FMO DATABASE

FMODB ID: 17Q1Z

Calculation Name: 1ENV-A-Xray372

Preferred Name: Envelope glycoprotein gp160

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 1ENV

Chain ID: A

ChEMBL ID: CHEMBL5826

UniProt ID: P03377

Base Structure: X-ray

Registration Date: 2023-09-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	121
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-808927.501113
FMO2-HF: Nuclear repulsion	758858.902524
FMO2-HF: Total energy	-50068.598588
FMO2-MP2: Total energy	-50216.474364

3D Structure

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:1:GLN)

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

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.
-21.463	-17.843	8.02	-5.621	-6.019	-0.047

Interaction energy analysis for fragmet #1(A:1:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.043 / q_NPA : 0.008

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

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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	3	GLU	-1	-0.833	-0.937	3.393	-2.912	-1.101	0.017	-0.715	-1.113	0.001
4	A	4	ASP	-1	-0.843	-0.923	2.018	-18.101	-17.027	7.999	-4.681	-4.391	-0.048
5	A	5	LYS	1	0.861	0.927	3.598	-1.223	-0.554	0.005	-0.223	-0.452	0.000
6	A	6	ILE	0	-0.002	0.004	5.300	0.748	0.814	-0.001	-0.002	-0.063	0.000
7	A	7	GLU	-1	-0.872	-0.931	7.358	-0.853	-0.853	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.858	-0.926	7.350	0.154	0.154	0.000	0.000	0.000	0.000
9	A	9	ILE	0	-0.066	-0.031	9.306	0.274	0.274	0.000	0.000	0.000	0.000
10	A	10	LEU	0	0.009	0.004	11.326	0.114	0.114	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.011	-0.003	12.356	0.105	0.105	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.827	0.889	10.765	-0.063	-0.063	0.000	0.000	0.000	0.000
13	A	13	ILE	0	0.003	0.004	15.241	0.048	0.048	0.000	0.000	0.000	0.000
14	A	14	TYR	0	0.041	0.022	16.604	0.011	0.011	0.000	0.000	0.000	0.000
15	A	15	HIS	0	-0.021	-0.002	16.310	0.051	0.051	0.000	0.000	0.000	0.000
16	A	16	ILE	0	-0.011	-0.011	19.057	0.020	0.020	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.926	-0.956	21.238	-0.042	-0.042	0.000	0.000	0.000	0.000
18	A	18	ASN	0	0.005	0.010	22.900	0.013	0.013	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.811	-0.879	23.716	-0.014	-0.014	0.000	0.000	0.000	0.000
20	A	20	ILE	0	0.000	0.001	24.454	0.005	0.005	0.000	0.000	0.000	0.000
21	A	21	ALA	0	-0.047	-0.024	27.319	0.003	0.003	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.789	0.851	25.530	0.044	0.044	0.000	0.000	0.000	0.000
23	A	23	ILE	0	0.002	0.003	28.396	0.002	0.002	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.959	0.976	30.275	-0.014	-0.014	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.873	0.937	33.464	0.026	0.026	0.000	0.000	0.000	0.000
26	A	26	LEU	0	-0.006	0.004	34.853	0.000	0.000	0.000	0.000	0.000	0.000
27	A	27	ILE	0	0.012	-0.008	34.577	0.002	0.002	0.000	0.000	0.000	0.000
28	A	28	GLY	0	-0.004	0.008	37.817	0.002	0.002	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.847	-0.926	39.110	-0.012	-0.012	0.000	0.000	0.000	0.000
30	A	30	ALA	0	-0.037	-0.022	40.672	0.001	0.001	0.000	0.000	0.000	0.000
31	A	31	ARG	1	0.856	0.932	40.722	-0.027	-0.027	0.000	0.000	0.000	0.000
32	A	32	GLN	0	0.034	0.021	44.072	0.003	0.003	0.000	0.000	0.000	0.000
33	A	33	LEU	0	-0.014	0.005	45.163	0.000	0.000	0.000	0.000	0.000	0.000
34	A	34	LEU	0	0.017	0.008	45.514	0.000	0.000	0.000	0.000	0.000	0.000
35	A	35	SER	0	-0.005	-0.013	47.931	0.000	0.000	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.033	0.021	50.389	0.000	0.000	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.041	-0.027	48.733	0.000	0.000	0.000	0.000	0.000	0.000
38	A	38	VAL	0	0.043	0.025	51.414	0.000	0.000	0.000	0.000	0.000	0.000
39	A	39	GLN	0	0.030	0.014	53.972	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	40	GLN	0	-0.008	-0.007	55.737	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	41	GLN	0	-0.013	-0.005	55.299	0.000	0.000	0.000	0.000	0.000	0.000
42	A	42	ASN	0	0.026	0.021	58.483	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	43	ASN	0	-0.040	-0.032	59.820	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	44	LEU	0	-0.020	-0.018	59.738	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.024	0.033	62.591	0.000	0.000	0.000	0.000	0.000	0.000
46	A	46	ARG	1	0.900	0.933	62.286	-0.014	-0.014	0.000	0.000	0.000	0.000
47	A	47	ALA	0	-0.044	-0.014	66.106	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	48	ILE	0	0.022	0.007	64.760	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.851	-0.919	67.823	0.019	0.019	0.000	0.000	0.000	0.000
50	A	50	ALA	0	-0.038	-0.017	70.578	0.000	0.000	0.000	0.000	0.000	0.000
51	A	51	GLN	0	-0.032	-0.023	69.614	0.000	0.000	0.000	0.000	0.000	0.000
52	A	52	GLN	0	0.058	0.046	72.698	0.000	0.000	0.000	0.000	0.000	0.000
53	A	53	HIS	0	0.029	0.005	73.411	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.028	-0.013	76.299	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	55	LEU	0	0.012	0.003	74.972	0.000	0.000	0.000	0.000	0.000	0.000
56	A	56	GLN	0	0.003	0.004	77.976	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.011	0.003	80.601	0.000	0.000	0.000	0.000	0.000	0.000
58	A	58	THR	0	-0.076	-0.046	81.310	0.000	0.000	0.000	0.000	0.000	0.000
59	A	59	VAL	0	0.026	0.011	81.711	0.000	0.000	0.000	0.000	0.000	0.000
60	A	60	TRP	0	0.009	0.004	84.421	0.000	0.000	0.000	0.000	0.000	0.000
61	A	61	GLY	0	0.020	0.001	86.526	0.000	0.000	0.000	0.000	0.000	0.000
62	A	62	ILE	0	-0.021	-0.020	84.991	0.000	0.000	0.000	0.000	0.000	0.000
63	A	63	LYS	1	0.883	0.947	86.004	-0.015	-0.015	0.000	0.000	0.000	0.000
64	A	64	GLN	0	-0.019	-0.002	90.583	0.000	0.000	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.064	-0.035	90.637	0.000	0.000	0.000	0.000	0.000	0.000
66	A	66	GLN	0	0.031	0.012	89.276	0.000	0.000	0.000	0.000	0.000	0.000
67	A	67	ALA	0	0.015	0.011	94.462	0.000	0.000	0.000	0.000	0.000	0.000
68	A	68	ARG	1	0.929	0.957	95.325	-0.008	-0.008	0.000	0.000	0.000	0.000
69	A	69	ILE	0	0.007	0.011	96.376	0.000	0.000	0.000	0.000	0.000	0.000
70	A	70	LEU	0	0.025	0.019	98.257	0.000	0.000	0.000	0.000	0.000	0.000
71	A	71	ALA	0	-0.042	-0.025	100.227	0.000	0.000	0.000	0.000	0.000	0.000
72	A	72	VAL	0	-0.008	-0.013	102.098	0.000	0.000	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.858	-0.930	101.234	0.009	0.009	0.000	0.000	0.000	0.000
74	A	74	ARG	1	0.900	0.942	101.824	-0.011	-0.011	0.000	0.000	0.000	0.000
75	A	75	TYR	0	-0.061	-0.027	105.440	0.000	0.000	0.000	0.000	0.000	0.000
76	A	76	LEU	0	-0.041	-0.010	106.038	0.000	0.000	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.841	0.952	106.173	-0.010	-0.010	0.000	0.000	0.000	0.000
78	A	78	ASP	-1	-0.855	-0.920	109.740	0.008	0.008	0.000	0.000	0.000	0.000
79	A	79	GLN	0	-0.070	-0.054	105.930	0.000	0.000	0.000	0.000	0.000	0.000
80	A	80	ASN	0	0.028	0.011	102.412	0.000	0.000	0.000	0.000	0.000	0.000
81	A	81	ASN	0	-0.072	-0.052	99.100	0.001	0.001	0.000	0.000	0.000	0.000
82	A	82	MET	0	0.039	0.036	94.117	0.000	0.000	0.000	0.000	0.000	0.000
83	A	83	THR	0	0.023	0.007	92.889	0.000	0.000	0.000	0.000	0.000	0.000
84	A	117	TRP	0	0.014	0.021	88.943	0.000	0.000	0.000	0.000	0.000	0.000
85	A	118	MET	0	0.015	-0.017	89.562	0.000	0.000	0.000	0.000	0.000	0.000
86	A	119	GLU	-1	-0.830	-0.902	85.064	0.019	0.019	0.000	0.000	0.000	0.000
87	A	120	TRP	0	0.064	0.037	84.926	0.000	0.000	0.000	0.000	0.000	0.000
88	A	121	ASP	-1	-0.821	-0.921	84.347	0.015	0.015	0.000	0.000	0.000	0.000
89	A	122	ARG	1	0.816	0.903	83.799	-0.019	-0.019	0.000	0.000	0.000	0.000
90	A	123	GLU	-1	-0.861	-0.913	79.685	0.020	0.020	0.000	0.000	0.000	0.000
91	A	124	ILE	0	0.011	0.011	79.598	0.000	0.000	0.000	0.000	0.000	0.000
92	A	125	ASN	0	-0.007	0.005	79.748	0.000	0.000	0.000	0.000	0.000	0.000
93	A	126	ASN	0	-0.011	0.007	77.582	0.001	0.001	0.000	0.000	0.000	0.000
94	A	127	TYR	0	-0.036	-0.047	74.671	0.001	0.001	0.000	0.000	0.000	0.000
95	A	128	THR	0	-0.033	-0.020	74.737	0.000	0.000	0.000	0.000	0.000	0.000
96	A	129	SER	0	-0.020	-0.021	75.162	0.000	0.000	0.000	0.000	0.000	0.000
97	A	130	LEU	0	-0.016	0.009	69.602	0.001	0.001	0.000	0.000	0.000	0.000
98	A	131	ILE	0	-0.009	-0.010	70.619	0.001	0.001	0.000	0.000	0.000	0.000
99	A	132	HIS	0	0.018	-0.004	70.370	0.000	0.000	0.000	0.000	0.000	0.000
100	A	133	SER	0	-0.019	0.003	69.423	0.001	0.001	0.000	0.000	0.000	0.000
101	A	134	LEU	0	0.034	0.010	65.770	0.001	0.001	0.000	0.000	0.000	0.000
102	A	135	ILE	0	-0.036	0.003	65.705	0.000	0.000	0.000	0.000	0.000	0.000
103	A	136	GLU	-1	-0.903	-0.940	66.238	0.030	0.030	0.000	0.000	0.000	0.000
104	A	137	GLU	-1	-0.926	-0.972	63.350	0.034	0.034	0.000	0.000	0.000	0.000
105	A	138	SER	0	-0.051	-0.043	61.881	0.001	0.001	0.000	0.000	0.000	0.000
106	A	139	GLN	0	-0.059	-0.046	61.541	0.001	0.001	0.000	0.000	0.000	0.000
107	A	140	ASN	0	-0.013	-0.011	61.618	0.002	0.002	0.000	0.000	0.000	0.000
108	A	141	GLN	0	-0.022	-0.011	55.476	0.003	0.003	0.000	0.000	0.000	0.000
109	A	142	GLN	0	-0.066	-0.045	57.055	0.001	0.001	0.000	0.000	0.000	0.000
110	A	143	GLU	-1	-0.911	-0.959	57.450	0.029	0.029	0.000	0.000	0.000	0.000
111	A	144	LYS	1	0.853	0.936	54.908	-0.042	-0.042	0.000	0.000	0.000	0.000
112	A	145	ASN	0	0.003	-0.003	53.023	0.003	0.003	0.000	0.000	0.000	0.000
113	A	146	GLU	-1	-0.813	-0.883	52.568	0.022	0.022	0.000	0.000	0.000	0.000
114	A	147	GLN	0	-0.021	-0.005	53.088	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	148	GLU	-1	-0.946	-0.988	49.598	0.050	0.050	0.000	0.000	0.000	0.000
116	A	149	LEU	0	-0.048	-0.025	48.286	0.001	0.001	0.000	0.000	0.000	0.000
117	A	150	LEU	0	-0.030	-0.011	48.604	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	151	GLU	-1	-0.828	-0.895	47.934	0.043	0.043	0.000	0.000	0.000	0.000
119	A	152	LEU	0	-0.036	-0.001	43.163	0.003	0.003	0.000	0.000	0.000	0.000
120	A	153	ASP	-1	-0.867	-0.909	44.102	0.029	0.029	0.000	0.000	0.000	0.000
121	A	154	LYS	1	0.719	0.831	41.544	-0.044	-0.044	0.000	0.000	0.000	0.000

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