FMO DATABASE

FMODB ID: 7G1KK

Calculation Name: 3T8K-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3T8K

Chain ID: A

ChEMBL ID:

UniProt ID: C7NDE2

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:

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	184
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2062087.150508
FMO2-HF: Nuclear repulsion	1987359.458542
FMO2-HF: Total energy	-74727.691966
FMO2-MP2: Total energy	-74944.700073

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:SER)

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

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.
-10.179	-4.43	3.098	-3.934	-4.914	-0.023

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.024 / q_NPA : -0.027

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	ALA	0	0.091	0.056	3.866	-0.897	0.172	-0.008	-0.419	-0.642	0.001
4	A	1	MET	0	-0.027	-0.007	2.256	0.463	0.719	2.201	-1.008	-1.449	0.002
5	A	2	SER	0	-0.073	-0.040	3.412	1.815	2.252	0.003	-0.170	-0.271	0.000
6	A	3	GLU	-1	-0.878	-0.914	5.461	-0.545	-0.545	0.000	0.000	0.000	0.000
7	A	4	TYR	0	-0.044	-0.040	7.788	0.568	0.568	0.000	0.000	0.000	0.000
8	A	5	ARG	1	0.858	0.929	6.808	1.693	1.693	0.000	0.000	0.000	0.000
9	A	6	THR	0	0.011	-0.001	10.496	0.058	0.058	0.000	0.000	0.000	0.000
10	A	7	VAL	0	0.039	0.005	11.623	-0.080	-0.080	0.000	0.000	0.000	0.000
11	A	8	SER	0	-0.072	-0.050	12.693	-0.002	-0.002	0.000	0.000	0.000	0.000
12	A	9	ALA	0	-0.012	-0.009	12.494	0.022	0.022	0.000	0.000	0.000	0.000
13	A	10	ALA	0	0.060	0.029	9.859	0.004	0.004	0.000	0.000	0.000	0.000
14	A	11	ALA	0	-0.023	-0.014	11.850	0.084	0.084	0.000	0.000	0.000	0.000
15	A	12	MET	0	-0.037	-0.008	15.017	0.078	0.078	0.000	0.000	0.000	0.000
16	A	13	LEU	0	-0.049	-0.023	13.977	0.041	0.041	0.000	0.000	0.000	0.000
17	A	14	GLY	0	0.033	0.041	11.966	0.007	0.007	0.000	0.000	0.000	0.000
18	A	15	THR	0	-0.020	-0.051	10.691	0.144	0.144	0.000	0.000	0.000	0.000
19	A	16	TYR	0	0.004	-0.015	12.498	-0.079	-0.079	0.000	0.000	0.000	0.000
20	A	17	GLU	-1	-0.771	-0.889	9.578	0.014	0.014	0.000	0.000	0.000	0.000
21	A	18	ASP	-1	-0.768	-0.854	7.652	-0.843	-0.843	0.000	0.000	0.000	0.000
22	A	19	PHE	0	0.008	-0.009	8.205	-0.219	-0.219	0.000	0.000	0.000	0.000
23	A	20	LEU	0	-0.020	-0.009	10.108	0.002	0.002	0.000	0.000	0.000	0.000
24	A	21	GLU	-1	-0.833	-0.904	2.642	-7.751	-4.142	0.899	-2.219	-2.289	-0.027
25	A	22	LEU	0	-0.008	-0.003	6.201	0.190	0.190	0.000	0.000	0.000	0.000
26	A	23	PHE	0	-0.060	-0.031	8.107	0.165	0.165	0.000	0.000	0.000	0.000
27	A	24	GLU	-1	-0.856	-0.936	9.314	0.294	0.294	0.000	0.000	0.000	0.000
28	A	25	LYS	1	0.842	0.910	3.630	-5.094	-4.716	0.003	-0.118	-0.263	0.001
29	A	26	GLY	0	0.034	0.024	7.685	-0.109	-0.109	0.000	0.000	0.000	0.000
30	A	27	TYR	0	-0.122	-0.078	9.177	0.133	0.133	0.000	0.000	0.000	0.000
31	A	28	GLU	-1	-0.832	-0.893	12.134	-0.436	-0.436	0.000	0.000	0.000	0.000
32	A	29	ASP	-1	-0.768	-0.865	14.401	-0.031	-0.031	0.000	0.000	0.000	0.000
33	A	30	LYS	1	0.868	0.921	13.081	-0.182	-0.182	0.000	0.000	0.000	0.000
34	A	31	GLU	-1	-0.855	-0.915	16.961	-0.028	-0.028	0.000	0.000	0.000	0.000
35	A	32	SER	0	-0.056	-0.065	19.735	-0.005	-0.005	0.000	0.000	0.000	0.000
36	A	33	VAL	0	-0.022	-0.005	15.448	-0.010	-0.010	0.000	0.000	0.000	0.000
37	A	34	LEU	0	-0.013	0.007	18.850	-0.007	-0.007	0.000	0.000	0.000	0.000
38	A	35	LYS	1	0.829	0.908	21.157	0.047	0.047	0.000	0.000	0.000	0.000
39	A	36	SER	0	-0.013	-0.005	20.759	-0.013	-0.013	0.000	0.000	0.000	0.000
40	A	37	ASN	0	0.018	0.004	23.359	0.017	0.017	0.000	0.000	0.000	0.000
41	A	38	ILE	0	0.033	0.023	16.563	-0.006	-0.006	0.000	0.000	0.000	0.000
42	A	39	LEU	0	0.057	0.020	20.319	-0.016	-0.016	0.000	0.000	0.000	0.000
43	A	40	TYR	0	-0.028	-0.025	22.451	0.003	0.003	0.000	0.000	0.000	0.000
44	A	41	ASP	-1	-0.823	-0.877	18.724	-0.300	-0.300	0.000	0.000	0.000	0.000
45	A	42	VAL	0	0.007	0.009	17.869	-0.009	-0.009	0.000	0.000	0.000	0.000
46	A	43	LEU	0	-0.056	-0.034	19.916	0.008	0.008	0.000	0.000	0.000	0.000
47	A	44	ARG	1	0.800	0.877	22.129	0.245	0.245	0.000	0.000	0.000	0.000
48	A	45	ASN	0	-0.031	-0.007	16.067	0.009	0.009	0.000	0.000	0.000	0.000
49	A	46	ASN	0	-0.035	-0.024	20.102	0.047	0.047	0.000	0.000	0.000	0.000
50	A	47	ASN	0	0.039	0.034	16.218	0.051	0.051	0.000	0.000	0.000	0.000
51	A	48	ASP	-1	-0.757	-0.892	19.982	-0.090	-0.090	0.000	0.000	0.000	0.000
52	A	49	GLU	-1	-0.877	-0.920	17.503	0.021	0.021	0.000	0.000	0.000	0.000
53	A	50	ALA	0	0.010	0.007	16.275	0.014	0.014	0.000	0.000	0.000	0.000
54	A	51	ARG	1	0.805	0.907	17.896	0.085	0.085	0.000	0.000	0.000	0.000
55	A	52	TYR	0	0.012	0.017	20.889	0.008	0.008	0.000	0.000	0.000	0.000
56	A	53	LYS	1	0.798	0.871	15.611	-0.042	-0.042	0.000	0.000	0.000	0.000
57	A	54	ILE	0	-0.001	0.004	14.849	0.019	0.019	0.000	0.000	0.000	0.000
58	A	55	SER	0	-0.017	-0.014	17.788	0.002	0.002	0.000	0.000	0.000	0.000
59	A	56	MET	0	-0.031	-0.009	21.355	0.012	0.012	0.000	0.000	0.000	0.000
60	A	57	PHE	0	-0.013	-0.003	14.997	0.014	0.014	0.000	0.000	0.000	0.000
61	A	58	LEU	0	0.033	0.008	17.047	0.012	0.012	0.000	0.000	0.000	0.000
62	A	59	ILE	0	-0.002	-0.004	20.241	0.008	0.008	0.000	0.000	0.000	0.000
63	A	60	ASN	0	-0.048	-0.029	22.856	0.002	0.002	0.000	0.000	0.000	0.000
64	A	61	LYS	1	0.899	0.966	17.181	-0.082	-0.082	0.000	0.000	0.000	0.000
65	A	62	GLY	0	-0.013	0.004	21.852	0.004	0.004	0.000	0.000	0.000	0.000
66	A	63	ALA	0	-0.028	-0.012	21.430	-0.007	-0.007	0.000	0.000	0.000	0.000
67	A	64	ASP	-1	-0.822	-0.913	23.455	-0.065	-0.065	0.000	0.000	0.000	0.000
68	A	65	ILE	0	-0.032	-0.024	25.994	-0.008	-0.008	0.000	0.000	0.000	0.000
69	A	66	LYS	1	0.764	0.867	28.636	0.038	0.038	0.000	0.000	0.000	0.000
70	A	67	SER	0	0.003	0.015	27.109	0.003	0.003	0.000	0.000	0.000	0.000
71	A	68	ARG	1	0.787	0.865	29.693	0.071	0.071	0.000	0.000	0.000	0.000
72	A	69	THR	0	-0.012	-0.021	28.477	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	70	LYS	1	0.978	0.995	30.529	0.150	0.150	0.000	0.000	0.000	0.000
74	A	71	GLU	-1	-0.833	-0.900	32.417	-0.121	-0.121	0.000	0.000	0.000	0.000
75	A	72	GLY	0	-0.049	-0.027	34.161	0.009	0.009	0.000	0.000	0.000	0.000
76	A	73	THR	0	-0.051	-0.020	31.742	0.009	0.009	0.000	0.000	0.000	0.000
77	A	74	THR	0	0.046	0.014	31.370	-0.009	-0.009	0.000	0.000	0.000	0.000
78	A	75	LEU	0	0.073	0.032	26.011	-0.005	-0.005	0.000	0.000	0.000	0.000
79	A	76	PHE	0	0.031	-0.002	29.043	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	77	PHE	0	-0.021	0.003	31.045	0.001	0.001	0.000	0.000	0.000	0.000
81	A	78	PRO	0	-0.025	-0.007	26.108	0.002	0.002	0.000	0.000	0.000	0.000
82	A	79	LEU	0	0.018	0.028	27.827	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	80	PHE	0	0.032	-0.003	28.740	0.005	0.005	0.000	0.000	0.000	0.000
84	A	81	GLN	0	-0.060	-0.023	29.928	0.011	0.011	0.000	0.000	0.000	0.000
85	A	82	GLY	0	0.041	0.023	27.271	0.001	0.001	0.000	0.000	0.000	0.000
86	A	83	GLY	0	0.007	0.012	27.986	0.001	0.001	0.000	0.000	0.000	0.000
87	A	84	GLY	0	-0.007	-0.009	28.952	0.010	0.010	0.000	0.000	0.000	0.000
88	A	85	ASN	0	-0.056	-0.034	26.456	0.011	0.011	0.000	0.000	0.000	0.000
89	A	86	ASP	-1	-0.796	-0.884	26.670	-0.028	-0.028	0.000	0.000	0.000	0.000
90	A	87	ILE	0	0.059	0.031	29.139	-0.003	-0.003	0.000	0.000	0.000	0.000
91	A	88	THR	0	0.003	0.011	30.081	0.000	0.000	0.000	0.000	0.000	0.000
92	A	89	GLY	0	0.057	0.022	27.399	0.002	0.002	0.000	0.000	0.000	0.000
93	A	90	THR	0	-0.030	-0.033	28.392	-0.007	-0.007	0.000	0.000	0.000	0.000
94	A	91	THR	0	-0.042	-0.030	30.125	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	92	GLU	-1	-0.877	-0.954	29.335	0.000	0.000	0.000	0.000	0.000	0.000
96	A	93	LEU	0	-0.008	-0.003	24.961	0.000	0.000	0.000	0.000	0.000	0.000
97	A	94	CYS	0	-0.033	-0.006	29.078	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	95	LYS	1	0.794	0.901	32.556	0.002	0.002	0.000	0.000	0.000	0.000
99	A	96	ILE	0	0.044	0.019	28.294	0.000	0.000	0.000	0.000	0.000	0.000
100	A	97	PHE	0	0.000	-0.018	26.218	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	98	LEU	0	-0.029	-0.012	31.599	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	99	GLU	-1	-0.839	-0.908	33.494	-0.003	-0.003	0.000	0.000	0.000	0.000
103	A	100	LYS	1	0.884	0.958	27.351	0.013	0.013	0.000	0.000	0.000	0.000
104	A	101	GLY	0	-0.002	0.005	33.181	-0.003	-0.003	0.000	0.000	0.000	0.000
105	A	102	ALA	0	-0.003	0.009	32.176	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	103	ASP	-1	-0.782	-0.867	34.253	-0.050	-0.050	0.000	0.000	0.000	0.000
107	A	104	ILE	0	0.025	0.014	35.957	-0.006	-0.006	0.000	0.000	0.000	0.000
108	A	105	THR	0	-0.057	-0.036	37.725	0.001	0.001	0.000	0.000	0.000	0.000
109	A	106	ALA	0	-0.010	0.005	37.894	0.000	0.000	0.000	0.000	0.000	0.000
110	A	107	LEU	0	-0.011	-0.008	39.284	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	108	TYR	0	0.035	0.014	33.099	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	109	LYS	1	0.923	0.933	37.443	0.077	0.077	0.000	0.000	0.000	0.000
113	A	110	PRO	0	-0.006	0.012	35.315	0.003	0.003	0.000	0.000	0.000	0.000
114	A	111	TYR	0	0.010	-0.009	36.217	0.002	0.002	0.000	0.000	0.000	0.000
115	A	112	LYS	1	0.833	0.918	40.576	0.058	0.058	0.000	0.000	0.000	0.000
116	A	113	ILE	0	0.027	0.028	37.573	0.004	0.004	0.000	0.000	0.000	0.000
117	A	114	VAL	0	0.035	0.010	40.160	-0.003	-0.003	0.000	0.000	0.000	0.000
118	A	115	VAL	0	-0.007	0.003	34.412	-0.002	-0.002	0.000	0.000	0.000	0.000
119	A	116	PHE	0	0.093	0.037	35.466	-0.004	-0.004	0.000	0.000	0.000	0.000
120	A	117	LYS	1	0.831	0.926	37.251	0.060	0.060	0.000	0.000	0.000	0.000
121	A	118	ASN	0	0.012	0.004	33.403	0.005	0.005	0.000	0.000	0.000	0.000
122	A	119	ILE	0	0.021	0.018	35.072	0.001	0.001	0.000	0.000	0.000	0.000
123	A	120	PHE	0	-0.052	-0.030	37.127	0.003	0.003	0.000	0.000	0.000	0.000
124	A	121	ASN	0	-0.002	-0.018	37.306	0.006	0.006	0.000	0.000	0.000	0.000
125	A	122	TYR	0	-0.011	-0.002	32.454	0.000	0.000	0.000	0.000	0.000	0.000
126	A	123	PHE	0	-0.020	0.001	36.023	0.005	0.005	0.000	0.000	0.000	0.000
127	A	124	VAL	0	0.032	0.021	34.765	0.001	0.001	0.000	0.000	0.000	0.000
128	A	125	ASP	-1	-0.833	-0.928	37.944	-0.015	-0.015	0.000	0.000	0.000	0.000
129	A	126	GLU	-1	-0.731	-0.865	40.465	-0.025	-0.025	0.000	0.000	0.000	0.000
130	A	127	ASN	0	-0.044	-0.029	42.193	0.000	0.000	0.000	0.000	0.000	0.000
131	A	128	GLU	-1	-0.863	-0.937	36.481	-0.013	-0.013	0.000	0.000	0.000	0.000
132	A	129	MET	0	-0.032	0.002	37.191	-0.002	-0.002	0.000	0.000	0.000	0.000
133	A	130	ILE	0	-0.021	-0.002	39.523	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	131	PRO	0	-0.015	-0.011	37.682	0.000	0.000	0.000	0.000	0.000	0.000
135	A	132	LEU	0	0.061	0.038	34.967	-0.001	-0.001	0.000	0.000	0.000	0.000
136	A	133	TYR	0	-0.039	-0.069	38.096	-0.003	-0.003	0.000	0.000	0.000	0.000
137	A	134	LYS	1	0.945	0.975	41.623	0.006	0.006	0.000	0.000	0.000	0.000
138	A	135	LEU	0	-0.010	0.029	35.692	0.000	0.000	0.000	0.000	0.000	0.000
139	A	136	ILE	0	0.027	0.019	37.629	-0.001	-0.001	0.000	0.000	0.000	0.000
140	A	137	PHE	0	-0.024	-0.035	40.765	0.000	0.000	0.000	0.000	0.000	0.000
141	A	138	SER	0	-0.032	-0.028	42.899	0.002	0.002	0.000	0.000	0.000	0.000
142	A	139	GLN	0	-0.023	0.000	40.439	0.001	0.001	0.000	0.000	0.000	0.000
143	A	140	SER	0	-0.009	0.017	43.847	0.001	0.001	0.000	0.000	0.000	0.000
144	A	141	GLY	0	0.052	0.019	44.815	-0.002	-0.002	0.000	0.000	0.000	0.000
145	A	142	LEU	0	-0.006	0.001	41.857	-0.003	-0.003	0.000	0.000	0.000	0.000
146	A	143	GLN	0	0.001	-0.009	43.312	0.002	0.002	0.000	0.000	0.000	0.000
147	A	144	LEU	0	-0.021	-0.026	45.004	-0.002	-0.002	0.000	0.000	0.000	0.000
148	A	145	LEU	0	0.007	-0.008	47.394	0.000	0.000	0.000	0.000	0.000	0.000
149	A	146	ILE	0	-0.002	0.012	46.968	0.000	0.000	0.000	0.000	0.000	0.000
150	A	147	LYS	1	0.813	0.893	47.636	0.035	0.035	0.000	0.000	0.000	0.000
151	A	148	ASP	-1	-0.723	-0.869	44.222	-0.057	-0.057	0.000	0.000	0.000	0.000
152	A	149	LYS	1	0.811	0.905	41.209	0.082	0.082	0.000	0.000	0.000	0.000
153	A	150	TRP	0	-0.011	-0.008	40.883	-0.001	-0.001	0.000	0.000	0.000	0.000
154	A	151	GLY	0	0.001	0.021	48.053	0.002	0.002	0.000	0.000	0.000	0.000
155	A	152	LEU	0	-0.046	-0.019	46.372	0.003	0.003	0.000	0.000	0.000	0.000
156	A	153	THR	0	-0.035	-0.037	47.322	-0.002	-0.002	0.000	0.000	0.000	0.000
157	A	154	ALA	0	0.011	0.001	44.774	-0.001	-0.001	0.000	0.000	0.000	0.000
158	A	155	LEU	0	0.070	0.033	46.180	0.000	0.000	0.000	0.000	0.000	0.000
159	A	156	GLU	-1	-0.839	-0.901	49.355	-0.035	-0.035	0.000	0.000	0.000	0.000
160	A	157	PHE	0	-0.011	-0.008	41.731	0.000	0.000	0.000	0.000	0.000	0.000
161	A	158	VAL	0	0.049	0.023	44.572	0.000	0.000	0.000	0.000	0.000	0.000
162	A	159	LYS	1	0.913	0.969	47.081	0.031	0.031	0.000	0.000	0.000	0.000
163	A	160	ARG	1	0.867	0.945	49.003	0.042	0.042	0.000	0.000	0.000	0.000
164	A	161	CYS	0	-0.005	0.015	44.970	-0.003	-0.003	0.000	0.000	0.000	0.000
165	A	162	GLN	0	0.020	0.010	46.032	0.001	0.001	0.000	0.000	0.000	0.000
166	A	163	LYS	1	0.839	0.930	40.124	0.033	0.033	0.000	0.000	0.000	0.000
167	A	164	PRO	0	0.058	0.024	46.177	0.000	0.000	0.000	0.000	0.000	0.000
168	A	165	ILE	0	-0.015	-0.013	46.169	0.001	0.001	0.000	0.000	0.000	0.000
169	A	166	ALA	0	0.012	0.008	44.165	0.000	0.000	0.000	0.000	0.000	0.000
170	A	167	LEU	0	-0.005	-0.002	46.071	0.000	0.000	0.000	0.000	0.000	0.000
171	A	168	LYS	1	0.892	0.939	49.345	0.015	0.015	0.000	0.000	0.000	0.000
172	A	169	MET	0	-0.010	-0.009	45.437	0.001	0.001	0.000	0.000	0.000	0.000
173	A	170	MET	0	-0.039	-0.008	46.162	-0.001	-0.001	0.000	0.000	0.000	0.000
174	A	171	GLU	-1	-0.921	-0.964	49.027	-0.021	-0.021	0.000	0.000	0.000	0.000
175	A	172	ASP	-1	-0.858	-0.918	51.906	-0.014	-0.014	0.000	0.000	0.000	0.000
176	A	173	TYR	0	-0.053	-0.030	46.150	0.000	0.000	0.000	0.000	0.000	0.000
177	A	174	ILE	0	-0.005	-0.016	50.714	0.000	0.000	0.000	0.000	0.000	0.000
178	A	175	LYS	1	0.938	0.971	52.988	0.014	0.014	0.000	0.000	0.000	0.000
179	A	176	LYS	1	0.880	0.949	49.181	0.016	0.016	0.000	0.000	0.000	0.000
180	A	177	TYR	0	-0.033	-0.035	47.583	0.002	0.002	0.000	0.000	0.000	0.000
181	A	178	ASN	0	0.013	0.014	53.680	-0.001	-0.001	0.000	0.000	0.000	0.000
182	A	179	LEU	0	0.010	0.031	50.166	-0.001	-0.001	0.000	0.000	0.000	0.000
183	A	180	LYS	1	0.807	0.877	54.714	0.023	0.023	0.000	0.000	0.000	0.000
184	A	181	GLU	-1	-0.833	-0.897	54.468	-0.035	-0.035	0.000	0.000	0.000	0.000

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