FMO DATABASE

FMODB ID: J3889

Calculation Name: 3D5N-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3D5N

Chain ID: A

ChEMBL ID:

UniProt ID: Q97W15

Base Structure: X-ray

Registration Date: 2023-06-21

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	177
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1935552.247851
FMO2-HF: Nuclear repulsion	1865546.272236
FMO2-HF: Total energy	-70005.975615
FMO2-MP2: Total energy	-70209.21958

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.
-9.667	-4.8	8.709	-4.135	-9.44	-0.012

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 : 0.006 / q_NPA : 0.011

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	3	ILE	0	0.007	-0.007	3.029	0.465	3.205	1.996	-1.428	-3.307	0.004
4	A	4	GLY	0	0.064	0.052	5.511	-0.834	-0.796	-0.001	-0.018	-0.019	0.000
5	A	5	VAL	0	-0.058	-0.036	9.308	0.299	0.299	0.000	0.000	0.000	0.000
6	A	6	ILE	0	0.015	0.008	12.170	-0.056	-0.056	0.000	0.000	0.000	0.000
7	A	7	ILE	0	-0.001	-0.002	15.218	0.045	0.045	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.012	-0.009	18.144	-0.016	-0.016	0.000	0.000	0.000	0.000
9	A	9	ALA	0	0.040	0.006	20.913	0.008	0.008	0.000	0.000	0.000	0.000
10	A	10	ALA	0	-0.061	-0.008	24.260	-0.005	-0.005	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.046	0.013	26.497	0.006	0.006	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.803	-0.877	24.643	-0.007	-0.007	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.007	0.005	29.037	0.005	0.005	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.893	0.938	31.160	-0.012	-0.012	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.826	0.897	25.822	-0.024	-0.024	0.000	0.000	0.000	0.000
16	A	16	PHE	0	0.039	0.005	27.797	-0.005	-0.005	0.000	0.000	0.000	0.000
17	A	17	GLY	0	0.048	0.009	28.245	0.000	0.000	0.000	0.000	0.000	0.000
18	A	18	GLY	0	0.034	0.014	29.277	0.000	0.000	0.000	0.000	0.000	0.000
19	A	19	ASP	-1	-0.785	-0.882	31.160	-0.013	-0.013	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.755	0.854	31.505	-0.007	-0.007	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.050	-0.019	26.428	0.001	0.001	0.000	0.000	0.000	0.000
22	A	22	LEU	0	0.016	0.011	29.429	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	23	ALA	0	-0.013	0.014	32.093	0.000	0.000	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.872	0.921	31.211	0.028	0.028	0.000	0.000	0.000	0.000
25	A	25	ILE	0	0.049	0.027	28.105	0.004	0.004	0.000	0.000	0.000	0.000
26	A	26	ASP	-1	-0.798	-0.877	29.509	-0.011	-0.011	0.000	0.000	0.000	0.000
27	A	27	ASN	0	-0.011	-0.010	31.211	-0.004	-0.004	0.000	0.000	0.000	0.000
28	A	28	THR	0	-0.033	-0.011	27.170	-0.005	-0.005	0.000	0.000	0.000	0.000
29	A	29	PRO	0	0.046	0.008	28.413	0.006	0.006	0.000	0.000	0.000	0.000
30	A	30	ILE	0	0.017	0.020	26.640	-0.006	-0.006	0.000	0.000	0.000	0.000
31	A	31	ILE	0	0.044	0.025	22.864	0.000	0.000	0.000	0.000	0.000	0.000
32	A	32	MET	0	0.007	0.007	22.859	-0.005	-0.005	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.774	0.881	22.334	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	34	THR	0	-0.010	-0.028	19.878	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	35	ILE	0	0.013	0.008	18.192	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.944	0.974	17.389	0.028	0.028	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.058	-0.014	15.952	-0.021	-0.021	0.000	0.000	0.000	0.000
38	A	38	TYR	0	0.037	-0.002	12.737	0.005	0.005	0.000	0.000	0.000	0.000
39	A	39	GLY	0	-0.059	-0.022	12.717	-0.085	-0.085	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.842	-0.919	10.322	-0.486	-0.486	0.000	0.000	0.000	0.000
41	A	41	LEU	0	0.011	0.014	7.464	-0.119	-0.119	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.798	-0.885	7.444	-1.417	-1.417	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.783	0.898	10.617	0.442	0.442	0.000	0.000	0.000	0.000
44	A	44	ILE	0	-0.004	0.015	14.025	-0.007	-0.007	0.000	0.000	0.000	0.000
45	A	45	ILE	0	-0.022	-0.009	16.874	0.036	0.036	0.000	0.000	0.000	0.000
46	A	46	ILE	0	-0.017	0.004	19.270	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	47	VAL	0	0.031	0.004	22.109	0.012	0.012	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.046	-0.003	25.865	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.786	0.903	28.943	0.009	0.009	0.000	0.000	0.000	0.000
50	A	50	TYR	0	0.020	0.020	31.106	0.003	0.003	0.000	0.000	0.000	0.000
51	A	51	VAL	0	0.036	0.009	28.657	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	52	ASN	0	-0.041	-0.016	30.902	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.838	-0.927	32.852	-0.040	-0.040	0.000	0.000	0.000	0.000
54	A	54	MET	0	-0.024	0.004	27.491	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	55	LEU	0	0.027	0.014	26.657	-0.006	-0.006	0.000	0.000	0.000	0.000
56	A	56	PRO	0	0.024	0.006	28.012	-0.008	-0.008	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.056	-0.027	27.359	-0.001	-0.001	0.000	0.000	0.000	0.000
58	A	58	LEU	0	-0.025	-0.027	22.761	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	59	MET	0	-0.027	-0.004	23.909	-0.011	-0.011	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.870	-0.913	21.626	-0.161	-0.161	0.000	0.000	0.000	0.000
61	A	61	GLN	0	-0.050	-0.029	18.376	-0.054	-0.054	0.000	0.000	0.000	0.000
62	A	62	ILE	0	0.029	0.017	15.804	0.018	0.018	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.013	-0.004	19.563	0.007	0.007	0.000	0.000	0.000	0.000
64	A	64	ILE	0	-0.021	-0.010	19.754	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	65	TYR	0	-0.010	-0.005	23.644	0.013	0.013	0.000	0.000	0.000	0.000
66	A	66	ASN	0	0.019	-0.007	24.898	-0.006	-0.006	0.000	0.000	0.000	0.000
67	A	67	PRO	0	-0.002	-0.004	26.822	0.007	0.007	0.000	0.000	0.000	0.000
68	A	68	PHE	0	0.016	0.001	27.891	0.004	0.004	0.000	0.000	0.000	0.000
69	A	69	TRP	0	0.036	0.022	27.774	0.007	0.007	0.000	0.000	0.000	0.000
70	A	70	ASN	0	-0.042	-0.024	28.783	0.005	0.005	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.892	-0.924	28.465	-0.009	-0.009	0.000	0.000	0.000	0.000
72	A	72	GLY	0	0.014	-0.014	28.146	0.005	0.005	0.000	0.000	0.000	0.000
73	A	73	ILE	0	-0.008	-0.015	22.100	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	74	SER	0	-0.067	-0.040	21.841	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	75	THR	0	0.012	-0.013	21.842	-0.006	-0.006	0.000	0.000	0.000	0.000
76	A	76	SER	0	-0.043	-0.054	22.348	-0.014	-0.014	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.043	-0.018	15.779	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.897	0.964	17.746	0.006	0.006	0.000	0.000	0.000	0.000
79	A	79	LEU	0	-0.063	-0.017	18.887	-0.018	-0.018	0.000	0.000	0.000	0.000
80	A	80	GLY	0	0.023	0.008	17.512	-0.022	-0.022	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.002	-0.001	12.039	-0.026	-0.026	0.000	0.000	0.000	0.000
82	A	82	ARG	1	0.898	0.937	14.546	0.074	0.074	0.000	0.000	0.000	0.000
83	A	83	PHE	0	-0.018	-0.003	13.707	-0.006	-0.006	0.000	0.000	0.000	0.000
84	A	84	PHE	0	0.036	0.024	10.319	-0.027	-0.027	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.933	0.977	10.481	0.202	0.202	0.000	0.000	0.000	0.000
86	A	86	ASP	-1	-0.910	-0.959	10.371	-0.467	-0.467	0.000	0.000	0.000	0.000
87	A	87	TYR	0	-0.042	-0.049	6.860	-0.184	-0.184	0.000	0.000	0.000	0.000
88	A	88	ASP	-1	-0.836	-0.919	2.322	-5.733	-4.010	3.313	-1.881	-3.155	-0.018
89	A	89	ALA	0	-0.029	-0.015	4.243	-0.259	0.054	0.001	-0.029	-0.284	0.000
90	A	90	VAL	0	-0.005	0.004	6.082	-0.233	-0.233	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.002	-0.001	9.035	0.074	0.074	0.000	0.000	0.000	0.000
92	A	92	VAL	0	-0.016	-0.006	10.931	-0.139	-0.139	0.000	0.000	0.000	0.000
93	A	93	ALA	0	0.025	0.000	14.411	0.024	0.024	0.000	0.000	0.000	0.000
94	A	94	LEU	0	-0.009	-0.002	16.760	-0.017	-0.017	0.000	0.000	0.000	0.000
95	A	95	GLY	0	0.043	0.005	20.605	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.870	-0.932	22.892	0.015	0.015	0.000	0.000	0.000	0.000
97	A	97	MET	0	0.008	0.009	21.475	0.013	0.013	0.000	0.000	0.000	0.000
98	A	98	PRO	0	-0.026	0.002	21.827	0.002	0.002	0.000	0.000	0.000	0.000
99	A	99	PHE	0	-0.022	-0.027	23.037	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	100	VAL	0	-0.017	0.017	17.455	0.005	0.005	0.000	0.000	0.000	0.000
101	A	101	THR	0	0.008	-0.028	18.923	-0.022	-0.022	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.906	0.935	13.139	0.258	0.258	0.000	0.000	0.000	0.000
103	A	103	GLU	-1	-0.782	-0.888	14.140	0.128	0.128	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.768	-0.827	15.066	0.156	0.156	0.000	0.000	0.000	0.000
105	A	105	VAL	0	0.018	0.006	10.799	0.067	0.067	0.000	0.000	0.000	0.000
106	A	106	ASN	0	-0.025	-0.017	10.405	0.056	0.056	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.855	0.922	10.211	-0.074	-0.074	0.000	0.000	0.000	0.000
108	A	108	ILE	0	-0.001	0.009	9.862	0.108	0.108	0.000	0.000	0.000	0.000
109	A	109	ILE	0	0.025	0.008	4.801	0.298	0.298	0.000	0.000	0.000	0.000
110	A	110	ASN	0	-0.038	-0.020	6.293	0.602	0.602	0.000	0.000	0.000	0.000
111	A	111	THR	0	-0.041	-0.026	8.149	-0.011	-0.011	0.000	0.000	0.000	0.000
112	A	112	PHE	0	-0.042	-0.005	2.311	-1.851	-1.798	3.400	-0.779	-2.675	0.002
113	A	113	LYS	1	0.889	0.924	5.807	-1.032	-1.032	0.000	0.000	0.000	0.000
114	A	114	PRO	0	0.039	0.007	5.578	0.023	0.023	0.000	0.000	0.000	0.000
115	A	115	ASN	0	0.004	0.008	6.949	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	116	CYS	0	-0.099	-0.021	7.844	-0.044	-0.044	0.000	0.000	0.000	0.000
117	A	117	LYS	1	0.909	0.941	8.163	-0.028	-0.028	0.000	0.000	0.000	0.000
118	A	118	ALA	0	-0.018	-0.006	9.856	0.019	0.019	0.000	0.000	0.000	0.000
119	A	119	VAL	0	-0.007	0.002	8.634	-0.055	-0.055	0.000	0.000	0.000	0.000
120	A	120	ILE	0	-0.034	-0.020	11.476	-0.022	-0.022	0.000	0.000	0.000	0.000
121	A	121	PRO	0	0.037	0.033	14.249	-0.008	-0.008	0.000	0.000	0.000	0.000
122	A	122	THR	0	-0.045	-0.033	16.524	-0.027	-0.027	0.000	0.000	0.000	0.000
123	A	123	HIS	0	0.045	0.011	20.148	-0.014	-0.014	0.000	0.000	0.000	0.000
124	A	124	LYS	1	0.866	0.910	23.348	-0.091	-0.091	0.000	0.000	0.000	0.000
125	A	125	GLY	0	0.018	0.023	24.736	-0.009	-0.009	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.880	-0.926	24.932	0.090	0.090	0.000	0.000	0.000	0.000
127	A	127	ARG	1	0.940	0.958	19.112	-0.168	-0.168	0.000	0.000	0.000	0.000
128	A	128	GLY	0	-0.005	-0.004	19.577	-0.020	-0.020	0.000	0.000	0.000	0.000
129	A	129	ASN	0	-0.065	-0.019	17.154	0.043	0.043	0.000	0.000	0.000	0.000
130	A	130	PRO	0	0.035	0.010	13.784	-0.018	-0.018	0.000	0.000	0.000	0.000
131	A	131	VAL	0	-0.001	-0.018	13.284	0.043	0.043	0.000	0.000	0.000	0.000
132	A	132	LEU	0	-0.004	0.016	5.956	-0.113	-0.113	0.000	0.000	0.000	0.000
133	A	133	ILE	0	-0.022	-0.013	9.686	0.047	0.047	0.000	0.000	0.000	0.000
134	A	134	SER	0	0.029	0.005	6.135	0.060	0.060	0.000	0.000	0.000	0.000
135	A	135	LYS	1	0.883	0.903	5.881	0.620	0.620	0.000	0.000	0.000	0.000
136	A	136	SER	0	-0.093	-0.049	8.004	-0.049	-0.049	0.000	0.000	0.000	0.000
137	A	137	LEU	0	0.018	-0.002	10.198	-0.022	-0.022	0.000	0.000	0.000	0.000
138	A	138	PHE	0	-0.005	0.013	8.432	-0.025	-0.025	0.000	0.000	0.000	0.000
139	A	139	ASN	0	-0.006	-0.006	13.087	-0.012	-0.012	0.000	0.000	0.000	0.000
140	A	140	GLU	-1	-0.830	-0.905	15.788	0.025	0.025	0.000	0.000	0.000	0.000
141	A	141	ILE	0	-0.036	-0.013	14.561	-0.005	-0.005	0.000	0.000	0.000	0.000
142	A	142	GLU	-1	-0.850	-0.956	16.823	-0.043	-0.043	0.000	0.000	0.000	0.000
143	A	143	LYS	1	0.784	0.886	19.174	-0.019	-0.019	0.000	0.000	0.000	0.000
144	A	144	LEU	0	-0.061	-0.006	19.944	-0.001	-0.001	0.000	0.000	0.000	0.000
145	A	145	ARG	1	0.964	0.976	22.697	-0.011	-0.011	0.000	0.000	0.000	0.000
146	A	146	GLY	0	0.089	0.054	26.159	0.006	0.006	0.000	0.000	0.000	0.000
147	A	147	ASP	-1	-0.800	-0.852	26.363	0.022	0.022	0.000	0.000	0.000	0.000
148	A	148	VAL	0	-0.040	-0.007	24.004	0.007	0.007	0.000	0.000	0.000	0.000
149	A	149	GLY	0	0.082	0.034	22.202	-0.002	-0.002	0.000	0.000	0.000	0.000
150	A	150	ALA	0	0.059	0.009	16.898	0.001	0.001	0.000	0.000	0.000	0.000
151	A	151	ARG	1	0.965	0.986	18.705	-0.081	-0.081	0.000	0.000	0.000	0.000
152	A	152	VAL	0	-0.019	-0.014	20.416	0.002	0.002	0.000	0.000	0.000	0.000
153	A	153	ILE	0	-0.004	-0.001	16.691	-0.009	-0.009	0.000	0.000	0.000	0.000
154	A	154	LEU	0	0.046	0.016	14.414	-0.001	-0.001	0.000	0.000	0.000	0.000
155	A	155	ASN	0	-0.063	-0.032	17.881	0.004	0.004	0.000	0.000	0.000	0.000
156	A	156	LYS	1	0.898	0.956	19.998	-0.075	-0.075	0.000	0.000	0.000	0.000
157	A	157	ILE	0	0.022	0.034	14.355	-0.010	-0.010	0.000	0.000	0.000	0.000
158	A	158	LYS	1	0.864	0.915	17.833	-0.089	-0.089	0.000	0.000	0.000	0.000
159	A	159	ILE	0	0.038	0.011	17.340	0.019	0.019	0.000	0.000	0.000	0.000
160	A	160	GLU	-1	-0.817	-0.892	17.713	0.132	0.132	0.000	0.000	0.000	0.000
161	A	161	GLU	-1	-0.863	-0.919	13.639	0.117	0.117	0.000	0.000	0.000	0.000
162	A	162	LEU	0	-0.058	-0.018	12.756	0.046	0.046	0.000	0.000	0.000	0.000
163	A	164	PHE	0	0.023	0.003	13.461	0.021	0.021	0.000	0.000	0.000	0.000
164	A	165	ILE	0	0.003	0.004	13.324	0.004	0.004	0.000	0.000	0.000	0.000
165	A	166	GLU	-1	-0.804	-0.888	16.986	0.137	0.137	0.000	0.000	0.000	0.000
166	A	167	CYS	0	-0.054	-0.016	16.874	0.025	0.025	0.000	0.000	0.000	0.000
167	A	168	SER	0	-0.022	-0.039	19.491	-0.018	-0.018	0.000	0.000	0.000	0.000
168	A	169	GLU	-1	-0.815	-0.905	22.159	0.060	0.060	0.000	0.000	0.000	0.000
169	A	170	GLY	0	0.047	0.020	23.007	0.000	0.000	0.000	0.000	0.000	0.000
170	A	171	VAL	0	-0.013	-0.006	18.260	-0.003	-0.003	0.000	0.000	0.000	0.000
171	A	172	LEU	0	-0.072	-0.024	20.880	0.008	0.008	0.000	0.000	0.000	0.000
172	A	173	ILE	0	-0.031	-0.009	23.923	-0.007	-0.007	0.000	0.000	0.000	0.000
173	A	174	ASP	-1	-0.827	-0.902	24.995	0.040	0.040	0.000	0.000	0.000	0.000
174	A	175	ILE	0	-0.025	-0.034	26.646	-0.001	-0.001	0.000	0.000	0.000	0.000
175	A	176	ASP	-1	-0.779	-0.874	29.745	0.012	0.012	0.000	0.000	0.000	0.000
176	A	177	LYS	1	0.743	0.881	26.546	-0.074	-0.074	0.000	0.000	0.000	0.000
177	A	178	LYS	1	0.760	0.870	29.211	-0.044	-0.044	0.000	0.000	0.000	0.000

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