FMO DATABASE

FMODB ID: 669GZ

Calculation Name: 3PIM-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3PIM

Chain ID: A

ChEMBL ID:

UniProt ID: P40029

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:

Apendix: None

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
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1989555.796583
FMO2-HF: Nuclear repulsion	1916967.70973
FMO2-HF: Total energy	-72588.086853
FMO2-MP2: Total energy	-72799.113183

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:-2:HIS)

Summations of interaction energy for fragment #1(A:-2:HIS)

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.
-5.395	-1.716	2.562	-2.131	-4.11	-0.013

Interaction energy analysis for fragmet #1(A:-2:HIS)

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	0	HIS	0	-0.008	0.000	2.693	-5.468	-2.062	2.564	-2.120	-3.850	-0.013
4	A	1	GLY	0	0.057	0.031	4.839	-0.128	0.025	-0.001	-0.008	-0.144	0.000
5	A	2	SER	0	0.004	-0.014	4.683	-0.055	0.065	-0.001	-0.003	-0.116	0.000
6	A	3	SER	0	-0.023	-0.003	6.409	-0.069	-0.069	0.000	0.000	0.000	0.000
7	A	4	LEU	0	-0.004	0.014	8.053	-0.123	-0.123	0.000	0.000	0.000	0.000
8	A	5	ILE	0	-0.037	-0.027	9.971	-0.206	-0.206	0.000	0.000	0.000	0.000
9	A	6	SER	0	-0.036	-0.036	11.596	0.079	0.079	0.000	0.000	0.000	0.000
10	A	7	LYS	1	0.818	0.860	9.556	-1.031	-1.031	0.000	0.000	0.000	0.000
11	A	8	THR	0	-0.030	-0.019	13.033	-0.132	-0.132	0.000	0.000	0.000	0.000
12	A	9	ILE	0	-0.071	-0.009	15.160	-0.034	-0.034	0.000	0.000	0.000	0.000
13	A	10	LYS	1	0.881	0.933	16.206	0.186	0.186	0.000	0.000	0.000	0.000
14	A	11	TYR	0	-0.002	-0.016	13.173	0.054	0.054	0.000	0.000	0.000	0.000
15	A	12	ASP	-1	-0.784	-0.883	15.044	-0.744	-0.744	0.000	0.000	0.000	0.000
16	A	13	PRO	0	0.018	0.010	11.865	0.079	0.079	0.000	0.000	0.000	0.000
17	A	14	ALA	0	-0.031	0.000	15.091	0.033	0.033	0.000	0.000	0.000	0.000
18	A	15	LYS	1	0.705	0.827	17.240	0.507	0.507	0.000	0.000	0.000	0.000
19	A	16	ASP	-1	-0.796	-0.879	18.627	-0.296	-0.296	0.000	0.000	0.000	0.000
20	A	17	LYS	1	0.823	0.900	17.952	0.078	0.078	0.000	0.000	0.000	0.000
21	A	18	LEU	0	0.042	0.024	14.173	0.000	0.000	0.000	0.000	0.000	0.000
22	A	19	ILE	0	-0.047	-0.023	18.253	0.013	0.013	0.000	0.000	0.000	0.000
23	A	20	THR	0	0.038	0.009	17.530	-0.004	-0.004	0.000	0.000	0.000	0.000
24	A	21	LEU	0	-0.042	-0.005	20.184	0.009	0.009	0.000	0.000	0.000	0.000
25	A	22	ALA	0	0.064	0.033	23.724	0.004	0.004	0.000	0.000	0.000	0.000
26	A	23	CYS	0	0.004	0.012	25.795	-0.010	-0.010	0.000	0.000	0.000	0.000
27	A	24	GLY	0	0.021	0.015	28.923	-0.012	-0.012	0.000	0.000	0.000	0.000
28	A	25	CYS	0	-0.015	-0.007	28.509	0.011	0.011	0.000	0.000	0.000	0.000
29	A	26	PHE	0	0.070	0.030	23.322	-0.022	-0.022	0.000	0.000	0.000	0.000
30	A	27	TRP	0	-0.005	-0.011	25.727	-0.019	-0.019	0.000	0.000	0.000	0.000
31	A	28	GLY	0	-0.005	0.004	29.098	-0.017	-0.017	0.000	0.000	0.000	0.000
32	A	29	THR	0	-0.006	-0.030	26.561	-0.009	-0.009	0.000	0.000	0.000	0.000
33	A	30	GLU	-1	-0.815	-0.923	24.503	0.016	0.016	0.000	0.000	0.000	0.000
34	A	31	HIS	0	-0.008	0.002	27.938	-0.022	-0.022	0.000	0.000	0.000	0.000
35	A	32	MET	0	-0.018	-0.003	31.662	-0.015	-0.015	0.000	0.000	0.000	0.000
36	A	33	TYR	0	0.016	-0.021	27.959	-0.006	-0.006	0.000	0.000	0.000	0.000
37	A	34	ARG	1	0.901	0.938	26.493	0.041	0.041	0.000	0.000	0.000	0.000
38	A	35	LYS	1	0.898	0.966	30.540	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	36	TYR	0	-0.053	-0.040	33.310	-0.005	-0.005	0.000	0.000	0.000	0.000
40	A	37	LEU	0	-0.003	-0.005	30.161	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	38	ASN	0	-0.008	-0.006	29.069	-0.010	-0.010	0.000	0.000	0.000	0.000
42	A	39	ASP	-1	-0.874	-0.923	29.241	-0.104	-0.104	0.000	0.000	0.000	0.000
43	A	40	ARG	1	0.722	0.831	30.200	0.073	0.073	0.000	0.000	0.000	0.000
44	A	41	ILE	0	-0.052	-0.010	25.003	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	42	VAL	0	-0.053	-0.018	21.235	-0.008	-0.008	0.000	0.000	0.000	0.000
46	A	43	ASP	-1	-0.778	-0.884	20.733	-0.160	-0.160	0.000	0.000	0.000	0.000
47	A	44	CYS	0	-0.089	-0.042	21.699	0.007	0.007	0.000	0.000	0.000	0.000
48	A	45	LYS	1	0.879	0.945	18.683	0.064	0.064	0.000	0.000	0.000	0.000
49	A	46	VAL	0	0.019	0.021	20.679	0.025	0.025	0.000	0.000	0.000	0.000
50	A	47	GLY	0	0.011	0.001	18.933	0.006	0.006	0.000	0.000	0.000	0.000
51	A	48	TYR	0	-0.037	-0.022	18.533	-0.039	-0.039	0.000	0.000	0.000	0.000
52	A	49	ALA	0	0.021	0.006	17.319	0.066	0.066	0.000	0.000	0.000	0.000
53	A	50	ASN	0	0.016	-0.004	17.136	-0.006	-0.006	0.000	0.000	0.000	0.000
54	A	51	GLY	0	0.113	0.020	17.550	0.025	0.025	0.000	0.000	0.000	0.000
55	A	52	GLU	-1	-0.962	-0.972	16.541	0.600	0.600	0.000	0.000	0.000	0.000
56	A	53	GLU	-1	-0.876	-0.902	19.634	0.367	0.367	0.000	0.000	0.000	0.000
57	A	63	SER	0	0.065	0.040	29.414	-0.012	-0.012	0.000	0.000	0.000	0.000
58	A	64	TYR	0	0.018	-0.009	29.446	0.020	0.020	0.000	0.000	0.000	0.000
59	A	65	LYS	1	0.904	0.951	30.416	-0.205	-0.205	0.000	0.000	0.000	0.000
60	A	66	ARG	1	0.831	0.900	21.837	-0.532	-0.532	0.000	0.000	0.000	0.000
61	A	67	VAL	0	0.001	0.025	23.963	-0.036	-0.036	0.000	0.000	0.000	0.000
62	A	68	CYS	0	-0.064	0.004	24.105	0.039	0.039	0.000	0.000	0.000	0.000
63	A	69	GLY	0	0.064	0.041	24.329	0.015	0.015	0.000	0.000	0.000	0.000
64	A	70	GLY	0	0.038	0.018	21.480	0.040	0.040	0.000	0.000	0.000	0.000
65	A	71	ASP	-1	-0.796	-0.886	19.763	0.649	0.649	0.000	0.000	0.000	0.000
66	A	72	THR	0	-0.062	-0.046	22.608	-0.011	-0.011	0.000	0.000	0.000	0.000
67	A	73	ASP	-1	-0.788	-0.875	21.075	0.533	0.533	0.000	0.000	0.000	0.000
68	A	74	PHE	0	0.014	0.025	16.598	-0.022	-0.022	0.000	0.000	0.000	0.000
69	A	75	ALA	0	-0.026	-0.013	21.733	-0.045	-0.045	0.000	0.000	0.000	0.000
70	A	76	GLU	-1	-0.790	-0.851	22.108	0.225	0.225	0.000	0.000	0.000	0.000
71	A	77	VAL	0	-0.051	-0.026	19.447	-0.019	-0.019	0.000	0.000	0.000	0.000
72	A	78	LEU	0	-0.033	-0.010	22.402	-0.005	-0.005	0.000	0.000	0.000	0.000
73	A	79	GLN	0	0.011	0.009	14.703	-0.041	-0.041	0.000	0.000	0.000	0.000
74	A	80	VAL	0	-0.004	-0.015	19.973	-0.028	-0.028	0.000	0.000	0.000	0.000
75	A	81	SER	0	0.014	-0.001	18.865	-0.007	-0.007	0.000	0.000	0.000	0.000
76	A	82	TYR	0	0.052	0.002	20.305	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	83	ASN	0	0.070	0.024	21.999	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	84	PRO	0	-0.004	-0.007	22.561	0.024	0.024	0.000	0.000	0.000	0.000
79	A	85	LYS	1	0.909	0.963	25.594	0.237	0.237	0.000	0.000	0.000	0.000
80	A	86	VAL	0	-0.023	0.005	27.877	0.005	0.005	0.000	0.000	0.000	0.000
81	A	87	ILE	0	-0.008	0.002	27.045	0.018	0.018	0.000	0.000	0.000	0.000
82	A	88	THR	0	-0.001	-0.019	27.155	-0.006	-0.006	0.000	0.000	0.000	0.000
83	A	89	LEU	0	0.031	0.013	23.350	0.007	0.007	0.000	0.000	0.000	0.000
84	A	90	ARG	1	0.912	0.928	26.558	0.025	0.025	0.000	0.000	0.000	0.000
85	A	91	GLU	-1	-0.764	-0.832	30.133	-0.056	-0.056	0.000	0.000	0.000	0.000
86	A	92	LEU	0	0.020	0.015	24.820	0.010	0.010	0.000	0.000	0.000	0.000
87	A	93	THR	0	0.017	-0.006	27.818	0.020	0.020	0.000	0.000	0.000	0.000
88	A	94	ASP	-1	-0.796	-0.879	29.566	0.016	0.016	0.000	0.000	0.000	0.000
89	A	95	PHE	0	-0.051	-0.019	30.827	0.003	0.003	0.000	0.000	0.000	0.000
90	A	96	PHE	0	0.056	0.030	27.402	0.003	0.003	0.000	0.000	0.000	0.000
91	A	97	PHE	0	-0.034	-0.024	31.049	0.010	0.010	0.000	0.000	0.000	0.000
92	A	98	ARG	1	0.802	0.862	34.098	-0.013	-0.013	0.000	0.000	0.000	0.000
93	A	99	ILE	0	-0.045	-0.010	30.263	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	100	HIS	0	0.010	0.029	31.446	0.019	0.019	0.000	0.000	0.000	0.000
95	A	101	ASP	-1	-0.736	-0.809	35.424	0.088	0.088	0.000	0.000	0.000	0.000
96	A	102	PRO	0	-0.007	0.014	33.495	0.011	0.011	0.000	0.000	0.000	0.000
97	A	103	THR	0	-0.062	-0.061	34.292	0.008	0.008	0.000	0.000	0.000	0.000
98	A	104	THR	0	0.011	-0.008	36.829	0.003	0.003	0.000	0.000	0.000	0.000
99	A	105	SER	0	-0.063	-0.043	38.404	0.002	0.002	0.000	0.000	0.000	0.000
100	A	106	ASN	0	-0.038	-0.003	34.870	0.004	0.004	0.000	0.000	0.000	0.000
101	A	107	SER	0	-0.012	-0.043	35.276	0.006	0.006	0.000	0.000	0.000	0.000
102	A	108	GLN	0	-0.070	-0.021	37.107	0.017	0.017	0.000	0.000	0.000	0.000
103	A	109	GLY	0	0.103	0.028	38.252	-0.008	-0.008	0.000	0.000	0.000	0.000
104	A	110	PRO	0	-0.119	-0.036	37.323	0.011	0.011	0.000	0.000	0.000	0.000
105	A	111	ASP	-1	-0.848	-0.904	38.679	0.128	0.128	0.000	0.000	0.000	0.000
106	A	112	LYS	1	0.800	0.884	32.936	-0.155	-0.155	0.000	0.000	0.000	0.000
107	A	113	GLY	0	0.011	0.012	31.559	0.005	0.005	0.000	0.000	0.000	0.000
108	A	114	THR	0	0.018	-0.011	28.014	-0.015	-0.015	0.000	0.000	0.000	0.000
109	A	115	GLN	0	0.034	0.027	25.734	0.008	0.008	0.000	0.000	0.000	0.000
110	A	116	TYR	0	-0.070	-0.050	26.870	-0.005	-0.005	0.000	0.000	0.000	0.000
111	A	117	ARG	1	0.774	0.884	23.530	-0.352	-0.352	0.000	0.000	0.000	0.000
112	A	118	SER	0	0.028	0.012	28.243	0.003	0.003	0.000	0.000	0.000	0.000
113	A	119	GLY	0	-0.012	-0.027	25.569	0.013	0.013	0.000	0.000	0.000	0.000
114	A	120	LEU	0	-0.036	-0.009	24.067	-0.014	-0.014	0.000	0.000	0.000	0.000
115	A	121	PHE	0	0.017	0.002	18.790	0.008	0.008	0.000	0.000	0.000	0.000
116	A	122	ALA	0	0.024	0.006	19.293	-0.026	-0.026	0.000	0.000	0.000	0.000
117	A	123	HIS	0	0.047	0.033	14.075	0.071	0.071	0.000	0.000	0.000	0.000
118	A	124	SER	0	0.000	-0.022	15.418	-0.041	-0.041	0.000	0.000	0.000	0.000
119	A	125	ASP	-1	-0.818	-0.915	17.689	0.128	0.128	0.000	0.000	0.000	0.000
120	A	126	ALA	0	-0.041	-0.022	20.401	0.001	0.001	0.000	0.000	0.000	0.000
121	A	127	ASP	-1	-0.814	-0.875	19.451	-0.041	-0.041	0.000	0.000	0.000	0.000
122	A	128	LEU	0	0.010	0.013	21.379	0.002	0.002	0.000	0.000	0.000	0.000
123	A	129	LYS	1	0.974	0.990	23.239	-0.025	-0.025	0.000	0.000	0.000	0.000
124	A	130	GLU	-1	-0.846	-0.926	25.731	-0.016	-0.016	0.000	0.000	0.000	0.000
125	A	131	LEU	0	0.028	0.008	23.130	0.000	0.000	0.000	0.000	0.000	0.000
126	A	132	ALA	0	0.000	0.003	27.151	0.003	0.003	0.000	0.000	0.000	0.000
127	A	133	LYS	1	0.741	0.866	28.953	-0.015	-0.015	0.000	0.000	0.000	0.000
128	A	134	ILE	0	-0.031	-0.013	28.605	-0.002	-0.002	0.000	0.000	0.000	0.000
129	A	135	LYS	1	0.873	0.930	30.941	-0.134	-0.134	0.000	0.000	0.000	0.000
130	A	136	GLU	-1	-0.837	-0.917	32.660	0.082	0.082	0.000	0.000	0.000	0.000
131	A	137	GLU	-1	-0.805	-0.875	34.053	0.006	0.006	0.000	0.000	0.000	0.000
132	A	138	TRP	0	-0.015	-0.023	35.044	-0.002	-0.002	0.000	0.000	0.000	0.000
133	A	139	GLN	0	-0.028	-0.015	36.178	0.004	0.004	0.000	0.000	0.000	0.000
134	A	140	PRO	0	0.017	0.013	38.362	0.001	0.001	0.000	0.000	0.000	0.000
135	A	141	LYS	1	0.816	0.917	39.415	-0.031	-0.031	0.000	0.000	0.000	0.000
136	A	142	TRP	0	0.013	0.009	36.950	0.001	0.001	0.000	0.000	0.000	0.000
137	A	143	GLY	0	0.017	0.013	40.556	0.006	0.006	0.000	0.000	0.000	0.000
138	A	144	ASN	0	-0.064	-0.044	39.873	0.001	0.001	0.000	0.000	0.000	0.000
139	A	145	LYS	1	0.925	0.964	39.004	-0.076	-0.076	0.000	0.000	0.000	0.000
140	A	146	ILE	0	0.005	0.015	32.941	0.007	0.007	0.000	0.000	0.000	0.000
141	A	147	ALA	0	0.003	-0.008	33.615	0.006	0.006	0.000	0.000	0.000	0.000
142	A	148	THR	0	-0.046	-0.032	28.187	0.010	0.010	0.000	0.000	0.000	0.000
143	A	149	VAL	0	0.010	0.022	25.202	-0.007	-0.007	0.000	0.000	0.000	0.000
144	A	150	ILE	0	-0.019	-0.019	24.812	-0.008	-0.008	0.000	0.000	0.000	0.000
145	A	151	GLH	0	-0.049	-0.050	20.942	0.012	0.012	0.000	0.000	0.000	0.000
146	A	152	PRO	0	0.048	0.027	17.171	-0.036	-0.036	0.000	0.000	0.000	0.000
147	A	153	ILE	0	-0.037	-0.012	13.852	0.042	0.042	0.000	0.000	0.000	0.000
148	A	154	LYS	1	0.793	0.915	14.255	-0.595	-0.595	0.000	0.000	0.000	0.000
149	A	155	ASN	0	-0.029	-0.026	11.783	0.146	0.146	0.000	0.000	0.000	0.000
150	A	156	PHE	0	0.001	0.002	12.411	-0.200	-0.200	0.000	0.000	0.000	0.000
151	A	157	TYR	0	-0.005	0.005	12.232	0.219	0.219	0.000	0.000	0.000	0.000
152	A	158	ASP	-1	-0.690	-0.821	14.677	0.173	0.173	0.000	0.000	0.000	0.000
153	A	159	ALA	0	0.006	0.009	17.196	0.053	0.053	0.000	0.000	0.000	0.000
154	A	160	GLU	-1	-0.891	-0.959	19.820	0.182	0.182	0.000	0.000	0.000	0.000
155	A	161	GLU	-1	-0.809	-0.876	12.801	0.846	0.846	0.000	0.000	0.000	0.000
156	A	162	TYR	0	-0.007	-0.026	17.543	0.072	0.072	0.000	0.000	0.000	0.000
157	A	163	HIS	1	0.870	0.921	18.687	-0.275	-0.275	0.000	0.000	0.000	0.000
158	A	164	GLN	0	-0.024	-0.017	18.511	-0.004	-0.004	0.000	0.000	0.000	0.000
159	A	165	LEU	0	-0.031	0.004	14.825	0.011	0.011	0.000	0.000	0.000	0.000
160	A	166	TYR	0	-0.030	-0.022	17.929	0.049	0.049	0.000	0.000	0.000	0.000
161	A	167	LEU	0	-0.051	-0.039	21.500	-0.043	-0.043	0.000	0.000	0.000	0.000
162	A	168	ASP	-1	-0.765	-0.846	21.967	0.387	0.387	0.000	0.000	0.000	0.000
163	A	169	LYS	1	0.773	0.871	23.878	-0.425	-0.425	0.000	0.000	0.000	0.000
164	A	170	ASN	0	-0.060	-0.036	27.039	-0.041	-0.041	0.000	0.000	0.000	0.000
165	A	171	PRO	0	0.109	0.064	27.688	0.000	0.000	0.000	0.000	0.000	0.000
166	A	172	GLN	0	0.045	-0.005	28.701	-0.010	-0.010	0.000	0.000	0.000	0.000
167	A	173	GLY	0	0.030	0.031	29.031	-0.012	-0.012	0.000	0.000	0.000	0.000
168	A	174	TYR	0	0.003	-0.011	29.924	-0.011	-0.011	0.000	0.000	0.000	0.000
169	A	175	ALA	0	-0.013	-0.016	30.894	0.019	0.019	0.000	0.000	0.000	0.000
170	A	177	PRO	0	-0.007	-0.008	29.618	-0.013	-0.013	0.000	0.000	0.000	0.000
171	A	178	THR	0	-0.003	-0.012	25.851	-0.005	-0.005	0.000	0.000	0.000	0.000
172	A	179	HIS	0	0.022	0.011	29.078	0.001	0.001	0.000	0.000	0.000	0.000
173	A	180	TYR	0	-0.018	-0.024	26.972	0.009	0.009	0.000	0.000	0.000	0.000
174	A	181	LEU	0	0.028	0.026	28.936	0.003	0.003	0.000	0.000	0.000	0.000
175	A	182	ARG	1	0.785	0.893	29.375	-0.164	-0.164	0.000	0.000	0.000	0.000
176	A	183	GLU	-1	-0.888	-0.948	28.871	0.083	0.083	0.000	0.000	0.000	0.000
177	A	184	MET	0	-0.066	-0.005	31.700	0.008	0.008	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-2:HIS)