FMO DATABASE

FMODB ID: VQ6R1

Calculation Name: 1KTJ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1KTJ

Chain ID: A

ChEMBL ID:

UniProt ID: P49278

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	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	126
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1043813.090617
FMO2-HF: Nuclear repulsion	993317.029714
FMO2-HF: Total energy	-50496.060903
FMO2-MP2: Total energy	-50639.277352

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:1:SER)

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

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.
-12.564	-7.717	14.484	-8.472	-10.86	-0.033

Interaction energy analysis for fragmet #1(A:1:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.018 / q_NPA : -0.021

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	3	VAL	0	-0.047	-0.016	3.798	-1.220	0.055	-0.003	-0.483	-0.788	0.002
4	A	4	ASP	-1	-0.814	-0.866	5.952	0.762	0.762	0.000	0.000	0.000	0.000
5	A	5	VAL	0	-0.067	-0.040	9.605	-0.210	-0.210	0.000	0.000	0.000	0.000
6	A	6	LYS	1	0.910	0.957	12.303	0.222	0.222	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.775	-0.882	16.025	-0.021	-0.021	0.000	0.000	0.000	0.000
8	A	8	CYS	0	-0.148	-0.082	17.545	-0.044	-0.044	0.000	0.000	0.000	0.000
9	A	9	ALA	0	-0.034	-0.019	20.664	-0.009	-0.009	0.000	0.000	0.000	0.000
10	A	10	ASN	0	-0.031	-0.012	21.638	0.011	0.011	0.000	0.000	0.000	0.000
11	A	11	HIS	0	0.010	0.017	18.069	0.042	0.042	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.758	-0.865	18.047	0.105	0.105	0.000	0.000	0.000	0.000
13	A	13	ILE	0	-0.025	-0.020	12.747	0.031	0.031	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.802	0.884	13.040	-0.237	-0.237	0.000	0.000	0.000	0.000
15	A	15	LYS	1	1.001	0.993	7.159	-1.569	-1.569	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.016	0.011	7.104	-0.029	-0.029	0.000	0.000	0.000	0.000
17	A	17	LEU	0	-0.006	0.001	2.716	-2.656	-0.432	0.657	-1.218	-1.663	0.011
18	A	18	VAL	0	0.030	0.001	2.693	-1.004	0.628	0.175	-0.712	-1.096	0.000
19	A	19	PRO	0	-0.034	-0.023	2.051	-5.473	-7.356	10.249	-4.012	-4.353	-0.023
20	A	20	GLY	0	-0.022	-0.005	2.903	2.379	1.801	0.066	0.815	-0.304	0.000
21	A	21	CYS	0	-0.072	-0.008	3.415	1.150	1.560	0.003	-0.172	-0.242	0.000
22	A	22	HIS	0	-0.024	-0.035	2.248	-6.169	-4.516	3.335	-2.637	-2.351	-0.023
23	A	23	GLY	0	0.099	0.059	4.016	0.149	0.263	0.002	-0.053	-0.063	0.000
24	A	24	SER	0	-0.052	-0.076	7.172	-0.443	-0.443	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.938	-0.941	8.380	-0.314	-0.314	0.000	0.000	0.000	0.000
26	A	26	PRO	0	-0.059	-0.040	9.389	-0.213	-0.213	0.000	0.000	0.000	0.000
27	A	28	ILE	0	-0.041	-0.038	9.508	0.204	0.204	0.000	0.000	0.000	0.000
28	A	29	ILE	0	0.044	0.026	10.768	-0.162	-0.162	0.000	0.000	0.000	0.000
29	A	30	HIS	1	0.802	0.878	12.335	1.000	1.000	0.000	0.000	0.000	0.000
30	A	31	ARG	1	0.908	0.916	15.224	0.374	0.374	0.000	0.000	0.000	0.000
31	A	32	GLY	0	-0.063	-0.030	18.369	0.021	0.021	0.000	0.000	0.000	0.000
32	A	33	LYS	1	0.910	0.967	14.421	0.683	0.683	0.000	0.000	0.000	0.000
33	A	34	PRO	0	0.049	0.022	12.446	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	35	PHE	0	-0.003	-0.004	8.385	-0.116	-0.116	0.000	0.000	0.000	0.000
35	A	36	GLN	0	-0.009	-0.010	6.519	0.122	0.122	0.000	0.000	0.000	0.000
36	A	37	LEU	0	0.011	0.012	6.064	-0.748	-0.748	0.000	0.000	0.000	0.000
37	A	38	GLU	-1	-0.826	-0.873	5.641	0.936	0.936	0.000	0.000	0.000	0.000
38	A	39	ALA	0	-0.009	0.012	7.217	-0.017	-0.017	0.000	0.000	0.000	0.000
39	A	40	VAL	0	-0.008	0.003	9.522	0.060	0.060	0.000	0.000	0.000	0.000
40	A	41	PHE	0	0.013	0.006	11.978	-0.005	-0.005	0.000	0.000	0.000	0.000
41	A	42	GLU	-1	-0.934	-0.968	15.425	0.245	0.245	0.000	0.000	0.000	0.000
42	A	43	ALA	0	-0.022	0.001	18.836	-0.029	-0.029	0.000	0.000	0.000	0.000
43	A	44	ASN	0	0.010	-0.004	21.817	0.013	0.013	0.000	0.000	0.000	0.000
44	A	45	GLN	0	-0.018	-0.032	24.452	-0.008	-0.008	0.000	0.000	0.000	0.000
45	A	46	ASN	0	-0.023	-0.012	25.979	0.010	0.010	0.000	0.000	0.000	0.000
46	A	47	THR	0	0.010	0.030	25.046	-0.007	-0.007	0.000	0.000	0.000	0.000
47	A	48	LYS	1	0.932	0.951	26.673	0.016	0.016	0.000	0.000	0.000	0.000
48	A	49	THR	0	-0.054	-0.039	26.562	-0.011	-0.011	0.000	0.000	0.000	0.000
49	A	50	ALA	0	0.083	0.014	21.418	0.013	0.013	0.000	0.000	0.000	0.000
50	A	51	LYN	0	-0.064	-0.009	22.744	-0.016	-0.016	0.000	0.000	0.000	0.000
51	A	52	ILE	0	-0.014	-0.003	17.723	0.002	0.002	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.934	-0.967	21.173	-0.156	-0.156	0.000	0.000	0.000	0.000
53	A	54	ILE	0	-0.012	-0.020	16.683	-0.017	-0.017	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.953	0.987	20.072	0.213	0.213	0.000	0.000	0.000	0.000
55	A	56	ALA	0	0.029	0.012	18.943	-0.033	-0.033	0.000	0.000	0.000	0.000
56	A	57	SER	0	-0.043	-0.005	20.445	0.040	0.040	0.000	0.000	0.000	0.000
57	A	58	ILE	0	0.012	-0.016	20.150	-0.041	-0.041	0.000	0.000	0.000	0.000
58	A	59	ASP	-1	-0.870	-0.937	22.539	-0.263	-0.263	0.000	0.000	0.000	0.000
59	A	60	GLY	0	-0.018	-0.005	24.130	0.023	0.023	0.000	0.000	0.000	0.000
60	A	61	LEU	0	-0.019	-0.014	25.836	0.019	0.019	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.967	-0.979	24.898	-0.232	-0.232	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.053	-0.027	22.058	0.011	0.011	0.000	0.000	0.000	0.000
63	A	64	ASP	-1	-0.895	-0.950	23.393	-0.283	-0.283	0.000	0.000	0.000	0.000
64	A	65	VAL	0	-0.044	-0.021	18.242	-0.036	-0.036	0.000	0.000	0.000	0.000
65	A	66	PRO	0	0.043	0.035	20.980	0.014	0.014	0.000	0.000	0.000	0.000
66	A	67	GLY	0	-0.013	-0.023	20.412	-0.042	-0.042	0.000	0.000	0.000	0.000
67	A	68	ILE	0	-0.011	-0.008	16.945	-0.046	-0.046	0.000	0.000	0.000	0.000
68	A	69	ASP	-1	-0.781	-0.841	19.589	-0.181	-0.181	0.000	0.000	0.000	0.000
69	A	70	PRO	0	0.033	0.014	20.474	-0.008	-0.008	0.000	0.000	0.000	0.000
70	A	71	ASN	0	0.046	0.034	22.619	0.021	0.021	0.000	0.000	0.000	0.000
71	A	72	ALA	0	0.068	0.017	18.554	-0.011	-0.011	0.000	0.000	0.000	0.000
72	A	73	CYS	0	-0.081	-0.012	19.556	0.027	0.027	0.000	0.000	0.000	0.000
73	A	74	HIS	0	-0.086	-0.051	21.325	0.033	0.033	0.000	0.000	0.000	0.000
74	A	75	TYR	0	-0.075	-0.072	16.343	-0.012	-0.012	0.000	0.000	0.000	0.000
75	A	76	MET	0	-0.053	-0.015	16.950	0.025	0.025	0.000	0.000	0.000	0.000
76	A	77	LYS	1	0.934	0.976	18.100	-0.095	-0.095	0.000	0.000	0.000	0.000
77	A	79	PRO	0	0.032	-0.024	24.566	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	80	LEU	0	-0.055	-0.017	21.038	0.012	0.012	0.000	0.000	0.000	0.000
79	A	81	VAL	0	0.013	0.000	24.014	-0.005	-0.005	0.000	0.000	0.000	0.000
80	A	82	LYS	1	0.971	0.974	24.188	-0.059	-0.059	0.000	0.000	0.000	0.000
81	A	83	GLY	0	-0.001	0.003	23.692	0.004	0.004	0.000	0.000	0.000	0.000
82	A	84	GLN	0	-0.040	-0.013	21.577	0.019	0.019	0.000	0.000	0.000	0.000
83	A	85	GLN	0	-0.009	-0.004	15.525	0.033	0.033	0.000	0.000	0.000	0.000
84	A	86	TYR	0	-0.020	0.002	16.542	-0.006	-0.006	0.000	0.000	0.000	0.000
85	A	87	ASH	0	-0.094	-0.108	9.384	-0.066	-0.066	0.000	0.000	0.000	0.000
86	A	88	ILE	0	0.008	0.009	11.850	-0.029	-0.029	0.000	0.000	0.000	0.000
87	A	89	LYS	1	0.933	0.969	8.205	-0.057	-0.057	0.000	0.000	0.000	0.000
88	A	90	TYR	0	0.011	0.009	10.022	0.097	0.097	0.000	0.000	0.000	0.000
89	A	91	THR	0	-0.021	-0.019	10.339	-0.277	-0.277	0.000	0.000	0.000	0.000
90	A	92	TRP	0	0.016	0.007	12.130	0.097	0.097	0.000	0.000	0.000	0.000
91	A	93	ASN	0	-0.001	-0.015	14.023	-0.102	-0.102	0.000	0.000	0.000	0.000
92	A	94	VAL	0	0.017	0.028	14.222	0.055	0.055	0.000	0.000	0.000	0.000
93	A	95	PRO	0	0.052	0.035	17.065	0.042	0.042	0.000	0.000	0.000	0.000
94	A	96	LYS	1	0.960	0.959	20.505	0.342	0.342	0.000	0.000	0.000	0.000
95	A	97	ILE	0	0.000	-0.013	22.362	0.003	0.003	0.000	0.000	0.000	0.000
96	A	98	ALA	0	0.026	0.041	20.065	0.018	0.018	0.000	0.000	0.000	0.000
97	A	99	PRO	0	0.051	0.039	22.127	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	100	LYS	1	0.880	0.935	20.805	0.312	0.312	0.000	0.000	0.000	0.000
99	A	101	SER	0	0.050	0.026	20.101	0.023	0.023	0.000	0.000	0.000	0.000
100	A	102	GLU	-1	-0.836	-0.923	18.265	-0.525	-0.525	0.000	0.000	0.000	0.000
101	A	103	ASN	0	-0.042	-0.027	18.993	-0.016	-0.016	0.000	0.000	0.000	0.000
102	A	104	VAL	0	0.023	0.024	16.491	0.017	0.017	0.000	0.000	0.000	0.000
103	A	105	VAL	0	-0.008	0.004	17.288	-0.019	-0.019	0.000	0.000	0.000	0.000
104	A	106	VAL	0	0.003	0.002	14.868	0.017	0.017	0.000	0.000	0.000	0.000
105	A	107	THR	0	-0.027	-0.019	16.527	0.018	0.018	0.000	0.000	0.000	0.000
106	A	108	VAL	0	-0.013	-0.005	15.064	-0.007	-0.007	0.000	0.000	0.000	0.000
107	A	109	LYS	1	0.948	0.962	18.004	0.204	0.204	0.000	0.000	0.000	0.000
108	A	110	VAL	0	0.018	0.019	17.978	-0.019	-0.019	0.000	0.000	0.000	0.000
109	A	111	MET	0	0.005	0.012	21.183	0.031	0.031	0.000	0.000	0.000	0.000
110	A	112	GLY	0	0.027	0.008	24.794	-0.008	-0.008	0.000	0.000	0.000	0.000
111	A	113	ASP	-1	-0.816	-0.902	26.273	-0.034	-0.034	0.000	0.000	0.000	0.000
112	A	114	ASP	-1	-0.942	-0.958	29.277	0.000	0.000	0.000	0.000	0.000	0.000
113	A	115	GLY	0	-0.001	0.000	28.749	0.006	0.006	0.000	0.000	0.000	0.000
114	A	116	VAL	0	-0.043	-0.028	23.856	-0.005	-0.005	0.000	0.000	0.000	0.000
115	A	117	LEU	0	-0.028	-0.016	21.073	0.018	0.018	0.000	0.000	0.000	0.000
116	A	118	ALA	0	0.018	0.004	17.631	0.024	0.024	0.000	0.000	0.000	0.000
117	A	120	ALA	0	0.039	0.028	14.262	0.033	0.033	0.000	0.000	0.000	0.000
118	A	121	ILE	0	-0.017	-0.016	16.386	-0.032	-0.032	0.000	0.000	0.000	0.000
119	A	122	ALA	0	0.029	0.023	12.115	0.010	0.010	0.000	0.000	0.000	0.000
120	A	123	THR	0	0.025	-0.007	13.965	0.006	0.006	0.000	0.000	0.000	0.000
121	A	124	HIS	0	0.034	0.030	10.858	0.017	0.017	0.000	0.000	0.000	0.000
122	A	125	ALA	0	0.010	0.015	12.111	-0.109	-0.109	0.000	0.000	0.000	0.000
123	A	126	LYS	1	0.897	0.963	12.993	0.635	0.635	0.000	0.000	0.000	0.000
124	A	127	ILE	0	0.007	0.023	14.575	-0.095	-0.095	0.000	0.000	0.000	0.000
125	A	128	ARG	1	0.912	0.932	16.003	0.612	0.612	0.000	0.000	0.000	0.000
126	A	129	ASP	-1	-0.863	-0.907	17.934	-0.581	-0.581	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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