FMO DATABASE

FMODB ID: V5431

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	OptHSide
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	-807064.234471
FMO2-HF: Nuclear repulsion	756996.22975
FMO2-HF: Total energy	-50068.004721
FMO2-MP2: Total energy	-50215.97421

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.
-22.067	-14.341	4.25	-5.963	-6.013	-0.04

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 : 0.032 / 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	-0.876	-0.952	3.020	-5.006	-2.261	0.068	-1.184	-1.629	0.001
4	A	4	ASP	-1	-0.834	-0.926	2.359	-15.196	-10.859	4.178	-4.578	-3.937	-0.041
5	A	5	LYS	1	0.901	0.952	3.582	-2.394	-1.750	0.004	-0.201	-0.447	0.000
6	A	6	ILE	0	-0.007	-0.006	5.549	0.855	0.855	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.871	-0.917	7.011	-0.965	-0.965	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.911	-0.961	7.727	0.564	0.564	0.000	0.000	0.000	0.000
9	A	9	ILE	0	-0.074	-0.046	9.171	0.229	0.229	0.000	0.000	0.000	0.000
10	A	10	LEU	0	0.040	0.019	11.377	0.115	0.115	0.000	0.000	0.000	0.000
11	A	11	SER	0	0.013	0.018	12.487	0.077	0.077	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.852	0.909	10.751	-0.560	-0.560	0.000	0.000	0.000	0.000
13	A	13	ILE	0	0.006	-0.003	15.464	0.025	0.025	0.000	0.000	0.000	0.000
14	A	14	TYR	0	0.043	0.029	16.490	-0.007	-0.007	0.000	0.000	0.000	0.000
15	A	15	HIS	0	-0.003	-0.003	16.849	0.038	0.038	0.000	0.000	0.000	0.000
16	A	16	ILE	0	-0.037	-0.023	18.583	0.018	0.018	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.941	-0.962	21.194	-0.024	-0.024	0.000	0.000	0.000	0.000
18	A	18	ASN	0	-0.031	-0.013	22.998	0.005	0.005	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.811	-0.878	23.907	0.064	0.064	0.000	0.000	0.000	0.000
20	A	20	ILE	0	0.014	0.016	24.877	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	21	ALA	0	-0.010	-0.004	27.772	-0.002	-0.002	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.793	0.856	25.748	-0.027	-0.027	0.000	0.000	0.000	0.000
23	A	23	ILE	0	0.016	0.004	28.590	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.961	0.970	31.008	-0.042	-0.042	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.864	0.944	33.847	-0.006	-0.006	0.000	0.000	0.000	0.000
26	A	26	LEU	0	-0.006	0.004	35.199	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	27	ILE	0	-0.001	-0.014	34.703	0.000	0.000	0.000	0.000	0.000	0.000
28	A	28	GLY	0	-0.005	0.009	37.983	0.000	0.000	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.849	-0.930	39.418	0.011	0.011	0.000	0.000	0.000	0.000
30	A	30	ALA	0	-0.027	-0.022	40.878	-0.001	-0.001	0.000	0.000	0.000	0.000
31	A	31	ARG	1	0.904	0.957	40.919	-0.046	-0.046	0.000	0.000	0.000	0.000
32	A	32	GLN	0	0.024	0.012	44.204	0.002	0.002	0.000	0.000	0.000	0.000
33	A	33	LEU	0	-0.008	-0.001	45.536	0.000	0.000	0.000	0.000	0.000	0.000
34	A	34	LEU	0	0.025	0.017	45.173	0.000	0.000	0.000	0.000	0.000	0.000
35	A	35	SER	0	0.005	0.003	48.001	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.005	0.001	50.401	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.042	-0.031	48.840	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	38	VAL	0	0.048	0.024	51.438	0.000	0.000	0.000	0.000	0.000	0.000
39	A	39	GLN	0	0.019	0.013	53.953	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	40	GLN	0	-0.012	-0.017	55.835	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	41	GLN	0	-0.007	-0.006	55.339	0.001	0.001	0.000	0.000	0.000	0.000
42	A	42	ASN	0	0.021	0.025	58.374	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	43	ASN	0	-0.043	-0.026	60.101	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	44	LEU	0	-0.030	-0.027	59.398	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.029	0.030	62.473	0.000	0.000	0.000	0.000	0.000	0.000
46	A	46	ARG	1	0.930	0.952	62.950	-0.024	-0.024	0.000	0.000	0.000	0.000
47	A	47	ALA	0	-0.057	-0.015	66.112	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	48	ILE	0	0.034	0.009	64.601	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.865	-0.917	67.794	0.028	0.028	0.000	0.000	0.000	0.000
50	A	50	ALA	0	-0.029	-0.018	70.306	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	51	GLN	0	-0.039	-0.031	70.214	0.000	0.000	0.000	0.000	0.000	0.000
52	A	52	GLN	0	0.068	0.056	72.638	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	53	HIS	0	0.027	0.013	73.600	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.025	-0.010	76.291	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	55	LEU	0	0.019	-0.007	74.662	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	56	GLN	0	-0.003	-0.006	77.668	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.026	-0.007	80.423	-0.001	-0.001	0.000	0.000	0.000	0.000
58	A	58	THR	0	-0.068	-0.039	81.271	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	59	VAL	0	0.029	0.022	81.504	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	60	TRP	0	0.009	0.012	84.226	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	61	GLY	0	0.002	-0.011	86.223	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	62	ILE	0	-0.030	-0.024	84.808	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	63	LYS	1	0.899	0.943	85.702	-0.022	-0.022	0.000	0.000	0.000	0.000
64	A	64	GLN	0	-0.030	0.000	90.265	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.052	-0.034	90.848	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	66	GLN	0	0.028	0.027	89.129	0.000	0.000	0.000	0.000	0.000	0.000
67	A	67	ALA	0	0.016	0.018	94.283	0.000	0.000	0.000	0.000	0.000	0.000
68	A	68	ARG	1	0.923	0.946	95.801	-0.013	-0.013	0.000	0.000	0.000	0.000
69	A	69	ILE	0	0.007	0.010	96.243	0.000	0.000	0.000	0.000	0.000	0.000
70	A	70	LEU	0	0.026	0.029	98.278	0.000	0.000	0.000	0.000	0.000	0.000
71	A	71	ALA	0	-0.036	-0.028	99.970	0.000	0.000	0.000	0.000	0.000	0.000
72	A	72	VAL	0	-0.006	-0.008	102.165	0.000	0.000	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.865	-0.931	100.663	0.015	0.015	0.000	0.000	0.000	0.000
74	A	74	ARG	1	0.907	0.938	101.965	-0.016	-0.016	0.000	0.000	0.000	0.000
75	A	75	TYR	0	-0.059	-0.028	105.323	0.000	0.000	0.000	0.000	0.000	0.000
76	A	76	LEU	0	-0.010	-0.006	105.753	0.000	0.000	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.823	0.953	106.016	-0.015	-0.015	0.000	0.000	0.000	0.000
78	A	78	ASP	-1	-0.870	-0.924	109.506	0.013	0.013	0.000	0.000	0.000	0.000
79	A	79	GLN	0	-0.066	-0.053	105.657	0.000	0.000	0.000	0.000	0.000	0.000
80	A	80	ASN	0	0.024	0.011	102.038	0.000	0.000	0.000	0.000	0.000	0.000
81	A	81	ASN	0	-0.077	-0.054	98.736	0.001	0.001	0.000	0.000	0.000	0.000
82	A	82	MET	0	0.045	0.041	93.829	0.000	0.000	0.000	0.000	0.000	0.000
83	A	83	THR	0	0.023	0.011	92.349	0.000	0.000	0.000	0.000	0.000	0.000
84	A	117	TRP	0	0.014	0.029	88.754	0.000	0.000	0.000	0.000	0.000	0.000
85	A	118	MET	0	0.024	-0.027	89.363	0.000	0.000	0.000	0.000	0.000	0.000
86	A	119	GLU	-1	-0.846	-0.909	84.671	0.027	0.027	0.000	0.000	0.000	0.000
87	A	120	TRP	0	0.085	0.036	84.863	0.001	0.001	0.000	0.000	0.000	0.000
88	A	121	ASP	-1	-0.820	-0.926	84.409	0.022	0.022	0.000	0.000	0.000	0.000
89	A	122	ARG	1	0.810	0.908	83.652	-0.026	-0.026	0.000	0.000	0.000	0.000
90	A	123	GLU	-1	-0.873	-0.943	79.522	0.029	0.029	0.000	0.000	0.000	0.000
91	A	124	ILE	0	0.007	0.009	79.519	0.001	0.001	0.000	0.000	0.000	0.000
92	A	125	ASN	0	-0.014	0.003	79.791	0.000	0.000	0.000	0.000	0.000	0.000
93	A	126	ASN	0	-0.022	-0.006	77.523	0.001	0.001	0.000	0.000	0.000	0.000
94	A	127	TYR	0	-0.025	-0.023	74.314	0.001	0.001	0.000	0.000	0.000	0.000
95	A	128	THR	0	-0.035	-0.021	74.671	0.000	0.000	0.000	0.000	0.000	0.000
96	A	129	SER	0	-0.039	-0.030	75.164	0.000	0.000	0.000	0.000	0.000	0.000
97	A	130	LEU	0	0.010	0.010	69.362	0.001	0.001	0.000	0.000	0.000	0.000
98	A	131	ILE	0	-0.030	-0.018	70.425	0.001	0.001	0.000	0.000	0.000	0.000
99	A	132	HIS	0	0.034	0.009	70.412	0.000	0.000	0.000	0.000	0.000	0.000
100	A	133	SER	0	-0.015	0.021	69.013	0.000	0.000	0.000	0.000	0.000	0.000
101	A	134	LEU	0	0.031	0.004	65.592	0.000	0.000	0.000	0.000	0.000	0.000
102	A	135	ILE	0	-0.013	0.014	65.383	0.001	0.001	0.000	0.000	0.000	0.000
103	A	136	GLU	-1	-0.893	-0.929	66.179	0.038	0.038	0.000	0.000	0.000	0.000
104	A	137	GLU	-1	-0.945	-0.985	62.964	0.045	0.045	0.000	0.000	0.000	0.000
105	A	138	SER	0	-0.060	-0.057	61.626	0.002	0.002	0.000	0.000	0.000	0.000
106	A	139	GLN	0	-0.050	-0.033	61.563	0.001	0.001	0.000	0.000	0.000	0.000
107	A	140	ASN	0	-0.032	-0.019	61.264	0.001	0.001	0.000	0.000	0.000	0.000
108	A	141	GLN	0	-0.013	-0.019	55.052	0.002	0.002	0.000	0.000	0.000	0.000
109	A	142	GLN	0	-0.066	-0.045	56.933	0.002	0.002	0.000	0.000	0.000	0.000
110	A	143	GLU	-1	-0.903	-0.943	57.589	0.038	0.038	0.000	0.000	0.000	0.000
111	A	144	LYS	1	0.865	0.935	54.610	-0.055	-0.055	0.000	0.000	0.000	0.000
112	A	145	ASN	0	0.016	0.005	52.636	0.003	0.003	0.000	0.000	0.000	0.000
113	A	146	GLU	-1	-0.820	-0.882	52.387	0.034	0.034	0.000	0.000	0.000	0.000
114	A	147	GLN	0	-0.017	-0.008	53.128	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	148	GLU	-1	-0.957	-0.988	49.079	0.065	0.065	0.000	0.000	0.000	0.000
116	A	149	LEU	0	-0.049	-0.029	48.109	0.001	0.001	0.000	0.000	0.000	0.000
117	A	150	LEU	0	0.002	0.003	48.804	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	151	GLU	-1	-0.858	-0.907	47.629	0.053	0.053	0.000	0.000	0.000	0.000
119	A	152	LEU	0	-0.015	-0.007	43.084	0.002	0.002	0.000	0.000	0.000	0.000
120	A	153	ASP	-1	-0.975	-0.960	43.869	0.040	0.040	0.000	0.000	0.000	0.000
121	A	154	LYS	1	0.752	0.867	42.212	-0.057	-0.057	0.000	0.000	0.000	0.000

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