FMO DATABASE

FMODB ID: K2ZN3

Calculation Name: 3F62-A-Xray540

Preferred Name: Interleukin-18

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3F62

Chain ID: A

ChEMBL ID: CHEMBL1741305

UniProt ID: Q14116

Base Structure: X-ray

Registration Date: 2025-07-08

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	205
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-822211.042004
FMO2-HF: Nuclear repulsion	777906.536635
FMO2-HF: Total energy	-44304.50537
FMO2-MP2: Total energy	-44428.320043

3D Structure Molmil

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:18:GLY)

Summations of interaction energy for fragment #1(A:18:GLY)

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.
2.466	3.488	-0.002	-0.379	-0.64	0.001

Interaction energy analysis for fragmet #1(A:18:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.029 / q_NPA : -0.008

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	19	ALA	0	-0.099	0.108	4.496	0.448	0.606	0.000	-0.062	-0.095	0.000
4	A	20	MET	0	0.023	-0.081	3.844	0.352	1.216	-0.002	-0.317	-0.545	0.001
5	A	20	MET	0	-0.111	0.075	4.934	0.279	0.279	0.000	0.000	0.000	0.000
6	A	21	VAL	0	0.056	-0.097	5.978	0.203	0.203	0.000	0.000	0.000	0.000
7	A	21	VAL	0	-0.064	0.066	7.236	0.029	0.029	0.000	0.000	0.000	0.000
8	A	22	GLU	0	0.129	-0.108	8.146	0.128	0.128	0.000	0.000	0.000	0.000
9	A	22	GLU	-1	-0.988	-0.838	12.402	0.019	0.019	0.000	0.000	0.000	0.000
10	A	23	THR	0	-0.024	-0.117	10.569	0.057	0.057	0.000	0.000	0.000	0.000
11	A	23	THR	0	0.010	0.104	8.913	0.104	0.104	0.000	0.000	0.000	0.000
12	A	24	LYS	0	0.060	-0.089	10.993	-0.060	-0.060	0.000	0.000	0.000	0.000
13	A	24	LYS	1	0.798	1.026	13.932	-0.224	-0.224	0.000	0.000	0.000	0.000
14	A	25	CYS	0	0.127	-0.107	14.471	0.058	0.058	0.000	0.000	0.000	0.000
15	A	25	CYS	0	-0.083	0.132	15.008	0.005	0.005	0.000	0.000	0.000	0.000
16	A	26	PRO	0	-0.016	-0.100	16.515	-0.040	-0.040	0.000	0.000	0.000	0.000
17	A	27	ASN	0	0.086	0.033	16.267	0.024	0.024	0.000	0.000	0.000	0.000
18	A	27	ASN	0	-0.108	0.065	15.562	-0.027	-0.027	0.000	0.000	0.000	0.000
19	A	28	LEU	0	0.144	-0.094	17.539	0.042	0.042	0.000	0.000	0.000	0.000
20	A	28	LEU	0	-0.089	0.095	21.271	-0.005	-0.005	0.000	0.000	0.000	0.000
21	A	29	ASP	0	-0.008	-0.129	19.403	-0.026	-0.026	0.000	0.000	0.000	0.000
22	A	29	ASP	-1	-0.840	-0.765	18.784	0.225	0.225	0.000	0.000	0.000	0.000
23	A	30	ILE	0	0.084	-0.095	20.565	0.018	0.018	0.000	0.000	0.000	0.000
24	A	30	ILE	0	-0.099	0.082	24.040	-0.002	-0.002	0.000	0.000	0.000	0.000
25	A	31	VAL	0	0.143	-0.054	21.611	-0.017	-0.017	0.000	0.000	0.000	0.000
26	A	31	VAL	0	-0.075	0.100	19.450	0.002	0.002	0.000	0.000	0.000	0.000
27	A	32	THR	0	-0.015	-0.119	22.708	-0.002	-0.002	0.000	0.000	0.000	0.000
28	A	32	THR	0	-0.001	0.089	26.068	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	33	SER	0	0.008	-0.055	25.419	0.002	0.002	0.000	0.000	0.000	0.000
30	A	33	SER	0	-0.054	0.035	25.671	0.004	0.004	0.000	0.000	0.000	0.000
31	A	34	SER	0	0.043	-0.098	27.423	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	34	SER	0	-0.058	0.068	30.914	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	35	GLY	0	0.022	-0.077	30.994	0.001	0.001	0.000	0.000	0.000	0.000
34	A	36	GLU	0	0.035	-0.038	29.011	-0.004	-0.004	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.830	-0.744	27.858	0.129	0.129	0.000	0.000	0.000	0.000
36	A	37	PHE	0	0.030	-0.084	27.175	0.000	0.000	0.000	0.000	0.000	0.000
37	A	37	PHE	0	-0.032	0.090	27.553	0.000	0.000	0.000	0.000	0.000	0.000
38	A	38	HIS	0	0.101	-0.084	23.438	-0.008	-0.008	0.000	0.000	0.000	0.000
39	A	38	HIS	0	-0.139	0.061	22.482	0.018	0.018	0.000	0.000	0.000	0.000
40	A	39	CYS	0	0.147	-0.093	22.536	0.016	0.016	0.000	0.000	0.000	0.000
41	A	39	CYS	0	-0.229	0.197	23.959	0.005	0.005	0.000	0.000	0.000	0.000
42	A	40	SER	0	-0.017	-0.099	18.770	-0.005	-0.005	0.000	0.000	0.000	0.000
43	A	40	SER	0	-0.035	0.066	17.883	0.025	0.025	0.000	0.000	0.000	0.000
44	A	41	GLY	0	0.026	-0.090	17.870	-0.020	-0.020	0.000	0.000	0.000	0.000
45	A	42	CYS	0	0.025	0.001	15.538	-0.012	-0.012	0.000	0.000	0.000	0.000
46	A	42	CYS	0	-0.117	0.112	15.132	0.022	0.022	0.000	0.000	0.000	0.000
47	A	43	VAL	0	0.127	-0.115	16.876	-0.034	-0.034	0.000	0.000	0.000	0.000
48	A	43	VAL	0	-0.061	0.106	19.084	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	44	GLU	0	0.069	-0.091	15.640	0.046	0.046	0.000	0.000	0.000	0.000
50	A	44	GLU	-1	-0.999	-0.864	14.121	0.244	0.244	0.000	0.000	0.000	0.000
51	A	45	HIS	0	0.180	-0.083	16.751	-0.004	-0.004	0.000	0.000	0.000	0.000
52	A	45	HIS	0	-0.087	0.105	19.932	0.003	0.003	0.000	0.000	0.000	0.000
53	A	46	MET	0	-0.012	-0.093	19.976	0.009	0.009	0.000	0.000	0.000	0.000
54	A	46	MET	0	-0.129	0.073	23.743	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	47	PRO	0	0.092	-0.072	18.932	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	48	GLU	0	0.097	0.026	21.175	0.012	0.012	0.000	0.000	0.000	0.000
57	A	48	GLU	-1	-0.860	-0.813	23.440	0.162	0.162	0.000	0.000	0.000	0.000
58	A	49	PHE	0	-0.017	-0.097	24.316	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	49	PHE	0	-0.104	0.073	26.294	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	50	SER	0	0.077	-0.110	23.687	-0.008	-0.008	0.000	0.000	0.000	0.000
61	A	50	SER	0	-0.039	0.064	22.765	0.010	0.010	0.000	0.000	0.000	0.000
62	A	51	TYR	0	0.002	-0.102	25.175	0.006	0.006	0.000	0.000	0.000	0.000
63	A	51	TYR	0	-0.055	0.097	27.831	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	52	MET	0	0.113	-0.097	24.887	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	52	MET	0	-0.118	0.099	21.372	0.002	0.002	0.000	0.000	0.000	0.000
66	A	53	TYR	0	0.050	-0.095	26.215	0.000	0.000	0.000	0.000	0.000	0.000
67	A	53	TYR	0	-0.079	0.082	29.361	-0.004	-0.004	0.000	0.000	0.000	0.000
68	A	54	TRP	0	0.058	-0.100	28.951	0.007	0.007	0.000	0.000	0.000	0.000
69	A	54	TRP	0	-0.100	0.091	26.824	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	55	LEU	0	0.124	-0.094	31.113	-0.004	-0.004	0.000	0.000	0.000	0.000
71	A	55	LEU	0	-0.112	0.083	33.367	0.000	0.000	0.000	0.000	0.000	0.000
72	A	56	ALA	0	0.093	-0.099	33.792	0.005	0.005	0.000	0.000	0.000	0.000
73	A	56	ALA	0	-0.070	0.102	35.986	0.000	0.000	0.000	0.000	0.000	0.000
74	A	57	LYS	0	0.079	-0.104	36.513	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	57	LYS	1	0.697	0.968	38.908	-0.051	-0.051	0.000	0.000	0.000	0.000
76	A	58	ASP	0	0.111	-0.095	39.379	0.003	0.003	0.000	0.000	0.000	0.000
77	A	58	ASP	-1	-0.861	-0.764	43.143	0.048	0.048	0.000	0.000	0.000	0.000
78	A	59	MET	0	0.059	-0.088	41.151	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	59	MET	0	-0.130	0.091	39.098	0.001	0.001	0.000	0.000	0.000	0.000
80	A	60	LYS	0	0.099	-0.090	42.304	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	60	LYS	1	0.777	1.034	45.068	-0.043	-0.043	0.000	0.000	0.000	0.000
82	A	61	SER	0	-0.012	-0.099	45.413	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	61	SER	0	-0.063	0.033	46.170	0.000	0.000	0.000	0.000	0.000	0.000
84	A	62	ASP	0	0.029	-0.131	45.802	0.002	0.002	0.000	0.000	0.000	0.000
85	A	62	ASP	-1	-0.903	-0.806	48.874	0.038	0.038	0.000	0.000	0.000	0.000
86	A	63	GLU	0	0.094	-0.102	46.457	0.001	0.001	0.000	0.000	0.000	0.000
87	A	63	GLU	-1	-0.936	-0.807	45.051	0.048	0.048	0.000	0.000	0.000	0.000
88	A	64	ASP	0	0.122	-0.113	43.912	0.002	0.002	0.000	0.000	0.000	0.000
89	A	64	ASP	-1	-0.962	-0.809	43.084	0.054	0.054	0.000	0.000	0.000	0.000
90	A	65	THR	0	0.011	-0.095	39.244	0.000	0.000	0.000	0.000	0.000	0.000
91	A	65	THR	0	-0.072	0.047	37.129	0.001	0.001	0.000	0.000	0.000	0.000
92	A	66	LYS	0	0.013	-0.076	39.242	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	66	LYS	1	0.749	0.979	40.514	-0.055	-0.055	0.000	0.000	0.000	0.000
94	A	67	PHE	0	0.076	-0.095	36.302	0.004	0.004	0.000	0.000	0.000	0.000
95	A	67	PHE	0	-0.054	0.105	34.932	0.000	0.000	0.000	0.000	0.000	0.000
96	A	68	ILE	0	0.112	-0.090	35.428	-0.006	-0.006	0.000	0.000	0.000	0.000
97	A	68	ILE	0	-0.093	0.111	33.462	0.001	0.001	0.000	0.000	0.000	0.000
98	A	69	GLU	0	0.088	-0.102	36.772	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	69	GLU	-1	-0.904	-0.817	37.647	0.080	0.080	0.000	0.000	0.000	0.000
100	A	70	HIS	0	0.015	-0.131	39.182	-0.004	-0.004	0.000	0.000	0.000	0.000
101	A	70	HIS	0	-0.098	0.069	40.616	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	71	LEU	0	-0.013	-0.118	40.528	-0.004	-0.004	0.000	0.000	0.000	0.000
103	A	71	LEU	0	-0.053	0.125	37.701	0.000	0.000	0.000	0.000	0.000	0.000
104	A	72	GLY	0	0.019	-0.084	41.826	-0.003	-0.003	0.000	0.000	0.000	0.000
105	A	73	ASP	0	0.033	-0.050	41.681	0.004	0.004	0.000	0.000	0.000	0.000
106	A	73	ASP	-1	-0.923	-0.809	44.334	0.053	0.053	0.000	0.000	0.000	0.000
107	A	74	GLY	0	0.015	-0.095	40.846	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	75	ILE	0	0.052	-0.019	36.832	0.001	0.001	0.000	0.000	0.000	0.000
109	A	75	ILE	0	-0.081	0.109	35.278	0.000	0.000	0.000	0.000	0.000	0.000
110	A	76	ASN	0	0.042	-0.064	35.092	-0.004	-0.004	0.000	0.000	0.000	0.000
111	A	76	ASN	0	-0.124	0.032	32.743	-0.003	-0.003	0.000	0.000	0.000	0.000
112	A	77	GLU	0	0.150	-0.063	31.211	0.002	0.002	0.000	0.000	0.000	0.000
113	A	77	GLU	-1	-0.863	-0.821	30.336	0.117	0.117	0.000	0.000	0.000	0.000
114	A	78	ASP	0	0.078	-0.099	29.029	-0.010	-0.010	0.000	0.000	0.000	0.000
115	A	78	ASP	-1	-0.914	-0.794	28.157	0.125	0.125	0.000	0.000	0.000	0.000
116	A	79	GLU	0	0.060	-0.109	28.694	0.003	0.003	0.000	0.000	0.000	0.000
117	A	79	GLU	-1	-0.921	-0.818	28.412	0.127	0.127	0.000	0.000	0.000	0.000
118	A	80	THR	0	0.024	-0.093	25.319	0.009	0.009	0.000	0.000	0.000	0.000
119	A	80	THR	0	-0.086	0.059	23.742	-0.004	-0.004	0.000	0.000	0.000	0.000
120	A	81	VAL	0	0.108	-0.087	22.091	-0.006	-0.006	0.000	0.000	0.000	0.000
121	A	81	VAL	0	-0.103	0.104	20.120	0.003	0.003	0.000	0.000	0.000	0.000
122	A	82	ARG	0	0.126	-0.088	20.263	0.023	0.023	0.000	0.000	0.000	0.000
123	A	82	ARG	1	0.752	1.015	20.559	-0.216	-0.216	0.000	0.000	0.000	0.000
124	A	83	THR	0	-0.052	-0.092	16.312	-0.029	-0.029	0.000	0.000	0.000	0.000
125	A	83	THR	0	-0.065	0.029	15.365	0.026	0.026	0.000	0.000	0.000	0.000
126	A	84	THR	0	0.061	-0.079	14.568	0.019	0.019	0.000	0.000	0.000	0.000
127	A	84	THR	0	-0.048	0.061	14.645	-0.022	-0.022	0.000	0.000	0.000	0.000
128	A	85	ASP	0	0.038	-0.116	10.395	-0.100	-0.100	0.000	0.000	0.000	0.000
129	A	85	ASP	-1	-0.913	-0.812	8.244	1.066	1.066	0.000	0.000	0.000	0.000
130	A	86	GLY	0	-0.046	-0.111	8.492	0.070	0.070	0.000	0.000	0.000	0.000
131	A	87	GLY	0	-0.032	-0.014	9.361	-0.058	-0.058	0.000	0.000	0.000	0.000
132	A	88	ILE	0	0.090	-0.004	11.526	-0.117	-0.117	0.000	0.000	0.000	0.000
133	A	88	ILE	0	-0.087	0.117	10.352	0.005	0.005	0.000	0.000	0.000	0.000
134	A	89	THR	0	0.086	-0.084	13.031	0.047	0.047	0.000	0.000	0.000	0.000
135	A	89	THR	0	-0.024	0.101	16.842	-0.017	-0.017	0.000	0.000	0.000	0.000
136	A	90	THR	0	0.004	-0.098	15.286	-0.015	-0.015	0.000	0.000	0.000	0.000
137	A	90	THR	0	-0.082	0.050	13.838	0.033	0.033	0.000	0.000	0.000	0.000
138	A	91	LEU	0	0.092	-0.074	16.386	-0.003	-0.003	0.000	0.000	0.000	0.000
139	A	91	LEU	0	-0.042	0.119	20.146	-0.006	-0.006	0.000	0.000	0.000	0.000
140	A	92	ARG	0	0.095	-0.101	19.586	0.021	0.021	0.000	0.000	0.000	0.000
141	A	92	ARG	1	0.841	1.045	14.086	-0.454	-0.454	0.000	0.000	0.000	0.000
142	A	93	LYS	0	0.095	-0.095	21.382	-0.005	-0.005	0.000	0.000	0.000	0.000
143	A	93	LYS	1	0.690	1.012	25.352	-0.141	-0.141	0.000	0.000	0.000	0.000
144	A	94	VAL	0	0.098	-0.121	25.085	0.002	0.002	0.000	0.000	0.000	0.000
145	A	94	VAL	0	-0.052	0.131	24.977	0.001	0.001	0.000	0.000	0.000	0.000
146	A	95	LEU	0	0.132	-0.078	26.854	-0.005	-0.005	0.000	0.000	0.000	0.000
147	A	95	LEU	0	-0.138	0.095	29.621	0.000	0.000	0.000	0.000	0.000	0.000
148	A	96	HIS	0	0.068	-0.096	30.220	0.002	0.002	0.000	0.000	0.000	0.000
149	A	96	HIS	1	0.714	0.959	29.582	-0.115	-0.115	0.000	0.000	0.000	0.000
150	A	97	VAL	0	0.073	-0.097	32.437	-0.003	-0.003	0.000	0.000	0.000	0.000
151	A	97	VAL	0	-0.082	0.106	32.984	-0.001	-0.001	0.000	0.000	0.000	0.000
152	A	98	THR	0	0.065	-0.053	35.308	0.000	0.000	0.000	0.000	0.000	0.000
153	A	98	THR	0	-0.060	0.042	36.381	0.000	0.000	0.000	0.000	0.000	0.000
154	A	99	ASP	0	0.122	-0.095	37.838	-0.003	-0.003	0.000	0.000	0.000	0.000
155	A	99	ASP	-1	-0.939	-0.804	41.479	0.053	0.053	0.000	0.000	0.000	0.000
156	A	100	THR	0	0.030	-0.117	38.468	0.001	0.001	0.000	0.000	0.000	0.000
157	A	100	THR	0	-0.052	0.062	36.509	-0.002	-0.002	0.000	0.000	0.000	0.000
158	A	101	ASN	0	0.126	-0.038	39.167	0.000	0.000	0.000	0.000	0.000	0.000
159	A	101	ASN	0	-0.147	0.049	43.653	-0.001	-0.001	0.000	0.000	0.000	0.000
160	A	102	LYS	0	0.115	-0.113	42.741	-0.001	-0.001	0.000	0.000	0.000	0.000
161	A	102	LYS	1	0.729	1.016	42.717	-0.057	-0.057	0.000	0.000	0.000	0.000
162	A	103	PHE	0	0.038	-0.099	38.994	-0.002	-0.002	0.000	0.000	0.000	0.000
163	A	103	PHE	0	-0.092	0.091	38.111	0.001	0.001	0.000	0.000	0.000	0.000
164	A	104	ALA	0	0.117	-0.114	38.833	0.004	0.004	0.000	0.000	0.000	0.000
165	A	104	ALA	0	-0.063	0.100	41.009	-0.001	-0.001	0.000	0.000	0.000	0.000
166	A	105	HIS	0	-0.021	-0.084	39.964	0.000	0.000	0.000	0.000	0.000	0.000
167	A	105	HIS	0	-0.074	0.068	42.864	-0.001	-0.001	0.000	0.000	0.000	0.000
168	A	106	TYR	0	0.089	-0.108	38.735	-0.003	-0.003	0.000	0.000	0.000	0.000
169	A	106	TYR	0	-0.058	0.119	37.969	0.001	0.001	0.000	0.000	0.000	0.000
170	A	107	ARG	0	0.143	-0.077	35.540	0.003	0.003	0.000	0.000	0.000	0.000
171	A	107	ARG	1	0.763	1.020	34.024	-0.076	-0.076	0.000	0.000	0.000	0.000
172	A	108	PHE	0	0.046	-0.095	32.785	-0.003	-0.003	0.000	0.000	0.000	0.000
173	A	108	PHE	0	-0.085	0.105	32.085	0.001	0.001	0.000	0.000	0.000	0.000
174	A	109	THR	0	0.004	-0.097	30.502	0.002	0.002	0.000	0.000	0.000	0.000
175	A	109	THR	0	-0.089	0.031	30.525	-0.004	-0.004	0.000	0.000	0.000	0.000
176	A	110	CYS	0	0.195	-0.052	26.784	-0.006	-0.006	0.000	0.000	0.000	0.000
177	A	111	VAL	0	0.038	-0.135	27.729	0.001	0.001	0.000	0.000	0.000	0.000
178	A	111	VAL	0	-0.079	0.105	29.043	-0.002	-0.002	0.000	0.000	0.000	0.000
179	A	112	LEU	0	0.141	-0.081	24.030	0.000	0.000	0.000	0.000	0.000	0.000
180	A	112	LEU	0	-0.131	0.103	20.909	0.003	0.003	0.000	0.000	0.000	0.000
181	A	113	THR	0	-0.015	-0.095	25.503	-0.003	-0.003	0.000	0.000	0.000	0.000
182	A	113	THR	0	-0.010	0.058	28.410	-0.001	-0.001	0.000	0.000	0.000	0.000
183	A	114	THR	0	0.002	-0.070	24.044	0.011	0.011	0.000	0.000	0.000	0.000
184	A	114	THR	0	0.008	0.064	22.138	0.003	0.003	0.000	0.000	0.000	0.000
185	A	115	LEU	0	0.077	-0.081	25.382	-0.008	-0.008	0.000	0.000	0.000	0.000
186	A	115	LEU	0	-0.072	0.105	25.961	0.000	0.000	0.000	0.000	0.000	0.000
187	A	116	ASP	0	0.106	-0.104	24.522	-0.013	-0.013	0.000	0.000	0.000	0.000
188	A	116	ASP	-1	-0.970	-0.824	22.621	0.136	0.136	0.000	0.000	0.000	0.000
189	A	117	GLY	0	-0.037	-0.112	25.925	-0.010	-0.010	0.000	0.000	0.000	0.000
190	A	118	VAL	0	0.078	0.008	26.713	0.013	0.013	0.000	0.000	0.000	0.000
191	A	118	VAL	0	-0.083	0.092	28.670	-0.002	-0.002	0.000	0.000	0.000	0.000
192	A	119	SER	0	-0.023	-0.111	24.589	-0.011	-0.011	0.000	0.000	0.000	0.000
193	A	119	SER	0	-0.004	0.085	24.100	0.007	0.007	0.000	0.000	0.000	0.000
194	A	120	LYS	0	0.092	-0.082	26.090	0.006	0.006	0.000	0.000	0.000	0.000
195	A	120	LYS	1	0.875	1.054	28.853	-0.094	-0.094	0.000	0.000	0.000	0.000
196	A	121	LYS	0	0.053	-0.093	25.382	-0.003	-0.003	0.000	0.000	0.000	0.000
197	A	121	LYS	1	0.719	0.981	21.374	-0.184	-0.184	0.000	0.000	0.000	0.000
198	A	122	ASN	0	0.058	-0.075	26.809	0.002	0.002	0.000	0.000	0.000	0.000
199	A	122	ASN	0	-0.064	0.068	30.477	-0.002	-0.002	0.000	0.000	0.000	0.000
200	A	123	ILE	0	0.040	-0.080	28.646	0.003	0.003	0.000	0.000	0.000	0.000
201	A	123	ILE	0	-0.038	0.110	27.068	0.001	0.001	0.000	0.000	0.000	0.000
202	A	124	TRP	0	0.035	-0.132	30.470	-0.002	-0.002	0.000	0.000	0.000	0.000
203	A	124	TRP	0	-0.001	0.116	32.786	-0.002	-0.002	0.000	0.000	0.000	0.000
204	A	125	LEU	0	-0.064	-0.118	32.438	0.004	0.004	0.000	0.000	0.000	0.000
205	A	125	LEU	0	0.074	0.064	33.577	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:18:GLY)