FMO DATABASE

FMODB ID: NNN3Q

Calculation Name: 3QQN-A-Xray372

Preferred Name: Basigin

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 3QQN

Chain ID: A

ChEMBL ID: CHEMBL3580492

UniProt ID: P35613

Base Structure: X-ray

Registration Date: 2023-09-21

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	OptAll
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	116
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-928280.048339
FMO2-HF: Nuclear repulsion	881966.031677
FMO2-HF: Total energy	-46314.016661
FMO2-MP2: Total energy	-46448.841939

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:MET)

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

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.
-12.794	-15.109	12.652	-5.015	-5.319	0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.026 / q_NPA : -0.004

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	3	GLY	0	-0.011	-0.004	3.362	-2.313	-0.060	0.086	-1.154	-1.185	-0.002
4	A	4	PHE	0	-0.022	-0.023	4.920	0.349	0.403	-0.001	-0.006	-0.046	0.000
5	A	5	VAL	0	-0.024	-0.016	8.531	-0.038	-0.038	0.000	0.000	0.000	0.000
6	A	6	GLN	0	-0.016	-0.006	10.958	0.168	0.168	0.000	0.000	0.000	0.000
7	A	7	ALA	0	0.031	0.023	13.475	-0.041	-0.041	0.000	0.000	0.000	0.000
8	A	8	PRO	0	0.022	0.018	14.554	0.048	0.048	0.000	0.000	0.000	0.000
9	A	9	LEU	0	0.001	-0.002	18.047	-0.008	-0.008	0.000	0.000	0.000	0.000
10	A	10	SER	0	0.043	0.009	21.004	0.013	0.013	0.000	0.000	0.000	0.000
11	A	11	GLN	0	-0.048	-0.008	23.428	0.024	0.024	0.000	0.000	0.000	0.000
12	A	12	GLN	0	-0.016	-0.009	27.010	0.002	0.002	0.000	0.000	0.000	0.000
13	A	13	ARG	1	0.809	0.896	28.308	0.161	0.161	0.000	0.000	0.000	0.000
14	A	14	TRP	0	0.044	0.031	33.104	0.002	0.002	0.000	0.000	0.000	0.000
15	A	15	VAL	0	0.061	0.027	36.131	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	16	GLY	0	-0.043	-0.013	37.834	0.003	0.003	0.000	0.000	0.000	0.000
17	A	17	GLY	0	-0.033	-0.010	35.786	0.001	0.001	0.000	0.000	0.000	0.000
18	A	18	SER	0	0.015	0.009	31.960	0.001	0.001	0.000	0.000	0.000	0.000
19	A	19	VAL	0	-0.035	-0.022	26.618	-0.004	-0.004	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.865	-0.912	24.501	-0.190	-0.190	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.059	-0.014	20.686	-0.014	-0.014	0.000	0.000	0.000	0.000
22	A	22	HIS	1	0.829	0.885	18.410	0.363	0.363	0.000	0.000	0.000	0.000
23	A	23	CYS	0	-0.018	0.011	14.019	-0.050	-0.050	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.798	-0.873	13.446	-0.435	-0.435	0.000	0.000	0.000	0.000
25	A	25	ALA	0	0.005	-0.006	8.500	-0.141	-0.141	0.000	0.000	0.000	0.000
26	A	26	VAL	0	0.020	0.014	6.360	0.361	0.361	0.000	0.000	0.000	0.000
27	A	27	GLY	0	0.052	0.005	4.578	-1.491	-1.485	-0.001	-0.041	0.036	0.000
28	A	28	SER	0	-0.023	0.004	3.647	-0.480	-0.163	0.000	-0.073	-0.244	0.000
29	A	29	PRO	0	0.007	-0.017	4.289	1.860	2.105	0.000	-0.023	-0.222	0.000
30	A	30	VAL	0	-0.005	0.016	6.493	0.089	0.089	0.000	0.000	0.000	0.000
31	A	31	PRO	0	-0.071	-0.020	6.192	0.249	0.249	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.739	-0.845	8.008	-0.006	-0.006	0.000	0.000	0.000	0.000
33	A	33	ILE	0	-0.007	-0.029	10.004	-0.194	-0.194	0.000	0.000	0.000	0.000
34	A	34	GLN	0	-0.039	-0.006	12.702	0.077	0.077	0.000	0.000	0.000	0.000
35	A	35	TRP	0	0.036	-0.001	15.105	-0.090	-0.090	0.000	0.000	0.000	0.000
36	A	36	TRP	0	-0.035	-0.008	16.143	0.053	0.053	0.000	0.000	0.000	0.000
37	A	37	PHE	0	0.047	0.007	19.689	-0.024	-0.024	0.000	0.000	0.000	0.000
38	A	38	GLU	-1	-0.835	-0.918	22.359	-0.176	-0.176	0.000	0.000	0.000	0.000
39	A	39	GLY	0	0.059	0.040	24.299	-0.008	-0.008	0.000	0.000	0.000	0.000
40	A	40	GLN	0	-0.007	-0.014	27.680	0.001	0.001	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.055	0.021	29.427	0.010	0.010	0.000	0.000	0.000	0.000
42	A	42	PRO	0	-0.050	-0.036	29.822	-0.004	-0.004	0.000	0.000	0.000	0.000
43	A	43	ASN	0	-0.107	-0.048	30.979	0.012	0.012	0.000	0.000	0.000	0.000
44	A	44	ASP	-1	-0.875	-0.913	27.885	-0.097	-0.097	0.000	0.000	0.000	0.000
45	A	45	ILE	0	-0.029	-0.026	24.201	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	46	MET	0	-0.096	-0.032	18.455	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	47	SER	0	-0.056	-0.033	21.264	0.009	0.009	0.000	0.000	0.000	0.000
48	A	48	GLN	0	-0.036	-0.032	16.937	-0.040	-0.040	0.000	0.000	0.000	0.000
49	A	49	LEU	0	-0.010	-0.008	20.903	0.019	0.019	0.000	0.000	0.000	0.000
50	A	50	TRP	0	-0.023	-0.024	21.235	-0.006	-0.006	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.846	-0.921	23.446	-0.113	-0.113	0.000	0.000	0.000	0.000
52	A	52	GLY	0	0.074	0.036	25.387	0.013	0.013	0.000	0.000	0.000	0.000
53	A	53	ALA	0	-0.049	-0.019	26.510	0.007	0.007	0.000	0.000	0.000	0.000
54	A	54	ARG	1	0.796	0.867	27.069	0.137	0.137	0.000	0.000	0.000	0.000
55	A	55	LEU	0	-0.012	-0.014	31.472	0.001	0.001	0.000	0.000	0.000	0.000
56	A	56	ASP	-1	-0.865	-0.943	31.230	-0.080	-0.080	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.776	0.896	31.842	0.100	0.100	0.000	0.000	0.000	0.000
58	A	58	VAL	0	-0.026	-0.001	25.570	-0.010	-0.010	0.000	0.000	0.000	0.000
59	A	59	HIS	1	0.860	0.920	26.720	0.114	0.114	0.000	0.000	0.000	0.000
60	A	60	ILE	0	-0.042	-0.031	20.059	-0.020	-0.020	0.000	0.000	0.000	0.000
61	A	61	HIS	0	0.050	0.039	22.149	0.022	0.022	0.000	0.000	0.000	0.000
62	A	62	ALA	0	-0.017	-0.011	16.907	-0.041	-0.041	0.000	0.000	0.000	0.000
63	A	63	THR	0	-0.033	-0.004	17.513	0.048	0.048	0.000	0.000	0.000	0.000
64	A	64	TYR	0	0.033	0.008	12.653	-0.064	-0.064	0.000	0.000	0.000	0.000
65	A	65	HIS	0	0.037	0.027	14.311	0.055	0.055	0.000	0.000	0.000	0.000
66	A	66	GLN	0	-0.003	-0.006	12.720	-0.032	-0.032	0.000	0.000	0.000	0.000
67	A	67	HIS	0	-0.078	-0.036	11.461	-0.062	-0.062	0.000	0.000	0.000	0.000
68	A	68	ALA	0	0.000	0.005	10.942	0.119	0.119	0.000	0.000	0.000	0.000
69	A	69	ALA	0	-0.004	-0.001	12.808	-0.110	-0.110	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.006	-0.020	16.069	0.063	0.063	0.000	0.000	0.000	0.000
71	A	71	THR	0	-0.014	-0.005	18.019	-0.049	-0.049	0.000	0.000	0.000	0.000
72	A	72	ILE	0	0.000	0.031	21.239	0.020	0.020	0.000	0.000	0.000	0.000
73	A	73	SER	0	0.000	-0.039	23.044	-0.012	-0.012	0.000	0.000	0.000	0.000
74	A	74	ILE	0	-0.045	-0.021	26.567	0.008	0.008	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.821	-0.902	29.714	-0.107	-0.107	0.000	0.000	0.000	0.000
76	A	76	THR	0	-0.037	-0.029	33.377	0.003	0.003	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.029	0.002	30.645	0.001	0.001	0.000	0.000	0.000	0.000
78	A	78	VAL	0	0.031	0.013	34.314	0.007	0.007	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.870	-0.931	34.086	-0.090	-0.090	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.880	-0.943	33.049	-0.094	-0.094	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.777	-0.860	30.073	-0.122	-0.122	0.000	0.000	0.000	0.000
82	A	82	THR	0	-0.032	-0.002	28.791	-0.019	-0.019	0.000	0.000	0.000	0.000
83	A	83	GLY	0	0.012	-0.007	26.777	0.009	0.009	0.000	0.000	0.000	0.000
84	A	84	THR	0	-0.033	-0.009	20.304	-0.011	-0.011	0.000	0.000	0.000	0.000
85	A	85	TYR	0	-0.003	-0.014	21.139	0.012	0.012	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-0.737	-0.851	15.323	-0.412	-0.412	0.000	0.000	0.000	0.000
87	A	88	ARG	1	0.788	0.887	11.841	0.250	0.250	0.000	0.000	0.000	0.000
88	A	89	ALA	0	0.051	0.017	8.649	0.068	0.068	0.000	0.000	0.000	0.000
89	A	90	SER	0	-0.016	-0.018	5.565	-0.173	-0.173	0.000	0.000	0.000	0.000
90	A	91	ASN	0	0.036	0.003	1.959	-10.936	-16.204	12.569	-3.713	-3.587	0.003
91	A	92	ASP	-1	-0.889	-0.933	5.116	1.424	1.424	0.000	0.000	0.000	0.000
92	A	93	PRO	0	-0.004	-0.013	5.987	-0.405	-0.405	0.000	0.000	0.000	0.000
93	A	94	ASP	-1	-0.870	-0.934	9.387	0.298	0.298	0.000	0.000	0.000	0.000
94	A	95	ARG	1	0.709	0.834	8.284	-0.528	-0.528	0.000	0.000	0.000	0.000
95	A	96	ASN	0	0.007	-0.006	10.648	-0.124	-0.124	0.000	0.000	0.000	0.000
96	A	97	HIS	0	0.002	0.013	14.216	0.031	0.031	0.000	0.000	0.000	0.000
97	A	98	LEU	0	0.012	0.023	13.280	-0.025	-0.025	0.000	0.000	0.000	0.000
98	A	99	THR	0	0.037	0.023	16.642	-0.033	-0.033	0.000	0.000	0.000	0.000
99	A	100	ARG	1	0.864	0.902	17.768	-0.099	-0.099	0.000	0.000	0.000	0.000
100	A	101	ALA	0	0.084	0.041	15.458	-0.009	-0.009	0.000	0.000	0.000	0.000
101	A	102	PRO	0	-0.050	0.001	14.829	0.022	0.022	0.000	0.000	0.000	0.000
102	A	103	ARG	1	0.907	0.934	10.339	-0.241	-0.241	0.000	0.000	0.000	0.000
103	A	104	VAL	0	0.027	0.029	7.901	-0.030	-0.030	0.000	0.000	0.000	0.000
104	A	105	LYS	1	0.906	0.953	8.301	0.020	0.020	0.000	0.000	0.000	0.000
105	A	106	TRP	0	0.023	0.019	7.290	-0.110	-0.110	0.000	0.000	0.000	0.000
106	A	107	VAL	0	-0.032	-0.002	4.741	0.043	0.121	-0.001	-0.005	-0.071	0.000
107	A	108	ARG	1	0.886	0.910	7.974	0.533	0.533	0.000	0.000	0.000	0.000
108	A	109	ALA	0	-0.007	0.001	11.048	-0.081	-0.081	0.000	0.000	0.000	0.000
109	A	110	GLN	0	-0.045	-0.042	13.339	0.064	0.064	0.000	0.000	0.000	0.000
110	A	111	ALA	0	-0.002	0.011	17.077	-0.008	-0.008	0.000	0.000	0.000	0.000
111	A	112	VAL	0	-0.001	-0.001	20.521	0.014	0.014	0.000	0.000	0.000	0.000
112	A	113	VAL	0	-0.003	0.002	23.988	0.000	0.000	0.000	0.000	0.000	0.000
113	A	114	LEU	0	-0.004	-0.005	26.860	0.007	0.007	0.000	0.000	0.000	0.000
114	A	115	VAL	0	-0.005	-0.004	30.435	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	116	LEU	0	0.005	0.008	33.479	0.004	0.004	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.919	-0.961	36.899	-0.074	-0.074	0.000	0.000	0.000	0.000

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