FMO DATABASE

FMODB ID: VRMG1

Calculation Name: 2CWR-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2CWR

Chain ID: A

ChEMBL ID:

UniProt ID: Q8U1H5

Base Structure: X-ray

Registration Date: 2023-06-20

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	97
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-658602.683425
FMO2-HF: Nuclear repulsion	622846.132989
FMO2-HF: Total energy	-35756.550436
FMO2-MP2: Total energy	-35863.804115

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:262:PRO)

Summations of interaction energy for fragment #1(A:262: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.
-3.635	-1.652	0.018	-0.751	-1.248	0

Interaction energy analysis for fragmet #1(A:262:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.006 / q_NPA : -0.029

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].
3	A	264	SER	0	-0.029	-0.015	3.470	-1.268	0.347	0.019	-0.700	-0.933
4	A	265	GLY	0	0.013	-0.013	5.325	0.691	0.755	-0.001	-0.004	-0.059
5	A	266	SER	0	-0.065	-0.028	8.639	-0.040	-0.040	0.000	0.000	0.000
6	A	267	LEU	0	0.023	0.012	11.222	0.045	0.045	0.000	0.000	0.000
7	A	268	GLU	-1	-0.900	-0.930	14.268	-0.362	-0.362	0.000	0.000	0.000
8	A	269	VAL	0	0.030	0.003	17.787	0.015	0.015	0.000	0.000	0.000
9	A	270	LYS	1	0.799	0.891	21.192	0.277	0.277	0.000	0.000	0.000
10	A	271	VAL	0	0.017	0.011	24.738	0.005	0.005	0.000	0.000	0.000
11	A	272	ASN	0	-0.036	-0.022	27.270	0.007	0.007	0.000	0.000	0.000
12	A	273	ASP	-1	-0.793	-0.882	31.038	-0.111	-0.111	0.000	0.000	0.000
13	A	274	TRP	0	-0.001	0.005	33.036	0.002	0.002	0.000	0.000	0.000
14	A	275	GLY	0	-0.011	-0.006	35.952	0.007	0.007	0.000	0.000	0.000
15	A	276	SER	0	-0.033	-0.031	36.757	-0.002	-0.002	0.000	0.000	0.000
16	A	277	GLY	0	0.046	-0.010	34.214	0.003	0.003	0.000	0.000	0.000
17	A	278	ALA	0	-0.016	0.015	30.271	-0.001	-0.001	0.000	0.000	0.000
18	A	279	GLU	-1	-0.877	-0.930	29.231	-0.127	-0.127	0.000	0.000	0.000
19	A	280	TYR	0	0.020	-0.008	24.105	-0.004	-0.004	0.000	0.000	0.000
20	A	281	ASP	-1	-0.834	-0.916	24.700	-0.180	-0.180	0.000	0.000	0.000
21	A	282	VAL	0	-0.038	-0.025	18.228	-0.021	-0.021	0.000	0.000	0.000
22	A	283	THR	0	-0.037	-0.030	18.207	0.026	0.026	0.000	0.000	0.000
23	A	284	LEU	0	-0.009	0.005	13.887	-0.040	-0.040	0.000	0.000	0.000
24	A	285	ASN	0	-0.017	-0.010	13.395	0.097	0.097	0.000	0.000	0.000
25	A	286	LEU	0	-0.010	0.000	10.002	-0.183	-0.183	0.000	0.000	0.000
26	A	287	ASP	-1	-0.775	-0.869	6.287	-2.284	-2.284	0.000	0.000	0.000
27	A	288	GLY	0	0.014	0.003	9.967	0.195	0.195	0.000	0.000	0.000
28	A	289	GLN	0	-0.114	-0.060	11.732	0.001	0.001	0.000	0.000	0.000
29	A	290	TYR	0	-0.018	-0.047	7.749	0.239	0.239	0.000	0.000	0.000
30	A	291	ASP	-1	-0.855	-0.907	12.878	-0.069	-0.069	0.000	0.000	0.000
31	A	292	TRP	0	-0.037	-0.018	12.507	0.009	0.009	0.000	0.000	0.000
32	A	293	THR	0	-0.011	-0.022	13.182	0.091	0.091	0.000	0.000	0.000
33	A	294	VAL	0	-0.011	-0.004	13.978	-0.073	-0.073	0.000	0.000	0.000
34	A	295	LYS	1	0.835	0.913	14.690	0.186	0.186	0.000	0.000	0.000
35	A	296	VAL	0	0.011	-0.002	18.126	-0.032	-0.032	0.000	0.000	0.000
36	A	297	LYS	1	0.823	0.922	20.964	0.134	0.134	0.000	0.000	0.000
37	A	298	LEU	0	-0.027	-0.015	23.270	-0.009	-0.009	0.000	0.000	0.000
38	A	299	ALA	0	0.036	0.036	26.862	0.004	0.004	0.000	0.000	0.000
39	A	300	PRO	0	-0.031	-0.037	29.453	0.007	0.007	0.000	0.000	0.000
40	A	301	GLY	0	-0.034	-0.017	32.635	0.000	0.000	0.000	0.000	0.000
41	A	302	ALA	0	-0.001	0.005	30.560	0.002	0.002	0.000	0.000	0.000
42	A	303	THR	0	-0.040	-0.024	30.936	0.004	0.004	0.000	0.000	0.000
43	A	304	VAL	0	-0.024	-0.012	26.702	-0.004	-0.004	0.000	0.000	0.000
44	A	305	GLY	0	-0.021	0.000	30.124	0.007	0.007	0.000	0.000	0.000
45	A	306	SER	0	-0.042	-0.026	31.365	0.004	0.004	0.000	0.000	0.000
46	A	307	PHE	0	0.027	0.000	26.561	-0.007	-0.007	0.000	0.000	0.000
47	A	308	TRP	0	-0.012	0.010	26.860	0.018	0.018	0.000	0.000	0.000
48	A	309	SER	0	-0.001	-0.013	24.376	-0.008	-0.008	0.000	0.000	0.000
49	A	310	ALA	0	0.017	0.019	22.258	-0.016	-0.016	0.000	0.000	0.000
50	A	311	ASN	0	-0.046	-0.019	22.777	0.023	0.023	0.000	0.000	0.000
51	A	312	LYS	1	0.839	0.912	23.236	0.069	0.069	0.000	0.000	0.000
52	A	313	GLN	0	-0.030	-0.008	23.090	0.013	0.013	0.000	0.000	0.000
53	A	314	GLU	-1	-0.763	-0.883	24.713	-0.097	-0.097	0.000	0.000	0.000
54	A	315	GLY	0	0.020	0.008	27.001	0.012	0.012	0.000	0.000	0.000
55	A	316	ASN	0	-0.042	-0.037	28.109	-0.007	-0.007	0.000	0.000	0.000
56	A	317	GLY	0	0.029	0.034	27.351	0.000	0.000	0.000	0.000	0.000
57	A	318	TYR	0	-0.041	-0.022	20.363	0.000	0.000	0.000	0.000	0.000
58	A	319	VAL	0	0.004	0.003	23.246	0.014	0.014	0.000	0.000	0.000
59	A	320	ILE	0	-0.032	-0.014	18.445	-0.018	-0.018	0.000	0.000	0.000
60	A	321	PHE	0	0.028	0.016	19.735	0.021	0.021	0.000	0.000	0.000
61	A	322	THR	0	0.007	0.007	17.420	-0.022	-0.022	0.000	0.000	0.000
62	A	323	PRO	0	0.018	0.036	17.001	0.013	0.013	0.000	0.000	0.000
63	A	324	VAL	0	0.007	0.009	19.998	0.028	0.028	0.000	0.000	0.000
64	A	325	SER	0	-0.046	-0.043	21.745	-0.016	-0.016	0.000	0.000	0.000
65	A	326	TRP	0	0.065	0.024	21.824	0.002	0.002	0.000	0.000	0.000
66	A	327	ASN	0	-0.066	-0.039	20.911	-0.031	-0.031	0.000	0.000	0.000
67	A	328	LYS	1	0.883	0.912	16.318	0.037	0.037	0.000	0.000	0.000
68	A	329	GLY	0	0.066	0.064	15.187	-0.049	-0.049	0.000	0.000	0.000
69	A	330	PRO	0	-0.020	-0.007	14.408	0.078	0.078	0.000	0.000	0.000
70	A	331	THR	0	0.023	0.006	14.644	-0.075	-0.075	0.000	0.000	0.000
71	A	332	ALA	0	-0.064	-0.015	16.826	0.050	0.050	0.000	0.000	0.000
72	A	333	THR	0	0.018	-0.001	18.514	-0.023	-0.023	0.000	0.000	0.000
73	A	334	PHE	0	-0.029	-0.022	18.052	0.030	0.030	0.000	0.000	0.000
74	A	335	GLY	0	0.091	0.054	22.805	-0.019	-0.019	0.000	0.000	0.000
75	A	336	PHE	0	-0.034	-0.015	22.100	0.016	0.016	0.000	0.000	0.000
76	A	337	ILE	0	0.010	0.017	27.308	-0.006	-0.006	0.000	0.000	0.000
77	A	338	VAL	0	-0.043	-0.026	27.443	0.006	0.006	0.000	0.000	0.000
78	A	339	ASN	0	0.010	0.003	30.710	-0.003	-0.003	0.000	0.000	0.000
79	A	340	GLY	0	0.033	-0.002	33.672	0.000	0.000	0.000	0.000	0.000
80	A	341	PRO	0	-0.024	-0.008	34.401	0.001	0.001	0.000	0.000	0.000
81	A	342	GLN	0	0.000	0.006	35.095	-0.004	-0.004	0.000	0.000	0.000
82	A	343	GLY	0	-0.011	-0.004	33.765	0.003	0.003	0.000	0.000	0.000
83	A	344	ASP	-1	-0.884	-0.937	27.938	-0.144	-0.144	0.000	0.000	0.000
84	A	345	LYS	1	0.749	0.885	29.400	0.109	0.109	0.000	0.000	0.000
85	A	346	VAL	0	-0.039	-0.027	23.343	0.005	0.005	0.000	0.000	0.000
86	A	347	GLU	-1	-0.829	-0.903	24.515	-0.117	-0.117	0.000	0.000	0.000
87	A	348	GLU	-1	-0.859	-0.903	17.480	-0.228	-0.228	0.000	0.000	0.000
88	A	349	ILE	0	-0.009	-0.013	17.429	0.018	0.018	0.000	0.000	0.000
89	A	350	THR	0	-0.021	-0.032	13.022	-0.058	-0.058	0.000	0.000	0.000
90	A	351	LEU	0	-0.007	0.004	10.331	0.054	0.054	0.000	0.000	0.000
91	A	352	GLU	-1	-0.809	-0.897	9.922	-0.259	-0.259	0.000	0.000	0.000
92	A	353	ILE	0	0.029	0.004	7.604	0.069	0.069	0.000	0.000	0.000
93	A	354	ASN	0	-0.037	-0.016	6.217	-0.061	-0.061	0.000	0.000	0.000
94	A	355	GLY	0	0.013	0.013	8.902	0.154	0.154	0.000	0.000	0.000
95	A	356	GLN	0	-0.052	-0.022	4.104	-0.217	0.087	0.000	-0.047	-0.256
96	A	357	VAL	0	0.030	0.009	7.551	-0.153	-0.153	0.000	0.000	0.000
97	A	358	ILE	0	-0.048	-0.011	5.502	-0.088	-0.088	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:262:PRO)