FMO DATABASE

FMODB ID: K9GM3

Calculation Name: 1U78-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1U78

Chain ID: A

ChEMBL ID:

UniProt ID: P34257

Base Structure: X-ray

Registration Date: 2023-06-22

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	OptHSide
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	103
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-636289.253435
FMO2-HF: Nuclear repulsion	595078.088859
FMO2-HF: Total energy	-41211.164576
FMO2-MP2: Total energy	-41330.44829

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:PRO)

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

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.
-14.951	-8.57	1.416	-3.392	-4.406	-0.01

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.007 / q_NPA : -0.010

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	GLY	0	0.049	0.035	2.418	-1.119	1.799	0.261	-1.437	-1.742	0.004
4	A	5	SER	0	0.030	0.010	2.882	-5.950	-3.445	0.555	-1.562	-1.498	-0.017
5	A	6	ALA	0	-0.020	0.006	4.445	-0.043	0.146	-0.001	-0.014	-0.174	0.000
6	A	7	LEU	0	0.002	-0.004	5.087	0.185	0.198	-0.001	-0.002	-0.010	0.000
7	A	8	SER	0	0.019	-0.023	8.329	0.198	0.198	0.000	0.000	0.000	0.000
8	A	9	ASP	-1	-0.795	-0.905	11.148	-0.315	-0.315	0.000	0.000	0.000	0.000
9	A	10	THR	0	0.009	0.024	14.428	0.036	0.036	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.728	-0.814	10.984	-1.134	-1.134	0.000	0.000	0.000	0.000
11	A	12	ARG	1	0.785	0.886	10.462	0.450	0.450	0.000	0.000	0.000	0.000
12	A	13	ALA	0	0.087	0.052	14.128	0.048	0.048	0.000	0.000	0.000	0.000
13	A	14	GLN	0	-0.043	-0.024	16.818	-0.011	-0.011	0.000	0.000	0.000	0.000
14	A	15	LEU	0	-0.020	-0.024	12.355	0.035	0.035	0.000	0.000	0.000	0.000
15	A	16	ASP	-1	-0.820	-0.885	16.785	-0.132	-0.132	0.000	0.000	0.000	0.000
16	A	17	VAL	0	0.014	0.005	19.129	0.025	0.025	0.000	0.000	0.000	0.000
17	A	18	MET	0	0.001	-0.003	17.779	0.014	0.014	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.969	0.978	19.608	0.054	0.054	0.000	0.000	0.000	0.000
19	A	20	LEU	0	-0.013	-0.002	21.524	0.017	0.017	0.000	0.000	0.000	0.000
20	A	21	LEU	0	-0.031	0.002	24.303	0.008	0.008	0.000	0.000	0.000	0.000
21	A	22	ASN	0	-0.081	-0.040	24.611	0.006	0.006	0.000	0.000	0.000	0.000
22	A	23	VAL	0	0.011	0.024	21.568	0.000	0.000	0.000	0.000	0.000	0.000
23	A	24	SER	0	0.026	0.004	21.965	0.003	0.003	0.000	0.000	0.000	0.000
24	A	25	LEU	0	0.065	0.007	15.806	-0.018	-0.018	0.000	0.000	0.000	0.000
25	A	26	HIS	0	-0.005	-0.016	17.203	-0.064	-0.064	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.775	-0.871	18.400	-0.255	-0.255	0.000	0.000	0.000	0.000
27	A	28	MET	0	0.004	0.020	16.792	-0.032	-0.032	0.000	0.000	0.000	0.000
28	A	29	SER	0	-0.087	-0.074	13.627	-0.024	-0.024	0.000	0.000	0.000	0.000
29	A	30	ARG	1	0.884	0.913	15.196	0.163	0.163	0.000	0.000	0.000	0.000
30	A	31	LYS	1	0.873	0.938	17.881	0.224	0.224	0.000	0.000	0.000	0.000
31	A	32	ILE	0	0.035	0.021	12.823	-0.013	-0.013	0.000	0.000	0.000	0.000
32	A	33	SER	0	-0.022	0.009	13.648	-0.093	-0.093	0.000	0.000	0.000	0.000
33	A	34	ARG	1	0.818	0.883	6.533	1.653	1.653	0.000	0.000	0.000	0.000
34	A	35	SER	0	-0.003	0.009	7.565	0.183	0.183	0.000	0.000	0.000	0.000
35	A	36	ARG	1	1.039	1.005	10.391	0.181	0.181	0.000	0.000	0.000	0.000
36	A	37	HIS	0	-0.027	-0.016	6.908	-0.142	-0.142	0.000	0.000	0.000	0.000
37	A	38	CYS	0	-0.034	0.000	6.414	0.021	0.021	0.000	0.000	0.000	0.000
38	A	39	ILE	0	0.121	0.063	8.562	0.095	0.095	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.878	0.942	11.977	-0.043	-0.043	0.000	0.000	0.000	0.000
40	A	41	VAL	0	-0.023	-0.005	9.255	0.045	0.045	0.000	0.000	0.000	0.000
41	A	42	TYR	0	-0.051	-0.056	10.446	0.023	0.023	0.000	0.000	0.000	0.000
42	A	43	LEU	0	0.031	-0.001	11.882	0.027	0.027	0.000	0.000	0.000	0.000
43	A	44	LYS	1	0.831	0.909	14.982	-0.116	-0.116	0.000	0.000	0.000	0.000
44	A	45	ASP	-1	-0.827	-0.888	14.878	0.242	0.242	0.000	0.000	0.000	0.000
45	A	46	PRO	0	0.042	0.045	13.952	0.027	0.027	0.000	0.000	0.000	0.000
46	A	47	VAL	0	-0.014	-0.010	14.080	-0.010	-0.010	0.000	0.000	0.000	0.000
47	A	48	SER	0	-0.044	-0.040	13.976	0.026	0.026	0.000	0.000	0.000	0.000
48	A	49	TYR	0	0.028	-0.004	6.067	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	50	GLY	0	-0.060	-0.028	7.814	-0.069	-0.069	0.000	0.000	0.000	0.000
50	A	51	THR	0	0.031	0.021	8.795	0.039	0.039	0.000	0.000	0.000	0.000
51	A	52	SER	0	0.000	0.020	9.329	-0.048	-0.048	0.000	0.000	0.000	0.000
52	A	53	LYS	1	0.911	0.952	8.978	-0.412	-0.412	0.000	0.000	0.000	0.000
53	A	54	ARG	1	1.007	1.003	2.376	-7.294	-6.538	0.602	-0.377	-0.982	0.003
54	A	55	ALA	0	-0.024	-0.016	10.076	-0.193	-0.193	0.000	0.000	0.000	0.000
55	A	56	PRO	0	0.026	0.023	12.224	0.133	0.133	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.936	0.967	13.447	-0.351	-0.351	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.987	0.992	15.275	-0.654	-0.654	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.836	0.888	19.074	-0.229	-0.229	0.000	0.000	0.000	0.000
59	A	60	ALA	0	-0.001	-0.008	21.441	0.010	0.010	0.000	0.000	0.000	0.000
60	A	61	LEU	0	0.013	0.013	23.876	-0.011	-0.011	0.000	0.000	0.000	0.000
61	A	62	SER	0	-0.026	-0.036	26.042	0.016	0.016	0.000	0.000	0.000	0.000
62	A	63	VAL	0	0.071	0.014	27.658	-0.014	-0.014	0.000	0.000	0.000	0.000
63	A	64	ARG	1	0.938	0.985	29.634	-0.161	-0.161	0.000	0.000	0.000	0.000
64	A	65	ASP	-1	-0.756	-0.851	30.323	0.149	0.149	0.000	0.000	0.000	0.000
65	A	66	GLU	-1	-0.796	-0.886	26.615	0.164	0.164	0.000	0.000	0.000	0.000
66	A	67	ARG	1	0.990	0.992	31.099	-0.139	-0.139	0.000	0.000	0.000	0.000
67	A	68	ASN	0	-0.002	0.002	34.325	-0.011	-0.011	0.000	0.000	0.000	0.000
68	A	69	VAL	0	0.003	0.003	32.152	-0.008	-0.008	0.000	0.000	0.000	0.000
69	A	70	ILE	0	0.006	0.001	31.989	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	71	ARG	1	0.938	0.976	35.938	-0.097	-0.097	0.000	0.000	0.000	0.000
71	A	72	ALA	0	0.034	0.016	38.474	-0.005	-0.005	0.000	0.000	0.000	0.000
72	A	73	ALA	0	-0.022	-0.020	37.304	-0.005	-0.005	0.000	0.000	0.000	0.000
73	A	74	SER	0	-0.062	-0.036	38.788	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	75	ASN	0	-0.081	-0.032	40.889	-0.005	-0.005	0.000	0.000	0.000	0.000
75	A	76	SER	0	0.013	0.014	43.206	-0.004	-0.004	0.000	0.000	0.000	0.000
76	A	77	CYS	0	0.009	0.006	42.492	0.002	0.002	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.958	1.003	41.278	-0.047	-0.047	0.000	0.000	0.000	0.000
78	A	79	THR	0	-0.045	-0.069	39.178	0.001	0.001	0.000	0.000	0.000	0.000
79	A	80	ALA	0	0.026	-0.006	33.867	0.004	0.004	0.000	0.000	0.000	0.000
80	A	81	ARG	1	0.922	0.951	35.628	-0.032	-0.032	0.000	0.000	0.000	0.000
81	A	82	ASP	-1	-0.755	-0.836	36.703	0.041	0.041	0.000	0.000	0.000	0.000
82	A	83	ILE	0	0.071	0.038	35.763	0.005	0.005	0.000	0.000	0.000	0.000
83	A	84	ARG	1	0.830	0.926	31.050	-0.072	-0.072	0.000	0.000	0.000	0.000
84	A	85	ASN	0	-0.008	-0.020	35.284	0.009	0.009	0.000	0.000	0.000	0.000
85	A	86	GLU	-1	-0.900	-0.930	38.102	0.060	0.060	0.000	0.000	0.000	0.000
86	A	87	LEU	0	-0.038	-0.029	36.054	0.003	0.003	0.000	0.000	0.000	0.000
87	A	88	GLN	0	-0.004	-0.002	36.124	0.008	0.008	0.000	0.000	0.000	0.000
88	A	89	LEU	0	0.027	0.007	31.679	0.007	0.007	0.000	0.000	0.000	0.000
89	A	90	SER	0	-0.100	-0.040	29.827	0.012	0.012	0.000	0.000	0.000	0.000
90	A	91	ALA	0	0.073	0.044	27.217	0.011	0.011	0.000	0.000	0.000	0.000
91	A	92	SER	0	0.026	0.003	25.924	-0.011	-0.011	0.000	0.000	0.000	0.000
92	A	93	LYS	1	1.051	1.012	28.435	-0.019	-0.019	0.000	0.000	0.000	0.000
93	A	94	ARG	1	0.931	0.959	26.878	-0.025	-0.025	0.000	0.000	0.000	0.000
94	A	95	THR	0	0.008	-0.009	25.163	0.004	0.004	0.000	0.000	0.000	0.000
95	A	96	ILE	0	0.047	0.034	27.082	0.005	0.005	0.000	0.000	0.000	0.000
96	A	97	LEU	0	0.022	0.010	30.486	0.000	0.000	0.000	0.000	0.000	0.000
97	A	98	ASN	0	-0.033	-0.014	24.693	-0.013	-0.013	0.000	0.000	0.000	0.000
98	A	99	VAL	0	-0.040	-0.012	27.653	0.003	0.003	0.000	0.000	0.000	0.000
99	A	100	ILE	0	0.048	0.010	29.166	0.000	0.000	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.961	0.985	28.742	-0.030	-0.030	0.000	0.000	0.000	0.000
101	A	102	ARG	1	0.891	0.943	23.407	-0.134	-0.134	0.000	0.000	0.000	0.000
102	A	103	SER	0	-0.035	-0.005	29.290	0.008	0.008	0.000	0.000	0.000	0.000
103	A	104	GLY	0	0.016	0.031	32.332	-0.005	-0.005	0.000	0.000	0.000	0.000

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