FMO DATABASE

FMODB ID: 49V6N

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	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	90
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-595248.876003
FMO2-HF: Nuclear repulsion	560505.613815
FMO2-HF: Total energy	-34743.262187
FMO2-MP2: Total energy	-34844.292568

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.
6.662	-1.541	16.728	-4.006	-4.52	-0.003

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 : -0.004 / q_NPA : -0.005

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	-0.019	-0.016	3.311	-2.754	-0.842	0.060	-0.958	-1.014	0.001
4	A	1148	GLN	0	0.018	0.020	5.837	0.532	0.532	0.000	0.000	0.000	0.000
5	A	1149	PRO	0	0.014	0.016	6.773	-0.486	-0.486	0.000	0.000	0.000	0.000
6	A	1150	ARG	1	0.865	0.924	5.311	3.010	3.010	0.000	0.000	0.000	0.000
7	A	1151	ARG	1	1.005	0.993	9.052	0.744	0.744	0.000	0.000	0.000	0.000
8	A	1152	VAL	0	-0.050	-0.030	10.606	-0.128	-0.128	0.000	0.000	0.000	0.000
9	A	1153	GLU	-1	-0.924	-0.952	12.944	-0.433	-0.433	0.000	0.000	0.000	0.000
10	A	1154	LEU	0	-0.059	-0.024	15.945	-0.012	-0.012	0.000	0.000	0.000	0.000
11	A	1155	TRP	0	0.039	0.022	18.627	0.062	0.062	0.000	0.000	0.000	0.000
12	A	1156	ARG	1	0.832	0.899	21.901	0.372	0.372	0.000	0.000	0.000	0.000
13	A	1157	GLU	-1	-0.806	-0.883	24.213	-0.328	-0.328	0.000	0.000	0.000	0.000
14	A	1158	PRO	0	-0.019	-0.018	27.237	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	1159	SER	0	-0.036	-0.016	30.471	0.007	0.007	0.000	0.000	0.000	0.000
16	A	1160	LYS	1	1.047	1.010	27.764	0.240	0.240	0.000	0.000	0.000	0.000
17	A	1161	SER	0	-0.107	-0.040	26.068	-0.012	-0.012	0.000	0.000	0.000	0.000
18	A	1162	LEU	0	0.082	0.025	21.148	0.004	0.004	0.000	0.000	0.000	0.000
19	A	1163	GLY	0	0.058	0.033	21.157	-0.033	-0.033	0.000	0.000	0.000	0.000
20	A	1164	ILE	0	-0.006	0.012	17.692	-0.035	-0.035	0.000	0.000	0.000	0.000
21	A	1165	SER	0	-0.032	-0.005	20.777	0.069	0.069	0.000	0.000	0.000	0.000
22	A	1166	ILE	0	0.017	0.008	19.907	-0.060	-0.060	0.000	0.000	0.000	0.000
23	A	1167	VAL	0	-0.014	-0.010	20.917	0.062	0.062	0.000	0.000	0.000	0.000
24	A	1168	GLY	0	0.017	0.014	21.600	-0.047	-0.047	0.000	0.000	0.000	0.000
25	A	1169	GLY	0	0.099	0.047	23.407	0.011	0.011	0.000	0.000	0.000	0.000
26	A	1170	ARG	1	0.821	0.885	24.596	0.362	0.362	0.000	0.000	0.000	0.000
27	A	1184	GLY	0	-0.008	-0.016	18.738	0.007	0.007	0.000	0.000	0.000	0.000
28	A	1185	ILE	0	0.008	0.022	18.972	0.037	0.037	0.000	0.000	0.000	0.000
29	A	1186	PHE	0	0.000	-0.013	14.777	-0.086	-0.086	0.000	0.000	0.000	0.000
30	A	1187	ILE	0	0.051	0.036	14.262	0.114	0.114	0.000	0.000	0.000	0.000
31	A	1188	LYS	1	0.892	0.952	17.226	0.479	0.479	0.000	0.000	0.000	0.000
32	A	1189	HIS	0	0.014	-0.019	19.359	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	1190	VAL	0	0.034	0.011	15.636	-0.011	-0.011	0.000	0.000	0.000	0.000
34	A	1191	LEU	0	-0.041	-0.015	19.007	0.032	0.032	0.000	0.000	0.000	0.000
35	A	1192	GLU	-1	-0.862	-0.910	19.038	-0.537	-0.537	0.000	0.000	0.000	0.000
36	A	1193	ASP	-1	-0.958	-0.970	21.018	-0.327	-0.327	0.000	0.000	0.000	0.000
37	A	1194	SER	0	-0.030	-0.048	21.009	0.002	0.002	0.000	0.000	0.000	0.000
38	A	1195	PRO	0	0.017	0.008	20.644	-0.028	-0.028	0.000	0.000	0.000	0.000
39	A	1196	ALA	0	-0.017	-0.010	17.098	-0.052	-0.052	0.000	0.000	0.000	0.000
40	A	1197	GLY	0	-0.013	0.003	16.107	-0.100	-0.100	0.000	0.000	0.000	0.000
41	A	1198	LYS	1	0.876	0.908	16.775	0.325	0.325	0.000	0.000	0.000	0.000
42	A	1199	ASN	0	-0.004	0.033	12.485	-0.168	-0.168	0.000	0.000	0.000	0.000
43	A	1200	GLY	0	0.061	0.044	13.181	-0.063	-0.063	0.000	0.000	0.000	0.000
44	A	1201	THR	0	-0.089	-0.071	8.296	-0.260	-0.260	0.000	0.000	0.000	0.000
45	A	1202	LEU	0	-0.044	-0.007	9.525	-0.323	-0.323	0.000	0.000	0.000	0.000
46	A	1203	LYS	1	0.871	0.922	7.445	2.665	2.665	0.000	0.000	0.000	0.000
47	A	1204	PRO	0	-0.001	-0.018	13.147	-0.032	-0.032	0.000	0.000	0.000	0.000
48	A	1205	GLY	0	-0.026	-0.010	13.556	-0.077	-0.077	0.000	0.000	0.000	0.000
49	A	1206	ASP	-1	-0.773	-0.867	10.295	-2.141	-2.141	0.000	0.000	0.000	0.000
50	A	1207	ARG	1	0.853	0.927	12.021	1.033	1.033	0.000	0.000	0.000	0.000
51	A	1208	ILE	0	0.000	-0.001	13.094	-0.138	-0.138	0.000	0.000	0.000	0.000
52	A	1209	VAL	0	-0.044	-0.036	13.216	0.078	0.078	0.000	0.000	0.000	0.000
53	A	1210	GLU	-1	-0.842	-0.922	15.917	-0.551	-0.551	0.000	0.000	0.000	0.000
54	A	1211	VAL	0	-0.008	-0.008	17.445	-0.081	-0.081	0.000	0.000	0.000	0.000
55	A	1212	ASP	-1	-0.847	-0.940	19.879	-0.422	-0.422	0.000	0.000	0.000	0.000
56	A	1213	GLY	0	-0.021	-0.001	19.974	0.047	0.047	0.000	0.000	0.000	0.000
57	A	1214	MET	0	-0.051	-0.014	21.154	0.029	0.029	0.000	0.000	0.000	0.000
58	A	1215	ASP	-1	-0.799	-0.907	19.906	-0.583	-0.583	0.000	0.000	0.000	0.000
59	A	1216	LEU	0	-0.033	-0.030	19.298	0.037	0.037	0.000	0.000	0.000	0.000
60	A	1217	ARG	1	0.779	0.884	14.696	0.654	0.654	0.000	0.000	0.000	0.000
61	A	1218	ASP	-1	-0.890	-0.949	19.336	-0.464	-0.464	0.000	0.000	0.000	0.000
62	A	1219	ALA	0	-0.032	0.011	22.483	0.039	0.039	0.000	0.000	0.000	0.000
63	A	1220	SER	0	0.016	0.006	24.339	-0.016	-0.016	0.000	0.000	0.000	0.000
64	A	1221	HIS	0	-0.056	-0.035	25.068	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	1222	GLU	-1	-0.783	-0.884	26.515	-0.330	-0.330	0.000	0.000	0.000	0.000
66	A	1223	GLN	0	0.047	0.018	26.441	0.001	0.001	0.000	0.000	0.000	0.000
67	A	1224	ALA	0	0.034	0.024	22.876	-0.004	-0.004	0.000	0.000	0.000	0.000
68	A	1225	VAL	0	-0.020	-0.009	24.722	-0.008	-0.008	0.000	0.000	0.000	0.000
69	A	1226	GLU	-1	-0.898	-0.925	26.754	-0.263	-0.263	0.000	0.000	0.000	0.000
70	A	1227	ALA	0	0.027	0.014	24.813	0.009	0.009	0.000	0.000	0.000	0.000
71	A	1228	ILE	0	0.015	0.011	21.240	-0.008	-0.008	0.000	0.000	0.000	0.000
72	A	1229	ARG	1	0.875	0.923	24.450	0.332	0.332	0.000	0.000	0.000	0.000
73	A	1230	LYS	1	0.807	0.887	27.663	0.271	0.271	0.000	0.000	0.000	0.000
74	A	1231	ALA	0	0.052	0.056	23.893	0.013	0.013	0.000	0.000	0.000	0.000
75	A	1232	GLY	0	0.016	0.016	25.668	0.022	0.022	0.000	0.000	0.000	0.000
76	A	1233	ASN	0	0.010	0.016	24.332	-0.050	-0.050	0.000	0.000	0.000	0.000
77	A	1234	PRO	0	0.014	0.005	20.120	0.034	0.034	0.000	0.000	0.000	0.000
78	A	1235	VAL	0	-0.021	-0.012	19.886	0.017	0.017	0.000	0.000	0.000	0.000
79	A	1236	VAL	0	0.006	-0.001	16.564	-0.066	-0.066	0.000	0.000	0.000	0.000
80	A	1237	PHE	0	0.008	0.000	14.872	0.044	0.044	0.000	0.000	0.000	0.000
81	A	1238	MET	0	-0.018	0.020	11.724	-0.080	-0.080	0.000	0.000	0.000	0.000
82	A	1239	VAL	0	0.007	-0.009	10.441	0.102	0.102	0.000	0.000	0.000	0.000
83	A	1240	GLN	0	-0.037	-0.021	8.168	-0.189	-0.189	0.000	0.000	0.000	0.000
84	A	1241	SER	0	-0.006	-0.009	6.289	0.089	0.089	0.000	0.000	0.000	0.000
85	A	1242	ILE	0	-0.006	-0.007	2.027	5.665	-4.450	16.668	-3.048	-3.506	-0.004
86	A	1243	ILE	0	0.008	0.006	5.707	0.368	0.368	0.000	0.000	0.000	0.000
87	A	1244	SER	0	-0.006	0.005	7.863	-0.035	-0.035	0.000	0.000	0.000	0.000
88	A	1245	THR	0	0.021	-0.009	9.431	0.070	0.070	0.000	0.000	0.000	0.000
89	A	1246	ARG	1	0.945	0.986	13.068	0.377	0.377	0.000	0.000	0.000	0.000
90	A	1247	LEU	0	0.045	0.025	15.496	0.021	0.021	0.000	0.000	0.000	0.000

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