FMO DATABASE

FMODB ID: YV792

Calculation Name: 4MMN-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4MMN

Chain ID: A

ChEMBL ID:

UniProt ID: Q9HJW5

Base Structure: X-ray

Registration Date: 2023-09-23

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	141
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1353843.259099
FMO2-HF: Nuclear repulsion	1297683.384346
FMO2-HF: Total energy	-56159.874752
FMO2-MP2: Total energy	-56322.522265

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:2:ASP)

Summations of interaction energy for fragment #1(A:2:ASP)

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.
55.22	59.707	2.348	-2.916	-3.919	0

Interaction energy analysis for fragmet #1(A:2:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.883 / q_NPA : -0.955

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	4	LYS	1	0.838	0.910	3.839	-42.213	-39.863	0.024	-1.171	-1.203	0.006
4	A	5	GLU	-1	-0.947	-0.963	2.059	31.247	32.667	2.317	-1.466	-2.271	-0.006
5	A	6	PHE	0	0.009	-0.003	3.649	-6.667	-5.950	0.007	-0.279	-0.445	0.000
6	A	7	ALA	0	0.005	-0.003	5.923	-4.963	-4.963	0.000	0.000	0.000	0.000
7	A	8	ARG	1	0.876	0.904	6.239	-29.744	-29.744	0.000	0.000	0.000	0.000
8	A	9	SER	0	-0.033	-0.008	7.744	-3.162	-3.162	0.000	0.000	0.000	0.000
9	A	10	GLN	0	-0.012	-0.013	9.651	-1.830	-1.830	0.000	0.000	0.000	0.000
10	A	11	MET	0	-0.003	0.008	11.420	-1.312	-1.312	0.000	0.000	0.000	0.000
11	A	12	GLN	0	0.053	0.019	12.208	-1.290	-1.290	0.000	0.000	0.000	0.000
12	A	13	ALA	0	-0.026	-0.014	13.690	-1.412	-1.412	0.000	0.000	0.000	0.000
13	A	14	ALA	0	-0.009	-0.004	15.629	-1.231	-1.231	0.000	0.000	0.000	0.000
14	A	15	CYS	0	-0.029	-0.003	16.374	-1.066	-1.066	0.000	0.000	0.000	0.000
15	A	16	GLN	0	-0.024	-0.021	18.017	-0.733	-0.733	0.000	0.000	0.000	0.000
16	A	17	TYR	0	-0.009	-0.017	19.713	-0.890	-0.890	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.018	-0.010	20.607	-0.771	-0.771	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.863	0.932	22.560	-11.649	-11.649	0.000	0.000	0.000	0.000
19	A	20	GLU	-1	-0.873	-0.908	22.972	12.373	12.373	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.782	0.882	24.665	-12.695	-12.695	0.000	0.000	0.000	0.000
21	A	22	ASN	0	-0.029	0.000	26.368	-0.714	-0.714	0.000	0.000	0.000	0.000
22	A	23	PRO	0	0.006	0.006	28.563	0.102	0.102	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.811	0.871	30.112	-9.330	-9.330	0.000	0.000	0.000	0.000
24	A	25	TYR	0	-0.031	-0.032	25.398	0.005	0.005	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.814	-0.892	26.754	9.840	9.840	0.000	0.000	0.000	0.000
26	A	27	TRP	0	-0.008	-0.003	20.568	0.283	0.283	0.000	0.000	0.000	0.000
27	A	28	VAL	0	-0.004	-0.007	20.354	-0.193	-0.193	0.000	0.000	0.000	0.000
28	A	29	GLY	0	0.034	0.007	18.456	0.402	0.402	0.000	0.000	0.000	0.000
29	A	30	PHE	0	-0.008	-0.007	15.258	-0.175	-0.175	0.000	0.000	0.000	0.000
30	A	31	TYR	0	0.005	-0.001	16.177	0.705	0.705	0.000	0.000	0.000	0.000
31	A	32	VAL	0	-0.021	-0.031	13.596	-0.028	-0.028	0.000	0.000	0.000	0.000
32	A	33	LEU	0	-0.026	-0.004	16.640	-0.399	-0.399	0.000	0.000	0.000	0.000
33	A	34	GLU	-1	-0.789	-0.885	11.841	22.857	22.857	0.000	0.000	0.000	0.000
34	A	35	HIS	0	-0.011	-0.022	15.180	-0.839	-0.839	0.000	0.000	0.000	0.000
35	A	36	GLY	0	-0.020	-0.011	19.577	-0.659	-0.659	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.848	0.926	20.205	-13.437	-13.437	0.000	0.000	0.000	0.000
37	A	38	LEU	0	0.026	0.023	19.441	0.792	0.792	0.000	0.000	0.000	0.000
38	A	39	LYS	1	0.828	0.907	14.863	-17.965	-17.965	0.000	0.000	0.000	0.000
39	A	40	LEU	0	-0.024	0.006	16.268	0.478	0.478	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.817	-0.890	10.065	24.509	24.509	0.000	0.000	0.000	0.000
41	A	42	ALA	0	-0.037	-0.016	11.677	1.296	1.296	0.000	0.000	0.000	0.000
42	A	43	PHE	0	0.015	-0.001	14.156	-0.787	-0.787	0.000	0.000	0.000	0.000
43	A	44	VAL	0	-0.058	-0.013	17.511	0.338	0.338	0.000	0.000	0.000	0.000
44	A	45	GLY	0	0.049	0.015	20.179	-0.434	-0.434	0.000	0.000	0.000	0.000
45	A	46	GLU	-1	-0.940	-0.965	22.638	10.297	10.297	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.914	0.946	20.137	-12.382	-12.382	0.000	0.000	0.000	0.000
47	A	48	THR	0	0.071	0.044	21.506	-0.496	-0.496	0.000	0.000	0.000	0.000
48	A	49	ASP	-1	-0.893	-0.950	22.532	10.810	10.810	0.000	0.000	0.000	0.000
49	A	50	HIS	0	-0.031	-0.001	23.556	0.368	0.368	0.000	0.000	0.000	0.000
50	A	51	VAL	0	-0.002	0.000	17.388	0.358	0.358	0.000	0.000	0.000	0.000
51	A	52	GLU	-1	-0.882	-0.944	18.495	14.735	14.735	0.000	0.000	0.000	0.000
52	A	53	ILE	0	0.019	0.023	20.530	-0.595	-0.595	0.000	0.000	0.000	0.000
53	A	54	ASN	0	-0.083	-0.052	23.210	0.598	0.598	0.000	0.000	0.000	0.000
54	A	55	LEU	0	-0.001	-0.002	24.445	-0.228	-0.228	0.000	0.000	0.000	0.000
55	A	56	GLY	0	-0.048	-0.041	26.462	-0.318	-0.318	0.000	0.000	0.000	0.000
56	A	57	ASP	-1	-0.890	-0.921	27.874	9.609	9.609	0.000	0.000	0.000	0.000
57	A	58	GLY	0	0.059	0.021	27.880	0.409	0.409	0.000	0.000	0.000	0.000
58	A	59	LEU	0	-0.057	-0.034	29.575	-0.056	-0.056	0.000	0.000	0.000	0.000
59	A	60	CYS	0	0.076	0.040	24.336	-0.012	-0.012	0.000	0.000	0.000	0.000
60	A	61	SER	0	0.025	0.006	26.095	0.270	0.270	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.078	-0.035	27.088	-0.083	-0.083	0.000	0.000	0.000	0.000
62	A	63	ALA	0	0.043	0.033	26.474	-0.157	-0.157	0.000	0.000	0.000	0.000
63	A	64	VAL	0	0.006	0.001	22.516	-0.023	-0.023	0.000	0.000	0.000	0.000
64	A	65	LEU	0	-0.042	-0.015	25.930	-0.137	-0.137	0.000	0.000	0.000	0.000
65	A	66	LYS	1	0.801	0.883	28.940	-9.860	-9.860	0.000	0.000	0.000	0.000
66	A	67	ASN	0	-0.011	0.012	26.216	-0.342	-0.342	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.853	-0.922	28.639	9.947	9.947	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.005	-0.003	28.436	0.156	0.156	0.000	0.000	0.000	0.000
69	A	70	VAL	0	-0.036	-0.006	29.482	-0.385	-0.385	0.000	0.000	0.000	0.000
70	A	71	ASN	0	-0.043	-0.038	30.415	0.275	0.275	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.817	-0.873	32.701	7.905	7.905	0.000	0.000	0.000	0.000
72	A	73	TYR	0	-0.005	-0.016	34.348	0.101	0.101	0.000	0.000	0.000	0.000
73	A	74	ASP	-1	-0.784	-0.913	37.133	7.288	7.288	0.000	0.000	0.000	0.000
74	A	75	VAL	0	0.015	0.033	32.947	-0.143	-0.143	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.848	0.932	35.972	-8.207	-8.207	0.000	0.000	0.000	0.000
76	A	77	SER	0	-0.071	-0.047	39.087	-0.151	-0.151	0.000	0.000	0.000	0.000
77	A	78	ASN	0	0.005	-0.005	36.060	-0.071	-0.071	0.000	0.000	0.000	0.000
78	A	79	PRO	0	-0.054	-0.046	37.207	0.131	0.131	0.000	0.000	0.000	0.000
79	A	80	LYS	1	0.904	0.954	33.362	-8.501	-8.501	0.000	0.000	0.000	0.000
80	A	81	TYR	0	0.026	0.021	31.476	0.136	0.136	0.000	0.000	0.000	0.000
81	A	82	LEU	0	-0.026	-0.006	27.734	-0.177	-0.177	0.000	0.000	0.000	0.000
82	A	83	ALA	0	-0.008	-0.001	29.856	0.191	0.191	0.000	0.000	0.000	0.000
83	A	84	CYS	0	0.000	0.008	25.647	0.061	0.061	0.000	0.000	0.000	0.000
84	A	85	PHE	0	0.036	0.020	24.184	0.111	0.111	0.000	0.000	0.000	0.000
85	A	86	PRO	0	-0.043	-0.018	30.100	-0.198	-0.198	0.000	0.000	0.000	0.000
86	A	87	SER	0	-0.079	-0.065	32.701	-0.223	-0.223	0.000	0.000	0.000	0.000
87	A	88	THR	0	-0.027	-0.005	29.857	-0.290	-0.290	0.000	0.000	0.000	0.000
88	A	89	GLN	0	-0.095	-0.081	33.322	-0.426	-0.426	0.000	0.000	0.000	0.000
89	A	90	SER	0	-0.036	-0.032	33.221	-0.255	-0.255	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.807	-0.914	28.334	10.277	10.277	0.000	0.000	0.000	0.000
91	A	92	ILE	0	-0.067	-0.039	27.711	-0.263	-0.263	0.000	0.000	0.000	0.000
92	A	93	VAL	0	0.012	0.023	24.583	0.396	0.396	0.000	0.000	0.000	0.000
93	A	94	VAL	0	-0.002	-0.018	24.421	-0.411	-0.411	0.000	0.000	0.000	0.000
94	A	95	PRO	0	-0.016	-0.001	23.211	0.685	0.685	0.000	0.000	0.000	0.000
95	A	96	VAL	0	-0.001	0.008	17.703	-0.028	-0.028	0.000	0.000	0.000	0.000
96	A	97	ARG	1	0.824	0.908	21.021	-11.287	-11.287	0.000	0.000	0.000	0.000
97	A	98	TYR	0	0.023	-0.004	15.198	0.391	0.391	0.000	0.000	0.000	0.000
98	A	99	GLN	0	-0.051	-0.037	19.817	-0.053	-0.053	0.000	0.000	0.000	0.000
99	A	100	GLY	0	0.007	0.015	22.570	-0.466	-0.466	0.000	0.000	0.000	0.000
100	A	101	GLU	-1	-0.775	-0.869	21.847	13.622	13.622	0.000	0.000	0.000	0.000
101	A	102	PRO	0	-0.005	0.006	22.602	0.482	0.482	0.000	0.000	0.000	0.000
102	A	103	ILE	0	-0.031	-0.017	16.130	0.144	0.144	0.000	0.000	0.000	0.000
103	A	104	GLY	0	0.043	0.011	17.833	0.835	0.835	0.000	0.000	0.000	0.000
104	A	105	GLU	-1	-0.867	-0.940	19.184	12.045	12.045	0.000	0.000	0.000	0.000
105	A	106	ILE	0	-0.039	-0.006	19.437	0.654	0.654	0.000	0.000	0.000	0.000
106	A	107	ASP	-1	-0.843	-0.938	21.169	11.380	11.380	0.000	0.000	0.000	0.000
107	A	108	ILE	0	-0.025	-0.015	22.725	0.382	0.382	0.000	0.000	0.000	0.000
108	A	109	ASP	-1	-0.770	-0.868	25.486	9.711	9.711	0.000	0.000	0.000	0.000
109	A	110	SER	0	-0.052	-0.048	28.135	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	111	ASP	-1	-0.747	-0.859	31.138	8.762	8.762	0.000	0.000	0.000	0.000
111	A	112	LYS	1	0.785	0.917	34.203	-8.380	-8.380	0.000	0.000	0.000	0.000
112	A	113	LYS	1	0.880	0.963	35.649	-7.202	-7.202	0.000	0.000	0.000	0.000
113	A	114	ALA	0	-0.005	-0.019	37.481	-0.089	-0.089	0.000	0.000	0.000	0.000
114	A	115	ALA	0	-0.067	-0.023	33.136	-0.112	-0.112	0.000	0.000	0.000	0.000
115	A	116	PHE	0	0.028	0.002	29.784	0.094	0.094	0.000	0.000	0.000	0.000
116	A	117	SER	0	-0.025	-0.033	33.840	-0.198	-0.198	0.000	0.000	0.000	0.000
117	A	118	LYS	1	0.846	0.888	33.910	-8.448	-8.448	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.838	-0.894	33.849	8.766	8.766	0.000	0.000	0.000	0.000
119	A	120	ASP	-1	-0.732	-0.817	30.142	10.031	10.031	0.000	0.000	0.000	0.000
120	A	121	GLU	-1	-0.729	-0.840	29.250	9.434	9.434	0.000	0.000	0.000	0.000
121	A	122	ALA	0	0.011	0.024	29.492	0.345	0.345	0.000	0.000	0.000	0.000
122	A	123	MET	0	-0.035	-0.006	26.670	0.416	0.416	0.000	0.000	0.000	0.000
123	A	124	LEU	0	0.034	0.002	24.390	0.570	0.570	0.000	0.000	0.000	0.000
124	A	125	SER	0	0.011	-0.007	24.428	0.501	0.501	0.000	0.000	0.000	0.000
125	A	126	SER	0	-0.047	-0.029	24.779	0.405	0.405	0.000	0.000	0.000	0.000
126	A	127	ILE	0	-0.028	-0.021	20.658	0.595	0.595	0.000	0.000	0.000	0.000
127	A	128	ALA	0	0.030	0.015	20.466	0.925	0.925	0.000	0.000	0.000	0.000
128	A	129	ASP	-1	-0.900	-0.959	20.049	13.903	13.903	0.000	0.000	0.000	0.000
129	A	130	LEU	0	-0.095	-0.052	20.015	0.766	0.766	0.000	0.000	0.000	0.000
130	A	131	MET	0	-0.022	0.003	13.989	1.251	1.251	0.000	0.000	0.000	0.000
131	A	132	ALA	0	0.035	0.030	15.550	1.470	1.470	0.000	0.000	0.000	0.000
132	A	133	PRO	0	-0.070	-0.054	14.074	0.880	0.880	0.000	0.000	0.000	0.000
133	A	134	LEU	0	-0.014	0.005	10.516	1.979	1.979	0.000	0.000	0.000	0.000
134	A	135	VAL	0	0.070	0.018	11.134	1.709	1.709	0.000	0.000	0.000	0.000
135	A	136	HIS	1	0.872	0.954	12.059	-22.707	-22.707	0.000	0.000	0.000	0.000
136	A	137	GLU	-1	-0.888	-0.947	7.566	36.506	36.506	0.000	0.000	0.000	0.000
137	A	138	PHE	0	-0.060	-0.034	6.877	1.969	1.969	0.000	0.000	0.000	0.000
138	A	139	PHE	0	0.005	0.030	11.321	-1.845	-1.845	0.000	0.000	0.000	0.000
139	A	140	VAL	0	-0.051	-0.030	13.352	0.823	0.823	0.000	0.000	0.000	0.000
140	A	141	LYS	1	0.808	0.887	15.964	-15.016	-15.016	0.000	0.000	0.000	0.000
141	A	142	LEU	0	-0.004	0.000	19.677	-0.055	-0.055	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ASP)