FMO DATABASE

FMODB ID: NNNQQ

Calculation Name: 1KHI-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1KHI

Chain ID: A

ChEMBL ID:

UniProt ID: P87252

Base Structure: X-ray

Registration Date: 2023-09-21

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	147
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1254964.837646
FMO2-HF: Nuclear repulsion	1197768.173392
FMO2-HF: Total energy	-57196.664254
FMO2-MP2: Total energy	-57361.062155

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:27:GLY)

Summations of interaction energy for fragment #1(A:27: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.
-1.087	1.142	0.599	-1.24	-1.587	0

Interaction energy analysis for fragmet #1(A:27:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.004 / q_NPA : -0.013

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	29	ALA	0	0.047	0.019	3.797	-1.660	-0.636	-0.006	-0.568	-0.449	0.002
4	A	30	SER	0	0.003	-0.016	6.537	0.247	0.247	0.000	0.000	0.000	0.000
5	A	31	GLN	0	-0.065	-0.016	7.758	0.213	0.213	0.000	0.000	0.000	0.000
6	A	32	THR	0	-0.006	-0.012	9.768	-0.006	-0.006	0.000	0.000	0.000	0.000
7	A	33	VAL	0	0.022	0.019	13.432	0.055	0.055	0.000	0.000	0.000	0.000
8	A	34	THR	0	0.004	-0.007	17.078	-0.024	-0.024	0.000	0.000	0.000	0.000
9	A	35	ILE	0	0.012	0.011	20.071	0.018	0.018	0.000	0.000	0.000	0.000
10	A	36	PRO	0	0.021	0.000	22.644	-0.005	-0.005	0.000	0.000	0.000	0.000
11	A	37	CYS	0	0.030	0.034	26.060	-0.007	-0.007	0.000	0.000	0.000	0.000
12	A	38	HIS	0	-0.024	0.001	27.266	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	39	HIS	0	-0.094	-0.059	26.653	0.010	0.010	0.000	0.000	0.000	0.000
14	A	40	ILE	0	-0.008	0.023	23.368	-0.005	-0.005	0.000	0.000	0.000	0.000
15	A	41	ARG	1	0.894	0.940	26.125	0.096	0.096	0.000	0.000	0.000	0.000
16	A	42	LEU	0	-0.015	-0.011	25.908	-0.011	-0.011	0.000	0.000	0.000	0.000
17	A	43	GLY	0	-0.015	-0.007	24.690	0.008	0.008	0.000	0.000	0.000	0.000
18	A	44	ASP	-1	-0.822	-0.892	22.240	-0.147	-0.147	0.000	0.000	0.000	0.000
19	A	45	ILE	0	-0.026	-0.027	15.828	-0.017	-0.017	0.000	0.000	0.000	0.000
20	A	46	LEU	0	-0.017	-0.014	17.858	0.015	0.015	0.000	0.000	0.000	0.000
21	A	47	ILE	0	-0.037	-0.008	12.470	-0.038	-0.038	0.000	0.000	0.000	0.000
22	A	48	LEU	0	-0.008	-0.009	15.653	0.045	0.045	0.000	0.000	0.000	0.000
23	A	49	GLN	0	0.035	-0.012	16.564	-0.053	-0.053	0.000	0.000	0.000	0.000
24	A	50	GLY	0	-0.015	-0.008	13.483	-0.038	-0.038	0.000	0.000	0.000	0.000
25	A	51	ARG	1	0.874	0.951	11.634	0.364	0.364	0.000	0.000	0.000	0.000
26	A	52	PRO	0	0.028	0.019	10.915	0.110	0.110	0.000	0.000	0.000	0.000
27	A	53	CYS	0	-0.051	-0.003	13.944	0.001	0.001	0.000	0.000	0.000	0.000
28	A	54	GLN	0	0.002	0.018	17.578	0.011	0.011	0.000	0.000	0.000	0.000
29	A	55	VAL	0	-0.003	-0.001	20.604	0.004	0.004	0.000	0.000	0.000	0.000
30	A	56	ILE	0	-0.008	-0.017	23.392	0.014	0.014	0.000	0.000	0.000	0.000
31	A	57	ARG	1	0.950	0.964	26.516	0.129	0.129	0.000	0.000	0.000	0.000
32	A	58	ILE	0	0.040	0.037	27.273	-0.011	-0.011	0.000	0.000	0.000	0.000
33	A	59	SER	0	-0.093	-0.039	29.326	0.009	0.009	0.000	0.000	0.000	0.000
34	A	60	THR	0	0.054	0.027	31.033	-0.003	-0.003	0.000	0.000	0.000	0.000
35	A	61	SER	0	-0.051	-0.018	31.419	0.002	0.002	0.000	0.000	0.000	0.000
36	A	62	ALA	0	0.034	0.000	33.354	0.005	0.005	0.000	0.000	0.000	0.000
37	A	63	ALA	0	-0.012	-0.002	34.436	0.004	0.004	0.000	0.000	0.000	0.000
38	A	64	THR	0	0.004	0.003	31.251	0.003	0.003	0.000	0.000	0.000	0.000
39	A	65	GLY	0	0.028	0.023	34.401	0.003	0.003	0.000	0.000	0.000	0.000
40	A	66	GLN	0	-0.086	-0.044	28.314	0.008	0.008	0.000	0.000	0.000	0.000
41	A	67	HIS	0	0.012	0.014	28.176	-0.003	-0.003	0.000	0.000	0.000	0.000
42	A	68	ARG	1	0.962	0.976	27.109	0.119	0.119	0.000	0.000	0.000	0.000
43	A	69	TYR	0	0.009	-0.019	23.394	0.011	0.011	0.000	0.000	0.000	0.000
44	A	70	LEU	0	0.044	0.030	24.168	-0.012	-0.012	0.000	0.000	0.000	0.000
45	A	71	GLY	0	0.031	-0.005	21.483	0.011	0.011	0.000	0.000	0.000	0.000
46	A	72	VAL	0	-0.028	-0.002	20.199	-0.008	-0.008	0.000	0.000	0.000	0.000
47	A	73	ASP	-1	-0.778	-0.898	14.776	-0.584	-0.584	0.000	0.000	0.000	0.000
48	A	74	LEU	0	0.009	-0.014	14.232	0.026	0.026	0.000	0.000	0.000	0.000
49	A	75	PHE	0	-0.022	-0.014	9.894	0.000	0.000	0.000	0.000	0.000	0.000
50	A	76	THR	0	-0.018	-0.025	14.550	0.054	0.054	0.000	0.000	0.000	0.000
51	A	77	LYS	1	0.862	0.928	16.921	0.341	0.341	0.000	0.000	0.000	0.000
52	A	78	GLN	0	-0.009	0.012	18.966	0.044	0.044	0.000	0.000	0.000	0.000
53	A	79	LEU	0	0.003	0.000	20.186	-0.012	-0.012	0.000	0.000	0.000	0.000
54	A	80	HIS	0	-0.006	0.000	18.074	-0.037	-0.037	0.000	0.000	0.000	0.000
55	A	81	GLU	-1	-0.920	-0.975	21.335	-0.149	-0.149	0.000	0.000	0.000	0.000
56	A	82	GLU	-1	-0.868	-0.921	19.020	-0.301	-0.301	0.000	0.000	0.000	0.000
57	A	83	SER	0	-0.061	-0.029	22.916	0.016	0.016	0.000	0.000	0.000	0.000
58	A	84	SER	0	0.015	0.011	24.003	-0.010	-0.010	0.000	0.000	0.000	0.000
59	A	85	PHE	0	0.031	-0.006	22.031	0.006	0.006	0.000	0.000	0.000	0.000
60	A	86	VAL	0	-0.033	-0.014	27.123	0.000	0.000	0.000	0.000	0.000	0.000
61	A	87	SER	0	0.002	0.020	26.727	0.003	0.003	0.000	0.000	0.000	0.000
62	A	88	ASN	0	0.014	-0.020	28.871	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	89	PRO	0	-0.015	0.008	28.227	0.005	0.005	0.000	0.000	0.000	0.000
64	A	90	ALA	0	0.053	0.026	30.482	0.005	0.005	0.000	0.000	0.000	0.000
65	A	91	PRO	0	0.042	0.006	34.040	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	92	SER	0	-0.008	-0.011	37.570	0.000	0.000	0.000	0.000	0.000	0.000
67	A	93	VAL	0	-0.034	0.006	31.917	-0.002	-0.002	0.000	0.000	0.000	0.000
68	A	94	VAL	0	-0.001	0.003	32.411	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	95	VAL	0	-0.034	-0.011	26.997	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	96	GLN	0	0.079	0.028	27.561	-0.011	-0.011	0.000	0.000	0.000	0.000
71	A	97	THR	0	-0.066	-0.063	23.067	0.001	0.001	0.000	0.000	0.000	0.000
72	A	98	MET	0	0.079	0.050	20.584	0.001	0.001	0.000	0.000	0.000	0.000
73	A	99	LEU	0	0.008	0.011	15.106	0.014	0.014	0.000	0.000	0.000	0.000
74	A	100	GLY	0	0.056	0.032	16.845	-0.019	-0.019	0.000	0.000	0.000	0.000
75	A	101	PRO	0	-0.010	-0.010	12.421	-0.004	-0.004	0.000	0.000	0.000	0.000
76	A	102	VAL	0	-0.019	0.005	11.968	0.056	0.056	0.000	0.000	0.000	0.000
77	A	103	PHE	0	-0.015	-0.007	11.916	-0.032	-0.032	0.000	0.000	0.000	0.000
78	A	104	LYS	1	0.972	0.992	7.741	-0.187	-0.187	0.000	0.000	0.000	0.000
79	A	105	GLN	0	0.041	0.013	13.652	-0.022	-0.022	0.000	0.000	0.000	0.000
80	A	106	TYR	0	-0.074	-0.043	9.676	0.062	0.062	0.000	0.000	0.000	0.000
81	A	107	ARG	1	0.939	0.951	16.753	-0.044	-0.044	0.000	0.000	0.000	0.000
82	A	108	VAL	0	0.036	0.022	19.094	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	109	LEU	0	-0.045	-0.033	20.470	0.007	0.007	0.000	0.000	0.000	0.000
84	A	110	ASP	-1	-0.884	-0.960	22.257	-0.035	-0.035	0.000	0.000	0.000	0.000
85	A	111	MET	0	-0.102	-0.027	22.213	-0.008	-0.008	0.000	0.000	0.000	0.000
86	A	112	GLN	0	0.059	0.036	22.923	0.010	0.010	0.000	0.000	0.000	0.000
87	A	113	ASP	-1	-0.908	-0.959	22.946	-0.092	-0.092	0.000	0.000	0.000	0.000
88	A	114	GLY	0	-0.009	0.011	22.337	-0.010	-0.010	0.000	0.000	0.000	0.000
89	A	115	SER	0	-0.084	-0.033	17.920	-0.017	-0.017	0.000	0.000	0.000	0.000
90	A	116	ILE	0	0.000	-0.016	17.699	0.017	0.017	0.000	0.000	0.000	0.000
91	A	117	VAL	0	0.005	0.024	17.821	-0.009	-0.009	0.000	0.000	0.000	0.000
92	A	118	ALA	0	-0.009	-0.017	15.330	0.004	0.004	0.000	0.000	0.000	0.000
93	A	119	MET	0	-0.023	0.010	16.497	0.013	0.013	0.000	0.000	0.000	0.000
94	A	120	THR	0	-0.029	-0.017	12.109	-0.011	-0.011	0.000	0.000	0.000	0.000
95	A	121	GLU	-1	-0.958	-0.988	15.379	0.097	0.097	0.000	0.000	0.000	0.000
96	A	122	THR	0	-0.044	-0.030	15.179	0.011	0.011	0.000	0.000	0.000	0.000
97	A	123	GLY	0	0.019	0.003	17.474	0.008	0.008	0.000	0.000	0.000	0.000
98	A	124	ASP	-1	-0.932	-0.956	11.499	0.228	0.228	0.000	0.000	0.000	0.000
99	A	125	VAL	0	0.040	0.011	15.122	-0.029	-0.029	0.000	0.000	0.000	0.000
100	A	126	LYS	1	0.875	0.948	8.757	-0.105	-0.105	0.000	0.000	0.000	0.000
101	A	127	GLN	0	0.038	0.007	14.250	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	128	ASN	0	-0.007	-0.007	15.234	0.008	0.008	0.000	0.000	0.000	0.000
103	A	129	LEU	0	0.000	0.013	12.226	-0.037	-0.037	0.000	0.000	0.000	0.000
104	A	130	PRO	0	0.041	0.020	12.755	0.025	0.025	0.000	0.000	0.000	0.000
105	A	131	VAL	0	0.016	-0.002	15.521	-0.006	-0.006	0.000	0.000	0.000	0.000
106	A	132	ILE	0	-0.017	-0.002	17.104	-0.005	-0.005	0.000	0.000	0.000	0.000
107	A	133	ASP	-1	-0.925	-0.956	18.656	-0.134	-0.134	0.000	0.000	0.000	0.000
108	A	134	GLN	0	0.030	-0.003	21.719	0.015	0.015	0.000	0.000	0.000	0.000
109	A	135	SER	0	0.006	0.001	23.450	0.010	0.010	0.000	0.000	0.000	0.000
110	A	136	SER	0	0.014	0.005	26.552	0.009	0.009	0.000	0.000	0.000	0.000
111	A	137	LEU	0	-0.006	0.007	19.891	0.012	0.012	0.000	0.000	0.000	0.000
112	A	138	TRP	0	0.080	0.043	21.523	0.005	0.005	0.000	0.000	0.000	0.000
113	A	139	ASN	0	0.047	0.014	24.645	0.010	0.010	0.000	0.000	0.000	0.000
114	A	140	ARG	1	0.842	0.928	24.377	0.116	0.116	0.000	0.000	0.000	0.000
115	A	141	LEU	0	0.035	0.004	21.241	0.008	0.008	0.000	0.000	0.000	0.000
116	A	142	GLN	0	0.043	0.012	25.536	0.005	0.005	0.000	0.000	0.000	0.000
117	A	143	LYS	1	0.983	0.997	27.664	0.059	0.059	0.000	0.000	0.000	0.000
118	A	144	ALA	0	-0.023	-0.017	27.372	0.006	0.006	0.000	0.000	0.000	0.000
119	A	145	PHE	0	0.012	0.000	25.449	0.007	0.007	0.000	0.000	0.000	0.000
120	A	146	GLU	-1	-0.983	-1.009	28.050	-0.040	-0.040	0.000	0.000	0.000	0.000
121	A	147	SER	0	-0.064	-0.018	31.239	0.004	0.004	0.000	0.000	0.000	0.000
122	A	148	GLY	0	0.067	0.031	31.001	0.003	0.003	0.000	0.000	0.000	0.000
123	A	149	ARG	1	0.950	1.025	27.286	0.028	0.028	0.000	0.000	0.000	0.000
124	A	150	GLY	0	0.038	0.033	25.990	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	151	SER	0	-0.082	-0.059	26.083	0.004	0.004	0.000	0.000	0.000	0.000
126	A	152	VAL	0	0.033	0.031	23.321	-0.003	-0.003	0.000	0.000	0.000	0.000
127	A	153	ARG	1	0.837	0.916	20.491	0.015	0.015	0.000	0.000	0.000	0.000
128	A	154	VAL	0	0.034	0.018	16.649	-0.008	-0.008	0.000	0.000	0.000	0.000
129	A	155	LEU	0	-0.022	-0.015	16.687	0.016	0.016	0.000	0.000	0.000	0.000
130	A	156	VAL	0	-0.019	-0.023	10.695	-0.024	-0.024	0.000	0.000	0.000	0.000
131	A	157	VAL	0	0.026	0.024	10.108	0.019	0.019	0.000	0.000	0.000	0.000
132	A	158	SER	0	-0.010	-0.026	5.802	0.041	0.041	0.000	0.000	0.000	0.000
133	A	159	ASP	-1	-0.833	-0.935	5.960	-1.466	-1.466	0.000	0.000	0.000	0.000
134	A	160	HIS	0	-0.025	-0.012	3.844	0.051	0.356	0.007	-0.137	-0.175	0.000
135	A	161	GLY	0	-0.025	-0.007	2.529	-0.323	0.465	0.572	-0.577	-0.784	-0.002
136	A	162	ARG	1	0.895	0.967	3.530	1.870	1.982	0.026	0.042	-0.179	0.000
137	A	163	GLU	-1	-0.806	-0.894	6.656	-0.089	-0.089	0.000	0.000	0.000	0.000
138	A	164	MET	0	-0.034	-0.011	8.965	0.027	0.027	0.000	0.000	0.000	0.000
139	A	165	ALA	0	0.006	0.019	12.642	0.006	0.006	0.000	0.000	0.000	0.000
140	A	166	VAL	0	-0.014	-0.033	14.652	-0.010	-0.010	0.000	0.000	0.000	0.000
141	A	167	ASP	-1	-0.824	-0.908	17.326	-0.115	-0.115	0.000	0.000	0.000	0.000
142	A	168	MET	0	-0.092	-0.038	19.566	0.002	0.002	0.000	0.000	0.000	0.000
143	A	169	LYS	1	0.860	0.925	22.060	0.038	0.038	0.000	0.000	0.000	0.000
144	A	170	VAL	0	0.006	0.017	24.088	0.005	0.005	0.000	0.000	0.000	0.000
145	A	171	VAL	0	-0.084	-0.070	24.754	0.001	0.001	0.000	0.000	0.000	0.000
146	A	172	HIS	0	0.043	0.007	25.899	-0.002	-0.002	0.000	0.000	0.000	0.000
147	A	173	GLY	0	0.032	0.043	29.886	0.004	0.004	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:27:GLY)