 0.00 A.
Peak 248 from 2DNOESY.peaks (7.29, 3.99 ppm; 4.35 A):
1 out of 4 assignments used, quality = 1.00:
H HIS+ 12 + HA ASP 11 OK 100 100 100 100 3.4-3.5 3.6=100
HE ARG 7 - HA ASP 11 far 0 85 0 - 6.1-10.0
H HIS+ 12 - HA GLU 14 far 0 96 0 - 7.7-7.8
H HIS+ 12 - HA ILE 15 far 0 96 0 - 7.9-8.0
Violated in 0 structures by 0.00 A.
Peak 249 from 2DNOESY.peaks (6.07, 2.25 ppm; 3.99 A):
1 out of 3 assignments used, quality = 0.91:
HD2 HIS+ 12 + HB2 HIS+ 12 OK 91 91 100 100 3.4-3.6 3.9=100
HD2 HIS+ 12 - HB2 ASP 11 far 0 42 0 - 5.5-6.4
HD2 HIS+ 12 - HG3 GLU 14 far 0 91 0 - 7.2-10.6
Violated in 0 structures by 0.00 A.
Peak 250 from 2DNOESY.peaks (6.07, 2.60 ppm; 4.31 A):
1 out of 1 assignment used, quality = 0.97:
HD2 HIS+ 12 + HB3 HIS+ 12 OK 97 97 100 100 2.7-2.8 3.9=100
Violated in 0 structures by 0.00 A.
Peak 251 from 2DNOESY.peaks (7.29, 1.86 ppm; 5.22 A increased from 4.91 A):
1 out of 2 assignments used, quality = 0.32:
HE ARG 7 + HG3 PRO 6 OK 32 80 100 41 4.2-5.2 7.1/247=35
H HIS+ 12 - HG3 PRO 6 far 0 97 0 - 9.1-9.4
Violated in 0 structures by 0.00 A.
Peak 253 from 2DNOESY.peaks (7.29, 2.97 ppm; 3.52 A):
1 out of 4 assignments used, quality = 0.98:
HE ARG 7 + HD3 ARG 7 OK 98 98 100 100 2.3-2.9 2.9=100
HE ARG 7 - HB3 ASP 5 far 0 63 0 - 5.7-7.6
H HIS+ 12 - HD3 ARG 7 far 0 84 0 - 6.1-8.8
H HIS+ 12 - HB3 ASP 5 far 0 54 0 - 8.6-9.0
Violated in 0 structures by 0.00 A.
Peak 254 from 2DNOESY.peaks (7.29, 1.77 ppm; 4.73 A):
1 out of 2 assignments used, quality = 0.97:
HE ARG 7 + HB3 ARG 7 OK 97 97 100 99 2.8-4.5 4.9=89, 255/1.8=86...(4)
H HIS+ 12 - HB3 ARG 7 far 0 86 0 - 6.6-7.2
Violated in 0 structures by 0.00 A.
Peak 255 from 2DNOESY.peaks (7.29, 1.65 ppm; 4.41 A):
1 out of 2 assignments used, quality = 0.95:
HE ARG 7 + HB2 ARG 7 OK 95 99 100 96 2.0-3.6 4.9=72, 254/1.8=70...(4)
H HIS+ 12 - HB2 ARG 7 far 0 88 0 - 7.5-7.9
Violated in 0 structures by 0.00 A.
Peak 256 from 2DNOESY.peaks (7.29, 1.45 ppm; 4.67 A):
1 out of 2 assignments used, quality = 0.99:
HE ARG 7 + HG3 ARG 7 OK 99 99 100 100 2.5-4.0 3.7=100
H HIS+ 12 - HG3 ARG 7 far 0 85 0 - 7.1-7.7
Violated in 0 structures by 0.00 A.
Peak 257 from 2DNOESY.peaks (7.29, 1.39 ppm; 4.09 A):
1 out of 3 assignments used, quality = 1.00:
HE ARG 7 + HG2 ARG 7 OK 100 100 100 100 2.3-4.0 3.7=100
H HIS+ 12 - HG2 ARG 7 far 0 88 0 - 5.6-6.2
H HIS+ 12 - HG13 ILE 15 far 0 82 0 - 5.7-5.9
Violated in 0 structures by 0.00 A.
Peak 258 from 2DNOESY.peaks (3.22, 4.99 ppm; 3.34 A):
1 out of 1 assignment used, quality = 0.93:
HD3 PRO 13 + HA HIS+ 12 OK 93 93 100 100 3.0-3.0 2.5=100
Violated in 0 structures by 0.00 A.
Peak 259 from 2DNOESY.peaks (3.06, 4.99 ppm; 3.72 A):
1 out of 2 assignments used, quality = 0.99:
HD2 PRO 13 + HA HIS+ 12 OK 99 99 100 100 2.1-2.1 2.5=100
HB2 CYSS 3 - HA HIS+ 12 far 0 44 0 - 9.5-10.2
Violated in 0 structures by 0.00 A.
Peak 260 from 2DNOESY.peaks (3.23, 4.19 ppm; 4.60 A):
1 out of 1 assignment used, quality = 0.96:
HD3 PRO 13 + HA PRO 13 OK 96 96 100 100 3.6-3.6 3.6=100
Violated in 0 structures by 0.00 A.
Peak 261 from 2DNOESY.peaks (3.06, 4.19 ppm; 4.64 A):
1 out of 2 assignments used, quality = 1.00:
HD2 PRO 13 + HA PRO 13 OK 100 100 100 100 4.1-4.1 3.6=100
HB2 CYSS 3 - HA PRO 13 far 0 41 0 - 8.8-9.4
Violated in 0 structures by 0.00 A.
Peak 262 from 2DNOESY.peaks (2.00, 3.23 ppm; 4.53 A):
1 out of 4 assignments used, quality = 0.99:
HB3 PRO 13 + HD3 PRO 13 OK 99 99 100 100 3.0-3.0 3.0=100
HG2 GLU 14 - HD3 PRO 13 far 0 60 0 - 5.2-8.2
HB3 PRO 13 - HB3 CYSS 16 far 0 63 0 - 7.1-7.4
HG2 GLU 14 - HB3 CYSS 16 far 0 39 0 - 7.8-8.6
Violated in 0 structures by 0.00 A.
Peak 265 from 2DNOESY.peaks (1.68, 3.23 ppm; 3.19 A):
1 out of 4 assignments used, quality = 0.97:
HG3 PRO 13 + HD3 PRO 13 OK 97 97 100 100 3.0-3.0 2.3=100
HB2 GLU 14 - HD3 PRO 13 far 0 97 0 - 6.1-7.4
HB2 GLU 14 - HB3 CYSS 16 far 0 66 0 - 8.3-8.9
HG3 PRO 13 - HB3 CYSS 16 far 0 66 0 - 8.4-8.7
Violated in 0 structures by 0.00 A.
Peak 266 from 2DNOESY.peaks (2.00, 3.06 ppm; 4.27 A):
1 out of 2 assignments used, quality = 1.00:
HB3 PRO 13 + HD2 PRO 13 OK 100 100 100 100 3.9-3.9 3.0=100
HG2 GLU 14 - HD2 PRO 13 poor 10 61 35 44 3.7-6.7 5.0/278=37, ~442=6
Violated in 0 structures by 0.00 A.
Peak 267 from 2DNOESY.peaks (1.68, 3.06 ppm; 3.28 A):
1 out of 2 assignments used, quality = 0.97:
HG3 PRO 13 + HD2 PRO 13 OK 97 97 100 100 2.3-2.3 2.3=100
HB2 GLU 14 - HD2 PRO 13 far 0 95 0 - 4.7-5.9
Violated in 0 structures by 0.00 A.
Peak 268 from 2DNOESY.peaks (7.29, 3.23 ppm; 4.67 A):
1 out of 3 assignments used, quality = 0.99:
H HIS+ 12 + HD3 PRO 13 OK 99 99 100 100 3.0-3.2 4.8=92, 269/1.8=85...(4)
H HIS+ 12 - HB3 CYSS 16 far 0 59 0 - 6.8-7.6
HE ARG 7 - HD3 PRO 13 far 0 91 0 - 8.2-11.9
Violated in 0 structures by 0.00 A.
Peak 269 from 2DNOESY.peaks (7.29, 3.06 ppm; 4.39 A):
1 out of 3 assignments used, quality = 0.97:
H HIS+ 12 + HD2 PRO 13 OK 97 99 100 98 3.8-3.9 4.8=77, 268/1.8=71...(4)
H HIS+ 12 - HB2 CYSS 3 far 0 63 0 - 8.8-9.4
HE ARG 7 - HD2 PRO 13 far 0 87 0 - 9.6-13.1
Violated in 0 structures by 0.00 A.
Peak 270 from 2DNOESY.peaks (7.29, 1.69 ppm; 5.50 A increased from 5.29 A):
1 out of 3 assignments used, quality = 0.47:
H HIS+ 12 + HB ILE 15 OK 47 56 100 84 5.3-5.4 4.0/404=70, 94/405=43
H HIS+ 12 - HG3 PRO 13 far 0 98 0 - 5.6-5.8
H HIS+ 12 - HB2 GLU 14 far 0 99 0 - 7.9-8.7
Violated in 0 structures by 0.00 A.
Peak 271 from 2DNOESY.peaks (3.66, 4.07 ppm; 5.50 A):
1 out of 5 assignments used, quality = 0.99:
HD2 PRO 6 + HA PRO 6 OK 99 99 100 100 4.1-4.1 3.6=100
HA3 GLY 21 - HA ALA 19 far 0 37 0 - 6.0-7.8
HB3 SER 4 - HA PRO 6 far 0 97 0 - 8.8-8.9
HA3 GLY 22 - HA ALA 19 far 0 90 0 - 9.0-11.0
HB3 SER 4 - HA ALA 19 far 0 88 0 - 9.4-14.1
Violated in 0 structures by 0.00 A.
Peak 272 from 2DNOESY.peaks (3.66, 3.95 ppm; 3.06 A):
1 out of 2 assignments used, quality = 1.00:
HD2 PRO 6 + HD3 PRO 6 OK 100 100 100 100 1.8-1.8 1.8=100
HB3 SER 4 - HD3 PRO 6 far 0 100 0 - 7.7-7.9
Violated in 0 structures by 0.00 A.
Peak 273 from 2DNOESY.peaks (7.79, 3.66 ppm; 3.94 A):
1 out of 5 assignments used, quality = 0.91:
H ARG 7 + HD2 PRO 6 OK 91 99 100 92 2.6-2.7 247/2.3=59, 274/1.8=59...(4)
H ALA 19 - HA3 GLY 21 far 0 36 0 - 6.4-8.9
H ARG 7 - HB3 SER 4 far 0 100 0 - 8.8-9.2
H ALA 19 - HA3 GLY 22 far 0 77 0 - 8.9-11.9
H ALA 19 - HB3 SER 4 far 0 78 0 - 9.8-13.9
Violated in 0 structures by 0.00 A.
Peak 274 from 2DNOESY.peaks (7.79, 3.95 ppm; 4.55 A):
1 out of 1 assignment used, quality = 0.99:
H ARG 7 + HD3 PRO 6 OK 99 100 100 99 3.8-3.9 273/1.8=91, 247/2.3=76...(4)
Violated in 0 structures by 0.00 A.
Peak 276 from 2DNOESY.peaks (9.34, 4.19 ppm; 4.28 A):
1 out of 1 assignment used, quality = 0.98:
H GLU 14 + HA PRO 13 OK 98 98 100 100 3.4-3.4 3.6=100
Violated in 0 structures by 0.00 A.
Peak 277 from 2DNOESY.peaks (9.34, 3.23 ppm; 3.98 A):
1 out of 2 assignments used, quality = 0.95:
H GLU 14 + HD3 PRO 13 OK 95 99 100 95 4.0-4.0 278/1.8=62, 279/2.3=61...(4)
H GLU 14 - HB3 CYSS 16 far 0 46 0 - 6.4-6.6
Violated in 0 structures by 0.00 A.
Peak 278 from 2DNOESY.peaks (9.34, 3.06 ppm; 4.49 A):
1 out of 2 assignments used, quality = 0.98:
H GLU 14 + HD2 PRO 13 OK 98 99 100 99 2.9-2.9 277/1.8=89, 280/2.5=73...(5)
H GLU 14 - HB2 CYSS 3 far 0 49 0 - 9.3-10.0
Violated in 0 structures by 0.00 A.
Peak 279 from 2DNOESY.peaks (9.33, 1.68 ppm; 3.34 A):
2 out of 3 assignments used, quality = 0.79:
H GLU 14 + HG3 PRO 13 OK 73 96 100 76 3.1-3.1 277/2.3=47, 278/2.3=38
H GLU 14 + HB2 GLU 14 OK 23 96 25 95 3.0-3.7 3.7=74, 144/1.8=62...(5)
H GLU 14 - HB ILE 15 far 0 44 0 - 4.3-4.4
Violated in 0 structures by 0.00 A.
Peak 280 from 2DNOESY.peaks (9.34, 4.99 ppm; 4.28 A):
1 out of 1 assignment used, quality = 0.87:
H GLU 14 + HA HIS+ 12 OK 87 90 100 96 3.1-3.1 277/2.5=73, 278/2.5=63...(5)
Violated in 0 structures by 0.00 A.
Peak 281 from 2DNOESY.peaks (7.16, 2.60 ppm; 4.66 A):
1 out of 1 assignment used, quality = 0.95:
H ILE 15 + HB3 HIS+ 12 OK 95 96 100 99 4.1-4.4 3.8/404=65, 4.4/411=59...(6)
Violated in 0 structures by 0.00 A.
Peak 282 from 2DNOESY.peaks (7.16, 2.25 ppm; 4.90 A):
2 out of 3 assignments used, quality = 1.00:
H ILE 15 + HB2 HIS+ 12 OK 97 98 100 100 2.6-2.8 281/1.8=85, 160/374=53...(8)
H ILE 15 + HG3 GLU 14 OK 95 98 100 97 2.4-4.6 146/1.8=79, 159/5.0=58...(7)
H ILE 15 - HB2 ASP 11 far 0 52 0 - 9.0-9.3
Violated in 0 structures by 0.00 A.
Peak 283 from 2DNOESY.peaks (7.16, 1.40 ppm; 4.22 A):
1 out of 1 assignment used, quality = 0.99:
H ILE 15 + HG13 ILE 15 OK 99 100 100 99 1.9-2.1 4.5=85, 284/1.8=75...(7)
Violated in 0 structures by 0.00 A.
Peak 284 from 2DNOESY.peaks (7.16, 0.94 ppm; 4.31 A):
1 out of 1 assignment used, quality = 0.97:
H ILE 15 + HG12 ILE 15 OK 97 97 100 100 3.1-3.3 4.5=90, 407/1.8=79...(7)
Violated in 0 structures by 0.00 A.
Peak 285 from 2DNOESY.peaks (7.16, 0.74 ppm; 4.48 A):
1 out of 1 assignment used, quality = 1.00:
H ILE 15 + QG2 ILE 15 OK 100 100 100 100 3.8-3.8 4.0=100
Violated in 0 structures by 0.00 A.
Peak 286 from 2DNOESY.peaks (8.04, 3.98 ppm; 3.79 A):
2 out of 4 assignments used, quality = 1.00:
H CYSS 16 + HA ILE 15 OK 100 100 100 100 3.4-3.5 3.6=100
H CYSS 16 + HA GLU 14 OK 60 100 75 81 3.8-4.0 160/3.5=62, 161/2.9=43...(4)
H CYSS 16 - HA ALA 20 far 0 82 0 - 5.4-9.8
H CYSS 16 - HA ASP 11 far 0 96 0 - 8.8-9.1
Violated in 0 structures by 0.00 A.
Peak 287 from 2DNOESY.peaks (8.04, 4.18 ppm; 4.24 A increased from 3.99 A):
1 out of 1 assignment used, quality = 0.77:
H CYSS 16 + HA PRO 13 OK 77 96 100 80 3.9-4.2 354/328=60, 161/3.6=48
Violated in 0 structures by 0.00 A.
Peak 288 from 2DNOESY.peaks (7.53, 3.25 ppm; 4.30 A):
0 out of 2 assignments used, quality = 0.00:
HD21 ASN 9 - HB3 CYSS 16 lone 5 100 100 5 3.4-4.1
HD21 ASN 9 - HD3 PRO 13 far 0 49 0 - 8.7-9.2
Violated in 0 structures by 0.00 A.
Peak 289 from 2DNOESY.peaks (6.76, 4.15 ppm; 4.66 A increased from 3.92 A):
1 out of 2 assignments used, quality = 0.88:
QD PHE 8 + HA HIS+ 2 OK 88 88 100 100 4.5-4.7 220/3.0=75, 297/3.0=68...(7)
QD PHE 8 - HA ASN 9 far 5 96 5 - 4.6-5.1
Violated in 1 structures by 0.00 A.
Peak 290 from 2DNOESY.peaks (6.76, 4.26 ppm; 3.29 A):
1 out of 1 assignment used, quality = 0.67:
QD PHE 8 + HA CYSS 3 OK 67 100 100 67 2.0-2.1 2.2/432=35, 327/3.0=29
Violated in 0 structures by 0.00 A.
Peak 291 from 2DNOESY.peaks (6.76, 3.19 ppm; 3.33 A):
1 out of 1 assignment used, quality = 0.99:
QD PHE 8 + HB3 PHE 8 OK 99 99 100 100 2.5-2.7 2.5=100
Violated in 0 structures by 0.00 A.
Peak 293 from 2DNOESY.peaks (6.76, 2.98 ppm; 5.50 A increased from 4.76 A):
1 out of 2 assignments used, quality = 1.00:
QD PHE 8 + HB3 ASP 5 OK 100 100 100 100 5.3-5.5 2.5/452=98, 224/230=76...(4)
QD PHE 8 - HD3 ARG 7 far 0 70 0 - 6.7-7.9
Violated in 12 structures by 0.00 A.
Peak 294 from 2DNOESY.peaks (6.76, 2.84 ppm; 3.13 A):
1 out of 1 assignment used, quality = 1.00:
QD PHE 8 + HB2 PHE 8 OK 100 100 100 100 2.3-2.3 2.5=100
Violated in 0 structures by 0.00 A.
Peak 295 from 2DNOESY.peaks (6.76, 2.25 ppm; 4.96 A increased from 4.41 A):
1 out of 3 assignments used, quality = 0.99:
QD PHE 8 + HB2 HIS+ 12 OK 99 100 100 100 4.8-5.0 2.2/301=76, 310/3.9=65...(6)
QD PHE 8 - HB2 ASP 11 far 0 46 0 - 6.2-7.3
QD PHE 8 - HG3 GLU 14 far 0 99 0 - 8.3-10.7
Violated in 3 structures by 0.00 A.
Peak 296 from 2DNOESY.peaks (6.76, 1.94 ppm; 4.59 A):
1 out of 1 assignment used, quality = 1.00:
QD PHE 8 + HB3 HIS+ 2 OK 100 100 100 100 2.8-3.5 297/1.8=82, 2.2/300=75...(8)
Violated in 0 structures by 0.00 A.
Peak 297 from 2DNOESY.peaks (6.76, 1.74 ppm; 4.43 A):
1 out of 2 assignments used, quality = 0.99:
QD PHE 8 + HB2 HIS+ 2 OK 99 99 100 100 2.9-3.3 2.2/304=76, 296/1.8=74...(8)
QD PHE 8 - HB2 PRO 6 far 0 100 0 - 8.4-8.6
Violated in 0 structures by 0.00 A.
Peak 298 from 2DNOESY.peaks (6.76, 0.73 ppm; 4.26 A increased from 4.01 A):
1 out of 1 assignment used, quality = 0.99:
QD PHE 8 + QG2 ILE 15 OK 99 100 100 99 3.7-4.1 2.2/306=88, 3.8/307=56...(5)
Violated in 0 structures by 0.00 A.
Peak 299 from 2DNOESY.peaks (6.76, 0.59 ppm; 4.67 A increased from 4.15 A):
1 out of 1 assignment used, quality = 0.97:
QD PHE 8 + QD1 ILE 15 OK 97 97 100 100 4.2-4.4 2.2/308=94, 3.8/309=73...(6)
Violated in 0 structures by 0.00 A.
Peak 300 from 2DNOESY.peaks (6.68, 1.94 ppm; 4.51 A):
1 out of 1 assignment used, quality = 0.99:
QE PHE 8 + HB3 HIS+ 2 OK 99 99 100 100 3.6-4.5 304/1.8=84, 2.2/296=71...(7)
Violated in 0 structures by 0.00 A.
Peak 301 from 2DNOESY.peaks (6.68, 2.25 ppm; 4.94 A increased from 4.16 A):
1 out of 3 assignments used, quality = 0.99:
QE PHE 8 + HB2 HIS+ 12 OK 99 99 100 100 4.7-4.7 437/1.8=90, 2.2/295=75...(6)
QE PHE 8 - HB2 ASP 11 far 0 43 0 - 7.5-8.4
QE PHE 8 - HG3 GLU 14 far 0 98 0 - 7.9-9.9
Violated in 0 structures by 0.00 A.
Peak 302 from 2DNOESY.peaks (6.58, 2.25 ppm; 5.40 A increased from 5.08 A):
1 out of 3 assignments used, quality = 0.99:
HZ PHE 8 + HB2 HIS+ 12 OK 99 99 100 100 5.2-5.3 2.2/301=86, ~437=73...(6)
HZ PHE 8 - HG3 GLU 14 far 0 98 0 - 8.3-10.9
HZ PHE 8 - HB2 ASP 11 far 0 43 0 - 9.7-10.6
Violated in 0 structures by 0.00 A.
Peak 303 from 2DNOESY.peaks (6.58, 1.94 ppm; 5.26 A):
1 out of 1 assignment used, quality = 0.93:
HZ PHE 8 + HB3 HIS+ 2 OK 93 98 95 100 4.4-5.5 2.2/300=90, 305/1.8=89...(5)
Violated in 1 structures by 0.01 A.
Peak 304 from 2DNOESY.peaks (6.68, 1.74 ppm; 4.27 A):
1 out of 1 assignment used, quality = 0.99:
QE PHE 8 + HB2 HIS+ 2 OK 99 99 100 100 2.9-3.4 300/1.8=71, 2.2/297=68...(7)
Violated in 0 structures by 0.00 A.
Peak 305 from 2DNOESY.peaks (6.58, 1.74 ppm; 4.88 A):
1 out of 1 assignment used, quality = 0.95:
HZ PHE 8 + HB2 HIS+ 2 OK 95 95 100 100 3.5-3.9 2.2/304=87, 303/1.8=71...(5)
Violated in 0 structures by 0.00 A.
Peak 306 from 2DNOESY.peaks (6.68, 0.73 ppm; 3.43 A):
1 out of 1 assignment used, quality = 0.95:
QE PHE 8 + QG2 ILE 15 OK 95 100 100 95 2.2-2.7 2.2/307=53, 308/450=51...(7)
Violated in 0 structures by 0.00 A.
Peak 307 from 2DNOESY.peaks (6.58, 0.74 ppm; 3.93 A):
1 out of 1 assignment used, quality = 0.98:
HZ PHE 8 + QG2 ILE 15 OK 98 100 100 98 2.1-2.6 2.2/306=80, 309/450=67...(5)
Violated in 0 structures by 0.00 A.
Peak 308 from 2DNOESY.peaks (6.68, 0.59 ppm; 3.51 A):
1 out of 1 assignment used, quality = 0.97:
QE PHE 8 + QD1 ILE 15 OK 97 100 100 98 3.1-3.4 2.2/309=67, 306/450=55...(8)
Violated in 0 structures by 0.00 A.
Peak 309 from 2DNOESY.peaks (6.58, 0.59 ppm; 3.46 A):
1 out of 1 assignment used, quality = 0.92:
HZ PHE 8 + QD1 ILE 15 OK 92 98 100 93 3.1-3.3 2.2/308=64, 307/450=45...(6)
Violated in 0 structures by 0.00 A.
Peak 310 from 2DNOESY.peaks (6.76, 6.07 ppm; 4.35 A):
1 out of 1 assignment used, quality = 0.98:
QD PHE 8 + HD2 HIS+ 12 OK 98 100 100 98 2.3-2.9 2.2/311=73, 3.7/340=59...(5)
Violated in 0 structures by 0.00 A.
Peak 311 from 2DNOESY.peaks (6.68, 6.07 ppm; 4.28 A):
1 out of 1 assignment used, quality = 0.98:
QE PHE 8 + HD2 HIS+ 12 OK 98 99 100 99 2.3-2.8 2.2/310=70, 2.2/312=58...(6)
Violated in 0 structures by 0.00 A.
Peak 312 from 2DNOESY.peaks (6.58, 6.07 ppm; 4.90 A):
1 out of 1 assignment used, quality = 0.97:
HZ PHE 8 + HD2 HIS+ 12 OK 97 97 100 99 3.8-4.5 2.2/311=87, 309/358=67...(5)
Violated in 0 structures by 0.00 A.
Peak 313 from 2DNOESY.peaks (8.11, 6.07 ppm; 4.77 A):
1 out of 1 assignment used, quality = 1.00:
HE1 HIS+ 12 + HD2 HIS+ 12 OK 100 100 100 100 4.2-4.2 4.2=100
Violated in 0 structures by 0.00 A.
Peak 314 from 2DNOESY.peaks (8.11, 4.01 ppm; 3.81 A):
0 out of 4 assignments used, quality = 0.00:
HE1 HIS+ 12 - HA ASP 11 far 0 53 0 - 5.8-6.6
HE1 HIS+ 12 - HA PHE 8 far 0 94 0 - 6.6-7.1
HE1 HIS+ 12 - HA ILE 15 far 0 37 0 - 8.1-8.7
HE1 HIS+ 12 - HA GLU 14 far 0 37 0 - 9.8-10.2
Violated in 20 structures by 1.85 A.
Peak 315 from 2DNOESY.peaks (8.11, 2.23 ppm; 3.92 A):
0 out of 3 assignments used, quality = 0.00:
HE1 HIS+ 12 - HB2 HIS+ 12 far 0 49 0 - 4.9-5.0
HE1 HIS+ 12 - HB2 ASP 11 far 0 100 0 - 5.4-6.5
HE1 HIS+ 12 - HG3 GLU 14 far 0 53 0 - 6.4-10.1
Violated in 20 structures by 0.75 A.
Peak 316 from 2DNOESY.peaks (8.11, 1.86 ppm; 4.07 A):
0 out of 0 assignments used, quality = 0.00:
Peak 317 from 2DNOESY.peaks (8.11, 6.68 ppm; 4.01 A):
0 out of 1 assignment used, quality = 0.00:
HE1 HIS+ 12 - QE PHE 8 far 0 99 0 - 5.4-5.9
Violated in 20 structures by 1.64 A.
Peak 318 from 2DNOESY.peaks (8.11, 6.76 ppm; 3.73 A):
0 out of 1 assignment used, quality = 0.00:
HE1 HIS+ 12 - QD PHE 8 far 0 97 0 - 6.3-6.5
Violated in 20 structures by 2.61 A.
Peak 319 from 2DNOESY.peaks (8.57, 3.55 ppm; 3.43 A):
1 out of 1 assignment used, quality = 0.89:
H HIS+ 2 + HA3 GLY 1 OK 89 100 100 89 2.1-3.1 3.6=88
Violated in 0 structures by 0.00 A.
Peak 320 from 2DNOESY.peaks (8.57, 3.40 ppm; 3.79 A):
1 out of 1 assignment used, quality = 1.00:
H HIS+ 2 + HA2 GLY 1 OK 100 100 100 100 3.2-3.6 3.6=100
Violated in 0 structures by 0.00 A.
Peak 321 from 2DNOESY.peaks (8.57, 8.36 ppm; 4.50 A):
0 out of 0 assignments used, quality = 0.00:
Peak 322 from 2DNOESY.peaks (8.36, 7.88 ppm; 4.25 A):
0 out of 0 assignments used, quality = 0.00:
Peak 323 from 2DNOESY.peaks (7.90, 1.94 ppm; 4.89 A):
1 out of 1 assignment used, quality = 1.00:
H CYSS 3 + HB3 HIS+ 2 OK 100 100 100 100 3.8-4.3 4.2=100
Violated in 0 structures by 0.00 A.
Peak 324 from 2DNOESY.peaks (7.90, 1.74 ppm; 4.71 A):
1 out of 2 assignments used, quality = 0.99:
H CYSS 3 + HB2 HIS+ 2 OK 99 99 100 100 2.9-4.0 4.2=100
H CYSS 3 - HB3 ARG 7 far 0 40 0 - 8.2-8.7
Violated in 0 structures by 0.00 A.
Peak 325 from 2DNOESY.peaks (7.90, 7.62 ppm; 3.51 A):
1 out of 1 assignment used, quality = 0.89:
H CYSS 3 + H SER 4 OK 89 99 100 89 2.6-2.7 4.6=43, 349/188=38...(5)
Violated in 0 structures by 0.00 A.
Peak 326 from 2DNOESY.peaks (7.90, 7.50 ppm; 4.95 A):
1 out of 1 assignment used, quality = 0.97:
H CYSS 3 + H ASP 5 OK 97 98 100 99 4.3-4.5 325/187=83, 3.0/232=75
Violated in 0 structures by 0.00 A.
Peak 327 from 2DNOESY.peaks (7.90, 6.76 ppm; 4.77 A):
1 out of 1 assignment used, quality = 0.99:
H CYSS 3 + QD PHE 8 OK 99 99 100 100 2.7-3.1 3.0/290=90, 3.6/289=61...(7)
Violated in 0 structures by 0.00 A.
Peak 328 from 2DNOESY.peaks (8.19, 4.18 ppm; 4.03 A increased from 3.80 A):
1 out of 1 assignment used, quality = 0.53:
H GLY 17 + HA PRO 13 OK 53 99 100 54 3.5-3.8 354/287=52
Violated in 0 structures by 0.00 A.
Peak 329 from 2DNOESY.peaks (8.19, 2.54 ppm; 4.36 A):
1 out of 4 assignments used, quality = 0.99:
H GLY 17 + HB2 CYSS 16 OK 99 99 100 100 2.3-3.1 4.3=100
H GLY 17 - HB3 ASN 9 far 0 76 0 - 6.7-7.4
H GLY 21 - HB2 CYSS 16 far 0 69 0 - 6.8-10.0
H GLY 21 - HB3 ASN 9 far 0 53 0 - 9.2-12.7
Violated in 0 structures by 0.00 A.
Peak 330 from 2DNOESY.peaks (8.19, 3.25 ppm; 4.90 A):
1 out of 3 assignments used, quality = 0.99:
H GLY 17 + HB3 CYSS 16 OK 99 99 100 100 2.6-3.6 4.3=100
H GLY 21 - HB3 CYSS 16 far 0 77 0 - 5.9-8.6
H GLY 17 - HD3 PRO 13 far 0 59 0 - 6.6-7.2
Violated in 0 structures by 0.00 A.
Peak 331 from 2DNOESY.peaks (8.15, 3.80 ppm; 3.53 A):
1 out of 1 assignment used, quality = 0.97:
H GLY 18 + HA2 GLY 17 OK 97 99 100 98 2.2-3.5 3.6=98
Violated in 0 structures by 0.00 A.
Peak 332 from 2DNOESY.peaks (8.15, 4.03 ppm; 3.97 A):
1 out of 2 assignments used, quality = 1.00:
H GLY 18 + HA3 GLY 17 OK 100 100 100 100 2.1-3.6 3.6=100
H GLY 18 - HA PHE 8 far 0 82 0 - 9.1-13.2
Violated in 0 structures by 0.00 A.
Peak 334 from 2DNOESY.peaks (8.18, 3.99 ppm; 3.25 A):
1 out of 9 assignments used, quality = 0.81:
H GLY 21 + HA ALA 20 OK 81 100 100 81 2.2-2.8 3.6=75, 355/337=21
H GLY 17 - HA GLU 14 lone 4 64 60 11 3.1-3.9 354/286=9
H GLY 21 - HA SER 4 far 0 99 0 - 4.1-9.9
H GLY 17 - HA ILE 15 far 0 64 0 - 4.6-5.7
H GLY 17 - HA ALA 20 far 0 78 0 - 6.0-9.0
H GLY 21 - HA ILE 15 far 0 82 0 - 7.4-12.4
HE1 HIS+ 2 - HA PHE 8 far 0 47 0 - 7.9-9.7
H GLY 17 - HA PHE 8 far 0 41 0 - 8.4-8.8
H GLY 17 - HA ASP 11 far 0 74 0 - 9.6-10.1
Violated in 0 structures by 0.00 A.
Peak 335 from 2DNOESY.peaks (8.18, 3.64 ppm; 3.02 A):
1 out of 7 assignments used, quality = 1.00:
H GLY 21 + HA3 GLY 21 OK 100 100 100 100 2.3-3.0 3.0=100
H GLY 21 - HA3 GLY 22 far 0 53 0 - 4.2-5.3
H GLY 21 - HB3 SER 4 far 0 46 0 - 4.8-9.6
HE1 HIS+ 2 - HA3 GLY 22 far 0 45 0 - 7.2-10.6
HE1 HIS+ 2 - HB3 SER 4 far 0 39 0 - 8.7-11.1
H GLY 17 - HA3 GLY 21 far 0 74 0 - 9.6-11.9
H GLY 17 - HA3 GLY 22 far 0 39 0 - 9.9-13.4
Violated in 0 structures by 0.00 A.
Peak 336 from 2DNOESY.peaks (8.18, 1.10 ppm; 3.70 A):
1 out of 3 assignments used, quality = 1.00:
H GLY 21 + QB ALA 20 OK 100 100 100 100 2.3-3.7 3.6=100
H GLY 17 - QB ALA 20 far 0 78 0 - 4.7-9.3
HE1 HIS+ 2 - QB ALA 20 far 0 88 0 - 8.5-13.3
Violated in 0 structures by 0.00 A.
Peak 337 from 2DNOESY.peaks (7.87, 3.99 ppm; 5.24 A increased from 4.93 A):
1 out of 4 assignments used, quality = 0.77:
H GLY 22 + HA ALA 20 OK 77 100 90 86 4.0-5.4 355/3.6=85
H GLY 22 - HA SER 4 far 5 99 5 - 5.2-9.1
H GLY 22 - HA ILE 15 far 0 82 0 - 8.1-11.0
H GLY 22 - HA PHE 8 far 0 53 0 - 9.7-12.3
Violated in 3 structures by 0.02 A.
Peak 338 from 2DNOESY.peaks (7.88, 1.19 ppm; 4.32 A):
0 out of 1 assignment used, quality = 0.00:
H GLY 22 - QB ALA 19 far 0 100 0 - 4.9-8.1
Violated in 20 structures by 2.48 A.
Peak 339 from 2DNOESY.peaks (7.88, 3.50 ppm; 3.89 A):
2 out of 2 assignments used, quality = 1.00:
H GLY 22 + HA2 GLY 22 OK 100 100 100 100 2.3-3.0 3.0=100
H GLY 22 + HA2 GLY 21 OK 88 88 100 100 2.4-3.6 3.6=100
Violated in 0 structures by 0.00 A.
Peak 340 from 2DNOESY.peaks (6.07, 4.01 ppm; 4.00 A):
1 out of 3 assignments used, quality = 0.72:
HD2 HIS+ 12 + HA PHE 8 OK 72 100 100 72 2.9-3.2 310/3.7=46, 311/434=37
HD2 HIS+ 12 - HA ASP 11 far 0 37 0 - 6.4-6.9
HD2 HIS+ 12 - HA ALA 20 far 0 56 0 - 9.3-13.9
Violated in 0 structures by 0.00 A.
Peak 341 from 2DNOESY.peaks (7.53, 6.72 ppm; 2.40 A):
1 out of 2 assignments used, quality = 1.00:
HD21 ASN 9 + HD22 ASN 9 OK 100 100 100 100 1.7-1.7 1.7=100
HD21 ASN 9 - HD2 HIS+ 2 far 0 100 0 - 8.8-9.4
Violated in 0 structures by 0.00 A.
Peak 342 from 2DNOESY.peaks (7.53, 4.26 ppm; 4.53 A):
1 out of 1 assignment used, quality = 0.91:
HD21 ASN 9 + HA CYSS 3 OK 91 99 100 92 2.1-2.3 1.7/438=72, 350/3.0=68
Violated in 0 structures by 0.00 A.
Peak 343 from 2DNOESY.peaks (7.53, 4.15 ppm; 4.52 A):
1 out of 2 assignments used, quality = 0.97:
HD21 ASN 9 + HA ASN 9 OK 97 97 100 100 3.7-4.0 4.4=100
HD21 ASN 9 - HA HIS+ 2 far 0 90 0 - 6.6-6.9
Violated in 0 structures by 0.00 A.
Peak 345 from 2DNOESY.peaks (7.53, 4.00 ppm; 5.27 A increased from 4.68 A):
0 out of 5 assignments used, quality = 0.00:
HD21 ASN 9 - HA ALA 20 far 15 99 15 - 4.4-9.1
HD21 ASN 9 - HA SER 4 lone 8 100 90 9 4.9-5.5
HD21 ASN 9 - HA PHE 8 far 0 60 0 - 5.5-5.5
HD21 ASN 9 - HA ILE 15 far 0 76 0 - 8.7-9.2
HD21 ASN 9 - HA GLU 14 far 0 76 0 - 9.3-10.1
Violated in 0 structures by 0.00 A.
Peak 346 from 2DNOESY.peaks (7.53, 4.07 ppm; 4.71 A):
1 out of 2 assignments used, quality = 0.95:
HD21 ASN 9 + HA PRO 6 OK 95 100 100 96 4.1-4.5 3.5/386=75, 1.7/440=69
HD21 ASN 9 - HA ALA 19 far 0 82 0 - 6.6-10.9
Violated in 0 structures by 0.00 A.
Peak 347 from 2DNOESY.peaks (7.53, 3.25 ppm; 4.30 A):
0 out of 2 assignments used, quality = 0.00:
HD21 ASN 9 - HB3 CYSS 16 lone 5 100 100 5 3.4-4.1
HD21 ASN 9 - HD3 PRO 13 far 0 53 0 - 8.7-9.2
Violated in 0 structures by 0.00 A.
Peak 349 from 2DNOESY.peaks (7.90, 2.87 ppm; 3.29 A):
1 out of 1 assignment used, quality = 0.88:
H CYSS 3 + HB3 CYSS 3 OK 88 100 100 88 2.7-2.9 103/1.8=58, 3.9=58, 325/188=31
Violated in 0 structures by 0.00 A.
Peak 350 from 2DNOESY.peaks (7.53, 3.08 ppm; 4.24 A increased from 3.77 A):
1 out of 2 assignments used, quality = 0.74:
HD21 ASN 9 + HB2 CYSS 3 OK 74 100 100 74 4.0-4.2 342/3.0=56, ~438=37
HD21 ASN 9 - HD2 PRO 13 far 0 53 0 - 9.4-9.9
Violated in 2 structures by 0.00 A.
Peak 351 from 2DNOESY.peaks (7.53, 2.86 ppm; 3.31 A):
0 out of 2 assignments used, quality = 0.00:
HD21 ASN 9 - HB2 PHE 8 lone 7 53 100 14 3.0-3.1 5.7/198=12
HD21 ASN 9 - HB3 CYSS 3 far 0 92 0 - 3.8-4.2
Violated in 0 structures by 0.00 A.
Peak 352 from 2DNOESY.peaks (7.53, 2.56 ppm; 3.74 A):
1 out of 2 assignments used, quality = 0.85:
HD21 ASN 9 + HB3 ASN 9 OK 85 100 85 100 3.6-4.1 3.5=100
HD21 ASN 9 - HB2 CYSS 16 far 12 82 15 - 3.6-4.4
Violated in 3 structures by 0.05 A.
Peak 353 from 2DNOESY.peaks (8.19, 4.72 ppm; 4.14 A):
1 out of 2 assignments used, quality = 0.98:
H GLY 17 + HA CYSS 16 OK 98 98 100 100 3.5-3.6 3.6=100
H GLY 21 - HA CYSS 16 far 0 65 0 - 4.8-8.3
Violated in 0 structures by 0.00 A.
Peak 354 from 2DNOESY.peaks (8.19, 8.04 ppm; 3.37 A):
1 out of 2 assignments used, quality = 0.80:
H GLY 17 + H CYSS 16 OK 80 99 100 81 1.9-2.6 4.7=38, 4.3/150=34...(4)
H GLY 21 - H CYSS 16 far 0 65 0 - 7.5-11.1
Violated in 0 structures by 0.00 A.
Peak 355 from 2DNOESY.peaks (8.18, 7.88 ppm; 3.66 A):
1 out of 6 assignments used, quality = 0.69:
H GLY 21 + H GLY 22 OK 69 98 100 70 1.9-3.6 4.7=49, 3.6/337=29, 3.0/179=16
H GLY 21 - H CYSS 3 far 0 42 0 - 4.9-6.9
HE1 HIS+ 2 - H CYSS 3 far 0 33 0 - 6.7-7.9
HE1 HIS+ 2 - H GLY 22 far 0 77 0 - 8.4-12.0
H GLY 17 - H CYSS 3 far 0 28 0 - 8.9-9.5
H GLY 17 - H GLY 22 far 0 65 0 - 9.2-11.9
Violated in 0 structures by 0.00 A.
Peak 356 from 2DNOESY.peaks (8.19, 6.72 ppm; 5.04 A):
1 out of 4 assignments used, quality = 1.00:
HE1 HIS+ 2 + HD2 HIS+ 2 OK 100 100 100 100 4.2-4.2 4.2=100
H GLY 17 - HD22 ASN 9 far 10 98 10 - 5.1-7.5
H GLY 21 - HD22 ASN 9 far 0 85 0 - 7.3-10.8
H GLY 21 - HD2 HIS+ 2 far 0 85 0 - 8.6-12.8
Violated in 0 structures by 0.00 A.
Peak 357 from 2DNOESY.peaks (6.07, 1.86 ppm; 4.59 A):
0 out of 0 assignments used, quality = 0.00:
Peak 358 from 2DNOESY.peaks (6.07, 0.60 ppm; 4.41 A):
1 out of 1 assignment used, quality = 0.96:
HD2 HIS+ 12 + QD1 ILE 15 OK 96 99 100 97 2.7-3.2 3.9/411=60, 311/308=59...(5)
Violated in 0 structures by 0.00 A.
Peak 359 from 2DNOESY.peaks (6.07, 4.99 ppm; 4.93 A):
1 out of 1 assignment used, quality = 0.95:
HD2 HIS+ 12 + HA HIS+ 12 OK 95 95 100 100 4.7-4.8 4.7=100
Violated in 0 structures by 0.00 A.
Peak 360 from 2DNOESY.peaks (6.76, 3.08 ppm; 5.01 A):
1 out of 2 assignments used, quality = 0.98:
QD PHE 8 + HB2 CYSS 3 OK 98 99 100 99 2.7-2.9 290/3.0=93, 327/103=63, ~432=49
QD PHE 8 - HD2 PRO 13 far 0 46 0 - 8.0-8.1
Violated in 0 structures by 0.00 A.
Peak 361 from 2DNOESY.peaks (8.35, 3.54 ppm; 3.16 A):
0 out of 0 assignments used, quality = 0.00:
Peak 363 from 2DNOESY.peaks (7.63, 4.16 ppm; 4.47 A):
1 out of 2 assignments used, quality = 0.87:
H SER 4 + HA HIS+ 2 OK 87 100 100 88 3.1-3.7 325/3.6=71, 187/233=55
H SER 4 - HA ASN 9 far 0 98 0 - 8.2-8.5
Violated in 0 structures by 0.00 A.
Peak 364 from 2DNOESY.peaks (8.58, 4.07 ppm; 4.11 A):
1 out of 3 assignments used, quality = 0.77:
H ASN 9 + HA PRO 6 OK 77 97 100 79 3.4-3.5 84/386=60, 5.7/346=27
H HIS+ 2 - HA PRO 6 far 0 72 0 - 9.8-10.1
H HIS+ 2 - HA ALA 19 far 0 54 0 - 10.0-12.6
Violated in 0 structures by 0.00 A.
Peak 365 from 2DNOESY.peaks (8.58, 2.98 ppm; 5.50 A increased from 4.83 A):
1 out of 3 assignments used, quality = 0.99:
H ASN 9 + HB3 ASP 5 OK 99 100 100 99 5.2-5.5 221/231=89, 4.3/452=79
H ASN 9 - HD3 ARG 7 lone 3 73 40 11 5.3-6.8
H HIS+ 2 - HB3 ASP 5 far 0 70 0 - 6.6-7.4
Violated in 15 structures by 0.01 A.
Peak 366 from 2DNOESY.peaks (6.88, 6.52 ppm; 2.61 A):
1 out of 1 assignment used, quality = 1.00:
QD TYR 10 + QE TYR 10 OK 100 100 100 100 2.2-2.2 2.2=100
Violated in 0 structures by 0.00 A.
Peak 367 from 2DNOESY.peaks (6.82, 6.52 ppm; 3.35 A):
1 out of 1 assignment used, quality = 1.00:
HH TYR 10 + QE TYR 10 OK 100 100 100 100 2.2-2.6 2.6=100
Violated in 0 structures by 0.00 A.
Peak 368 from 2DNOESY.peaks (6.52, 6.51 ppm; diagonal):
1 out of 1 assignment used, quality = 1.00:
QE TYR 10 + QE TYR 10 OK 100 100 - 100
Peak 369 from 2DNOESY.peaks (6.52, 2.78 ppm; 5.15 A):
1 out of 1 assignment used, quality = 1.00:
QE TYR 10 + HB2 TYR 10 OK 100 100 100 100 4.4-4.5 4.4=100
Violated in 0 structures by 0.00 A.
Peak 370 from 2DNOESY.peaks (6.51, 2.89 ppm; 5.31 A):
1 out of 1 assignment used, quality = 0.99:
QE TYR 10 + HB3 TYR 10 OK 99 99 100 100 4.4-4.5 4.4=100
Violated in 0 structures by 0.00 A.
Peak 371 from 2DNOESY.peaks (6.52, 3.75 ppm; 5.50 A):
1 out of 1 assignment used, quality = 1.00:
QE TYR 10 + HA TYR 10 OK 100 100 100 100 4.3-4.7 2.2/205=100, 5.7=92, ~217=63
Violated in 0 structures by 0.00 A.
Peak 372 from 2DNOESY.peaks (6.88, 3.99 ppm; 4.32 A):
1 out of 1 assignment used, quality = 0.87:
QD TYR 10 + HA ASP 11 OK 87 100 100 88 3.3-4.3 215/3.0=65, ~212=40, ~211=38
Violated in 0 structures by 0.00 A.
Peak 373 from 2DNOESY.peaks (6.88, 3.92 ppm; 5.10 A):
1 out of 1 assignment used, quality = 0.99:
QD TYR 10 + HA ARG 7 OK 99 99 100 99 4.0-4.9 2.5/422=93, 2.5/421=90
Violated in 0 structures by 0.00 A.
Peak 374 from 2DNOESY.peaks (8.04, 2.26 ppm; 4.85 A):
2 out of 2 assignments used, quality = 0.92:
H CYSS 16 + HB2 HIS+ 12 OK 90 96 100 94 3.7-4.1 157/414=48, 151/405=47...(7)
H CYSS 16 + HG3 GLU 14 OK 20 94 25 85 4.8-6.5 161/5.0=47, 160/282=31...(6)
Violated in 0 structures by 0.00 A.
Peak 375 from 2DNOESY.peaks (7.78, 3.58 ppm; 3.81 A):
0 out of 0 assignments used, quality = 0.00:
Peak 376 from 2DNOESY.peaks (8.15, 7.78 ppm; 3.64 A):
1 out of 1 assignment used, quality = 0.50:
H GLY 18 + H ALA 19 OK 50 99 100 51 2.2-3.3 4.6=49
Violated in 0 structures by 0.00 A.
Peak 377 from 2DNOESY.peaks (3.55, 3.40 ppm; 3.20 A):
1 out of 1 assignment used, quality = 0.98:
HA3 GLY 1 + HA2 GLY 1 OK 98 98 100 100 1.8-1.8 1.8=100
Violated in 0 structures by 0.00 A.
Peak 378 from 2DNOESY.peaks (1.94, 4.15 ppm; 4.41 A):
1 out of 2 assignments used, quality = 0.96:
HB3 HIS+ 2 + HA HIS+ 2 OK 96 96 100 100 2.4-2.7 3.0=100
HB3 HIS+ 2 - HA ASN 9 far 0 98 0 - 7.5-8.2
Violated in 0 structures by 0.00 A.
Peak 379 from 2DNOESY.peaks (1.74, 4.16 ppm; 4.28 A):
1 out of 3 assignments used, quality = 0.97:
HB2 HIS+ 2 + HA HIS+ 2 OK 97 97 100 100 3.0-3.0 3.0=100
HB2 PRO 6 - HA ASN 9 far 0 93 0 - 7.0-7.1
HB2 HIS+ 2 - HA ASN 9 far 0 97 0 - 7.7-8.4
Violated in 0 structures by 0.00 A.
Peak 380 from 2DNOESY.peaks (3.08, 4.26 ppm; 5.22 A):
1 out of 1 assignment used, quality = 1.00:
HB2 CYSS 3 + HA CYSS 3 OK 100 100 100 100 2.6-2.7 3.0=100
Violated in 0 structures by 0.00 A.
Peak 381 from 2DNOESY.peaks (2.87, 4.26 ppm; 3.56 A):
1 out of 1 assignment used, quality = 1.00:
HB3 CYSS 3 + HA CYSS 3 OK 100 100 100 100 3.0-3.0 3.0=100
Violated in 0 structures by 0.00 A.
Peak 382 from 2DNOESY.peaks (3.72, 4.00 ppm; 3.34 A):
1 out of 3 assignments used, quality = 1.00:
HB2 SER 4 + HA SER 4 OK 100 100 100 100 2.3-2.6 3.0=100
HB2 SER 4 - HA ALA 20 far 0 98 0 - 6.4-12.2
HB2 SER 4 - HA PHE 8 far 0 63 0 - 9.9-10.4
Violated in 0 structures by 0.00 A.
Peak 383 from 2DNOESY.peaks (3.66, 4.00 ppm; 3.11 A):
1 out of 10 assignments used, quality = 0.99:
HB3 SER 4 + HA SER 4 OK 99 99 100 100 2.3-2.6 3.0=100
HA3 GLY 22 - HA SER 4 far 0 100 0 - 5.2-9.1
HA3 GLY 22 - HA ALA 20 far 0 99 0 - 5.8-7.4
HB3 SER 4 - HA ALA 20 far 0 98 0 - 5.9-10.7
HD2 PRO 6 - HA SER 4 far 0 100 0 - 7.0-7.0
HD2 PRO 6 - HA PHE 8 far 0 63 0 - 7.5-7.6
HA3 GLY 22 - HA ILE 15 far 0 73 0 - 8.9-13.1
HA3 GLY 22 - HA PHE 8 far 0 63 0 - 9.2-12.2
HB3 SER 4 - HA PHE 8 far 0 62 0 - 9.6-10.3
HD2 PRO 6 - HA ALA 20 far 0 99 0 - 9.7-15.5
Violated in 0 structures by 0.00 A.
Peak 384 from 2DNOESY.peaks (2.98, 4.79 ppm; 3.94 A):
1 out of 2 assignments used, quality = 0.97:
HB3 ASP 5 + HA ASP 5 OK 97 97 100 100 3.0-3.0 3.0=100
HD3 ARG 7 - HA ASP 5 far 0 56 0 - 7.5-8.6
Violated in 0 structures by 0.00 A.
Peak 385 from 2DNOESY.peaks (2.46, 4.79 ppm; 4.08 A):
1 out of 1 assignment used, quality = 0.94:
HB2 ASP 5 + HA ASP 5 OK 94 94 100 100 2.3-2.5 3.0=100
Violated in 0 structures by 0.00 A.
Peak 386 from 2DNOESY.peaks (2.55, 4.07 ppm; 3.66 A):
1 out of 4 assignments used, quality = 0.68:
HB3 ASN 9 + HA PRO 6 OK 68 91 100 75 2.4-2.8 84/364=43, 3.5/346=35
HB2 CYSS 16 - HA ALA 19 far 0 77 0 - 6.8-9.1
HB2 CYSS 16 - HA PRO 6 far 0 94 0 - 6.8-7.4
HB3 ASN 9 - HA ALA 19 far 0 75 0 - 8.6-12.9
Violated in 0 structures by 0.00 A.
Peak 387 from 2DNOESY.peaks (2.85, 4.07 ppm; 4.18 A):
0 out of 4 assignments used, quality = 0.00:
HB2 PHE 8 - HA PRO 6 far 0 74 0 - 5.3-5.5
HB3 CYSS 3 - HA ALA 19 far 0 46 0 - 5.8-9.6
HB3 CYSS 3 - HA PRO 6 far 0 53 0 - 7.7-8.1
HB2 PHE 8 - HA ALA 19 far 0 65 0 - 9.3-12.5
Violated in 20 structures by 1.03 A.
Peak 388 from 2DNOESY.peaks (2.11, 4.07 ppm; 3.43 A):
1 out of 1 assignment used, quality = 1.00:
HB3 PRO 6 + HA PRO 6 OK 100 100 100 100 2.3-2.3 2.3=100
Violated in 0 structures by 0.00 A.
Peak 389 from 2DNOESY.peaks (1.86, 4.07 ppm; 4.36 A):
1 out of 1 assignment used, quality = 1.00:
HG3 PRO 6 + HA PRO 6 OK 100 100 100 100 3.9-3.9 3.8=100
Violated in 0 structures by 0.00 A.
Peak 390 from 2DNOESY.peaks (1.80, 4.07 ppm; 4.21 A):
1 out of 2 assignments used, quality = 1.00:
HG2 PRO 6 + HA PRO 6 OK 100 100 100 100 4.0-4.0 3.8=100
HB3 GLU 14 - HA ALA 19 far 0 78 0 - 9.1-13.6
Violated in 0 structures by 0.00 A.
Peak 391 from 2DNOESY.peaks (1.74, 4.07 ppm; 4.02 A):
1 out of 2 assignments used, quality = 0.99:
HB2 PRO 6 + HA PRO 6 OK 99 99 100 100 2.7-2.7 2.3=100
HB2 HIS+ 2 - HA PRO 6 far 0 98 0 - 9.2-9.5
Violated in 0 structures by 0.00 A.
Peak 392 from 2DNOESY.peaks (2.11, 3.66 ppm; 5.02 A):
1 out of 2 assignments used, quality = 0.99:
HB3 PRO 6 + HD2 PRO 6 OK 99 99 100 100 3.9-3.9 3.0=100
HB3 PRO 6 - HB3 SER 4 far 0 97 0 - 9.9-10.0
Violated in 0 structures by 0.00 A.
Peak 393 from 2DNOESY.peaks (1.86, 3.66 ppm; 3.76 A):
1 out of 1 assignment used, quality = 0.99:
HG3 PRO 6 + HD2 PRO 6 OK 99 99 100 100 2.3-2.3 2.3=100
Violated in 0 structures by 0.00 A.
Peak 394 from 2DNOESY.peaks (1.80, 3.66 ppm; 3.93 A):
1 out of 1 assignment used, quality = 1.00:
HG2 PRO 6 + HD2 PRO 6 OK 100 100 100 100 2.7-2.7 2.3=100
Violated in 0 structures by 0.00 A.
Peak 395 from 2DNOESY.peaks (1.74, 3.66 ppm; 4.24 A):
1 out of 5 assignments used, quality = 0.98:
HB2 PRO 6 + HD2 PRO 6 OK 98 98 100 100 4.0-4.0 3.0=100
HB2 HIS+ 2 - HA3 GLY 22 far 0 96 0 - 4.8-7.9
HB2 HIS+ 2 - HB3 SER 4 far 0 94 0 - 6.8-7.6
HB2 HIS+ 2 - HA3 GLY 21 far 0 62 0 - 7.8-10.7
HB2 HIS+ 2 - HD2 PRO 6 far 0 96 0 - 9.1-9.8
Violated in 0 structures by 0.00 A.
Peak 396 from 2DNOESY.peaks (2.97, 3.92 ppm; 3.84 A):
1 out of 2 assignments used, quality = 0.85:
HD3 ARG 7 + HA ARG 7 OK 85 98 100 87 2.0-3.4 4.9=49, 123/3.0=25...(6)
HB3 ASP 5 - HA ARG 7 far 0 56 0 - 5.2-5.9
Violated in 0 structures by 0.00 A.
Peak 397 from 2DNOESY.peaks (1.76, 2.97 ppm; 4.31 A):
2 out of 2 assignments used, quality = 0.97:
HB3 ARG 7 + HD3 ARG 7 OK 94 94 100 100 3.4-3.8 3.7=100
HB3 ARG 7 + HB3 ASP 5 OK 51 69 100 74 3.2-3.9 242/241=60, 124/123=22
Violated in 0 structures by 0.00 A.
Peak 398 from 2DNOESY.peaks (1.64, 2.97 ppm; 4.20 A):
1 out of 2 assignments used, quality = 0.97:
HB2 ARG 7 + HD3 ARG 7 OK 97 97 100 100 2.1-3.1 3.7=100
HB2 ARG 7 - HB3 ASP 5 poor 19 65 40 73 3.8-4.8 243/241=52, 1.8/397=26
Violated in 0 structures by 0.00 A.
Peak 399 from 2DNOESY.peaks (1.44, 2.97 ppm; 3.72 A):
1 out of 2 assignments used, quality = 0.96:
HG3 ARG 7 + HD3 ARG 7 OK 96 96 100 100 2.6-3.0 3.0=100
HG3 ARG 7 - HB3 ASP 5 far 0 73 0 - 5.4-6.0
Violated in 0 structures by 0.00 A.
Peak 400 from 2DNOESY.peaks (1.38, 2.97 ppm; 3.69 A):
1 out of 2 assignments used, quality = 0.85:
HG2 ARG 7 + HD3 ARG 7 OK 85 85 100 100 2.4-3.0 3.0=100
HG2 ARG 7 - HB3 ASP 5 far 0 65 0 - 5.6-6.5
Violated in 0 structures by 0.00 A.
Peak 401 from 2DNOESY.peaks (3.19, 4.01 ppm; 4.65 A):
1 out of 3 assignments used, quality = 0.96:
HB3 PHE 8 + HA PHE 8 OK 96 96 100 100 2.6-2.6 3.0=100
HB3 PHE 8 - HA SER 4 far 0 54 0 - 7.0-7.2
HB3 PHE 8 - HA ALA 20 far 0 47 0 - 8.3-11.4
Violated in 0 structures by 0.00 A.
Peak 402 from 2DNOESY.peaks (2.84, 4.02 ppm; 4.26 A):
1 out of 4 assignments used, quality = 0.96:
HB2 PHE 8 + HA PHE 8 OK 96 96 100 100 3.0-3.0 3.0=100
HB2 PHE 8 - HA SER 4 far 0 48 0 - 6.2-6.4
HB2 PHE 8 - HA ALA 20 far 0 42 0 - 6.8-9.9
HB2 PHE 8 - HA3 GLY 17 far 0 88 0 - 9.6-10.6
Violated in 0 structures by 0.00 A.
Peak 403 from 2DNOESY.peaks (2.55, 4.16 ppm; 3.87 A):
1 out of 4 assignments used, quality = 0.95:
HB3 ASN 9 + HA ASN 9 OK 95 95 100 100 3.0-3.0 3.0=100
HB2 CYSS 16 - HA ASN 9 lone 3 87 100 4 2.3-3.0
HB3 ASN 9 - HA HIS+ 2 far 0 96 0 - 9.1-9.7
HB2 CYSS 16 - HA HIS+ 2 far 0 88 0 - 9.1-9.8
Violated in 0 structures by 0.00 A.
Peak 404 from 2DNOESY.peaks (1.70, 2.60 ppm; 3.95 A):
1 out of 3 assignments used, quality = 0.93:
HB ILE 15 + HB3 HIS+ 12 OK 93 94 100 99 2.9-3.1 3.2/411=59, 3.0/406=46...(11)
HG3 PRO 13 - HB3 HIS+ 12 far 0 48 0 - 6.6-6.7
HB2 GLU 14 - HB3 HIS+ 12 far 0 53 0 - 7.5-7.9
Violated in 0 structures by 0.00 A.
Peak 405 from 2DNOESY.peaks (1.70, 2.26 ppm; 4.32 A):
2 out of 7 assignments used, quality = 0.98:
HB ILE 15 + HB2 HIS+ 12 OK 96 96 100 100 2.0-2.0 404/1.8=86, 2.1/414=52...(12)
HB2 GLU 14 + HG3 GLU 14 OK 43 43 100 100 2.3-3.0 3.0=100
HG3 PRO 13 - HG3 GLU 14 poor 16 40 40 - 3.4-6.2
HB ILE 15 - HG3 GLU 14 far 0 95 0 - 4.7-7.0
HG3 PRO 13 - HB2 HIS+ 12 far 0 40 0 - 6.1-6.1
HB2 GLU 14 - HB2 HIS+ 12 far 0 44 0 - 6.1-6.4
HB ILE 15 - HB2 ASP 11 far 0 39 0 - 8.7-9.0
Violated in 0 structures by 0.00 A.
Peak 406 from 2DNOESY.peaks (1.39, 2.60 ppm; 4.74 A):
1 out of 2 assignments used, quality = 0.94:
HG13 ILE 15 + HB3 HIS+ 12 OK 94 94 100 100 4.0-4.2 2.1/411=93, 3.0/404=79...(10)
HG2 ARG 7 - HB3 HIS+ 12 far 0 98 0 - 6.5-7.4
Violated in 0 structures by 0.00 A.
Peak 407 from 2DNOESY.peaks (7.16, 1.40 ppm; 4.22 A):
1 out of 1 assignment used, quality = 0.99:
H ILE 15 + HG13 ILE 15 OK 99 100 100 99 1.9-2.1 4.5=85, 284/1.8=75...(7)
Violated in 0 structures by 0.00 A.
Peak 408 from 2DNOESY.peaks (7.16, 1.40 ppm; 4.22 A):
1 out of 1 assignment used, quality = 0.99:
H ILE 15 + HG13 ILE 15 OK 99 100 100 99 1.9-2.1 4.5=85, 284/1.8=75...(7)
Violated in 0 structures by 0.00 A.
Peak 409 from 2DNOESY.peaks (0.93, 2.60 ppm; 5.50 A increased from 4.77 A):
1 out of 1 assignment used, quality = 0.99:
HG12 ILE 15 + HB3 HIS+ 12 OK 99 99 100 100 5.2-5.5 2.1/411=100, 1.8/406=95...(10)
Violated in 0 structures by 0.00 A.
Peak 410 from 2DNOESY.peaks (0.74, 2.60 ppm; 5.50 A):
1 out of 1 assignment used, quality = 1.00:
QG2 ILE 15 + HB3 HIS+ 12 OK 100 100 100 100 4.1-4.3 2.1/404=99, 450/411=94...(11)
Violated in 0 structures by 0.00 A.
Peak 411 from 2DNOESY.peaks (0.59, 2.60 ppm; 3.76 A):
1 out of 1 assignment used, quality = 0.95:
QD1 ILE 15 + HB3 HIS+ 12 OK 95 96 100 99 3.0-3.2 3.2/404=51, 2.1/406=46...(12)
Violated in 0 structures by 0.00 A.
Peak 412 from 2DNOESY.peaks (1.40, 2.25 ppm; 4.85 A):
2 out of 5 assignments used, quality = 0.98:
HG13 ILE 15 + HB2 HIS+ 12 OK 92 92 100 100 2.2-2.4 406/1.8=79, ~411=72...(11)
HG13 ILE 15 + HG3 GLU 14 OK 70 94 75 99 2.9-5.6 416/1.8=84, ~417=55...(8)
HG2 ARG 7 - HB2 ASP 11 lone 7 60 95 12 4.0-5.0 245/3.9=5
HG2 ARG 7 - HB2 HIS+ 12 far 0 76 0 - 8.1-9.0
HG13 ILE 15 - HB2 ASP 11 far 0 73 0 - 8.7-9.0
Violated in 0 structures by 0.00 A.
Peak 413 from 2DNOESY.peaks (0.93, 2.26 ppm; 5.29 A):
2 out of 2 assignments used, quality = 0.99:
HG12 ILE 15 + HB2 HIS+ 12 OK 97 97 100 100 3.7-3.8 ~411=81, 409/1.8=77...(11)
HG12 ILE 15 + HG3 GLU 14 OK 72 96 75 100 3.4-5.9 ~416=73, 417/1.8=72...(8)
Violated in 0 structures by 0.00 A.
Peak 414 from 2DNOESY.peaks (0.74, 2.25 ppm; 5.19 A):
1 out of 3 assignments used, quality = 0.98:
QG2 ILE 15 + HB2 HIS+ 12 OK 98 98 100 100 3.5-3.5 ~404=76, 410/1.8=74...(14)
QG2 ILE 15 - HG3 GLU 14 far 10 98 10 - 4.9-6.6
QG2 ILE 15 - HB2 ASP 11 far 0 59 0 - 8.8-9.1
Violated in 0 structures by 0.00 A.
Peak 415 from 2DNOESY.peaks (0.59, 2.24 ppm; 4.55 A):
2 out of 3 assignments used, quality = 0.87:
QD1 ILE 15 + HB2 HIS+ 12 OK 75 75 100 100 2.2-2.4 411/1.8=94, 358/3.9=53...(15)
QD1 ILE 15 + HG3 GLU 14 OK 49 78 65 96 4.2-6.7 ~416=53, 419/1.8=47...(8)
QD1 ILE 15 - HB2 ASP 11 far 0 78 0 - 7.1-7.1
Violated in 0 structures by 0.00 A.
Peak 416 from 2DNOESY.peaks (1.40, 2.01 ppm; 4.63 A):
1 out of 2 assignments used, quality = 0.97:
HG13 ILE 15 + HG2 GLU 14 OK 97 98 100 98 2.2-4.3 1.8/417=64, 2.1/419=57...(7)
HG13 ILE 15 - HB3 PRO 13 far 0 79 0 - 7.6-7.9
Violated in 0 structures by 0.00 A.
Peak 417 from 2DNOESY.peaks (0.92, 2.01 ppm; 5.22 A):
1 out of 2 assignments used, quality = 0.85:
HG12 ILE 15 + HG2 GLU 14 OK 85 85 100 100 3.0-4.3 1.8/416=92, 2.1/419=73...(7)
HG12 ILE 15 - HB3 PRO 13 far 0 65 0 - 9.2-9.5
Violated in 0 structures by 0.00 A.
Peak 418 from 2DNOESY.peaks (0.73, 2.01 ppm; 5.36 A increased from 5.04 A):
1 out of 2 assignments used, quality = 0.98:
QG2 ILE 15 + HG2 GLU 14 OK 98 98 100 100 4.5-5.2 3.2/416=79, 3.2/417=69...(7)
QG2 ILE 15 - HB3 PRO 13 far 0 79 0 - 8.4-8.5
Violated in 0 structures by 0.00 A.
Peak 419 from 2DNOESY.peaks (0.60, 2.01 ppm; 5.43 A):
1 out of 2 assignments used, quality = 0.96:
QD1 ILE 15 + HG2 GLU 14 OK 96 96 100 100 3.7-5.4 2.1/416=92, 2.1/417=82...(7)
QD1 ILE 15 - HB3 PRO 13 far 0 73 0 - 7.8-7.9
Violated in 0 structures by 0.00 A.
Peak 420 from 2DNOESY.peaks (1.68, 5.00 ppm; 4.38 A):
1 out of 2 assignments used, quality = 0.97:
HG3 PRO 13 + HA HIS+ 12 OK 97 100 100 97 4.2-4.3 4.6=86, 279/280=43...(4)
HB2 GLU 14 - HA HIS+ 12 far 0 99 0 - 5.5-6.3
Violated in 0 structures by 0.00 A.
Peak 421 from 2DNOESY.peaks (2.88, 3.91 ppm; 4.05 A):
1 out of 1 assignment used, quality = 0.85:
HB3 TYR 10 + HA ARG 7 OK 85 93 100 91 3.1-3.8 1.8/422=81, 2.5/373=45
Violated in 0 structures by 0.00 A.
Peak 422 from 2DNOESY.peaks (2.77, 3.91 ppm; 3.86 A):
1 out of 1 assignment used, quality = 0.81:
HB2 TYR 10 + HA ARG 7 OK 81 96 100 84 2.7-3.4 1.8/421=70, 2.5/373=40
Violated in 0 structures by 0.00 A.
Peak 423 from 2DNOESY.peaks (2.46, 3.19 ppm; 5.40 A):
1 out of 1 assignment used, quality = 0.99:
HB2 ASP 5 + HB3 PHE 8 OK 99 99 100 100 4.7-5.4 1.8/452=100, 229/81=80...(4)
Violated in 0 structures by 0.00 A.
Peak 424 from 2DNOESY.peaks (2.46, 2.98 ppm; 3.60 A):
1 out of 2 assignments used, quality = 0.96:
HB2 ASP 5 + HB3 ASP 5 OK 96 96 100 100 1.8-1.8 1.8=100
HB2 ASP 5 - HD3 ARG 7 far 0 70 0 - 5.3-7.2
Violated in 0 structures by 0.00 A.
Peak 425 from 2DNOESY.peaks (2.54, 3.08 ppm; 5.48 A increased from 4.39 A):
0 out of 4 assignments used, quality = 0.00:
HB2 CYSS 16 - HB2 CYSS 3 lone 10 99 100 11 5.3-5.5
HB2 CYSS 16 - HD2 PRO 13 far 0 52 0 - 6.6-6.9
HB3 ASN 9 - HB2 CYSS 3 far 0 66 0 - 7.5-8.2
HB3 ASN 9 - HD2 PRO 13 far 0 35 0 - 8.0-8.5
Violated in 0 structures by 0.00 A.
Peak 426 from 2DNOESY.peaks (2.55, 3.25 ppm; 2.80 A):
1 out of 4 assignments used, quality = 1.00:
HB2 CYSS 16 + HB3 CYSS 16 OK 100 100 100 100 1.8-1.8 1.8=100
HB3 ASN 9 - HB3 CYSS 16 far 0 74 0 - 4.8-5.7
HB2 CYSS 16 - HD3 PRO 13 far 0 49 0 - 6.4-6.8
HB3 ASN 9 - HD3 PRO 13 far 0 36 0 - 6.7-7.3
Violated in 0 structures by 0.00 A.
Peak 427 from 2DNOESY.peaks (8.57, 4.16 ppm; 3.58 A):
2 out of 4 assignments used, quality = 1.00:
H HIS+ 2 + HA HIS+ 2 OK 99 99 100 100 2.9-2.9 3.0=100
H ASN 9 + HA ASN 9 OK 70 70 100 100 2.9-2.9 3.0=100
H ASN 9 - HA HIS+ 2 far 0 73 0 - 7.7-8.5
H HIS+ 2 - HA ASN 9 far 0 94 0 - 8.4-9.3
Violated in 0 structures by 0.00 A.
Peak 428 from 2DNOESY.peaks (8.36, 4.09 ppm; 4.23 A):
0 out of 0 assignments used, quality = 0.00:
Peak 429 from 2DNOESY.peaks (8.52, 3.91 ppm; 4.89 A):
0 out of 0 assignments used, quality = 0.00:
Peak 430 from 2DNOESY.peaks (8.43, 3.89 ppm; 3.83 A):
0 out of 0 assignments used, quality = 0.00:
Peak 431 from 2DNOESY.peaks (8.36, 8.56 ppm; 4.46 A):
0 out of 0 assignments used, quality = 0.00:
Peak 432 from 2DNOESY.peaks (6.69, 4.26 ppm; 4.60 A increased from 4.09 A):
1 out of 1 assignment used, quality = 0.98:
QE PHE 8 + HA CYSS 3 OK 98 99 100 99 4.2-4.4 2.2/290=96, ~327=40, ~360=38
Violated in 0 structures by 0.00 A.
Peak 433 from 2DNOESY.peaks (6.69, 4.15 ppm; 5.50 A increased from 4.66 A):
1 out of 2 assignments used, quality = 0.93:
QE PHE 8 + HA HIS+ 2 OK 93 93 100 100 5.1-5.5 2.2/289=92, 304/3.0=88...(8)
QE PHE 8 - HA ASN 9 far 0 98 0 - 6.1-6.5
Violated in 11 structures by 0.00 A.
Peak 434 from 2DNOESY.peaks (6.69, 4.01 ppm; 4.59 A):
1 out of 5 assignments used, quality = 0.86:
QE PHE 8 + HA PHE 8 OK 86 97 100 89 4.2-4.4 311/340=56, 5.6=54, ~224=44
QE PHE 8 - HA ALA 20 far 3 66 5 - 4.6-9.1
QE PHE 8 - HA SER 4 far 0 72 0 - 8.2-8.3
QE PHE 8 - HA ASP 11 far 0 46 0 - 8.5-8.9
QE PHE 8 - HA3 GLY 17 far 0 69 0 - 8.9-9.5
Violated in 0 structures by 0.00 A.
Peak 435 from 2DNOESY.peaks (6.69, 3.19 ppm; 4.66 A increased from 4.15 A):
1 out of 1 assignment used, quality = 0.99:
QE PHE 8 + HB3 PHE 8 OK 99 99 100 100 4.4-4.5 4.4=100
Violated in 0 structures by 0.00 A.
Peak 436 from 2DNOESY.peaks (6.69, 2.84 ppm; 4.43 A increased from 3.94 A):
1 out of 2 assignments used, quality = 0.97:
QE PHE 8 + HB2 PHE 8 OK 97 97 100 100 4.4-4.4 4.4=100
QE PHE 8 - HB3 CYSS 3 far 0 36 0 - 5.1-5.4
Violated in 0 structures by 0.00 A.
Peak 437 from 2DNOESY.peaks (6.69, 2.60 ppm; 4.44 A):
1 out of 1 assignment used, quality = 0.95:
QE PHE 8 + HB3 HIS+ 12 OK 95 96 100 99 4.2-4.5 308/411=66, 301/1.8=65...(6)
Violated in 1 structures by 0.00 A.
Peak 438 from 2DNOESY.peaks (6.72, 4.26 ppm; 4.80 A):
1 out of 2 assignments used, quality = 0.93:
HD22 ASN 9 + HA CYSS 3 OK 93 99 100 94 2.9-3.4 1.7/342=86, ~350=53
HD2 HIS+ 2 - HA CYSS 3 far 0 99 0 - 7.0-7.4
Violated in 0 structures by 0.00 A.
Peak 439 from 2DNOESY.peaks (6.72, 4.15 ppm; 3.95 A):
2 out of 4 assignments used, quality = 0.83:
HD22 ASN 9 + HA ASN 9 OK 71 99 100 72 2.1-3.3 4.4=71
HD2 HIS+ 2 + HA HIS+ 2 OK 42 95 70 62 2.3-4.8 4.7=61
HD22 ASN 9 - HA HIS+ 2 far 0 95 0 - 6.7-7.8
HD2 HIS+ 2 - HA ASN 9 far 0 99 0 - 9.6-11.3
Violated in 0 structures by 0.00 A.
Peak 440 from 2DNOESY.peaks (6.72, 4.06 ppm; 5.12 A):
1 out of 3 assignments used, quality = 0.93:
HD22 ASN 9 + HA PRO 6 OK 93 93 100 99 3.0-5.0 1.7/346=88, 3.5/386=83
HD22 ASN 9 - HA ALA 19 far 0 66 0 - 8.2-12.0
HD2 HIS+ 2 - HA PRO 6 far 0 93 0 - 9.7-12.0
Violated in 0 structures by 0.00 A.
Peak 441 from 2DNOESY.peaks (2.60, 4.99 ppm; 5.50 A):
1 out of 1 assignment used, quality = 0.95:
HB3 HIS+ 12 + HA HIS+ 12 OK 95 95 100 100 3.0-3.0 3.0=100
Violated in 0 structures by 0.00 A.
Peak 442 from 2DNOESY.peaks (2.26, 4.99 ppm; 3.95 A):
1 out of 2 assignments used, quality = 0.95:
HB2 HIS+ 12 + HA HIS+ 12 OK 95 95 100 100 2.5-2.5 3.0=100
HG3 GLU 14 - HA HIS+ 12 poor 14 93 40 37 3.3-7.3 5.0/280=33, ~266=3
Violated in 0 structures by 0.00 A.
Peak 443 from 2DNOESY.peaks (2.54, 4.72 ppm; 3.98 A):
1 out of 2 assignments used, quality = 0.92:
HB2 CYSS 16 + HA CYSS 16 OK 92 92 100 100 3.0-3.0 3.0=100
HB3 ASN 9 - HA CYSS 16 far 0 55 0 - 7.3-8.1
Violated in 0 structures by 0.00 A.
Peak 444 from 2DNOESY.peaks (3.25, 4.72 ppm; 5.50 A):
1 out of 2 assignments used, quality = 0.94:
HB3 CYSS 16 + HA CYSS 16 OK 94 94 100 100 2.6-2.7 3.0=100
HD3 PRO 13 - HA CYSS 16 far 0 47 0 - 8.9-9.2
Violated in 0 structures by 0.00 A.
Peak 445 from 2DNOESY.peaks (0.74, 1.71 ppm; 3.96 A):
1 out of 3 assignments used, quality = 1.00:
QG2 ILE 15 + HB ILE 15 OK 100 100 100 100 2.1-2.1 2.1=100
QG2 ILE 15 - HB2 GLU 14 far 0 49 0 - 5.8-6.8
QG2 ILE 15 - HG3 PRO 13 far 0 46 0 - 7.9-8.0
Violated in 0 structures by 0.00 A.
Peak 446 from 2DNOESY.peaks (0.73, 1.40 ppm; 4.09 A):
1 out of 2 assignments used, quality = 0.98:
QG2 ILE 15 + QG1 ILE 15 OK 98 98 100 100 2.3-2.4 2.3=100
QG2 ILE 15 - HG2 ARG 7 far 0 76 0 - 8.7-9.6
Violated in 0 structures by 0.00 A.
Peak 447 from 2DNOESY.peaks (0.59, 1.71 ppm; 3.54 A):
1 out of 3 assignments used, quality = 1.00:
QD1 ILE 15 + HB ILE 15 OK 100 100 100 100 2.3-2.4 3.2=100
QD1 ILE 15 - HB2 GLU 14 far 0 49 0 - 5.6-6.4
QD1 ILE 15 - HG3 PRO 13 far 0 46 0 - 6.8-6.9
Violated in 0 structures by 0.00 A.
Peak 448 from 2DNOESY.peaks (0.73, 0.93 ppm; 3.70 A):
1 out of 1 assignment used, quality = 0.99:
QG2 ILE 15 + HG12 ILE 15 OK 99 99 100 100 2.4-2.4 3.2=100
Violated in 0 structures by 0.00 A.
Peak 449 from 2DNOESY.peaks (0.60, 0.93 ppm; 3.44 A):
1 out of 1 assignment used, quality = 0.95:
QD1 ILE 15 + HG12 ILE 15 OK 95 95 100 100 2.1-2.1 2.1=100
Violated in 0 structures by 0.00 A.
Peak 450 from 2DNOESY.peaks (0.59, 0.74 ppm; 3.02 A):
1 out of 1 assignment used, quality = 0.96:
QD1 ILE 15 + QG2 ILE 15 OK 96 98 100 98 2.0-2.1 3.1=90, 308/306=35...(8)
Violated in 0 structures by 0.00 A.
Peak 451 from 2DNOESY.peaks (2.56, 2.85 ppm; 2.72 A):
0 out of 4 assignments used, quality = 0.00:
HB2 CYSS 16 - HB2 PHE 8 far 0 59 0 - 4.9-5.8
HB3 ASN 9 - HB2 PHE 8 far 0 76 0 - 5.0-5.4
HB2 CYSS 16 - HB3 CYSS 3 far 0 57 0 - 6.1-6.3
HB3 ASN 9 - HB3 CYSS 3 far 0 73 0 - 7.4-8.2
Violated in 20 structures by 1.68 A.
Peak 452 from 2DNOESY.peaks (2.98, 3.19 ppm; 3.74 A):
1 out of 2 assignments used, quality = 0.90:
HB3 ASP 5 + HB3 PHE 8 OK 90 100 100 90 3.4-3.7 231/81=51, 228/225=41...(5)
HD3 ARG 7 - HB3 PHE 8 far 0 65 0 - 6.7-7.4
Violated in 0 structures by 0.00 A.
Average quality of peak assignments : 0.866
Average number of used assignments : 0.997
Peaks with increased upper limit : 34
Peaks with decreased upper limit : 0
Protons used in less than 30% of expected peaks:
Peak observation distance: 3.47 A
Atom Residue Shift Peaks Used Expect
HB2 PRO 6 1.738 5 2 7
HB3 PRO 6 2.114 2 2 7
HA ILE 15 3.983 10 2 7
QG1 ILE 15 1.399 1 1 11
Peaks:
selected : 317
assigned : 292
unassigned : 25
without assignment possibility : 12
with violation below 0.5 A : 5
with violation between 0.5 and 3.0 A : 8
with violation above 3.0 A : 0
with diagonal assignment : 1
Cross peaks:
with off-diagonal assignment : 291
with unique assignment : 267
with short-range assignment |i-j|<=1: 223
with medium-range assignment 1<|i-j|<5 : 46
with long-range assignment |i-j|>=5: 22
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