REMARK This is a manually constructed test file for FirstGlance. REMARK The ConSurf result header section was copied from a job on 7mgp. REMARK The ATOM & HETATM lines are from 7mgp, whose Biological Unit 1 has REMARK six copies of the asymmetric unit. The PDB format header section was REMARK minimized as if for an unpublished model, keeping REMARK 350. !! ====== IDENTIFICATION SECTION ====== !js.init ! consurf_version = "3.0"; ! consurf_run_number = "1655943934"; ! consurf_run_date = "2022-6-23"; ! consurf_run_submission_time = "3:25:47"; ! consurf_run_completion_time = "3:33:16"; ! ! consurf_pdb_id = "CONSERVATION_PDB"; ! consurf_chain = "A"; ! consurf_identical_chains = ""; ! consurf_msa_filename = ""; ! consurf_msa_query_seq_name = "CONSERVATION_PDBA"; ! consurf_tree_filename = ""; ! ! consurf_psi_blast_e_value = 0.0001; ! consurf_psi_blast_database = "UNIREF90"; ! consurf_psi_blast_iterations = 1; ! consurf_max_seqs = 150; ! consurf_alignment = "MAFFT"; ! consurf_method = "Bayes"; ! consurf_substitution_model = "LG"; ! ! consurf_seqres_length = 99; ! consurf_atom_seq_length = 93; ! consurf_unique_seqs = 5530; ! consurf_grade_freqs_isd = Array(1,13,3,7,8,10,15,11,10,11); ! consurf_grade_freqs = Array(0,13,3,7,8,11,15,11,10,11); ! ! seq3d_grades_isd = ! ".........1979669818563674879795979391631141465757663639686894685278215711" + ! "4735473689488612511541650." ; ! ! seq3d_grades = ! ".........1979669818563674879795979391631141465757663639686894685278215711" + ! "4735473689488612511541655." ; ! ! !! ====== CONTROL PANEL OPTIONS SECTION ====== !js.init ! pipe_title = "ConSurf View: MODEL chain A." !! pipe_subtitle is from TITLE else COMPND !! ! pipe_subtitle = ! "" ; ! pipe_title_enlarged = false; ! pipe_background_color = "white"; ! !! Specify the custom consurf control panel !! ! pipe_cp1 = "consurf/consurf.htm"; ! !! If you want the frontispiece to be reset every time you enter this !! page, use false. If this is a one-page presentation (no contents) !! and you want to be able to return from QuickViews without resetting !! the view, use true. !! ! frontispiece_conditional_on_return = true; ! !! Open the command input slot/message box to 30% of window height. !! ! pipe_show_commands = true; ! pipe_show_commands_pct = 30; ! !! Don't show the PiPE presentation controls in the lower left frame. !! ! pipe_hide_controls = true; ! !! Hide development viewing mode links at the bottom of the control panel. !! ! pipe_tech_info = false; ! !! pipe_start_spinning = true; // default is PE's Preference setting. !! top.nonStopSpin = true; // default: spinning stops after 3 min. !! !! ====== COLORS SECTION ====== !! !color color_carbon C8C8C8 !color color_sulfur FFC832 ! !! Ten ConSurf color grades follow: !! !color color_grade0 FFFF96 insufficient data yellow !color color_grade1 10C8D1 turquoise variable !color color_grade2 8CFFFF !color color_grade3 D7FFFF !color color_grade4 EAFFFF !color color_grade5 FFFFFF !color color_grade6 FCEDF4 !color color_grade7 FAC9DE !color color_grade8 F07DAB !color color_grade9 A02560 burgundy conserved ! ! !! ====== SCRIPTS SECTION ====== !!---------------------------------------- !! !spt #name=select_and_chain ! select selected and :A ! !!---------------------------------------- !! !spt #name=view01 ! @spt consurf_view_isd ! !!---------------------------------------- !! !spt #name=hide_all ! restrict none ! ssbonds off ! hbonds off ! dots off ! list * delete ! !!---------------------------------------- !! common_spt uses CPK carbon gray (or phosphorus yellow) for backbones. !! !spt #name=common_spt ! @spt hide_all ! select all ! color [xC8C8C8] # rasmol/chime carbon gray ! select nucleic ! color [xFFA500] # phosphorus orange ! select hetero ! color cpk ! select not hetero ! backbone 0.4 ! javascript top.water=0 ! ! ssbonds 0.3 ! set ssbonds backbone ! color ssbonds @color_sulfur ! ! select hetero and not water ! spacefill 0.45 ! wireframe 0.15 ! dots 50 ! ! select protein ! center selected ! !!---------------------------------------- !! !spt #name=consurf_view_isd ! @spt common_spt ! @for $=0, 9 ! @spt select_isd_grade$ ! @spt select_and_chain ! color @color_grade$ ! spacefill ! @endfor ! zoom 115 ! !!---------------------------------------- !! !spt #name=select_isd_grade9 ! ! select ALA4, GLY6, GLU9, ASP21, MET23, ALA25, ALA27, VAL29, GLY48, VAL53 ! select selected or ILE76 ! ! !!---------------------------------------- !! !spt #name=select_isd_grade8 ! ! select THR10, GLY12, ALA19, VAL50, ALA52, SER56, GLY60, VAL75, ARG78, PRO79 ! ! !!---------------------------------------- !! !spt #name=select_isd_grade7 ! ! select LEU5, ILE17, ALA20, ALA22, SER26, GLY40, VAL42, SER59, ALA64, GLY68 ! select selected or THR72 ! ! !!---------------------------------------- !! !spt #name=select_isd_grade6 ! ! select LEU7, ILE8, VAL14, CYS16, LEU31, GLY38, THR43, VAL44, VAL46, ASP49 ! select selected or GLY51, ALA55, LEU74, HIS80, LYS89 ! ! !!---------------------------------------- !! !spt #name=select_isd_grade5 ! ! select LEU13, CYS24, SER39, LEU41, VAL57, SER63, VAL70, ILE83, ILE86, HIS90 ! ! !!---------------------------------------- !! !spt #name=select_isd_grade4 ! ! select ALA18, GLU35, ILE37, LYS54, ILE67, VAL71, ALA77, VAL87 ! ! !!---------------------------------------- !! !spt #name=select_isd_grade3 ! ! select ALA15, ASN28, ILE32, MET45, LYS47, GLU69, SER73 ! ! !!---------------------------------------- !! !spt #name=select_isd_grade2 ! ! select ASP58, LEU61, ASP82 ! ! !!---------------------------------------- !! !spt #name=select_isd_grade1 ! ! select ASP3, LYS11, GLU30, GLY33, TYR34, ASN36, GLU62, GLN65, HIS66, ASN81 ! select selected or ASN84, LYS85, ILE88 ! ! !!---------------------------------------- !! !spt #name=select_isd_grade0 ! select LYS91 ! ! !!---------------------------------------- !! !spt #name=select_grade9 ! ! select ALA4, GLY6, GLU9, ASP21, MET23, ALA25, ALA27, VAL29, GLY48, VAL53 ! select selected or ILE76 ! ! !!---------------------------------------- !! !spt #name=select_grade8 ! ! select THR10, GLY12, ALA19, VAL50, ALA52, SER56, GLY60, VAL75, ARG78, PRO79 ! ! !!---------------------------------------- !! !spt #name=select_grade7 ! ! select LEU5, ILE17, ALA20, ALA22, SER26, GLY40, VAL42, SER59, ALA64, GLY68 ! select selected or THR72 ! ! !!---------------------------------------- !! !spt #name=select_grade6 ! ! select LEU7, ILE8, VAL14, CYS16, LEU31, GLY38, THR43, VAL44, VAL46, ASP49 ! select selected or GLY51, ALA55, LEU74, HIS80, LYS89 ! ! !!---------------------------------------- !! !spt #name=select_grade5 ! ! select LEU13, CYS24, SER39, LEU41, VAL57, SER63, VAL70, ILE83, ILE86, HIS90 ! select selected or LYS91 ! ! !!---------------------------------------- !! !spt #name=select_grade4 ! ! select ALA18, GLU35, ILE37, LYS54, ILE67, VAL71, ALA77, VAL87 ! ! !!---------------------------------------- !! !spt #name=select_grade3 ! ! select ALA15, ASN28, ILE32, MET45, LYS47, GLU69, SER73 ! ! !!---------------------------------------- !! !spt #name=select_grade2 ! ! select ASP58, LEU61, ASP82 ! ! !!---------------------------------------- !! !spt #name=select_grade1 ! ! select ASP3, LYS11, GLU30, GLY33, TYR34, ASN36, GLU62, GLN65, HIS66, ASN81 ! select selected or ASN84, LYS85, ILE88 ! ! !!---------------------------------------- !! !spt #name=select_grade0 ! select none !! !! ====== END OF CONSURF PiPE BLOCK ====== COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN; COMPND 3 CHAIN: A; EXPDTA X-RAY DIFFRACTION REVDAT 1 REMARK 3 REFINEMENT. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 9460 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24220 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -97.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 5 0.500000 0.866025 0.000000 0.00000 REMARK 350 BIOMT2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 350 BIOMT2 6 0.866025 0.500000 0.000000 0.00000 REMARK 350 BIOMT3 6 0.000000 0.000000 1.000000 0.00000 ATOM 1 N HIS A -5 17.335 27.077 37.489 1.00 51.13 N ANISOU 1 N HIS A -5 10144 4578 4707 1661 -798 -113 N ATOM 2 CA HIS A -5 18.576 26.748 36.787 1.00 51.27 C ANISOU 2 CA HIS A -5 9929 4669 4884 1562 -1061 -152 C ATOM 3 C HIS A -5 18.623 25.244 36.531 1.00 50.54 C ANISOU 3 C HIS A -5 9776 4616 4811 1522 -918 -116 C ATOM 4 O HIS A -5 19.336 24.505 37.210 1.00 49.96 O ANISOU 4 O HIS A -5 9920 4439 4624 1623 -1042 -139 O ATOM 5 CB BHIS A -5 19.806 27.231 37.582 1.00 52.64 C ANISOU 5 CB BHIS A -5 10320 4699 4980 1683 -1445 -234 C ATOM 6 CG BHIS A -5 19.665 28.631 38.100 1.00 55.27 C ANISOU 6 CG BHIS A -5 10805 4951 5243 1762 -1572 -270 C ATOM 7 ND1BHIS A -5 19.722 28.909 39.454 1.00 57.30 N ANISOU 7 ND1BHIS A -5 11515 5010 5248 1976 -1678 -305 N ATOM 8 CD2BHIS A -5 19.402 29.779 37.429 1.00 56.68 C ANISOU 8 CD2BHIS A -5 10762 5215 5558 1662 -1591 -272 C ATOM 9 CE1BHIS A -5 19.535 30.215 39.561 1.00 58.05 C ANISOU 9 CE1BHIS A -5 11633 5079 5344 1994 -1770 -331 C ATOM 10 NE2BHIS A -5 19.340 30.782 38.370 1.00 57.96 N ANISOU 10 NE2BHIS A -5 11219 5237 5566 1806 -1721 -312 N ATOM 11 N HIS A -4 17.828 24.795 35.559 1.00 50.01 N ANISOU 11 N HIS A -4 9425 4690 4886 1381 -666 -63 N ATOM 12 CA HIS A -4 17.741 23.389 35.186 1.00 49.75 C ANISOU 12 CA HIS A -4 9299 4707 4896 1325 -507 -26 C ATOM 13 C HIS A -4 18.727 23.095 34.052 1.00 50.31 C ANISOU 13 C HIS A -4 9039 4906 5170 1182 -689 -48 C ATOM 14 O HIS A -4 18.888 23.903 33.138 1.00 50.20 O ANISOU 14 O HIS A -4 8763 4994 5317 1069 -777 -62 O ATOM 15 CB HIS A -4 16.308 23.037 34.720 1.00 49.38 C ANISOU 15 CB HIS A -4 9114 4728 4922 1252 -142 34 C ATOM 16 CG HIS A -4 15.241 23.197 35.766 1.00 49.54 C ANISOU 16 CG HIS A -4 9427 4616 4780 1381 109 63 C ATOM 17 ND1 HIS A -4 13.914 22.911 35.488 1.00 50.75 N ANISOU 17 ND1 HIS A -4 9462 4795 5024 1330 447 107 N ATOM 18 CD2 HIS A -4 15.334 23.609 37.052 1.00 49.85 C ANISOU 18 CD2 HIS A -4 9868 4486 4587 1560 70 51 C ATOM 19 CE1 HIS A -4 13.250 23.151 36.607 1.00 50.67 C ANISOU 19 CE1 HIS A -4 9774 4633 4846 1473 631 125 C ATOM 20 NE2 HIS A -4 14.061 23.577 37.573 1.00 50.55 N ANISOU 20 NE2 HIS A -4 10096 4497 4614 1619 416 96 N ATOM 21 N HIS A -3 19.377 21.938 34.107 1.00 50.20 N ANISOU 21 N HIS A -3 9051 4878 5147 1193 -732 -51 N ATOM 22 CA HIS A -3 20.313 21.518 33.076 1.00 50.98 C ANISOU 22 CA HIS A -3 8852 5083 5434 1069 -872 -70 C ATOM 23 C HIS A -3 19.817 20.220 32.450 1.00 51.20 C ANISOU 23 C HIS A -3 8745 5194 5515 989 -642 -21 C ATOM 24 O HIS A -3 19.419 19.300 33.167 1.00 50.35 O ANISOU 24 O HIS A -3 8854 5006 5271 1073 -494 6 O ATOM 25 CB HIS A -3 21.727 21.357 33.652 1.00 52.27 C ANISOU 25 CB HIS A -3 9137 5146 5576 1154 -1187 -138 C ATOM 26 CG HIS A -3 22.234 22.596 34.324 1.00 55.50 C ANISOU 26 CG HIS A -3 9690 5452 5946 1242 -1439 -198 C ATOM 27 ND1 HIS A -3 22.844 23.612 33.602 1.00 57.85 N ANISOU 27 ND1 HIS A -3 9736 5806 6438 1143 -1613 -235 N ATOM 28 CD2 HIS A -3 22.177 22.960 35.626 1.00 56.58 C ANISOU 28 CD2 HIS A -3 10206 5421 5869 1421 -1532 -227 C ATOM 29 CE1 HIS A -3 23.149 24.547 34.488 1.00 58.12 C ANISOU 29 CE1 HIS A -3 9984 5710 6388 1258 -1820 -289 C ATOM 30 NE2 HIS A -3 22.768 24.200 35.718 1.00 57.78 N ANISOU 30 NE2 HIS A -3 10331 5531 6093 1432 -1789 -288 N ATOM 31 N HIS A -2 19.791 20.167 31.110 1.00 51.67 N ANISOU 31 N HIS A -2 8464 5400 5766 833 -602 -7 N ATOM 32 CA HIS A -2 19.332 18.994 30.370 1.00 52.62 C ANISOU 32 CA HIS A -2 8429 5603 5960 749 -411 32 C ATOM 33 C HIS A -2 20.504 18.134 29.888 1.00 53.44 C ANISOU 33 C HIS A -2 8417 5742 6144 708 -552 11 C ATOM 34 O HIS A -2 21.599 18.653 29.666 1.00 53.77 O ANISOU 34 O HIS A -2 8374 5788 6270 691 -779 -33 O ATOM 35 CB HIS A -2 18.460 19.418 29.176 1.00 53.43 C ANISOU 35 CB HIS A -2 8260 5831 6210 620 -277 55 C ATOM 36 N ASP A 3 23.838 20.954 19.735 1.00 33.11 N ANISOU 36 N ASP A 3 4136 3752 4692 -142 -624 52 N ATOM 37 CA ASP A 3 22.842 21.939 19.307 1.00 32.12 C ANISOU 37 CA ASP A 3 4038 3650 4517 -159 -579 71 C ATOM 38 C ASP A 3 22.123 21.493 18.031 1.00 30.34 C ANISOU 38 C ASP A 3 3763 3491 4274 -204 -455 100 C ATOM 39 O ASP A 3 20.897 21.431 18.022 1.00 31.26 O ANISOU 39 O ASP A 3 3921 3636 4321 -182 -405 103 O ATOM 40 CB ASP A 3 23.477 23.325 19.119 1.00 34.67 C ANISOU 40 CB ASP A 3 4331 3921 4922 -194 -654 65 C ATOM 41 N ALA A 4 22.878 21.183 16.966 1.00 27.30 N ANISOU 41 N ALA A 4 3295 3116 3962 -258 -407 115 N ATOM 42 CA ALA A 4 22.274 20.764 15.707 1.00 24.88 C ANISOU 42 CA ALA A 4 2975 2854 3625 -286 -310 137 C ATOM 43 C ALA A 4 21.623 19.401 15.829 1.00 22.32 C ANISOU 43 C ALA A 4 2655 2572 3253 -259 -263 132 C ATOM 44 O ALA A 4 22.043 18.577 16.644 1.00 22.28 O ANISOU 44 O ALA A 4 2650 2562 3253 -234 -280 121 O ATOM 45 CB ALA A 4 23.318 20.746 14.609 1.00 24.94 C ANISOU 45 CB ALA A 4 2923 2842 3710 -338 -252 158 C ATOM 46 N LEU A 5 20.590 19.166 15.020 1.00 20.36 N ANISOU 46 N LEU A 5 2417 2353 2965 -261 -215 134 N ATOM 47 CA LEU A 5 19.842 17.909 15.023 1.00 20.17 C ANISOU 47 CA LEU A 5 2385 2358 2922 -242 -168 124 C ATOM 48 C LEU A 5 19.975 17.281 13.629 1.00 19.82 C ANISOU 48 C LEU A 5 2321 2330 2882 -267 -126 131 C ATOM 49 O LEU A 5 19.776 17.964 12.641 1.00 19.45 O ANISOU 49 O LEU A 5 2303 2271 2817 -276 -131 137 O ATOM 50 CB LEU A 5 18.359 18.240 15.304 1.00 20.44 C ANISOU 50 CB LEU A 5 2439 2388 2937 -213 -166 104 C ATOM 51 CG LEU A 5 17.372 17.068 15.352 1.00 22.00 C ANISOU 51 CG LEU A 5 2610 2594 3156 -198 -109 85 C ATOM 52 CD1 LEU A 5 17.714 16.119 16.481 1.00 21.88 C ANISOU 52 CD1 LEU A 5 2616 2569 3128 -178 -64 92 C ATOM 53 CD2 LEU A 5 15.942 17.572 15.489 1.00 23.09 C ANISOU 53 CD2 LEU A 5 2738 2712 3324 -174 -104 57 C ATOM 54 N GLY A 6 20.305 15.994 13.558 1.00 18.47 N ANISOU 54 N GLY A 6 2123 2175 2721 -267 -88 131 N ATOM 55 CA GLY A 6 20.403 15.297 12.280 1.00 17.62 C ANISOU 55 CA GLY A 6 2016 2075 2603 -279 -49 135 C ATOM 56 C GLY A 6 19.409 14.155 12.282 1.00 17.48 C ANISOU 56 C GLY A 6 1987 2070 2585 -260 -39 111 C ATOM 57 O GLY A 6 19.288 13.479 13.297 1.00 18.51 O ANISOU 57 O GLY A 6 2098 2205 2731 -249 -22 106 O ATOM 58 N LEU A 7 18.648 13.961 11.191 1.00 16.36 N ANISOU 58 N LEU A 7 1868 1919 2430 -250 -55 92 N ATOM 59 CA LEU A 7 17.622 12.915 11.166 1.00 17.46 C ANISOU 59 CA LEU A 7 1976 2052 2605 -235 -59 57 C ATOM 60 C LEU A 7 17.710 12.127 9.892 1.00 17.59 C ANISOU 60 C LEU A 7 2028 2057 2598 -226 -69 46 C ATOM 61 O LEU A 7 17.893 12.721 8.826 1.00 17.34 O ANISOU 61 O LEU A 7 2073 2004 2511 -213 -96 50 O ATOM 62 CB LEU A 7 16.236 13.570 11.208 1.00 19.03 C ANISOU 62 CB LEU A 7 2159 2224 2847 -217 -112 19 C ATOM 63 CG LEU A 7 15.958 14.510 12.387 1.00 21.44 C ANISOU 63 CG LEU A 7 2451 2530 3167 -214 -100 26 C ATOM 64 CD1 LEU A 7 16.150 15.939 11.989 1.00 24.54 C ANISOU 64 CD1 LEU A 7 2893 2916 3515 -211 -153 36 C ATOM 65 CD2 LEU A 7 14.526 14.336 12.864 1.00 23.30 C ANISOU 65 CD2 LEU A 7 2625 2731 3495 -196 -90 -17 C ATOM 66 N ILE A 8 17.550 10.794 9.986 1.00 16.78 N ANISOU 66 N ILE A 8 1891 1957 2529 -226 -47 31 N ATOM 67 CA ILE A 8 17.438 9.941 8.813 1.00 16.67 C ANISOU 67 CA ILE A 8 1917 1920 2496 -207 -73 8 C ATOM 68 C ILE A 8 16.215 9.066 9.019 1.00 17.59 C ANISOU 68 C ILE A 8 1968 2007 2707 -201 -107 -42 C ATOM 69 O ILE A 8 16.101 8.459 10.078 1.00 17.08 O ANISOU 69 O ILE A 8 1840 1952 2699 -220 -44 -35 O ATOM 70 CB ILE A 8 18.696 9.083 8.565 1.00 17.31 C ANISOU 70 CB ILE A 8 2019 2021 2536 -213 -5 40 C ATOM 71 CG1 ILE A 8 19.873 9.996 8.186 1.00 17.52 C ANISOU 71 CG1 ILE A 8 2094 2053 2510 -222 42 83 C ATOM 72 CG2 ILE A 8 18.437 8.018 7.466 1.00 17.98 C ANISOU 72 CG2 ILE A 8 2155 2076 2600 -185 -34 11 C ATOM 73 CD1 ILE A 8 21.212 9.272 8.057 1.00 19.40 C ANISOU 73 CD1 ILE A 8 2323 2302 2746 -230 124 111 C ATOM 74 N GLU A 9 15.333 9.011 8.024 1.00 17.65 N ANISOU 74 N GLU A 9 2002 1966 2741 -169 -205 -95 N ATOM 75 CA GLU A 9 14.121 8.188 8.065 1.00 18.27 C ANISOU 75 CA GLU A 9 1996 1992 2953 -164 -255 -159 C ATOM 76 C GLU A 9 14.218 7.143 6.972 1.00 20.46 C ANISOU 76 C GLU A 9 2332 2236 3206 -137 -316 -189 C ATOM 77 O GLU A 9 14.549 7.474 5.839 1.00 20.92 O ANISOU 77 O GLU A 9 2518 2273 3157 -95 -383 -193 O ATOM 78 CB GLU A 9 12.883 9.069 7.838 1.00 19.46 C ANISOU 78 CB GLU A 9 2112 2091 3193 -139 -361 -219 C ATOM 79 CG GLU A 9 11.577 8.301 7.981 1.00 21.58 C ANISOU 79 CG GLU A 9 2252 2287 3659 -140 -405 -294 C ATOM 80 CD GLU A 9 10.430 9.218 8.360 1.00 28.87 C ANISOU 80 CD GLU A 9 3084 3167 4717 -130 -448 -342 C ATOM 81 OE1 GLU A 9 10.488 10.417 7.999 1.00 29.87 O ANISOU 81 OE1 GLU A 9 3283 3303 4763 -101 -518 -339 O ATOM 82 OE2 GLU A 9 9.496 8.756 9.058 1.00 28.99 O ANISOU 82 OE2 GLU A 9 2957 3133 4925 -151 -394 -380 O ATOM 83 N THR A 10 14.052 5.862 7.335 1.00 20.40 N ANISOU 83 N THR A 10 2256 2215 3279 -157 -276 -202 N ATOM 84 CA THR A 10 14.145 4.780 6.364 1.00 21.14 C ANISOU 84 CA THR A 10 2407 2272 3354 -129 -336 -234 C ATOM 85 C THR A 10 12.865 3.954 6.378 1.00 22.44 C ANISOU 85 C THR A 10 2463 2355 3707 -132 -410 -313 C ATOM 86 O THR A 10 12.093 3.993 7.343 1.00 21.66 O ANISOU 86 O THR A 10 2233 2238 3760 -169 -354 -326 O ATOM 87 CB THR A 10 15.344 3.851 6.726 1.00 22.05 C ANISOU 87 CB THR A 10 2544 2440 3396 -151 -217 -176 C ATOM 88 OG1 THR A 10 15.092 3.273 8.010 1.00 23.00 O ANISOU 88 OG1 THR A 10 2556 2568 3615 -195 -123 -163 O ATOM 89 CG2 THR A 10 16.662 4.593 6.765 1.00 21.95 C ANISOU 89 CG2 THR A 10 2602 2491 3248 -154 -139 -107 C ATOM 90 N LYS A 11 12.664 3.184 5.319 1.00 24.70 N ANISOU 90 N LYS A 11 2809 2581 3994 -92 -526 -367 N ATOM 91 CA LYS A 11 11.652 2.174 5.325 1.00 27.32 C ANISOU 91 CA LYS A 11 3031 2828 4522 -101 -590 -442 C ATOM 92 C LYS A 11 12.211 0.849 5.749 1.00 28.11 C ANISOU 92 C LYS A 11 3114 2947 4622 -135 -480 -408 C ATOM 93 O LYS A 11 13.010 0.262 5.027 1.00 31.05 O ANISOU 93 O LYS A 11 3605 3333 4861 -104 -498 -393 O ATOM 94 CB LYS A 11 10.938 2.104 3.960 1.00 30.61 C ANISOU 94 CB LYS A 11 3521 3142 4969 -26 -822 -540 C ATOM 95 CG LYS A 11 9.598 1.380 4.024 1.00 36.48 C ANISOU 95 CG LYS A 11 4099 3770 5994 -38 -926 -644 C ATOM 96 CD LYS A 11 8.698 1.846 2.887 1.00 43.61 C ANISOU 96 CD LYS A 11 5050 4560 6958 46 -1193 -756 C ATOM 97 CE LYS A 11 7.234 1.564 3.121 1.00 49.52 C ANISOU 97 CE LYS A 11 5579 5185 8051 30 -1300 -870 C ATOM 98 NZ LYS A 11 6.371 2.464 2.304 1.00 53.04 N ANISOU 98 NZ LYS A 11 6053 5538 8563 112 -1551 -973 N ATOM 99 N GLY A 12 12.003 0.509 7.005 1.00 26.21 N ANISOU 99 N GLY A 12 2755 2715 4490 -194 -334 -379 N ATOM 100 CA GLY A 12 12.567 -0.706 7.581 1.00 25.62 C ANISOU 100 CA GLY A 12 2678 2654 4403 -224 -215 -339 C ATOM 101 C GLY A 12 13.573 -0.393 8.682 1.00 24.11 C ANISOU 101 C GLY A 12 2522 2552 4089 -247 -56 -247 C ATOM 102 O GLY A 12 14.260 0.639 8.654 1.00 23.52 O ANISOU 102 O GLY A 12 2507 2544 3885 -232 -55 -207 O ATOM 103 N LEU A 13 13.639 -1.279 9.686 1.00 23.26 N ANISOU 103 N LEU A 13 2384 2428 4027 -278 73 -217 N ATOM 104 CA LEU A 13 14.511 -1.108 10.849 1.00 22.52 C ANISOU 104 CA LEU A 13 2339 2390 3826 -286 201 -142 C ATOM 105 C LEU A 13 15.972 -1.362 10.546 1.00 20.89 C ANISOU 105 C LEU A 13 2228 2255 3452 -261 191 -101 C ATOM 106 O LEU A 13 16.838 -0.648 11.075 1.00 20.65 O ANISOU 106 O LEU A 13 2239 2284 3322 -251 224 -55 O ATOM 107 CB LEU A 13 14.042 -2.071 11.952 1.00 23.14 C ANISOU 107 CB LEU A 13 2390 2400 4002 -313 340 -129 C ATOM 108 CG LEU A 13 14.822 -2.065 13.266 1.00 24.42 C ANISOU 108 CG LEU A 13 2640 2588 4052 -303 462 -60 C ATOM 109 CD1 LEU A 13 14.842 -0.666 13.894 1.00 25.79 C ANISOU 109 CD1 LEU A 13 2828 2796 4174 -293 479 -36 C ATOM 110 CD2 LEU A 13 14.244 -3.091 14.245 1.00 25.29 C ANISOU 110 CD2 LEU A 13 2757 2602 4249 -322 612 -48 C ATOM 111 N VAL A 14 16.283 -2.388 9.738 1.00 20.19 N ANISOU 111 N VAL A 14 2170 2154 3346 -246 148 -121 N ATOM 112 CA VAL A 14 17.697 -2.714 9.455 1.00 20.24 C ANISOU 112 CA VAL A 14 2255 2218 3217 -219 159 -84 C ATOM 113 C VAL A 14 18.432 -1.574 8.772 1.00 19.76 C ANISOU 113 C VAL A 14 2237 2212 3057 -197 121 -67 C ATOM 114 O VAL A 14 19.543 -1.220 9.186 1.00 19.54 O ANISOU 114 O VAL A 14 2229 2234 2961 -191 168 -25 O ATOM 115 CB VAL A 14 17.810 -4.026 8.683 1.00 20.49 C ANISOU 115 CB VAL A 14 2319 2216 3252 -202 125 -112 C ATOM 116 CG1 VAL A 14 19.266 -4.359 8.334 1.00 20.90 C ANISOU 116 CG1 VAL A 14 2442 2320 3181 -169 148 -80 C ATOM 117 CG2 VAL A 14 17.159 -5.144 9.483 1.00 20.83 C ANISOU 117 CG2 VAL A 14 2320 2193 3400 -231 185 -121 C ATOM 118 N ALA A 15 17.809 -0.939 7.748 1.00 19.77 N ANISOU 118 N ALA A 15 2258 2192 3062 -182 34 -103 N ATOM 119 CA ALA A 15 18.438 0.216 7.092 1.00 19.04 C ANISOU 119 CA ALA A 15 2228 2135 2872 -160 18 -82 C ATOM 120 C ALA A 15 18.660 1.364 8.114 1.00 18.50 C ANISOU 120 C ALA A 15 2114 2109 2807 -187 67 -44 C ATOM 121 O ALA A 15 19.677 2.053 8.074 1.00 18.97 O ANISOU 121 O ALA A 15 2200 2206 2801 -184 104 -7 O ATOM 122 CB ALA A 15 17.547 0.693 5.947 1.00 19.05 C ANISOU 122 CB ALA A 15 2282 2083 2873 -128 -100 -133 C ATOM 123 N CYS A 16 17.728 1.508 9.070 1.00 18.42 N ANISOU 123 N CYS A 16 2033 2081 2885 -213 78 -55 N ATOM 124 CA CYS A 16 17.855 2.540 10.115 1.00 18.53 C ANISOU 124 CA CYS A 16 2024 2124 2894 -228 120 -23 C ATOM 125 C CYS A 16 19.037 2.252 11.035 1.00 18.00 C ANISOU 125 C CYS A 16 1975 2088 2775 -226 183 20 C ATOM 126 O CYS A 16 19.824 3.155 11.360 1.00 17.97 O ANISOU 126 O CYS A 16 1981 2116 2730 -224 184 47 O ATOM 127 CB CYS A 16 16.566 2.682 10.910 1.00 20.27 C ANISOU 127 CB CYS A 16 2180 2300 3220 -246 141 -45 C ATOM 128 SG CYS A 16 16.552 4.162 11.954 1.00 28.91 S ANISOU 128 SG CYS A 16 3275 3419 4293 -249 171 -16 S ATOM 129 N ILE A 17 19.183 0.986 11.440 1.00 17.39 N ANISOU 129 N ILE A 17 1904 1992 2711 -223 222 21 N ATOM 130 CA ILE A 17 20.316 0.600 12.281 1.00 17.69 C ANISOU 130 CA ILE A 17 1972 2045 2703 -206 254 51 C ATOM 131 C ILE A 17 21.631 0.787 11.521 1.00 18.34 C ANISOU 131 C ILE A 17 2059 2166 2744 -192 233 61 C ATOM 132 O ILE A 17 22.606 1.300 12.097 1.00 19.14 O ANISOU 132 O ILE A 17 2154 2283 2835 -181 228 78 O ATOM 133 CB ILE A 17 20.129 -0.824 12.830 1.00 18.45 C ANISOU 133 CB ILE A 17 2093 2100 2817 -199 300 48 C ATOM 134 CG1 ILE A 17 18.980 -0.815 13.884 1.00 19.38 C ANISOU 134 CG1 ILE A 17 2217 2162 2985 -212 367 51 C ATOM 135 CG2 ILE A 17 21.469 -1.344 13.462 1.00 18.82 C ANISOU 135 CG2 ILE A 17 2185 2157 2809 -165 300 68 C ATOM 136 CD1 ILE A 17 18.568 -2.198 14.306 1.00 22.41 C ANISOU 136 CD1 ILE A 17 2627 2482 3406 -214 436 49 C ATOM 137 N ALA A 18 21.647 0.495 10.204 1.00 18.37 N ANISOU 137 N ALA A 18 2075 2171 2734 -187 222 47 N ATOM 138 CA ALA A 18 22.866 0.741 9.397 1.00 18.81 C ANISOU 138 CA ALA A 18 2143 2246 2758 -171 243 61 C ATOM 139 C ALA A 18 23.196 2.234 9.387 1.00 18.77 C ANISOU 139 C ALA A 18 2124 2256 2753 -185 244 79 C ATOM 140 O ALA A 18 24.357 2.619 9.532 1.00 18.86 O ANISOU 140 O ALA A 18 2104 2275 2788 -184 272 96 O ATOM 141 CB ALA A 18 22.669 0.253 7.965 1.00 19.55 C ANISOU 141 CB ALA A 18 2297 2319 2811 -151 240 43 C ATOM 142 N ALA A 19 22.152 3.081 9.250 1.00 17.81 N ANISOU 142 N ALA A 19 2015 2129 2624 -198 207 71 N ATOM 143 CA ALA A 19 22.353 4.514 9.274 1.00 18.14 C ANISOU 143 CA ALA A 19 2052 2179 2662 -211 203 88 C ATOM 144 C ALA A 19 22.910 4.959 10.627 1.00 18.06 C ANISOU 144 C ALA A 19 1993 2181 2688 -220 198 102 C ATOM 145 O ALA A 19 23.893 5.710 10.647 1.00 17.61 O ANISOU 145 O ALA A 19 1911 2125 2655 -227 209 117 O ATOM 146 CB ALA A 19 21.026 5.230 8.968 1.00 18.69 C ANISOU 146 CB ALA A 19 2145 2234 2723 -214 148 68 C ATOM 147 N ALA A 20 22.304 4.501 11.751 1.00 16.97 N ANISOU 147 N ALA A 20 1852 2037 2560 -215 183 94 N ATOM 148 CA ALA A 20 22.719 4.927 13.084 1.00 17.64 C ANISOU 148 CA ALA A 20 1937 2115 2652 -205 162 102 C ATOM 149 C ALA A 20 24.155 4.522 13.346 1.00 17.88 C ANISOU 149 C ALA A 20 1946 2140 2709 -185 147 103 C ATOM 150 O ALA A 20 24.935 5.322 13.849 1.00 18.72 O ANISOU 150 O ALA A 20 2029 2236 2849 -180 105 102 O ATOM 151 CB ALA A 20 21.797 4.350 14.135 1.00 19.22 C ANISOU 151 CB ALA A 20 2177 2287 2840 -191 180 99 C ATOM 152 N ASP A 21 24.525 3.296 12.934 1.00 17.32 N ANISOU 152 N ASP A 21 1873 2068 2639 -173 174 97 N ATOM 153 CA ASP A 21 25.904 2.834 13.116 1.00 18.75 C ANISOU 153 CA ASP A 21 2018 2238 2869 -149 157 88 C ATOM 154 C ASP A 21 26.887 3.740 12.365 1.00 19.70 C ANISOU 154 C ASP A 21 2066 2358 3060 -168 178 92 C ATOM 155 O ASP A 21 27.870 4.186 12.962 1.00 21.13 O ANISOU 155 O ASP A 21 2193 2514 3323 -157 130 79 O ATOM 156 CB ASP A 21 26.038 1.381 12.650 1.00 20.51 C ANISOU 156 CB ASP A 21 2254 2459 3078 -132 191 81 C ATOM 157 CG ASP A 21 27.415 0.833 12.966 1.00 25.73 C ANISOU 157 CG ASP A 21 2874 3100 3803 -97 164 64 C ATOM 158 OD1 ASP A 21 27.765 0.765 14.162 1.00 27.28 O ANISOU 158 OD1 ASP A 21 3092 3266 4007 -62 88 49 O ATOM 159 OD2 ASP A 21 28.141 0.484 12.023 1.00 28.26 O ANISOU 159 OD2 ASP A 21 3148 3423 4166 -96 216 61 O ATOM 160 N ALA A 22 26.617 4.040 11.093 1.00 18.97 N ANISOU 160 N ALA A 22 1985 2277 2945 -190 247 107 N ATOM 161 CA ALA A 22 27.500 4.896 10.298 1.00 20.24 C ANISOU 161 CA ALA A 22 2103 2420 3169 -209 309 120 C ATOM 162 C ALA A 22 27.530 6.321 10.842 1.00 20.44 C ANISOU 162 C ALA A 22 2099 2434 3233 -233 267 125 C ATOM 163 O ALA A 22 28.572 6.978 10.825 1.00 22.14 O ANISOU 163 O ALA A 22 2238 2615 3558 -247 287 124 O ATOM 164 CB ALA A 22 27.031 4.919 8.859 1.00 21.07 C ANISOU 164 CB ALA A 22 2285 2522 3199 -211 389 137 C ATOM 165 N MET A 23 26.379 6.805 11.321 1.00 19.95 N ANISOU 165 N MET A 23 2090 2392 3099 -237 213 128 N ATOM 166 CA MET A 23 26.278 8.146 11.897 1.00 20.26 C ANISOU 166 CA MET A 23 2118 2421 3159 -253 165 131 C ATOM 167 C MET A 23 27.207 8.285 13.103 1.00 22.45 C ANISOU 167 C MET A 23 2341 2668 3521 -236 83 109 C ATOM 168 O MET A 23 27.927 9.282 13.216 1.00 24.25 O ANISOU 168 O MET A 23 2512 2863 3840 -253 60 104 O ATOM 169 CB MET A 23 24.820 8.434 12.324 1.00 20.11 C ANISOU 169 CB MET A 23 2164 2421 3055 -250 126 131 C ATOM 170 CG MET A 23 23.925 8.753 11.148 1.00 20.69 C ANISOU 170 CG MET A 23 2285 2504 3073 -262 161 139 C ATOM 171 SD MET A 23 22.188 8.673 11.665 1.00 22.42 S ANISOU 171 SD MET A 23 2540 2732 3248 -253 119 121 S ATOM 172 CE MET A 23 21.777 10.363 11.562 1.00 19.57 C ANISOU 172 CE MET A 23 2196 2363 2877 -265 86 127 C ATOM 173 N CYS A 24 27.177 7.301 14.007 1.00 22.11 N ANISOU 173 N CYS A 24 2327 2622 3453 -196 29 90 N ATOM 174 CA CYS A 24 28.011 7.351 15.204 1.00 23.57 C ANISOU 174 CA CYS A 24 2498 2761 3699 -156 -82 59 C ATOM 175 C CYS A 24 29.472 7.142 14.917 1.00 24.71 C ANISOU 175 C CYS A 24 2527 2868 3995 -154 -94 33 C ATOM 176 O CYS A 24 30.324 7.724 15.598 1.00 25.92 O ANISOU 176 O CYS A 24 2623 2965 4260 -137 -198 -1 O ATOM 177 CB CYS A 24 27.515 6.338 16.225 1.00 25.43 C ANISOU 177 CB CYS A 24 2836 2985 3840 -103 -125 50 C ATOM 178 SG CYS A 24 25.848 6.687 16.811 1.00 28.51 S ANISOU 178 SG CYS A 24 3345 3388 4099 -101 -92 74 S ATOM 179 N ALA A 25 29.778 6.294 13.935 1.00 24.34 N ANISOU 179 N ALA A 25 2441 2838 3968 -165 5 42 N ATOM 180 CA ALA A 25 31.168 5.991 13.615 1.00 26.01 C ANISOU 180 CA ALA A 25 2530 3007 4346 -159 20 15 C ATOM 181 C ALA A 25 31.877 7.138 12.895 1.00 27.12 C ANISOU 181 C ALA A 25 2564 3110 4629 -209 96 23 C ATOM 182 O ALA A 25 33.090 7.261 12.986 1.00 29.21 O ANISOU 182 O ALA A 25 2696 3311 5090 -207 79 -12 O ATOM 183 CB ALA A 25 31.218 4.743 12.754 1.00 26.89 C ANISOU 183 CB ALA A 25 2652 3143 4422 -150 122 26 C ATOM 184 N SER A 26 31.139 7.939 12.134 1.00 25.94 N ANISOU 184 N SER A 26 2471 2986 4397 -250 186 66 N ATOM 185 CA SER A 26 31.726 8.936 11.253 1.00 26.82 C ANISOU 185 CA SER A 26 2519 3052 4617 -297 302 87 C ATOM 186 C SER A 26 31.926 10.309 11.818 1.00 26.77 C ANISOU 186 C SER A 26 2464 3004 4703 -325 231 77 C ATOM 187 O SER A 26 32.493 11.156 11.123 1.00 27.83 O ANISOU 187 O SER A 26 2539 3083 4951 -368 340 94 O ATOM 188 CB SER A 26 30.851 9.075 10.018 1.00 29.25 C ANISOU 188 CB SER A 26 2950 3393 4773 -314 433 137 C ATOM 189 OG SER A 26 29.586 9.596 10.412 1.00 32.13 O ANISOU 189 OG SER A 26 3412 3802 4995 -315 349 147 O ATOM 190 N ALA A 27 31.347 10.598 12.982 1.00 25.96 N ANISOU 190 N ALA A 27 2413 2920 4532 -300 72 57 N ATOM 191 CA ALA A 27 31.438 11.946 13.541 1.00 25.95 C ANISOU 191 CA ALA A 27 2386 2876 4597 -320 -10 46 C ATOM 192 C ALA A 27 31.207 11.959 15.058 1.00 26.30 C ANISOU 192 C ALA A 27 2483 2910 4599 -265 -208 5 C ATOM 193 O ALA A 27 30.702 10.979 15.628 1.00 26.18 O ANISOU 193 O ALA A 27 2556 2930 4462 -215 -256 -2 O ATOM 194 CB ALA A 27 30.437 12.869 12.822 1.00 26.56 C ANISOU 194 CB ALA A 27 2558 2985 4548 -357 75 96 C ATOM 195 N ASN A 28 31.583 13.059 15.719 1.00 27.21 N ANISOU 195 N ASN A 28 2563 2965 4811 -268 -320 -24 N ATOM 196 CA ASN A 28 31.380 13.202 17.145 1.00 27.77 C ANISOU 196 CA ASN A 28 2721 3007 4825 -202 -512 -64 C ATOM 197 C ASN A 28 29.947 13.685 17.370 1.00 26.66 C ANISOU 197 C ASN A 28 2733 2924 4474 -198 -489 -24 C ATOM 198 O ASN A 28 29.716 14.886 17.540 1.00 26.71 O ANISOU 198 O ASN A 28 2755 2909 4485 -216 -524 -20 O ATOM 199 CB ASN A 28 32.390 14.206 17.721 1.00 30.48 C ANISOU 199 CB ASN A 28 2964 3245 5371 -201 -658 -120 C ATOM 200 CG ASN A 28 32.224 14.434 19.204 1.00 35.63 C ANISOU 200 CG ASN A 28 3742 3847 5950 -116 -877 -168 C ATOM 201 OD1 ASN A 28 31.605 13.631 19.905 1.00 36.42 O ANISOU 201 OD1 ASN A 28 3995 3972 5870 -47 -917 -165 O ATOM 202 ND2 ASN A 28 32.755 15.543 19.713 1.00 37.45 N ANISOU 202 ND2 ASN A 28 3928 3990 6312 -114 -1016 -212 N ATOM 203 N VAL A 29 28.986 12.754 17.346 1.00 25.50 N ANISOU 203 N VAL A 29 2686 2841 4162 -176 -423 4 N ATOM 204 CA VAL A 29 27.573 13.037 17.582 1.00 25.25 C ANISOU 204 CA VAL A 29 2779 2854 3962 -168 -388 34 C ATOM 205 C VAL A 29 27.030 12.087 18.661 1.00 27.38 C ANISOU 205 C VAL A 29 3178 3117 4109 -96 -427 24 C ATOM 206 O VAL A 29 27.642 11.052 18.933 1.00 27.87 O ANISOU 206 O VAL A 29 3238 3158 4192 -61 -460 4 O ATOM 207 CB VAL A 29 26.776 12.870 16.269 1.00 24.54 C ANISOU 207 CB VAL A 29 2675 2831 3818 -220 -237 77 C ATOM 208 CG1 VAL A 29 27.230 13.871 15.210 1.00 25.43 C ANISOU 208 CG1 VAL A 29 2711 2932 4017 -279 -178 94 C ATOM 209 CG2 VAL A 29 26.864 11.429 15.747 1.00 24.10 C ANISOU 209 CG2 VAL A 29 2604 2806 3747 -215 -166 82 C ATOM 210 N GLU A 30 25.871 12.429 19.251 1.00 27.60 N ANISOU 210 N GLU A 30 3323 3150 4012 -72 -408 41 N ATOM 211 CA GLU A 30 25.202 11.595 20.245 1.00 28.19 C ANISOU 211 CA GLU A 30 3543 3202 3965 -6 -395 43 C ATOM 212 C GLU A 30 23.918 11.060 19.591 1.00 26.73 C ANISOU 212 C GLU A 30 3355 3075 3725 -44 -242 77 C ATOM 213 O GLU A 30 23.180 11.840 18.993 1.00 25.71 O ANISOU 213 O GLU A 30 3188 2980 3601 -85 -194 91 O ATOM 214 CB GLU A 30 24.813 12.436 21.470 1.00 32.68 C ANISOU 214 CB GLU A 30 4256 3710 4451 57 -467 32 C ATOM 215 CG GLU A 30 24.187 11.603 22.573 1.00 41.79 C ANISOU 215 CG GLU A 30 5597 4813 5469 137 -428 39 C ATOM 216 CD GLU A 30 24.891 11.707 23.909 1.00 52.28 C ANISOU 216 CD GLU A 30 7093 6037 6736 243 -585 2 C ATOM 217 OE1 GLU A 30 25.344 12.824 24.252 1.00 55.55 O ANISOU 217 OE1 GLU A 30 7513 6412 7183 261 -716 -26 O ATOM 218 OE2 GLU A 30 24.991 10.675 24.613 1.00 55.30 O ANISOU 218 OE2 GLU A 30 7613 6363 7035 314 -589 -2 O ATOM 219 N LEU A 31 23.658 9.751 19.698 1.00 26.60 N ANISOU 219 N LEU A 31 3379 3059 3671 -26 -179 84 N ATOM 220 CA LEU A 31 22.434 9.135 19.173 1.00 27.11 C ANISOU 220 CA LEU A 31 3432 3156 3713 -57 -49 104 C ATOM 221 C LEU A 31 21.383 9.481 20.228 1.00 28.19 C ANISOU 221 C LEU A 31 3689 3245 3778 -17 2 113 C ATOM 222 O LEU A 31 21.456 8.962 21.336 1.00 28.59 O ANISOU 222 O LEU A 31 3877 3230 3755 49 7 114 O ATOM 223 CB LEU A 31 22.632 7.611 19.107 1.00 27.78 C ANISOU 223 CB LEU A 31 3529 3234 3790 -46 -7 105 C ATOM 224 CG LEU A 31 21.696 6.823 18.199 1.00 30.61 C ANISOU 224 CG LEU A 31 3831 3627 4175 -91 99 115 C ATOM 225 CD1 LEU A 31 22.091 5.335 18.198 1.00 31.91 C ANISOU 225 CD1 LEU A 31 4015 3777 4332 -75 123 114 C ATOM 226 CD2 LEU A 31 20.255 6.913 18.661 1.00 32.02 C ANISOU 226 CD2 LEU A 31 4053 3775 4340 -90 194 123 C ATOM 227 N ILE A 32 20.438 10.370 19.912 1.00 28.43 N ANISOU 227 N ILE A 32 3682 3294 3825 -45 44 117 N ATOM 228 CA ILE A 32 19.467 10.858 20.899 1.00 30.24 C ANISOU 228 CA ILE A 32 4015 3471 4003 -4 106 123 C ATOM 229 C ILE A 32 18.017 10.557 20.609 1.00 31.14 C ANISOU 229 C ILE A 32 4082 3581 4167 -30 244 127 C ATOM 230 O ILE A 32 17.171 10.826 21.467 1.00 31.87 O ANISOU 230 O ILE A 32 4258 3616 4236 6 333 133 O ATOM 231 CB ILE A 32 19.622 12.389 21.114 1.00 32.00 C ANISOU 231 CB ILE A 32 4253 3693 4214 6 20 116 C ATOM 232 CG1 ILE A 32 19.329 13.160 19.815 1.00 33.77 C ANISOU 232 CG1 ILE A 32 4335 3981 4513 -62 5 112 C ATOM 233 CG2 ILE A 32 21.011 12.730 21.644 1.00 33.06 C ANISOU 233 CG2 ILE A 32 4437 3799 4325 43 -128 100 C ATOM 234 CD1 ILE A 32 18.042 13.844 19.724 1.00 35.50 C ANISOU 234 CD1 ILE A 32 4538 4197 4751 -68 65 109 C ATOM 235 N GLY A 33 17.719 10.098 19.406 1.00 29.82 N ANISOU 235 N GLY A 33 3786 3462 4082 -88 256 118 N ATOM 236 CA GLY A 33 16.339 9.824 19.034 1.00 29.32 C ANISOU 236 CA GLY A 33 3651 3381 4107 -113 353 104 C ATOM 237 C GLY A 33 16.185 8.549 18.240 1.00 27.36 C ANISOU 237 C GLY A 33 3329 3142 3923 -147 383 94 C ATOM 238 O GLY A 33 17.064 8.175 17.462 1.00 25.28 O ANISOU 238 O GLY A 33 3036 2926 3642 -165 310 94 O ATOM 239 N TYR A 34 15.052 7.892 18.413 1.00 26.92 N ANISOU 239 N TYR A 34 3239 3032 3957 -155 496 82 N ATOM 240 CA TYR A 34 14.774 6.662 17.684 1.00 27.43 C ANISOU 240 CA TYR A 34 3231 3089 4103 -188 519 65 C ATOM 241 C TYR A 34 13.266 6.497 17.723 1.00 28.27 C ANISOU 241 C TYR A 34 3247 3124 4369 -205 620 34 C ATOM 242 O TYR A 34 12.692 6.537 18.817 1.00 29.76 O ANISOU 242 O TYR A 34 3490 3241 4575 -183 760 50 O ATOM 243 CB TYR A 34 15.478 5.483 18.361 1.00 27.75 C ANISOU 243 CB TYR A 34 3368 3103 4073 -167 575 93 C ATOM 244 N GLU A 35 12.612 6.410 16.552 1.00 26.85 N ANISOU 244 N GLU A 35 2938 2949 4313 -237 547 -15 N ATOM 245 CA GLU A 35 11.155 6.289 16.537 1.00 27.87 C ANISOU 245 CA GLU A 35 2948 2996 4645 -253 619 -61 C ATOM 246 C GLU A 35 10.642 5.505 15.360 1.00 28.45 C ANISOU 246 C GLU A 35 2905 3047 4858 -281 534 -119 C ATOM 247 O GLU A 35 11.161 5.612 14.266 1.00 28.10 O ANISOU 247 O GLU A 35 2867 3059 4750 -278 381 -135 O ATOM 248 CB GLU A 35 10.490 7.673 16.563 1.00 30.26 C ANISOU 248 CB GLU A 35 3207 3296 4994 -238 585 -85 C ATOM 249 CG GLU A 35 8.978 7.633 16.764 1.00 37.53 C ANISOU 249 CG GLU A 35 3992 4114 6153 -247 683 -137 C ATOM 250 CD GLU A 35 8.567 6.971 18.068 1.00 44.62 C ANISOU 250 CD GLU A 35 4931 4919 7103 -245 926 -102 C ATOM 251 OE1 GLU A 35 8.496 7.669 19.106 1.00 48.36 O ANISOU 251 OE1 GLU A 35 5497 5368 7509 -210 1040 -68 O ATOM 252 OE2 GLU A 35 8.345 5.740 18.051 1.00 45.42 O ANISOU 252 OE2 GLU A 35 4995 4962 7301 -272 1007 -108 O ATOM 253 N ASN A 36 9.604 4.718 15.575 1.00 29.33 N ANISOU 253 N ASN A 36 2915 3059 5169 -303 636 -153 N ATOM 254 CA ASN A 36 8.960 3.971 14.534 1.00 31.30 C ANISOU 254 CA ASN A 36 3042 3261 5591 -326 542 -224 C ATOM 255 C ASN A 36 7.505 4.483 14.516 1.00 33.01 C ANISOU 255 C ASN A 36 3094 3382 6067 -331 554 -296 C ATOM 256 O ASN A 36 6.842 4.402 15.544 1.00 34.44 O ANISOU 256 O ASN A 36 3234 3482 6369 -342 753 -283 O ATOM 257 CB ASN A 36 9.052 2.490 14.892 1.00 33.73 C ANISOU 257 CB ASN A 36 3359 3513 5944 -352 659 -206 C ATOM 258 CG ASN A 36 8.090 1.643 14.166 1.00 38.80 C ANISOU 258 CG ASN A 36 3849 4060 6834 -380 612 -285 C ATOM 259 OD1 ASN A 36 7.472 0.762 14.762 1.00 41.24 O ANISOU 259 OD1 ASN A 36 4095 4264 7308 -412 773 -289 O ATOM 260 ND2 ASN A 36 7.924 1.903 12.867 1.00 39.50 N ANISOU 260 ND2 ASN A 36 3885 4166 6959 -365 388 -354 N ATOM 261 N ILE A 37 7.021 4.997 13.364 1.00 33.13 N ANISOU 261 N ILE A 37 3027 3393 6168 -315 348 -374 N ATOM 262 CA ILE A 37 5.678 5.595 13.245 1.00 34.69 C ANISOU 262 CA ILE A 37 3058 3498 6624 -308 315 -457 C ATOM 263 C ILE A 37 4.644 4.823 12.434 1.00 37.46 C ANISOU 263 C ILE A 37 3233 3731 7269 -320 203 -567 C ATOM 264 O ILE A 37 3.579 5.386 12.128 1.00 38.46 O ANISOU 264 O ILE A 37 3212 3776 7623 -303 114 -656 O ATOM 265 CB ILE A 37 5.799 7.005 12.639 1.00 34.22 C ANISOU 265 CB ILE A 37 3047 3502 6453 -264 140 -475 C ATOM 266 CG1 ILE A 37 6.299 6.920 11.180 1.00 35.09 C ANISOU 266 CG1 ILE A 37 3233 3651 6449 -234 -107 -510 C ATOM 267 CG2 ILE A 37 6.660 7.891 13.507 1.00 34.00 C ANISOU 267 CG2 ILE A 37 3162 3567 6190 -253 242 -382 C ATOM 268 CD1 ILE A 37 6.270 8.136 10.428 1.00 37.24 C ANISOU 268 CD1 ILE A 37 3560 3949 6640 -186 -283 -540 C ATOM 269 N GLY A 38 4.960 3.598 12.037 1.00 38.08 N ANISOU 269 N GLY A 38 3327 3793 7350 -341 181 -571 N ATOM 270 CA GLY A 38 4.033 2.851 11.195 1.00 39.03 C ANISOU 270 CA GLY A 38 3289 3791 7749 -347 39 -685 C ATOM 271 C GLY A 38 4.408 2.974 9.735 1.00 38.97 C ANISOU 271 C GLY A 38 3373 3820 7615 -293 -261 -738 C ATOM 272 O GLY A 38 5.353 3.702 9.378 1.00 39.20 O ANISOU 272 O GLY A 38 3577 3965 7352 -257 -332 -682 O ATOM 273 N SER A 39 3.735 2.184 8.881 1.00 38.00 N ANISOU 273 N SER A 39 3150 3584 7703 -284 -430 -844 N ATOM 274 CA SER A 39 4.101 2.057 7.459 1.00 37.52 C ANISOU 274 CA SER A 39 3219 3531 7507 -219 -712 -897 C ATOM 275 C SER A 39 5.600 1.713 7.287 1.00 34.06 C ANISOU 275 C SER A 39 3008 3227 6708 -214 -659 -788 C ATOM 276 O SER A 39 6.205 2.057 6.279 1.00 35.10 O ANISOU 276 O SER A 39 3309 3403 6626 -153 -824 -790 O ATOM 277 CB SER A 39 3.744 3.303 6.661 1.00 41.45 C ANISOU 277 CB SER A 39 3761 4020 7970 -144 -941 -961 C ATOM 278 OG SER A 39 4.035 3.155 5.279 1.00 45.80 O ANISOU 278 OG SER A 39 4472 4549 8381 -67 -1205 -1015 O ATOM 279 N GLY A 40 6.189 1.093 8.307 1.00 31.48 N ANISOU 279 N GLY A 40 2690 2953 6318 -272 -417 -695 N ATOM 280 CA GLY A 40 7.583 0.691 8.313 1.00 28.40 C ANISOU 280 CA GLY A 40 2479 2676 5636 -272 -349 -599 C ATOM 281 C GLY A 40 8.574 1.830 8.374 1.00 25.65 C ANISOU 281 C GLY A 40 2277 2454 5016 -246 -332 -521 C ATOM 282 O GLY A 40 9.744 1.618 8.089 1.00 25.43 O ANISOU 282 O GLY A 40 2390 2507 4764 -233 -321 -460 O ATOM 283 N LEU A 41 8.125 3.053 8.702 1.00 23.69 N ANISOU 283 N LEU A 41 1989 2214 4799 -237 -332 -525 N ATOM 284 CA LEU A 41 9.027 4.206 8.730 1.00 24.30 C ANISOU 284 CA LEU A 41 2198 2397 4638 -215 -326 -457 C ATOM 285 C LEU A 41 9.722 4.288 10.063 1.00 24.68 C ANISOU 285 C LEU A 41 2271 2515 4593 -253 -115 -362 C ATOM 286 O LEU A 41 9.068 4.362 11.110 1.00 25.97 O ANISOU 286 O LEU A 41 2344 2637 4886 -279 20 -357 O ATOM 287 CB LEU A 41 8.248 5.503 8.439 1.00 25.60 C ANISOU 287 CB LEU A 41 2327 2533 4868 -181 -440 -509 C ATOM 288 CG LEU A 41 7.486 5.492 7.112 1.00 28.44 C ANISOU 288 CG LEU A 41 2683 2800 5323 -124 -689 -619 C ATOM 289 CD1 LEU A 41 6.651 6.739 6.937 1.00 29.77 C ANISOU 289 CD1 LEU A 41 2808 2927 5577 -85 -805 -677 C ATOM 290 CD2 LEU A 41 8.417 5.347 5.943 1.00 29.64 C ANISOU 290 CD2 LEU A 41 3037 2986 5241 -74 -805 -602 C ATOM 291 N VAL A 42 11.061 4.337 10.040 1.00 22.25 N ANISOU 291 N VAL A 42 2095 2299 4061 -248 -86 -289 N ATOM 292 CA VAL A 42 11.834 4.383 11.266 1.00 21.69 C ANISOU 292 CA VAL A 42 2068 2282 3892 -268 73 -209 C ATOM 293 C VAL A 42 12.787 5.565 11.168 1.00 21.44 C ANISOU 293 C VAL A 42 2131 2331 3684 -250 38 -163 C ATOM 294 O VAL A 42 13.390 5.761 10.117 1.00 21.77 O ANISOU 294 O VAL A 42 2242 2402 3626 -230 -56 -164 O ATOM 295 CB VAL A 42 12.611 3.060 11.520 1.00 23.11 C ANISOU 295 CB VAL A 42 2293 2473 4015 -281 148 -173 C ATOM 296 CG1 VAL A 42 13.246 3.075 12.900 1.00 23.62 C ANISOU 296 CG1 VAL A 42 2414 2564 3996 -287 291 -105 C ATOM 297 CG2 VAL A 42 11.700 1.836 11.374 1.00 24.45 C ANISOU 297 CG2 VAL A 42 2373 2552 4366 -301 163 -225 C ATOM 298 N THR A 43 12.878 6.383 12.219 1.00 19.99 N ANISOU 298 N THR A 43 1958 2168 3470 -253 117 -125 N ATOM 299 CA THR A 43 13.748 7.562 12.194 1.00 19.67 C ANISOU 299 CA THR A 43 1992 2189 3291 -241 81 -86 C ATOM 300 C THR A 43 14.777 7.486 13.278 1.00 19.29 C ANISOU 300 C THR A 43 2005 2176 3147 -243 166 -27 C ATOM 301 O THR A 43 14.453 7.155 14.426 1.00 20.31 O ANISOU 301 O THR A 43 2137 2272 3306 -241 267 -13 O ATOM 302 CB THR A 43 12.917 8.851 12.374 1.00 22.15 C ANISOU 302 CB THR A 43 2275 2485 3655 -229 50 -109 C ATOM 303 OG1 THR A 43 11.957 8.919 11.318 1.00 24.24 O ANISOU 303 OG1 THR A 43 2487 2702 4019 -215 -64 -177 O ATOM 304 CG2 THR A 43 13.785 10.102 12.365 1.00 22.87 C ANISOU 304 CG2 THR A 43 2444 2629 3616 -221 13 -70 C ATOM 305 N VAL A 44 16.028 7.781 12.929 1.00 18.41 N ANISOU 305 N VAL A 44 1951 2116 2926 -240 129 5 N ATOM 306 CA VAL A 44 17.097 7.882 13.920 1.00 19.32 C ANISOU 306 CA VAL A 44 2119 2255 2968 -233 167 47 C ATOM 307 C VAL A 44 17.527 9.342 13.962 1.00 18.94 C ANISOU 307 C VAL A 44 2093 2229 2875 -230 118 61 C ATOM 308 O VAL A 44 17.509 10.037 12.928 1.00 18.32 O ANISOU 308 O VAL A 44 2011 2163 2788 -237 63 53 O ATOM 309 CB VAL A 44 18.293 6.951 13.651 1.00 21.70 C ANISOU 309 CB VAL A 44 2441 2579 3225 -232 168 64 C ATOM 310 CG1 VAL A 44 18.808 7.103 12.226 1.00 22.20 C ANISOU 310 CG1 VAL A 44 2503 2666 3265 -239 121 60 C ATOM 311 CG2 VAL A 44 19.389 7.164 14.686 1.00 23.37 C ANISOU 311 CG2 VAL A 44 2698 2797 3386 -214 169 91 C ATOM 312 N MET A 45 17.811 9.847 15.167 1.00 18.55 N ANISOU 312 N MET A 45 2084 2169 2794 -213 135 79 N ATOM 313 CA MET A 45 18.182 11.260 15.333 1.00 19.35 C ANISOU 313 CA MET A 45 2207 2281 2865 -209 82 89 C ATOM 314 C MET A 45 19.465 11.379 16.099 1.00 19.82 C ANISOU 314 C MET A 45 2307 2338 2884 -194 52 107 C ATOM 315 O MET A 45 19.652 10.678 17.096 1.00 20.32 O ANISOU 315 O MET A 45 2423 2375 2923 -163 75 111 O ATOM 316 CB MET A 45 17.106 12.014 16.128 1.00 20.65 C ANISOU 316 CB MET A 45 2389 2415 3044 -190 107 79 C ATOM 317 CG MET A 45 15.705 11.717 15.671 1.00 22.78 C ANISOU 317 CG MET A 45 2595 2661 3399 -197 142 47 C ATOM 318 SD MET A 45 14.520 12.744 16.600 1.00 30.43 S ANISOU 318 SD MET A 45 3570 3585 4407 -170 187 34 S ATOM 319 CE MET A 45 12.994 12.017 16.067 1.00 28.68 C ANISOU 319 CE MET A 45 3232 3315 4348 -182 235 -17 C ATOM 320 N VAL A 46 20.332 12.297 15.683 1.00 18.60 N ANISOU 320 N VAL A 46 2138 2197 2734 -210 -4 115 N ATOM 321 CA VAL A 46 21.589 12.559 16.365 1.00 19.07 C ANISOU 321 CA VAL A 46 2209 2237 2799 -196 -60 118 C ATOM 322 C VAL A 46 21.711 14.045 16.702 1.00 20.33 C ANISOU 322 C VAL A 46 2385 2378 2961 -196 -121 117 C ATOM 323 O VAL A 46 21.078 14.888 16.069 1.00 19.95 O ANISOU 323 O VAL A 46 2327 2341 2911 -217 -113 121 O ATOM 324 CB VAL A 46 22.813 12.078 15.551 1.00 21.08 C ANISOU 324 CB VAL A 46 2401 2503 3106 -220 -60 121 C ATOM 325 CG1 VAL A 46 22.729 10.569 15.268 1.00 22.17 C ANISOU 325 CG1 VAL A 46 2534 2656 3234 -214 -9 119 C ATOM 326 CG2 VAL A 46 22.967 12.887 14.263 1.00 21.76 C ANISOU 326 CG2 VAL A 46 2451 2599 3216 -261 -36 134 C ATOM 327 N LYS A 47 22.520 14.360 17.701 1.00 21.15 N ANISOU 327 N LYS A 47 2522 2442 3071 -165 -197 106 N ATOM 328 CA LYS A 47 22.779 15.758 18.069 1.00 22.79 C ANISOU 328 CA LYS A 47 2745 2620 3295 -163 -273 100 C ATOM 329 C LYS A 47 24.264 15.949 18.209 1.00 23.28 C ANISOU 329 C LYS A 47 2753 2643 3451 -168 -361 82 C ATOM 330 O LYS A 47 25.000 15.022 18.550 1.00 23.99 O ANISOU 330 O LYS A 47 2832 2715 3569 -144 -391 66 O ATOM 331 CB LYS A 47 22.076 16.147 19.372 1.00 26.70 C ANISOU 331 CB LYS A 47 3358 3076 3709 -102 -302 91 C ATOM 332 CG LYS A 47 20.635 16.589 19.180 1.00 33.52 C ANISOU 332 CG LYS A 47 4242 3961 4533 -105 -226 101 C ATOM 333 CD LYS A 47 20.105 17.339 20.403 1.00 40.43 C ANISOU 333 CD LYS A 47 5233 4785 5342 -45 -249 93 C ATOM 334 CE LYS A 47 18.760 17.991 20.157 1.00 45.38 C ANISOU 334 CE LYS A 47 5853 5425 5964 -50 -183 95 C ATOM 335 NZ LYS A 47 18.880 19.433 19.778 1.00 47.91 N ANISOU 335 NZ LYS A 47 6154 5746 6301 -70 -258 91 N ATOM 336 N GLY A 48 24.710 17.159 17.944 1.00 23.10 N ANISOU 336 N GLY A 48 2689 2595 3494 -199 -404 80 N ATOM 337 CA GLY A 48 26.116 17.521 18.051 1.00 23.92 C ANISOU 337 CA GLY A 48 2711 2641 3738 -213 -487 55 C ATOM 338 C GLY A 48 26.374 18.878 17.426 1.00 24.15 C ANISOU 338 C GLY A 48 2687 2643 3846 -267 -480 65 C ATOM 339 O GLY A 48 25.434 19.602 17.080 1.00 24.67 O ANISOU 339 O GLY A 48 2806 2735 3831 -280 -439 89 O ATOM 340 N ASP A 49 27.655 19.209 17.213 1.00 24.81 N ANISOU 340 N ASP A 49 2658 2664 4103 -301 -511 47 N ATOM 341 CA ASP A 49 28.004 20.466 16.544 1.00 24.27 C ANISOU 341 CA ASP A 49 2535 2552 4134 -362 -476 62 C ATOM 342 C ASP A 49 27.541 20.368 15.080 1.00 23.73 C ANISOU 342 C ASP A 49 2477 2530 4008 -409 -298 115 C ATOM 343 O ASP A 49 27.466 19.263 14.536 1.00 24.55 O ANISOU 343 O ASP A 49 2575 2679 4073 -405 -215 128 O ATOM 344 CB ASP A 49 29.535 20.731 16.596 1.00 26.07 C ANISOU 344 CB ASP A 49 2614 2683 4608 -394 -524 25 C ATOM 345 CG ASP A 49 30.105 20.910 18.001 1.00 33.32 C ANISOU 345 CG ASP A 49 3529 3528 5604 -335 -743 -44 C ATOM 346 OD1 ASP A 49 29.307 21.093 18.949 1.00 34.49 O ANISOU 346 OD1 ASP A 49 3819 3691 5594 -271 -845 -54 O ATOM 347 OD2 ASP A 49 31.360 20.904 18.145 1.00 37.56 O ANISOU 347 OD2 ASP A 49 3927 3976 6369 -348 -814 -92 O ATOM 348 N VAL A 50 27.236 21.497 14.441 1.00 23.49 N ANISOU 348 N VAL A 50 2481 2480 3965 -445 -248 144 N ATOM 349 CA VAL A 50 26.750 21.513 13.065 1.00 23.37 C ANISOU 349 CA VAL A 50 2523 2486 3870 -470 -103 190 C ATOM 350 C VAL A 50 27.599 20.714 12.076 1.00 23.17 C ANISOU 350 C VAL A 50 2441 2443 3921 -498 38 209 C ATOM 351 O VAL A 50 27.059 19.864 11.372 1.00 22.96 O ANISOU 351 O VAL A 50 2475 2466 3784 -479 108 227 O ATOM 352 CB VAL A 50 26.529 22.951 12.540 1.00 25.00 C ANISOU 352 CB VAL A 50 2788 2644 4068 -500 -75 215 C ATOM 353 CG1 VAL A 50 25.945 22.909 11.134 1.00 25.40 C ANISOU 353 CG1 VAL A 50 2945 2703 4002 -502 52 258 C ATOM 354 CG2 VAL A 50 25.600 23.719 13.474 1.00 26.08 C ANISOU 354 CG2 VAL A 50 2990 2801 4119 -464 -207 195 C ATOM 355 N GLY A 51 28.916 20.951 12.046 1.00 23.56 N ANISOU 355 N GLY A 51 2369 2412 4172 -539 78 201 N ATOM 356 CA GLY A 51 29.800 20.240 11.125 1.00 23.90 C ANISOU 356 CA GLY A 51 2348 2421 4313 -563 238 219 C ATOM 357 C GLY A 51 29.745 18.743 11.333 1.00 23.05 C ANISOU 357 C GLY A 51 2221 2380 4155 -522 216 199 C ATOM 358 O GLY A 51 29.568 17.979 10.376 1.00 24.03 O ANISOU 358 O GLY A 51 2402 2530 4199 -514 339 227 O ATOM 359 N ALA A 52 29.777 18.336 12.604 1.00 22.05 N ANISOU 359 N ALA A 52 2050 2277 4050 -487 51 152 N ATOM 360 CA ALA A 52 29.698 16.924 12.984 1.00 22.63 C ANISOU 360 CA ALA A 52 2121 2405 4072 -442 13 131 C ATOM 361 C ALA A 52 28.384 16.313 12.533 1.00 22.34 C ANISOU 361 C ALA A 52 2213 2453 3821 -417 55 159 C ATOM 362 O ALA A 52 28.393 15.227 11.961 1.00 22.46 O ANISOU 362 O ALA A 52 2236 2498 3800 -405 128 167 O ATOM 363 CB ALA A 52 29.847 16.774 14.497 1.00 23.65 C ANISOU 363 CB ALA A 52 2234 2524 4229 -394 -179 78 C ATOM 364 N VAL A 53 27.254 17.010 12.756 1.00 20.82 N ANISOU 364 N VAL A 53 2115 2290 3505 -406 5 168 N ATOM 365 CA VAL A 53 25.955 16.471 12.387 1.00 20.34 C ANISOU 365 CA VAL A 53 2152 2293 3285 -381 24 180 C ATOM 366 C VAL A 53 25.856 16.333 10.879 1.00 20.52 C ANISOU 366 C VAL A 53 2226 2309 3260 -395 148 211 C ATOM 367 O VAL A 53 25.366 15.320 10.409 1.00 21.31 O ANISOU 367 O VAL A 53 2366 2444 3288 -373 176 210 O ATOM 368 CB VAL A 53 24.806 17.303 12.980 1.00 20.94 C ANISOU 368 CB VAL A 53 2297 2385 3275 -362 -53 174 C ATOM 369 CG1 VAL A 53 23.471 16.884 12.398 1.00 21.99 C ANISOU 369 CG1 VAL A 53 2502 2560 3291 -342 -30 178 C ATOM 370 CG2 VAL A 53 24.790 17.194 14.495 1.00 20.84 C ANISOU 370 CG2 VAL A 53 2281 2370 3268 -326 -161 145 C ATOM 371 N LYS A 54 26.342 17.331 10.117 1.00 20.70 N ANISOU 371 N LYS A 54 2267 2274 3324 -427 224 238 N ATOM 372 CA LYS A 54 26.285 17.230 8.650 1.00 21.56 C ANISOU 372 CA LYS A 54 2476 2355 3363 -425 354 271 C ATOM 373 C LYS A 54 27.093 16.014 8.155 1.00 21.87 C ANISOU 373 C LYS A 54 2473 2389 3447 -420 454 274 C ATOM 374 O LYS A 54 26.602 15.220 7.340 1.00 22.48 O ANISOU 374 O LYS A 54 2645 2483 3415 -387 493 280 O ATOM 375 CB LYS A 54 26.841 18.504 8.005 1.00 22.16 C ANISOU 375 CB LYS A 54 2588 2345 3486 -460 449 305 C ATOM 376 CG LYS A 54 25.930 19.715 8.159 1.00 26.16 C ANISOU 376 CG LYS A 54 3177 2848 3914 -455 365 307 C ATOM 377 CD LYS A 54 26.555 20.886 7.394 1.00 30.81 C ANISOU 377 CD LYS A 54 3823 3337 4547 -489 486 348 C ATOM 378 CE LYS A 54 25.696 22.114 7.440 1.00 35.99 C ANISOU 378 CE LYS A 54 4576 3980 5118 -480 407 352 C ATOM 379 NZ LYS A 54 26.351 23.249 6.730 1.00 39.81 N ANISOU 379 NZ LYS A 54 5124 4352 5648 -517 537 396 N ATOM 380 N ALA A 55 28.305 15.831 8.692 1.00 21.56 N ANISOU 380 N ALA A 55 2291 2320 3579 -446 476 262 N ATOM 381 CA ALA A 55 29.134 14.689 8.313 1.00 22.25 C ANISOU 381 CA ALA A 55 2321 2399 3734 -438 567 258 C ATOM 382 C ALA A 55 28.441 13.360 8.691 1.00 22.25 C ANISOU 382 C ALA A 55 2345 2479 3632 -395 482 234 C ATOM 383 O ALA A 55 28.450 12.395 7.919 1.00 23.01 O ANISOU 383 O ALA A 55 2489 2581 3671 -372 559 241 O ATOM 384 CB ALA A 55 30.478 14.792 9.022 1.00 23.12 C ANISOU 384 CB ALA A 55 2249 2455 4078 -466 559 231 C ATOM 385 N SER A 56 27.819 13.339 9.877 1.00 20.30 N ANISOU 385 N SER A 56 2078 2278 3357 -382 333 206 N ATOM 386 CA ASER A 56 27.136 12.147 10.374 0.50 20.34 C ANISOU 386 CA ASER A 56 2107 2341 3282 -346 267 186 C ATOM 387 CA BSER A 56 27.135 12.163 10.389 0.50 19.93 C ANISOU 387 CA BSER A 56 2054 2288 3230 -346 266 185 C ATOM 388 C SER A 56 25.957 11.759 9.488 1.00 20.05 C ANISOU 388 C SER A 56 2183 2333 3102 -327 291 196 C ATOM 389 O SER A 56 25.815 10.585 9.146 1.00 20.45 O ANISOU 389 O SER A 56 2253 2402 3114 -305 313 188 O ATOM 390 CB ASER A 56 26.692 12.335 11.820 0.50 21.91 C ANISOU 390 CB ASER A 56 2292 2559 3473 -329 135 160 C ATOM 391 CB BSER A 56 26.688 12.423 11.822 0.50 20.32 C ANISOU 391 CB BSER A 56 2092 2357 3274 -331 133 161 C ATOM 392 OG ASER A 56 25.487 13.082 11.899 0.50 22.65 O ANISOU 392 OG ASER A 56 2460 2672 3474 -328 98 167 O ATOM 393 OG BSER A 56 26.050 11.303 12.406 0.50 18.92 O ANISOU 393 OG BSER A 56 1945 2216 3028 -297 94 146 O ATOM 394 N VAL A 57 25.130 12.733 9.085 1.00 20.29 N ANISOU 394 N VAL A 57 2290 2356 3063 -330 274 206 N ATOM 395 CA VAL A 57 23.978 12.443 8.218 1.00 21.34 C ANISOU 395 CA VAL A 57 2531 2496 3080 -301 261 200 C ATOM 396 C VAL A 57 24.433 11.975 6.825 1.00 22.59 C ANISOU 396 C VAL A 57 2777 2615 3190 -282 364 218 C ATOM 397 O VAL A 57 23.899 10.999 6.314 1.00 23.09 O ANISOU 397 O VAL A 57 2895 2687 3190 -250 346 200 O ATOM 398 CB VAL A 57 23.036 13.649 8.136 1.00 21.76 C ANISOU 398 CB VAL A 57 2647 2539 3084 -298 200 198 C ATOM 399 CG1 VAL A 57 21.921 13.406 7.120 1.00 22.48 C ANISOU 399 CG1 VAL A 57 2851 2614 3077 -257 160 179 C ATOM 400 CG2 VAL A 57 22.455 13.957 9.505 1.00 21.91 C ANISOU 400 CG2 VAL A 57 2598 2590 3136 -303 112 178 C ATOM 401 N ASP A 58 25.469 12.619 6.242 1.00 23.38 N ANISOU 401 N ASP A 58 2892 2660 3330 -301 482 252 N ATOM 402 CA ASP A 58 25.993 12.167 4.934 1.00 24.55 C ANISOU 402 CA ASP A 58 3148 2754 3426 -274 617 275 C ATOM 403 C ASP A 58 26.465 10.716 4.987 1.00 25.21 C ANISOU 403 C ASP A 58 3174 2864 3541 -259 646 260 C ATOM 404 O ASP A 58 26.156 9.926 4.095 1.00 26.11 O ANISOU 404 O ASP A 58 3403 2962 3556 -214 669 256 O ATOM 405 CB ASP A 58 27.136 13.068 4.449 1.00 28.44 C ANISOU 405 CB ASP A 58 3643 3167 3997 -304 780 317 C ATOM 406 CG ASP A 58 26.703 14.413 3.909 1.00 37.50 C ANISOU 406 CG ASP A 58 4919 4258 5069 -304 795 343 C ATOM 407 OD1 ASP A 58 25.475 14.646 3.792 1.00 40.68 O ANISOU 407 OD1 ASP A 58 5424 4684 5349 -270 666 324 O ATOM 408 OD2 ASP A 58 27.587 15.244 3.613 1.00 41.49 O ANISOU 408 OD2 ASP A 58 5421 4689 5656 -337 935 379 O ATOM 409 N SER A 59 27.165 10.351 6.063 1.00 24.90 N ANISOU 409 N SER A 59 2970 2856 3634 -287 622 246 N ATOM 410 CA SER A 59 27.665 8.992 6.221 1.00 25.55 C ANISOU 410 CA SER A 59 2994 2960 3755 -270 638 229 C ATOM 411 C SER A 59 26.547 8.000 6.451 1.00 24.14 C ANISOU 411 C SER A 59 2859 2832 3481 -241 529 201 C ATOM 412 O SER A 59 26.599 6.888 5.937 1.00 24.21 O ANISOU 412 O SER A 59 2907 2841 3452 -212 559 192 O ATOM 413 CB SER A 59 28.651 8.911 7.369 1.00 29.12 C ANISOU 413 CB SER A 59 3277 3418 4371 -294 606 210 C ATOM 414 OG SER A 59 29.280 7.641 7.384 1.00 34.27 O ANISOU 414 OG SER A 59 3879 4075 5068 -271 635 194 O ATOM 415 N GLY A 60 25.553 8.397 7.228 1.00 23.29 N ANISOU 415 N GLY A 60 2741 2758 3349 -250 415 185 N ATOM 416 CA GLY A 60 24.413 7.530 7.504 1.00 23.96 C ANISOU 416 CA GLY A 60 2848 2875 3382 -231 330 156 C ATOM 417 C GLY A 60 23.615 7.243 6.246 1.00 24.68 C ANISOU 417 C GLY A 60 3064 2938 3375 -197 321 145 C ATOM 418 O GLY A 60 23.132 6.123 6.048 1.00 24.42 O ANISOU 418 O GLY A 60 3051 2908 3320 -174 288 120 O ATOM 419 N LEU A 61 23.446 8.261 5.404 1.00 25.70 N ANISOU 419 N LEU A 61 3292 3028 3445 -186 336 159 N ATOM 420 CA LEU A 61 22.715 8.148 4.143 1.00 28.40 C ANISOU 420 CA LEU A 61 3795 3320 3677 -133 302 142 C ATOM 421 C LEU A 61 23.404 7.148 3.224 1.00 30.57 C ANISOU 421 C LEU A 61 4153 3562 3901 -96 388 149 C ATOM 422 O LEU A 61 22.755 6.238 2.710 1.00 31.02 O ANISOU 422 O LEU A 61 4279 3601 3906 -54 318 114 O ATOM 423 CB LEU A 61 22.676 9.520 3.449 1.00 29.57 C ANISOU 423 CB LEU A 61 4060 3416 3758 -121 324 165 C ATOM 424 CG LEU A 61 21.608 10.449 3.914 1.00 32.74 C ANISOU 424 CG LEU A 61 4444 3829 4169 -128 204 142 C ATOM 425 CD1 LEU A 61 21.832 11.846 3.333 1.00 33.93 C ANISOU 425 CD1 LEU A 61 4706 3925 4260 -122 247 174 C ATOM 426 CD2 LEU A 61 20.247 9.912 3.514 1.00 33.67 C ANISOU 426 CD2 LEU A 61 4614 3925 4253 -81 57 82 C ATOM 427 N GLU A 62 24.722 7.283 3.041 1.00 31.31 N ANISOU 427 N GLU A 62 4231 3638 4029 -109 541 190 N ATOM 428 CA GLU A 62 25.483 6.388 2.174 1.00 33.31 C ANISOU 428 CA GLU A 62 4563 3852 4243 -70 655 201 C ATOM 429 C GLU A 62 25.362 4.938 2.642 1.00 34.16 C ANISOU 429 C GLU A 62 4591 4004 4384 -64 596 168 C ATOM 430 O GLU A 62 25.034 4.061 1.846 1.00 35.47 O ANISOU 430 O GLU A 62 4873 4138 4464 -12 575 148 O ATOM 431 CB GLU A 62 26.956 6.827 2.118 1.00 36.84 C ANISOU 431 CB GLU A 62 4948 4267 4784 -98 844 245 C ATOM 432 CG GLU A 62 27.734 6.192 0.980 1.00 43.00 C ANISOU 432 CG GLU A 62 5850 4976 5510 -47 1010 266 C ATOM 433 N SER A 63 25.524 4.705 3.946 1.00 33.17 N ANISOU 433 N SER A 63 4291 3940 4371 -111 551 160 N ATOM 434 CA SER A 63 25.441 3.366 4.512 1.00 33.18 C ANISOU 434 CA SER A 63 4226 3976 4405 -106 503 134 C ATOM 435 C SER A 63 24.031 2.777 4.405 1.00 32.35 C ANISOU 435 C SER A 63 4173 3870 4247 -88 377 94 C ATOM 436 O SER A 63 23.891 1.614 4.034 1.00 32.84 O ANISOU 436 O SER A 63 4274 3918 4285 -59 360 72 O ATOM 437 CB SER A 63 25.903 3.389 5.965 1.00 35.65 C ANISOU 437 CB SER A 63 4382 4334 4831 -146 477 134 C ATOM 438 OG SER A 63 25.615 2.186 6.657 1.00 40.72 O ANISOU 438 OG SER A 63 4985 4999 5489 -140 421 111 O ATOM 439 N ALA A 64 22.991 3.575 4.713 1.00 30.37 N ANISOU 439 N ALA A 64 3916 3624 3999 -105 288 80 N ATOM 440 CA ALA A 64 21.620 3.081 4.660 1.00 30.02 C ANISOU 440 CA ALA A 64 3886 3562 3957 -92 168 32 C ATOM 441 C ALA A 64 21.167 2.818 3.230 1.00 30.26 C ANISOU 441 C ALA A 64 4077 3526 3894 -30 113 1 C ATOM 442 O ALA A 64 20.551 1.788 2.974 1.00 29.76 O ANISOU 442 O ALA A 64 4029 3435 3843 -7 38 -42 O ATOM 443 CB ALA A 64 20.674 4.050 5.345 1.00 29.93 C ANISOU 443 CB ALA A 64 3816 3563 3995 -120 99 20 C ATOM 444 N GLN A 65 21.528 3.710 2.285 1.00 30.35 N ANISOU 444 N GLN A 65 4226 3497 3809 5 154 24 N ATOM 445 CA GLN A 65 21.132 3.559 0.883 1.00 31.56 C ANISOU 445 CA GLN A 65 4588 3565 3840 87 94 -5 C ATOM 446 C GLN A 65 21.625 2.279 0.237 1.00 32.39 C ANISOU 446 C GLN A 65 4775 3641 3892 132 134 -13 C ATOM 447 O GLN A 65 21.004 1.815 -0.726 1.00 33.39 O ANISOU 447 O GLN A 65 5058 3691 3936 204 28 -60 O ATOM 448 CB GLN A 65 21.542 4.776 0.049 1.00 33.13 C ANISOU 448 CB GLN A 65 4951 3711 3926 121 165 33 C ATOM 449 CG GLN A 65 20.621 5.958 0.259 1.00 36.00 C ANISOU 449 CG GLN A 65 5308 4066 4302 112 54 14 C ATOM 450 CD GLN A 65 21.038 7.150 -0.558 1.00 41.67 C ANISOU 450 CD GLN A 65 6208 4721 4902 148 131 55 C ATOM 451 OE1 GLN A 65 22.227 7.375 -0.816 1.00 42.73 O ANISOU 451 OE1 GLN A 65 6385 4843 5007 138 320 116 O ATOM 452 NE2 GLN A 65 20.064 7.939 -0.976 1.00 43.19 N ANISOU 452 NE2 GLN A 65 6509 4861 5041 192 -10 20 N ATOM 453 N HIS A 66 22.713 1.695 0.752 1.00 32.17 N ANISOU 453 N HIS A 66 4647 3661 3915 98 268 24 N ATOM 454 CA HIS A 66 23.223 0.444 0.213 1.00 33.90 C ANISOU 454 CA HIS A 66 4932 3856 4094 141 313 16 C ATOM 455 C HIS A 66 22.505 -0.793 0.706 1.00 33.22 C ANISOU 455 C HIS A 66 4761 3785 4075 130 196 -33 C ATOM 456 O HIS A 66 22.780 -1.874 0.196 1.00 34.08 O ANISOU 456 O HIS A 66 4940 3866 4145 172 207 -48 O ATOM 457 CB HIS A 66 24.726 0.301 0.452 1.00 36.57 C ANISOU 457 CB HIS A 66 5201 4222 4472 121 503 67 C ATOM 458 CG HIS A 66 25.517 1.058 -0.563 1.00 41.67 C ANISOU 458 CG HIS A 66 5999 4802 5030 162 658 110 C ATOM 459 ND1 HIS A 66 25.724 0.552 -1.833 1.00 43.73 N ANISOU 459 ND1 HIS A 66 6481 4978 5155 249 720 109 N ATOM 460 CD2 HIS A 66 26.053 2.298 -0.491 1.00 43.43 C ANISOU 460 CD2 HIS A 66 6201 5018 5282 130 765 154 C ATOM 461 CE1 HIS A 66 26.405 1.482 -2.479 1.00 44.58 C ANISOU 461 CE1 HIS A 66 6702 5027 5210 268 885 157 C ATOM 462 NE2 HIS A 66 26.625 2.551 -1.712 1.00 44.81 N ANISOU 462 NE2 HIS A 66 6581 5100 5345 193 918 185 N ATOM 463 N ILE A 67 21.647 -0.668 1.742 1.00 31.85 N ANISOU 463 N ILE A 67 4438 3652 4013 73 107 -55 N ATOM 464 CA ILE A 67 20.942 -1.849 2.227 1.00 31.53 C ANISOU 464 CA ILE A 67 4318 3606 4057 57 25 -98 C ATOM 465 C ILE A 67 19.426 -1.669 2.295 1.00 29.20 C ANISOU 465 C ILE A 67 3986 3268 3840 49 -130 -158 C ATOM 466 O ILE A 67 18.720 -2.667 2.419 1.00 28.85 O ANISOU 466 O ILE A 67 3896 3187 3877 44 -205 -205 O ATOM 467 CB ILE A 67 21.505 -2.384 3.548 1.00 33.27 C ANISOU 467 CB ILE A 67 4386 3891 4364 0 106 -68 C ATOM 468 CG1 ILE A 67 21.256 -1.419 4.672 1.00 34.05 C ANISOU 468 CG1 ILE A 67 4371 4035 4532 -55 116 -46 C ATOM 469 CG2 ILE A 67 22.983 -2.816 3.471 1.00 33.75 C ANISOU 469 CG2 ILE A 67 4458 3977 4387 16 231 -28 C ATOM 470 CD1 ILE A 67 20.967 -2.179 5.888 1.00 35.38 C ANISOU 470 CD1 ILE A 67 4434 4219 4790 -94 123 -49 C ATOM 471 N GLY A 68 18.924 -0.439 2.169 1.00 28.19 N ANISOU 471 N GLY A 68 3876 3132 3704 50 -178 -163 N ATOM 472 CA GLY A 68 17.488 -0.224 2.206 1.00 28.06 C ANISOU 472 CA GLY A 68 3808 3064 3789 49 -330 -230 C ATOM 473 C GLY A 68 17.049 1.085 1.612 1.00 28.50 C ANISOU 473 C GLY A 68 3952 3087 3789 85 -409 -243 C ATOM 474 O GLY A 68 17.852 1.828 1.042 1.00 29.01 O ANISOU 474 O GLY A 68 4148 3158 3716 115 -339 -197 O ATOM 475 N GLU A 69 15.786 1.394 1.808 1.00 28.39 N ANISOU 475 N GLU A 69 3857 3031 3900 80 -541 -306 N ATOM 476 CA GLU A 69 15.215 2.612 1.274 1.00 28.65 C ANISOU 476 CA GLU A 69 3969 3021 3897 122 -647 -333 C ATOM 477 C GLU A 69 15.289 3.750 2.284 1.00 28.43 C ANISOU 477 C GLU A 69 3828 3065 3909 61 -557 -284 C ATOM 478 O GLU A 69 14.734 3.637 3.370 1.00 27.78 O ANISOU 478 O GLU A 69 3567 3010 3977 2 -530 -293 O ATOM 479 CB GLU A 69 13.763 2.363 0.876 1.00 32.17 C ANISOU 479 CB GLU A 69 4378 3363 4482 160 -866 -444 C ATOM 480 CG GLU A 69 13.031 3.597 0.384 1.00 39.62 C ANISOU 480 CG GLU A 69 5392 4250 5414 212 -1009 -488 C ATOM 481 CD GLU A 69 11.542 3.409 0.153 1.00 48.88 C ANISOU 481 CD GLU A 69 6477 5313 6784 246 -1239 -612 C ATOM 482 OE1 GLU A 69 11.038 2.280 0.364 1.00 50.30 O ANISOU 482 OE1 GLU A 69 6531 5452 7127 222 -1281 -665 O ATOM 483 OE2 GLU A 69 10.875 4.399 -0.229 1.00 52.07 O ANISOU 483 OE2 GLU A 69 6929 5660 7197 297 -1380 -661 O ATOM 484 N VAL A 70 15.944 4.844 1.914 1.00 28.83 N ANISOU 484 N VAL A 70 3995 3132 3826 80 -505 -235 N ATOM 485 CA VAL A 70 15.960 6.042 2.740 1.00 29.15 C ANISOU 485 CA VAL A 70 3953 3225 3898 34 -450 -198 C ATOM 486 C VAL A 70 14.799 6.881 2.254 1.00 29.77 C ANISOU 486 C VAL A 70 4074 3233 4004 82 -618 -263 C ATOM 487 O VAL A 70 14.704 7.158 1.055 1.00 31.27 O ANISOU 487 O VAL A 70 4458 3346 4078 161 -717 -290 O ATOM 488 CB VAL A 70 17.281 6.815 2.609 1.00 30.31 C ANISOU 488 CB VAL A 70 4189 3411 3916 24 -306 -115 C ATOM 489 CG1 VAL A 70 17.184 8.179 3.286 1.00 31.05 C ANISOU 489 CG1 VAL A 70 4226 3537 4035 -11 -287 -89 C ATOM 490 CG2 VAL A 70 18.434 6.000 3.171 1.00 30.62 C ANISOU 490 CG2 VAL A 70 4158 3512 3964 -20 -157 -63 C ATOM 491 N VAL A 71 13.889 7.230 3.149 1.00 28.01 N ANISOU 491 N VAL A 71 3685 3021 3937 44 -654 -295 N ATOM 492 CA VAL A 71 12.747 8.038 2.803 1.00 28.34 C ANISOU 492 CA VAL A 71 3733 2994 4042 89 -818 -365 C ATOM 493 C VAL A 71 13.191 9.492 2.735 1.00 27.89 C ANISOU 493 C VAL A 71 3773 2959 3864 97 -782 -314 C ATOM 494 O VAL A 71 12.904 10.179 1.756 1.00 28.48 O ANISOU 494 O VAL A 71 4012 2962 3847 171 -904 -345 O ATOM 495 CB VAL A 71 11.599 7.805 3.799 1.00 29.99 C ANISOU 495 CB VAL A 71 3712 3192 4490 45 -841 -420 C ATOM 496 CG1 VAL A 71 10.479 8.824 3.601 1.00 31.06 C ANISOU 496 CG1 VAL A 71 3823 3262 4717 87 -994 -491 C ATOM 497 CG2 VAL A 71 11.065 6.382 3.655 1.00 30.22 C ANISOU 497 CG2 VAL A 71 3661 3166 4655 44 -896 -482 C ATOM 498 N THR A 72 13.898 9.972 3.771 1.00 26.38 N ANISOU 498 N THR A 72 3496 2856 3670 28 -623 -240 N ATOM 499 CA THR A 72 14.384 11.360 3.756 1.00 26.37 C ANISOU 499 CA THR A 72 3577 2872 3571 27 -582 -190 C ATOM 500 C THR A 72 15.473 11.578 4.810 1.00 24.86 C ANISOU 500 C THR A 72 3304 2769 3373 -46 -409 -108 C ATOM 501 O THR A 72 15.777 10.687 5.604 1.00 25.20 O ANISOU 501 O THR A 72 3237 2859 3481 -88 -332 -93 O ATOM 502 CB THR A 72 13.217 12.372 3.842 1.00 29.66 C ANISOU 502 CB THR A 72 3965 3246 4059 56 -714 -246 C ATOM 503 OG1 THR A 72 13.699 13.642 3.369 1.00 32.16 O ANISOU 503 OG1 THR A 72 4432 3547 4240 79 -705 -205 O ATOM 504 CG2 THR A 72 12.686 12.494 5.246 1.00 30.37 C ANISOU 504 CG2 THR A 72 3850 3385 4305 -2 -660 -250 C ATOM 505 N SER A 73 16.105 12.733 4.771 1.00 23.66 N ANISOU 505 N SER A 73 3220 2625 3145 -54 -359 -60 N ATOM 506 CA SER A 73 17.148 13.098 5.702 1.00 23.56 C ANISOU 506 CA SER A 73 3136 2673 3142 -115 -230 4 C ATOM 507 C SER A 73 17.132 14.610 5.844 1.00 24.15 C ANISOU 507 C SER A 73 3247 2737 3190 -119 -242 24 C ATOM 508 O SER A 73 16.629 15.334 4.962 1.00 25.91 O ANISOU 508 O SER A 73 3596 2900 3348 -71 -321 4 O ATOM 509 CB SER A 73 18.503 12.615 5.202 1.00 25.20 C ANISOU 509 CB SER A 73 3403 2885 3287 -125 -112 55 C ATOM 510 OG SER A 73 18.816 13.239 3.966 1.00 27.70 O ANISOU 510 OG SER A 73 3900 3136 3489 -85 -95 73 O ATOM 511 N LEU A 74 17.625 15.089 6.974 1.00 21.73 N ANISOU 511 N LEU A 74 2847 2477 2934 -166 -183 56 N ATOM 512 CA LEU A 74 17.587 16.503 7.267 1.00 21.05 C ANISOU 512 CA LEU A 74 2781 2380 2836 -174 -200 71 C ATOM 513 C LEU A 74 18.580 16.849 8.354 1.00 20.65 C ANISOU 513 C LEU A 74 2650 2367 2829 -224 -126 112 C ATOM 514 O LEU A 74 18.777 16.063 9.283 1.00 20.31 O ANISOU 514 O LEU A 74 2514 2362 2839 -241 -100 110 O ATOM 515 CB LEU A 74 16.176 16.826 7.802 1.00 21.14 C ANISOU 515 CB LEU A 74 2734 2389 2910 -151 -300 17 C ATOM 516 CG LEU A 74 15.926 18.240 8.344 1.00 24.13 C ANISOU 516 CG LEU A 74 3116 2762 3292 -153 -329 23 C ATOM 517 CD1 LEU A 74 16.069 19.262 7.250 1.00 25.39 C ANISOU 517 CD1 LEU A 74 3424 2865 3358 -126 -366 36 C ATOM 518 CD2 LEU A 74 14.547 18.349 8.973 1.00 25.27 C ANISOU 518 CD2 LEU A 74 3177 2900 3525 -128 -398 -33 C ATOM 519 N VAL A 75 19.164 18.050 8.265 1.00 20.02 N ANISOU 519 N VAL A 75 2616 2262 2731 -241 -105 144 N ATOM 520 CA VAL A 75 19.972 18.609 9.332 1.00 20.30 C ANISOU 520 CA VAL A 75 2576 2312 2825 -280 -78 167 C ATOM 521 C VAL A 75 19.316 19.922 9.719 1.00 20.88 C ANISOU 521 C VAL A 75 2675 2370 2889 -271 -145 158 C ATOM 522 O VAL A 75 19.109 20.767 8.846 1.00 21.26 O ANISOU 522 O VAL A 75 2821 2373 2883 -257 -159 166 O ATOM 523 CB VAL A 75 21.444 18.881 8.923 1.00 21.42 C ANISOU 523 CB VAL A 75 2721 2420 2997 -318 18 210 C ATOM 524 CG1 VAL A 75 22.170 19.647 10.027 1.00 22.49 C ANISOU 524 CG1 VAL A 75 2776 2549 3217 -352 1 217 C ATOM 525 CG2 VAL A 75 22.161 17.573 8.632 1.00 21.71 C ANISOU 525 CG2 VAL A 75 2721 2471 3057 -323 91 216 C ATOM 526 N ILE A 76 19.020 20.119 11.001 1.00 20.31 N ANISOU 526 N ILE A 76 2537 2323 2857 -270 -182 143 N ATOM 527 CA ILE A 76 18.483 21.401 11.462 1.00 21.54 C ANISOU 527 CA ILE A 76 2718 2460 3005 -258 -241 135 C ATOM 528 C ILE A 76 19.606 21.978 12.309 1.00 22.09 C ANISOU 528 C ILE A 76 2758 2517 3117 -289 -234 158 C ATOM 529 O ILE A 76 19.872 21.469 13.391 1.00 22.13 O ANISOU 529 O ILE A 76 2714 2540 3152 -284 -242 149 O ATOM 530 CB ILE A 76 17.183 21.254 12.259 1.00 22.56 C ANISOU 530 CB ILE A 76 2814 2607 3152 -221 -281 95 C ATOM 531 CG1 ILE A 76 16.121 20.512 11.427 1.00 23.52 C ANISOU 531 CG1 ILE A 76 2931 2725 3281 -193 -303 58 C ATOM 532 CG2 ILE A 76 16.687 22.649 12.615 1.00 22.83 C ANISOU 532 CG2 ILE A 76 2883 2615 3174 -203 -337 87 C ATOM 533 CD1 ILE A 76 14.805 20.236 12.195 1.00 24.04 C ANISOU 533 CD1 ILE A 76 2928 2790 3415 -162 -315 13 C ATOM 534 N ALA A 77 20.270 23.026 11.817 1.00 22.76 N ANISOU 534 N ALA A 77 2881 2556 3210 -316 -224 182 N ATOM 535 CA ALA A 77 21.428 23.589 12.509 1.00 23.51 C ANISOU 535 CA ALA A 77 2928 2620 3385 -351 -230 195 C ATOM 536 C ALA A 77 21.150 24.120 13.920 1.00 24.04 C ANISOU 536 C ALA A 77 2986 2687 3461 -325 -321 170 C ATOM 537 O ALA A 77 21.947 23.898 14.842 1.00 24.86 O ANISOU 537 O ALA A 77 3044 2779 3624 -326 -357 159 O ATOM 538 CB ALA A 77 22.084 24.667 11.658 1.00 24.26 C ANISOU 538 CB ALA A 77 3066 2646 3506 -389 -184 226 C ATOM 539 N ARG A 78 20.035 24.836 14.078 1.00 23.72 N ANISOU 539 N ARG A 78 3001 2650 3361 -291 -365 156 N ATOM 540 CA ARG A 78 19.645 25.443 15.348 1.00 24.99 C ANISOU 540 CA ARG A 78 3184 2801 3510 -255 -435 134 C ATOM 541 C ARG A 78 18.144 25.231 15.468 1.00 24.89 C ANISOU 541 C ARG A 78 3193 2818 3447 -206 -428 111 C ATOM 542 O ARG A 78 17.350 26.080 15.030 1.00 24.30 O ANISOU 542 O ARG A 78 3156 2730 3349 -190 -455 101 O ATOM 543 CB ARG A 78 19.934 26.961 15.309 1.00 27.85 C ANISOU 543 CB ARG A 78 3587 3110 3886 -270 -488 141 C ATOM 544 CG ARG A 78 21.401 27.314 15.125 1.00 33.78 C ANISOU 544 CG ARG A 78 4294 3807 4734 -326 -485 159 C ATOM 545 CD ARG A 78 22.139 27.322 16.453 1.00 37.89 C ANISOU 545 CD ARG A 78 4786 4297 5316 -310 -574 132 C ATOM 546 NE ARG A 78 23.587 27.439 16.278 1.00 41.62 N ANISOU 546 NE ARG A 78 5174 4708 5932 -365 -578 135 N ATOM 547 CZ ARG A 78 24.418 26.406 16.174 1.00 43.07 C ANISOU 547 CZ ARG A 78 5276 4897 6193 -383 -543 132 C ATOM 548 NH1 ARG A 78 23.955 25.166 16.216 1.00 42.37 N ANISOU 548 NH1 ARG A 78 5192 4875 6032 -353 -503 131 N ATOM 549 NH2 ARG A 78 25.724 26.608 16.034 1.00 42.37 N ANISOU 549 NH2 ARG A 78 5089 4736 6274 -432 -544 126 N ATOM 550 N PRO A 79 17.732 24.060 15.962 1.00 24.73 N ANISOU 550 N PRO A 79 3144 2828 3426 -184 -385 98 N ATOM 551 CA PRO A 79 16.289 23.789 16.073 1.00 25.28 C ANISOU 551 CA PRO A 79 3204 2907 3494 -144 -358 71 C ATOM 552 C PRO A 79 15.612 24.762 17.019 1.00 25.45 C ANISOU 552 C PRO A 79 3272 2900 3499 -98 -381 54 C ATOM 553 O PRO A 79 16.196 25.148 18.037 1.00 25.57 O ANISOU 553 O PRO A 79 3341 2891 3485 -81 -406 61 O ATOM 554 CB PRO A 79 16.222 22.353 16.628 1.00 26.80 C ANISOU 554 CB PRO A 79 3365 3119 3701 -135 -288 68 C ATOM 555 CG PRO A 79 17.594 21.817 16.550 1.00 27.55 C ANISOU 555 CG PRO A 79 3450 3223 3795 -168 -293 92 C ATOM 556 CD PRO A 79 18.544 22.959 16.514 1.00 25.14 C ANISOU 556 CD PRO A 79 3168 2890 3493 -190 -359 105 C ATOM 557 N HIS A 80 14.358 25.127 16.720 1.00 24.99 N ANISOU 557 N HIS A 80 3198 2833 3466 -70 -381 25 N ATOM 558 CA HIS A 80 13.600 26.004 17.613 1.00 26.10 C ANISOU 558 CA HIS A 80 3377 2940 3600 -19 -383 5 C ATOM 559 C HIS A 80 13.424 25.320 18.977 1.00 27.77 C ANISOU 559 C HIS A 80 3619 3134 3800 21 -292 7 C ATOM 560 O HIS A 80 13.251 24.104 19.009 1.00 27.84 O ANISOU 560 O HIS A 80 3582 3154 3840 14 -213 7 O ATOM 561 CB HIS A 80 12.215 26.264 17.017 1.00 26.67 C ANISOU 561 CB HIS A 80 3395 2999 3740 9 -390 -38 C ATOM 562 CG HIS A 80 11.539 27.433 17.650 1.00 30.19 C ANISOU 562 CG HIS A 80 3881 3407 4182 59 -408 -58 C ATOM 563 ND1 HIS A 80 10.807 27.300 18.818 1.00 32.35 N ANISOU 563 ND1 HIS A 80 4159 3649 4482 110 -311 -73 N ATOM 564 CD2 HIS A 80 11.527 28.732 17.269 1.00 31.39 C ANISOU 564 CD2 HIS A 80 4083 3540 4303 68 -501 -63 C ATOM 565 CE1 HIS A 80 10.371 28.519 19.105 1.00 32.53 C ANISOU 565 CE1 HIS A 80 4228 3640 4491 150 -353 -90 C ATOM 566 NE2 HIS A 80 10.781 29.411 18.204 1.00 32.80 N ANISOU 566 NE2 HIS A 80 4288 3684 4492 126 -475 -85 N ATOM 567 N ASN A 81 13.469 26.085 20.089 1.00 29.55 N ANISOU 567 N ASN A 81 3940 3319 3968 69 -299 8 N ATOM 568 CA ASN A 81 13.308 25.522 21.430 1.00 32.06 C ANISOU 568 CA ASN A 81 4342 3595 4242 126 -206 12 C ATOM 569 C ASN A 81 12.042 24.677 21.568 1.00 34.21 C ANISOU 569 C ASN A 81 4553 3851 4592 147 -53 -4 C ATOM 570 O ASN A 81 12.084 23.621 22.184 1.00 34.74 O ANISOU 570 O ASN A 81 4655 3899 4646 162 49 9 O ATOM 571 CB ASN A 81 13.304 26.610 22.490 1.00 33.87 C ANISOU 571 CB ASN A 81 4707 3768 4394 192 -239 8 C ATOM 572 CG ASN A 81 14.658 27.236 22.732 1.00 38.77 C ANISOU 572 CG ASN A 81 5402 4375 4954 183 -386 18 C ATOM 573 OD1 ASN A 81 15.712 26.620 22.499 1.00 40.59 O ANISOU 573 OD1 ASN A 81 5606 4625 5192 143 -436 30 O ATOM 574 ND2 ASN A 81 14.654 28.476 23.218 1.00 39.99 N ANISOU 574 ND2 ASN A 81 5644 4487 5065 222 -461 7 N ATOM 575 N ASP A 82 10.945 25.098 20.932 1.00 35.25 N ANISOU 575 N ASP A 82 4588 3982 4824 147 -42 -38 N ATOM 576 CA ASP A 82 9.682 24.366 21.026 1.00 37.25 C ANISOU 576 CA ASP A 82 4747 4200 5206 163 99 -67 C ATOM 577 C ASP A 82 9.718 22.987 20.357 1.00 38.02 C ANISOU 577 C ASP A 82 4744 4325 5378 113 133 -68 C ATOM 578 O ASP A 82 8.957 22.101 20.739 1.00 39.40 O ANISOU 578 O ASP A 82 4865 4457 5649 122 278 -80 O ATOM 579 CB ASP A 82 8.529 25.234 20.503 1.00 41.03 C ANISOU 579 CB ASP A 82 5133 4657 5800 183 67 -118 C ATOM 580 CG ASP A 82 8.495 26.624 21.132 1.00 49.22 C ANISOU 580 CG ASP A 82 6275 5666 6761 235 29 -117 C ATOM 581 OD1 ASP A 82 9.092 26.804 22.231 1.00 50.77 O ANISOU 581 OD1 ASP A 82 6620 5838 6831 272 68 -84 O ATOM 582 OD2 ASP A 82 7.880 27.532 20.532 1.00 52.33 O ANISOU 582 OD2 ASP A 82 6615 6054 7215 248 -54 -155 O ATOM 583 N ILE A 83 10.644 22.764 19.421 1.00 37.08 N ANISOU 583 N ILE A 83 4609 4265 5215 61 18 -53 N ATOM 584 CA ILE A 83 10.781 21.466 18.755 1.00 37.07 C ANISOU 584 CA ILE A 83 4530 4288 5265 19 39 -54 C ATOM 585 C ILE A 83 11.350 20.398 19.728 1.00 36.73 C ANISOU 585 C ILE A 83 4557 4234 5166 25 147 -18 C ATOM 586 O ILE A 83 11.099 19.209 19.541 1.00 36.71 O ANISOU 586 O ILE A 83 4493 4227 5230 4 220 -23 O ATOM 587 CB ILE A 83 11.569 21.644 17.419 1.00 38.03 C ANISOU 587 CB ILE A 83 4637 4463 5349 -26 -100 -48 C ATOM 588 CG1 ILE A 83 10.590 21.776 16.238 1.00 39.01 C ANISOU 588 CG1 ILE A 83 4671 4574 5576 -25 -171 -101 C ATOM 589 CG2 ILE A 83 12.636 20.594 17.157 1.00 38.64 C ANISOU 589 CG2 ILE A 83 4724 4578 5380 -64 -94 -16 C ATOM 590 CD1 ILE A 83 9.475 22.774 16.459 1.00 40.33 C ANISOU 590 CD1 ILE A 83 4809 4696 5817 20 -187 -143 C ATOM 591 N ASN A 84 12.017 20.834 20.818 1.00 36.13 N ANISOU 591 N ASN A 84 4621 4136 4969 64 153 11 N ATOM 592 CA ASN A 84 12.505 19.934 21.860 1.00 36.15 C ANISOU 592 CA ASN A 84 4734 4105 4897 94 239 39 C ATOM 593 C ASN A 84 11.337 19.125 22.464 1.00 35.77 C ANISOU 593 C ASN A 84 4674 3989 4929 121 440 33 C ATOM 594 O ASN A 84 11.516 17.955 22.778 1.00 35.78 O ANISOU 594 O ASN A 84 4705 3970 4921 119 528 51 O ATOM 595 CB ASN A 84 13.232 20.720 22.939 1.00 37.70 C ANISOU 595 CB ASN A 84 5103 4264 4957 153 183 55 C ATOM 596 CG ASN A 84 13.964 19.835 23.911 1.00 42.53 C ANISOU 596 CG ASN A 84 5859 4833 5468 196 215 78 C ATOM 597 OD1 ASN A 84 14.872 19.090 23.534 1.00 44.34 O ANISOU 597 OD1 ASN A 84 6058 5097 5690 163 151 86 O ATOM 598 ND2 ASN A 84 13.571 19.886 25.176 1.00 43.11 N ANISOU 598 ND2 ASN A 84 6107 4818 5457 281 318 87 N ATOM 599 N LYS A 85 10.129 19.720 22.529 1.00 35.50 N ANISOU 599 N LYS A 85 4578 3913 4996 141 517 4 N ATOM 600 CA LYS A 85 8.915 19.059 23.024 1.00 35.93 C ANISOU 600 CA LYS A 85 4584 3885 5182 160 731 -9 C ATOM 601 C LYS A 85 8.523 17.836 22.188 1.00 36.42 C ANISOU 601 C LYS A 85 4482 3956 5399 98 766 -30 C ATOM 602 O LYS A 85 7.937 16.903 22.729 1.00 37.61 O ANISOU 602 O LYS A 85 4625 4032 5633 104 956 -25 O ATOM 603 CB LYS A 85 7.740 20.051 23.115 1.00 37.34 C ANISOU 603 CB LYS A 85 4693 4016 5477 191 784 -48 C ATOM 604 N ILE A 86 8.860 17.816 20.892 1.00 35.65 N ANISOU 604 N ILE A 86 4273 3936 5336 45 593 -53 N ATOM 605 CA ILE A 86 8.600 16.666 20.023 1.00 35.68 C ANISOU 605 CA ILE A 86 4144 3947 5467 -5 589 -78 C ATOM 606 C ILE A 86 9.785 15.704 20.107 1.00 34.68 C ANISOU 606 C ILE A 86 4105 3861 5210 -25 576 -32 C ATOM 607 O ILE A 86 9.600 14.499 20.105 1.00 34.69 O ANISOU 607 O ILE A 86 4067 3833 5279 -46 666 -31 O ATOM 608 CB ILE A 86 8.399 17.096 18.536 1.00 37.57 C ANISOU 608 CB ILE A 86 4260 4232 5781 -34 399 -128 C ATOM 609 CG1 ILE A 86 7.117 17.918 18.349 1.00 39.55 C ANISOU 609 CG1 ILE A 86 4400 4430 6197 -8 389 -190 C ATOM 610 CG2 ILE A 86 8.435 15.875 17.576 1.00 37.93 C ANISOU 610 CG2 ILE A 86 4215 4290 5906 -77 356 -149 C ATOM 611 CD1 ILE A 86 6.886 18.386 16.893 1.00 41.53 C ANISOU 611 CD1 ILE A 86 4571 4706 6503 -16 178 -246 C ATOM 612 N VAL A 87 11.010 16.242 20.077 1.00 33.88 N ANISOU 612 N VAL A 87 4106 3822 4946 -21 452 -1 N ATOM 613 CA VAL A 87 12.217 15.433 20.059 1.00 34.07 C ANISOU 613 CA VAL A 87 4194 3883 4869 -37 413 32 C ATOM 614 C VAL A 87 12.341 14.567 21.305 1.00 34.21 C ANISOU 614 C VAL A 87 4335 3837 4825 2 554 63 C ATOM 615 O VAL A 87 12.660 13.383 21.178 1.00 34.29 O ANISOU 615 O VAL A 87 4340 3848 4841 -17 588 73 O ATOM 616 CB VAL A 87 13.446 16.334 19.803 1.00 34.78 C ANISOU 616 CB VAL A 87 4341 4029 4844 -41 257 49 C ATOM 617 CG1 VAL A 87 14.759 15.603 20.060 1.00 35.03 C ANISOU 617 CG1 VAL A 87 4443 4080 4788 -42 221 77 C ATOM 618 CG2 VAL A 87 13.402 16.891 18.384 1.00 35.18 C ANISOU 618 CG2 VAL A 87 4292 4132 4945 -82 142 27 C ATOM 619 N ILE A 88 12.014 15.113 22.500 1.00 34.05 N ANISOU 619 N ILE A 88 4446 3749 4744 65 646 77 N ATOM 620 CA ILE A 88 12.111 14.301 23.721 1.00 34.83 C ANISOU 620 CA ILE A 88 4714 3763 4756 119 791 109 C ATOM 621 C ILE A 88 11.111 13.134 23.739 1.00 35.37 C ANISOU 621 C ILE A 88 4710 3767 4964 96 992 107 C ATOM 622 O ILE A 88 11.339 12.155 24.458 1.00 36.31 O ANISOU 622 O ILE A 88 4956 3823 5016 125 1104 137 O ATOM 623 CB ILE A 88 12.046 15.129 25.008 1.00 35.82 C ANISOU 623 CB ILE A 88 5042 3812 4756 208 847 126 C ATOM 624 CG1 ILE A 88 10.683 15.793 25.161 1.00 37.16 C ANISOU 624 CG1 ILE A 88 5147 3929 5041 220 988 107 C ATOM 625 CG2 ILE A 88 13.200 16.124 25.065 1.00 36.49 C ANISOU 625 CG2 ILE A 88 5207 3945 4713 231 630 124 C ATOM 626 CD1 ILE A 88 10.445 16.250 26.489 1.00 39.25 C ANISOU 626 CD1 ILE A 88 5630 4092 5190 315 1113 129 C ATOM 627 N LYS A 89 10.035 13.200 22.938 1.00 34.61 N ANISOU 627 N LYS A 89 4410 3672 5068 47 1026 66 N ATOM 628 CA LYS A 89 9.087 12.082 22.845 1.00 35.56 C ANISOU 628 CA LYS A 89 4421 3719 5370 15 1198 52 C ATOM 629 C LYS A 89 9.723 10.850 22.174 1.00 36.72 C ANISOU 629 C LYS A 89 4527 3910 5516 -32 1133 56 C ATOM 630 O LYS A 89 9.226 9.734 22.338 1.00 37.67 O ANISOU 630 O LYS A 89 4615 3958 5740 -52 1282 58 O ATOM 631 CB LYS A 89 7.850 12.491 22.039 1.00 37.26 C ANISOU 631 CB LYS A 89 4408 3919 5829 -22 1194 -12 C ATOM 632 CG LYS A 89 7.038 13.580 22.695 1.00 41.58 C ANISOU 632 CG LYS A 89 4970 4407 6422 25 1290 -24 C ATOM 633 CD LYS A 89 5.774 13.874 21.911 1.00 45.73 C ANISOU 633 CD LYS A 89 5251 4899 7224 -5 1278 -100 C ATOM 634 CE LYS A 89 5.036 15.045 22.514 1.00 49.48 C ANISOU 634 CE LYS A 89 5736 5322 7743 47 1358 -115 C ATOM 635 NZ LYS A 89 4.676 14.791 23.933 1.00 51.67 N ANISOU 635 NZ LYS A 89 6159 5480 7992 98 1653 -69 N ATOM 636 N HIS A 90 10.790 11.052 21.390 1.00 36.55 N ANISOU 636 N HIS A 90 4499 3995 5393 -52 924 56 N ATOM 637 CA HIS A 90 11.443 9.939 20.694 1.00 37.60 C ANISOU 637 CA HIS A 90 4596 4171 5521 -91 860 59 C ATOM 638 C HIS A 90 12.849 9.659 21.265 1.00 38.74 C ANISOU 638 C HIS A 90 4909 4343 5469 -56 801 101 C ATOM 639 O HIS A 90 13.659 9.043 20.587 1.00 38.16 O ANISOU 639 O HIS A 90 4805 4326 5369 -82 705 101 O ATOM 640 CB HIS A 90 11.517 10.222 19.176 1.00 38.75 C ANISOU 640 CB HIS A 90 4592 4397 5733 -137 682 18 C ATOM 641 CG HIS A 90 10.284 10.859 18.607 1.00 41.22 C ANISOU 641 CG HIS A 90 4762 4683 6217 -150 667 -36 C ATOM 642 ND1 HIS A 90 9.045 10.248 18.704 1.00 43.13 N ANISOU 642 ND1 HIS A 90 4888 4835 6665 -165 794 -73 N ATOM 643 CD2 HIS A 90 10.132 12.062 18.005 1.00 42.51 C ANISOU 643 CD2 HIS A 90 4885 4884 6381 -144 541 -62 C ATOM 644 CE1 HIS A 90 8.189 11.081 18.135 1.00 43.57 C ANISOU 644 CE1 HIS A 90 4825 4878 6851 -164 721 -128 C ATOM 645 NE2 HIS A 90 8.794 12.189 17.707 1.00 43.59 N ANISOU 645 NE2 HIS A 90 4882 4959 6722 -148 568 -121 N ATOM 646 N LYS A 91 13.127 10.086 22.510 1.00 39.79 N ANISOU 646 N LYS A 91 5223 4423 5471 11 853 130 N ATOM 647 CA LYS A 91 14.423 9.921 23.158 1.00 41.29 C ANISOU 647 CA LYS A 91 5583 4615 5489 62 766 156 C ATOM 648 C LYS A 91 14.844 8.460 23.305 1.00 42.58 C ANISOU 648 C LYS A 91 5803 4750 5627 64 816 172 C ATOM 649 O LYS A 91 15.993 8.129 23.001 1.00 43.31 O ANISOU 649 O LYS A 91 5904 4893 5660 64 679 171 O ATOM 650 CB LYS A 91 14.443 10.642 24.519 1.00 43.14 C ANISOU 650 CB LYS A 91 6032 4769 5590 151 809 174 C TER 651 LYS A 91 HETATM 652 O HOH A 101 14.425 -0.838 3.446 1.00 35.57 O HETATM 653 O HOH A 102 28.365 8.667 18.585 1.00 42.16 O HETATM 654 O HOH A 103 30.619 9.233 17.681 1.00 39.81 O HETATM 655 O HOH A 104 9.784 7.482 11.402 1.00 28.98 O HETATM 656 O HOH A 105 18.660 2.591 -1.600 1.00 42.00 O HETATM 657 O HOH A 106 29.847 17.463 18.029 1.00 35.59 O HETATM 658 O HOH A 107 28.837 5.490 5.400 1.00 32.54 O HETATM 659 O HOH A 108 30.677 -0.318 12.619 1.00 32.92 O HETATM 660 O HOH A 109 9.462 12.384 6.390 1.00 25.15 O HETATM 661 O HOH A 110 24.960 16.733 5.501 1.00 36.67 O HETATM 662 O HOH A 111 27.100 25.251 8.483 1.00 45.96 O HETATM 663 O HOH A 112 16.905 16.352 2.392 1.00 40.15 O HETATM 664 O HOH A 113 30.759 18.451 7.897 1.00 31.07 O HETATM 665 O HOH A 114 33.051 22.225 16.333 1.00 37.39 O HETATM 666 O HOH A 115 20.572 15.421 4.347 1.00 38.04 O HETATM 667 O HOH A 116 17.720 11.919 1.710 1.00 35.92 O HETATM 668 O HOH A 117 18.116 25.719 39.896 1.00 33.99 O HETATM 669 O HOH A 118 17.405 5.033 -0.581 1.00 38.89 O HETATM 670 O HOH A 119 15.206 22.205 20.162 1.00 35.42 O HETATM 671 O HOH A 120 31.868 19.950 14.009 1.00 37.23 O HETATM 672 O HOH A 121 25.322 8.453 21.845 1.00 41.66 O HETATM 673 O HOH A 122 14.242 29.045 19.725 1.00 35.68 O HETATM 674 O HOH A 123 15.794 19.720 19.523 1.00 37.61 O HETATM 675 O HOH A 124 27.027 23.855 16.675 1.00 24.87 O HETATM 676 O HOH A 125 33.453 15.122 13.901 1.00 16.97 O HETATM 677 O HOH A 126 22.527 16.343 4.917 1.00 46.69 O HETATM 678 O HOH A 127 29.637 23.016 8.328 1.00 46.38 O