FMO DATABASE

FMODB ID: N6Y7Q

Calculation Name: 1OI4-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1OI4

Chain ID: A

ChEMBL ID:

UniProt ID: P45470

Base Structure: X-ray

Registration Date: 2025-10-11

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	191
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2159175.939734
FMO2-HF: Nuclear repulsion	2086287.345087
FMO2-HF: Total energy	-72888.594646
FMO2-MP2: Total energy	-73106.935024

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:SER)

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

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.
-161.302	-162.276	21.032	-11.475	-8.582	-0.135

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.776 / q_NPA : 0.858

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].
3	A	4	TYR	0	-0.059	-0.052	3.019	-4.781	-2.577	0.051	-1.173	-1.082	-0.006
67	A	68	LYS	1	0.801	0.876	4.678	43.260	43.307	-0.001	-0.002	-0.043	0.000
69	A	70	GLU	-1	-0.909	-0.928	1.847	-139.053	-142.278	20.982	-10.300	-7.457	-0.129
4	A	5	HIS	0	0.001	0.008	5.697	3.403	3.403	0.000	0.000	0.000	0.000
5	A	6	HIS	0	-0.029	-0.023	8.191	0.123	0.123	0.000	0.000	0.000	0.000
6	A	7	HIS	0	0.027	0.012	9.726	2.047	2.047	0.000	0.000	0.000	0.000
7	A	8	HIS	0	-0.057	-0.024	11.738	0.840	0.840	0.000	0.000	0.000	0.000
8	A	9	HIS	1	0.853	0.904	14.930	18.385	18.385	0.000	0.000	0.000	0.000
9	A	10	HIS	1	0.767	0.857	16.415	15.871	15.871	0.000	0.000	0.000	0.000
10	A	11	LEU	0	0.048	0.025	19.303	-0.583	-0.583	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.808	-0.902	17.527	-16.808	-16.808	0.000	0.000	0.000	0.000
12	A	13	SER	0	-0.035	-0.030	20.988	0.465	0.465	0.000	0.000	0.000	0.000
13	A	14	THR	0	0.012	0.008	21.479	0.606	0.606	0.000	0.000	0.000	0.000
14	A	15	SER	0	-0.013	0.005	23.291	0.508	0.508	0.000	0.000	0.000	0.000
15	A	16	LEU	0	0.042	0.005	25.100	0.285	0.285	0.000	0.000	0.000	0.000
16	A	17	TYR	0	0.006	0.008	26.363	0.509	0.509	0.000	0.000	0.000	0.000
17	A	18	LYS	1	0.872	0.939	23.572	13.366	13.366	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.924	0.956	27.706	9.555	9.555	0.000	0.000	0.000	0.000
19	A	20	ALA	0	0.001	0.003	31.315	0.262	0.262	0.000	0.000	0.000	0.000
20	A	21	GLY	0	0.011	0.014	29.706	0.201	0.201	0.000	0.000	0.000	0.000
21	A	22	LEU	0	-0.024	-0.020	30.751	0.059	0.059	0.000	0.000	0.000	0.000
22	A	23	SER	0	-0.048	-0.024	25.654	0.169	0.169	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.870	0.936	25.915	11.365	11.365	0.000	0.000	0.000	0.000
24	A	25	LYS	1	0.786	0.878	24.633	10.678	10.678	0.000	0.000	0.000	0.000
25	A	26	ILE	0	-0.007	-0.005	19.978	0.263	0.263	0.000	0.000	0.000	0.000
26	A	27	ALA	0	0.013	0.016	21.901	-0.373	-0.373	0.000	0.000	0.000	0.000
27	A	28	VAL	0	0.005	-0.012	16.788	-0.598	-0.598	0.000	0.000	0.000	0.000
28	A	29	LEU	0	-0.013	0.015	20.227	0.211	0.211	0.000	0.000	0.000	0.000
29	A	30	ILE	0	-0.050	-0.028	14.595	-0.608	-0.608	0.000	0.000	0.000	0.000
30	A	31	THR	0	-0.014	-0.033	17.790	0.653	0.653	0.000	0.000	0.000	0.000
31	A	32	ASP	-1	-0.791	-0.901	15.449	-19.709	-19.709	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.840	-0.903	12.965	-18.432	-18.432	0.000	0.000	0.000	0.000
33	A	34	PHE	0	0.013	0.013	9.892	-0.142	-0.142	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.833	-0.902	7.824	-39.391	-39.391	0.000	0.000	0.000	0.000
35	A	36	ASP	-1	-0.755	-0.877	5.625	-40.886	-40.886	0.000	0.000	0.000	0.000
36	A	37	SER	0	0.007	0.004	5.627	1.895	1.895	0.000	0.000	0.000	0.000
37	A	38	GLU	-1	-0.755	-0.911	7.099	-21.741	-21.741	0.000	0.000	0.000	0.000
38	A	39	PHE	0	-0.017	0.002	10.357	2.641	2.641	0.000	0.000	0.000	0.000
39	A	40	THR	0	-0.023	-0.034	7.239	0.174	0.174	0.000	0.000	0.000	0.000
40	A	41	SER	0	0.007	0.019	8.674	2.287	2.287	0.000	0.000	0.000	0.000
41	A	42	PRO	0	0.034	0.014	10.200	1.456	1.456	0.000	0.000	0.000	0.000
42	A	43	ALA	0	0.017	0.012	12.884	1.468	1.468	0.000	0.000	0.000	0.000
43	A	44	ASP	-1	-0.795	-0.874	10.348	-26.820	-26.820	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.902	-0.927	13.358	-19.765	-19.765	0.000	0.000	0.000	0.000
45	A	46	PHE	0	0.013	-0.011	15.749	1.192	1.192	0.000	0.000	0.000	0.000
46	A	47	ARG	1	0.900	0.966	13.476	21.783	21.783	0.000	0.000	0.000	0.000
47	A	48	LYS	1	0.801	0.886	12.679	23.052	23.052	0.000	0.000	0.000	0.000
48	A	49	ALA	0	-0.025	-0.001	18.682	0.763	0.763	0.000	0.000	0.000	0.000
49	A	50	GLY	0	-0.014	0.004	21.438	0.733	0.733	0.000	0.000	0.000	0.000
50	A	51	HIS	0	0.050	0.026	21.538	0.788	0.788	0.000	0.000	0.000	0.000
51	A	52	GLU	-1	-0.914	-0.939	21.351	-14.068	-14.068	0.000	0.000	0.000	0.000
52	A	53	VAL	0	-0.003	0.007	16.970	0.121	0.121	0.000	0.000	0.000	0.000
53	A	54	ILE	0	-0.016	-0.017	20.035	0.013	0.013	0.000	0.000	0.000	0.000
54	A	55	THR	0	-0.039	-0.041	16.806	0.230	0.230	0.000	0.000	0.000	0.000
55	A	56	ILE	0	-0.023	0.001	20.066	0.542	0.542	0.000	0.000	0.000	0.000
56	A	57	GLU	-1	-0.724	-0.846	21.099	-15.252	-15.252	0.000	0.000	0.000	0.000
57	A	58	LYS	1	0.918	0.949	23.348	13.776	13.776	0.000	0.000	0.000	0.000
58	A	59	GLN	0	-0.011	-0.003	24.794	0.197	0.197	0.000	0.000	0.000	0.000
59	A	60	ALA	0	0.042	0.037	24.071	-0.624	-0.624	0.000	0.000	0.000	0.000
60	A	61	GLY	0	-0.018	-0.017	23.157	0.328	0.328	0.000	0.000	0.000	0.000
61	A	62	LYS	1	0.812	0.908	19.727	15.387	15.387	0.000	0.000	0.000	0.000
62	A	63	THR	0	-0.048	-0.028	15.874	-0.671	-0.671	0.000	0.000	0.000	0.000
63	A	64	VAL	0	-0.023	0.000	15.455	0.494	0.494	0.000	0.000	0.000	0.000
64	A	65	LYS	1	0.898	0.930	12.116	21.970	21.970	0.000	0.000	0.000	0.000
65	A	66	GLY	0	0.038	0.027	9.220	1.636	1.636	0.000	0.000	0.000	0.000
66	A	67	LYS	1	0.860	0.920	10.055	23.265	23.265	0.000	0.000	0.000	0.000
68	A	69	GLY	0	-0.012	0.005	7.145	-1.160	-1.160	0.000	0.000	0.000	0.000
70	A	71	ALA	0	0.053	0.022	5.409	-0.339	-0.339	0.000	0.000	0.000	0.000
71	A	72	SER	0	-0.063	-0.040	8.036	3.941	3.941	0.000	0.000	0.000	0.000
72	A	73	VAL	0	0.019	0.019	11.713	-0.150	-0.150	0.000	0.000	0.000	0.000
73	A	74	THR	0	0.007	0.011	14.212	0.616	0.616	0.000	0.000	0.000	0.000
74	A	75	ILE	0	-0.011	0.018	18.002	-0.446	-0.446	0.000	0.000	0.000	0.000
75	A	76	ASP	-1	-0.789	-0.858	20.401	-15.297	-15.297	0.000	0.000	0.000	0.000
76	A	77	LYS	1	0.849	0.913	22.869	11.911	11.911	0.000	0.000	0.000	0.000
77	A	78	SER	0	-0.023	-0.016	24.873	-0.590	-0.590	0.000	0.000	0.000	0.000
78	A	79	ILE	0	0.012	-0.020	26.796	0.162	0.162	0.000	0.000	0.000	0.000
79	A	80	ASP	-1	-0.859	-0.910	28.299	-10.110	-10.110	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.842	-0.896	28.867	-10.833	-10.833	0.000	0.000	0.000	0.000
81	A	82	VAL	0	-0.038	-0.017	27.231	-0.158	-0.158	0.000	0.000	0.000	0.000
82	A	83	THR	0	0.014	0.004	30.465	0.178	0.178	0.000	0.000	0.000	0.000
83	A	84	PRO	0	0.056	0.020	29.841	-0.222	-0.222	0.000	0.000	0.000	0.000
84	A	85	ALA	0	0.001	0.007	30.922	-0.063	-0.063	0.000	0.000	0.000	0.000
85	A	86	GLU	-1	-0.848	-0.915	29.285	-10.771	-10.771	0.000	0.000	0.000	0.000
86	A	87	PHE	0	0.037	0.013	25.659	-0.264	-0.264	0.000	0.000	0.000	0.000
87	A	88	ASP	-1	-0.817	-0.895	26.910	-10.827	-10.827	0.000	0.000	0.000	0.000
88	A	89	ALA	0	0.011	0.001	23.842	0.161	0.161	0.000	0.000	0.000	0.000
89	A	90	LEU	0	-0.030	-0.001	22.482	-0.139	-0.139	0.000	0.000	0.000	0.000
90	A	91	LEU	0	-0.014	0.000	15.207	-0.040	-0.040	0.000	0.000	0.000	0.000
91	A	92	LEU	0	-0.020	-0.021	19.267	0.108	0.108	0.000	0.000	0.000	0.000
92	A	93	PRO	0	0.021	0.006	13.819	-0.135	-0.135	0.000	0.000	0.000	0.000
93	A	94	GLY	0	0.035	0.013	14.428	1.187	1.187	0.000	0.000	0.000	0.000
94	A	95	GLY	0	-0.024	-0.015	13.559	-0.933	-0.933	0.000	0.000	0.000	0.000
95	A	96	HIS	0	0.063	0.015	14.153	0.378	0.378	0.000	0.000	0.000	0.000
96	A	97	SER	0	0.034	0.039	16.007	1.148	1.148	0.000	0.000	0.000	0.000
97	A	98	PRO	0	-0.009	-0.016	17.092	0.924	0.924	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.947	-0.972	20.150	-12.836	-12.836	0.000	0.000	0.000	0.000
99	A	100	TYR	0	-0.065	-0.071	18.006	1.037	1.037	0.000	0.000	0.000	0.000
100	A	101	LEU	0	-0.034	-0.006	20.775	0.560	0.560	0.000	0.000	0.000	0.000
101	A	102	ARG	1	0.870	0.939	23.762	12.946	12.946	0.000	0.000	0.000	0.000
102	A	103	GLY	0	0.009	0.013	26.083	0.474	0.474	0.000	0.000	0.000	0.000
103	A	104	ASP	-1	-0.808	-0.884	27.325	-10.700	-10.700	0.000	0.000	0.000	0.000
104	A	105	ASN	0	0.037	-0.001	29.022	-0.224	-0.224	0.000	0.000	0.000	0.000
105	A	106	ARG	1	0.795	0.877	29.431	10.865	10.865	0.000	0.000	0.000	0.000
106	A	107	PHE	0	0.035	0.013	24.075	-0.036	-0.036	0.000	0.000	0.000	0.000
107	A	108	VAL	0	0.010	0.022	27.545	-0.136	-0.136	0.000	0.000	0.000	0.000
108	A	109	THR	0	-0.044	-0.027	29.363	0.208	0.208	0.000	0.000	0.000	0.000
109	A	110	PHE	0	0.026	0.010	26.319	0.093	0.093	0.000	0.000	0.000	0.000
110	A	111	THR	0	-0.013	-0.027	26.248	-0.205	-0.205	0.000	0.000	0.000	0.000
111	A	112	ARG	1	0.887	0.944	28.067	9.593	9.593	0.000	0.000	0.000	0.000
112	A	113	ASP	-1	-0.880	-0.949	31.612	-9.201	-9.201	0.000	0.000	0.000	0.000
113	A	114	PHE	0	-0.029	-0.007	27.560	0.132	0.132	0.000	0.000	0.000	0.000
114	A	115	VAL	0	-0.007	0.015	28.565	0.093	0.093	0.000	0.000	0.000	0.000
115	A	116	ASN	0	0.006	-0.004	30.896	0.178	0.178	0.000	0.000	0.000	0.000
116	A	117	SER	0	-0.091	-0.049	31.948	0.248	0.248	0.000	0.000	0.000	0.000
117	A	118	GLY	0	-0.006	-0.003	33.584	0.126	0.126	0.000	0.000	0.000	0.000
118	A	119	LYS	1	0.803	0.906	29.356	10.183	10.183	0.000	0.000	0.000	0.000
119	A	120	PRO	0	0.012	0.003	25.937	-0.105	-0.105	0.000	0.000	0.000	0.000
120	A	121	VAL	0	-0.027	-0.011	23.787	-0.181	-0.181	0.000	0.000	0.000	0.000
121	A	122	PHE	0	0.027	0.013	19.745	0.019	0.019	0.000	0.000	0.000	0.000
122	A	123	ALA	0	-0.002	-0.007	19.626	-0.473	-0.473	0.000	0.000	0.000	0.000
123	A	124	ILE	0	-0.015	-0.001	13.770	0.459	0.459	0.000	0.000	0.000	0.000
124	A	125	CYS	0	0.002	0.018	13.756	0.177	0.177	0.000	0.000	0.000	0.000
125	A	126	HIS	0	-0.040	-0.039	16.125	1.516	1.516	0.000	0.000	0.000	0.000
126	A	127	GLY	0	0.036	0.034	18.058	0.824	0.824	0.000	0.000	0.000	0.000
127	A	128	PRO	0	0.003	-0.023	19.711	0.803	0.803	0.000	0.000	0.000	0.000
128	A	129	GLN	0	0.022	0.004	21.332	0.306	0.306	0.000	0.000	0.000	0.000
129	A	130	LEU	0	0.003	0.009	21.982	0.614	0.614	0.000	0.000	0.000	0.000
130	A	131	LEU	0	0.010	0.002	24.418	0.532	0.532	0.000	0.000	0.000	0.000
131	A	132	ILE	0	-0.020	-0.012	25.652	0.483	0.483	0.000	0.000	0.000	0.000
132	A	133	SER	0	-0.002	0.001	27.902	0.269	0.269	0.000	0.000	0.000	0.000
133	A	134	ALA	0	-0.023	-0.003	29.329	0.363	0.363	0.000	0.000	0.000	0.000
134	A	135	ASP	-1	-0.954	-0.970	31.124	-8.847	-8.847	0.000	0.000	0.000	0.000
135	A	136	VAL	0	-0.006	0.006	30.024	0.245	0.245	0.000	0.000	0.000	0.000
136	A	137	ILE	0	-0.005	-0.022	28.139	-0.093	-0.093	0.000	0.000	0.000	0.000
137	A	138	ARG	1	0.923	0.984	31.570	8.926	8.926	0.000	0.000	0.000	0.000
138	A	139	GLY	0	-0.005	-0.008	34.898	0.158	0.158	0.000	0.000	0.000	0.000
139	A	140	ARG	1	0.723	0.851	31.331	10.271	10.271	0.000	0.000	0.000	0.000
140	A	141	LYS	1	0.864	0.942	30.263	9.423	9.423	0.000	0.000	0.000	0.000
141	A	142	LEU	0	0.004	-0.016	25.520	-0.239	-0.239	0.000	0.000	0.000	0.000
142	A	143	THR	0	-0.001	-0.014	21.423	0.029	0.029	0.000	0.000	0.000	0.000
143	A	144	ALA	0	0.029	0.004	21.071	-0.149	-0.149	0.000	0.000	0.000	0.000
144	A	145	VAL	0	0.018	0.019	16.710	0.090	0.090	0.000	0.000	0.000	0.000
145	A	146	LYS	1	0.968	0.960	19.327	16.523	16.523	0.000	0.000	0.000	0.000
146	A	147	PRO	0	-0.010	-0.002	19.933	0.624	0.624	0.000	0.000	0.000	0.000
147	A	148	ILE	0	0.053	0.034	21.419	0.513	0.513	0.000	0.000	0.000	0.000
148	A	149	ILE	0	-0.027	0.001	23.578	0.479	0.479	0.000	0.000	0.000	0.000
149	A	150	ILE	0	-0.023	-0.007	26.194	0.437	0.437	0.000	0.000	0.000	0.000
150	A	151	ASP	-1	-0.860	-0.935	26.682	-11.322	-11.322	0.000	0.000	0.000	0.000
151	A	152	VAL	0	-0.010	-0.011	25.469	0.302	0.302	0.000	0.000	0.000	0.000
152	A	153	LYS	1	0.926	0.973	28.628	10.976	10.976	0.000	0.000	0.000	0.000
153	A	154	ASN	0	0.003	0.008	31.820	0.516	0.516	0.000	0.000	0.000	0.000
154	A	155	ALA	0	0.000	-0.003	30.914	0.324	0.324	0.000	0.000	0.000	0.000
155	A	156	GLY	0	-0.019	-0.014	32.919	0.161	0.161	0.000	0.000	0.000	0.000
156	A	157	ALA	0	-0.007	0.011	30.305	0.193	0.193	0.000	0.000	0.000	0.000
157	A	158	GLU	-1	-0.838	-0.901	32.190	-9.368	-9.368	0.000	0.000	0.000	0.000
158	A	159	PHE	0	-0.017	-0.022	24.249	-0.190	-0.190	0.000	0.000	0.000	0.000
159	A	160	TYR	0	-0.054	-0.046	27.427	0.406	0.406	0.000	0.000	0.000	0.000
160	A	161	ASP	-1	-0.894	-0.927	23.220	-14.297	-14.297	0.000	0.000	0.000	0.000
161	A	162	GLN	0	-0.024	-0.027	23.682	0.670	0.670	0.000	0.000	0.000	0.000
162	A	163	GLU	-1	-0.873	-0.934	19.111	-15.894	-15.894	0.000	0.000	0.000	0.000
163	A	164	VAL	0	-0.027	-0.003	19.513	-0.703	-0.703	0.000	0.000	0.000	0.000
164	A	165	VAL	0	-0.054	-0.003	21.992	0.653	0.653	0.000	0.000	0.000	0.000
165	A	166	VAL	0	0.025	0.008	24.667	-0.388	-0.388	0.000	0.000	0.000	0.000
166	A	167	ASP	-1	-0.780	-0.868	26.905	-9.541	-9.541	0.000	0.000	0.000	0.000
167	A	168	LYS	1	0.837	0.897	30.029	9.406	9.406	0.000	0.000	0.000	0.000
168	A	169	ASP	-1	-0.821	-0.882	29.486	-10.340	-10.340	0.000	0.000	0.000	0.000
169	A	170	GLN	0	-0.010	0.014	28.935	0.123	0.123	0.000	0.000	0.000	0.000
170	A	171	LEU	0	-0.008	0.002	26.120	-0.464	-0.464	0.000	0.000	0.000	0.000
171	A	172	VAL	0	0.024	0.013	20.948	0.158	0.158	0.000	0.000	0.000	0.000
172	A	173	THR	0	-0.010	-0.003	21.054	-0.256	-0.256	0.000	0.000	0.000	0.000
173	A	174	SER	0	0.049	-0.008	17.193	0.260	0.260	0.000	0.000	0.000	0.000
174	A	175	ARG	1	0.780	0.868	18.234	15.796	15.796	0.000	0.000	0.000	0.000
175	A	176	THR	0	-0.038	-0.041	13.593	-0.353	-0.353	0.000	0.000	0.000	0.000
176	A	177	PRO	0	0.044	0.007	8.827	0.747	0.747	0.000	0.000	0.000	0.000
177	A	178	ASP	-1	-0.907	-0.945	10.975	-27.250	-27.250	0.000	0.000	0.000	0.000
178	A	179	ASP	-1	-0.746	-0.849	12.486	-17.321	-17.321	0.000	0.000	0.000	0.000
179	A	180	LEU	0	-0.019	-0.008	9.459	1.022	1.022	0.000	0.000	0.000	0.000
180	A	181	PRO	0	-0.020	-0.010	12.586	0.910	0.910	0.000	0.000	0.000	0.000
181	A	182	ALA	0	0.002	0.014	15.114	1.098	1.098	0.000	0.000	0.000	0.000
182	A	183	PHE	0	0.004	-0.012	15.223	0.786	0.786	0.000	0.000	0.000	0.000
183	A	184	ASN	0	0.021	-0.010	12.581	1.145	1.145	0.000	0.000	0.000	0.000
184	A	185	ARG	1	0.835	0.929	17.014	15.188	15.188	0.000	0.000	0.000	0.000
185	A	186	GLU	-1	-0.793	-0.894	20.093	-12.308	-12.308	0.000	0.000	0.000	0.000
186	A	187	ALA	0	-0.004	-0.002	19.100	0.588	0.588	0.000	0.000	0.000	0.000
187	A	188	LEU	0	-0.027	-0.024	18.535	0.500	0.500	0.000	0.000	0.000	0.000
188	A	189	ARG	1	0.795	0.887	21.858	12.130	12.130	0.000	0.000	0.000	0.000
189	A	190	LEU	0	-0.052	-0.025	24.640	0.517	0.517	0.000	0.000	0.000	0.000
190	A	191	LEU	0	-0.056	-0.017	21.536	0.262	0.262	0.000	0.000	0.000	0.000
191	A	192	GLY	-1	-0.881	-0.912	25.572	-10.745	-10.745	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

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