FMO DATABASE

FMODB ID: 52VYZ

Calculation Name: 2FCF-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2FCF

Chain ID: A

ChEMBL ID:

UniProt ID: O75970

Base Structure: X-ray

Registration Date: 2023-09-19

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	90
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-595288.049534
FMO2-HF: Nuclear repulsion	560544.514869
FMO2-HF: Total energy	-34743.534665
FMO2-MP2: Total energy	-34844.560531

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:1145:GLN)

Summations of interaction energy for fragment #1(A:1145:GLN)

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.
-0.854	1.946	1.274	-1.403	-2.671	0.002

Interaction energy analysis for fragmet #1(A:1145:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.000 / q_NPA : -0.008

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

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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	1147	MET	0	-0.021	-0.016	3.338	-2.975	-1.089	0.048	-0.917	-1.017	0.002
4	A	1148	GLN	0	0.028	0.025	5.849	0.398	0.398	0.000	0.000	0.000	0.000
5	A	1149	PRO	0	0.008	0.011	6.799	-0.452	-0.452	0.000	0.000	0.000	0.000
6	A	1150	ARG	1	0.816	0.885	5.811	3.025	3.025	0.000	0.000	0.000	0.000
7	A	1151	ARG	1	0.920	0.933	9.108	0.597	0.597	0.000	0.000	0.000	0.000
8	A	1152	VAL	0	-0.049	-0.030	10.495	-0.119	-0.119	0.000	0.000	0.000	0.000
9	A	1153	GLU	-1	-0.829	-0.892	13.016	-0.394	-0.394	0.000	0.000	0.000	0.000
10	A	1154	LEU	0	-0.059	-0.022	15.768	-0.022	-0.022	0.000	0.000	0.000	0.000
11	A	1155	TRP	0	0.033	0.014	18.606	0.067	0.067	0.000	0.000	0.000	0.000
12	A	1156	ARG	1	0.831	0.897	21.877	0.368	0.368	0.000	0.000	0.000	0.000
13	A	1157	GLU	-1	-0.791	-0.890	24.147	-0.360	-0.360	0.000	0.000	0.000	0.000
14	A	1158	PRO	0	-0.013	-0.017	27.139	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	1159	SER	0	-0.030	-0.010	30.347	0.009	0.009	0.000	0.000	0.000	0.000
16	A	1160	LYS	1	1.031	1.000	27.627	0.250	0.250	0.000	0.000	0.000	0.000
17	A	1161	SER	0	-0.106	-0.036	26.069	-0.008	-0.008	0.000	0.000	0.000	0.000
18	A	1162	LEU	0	0.081	0.026	21.257	0.002	0.002	0.000	0.000	0.000	0.000
19	A	1163	GLY	0	0.060	0.031	21.008	-0.035	-0.035	0.000	0.000	0.000	0.000
20	A	1164	ILE	0	-0.010	0.009	17.479	-0.042	-0.042	0.000	0.000	0.000	0.000
21	A	1165	SER	0	-0.037	-0.004	20.601	0.076	0.076	0.000	0.000	0.000	0.000
22	A	1166	ILE	0	0.016	0.003	19.712	-0.064	-0.064	0.000	0.000	0.000	0.000
23	A	1167	VAL	0	-0.011	-0.013	21.017	0.062	0.062	0.000	0.000	0.000	0.000
24	A	1168	GLY	0	0.026	0.021	21.550	-0.046	-0.046	0.000	0.000	0.000	0.000
25	A	1169	GLY	0	0.082	0.038	23.362	0.011	0.011	0.000	0.000	0.000	0.000
26	A	1170	ARG	1	0.815	0.871	24.557	0.358	0.358	0.000	0.000	0.000	0.000
27	A	1184	GLY	0	0.027	0.007	18.713	-0.004	-0.004	0.000	0.000	0.000	0.000
28	A	1185	ILE	0	-0.037	-0.010	18.933	0.034	0.034	0.000	0.000	0.000	0.000
29	A	1186	PHE	0	0.001	-0.010	14.830	-0.083	-0.083	0.000	0.000	0.000	0.000
30	A	1187	ILE	0	0.048	0.034	14.154	0.115	0.115	0.000	0.000	0.000	0.000
31	A	1188	LYS	1	0.891	0.952	17.247	0.529	0.529	0.000	0.000	0.000	0.000
32	A	1189	HIS	0	0.023	-0.015	19.376	-0.005	-0.005	0.000	0.000	0.000	0.000
33	A	1190	VAL	0	0.030	0.009	15.331	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	1191	LEU	0	-0.042	-0.014	18.741	0.029	0.029	0.000	0.000	0.000	0.000
35	A	1192	GLU	-1	-0.857	-0.914	18.816	-0.623	-0.623	0.000	0.000	0.000	0.000
36	A	1193	ASP	-1	-0.901	-0.949	20.737	-0.374	-0.374	0.000	0.000	0.000	0.000
37	A	1194	SER	0	-0.047	-0.051	20.731	0.011	0.011	0.000	0.000	0.000	0.000
38	A	1195	PRO	0	0.024	0.016	20.497	-0.035	-0.035	0.000	0.000	0.000	0.000
39	A	1196	ALA	0	-0.021	-0.015	16.947	-0.058	-0.058	0.000	0.000	0.000	0.000
40	A	1197	GLY	0	-0.021	-0.001	15.898	-0.114	-0.114	0.000	0.000	0.000	0.000
41	A	1198	LYS	1	0.818	0.900	16.511	0.357	0.357	0.000	0.000	0.000	0.000
42	A	1199	ASN	0	-0.019	0.017	12.408	-0.203	-0.203	0.000	0.000	0.000	0.000
43	A	1200	GLY	0	0.070	0.048	12.992	-0.070	-0.070	0.000	0.000	0.000	0.000
44	A	1201	THR	0	-0.074	-0.047	8.186	-0.284	-0.284	0.000	0.000	0.000	0.000
45	A	1202	LEU	0	-0.034	0.006	9.302	-0.348	-0.348	0.000	0.000	0.000	0.000
46	A	1203	LYS	1	0.892	0.925	7.767	2.723	2.723	0.000	0.000	0.000	0.000
47	A	1204	PRO	0	0.002	-0.016	12.951	-0.021	-0.021	0.000	0.000	0.000	0.000
48	A	1205	GLY	0	-0.034	-0.014	13.565	-0.096	-0.096	0.000	0.000	0.000	0.000
49	A	1206	ASP	-1	-0.762	-0.846	10.246	-2.441	-2.441	0.000	0.000	0.000	0.000
50	A	1207	ARG	1	0.860	0.934	11.974	1.004	1.004	0.000	0.000	0.000	0.000
51	A	1208	ILE	0	0.004	0.002	13.064	-0.127	-0.127	0.000	0.000	0.000	0.000
52	A	1209	VAL	0	-0.036	-0.034	13.164	0.078	0.078	0.000	0.000	0.000	0.000
53	A	1210	GLU	-1	-0.810	-0.884	15.907	-0.490	-0.490	0.000	0.000	0.000	0.000
54	A	1211	VAL	0	-0.008	-0.010	17.444	-0.083	-0.083	0.000	0.000	0.000	0.000
55	A	1212	ASP	-1	-0.832	-0.929	20.025	-0.398	-0.398	0.000	0.000	0.000	0.000
56	A	1213	GLY	0	-0.016	-0.001	19.990	0.046	0.046	0.000	0.000	0.000	0.000
57	A	1214	MET	0	-0.050	-0.013	21.177	0.031	0.031	0.000	0.000	0.000	0.000
58	A	1215	ASP	-1	-0.803	-0.908	19.862	-0.545	-0.545	0.000	0.000	0.000	0.000
59	A	1216	LEU	0	-0.034	-0.032	19.341	0.032	0.032	0.000	0.000	0.000	0.000
60	A	1217	ARG	1	0.760	0.861	15.024	0.563	0.563	0.000	0.000	0.000	0.000
61	A	1218	ASP	-1	-0.889	-0.952	19.323	-0.451	-0.451	0.000	0.000	0.000	0.000
62	A	1219	ALA	0	-0.044	0.006	22.467	0.038	0.038	0.000	0.000	0.000	0.000
63	A	1220	SER	0	0.004	-0.023	24.311	-0.018	-0.018	0.000	0.000	0.000	0.000
64	A	1221	HIS	0	-0.053	-0.034	24.867	0.000	0.000	0.000	0.000	0.000	0.000
65	A	1222	GLU	-1	-0.773	-0.867	26.479	-0.329	-0.329	0.000	0.000	0.000	0.000
66	A	1223	GLN	0	0.062	0.048	26.720	0.000	0.000	0.000	0.000	0.000	0.000
67	A	1224	ALA	0	0.039	0.025	22.823	-0.002	-0.002	0.000	0.000	0.000	0.000
68	A	1225	VAL	0	-0.016	-0.008	24.699	-0.009	-0.009	0.000	0.000	0.000	0.000
69	A	1226	GLU	-1	-0.894	-0.926	26.726	-0.258	-0.258	0.000	0.000	0.000	0.000
70	A	1227	ALA	0	0.029	0.016	24.835	0.009	0.009	0.000	0.000	0.000	0.000
71	A	1228	ILE	0	0.013	0.009	21.159	-0.007	-0.007	0.000	0.000	0.000	0.000
72	A	1229	ARG	1	0.874	0.925	24.476	0.341	0.341	0.000	0.000	0.000	0.000
73	A	1230	LYS	1	0.818	0.895	27.659	0.263	0.263	0.000	0.000	0.000	0.000
74	A	1231	ALA	0	0.047	0.050	23.960	0.015	0.015	0.000	0.000	0.000	0.000
75	A	1232	GLY	0	0.028	0.033	25.770	0.019	0.019	0.000	0.000	0.000	0.000
76	A	1233	ASN	0	0.001	0.010	24.392	-0.052	-0.052	0.000	0.000	0.000	0.000
77	A	1234	PRO	0	0.007	-0.002	20.185	0.034	0.034	0.000	0.000	0.000	0.000
78	A	1235	VAL	0	-0.026	-0.011	20.132	0.019	0.019	0.000	0.000	0.000	0.000
79	A	1236	VAL	0	-0.003	-0.006	16.856	-0.068	-0.068	0.000	0.000	0.000	0.000
80	A	1237	PHE	0	0.010	-0.002	14.943	0.044	0.044	0.000	0.000	0.000	0.000
81	A	1238	MET	0	-0.013	0.029	11.782	-0.073	-0.073	0.000	0.000	0.000	0.000
82	A	1239	VAL	0	-0.005	-0.018	10.584	0.089	0.089	0.000	0.000	0.000	0.000
83	A	1240	GLN	0	-0.037	-0.016	7.742	-0.111	-0.111	0.000	0.000	0.000	0.000
84	A	1241	SER	0	-0.013	-0.032	6.301	0.094	0.094	0.000	0.000	0.000	0.000
85	A	1242	ILE	0	-0.011	0.001	2.370	-1.162	-0.248	1.226	-0.486	-1.654	0.000
86	A	1243	ILE	0	0.007	0.005	5.691	0.465	0.465	0.000	0.000	0.000	0.000
87	A	1244	SER	0	0.008	0.010	7.865	-0.024	-0.024	0.000	0.000	0.000	0.000
88	A	1245	THR	0	0.004	-0.013	9.437	0.074	0.074	0.000	0.000	0.000	0.000
89	A	1246	ARG	1	0.952	0.985	13.075	0.335	0.335	0.000	0.000	0.000	0.000
90	A	1247	LEU	0	0.043	0.026	15.496	0.020	0.020	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1145:GLN)