FMO DATABASE

FMODB ID: R9118

Calculation Name: 5H77-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5H77

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2023-06-21

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	84
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-519394.087587
FMO2-HF: Nuclear repulsion	486333.361673
FMO2-HF: Total energy	-33060.725914
FMO2-MP2: Total energy	-33159.826426

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:4:PRO)

Summations of interaction energy for fragment #1(A:4: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.
-1.289	1.118	1.6	-1.13	-2.879	-0.001

Interaction energy analysis for fragmet #1(A:4:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.014 / q_NPA : -0.019

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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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	6	GLY	0	0.049	0.023	3.896	-0.956	0.179	-0.010	-0.434	-0.692	0.002
4	A	7	LEU	0	-0.007	0.003	2.356	-0.700	0.383	1.611	-0.662	-2.032	-0.003
5	A	8	THR	0	0.023	0.002	4.379	0.613	0.802	-0.001	-0.034	-0.155	0.000
6	A	9	GLU	-1	-0.867	-0.939	7.242	-1.291	-1.291	0.000	0.000	0.000	0.000
7	A	10	LEU	0	-0.010	0.007	7.211	0.221	0.221	0.000	0.000	0.000	0.000
8	A	11	LEU	0	0.012	0.001	7.016	0.202	0.202	0.000	0.000	0.000	0.000
9	A	12	GLN	0	-0.006	0.010	10.097	0.216	0.216	0.000	0.000	0.000	0.000
10	A	13	GLY	0	0.011	0.009	12.282	0.099	0.099	0.000	0.000	0.000	0.000
11	A	14	TYR	0	-0.018	-0.026	12.802	0.064	0.064	0.000	0.000	0.000	0.000
12	A	15	THR	0	-0.019	-0.024	13.769	0.071	0.071	0.000	0.000	0.000	0.000
13	A	16	VAL	0	-0.035	-0.020	16.180	0.054	0.054	0.000	0.000	0.000	0.000
14	A	17	GLU	-1	-0.814	-0.898	17.730	-0.214	-0.214	0.000	0.000	0.000	0.000
15	A	18	VAL	0	0.000	0.012	18.123	0.031	0.031	0.000	0.000	0.000	0.000
16	A	19	LEU	0	-0.045	-0.025	20.135	0.030	0.030	0.000	0.000	0.000	0.000
17	A	20	ARG	1	0.828	0.909	21.102	0.257	0.257	0.000	0.000	0.000	0.000
18	A	21	GLN	0	-0.037	-0.041	21.873	0.021	0.021	0.000	0.000	0.000	0.000
19	A	22	GLN	0	-0.082	-0.029	24.415	0.014	0.014	0.000	0.000	0.000	0.000
20	A	23	PRO	0	-0.003	0.020	21.705	0.013	0.013	0.000	0.000	0.000	0.000
21	A	24	PRO	0	-0.010	-0.016	24.992	-0.003	-0.003	0.000	0.000	0.000	0.000
22	A	25	ASP	-1	-0.830	-0.908	22.835	-0.192	-0.192	0.000	0.000	0.000	0.000
23	A	26	LEU	0	0.032	0.001	19.135	-0.010	-0.010	0.000	0.000	0.000	0.000
24	A	27	VAL	0	-0.015	0.000	18.418	-0.038	-0.038	0.000	0.000	0.000	0.000
25	A	28	GLU	-1	-0.884	-0.943	19.101	-0.195	-0.195	0.000	0.000	0.000	0.000
26	A	29	PHE	0	-0.024	-0.013	18.573	-0.008	-0.008	0.000	0.000	0.000	0.000
27	A	30	ALA	0	-0.006	0.001	15.085	-0.023	-0.023	0.000	0.000	0.000	0.000
28	A	31	VAL	0	0.003	0.002	16.165	-0.026	-0.026	0.000	0.000	0.000	0.000
29	A	32	GLU	-1	-0.769	-0.852	18.148	-0.203	-0.203	0.000	0.000	0.000	0.000
30	A	33	TYR	0	-0.021	-0.012	13.484	-0.018	-0.018	0.000	0.000	0.000	0.000
31	A	34	PHE	0	0.005	-0.023	11.531	-0.028	-0.028	0.000	0.000	0.000	0.000
32	A	35	THR	0	-0.031	-0.005	14.772	0.008	0.008	0.000	0.000	0.000	0.000
33	A	36	ARG	1	0.776	0.868	17.884	0.236	0.236	0.000	0.000	0.000	0.000
34	A	37	LEU	0	0.009	0.004	12.713	0.011	0.011	0.000	0.000	0.000	0.000
35	A	38	ARG	1	0.900	0.949	14.826	0.234	0.234	0.000	0.000	0.000	0.000
36	A	39	GLN	0	0.042	0.022	15.783	0.009	0.009	0.000	0.000	0.000	0.000
37	A	40	GLN	0	-0.012	-0.002	16.737	-0.011	-0.011	0.000	0.000	0.000	0.000
38	A	41	ARG	1	0.849	0.906	9.526	0.392	0.392	0.000	0.000	0.000	0.000
39	A	42	ALA	0	0.020	0.013	16.108	0.024	0.024	0.000	0.000	0.000	0.000
40	A	43	PHE	0	0.003	-0.009	18.639	0.020	0.020	0.000	0.000	0.000	0.000
41	A	44	TYR	0	-0.002	0.000	16.556	0.014	0.014	0.000	0.000	0.000	0.000
42	A	45	GLU	-1	-0.861	-0.931	14.049	-0.188	-0.188	0.000	0.000	0.000	0.000
43	A	46	ILE	0	0.011	0.010	18.691	0.022	0.022	0.000	0.000	0.000	0.000
44	A	47	LEU	0	-0.045	-0.023	22.056	0.015	0.015	0.000	0.000	0.000	0.000
45	A	48	HIS	0	-0.014	-0.001	19.618	0.023	0.023	0.000	0.000	0.000	0.000
46	A	49	LEU	0	-0.011	0.012	21.514	0.014	0.014	0.000	0.000	0.000	0.000
47	A	50	PRO	0	-0.010	-0.001	23.798	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	51	ASN	0	-0.045	-0.029	26.613	0.000	0.000	0.000	0.000	0.000	0.000
49	A	52	LEU	0	-0.010	0.018	26.985	0.001	0.001	0.000	0.000	0.000	0.000
50	A	53	ASN	0	-0.015	-0.019	30.113	-0.003	-0.003	0.000	0.000	0.000	0.000
51	A	54	GLU	-1	-0.928	-0.976	31.472	-0.047	-0.047	0.000	0.000	0.000	0.000
52	A	55	GLU	-1	-0.849	-0.919	31.881	-0.038	-0.038	0.000	0.000	0.000	0.000
53	A	56	GLN	0	-0.021	-0.029	31.418	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	57	ARG	1	0.813	0.914	25.606	0.046	0.046	0.000	0.000	0.000	0.000
55	A	58	ASN	0	-0.011	-0.010	28.271	-0.005	-0.005	0.000	0.000	0.000	0.000
56	A	59	ALA	0	0.028	0.028	30.331	-0.005	-0.005	0.000	0.000	0.000	0.000
57	A	60	PHE	0	0.019	0.007	26.056	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	61	ILE	0	0.006	0.006	24.968	-0.008	-0.008	0.000	0.000	0.000	0.000
59	A	62	GLN	0	-0.003	-0.017	26.881	-0.008	-0.008	0.000	0.000	0.000	0.000
60	A	63	SER	0	-0.027	-0.031	27.682	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	64	LEU	0	-0.030	-0.001	21.926	-0.004	-0.004	0.000	0.000	0.000	0.000
62	A	65	LYS	1	0.817	0.918	24.738	0.076	0.076	0.000	0.000	0.000	0.000
63	A	66	ASP	-1	-0.865	-0.913	27.323	-0.086	-0.086	0.000	0.000	0.000	0.000
64	A	67	ASP	-1	-0.843	-0.911	26.450	-0.123	-0.123	0.000	0.000	0.000	0.000
65	A	68	PRO	0	0.004	-0.006	21.342	0.002	0.002	0.000	0.000	0.000	0.000
66	A	69	SER	0	-0.069	-0.041	22.207	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	70	GLN	0	0.009	0.002	23.753	0.009	0.009	0.000	0.000	0.000	0.000
68	A	71	SER	0	0.019	-0.003	19.783	0.006	0.006	0.000	0.000	0.000	0.000
69	A	72	ALA	0	-0.007	-0.002	19.476	0.005	0.005	0.000	0.000	0.000	0.000
70	A	73	ASN	0	-0.014	-0.010	20.809	0.012	0.012	0.000	0.000	0.000	0.000
71	A	74	LEU	0	-0.008	0.007	23.663	0.008	0.008	0.000	0.000	0.000	0.000
72	A	75	LEU	0	0.021	0.016	17.569	0.007	0.007	0.000	0.000	0.000	0.000
73	A	76	ALA	0	-0.005	-0.002	21.970	0.011	0.011	0.000	0.000	0.000	0.000
74	A	77	GLU	-1	-0.882	-0.948	23.475	-0.016	-0.016	0.000	0.000	0.000	0.000
75	A	78	ALA	0	0.030	0.021	24.368	0.005	0.005	0.000	0.000	0.000	0.000
76	A	79	LYS	1	0.813	0.888	20.978	0.003	0.003	0.000	0.000	0.000	0.000
77	A	80	LYS	1	0.861	0.940	24.556	0.020	0.020	0.000	0.000	0.000	0.000
78	A	81	LEU	0	-0.011	0.008	27.501	0.004	0.004	0.000	0.000	0.000	0.000
79	A	82	ASN	0	0.044	-0.018	25.073	0.000	0.000	0.000	0.000	0.000	0.000
80	A	83	ASP	-1	-0.851	-0.910	24.501	0.015	0.015	0.000	0.000	0.000	0.000
81	A	84	ALA	0	-0.030	-0.009	28.066	0.006	0.006	0.000	0.000	0.000	0.000
82	A	85	GLN	0	-0.010	0.017	31.437	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	86	ALA	0	-0.004	-0.003	31.997	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	87	PRO	0	-0.049	-0.017	31.964	0.007	0.007	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:PRO)