FMO DATABASE

FMODB ID: 6NVQZ

Calculation Name: 3VUT-A-Xray372

Preferred Name: Dual specificity mitogen-activated protein kinase kinase 4

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 3VUT

Chain ID: A

ChEMBL ID: CHEMBL2897

UniProt ID: P45985

Base Structure: X-ray

Registration Date: 2023-09-19

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	203
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2418157.818811
FMO2-HF: Nuclear repulsion	2334446.537593
FMO2-HF: Total energy	-83711.281219
FMO2-MP2: Total energy	-83950.791326

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:142:GLN)

Summations of interaction energy for fragment #1(A:142:GLN)

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.
-10.772	-5.703	5.44	-3.962	-6.549	-0.013

Interaction energy analysis for fragmet #1(A:142:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.021 / q_NPA : 0.002

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	144	GLN	0	-0.001	-0.001	3.574	-3.415	-0.550	-0.014	-1.406	-1.446	0.000
4	A	145	LEU	0	0.049	0.025	2.194	-2.390	-1.368	1.857	-1.265	-1.615	-0.002
5	A	146	LEU	0	-0.052	-0.028	2.252	-4.186	-3.082	3.598	-1.285	-3.417	-0.011
6	A	147	MET	0	0.041	0.075	4.998	0.089	0.167	-0.001	-0.006	-0.071	0.000
7	A	148	ASP	-1	-0.842	-0.935	7.559	0.517	0.517	0.000	0.000	0.000	0.000
8	A	149	LEU	0	-0.074	-0.037	6.743	0.080	0.080	0.000	0.000	0.000	0.000
9	A	150	ASP	-1	-0.771	-0.897	9.054	-2.403	-2.403	0.000	0.000	0.000	0.000
10	A	151	VAL	0	-0.008	-0.008	11.801	0.201	0.201	0.000	0.000	0.000	0.000
11	A	152	VAL	0	-0.049	-0.013	13.171	0.094	0.094	0.000	0.000	0.000	0.000
12	A	153	MET	0	-0.036	-0.006	12.993	0.005	0.005	0.000	0.000	0.000	0.000
13	A	154	ARG	0	0.042	0.017	13.307	-0.067	-0.067	0.000	0.000	0.000	0.000
14	A	155	SER	0	0.010	0.017	18.050	0.040	0.040	0.000	0.000	0.000	0.000
15	A	156	SER	0	0.008	0.013	19.306	0.021	0.021	0.000	0.000	0.000	0.000
16	A	157	ASH	0	-0.130	-0.102	22.113	-0.010	-0.010	0.000	0.000	0.000	0.000
17	A	158	CYS	0	0.063	0.047	23.386	-0.014	-0.014	0.000	0.000	0.000	0.000
18	A	159	PRO	0	0.000	0.011	24.288	0.003	0.003	0.000	0.000	0.000	0.000
19	A	160	TYR	0	-0.010	-0.010	15.405	-0.028	-0.028	0.000	0.000	0.000	0.000
20	A	161	ILE	0	-0.002	0.016	17.340	0.047	0.047	0.000	0.000	0.000	0.000
21	A	162	VAL	0	-0.034	-0.023	18.327	-0.061	-0.061	0.000	0.000	0.000	0.000
22	A	163	GLN	0	-0.083	-0.040	10.866	0.011	0.011	0.000	0.000	0.000	0.000
23	A	164	PHE	0	-0.039	-0.064	12.089	0.056	0.056	0.000	0.000	0.000	0.000
24	A	177	CYS	0	-0.013	-0.017	12.081	-0.031	-0.031	0.000	0.000	0.000	0.000
25	A	178	MET	0	-0.006	-0.014	13.920	0.096	0.096	0.000	0.000	0.000	0.000
26	A	179	GLU	-1	-0.780	-0.847	17.664	-0.412	-0.412	0.000	0.000	0.000	0.000
27	A	180	LEU	0	-0.030	-0.027	20.739	-0.029	-0.029	0.000	0.000	0.000	0.000
28	A	181	MET	0	-0.018	0.021	23.624	0.011	0.011	0.000	0.000	0.000	0.000
29	A	182	SER	0	0.021	0.009	26.582	0.011	0.011	0.000	0.000	0.000	0.000
30	A	183	THR	0	-0.012	-0.019	28.404	0.006	0.006	0.000	0.000	0.000	0.000
31	A	184	SER	0	0.013	0.017	26.284	0.003	0.003	0.000	0.000	0.000	0.000
32	A	185	PHE	0	0.064	-0.005	28.166	0.021	0.021	0.000	0.000	0.000	0.000
33	A	186	ASP	-1	-0.883	-0.915	29.143	-0.272	-0.272	0.000	0.000	0.000	0.000
34	A	187	LYS	1	0.950	0.964	28.812	0.270	0.270	0.000	0.000	0.000	0.000
35	A	188	PHE	0	-0.010	0.007	32.796	0.013	0.013	0.000	0.000	0.000	0.000
36	A	189	TYR	0	-0.059	-0.075	32.521	0.014	0.014	0.000	0.000	0.000	0.000
37	A	190	LYS	1	0.824	0.903	31.727	0.268	0.268	0.000	0.000	0.000	0.000
38	A	191	TYR	0	-0.057	-0.017	37.101	0.008	0.008	0.000	0.000	0.000	0.000
39	A	192	VAL	0	0.056	0.038	38.944	0.009	0.009	0.000	0.000	0.000	0.000
40	A	193	TYR	0	0.010	-0.032	39.118	-0.005	-0.005	0.000	0.000	0.000	0.000
41	A	194	SER	0	-0.122	-0.054	41.356	0.009	0.009	0.000	0.000	0.000	0.000
42	A	195	VAL	0	-0.037	-0.036	43.267	0.005	0.005	0.000	0.000	0.000	0.000
43	A	196	LEU	0	-0.068	-0.035	43.072	0.008	0.008	0.000	0.000	0.000	0.000
44	A	197	ASP	-1	-0.871	-0.926	45.054	-0.129	-0.129	0.000	0.000	0.000	0.000
45	A	198	ASP	-1	-0.867	-0.937	43.639	-0.140	-0.140	0.000	0.000	0.000	0.000
46	A	199	VAL	0	-0.001	0.036	43.856	-0.006	-0.006	0.000	0.000	0.000	0.000
47	A	200	ILE	0	-0.074	-0.045	37.045	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	201	PRO	0	0.025	0.018	41.196	-0.003	-0.003	0.000	0.000	0.000	0.000
49	A	202	GLU	-1	-0.760	-0.864	40.751	-0.171	-0.171	0.000	0.000	0.000	0.000
50	A	203	GLU	-1	-0.909	-0.966	40.279	-0.149	-0.149	0.000	0.000	0.000	0.000
51	A	204	ILE	0	-0.026	-0.010	36.805	-0.008	-0.008	0.000	0.000	0.000	0.000
52	A	205	LEU	0	0.028	0.012	36.345	-0.018	-0.018	0.000	0.000	0.000	0.000
53	A	206	GLY	0	0.033	0.026	35.635	-0.017	-0.017	0.000	0.000	0.000	0.000
54	A	207	LYS	1	0.817	0.897	34.781	0.171	0.171	0.000	0.000	0.000	0.000
55	A	208	ILE	0	0.028	0.023	30.724	-0.020	-0.020	0.000	0.000	0.000	0.000
56	A	209	THR	0	-0.024	-0.010	30.823	-0.028	-0.028	0.000	0.000	0.000	0.000
57	A	210	LEU	0	-0.018	0.001	31.221	-0.021	-0.021	0.000	0.000	0.000	0.000
58	A	211	ALA	0	-0.026	-0.018	28.573	-0.017	-0.017	0.000	0.000	0.000	0.000
59	A	212	THR	0	0.013	-0.023	26.538	-0.031	-0.031	0.000	0.000	0.000	0.000
60	A	213	VAL	0	0.014	0.009	26.230	-0.037	-0.037	0.000	0.000	0.000	0.000
61	A	214	LYS	1	0.928	0.972	27.012	0.264	0.264	0.000	0.000	0.000	0.000
62	A	215	ALA	0	0.018	0.019	23.009	-0.022	-0.022	0.000	0.000	0.000	0.000
63	A	216	LEU	0	0.000	0.002	21.886	-0.054	-0.054	0.000	0.000	0.000	0.000
64	A	217	ASN	0	0.011	-0.009	22.406	-0.047	-0.047	0.000	0.000	0.000	0.000
65	A	218	HIS	1	0.838	0.923	20.280	0.498	0.498	0.000	0.000	0.000	0.000
66	A	219	LEU	0	0.010	0.003	16.137	-0.025	-0.025	0.000	0.000	0.000	0.000
67	A	220	LYS	1	0.890	0.955	18.336	0.462	0.462	0.000	0.000	0.000	0.000
68	A	221	GLU	-1	-0.846	-0.924	20.947	-0.432	-0.432	0.000	0.000	0.000	0.000
69	A	222	ASN	0	-0.043	-0.021	19.594	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	223	LEU	0	0.035	0.029	14.775	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	224	LYS	1	0.798	0.897	17.190	0.517	0.517	0.000	0.000	0.000	0.000
72	A	225	ILE	0	0.021	0.011	13.681	-0.034	-0.034	0.000	0.000	0.000	0.000
73	A	226	ILE	0	-0.024	-0.014	17.230	0.060	0.060	0.000	0.000	0.000	0.000
74	A	227	HIS	1	0.789	0.902	16.821	0.748	0.748	0.000	0.000	0.000	0.000
75	A	228	ARG	1	0.796	0.887	15.562	0.905	0.905	0.000	0.000	0.000	0.000
76	A	229	ASP	-1	-0.752	-0.867	18.442	-0.571	-0.571	0.000	0.000	0.000	0.000
77	A	230	ILE	0	-0.045	-0.007	21.792	-0.025	-0.025	0.000	0.000	0.000	0.000
78	A	231	LYS	1	0.971	0.976	23.972	0.491	0.491	0.000	0.000	0.000	0.000
79	A	232	PRO	0	0.088	0.051	26.594	-0.023	-0.023	0.000	0.000	0.000	0.000
80	A	233	SER	0	-0.036	-0.023	25.022	0.013	0.013	0.000	0.000	0.000	0.000
81	A	234	ASN	0	-0.085	-0.056	22.163	0.000	0.000	0.000	0.000	0.000	0.000
82	A	235	ILE	0	0.001	0.009	23.570	-0.031	-0.031	0.000	0.000	0.000	0.000
83	A	236	LEU	0	0.000	-0.006	22.472	0.025	0.025	0.000	0.000	0.000	0.000
84	A	237	LEU	0	0.033	0.027	26.867	0.004	0.004	0.000	0.000	0.000	0.000
85	A	238	ASP	-1	-0.733	-0.899	28.315	-0.248	-0.248	0.000	0.000	0.000	0.000
86	A	239	ARG	1	0.879	0.913	30.732	0.136	0.136	0.000	0.000	0.000	0.000
87	A	240	SER	0	-0.026	-0.003	31.191	0.017	0.017	0.000	0.000	0.000	0.000
88	A	241	GLY	0	0.017	0.018	32.883	0.006	0.006	0.000	0.000	0.000	0.000
89	A	242	ASN	0	-0.081	-0.039	27.691	0.006	0.006	0.000	0.000	0.000	0.000
90	A	243	ILE	0	-0.008	-0.006	28.404	-0.021	-0.021	0.000	0.000	0.000	0.000
91	A	244	LYS	1	0.765	0.871	23.657	0.318	0.318	0.000	0.000	0.000	0.000
92	A	245	LEU	0	-0.042	-0.029	20.846	0.004	0.004	0.000	0.000	0.000	0.000
93	A	246	CYS	0	-0.033	0.003	20.799	-0.032	-0.032	0.000	0.000	0.000	0.000
94	A	247	ASP	-1	-0.801	-0.922	15.776	-0.982	-0.982	0.000	0.000	0.000	0.000
95	A	248	PHE	0	0.012	0.009	15.042	0.024	0.024	0.000	0.000	0.000	0.000
96	A	249	GLY	0	0.079	0.055	12.834	-0.173	-0.173	0.000	0.000	0.000	0.000
97	A	250	ILE	0	-0.003	0.010	6.151	-0.084	-0.084	0.000	0.000	0.000	0.000
98	A	251	SER	0	-0.066	-0.043	9.539	0.000	0.000	0.000	0.000	0.000	0.000
99	A	252	GLY	0	-0.062	-0.024	8.786	0.229	0.229	0.000	0.000	0.000	0.000
100	A	285	ASP	-1	-0.806	-0.902	23.411	-0.487	-0.487	0.000	0.000	0.000	0.000
101	A	286	VAL	0	0.024	-0.011	23.772	0.009	0.009	0.000	0.000	0.000	0.000
102	A	287	ARG	1	0.831	0.901	24.663	0.366	0.366	0.000	0.000	0.000	0.000
103	A	288	SER	0	-0.009	0.010	24.386	0.042	0.042	0.000	0.000	0.000	0.000
104	A	289	ASP	-1	-0.766	-0.884	22.164	-0.594	-0.594	0.000	0.000	0.000	0.000
105	A	290	VAL	0	-0.054	-0.015	25.652	0.018	0.018	0.000	0.000	0.000	0.000
106	A	291	TRP	0	0.039	0.027	29.052	0.022	0.022	0.000	0.000	0.000	0.000
107	A	292	SER	0	0.008	0.005	26.043	0.026	0.026	0.000	0.000	0.000	0.000
108	A	293	LEU	0	-0.007	0.011	28.028	0.008	0.008	0.000	0.000	0.000	0.000
109	A	294	GLY	0	0.036	0.009	29.594	0.018	0.018	0.000	0.000	0.000	0.000
110	A	295	ILE	0	-0.018	-0.011	31.169	0.017	0.017	0.000	0.000	0.000	0.000
111	A	296	THR	0	-0.023	-0.029	28.894	0.005	0.005	0.000	0.000	0.000	0.000
112	A	297	LEU	0	-0.009	-0.018	31.426	0.011	0.011	0.000	0.000	0.000	0.000
113	A	298	TYR	0	0.018	0.014	34.330	0.013	0.013	0.000	0.000	0.000	0.000
114	A	299	GLU	-1	-0.846	-0.921	31.584	-0.285	-0.285	0.000	0.000	0.000	0.000
115	A	300	LEU	0	-0.041	-0.021	31.849	0.008	0.008	0.000	0.000	0.000	0.000
116	A	301	ALA	0	0.008	0.012	36.147	0.011	0.011	0.000	0.000	0.000	0.000
117	A	302	THR	0	-0.001	0.001	38.965	0.014	0.014	0.000	0.000	0.000	0.000
118	A	303	GLY	0	0.060	0.061	38.650	-0.008	-0.008	0.000	0.000	0.000	0.000
119	A	304	ARG	1	0.839	0.911	37.190	0.196	0.196	0.000	0.000	0.000	0.000
120	A	305	PHE	0	0.000	-0.003	31.230	0.001	0.001	0.000	0.000	0.000	0.000
121	A	306	PRO	0	0.027	0.008	35.010	0.009	0.009	0.000	0.000	0.000	0.000
122	A	307	TYR	0	-0.017	-0.006	36.368	0.012	0.012	0.000	0.000	0.000	0.000
123	A	308	PRO	0	-0.033	0.000	36.771	-0.010	-0.010	0.000	0.000	0.000	0.000
124	A	309	LYS	1	0.840	0.915	39.049	0.150	0.150	0.000	0.000	0.000	0.000
125	A	310	TRP	0	0.106	0.038	39.148	0.002	0.002	0.000	0.000	0.000	0.000
126	A	311	ASN	0	0.072	0.030	39.058	-0.010	-0.010	0.000	0.000	0.000	0.000
127	A	312	SER	0	-0.020	0.010	36.575	-0.002	-0.002	0.000	0.000	0.000	0.000
128	A	313	VAL	0	0.072	0.028	30.758	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	314	PHE	0	0.009	0.007	33.594	-0.010	-0.010	0.000	0.000	0.000	0.000
130	A	315	ASP	-1	-0.882	-0.945	34.573	-0.174	-0.174	0.000	0.000	0.000	0.000
131	A	316	GLN	0	-0.037	-0.045	35.063	0.000	0.000	0.000	0.000	0.000	0.000
132	A	317	LEU	0	-0.009	0.011	29.846	-0.009	-0.009	0.000	0.000	0.000	0.000
133	A	318	THR	0	-0.021	-0.013	33.855	-0.004	-0.004	0.000	0.000	0.000	0.000
134	A	319	GLN	0	-0.076	-0.043	36.201	-0.005	-0.005	0.000	0.000	0.000	0.000
135	A	320	VAL	0	0.017	0.020	33.099	0.004	0.004	0.000	0.000	0.000	0.000
136	A	321	VAL	0	-0.064	-0.029	33.499	-0.005	-0.005	0.000	0.000	0.000	0.000
137	A	322	LYS	1	0.923	0.932	36.722	0.180	0.180	0.000	0.000	0.000	0.000
138	A	323	GLY	0	0.016	0.037	40.029	0.011	0.011	0.000	0.000	0.000	0.000
139	A	324	ASP	-1	-0.883	-0.932	40.412	-0.173	-0.173	0.000	0.000	0.000	0.000
140	A	325	PRO	0	-0.013	-0.007	38.718	-0.007	-0.007	0.000	0.000	0.000	0.000
141	A	326	PRO	0	0.020	0.009	37.613	0.009	0.009	0.000	0.000	0.000	0.000
142	A	327	GLN	0	-0.017	-0.013	40.782	0.004	0.004	0.000	0.000	0.000	0.000
143	A	328	LEU	0	0.065	0.046	40.123	0.005	0.005	0.000	0.000	0.000	0.000
144	A	329	SER	0	-0.073	-0.034	42.589	0.009	0.009	0.000	0.000	0.000	0.000
145	A	330	ASN	0	-0.033	-0.008	45.651	0.009	0.009	0.000	0.000	0.000	0.000
146	A	331	SER	0	-0.013	-0.007	47.397	0.008	0.008	0.000	0.000	0.000	0.000
147	A	332	GLU	-1	-0.949	-0.974	48.642	-0.135	-0.135	0.000	0.000	0.000	0.000
148	A	333	GLU	-1	-0.923	-0.955	48.252	-0.111	-0.111	0.000	0.000	0.000	0.000
149	A	334	ARG	1	0.857	0.931	48.419	0.115	0.115	0.000	0.000	0.000	0.000
150	A	335	GLU	-1	-0.847	-0.929	47.672	-0.124	-0.124	0.000	0.000	0.000	0.000
151	A	336	PHE	0	-0.017	-0.021	43.784	-0.006	-0.006	0.000	0.000	0.000	0.000
152	A	337	SER	0	-0.009	-0.018	44.640	-0.005	-0.005	0.000	0.000	0.000	0.000
153	A	338	PRO	0	0.019	-0.013	45.881	-0.005	-0.005	0.000	0.000	0.000	0.000
154	A	339	SER	0	-0.020	-0.007	43.523	-0.004	-0.004	0.000	0.000	0.000	0.000
155	A	340	PHE	0	0.080	0.049	37.035	-0.011	-0.011	0.000	0.000	0.000	0.000
156	A	341	ILE	0	0.051	0.032	40.517	-0.011	-0.011	0.000	0.000	0.000	0.000
157	A	342	ASN	0	-0.026	-0.024	41.892	-0.009	-0.009	0.000	0.000	0.000	0.000
158	A	343	PHE	0	0.017	0.013	33.397	-0.007	-0.007	0.000	0.000	0.000	0.000
159	A	344	VAL	0	0.032	0.008	36.298	-0.013	-0.013	0.000	0.000	0.000	0.000
160	A	345	ASN	0	0.027	-0.010	36.925	-0.016	-0.016	0.000	0.000	0.000	0.000
161	A	346	LEU	0	-0.037	-0.001	37.233	-0.003	-0.003	0.000	0.000	0.000	0.000
162	A	347	CYS	0	-0.080	-0.030	32.930	-0.013	-0.013	0.000	0.000	0.000	0.000
163	A	348	LEU	0	-0.013	0.003	33.747	-0.016	-0.016	0.000	0.000	0.000	0.000
164	A	349	THR	0	0.001	-0.005	35.666	0.016	0.016	0.000	0.000	0.000	0.000
165	A	350	LYN	0	0.033	0.012	35.064	-0.018	-0.018	0.000	0.000	0.000	0.000
166	A	351	ASP	-1	-0.889	-0.941	35.198	-0.219	-0.219	0.000	0.000	0.000	0.000
167	A	352	GLU	-1	-0.736	-0.852	31.096	-0.342	-0.342	0.000	0.000	0.000	0.000
168	A	353	SER	0	-0.132	-0.073	32.879	0.020	0.020	0.000	0.000	0.000	0.000
169	A	354	LYS	1	0.883	0.935	34.378	0.230	0.230	0.000	0.000	0.000	0.000
170	A	355	ARG	1	0.858	0.938	29.702	0.323	0.323	0.000	0.000	0.000	0.000
171	A	356	PRO	0	0.012	0.015	33.159	-0.011	-0.011	0.000	0.000	0.000	0.000
172	A	357	LYS	1	0.879	0.921	27.116	0.363	0.363	0.000	0.000	0.000	0.000
173	A	358	TYR	0	0.075	0.015	24.388	0.033	0.033	0.000	0.000	0.000	0.000
174	A	359	LYS	1	0.801	0.889	29.991	0.270	0.270	0.000	0.000	0.000	0.000
175	A	360	GLU	-1	-0.781	-0.875	32.309	-0.233	-0.233	0.000	0.000	0.000	0.000
176	A	361	LEU	0	0.002	0.000	31.066	0.010	0.010	0.000	0.000	0.000	0.000
177	A	362	LEU	0	-0.002	-0.004	29.977	0.006	0.006	0.000	0.000	0.000	0.000
178	A	363	LYS	1	0.913	0.954	33.595	0.209	0.209	0.000	0.000	0.000	0.000
179	A	364	HIS	0	-0.021	0.008	36.867	0.011	0.011	0.000	0.000	0.000	0.000
180	A	365	PRO	0	0.010	-0.013	38.808	-0.001	-0.001	0.000	0.000	0.000	0.000
181	A	366	PHE	0	0.024	0.016	37.005	0.004	0.004	0.000	0.000	0.000	0.000
182	A	367	ILE	0	-0.039	-0.004	33.979	0.000	0.000	0.000	0.000	0.000	0.000
183	A	368	LEU	0	0.039	0.024	37.212	0.003	0.003	0.000	0.000	0.000	0.000
184	A	369	MET	0	-0.029	0.002	39.021	0.012	0.012	0.000	0.000	0.000	0.000
185	A	370	TYR	0	0.013	-0.027	37.910	0.007	0.007	0.000	0.000	0.000	0.000
186	A	371	GLU	-1	-0.943	-0.981	33.820	-0.232	-0.232	0.000	0.000	0.000	0.000
187	A	372	GLU	-1	-0.912	-0.957	36.445	-0.164	-0.164	0.000	0.000	0.000	0.000
188	A	373	ARG	1	0.807	0.914	38.544	0.166	0.166	0.000	0.000	0.000	0.000
189	A	374	ALA	0	-0.052	-0.008	39.556	-0.006	-0.006	0.000	0.000	0.000	0.000
190	A	375	VAL	0	0.029	0.018	40.626	0.008	0.008	0.000	0.000	0.000	0.000
191	A	376	GLU	-1	-0.826	-0.914	40.171	-0.148	-0.148	0.000	0.000	0.000	0.000
192	A	377	VAL	0	-0.021	-0.015	35.322	-0.006	-0.006	0.000	0.000	0.000	0.000
193	A	378	ALA	0	0.053	0.032	36.350	-0.003	-0.003	0.000	0.000	0.000	0.000
194	A	379	CYS	0	-0.035	-0.012	37.339	0.003	0.003	0.000	0.000	0.000	0.000
195	A	380	TYR	0	0.065	0.025	38.361	0.000	0.000	0.000	0.000	0.000	0.000
196	A	381	VAL	0	0.015	-0.004	33.934	0.000	0.000	0.000	0.000	0.000	0.000
197	A	382	CYS	0	-0.075	-0.036	37.361	0.000	0.000	0.000	0.000	0.000	0.000
198	A	383	LYS	1	0.967	0.992	38.635	0.111	0.111	0.000	0.000	0.000	0.000
199	A	384	ILE	0	0.008	0.010	38.484	0.006	0.006	0.000	0.000	0.000	0.000
200	A	385	LEU	0	0.011	0.000	33.763	-0.004	-0.004	0.000	0.000	0.000	0.000
201	A	386	ASP	-1	-0.837	-0.928	37.818	-0.126	-0.126	0.000	0.000	0.000	0.000
202	A	387	GLN	0	-0.095	-0.042	40.436	0.010	0.010	0.000	0.000	0.000	0.000
203	A	388	MET	0	-0.060	0.011	34.586	-0.002	-0.002	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:142:GLN)