FMO DATABASE

FMODB ID: QN5JY

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

Total energy (hartree)

FMO2-HF: Electronic energy	-712836.602662
FMO2-HF: Nuclear repulsion	675054.305762
FMO2-HF: Total energy	-37782.296899
FMO2-MP2: Total energy	-37893.740729

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.
-4.739	-1.022	0.711	-1.993	-2.434	0.002

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 : 0.129 / 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].	q(I=>J)Charge transfer value from I to J fragmens [e].
4	A	30	GLY	0	0.036	0.024	3.841	-2.908	-1.686	-0.004	-0.755	-0.462	0.004
5	A	31	ASN	0	0.135	0.038	6.479	0.385	0.385	0.000	0.000	0.000	0.000
6	A	31	ASN	0	-0.106	0.088	10.499	0.126	0.126	0.000	0.000	0.000	0.000
7	A	32	TYR	0	0.077	-0.100	8.080	-0.351	-0.351	0.000	0.000	0.000	0.000
8	A	32	TYR	0	-0.132	0.064	2.561	-0.228	0.949	0.196	-0.565	-0.808	-0.004
9	A	33	PHE	0	0.173	-0.062	9.025	0.155	0.155	0.000	0.000	0.000	0.000
10	A	33	PHE	0	-0.099	0.089	12.779	0.021	0.021	0.000	0.000	0.000	0.000
11	A	34	VAL	0	-0.016	-0.150	11.782	0.007	0.007	0.000	0.000	0.000	0.000
12	A	34	VAL	0	-0.060	0.123	10.660	0.014	0.014	0.000	0.000	0.000	0.000
13	A	35	ASN	0	0.162	-0.059	13.257	0.001	0.001	0.000	0.000	0.000	0.000
14	A	35	ASN	0	-0.151	0.046	16.527	-0.007	-0.007	0.000	0.000	0.000	0.000
15	A	36	VAL	0	0.118	-0.094	15.821	0.028	0.028	0.000	0.000	0.000	0.000
16	A	36	VAL	0	-0.073	0.124	15.711	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	37	PHE	0	0.055	-0.115	17.587	-0.001	-0.001	0.000	0.000	0.000	0.000
18	A	37	PHE	0	-0.107	0.079	17.948	0.007	0.007	0.000	0.000	0.000	0.000
19	A	38	VAL	0	0.139	-0.077	19.405	0.007	0.007	0.000	0.000	0.000	0.000
20	A	38	VAL	0	-0.058	0.125	21.182	-0.002	-0.002	0.000	0.000	0.000	0.000
21	A	39	ASN	0	0.102	-0.056	22.155	0.001	0.001	0.000	0.000	0.000	0.000
22	A	39	ASN	0	-0.119	0.059	24.373	0.004	0.004	0.000	0.000	0.000	0.000
23	A	40	GLY	0	0.016	-0.112	22.724	0.002	0.002	0.000	0.000	0.000	0.000
24	A	41	ARG	0	0.045	-0.025	23.955	0.002	0.002	0.000	0.000	0.000	0.000
25	A	41	ARG	1	0.870	1.081	25.586	0.015	0.015	0.000	0.000	0.000	0.000
26	A	42	LYS	0	0.129	-0.079	21.748	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	42	LYS	1	0.842	1.064	20.441	0.177	0.177	0.000	0.000	0.000	0.000
28	A	43	VAL	0	-0.066	-0.123	21.777	0.005	0.005	0.000	0.000	0.000	0.000
29	A	43	VAL	0	-0.025	0.103	21.385	0.000	0.000	0.000	0.000	0.000	0.000
30	A	44	ASP	0	0.003	-0.136	20.865	0.004	0.004	0.000	0.000	0.000	0.000
31	A	44	ASP	-1	-0.844	-0.799	19.883	-0.289	-0.289	0.000	0.000	0.000	0.000
32	A	45	SER	0	0.004	-0.126	17.825	0.016	0.016	0.000	0.000	0.000	0.000
33	A	45	SER	0	-0.089	0.028	18.400	0.014	0.014	0.000	0.000	0.000	0.000
34	A	46	GLY	0	-0.022	-0.050	16.342	0.026	0.026	0.000	0.000	0.000	0.000
35	A	47	ASN	0	0.122	0.056	13.180	0.000	0.000	0.000	0.000	0.000	0.000
36	A	47	ASN	0	-0.083	0.061	13.266	-0.081	-0.081	0.000	0.000	0.000	0.000
37	A	48	ILE	0	-0.005	-0.113	11.996	0.090	0.090	0.000	0.000	0.000	0.000
38	A	48	ILE	0	-0.052	0.100	11.432	0.029	0.029	0.000	0.000	0.000	0.000
39	A	49	ASP	0	0.108	-0.106	10.046	-0.246	-0.246	0.000	0.000	0.000	0.000
40	A	49	ASP	-1	-0.987	-0.854	10.321	-1.387	-1.387	0.000	0.000	0.000	0.000
41	A	50	PHE	0	0.066	-0.090	7.098	0.391	0.391	0.000	0.000	0.000	0.000
42	A	50	PHE	0	-0.110	0.080	6.372	0.090	0.090	0.000	0.000	0.000	0.000
43	A	51	ARG	0	0.093	-0.090	7.103	-0.708	-0.708	0.000	0.000	0.000	0.000
44	A	51	ARG	1	0.873	1.083	9.161	0.319	0.319	0.000	0.000	0.000	0.000
45	A	52	LEU	0	0.153	-0.109	7.221	0.092	0.092	0.000	0.000	0.000	0.000
46	A	52	LEU	0	-0.137	0.099	4.716	0.010	0.070	-0.001	-0.004	-0.055	0.000
47	A	53	GLU	0	0.063	-0.116	7.763	-0.134	-0.134	0.000	0.000	0.000	0.000
48	A	53	GLU	-1	-1.014	-0.842	11.007	-0.060	-0.060	0.000	0.000	0.000	0.000
49	A	54	LYS	0	0.194	-0.058	11.307	0.152	0.152	0.000	0.000	0.000	0.000
50	A	54	LYS	1	0.815	1.057	13.092	-0.608	-0.608	0.000	0.000	0.000	0.000
51	A	55	HIS	0	0.070	-0.106	13.514	-0.088	-0.088	0.000	0.000	0.000	0.000
52	A	55	HIS	0	-0.065	0.118	14.475	0.022	0.022	0.000	0.000	0.000	0.000
53	A	56	ASN	0	0.070	-0.096	15.970	0.055	0.055	0.000	0.000	0.000	0.000
54	A	56	ASN	0	-0.113	0.078	18.807	-0.016	-0.016	0.000	0.000	0.000	0.000
55	A	57	GLY	0	0.026	-0.117	17.021	0.014	0.014	0.000	0.000	0.000	0.000
56	A	58	LYS	0	0.032	-0.002	13.803	0.057	0.057	0.000	0.000	0.000	0.000
57	A	58	LYS	1	0.899	1.077	13.418	-0.570	-0.570	0.000	0.000	0.000	0.000
58	A	59	GLU	0	0.114	-0.108	9.738	-0.211	-0.211	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.960	-0.825	8.523	0.855	0.855	0.000	0.000	0.000	0.000
60	A	60	LEU	0	0.019	-0.131	7.835	0.321	0.321	0.000	0.000	0.000	0.000
61	A	60	LEU	0	-0.106	0.110	9.233	-0.033	-0.033	0.000	0.000	0.000	0.000
62	A	61	LEU	0	0.083	-0.102	5.517	-0.008	-0.008	0.000	0.000	0.000	0.000
63	A	61	LEU	0	-0.066	0.098	2.331	-0.798	0.062	0.500	-0.533	-0.827	0.003
64	A	62	TRP	0	0.102	-0.123	6.624	0.006	0.006	0.000	0.000	0.000	0.000
65	A	62	TRP	0	-0.054	0.151	10.614	0.032	0.032	0.000	0.000	0.000	0.000
66	A	63	PRO	0	-0.038	-0.112	9.896	-0.182	-0.182	0.000	0.000	0.000	0.000
67	A	64	CYS	0	0.158	-0.053	11.572	0.135	0.135	0.000	0.000	0.000	0.000
68	A	64	CYS	0	-0.297	0.249	13.605	-0.024	-0.024	0.000	0.000	0.000	0.000
69	A	65	LEU	0	0.029	-0.103	14.132	-0.071	-0.071	0.000	0.000	0.000	0.000
70	A	65	LEU	0	-0.078	0.082	15.100	0.010	0.010	0.000	0.000	0.000	0.000
71	A	66	SER	0	0.159	-0.039	17.166	0.032	0.032	0.000	0.000	0.000	0.000
72	A	66	SER	0	-0.057	0.085	20.286	0.012	0.012	0.000	0.000	0.000	0.000
73	A	67	SER	0	0.089	-0.069	20.559	0.010	0.010	0.000	0.000	0.000	0.000
74	A	67	SER	0	0.015	0.104	24.587	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	68	LEU	0	0.121	-0.094	23.823	0.023	0.023	0.000	0.000	0.000	0.000
76	A	68	LEU	0	-0.086	0.113	23.823	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	69	GLN	0	0.061	-0.127	20.264	0.020	0.020	0.000	0.000	0.000	0.000
78	A	69	GLN	0	-0.066	0.122	16.887	0.006	0.006	0.000	0.000	0.000	0.000
79	A	70	LEU	0	0.028	-0.109	21.739	0.003	0.003	0.000	0.000	0.000	0.000
80	A	70	LEU	0	-0.013	0.127	19.767	0.001	0.001	0.000	0.000	0.000	0.000
81	A	71	THR	0	0.120	-0.068	22.576	0.017	0.017	0.000	0.000	0.000	0.000
82	A	71	THR	0	-0.078	0.084	26.266	0.006	0.006	0.000	0.000	0.000	0.000
83	A	72	LYS	0	0.029	-0.112	24.259	0.023	0.023	0.000	0.000	0.000	0.000
84	A	72	LYS	1	0.814	1.049	21.949	0.264	0.264	0.000	0.000	0.000	0.000
85	A	73	TYR	0	-0.057	-0.155	22.137	0.008	0.008	0.000	0.000	0.000	0.000
86	A	73	TYR	0	-0.041	0.095	17.277	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	74	GLY	0	0.003	-0.111	23.520	0.016	0.016	0.000	0.000	0.000	0.000
88	A	75	ILE	0	0.080	0.034	24.884	0.017	0.017	0.000	0.000	0.000	0.000
89	A	75	ILE	0	-0.091	0.073	22.255	0.001	0.001	0.000	0.000	0.000	0.000
90	A	76	ASP	0	0.116	-0.147	26.295	-0.017	-0.017	0.000	0.000	0.000	0.000
91	A	76	ASP	-1	-0.965	-0.831	30.363	-0.053	-0.053	0.000	0.000	0.000	0.000
92	A	77	ILE	0	0.064	-0.100	27.185	0.015	0.015	0.000	0.000	0.000	0.000
93	A	77	ILE	0	-0.057	0.099	25.467	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	78	ASP	0	0.142	-0.140	27.928	0.002	0.002	0.000	0.000	0.000	0.000
95	A	78	ASP	-1	-1.024	-0.819	32.159	-0.074	-0.074	0.000	0.000	0.000	0.000
96	A	79	LYS	0	0.031	-0.125	30.905	0.004	0.004	0.000	0.000	0.000	0.000
97	A	79	LYS	1	0.806	1.073	30.822	0.032	0.032	0.000	0.000	0.000	0.000
98	A	80	TYR	0	-0.015	-0.114	27.762	0.010	0.010	0.000	0.000	0.000	0.000
99	A	80	TYR	0	-0.095	0.090	27.111	0.006	0.006	0.000	0.000	0.000	0.000
100	A	81	PRO	0	0.085	-0.085	27.712	-0.007	-0.007	0.000	0.000	0.000	0.000
101	A	82	ASP	0	0.084	-0.002	27.367	-0.014	-0.014	0.000	0.000	0.000	0.000
102	A	82	ASP	-1	-0.971	-0.838	26.711	-0.011	-0.011	0.000	0.000	0.000	0.000
103	A	83	LEU	0	0.062	-0.077	23.555	0.004	0.004	0.000	0.000	0.000	0.000
104	A	83	LEU	0	-0.116	0.060	22.277	-0.003	-0.003	0.000	0.000	0.000	0.000
105	A	84	ILE	0	0.107	-0.106	23.266	-0.013	-0.013	0.000	0.000	0.000	0.000
106	A	84	ILE	0	-0.043	0.102	24.731	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	85	LYS	0	0.028	-0.081	25.480	-0.009	-0.009	0.000	0.000	0.000	0.000
108	A	85	LYS	1	0.873	1.061	28.561	0.040	0.040	0.000	0.000	0.000	0.000
109	A	86	SER	0	-0.057	-0.097	24.687	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	86	SER	0	0.011	0.091	24.141	0.002	0.002	0.000	0.000	0.000	0.000
111	A	87	GLY	0	0.036	-0.097	21.670	0.009	0.009	0.000	0.000	0.000	0.000
112	A	88	THR	0	-0.019	0.020	21.661	0.010	0.010	0.000	0.000	0.000	0.000
113	A	88	THR	0	-0.032	0.053	20.714	-0.018	-0.018	0.000	0.000	0.000	0.000
114	A	89	GLU	0	0.106	-0.103	22.341	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	89	GLU	-1	-1.014	-0.838	25.278	-0.148	-0.148	0.000	0.000	0.000	0.000
116	A	90	GLN	0	0.021	-0.117	20.864	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	90	GLN	0	-0.040	0.098	20.021	0.006	0.006	0.000	0.000	0.000	0.000
118	A	91	CYS	0	0.029	-0.160	17.732	-0.048	-0.048	0.000	0.000	0.000	0.000
119	A	92	VAL	0	0.142	-0.025	18.589	0.019	0.019	0.000	0.000	0.000	0.000
120	A	92	VAL	0	-0.082	0.050	19.221	0.003	0.003	0.000	0.000	0.000	0.000
121	A	93	ASP	0	0.125	-0.146	18.510	-0.018	-0.018	0.000	0.000	0.000	0.000
122	A	93	ASP	-1	-0.947	-0.776	20.228	0.005	0.005	0.000	0.000	0.000	0.000
123	A	94	LEU	0	0.082	-0.113	18.034	0.011	0.011	0.000	0.000	0.000	0.000
124	A	94	LEU	0	-0.128	0.082	15.579	0.000	0.000	0.000	0.000	0.000	0.000
125	A	95	LEU	0	0.042	-0.099	19.367	0.004	0.004	0.000	0.000	0.000	0.000
126	A	95	LEU	0	-0.081	0.100	17.447	0.006	0.006	0.000	0.000	0.000	0.000
127	A	96	ALA	0	0.125	-0.092	20.539	0.019	0.019	0.000	0.000	0.000	0.000
128	A	96	ALA	0	-0.066	0.109	23.940	-0.004	-0.004	0.000	0.000	0.000	0.000
129	A	97	ILE	0	-0.002	-0.129	22.991	0.000	0.000	0.000	0.000	0.000	0.000
130	A	97	ILE	0	-0.087	0.089	22.156	-0.003	-0.003	0.000	0.000	0.000	0.000
131	A	98	PRO	0	-0.017	-0.071	23.745	0.015	0.015	0.000	0.000	0.000	0.000
132	A	99	HIS	0	0.082	0.034	25.121	-0.008	-0.008	0.000	0.000	0.000	0.000
133	A	99	HIS	0	-0.138	0.059	26.851	0.005	0.005	0.000	0.000	0.000	0.000
134	A	100	SER	0	0.057	-0.098	22.243	-0.003	-0.003	0.000	0.000	0.000	0.000
135	A	100	SER	0	-0.062	0.047	21.567	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	101	ASP	0	0.076	-0.117	18.799	0.013	0.013	0.000	0.000	0.000	0.000
137	A	101	ASP	-1	-1.022	-0.856	18.370	0.171	0.171	0.000	0.000	0.000	0.000
138	A	102	VAL	0	0.070	-0.137	15.411	-0.030	-0.030	0.000	0.000	0.000	0.000
139	A	102	VAL	0	-0.081	0.128	13.291	-0.011	-0.011	0.000	0.000	0.000	0.000
140	A	103	GLN	0	0.106	-0.137	12.858	0.052	0.052	0.000	0.000	0.000	0.000
141	A	103	GLN	0	-0.119	0.121	12.438	0.052	0.052	0.000	0.000	0.000	0.000
142	A	104	PHE	0	0.123	-0.088	9.217	-0.083	-0.083	0.000	0.000	0.000	0.000
143	A	104	PHE	0	-0.053	0.115	5.625	0.057	0.057	0.000	0.000	0.000	0.000
144	A	105	TYR	0	0.039	-0.091	9.689	0.199	0.199	0.000	0.000	0.000	0.000
145	A	105	TYR	0	-0.160	0.057	12.612	-0.009	-0.009	0.000	0.000	0.000	0.000
146	A	106	PHE	0	0.198	-0.097	7.004	-0.242	-0.242	0.000	0.000	0.000	0.000
147	A	106	PHE	0	-0.076	0.115	3.399	0.285	0.683	0.020	-0.136	-0.282	-0.001
148	A	107	ASN	0	0.110	-0.073	8.245	-0.196	-0.196	0.000	0.000	0.000	0.000
149	A	107	ASN	0	-0.093	0.061	9.628	0.115	0.115	0.000	0.000	0.000	0.000
150	A	108	GLN	0	0.011	-0.088	10.543	-0.069	-0.069	0.000	0.000	0.000	0.000
151	A	108	GLN	0	-0.079	0.074	13.758	-0.033	-0.033	0.000	0.000	0.000	0.000
152	A	109	GLN	0	0.072	-0.095	10.608	-0.016	-0.016	0.000	0.000	0.000	0.000
153	A	109	GLN	0	-0.125	0.111	10.074	0.058	0.058	0.000	0.000	0.000	0.000
154	A	110	LYS	0	0.174	-0.078	11.604	-0.069	-0.069	0.000	0.000	0.000	0.000
155	A	110	LYS	1	0.789	1.049	14.054	-0.023	-0.023	0.000	0.000	0.000	0.000
156	A	111	LEU	0	0.143	-0.096	12.458	0.081	0.081	0.000	0.000	0.000	0.000
157	A	111	LEU	0	-0.086	0.120	11.789	-0.015	-0.015	0.000	0.000	0.000	0.000
158	A	112	SER	0	0.036	-0.090	13.732	-0.033	-0.033	0.000	0.000	0.000	0.000
159	A	112	SER	0	-0.075	0.068	16.241	0.006	0.006	0.000	0.000	0.000	0.000
160	A	113	LEU	0	0.043	-0.105	16.336	0.036	0.036	0.000	0.000	0.000	0.000
161	A	113	LEU	0	-0.061	0.106	16.137	-0.007	-0.007	0.000	0.000	0.000	0.000
162	A	114	ILE	0	0.082	-0.144	18.738	-0.017	-0.017	0.000	0.000	0.000	0.000
163	A	114	ILE	0	-0.069	0.155	19.956	0.001	0.001	0.000	0.000	0.000	0.000
164	A	115	VAL	0	0.052	-0.072	21.688	0.013	0.013	0.000	0.000	0.000	0.000
165	A	115	VAL	0	-0.023	0.099	22.354	-0.003	-0.003	0.000	0.000	0.000	0.000
166	A	116	PRO	0	0.050	-0.067	24.378	-0.001	-0.001	0.000	0.000	0.000	0.000
167	A	117	PRO	0	0.017	-0.017	27.932	-0.011	-0.011	0.000	0.000	0.000	0.000
168	A	118	GLN	0	0.074	-0.004	30.542	-0.009	-0.009	0.000	0.000	0.000	0.000
169	A	118	GLN	0	-0.021	0.119	30.994	0.000	0.000	0.000	0.000	0.000	0.000
170	A	119	ALA	0	0.017	-0.102	27.418	-0.004	-0.004	0.000	0.000	0.000	0.000
171	A	119	ALA	0	-0.014	0.097	26.808	0.001	0.001	0.000	0.000	0.000	0.000
172	A	120	LEU	0	0.064	-0.085	28.236	-0.012	-0.012	0.000	0.000	0.000	0.000
173	A	120	LEU	0	-0.120	0.080	26.577	0.001	0.001	0.000	0.000	0.000	0.000
174	A	121	LEU	0	0.091	-0.112	29.429	0.007	0.007	0.000	0.000	0.000	0.000
175	A	121	LEU	0	-0.117	0.105	29.095	-0.001	-0.001	0.000	0.000	0.000	0.000
176	A	122	PRO	0	-0.018	-0.095	31.561	0.003	0.003	0.000	0.000	0.000	0.000
177	A	123	ARG	0	-0.049	-0.015	32.485	0.007	0.007	0.000	0.000	0.000	0.000
178	A	123	ARG	1	0.923	0.982	27.656	0.106	0.106	0.000	0.000	0.000	0.000

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