FMO DATABASE

FMODB ID: 2L98R

Calculation Name: 1YN5-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1YN5

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H3

Base Structure: X-ray

Registration Date: 2025-07-09

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	199
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-775968.142853
FMO2-HF: Nuclear repulsion	735483.061233
FMO2-HF: Total energy	-40485.08162
FMO2-MP2: Total energy	-40603.981095

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:42:ALA)

Summations of interaction energy for fragment #1(A:42:ALA)

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.
-8.234	-0.394	1.057	-4.501	-4.398	-0.011

Interaction energy analysis for fragmet #1(A:42:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.183 / q_NPA : 0.046

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].	q(I=>J)Charge transfer value from I to J fragmens [e].
4	A	43	LYS	1	0.834	1.099	4.157	0.604	1.064	0.000	-0.256	-0.204	0.000
5	A	44	GLU	0	0.142	-0.117	3.766	-4.113	-1.010	-0.045	-1.739	-1.319	0.003
6	A	44	GLU	-1	-0.929	-0.810	5.343	1.677	1.677	0.000	0.000	0.000	0.000
7	A	45	MET	0	0.062	-0.082	5.666	-0.610	-0.610	0.000	0.000	0.000	0.000
8	A	45	MET	0	-0.133	0.106	8.756	-0.095	-0.095	0.000	0.000	0.000	0.000
9	A	46	GLN	0	0.107	-0.098	8.400	0.215	0.215	0.000	0.000	0.000	0.000
10	A	46	GLN	0	-0.059	0.117	8.877	0.058	0.058	0.000	0.000	0.000	0.000
11	A	47	ASN	0	0.111	-0.090	10.489	-0.103	-0.103	0.000	0.000	0.000	0.000
12	A	47	ASN	0	-0.125	0.063	15.333	-0.022	-0.022	0.000	0.000	0.000	0.000
13	A	48	VAL	0	0.073	-0.151	14.229	0.045	0.045	0.000	0.000	0.000	0.000
14	A	48	VAL	0	-0.107	0.106	12.595	-0.012	-0.012	0.000	0.000	0.000	0.000
15	A	49	PRO	0	-0.016	-0.084	15.316	-0.014	-0.014	0.000	0.000	0.000	0.000
16	A	50	TYR	0	0.072	0.002	19.087	-0.014	-0.014	0.000	0.000	0.000	0.000
17	A	50	TYR	0	-0.125	0.018	18.969	-0.006	-0.006	0.000	0.000	0.000	0.000
18	A	51	THR	0	0.021	-0.093	21.143	0.012	0.012	0.000	0.000	0.000	0.000
19	A	51	THR	0	-0.012	0.056	24.514	0.000	0.000	0.000	0.000	0.000	0.000
20	A	52	ILE	0	0.137	-0.123	24.866	-0.013	-0.013	0.000	0.000	0.000	0.000
21	A	52	ILE	0	-0.080	0.133	24.489	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	53	ALA	0	0.149	-0.103	26.986	0.009	0.009	0.000	0.000	0.000	0.000
23	A	53	ALA	0	-0.129	0.109	30.146	0.001	0.001	0.000	0.000	0.000	0.000
24	A	54	VAL	0	0.051	-0.127	30.387	-0.007	-0.007	0.000	0.000	0.000	0.000
25	A	54	VAL	0	-0.100	0.108	30.724	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	55	ASP	0	-0.003	-0.134	32.706	0.005	0.005	0.000	0.000	0.000	0.000
27	A	55	ASP	-1	-0.855	-0.790	36.876	-0.072	-0.072	0.000	0.000	0.000	0.000
28	A	56	GLY	0	-0.006	-0.119	34.480	0.005	0.005	0.000	0.000	0.000	0.000
29	A	57	ILE	0	0.092	0.002	34.745	0.004	0.004	0.000	0.000	0.000	0.000
30	A	57	ILE	0	-0.071	0.119	34.009	0.000	0.000	0.000	0.000	0.000	0.000
31	A	58	MET	0	0.074	-0.119	30.988	-0.009	-0.009	0.000	0.000	0.000	0.000
32	A	58	MET	0	-0.059	0.147	28.383	0.002	0.002	0.000	0.000	0.000	0.000
33	A	59	ALA	0	0.108	-0.112	28.493	0.005	0.005	0.000	0.000	0.000	0.000
34	A	59	ALA	0	-0.029	0.123	27.961	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	60	PHE	0	0.143	-0.010	29.976	0.002	0.002	0.000	0.000	0.000	0.000
36	A	60	PHE	0	-0.113	0.084	31.547	0.001	0.001	0.000	0.000	0.000	0.000
37	A	61	ASN	0	-0.019	-0.110	28.802	0.003	0.003	0.000	0.000	0.000	0.000
38	A	61	ASN	0	-0.175	0.023	27.939	0.001	0.001	0.000	0.000	0.000	0.000
39	A	62	GLN	0	0.237	-0.160	25.108	-0.005	-0.005	0.000	0.000	0.000	0.000
40	A	62	GLN	0	-0.138	0.133	23.192	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	63	SER	0	-0.014	-0.043	22.541	0.017	0.017	0.000	0.000	0.000	0.000
42	A	63	SER	0	-0.033	0.093	21.935	0.002	0.002	0.000	0.000	0.000	0.000
43	A	64	TYR	0	0.090	-0.125	18.247	-0.005	-0.005	0.000	0.000	0.000	0.000
44	A	64	TYR	0	-0.070	0.106	17.188	0.008	0.008	0.000	0.000	0.000	0.000
45	A	65	LEU	0	0.118	-0.088	16.001	0.005	0.005	0.000	0.000	0.000	0.000
46	A	65	LEU	0	-0.105	0.127	13.649	-0.009	-0.009	0.000	0.000	0.000	0.000
47	A	66	ASN	0	0.148	-0.075	12.346	0.022	0.022	0.000	0.000	0.000	0.000
48	A	66	ASN	0	-0.106	0.054	11.564	0.022	0.022	0.000	0.000	0.000	0.000
49	A	67	LEU	0	0.013	-0.188	9.360	-0.073	-0.073	0.000	0.000	0.000	0.000
50	A	67	LEU	0	-0.039	0.143	9.125	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	68	PRO	0	-0.019	-0.094	4.303	0.300	0.404	-0.001	-0.046	-0.057	0.000
52	A	69	LYS	0	0.135	0.042	5.055	-0.285	-0.159	-0.002	-0.011	-0.113	0.000
53	A	69	LYS	1	0.829	1.056	3.456	-2.071	-1.848	0.005	-0.052	-0.176	0.000
54	A	70	ASP	0	0.029	-0.154	2.898	-2.475	-1.192	0.428	-0.757	-0.954	-0.007
55	A	70	ASP	-1	-0.966	-0.807	2.438	0.423	1.004	0.453	-0.558	-0.476	0.001
56	A	71	SER	0	0.026	-0.083	3.198	-1.245	0.011	0.092	-0.640	-0.709	-0.005
57	A	71	SER	0	-0.030	0.054	3.013	-1.420	-0.694	0.129	-0.430	-0.425	-0.003
58	A	72	GLN	0	0.176	-0.025	4.643	0.362	0.340	-0.002	-0.012	0.035	0.000
59	A	72	GLN	0	-0.079	0.108	6.659	0.141	0.141	0.000	0.000	0.000	0.000
60	A	73	LEU	0	0.098	-0.107	8.233	-0.142	-0.142	0.000	0.000	0.000	0.000
61	A	73	LEU	0	-0.085	0.114	6.608	0.012	0.012	0.000	0.000	0.000	0.000
62	A	74	SER	0	0.135	-0.034	9.830	0.116	0.116	0.000	0.000	0.000	0.000
63	A	74	SER	0	-0.037	0.097	13.566	0.030	0.030	0.000	0.000	0.000	0.000
64	A	75	TYR	0	0.084	-0.099	13.468	-0.014	-0.014	0.000	0.000	0.000	0.000
65	A	75	TYR	0	-0.094	0.087	16.511	0.013	0.013	0.000	0.000	0.000	0.000
66	A	76	LEU	0	0.071	-0.105	16.377	0.039	0.039	0.000	0.000	0.000	0.000
67	A	76	LEU	0	-0.058	0.120	17.305	-0.002	-0.002	0.000	0.000	0.000	0.000
68	A	77	ASP	0	0.137	-0.111	14.195	0.069	0.069	0.000	0.000	0.000	0.000
69	A	77	ASP	-1	-1.013	-0.825	13.364	-0.712	-0.712	0.000	0.000	0.000	0.000
70	A	78	LEU	0	0.062	-0.143	15.161	0.020	0.020	0.000	0.000	0.000	0.000
71	A	78	LEU	0	-0.095	0.127	14.299	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	79	GLY	0	-0.022	-0.107	15.790	0.044	0.044	0.000	0.000	0.000	0.000
73	A	80	ASN	0	0.109	0.026	18.463	0.046	0.046	0.000	0.000	0.000	0.000
74	A	80	ASN	0	-0.084	0.080	18.012	0.021	0.021	0.000	0.000	0.000	0.000
75	A	81	LYS	0	0.049	-0.097	17.043	0.033	0.033	0.000	0.000	0.000	0.000
76	A	81	LYS	1	0.884	1.074	12.232	0.599	0.599	0.000	0.000	0.000	0.000
77	A	82	VAL	0	0.098	-0.096	18.351	0.026	0.026	0.000	0.000	0.000	0.000
78	A	82	VAL	0	-0.079	0.100	19.197	0.002	0.002	0.000	0.000	0.000	0.000
79	A	83	LYS	0	0.141	-0.073	20.903	0.027	0.027	0.000	0.000	0.000	0.000
80	A	83	LYS	1	0.730	0.988	22.489	0.246	0.246	0.000	0.000	0.000	0.000
81	A	84	ALA	0	0.105	-0.107	21.430	0.026	0.026	0.000	0.000	0.000	0.000
82	A	84	ALA	0	-0.113	0.100	20.726	-0.006	-0.006	0.000	0.000	0.000	0.000
83	A	85	LEU	0	0.093	-0.082	21.885	0.017	0.017	0.000	0.000	0.000	0.000
84	A	85	LEU	0	-0.099	0.090	19.599	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	86	LEU	0	0.063	-0.076	23.255	0.019	0.019	0.000	0.000	0.000	0.000
86	A	86	LEU	0	-0.125	0.067	25.368	0.002	0.002	0.000	0.000	0.000	0.000
87	A	87	TYR	0	0.128	-0.078	26.173	0.017	0.017	0.000	0.000	0.000	0.000
88	A	87	TYR	0	-0.101	0.072	26.543	0.002	0.002	0.000	0.000	0.000	0.000
89	A	88	ASP	0	0.058	-0.116	25.401	0.016	0.016	0.000	0.000	0.000	0.000
90	A	88	ASP	-1	-1.006	-0.853	24.493	-0.168	-0.168	0.000	0.000	0.000	0.000
91	A	89	GLU	0	0.075	-0.102	26.440	0.011	0.011	0.000	0.000	0.000	0.000
92	A	89	GLU	-1	-0.940	-0.792	24.270	-0.108	-0.108	0.000	0.000	0.000	0.000
93	A	90	ARG	0	-0.055	-0.149	27.954	0.012	0.012	0.000	0.000	0.000	0.000
94	A	90	ARG	1	0.749	1.026	29.013	0.081	0.081	0.000	0.000	0.000	0.000
95	A	91	GLY	0	0.073	-0.065	30.125	0.007	0.007	0.000	0.000	0.000	0.000
96	A	92	VAL	0	0.040	-0.041	30.354	0.005	0.005	0.000	0.000	0.000	0.000
97	A	92	VAL	0	-0.121	0.113	29.518	0.000	0.000	0.000	0.000	0.000	0.000
98	A	93	THR	0	0.018	-0.070	29.718	-0.012	-0.012	0.000	0.000	0.000	0.000
99	A	93	THR	0	0.011	0.080	32.686	0.000	0.000	0.000	0.000	0.000	0.000
100	A	94	PRO	0	0.088	-0.093	28.806	0.002	0.002	0.000	0.000	0.000	0.000
101	A	95	GLU	0	0.102	-0.044	30.864	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	95	GLU	-1	-0.985	-0.830	35.353	-0.092	-0.092	0.000	0.000	0.000	0.000
103	A	96	LYS	0	0.047	-0.129	33.510	0.007	0.007	0.000	0.000	0.000	0.000
104	A	96	LYS	1	0.888	1.109	33.035	0.082	0.082	0.000	0.000	0.000	0.000
105	A	97	ILE	0	0.077	-0.086	30.480	0.009	0.009	0.000	0.000	0.000	0.000
106	A	97	ILE	0	-0.050	0.099	27.610	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	98	ARG	0	0.031	-0.121	31.922	0.000	0.000	0.000	0.000	0.000	0.000
108	A	98	ARG	1	0.868	1.075	32.680	0.122	0.122	0.000	0.000	0.000	0.000
109	A	99	ASN	0	0.076	-0.082	34.072	0.001	0.001	0.000	0.000	0.000	0.000
110	A	99	ASN	0	-0.093	0.080	37.704	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	100	ALA	0	0.076	-0.091	34.160	0.008	0.008	0.000	0.000	0.000	0.000
112	A	100	ALA	0	-0.099	0.110	33.558	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	101	LYS	0	0.114	-0.053	35.634	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	101	LYS	1	0.809	1.031	36.923	0.071	0.071	0.000	0.000	0.000	0.000
115	A	102	SER	0	-0.006	-0.123	33.393	0.000	0.000	0.000	0.000	0.000	0.000
116	A	102	SER	0	-0.042	0.067	32.693	0.004	0.004	0.000	0.000	0.000	0.000
117	A	103	ALA	0	0.093	-0.077	29.965	0.008	0.008	0.000	0.000	0.000	0.000
118	A	103	ALA	0	-0.062	0.109	29.163	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	104	VAL	0	-0.008	-0.122	26.604	-0.007	-0.007	0.000	0.000	0.000	0.000
120	A	104	VAL	0	-0.057	0.139	26.480	0.001	0.001	0.000	0.000	0.000	0.000
121	A	105	TYR	0	0.127	-0.034	22.875	0.011	0.011	0.000	0.000	0.000	0.000
122	A	105	TYR	0	-0.037	0.077	19.100	-0.013	-0.013	0.000	0.000	0.000	0.000
123	A	106	THR	0	0.000	-0.122	23.370	-0.015	-0.015	0.000	0.000	0.000	0.000
124	A	106	THR	0	-0.019	0.093	23.809	0.004	0.004	0.000	0.000	0.000	0.000
125	A	107	ILE	0	0.069	-0.106	19.190	0.009	0.009	0.000	0.000	0.000	0.000
126	A	107	ILE	0	-0.048	0.105	16.939	-0.006	-0.006	0.000	0.000	0.000	0.000
127	A	108	THR	0	0.029	-0.070	19.648	0.005	0.005	0.000	0.000	0.000	0.000
128	A	108	THR	0	-0.076	0.061	20.745	0.008	0.008	0.000	0.000	0.000	0.000
129	A	109	TRP	0	0.133	-0.081	17.131	-0.009	-0.009	0.000	0.000	0.000	0.000
130	A	109	TRP	0	-0.100	0.119	14.167	-0.019	-0.019	0.000	0.000	0.000	0.000
131	A	110	LYS	0	0.074	-0.120	16.624	0.015	0.015	0.000	0.000	0.000	0.000
132	A	110	LYS	1	0.769	1.039	12.692	0.048	0.048	0.000	0.000	0.000	0.000
133	A	111	ASP	0	-0.018	-0.149	17.894	0.023	0.023	0.000	0.000	0.000	0.000
134	A	111	ASP	-1	-0.817	-0.716	19.962	-0.084	-0.084	0.000	0.000	0.000	0.000
135	A	112	GLY	0	-0.041	-0.109	20.702	0.008	0.008	0.000	0.000	0.000	0.000
136	A	113	SER	0	0.028	-0.003	22.146	0.003	0.003	0.000	0.000	0.000	0.000
137	A	113	SER	0	-0.056	0.036	21.327	-0.008	-0.008	0.000	0.000	0.000	0.000
138	A	114	LYS	0	-0.004	-0.144	21.926	-0.007	-0.007	0.000	0.000	0.000	0.000
139	A	114	LYS	1	0.884	1.075	23.771	0.075	0.075	0.000	0.000	0.000	0.000
140	A	115	LYS	0	0.114	-0.086	21.583	0.009	0.009	0.000	0.000	0.000	0.000
141	A	115	LYS	1	0.843	1.075	19.682	0.230	0.230	0.000	0.000	0.000	0.000
142	A	116	GLU	0	0.092	-0.145	22.585	-0.012	-0.012	0.000	0.000	0.000	0.000
143	A	116	GLU	-1	-0.985	-0.804	26.368	-0.111	-0.111	0.000	0.000	0.000	0.000
144	A	117	VAL	0	0.042	-0.139	22.604	0.004	0.004	0.000	0.000	0.000	0.000
145	A	117	VAL	0	-0.121	0.115	20.706	-0.005	-0.005	0.000	0.000	0.000	0.000
146	A	118	ASP	0	0.197	-0.115	24.015	0.001	0.001	0.000	0.000	0.000	0.000
147	A	118	ASP	-1	-0.967	-0.818	27.857	-0.135	-0.135	0.000	0.000	0.000	0.000
148	A	119	LEU	0	0.056	-0.104	25.892	-0.012	-0.012	0.000	0.000	0.000	0.000
149	A	119	LEU	0	-0.098	0.082	23.185	-0.001	-0.001	0.000	0.000	0.000	0.000
150	A	120	LYS	0	0.056	-0.103	26.733	-0.005	-0.005	0.000	0.000	0.000	0.000
151	A	120	LYS	1	0.740	1.017	31.083	0.106	0.106	0.000	0.000	0.000	0.000
152	A	121	LYS	0	0.036	-0.090	28.430	0.008	0.008	0.000	0.000	0.000	0.000
153	A	121	LYS	1	0.825	1.051	28.463	0.127	0.127	0.000	0.000	0.000	0.000
154	A	122	ASP	0	0.200	-0.027	25.612	-0.009	-0.009	0.000	0.000	0.000	0.000
155	A	122	ASP	-1	-0.948	-0.826	24.401	-0.230	-0.230	0.000	0.000	0.000	0.000
156	A	123	SER	0	-0.017	-0.126	24.905	0.013	0.013	0.000	0.000	0.000	0.000
157	A	123	SER	0	-0.035	0.060	26.852	0.003	0.003	0.000	0.000	0.000	0.000
158	A	124	TYR	0	0.042	-0.104	22.794	-0.012	-0.012	0.000	0.000	0.000	0.000
159	A	124	TYR	0	-0.041	0.106	19.692	0.006	0.006	0.000	0.000	0.000	0.000
160	A	125	THR	0	0.011	-0.090	21.060	0.025	0.025	0.000	0.000	0.000	0.000
161	A	125	THR	0	-0.030	0.073	18.953	-0.006	-0.006	0.000	0.000	0.000	0.000
162	A	126	ALA	0	0.142	-0.096	18.234	-0.025	-0.025	0.000	0.000	0.000	0.000
163	A	126	ALA	0	-0.053	0.129	18.575	0.004	0.004	0.000	0.000	0.000	0.000
164	A	127	ASN	0	0.071	-0.075	16.591	-0.047	-0.047	0.000	0.000	0.000	0.000
165	A	127	ASN	0	-0.142	0.049	17.886	0.001	0.001	0.000	0.000	0.000	0.000
166	A	128	LEU	0	0.098	-0.134	12.739	0.012	0.012	0.000	0.000	0.000	0.000
167	A	128	LEU	0	-0.052	0.130	11.396	-0.012	-0.012	0.000	0.000	0.000	0.000
168	A	129	PHE	0	0.034	-0.071	12.129	0.072	0.072	0.000	0.000	0.000	0.000
169	A	129	PHE	0	-0.097	0.055	11.347	0.000	0.000	0.000	0.000	0.000	0.000
170	A	130	ASP	0	0.178	-0.114	9.601	-0.152	-0.152	0.000	0.000	0.000	0.000
171	A	130	ASP	-1	-1.036	-0.820	8.999	-0.392	-0.392	0.000	0.000	0.000	0.000
172	A	131	SER	0	0.061	-0.124	7.314	0.178	0.178	0.000	0.000	0.000	0.000
173	A	131	SER	0	-0.139	0.036	6.732	-0.147	-0.147	0.000	0.000	0.000	0.000
174	A	132	ASN	0	0.044	-0.100	8.545	0.066	0.066	0.000	0.000	0.000	0.000
175	A	132	ASN	0	-0.070	0.107	6.803	0.027	0.027	0.000	0.000	0.000	0.000
176	A	133	SER	0	0.043	-0.124	9.773	0.100	0.100	0.000	0.000	0.000	0.000
177	A	133	SER	0	-0.018	0.091	12.637	0.018	0.018	0.000	0.000	0.000	0.000
178	A	134	ILE	0	0.056	-0.110	12.184	0.050	0.050	0.000	0.000	0.000	0.000
179	A	134	ILE	0	-0.049	0.140	12.243	-0.006	-0.006	0.000	0.000	0.000	0.000
180	A	135	LYS	0	0.069	-0.107	13.975	0.028	0.028	0.000	0.000	0.000	0.000
181	A	135	LYS	1	0.850	1.065	17.687	0.026	0.026	0.000	0.000	0.000	0.000
182	A	136	GLN	0	0.083	-0.123	16.824	0.011	0.011	0.000	0.000	0.000	0.000
183	A	136	GLN	0	-0.127	0.078	20.185	0.014	0.014	0.000	0.000	0.000	0.000
184	A	137	ILE	0	0.040	-0.128	18.912	-0.008	-0.008	0.000	0.000	0.000	0.000
185	A	137	ILE	0	-0.086	0.109	15.872	-0.006	-0.006	0.000	0.000	0.000	0.000
186	A	138	ASP	0	0.111	-0.076	20.056	0.005	0.005	0.000	0.000	0.000	0.000
187	A	138	ASP	-1	-0.948	-0.782	24.323	-0.089	-0.089	0.000	0.000	0.000	0.000
188	A	139	ILE	0	0.175	-0.112	23.811	-0.007	-0.007	0.000	0.000	0.000	0.000
189	A	139	ILE	0	-0.128	0.118	21.560	-0.002	-0.002	0.000	0.000	0.000	0.000
190	A	140	ASN	0	0.088	-0.092	25.142	0.011	0.011	0.000	0.000	0.000	0.000
191	A	140	ASN	0	-0.155	0.059	28.699	0.002	0.002	0.000	0.000	0.000	0.000
192	A	141	VAL	0	0.105	-0.104	28.784	-0.005	-0.005	0.000	0.000	0.000	0.000
193	A	141	VAL	0	-0.065	0.121	28.807	-0.001	-0.001	0.000	0.000	0.000	0.000
194	A	142	LYS	0	0.119	-0.051	31.224	0.007	0.007	0.000	0.000	0.000	0.000
195	A	142	LYS	1	0.799	1.035	33.711	0.074	0.074	0.000	0.000	0.000	0.000
196	A	143	THR	0	0.069	-0.073	34.950	-0.004	-0.004	0.000	0.000	0.000	0.000
197	A	143	THR	0	-0.062	0.052	36.335	-0.002	-0.002	0.000	0.000	0.000	0.000
198	A	144	LYS	0	0.020	-0.053	37.111	0.001	0.001	0.000	0.000	0.000	0.000
199	A	144	LYS	1	0.969	0.958	38.180	0.066	0.066	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:42:ALA)