FMO DATABASE

FMODB ID: JQ1Z9

Calculation Name: 3KBG-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3KBG

Chain ID: A

ChEMBL ID:

UniProt ID: Q56230

Base Structure: X-ray

Registration Date: 2023-09-24

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	194
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2064170.550035
FMO2-HF: Nuclear repulsion	1989239.369844
FMO2-HF: Total energy	-74931.180191
FMO2-MP2: Total energy	-75150.306674

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:34:LYS)

Summations of interaction energy for fragment #1(A:34: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.
74.333	81.868	9.617	-5.865	-11.287	-0.063

Interaction energy analysis for fragmet #1(A:34:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.950 / q_NPA : 0.982

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	36	GLN	0	-0.035	-0.021	3.004	2.177	4.966	0.052	-1.252	-1.589	0.004
4	A	37	SER	0	-0.019	-0.002	6.094	3.717	3.717	0.000	0.000	0.000	0.000
5	A	38	VAL	0	0.014	0.011	6.164	-1.586	-1.586	0.000	0.000	0.000	0.000
6	A	39	THR	0	-0.021	-0.017	8.930	2.661	2.661	0.000	0.000	0.000	0.000
7	A	40	LEU	0	0.061	0.027	12.170	-0.959	-0.959	0.000	0.000	0.000	0.000
8	A	41	LEU	0	0.015	-0.003	14.592	0.033	0.033	0.000	0.000	0.000	0.000
9	A	42	SER	0	-0.031	-0.003	10.448	0.160	0.160	0.000	0.000	0.000	0.000
10	A	43	ILE	0	0.053	0.038	9.385	-0.642	-0.642	0.000	0.000	0.000	0.000
11	A	44	ILE	0	0.022	0.011	11.761	0.387	0.387	0.000	0.000	0.000	0.000
12	A	45	ARG	1	0.920	0.957	13.782	19.475	19.475	0.000	0.000	0.000	0.000
13	A	46	ASP	-1	-0.867	-0.931	8.728	-30.250	-30.250	0.000	0.000	0.000	0.000
14	A	47	TYR	0	0.028	0.019	11.597	0.165	0.165	0.000	0.000	0.000	0.000
15	A	48	LEU	0	0.021	0.000	13.958	0.759	0.759	0.000	0.000	0.000	0.000
16	A	49	LYS	1	0.847	0.910	11.097	25.791	25.791	0.000	0.000	0.000	0.000
17	A	50	LEU	0	-0.043	0.000	12.212	0.539	0.539	0.000	0.000	0.000	0.000
18	A	51	SER	0	-0.054	-0.017	15.938	0.931	0.931	0.000	0.000	0.000	0.000
19	A	52	ASP	-1	-0.796	-0.871	18.355	-13.965	-13.965	0.000	0.000	0.000	0.000
20	A	53	LYS	1	0.929	0.956	19.359	13.283	13.283	0.000	0.000	0.000	0.000
21	A	54	GLU	-1	-0.862	-0.910	15.934	-16.537	-16.537	0.000	0.000	0.000	0.000
22	A	55	ARG	1	0.746	0.812	18.244	15.020	15.020	0.000	0.000	0.000	0.000
23	A	56	GLU	-1	-0.811	-0.884	21.302	-11.924	-11.924	0.000	0.000	0.000	0.000
24	A	57	ALA	0	0.005	0.009	18.072	0.240	0.240	0.000	0.000	0.000	0.000
25	A	58	ALA	0	-0.002	-0.008	20.047	0.167	0.167	0.000	0.000	0.000	0.000
26	A	59	ARG	1	0.917	0.949	21.890	12.064	12.064	0.000	0.000	0.000	0.000
27	A	60	ILE	0	0.022	-0.004	22.139	0.443	0.443	0.000	0.000	0.000	0.000
28	A	61	LEU	0	0.016	0.004	18.596	0.275	0.275	0.000	0.000	0.000	0.000
29	A	62	ALA	0	-0.022	-0.002	22.836	0.418	0.418	0.000	0.000	0.000	0.000
30	A	63	ASN	0	0.006	0.005	26.014	0.640	0.640	0.000	0.000	0.000	0.000
31	A	64	GLY	0	-0.016	-0.002	26.462	0.298	0.298	0.000	0.000	0.000	0.000
32	A	65	LEU	0	-0.042	-0.007	25.566	0.163	0.163	0.000	0.000	0.000	0.000
33	A	66	VAL	0	0.008	0.010	19.490	-0.312	-0.312	0.000	0.000	0.000	0.000
34	A	67	LYS	1	0.849	0.920	21.898	11.805	11.805	0.000	0.000	0.000	0.000
35	A	68	VAL	0	0.039	0.015	17.182	-0.675	-0.675	0.000	0.000	0.000	0.000
36	A	69	ASP	-1	-0.768	-0.868	18.946	-14.425	-14.425	0.000	0.000	0.000	0.000
37	A	70	GLY	0	0.030	0.019	21.236	0.490	0.490	0.000	0.000	0.000	0.000
38	A	71	LYS	1	0.913	0.961	23.354	12.443	12.443	0.000	0.000	0.000	0.000
39	A	72	THR	0	0.020	0.003	23.292	-0.545	-0.545	0.000	0.000	0.000	0.000
40	A	73	VAL	0	-0.031	-0.010	19.732	0.249	0.249	0.000	0.000	0.000	0.000
41	A	74	ARG	1	0.919	0.942	22.374	11.041	11.041	0.000	0.000	0.000	0.000
42	A	75	GLU	-1	-0.816	-0.878	19.874	-14.078	-14.078	0.000	0.000	0.000	0.000
43	A	76	LYS	1	1.010	0.997	18.247	15.645	15.645	0.000	0.000	0.000	0.000
44	A	77	LYS	1	0.826	0.871	16.345	12.990	12.990	0.000	0.000	0.000	0.000
45	A	78	PHE	0	-0.003	0.012	16.003	-0.288	-0.288	0.000	0.000	0.000	0.000
46	A	79	ALA	0	0.013	0.011	12.203	-0.718	-0.718	0.000	0.000	0.000	0.000
47	A	80	VAL	0	-0.015	-0.007	11.260	1.150	1.150	0.000	0.000	0.000	0.000
48	A	81	GLY	0	0.060	0.001	9.455	-2.281	-2.281	0.000	0.000	0.000	0.000
49	A	82	PHE	0	0.021	0.016	9.101	1.057	1.057	0.000	0.000	0.000	0.000
50	A	83	MET	0	-0.018	0.000	10.826	1.267	1.267	0.000	0.000	0.000	0.000
51	A	84	ASP	-1	-0.809	-0.878	13.756	-17.274	-17.274	0.000	0.000	0.000	0.000
52	A	85	VAL	0	0.010	0.001	15.601	-0.635	-0.635	0.000	0.000	0.000	0.000
53	A	86	ILE	0	-0.003	-0.008	14.205	0.327	0.327	0.000	0.000	0.000	0.000
54	A	87	GLU	-1	-0.889	-0.934	18.240	-11.653	-11.653	0.000	0.000	0.000	0.000
55	A	88	ILE	0	0.012	-0.004	17.721	-0.084	-0.084	0.000	0.000	0.000	0.000
56	A	89	ASN	0	-0.038	-0.032	22.290	0.157	0.157	0.000	0.000	0.000	0.000
57	A	90	GLY	0	0.039	0.030	25.931	0.292	0.292	0.000	0.000	0.000	0.000
58	A	91	GLU	-1	-0.775	-0.874	23.476	-12.321	-12.321	0.000	0.000	0.000	0.000
59	A	92	SER	0	-0.011	0.003	21.714	-0.140	-0.140	0.000	0.000	0.000	0.000
60	A	93	TYR	0	-0.008	0.001	16.701	-0.077	-0.077	0.000	0.000	0.000	0.000
61	A	94	ARG	1	0.782	0.878	14.875	15.966	15.966	0.000	0.000	0.000	0.000
62	A	95	VAL	0	-0.017	0.003	9.863	-1.071	-1.071	0.000	0.000	0.000	0.000
63	A	96	VAL	0	0.006	-0.016	10.815	1.104	1.104	0.000	0.000	0.000	0.000
64	A	97	TYR	0	-0.017	-0.029	4.456	-0.138	0.008	-0.001	-0.015	-0.130	0.000
65	A	98	ASN	0	0.053	0.030	4.705	-1.803	-1.662	-0.001	-0.005	-0.135	0.000
66	A	99	ASP	-1	-0.800	-0.904	6.465	-29.532	-29.532	0.000	0.000	0.000	0.000
67	A	100	GLN	0	-0.073	-0.032	2.904	-2.239	-1.518	0.122	-0.261	-0.581	-0.001
68	A	101	GLY	0	0.023	0.006	2.280	-20.955	-18.891	4.472	-2.559	-3.978	-0.041
69	A	102	ALA	0	-0.058	-0.033	2.505	-6.996	-5.462	4.930	-1.979	-4.485	-0.024
70	A	103	LEU	0	-0.005	0.007	3.582	7.415	7.555	0.043	0.206	-0.389	-0.001
71	A	104	VAL	0	-0.005	-0.009	6.177	-0.881	-0.881	0.000	0.000	0.000	0.000
72	A	105	LEU	0	-0.020	-0.002	9.482	1.684	1.684	0.000	0.000	0.000	0.000
73	A	106	MET	0	0.000	0.014	13.142	-0.595	-0.595	0.000	0.000	0.000	0.000
74	A	107	LYS	1	0.811	0.892	15.647	14.218	14.218	0.000	0.000	0.000	0.000
75	A	108	GLU	-1	-0.777	-0.886	19.146	-14.651	-14.651	0.000	0.000	0.000	0.000
76	A	109	THR	0	-0.010	-0.007	20.944	0.610	0.610	0.000	0.000	0.000	0.000
77	A	110	LYS	1	0.883	0.894	24.269	11.629	11.629	0.000	0.000	0.000	0.000
78	A	111	GLU	-1	-0.910	-0.938	26.670	-10.251	-10.251	0.000	0.000	0.000	0.000
79	A	112	ARG	1	0.963	0.988	22.078	12.819	12.819	0.000	0.000	0.000	0.000
80	A	113	ALA	0	-0.037	-0.018	22.133	-0.339	-0.339	0.000	0.000	0.000	0.000
81	A	114	SER	0	-0.043	-0.006	23.206	-0.034	-0.034	0.000	0.000	0.000	0.000
82	A	115	MET	0	0.012	0.020	21.474	0.336	0.336	0.000	0.000	0.000	0.000
83	A	116	LYS	1	0.772	0.866	16.483	15.337	15.337	0.000	0.000	0.000	0.000
84	A	117	LEU	0	-0.031	0.013	17.587	0.602	0.602	0.000	0.000	0.000	0.000
85	A	118	LEU	0	0.001	-0.008	17.289	-0.875	-0.875	0.000	0.000	0.000	0.000
86	A	119	LYS	1	0.856	0.938	12.805	18.502	18.502	0.000	0.000	0.000	0.000
87	A	120	VAL	0	0.000	-0.002	17.422	-0.156	-0.156	0.000	0.000	0.000	0.000
88	A	121	ARG	1	0.930	0.966	12.702	17.227	17.227	0.000	0.000	0.000	0.000
89	A	122	SER	0	0.019	0.004	17.013	-0.217	-0.217	0.000	0.000	0.000	0.000
90	A	123	LYS	1	0.853	0.921	19.854	10.664	10.664	0.000	0.000	0.000	0.000
91	A	124	VAL	0	0.014	0.022	23.604	-0.060	-0.060	0.000	0.000	0.000	0.000
92	A	125	ILE	0	-0.031	-0.022	26.467	0.110	0.110	0.000	0.000	0.000	0.000
93	A	126	ALA	0	0.025	0.027	29.592	0.082	0.082	0.000	0.000	0.000	0.000
94	A	127	PRO	0	0.040	0.000	32.902	0.017	0.017	0.000	0.000	0.000	0.000
95	A	128	GLY	0	0.029	0.012	36.355	-0.037	-0.037	0.000	0.000	0.000	0.000
96	A	129	ASN	0	-0.041	-0.019	33.938	-0.073	-0.073	0.000	0.000	0.000	0.000
97	A	130	ARG	1	0.994	1.019	31.556	8.671	8.671	0.000	0.000	0.000	0.000
98	A	131	ILE	0	-0.020	-0.016	27.546	-0.198	-0.198	0.000	0.000	0.000	0.000
99	A	132	GLN	0	0.018	0.022	26.106	0.327	0.327	0.000	0.000	0.000	0.000
100	A	133	LEU	0	0.011	-0.004	23.535	-0.228	-0.228	0.000	0.000	0.000	0.000
101	A	134	GLY	0	0.046	0.024	20.631	0.098	0.098	0.000	0.000	0.000	0.000
102	A	135	THR	0	0.030	-0.020	18.615	-0.103	-0.103	0.000	0.000	0.000	0.000
103	A	136	HIS	0	-0.051	-0.040	12.293	0.557	0.557	0.000	0.000	0.000	0.000
104	A	137	ASP	-1	-0.742	-0.856	13.920	-15.799	-15.799	0.000	0.000	0.000	0.000
105	A	138	GLY	0	-0.047	-0.023	15.814	0.135	0.135	0.000	0.000	0.000	0.000
106	A	139	ARG	1	0.821	0.909	18.233	14.233	14.233	0.000	0.000	0.000	0.000
107	A	140	THR	0	-0.023	-0.019	21.346	-0.171	-0.171	0.000	0.000	0.000	0.000
108	A	141	PHE	0	0.007	0.013	22.437	0.258	0.258	0.000	0.000	0.000	0.000
109	A	142	ILE	0	-0.016	-0.013	26.767	-0.090	-0.090	0.000	0.000	0.000	0.000
110	A	143	THR	0	-0.010	-0.003	28.634	0.218	0.218	0.000	0.000	0.000	0.000
111	A	144	ASP	-1	-0.836	-0.923	31.060	-8.191	-8.191	0.000	0.000	0.000	0.000
112	A	145	ASP	-1	-0.787	-0.870	31.055	-8.963	-8.963	0.000	0.000	0.000	0.000
113	A	146	LYS	1	0.926	0.952	30.288	7.575	7.575	0.000	0.000	0.000	0.000
114	A	147	SER	0	-0.101	-0.068	30.038	-0.277	-0.277	0.000	0.000	0.000	0.000
115	A	148	ILE	0	0.021	0.011	24.741	-0.294	-0.294	0.000	0.000	0.000	0.000
116	A	149	LYS	1	0.843	0.917	23.814	9.911	9.911	0.000	0.000	0.000	0.000
117	A	150	VAL	0	0.025	0.012	18.076	-0.202	-0.202	0.000	0.000	0.000	0.000
118	A	151	GLY	0	-0.025	-0.018	17.760	0.041	0.041	0.000	0.000	0.000	0.000
119	A	152	ASP	-1	-0.754	-0.855	18.811	-11.494	-11.494	0.000	0.000	0.000	0.000
120	A	153	VAL	0	-0.030	-0.023	18.004	-0.484	-0.484	0.000	0.000	0.000	0.000
121	A	154	LEU	0	-0.010	0.012	20.775	0.629	0.629	0.000	0.000	0.000	0.000
122	A	155	ALA	0	0.006	0.013	21.633	-0.641	-0.641	0.000	0.000	0.000	0.000
123	A	156	VAL	0	0.009	-0.007	22.139	0.500	0.500	0.000	0.000	0.000	0.000
124	A	157	SER	0	-0.004	-0.013	24.267	-0.398	-0.398	0.000	0.000	0.000	0.000
125	A	158	VAL	0	-0.004	-0.022	22.326	-0.026	-0.026	0.000	0.000	0.000	0.000
126	A	159	PRO	0	-0.034	-0.026	25.126	0.044	0.044	0.000	0.000	0.000	0.000
127	A	160	ASP	-1	-0.795	-0.873	28.568	-9.409	-9.409	0.000	0.000	0.000	0.000
128	A	161	MET	0	-0.057	-0.020	23.606	-0.044	-0.044	0.000	0.000	0.000	0.000
129	A	162	LYS	1	0.873	0.951	27.146	8.991	8.991	0.000	0.000	0.000	0.000
130	A	163	ILE	0	-0.001	-0.007	26.020	-0.301	-0.301	0.000	0.000	0.000	0.000
131	A	164	SER	0	0.008	-0.002	27.390	0.247	0.247	0.000	0.000	0.000	0.000
132	A	165	GLU	-1	-0.828	-0.911	26.775	-9.658	-9.658	0.000	0.000	0.000	0.000
133	A	166	ILE	0	-0.007	0.003	25.125	-0.387	-0.387	0.000	0.000	0.000	0.000
134	A	167	ILE	0	-0.053	-0.028	21.379	0.330	0.330	0.000	0.000	0.000	0.000
135	A	168	LYS	1	0.863	0.930	22.791	10.036	10.036	0.000	0.000	0.000	0.000
136	A	169	MET	0	0.012	-0.001	16.859	-0.090	-0.090	0.000	0.000	0.000	0.000
137	A	170	GLN	0	-0.052	-0.025	22.316	0.272	0.272	0.000	0.000	0.000	0.000
138	A	171	PRO	0	0.031	-0.011	24.576	-0.305	-0.305	0.000	0.000	0.000	0.000
139	A	172	GLY	0	-0.012	0.006	25.871	0.301	0.301	0.000	0.000	0.000	0.000
140	A	173	ASN	0	-0.044	-0.021	23.456	0.306	0.306	0.000	0.000	0.000	0.000
141	A	174	LYS	1	0.906	0.963	20.164	12.749	12.749	0.000	0.000	0.000	0.000
142	A	175	ALA	0	-0.009	-0.013	16.600	0.038	0.038	0.000	0.000	0.000	0.000
143	A	176	TYR	0	0.022	-0.009	9.828	-0.080	-0.080	0.000	0.000	0.000	0.000
144	A	177	ILE	0	-0.022	0.001	9.995	0.146	0.146	0.000	0.000	0.000	0.000
145	A	178	THR	0	0.015	0.001	7.909	-0.721	-0.721	0.000	0.000	0.000	0.000
146	A	179	ALA	0	-0.008	-0.003	5.132	-3.738	-3.738	0.000	0.000	0.000	0.000
147	A	180	GLY	0	0.017	0.009	5.483	3.017	3.017	0.000	0.000	0.000	0.000
148	A	181	SER	0	0.018	-0.008	7.458	-1.556	-1.556	0.000	0.000	0.000	0.000
149	A	182	HIS	1	0.876	0.927	9.750	19.525	19.525	0.000	0.000	0.000	0.000
150	A	183	VAL	0	0.001	0.014	5.315	1.142	1.142	0.000	0.000	0.000	0.000
151	A	184	ASN	0	-0.020	-0.012	8.531	0.958	0.958	0.000	0.000	0.000	0.000
152	A	185	GLN	0	0.053	0.069	10.327	2.718	2.718	0.000	0.000	0.000	0.000
153	A	186	THR	0	-0.007	-0.022	13.580	-0.019	-0.019	0.000	0.000	0.000	0.000
154	A	187	GLY	0	-0.011	-0.001	16.637	0.158	0.158	0.000	0.000	0.000	0.000
155	A	188	THR	0	-0.054	-0.055	19.581	-0.004	-0.004	0.000	0.000	0.000	0.000
156	A	189	ILE	0	-0.030	0.003	19.969	0.027	0.027	0.000	0.000	0.000	0.000
157	A	190	SER	0	-0.011	-0.017	22.770	0.448	0.448	0.000	0.000	0.000	0.000
158	A	191	LYS	1	0.888	0.928	23.894	11.461	11.461	0.000	0.000	0.000	0.000
159	A	192	ILE	0	-0.005	-0.002	21.281	-0.571	-0.571	0.000	0.000	0.000	0.000
160	A	193	GLU	-1	-0.808	-0.869	22.397	-10.974	-10.974	0.000	0.000	0.000	0.000
161	A	194	ALA	0	-0.010	-0.010	22.153	-0.507	-0.507	0.000	0.000	0.000	0.000
162	A	195	LYS	1	0.925	0.970	23.339	10.129	10.129	0.000	0.000	0.000	0.000
163	A	196	GLU	-1	-0.913	-0.949	23.904	-9.843	-9.843	0.000	0.000	0.000	0.000
164	A	197	GLY	0	0.041	0.014	23.880	0.132	0.132	0.000	0.000	0.000	0.000
165	A	198	SER	0	0.006	-0.007	20.028	-0.013	-0.013	0.000	0.000	0.000	0.000
166	A	199	SER	0	0.008	-0.005	19.973	-0.133	-0.133	0.000	0.000	0.000	0.000
167	A	200	ALA	0	0.072	0.062	17.895	-0.680	-0.680	0.000	0.000	0.000	0.000
168	A	201	ASN	0	-0.114	-0.078	18.338	0.287	0.287	0.000	0.000	0.000	0.000
169	A	202	LEU	0	-0.020	-0.010	16.729	-0.774	-0.774	0.000	0.000	0.000	0.000
170	A	203	VAL	0	-0.035	-0.012	17.420	0.746	0.746	0.000	0.000	0.000	0.000
171	A	204	HIS	0	-0.020	-0.032	18.466	-0.694	-0.694	0.000	0.000	0.000	0.000
172	A	205	PHE	0	0.013	0.001	16.484	0.226	0.226	0.000	0.000	0.000	0.000
173	A	206	GLN	0	0.008	-0.010	21.617	0.167	0.167	0.000	0.000	0.000	0.000
174	A	207	GLU	-1	-0.800	-0.887	20.479	-13.035	-13.035	0.000	0.000	0.000	0.000
175	A	208	GLY	0	0.006	0.021	21.859	-0.216	-0.216	0.000	0.000	0.000	0.000
176	A	209	PHE	0	-0.028	-0.018	15.273	-0.516	-0.516	0.000	0.000	0.000	0.000
177	A	210	SER	0	0.019	0.004	17.890	0.283	0.283	0.000	0.000	0.000	0.000
178	A	211	THR	0	-0.006	0.000	12.589	-0.963	-0.963	0.000	0.000	0.000	0.000
179	A	212	ILE	0	0.045	0.027	10.741	0.840	0.840	0.000	0.000	0.000	0.000
180	A	213	LYS	1	1.021	1.001	13.578	12.125	12.125	0.000	0.000	0.000	0.000
181	A	214	ASP	-1	-0.914	-0.953	10.932	-17.719	-17.719	0.000	0.000	0.000	0.000
182	A	215	HIS	0	-0.012	-0.012	8.073	-1.148	-1.148	0.000	0.000	0.000	0.000
183	A	216	VAL	0	-0.003	0.021	10.705	-0.447	-0.447	0.000	0.000	0.000	0.000
184	A	217	PHE	0	-0.007	0.002	12.553	0.585	0.585	0.000	0.000	0.000	0.000
185	A	218	MET	0	-0.016	0.005	14.718	-0.140	-0.140	0.000	0.000	0.000	0.000
186	A	219	ILE	0	0.014	-0.015	16.572	-0.132	-0.132	0.000	0.000	0.000	0.000
187	A	220	GLY	0	-0.001	0.008	19.487	0.283	0.283	0.000	0.000	0.000	0.000
188	A	221	SER	0	-0.027	-0.016	23.107	0.074	0.074	0.000	0.000	0.000	0.000
189	A	222	SER	0	0.034	-0.002	26.396	-0.015	-0.015	0.000	0.000	0.000	0.000
190	A	223	LYS	1	0.835	0.923	28.589	10.156	10.156	0.000	0.000	0.000	0.000
191	A	224	PHE	0	0.037	0.023	23.479	0.019	0.019	0.000	0.000	0.000	0.000
192	A	225	SER	0	0.004	-0.007	24.109	-0.395	-0.395	0.000	0.000	0.000	0.000
193	A	226	PHE	0	0.005	0.014	17.970	0.108	0.108	0.000	0.000	0.000	0.000
194	A	227	VAL	0	0.004	0.003	20.222	0.123	0.123	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:34:LYS)