FMO DATABASE

FMODB ID: N1RRQ

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	OptHSide
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	-1937441.836315
FMO2-HF: Nuclear repulsion	1867436.775144
FMO2-HF: Total energy	-70005.061171
FMO2-MP2: Total energy	-70208.473922

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.
-10.591	-5.333	8.947	-4.357	-9.849	-0.017

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 : 0.005 / q_NPA : 0.010

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	-0.009	3.073	0.120	2.834	1.960	-1.406	-3.267	0.004
4	A	4	GLY	0	0.057	0.043	5.553	-0.805	-0.767	-0.001	-0.018	-0.019	0.000
5	A	5	VAL	0	-0.058	-0.023	9.263	0.287	0.287	0.000	0.000	0.000	0.000
6	A	6	ILE	0	0.007	-0.001	11.811	-0.061	-0.061	0.000	0.000	0.000	0.000
7	A	7	ILE	0	-0.023	-0.017	14.849	0.041	0.041	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.002	-0.004	17.805	-0.016	-0.016	0.000	0.000	0.000	0.000
9	A	9	ALA	0	0.028	-0.002	20.458	0.005	0.005	0.000	0.000	0.000	0.000
10	A	10	ALA	0	-0.042	0.001	23.866	-0.006	-0.006	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.055	-0.010	26.187	0.004	0.004	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.855	-0.882	24.283	0.004	0.004	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.039	0.017	28.801	0.005	0.005	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.892	0.941	30.939	-0.015	-0.015	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.819	0.887	25.710	-0.030	-0.030	0.000	0.000	0.000	0.000
16	A	16	PHE	0	0.031	0.009	27.841	-0.005	-0.005	0.000	0.000	0.000	0.000
17	A	17	GLY	0	0.066	0.004	28.523	0.000	0.000	0.000	0.000	0.000	0.000
18	A	18	GLY	0	-0.013	-0.019	29.137	0.000	0.000	0.000	0.000	0.000	0.000
19	A	19	ASP	-1	-0.762	-0.877	31.042	-0.009	-0.009	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.860	0.931	31.454	-0.010	-0.010	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.063	-0.023	26.078	0.000	0.000	0.000	0.000	0.000	0.000
22	A	22	LEU	0	0.036	0.022	29.063	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	23	ALA	0	-0.023	0.007	31.668	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.857	0.919	31.051	0.023	0.023	0.000	0.000	0.000	0.000
25	A	25	ILE	0	0.040	0.019	28.006	0.004	0.004	0.000	0.000	0.000	0.000
26	A	26	ASP	-1	-0.820	-0.885	29.518	-0.004	-0.004	0.000	0.000	0.000	0.000
27	A	27	ASN	0	-0.022	-0.024	31.248	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	28	THR	0	0.014	0.006	27.690	-0.004	-0.004	0.000	0.000	0.000	0.000
29	A	29	PRO	0	0.027	0.010	28.285	0.005	0.005	0.000	0.000	0.000	0.000
30	A	30	ILE	0	0.018	0.016	26.237	-0.004	-0.004	0.000	0.000	0.000	0.000
31	A	31	ILE	0	0.033	0.023	22.844	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	32	MET	0	0.018	0.008	22.888	-0.004	-0.004	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.800	0.897	22.442	-0.005	-0.005	0.000	0.000	0.000	0.000
34	A	34	THR	0	-0.022	-0.048	19.735	-0.007	-0.007	0.000	0.000	0.000	0.000
35	A	35	ILE	0	0.024	0.016	18.271	-0.003	-0.003	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.958	0.994	17.313	0.024	0.024	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.030	-0.016	15.809	-0.028	-0.028	0.000	0.000	0.000	0.000
38	A	38	TYR	0	0.031	0.009	12.545	0.019	0.019	0.000	0.000	0.000	0.000
39	A	39	GLY	0	-0.077	-0.042	12.392	-0.085	-0.085	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.920	-0.953	9.785	-0.532	-0.532	0.000	0.000	0.000	0.000
41	A	41	LEU	0	0.014	0.029	7.091	-0.132	-0.132	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.806	-0.890	8.066	-1.071	-1.071	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.830	0.927	10.830	0.392	0.392	0.000	0.000	0.000	0.000
44	A	44	ILE	0	0.052	0.028	14.140	-0.014	-0.014	0.000	0.000	0.000	0.000
45	A	45	ILE	0	-0.034	-0.004	17.060	0.034	0.034	0.000	0.000	0.000	0.000
46	A	46	ILE	0	-0.018	0.003	18.904	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	47	VAL	0	0.007	-0.007	21.971	0.012	0.012	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.074	0.019	25.659	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.793	0.918	28.526	0.005	0.005	0.000	0.000	0.000	0.000
50	A	50	TYR	0	0.022	0.024	30.713	0.002	0.002	0.000	0.000	0.000	0.000
51	A	51	VAL	0	0.031	0.012	28.755	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	52	ASN	0	-0.044	-0.020	30.810	-0.004	-0.004	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.839	-0.918	33.116	-0.030	-0.030	0.000	0.000	0.000	0.000
54	A	54	MET	0	-0.037	-0.005	27.706	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	55	LEU	0	0.050	0.012	26.693	-0.005	-0.005	0.000	0.000	0.000	0.000
56	A	56	PRO	0	0.006	0.013	28.110	-0.008	-0.008	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.038	-0.026	27.477	0.000	0.000	0.000	0.000	0.000	0.000
58	A	58	LEU	0	-0.061	-0.042	22.978	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	59	MET	0	-0.026	-0.005	24.076	-0.009	-0.009	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.879	-0.914	21.705	-0.144	-0.144	0.000	0.000	0.000	0.000
61	A	61	GLN	0	-0.047	-0.029	18.456	-0.046	-0.046	0.000	0.000	0.000	0.000
62	A	62	ILE	0	0.025	0.023	16.371	0.013	0.013	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.017	-0.016	20.020	0.006	0.006	0.000	0.000	0.000	0.000
64	A	64	ILE	0	-0.013	-0.002	19.702	0.001	0.001	0.000	0.000	0.000	0.000
65	A	65	TYR	0	0.003	-0.003	23.510	0.011	0.011	0.000	0.000	0.000	0.000
66	A	66	ASN	0	0.041	-0.009	24.812	-0.006	-0.006	0.000	0.000	0.000	0.000
67	A	67	PRO	0	-0.030	-0.009	26.781	0.006	0.006	0.000	0.000	0.000	0.000
68	A	68	PHE	0	0.022	-0.002	27.903	0.003	0.003	0.000	0.000	0.000	0.000
69	A	69	TRP	0	0.060	0.030	27.597	0.006	0.006	0.000	0.000	0.000	0.000
70	A	70	ASN	0	-0.044	-0.023	28.597	0.006	0.006	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.984	-0.982	29.005	-0.007	-0.007	0.000	0.000	0.000	0.000
72	A	72	GLY	0	-0.009	-0.023	28.003	0.004	0.004	0.000	0.000	0.000	0.000
73	A	73	ILE	0	0.016	-0.013	22.018	-0.002	-0.002	0.000	0.000	0.000	0.000
74	A	74	SER	0	-0.102	-0.051	21.753	0.000	0.000	0.000	0.000	0.000	0.000
75	A	75	THR	0	0.048	0.018	21.859	-0.005	-0.005	0.000	0.000	0.000	0.000
76	A	76	SER	0	-0.036	-0.043	22.166	-0.013	-0.013	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.049	-0.027	15.868	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.884	0.953	17.609	0.002	0.002	0.000	0.000	0.000	0.000
79	A	79	LEU	0	-0.059	-0.008	18.889	-0.017	-0.017	0.000	0.000	0.000	0.000
80	A	80	GLY	0	0.025	-0.005	17.242	-0.020	-0.020	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.005	0.000	12.001	-0.018	-0.018	0.000	0.000	0.000	0.000
82	A	82	ARG	1	0.912	0.952	14.427	0.064	0.064	0.000	0.000	0.000	0.000
83	A	83	PHE	0	-0.015	-0.007	13.866	-0.010	-0.010	0.000	0.000	0.000	0.000
84	A	84	PHE	0	0.037	0.032	10.339	-0.017	-0.017	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.937	0.984	10.610	0.184	0.184	0.000	0.000	0.000	0.000
86	A	86	ASP	-1	-0.927	-0.973	10.668	-0.395	-0.395	0.000	0.000	0.000	0.000
87	A	87	TYR	0	-0.031	-0.036	6.939	-0.138	-0.138	0.000	0.000	0.000	0.000
88	A	88	ASP	-1	-0.871	-0.949	2.252	-6.365	-4.403	3.625	-2.137	-3.450	-0.022
89	A	89	ALA	0	-0.042	-0.027	4.262	-0.423	-0.114	0.001	-0.033	-0.278	0.000
90	A	90	VAL	0	0.010	0.012	6.012	-0.117	-0.117	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.006	-0.014	8.949	0.091	0.091	0.000	0.000	0.000	0.000
92	A	92	VAL	0	-0.034	-0.021	10.527	-0.141	-0.141	0.000	0.000	0.000	0.000
93	A	93	ALA	0	0.000	0.004	14.126	0.006	0.006	0.000	0.000	0.000	0.000
94	A	94	LEU	0	0.006	0.001	16.480	-0.016	-0.016	0.000	0.000	0.000	0.000
95	A	95	GLY	0	0.071	0.021	20.265	-0.006	-0.006	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.902	-0.940	22.553	0.023	0.023	0.000	0.000	0.000	0.000
97	A	97	MET	0	0.003	0.004	21.137	0.012	0.012	0.000	0.000	0.000	0.000
98	A	98	PRO	0	-0.029	-0.004	21.274	0.002	0.002	0.000	0.000	0.000	0.000
99	A	99	PHE	0	-0.017	-0.027	23.082	-0.007	-0.007	0.000	0.000	0.000	0.000
100	A	100	VAL	0	-0.012	0.030	16.784	0.006	0.006	0.000	0.000	0.000	0.000
101	A	101	THR	0	-0.001	-0.036	18.760	-0.021	-0.021	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.917	0.927	14.435	0.163	0.163	0.000	0.000	0.000	0.000
103	A	103	GLU	-1	-0.802	-0.899	13.966	0.120	0.120	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.760	-0.823	14.429	0.147	0.147	0.000	0.000	0.000	0.000
105	A	105	VAL	0	0.038	0.009	10.617	0.065	0.065	0.000	0.000	0.000	0.000
106	A	106	ASN	0	-0.024	-0.010	10.056	0.049	0.049	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.892	0.944	9.762	-0.075	-0.075	0.000	0.000	0.000	0.000
108	A	108	ILE	0	0.001	0.004	9.832	0.097	0.097	0.000	0.000	0.000	0.000
109	A	109	ILE	0	0.028	0.010	4.657	0.175	0.284	-0.001	-0.004	-0.104	0.000
110	A	110	ASN	0	-0.036	-0.019	5.899	0.556	0.556	0.000	0.000	0.000	0.000
111	A	111	THR	0	-0.057	-0.024	7.939	-0.031	-0.031	0.000	0.000	0.000	0.000
112	A	112	PHE	0	-0.037	-0.013	2.303	-1.880	-1.815	3.364	-0.756	-2.674	0.001
113	A	113	LYS	1	0.882	0.917	5.397	-0.830	-0.830	0.000	0.000	0.000	0.000
114	A	114	PRO	0	0.048	0.009	5.236	0.055	0.055	0.000	0.000	0.000	0.000
115	A	115	ASN	0	-0.001	0.002	6.591	0.016	0.016	0.000	0.000	0.000	0.000
116	A	116	CYS	0	-0.102	-0.024	7.770	-0.020	-0.020	0.000	0.000	0.000	0.000
117	A	117	LYS	1	0.911	0.949	7.886	-0.052	-0.052	0.000	0.000	0.000	0.000
118	A	118	ALA	0	0.001	-0.006	9.599	0.035	0.035	0.000	0.000	0.000	0.000
119	A	119	VAL	0	-0.019	0.010	8.372	-0.066	-0.066	0.000	0.000	0.000	0.000
120	A	120	ILE	0	-0.058	-0.045	11.184	-0.032	-0.032	0.000	0.000	0.000	0.000
121	A	121	PRO	0	0.043	0.041	14.111	-0.015	-0.015	0.000	0.000	0.000	0.000
122	A	122	THR	0	-0.053	-0.047	16.245	-0.026	-0.026	0.000	0.000	0.000	0.000
123	A	123	HIS	0	0.034	0.024	19.747	-0.012	-0.012	0.000	0.000	0.000	0.000
124	A	124	LYS	1	0.904	0.939	22.893	-0.090	-0.090	0.000	0.000	0.000	0.000
125	A	125	GLY	0	0.009	0.016	24.920	-0.009	-0.009	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.911	-0.955	24.519	0.093	0.093	0.000	0.000	0.000	0.000
127	A	127	ARG	1	0.943	0.964	19.218	-0.156	-0.156	0.000	0.000	0.000	0.000
128	A	128	GLY	0	0.010	-0.005	19.461	-0.020	-0.020	0.000	0.000	0.000	0.000
129	A	129	ASN	0	-0.103	-0.035	17.084	0.040	0.040	0.000	0.000	0.000	0.000
130	A	130	PRO	0	0.045	0.009	13.750	-0.021	-0.021	0.000	0.000	0.000	0.000
131	A	131	VAL	0	0.024	-0.011	13.153	0.041	0.041	0.000	0.000	0.000	0.000
132	A	132	LEU	0	-0.019	0.008	5.780	-0.183	-0.122	-0.001	-0.003	-0.057	0.000
133	A	133	ILE	0	-0.001	-0.002	9.793	0.001	0.001	0.000	0.000	0.000	0.000
134	A	134	SER	0	0.047	0.011	5.957	0.081	0.081	0.000	0.000	0.000	0.000
135	A	135	LYS	1	0.897	0.930	6.192	0.494	0.494	0.000	0.000	0.000	0.000
136	A	136	SER	0	-0.079	-0.040	8.245	-0.038	-0.038	0.000	0.000	0.000	0.000
137	A	137	LEU	0	0.003	-0.019	10.285	-0.022	-0.022	0.000	0.000	0.000	0.000
138	A	138	PHE	0	-0.010	0.020	8.271	-0.019	-0.019	0.000	0.000	0.000	0.000
139	A	139	ASN	0	-0.001	-0.006	12.960	-0.010	-0.010	0.000	0.000	0.000	0.000
140	A	140	GLU	-1	-0.823	-0.906	15.538	0.028	0.028	0.000	0.000	0.000	0.000
141	A	141	ILE	0	-0.022	-0.005	14.468	-0.006	-0.006	0.000	0.000	0.000	0.000
142	A	142	GLU	-1	-0.869	-0.960	16.892	-0.028	-0.028	0.000	0.000	0.000	0.000
143	A	143	LYS	1	0.787	0.882	19.144	-0.013	-0.013	0.000	0.000	0.000	0.000
144	A	144	LEU	0	-0.072	-0.009	19.599	-0.002	-0.002	0.000	0.000	0.000	0.000
145	A	145	ARG	1	0.968	0.977	22.524	-0.014	-0.014	0.000	0.000	0.000	0.000
146	A	146	GLY	0	0.111	0.057	25.994	0.006	0.006	0.000	0.000	0.000	0.000
147	A	147	ASP	-1	-0.762	-0.827	26.259	0.025	0.025	0.000	0.000	0.000	0.000
148	A	148	VAL	0	-0.077	-0.014	23.702	0.007	0.007	0.000	0.000	0.000	0.000
149	A	149	GLY	0	0.080	0.029	21.718	-0.001	-0.001	0.000	0.000	0.000	0.000
150	A	150	ALA	0	0.092	0.023	16.522	-0.004	-0.004	0.000	0.000	0.000	0.000
151	A	151	ARG	1	0.953	0.976	18.412	-0.083	-0.083	0.000	0.000	0.000	0.000
152	A	152	VAL	0	-0.011	-0.006	20.242	-0.001	-0.001	0.000	0.000	0.000	0.000
153	A	153	ILE	0	0.006	0.002	16.265	-0.005	-0.005	0.000	0.000	0.000	0.000
154	A	154	LEU	0	0.038	0.024	14.242	0.001	0.001	0.000	0.000	0.000	0.000
155	A	155	ASN	0	-0.087	-0.044	17.793	-0.001	-0.001	0.000	0.000	0.000	0.000
156	A	156	LYS	1	0.933	0.971	19.970	-0.069	-0.069	0.000	0.000	0.000	0.000
157	A	157	ILE	0	0.014	0.023	14.581	-0.007	-0.007	0.000	0.000	0.000	0.000
158	A	158	LYS	1	0.883	0.928	18.302	-0.065	-0.065	0.000	0.000	0.000	0.000
159	A	159	ILE	0	0.060	0.029	17.198	0.017	0.017	0.000	0.000	0.000	0.000
160	A	160	GLU	-1	-0.846	-0.906	17.670	0.107	0.107	0.000	0.000	0.000	0.000
161	A	161	GLU	-1	-0.872	-0.939	13.502	0.079	0.079	0.000	0.000	0.000	0.000
162	A	162	LEU	0	-0.057	-0.004	12.535	0.045	0.045	0.000	0.000	0.000	0.000
163	A	164	PHE	0	0.025	0.020	13.362	0.050	0.050	0.000	0.000	0.000	0.000
164	A	165	ILE	0	0.025	0.003	12.927	0.016	0.016	0.000	0.000	0.000	0.000
165	A	166	GLU	-1	-0.850	-0.914	16.482	0.138	0.138	0.000	0.000	0.000	0.000
166	A	167	CYS	0	-0.078	-0.014	16.094	0.014	0.014	0.000	0.000	0.000	0.000
167	A	168	SER	0	-0.009	-0.047	18.746	-0.016	-0.016	0.000	0.000	0.000	0.000
168	A	169	GLU	-1	-0.830	-0.935	21.700	0.064	0.064	0.000	0.000	0.000	0.000
169	A	170	GLY	0	0.016	0.008	22.436	-0.002	-0.002	0.000	0.000	0.000	0.000
170	A	171	VAL	0	-0.042	-0.016	17.881	-0.001	-0.001	0.000	0.000	0.000	0.000
171	A	172	LEU	0	-0.065	-0.022	20.638	0.010	0.010	0.000	0.000	0.000	0.000
172	A	173	ILE	0	-0.048	-0.014	23.823	-0.008	-0.008	0.000	0.000	0.000	0.000
173	A	174	ASP	-1	-0.823	-0.910	24.556	0.049	0.049	0.000	0.000	0.000	0.000
174	A	175	ILE	0	-0.037	-0.046	26.383	-0.003	-0.003	0.000	0.000	0.000	0.000
175	A	176	ASP	-1	-0.825	-0.920	29.331	0.017	0.017	0.000	0.000	0.000	0.000
176	A	177	LYS	1	0.759	0.906	26.452	-0.073	-0.073	0.000	0.000	0.000	0.000
177	A	178	LYS	1	0.879	0.959	29.151	-0.043	-0.043	0.000	0.000	0.000	0.000

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