FMO DATABASE

FMODB ID: LR5Q9

Calculation Name: 2DT5-A-Xray549

Preferred Name:

Target Type:

Ligand Name: nicotinamide-adenine-dinucleotide

Ligand 3-letter code: NAD

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2DT5

Chain ID: A

ChEMBL ID:

UniProt ID: Q5SHS3

Base Structure: X-ray

Registration Date: 2025-10-11

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	210
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2136174.361729
FMO2-HF: Nuclear repulsion	2056750.756933
FMO2-HF: Total energy	-79423.604796
FMO2-MP2: Total energy	-79659.000118

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:2:LYS)

Summations of interaction energy for fragment #1(A:2: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.
-35.498	-33.471	-0.001	-0.559	-1.467	-0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.843 / q_NPA : 1.907

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	4	PRO	0	-0.038	-0.010	3.759	-1.146	0.639	0.001	-0.542	-1.244	-0.001
4	A	5	GLU	-1	-0.831	-0.913	4.710	-46.417	-46.287	-0.001	-0.011	-0.118	0.000
50	A	51	TYR	0	-0.089	-0.030	4.744	-6.121	-6.009	-0.001	-0.006	-0.105	0.000
5	A	6	ALA	0	0.041	0.016	7.819	5.734	5.734	0.000	0.000	0.000	0.000
6	A	7	ALA	0	-0.042	-0.021	7.603	4.037	4.037	0.000	0.000	0.000	0.000
7	A	8	ILE	0	0.022	0.005	7.888	3.855	3.855	0.000	0.000	0.000	0.000
8	A	9	SER	0	0.021	0.001	10.583	4.827	4.827	0.000	0.000	0.000	0.000
9	A	10	ARG	1	0.872	0.937	9.767	50.709	50.709	0.000	0.000	0.000	0.000
10	A	11	LEU	0	-0.014	0.001	11.696	2.895	2.895	0.000	0.000	0.000	0.000
11	A	12	ILE	0	0.022	0.009	14.383	2.669	2.669	0.000	0.000	0.000	0.000
12	A	13	THR	0	-0.010	-0.007	16.807	2.542	2.542	0.000	0.000	0.000	0.000
13	A	14	TYR	0	-0.039	-0.062	14.557	2.080	2.080	0.000	0.000	0.000	0.000
14	A	15	LEU	0	-0.036	-0.008	18.212	1.434	1.434	0.000	0.000	0.000	0.000
15	A	16	ARG	1	0.869	0.906	20.424	29.282	29.282	0.000	0.000	0.000	0.000
16	A	17	ILE	0	0.017	0.020	21.174	1.184	1.184	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.035	-0.022	21.019	1.067	1.067	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-0.826	-0.903	24.152	-25.217	-25.217	0.000	0.000	0.000	0.000
19	A	20	GLU	-1	-0.892	-0.943	26.696	-20.117	-20.117	0.000	0.000	0.000	0.000
20	A	21	LEU	0	-0.047	-0.024	25.779	0.802	0.802	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.865	-0.918	28.747	-21.035	-21.035	0.000	0.000	0.000	0.000
22	A	23	ALA	0	-0.002	0.005	30.525	0.751	0.751	0.000	0.000	0.000	0.000
23	A	24	GLN	0	-0.056	-0.023	30.918	0.737	0.737	0.000	0.000	0.000	0.000
24	A	25	GLY	0	0.007	0.013	33.827	0.427	0.427	0.000	0.000	0.000	0.000
25	A	26	VAL	0	-0.056	-0.024	30.081	0.238	0.238	0.000	0.000	0.000	0.000
26	A	27	HIS	0	0.021	0.005	30.578	-0.624	-0.624	0.000	0.000	0.000	0.000
27	A	28	ARG	1	0.915	0.945	28.759	18.985	18.985	0.000	0.000	0.000	0.000
28	A	29	THR	0	0.048	0.020	24.538	0.149	0.149	0.000	0.000	0.000	0.000
29	A	30	SER	0	0.043	0.022	25.834	-0.875	-0.875	0.000	0.000	0.000	0.000
30	A	31	SER	0	0.022	-0.007	21.050	-0.299	-0.299	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.950	-0.974	22.412	-21.829	-21.829	0.000	0.000	0.000	0.000
32	A	33	GLN	0	0.068	0.063	25.133	-0.375	-0.375	0.000	0.000	0.000	0.000
33	A	34	LEU	0	0.017	-0.002	20.747	-0.211	-0.211	0.000	0.000	0.000	0.000
34	A	35	GLY	0	0.016	0.007	21.102	-0.652	-0.652	0.000	0.000	0.000	0.000
35	A	36	GLY	0	0.012	0.004	22.090	-0.115	-0.115	0.000	0.000	0.000	0.000
36	A	37	LEU	0	-0.030	-0.022	24.689	0.341	0.341	0.000	0.000	0.000	0.000
37	A	38	ALA	0	-0.030	-0.023	19.383	-0.167	-0.167	0.000	0.000	0.000	0.000
38	A	39	GLN	0	-0.022	0.006	20.707	-0.930	-0.930	0.000	0.000	0.000	0.000
39	A	40	VAL	0	0.006	0.017	16.456	-1.046	-1.046	0.000	0.000	0.000	0.000
40	A	41	THR	0	0.066	0.025	18.020	0.697	0.697	0.000	0.000	0.000	0.000
41	A	42	ALA	0	0.054	0.013	18.978	-1.131	-1.131	0.000	0.000	0.000	0.000
42	A	43	PHE	0	-0.073	-0.044	14.595	-0.295	-0.295	0.000	0.000	0.000	0.000
43	A	44	GLN	0	-0.003	-0.005	11.446	-1.222	-1.222	0.000	0.000	0.000	0.000
44	A	45	VAL	0	0.050	0.033	14.780	-1.977	-1.977	0.000	0.000	0.000	0.000
45	A	46	ARG	1	0.909	0.949	16.264	27.103	27.103	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.937	0.997	9.869	44.767	44.767	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.751	-0.841	11.217	-48.163	-48.163	0.000	0.000	0.000	0.000
48	A	49	LEU	0	-0.008	-0.003	12.190	-2.079	-2.079	0.000	0.000	0.000	0.000
49	A	50	SER	0	-0.027	-0.035	14.046	0.520	0.520	0.000	0.000	0.000	0.000
51	A	52	PHE	0	-0.016	-0.027	8.453	-4.362	-4.362	0.000	0.000	0.000	0.000
52	A	53	GLY	0	0.010	0.020	12.114	1.272	1.272	0.000	0.000	0.000	0.000
53	A	54	SER	0	-0.022	-0.025	15.090	1.706	1.706	0.000	0.000	0.000	0.000
54	A	55	TYR	0	-0.013	-0.017	15.038	-0.267	-0.267	0.000	0.000	0.000	0.000
55	A	56	GLY	0	-0.003	-0.002	19.161	1.064	1.064	0.000	0.000	0.000	0.000
56	A	57	THR	0	0.014	0.011	22.061	0.464	0.464	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.930	0.949	22.808	24.746	24.746	0.000	0.000	0.000	0.000
58	A	59	GLY	0	0.017	0.012	26.528	0.528	0.528	0.000	0.000	0.000	0.000
59	A	60	VAL	0	-0.001	0.005	29.023	0.476	0.476	0.000	0.000	0.000	0.000
60	A	61	GLY	0	0.000	0.005	26.323	0.248	0.248	0.000	0.000	0.000	0.000
61	A	62	TYR	0	-0.021	-0.016	18.976	0.152	0.152	0.000	0.000	0.000	0.000
62	A	63	THR	0	0.021	0.000	24.969	1.054	1.054	0.000	0.000	0.000	0.000
63	A	64	VAL	0	0.024	0.026	25.677	-0.935	-0.935	0.000	0.000	0.000	0.000
64	A	65	PRO	0	0.041	0.023	25.450	-0.909	-0.909	0.000	0.000	0.000	0.000
65	A	66	VAL	0	-0.063	-0.028	24.198	-0.380	-0.380	0.000	0.000	0.000	0.000
66	A	67	LEU	0	0.050	0.016	19.020	-0.901	-0.901	0.000	0.000	0.000	0.000
67	A	68	LYS	1	0.867	0.922	20.783	21.315	21.315	0.000	0.000	0.000	0.000
68	A	69	ARG	1	0.930	0.965	21.694	24.538	24.538	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.864	-0.916	18.722	-30.761	-30.761	0.000	0.000	0.000	0.000
70	A	71	LEU	0	0.014	0.001	15.630	-1.864	-1.864	0.000	0.000	0.000	0.000
71	A	72	ARG	1	0.973	0.979	16.980	24.854	24.854	0.000	0.000	0.000	0.000
72	A	73	HIS	0	-0.041	-0.008	16.987	0.678	0.678	0.000	0.000	0.000	0.000
73	A	74	ILE	0	-0.029	-0.021	12.542	-0.941	-0.941	0.000	0.000	0.000	0.000
74	A	75	LEU	0	-0.025	-0.003	12.385	-3.265	-3.265	0.000	0.000	0.000	0.000
75	A	76	GLY	0	0.003	0.010	14.330	0.254	0.254	0.000	0.000	0.000	0.000
76	A	77	LEU	0	0.028	0.016	16.127	1.543	1.543	0.000	0.000	0.000	0.000
77	A	78	ASN	0	-0.061	-0.030	18.971	0.751	0.751	0.000	0.000	0.000	0.000
78	A	79	ARG	1	0.903	0.967	16.820	32.979	32.979	0.000	0.000	0.000	0.000
79	A	80	LYS	1	0.882	0.951	20.620	22.821	22.821	0.000	0.000	0.000	0.000
80	A	81	TRP	0	-0.019	-0.018	14.044	-0.107	-0.107	0.000	0.000	0.000	0.000
81	A	82	GLY	0	0.024	0.006	19.770	0.857	0.857	0.000	0.000	0.000	0.000
82	A	83	LEU	0	-0.019	-0.016	18.084	-1.518	-1.518	0.000	0.000	0.000	0.000
83	A	84	CYS	0	-0.029	-0.002	20.278	1.041	1.041	0.000	0.000	0.000	0.000
84	A	85	ILE	0	0.023	0.025	20.808	-1.221	-1.221	0.000	0.000	0.000	0.000
85	A	86	VAL	0	0.034	0.010	21.507	1.040	1.040	0.000	0.000	0.000	0.000
86	A	87	GLY	0	0.056	0.023	22.755	-0.739	-0.739	0.000	0.000	0.000	0.000
87	A	88	MET	0	-0.021	0.020	25.580	-0.596	-0.596	0.000	0.000	0.000	0.000
88	A	89	GLY	0	0.037	0.013	27.909	0.879	0.879	0.000	0.000	0.000	0.000
89	A	90	ARG	1	0.934	0.957	29.344	19.025	19.025	0.000	0.000	0.000	0.000
90	A	91	LEU	0	0.045	0.031	22.289	0.280	0.280	0.000	0.000	0.000	0.000
91	A	92	GLY	0	0.091	0.045	24.900	-0.308	-0.308	0.000	0.000	0.000	0.000
92	A	93	SER	0	-0.028	-0.034	25.875	0.284	0.284	0.000	0.000	0.000	0.000
93	A	94	ALA	0	0.009	0.000	27.800	0.137	0.137	0.000	0.000	0.000	0.000
94	A	95	LEU	0	-0.022	-0.012	21.476	-0.102	-0.102	0.000	0.000	0.000	0.000
95	A	96	ALA	0	0.018	0.006	25.449	-0.306	-0.306	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.862	-0.910	27.507	-18.251	-18.251	0.000	0.000	0.000	0.000
97	A	98	TYR	0	-0.018	0.008	22.896	0.105	0.105	0.000	0.000	0.000	0.000
98	A	99	PRO	0	-0.023	-0.019	26.487	-0.488	-0.488	0.000	0.000	0.000	0.000
99	A	100	GLY	0	-0.017	-0.007	24.178	0.054	0.054	0.000	0.000	0.000	0.000
100	A	101	PHE	0	-0.023	-0.009	20.773	-1.185	-1.185	0.000	0.000	0.000	0.000
101	A	102	GLY	0	0.008	0.009	22.104	-0.904	-0.904	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.932	-0.970	24.556	-22.723	-22.723	0.000	0.000	0.000	0.000
103	A	104	SER	0	-0.036	-0.031	20.112	0.430	0.430	0.000	0.000	0.000	0.000
104	A	105	PHE	0	-0.021	-0.011	15.850	-0.998	-0.998	0.000	0.000	0.000	0.000
105	A	106	GLU	-1	-0.792	-0.888	21.071	-21.105	-21.105	0.000	0.000	0.000	0.000
106	A	107	LEU	0	-0.010	0.011	23.177	-0.428	-0.428	0.000	0.000	0.000	0.000
107	A	108	ARG	1	0.792	0.894	23.023	24.708	24.708	0.000	0.000	0.000	0.000
108	A	109	GLY	0	0.032	0.012	26.004	0.543	0.543	0.000	0.000	0.000	0.000
109	A	110	PHE	0	0.014	0.004	25.423	-0.970	-0.970	0.000	0.000	0.000	0.000
110	A	111	PHE	0	0.025	0.016	24.463	0.534	0.534	0.000	0.000	0.000	0.000
111	A	112	ASP	-1	-0.778	-0.906	26.831	-20.316	-20.316	0.000	0.000	0.000	0.000
112	A	113	VAL	0	0.002	-0.006	29.084	0.061	0.061	0.000	0.000	0.000	0.000
113	A	114	ASP	-1	-0.814	-0.886	30.866	-16.457	-16.457	0.000	0.000	0.000	0.000
114	A	115	PRO	0	0.018	0.002	33.924	-0.135	-0.135	0.000	0.000	0.000	0.000
115	A	116	GLU	-1	-0.899	-0.940	36.917	-14.519	-14.519	0.000	0.000	0.000	0.000
116	A	117	LYS	1	0.661	0.813	31.671	18.320	18.320	0.000	0.000	0.000	0.000
117	A	118	VAL	0	-0.021	-0.018	32.665	-0.133	-0.133	0.000	0.000	0.000	0.000
118	A	119	GLY	0	0.006	0.012	34.924	0.467	0.467	0.000	0.000	0.000	0.000
119	A	120	ARG	1	0.913	0.968	32.368	17.981	17.981	0.000	0.000	0.000	0.000
120	A	121	PRO	0	0.004	0.000	34.901	-0.506	-0.506	0.000	0.000	0.000	0.000
121	A	122	VAL	0	-0.022	-0.024	30.493	-0.078	-0.078	0.000	0.000	0.000	0.000
122	A	123	ARG	1	0.847	0.899	30.509	18.704	18.704	0.000	0.000	0.000	0.000
123	A	124	GLY	0	0.015	0.010	30.567	-0.579	-0.579	0.000	0.000	0.000	0.000
124	A	125	GLY	0	-0.023	-0.013	31.545	-0.280	-0.280	0.000	0.000	0.000	0.000
125	A	126	VAL	0	-0.015	0.000	32.152	0.445	0.445	0.000	0.000	0.000	0.000
126	A	127	ILE	0	-0.037	-0.003	30.315	-0.679	-0.679	0.000	0.000	0.000	0.000
127	A	128	GLU	-1	-0.806	-0.878	29.855	-18.157	-18.157	0.000	0.000	0.000	0.000
128	A	129	HIS	0	0.075	0.023	30.408	-0.609	-0.609	0.000	0.000	0.000	0.000
129	A	130	VAL	0	-0.020	-0.020	25.130	-0.311	-0.311	0.000	0.000	0.000	0.000
130	A	131	ASP	-1	-0.874	-0.946	26.855	-19.743	-19.743	0.000	0.000	0.000	0.000
131	A	132	LEU	0	-0.040	-0.018	29.239	0.078	0.078	0.000	0.000	0.000	0.000
132	A	133	LEU	0	-0.003	0.014	22.415	-0.274	-0.274	0.000	0.000	0.000	0.000
133	A	134	PRO	0	0.034	0.004	24.958	-0.466	-0.466	0.000	0.000	0.000	0.000
134	A	135	GLN	0	-0.023	-0.009	25.929	-0.016	-0.016	0.000	0.000	0.000	0.000
135	A	136	ARG	1	0.784	0.862	26.467	19.255	19.255	0.000	0.000	0.000	0.000
136	A	137	VAL	0	0.041	0.036	20.114	-0.042	-0.042	0.000	0.000	0.000	0.000
137	A	138	PRO	0	0.024	0.013	22.721	-0.565	-0.565	0.000	0.000	0.000	0.000
138	A	139	GLY	0	-0.039	-0.016	22.823	0.801	0.801	0.000	0.000	0.000	0.000
139	A	140	ARG	1	0.800	0.900	23.490	21.645	21.645	0.000	0.000	0.000	0.000
140	A	141	ILE	0	-0.003	-0.005	19.639	0.091	0.091	0.000	0.000	0.000	0.000
141	A	142	GLU	-1	-0.874	-0.925	16.140	-28.357	-28.357	0.000	0.000	0.000	0.000
142	A	143	ILE	0	0.012	-0.004	13.900	-2.009	-2.009	0.000	0.000	0.000	0.000
143	A	144	ALA	0	0.035	0.014	15.902	2.004	2.004	0.000	0.000	0.000	0.000
144	A	145	LEU	0	-0.031	-0.012	16.412	-1.911	-1.911	0.000	0.000	0.000	0.000
145	A	146	LEU	0	-0.025	-0.004	17.271	1.661	1.661	0.000	0.000	0.000	0.000
146	A	147	THR	0	-0.010	-0.033	19.147	-0.749	-0.749	0.000	0.000	0.000	0.000
147	A	148	VAL	0	-0.029	0.005	21.756	1.276	1.276	0.000	0.000	0.000	0.000
148	A	149	PRO	0	0.001	-0.004	22.909	-0.784	-0.784	0.000	0.000	0.000	0.000
149	A	150	ARG	1	0.934	0.951	21.635	23.000	23.000	0.000	0.000	0.000	0.000
150	A	151	GLU	-1	-0.844	-0.919	22.444	-23.145	-23.145	0.000	0.000	0.000	0.000
151	A	152	ALA	0	-0.004	-0.004	24.442	0.385	0.385	0.000	0.000	0.000	0.000
152	A	153	ALA	0	-0.019	-0.002	19.099	-0.270	-0.270	0.000	0.000	0.000	0.000
153	A	154	GLN	0	0.039	0.007	16.337	-1.559	-1.559	0.000	0.000	0.000	0.000
154	A	155	LYS	1	0.984	1.001	19.417	22.380	22.380	0.000	0.000	0.000	0.000
155	A	156	ALA	0	0.008	-0.010	21.318	0.366	0.366	0.000	0.000	0.000	0.000
156	A	157	ALA	0	0.022	0.014	15.935	-0.152	-0.152	0.000	0.000	0.000	0.000
157	A	158	ASP	-1	-0.844	-0.919	17.879	-28.656	-28.656	0.000	0.000	0.000	0.000
158	A	159	LEU	0	-0.060	-0.033	19.586	0.409	0.409	0.000	0.000	0.000	0.000
159	A	160	LEU	0	0.002	-0.003	17.786	0.372	0.372	0.000	0.000	0.000	0.000
160	A	161	VAL	0	-0.014	-0.012	14.876	-0.271	-0.271	0.000	0.000	0.000	0.000
161	A	162	ALA	0	-0.033	-0.014	17.586	0.197	0.197	0.000	0.000	0.000	0.000
162	A	163	ALA	0	-0.039	-0.005	20.926	0.877	0.877	0.000	0.000	0.000	0.000
163	A	164	GLY	0	0.009	0.002	18.658	0.500	0.500	0.000	0.000	0.000	0.000
164	A	165	ILE	0	-0.080	-0.028	14.675	-0.484	-0.484	0.000	0.000	0.000	0.000
165	A	166	LYS	1	0.923	0.950	12.959	30.901	30.901	0.000	0.000	0.000	0.000
166	A	167	GLY	0	-0.002	0.007	11.202	-3.993	-3.993	0.000	0.000	0.000	0.000
167	A	168	ILE	0	-0.001	0.000	11.541	3.348	3.348	0.000	0.000	0.000	0.000
168	A	169	LEU	0	0.000	0.011	11.977	-2.945	-2.945	0.000	0.000	0.000	0.000
169	A	170	ASN	0	0.007	-0.025	13.558	4.805	4.805	0.000	0.000	0.000	0.000
170	A	171	PHE	0	0.041	0.003	15.340	-0.850	-0.850	0.000	0.000	0.000	0.000
171	A	172	ALA	0	-0.002	0.017	18.263	1.281	1.281	0.000	0.000	0.000	0.000
172	A	173	PRO	0	-0.045	-0.024	17.562	-1.547	-1.547	0.000	0.000	0.000	0.000
173	A	174	VAL	0	-0.036	-0.028	16.384	1.397	1.397	0.000	0.000	0.000	0.000
174	A	175	VAL	0	-0.006	0.000	11.371	-1.853	-1.853	0.000	0.000	0.000	0.000
175	A	176	LEU	0	-0.025	-0.007	12.746	1.953	1.953	0.000	0.000	0.000	0.000
176	A	177	GLU	-1	-0.937	-0.960	12.125	-36.470	-36.470	0.000	0.000	0.000	0.000
177	A	178	VAL	0	0.002	-0.005	10.037	2.193	2.193	0.000	0.000	0.000	0.000
178	A	179	PRO	0	0.008	0.010	11.684	-1.876	-1.876	0.000	0.000	0.000	0.000
179	A	180	LYS	1	0.890	0.931	7.779	42.248	42.248	0.000	0.000	0.000	0.000
180	A	181	GLU	-1	-0.891	-0.945	7.880	-46.388	-46.388	0.000	0.000	0.000	0.000
181	A	182	VAL	0	-0.043	-0.009	10.201	1.221	1.221	0.000	0.000	0.000	0.000
182	A	183	ALA	0	-0.018	-0.005	7.130	-3.559	-3.559	0.000	0.000	0.000	0.000
183	A	184	VAL	0	0.003	-0.015	7.253	5.675	5.675	0.000	0.000	0.000	0.000
184	A	185	GLU	-1	-0.919	-0.945	6.767	-73.453	-73.453	0.000	0.000	0.000	0.000
185	A	186	ASN	0	-0.013	-0.008	9.765	6.760	6.760	0.000	0.000	0.000	0.000
186	A	187	VAL	0	0.017	0.014	12.240	-1.266	-1.266	0.000	0.000	0.000	0.000
187	A	188	ASP	-1	-0.840	-0.916	15.037	-33.804	-33.804	0.000	0.000	0.000	0.000
188	A	189	PHE	0	0.019	0.001	17.480	-0.270	-0.270	0.000	0.000	0.000	0.000
189	A	190	LEU	0	0.004	-0.002	18.748	1.321	1.321	0.000	0.000	0.000	0.000
190	A	191	ALA	0	0.049	0.033	15.948	0.771	0.771	0.000	0.000	0.000	0.000
191	A	192	GLY	0	-0.036	-0.017	18.005	0.304	0.304	0.000	0.000	0.000	0.000
192	A	193	LEU	0	0.017	-0.003	21.048	0.902	0.902	0.000	0.000	0.000	0.000
193	A	194	THR	0	-0.022	-0.017	19.254	1.044	1.044	0.000	0.000	0.000	0.000
194	A	195	ARG	1	0.962	0.982	16.438	33.545	33.545	0.000	0.000	0.000	0.000
195	A	196	LEU	0	0.011	0.009	21.929	0.868	0.868	0.000	0.000	0.000	0.000
196	A	197	SER	0	-0.021	-0.004	24.622	1.086	1.086	0.000	0.000	0.000	0.000
197	A	198	PHE	0	0.031	0.014	22.929	0.636	0.636	0.000	0.000	0.000	0.000
198	A	199	ALA	0	0.041	0.011	24.984	0.704	0.704	0.000	0.000	0.000	0.000
199	A	200	ILE	0	-0.044	-0.029	26.950	0.805	0.805	0.000	0.000	0.000	0.000
200	A	201	LEU	0	-0.029	-0.007	27.524	0.754	0.754	0.000	0.000	0.000	0.000
201	A	202	ASN	0	-0.081	-0.027	26.755	0.761	0.761	0.000	0.000	0.000	0.000
202	A	203	PRO	0	0.027	0.015	28.665	-0.392	-0.392	0.000	0.000	0.000	0.000
203	A	204	LYS	1	0.884	0.929	30.750	17.603	17.603	0.000	0.000	0.000	0.000
204	A	205	TRP	0	0.016	0.014	20.413	0.051	0.051	0.000	0.000	0.000	0.000
205	A	206	ARG	1	0.853	0.896	24.951	21.775	21.775	0.000	0.000	0.000	0.000
206	A	207	GLU	-1	-0.893	-0.938	18.144	-31.010	-31.010	0.000	0.000	0.000	0.000
207	A	208	GLU	-1	-0.793	-0.897	21.648	-23.854	-23.854	0.000	0.000	0.000	0.000
208	A	209	MET	0	-0.126	-0.055	23.550	0.839	0.839	0.000	0.000	0.000	0.000
209	A	210	MET	0	-0.082	-0.040	17.825	0.135	0.135	0.000	0.000	0.000	0.000
210	A	211	GLY	-1	-0.960	-0.952	20.661	-27.332	-27.332	0.000	0.000	0.000	0.000

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