FMO DATABASE

FMODB ID: YZ252

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	OptH
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	-806391.686721
FMO2-HF: Nuclear repulsion	756324.87826
FMO2-HF: Total energy	-50066.808461
FMO2-MP2: Total energy	-50214.871348

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.
-12.149	-7.581	2.637	-3.094	-4.112	-0.004

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 : 0.050 / 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].
3	A	3	GLU	-1	-0.909	-0.969	3.010	-5.774	-2.842	0.067	-1.254	-1.745	0.000
4	A	4	ASP	-1	-0.837	-0.917	2.098	-6.199	-5.303	2.565	-1.620	-1.841	-0.004
5	A	5	LYS	1	0.898	0.947	3.556	-0.641	0.099	0.005	-0.220	-0.526	0.000
6	A	6	ILE	0	-0.029	-0.017	5.528	1.010	1.010	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.875	-0.914	6.977	-0.922	-0.922	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.955	-0.989	7.170	0.475	0.475	0.000	0.000	0.000	0.000
9	A	9	ILE	0	-0.100	-0.057	9.347	0.252	0.252	0.000	0.000	0.000	0.000
10	A	10	LEU	0	0.048	0.016	11.345	0.136	0.136	0.000	0.000	0.000	0.000
11	A	11	SER	0	0.024	0.027	12.463	0.082	0.082	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.921	0.948	12.167	-0.755	-0.755	0.000	0.000	0.000	0.000
13	A	13	ILE	0	0.001	-0.004	15.444	0.030	0.030	0.000	0.000	0.000	0.000
14	A	14	TYR	0	0.050	0.033	16.415	-0.007	-0.007	0.000	0.000	0.000	0.000
15	A	15	HIS	0	0.000	-0.003	17.404	0.013	0.013	0.000	0.000	0.000	0.000
16	A	16	ILE	0	-0.034	-0.024	18.875	0.019	0.019	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.953	-0.963	21.171	-0.044	-0.044	0.000	0.000	0.000	0.000
18	A	18	ASN	0	-0.017	-0.023	22.971	-0.011	-0.011	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.915	-0.935	24.010	0.145	0.145	0.000	0.000	0.000	0.000
20	A	20	ILE	0	0.028	0.015	25.451	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	21	ALA	0	0.007	0.002	27.750	-0.003	-0.003	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.850	0.915	25.845	-0.081	-0.081	0.000	0.000	0.000	0.000
23	A	23	ILE	0	0.024	0.007	28.769	-0.003	-0.003	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.951	0.967	31.441	-0.038	-0.038	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.954	1.003	33.827	-0.026	-0.026	0.000	0.000	0.000	0.000
26	A	26	LEU	0	0.011	0.010	35.239	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	27	ILE	0	-0.005	-0.013	34.986	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	28	GLY	0	-0.016	0.000	37.976	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.943	-0.989	39.498	0.034	0.034	0.000	0.000	0.000	0.000
30	A	30	ALA	0	-0.018	-0.018	40.924	-0.001	-0.001	0.000	0.000	0.000	0.000
31	A	31	ARG	1	0.899	0.946	40.878	-0.049	-0.049	0.000	0.000	0.000	0.000
32	A	32	GLN	0	0.049	0.031	44.193	0.001	0.001	0.000	0.000	0.000	0.000
33	A	33	LEU	0	-0.036	-0.009	45.523	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	34	LEU	0	0.028	0.008	45.068	0.001	0.001	0.000	0.000	0.000	0.000
35	A	35	SER	0	0.003	0.002	47.994	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	36	GLY	0	-0.001	-0.002	50.402	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.038	-0.029	49.049	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	38	VAL	0	0.066	0.032	51.477	0.000	0.000	0.000	0.000	0.000	0.000
39	A	39	GLN	0	0.020	0.013	53.941	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	40	GLN	0	-0.025	-0.021	55.829	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	41	GLN	0	-0.018	-0.018	55.313	0.000	0.000	0.000	0.000	0.000	0.000
42	A	42	ASN	0	0.078	0.062	58.366	0.000	0.000	0.000	0.000	0.000	0.000
43	A	43	ASN	0	-0.096	-0.054	60.377	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	44	LEU	0	-0.036	-0.031	59.265	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.040	0.035	62.459	0.000	0.000	0.000	0.000	0.000	0.000
46	A	46	ARG	1	0.988	0.993	63.709	-0.030	-0.030	0.000	0.000	0.000	0.000
47	A	47	ALA	0	-0.052	-0.013	66.106	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	48	ILE	0	0.032	0.008	64.723	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.900	-0.947	67.895	0.032	0.032	0.000	0.000	0.000	0.000
50	A	50	ALA	0	-0.027	-0.016	70.294	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	51	GLN	0	-0.040	-0.033	70.787	0.000	0.000	0.000	0.000	0.000	0.000
52	A	52	GLN	0	0.060	0.049	72.620	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	53	HIS	0	0.033	0.016	73.908	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.021	-0.011	76.259	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	55	LEU	0	0.028	-0.006	74.701	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	56	GLN	0	0.017	0.015	77.299	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.056	-0.019	80.412	-0.001	-0.001	0.000	0.000	0.000	0.000
58	A	58	THR	0	-0.069	-0.042	81.281	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	59	VAL	0	0.046	0.036	81.675	0.000	0.000	0.000	0.000	0.000	0.000
60	A	60	TRP	0	0.001	0.004	84.219	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	61	GLY	0	0.004	-0.011	86.220	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	62	ILE	0	-0.025	-0.018	85.022	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	63	LYS	1	0.960	0.981	85.812	-0.027	-0.027	0.000	0.000	0.000	0.000
64	A	64	GLN	0	-0.042	-0.006	90.257	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.045	-0.031	91.436	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	66	GLN	0	0.038	0.043	89.170	0.000	0.000	0.000	0.000	0.000	0.000
67	A	67	ALA	0	0.014	0.021	94.278	0.000	0.000	0.000	0.000	0.000	0.000
68	A	68	ARG	1	0.922	0.942	96.447	-0.018	-0.018	0.000	0.000	0.000	0.000
69	A	69	ILE	0	0.014	0.016	96.551	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	70	LEU	0	0.031	0.031	98.325	0.000	0.000	0.000	0.000	0.000	0.000
71	A	71	ALA	0	-0.050	-0.031	99.965	0.000	0.000	0.000	0.000	0.000	0.000
72	A	72	VAL	0	0.004	-0.003	102.147	0.000	0.000	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.889	-0.946	100.346	0.021	0.021	0.000	0.000	0.000	0.000
74	A	74	ARG	1	0.929	0.945	102.506	-0.020	-0.020	0.000	0.000	0.000	0.000
75	A	75	TYR	0	-0.068	-0.031	105.333	0.000	0.000	0.000	0.000	0.000	0.000
76	A	76	LEU	0	0.002	0.003	106.506	0.000	0.000	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.830	0.971	106.364	-0.019	-0.019	0.000	0.000	0.000	0.000
78	A	78	ASP	-1	-0.878	-0.944	109.180	0.018	0.018	0.000	0.000	0.000	0.000
79	A	79	GLN	0	-0.065	-0.057	105.580	0.000	0.000	0.000	0.000	0.000	0.000
80	A	80	ASN	0	0.021	0.010	101.906	0.000	0.000	0.000	0.000	0.000	0.000
81	A	81	ASN	0	-0.077	-0.054	98.564	0.001	0.001	0.000	0.000	0.000	0.000
82	A	82	MET	0	0.042	0.044	93.490	0.000	0.000	0.000	0.000	0.000	0.000
83	A	83	THR	0	0.027	0.011	92.312	0.000	0.000	0.000	0.000	0.000	0.000
84	A	117	TRP	0	-0.006	0.008	88.762	0.000	0.000	0.000	0.000	0.000	0.000
85	A	118	MET	0	0.029	-0.024	89.354	0.001	0.001	0.000	0.000	0.000	0.000
86	A	119	GLU	-1	-0.908	-0.958	84.095	0.034	0.034	0.000	0.000	0.000	0.000
87	A	120	TRP	0	0.070	0.029	84.711	0.000	0.000	0.000	0.000	0.000	0.000
88	A	121	ASP	-1	-0.875	-0.961	84.400	0.027	0.027	0.000	0.000	0.000	0.000
89	A	122	ARG	1	0.879	0.958	83.720	-0.031	-0.031	0.000	0.000	0.000	0.000
90	A	123	GLU	-1	-0.910	-0.962	80.108	0.036	0.036	0.000	0.000	0.000	0.000
91	A	124	ILE	0	0.000	0.006	79.507	0.001	0.001	0.000	0.000	0.000	0.000
92	A	125	ASN	0	-0.021	-0.008	79.777	0.000	0.000	0.000	0.000	0.000	0.000
93	A	126	ASN	0	-0.025	-0.015	77.399	0.000	0.000	0.000	0.000	0.000	0.000
94	A	127	TYR	0	0.011	-0.002	73.559	0.001	0.001	0.000	0.000	0.000	0.000
95	A	128	THR	0	-0.022	-0.009	74.656	0.000	0.000	0.000	0.000	0.000	0.000
96	A	129	SER	0	-0.024	-0.015	75.145	0.000	0.000	0.000	0.000	0.000	0.000
97	A	130	LEU	0	0.000	0.005	69.762	0.001	0.001	0.000	0.000	0.000	0.000
98	A	131	ILE	0	-0.019	-0.016	70.429	0.001	0.001	0.000	0.000	0.000	0.000
99	A	132	HIS	0	0.026	0.003	70.394	0.000	0.000	0.000	0.000	0.000	0.000
100	A	133	SER	0	0.011	0.030	68.802	0.000	0.000	0.000	0.000	0.000	0.000
101	A	134	LEU	0	0.001	-0.008	65.550	0.000	0.000	0.000	0.000	0.000	0.000
102	A	135	ILE	0	-0.018	0.011	65.362	0.001	0.001	0.000	0.000	0.000	0.000
103	A	136	GLU	-1	-0.901	-0.935	66.156	0.040	0.040	0.000	0.000	0.000	0.000
104	A	137	GLU	-1	-0.975	-1.003	62.853	0.051	0.051	0.000	0.000	0.000	0.000
105	A	138	SER	0	-0.063	-0.055	61.602	0.002	0.002	0.000	0.000	0.000	0.000
106	A	139	GLN	0	-0.028	-0.009	61.541	0.000	0.000	0.000	0.000	0.000	0.000
107	A	140	ASN	0	0.023	0.015	61.203	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	141	GLN	0	-0.064	-0.051	54.813	0.001	0.001	0.000	0.000	0.000	0.000
109	A	142	GLN	0	-0.070	-0.035	56.907	0.003	0.003	0.000	0.000	0.000	0.000
110	A	143	GLU	-1	-0.899	-0.942	57.563	0.038	0.038	0.000	0.000	0.000	0.000
111	A	144	LYS	1	0.913	0.960	54.557	-0.057	-0.057	0.000	0.000	0.000	0.000
112	A	145	ASN	0	0.028	0.012	52.607	0.002	0.002	0.000	0.000	0.000	0.000
113	A	146	GLU	-1	-0.883	-0.935	52.360	0.038	0.038	0.000	0.000	0.000	0.000
114	A	147	GLN	0	0.014	0.018	53.247	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	148	GLU	-1	-0.980	-0.998	49.027	0.067	0.067	0.000	0.000	0.000	0.000
116	A	149	LEU	0	-0.050	-0.024	47.880	0.001	0.001	0.000	0.000	0.000	0.000
117	A	150	LEU	0	0.006	0.004	48.776	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	151	GLU	-1	-0.880	-0.934	47.775	0.046	0.046	0.000	0.000	0.000	0.000
119	A	152	LEU	0	-0.008	-0.008	43.081	0.001	0.001	0.000	0.000	0.000	0.000
120	A	153	ASP	-1	-0.989	-0.960	43.836	0.035	0.035	0.000	0.000	0.000	0.000
121	A	154	LYS	1	0.756	0.875	41.849	-0.050	-0.050	0.000	0.000	0.000	0.000

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