FMO DATABASE

FMODB ID: JMZ19

Calculation Name: 2IFT-A-Xray311

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2IFT

Chain ID: A

ChEMBL ID:

UniProt ID: P44869

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	180
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1981714.933702
FMO2-HF: Nuclear repulsion	1911272.750099
FMO2-HF: Total energy	-70442.183603
FMO2-MP2: Total energy	-70650.663333

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:10:ACE )

Summations of interaction energy for fragment #1(A:10:ACE )

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.
0.798	1.706	-0.002	-0.423	-0.482	0

Interaction energy analysis for fragmet #1(A:10:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.012 / q_NPA : -0.006

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].
3	A	12	GLU	-1	-0.858	-0.926	3.845	0.633	1.409	-0.005	-0.342	-0.428
4	A	13	VAL	0	0.044	0.022	7.259	0.037	0.037	0.000	0.000	0.000
5	A	14	ARG	1	0.854	0.914	10.873	0.320	0.320	0.000	0.000	0.000
6	A	15	ILE	0	0.022	0.033	13.657	-0.001	-0.001	0.000	0.000	0.000
7	A	16	ILE	0	0.025	0.028	17.172	0.024	0.024	0.000	0.000	0.000
8	A	17	ALA	0	-0.036	-0.037	19.723	0.026	0.026	0.000	0.000	0.000
9	A	18	GLY	0	0.065	0.078	22.346	-0.007	-0.007	0.000	0.000	0.000
10	A	19	LEU	0	-0.011	-0.014	24.262	0.001	0.001	0.000	0.000	0.000
11	A	20	TRP	0	-0.025	-0.019	19.271	0.003	0.003	0.000	0.000	0.000
12	A	21	ARG	1	0.902	0.984	19.131	0.108	0.108	0.000	0.000	0.000
13	A	22	GLY	0	-0.028	-0.025	17.883	0.020	0.020	0.000	0.000	0.000
14	A	23	ARG	1	0.953	0.986	14.804	0.100	0.100	0.000	0.000	0.000
15	A	24	LYS	1	0.824	0.897	9.476	0.291	0.291	0.000	0.000	0.000
16	A	25	LEU	0	-0.036	-0.015	10.947	0.089	0.089	0.000	0.000	0.000
17	A	26	PRO	0	0.009	0.019	6.921	-0.183	-0.183	0.000	0.000	0.000
18	A	27	VAL	0	0.013	0.015	5.606	0.200	0.200	0.000	0.000	0.000
19	A	28	LEU	0	-0.018	-0.010	4.197	-0.538	-0.549	0.001	-0.031	0.041
20	A	29	NME	0	0.037	0.038	3.924	0.341	0.484	0.002	-0.050	-0.095
21	A	37	ACE	0	0.037	-0.041	18.193	-0.003	-0.003	0.000	0.000	0.000
22	A	38	ASP	-1	-0.787	-0.871	19.168	-0.175	-0.175	0.000	0.000	0.000
23	A	39	ARG	1	0.858	0.892	22.495	0.168	0.168	0.000	0.000	0.000
24	A	40	VAL	0	-0.024	-0.023	25.952	0.011	0.011	0.000	0.000	0.000
25	A	41	LYN	0	0.092	0.089	19.352	-0.001	-0.001	0.000	0.000	0.000
26	A	42	GLU	-1	-0.859	-0.922	24.183	-0.152	-0.152	0.000	0.000	0.000
27	A	43	THR	0	-0.064	-0.032	26.507	0.012	0.012	0.000	0.000	0.000
28	A	44	LEU	0	0.017	0.031	25.794	0.009	0.009	0.000	0.000	0.000
29	A	45	PHE	0	0.052	0.000	22.702	0.010	0.010	0.000	0.000	0.000
30	A	46	ASN	0	-0.058	-0.027	28.300	0.004	0.004	0.000	0.000	0.000
31	A	47	TRP	0	-0.021	-0.025	31.250	0.006	0.006	0.000	0.000	0.000
32	A	48	LEU	0	0.063	0.043	28.463	0.005	0.005	0.000	0.000	0.000
33	A	49	MET	0	-0.059	-0.007	30.081	0.003	0.003	0.000	0.000	0.000
34	A	50	PRO	0	-0.051	-0.016	32.436	0.004	0.004	0.000	0.000	0.000
35	A	51	TYR	0	0.037	0.001	34.591	0.005	0.005	0.000	0.000	0.000
36	A	52	ILE	0	-0.030	-0.005	27.542	0.001	0.001	0.000	0.000	0.000
37	A	53	HIS	0	0.072	0.039	31.077	0.000	0.000	0.000	0.000	0.000
38	A	54	GLN	0	-0.100	-0.060	32.694	0.006	0.006	0.000	0.000	0.000
39	A	55	SER	0	-0.060	-0.017	30.473	-0.001	-0.001	0.000	0.000	0.000
40	A	56	GLU	-1	-0.944	-0.986	29.631	-0.067	-0.067	0.000	0.000	0.000
41	A	57	CYS	0	-0.044	-0.036	25.471	-0.003	-0.003	0.000	0.000	0.000
42	A	58	LEU	0	0.018	0.021	24.619	0.003	0.003	0.000	0.000	0.000
43	A	59	ASP	-1	-0.875	-0.944	18.948	-0.241	-0.241	0.000	0.000	0.000
44	A	60	GLY	0	0.002	-0.012	21.529	0.001	0.001	0.000	0.000	0.000
45	A	61	PHE	0	0.009	-0.001	19.181	0.020	0.020	0.000	0.000	0.000
46	A	62	ALA	0	0.044	0.040	16.696	-0.025	-0.025	0.000	0.000	0.000
47	A	63	GLY	0	0.080	0.049	13.565	-0.044	-0.044	0.000	0.000	0.000
48	A	64	SER	0	-0.071	-0.055	10.380	0.008	0.008	0.000	0.000	0.000
49	A	65	GLY	0	0.055	0.025	11.758	0.032	0.032	0.000	0.000	0.000
50	A	66	SER	0	-0.032	-0.019	13.847	0.037	0.037	0.000	0.000	0.000
51	A	67	LEU	0	0.059	0.039	15.388	0.038	0.038	0.000	0.000	0.000
52	A	68	GLY	0	0.086	0.040	18.768	0.027	0.027	0.000	0.000	0.000
53	A	69	PHE	0	-0.012	-0.036	13.611	0.030	0.030	0.000	0.000	0.000
54	A	70	GLU	-1	-0.825	-0.898	18.583	-0.199	-0.199	0.000	0.000	0.000
55	A	71	ALA	0	0.031	0.003	20.306	0.022	0.022	0.000	0.000	0.000
56	A	72	LEU	0	-0.028	-0.010	20.078	0.015	0.015	0.000	0.000	0.000
57	A	73	SER	0	-0.068	-0.072	20.822	0.020	0.020	0.000	0.000	0.000
58	A	74	ARG	1	0.808	0.895	22.732	0.164	0.164	0.000	0.000	0.000
59	A	75	GLN	0	-0.040	-0.024	25.820	0.007	0.007	0.000	0.000	0.000
60	A	76	ALA	0	0.022	0.021	26.411	0.006	0.006	0.000	0.000	0.000
61	A	77	LYS	1	0.906	0.984	28.166	0.057	0.057	0.000	0.000	0.000
62	A	78	LYS	1	0.946	0.958	27.270	0.069	0.069	0.000	0.000	0.000
63	A	79	VAL	0	-0.018	0.023	21.790	-0.005	-0.005	0.000	0.000	0.000
64	A	80	THR	0	0.006	0.004	24.148	0.008	0.008	0.000	0.000	0.000
65	A	81	PHE	0	-0.035	-0.040	17.999	-0.010	-0.010	0.000	0.000	0.000
66	A	82	LEU	0	-0.004	0.012	21.079	0.015	0.015	0.000	0.000	0.000
67	A	83	GLU	-1	-0.854	-0.942	15.597	-0.249	-0.249	0.000	0.000	0.000
68	A	84	LEU	0	-0.002	0.005	18.958	0.020	0.020	0.000	0.000	0.000
69	A	85	ASP	-1	-0.814	-0.900	14.280	-0.101	-0.101	0.000	0.000	0.000
70	A	86	LYS	1	0.928	0.941	15.917	0.002	0.002	0.000	0.000	0.000
71	A	87	THR	0	-0.043	-0.033	10.725	0.029	0.029	0.000	0.000	0.000
72	A	88	VAL	0	0.015	0.018	10.919	-0.006	-0.006	0.000	0.000	0.000
73	A	89	ALA	0	0.041	0.022	12.506	-0.011	-0.011	0.000	0.000	0.000
74	A	90	ASN	0	-0.022	-0.012	13.959	0.009	0.009	0.000	0.000	0.000
75	A	91	GLN	0	-0.029	-0.005	8.782	0.103	0.103	0.000	0.000	0.000
76	A	92	LEU	0	0.027	0.019	12.024	0.010	0.010	0.000	0.000	0.000
77	A	93	LYS	1	0.987	0.990	14.534	0.068	0.068	0.000	0.000	0.000
78	A	94	LYS	1	0.963	0.987	10.596	-0.060	-0.060	0.000	0.000	0.000
79	A	95	ASN	0	0.017	-0.007	10.571	0.061	0.061	0.000	0.000	0.000
80	A	96	LEU	0	0.026	0.014	14.566	0.009	0.009	0.000	0.000	0.000
81	A	97	GLN	0	-0.081	-0.020	17.294	0.015	0.015	0.000	0.000	0.000
82	A	98	THR	0	-0.077	-0.032	14.525	0.014	0.014	0.000	0.000	0.000
83	A	99	LEU	0	-0.063	-0.037	16.275	0.007	0.007	0.000	0.000	0.000
84	A	100	LYS	1	0.906	0.946	19.239	0.037	0.037	0.000	0.000	0.000
85	A	101	CYS	0	0.023	0.027	21.451	-0.007	-0.007	0.000	0.000	0.000
86	A	102	SER	0	-0.022	-0.004	23.848	0.003	0.003	0.000	0.000	0.000
87	A	103	SER	0	0.042	-0.004	25.846	-0.006	-0.006	0.000	0.000	0.000
88	A	104	GLU	-1	-0.905	-0.938	27.054	-0.044	-0.044	0.000	0.000	0.000
89	A	105	GLN	0	-0.039	-0.006	25.444	0.003	0.003	0.000	0.000	0.000
90	A	106	ALA	0	-0.015	-0.019	21.886	-0.011	-0.011	0.000	0.000	0.000
91	A	107	GLU	-1	-0.920	-0.955	23.714	-0.055	-0.055	0.000	0.000	0.000
92	A	108	VAL	0	-0.050	-0.016	18.533	-0.011	-0.011	0.000	0.000	0.000
93	A	109	ILE	0	-0.004	0.005	21.577	0.015	0.015	0.000	0.000	0.000
94	A	110	ASN	0	-0.046	-0.035	19.914	-0.018	-0.018	0.000	0.000	0.000
95	A	111	GLN	0	0.026	0.003	21.791	0.012	0.012	0.000	0.000	0.000
96	A	112	SER	0	0.065	0.050	22.507	-0.016	-0.016	0.000	0.000	0.000
97	A	113	SER	0	0.039	-0.024	23.593	0.014	0.014	0.000	0.000	0.000
98	A	114	LEU	0	-0.031	-0.008	25.532	0.006	0.006	0.000	0.000	0.000
99	A	115	ASP	-1	-0.902	-0.961	27.345	-0.057	-0.057	0.000	0.000	0.000
100	A	116	PHE	0	-0.006	-0.009	27.006	0.005	0.005	0.000	0.000	0.000
101	A	117	LEU	0	-0.013	-0.015	28.081	0.004	0.004	0.000	0.000	0.000
102	A	118	LYS	1	0.919	0.978	30.870	0.064	0.064	0.000	0.000	0.000
103	A	119	GLN	0	-0.002	0.021	33.246	0.003	0.003	0.000	0.000	0.000
104	A	120	PRO	0	0.019	0.016	35.144	-0.002	-0.002	0.000	0.000	0.000
105	A	121	GLN	0	-0.080	-0.044	34.668	0.004	0.004	0.000	0.000	0.000
106	A	122	ASN	0	0.018	0.006	37.890	0.001	0.001	0.000	0.000	0.000
107	A	123	GLN	0	-0.034	-0.013	38.990	0.003	0.003	0.000	0.000	0.000
108	A	124	PRO	0	0.048	0.046	36.729	-0.002	-0.002	0.000	0.000	0.000
109	A	125	HIS	1	0.784	0.869	31.906	0.060	0.060	0.000	0.000	0.000
110	A	126	PHE	0	-0.009	-0.005	28.443	-0.002	-0.002	0.000	0.000	0.000
111	A	127	ASP	-1	-0.804	-0.897	31.603	-0.067	-0.067	0.000	0.000	0.000
112	A	128	VAL	0	-0.004	-0.019	27.053	-0.001	-0.001	0.000	0.000	0.000
113	A	129	VAL	0	0.016	0.017	26.810	-0.002	-0.002	0.000	0.000	0.000
114	A	130	PHE	0	-0.031	-0.012	22.282	-0.001	-0.001	0.000	0.000	0.000
115	A	131	LEU	0	-0.012	-0.017	23.373	-0.002	-0.002	0.000	0.000	0.000
116	A	132	ASP	-1	-0.889	-0.954	18.143	-0.268	-0.268	0.000	0.000	0.000
117	A	133	PRO	0	-0.018	0.015	19.403	-0.022	-0.022	0.000	0.000	0.000
118	A	134	PRO	0	0.012	-0.008	17.915	-0.001	-0.001	0.000	0.000	0.000
119	A	135	PHE	0	0.019	0.006	20.177	0.020	0.020	0.000	0.000	0.000
120	A	136	HIS	0	-0.055	-0.045	21.925	0.006	0.006	0.000	0.000	0.000
121	A	137	PHE	0	0.030	0.024	23.287	0.011	0.011	0.000	0.000	0.000
122	A	138	ASN	0	0.006	-0.002	26.862	0.000	0.000	0.000	0.000	0.000
123	A	139	LEU	0	0.028	0.017	23.138	0.006	0.006	0.000	0.000	0.000
124	A	140	ALA	0	0.046	0.018	25.747	0.003	0.003	0.000	0.000	0.000
125	A	141	GLU	-1	-0.876	-0.942	27.204	-0.081	-0.081	0.000	0.000	0.000
126	A	142	GLN	0	-0.043	-0.027	29.074	0.009	0.009	0.000	0.000	0.000
127	A	143	ALA	0	0.002	-0.002	27.362	0.005	0.005	0.000	0.000	0.000
128	A	144	ILE	0	-0.010	0.003	29.494	0.003	0.003	0.000	0.000	0.000
129	A	145	SER	0	0.011	0.011	31.888	0.005	0.005	0.000	0.000	0.000
130	A	146	LEU	0	0.024	0.014	30.607	0.004	0.004	0.000	0.000	0.000
131	A	147	LEU	0	-0.060	-0.025	29.435	0.003	0.003	0.000	0.000	0.000
132	A	148	CYS	0	-0.043	-0.022	33.344	0.004	0.004	0.000	0.000	0.000
133	A	149	GLU	-1	-0.940	-0.973	36.801	-0.051	-0.051	0.000	0.000	0.000
134	A	150	ASN	0	-0.066	-0.035	34.864	0.007	0.007	0.000	0.000	0.000
135	A	151	ASN	0	-0.018	-0.010	36.983	-0.001	-0.001	0.000	0.000	0.000
136	A	152	TRP	0	0.033	0.012	31.643	-0.001	-0.001	0.000	0.000	0.000
137	A	153	LEU	0	-0.027	-0.007	31.909	-0.003	-0.003	0.000	0.000	0.000
138	A	154	LYS	1	0.939	0.987	34.715	0.065	0.065	0.000	0.000	0.000
139	A	155	PRO	0	0.031	0.011	37.025	-0.003	-0.003	0.000	0.000	0.000
140	A	156	ASN	0	-0.022	-0.022	38.201	0.000	0.000	0.000	0.000	0.000
141	A	157	ALA	0	0.002	0.028	33.098	-0.004	-0.004	0.000	0.000	0.000
142	A	158	LEU	0	-0.024	-0.013	31.021	0.000	0.000	0.000	0.000	0.000
143	A	159	ILE	0	-0.001	-0.011	29.203	-0.005	-0.005	0.000	0.000	0.000
144	A	160	TYR	0	-0.104	-0.112	21.992	0.012	0.012	0.000	0.000	0.000
145	A	161	VAL	0	0.013	0.002	25.690	-0.004	-0.004	0.000	0.000	0.000
146	A	162	GLU	-1	-0.814	-0.847	20.162	-0.251	-0.251	0.000	0.000	0.000
147	A	163	THR	0	-0.016	-0.026	23.919	0.003	0.003	0.000	0.000	0.000
148	A	164	GLU	-1	-0.849	-0.905	24.365	-0.151	-0.151	0.000	0.000	0.000
149	A	165	LYS	1	0.859	0.931	25.718	0.130	0.130	0.000	0.000	0.000
150	A	166	ASP	-1	-0.914	-0.958	27.587	-0.076	-0.076	0.000	0.000	0.000
151	A	167	LYS	1	0.852	0.899	30.922	0.078	0.078	0.000	0.000	0.000
152	A	168	PRO	0	-0.042	0.010	29.930	0.004	0.004	0.000	0.000	0.000
153	A	169	LEU	0	0.010	0.010	29.989	0.002	0.002	0.000	0.000	0.000
154	A	170	ILE	0	0.032	0.030	33.640	0.002	0.002	0.000	0.000	0.000
155	A	171	THR	0	-0.060	-0.032	36.182	-0.004	-0.004	0.000	0.000	0.000
156	A	172	PRO	0	0.039	0.045	35.636	0.004	0.004	0.000	0.000	0.000
157	A	173	GLU	-1	-0.911	-0.981	38.600	-0.047	-0.047	0.000	0.000	0.000
158	A	174	ASN	0	0.004	0.028	39.433	0.000	0.000	0.000	0.000	0.000
159	A	175	TRP	0	0.003	-0.010	32.338	-0.006	-0.006	0.000	0.000	0.000
160	A	176	THR	0	-0.008	-0.006	38.117	0.003	0.003	0.000	0.000	0.000
161	A	177	LEU	0	-0.010	-0.002	33.291	-0.004	-0.004	0.000	0.000	0.000
162	A	178	LEU	0	-0.012	0.002	34.414	0.003	0.003	0.000	0.000	0.000
163	A	179	LYS	1	0.835	0.896	31.331	0.086	0.086	0.000	0.000	0.000
164	A	180	GLU	-1	-0.803	-0.905	31.068	-0.095	-0.095	0.000	0.000	0.000
165	A	181	LYS	1	0.853	0.950	28.338	0.123	0.123	0.000	0.000	0.000
166	A	182	THR	0	0.089	0.046	27.776	-0.009	-0.009	0.000	0.000	0.000
167	A	183	THR	0	-0.043	-0.021	23.842	0.005	0.005	0.000	0.000	0.000
168	A	184	GLY	0	0.008	0.004	23.874	-0.016	-0.016	0.000	0.000	0.000
169	A	185	ILE	0	0.020	-0.034	19.881	0.014	0.014	0.000	0.000	0.000
170	A	186	VAL	0	0.033	0.036	20.692	0.003	0.003	0.000	0.000	0.000
171	A	187	SER	0	-0.022	-0.013	24.069	0.009	0.009	0.000	0.000	0.000
172	A	188	TYR	0	-0.018	-0.013	21.431	-0.007	-0.007	0.000	0.000	0.000
173	A	189	ARG	1	0.876	0.931	26.662	0.117	0.117	0.000	0.000	0.000
174	A	190	LEU	0	-0.017	-0.002	28.515	-0.007	-0.007	0.000	0.000	0.000
175	A	191	TYR	0	0.037	0.007	30.852	0.005	0.005	0.000	0.000	0.000
176	A	192	GLN	0	-0.021	-0.012	33.325	-0.003	-0.003	0.000	0.000	0.000
177	A	193	ASN	0	-0.063	-0.049	36.023	0.004	0.004	0.000	0.000	0.000
178	A	194	LEU	0	-0.037	-0.014	37.637	0.002	0.002	0.000	0.000	0.000
179	A	195	GLU	-1	-0.806	-0.897	40.082	-0.054	-0.054	0.000	0.000	0.000
180	A	196	NME	0	-0.057	-0.026	43.512	0.001	0.001	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:10:ACE )