FMO DATABASE

FMODB ID: RYKM8

Calculation Name: 2F6E-A-Xray540

Preferred Name: Toxin A

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2F6E

Chain ID: A

ChEMBL ID: CHEMBL3580504

UniProt ID: P16154

Base Structure: X-ray

Registration Date: 2025-07-08

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	227
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1010205.088987
FMO2-HF: Nuclear repulsion	961827.089156
FMO2-HF: Total energy	-48377.999832
FMO2-MP2: Total energy	-48520.107264

3D Structure Molmil

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:2:TYR)

Summations of interaction energy for fragment #1(A:2:TYR)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
1.074	3.044	-0.02	-1.007	-0.942	0

Interaction energy analysis for fragmet #1(A:2:TYR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.188 / q_NPA : 0.010

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].
4	A	3	TYR	0	-0.059	0.103	3.966	-0.041	0.345	0.004	-0.158	-0.231
5	A	4	PHE	0	0.141	-0.108	3.814	-0.283	1.200	-0.019	-0.841	-0.624
6	A	4	PHE	0	-0.062	0.122	6.432	-0.011	-0.011	0.000	0.000	0.000
7	A	5	GLU	0	0.024	-0.130	7.048	-0.033	-0.033	0.000	0.000	0.000
8	A	5	GLU	-1	-0.962	-0.824	9.077	0.180	0.180	0.000	0.000	0.000
9	A	6	PRO	0	0.006	-0.111	10.498	0.031	0.031	0.000	0.000	0.000
10	A	7	ASN	0	0.076	0.026	13.186	0.112	0.112	0.000	0.000	0.000
11	A	7	ASN	0	-0.093	0.103	14.538	-0.047	-0.047	0.000	0.000	0.000
12	A	8	THR	0	0.052	-0.076	16.117	0.004	0.004	0.000	0.000	0.000
13	A	8	THR	0	-0.041	0.055	17.296	-0.022	-0.022	0.000	0.000	0.000
14	A	9	ALA	0	0.141	-0.083	18.546	0.005	0.005	0.000	0.000	0.000
15	A	9	ALA	0	-0.060	0.119	20.886	0.007	0.007	0.000	0.000	0.000
16	A	10	ILE	0	0.009	-0.126	21.428	-0.029	-0.029	0.000	0.000	0.000
17	A	10	ILE	0	-0.025	0.120	24.818	0.001	0.001	0.000	0.000	0.000
18	A	11	GLY	0	0.014	-0.086	24.110	0.022	0.022	0.000	0.000	0.000
19	A	12	ALA	0	0.083	-0.020	22.668	-0.034	-0.034	0.000	0.000	0.000
20	A	12	ALA	0	-0.064	0.131	24.340	0.003	0.003	0.000	0.000	0.000
21	A	13	ASN	0	0.073	-0.107	20.513	0.024	0.024	0.000	0.000	0.000
22	A	13	ASN	0	-0.098	0.065	18.810	0.019	0.019	0.000	0.000	0.000
23	A	14	GLY	0	-0.007	-0.100	16.364	-0.024	-0.024	0.000	0.000	0.000
24	A	15	TYR	0	0.163	0.020	13.702	0.052	0.052	0.000	0.000	0.000
25	A	15	TYR	0	-0.124	0.078	12.714	-0.030	-0.030	0.000	0.000	0.000
26	A	16	LYS	0	-0.010	-0.138	15.150	-0.024	-0.024	0.000	0.000	0.000
27	A	16	LYS	1	0.821	1.066	18.791	0.339	0.339	0.000	0.000	0.000
28	A	17	ILE	0	0.123	-0.091	18.044	-0.004	-0.004	0.000	0.000	0.000
29	A	17	ILE	0	-0.080	0.108	15.685	-0.003	-0.003	0.000	0.000	0.000
30	A	18	ILE	0	0.049	-0.120	19.135	0.025	0.025	0.000	0.000	0.000
31	A	18	ILE	0	-0.077	0.098	21.914	0.007	0.007	0.000	0.000	0.000
32	A	19	ASP	0	0.065	-0.079	22.770	-0.013	-0.013	0.000	0.000	0.000
33	A	19	ASP	-1	-0.910	-0.820	25.517	-0.263	-0.263	0.000	0.000	0.000
34	A	20	ASN	0	0.022	-0.084	21.201	0.007	0.007	0.000	0.000	0.000
35	A	20	ASN	0	-0.097	0.062	22.155	-0.019	-0.019	0.000	0.000	0.000
36	A	21	LYS	0	0.132	-0.102	20.035	-0.035	-0.035	0.000	0.000	0.000
37	A	21	LYS	1	0.775	1.020	21.264	0.307	0.307	0.000	0.000	0.000
38	A	22	ASN	0	0.069	-0.069	16.220	0.026	0.026	0.000	0.000	0.000
39	A	22	ASN	0	-0.102	0.046	14.600	0.031	0.031	0.000	0.000	0.000
40	A	23	PHE	0	0.101	-0.074	17.664	0.008	0.008	0.000	0.000	0.000
41	A	23	PHE	0	-0.066	0.088	20.115	0.009	0.009	0.000	0.000	0.000
42	A	24	TYR	0	0.141	-0.082	16.472	-0.048	-0.048	0.000	0.000	0.000
43	A	24	TYR	0	-0.096	0.105	13.174	0.033	0.033	0.000	0.000	0.000
44	A	25	PHE	0	0.064	-0.119	17.488	0.036	0.036	0.000	0.000	0.000
45	A	25	PHE	0	-0.120	0.103	20.026	0.002	0.002	0.000	0.000	0.000
46	A	26	ARG	0	0.149	-0.087	19.072	-0.004	-0.004	0.000	0.000	0.000
47	A	26	ARG	1	0.879	1.089	15.925	0.033	0.033	0.000	0.000	0.000
48	A	27	ASN	0	0.016	-0.101	21.110	-0.002	-0.002	0.000	0.000	0.000
49	A	27	ASN	0	-0.074	0.079	24.588	0.010	0.010	0.000	0.000	0.000
50	A	28	GLY	0	0.051	-0.070	23.735	0.004	0.004	0.000	0.000	0.000
51	A	29	LEU	0	0.023	-0.044	24.281	-0.013	-0.013	0.000	0.000	0.000
52	A	29	LEU	0	-0.051	0.123	25.400	0.002	0.002	0.000	0.000	0.000
53	A	30	PRO	0	0.030	-0.077	21.879	-0.003	-0.003	0.000	0.000	0.000
54	A	31	GLN	0	0.061	-0.018	20.058	0.024	0.024	0.000	0.000	0.000
55	A	31	GLN	0	-0.134	0.079	19.118	0.019	0.019	0.000	0.000	0.000
56	A	32	ILE	0	0.102	-0.085	19.736	-0.046	-0.046	0.000	0.000	0.000
57	A	32	ILE	0	-0.107	0.112	20.599	0.004	0.004	0.000	0.000	0.000
58	A	33	GLY	0	-0.061	-0.149	17.236	0.048	0.048	0.000	0.000	0.000
59	A	34	VAL	0	0.079	-0.005	13.505	-0.068	-0.068	0.000	0.000	0.000
60	A	34	VAL	0	-0.066	0.120	11.373	-0.006	-0.006	0.000	0.000	0.000
61	A	35	PHE	0	0.060	-0.116	11.554	0.111	0.111	0.000	0.000	0.000
62	A	35	PHE	0	-0.077	0.102	12.654	0.025	0.025	0.000	0.000	0.000
63	A	36	LYS	0	0.099	-0.120	8.072	-0.144	-0.144	0.000	0.000	0.000
64	A	36	LYS	1	0.806	1.086	4.696	-0.872	-0.830	-0.001	-0.004	-0.036
65	A	37	GLY	0	0.040	-0.063	8.172	0.249	0.249	0.000	0.000	0.000
66	A	38	PRO	0	-0.010	-0.014	7.109	-0.658	-0.658	0.000	0.000	0.000
67	A	39	ASN	0	0.024	0.029	6.315	-0.770	-0.770	0.000	0.000	0.000
68	A	39	ASN	0	-0.115	0.062	8.092	-0.148	-0.148	0.000	0.000	0.000
69	A	40	GLY	0	0.108	-0.091	4.935	-0.115	-0.085	-0.002	-0.005	-0.024
70	A	41	PHE	0	0.036	-0.012	5.925	0.314	0.343	-0.002	0.001	-0.027
71	A	41	PHE	0	-0.020	0.112	5.358	-0.195	-0.195	0.000	0.000	0.000
72	A	42	GLU	0	0.058	-0.100	8.366	-0.032	-0.032	0.000	0.000	0.000
73	A	42	GLU	-1	-0.847	-0.778	10.431	-1.050	-1.050	0.000	0.000	0.000
74	A	43	TYR	0	0.127	-0.086	11.785	0.086	0.086	0.000	0.000	0.000
75	A	43	TYR	0	-0.079	0.090	15.211	0.018	0.018	0.000	0.000	0.000
76	A	44	PHE	0	0.077	-0.085	15.195	-0.018	-0.018	0.000	0.000	0.000
77	A	44	PHE	0	-0.156	0.090	12.839	-0.014	-0.014	0.000	0.000	0.000
78	A	45	ALA	0	0.117	-0.105	17.563	0.052	0.052	0.000	0.000	0.000
79	A	45	ALA	0	-0.041	0.106	19.573	-0.003	-0.003	0.000	0.000	0.000
80	A	46	PRO	0	0.051	-0.092	20.589	0.002	0.002	0.000	0.000	0.000
81	A	47	ALA	0	0.150	0.032	24.306	-0.025	-0.025	0.000	0.000	0.000
82	A	47	ALA	0	-0.075	0.110	27.681	0.003	0.003	0.000	0.000	0.000
83	A	48	ASN	0	-0.096	-0.110	26.629	0.008	0.008	0.000	0.000	0.000
84	A	48	ASN	0	-0.073	0.060	29.170	-0.007	-0.007	0.000	0.000	0.000
85	A	49	THR	0	0.110	-0.057	23.628	0.017	0.017	0.000	0.000	0.000
86	A	49	THR	0	-0.106	0.021	22.153	0.002	0.002	0.000	0.000	0.000
87	A	50	ASP	0	0.076	-0.129	23.116	0.011	0.011	0.000	0.000	0.000
88	A	50	ASP	-1	-0.969	-0.846	22.483	-0.321	-0.321	0.000	0.000	0.000
89	A	51	ALA	0	0.006	-0.104	24.496	-0.003	-0.003	0.000	0.000	0.000
90	A	51	ALA	0	-0.064	0.102	25.479	-0.003	-0.003	0.000	0.000	0.000
91	A	52	ASN	0	0.003	-0.067	27.056	-0.010	-0.010	0.000	0.000	0.000
92	A	52	ASN	0	-0.127	0.044	29.642	0.008	0.008	0.000	0.000	0.000
93	A	53	ASN	0	0.168	-0.059	23.906	0.007	0.007	0.000	0.000	0.000
94	A	53	ASN	0	-0.087	0.054	23.232	-0.001	-0.001	0.000	0.000	0.000
95	A	54	ILE	0	0.113	-0.058	25.100	0.020	0.020	0.000	0.000	0.000
96	A	54	ILE	0	-0.085	0.082	24.686	0.001	0.001	0.000	0.000	0.000
97	A	55	GLU	0	0.083	-0.126	24.025	-0.028	-0.028	0.000	0.000	0.000
98	A	55	GLU	-1	-0.896	-0.801	25.652	-0.145	-0.145	0.000	0.000	0.000
99	A	56	GLY	0	-0.020	-0.105	20.921	0.004	0.004	0.000	0.000	0.000
100	A	57	GLN	0	0.167	0.008	19.763	-0.036	-0.036	0.000	0.000	0.000
101	A	57	GLN	0	-0.115	0.100	20.879	0.030	0.030	0.000	0.000	0.000
102	A	58	ALA	0	0.038	-0.128	16.196	0.046	0.046	0.000	0.000	0.000
103	A	58	ALA	0	-0.071	0.118	15.388	-0.021	-0.021	0.000	0.000	0.000
104	A	59	ILE	0	-0.073	-0.135	17.328	-0.004	-0.004	0.000	0.000	0.000
105	A	59	ILE	0	-0.090	0.105	18.112	0.008	0.008	0.000	0.000	0.000
106	A	60	ARG	0	0.176	-0.102	16.751	-0.078	-0.078	0.000	0.000	0.000
107	A	60	ARG	1	0.754	1.050	18.549	0.370	0.370	0.000	0.000	0.000
108	A	61	TYR	0	0.090	-0.111	17.121	0.060	0.060	0.000	0.000	0.000
109	A	61	TYR	0	-0.144	0.060	16.568	0.008	0.008	0.000	0.000	0.000
110	A	62	GLN	0	0.038	-0.111	16.269	-0.055	-0.055	0.000	0.000	0.000
111	A	62	GLN	0	-0.110	0.074	17.130	0.044	0.044	0.000	0.000	0.000
112	A	63	ASN	0	0.084	-0.047	16.550	0.043	0.043	0.000	0.000	0.000
113	A	63	ASN	0	-0.085	0.068	17.142	-0.026	-0.026	0.000	0.000	0.000
114	A	64	ARG	0	0.103	-0.124	17.468	0.050	0.050	0.000	0.000	0.000
115	A	64	ARG	1	0.915	1.106	19.041	0.222	0.222	0.000	0.000	0.000
116	A	65	PHE	0	0.110	-0.085	17.373	-0.045	-0.045	0.000	0.000	0.000
117	A	65	PHE	0	-0.042	0.118	18.348	-0.005	-0.005	0.000	0.000	0.000
118	A	66	LEU	0	0.056	-0.111	18.135	-0.013	-0.013	0.000	0.000	0.000
119	A	66	LEU	0	-0.090	0.117	16.558	-0.008	-0.008	0.000	0.000	0.000
120	A	67	HIS	0	0.109	-0.096	18.778	0.019	0.019	0.000	0.000	0.000
121	A	67	HIS	0	-0.076	0.115	22.512	0.009	0.009	0.000	0.000	0.000
122	A	68	LEU	0	0.096	-0.114	19.810	-0.014	-0.014	0.000	0.000	0.000
123	A	68	LEU	0	-0.089	0.117	18.062	-0.005	-0.005	0.000	0.000	0.000
124	A	69	LEU	0	-0.034	-0.124	19.899	0.017	0.017	0.000	0.000	0.000
125	A	69	LEU	0	-0.054	0.113	20.080	0.000	0.000	0.000	0.000	0.000
126	A	70	GLY	0	0.045	-0.099	21.866	0.020	0.020	0.000	0.000	0.000
127	A	71	ASN	0	0.093	0.036	17.749	0.027	0.027	0.000	0.000	0.000
128	A	71	ASN	0	-0.084	0.079	16.819	0.033	0.033	0.000	0.000	0.000
129	A	72	ILE	0	0.091	-0.094	17.653	-0.044	-0.044	0.000	0.000	0.000
130	A	72	ILE	0	-0.044	0.108	18.054	-0.001	-0.001	0.000	0.000	0.000
131	A	73	TYR	0	0.068	-0.088	14.599	0.073	0.073	0.000	0.000	0.000
132	A	73	TYR	0	-0.046	0.091	12.615	-0.029	-0.029	0.000	0.000	0.000
133	A	74	TYR	0	0.115	-0.087	13.719	0.010	0.010	0.000	0.000	0.000
134	A	74	TYR	0	-0.046	0.109	14.163	-0.008	-0.008	0.000	0.000	0.000
135	A	75	PHE	0	0.041	-0.111	12.756	-0.054	-0.054	0.000	0.000	0.000
136	A	75	PHE	0	-0.080	0.128	12.415	0.026	0.026	0.000	0.000	0.000
137	A	76	GLY	0	0.076	-0.065	12.251	0.085	0.085	0.000	0.000	0.000
138	A	77	ASN	0	0.116	0.011	13.594	-0.001	-0.001	0.000	0.000	0.000
139	A	77	ASN	0	-0.086	0.084	15.861	-0.015	-0.015	0.000	0.000	0.000
140	A	78	ASN	0	0.046	-0.090	11.907	0.096	0.096	0.000	0.000	0.000
141	A	78	ASN	0	-0.030	0.098	8.956	0.141	0.141	0.000	0.000	0.000
142	A	79	SER	0	0.030	-0.072	12.722	-0.122	-0.122	0.000	0.000	0.000
143	A	79	SER	0	-0.020	0.083	14.448	0.052	0.052	0.000	0.000	0.000
144	A	80	LYS	0	0.052	-0.117	9.005	0.131	0.131	0.000	0.000	0.000
145	A	80	LYS	1	0.782	1.042	8.185	1.262	1.262	0.000	0.000	0.000
146	A	81	ALA	0	0.050	-0.096	9.743	0.023	0.023	0.000	0.000	0.000
147	A	81	ALA	0	-0.040	0.107	9.538	0.037	0.037	0.000	0.000	0.000
148	A	82	VAL	0	0.032	-0.115	8.040	-0.358	-0.358	0.000	0.000	0.000
149	A	82	VAL	0	-0.106	0.092	10.544	0.008	0.008	0.000	0.000	0.000
150	A	83	THR	0	0.003	-0.108	6.957	0.010	0.010	0.000	0.000	0.000
151	A	83	THR	0	-0.036	0.080	5.628	0.367	0.367	0.000	0.000	0.000
152	A	84	GLY	0	0.035	-0.079	8.282	-0.089	-0.089	0.000	0.000	0.000
153	A	85	TRP	0	0.086	0.012	9.643	-0.148	-0.148	0.000	0.000	0.000
154	A	85	TRP	0	-0.058	0.090	12.871	-0.043	-0.043	0.000	0.000	0.000
155	A	86	GLN	0	0.002	-0.123	12.317	-0.041	-0.041	0.000	0.000	0.000
156	A	86	GLN	0	-0.058	0.099	10.146	-0.088	-0.088	0.000	0.000	0.000
157	A	87	THR	0	0.030	-0.080	14.515	0.037	0.037	0.000	0.000	0.000
158	A	87	THR	0	-0.021	0.078	17.739	0.009	0.009	0.000	0.000	0.000
159	A	88	ILE	0	0.063	-0.100	18.167	-0.042	-0.042	0.000	0.000	0.000
160	A	88	ILE	0	-0.075	0.105	15.994	-0.004	-0.004	0.000	0.000	0.000
161	A	89	ASN	0	0.037	-0.093	19.915	0.020	0.020	0.000	0.000	0.000
162	A	89	ASN	0	-0.105	0.070	23.931	-0.011	-0.011	0.000	0.000	0.000
163	A	90	GLY	0	0.032	-0.104	22.712	0.009	0.009	0.000	0.000	0.000
164	A	91	ASN	0	0.079	0.018	22.536	0.017	0.017	0.000	0.000	0.000
165	A	91	ASN	0	-0.068	0.091	22.342	0.008	0.008	0.000	0.000	0.000
166	A	92	MET	0	0.105	-0.089	18.842	-0.032	-0.032	0.000	0.000	0.000
167	A	92	MET	0	-0.074	0.110	17.471	0.008	0.008	0.000	0.000	0.000
168	A	93	TYR	0	0.074	-0.091	16.898	0.009	0.009	0.000	0.000	0.000
169	A	93	TYR	0	-0.044	0.095	16.166	-0.022	-0.022	0.000	0.000	0.000
170	A	94	TYR	0	0.141	-0.080	13.699	-0.019	-0.019	0.000	0.000	0.000
171	A	94	TYR	0	-0.047	0.113	10.756	0.048	0.048	0.000	0.000	0.000
172	A	95	PHE	0	0.055	-0.083	11.702	0.013	0.013	0.000	0.000	0.000
173	A	95	PHE	0	-0.143	0.087	11.059	-0.062	-0.062	0.000	0.000	0.000
174	A	96	MET	0	0.158	-0.106	10.064	0.221	0.221	0.000	0.000	0.000
175	A	96	MET	0	-0.086	0.141	11.291	0.005	0.005	0.000	0.000	0.000
176	A	97	PRO	0	0.030	-0.109	5.602	-0.139	-0.139	0.000	0.000	0.000
177	A	98	ASP	0	0.021	-0.020	5.593	0.451	0.451	0.000	0.000	0.000
178	A	98	ASP	-1	-0.909	-0.816	8.218	1.164	1.164	0.000	0.000	0.000
179	A	99	THR	0	-0.028	-0.163	7.482	-0.251	-0.251	0.000	0.000	0.000
180	A	99	THR	0	-0.011	0.095	11.106	-0.063	-0.063	0.000	0.000	0.000
181	A	100	ALA	0	0.064	-0.067	8.939	-0.155	-0.155	0.000	0.000	0.000
182	A	100	ALA	0	-0.042	0.098	8.524	-0.076	-0.076	0.000	0.000	0.000
183	A	101	MET	0	0.040	-0.122	9.828	-0.153	-0.153	0.000	0.000	0.000
184	A	101	MET	0	-0.103	0.100	13.202	0.006	0.006	0.000	0.000	0.000
185	A	102	ALA	0	0.104	-0.100	13.312	0.130	0.130	0.000	0.000	0.000
186	A	102	ALA	0	-0.074	0.104	16.341	-0.015	-0.015	0.000	0.000	0.000
187	A	103	ALA	0	0.063	-0.129	15.523	-0.015	-0.015	0.000	0.000	0.000
188	A	103	ALA	0	-0.079	0.131	16.089	0.011	0.011	0.000	0.000	0.000
189	A	104	ALA	0	0.052	-0.148	17.130	-0.026	-0.026	0.000	0.000	0.000
190	A	104	ALA	0	-0.069	0.131	19.960	-0.008	-0.008	0.000	0.000	0.000
191	A	105	GLY	0	-0.092	-0.129	20.692	0.008	0.008	0.000	0.000	0.000
192	A	106	GLY	0	0.025	0.004	23.521	-0.001	-0.001	0.000	0.000	0.000
193	A	107	LEU	0	0.048	-0.030	23.166	-0.002	-0.002	0.000	0.000	0.000
194	A	107	LEU	0	-0.068	0.106	24.466	-0.004	-0.004	0.000	0.000	0.000
195	A	108	PHE	0	0.042	-0.081	19.020	-0.002	-0.002	0.000	0.000	0.000
196	A	108	PHE	0	-0.081	0.080	17.279	0.013	0.013	0.000	0.000	0.000
197	A	109	GLU	0	0.154	-0.110	19.477	-0.031	-0.031	0.000	0.000	0.000
198	A	109	GLU	-1	-1.000	-0.827	19.773	0.461	0.461	0.000	0.000	0.000
199	A	110	ILE	0	0.044	-0.108	15.839	0.080	0.080	0.000	0.000	0.000
200	A	110	ILE	0	-0.134	0.078	13.903	-0.018	-0.018	0.000	0.000	0.000
201	A	111	ASP	0	0.039	-0.112	15.365	-0.072	-0.072	0.000	0.000	0.000
202	A	111	ASP	-1	-1.025	-0.867	13.374	1.133	1.133	0.000	0.000	0.000
203	A	112	GLY	0	0.035	-0.108	16.211	-0.058	-0.058	0.000	0.000	0.000
204	A	113	VAL	0	0.077	0.005	19.312	-0.054	-0.054	0.000	0.000	0.000
205	A	113	VAL	0	-0.091	0.089	19.873	-0.008	-0.008	0.000	0.000	0.000
206	A	114	ILE	0	0.052	-0.088	20.232	0.045	0.045	0.000	0.000	0.000
207	A	114	ILE	0	-0.060	0.106	22.911	-0.008	-0.008	0.000	0.000	0.000
208	A	115	TYR	0	0.025	-0.136	21.277	-0.033	-0.033	0.000	0.000	0.000
209	A	115	TYR	0	-0.029	0.105	18.471	-0.030	-0.030	0.000	0.000	0.000
210	A	116	PHE	0	0.101	-0.066	22.505	0.022	0.022	0.000	0.000	0.000
211	A	116	PHE	0	-0.059	0.088	25.808	-0.005	-0.005	0.000	0.000	0.000
212	A	117	PHE	0	0.022	-0.119	21.269	-0.013	-0.013	0.000	0.000	0.000
213	A	117	PHE	0	-0.084	0.119	17.699	0.019	0.019	0.000	0.000	0.000
214	A	118	GLY	0	0.073	-0.064	22.715	-0.004	-0.004	0.000	0.000	0.000
215	A	119	VAL	0	0.077	-0.010	23.253	0.018	0.018	0.000	0.000	0.000
216	A	119	VAL	0	-0.044	0.110	25.863	-0.001	-0.001	0.000	0.000	0.000
217	A	120	ASP	0	0.021	-0.127	23.509	-0.001	-0.001	0.000	0.000	0.000
218	A	120	ASP	-1	-0.915	-0.826	24.514	0.083	0.083	0.000	0.000	0.000
219	A	121	GLY	0	-0.033	-0.133	20.047	-0.019	-0.019	0.000	0.000	0.000
220	A	122	VAL	0	0.055	0.002	19.908	0.029	0.029	0.000	0.000	0.000
221	A	122	VAL	0	-0.088	0.109	22.485	-0.004	-0.004	0.000	0.000	0.000
222	A	123	LYS	0	0.136	-0.103	20.888	0.006	0.006	0.000	0.000	0.000
223	A	123	LYS	1	0.751	1.031	19.874	-0.225	-0.225	0.000	0.000	0.000
224	A	124	ALA	0	0.084	-0.139	21.903	-0.025	-0.025	0.000	0.000	0.000
225	A	124	ALA	0	-0.095	0.141	25.905	0.000	0.000	0.000	0.000	0.000
226	A	125	PRO	0	-0.083	-0.134	24.884	0.020	0.020	0.000	0.000	0.000
227	A	126	GLY	0	0.008	0.017	26.486	0.001	0.001	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:TYR)