FMO DATABASE

FMODB ID: ZN91N

Calculation Name: 4B0E-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4B0E

Chain ID: A

ChEMBL ID:

UniProt ID: P26949

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	OptHSide
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	178
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-713388.327475
FMO2-HF: Nuclear repulsion	675604.509535
FMO2-HF: Total energy	-37783.81794
FMO2-MP2: Total energy	-37895.228959

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:28:LEU)

Summations of interaction energy for fragment #1(A:28:LEU)

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.
-7.505	-3.489	0.733	-2.087	-2.664	0.004

Interaction energy analysis for fragmet #1(A:28:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.141 / q_NPA : 0.006

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	30	GLY	0	0.023	0.020	3.841	-3.164	-2.444	-0.003	-0.425	-0.293	0.002
5	A	31	ASN	0	0.167	0.048	6.479	0.695	0.695	0.000	0.000	0.000	0.000
6	A	31	ASN	0	-0.117	0.078	10.309	0.043	0.043	0.000	0.000	0.000	0.000
7	A	32	TYR	0	0.043	-0.121	7.925	-0.502	-0.502	0.000	0.000	0.000	0.000
8	A	32	TYR	0	-0.113	0.073	2.437	-0.678	0.710	0.323	-0.727	-0.984	-0.006
9	A	33	PHE	0	0.163	-0.063	8.877	0.195	0.195	0.000	0.000	0.000	0.000
10	A	33	PHE	0	-0.107	0.089	12.619	0.012	0.012	0.000	0.000	0.000	0.000
11	A	34	VAL	0	-0.022	-0.134	11.654	-0.026	-0.026	0.000	0.000	0.000	0.000
12	A	34	VAL	0	-0.058	0.119	10.393	0.028	0.028	0.000	0.000	0.000	0.000
13	A	35	ASN	0	0.178	-0.053	13.086	-0.034	-0.034	0.000	0.000	0.000	0.000
14	A	35	ASN	0	-0.122	0.051	15.820	-0.019	-0.019	0.000	0.000	0.000	0.000
15	A	36	VAL	0	0.106	-0.101	15.661	0.075	0.075	0.000	0.000	0.000	0.000
16	A	36	VAL	0	-0.061	0.115	15.816	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	37	PHE	0	0.047	-0.099	17.520	-0.050	-0.050	0.000	0.000	0.000	0.000
18	A	37	PHE	0	-0.107	0.076	17.862	-0.002	-0.002	0.000	0.000	0.000	0.000
19	A	38	VAL	0	0.139	-0.087	19.662	0.048	0.048	0.000	0.000	0.000	0.000
20	A	38	VAL	0	-0.057	0.129	21.499	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	39	ASN	0	0.112	-0.062	22.442	-0.021	-0.021	0.000	0.000	0.000	0.000
22	A	39	ASN	0	-0.121	0.075	24.996	0.018	0.018	0.000	0.000	0.000	0.000
23	A	40	GLY	0	0.013	-0.119	23.029	-0.022	-0.022	0.000	0.000	0.000	0.000
24	A	41	ARG	0	0.047	-0.031	24.170	-0.010	-0.010	0.000	0.000	0.000	0.000
25	A	41	ARG	1	0.853	1.074	25.528	-0.137	-0.137	0.000	0.000	0.000	0.000
26	A	42	LYS	0	0.125	-0.076	21.651	0.023	0.023	0.000	0.000	0.000	0.000
27	A	42	LYS	1	0.764	1.028	20.012	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	43	VAL	0	-0.031	-0.130	21.683	-0.020	-0.020	0.000	0.000	0.000	0.000
29	A	43	VAL	0	-0.065	0.117	21.386	0.000	0.000	0.000	0.000	0.000	0.000
30	A	44	ASP	0	0.085	-0.123	20.582	-0.015	-0.015	0.000	0.000	0.000	0.000
31	A	44	ASP	-1	-0.829	-0.778	19.599	-0.044	-0.044	0.000	0.000	0.000	0.000
32	A	45	SER	0	-0.009	-0.089	17.635	0.040	0.040	0.000	0.000	0.000	0.000
33	A	45	SER	0	-0.065	0.081	18.409	0.008	0.008	0.000	0.000	0.000	0.000
34	A	46	GLY	0	0.000	-0.101	16.166	-0.016	-0.016	0.000	0.000	0.000	0.000
35	A	47	ASN	0	0.135	0.061	13.018	0.043	0.043	0.000	0.000	0.000	0.000
36	A	47	ASN	0	-0.112	0.059	13.506	0.054	0.054	0.000	0.000	0.000	0.000
37	A	48	ILE	0	0.029	-0.108	11.808	0.010	0.010	0.000	0.000	0.000	0.000
38	A	48	ILE	0	-0.072	0.101	11.776	0.026	0.026	0.000	0.000	0.000	0.000
39	A	49	ASP	0	0.101	-0.118	9.957	-0.152	-0.152	0.000	0.000	0.000	0.000
40	A	49	ASP	-1	-0.968	-0.836	9.958	-0.691	-0.691	0.000	0.000	0.000	0.000
41	A	50	PHE	0	0.053	-0.095	7.464	0.133	0.133	0.000	0.000	0.000	0.000
42	A	50	PHE	0	-0.100	0.080	6.597	0.176	0.176	0.000	0.000	0.000	0.000
43	A	51	ARG	0	0.093	-0.084	7.103	-0.455	-0.455	0.000	0.000	0.000	0.000
44	A	51	ARG	1	0.808	1.015	9.226	-0.549	-0.549	0.000	0.000	0.000	0.000
45	A	52	LEU	0	0.143	-0.087	7.213	0.370	0.370	0.000	0.000	0.000	0.000
46	A	52	LEU	0	-0.106	0.087	4.503	-0.053	0.013	-0.001	-0.007	-0.059	0.000
47	A	53	GLU	0	0.037	-0.124	7.779	-0.362	-0.362	0.000	0.000	0.000	0.000
48	A	53	GLU	-1	-0.922	-0.788	11.230	0.616	0.616	0.000	0.000	0.000	0.000
49	A	54	LYS	0	0.133	-0.072	11.376	0.249	0.249	0.000	0.000	0.000	0.000
50	A	54	LYS	1	0.761	1.014	12.937	-1.032	-1.032	0.000	0.000	0.000	0.000
51	A	55	HIS	0	0.083	-0.094	13.523	-0.151	-0.151	0.000	0.000	0.000	0.000
52	A	55	HIS	0	-0.066	0.115	14.786	-0.025	-0.025	0.000	0.000	0.000	0.000
53	A	56	ASN	0	0.097	-0.080	16.331	0.054	0.054	0.000	0.000	0.000	0.000
54	A	56	ASN	0	-0.119	0.072	19.472	-0.032	-0.032	0.000	0.000	0.000	0.000
55	A	57	GLY	0	0.031	-0.122	17.021	-0.005	-0.005	0.000	0.000	0.000	0.000
56	A	58	LYS	0	0.056	0.001	14.077	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	58	LYS	1	0.893	1.083	14.118	-0.815	-0.815	0.000	0.000	0.000	0.000
58	A	59	GLU	0	0.084	-0.109	9.770	-0.210	-0.210	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.928	-0.794	8.593	1.409	1.409	0.000	0.000	0.000	0.000
60	A	60	LEU	0	0.026	-0.107	8.742	0.317	0.317	0.000	0.000	0.000	0.000
61	A	60	LEU	0	-0.086	0.098	10.190	-0.067	-0.067	0.000	0.000	0.000	0.000
62	A	61	LEU	0	0.105	-0.089	6.443	-0.287	-0.287	0.000	0.000	0.000	0.000
63	A	61	LEU	0	-0.078	0.093	3.033	-2.394	-1.061	0.331	-0.752	-0.912	0.009
64	A	62	TRP	0	0.095	-0.141	7.594	-0.242	-0.242	0.000	0.000	0.000	0.000
65	A	62	TRP	0	-0.046	0.147	11.416	0.026	0.026	0.000	0.000	0.000	0.000
66	A	63	PRO	0	-0.041	-0.109	10.545	-0.111	-0.111	0.000	0.000	0.000	0.000
67	A	64	CYS	0	0.120	-0.018	12.111	0.051	0.051	0.000	0.000	0.000	0.000
68	A	64	CYS	0	-0.260	0.169	13.663	-0.033	-0.033	0.000	0.000	0.000	0.000
69	A	65	LEU	0	0.028	-0.110	14.487	-0.084	-0.084	0.000	0.000	0.000	0.000
70	A	65	LEU	0	-0.078	0.085	15.274	0.001	0.001	0.000	0.000	0.000	0.000
71	A	66	SER	0	0.159	-0.038	17.509	0.029	0.029	0.000	0.000	0.000	0.000
72	A	66	SER	0	-0.062	0.054	20.332	-0.008	-0.008	0.000	0.000	0.000	0.000
73	A	67	SER	0	0.078	-0.098	20.838	0.022	0.022	0.000	0.000	0.000	0.000
74	A	67	SER	0	-0.029	0.065	25.175	-0.005	-0.005	0.000	0.000	0.000	0.000
75	A	68	LEU	0	0.111	-0.071	24.176	0.012	0.012	0.000	0.000	0.000	0.000
76	A	68	LEU	0	-0.080	0.115	23.945	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	69	GLN	0	0.083	-0.128	20.347	-0.006	-0.006	0.000	0.000	0.000	0.000
78	A	69	GLN	0	-0.047	0.141	16.584	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	70	LEU	0	0.017	-0.112	21.828	0.003	0.003	0.000	0.000	0.000	0.000
80	A	70	LEU	0	-0.023	0.133	20.215	0.004	0.004	0.000	0.000	0.000	0.000
81	A	71	THR	0	0.065	-0.075	22.874	0.012	0.012	0.000	0.000	0.000	0.000
82	A	71	THR	0	-0.043	0.081	26.604	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	72	LYS	0	0.062	-0.087	24.245	0.004	0.004	0.000	0.000	0.000	0.000
84	A	72	LYS	1	0.772	1.011	21.512	0.045	0.045	0.000	0.000	0.000	0.000
85	A	73	TYR	0	-0.038	-0.148	22.327	-0.015	-0.015	0.000	0.000	0.000	0.000
86	A	73	TYR	0	-0.041	0.097	18.122	0.008	0.008	0.000	0.000	0.000	0.000
87	A	74	GLY	0	-0.005	-0.107	23.634	0.013	0.013	0.000	0.000	0.000	0.000
88	A	75	ILE	0	0.098	0.022	25.347	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	75	ILE	0	-0.109	0.083	22.551	0.006	0.006	0.000	0.000	0.000	0.000
90	A	76	ASP	0	0.132	-0.116	26.706	-0.012	-0.012	0.000	0.000	0.000	0.000
91	A	76	ASP	-1	-0.941	-0.804	30.892	0.094	0.094	0.000	0.000	0.000	0.000
92	A	77	ILE	0	0.070	-0.122	27.767	0.013	0.013	0.000	0.000	0.000	0.000
93	A	77	ILE	0	-0.073	0.098	25.903	0.002	0.002	0.000	0.000	0.000	0.000
94	A	78	ASP	0	0.127	-0.109	28.475	0.011	0.011	0.000	0.000	0.000	0.000
95	A	78	ASP	-1	-1.005	-0.830	32.335	0.070	0.070	0.000	0.000	0.000	0.000
96	A	79	LYS	0	0.035	-0.114	31.533	-0.004	-0.004	0.000	0.000	0.000	0.000
97	A	79	LYS	1	0.755	0.999	31.441	-0.102	-0.102	0.000	0.000	0.000	0.000
98	A	80	TYR	0	-0.030	-0.091	28.571	0.001	0.001	0.000	0.000	0.000	0.000
99	A	80	TYR	0	-0.084	0.083	27.833	0.008	0.008	0.000	0.000	0.000	0.000
100	A	81	PRO	0	0.128	-0.074	28.476	0.006	0.006	0.000	0.000	0.000	0.000
101	A	82	ASP	0	0.097	0.005	27.962	-0.011	-0.011	0.000	0.000	0.000	0.000
102	A	82	ASP	-1	-0.941	-0.802	27.485	0.162	0.162	0.000	0.000	0.000	0.000
103	A	83	LEU	0	0.084	-0.100	24.267	0.018	0.018	0.000	0.000	0.000	0.000
104	A	83	LEU	0	-0.122	0.066	23.120	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	84	ILE	0	0.086	-0.081	23.793	0.016	0.016	0.000	0.000	0.000	0.000
106	A	84	ILE	0	-0.079	0.091	25.227	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	85	LYS	0	0.085	-0.056	25.694	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	85	LYS	1	0.797	0.999	29.108	-0.129	-0.129	0.000	0.000	0.000	0.000
109	A	86	SER	0	-0.071	-0.117	24.917	-0.014	-0.014	0.000	0.000	0.000	0.000
110	A	86	SER	0	0.023	0.085	24.275	-0.005	-0.005	0.000	0.000	0.000	0.000
111	A	87	GLY	0	0.017	-0.091	21.744	0.036	0.036	0.000	0.000	0.000	0.000
112	A	88	THR	0	-0.043	0.006	21.866	-0.015	-0.015	0.000	0.000	0.000	0.000
113	A	88	THR	0	-0.029	0.060	20.765	-0.016	-0.016	0.000	0.000	0.000	0.000
114	A	89	GLU	0	0.135	-0.093	22.573	0.021	0.021	0.000	0.000	0.000	0.000
115	A	89	GLU	-1	-0.922	-0.796	25.374	0.036	0.036	0.000	0.000	0.000	0.000
116	A	90	GLN	0	0.011	-0.121	20.831	0.001	0.001	0.000	0.000	0.000	0.000
117	A	90	GLN	0	-0.042	0.100	19.948	0.013	0.013	0.000	0.000	0.000	0.000
118	A	91	CYS	0	-0.001	-0.104	17.650	-0.027	-0.027	0.000	0.000	0.000	0.000
119	A	92	VAL	0	0.164	-0.033	18.772	0.014	0.014	0.000	0.000	0.000	0.000
120	A	92	VAL	0	-0.092	0.070	19.917	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	93	ASP	0	0.080	-0.140	19.101	0.045	0.045	0.000	0.000	0.000	0.000
122	A	93	ASP	-1	-0.917	-0.797	20.611	0.356	0.356	0.000	0.000	0.000	0.000
123	A	94	LEU	0	0.055	-0.093	18.861	-0.040	-0.040	0.000	0.000	0.000	0.000
124	A	94	LEU	0	-0.098	0.071	16.255	0.006	0.006	0.000	0.000	0.000	0.000
125	A	95	LEU	0	0.031	-0.112	20.248	-0.010	-0.010	0.000	0.000	0.000	0.000
126	A	95	LEU	0	-0.056	0.101	18.347	0.009	0.009	0.000	0.000	0.000	0.000
127	A	96	ALA	0	0.113	-0.076	21.483	-0.003	-0.003	0.000	0.000	0.000	0.000
128	A	96	ALA	0	-0.079	0.103	24.580	-0.007	-0.007	0.000	0.000	0.000	0.000
129	A	97	ILE	0	0.023	-0.131	23.933	-0.031	-0.031	0.000	0.000	0.000	0.000
130	A	97	ILE	0	-0.114	0.091	23.267	-0.005	-0.005	0.000	0.000	0.000	0.000
131	A	98	PRO	0	-0.018	-0.086	24.727	0.029	0.029	0.000	0.000	0.000	0.000
132	A	99	HIS	0	0.059	0.042	26.116	-0.006	-0.006	0.000	0.000	0.000	0.000
133	A	99	HIS	0	-0.133	0.054	27.858	0.008	0.008	0.000	0.000	0.000	0.000
134	A	100	SER	0	0.058	-0.089	23.100	-0.023	-0.023	0.000	0.000	0.000	0.000
135	A	100	SER	0	-0.035	0.045	22.436	0.010	0.010	0.000	0.000	0.000	0.000
136	A	101	ASP	0	0.072	-0.109	19.755	0.017	0.017	0.000	0.000	0.000	0.000
137	A	101	ASP	-1	-1.015	-0.865	19.232	0.498	0.498	0.000	0.000	0.000	0.000
138	A	102	VAL	0	0.079	-0.126	16.292	-0.069	-0.069	0.000	0.000	0.000	0.000
139	A	102	VAL	0	-0.092	0.117	14.195	-0.002	-0.002	0.000	0.000	0.000	0.000
140	A	103	GLN	0	0.090	-0.109	13.673	0.120	0.120	0.000	0.000	0.000	0.000
141	A	103	GLN	0	-0.106	0.093	13.379	0.122	0.122	0.000	0.000	0.000	0.000
142	A	104	PHE	0	0.132	-0.079	9.755	-0.268	-0.268	0.000	0.000	0.000	0.000
143	A	104	PHE	0	-0.064	0.104	5.613	0.050	0.050	0.000	0.000	0.000	0.000
144	A	105	TYR	0	0.056	-0.083	10.218	0.329	0.329	0.000	0.000	0.000	0.000
145	A	105	TYR	0	-0.163	0.060	12.799	-0.023	-0.023	0.000	0.000	0.000	0.000
146	A	106	PHE	0	0.213	-0.094	6.971	-0.403	-0.403	0.000	0.000	0.000	0.000
147	A	106	PHE	0	-0.099	0.115	2.893	0.116	0.625	0.083	-0.176	-0.416	-0.001
148	A	107	ASN	0	0.095	-0.073	8.123	-0.324	-0.324	0.000	0.000	0.000	0.000
149	A	107	ASN	0	-0.096	0.056	9.474	0.154	0.154	0.000	0.000	0.000	0.000
150	A	108	GLN	0	0.034	-0.089	10.506	-0.151	-0.151	0.000	0.000	0.000	0.000
151	A	108	GLN	0	-0.076	0.067	13.612	-0.012	-0.012	0.000	0.000	0.000	0.000
152	A	109	GLN	0	0.073	-0.090	10.481	-0.023	-0.023	0.000	0.000	0.000	0.000
153	A	109	GLN	0	-0.131	0.093	9.776	-0.059	-0.059	0.000	0.000	0.000	0.000
154	A	110	LYS	0	0.164	-0.069	11.480	-0.114	-0.114	0.000	0.000	0.000	0.000
155	A	110	LYS	1	0.797	1.046	14.089	-0.299	-0.299	0.000	0.000	0.000	0.000
156	A	111	LEU	0	0.123	-0.097	12.560	0.175	0.175	0.000	0.000	0.000	0.000
157	A	111	LEU	0	-0.090	0.121	12.451	-0.011	-0.011	0.000	0.000	0.000	0.000
158	A	112	SER	0	0.034	-0.081	13.899	-0.108	-0.108	0.000	0.000	0.000	0.000
159	A	112	SER	0	-0.072	0.048	16.830	-0.016	-0.016	0.000	0.000	0.000	0.000
160	A	113	LEU	0	0.042	-0.087	16.888	0.094	0.094	0.000	0.000	0.000	0.000
161	A	113	LEU	0	-0.056	0.095	16.642	-0.009	-0.009	0.000	0.000	0.000	0.000
162	A	114	ILE	0	0.057	-0.118	19.266	-0.050	-0.050	0.000	0.000	0.000	0.000
163	A	114	ILE	0	-0.066	0.123	20.458	-0.002	-0.002	0.000	0.000	0.000	0.000
164	A	115	VAL	0	0.093	-0.083	22.328	0.032	0.032	0.000	0.000	0.000	0.000
165	A	115	VAL	0	-0.036	0.115	22.866	-0.003	-0.003	0.000	0.000	0.000	0.000
166	A	116	PRO	0	0.057	-0.065	25.072	-0.016	-0.016	0.000	0.000	0.000	0.000
167	A	117	PRO	0	0.025	-0.010	28.665	-0.007	-0.007	0.000	0.000	0.000	0.000
168	A	118	GLN	0	0.078	0.012	31.148	-0.010	-0.010	0.000	0.000	0.000	0.000
169	A	118	GLN	0	-0.024	0.111	31.813	-0.002	-0.002	0.000	0.000	0.000	0.000
170	A	119	ALA	0	0.023	-0.123	28.120	-0.015	-0.015	0.000	0.000	0.000	0.000
171	A	119	ALA	0	-0.028	0.112	27.473	0.005	0.005	0.000	0.000	0.000	0.000
172	A	120	LEU	0	0.067	-0.093	28.771	0.001	0.001	0.000	0.000	0.000	0.000
173	A	120	LEU	0	-0.105	0.084	26.970	0.002	0.002	0.000	0.000	0.000	0.000
174	A	121	LEU	0	0.078	-0.102	29.884	-0.002	-0.002	0.000	0.000	0.000	0.000
175	A	121	LEU	0	-0.131	0.098	29.155	-0.004	-0.004	0.000	0.000	0.000	0.000
176	A	122	PRO	0	-0.012	-0.108	31.908	0.001	0.001	0.000	0.000	0.000	0.000
177	A	123	ARG	0	-0.027	-0.006	32.579	0.000	0.000	0.000	0.000	0.000	0.000
178	A	123	ARG	1	0.873	0.954	27.489	-0.054	-0.054	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:28:LEU)