FMO DATABASE

FMODB ID: MVMMZ

Calculation Name: 5HIZ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5HIZ

Chain ID: A

ChEMBL ID:

UniProt ID: P0C6Y4

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	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	99
LigandResidueName
LigandFragmentNumber	0
LigandCharge	CYM=-1
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-709991.527308
FMO2-HF: Nuclear repulsion	671829.14212
FMO2-HF: Total energy	-38162.385187
FMO2-MP2: Total energy	-38275.277746

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:7:GLY)

Summations of interaction energy for fragment #1(A:7:GLY)

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.
0.48	1.636	0.019	-0.421	-0.755	0

Interaction energy analysis for fragmet #1(A:7:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.037 / q_NPA : 0.007

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].
3	A	9	LEU	0	0.010	0.006	3.772	1.266	2.219	-0.004	-0.348	-0.601
4	A	10	LYS	1	0.989	1.004	5.640	-0.484	-0.484	0.000	0.000	0.000
5	A	11	GLN	0	0.029	0.008	9.357	0.061	0.061	0.000	0.000	0.000
6	A	12	ARG	1	0.854	0.909	12.196	-0.208	-0.208	0.000	0.000	0.000
7	A	13	SER	0	0.005	0.009	15.691	-0.014	-0.014	0.000	0.000	0.000
8	A	14	ILE	0	-0.005	0.017	18.388	0.015	0.015	0.000	0.000	0.000
9	A	15	LYS	1	0.885	0.933	20.465	-0.061	-0.061	0.000	0.000	0.000
10	A	16	ALA	0	-0.002	-0.003	21.675	0.013	0.013	0.000	0.000	0.000
11	A	17	GLU	-1	-0.877	-0.940	23.723	0.064	0.064	0.000	0.000	0.000
12	A	18	GLY	0	-0.010	-0.022	25.692	0.004	0.004	0.000	0.000	0.000
13	A	19	ASP	-1	-0.972	-0.984	28.021	0.036	0.036	0.000	0.000	0.000
14	A	20	GLY	0	0.010	0.007	31.182	-0.002	-0.002	0.000	0.000	0.000
15	A	21	ILE	0	0.027	0.028	28.427	-0.001	-0.001	0.000	0.000	0.000
16	A	22	VAL	0	0.029	0.010	27.536	0.005	0.005	0.000	0.000	0.000
17	A	23	GLY	0	-0.081	-0.040	25.892	-0.008	-0.008	0.000	0.000	0.000
18	A	24	GLU	-1	-0.857	-0.913	22.651	0.050	0.050	0.000	0.000	0.000
19	A	25	GLY	0	-0.008	-0.020	20.007	-0.006	-0.006	0.000	0.000	0.000
20	A	26	LYS	1	0.843	0.913	15.012	0.012	0.012	0.000	0.000	0.000
21	A	27	ALA	0	0.036	0.021	14.419	-0.004	-0.004	0.000	0.000	0.000
22	A	28	LEU	0	0.019	0.007	9.109	-0.015	-0.015	0.000	0.000	0.000
23	A	29	TYR	0	-0.030	-0.012	9.539	-0.020	-0.020	0.000	0.000	0.000
24	A	30	ASN	0	0.034	-0.005	4.856	-1.083	-1.080	-0.001	-0.006	0.004
25	A	31	ASN	0	-0.030	0.006	8.536	-0.080	-0.080	0.000	0.000	0.000
26	A	32	GLU	-1	-0.902	-0.940	7.391	2.203	2.203	0.000	0.000	0.000
27	A	33	GLY	0	-0.058	-0.015	11.166	-0.148	-0.148	0.000	0.000	0.000
28	A	34	GLY	0	0.041	0.002	11.798	0.112	0.112	0.000	0.000	0.000
29	A	35	ARG	1	0.984	0.984	14.560	-0.429	-0.429	0.000	0.000	0.000
30	A	36	THR	0	0.018	0.018	13.249	0.164	0.164	0.000	0.000	0.000
31	A	37	PHE	0	-0.004	-0.012	11.883	-0.103	-0.103	0.000	0.000	0.000
32	A	38	MET	0	0.005	0.017	10.703	0.128	0.128	0.000	0.000	0.000
33	A	39	TYR	0	-0.033	-0.028	4.649	0.077	0.130	-0.001	-0.001	-0.051
34	A	40	ALA	0	0.001	-0.014	10.168	-0.058	-0.058	0.000	0.000	0.000
35	A	41	PHE	0	0.013	0.007	12.373	-0.002	-0.002	0.000	0.000	0.000
36	A	42	ILE	0	0.036	0.033	12.995	-0.020	-0.020	0.000	0.000	0.000
37	A	43	SER	0	0.002	0.010	16.843	0.000	0.000	0.000	0.000	0.000
38	A	44	ASP	-1	-0.852	-0.938	20.604	-0.037	-0.037	0.000	0.000	0.000
39	A	45	LYS	1	0.912	0.954	23.766	-0.017	-0.017	0.000	0.000	0.000
40	A	46	PRO	0	-0.039	0.002	24.280	0.004	0.004	0.000	0.000	0.000
41	A	47	ASP	-1	-0.873	-0.958	25.719	0.018	0.018	0.000	0.000	0.000
42	A	48	LEU	0	-0.047	-0.008	22.633	0.005	0.005	0.000	0.000	0.000
43	A	49	ARG	1	0.930	0.946	23.999	-0.062	-0.062	0.000	0.000	0.000
44	A	50	VAL	0	-0.002	-0.008	22.383	0.011	0.011	0.000	0.000	0.000
45	A	51	VAL	0	-0.011	-0.002	18.545	-0.009	-0.009	0.000	0.000	0.000
46	A	52	LYS	1	0.988	1.000	21.423	-0.092	-0.092	0.000	0.000	0.000
47	A	53	TRP	0	-0.046	-0.036	14.392	-0.009	-0.009	0.000	0.000	0.000
48	A	54	GLU	-1	-0.859	-0.919	20.545	0.144	0.144	0.000	0.000	0.000
49	A	55	PHE	0	-0.026	-0.040	16.156	0.015	0.015	0.000	0.000	0.000
50	A	56	ASP	-1	-0.887	-0.941	17.958	0.326	0.326	0.000	0.000	0.000
51	A	57	GLY	0	0.015	0.020	21.543	-0.025	-0.025	0.000	0.000	0.000
52	A	58	GLY	0	-0.050	-0.034	21.820	0.019	0.019	0.000	0.000	0.000
53	A	59	CYM	-1	-0.834	-0.880	22.149	0.145	0.145	0.000	0.000	0.000
54	A	60	ASN	0	-0.129	-0.093	20.730	0.011	0.011	0.000	0.000	0.000
55	A	61	THR	0	0.034	0.011	21.907	-0.006	-0.006	0.000	0.000	0.000
56	A	62	ILE	0	-0.003	0.009	16.920	0.014	0.014	0.000	0.000	0.000
57	A	63	GLU	-1	-0.910	-0.947	20.183	0.099	0.099	0.000	0.000	0.000
58	A	64	LEU	0	-0.067	-0.034	17.514	0.015	0.015	0.000	0.000	0.000
59	A	65	GLU	-1	-0.888	-0.930	17.208	0.088	0.088	0.000	0.000	0.000
60	A	66	PRO	0	-0.006	-0.022	19.916	-0.004	-0.004	0.000	0.000	0.000
61	A	67	PRO	0	-0.018	0.018	19.590	-0.002	-0.002	0.000	0.000	0.000
62	A	68	ARG	1	0.914	0.958	17.558	0.040	0.040	0.000	0.000	0.000
63	A	69	LYS	1	0.944	0.941	19.118	0.016	0.016	0.000	0.000	0.000
64	A	70	PHE	0	-0.056	-0.038	16.011	-0.006	-0.006	0.000	0.000	0.000
65	A	71	LEU	0	0.051	0.043	20.717	0.005	0.005	0.000	0.000	0.000
66	A	72	VAL	0	0.008	-0.015	18.225	-0.016	-0.016	0.000	0.000	0.000
67	A	73	ASP	-1	-0.886	-0.954	21.495	-0.087	-0.087	0.000	0.000	0.000
68	A	74	SER	0	-0.040	0.010	23.380	-0.007	-0.007	0.000	0.000	0.000
69	A	75	PRO	0	0.032	0.006	25.167	0.005	0.005	0.000	0.000	0.000
70	A	76	ASN	0	-0.077	-0.058	27.983	0.003	0.003	0.000	0.000	0.000
71	A	77	GLY	0	0.005	0.028	29.990	0.005	0.005	0.000	0.000	0.000
72	A	78	ALA	0	0.051	0.025	25.976	-0.002	-0.002	0.000	0.000	0.000
73	A	79	GLN	0	0.005	0.022	23.865	0.012	0.012	0.000	0.000	0.000
74	A	80	ILE	0	-0.044	-0.028	23.764	-0.009	-0.009	0.000	0.000	0.000
75	A	81	LYS	1	0.952	0.985	19.004	0.071	0.071	0.000	0.000	0.000
76	A	82	TYR	0	0.010	-0.004	20.459	-0.003	-0.003	0.000	0.000	0.000
77	A	83	LEU	0	0.016	-0.003	12.985	0.003	0.003	0.000	0.000	0.000
78	A	84	TYR	0	-0.004	0.001	16.327	0.002	0.002	0.000	0.000	0.000
79	A	85	PHE	0	0.011	0.013	10.841	0.014	0.014	0.000	0.000	0.000
80	A	86	VAL	0	0.046	0.021	13.598	-0.017	-0.017	0.000	0.000	0.000
81	A	87	ARG	1	0.994	0.991	15.401	-0.104	-0.104	0.000	0.000	0.000
82	A	88	ASN	0	-0.035	-0.012	16.421	0.013	0.013	0.000	0.000	0.000
83	A	89	LEU	0	0.022	0.037	9.431	0.029	0.029	0.000	0.000	0.000
84	A	90	ASN	0	0.060	0.014	9.659	-0.003	-0.003	0.000	0.000	0.000
85	A	91	THR	0	0.073	0.009	10.859	0.031	0.031	0.000	0.000	0.000
86	A	92	LEU	0	-0.005	0.018	6.837	-0.005	-0.005	0.000	0.000	0.000
87	A	93	ARG	1	1.000	1.000	5.986	-0.853	-0.853	0.000	0.000	0.000
88	A	94	ARG	1	0.833	0.911	7.197	-0.160	-0.160	0.000	0.000	0.000
89	A	95	GLY	0	0.038	0.015	8.864	-0.052	-0.052	0.000	0.000	0.000
90	A	96	ALA	0	-0.012	-0.016	3.224	-0.230	-0.060	0.026	-0.064	-0.133
91	A	97	VAL	0	-0.051	-0.003	5.242	-0.339	-0.362	-0.001	-0.002	0.026
92	A	98	LEU	0	0.000	-0.001	7.511	-0.135	-0.135	0.000	0.000	0.000
93	A	99	GLY	0	0.019	0.012	7.143	-0.014	-0.014	0.000	0.000	0.000
94	A	100	TYR	0	0.014	0.000	5.834	-0.018	-0.018	0.000	0.000	0.000
95	A	101	ILE	0	-0.056	-0.038	7.674	0.097	0.097	0.000	0.000	0.000
96	A	102	GLY	0	-0.020	0.005	11.081	0.007	0.007	0.000	0.000	0.000
97	A	103	ALA	0	-0.007	0.004	9.453	0.014	0.014	0.000	0.000	0.000
98	A	104	THR	0	-0.110	-0.054	11.491	-0.006	-0.006	0.000	0.000	0.000
99	A	105	VAL	0	0.006	0.011	13.690	0.064	0.064	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:GLY)