FMO DATABASE

FMODB ID: 662JZ

Calculation Name: 3K1H-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3K1H

Chain ID: A

ChEMBL ID:

UniProt ID: O25709

Base Structure: X-ray

Registration Date: 2023-06-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	115
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-919001.613104
FMO2-HF: Nuclear repulsion	872950.698716
FMO2-HF: Total energy	-46050.914388
FMO2-MP2: Total energy	-46183.808651

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:33:PHE)

Summations of interaction energy for fragment #1(A:33:PHE)

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.
-13.534	-5.819	2.337	-4.096	-5.957	-0.032

Interaction energy analysis for fragmet #1(A:33:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.006 / q_NPA : -0.015

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	35	ARG	1	0.809	0.904	3.221	-0.899	2.058	0.049	-1.472	-1.534	-0.006
4	A	36	ASP	-1	-0.852	-0.911	5.579	-0.494	-0.494	0.000	0.000	0.000	0.000
5	A	37	MET	0	-0.082	-0.031	8.348	0.127	0.127	0.000	0.000	0.000	0.000
6	A	38	LYS	1	0.932	0.981	11.525	0.282	0.282	0.000	0.000	0.000	0.000
7	A	39	ASN	0	0.003	-0.016	13.928	0.029	0.029	0.000	0.000	0.000	0.000
8	A	40	ILE	0	0.099	0.047	16.287	-0.053	-0.053	0.000	0.000	0.000	0.000
9	A	41	ASN	0	-0.015	-0.010	18.161	-0.025	-0.025	0.000	0.000	0.000	0.000
10	A	42	GLU	-1	-0.895	-0.956	12.148	-0.419	-0.419	0.000	0.000	0.000	0.000
11	A	43	SER	0	0.032	0.019	13.567	-0.089	-0.089	0.000	0.000	0.000	0.000
12	A	44	VAL	0	0.040	0.021	14.612	-0.049	-0.049	0.000	0.000	0.000	0.000
13	A	45	GLY	0	-0.026	-0.011	16.006	-0.009	-0.009	0.000	0.000	0.000	0.000
14	A	46	ALA	0	0.013	0.000	10.693	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	47	LEU	0	0.046	0.019	12.664	-0.055	-0.055	0.000	0.000	0.000	0.000
16	A	48	GLN	0	-0.013	-0.005	14.585	0.020	0.020	0.000	0.000	0.000	0.000
17	A	49	VAL	0	-0.009	-0.005	13.513	0.027	0.027	0.000	0.000	0.000	0.000
18	A	50	LEU	0	0.038	0.016	10.658	0.027	0.027	0.000	0.000	0.000	0.000
19	A	51	GLN	0	0.000	0.003	13.733	0.038	0.038	0.000	0.000	0.000	0.000
20	A	52	ILE	0	-0.055	-0.026	17.214	0.042	0.042	0.000	0.000	0.000	0.000
21	A	53	ALA	0	0.003	0.003	14.447	0.043	0.043	0.000	0.000	0.000	0.000
22	A	54	CYS	0	0.043	0.018	14.347	0.014	0.014	0.000	0.000	0.000	0.000
23	A	55	LYS	1	0.981	0.991	16.980	0.375	0.375	0.000	0.000	0.000	0.000
24	A	56	LYS	1	0.869	0.946	19.365	0.363	0.363	0.000	0.000	0.000	0.000
25	A	57	LEU	0	0.000	0.007	14.920	0.037	0.037	0.000	0.000	0.000	0.000
26	A	58	PHE	0	0.036	0.030	19.595	0.029	0.029	0.000	0.000	0.000	0.000
27	A	59	ASN	0	0.016	-0.015	21.736	0.033	0.033	0.000	0.000	0.000	0.000
28	A	60	LYS	1	0.894	0.954	22.076	0.263	0.263	0.000	0.000	0.000	0.000
29	A	61	SER	0	-0.011	0.002	22.360	0.018	0.018	0.000	0.000	0.000	0.000
30	A	62	MET	0	-0.013	0.000	24.496	0.011	0.011	0.000	0.000	0.000	0.000
31	A	63	GLY	0	0.028	0.014	27.631	0.008	0.008	0.000	0.000	0.000	0.000
32	A	64	LEU	0	-0.085	-0.037	24.351	0.010	0.010	0.000	0.000	0.000	0.000
33	A	65	GLU	-1	-0.895	-0.959	28.253	-0.154	-0.154	0.000	0.000	0.000	0.000
34	A	66	ASP	-1	-0.910	-0.941	29.776	-0.107	-0.107	0.000	0.000	0.000	0.000
35	A	67	LYS	1	0.810	0.921	29.520	0.164	0.164	0.000	0.000	0.000	0.000
36	A	68	ASP	-1	-0.821	-0.904	32.331	-0.100	-0.100	0.000	0.000	0.000	0.000
37	A	69	ALA	0	0.041	-0.007	31.668	-0.008	-0.008	0.000	0.000	0.000	0.000
38	A	70	LEU	0	-0.020	0.010	30.840	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	71	GLN	0	0.022	0.004	30.357	-0.016	-0.016	0.000	0.000	0.000	0.000
40	A	72	ALA	0	0.023	0.016	27.939	-0.014	-0.014	0.000	0.000	0.000	0.000
41	A	73	SER	0	-0.098	-0.064	26.274	-0.015	-0.015	0.000	0.000	0.000	0.000
42	A	74	ILE	0	0.016	0.001	25.478	-0.010	-0.010	0.000	0.000	0.000	0.000
43	A	75	ILE	0	0.046	0.024	24.136	-0.013	-0.013	0.000	0.000	0.000	0.000
44	A	76	LYS	1	0.948	0.971	22.037	0.163	0.163	0.000	0.000	0.000	0.000
45	A	77	GLN	0	-0.016	0.001	19.500	-0.026	-0.026	0.000	0.000	0.000	0.000
46	A	78	GLU	-1	-0.904	-0.956	20.360	-0.208	-0.208	0.000	0.000	0.000	0.000
47	A	79	LEU	0	-0.061	-0.035	18.692	-0.031	-0.031	0.000	0.000	0.000	0.000
48	A	80	ARG	1	0.942	0.963	16.119	0.206	0.206	0.000	0.000	0.000	0.000
49	A	81	GLU	-1	-0.881	-0.935	15.287	-0.253	-0.253	0.000	0.000	0.000	0.000
50	A	82	ILE	0	-0.096	-0.046	15.714	-0.011	-0.011	0.000	0.000	0.000	0.000
51	A	83	VAL	0	-0.021	-0.013	10.871	-0.046	-0.046	0.000	0.000	0.000	0.000
52	A	84	GLU	-1	-0.961	-0.982	11.311	-0.424	-0.424	0.000	0.000	0.000	0.000
53	A	85	ASN	0	-0.049	-0.020	12.088	0.057	0.057	0.000	0.000	0.000	0.000
54	A	86	CYS	0	-0.096	-0.019	11.114	0.034	0.034	0.000	0.000	0.000	0.000
55	A	87	GLN	0	-0.019	-0.013	9.939	-0.057	-0.057	0.000	0.000	0.000	0.000
56	A	88	PHE	0	0.020	0.004	9.863	0.047	0.047	0.000	0.000	0.000	0.000
57	A	89	LEU	0	-0.022	-0.013	9.921	-0.011	-0.011	0.000	0.000	0.000	0.000
58	A	90	ALA	0	-0.002	0.011	10.104	0.044	0.044	0.000	0.000	0.000	0.000
59	A	91	SER	0	0.044	0.019	5.287	0.463	0.463	0.000	0.000	0.000	0.000
60	A	92	PRO	0	0.036	0.010	3.928	-0.627	-0.219	0.002	-0.052	-0.358	0.000
61	A	93	LEU	0	-0.025	-0.016	5.590	-0.291	-0.291	0.000	0.000	0.000	0.000
62	A	94	PHE	0	0.063	0.023	7.145	-0.196	-0.196	0.000	0.000	0.000	0.000
63	A	95	ASP	-1	-0.844	-0.912	4.197	-2.793	-2.552	-0.001	-0.033	-0.207	0.000
64	A	96	THR	0	-0.085	-0.044	2.354	-9.844	-6.254	2.284	-2.408	-3.467	-0.026
65	A	97	GLN	0	-0.050	-0.026	3.713	1.964	2.483	0.003	-0.131	-0.391	0.000
66	A	98	LEU	0	-0.025	-0.025	5.806	-0.206	-0.206	0.000	0.000	0.000	0.000
67	A	99	ASN	0	0.013	0.015	7.981	0.296	0.296	0.000	0.000	0.000	0.000
68	A	100	ILE	0	0.030	-0.004	10.487	0.026	0.026	0.000	0.000	0.000	0.000
69	A	101	ALA	0	-0.005	0.017	13.673	0.047	0.047	0.000	0.000	0.000	0.000
70	A	102	ILE	0	-0.021	-0.028	16.991	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	103	ASN	0	-0.017	-0.016	20.113	0.017	0.017	0.000	0.000	0.000	0.000
72	A	104	ASP	-1	-0.944	-0.962	22.098	-0.124	-0.124	0.000	0.000	0.000	0.000
73	A	105	GLU	-1	-0.947	-0.950	20.356	-0.172	-0.172	0.000	0.000	0.000	0.000
74	A	106	ILE	0	-0.048	-0.041	13.724	-0.030	-0.030	0.000	0.000	0.000	0.000
75	A	107	PHE	0	0.024	0.016	15.565	0.012	0.012	0.000	0.000	0.000	0.000
76	A	108	SER	0	-0.013	-0.034	10.470	-0.020	-0.020	0.000	0.000	0.000	0.000
77	A	109	MET	0	-0.020	0.016	10.726	0.132	0.132	0.000	0.000	0.000	0.000
78	A	110	ILE	0	0.011	0.004	4.897	-0.300	-0.300	0.000	0.000	0.000	0.000
79	A	111	VAL	0	-0.007	-0.004	8.274	0.372	0.372	0.000	0.000	0.000	0.000
80	A	112	VAL	0	0.028	0.003	7.566	-0.408	-0.408	0.000	0.000	0.000	0.000
81	A	113	ASN	0	0.034	-0.012	8.317	0.305	0.305	0.000	0.000	0.000	0.000
82	A	114	PRO	0	0.018	0.011	10.252	0.121	0.121	0.000	0.000	0.000	0.000
83	A	115	LEU	0	-0.048	-0.035	13.721	0.113	0.113	0.000	0.000	0.000	0.000
84	A	116	ASP	-1	-0.904	-0.943	12.975	-0.385	-0.385	0.000	0.000	0.000	0.000
85	A	117	LEU	0	0.002	-0.004	15.436	0.050	0.050	0.000	0.000	0.000	0.000
86	A	118	LEU	0	-0.065	-0.027	18.161	0.033	0.033	0.000	0.000	0.000	0.000
87	A	119	GLU	-1	-1.029	-1.005	20.431	-0.117	-0.117	0.000	0.000	0.000	0.000
88	A	120	ASN	0	0.016	0.019	22.061	0.018	0.018	0.000	0.000	0.000	0.000
89	A	121	VAL	0	0.048	0.007	22.456	-0.023	-0.023	0.000	0.000	0.000	0.000
90	A	122	GLY	0	0.044	0.021	23.311	-0.019	-0.019	0.000	0.000	0.000	0.000
91	A	123	GLU	-1	-0.915	-0.957	20.473	-0.212	-0.212	0.000	0.000	0.000	0.000
92	A	124	PHE	0	-0.036	-0.017	17.036	-0.042	-0.042	0.000	0.000	0.000	0.000
93	A	125	GLN	0	-0.043	-0.032	18.978	-0.034	-0.034	0.000	0.000	0.000	0.000
94	A	126	ALA	0	0.043	0.025	21.163	-0.018	-0.018	0.000	0.000	0.000	0.000
95	A	127	TYR	0	0.070	0.046	11.402	-0.098	-0.098	0.000	0.000	0.000	0.000
96	A	128	LEU	0	-0.026	-0.026	15.386	-0.055	-0.055	0.000	0.000	0.000	0.000
97	A	129	GLU	-1	-0.975	-0.979	17.711	-0.274	-0.274	0.000	0.000	0.000	0.000
98	A	130	GLU	-1	-0.945	-0.971	17.992	-0.341	-0.341	0.000	0.000	0.000	0.000
99	A	131	LYS	1	0.871	0.936	12.003	0.740	0.740	0.000	0.000	0.000	0.000
100	A	132	LEU	0	-0.069	-0.045	16.177	-0.018	-0.018	0.000	0.000	0.000	0.000
101	A	133	ASN	0	-0.026	-0.013	18.655	0.023	0.023	0.000	0.000	0.000	0.000
102	A	134	GLU	-1	-0.865	-0.925	14.901	-0.572	-0.572	0.000	0.000	0.000	0.000
103	A	135	ILE	0	-0.002	-0.010	14.178	0.003	0.003	0.000	0.000	0.000	0.000
104	A	136	LYS	1	0.915	0.960	17.425	0.281	0.281	0.000	0.000	0.000	0.000
105	A	137	GLU	-1	-0.930	-0.963	20.371	-0.243	-0.243	0.000	0.000	0.000	0.000
106	A	138	LEU	0	0.011	0.011	15.067	0.012	0.012	0.000	0.000	0.000	0.000
107	A	139	LEU	0	-0.055	-0.037	18.300	0.028	0.028	0.000	0.000	0.000	0.000
108	A	140	GLY	0	-0.006	0.010	20.326	0.031	0.031	0.000	0.000	0.000	0.000
109	A	141	TYR	0	0.066	0.025	20.543	0.016	0.016	0.000	0.000	0.000	0.000
110	A	142	LEU	0	-0.010	-0.012	16.936	0.018	0.018	0.000	0.000	0.000	0.000
111	A	143	SER	0	-0.037	-0.039	21.628	0.025	0.025	0.000	0.000	0.000	0.000
112	A	144	GLU	-1	-0.965	-0.971	24.657	-0.165	-0.165	0.000	0.000	0.000	0.000
113	A	145	SER	0	-0.047	-0.023	23.339	0.013	0.013	0.000	0.000	0.000	0.000
114	A	146	LEU	0	-0.098	-0.044	22.641	0.010	0.010	0.000	0.000	0.000	0.000
115	A	147	SER	0	-0.080	-0.014	26.036	0.023	0.023	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:33:PHE)