FMO DATABASE

FMODB ID: G5GM1

Calculation Name: 4JG2-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4JG2

Chain ID: A

ChEMBL ID:

UniProt ID: Q73EI2

Base Structure: X-ray

Registration Date: 2023-09-23

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	185
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1810683.331698
FMO2-HF: Nuclear repulsion	1740743.646183
FMO2-HF: Total energy	-69939.685515
FMO2-MP2: Total energy	-70146.909064

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:-11:LYS)

Summations of interaction energy for fragment #1(A:-11:LYS)

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.
-29.802	-16.888	24.572	-16.786	-20.705	-0.12

Interaction energy analysis for fragmet #1(A:-11:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.979 / q_NPA : 1.001

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].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	-9	THR	0	0.022	-0.003	3.817	-0.304	2.607	-0.013	-1.506	-1.392	0.009
4	A	-8	GLU	-1	-0.820	-0.850	1.759	-85.321	-88.268	18.163	-8.261	-6.955	-0.072
5	A	-7	ASN	0	0.059	0.017	4.528	2.714	2.828	-0.001	-0.010	-0.103	0.000
6	A	-6	LEU	0	0.038	0.008	4.956	-2.086	-2.086	0.000	0.000	0.000	0.000
7	A	-5	TYR	0	-0.023	0.002	6.139	-0.166	-0.166	0.000	0.000	0.000	0.000
8	A	-4	PHE	0	-0.040	-0.030	7.646	0.656	0.656	0.000	0.000	0.000	0.000
9	A	-3	GLN	0	-0.067	-0.012	2.611	-3.384	-2.298	0.839	-0.671	-1.255	0.000
10	A	-2	SER	0	-0.036	-0.062	2.476	-5.306	-0.456	1.687	-2.922	-3.615	-0.029
11	A	-1	ASN	0	-0.008	-0.006	4.310	2.214	2.537	-0.001	-0.027	-0.296	0.000
12	A	0	ALA	0	0.001	0.008	5.013	4.711	4.711	0.000	0.000	0.000	0.000
13	A	4	GLN	0	0.059	0.022	2.519	-21.426	-16.350	1.703	-2.623	-4.157	-0.024
14	A	5	ASN	0	-0.058	-0.029	2.218	-0.700	0.486	2.185	-0.803	-2.569	-0.004
15	A	6	ARG	1	0.903	0.923	3.704	30.845	31.005	0.011	0.043	-0.215	0.000
16	A	7	THR	0	0.074	0.049	7.006	2.528	2.528	0.000	0.000	0.000	0.000
17	A	8	LYS	1	0.916	0.973	4.753	45.727	45.882	-0.001	-0.006	-0.148	0.000
18	A	9	VAL	0	0.008	0.005	6.867	-0.419	-0.419	0.000	0.000	0.000	0.000
19	A	10	VAL	0	-0.042	-0.026	7.846	0.328	0.328	0.000	0.000	0.000	0.000
20	A	11	THR	0	0.029	0.009	10.311	0.236	0.236	0.000	0.000	0.000	0.000
21	A	12	SER	0	0.087	0.060	13.764	-0.327	-0.327	0.000	0.000	0.000	0.000
22	A	13	VAL	0	0.013	-0.014	15.528	0.137	0.137	0.000	0.000	0.000	0.000
23	A	14	ASN	0	-0.035	-0.012	18.063	0.887	0.887	0.000	0.000	0.000	0.000
24	A	15	THR	0	-0.021	0.005	17.611	0.258	0.258	0.000	0.000	0.000	0.000
25	A	16	ARG	1	0.867	0.935	20.185	10.454	10.454	0.000	0.000	0.000	0.000
26	A	17	LEU	0	-0.017	-0.002	20.476	-0.372	-0.372	0.000	0.000	0.000	0.000
27	A	18	SER	0	0.055	0.041	23.946	0.599	0.599	0.000	0.000	0.000	0.000
28	A	19	TYR	0	0.014	-0.010	25.782	-0.379	-0.379	0.000	0.000	0.000	0.000
29	A	20	PHE	0	-0.023	-0.022	22.374	-0.496	-0.496	0.000	0.000	0.000	0.000
30	A	21	HIS	0	-0.002	0.007	24.856	0.505	0.505	0.000	0.000	0.000	0.000
31	A	22	GLY	0	0.032	0.000	22.468	-0.443	-0.443	0.000	0.000	0.000	0.000
32	A	23	TRP	0	-0.010	-0.015	23.006	-0.493	-0.493	0.000	0.000	0.000	0.000
33	A	24	GLU	-1	-0.867	-0.930	25.658	-10.249	-10.249	0.000	0.000	0.000	0.000
34	A	25	PRO	0	-0.063	-0.010	24.791	-0.213	-0.213	0.000	0.000	0.000	0.000
35	A	26	VAL	0	0.091	0.027	26.436	0.402	0.402	0.000	0.000	0.000	0.000
36	A	27	SER	0	-0.009	-0.006	27.656	-0.327	-0.327	0.000	0.000	0.000	0.000
37	A	28	ILE	0	-0.014	-0.014	26.393	0.186	0.186	0.000	0.000	0.000	0.000
38	A	29	ASN	0	-0.033	-0.027	30.197	-0.154	-0.154	0.000	0.000	0.000	0.000
39	A	30	GLY	0	0.102	0.060	33.068	0.084	0.084	0.000	0.000	0.000	0.000
40	A	31	GLY	0	-0.060	-0.018	28.920	-0.089	-0.089	0.000	0.000	0.000	0.000
41	A	32	ALA	0	-0.034	-0.021	26.102	0.025	0.025	0.000	0.000	0.000	0.000
42	A	33	GLU	-1	-0.861	-0.926	26.702	-11.044	-11.044	0.000	0.000	0.000	0.000
43	A	34	LYS	1	0.781	0.885	21.525	12.281	12.281	0.000	0.000	0.000	0.000
44	A	35	TYR	0	0.098	0.068	20.643	0.382	0.382	0.000	0.000	0.000	0.000
45	A	36	SER	0	-0.063	-0.055	21.386	-0.385	-0.385	0.000	0.000	0.000	0.000
46	A	37	VAL	0	0.023	0.020	20.208	0.231	0.231	0.000	0.000	0.000	0.000
47	A	38	SER	0	-0.017	-0.012	21.810	-0.365	-0.365	0.000	0.000	0.000	0.000
48	A	39	VAL	0	-0.028	-0.013	17.530	0.214	0.214	0.000	0.000	0.000	0.000
49	A	40	LEU	0	0.014	0.008	20.956	-0.084	-0.084	0.000	0.000	0.000	0.000
50	A	41	ILE	0	-0.006	-0.019	17.605	-0.337	-0.337	0.000	0.000	0.000	0.000
51	A	42	PRO	0	0.083	0.046	20.321	0.320	0.320	0.000	0.000	0.000	0.000
52	A	43	LYS	1	0.825	0.886	21.411	10.137	10.137	0.000	0.000	0.000	0.000
53	A	44	THR	0	-0.030	-0.026	22.781	-0.124	-0.124	0.000	0.000	0.000	0.000
54	A	45	ASP	-1	-0.798	-0.863	16.558	-15.853	-15.853	0.000	0.000	0.000	0.000
55	A	46	LYS	1	0.931	0.943	17.731	11.385	11.385	0.000	0.000	0.000	0.000
56	A	47	GLU	-1	-0.914	-0.935	11.203	-18.601	-18.601	0.000	0.000	0.000	0.000
57	A	48	THR	0	-0.025	-0.049	13.198	-1.436	-1.436	0.000	0.000	0.000	0.000
58	A	49	ILE	0	-0.033	-0.012	14.185	-0.622	-0.622	0.000	0.000	0.000	0.000
59	A	50	ASN	0	-0.027	-0.016	14.517	0.119	0.119	0.000	0.000	0.000	0.000
60	A	51	ALA	0	0.014	0.013	9.972	-0.513	-0.513	0.000	0.000	0.000	0.000
61	A	52	ILE	0	0.001	-0.003	11.599	-1.073	-1.073	0.000	0.000	0.000	0.000
62	A	53	ASN	0	-0.011	-0.005	13.791	-0.114	-0.114	0.000	0.000	0.000	0.000
63	A	54	ALA	0	0.007	0.011	11.518	0.143	0.143	0.000	0.000	0.000	0.000
64	A	55	ALA	0	0.013	0.009	10.344	-0.622	-0.622	0.000	0.000	0.000	0.000
65	A	56	VAL	0	-0.047	-0.032	11.811	-0.149	-0.149	0.000	0.000	0.000	0.000
66	A	57	ASP	-1	-0.796	-0.882	15.361	-15.632	-15.632	0.000	0.000	0.000	0.000
67	A	58	ALA	0	-0.018	-0.002	10.993	0.180	0.180	0.000	0.000	0.000	0.000
68	A	59	ALA	0	0.007	0.006	12.866	-0.251	-0.251	0.000	0.000	0.000	0.000
69	A	60	ILE	0	-0.042	-0.025	13.672	0.866	0.866	0.000	0.000	0.000	0.000
70	A	61	GLU	-1	-0.912	-0.960	14.601	-18.741	-18.741	0.000	0.000	0.000	0.000
71	A	62	GLU	-1	-0.916	-0.953	9.045	-30.917	-30.917	0.000	0.000	0.000	0.000
72	A	63	GLY	0	-0.023	-0.011	13.855	0.478	0.478	0.000	0.000	0.000	0.000
73	A	64	ILE	0	-0.072	-0.037	16.979	0.781	0.781	0.000	0.000	0.000	0.000
74	A	65	ALA	0	-0.007	-0.003	14.835	0.637	0.637	0.000	0.000	0.000	0.000
75	A	66	LYS	1	0.886	0.964	15.667	18.652	18.652	0.000	0.000	0.000	0.000
76	A	67	PHE	0	-0.022	-0.031	17.530	0.431	0.431	0.000	0.000	0.000	0.000
77	A	68	GLY	0	0.019	0.036	20.624	0.743	0.743	0.000	0.000	0.000	0.000
78	A	69	GLY	0	0.025	0.009	22.536	0.111	0.111	0.000	0.000	0.000	0.000
79	A	70	LYS	1	0.927	0.962	23.962	9.886	9.886	0.000	0.000	0.000	0.000
80	A	71	LYS	1	1.025	1.002	20.471	14.520	14.520	0.000	0.000	0.000	0.000
81	A	72	PRO	0	-0.015	0.008	22.169	0.585	0.585	0.000	0.000	0.000	0.000
82	A	73	ASN	0	0.042	0.015	24.782	-0.428	-0.428	0.000	0.000	0.000	0.000
83	A	74	LYS	1	0.906	0.910	19.932	14.625	14.625	0.000	0.000	0.000	0.000
84	A	75	ALA	0	0.034	0.025	25.265	-0.082	-0.082	0.000	0.000	0.000	0.000
85	A	76	ALA	0	-0.059	-0.018	28.008	0.255	0.255	0.000	0.000	0.000	0.000
86	A	77	ILE	0	-0.070	-0.037	21.914	-0.018	-0.018	0.000	0.000	0.000	0.000
87	A	78	LYS	1	0.970	0.999	23.700	12.388	12.388	0.000	0.000	0.000	0.000
88	A	79	LEU	0	0.040	-0.005	20.708	-0.712	-0.712	0.000	0.000	0.000	0.000
89	A	80	PRO	0	-0.021	-0.012	17.614	0.626	0.626	0.000	0.000	0.000	0.000
90	A	81	LEU	0	-0.002	0.014	18.348	0.097	0.097	0.000	0.000	0.000	0.000
91	A	82	ARG	1	0.770	0.881	20.846	12.151	12.151	0.000	0.000	0.000	0.000
92	A	83	ASP	-1	-0.774	-0.892	24.234	-10.750	-10.750	0.000	0.000	0.000	0.000
93	A	84	GLY	0	-0.016	-0.020	26.579	0.285	0.285	0.000	0.000	0.000	0.000
94	A	85	ASP	-1	-0.795	-0.876	28.303	-9.575	-9.575	0.000	0.000	0.000	0.000
95	A	86	VAL	0	-0.038	-0.028	30.477	0.311	0.311	0.000	0.000	0.000	0.000
96	A	87	GLU	-1	-0.835	-0.896	27.732	-10.837	-10.837	0.000	0.000	0.000	0.000
97	A	88	ARG	1	0.839	0.917	28.917	10.151	10.151	0.000	0.000	0.000	0.000
98	A	89	ASP	-1	-0.871	-0.915	32.662	-8.301	-8.301	0.000	0.000	0.000	0.000
99	A	90	ASP	-1	-0.891	-0.950	32.237	-9.068	-9.068	0.000	0.000	0.000	0.000
100	A	91	GLU	-1	-0.899	-0.977	32.787	-8.533	-8.533	0.000	0.000	0.000	0.000
101	A	92	ALA	0	-0.059	-0.017	29.411	-0.158	-0.158	0.000	0.000	0.000	0.000
102	A	93	TYR	0	-0.039	-0.050	26.957	-0.556	-0.556	0.000	0.000	0.000	0.000
103	A	94	LYS	1	0.978	1.010	28.595	8.626	8.626	0.000	0.000	0.000	0.000
104	A	95	GLY	0	-0.008	0.007	28.500	-0.151	-0.151	0.000	0.000	0.000	0.000
105	A	96	HIS	0	-0.099	-0.056	23.621	-0.688	-0.688	0.000	0.000	0.000	0.000
106	A	97	TYR	0	0.033	0.015	21.415	0.263	0.263	0.000	0.000	0.000	0.000
107	A	98	PHE	0	-0.013	-0.015	22.060	-0.119	-0.119	0.000	0.000	0.000	0.000
108	A	99	VAL	0	0.000	0.009	17.477	-0.120	-0.120	0.000	0.000	0.000	0.000
109	A	100	ASN	0	-0.014	0.006	20.701	0.234	0.234	0.000	0.000	0.000	0.000
110	A	101	ALA	0	0.009	0.014	17.193	-0.311	-0.311	0.000	0.000	0.000	0.000
111	A	102	ASN	0	-0.030	-0.030	18.256	0.392	0.392	0.000	0.000	0.000	0.000
112	A	103	SER	0	0.040	0.027	16.774	-1.137	-1.137	0.000	0.000	0.000	0.000
113	A	104	LYS	1	0.960	0.971	18.505	13.964	13.964	0.000	0.000	0.000	0.000
114	A	105	THR	0	-0.004	0.010	16.561	0.681	0.681	0.000	0.000	0.000	0.000
115	A	106	PRO	0	0.028	0.015	18.821	-0.387	-0.387	0.000	0.000	0.000	0.000
116	A	107	PRO	0	-0.021	0.016	16.768	-0.876	-0.876	0.000	0.000	0.000	0.000
117	A	108	GLN	0	-0.001	-0.013	13.998	0.069	0.069	0.000	0.000	0.000	0.000
118	A	109	ILE	0	-0.009	-0.003	16.966	-0.752	-0.752	0.000	0.000	0.000	0.000
119	A	110	VAL	0	-0.006	0.007	15.643	0.453	0.453	0.000	0.000	0.000	0.000
120	A	111	ASP	-1	-0.696	-0.837	18.960	-13.809	-13.809	0.000	0.000	0.000	0.000
121	A	112	LYS	1	0.958	0.957	18.492	12.541	12.541	0.000	0.000	0.000	0.000
122	A	113	ALA	0	-0.057	-0.020	18.337	-0.433	-0.433	0.000	0.000	0.000	0.000
123	A	114	VAL	0	-0.057	-0.029	13.642	-0.555	-0.555	0.000	0.000	0.000	0.000
124	A	115	ARG	1	0.895	0.939	16.930	12.419	12.419	0.000	0.000	0.000	0.000
125	A	116	PRO	0	-0.004	-0.013	19.462	0.037	0.037	0.000	0.000	0.000	0.000
126	A	117	ILE	0	-0.001	0.007	21.101	0.492	0.492	0.000	0.000	0.000	0.000
127	A	118	LEU	0	-0.035	-0.024	23.769	-0.059	-0.059	0.000	0.000	0.000	0.000
128	A	119	ASP	-1	-0.814	-0.898	27.090	-9.541	-9.541	0.000	0.000	0.000	0.000
129	A	120	ARG	1	0.893	0.930	27.723	10.609	10.609	0.000	0.000	0.000	0.000
130	A	121	ASN	0	0.002	-0.005	28.726	-0.209	-0.209	0.000	0.000	0.000	0.000
131	A	122	GLU	-1	-0.922	-0.943	26.613	-10.483	-10.483	0.000	0.000	0.000	0.000
132	A	123	VAL	0	-0.093	-0.057	22.927	-0.429	-0.429	0.000	0.000	0.000	0.000
133	A	124	TYR	0	0.045	0.019	26.063	0.085	0.085	0.000	0.000	0.000	0.000
134	A	125	SER	0	0.019	-0.008	27.197	-0.487	-0.487	0.000	0.000	0.000	0.000
135	A	126	GLY	0	0.059	0.042	27.328	0.407	0.407	0.000	0.000	0.000	0.000
136	A	127	CYS	0	-0.064	0.013	24.958	-0.113	-0.113	0.000	0.000	0.000	0.000
137	A	128	TYR	0	0.008	-0.009	22.560	-0.245	-0.245	0.000	0.000	0.000	0.000
138	A	129	ALA	0	0.053	0.001	19.593	0.034	0.034	0.000	0.000	0.000	0.000
139	A	130	ARG	1	0.828	0.935	10.347	20.755	20.755	0.000	0.000	0.000	0.000
140	A	131	VAL	0	0.041	0.010	15.120	-0.016	-0.016	0.000	0.000	0.000	0.000
141	A	132	SER	0	-0.033	-0.012	10.142	-1.929	-1.929	0.000	0.000	0.000	0.000
142	A	133	LEU	0	-0.022	-0.001	11.235	1.224	1.224	0.000	0.000	0.000	0.000
143	A	134	ASN	0	0.013	0.006	7.882	-5.833	-5.833	0.000	0.000	0.000	0.000
144	A	135	PHE	0	-0.003	0.000	10.739	2.514	2.514	0.000	0.000	0.000	0.000
145	A	136	TYR	0	0.030	0.004	11.651	-1.339	-1.339	0.000	0.000	0.000	0.000
146	A	137	ALA	0	0.033	0.020	13.954	1.304	1.304	0.000	0.000	0.000	0.000
147	A	138	PHE	0	-0.047	-0.021	17.166	-0.111	-0.111	0.000	0.000	0.000	0.000
148	A	139	ASN	0	-0.014	-0.028	19.972	0.676	0.676	0.000	0.000	0.000	0.000
149	A	140	SER	0	0.056	0.025	23.441	-0.042	-0.042	0.000	0.000	0.000	0.000
150	A	141	ASN	0	0.002	-0.002	25.802	0.253	0.253	0.000	0.000	0.000	0.000
151	A	142	GLY	0	0.024	0.023	28.749	0.151	0.151	0.000	0.000	0.000	0.000
152	A	143	ASN	0	-0.032	0.001	26.213	0.211	0.211	0.000	0.000	0.000	0.000
153	A	144	LYS	1	0.999	0.977	23.929	10.679	10.679	0.000	0.000	0.000	0.000
154	A	145	GLY	0	0.003	0.016	21.955	0.458	0.458	0.000	0.000	0.000	0.000
155	A	146	VAL	0	-0.037	-0.004	16.025	-0.504	-0.504	0.000	0.000	0.000	0.000
156	A	147	ALA	0	-0.006	0.009	17.466	0.743	0.743	0.000	0.000	0.000	0.000
157	A	148	CYS	0	-0.003	-0.018	14.841	-1.041	-1.041	0.000	0.000	0.000	0.000
158	A	149	GLY	0	0.002	0.012	14.013	0.986	0.986	0.000	0.000	0.000	0.000
159	A	150	LEU	0	-0.023	-0.020	13.797	-1.174	-1.174	0.000	0.000	0.000	0.000
160	A	151	GLY	0	0.016	0.007	12.407	-0.577	-0.577	0.000	0.000	0.000	0.000
161	A	152	ASN	0	0.000	-0.018	11.485	2.379	2.379	0.000	0.000	0.000	0.000
162	A	153	ILE	0	0.039	0.024	14.704	-0.289	-0.289	0.000	0.000	0.000	0.000
163	A	154	GLN	0	-0.038	-0.012	15.328	-0.421	-0.421	0.000	0.000	0.000	0.000
164	A	155	LYS	1	0.850	0.921	17.386	11.766	11.766	0.000	0.000	0.000	0.000
165	A	156	ILE	0	-0.117	-0.056	17.670	-0.135	-0.135	0.000	0.000	0.000	0.000
166	A	157	ARG	1	0.940	0.956	21.705	11.534	11.534	0.000	0.000	0.000	0.000
167	A	158	ASP	-1	-0.757	-0.863	25.295	-10.729	-10.729	0.000	0.000	0.000	0.000
168	A	159	GLY	0	-0.030	-0.032	28.378	-0.095	-0.095	0.000	0.000	0.000	0.000
169	A	160	GLU	-1	-0.925	-0.950	29.665	-8.529	-8.529	0.000	0.000	0.000	0.000
170	A	161	PRO	0	0.050	0.023	31.552	-0.324	-0.324	0.000	0.000	0.000	0.000
171	A	162	LEU	0	-0.059	-0.023	28.933	0.167	0.167	0.000	0.000	0.000	0.000
172	A	163	GLY	0	0.028	0.019	32.734	-0.051	-0.051	0.000	0.000	0.000	0.000
173	A	164	GLY	0	-0.023	-0.018	32.949	-0.300	-0.300	0.000	0.000	0.000	0.000
174	A	165	ARG	1	0.957	0.966	27.380	10.874	10.874	0.000	0.000	0.000	0.000
175	A	166	THR	0	-0.012	-0.013	34.691	0.009	0.009	0.000	0.000	0.000	0.000
176	A	167	ASN	0	-0.013	-0.005	33.857	0.337	0.337	0.000	0.000	0.000	0.000
177	A	168	ALA	0	0.110	0.060	37.623	-0.020	-0.020	0.000	0.000	0.000	0.000
178	A	169	ALA	0	-0.041	-0.024	40.740	0.098	0.098	0.000	0.000	0.000	0.000
179	A	170	ASP	-1	-0.952	-0.968	35.935	-8.651	-8.651	0.000	0.000	0.000	0.000
180	A	171	ASP	-1	-0.963	-0.959	38.522	-8.338	-8.338	0.000	0.000	0.000	0.000
181	A	172	PHE	0	-0.106	-0.060	40.965	0.170	0.170	0.000	0.000	0.000	0.000
182	A	173	THR	0	0.037	0.022	44.514	-0.086	-0.086	0.000	0.000	0.000	0.000
183	A	174	THR	0	-0.019	-0.015	47.090	0.020	0.020	0.000	0.000	0.000	0.000
184	A	175	ILE	0	-0.037	-0.017	50.284	0.020	0.020	0.000	0.000	0.000	0.000
185	A	176	GLU	-1	-0.967	-0.982	52.782	-5.930	-5.930	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:-11:LYS)