FMO DATABASE

FMODB ID: NNY3Q

Calculation Name: 4N30-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4N30

Chain ID: A

ChEMBL ID:

UniProt ID: Q7WY37

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	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	181
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1901282.635733
FMO2-HF: Nuclear repulsion	1831007.595333
FMO2-HF: Total energy	-70275.040399
FMO2-MP2: Total energy	-70480.263881

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:40:LYS)

Summations of interaction energy for fragment #1(A:40: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.
-111.175	-101.999	0.705	-5.296	-4.583	-0.042

Interaction energy analysis for fragmet #1(A:40:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.936 / q_NPA : 0.968

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	42	LEU	0	0.008	-0.009	3.406	-6.020	-3.420	0.017	-1.424	-1.194	0.004
4	A	43	PRO	0	-0.014	-0.001	5.837	-0.871	-0.871	0.000	0.000	0.000	0.000
5	A	44	ALA	0	0.018	0.018	6.553	3.254	3.254	0.000	0.000	0.000	0.000
6	A	45	ASN	0	-0.008	-0.015	9.495	0.478	0.478	0.000	0.000	0.000	0.000
7	A	46	HIS	0	-0.016	-0.028	12.848	-0.123	-0.123	0.000	0.000	0.000	0.000
8	A	47	SER	0	0.069	0.043	12.401	0.255	0.255	0.000	0.000	0.000	0.000
9	A	48	LEU	0	-0.032	-0.023	10.160	-0.662	-0.662	0.000	0.000	0.000	0.000
10	A	49	TYR	0	-0.084	-0.065	13.314	1.454	1.454	0.000	0.000	0.000	0.000
11	A	50	GLY	0	0.060	0.017	14.039	-0.907	-0.907	0.000	0.000	0.000	0.000
12	A	51	ASP	-1	-0.833	-0.907	12.780	-23.589	-23.589	0.000	0.000	0.000	0.000
13	A	52	ALA	0	0.024	-0.001	10.130	-2.078	-2.078	0.000	0.000	0.000	0.000
14	A	53	LYS	1	0.841	0.913	8.223	23.117	23.117	0.000	0.000	0.000	0.000
15	A	54	ALA	0	-0.001	0.018	9.103	-0.636	-0.636	0.000	0.000	0.000	0.000
16	A	55	ARG	1	0.896	0.956	7.288	23.479	23.479	0.000	0.000	0.000	0.000
17	A	56	TRP	0	-0.045	-0.027	6.936	-5.498	-5.498	0.000	0.000	0.000	0.000
18	A	57	THR	0	0.010	-0.007	6.913	-0.915	-0.915	0.000	0.000	0.000	0.000
19	A	58	ILE	0	-0.003	-0.007	8.646	-0.319	-0.319	0.000	0.000	0.000	0.000
20	A	59	ASN	0	-0.063	-0.026	8.229	-0.057	-0.057	0.000	0.000	0.000	0.000
21	A	60	GLU	-1	-0.775	-0.887	12.173	-15.253	-15.253	0.000	0.000	0.000	0.000
22	A	61	TYR	0	-0.038	-0.015	11.748	-0.548	-0.548	0.000	0.000	0.000	0.000
23	A	62	ALA	0	0.046	-0.005	17.383	0.905	0.905	0.000	0.000	0.000	0.000
24	A	63	ASP	-1	-0.753	-0.868	20.625	-11.917	-11.917	0.000	0.000	0.000	0.000
25	A	64	LEU	0	0.038	0.003	23.249	0.187	0.187	0.000	0.000	0.000	0.000
26	A	65	GLU	-1	-0.775	-0.823	25.796	-9.636	-9.636	0.000	0.000	0.000	0.000
27	A	66	CYS	0	-0.040	0.006	25.958	0.526	0.526	0.000	0.000	0.000	0.000
28	A	67	PRO	0	0.047	0.027	28.030	-0.227	-0.227	0.000	0.000	0.000	0.000
29	A	68	PHE	0	0.011	-0.023	26.635	0.053	0.053	0.000	0.000	0.000	0.000
30	A	69	CYS	0	0.005	-0.003	23.690	-0.420	-0.420	0.000	0.000	0.000	0.000
31	A	70	LYS	1	0.943	0.993	24.835	9.596	9.596	0.000	0.000	0.000	0.000
32	A	71	VAL	0	-0.055	-0.027	27.358	0.011	0.011	0.000	0.000	0.000	0.000
33	A	72	TYR	0	-0.038	-0.053	19.799	-0.202	-0.202	0.000	0.000	0.000	0.000
34	A	73	THR	0	0.028	-0.004	20.446	-0.135	-0.135	0.000	0.000	0.000	0.000
35	A	74	PRO	0	0.009	0.005	21.866	-0.442	-0.442	0.000	0.000	0.000	0.000
36	A	75	ARG	1	0.901	0.955	23.798	10.870	10.870	0.000	0.000	0.000	0.000
37	A	76	LEU	0	0.007	0.007	16.830	-0.183	-0.183	0.000	0.000	0.000	0.000
38	A	77	LYS	1	0.863	0.940	19.094	13.125	13.125	0.000	0.000	0.000	0.000
39	A	78	ARG	1	0.999	1.009	20.161	11.917	11.917	0.000	0.000	0.000	0.000
40	A	79	TRP	0	-0.010	-0.012	15.950	-0.277	-0.277	0.000	0.000	0.000	0.000
41	A	80	VAL	0	-0.003	0.003	15.235	-0.233	-0.233	0.000	0.000	0.000	0.000
42	A	81	ASP	-1	-0.831	-0.885	17.677	-14.823	-14.823	0.000	0.000	0.000	0.000
43	A	82	SER	0	-0.111	-0.053	20.246	0.264	0.264	0.000	0.000	0.000	0.000
44	A	83	HIS	1	0.798	0.897	17.044	15.878	15.878	0.000	0.000	0.000	0.000
45	A	84	PRO	0	0.080	0.020	15.817	-1.048	-1.048	0.000	0.000	0.000	0.000
46	A	85	ASP	-1	-0.914	-0.935	13.033	-21.333	-21.333	0.000	0.000	0.000	0.000
47	A	86	VAL	0	-0.072	-0.038	11.339	-2.586	-2.586	0.000	0.000	0.000	0.000
48	A	87	ASN	0	-0.013	0.012	8.128	0.821	0.821	0.000	0.000	0.000	0.000
49	A	88	LEU	0	0.015	0.012	11.809	-0.444	-0.444	0.000	0.000	0.000	0.000
50	A	89	VAL	0	-0.036	-0.020	9.233	-0.166	-0.166	0.000	0.000	0.000	0.000
51	A	90	TRP	0	0.024	0.011	12.456	0.414	0.414	0.000	0.000	0.000	0.000
52	A	91	ARG	1	0.771	0.854	8.511	24.859	24.859	0.000	0.000	0.000	0.000
53	A	92	HIS	0	-0.016	-0.025	14.848	1.613	1.613	0.000	0.000	0.000	0.000
54	A	93	LEU	0	-0.025	-0.034	17.096	-0.335	-0.335	0.000	0.000	0.000	0.000
55	A	94	PRO	0	-0.002	0.015	19.616	0.448	0.448	0.000	0.000	0.000	0.000
56	A	95	LEU	0	0.000	-0.002	23.040	0.040	0.040	0.000	0.000	0.000	0.000
57	A	96	GLN	0	0.052	0.012	25.273	0.077	0.077	0.000	0.000	0.000	0.000
58	A	97	MET	0	-0.088	-0.045	27.578	0.330	0.330	0.000	0.000	0.000	0.000
59	A	98	HIS	0	-0.021	-0.031	27.441	0.574	0.574	0.000	0.000	0.000	0.000
60	A	99	GLY	0	0.007	0.006	29.604	0.101	0.101	0.000	0.000	0.000	0.000
61	A	100	GLU	-1	-0.781	-0.890	28.478	-10.623	-10.623	0.000	0.000	0.000	0.000
62	A	101	ALA	0	0.030	0.037	28.881	-0.260	-0.260	0.000	0.000	0.000	0.000
63	A	102	ALA	0	0.040	0.018	25.633	-0.252	-0.252	0.000	0.000	0.000	0.000
64	A	103	ARG	1	0.818	0.893	24.117	10.017	10.017	0.000	0.000	0.000	0.000
65	A	104	HIS	0	-0.003	-0.002	24.511	-0.556	-0.556	0.000	0.000	0.000	0.000
66	A	105	GLN	0	0.030	-0.020	26.260	0.111	0.111	0.000	0.000	0.000	0.000
67	A	106	ALA	0	0.000	-0.003	20.742	-0.301	-0.301	0.000	0.000	0.000	0.000
68	A	107	ARG	1	0.835	0.918	21.538	10.956	10.956	0.000	0.000	0.000	0.000
69	A	108	LEU	0	0.007	0.005	23.125	-0.215	-0.215	0.000	0.000	0.000	0.000
70	A	109	VAL	0	0.010	0.014	20.356	-0.061	-0.061	0.000	0.000	0.000	0.000
71	A	110	GLU	-1	-0.771	-0.863	16.733	-17.703	-17.703	0.000	0.000	0.000	0.000
72	A	111	CYS	0	-0.085	-0.031	19.971	-0.419	-0.419	0.000	0.000	0.000	0.000
73	A	112	ALA	0	0.020	0.007	22.911	0.208	0.208	0.000	0.000	0.000	0.000
74	A	113	GLY	0	-0.026	-0.018	19.172	0.075	0.075	0.000	0.000	0.000	0.000
75	A	114	ILE	0	-0.031	-0.009	19.651	-0.142	-0.142	0.000	0.000	0.000	0.000
76	A	115	GLN	0	-0.081	-0.039	21.019	0.304	0.304	0.000	0.000	0.000	0.000
77	A	116	GLY	0	0.022	-0.002	22.781	0.342	0.342	0.000	0.000	0.000	0.000
78	A	117	GLY	0	-0.034	0.003	18.943	-0.106	-0.106	0.000	0.000	0.000	0.000
79	A	118	ALA	0	0.065	0.027	16.916	0.363	0.363	0.000	0.000	0.000	0.000
80	A	119	LYS	1	0.951	0.972	18.822	12.376	12.376	0.000	0.000	0.000	0.000
81	A	120	ALA	0	0.011	0.026	22.215	0.430	0.430	0.000	0.000	0.000	0.000
82	A	121	PHE	0	0.033	0.023	17.421	0.316	0.316	0.000	0.000	0.000	0.000
83	A	122	TRP	0	0.003	-0.021	15.820	0.867	0.867	0.000	0.000	0.000	0.000
84	A	123	SER	0	-0.032	-0.025	21.829	0.480	0.480	0.000	0.000	0.000	0.000
85	A	124	ALA	0	0.025	0.019	24.038	0.494	0.494	0.000	0.000	0.000	0.000
86	A	125	ILE	0	0.002	0.005	19.912	0.378	0.378	0.000	0.000	0.000	0.000
87	A	126	ASP	-1	-0.887	-0.943	24.409	-12.266	-12.266	0.000	0.000	0.000	0.000
88	A	127	ALA	0	0.004	0.013	27.086	0.438	0.438	0.000	0.000	0.000	0.000
89	A	128	ILE	0	0.020	0.001	25.892	0.406	0.406	0.000	0.000	0.000	0.000
90	A	129	PHE	0	-0.016	-0.007	23.893	0.332	0.332	0.000	0.000	0.000	0.000
91	A	130	ALA	0	-0.090	-0.034	29.374	0.348	0.348	0.000	0.000	0.000	0.000
92	A	131	GLN	0	-0.023	-0.026	32.274	0.356	0.356	0.000	0.000	0.000	0.000
93	A	132	SER	0	-0.043	-0.044	31.533	0.395	0.395	0.000	0.000	0.000	0.000
94	A	133	ALA	0	-0.033	-0.012	33.561	0.047	0.047	0.000	0.000	0.000	0.000
95	A	134	GLY	0	-0.038	-0.013	32.096	0.022	0.022	0.000	0.000	0.000	0.000
96	A	135	ASN	0	-0.061	-0.043	31.838	0.142	0.142	0.000	0.000	0.000	0.000
97	A	136	GLY	0	0.012	-0.004	32.088	0.170	0.170	0.000	0.000	0.000	0.000
98	A	137	GLY	0	-0.097	-0.035	33.004	0.150	0.150	0.000	0.000	0.000	0.000
99	A	138	GLY	0	0.001	-0.012	32.316	0.132	0.132	0.000	0.000	0.000	0.000
100	A	139	LEU	0	-0.006	0.020	30.396	0.159	0.159	0.000	0.000	0.000	0.000
101	A	140	PRO	0	0.052	0.020	34.346	0.146	0.146	0.000	0.000	0.000	0.000
102	A	141	GLY	0	0.009	0.009	37.349	-0.039	-0.039	0.000	0.000	0.000	0.000
103	A	142	GLY	0	-0.018	-0.008	33.720	-0.043	-0.043	0.000	0.000	0.000	0.000
104	A	143	THR	0	-0.056	-0.025	32.920	-0.257	-0.257	0.000	0.000	0.000	0.000
105	A	144	LEU	0	-0.010	-0.008	28.572	-0.030	-0.030	0.000	0.000	0.000	0.000
106	A	145	ASP	-1	-0.921	-0.956	32.747	-8.482	-8.482	0.000	0.000	0.000	0.000
107	A	146	PHE	0	-0.021	-0.031	26.570	-0.365	-0.365	0.000	0.000	0.000	0.000
108	A	147	PRO	0	0.022	0.016	32.200	-0.156	-0.156	0.000	0.000	0.000	0.000
109	A	148	GLU	-1	-0.927	-0.962	30.872	-9.471	-9.471	0.000	0.000	0.000	0.000
110	A	149	LEU	0	-0.097	-0.039	26.420	-0.328	-0.328	0.000	0.000	0.000	0.000
111	A	150	ASP	-1	-0.856	-0.928	30.055	-9.017	-9.017	0.000	0.000	0.000	0.000
112	A	151	GLN	0	0.032	0.000	30.873	-0.292	-0.292	0.000	0.000	0.000	0.000
113	A	152	ALA	0	0.069	0.038	32.291	-0.088	-0.088	0.000	0.000	0.000	0.000
114	A	153	ARG	1	0.854	0.937	25.981	10.832	10.832	0.000	0.000	0.000	0.000
115	A	154	LEU	0	-0.033	-0.021	26.049	-0.295	-0.295	0.000	0.000	0.000	0.000
116	A	155	GLU	-1	-0.858	-0.932	28.158	-9.300	-9.300	0.000	0.000	0.000	0.000
117	A	156	LYS	1	0.914	0.963	30.156	9.047	9.047	0.000	0.000	0.000	0.000
118	A	158	ALA	0	0.040	0.020	25.483	-0.275	-0.275	0.000	0.000	0.000	0.000
119	A	159	LYS	1	0.755	0.853	26.496	9.144	9.144	0.000	0.000	0.000	0.000
120	A	160	ASP	-1	-0.819	-0.894	27.581	-9.473	-9.473	0.000	0.000	0.000	0.000
121	A	161	ASN	0	-0.024	-0.008	21.249	-0.293	-0.293	0.000	0.000	0.000	0.000
122	A	162	GLU	-1	-0.856	-0.942	21.959	-11.598	-11.598	0.000	0.000	0.000	0.000
123	A	163	LEU	0	-0.039	-0.007	17.555	-0.437	-0.437	0.000	0.000	0.000	0.000
124	A	164	ILE	0	0.072	0.029	17.176	-0.591	-0.591	0.000	0.000	0.000	0.000
125	A	165	ASP	-1	-0.801	-0.876	18.205	-12.702	-12.702	0.000	0.000	0.000	0.000
126	A	166	SER	0	-0.036	-0.045	16.350	-0.069	-0.069	0.000	0.000	0.000	0.000
127	A	167	ASP	-1	-0.904	-0.939	13.401	-18.928	-18.928	0.000	0.000	0.000	0.000
128	A	168	ILE	0	-0.036	-0.024	14.338	-0.723	-0.723	0.000	0.000	0.000	0.000
129	A	169	LYS	1	0.861	0.921	16.662	12.333	12.333	0.000	0.000	0.000	0.000
130	A	170	LEU	0	0.039	0.028	9.499	-0.140	-0.140	0.000	0.000	0.000	0.000
131	A	171	ASP	-1	-0.779	-0.864	11.831	-22.335	-22.335	0.000	0.000	0.000	0.000
132	A	172	ILE	0	0.010	0.006	13.609	-0.034	-0.034	0.000	0.000	0.000	0.000
133	A	173	ASP	-1	-0.866	-0.912	14.795	-14.476	-14.476	0.000	0.000	0.000	0.000
134	A	174	ILE	0	-0.041	-0.028	8.890	-0.286	-0.286	0.000	0.000	0.000	0.000
135	A	175	ALA	0	0.001	0.011	12.898	-0.106	-0.106	0.000	0.000	0.000	0.000
136	A	176	ARG	1	0.904	0.933	15.565	13.821	13.821	0.000	0.000	0.000	0.000
137	A	177	SER	0	-0.078	-0.034	13.551	0.120	0.120	0.000	0.000	0.000	0.000
138	A	178	LYS	1	0.908	0.957	9.764	23.598	23.598	0.000	0.000	0.000	0.000
139	A	179	GLY	0	0.015	0.004	15.851	0.185	0.185	0.000	0.000	0.000	0.000
140	A	180	ILE	0	-0.092	-0.041	15.258	0.375	0.375	0.000	0.000	0.000	0.000
141	A	181	THR	0	-0.006	-0.011	19.542	0.319	0.319	0.000	0.000	0.000	0.000
142	A	182	ALA	0	0.022	0.027	22.472	0.476	0.476	0.000	0.000	0.000	0.000
143	A	183	THR	0	0.001	0.041	21.085	-0.520	-0.520	0.000	0.000	0.000	0.000
144	A	184	PRO	0	0.021	-0.009	20.523	0.673	0.673	0.000	0.000	0.000	0.000
145	A	185	THR	0	-0.007	-0.024	17.234	0.451	0.451	0.000	0.000	0.000	0.000
146	A	186	LEU	0	-0.025	-0.008	15.365	-0.799	-0.799	0.000	0.000	0.000	0.000
147	A	187	VAL	0	-0.030	-0.022	10.121	0.307	0.307	0.000	0.000	0.000	0.000
148	A	188	ILE	0	0.027	0.024	10.982	-1.717	-1.717	0.000	0.000	0.000	0.000
149	A	189	ARG	1	0.877	0.925	3.662	41.977	42.222	0.002	-0.033	-0.214	0.000
150	A	190	ASP	-1	-0.711	-0.844	6.830	-36.383	-36.383	0.000	0.000	0.000	0.000
151	A	191	ASN	0	-0.083	-0.056	2.933	-22.001	-19.698	0.124	-1.277	-1.148	-0.012
152	A	192	GLN	0	0.006	0.012	2.524	-23.931	-20.096	0.565	-2.547	-1.853	-0.034
153	A	193	THR	0	-0.043	-0.039	5.219	0.817	0.859	-0.001	0.000	-0.041	0.000
154	A	194	GLY	0	-0.020	-0.002	4.183	0.960	1.062	-0.001	-0.015	-0.086	0.000
155	A	195	ARG	1	0.864	0.964	5.132	24.958	25.007	-0.001	0.000	-0.047	0.000
156	A	196	SER	0	-0.002	-0.018	8.090	-3.137	-3.137	0.000	0.000	0.000	0.000
157	A	197	VAL	0	0.013	0.013	9.798	1.581	1.581	0.000	0.000	0.000	0.000
158	A	198	LYS	1	0.881	0.951	13.387	15.510	15.510	0.000	0.000	0.000	0.000
159	A	199	LEU	0	-0.016	-0.012	15.563	0.868	0.868	0.000	0.000	0.000	0.000
160	A	200	GLU	-1	-0.939	-0.965	18.688	-13.599	-13.599	0.000	0.000	0.000	0.000
161	A	201	GLY	0	0.043	0.021	21.399	0.534	0.534	0.000	0.000	0.000	0.000
162	A	202	MET	0	-0.056	-0.023	21.851	-0.551	-0.551	0.000	0.000	0.000	0.000
163	A	203	ALA	0	-0.020	0.007	20.100	0.442	0.442	0.000	0.000	0.000	0.000
164	A	204	ASP	-1	-0.732	-0.823	22.037	-12.730	-12.730	0.000	0.000	0.000	0.000
165	A	205	GLU	-1	-0.902	-0.965	21.934	-13.059	-13.059	0.000	0.000	0.000	0.000
166	A	206	THR	0	0.001	-0.015	21.855	-0.506	-0.506	0.000	0.000	0.000	0.000
167	A	207	THR	0	-0.018	-0.015	20.427	-0.350	-0.350	0.000	0.000	0.000	0.000
168	A	208	LEU	0	-0.036	-0.009	16.827	-0.865	-0.865	0.000	0.000	0.000	0.000
169	A	209	LEU	0	-0.009	-0.007	17.451	-1.052	-1.052	0.000	0.000	0.000	0.000
170	A	210	SER	0	-0.026	-0.034	18.662	-0.477	-0.477	0.000	0.000	0.000	0.000
171	A	211	ALA	0	-0.004	0.007	16.173	-0.340	-0.340	0.000	0.000	0.000	0.000
172	A	212	ILE	0	0.037	0.007	13.101	-1.061	-1.061	0.000	0.000	0.000	0.000
173	A	213	ASP	-1	-0.803	-0.889	14.592	-15.994	-15.994	0.000	0.000	0.000	0.000
174	A	214	TRP	0	-0.011	-0.011	13.742	-0.510	-0.510	0.000	0.000	0.000	0.000
175	A	215	LEU	0	-0.111	-0.061	10.322	-0.418	-0.418	0.000	0.000	0.000	0.000
176	A	216	ALA	0	-0.002	-0.010	11.506	-0.908	-0.908	0.000	0.000	0.000	0.000
177	A	217	LYS	1	0.870	0.942	13.574	15.789	15.789	0.000	0.000	0.000	0.000
178	A	218	ASP	-1	-0.938	-0.968	16.775	-15.386	-15.386	0.000	0.000	0.000	0.000
179	A	219	LEU	0	-0.122	-0.069	11.231	-0.286	-0.286	0.000	0.000	0.000	0.000
180	A	220	LEU	0	0.008	-0.004	13.426	-1.632	-1.632	0.000	0.000	0.000	0.000
181	A	221	GLU	-1	-0.975	-0.961	15.629	-18.270	-18.270	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:40:LYS)