FMO DATABASE

FMODB ID: 9MQN2

Calculation Name: 3D33-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3D33

Chain ID: A

ChEMBL ID:

UniProt ID: A6KX32

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	175
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-666573.92369
FMO2-HF: Nuclear repulsion	629601.000213
FMO2-HF: Total energy	-36972.923477
FMO2-MP2: Total energy	-37079.94669

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:34:PRO)

Summations of interaction energy for fragment #1(A:34:PRO)

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.
-6.413	-3.068	0.127	-1.743	-1.731	-0.003

Interaction energy analysis for fragmet #1(A:34:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.026 / q_NPA : -0.035

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	35	VAL	0	-0.066	0.109	3.977	-0.054	0.491	0.003	-0.185	-0.364	0.000
4	A	36	LYS	0	0.112	-0.082	3.041	-4.091	-1.291	0.124	-1.558	-1.367	-0.003
5	A	36	LYS	1	0.782	1.023	6.418	1.768	1.768	0.000	0.000	0.000	0.000
6	A	37	ASP	0	0.073	-0.131	5.745	0.488	0.488	0.000	0.000	0.000	0.000
7	A	37	ASP	-1	-0.947	-0.813	7.047	-1.208	-1.208	0.000	0.000	0.000	0.000
8	A	38	VAL	0	-0.001	-0.124	7.792	-0.059	-0.059	0.000	0.000	0.000	0.000
9	A	38	VAL	0	-0.135	0.068	10.671	0.008	0.008	0.000	0.000	0.000	0.000
10	A	39	GLU	0	0.196	-0.094	11.459	0.080	0.080	0.000	0.000	0.000	0.000
11	A	39	GLU	-1	-1.035	-0.827	12.601	-0.662	-0.662	0.000	0.000	0.000	0.000
12	A	40	LEU	0	-0.011	-0.138	13.379	0.018	0.018	0.000	0.000	0.000	0.000
13	A	40	LEU	0	-0.103	0.076	15.000	0.015	0.015	0.000	0.000	0.000	0.000
14	A	41	ASP	0	0.114	-0.117	16.690	0.011	0.011	0.000	0.000	0.000	0.000
15	A	41	ASP	-1	-0.993	-0.821	19.327	-0.403	-0.403	0.000	0.000	0.000	0.000
16	A	42	GLY	0	-0.025	-0.112	20.012	0.007	0.007	0.000	0.000	0.000	0.000
17	A	43	ARG	0	0.098	0.004	23.314	0.005	0.005	0.000	0.000	0.000	0.000
18	A	43	ARG	1	0.685	0.956	26.754	0.157	0.157	0.000	0.000	0.000	0.000
19	A	44	TRP	0	0.111	-0.110	23.553	0.001	0.001	0.000	0.000	0.000	0.000
20	A	44	TRP	0	-0.066	0.121	23.012	-0.014	-0.014	0.000	0.000	0.000	0.000
21	A	45	ASP	0	0.063	-0.102	24.960	-0.002	-0.002	0.000	0.000	0.000	0.000
22	A	45	ASP	-1	-0.898	-0.801	29.006	-0.152	-0.152	0.000	0.000	0.000	0.000
23	A	46	ASP	0	-0.112	-0.154	27.407	-0.009	-0.009	0.000	0.000	0.000	0.000
24	A	46	ASP	-1	-0.814	-0.870	29.749	-0.106	-0.106	0.000	0.000	0.000	0.000
25	A	54	ASN	0	0.138	0.044	18.801	0.001	0.001	0.000	0.000	0.000	0.000
26	A	54	ASN	0	-0.138	0.027	15.983	-0.017	-0.017	0.000	0.000	0.000	0.000
27	A	55	CYS	0	0.102	-0.101	18.851	0.032	0.032	0.000	0.000	0.000	0.000
28	A	55	CYS	0	-0.099	0.128	17.864	0.005	0.005	0.000	0.000	0.000	0.000
29	A	56	PRO	0	-0.020	-0.104	17.679	-0.020	-0.020	0.000	0.000	0.000	0.000
30	A	57	ILE	0	0.036	-0.030	17.533	0.011	0.011	0.000	0.000	0.000	0.000
31	A	57	ILE	0	-0.012	0.139	17.087	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	58	THR	0	0.045	-0.061	12.857	-0.006	-0.006	0.000	0.000	0.000	0.000
33	A	58	THR	0	-0.032	0.071	11.815	-0.008	-0.008	0.000	0.000	0.000	0.000
34	A	59	VAL	0	0.108	-0.102	12.276	0.079	0.079	0.000	0.000	0.000	0.000
35	A	59	VAL	0	-0.080	0.117	12.496	0.006	0.006	0.000	0.000	0.000	0.000
36	A	60	PHE	0	0.050	-0.070	8.060	-0.047	-0.047	0.000	0.000	0.000	0.000
37	A	60	PHE	0	-0.080	0.083	7.157	0.079	0.079	0.000	0.000	0.000	0.000
38	A	61	THR	0	-0.001	-0.103	8.345	0.357	0.357	0.000	0.000	0.000	0.000
39	A	61	THR	0	-0.006	0.080	8.826	0.088	0.088	0.000	0.000	0.000	0.000
40	A	62	ASP	0	0.095	-0.123	6.878	-1.118	-1.118	0.000	0.000	0.000	0.000
41	A	62	ASP	-1	-0.996	-0.822	6.237	-1.054	-1.054	0.000	0.000	0.000	0.000
42	A	63	GLY	0	0.018	-0.102	7.468	0.540	0.540	0.000	0.000	0.000	0.000
43	A	64	TYR	0	-0.025	-0.012	9.475	-0.180	-0.180	0.000	0.000	0.000	0.000
44	A	64	TYR	0	-0.108	0.049	13.373	0.041	0.041	0.000	0.000	0.000	0.000
45	A	65	LEU	0	0.193	-0.101	11.783	0.130	0.130	0.000	0.000	0.000	0.000
46	A	65	LEU	0	-0.110	0.117	11.787	0.027	0.027	0.000	0.000	0.000	0.000
47	A	66	LEU	0	0.130	-0.083	11.333	-0.239	-0.239	0.000	0.000	0.000	0.000
48	A	66	LEU	0	-0.103	0.096	13.655	0.015	0.015	0.000	0.000	0.000	0.000
49	A	67	THR	0	-0.007	-0.119	12.117	0.143	0.143	0.000	0.000	0.000	0.000
50	A	67	THR	0	-0.047	0.074	11.381	0.069	0.069	0.000	0.000	0.000	0.000
51	A	68	LEU	0	0.115	-0.071	12.712	-0.130	-0.130	0.000	0.000	0.000	0.000
52	A	68	LEU	0	-0.069	0.103	16.372	0.006	0.006	0.000	0.000	0.000	0.000
53	A	69	LYS	0	0.069	-0.087	14.783	0.056	0.056	0.000	0.000	0.000	0.000
54	A	69	LYS	1	0.847	1.048	11.737	0.215	0.215	0.000	0.000	0.000	0.000
55	A	70	ASN	0	0.162	-0.087	15.877	-0.041	-0.041	0.000	0.000	0.000	0.000
56	A	70	ASN	0	-0.081	0.100	19.895	0.005	0.005	0.000	0.000	0.000	0.000
57	A	71	ALA	0	0.093	-0.094	18.594	0.026	0.026	0.000	0.000	0.000	0.000
58	A	71	ALA	0	-0.105	0.081	17.530	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	72	SER	0	-0.083	-0.113	19.296	0.029	0.029	0.000	0.000	0.000	0.000
60	A	72	SER	0	-0.013	0.068	22.481	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	73	PRO	0	-0.051	-0.133	22.276	-0.005	-0.005	0.000	0.000	0.000	0.000
62	A	74	ASP	0	0.079	0.012	24.634	0.015	0.015	0.000	0.000	0.000	0.000
63	A	74	ASP	-1	-0.840	-0.762	26.370	-0.154	-0.154	0.000	0.000	0.000	0.000
64	A	75	ARG	0	0.108	-0.059	27.352	0.009	0.009	0.000	0.000	0.000	0.000
65	A	75	ARG	1	0.604	0.905	26.674	0.157	0.157	0.000	0.000	0.000	0.000
66	A	76	ASP	0	0.148	-0.094	27.381	-0.011	-0.011	0.000	0.000	0.000	0.000
67	A	76	ASP	-1	-0.958	-0.825	30.367	-0.118	-0.118	0.000	0.000	0.000	0.000
68	A	77	MET	0	0.018	-0.108	25.023	0.001	0.001	0.000	0.000	0.000	0.000
69	A	77	MET	0	-0.086	0.087	21.275	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	78	THR	0	0.036	-0.099	25.986	0.011	0.011	0.000	0.000	0.000	0.000
71	A	78	THR	0	-0.081	0.053	26.978	0.003	0.003	0.000	0.000	0.000	0.000
72	A	79	ILE	0	0.080	-0.064	22.255	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	79	ILE	0	-0.082	0.083	19.782	-0.007	-0.007	0.000	0.000	0.000	0.000
74	A	80	ARG	0	0.122	-0.089	23.222	0.017	0.017	0.000	0.000	0.000	0.000
75	A	80	ARG	1	0.749	1.014	25.326	0.217	0.217	0.000	0.000	0.000	0.000
76	A	81	ILE	0	0.066	-0.103	21.694	-0.022	-0.022	0.000	0.000	0.000	0.000
77	A	81	ILE	0	-0.105	0.087	19.086	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	82	THR	0	0.009	-0.097	22.657	0.027	0.027	0.000	0.000	0.000	0.000
79	A	82	THR	0	-0.030	0.060	24.965	0.011	0.011	0.000	0.000	0.000	0.000
80	A	83	ASP	0	0.061	-0.051	23.412	-0.040	-0.040	0.000	0.000	0.000	0.000
81	A	83	ASP	-1	-0.849	-0.816	24.556	-0.261	-0.261	0.000	0.000	0.000	0.000
82	A	84	MET	0	0.094	-0.123	23.759	0.033	0.033	0.000	0.000	0.000	0.000
83	A	84	MET	0	-0.089	0.123	22.165	0.006	0.006	0.000	0.000	0.000	0.000
84	A	85	ALA	0	0.093	-0.093	25.208	0.012	0.012	0.000	0.000	0.000	0.000
85	A	85	ALA	0	-0.112	0.106	26.322	0.002	0.002	0.000	0.000	0.000	0.000
86	A	86	LYS	0	-0.055	-0.170	27.575	0.018	0.018	0.000	0.000	0.000	0.000
87	A	86	LYS	1	0.854	1.046	29.792	0.189	0.189	0.000	0.000	0.000	0.000
88	A	87	GLY	0	-0.006	-0.082	28.345	0.016	0.016	0.000	0.000	0.000	0.000
89	A	88	GLY	0	-0.036	-0.024	28.838	0.014	0.014	0.000	0.000	0.000	0.000
90	A	89	VAL	0	0.107	-0.018	26.986	-0.027	-0.027	0.000	0.000	0.000	0.000
91	A	89	VAL	0	-0.090	0.119	26.864	0.002	0.002	0.000	0.000	0.000	0.000
92	A	90	VAL	0	-0.008	-0.125	24.915	0.025	0.025	0.000	0.000	0.000	0.000
93	A	90	VAL	0	-0.084	0.104	22.862	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	91	TYR	0	0.111	-0.101	23.687	0.014	0.014	0.000	0.000	0.000	0.000
95	A	91	TYR	0	-0.086	0.089	22.655	-0.009	-0.009	0.000	0.000	0.000	0.000
96	A	92	GLU	0	0.060	-0.103	25.168	-0.022	-0.022	0.000	0.000	0.000	0.000
97	A	92	GLU	-1	-0.897	-0.786	27.621	-0.186	-0.186	0.000	0.000	0.000	0.000
98	A	93	ASN	0	0.082	-0.092	25.493	0.016	0.016	0.000	0.000	0.000	0.000
99	A	93	ASN	0	-0.140	0.048	23.802	0.014	0.014	0.000	0.000	0.000	0.000
100	A	94	ASP	0	0.137	-0.077	26.272	-0.020	-0.020	0.000	0.000	0.000	0.000
101	A	94	ASP	-1	-0.966	-0.802	29.879	-0.164	-0.164	0.000	0.000	0.000	0.000
102	A	95	ILE	0	0.074	-0.124	25.517	0.015	0.015	0.000	0.000	0.000	0.000
103	A	95	ILE	0	-0.128	0.094	22.968	-0.005	-0.005	0.000	0.000	0.000	0.000
104	A	96	PRO	0	-0.009	-0.113	27.053	0.000	0.000	0.000	0.000	0.000	0.000
105	A	97	GLU	0	0.181	-0.003	27.437	-0.011	-0.011	0.000	0.000	0.000	0.000
106	A	97	GLU	-1	-1.016	-0.824	28.287	-0.098	-0.098	0.000	0.000	0.000	0.000
107	A	98	VAL	0	0.036	-0.082	26.680	-0.007	-0.007	0.000	0.000	0.000	0.000
108	A	98	VAL	0	-0.088	0.086	29.285	0.002	0.002	0.000	0.000	0.000	0.000
109	A	99	GLN	0	0.000	-0.127	25.408	0.010	0.010	0.000	0.000	0.000	0.000
110	A	99	GLN	0	-0.077	0.081	25.438	-0.007	-0.007	0.000	0.000	0.000	0.000
111	A	100	SER	0	-0.009	-0.125	23.308	-0.015	-0.015	0.000	0.000	0.000	0.000
112	A	100	SER	0	-0.042	0.072	23.746	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	101	ALA	0	0.195	-0.070	20.876	-0.030	-0.030	0.000	0.000	0.000	0.000
114	A	101	ALA	0	-0.089	0.103	20.623	0.006	0.006	0.000	0.000	0.000	0.000
115	A	102	TYR	0	0.082	-0.091	17.772	-0.025	-0.025	0.000	0.000	0.000	0.000
116	A	102	TYR	0	-0.163	0.043	14.262	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	103	ILE	0	0.015	-0.114	17.561	0.043	0.043	0.000	0.000	0.000	0.000
118	A	103	ILE	0	-0.039	0.134	18.982	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	104	THR	0	0.025	-0.082	16.017	-0.065	-0.065	0.000	0.000	0.000	0.000
120	A	104	THR	0	-0.033	0.071	14.546	0.019	0.019	0.000	0.000	0.000	0.000
121	A	105	ILE	0	0.040	-0.114	16.150	0.068	0.068	0.000	0.000	0.000	0.000
122	A	105	ILE	0	-0.052	0.123	17.518	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	106	SER	0	0.071	-0.052	16.216	-0.085	-0.085	0.000	0.000	0.000	0.000
124	A	106	SER	0	-0.046	0.050	18.328	-0.004	-0.004	0.000	0.000	0.000	0.000
125	A	107	ILE	0	0.037	-0.098	16.255	0.065	0.065	0.000	0.000	0.000	0.000
126	A	107	ILE	0	-0.056	0.121	13.373	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	108	ALA	0	0.161	-0.088	16.964	-0.020	-0.020	0.000	0.000	0.000	0.000
128	A	108	ALA	0	-0.073	0.107	16.906	0.009	0.009	0.000	0.000	0.000	0.000
129	A	109	ASN	0	-0.001	-0.080	17.777	0.009	0.009	0.000	0.000	0.000	0.000
130	A	109	ASN	0	-0.127	0.047	21.940	0.003	0.003	0.000	0.000	0.000	0.000
131	A	110	PHE	0	0.063	-0.139	20.054	0.045	0.045	0.000	0.000	0.000	0.000
132	A	110	PHE	0	0.011	0.153	19.264	-0.005	-0.005	0.000	0.000	0.000	0.000
133	A	111	PRO	0	-0.004	-0.097	20.447	-0.016	-0.016	0.000	0.000	0.000	0.000
134	A	112	ALA	0	0.151	0.033	19.193	-0.039	-0.039	0.000	0.000	0.000	0.000
135	A	112	ALA	0	-0.106	0.102	19.588	0.005	0.005	0.000	0.000	0.000	0.000
136	A	113	GLU	0	0.063	-0.101	19.212	0.037	0.037	0.000	0.000	0.000	0.000
137	A	113	GLU	-1	-0.949	-0.843	21.868	-0.340	-0.340	0.000	0.000	0.000	0.000
138	A	114	GLU	0	0.089	-0.128	18.823	-0.072	-0.072	0.000	0.000	0.000	0.000
139	A	114	GLU	-1	-1.010	-0.843	18.424	-0.516	-0.516	0.000	0.000	0.000	0.000
140	A	115	TYR	0	0.032	-0.133	18.937	0.064	0.064	0.000	0.000	0.000	0.000
141	A	115	TYR	0	-0.126	0.064	18.694	0.023	0.023	0.000	0.000	0.000	0.000
142	A	116	LYS	0	0.149	-0.072	19.077	-0.067	-0.067	0.000	0.000	0.000	0.000
143	A	116	LYS	1	0.762	1.012	22.055	0.301	0.301	0.000	0.000	0.000	0.000
144	A	117	LEU	0	0.067	-0.124	18.338	0.042	0.042	0.000	0.000	0.000	0.000
145	A	117	LEU	0	-0.113	0.100	16.074	-0.016	-0.016	0.000	0.000	0.000	0.000
146	A	118	GLU	0	0.093	-0.105	19.839	-0.023	-0.023	0.000	0.000	0.000	0.000
147	A	118	GLU	-1	-0.898	-0.803	23.475	-0.264	-0.264	0.000	0.000	0.000	0.000
148	A	119	ILE	0	0.046	-0.098	21.210	0.008	0.008	0.000	0.000	0.000	0.000
149	A	119	ILE	0	-0.080	0.104	18.091	-0.004	-0.004	0.000	0.000	0.000	0.000
150	A	120	THR	0	0.029	-0.098	22.405	-0.003	-0.003	0.000	0.000	0.000	0.000
151	A	120	THR	0	-0.029	0.087	25.981	0.001	0.001	0.000	0.000	0.000	0.000
152	A	121	GLY	0	0.008	-0.094	25.880	0.000	0.000	0.000	0.000	0.000	0.000
153	A	122	THR	0	-0.004	-0.018	27.673	0.002	0.002	0.000	0.000	0.000	0.000
154	A	122	THR	0	-0.036	0.112	30.764	0.002	0.002	0.000	0.000	0.000	0.000
155	A	123	PRO	0	-0.008	-0.116	31.343	0.005	0.005	0.000	0.000	0.000	0.000
156	A	124	SER	0	0.000	0.026	30.721	0.000	0.000	0.000	0.000	0.000	0.000
157	A	124	SER	0	-0.039	0.047	31.006	0.000	0.000	0.000	0.000	0.000	0.000
158	A	125	GLY	0	0.042	-0.078	26.651	0.001	0.001	0.000	0.000	0.000	0.000
159	A	126	HIS	0	0.133	0.012	25.211	0.003	0.003	0.000	0.000	0.000	0.000
160	A	126	HIS	0	-0.158	0.052	25.203	-0.001	-0.001	0.000	0.000	0.000	0.000
161	A	127	LEU	0	0.086	-0.089	20.797	0.013	0.013	0.000	0.000	0.000	0.000
162	A	127	LEU	0	-0.088	0.108	19.289	-0.004	-0.004	0.000	0.000	0.000	0.000
163	A	128	THR	0	0.022	-0.104	20.718	-0.002	-0.002	0.000	0.000	0.000	0.000
164	A	128	THR	0	-0.032	0.076	21.086	0.012	0.012	0.000	0.000	0.000	0.000
165	A	129	GLY	0	0.076	-0.039	16.699	-0.016	-0.016	0.000	0.000	0.000	0.000
166	A	130	TYR	0	0.004	-0.022	16.249	0.049	0.049	0.000	0.000	0.000	0.000
167	A	130	TYR	0	-0.028	0.121	17.504	0.024	0.024	0.000	0.000	0.000	0.000
168	A	131	PHE	0	0.053	-0.094	14.438	-0.102	-0.102	0.000	0.000	0.000	0.000
169	A	131	PHE	0	-0.076	0.081	13.637	-0.003	-0.003	0.000	0.000	0.000	0.000
170	A	132	THR	0	0.074	-0.090	14.327	0.100	0.100	0.000	0.000	0.000	0.000
171	A	132	THR	0	-0.003	0.104	14.833	-0.028	-0.028	0.000	0.000	0.000	0.000
172	A	133	LYS	0	0.104	-0.094	13.938	-0.166	-0.166	0.000	0.000	0.000	0.000
173	A	133	LYS	1	0.677	1.007	15.673	0.422	0.422	0.000	0.000	0.000	0.000
174	A	134	GLU	0	-0.110	-0.170	14.447	0.112	0.112	0.000	0.000	0.000	0.000
175	A	134	GLU	-1	-0.807	-0.867	13.542	-0.511	-0.511	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:34:PRO)