CNRS Nantes University US2B US2B
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***  pedro  ***

elNémo ID: 2309120947474066980

Job options:

ID        	=	 2309120947474066980
JOBID     	=	 pedro
USERID    	=	 pedro.murcia
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER pedro

data_1EIN
# 
_entry.id   1EIN 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.289 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1EIN         
RCSB  RCSB010613   
WWPDB D_1000010613 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1EIN 
_pdbx_database_status.recvd_initial_deposition_date   2000-02-26 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Brozozowski, A.M.' 1 
'Savage, H.'        2 
# 
_citation.id                        primary 
_citation.title                     'Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase.' 
_citation.journal_abbrev            Biochemistry 
_citation.journal_volume            39 
_citation.page_first                15071 
_citation.page_last                 15082 
_citation.year                      2000 
_citation.journal_id_ASTM           BICHAW 
_citation.country                   US 
_citation.journal_id_ISSN           0006-2960 
_citation.journal_id_CSD            0033 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   11106485 
_citation.pdbx_database_id_DOI      10.1021/bi0013905 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Brzozowski, A.M.' 1 
primary 'Savage, H.'       2 
primary 'Verma, C.S.'      3 
primary 'Turkenburg, J.P.' 4 
primary 'Lawson, D.M.'     5 
primary 'Svendsen, A.'     6 
primary 'Patkar, S.'       7 
# 
_cell.entry_id           1EIN 
_cell.length_a           135.950 
_cell.length_b           135.950 
_cell.length_c           149.990 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              18 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1EIN 
_symmetry.space_group_name_H-M             'P 65' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                170 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     nat LIPASE                           29342.484 3   3.1.1.3 ? ? ? 
2 non-polymer syn 'DIUNDECYL PHOSPHATIDYL CHOLINE' 622.834   3   ?       ? ? ? 
3 water       nat water                            18.015    184 ?       ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;EVSQDLFNQFNLFAQYSAAAYCGKNNDAPAGTNITCTGNACPEVEKADATFLYSFEDSGVGDVTGFLALDNTNKLIVLSF
RGSRSIENWIGNLNFDLKEINDICSGCRGHDGFTSSWRSVADTLRQKVEDAVREHPDYRVVFTGHSLGGALATVAGADLR
GNGYDIDVFSYGAPRVGNRAFAEFLTVQTGGTLYRITHTNDIVPRLPPREFGYSHSSPEYWIKSGTLVPVTRNDIVKIEG
IDATGGNNQPNIPDIPAHLWYFGLIGTCL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;EVSQDLFNQFNLFAQYSAAAYCGKNNDAPAGTNITCTGNACPEVEKADATFLYSFEDSGVGDVTGFLALDNTNKLIVLSF
RGSRSIENWIGNLNFDLKEINDICSGCRGHDGFTSSWRSVADTLRQKVEDAVREHPDYRVVFTGHSLGGALATVAGADLR
GNGYDIDVFSYGAPRVGNRAFAEFLTVQTGGTLYRITHTNDIVPRLPPREFGYSHSSPEYWIKSGTLVPVTRNDIVKIEG
IDATGGNNQPNIPDIPAHLWYFGLIGTCL
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLU n 
1 2   VAL n 
1 3   SER n 
1 4   GLN n 
1 5   ASP n 
1 6   LEU n 
1 7   PHE n 
1 8   ASN n 
1 9   GLN n 
1 10  PHE n 
1 11  ASN n 
1 12  LEU n 
1 13  PHE n 
1 14  ALA n 
1 15  GLN n 
1 16  TYR n 
1 17  SER n 
1 18  ALA n 
1 19  ALA n 
1 20  ALA n 
1 21  TYR n 
1 22  CYS n 
1 23  GLY n 
1 24  LYS n 
1 25  ASN n 
1 26  ASN n 
1 27  ASP n 
1 28  ALA n 
1 29  PRO n 
1 30  ALA n 
1 31  GLY n 
1 32  THR n 
1 33  ASN n 
1 34  ILE n 
1 35  THR n 
1 36  CYS n 
1 37  THR n 
1 38  GLY n 
1 39  ASN n 
1 40  ALA n 
1 41  CYS n 
1 42  PRO n 
1 43  GLU n 
1 44  VAL n 
1 45  GLU n 
1 46  LYS n 
1 47  ALA n 
1 48  ASP n 
1 49  ALA n 
1 50  THR n 
1 51  PHE n 
1 52  LEU n 
1 53  TYR n 
1 54  SER n 
1 55  PHE n 
1 56  GLU n 
1 57  ASP n 
1 58  SER n 
1 59  GLY n 
1 60  VAL n 
1 61  GLY n 
1 62  ASP n 
1 63  VAL n 
1 64  THR n 
1 65  GLY n 
1 66  PHE n 
1 67  LEU n 
1 68  ALA n 
1 69  LEU n 
1 70  ASP n 
1 71  ASN n 
1 72  THR n 
1 73  ASN n 
1 74  LYS n 
1 75  LEU n 
1 76  ILE n 
1 77  VAL n 
1 78  LEU n 
1 79  SER n 
1 80  PHE n 
1 81  ARG n 
1 82  GLY n 
1 83  SER n 
1 84  ARG n 
1 85  SER n 
1 86  ILE n 
1 87  GLU n 
1 88  ASN n 
1 89  TRP n 
1 90  ILE n 
1 91  GLY n 
1 92  ASN n 
1 93  LEU n 
1 94  ASN n 
1 95  PHE n 
1 96  ASP n 
1 97  LEU n 
1 98  LYS n 
1 99  GLU n 
1 100 ILE n 
1 101 ASN n 
1 102 ASP n 
1 103 ILE n 
1 104 CYS n 
1 105 SER n 
1 106 GLY n 
1 107 CYS n 
1 108 ARG n 
1 109 GLY n 
1 110 HIS n 
1 111 ASP n 
1 112 GLY n 
1 113 PHE n 
1 114 THR n 
1 115 SER n 
1 116 SER n 
1 117 TRP n 
1 118 ARG n 
1 119 SER n 
1 120 VAL n 
1 121 ALA n 
1 122 ASP n 
1 123 THR n 
1 124 LEU n 
1 125 ARG n 
1 126 GLN n 
1 127 LYS n 
1 128 VAL n 
1 129 GLU n 
1 130 ASP n 
1 131 ALA n 
1 132 VAL n 
1 133 ARG n 
1 134 GLU n 
1 135 HIS n 
1 136 PRO n 
1 137 ASP n 
1 138 TYR n 
1 139 ARG n 
1 140 VAL n 
1 141 VAL n 
1 142 PHE n 
1 143 THR n 
1 144 GLY n 
1 145 HIS n 
1 146 SER n 
1 147 LEU n 
1 148 GLY n 
1 149 GLY n 
1 150 ALA n 
1 151 LEU n 
1 152 ALA n 
1 153 THR n 
1 154 VAL n 
1 155 ALA n 
1 156 GLY n 
1 157 ALA n 
1 158 ASP n 
1 159 LEU n 
1 160 ARG n 
1 161 GLY n 
1 162 ASN n 
1 163 GLY n 
1 164 TYR n 
1 165 ASP n 
1 166 ILE n 
1 167 ASP n 
1 168 VAL n 
1 169 PHE n 
1 170 SER n 
1 171 TYR n 
1 172 GLY n 
1 173 ALA n 
1 174 PRO n 
1 175 ARG n 
1 176 VAL n 
1 177 GLY n 
1 178 ASN n 
1 179 ARG n 
1 180 ALA n 
1 181 PHE n 
1 182 ALA n 
1 183 GLU n 
1 184 PHE n 
1 185 LEU n 
1 186 THR n 
1 187 VAL n 
1 188 GLN n 
1 189 THR n 
1 190 GLY n 
1 191 GLY n 
1 192 THR n 
1 193 LEU n 
1 194 TYR n 
1 195 ARG n 
1 196 ILE n 
1 197 THR n 
1 198 HIS n 
1 199 THR n 
1 200 ASN n 
1 201 ASP n 
1 202 ILE n 
1 203 VAL n 
1 204 PRO n 
1 205 ARG n 
1 206 LEU n 
1 207 PRO n 
1 208 PRO n 
1 209 ARG n 
1 210 GLU n 
1 211 PHE n 
1 212 GLY n 
1 213 TYR n 
1 214 SER n 
1 215 HIS n 
1 216 SER n 
1 217 SER n 
1 218 PRO n 
1 219 GLU n 
1 220 TYR n 
1 221 TRP n 
1 222 ILE n 
1 223 LYS n 
1 224 SER n 
1 225 GLY n 
1 226 THR n 
1 227 LEU n 
1 228 VAL n 
1 229 PRO n 
1 230 VAL n 
1 231 THR n 
1 232 ARG n 
1 233 ASN n 
1 234 ASP n 
1 235 ILE n 
1 236 VAL n 
1 237 LYS n 
1 238 ILE n 
1 239 GLU n 
1 240 GLY n 
1 241 ILE n 
1 242 ASP n 
1 243 ALA n 
1 244 THR n 
1 245 GLY n 
1 246 GLY n 
1 247 ASN n 
1 248 ASN n 
1 249 GLN n 
1 250 PRO n 
1 251 ASN n 
1 252 ILE n 
1 253 PRO n 
1 254 ASP n 
1 255 ILE n 
1 256 PRO n 
1 257 ALA n 
1 258 HIS n 
1 259 LEU n 
1 260 TRP n 
1 261 TYR n 
1 262 PHE n 
1 263 GLY n 
1 264 LEU n 
1 265 ILE n 
1 266 GLY n 
1 267 THR n 
1 268 CYS n 
1 269 LEU n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           ? 
_entity_src_nat.pdbx_end_seq_num           ? 
_entity_src_nat.common_name                ? 
_entity_src_nat.pdbx_organism_scientific   'Thermomyces lanuginosus' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      5541 
_entity_src_nat.genus                      Thermomyces 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    LIP_THELA 
_struct_ref.pdbx_db_accession          O59952 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;EVSQDLFNQFNLFAQYSAAAYCGKNNDAPAGTNITCTGNACPEVEKADATFLYSFEDSGVGDVTGFLALDNTNKLIVLSF
RGSRSIENWIGNLNFDLKEINDICSGCRGHDGFTSSWRSVADTLRQKVEDAVREHPDYRVVFTGHSLGGALATVAGADLR
GNGYDIDVFSYGAPRVGNRAFAEFLTVQTGGTLYRITHTNDIVPRLPPREFGYSHSSPEYWIKSGTLVPVTRNDIVKIEG
IDATGGNNQPNIPDIPAHLWYFGLIGTCL
;
_struct_ref.pdbx_align_begin           23 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 1EIN A 1 ? 269 ? O59952 23 ? 291 ? 1 269 
2 1 1EIN B 1 ? 269 ? O59952 23 ? 291 ? 1 269 
3 1 1EIN C 1 ? 269 ? O59952 23 ? 291 ? 1 269 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                          ? 'C3 H7 N O2'       89.093  
ARG 'L-peptide linking' y ARGININE                         ? 'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE                       ? 'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                  ? 'C4 H7 N O4'       133.103 
CYS 'L-peptide linking' y CYSTEINE                         ? 'C3 H7 N O2 S'     121.158 
GLN 'L-peptide linking' y GLUTAMINE                        ? 'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                  ? 'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                          ? 'C2 H5 N O2'       75.067  
HIS 'L-peptide linking' y HISTIDINE                        ? 'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                            ? 'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE                       ? 'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                          ? 'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                           ? 'C6 H15 N2 O2 1'   147.195 
PHE 'L-peptide linking' y PHENYLALANINE                    ? 'C9 H11 N O2'      165.189 
PLC non-polymer         . 'DIUNDECYL PHOSPHATIDYL CHOLINE' ? 'C32 H65 N O8 P 1' 622.834 
PRO 'L-peptide linking' y PROLINE                          ? 'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                           ? 'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                        ? 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                       ? 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                         ? 'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                           ? 'C5 H11 N O2'      117.146 
# 
_exptl.entry_id          1EIN 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      4.54 
_exptl_crystal.density_percent_sol   72.93 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              8.1 
_exptl_crystal_grow.pdbx_details    'PEG 5000, magnesium chloride, c8e5 , pH 8.1, VAPOR DIFFUSION, HANGING DROP, temperature 110K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           110 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'RIGAKU RAXIS' 
_diffrn_detector.pdbx_collection_date   1996-06-01 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.54 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'RIGAKU RU200' 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             1.54 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     1EIN 
_reflns.observed_criterion_sigma_I   0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             27.4 
_reflns.d_resolution_high            3.00 
_reflns.number_obs                   31460 
_reflns.number_all                   91965 
_reflns.percent_possible_obs         99.8 
_reflns.pdbx_Rmerge_I_obs            0.2 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        3.0 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              5.2 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             3.00 
_reflns_shell.d_res_low              3.16 
_reflns_shell.percent_possible_all   100.0 
_reflns_shell.Rmerge_I_obs           0.139 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        3.9 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      31460 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1EIN 
_refine.ls_number_reflns_obs                     31460 
_refine.ls_number_reflns_all                     164254 
_refine.pdbx_ls_sigma_I                          0 
_refine.pdbx_ls_sigma_F                          0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_d_res_low                             27.4 
_refine.ls_d_res_high                            3.0 
_refine.ls_percent_reflns_obs                    99.8 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.21 
_refine.ls_R_factor_R_free                       0.241 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  1588 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  'R-axis data' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            random 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        6189 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         126 
_refine_hist.number_atoms_solvent             184 
_refine_hist.number_atoms_total               6499 
_refine_hist.d_res_high                       3.0 
_refine_hist.d_res_low                        27.4 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
o_bond_d    0.008 ? ? ? 'X-RAY DIFFRACTION' ? 
o_angle_deg 0.029 ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_struct.entry_id                  1EIN 
_struct.title                     'THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE' 
_struct.pdbx_descriptor           'LIPASE (E.C.3.1.1.3)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1EIN 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            'alpha-beta structure, HYDROLASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
# 
loop_
_struct_biol.id 
_struct_biol.details 
_struct_biol.pdbx_parent_biol_id 
1 'The biological assembly is a monomer' ? 
2 ?                                      ? 
3 ?                                      ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  SER A 3   ? CYS A 22  ? SER A 3   CYS A 22  1 ? 20 
HELX_P HELX_P2  2  GLY A 23  ? ASP A 27  ? GLY A 23  ASP A 27  5 ? 5  
HELX_P HELX_P3  3  CYS A 41  ? ALA A 47  ? CYS A 41  ALA A 47  1 ? 7  
HELX_P HELX_P4  4  SER A 85  ? ASN A 92  ? SER A 85  ASN A 92  1 ? 8  
HELX_P HELX_P5  5  ASP A 111 ? HIS A 135 ? ASP A 111 HIS A 135 1 ? 25 
HELX_P HELX_P6  6  SER A 146 ? ARG A 160 ? SER A 146 ARG A 160 1 ? 15 
HELX_P HELX_P7  7  ASN A 178 ? GLN A 188 ? ASN A 178 GLN A 188 1 ? 11 
HELX_P HELX_P8  8  ILE A 202 ? LEU A 206 ? ILE A 202 LEU A 206 5 ? 5  
HELX_P HELX_P9  9  PRO A 208 ? GLY A 212 ? PRO A 208 GLY A 212 5 ? 5  
HELX_P HELX_P10 10 ILE A 255 ? LEU A 259 ? ILE A 255 LEU A 259 5 ? 5  
HELX_P HELX_P11 11 SER B 3   ? TYR B 21  ? SER B 3   TYR B 21  1 ? 19 
HELX_P HELX_P12 12 CYS B 22  ? ASP B 27  ? CYS B 22  ASP B 27  5 ? 6  
HELX_P HELX_P13 13 CYS B 41  ? ALA B 47  ? CYS B 41  ALA B 47  1 ? 7  
HELX_P HELX_P14 14 SER B 85  ? LEU B 93  ? SER B 85  LEU B 93  1 ? 9  
HELX_P HELX_P15 15 GLY B 112 ? HIS B 135 ? GLY B 112 HIS B 135 1 ? 24 
HELX_P HELX_P16 16 SER B 146 ? ARG B 160 ? SER B 146 ARG B 160 1 ? 15 
HELX_P HELX_P17 17 ASN B 178 ? GLN B 188 ? ASN B 178 GLN B 188 1 ? 11 
HELX_P HELX_P18 18 ILE B 202 ? LEU B 206 ? ILE B 202 LEU B 206 5 ? 5  
HELX_P HELX_P19 19 PRO B 208 ? GLY B 212 ? PRO B 208 GLY B 212 5 ? 5  
HELX_P HELX_P20 20 ILE B 255 ? LEU B 259 ? ILE B 255 LEU B 259 5 ? 5  
HELX_P HELX_P21 21 SER C 3   ? TYR C 21  ? SER C 3   TYR C 21  1 ? 19 
HELX_P HELX_P22 22 CYS C 22  ? ASP C 27  ? CYS C 22  ASP C 27  5 ? 6  
HELX_P HELX_P23 23 CYS C 41  ? ALA C 47  ? CYS C 41  ALA C 47  1 ? 7  
HELX_P HELX_P24 24 SER C 85  ? ASN C 94  ? SER C 85  ASN C 94  1 ? 10 
HELX_P HELX_P25 25 GLY C 112 ? SER C 119 ? GLY C 112 SER C 119 1 ? 8  
HELX_P HELX_P26 26 VAL C 120 ? HIS C 135 ? VAL C 120 HIS C 135 1 ? 16 
HELX_P HELX_P27 27 SER C 146 ? ARG C 160 ? SER C 146 ARG C 160 1 ? 15 
HELX_P HELX_P28 28 ASN C 178 ? GLN C 188 ? ASN C 178 GLN C 188 1 ? 11 
HELX_P HELX_P29 29 ILE C 202 ? LEU C 206 ? ILE C 202 LEU C 206 5 ? 5  
HELX_P HELX_P30 30 PRO C 208 ? GLY C 212 ? PRO C 208 GLY C 212 5 ? 5  
HELX_P HELX_P31 31 THR C 231 ? ASN C 233 ? THR C 231 ASN C 233 5 ? 3  
HELX_P HELX_P32 32 ILE C 255 ? LEU C 259 ? ILE C 255 LEU C 259 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1 disulf ? ? A CYS 22  SG ? ? ? 1_555 A CYS 268 SG ? ? A CYS 22  A CYS 268 1_555 ? ? ? ? ? ? ? 1.966 ? 
disulf2 disulf ? ? A CYS 36  SG ? ? ? 1_555 A CYS 41  SG ? ? A CYS 36  A CYS 41  1_555 ? ? ? ? ? ? ? 2.016 ? 
disulf3 disulf ? ? A CYS 104 SG ? ? ? 1_555 A CYS 107 SG ? ? A CYS 104 A CYS 107 1_555 ? ? ? ? ? ? ? 2.020 ? 
disulf4 disulf ? ? B CYS 22  SG ? ? ? 1_555 B CYS 268 SG ? ? B CYS 22  B CYS 268 1_555 ? ? ? ? ? ? ? 1.976 ? 
disulf5 disulf ? ? B CYS 36  SG ? ? ? 1_555 B CYS 41  SG ? ? B CYS 36  B CYS 41  1_555 ? ? ? ? ? ? ? 2.021 ? 
disulf6 disulf ? ? B CYS 104 SG ? ? ? 1_555 B CYS 107 SG ? ? B CYS 104 B CYS 107 1_555 ? ? ? ? ? ? ? 2.019 ? 
disulf7 disulf ? ? C CYS 22  SG ? ? ? 1_555 C CYS 268 SG ? ? C CYS 22  C CYS 268 1_555 ? ? ? ? ? ? ? 1.973 ? 
disulf8 disulf ? ? C CYS 36  SG ? ? ? 1_555 C CYS 41  SG ? ? C CYS 36  C CYS 41  1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf9 disulf ? ? C CYS 104 SG ? ? ? 1_555 C CYS 107 SG ? ? C CYS 104 C CYS 107 1_555 ? ? ? ? ? ? ? 2.026 ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LEU 206 A . ? LEU 206 A PRO 207 A ? PRO 207 A 1 -8.86 
2 SER 217 A . ? SER 217 A PRO 218 A ? PRO 218 A 1 -0.14 
3 LEU 206 B . ? LEU 206 B PRO 207 B ? PRO 207 B 1 -6.13 
4 SER 217 B . ? SER 217 B PRO 218 B ? PRO 218 B 1 1.56  
5 LEU 206 C . ? LEU 206 C PRO 207 C ? PRO 207 C 1 -6.72 
6 SER 217 C . ? SER 217 C PRO 218 C ? PRO 218 C 1 -0.71 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 8 ? 
B ? 2 ? 
C ? 8 ? 
D ? 2 ? 
E ? 8 ? 
F ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? parallel      
A 4 5 ? parallel      
A 5 6 ? parallel      
A 6 7 ? parallel      
A 7 8 ? anti-parallel 
B 1 2 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? parallel      
C 4 5 ? parallel      
C 5 6 ? parallel      
C 6 7 ? parallel      
C 7 8 ? anti-parallel 
D 1 2 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? anti-parallel 
E 3 4 ? parallel      
E 4 5 ? parallel      
E 5 6 ? parallel      
E 6 7 ? parallel      
E 7 8 ? anti-parallel 
F 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ALA A 49  ? SER A 58  ? ALA A 49  SER A 58  
A 2 VAL A 63  ? ASP A 70  ? VAL A 63  ASP A 70  
A 3 LEU A 75  ? PHE A 80  ? LEU A 75  PHE A 80  
A 4 ARG A 139 ? HIS A 145 ? ARG A 139 HIS A 145 
A 5 ASP A 167 ? TYR A 171 ? ASP A 167 TYR A 171 
A 6 LEU A 193 ? HIS A 198 ? LEU A 193 HIS A 198 
A 7 GLU A 219 ? ILE A 222 ? GLU A 219 ILE A 222 
A 8 ILE A 235 ? ILE A 238 ? ILE A 235 ILE A 238 
B 1 LEU A 97  ? GLU A 99  ? LEU A 97  GLU A 99  
B 2 ARG A 108 ? HIS A 110 ? ARG A 108 HIS A 110 
C 1 ALA B 49  ? SER B 58  ? ALA B 49  SER B 58  
C 2 VAL B 63  ? ASP B 70  ? VAL B 63  ASP B 70  
C 3 LEU B 75  ? PHE B 80  ? LEU B 75  PHE B 80  
C 4 ARG B 139 ? HIS B 145 ? ARG B 139 HIS B 145 
C 5 ASP B 167 ? TYR B 171 ? ASP B 167 TYR B 171 
C 6 LEU B 193 ? HIS B 198 ? LEU B 193 HIS B 198 
C 7 GLU B 219 ? ILE B 222 ? GLU B 219 ILE B 222 
C 8 ILE B 235 ? ILE B 238 ? ILE B 235 ILE B 238 
D 1 LEU B 97  ? GLU B 99  ? LEU B 97  GLU B 99  
D 2 ARG B 108 ? HIS B 110 ? ARG B 108 HIS B 110 
E 1 ALA C 49  ? SER C 58  ? ALA C 49  SER C 58  
E 2 VAL C 63  ? ASP C 70  ? VAL C 63  ASP C 70  
E 3 LEU C 75  ? PHE C 80  ? LEU C 75  PHE C 80  
E 4 ARG C 139 ? HIS C 145 ? ARG C 139 HIS C 145 
E 5 ILE C 166 ? TYR C 171 ? ILE C 166 TYR C 171 
E 6 LEU C 193 ? HIS C 198 ? LEU C 193 HIS C 198 
E 7 GLU C 219 ? ILE C 222 ? GLU C 219 ILE C 222 
E 8 ILE C 235 ? ILE C 238 ? ILE C 235 ILE C 238 
F 1 LEU C 97  ? GLU C 99  ? LEU C 97  GLU C 99  
F 2 ARG C 108 ? HIS C 110 ? ARG C 108 HIS C 110 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 O SER A 58  ? O SER A 58  N VAL A 63  ? N VAL A 63  
A 2 3 N ASP A 70  ? N ASP A 70  O LEU A 75  ? O LEU A 75  
A 3 4 N ILE A 76  ? N ILE A 76  O ARG A 139 ? O ARG A 139 
A 4 5 N PHE A 142 ? N PHE A 142 O ASP A 167 ? O ASP A 167 
A 5 6 O VAL A 168 ? O VAL A 168 N TYR A 194 ? N TYR A 194 
A 6 7 O ARG A 195 ? O ARG A 195 N TYR A 220 ? N TYR A 220 
A 7 8 N TRP A 221 ? N TRP A 221 O VAL A 236 ? O VAL A 236 
B 1 2 N LYS A 98  ? N LYS A 98  O GLY A 109 ? O GLY A 109 
C 1 2 O SER B 58  ? O SER B 58  N VAL B 63  ? N VAL B 63  
C 2 3 N ASP B 70  ? N ASP B 70  O LEU B 75  ? O LEU B 75  
C 3 4 N ILE B 76  ? N ILE B 76  O ARG B 139 ? O ARG B 139 
C 4 5 N PHE B 142 ? N PHE B 142 O ASP B 167 ? O ASP B 167 
C 5 6 O VAL B 168 ? O VAL B 168 N TYR B 194 ? N TYR B 194 
C 6 7 O ARG B 195 ? O ARG B 195 N TYR B 220 ? N TYR B 220 
C 7 8 N TRP B 221 ? N TRP B 221 O VAL B 236 ? O VAL B 236 
D 1 2 N LYS B 98  ? N LYS B 98  O GLY B 109 ? O GLY B 109 
E 1 2 O SER C 58  ? O SER C 58  N VAL C 63  ? N VAL C 63  
E 2 3 N ASP C 70  ? N ASP C 70  O LEU C 75  ? O LEU C 75  
E 3 4 N ILE C 76  ? N ILE C 76  O ARG C 139 ? O ARG C 139 
E 4 5 N PHE C 142 ? N PHE C 142 O ASP C 167 ? O ASP C 167 
E 5 6 O VAL C 168 ? O VAL C 168 N TYR C 194 ? N TYR C 194 
E 6 7 O ARG C 195 ? O ARG C 195 N TYR C 220 ? N TYR C 220 
E 7 8 N TRP C 221 ? N TRP C 221 O VAL C 236 ? O VAL C 236 
F 1 2 N LYS C 98  ? N LYS C 98  O GLY C 109 ? O GLY C 109 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE PLC A 601' 
AC2 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE PLC B 701' 
AC3 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE PLC C 801' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 10 SER A 83  ? SER A 83  . ? 1_555 ? 
2  AC1 10 ARG A 84  ? ARG A 84  . ? 1_555 ? 
3  AC1 10 TRP A 89  ? TRP A 89  . ? 1_555 ? 
4  AC1 10 ASN A 92  ? ASN A 92  . ? 1_555 ? 
5  AC1 10 SER A 146 ? SER A 146 . ? 1_555 ? 
6  AC1 10 VAL A 203 ? VAL A 203 . ? 1_555 ? 
7  AC1 10 ILE A 255 ? ILE A 255 . ? 1_555 ? 
8  AC1 10 PLC E .   ? PLC B 701 . ? 1_555 ? 
9  AC1 10 TRP C 89  ? TRP C 89  . ? 1_555 ? 
10 AC1 10 PLC F .   ? PLC C 801 . ? 1_555 ? 
11 AC2 8  TRP A 89  ? TRP A 89  . ? 1_555 ? 
12 AC2 8  PLC D .   ? PLC A 601 . ? 1_555 ? 
13 AC2 8  SER B 83  ? SER B 83  . ? 1_555 ? 
14 AC2 8  ASN B 92  ? ASN B 92  . ? 1_555 ? 
15 AC2 8  VAL B 203 ? VAL B 203 . ? 1_555 ? 
16 AC2 8  ILE B 255 ? ILE B 255 . ? 1_555 ? 
17 AC2 8  ILE C 255 ? ILE C 255 . ? 1_555 ? 
18 AC2 8  PLC F .   ? PLC C 801 . ? 1_555 ? 
19 AC3 8  ILE A 255 ? ILE A 255 . ? 1_555 ? 
20 AC3 8  PLC D .   ? PLC A 601 . ? 1_555 ? 
21 AC3 8  TRP B 89  ? TRP B 89  . ? 1_555 ? 
22 AC3 8  PLC E .   ? PLC B 701 . ? 1_555 ? 
23 AC3 8  ARG C 84  ? ARG C 84  . ? 1_555 ? 
24 AC3 8  ASN C 92  ? ASN C 92  . ? 1_555 ? 
25 AC3 8  VAL C 203 ? VAL C 203 . ? 1_555 ? 
26 AC3 8  ILE C 255 ? ILE C 255 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1EIN 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    1EIN 
_atom_sites.fract_transf_matrix[1][1]   0.00736 
_atom_sites.fract_transf_matrix[1][2]   0.00425 
_atom_sites.fract_transf_matrix[1][3]   0.00000 
_atom_sites.fract_transf_matrix[2][1]   0.00000 
_atom_sites.fract_transf_matrix[2][2]   0.00849 
_atom_sites.fract_transf_matrix[2][3]   0.00000 
_atom_sites.fract_transf_matrix[3][1]   0.00000 
_atom_sites.fract_transf_matrix[3][2]   0.00000 
_atom_sites.fract_transf_matrix[3][3]   0.00667 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . GLU A 1 1   ? -27.371 55.924  17.343  1.00 44.11 ? 1   GLU A N     1 
ATOM   2    C CA    . GLU A 1 1   ? -28.386 57.017  17.301  1.00 43.22 ? 1   GLU A CA    1 
ATOM   3    C C     . GLU A 1 1   ? -28.932 57.131  15.888  1.00 41.82 ? 1   GLU A C     1 
ATOM   4    O O     . GLU A 1 1   ? -29.570 58.143  15.581  1.00 42.74 ? 1   GLU A O     1 
ATOM   5    C CB    . GLU A 1 1   ? -27.736 58.313  17.760  1.00 48.82 ? 1   GLU A CB    1 
ATOM   6    C CG    . GLU A 1 1   ? -28.212 58.951  19.045  1.00 54.56 ? 1   GLU A CG    1 
ATOM   7    C CD    . GLU A 1 1   ? -29.050 60.204  18.803  1.00 57.51 ? 1   GLU A CD    1 
ATOM   8    O OE1   . GLU A 1 1   ? -29.449 60.871  19.795  1.00 59.46 ? 1   GLU A OE1   1 
ATOM   9    O OE2   . GLU A 1 1   ? -29.319 60.539  17.622  1.00 57.03 ? 1   GLU A OE2   1 
ATOM   10   N N     . VAL A 1 2   ? -28.582 56.210  14.999  1.00 39.81 ? 2   VAL A N     1 
ATOM   11   C CA    . VAL A 1 2   ? -29.078 56.284  13.619  1.00 37.45 ? 2   VAL A CA    1 
ATOM   12   C C     . VAL A 1 2   ? -29.421 54.913  13.064  1.00 36.48 ? 2   VAL A C     1 
ATOM   13   O O     . VAL A 1 2   ? -28.856 53.881  13.431  1.00 36.10 ? 2   VAL A O     1 
ATOM   14   C CB    . VAL A 1 2   ? -28.086 57.081  12.764  1.00 35.57 ? 2   VAL A CB    1 
ATOM   15   C CG1   . VAL A 1 2   ? -27.836 56.537  11.371  1.00 34.81 ? 2   VAL A CG1   1 
ATOM   16   C CG2   . VAL A 1 2   ? -28.549 58.535  12.647  1.00 32.86 ? 2   VAL A CG2   1 
ATOM   17   N N     . SER A 1 3   ? -30.427 54.861  12.188  1.00 35.58 ? 3   SER A N     1 
ATOM   18   C CA    . SER A 1 3   ? -30.779 53.576  11.590  1.00 34.82 ? 3   SER A CA    1 
ATOM   19   C C     . SER A 1 3   ? -29.577 53.103  10.775  1.00 34.48 ? 3   SER A C     1 
ATOM   20   O O     . SER A 1 3   ? -29.030 53.821  9.939   1.00 34.58 ? 3   SER A O     1 
ATOM   21   C CB    . SER A 1 3   ? -32.014 53.656  10.697  1.00 33.72 ? 3   SER A CB    1 
ATOM   22   O OG    . SER A 1 3   ? -31.721 54.442  9.548   1.00 35.03 ? 3   SER A OG    1 
ATOM   23   N N     . GLN A 1 4   ? -29.435 51.789  10.701  1.00 34.47 ? 4   GLN A N     1 
ATOM   24   C CA    . GLN A 1 4   ? -28.467 51.150  9.830   1.00 34.59 ? 4   GLN A CA    1 
ATOM   25   C C     . GLN A 1 4   ? -28.626 51.611  8.390   1.00 34.17 ? 4   GLN A C     1 
ATOM   26   O O     . GLN A 1 4   ? -27.635 51.692  7.674   1.00 34.74 ? 4   GLN A O     1 
ATOM   27   C CB    . GLN A 1 4   ? -28.615 49.629  9.890   1.00 37.40 ? 4   GLN A CB    1 
ATOM   28   C CG    . GLN A 1 4   ? -27.576 48.895  9.050   1.00 40.81 ? 4   GLN A CG    1 
ATOM   29   C CD    . GLN A 1 4   ? -26.206 49.048  9.688   1.00 43.78 ? 4   GLN A CD    1 
ATOM   30   O OE1   . GLN A 1 4   ? -25.246 49.462  9.044   1.00 44.90 ? 4   GLN A OE1   1 
ATOM   31   N NE2   . GLN A 1 4   ? -26.167 48.713  10.978  1.00 45.95 ? 4   GLN A NE2   1 
ATOM   32   N N     . ASP A 1 5   ? -29.820 51.819  7.872   1.00 33.77 ? 5   ASP A N     1 
ATOM   33   C CA    . ASP A 1 5   ? -30.011 52.301  6.521   1.00 33.20 ? 5   ASP A CA    1 
ATOM   34   C C     . ASP A 1 5   ? -29.553 53.744  6.424   1.00 32.55 ? 5   ASP A C     1 
ATOM   35   O O     . ASP A 1 5   ? -29.031 54.065  5.357   1.00 33.26 ? 5   ASP A O     1 
ATOM   36   C CB    . ASP A 1 5   ? -31.459 52.239  6.037   1.00 36.72 ? 5   ASP A CB    1 
ATOM   37   C CG    . ASP A 1 5   ? -32.090 50.876  6.266   1.00 38.91 ? 5   ASP A CG    1 
ATOM   38   O OD1   . ASP A 1 5   ? -32.388 50.163  5.286   1.00 37.74 ? 5   ASP A OD1   1 
ATOM   39   O OD2   . ASP A 1 5   ? -32.240 50.544  7.475   1.00 41.32 ? 5   ASP A OD2   1 
ATOM   40   N N     . LEU A 1 6   ? -29.782 54.596  7.420   1.00 31.46 ? 6   LEU A N     1 
ATOM   41   C CA    . LEU A 1 6   ? -29.318 55.982  7.289   1.00 30.24 ? 6   LEU A CA    1 
ATOM   42   C C     . LEU A 1 6   ? -27.788 56.001  7.285   1.00 30.22 ? 6   LEU A C     1 
ATOM   43   O O     . LEU A 1 6   ? -27.087 56.603  6.480   1.00 30.14 ? 6   LEU A O     1 
ATOM   44   C CB    . LEU A 1 6   ? -29.826 56.846  8.427   1.00 25.93 ? 6   LEU A CB    1 
ATOM   45   C CG    . LEU A 1 6   ? -30.442 58.208  8.130   1.00 23.93 ? 6   LEU A CG    1 
ATOM   46   C CD1   . LEU A 1 6   ? -29.904 59.241  9.102   1.00 21.87 ? 6   LEU A CD1   1 
ATOM   47   C CD2   . LEU A 1 6   ? -30.305 58.700  6.701   1.00 22.69 ? 6   LEU A CD2   1 
ATOM   48   N N     . PHE A 1 7   ? -27.231 55.189  8.184   1.00 30.06 ? 7   PHE A N     1 
ATOM   49   C CA    . PHE A 1 7   ? -25.800 54.981  8.270   1.00 29.83 ? 7   PHE A CA    1 
ATOM   50   C C     . PHE A 1 7   ? -25.262 54.512  6.923   1.00 29.86 ? 7   PHE A C     1 
ATOM   51   O O     . PHE A 1 7   ? -24.206 54.974  6.498   1.00 30.30 ? 7   PHE A O     1 
ATOM   52   C CB    . PHE A 1 7   ? -25.503 53.905  9.313   1.00 29.87 ? 7   PHE A CB    1 
ATOM   53   C CG    . PHE A 1 7   ? -24.020 53.691  9.457   1.00 30.50 ? 7   PHE A CG    1 
ATOM   54   C CD1   . PHE A 1 7   ? -23.310 54.463  10.364  1.00 30.51 ? 7   PHE A CD1   1 
ATOM   55   C CD2   . PHE A 1 7   ? -23.361 52.735  8.698   1.00 28.78 ? 7   PHE A CD2   1 
ATOM   56   C CE1   . PHE A 1 7   ? -21.951 54.279  10.499  1.00 29.41 ? 7   PHE A CE1   1 
ATOM   57   C CE2   . PHE A 1 7   ? -22.002 52.565  8.854   1.00 28.21 ? 7   PHE A CE2   1 
ATOM   58   C CZ    . PHE A 1 7   ? -21.299 53.330  9.760   1.00 28.26 ? 7   PHE A CZ    1 
ATOM   59   N N     . ASN A 1 8   ? -25.937 53.562  6.288   1.00 29.36 ? 8   ASN A N     1 
ATOM   60   C CA    . ASN A 1 8   ? -25.485 53.048  5.017   1.00 29.36 ? 8   ASN A CA    1 
ATOM   61   C C     . ASN A 1 8   ? -25.469 54.135  3.964   1.00 29.48 ? 8   ASN A C     1 
ATOM   62   O O     . ASN A 1 8   ? -24.509 54.257  3.205   1.00 30.19 ? 8   ASN A O     1 
ATOM   63   C CB    . ASN A 1 8   ? -26.302 51.851  4.577   1.00 31.13 ? 8   ASN A CB    1 
ATOM   64   C CG    . ASN A 1 8   ? -26.003 50.600  5.372   1.00 32.31 ? 8   ASN A CG    1 
ATOM   65   O OD1   . ASN A 1 8   ? -25.045 50.458  6.126   1.00 34.52 ? 8   ASN A OD1   1 
ATOM   66   N ND2   . ASN A 1 8   ? -26.908 49.639  5.233   1.00 33.89 ? 8   ASN A ND2   1 
ATOM   67   N N     . GLN A 1 9   ? -26.510 54.943  3.933   1.00 29.34 ? 9   GLN A N     1 
ATOM   68   C CA    . GLN A 1 9   ? -26.563 56.050  2.996   1.00 29.38 ? 9   GLN A CA    1 
ATOM   69   C C     . GLN A 1 9   ? -25.470 57.072  3.263   1.00 29.10 ? 9   GLN A C     1 
ATOM   70   O O     . GLN A 1 9   ? -24.731 57.371  2.337   1.00 28.92 ? 9   GLN A O     1 
ATOM   71   C CB    . GLN A 1 9   ? -27.936 56.715  3.142   1.00 32.46 ? 9   GLN A CB    1 
ATOM   72   C CG    . GLN A 1 9   ? -29.035 55.785  2.699   1.00 36.91 ? 9   GLN A CG    1 
ATOM   73   C CD    . GLN A 1 9   ? -30.190 56.480  2.037   1.00 39.00 ? 9   GLN A CD    1 
ATOM   74   O OE1   . GLN A 1 9   ? -30.339 56.420  0.829   1.00 41.31 ? 9   GLN A OE1   1 
ATOM   75   N NE2   . GLN A 1 9   ? -31.041 57.152  2.793   1.00 42.19 ? 9   GLN A NE2   1 
ATOM   76   N N     . PHE A 1 10  ? -25.226 57.412  4.520   1.00 28.85 ? 10  PHE A N     1 
ATOM   77   C CA    . PHE A 1 10  ? -24.252 58.398  4.936   1.00 28.93 ? 10  PHE A CA    1 
ATOM   78   C C     . PHE A 1 10  ? -22.848 58.048  4.454   1.00 29.52 ? 10  PHE A C     1 
ATOM   79   O O     . PHE A 1 10  ? -22.049 58.896  4.051   1.00 29.76 ? 10  PHE A O     1 
ATOM   80   C CB    . PHE A 1 10  ? -24.266 58.548  6.458   1.00 25.73 ? 10  PHE A CB    1 
ATOM   81   C CG    . PHE A 1 10  ? -25.308 59.466  7.018   1.00 24.99 ? 10  PHE A CG    1 
ATOM   82   C CD1   . PHE A 1 10  ? -26.324 59.998  6.230   1.00 24.32 ? 10  PHE A CD1   1 
ATOM   83   C CD2   . PHE A 1 10  ? -25.285 59.800  8.364   1.00 24.42 ? 10  PHE A CD2   1 
ATOM   84   C CE1   . PHE A 1 10  ? -27.276 60.839  6.753   1.00 22.34 ? 10  PHE A CE1   1 
ATOM   85   C CE2   . PHE A 1 10  ? -26.241 60.647  8.897   1.00 24.50 ? 10  PHE A CE2   1 
ATOM   86   C CZ    . PHE A 1 10  ? -27.236 61.171  8.091   1.00 23.04 ? 10  PHE A CZ    1 
ATOM   87   N N     . ASN A 1 11  ? -22.558 56.756  4.482   1.00 29.42 ? 11  ASN A N     1 
ATOM   88   C CA    . ASN A 1 11  ? -21.300 56.243  4.012   1.00 29.65 ? 11  ASN A CA    1 
ATOM   89   C C     . ASN A 1 11  ? -21.236 56.219  2.502   1.00 29.20 ? 11  ASN A C     1 
ATOM   90   O O     . ASN A 1 11  ? -20.228 56.558  1.889   1.00 29.72 ? 11  ASN A O     1 
ATOM   91   C CB    . ASN A 1 11  ? -21.159 54.815  4.568   1.00 35.08 ? 11  ASN A CB    1 
ATOM   92   C CG    . ASN A 1 11  ? -19.698 54.402  4.559   1.00 38.63 ? 11  ASN A CG    1 
ATOM   93   O OD1   . ASN A 1 11  ? -19.024 54.413  5.588   1.00 42.53 ? 11  ASN A OD1   1 
ATOM   94   N ND2   . ASN A 1 11  ? -19.205 54.056  3.379   1.00 39.29 ? 11  ASN A ND2   1 
ATOM   95   N N     . LEU A 1 12  ? -22.289 55.787  1.831   1.00 28.69 ? 12  LEU A N     1 
ATOM   96   C CA    . LEU A 1 12  ? -22.305 55.660  0.381   1.00 27.77 ? 12  LEU A CA    1 
ATOM   97   C C     . LEU A 1 12  ? -22.051 57.000  -0.295  1.00 27.74 ? 12  LEU A C     1 
ATOM   98   O O     . LEU A 1 12  ? -21.311 57.095  -1.272  1.00 28.13 ? 12  LEU A O     1 
ATOM   99   C CB    . LEU A 1 12  ? -23.660 55.135  -0.101  1.00 24.89 ? 12  LEU A CB    1 
ATOM   100  C CG    . LEU A 1 12  ? -23.741 54.960  -1.621  1.00 23.72 ? 12  LEU A CG    1 
ATOM   101  C CD1   . LEU A 1 12  ? -22.621 54.064  -2.117  1.00 21.22 ? 12  LEU A CD1   1 
ATOM   102  C CD2   . LEU A 1 12  ? -25.116 54.438  -2.005  1.00 22.25 ? 12  LEU A CD2   1 
ATOM   103  N N     . PHE A 1 13  ? -22.659 58.054  0.238   1.00 27.19 ? 13  PHE A N     1 
ATOM   104  C CA    . PHE A 1 13  ? -22.507 59.401  -0.289  1.00 26.48 ? 13  PHE A CA    1 
ATOM   105  C C     . PHE A 1 13  ? -21.254 60.101  0.172   1.00 25.59 ? 13  PHE A C     1 
ATOM   106  O O     . PHE A 1 13  ? -20.731 61.036  -0.428  1.00 25.31 ? 13  PHE A O     1 
ATOM   107  C CB    . PHE A 1 13  ? -23.812 60.176  -0.040  1.00 27.16 ? 13  PHE A CB    1 
ATOM   108  C CG    . PHE A 1 13  ? -24.987 59.584  -0.774  1.00 27.44 ? 13  PHE A CG    1 
ATOM   109  C CD1   . PHE A 1 13  ? -26.096 59.105  -0.097  1.00 27.20 ? 13  PHE A CD1   1 
ATOM   110  C CD2   . PHE A 1 13  ? -24.949 59.454  -2.159  1.00 27.80 ? 13  PHE A CD2   1 
ATOM   111  C CE1   . PHE A 1 13  ? -27.150 58.527  -0.785  1.00 26.47 ? 13  PHE A CE1   1 
ATOM   112  C CE2   . PHE A 1 13  ? -25.992 58.875  -2.853  1.00 26.76 ? 13  PHE A CE2   1 
ATOM   113  C CZ    . PHE A 1 13  ? -27.092 58.415  -2.165  1.00 26.26 ? 13  PHE A CZ    1 
ATOM   114  N N     . ALA A 1 14  ? -20.602 59.598  1.203   1.00 25.34 ? 14  ALA A N     1 
ATOM   115  C CA    . ALA A 1 14  ? -19.325 60.155  1.672   1.00 24.93 ? 14  ALA A CA    1 
ATOM   116  C C     . ALA A 1 14  ? -18.295 59.679  0.654   1.00 24.89 ? 14  ALA A C     1 
ATOM   117  O O     . ALA A 1 14  ? -17.540 60.482  0.116   1.00 25.22 ? 14  ALA A O     1 
ATOM   118  C CB    . ALA A 1 14  ? -18.910 59.696  3.047   1.00 23.08 ? 14  ALA A CB    1 
ATOM   119  N N     . GLN A 1 15  ? -18.513 58.465  0.149   1.00 24.80 ? 15  GLN A N     1 
ATOM   120  C CA    . GLN A 1 15  ? -17.601 58.012  -0.896  1.00 24.84 ? 15  GLN A CA    1 
ATOM   121  C C     . GLN A 1 15  ? -17.876 58.674  -2.226  1.00 24.96 ? 15  GLN A C     1 
ATOM   122  O O     . GLN A 1 15  ? -16.923 58.884  -2.967  1.00 25.20 ? 15  GLN A O     1 
ATOM   123  C CB    . GLN A 1 15  ? -17.627 56.514  -0.998  1.00 25.79 ? 15  GLN A CB    1 
ATOM   124  C CG    . GLN A 1 15  ? -17.115 55.803  0.240   1.00 27.16 ? 15  GLN A CG    1 
ATOM   125  C CD    . GLN A 1 15  ? -17.187 54.310  0.043   1.00 28.76 ? 15  GLN A CD    1 
ATOM   126  O OE1   . GLN A 1 15  ? -17.313 53.594  1.013   1.00 30.23 ? 15  GLN A OE1   1 
ATOM   127  N NE2   . GLN A 1 15  ? -17.132 53.721  -1.144  1.00 28.86 ? 15  GLN A NE2   1 
ATOM   128  N N     . TYR A 1 16  ? -19.105 59.018  -2.577  1.00 25.13 ? 16  TYR A N     1 
ATOM   129  C CA    . TYR A 1 16  ? -19.348 59.697  -3.846  1.00 25.11 ? 16  TYR A CA    1 
ATOM   130  C C     . TYR A 1 16  ? -18.722 61.089  -3.803  1.00 25.36 ? 16  TYR A C     1 
ATOM   131  O O     . TYR A 1 16  ? -18.341 61.634  -4.839  1.00 25.32 ? 16  TYR A O     1 
ATOM   132  C CB    . TYR A 1 16  ? -20.827 59.777  -4.153  1.00 25.37 ? 16  TYR A CB    1 
ATOM   133  C CG    . TYR A 1 16  ? -21.403 58.649  -4.967  1.00 25.81 ? 16  TYR A CG    1 
ATOM   134  C CD1   . TYR A 1 16  ? -21.090 58.516  -6.310  1.00 25.80 ? 16  TYR A CD1   1 
ATOM   135  C CD2   . TYR A 1 16  ? -22.294 57.743  -4.407  1.00 26.13 ? 16  TYR A CD2   1 
ATOM   136  C CE1   . TYR A 1 16  ? -21.643 57.504  -7.067  1.00 26.26 ? 16  TYR A CE1   1 
ATOM   137  C CE2   . TYR A 1 16  ? -22.829 56.706  -5.148  1.00 26.04 ? 16  TYR A CE2   1 
ATOM   138  C CZ    . TYR A 1 16  ? -22.515 56.606  -6.483  1.00 26.24 ? 16  TYR A CZ    1 
ATOM   139  O OH    . TYR A 1 16  ? -23.060 55.598  -7.247  1.00 26.08 ? 16  TYR A OH    1 
ATOM   140  N N     . SER A 1 17  ? -18.802 61.744  -2.645  1.00 25.29 ? 17  SER A N     1 
ATOM   141  C CA    . SER A 1 17  ? -18.189 63.046  -2.449  1.00 25.15 ? 17  SER A CA    1 
ATOM   142  C C     . SER A 1 17  ? -16.680 62.908  -2.669  1.00 25.33 ? 17  SER A C     1 
ATOM   143  O O     . SER A 1 17  ? -16.047 63.486  -3.556  1.00 25.57 ? 17  SER A O     1 
ATOM   144  C CB    . SER A 1 17  ? -18.460 63.592  -1.053  1.00 23.60 ? 17  SER A CB    1 
ATOM   145  O OG    . SER A 1 17  ? -19.827 63.816  -0.801  1.00 23.27 ? 17  SER A OG    1 
ATOM   146  N N     . ALA A 1 18  ? -16.074 62.002  -1.919  1.00 24.89 ? 18  ALA A N     1 
ATOM   147  C CA    . ALA A 1 18  ? -14.664 61.684  -1.985  1.00 24.29 ? 18  ALA A CA    1 
ATOM   148  C C     . ALA A 1 18  ? -14.186 61.490  -3.412  1.00 23.94 ? 18  ALA A C     1 
ATOM   149  O O     . ALA A 1 18  ? -13.068 61.821  -3.792  1.00 24.35 ? 18  ALA A O     1 
ATOM   150  C CB    . ALA A 1 18  ? -14.416 60.338  -1.289  1.00 24.83 ? 18  ALA A CB    1 
ATOM   151  N N     . ALA A 1 19  ? -14.933 60.696  -4.151  1.00 23.48 ? 19  ALA A N     1 
ATOM   152  C CA    . ALA A 1 19  ? -14.704 60.371  -5.535  1.00 23.51 ? 19  ALA A CA    1 
ATOM   153  C C     . ALA A 1 19  ? -14.573 61.571  -6.450  1.00 24.14 ? 19  ALA A C     1 
ATOM   154  O O     . ALA A 1 19  ? -13.959 61.475  -7.514  1.00 24.45 ? 19  ALA A O     1 
ATOM   155  C CB    . ALA A 1 19  ? -15.894 59.531  -6.013  1.00 22.48 ? 19  ALA A CB    1 
ATOM   156  N N     . ALA A 1 20  ? -15.238 62.686  -6.181  1.00 24.41 ? 20  ALA A N     1 
ATOM   157  C CA    . ALA A 1 20  ? -15.184 63.904  -6.951  1.00 24.64 ? 20  ALA A CA    1 
ATOM   158  C C     . ALA A 1 20  ? -13.792 64.536  -6.925  1.00 25.31 ? 20  ALA A C     1 
ATOM   159  O O     . ALA A 1 20  ? -13.482 65.375  -7.789  1.00 25.83 ? 20  ALA A O     1 
ATOM   160  C CB    . ALA A 1 20  ? -16.200 64.913  -6.425  1.00 22.28 ? 20  ALA A CB    1 
ATOM   161  N N     . TYR A 1 21  ? -12.991 64.257  -5.903  1.00 25.22 ? 21  TYR A N     1 
ATOM   162  C CA    . TYR A 1 21  ? -11.676 64.861  -5.853  1.00 26.20 ? 21  TYR A CA    1 
ATOM   163  C C     . TYR A 1 21  ? -10.697 64.152  -6.781  1.00 26.98 ? 21  TYR A C     1 
ATOM   164  O O     . TYR A 1 21  ? -9.729  64.776  -7.211  1.00 27.92 ? 21  TYR A O     1 
ATOM   165  C CB    . TYR A 1 21  ? -11.134 64.864  -4.450  1.00 25.38 ? 21  TYR A CB    1 
ATOM   166  C CG    . TYR A 1 21  ? -11.754 65.814  -3.460  1.00 24.34 ? 21  TYR A CG    1 
ATOM   167  C CD1   . TYR A 1 21  ? -11.232 67.075  -3.232  1.00 23.81 ? 21  TYR A CD1   1 
ATOM   168  C CD2   . TYR A 1 21  ? -12.819 65.417  -2.676  1.00 24.04 ? 21  TYR A CD2   1 
ATOM   169  C CE1   . TYR A 1 21  ? -11.746 67.913  -2.270  1.00 23.13 ? 21  TYR A CE1   1 
ATOM   170  C CE2   . TYR A 1 21  ? -13.350 66.251  -1.711  1.00 23.64 ? 21  TYR A CE2   1 
ATOM   171  C CZ    . TYR A 1 21  ? -12.801 67.490  -1.499  1.00 22.99 ? 21  TYR A CZ    1 
ATOM   172  O OH    . TYR A 1 21  ? -13.293 68.308  -0.511  1.00 22.68 ? 21  TYR A OH    1 
ATOM   173  N N     . CYS A 1 22  ? -10.892 62.866  -7.010  1.00 27.48 ? 22  CYS A N     1 
ATOM   174  C CA    . CYS A 1 22  ? -9.996  62.090  -7.850  1.00 27.96 ? 22  CYS A CA    1 
ATOM   175  C C     . CYS A 1 22  ? -9.924  62.722  -9.238  1.00 29.41 ? 22  CYS A C     1 
ATOM   176  O O     . CYS A 1 22  ? -10.922 62.790  -9.962  1.00 30.01 ? 22  CYS A O     1 
ATOM   177  C CB    . CYS A 1 22  ? -10.435 60.640  -7.958  1.00 23.99 ? 22  CYS A CB    1 
ATOM   178  S SG    . CYS A 1 22  ? -10.516 59.669  -6.470  1.00 22.23 ? 22  CYS A SG    1 
ATOM   179  N N     . GLY A 1 23  ? -8.706  63.025  -9.681  1.00 30.23 ? 23  GLY A N     1 
ATOM   180  C CA    . GLY A 1 23  ? -8.504  63.723  -10.930 1.00 31.49 ? 23  GLY A CA    1 
ATOM   181  C C     . GLY A 1 23  ? -9.185  63.075  -12.112 1.00 32.58 ? 23  GLY A C     1 
ATOM   182  O O     . GLY A 1 23  ? -9.944  63.700  -12.852 1.00 32.83 ? 23  GLY A O     1 
ATOM   183  N N     . LYS A 1 24  ? -9.010  61.767  -12.261 1.00 33.78 ? 24  LYS A N     1 
ATOM   184  C CA    . LYS A 1 24  ? -9.493  61.003  -13.392 1.00 35.09 ? 24  LYS A CA    1 
ATOM   185  C C     . LYS A 1 24  ? -11.004 61.004  -13.521 1.00 35.52 ? 24  LYS A C     1 
ATOM   186  O O     . LYS A 1 24  ? -11.498 60.739  -14.620 1.00 36.21 ? 24  LYS A O     1 
ATOM   187  C CB    . LYS A 1 24  ? -8.990  59.549  -13.376 1.00 38.34 ? 24  LYS A CB    1 
ATOM   188  C CG    . LYS A 1 24  ? -9.169  58.878  -12.028 1.00 42.79 ? 24  LYS A CG    1 
ATOM   189  C CD    . LYS A 1 24  ? -9.243  57.357  -12.060 1.00 44.81 ? 24  LYS A CD    1 
ATOM   190  C CE    . LYS A 1 24  ? -9.258  56.843  -10.616 1.00 46.48 ? 24  LYS A CE    1 
ATOM   191  N NZ    . LYS A 1 24  ? -9.088  55.364  -10.556 1.00 48.75 ? 24  LYS A NZ    1 
ATOM   192  N N     . ASN A 1 25  ? -11.751 61.306  -12.475 1.00 35.49 ? 25  ASN A N     1 
ATOM   193  C CA    . ASN A 1 25  ? -13.194 61.375  -12.474 1.00 35.53 ? 25  ASN A CA    1 
ATOM   194  C C     . ASN A 1 25  ? -13.736 62.737  -12.878 1.00 36.15 ? 25  ASN A C     1 
ATOM   195  O O     . ASN A 1 25  ? -14.842 63.099  -12.452 1.00 36.14 ? 25  ASN A O     1 
ATOM   196  C CB    . ASN A 1 25  ? -13.656 61.159  -11.012 1.00 34.13 ? 25  ASN A CB    1 
ATOM   197  C CG    . ASN A 1 25  ? -13.391 59.743  -10.557 1.00 33.46 ? 25  ASN A CG    1 
ATOM   198  O OD1   . ASN A 1 25  ? -13.203 58.885  -11.418 1.00 33.51 ? 25  ASN A OD1   1 
ATOM   199  N ND2   . ASN A 1 25  ? -13.372 59.498  -9.255  1.00 32.63 ? 25  ASN A ND2   1 
ATOM   200  N N     . ASN A 1 26  ? -12.930 63.616  -13.459 1.00 36.72 ? 26  ASN A N     1 
ATOM   201  C CA    . ASN A 1 26  ? -13.340 64.992  -13.731 1.00 37.08 ? 26  ASN A CA    1 
ATOM   202  C C     . ASN A 1 26  ? -13.300 65.281  -15.225 1.00 38.18 ? 26  ASN A C     1 
ATOM   203  O O     . ASN A 1 26  ? -13.796 66.291  -15.718 1.00 38.14 ? 26  ASN A O     1 
ATOM   204  C CB    . ASN A 1 26  ? -12.422 65.953  -12.984 1.00 33.45 ? 26  ASN A CB    1 
ATOM   205  C CG    . ASN A 1 26  ? -12.494 65.893  -11.479 1.00 32.15 ? 26  ASN A CG    1 
ATOM   206  O OD1   . ASN A 1 26  ? -11.557 66.367  -10.829 1.00 32.33 ? 26  ASN A OD1   1 
ATOM   207  N ND2   . ASN A 1 26  ? -13.542 65.355  -10.873 1.00 31.12 ? 26  ASN A ND2   1 
ATOM   208  N N     . ASP A 1 27  ? -12.760 64.312  -15.956 1.00 39.37 ? 27  ASP A N     1 
ATOM   209  C CA    . ASP A 1 27  ? -12.639 64.365  -17.407 1.00 40.49 ? 27  ASP A CA    1 
ATOM   210  C C     . ASP A 1 27  ? -12.862 62.954  -17.954 1.00 40.50 ? 27  ASP A C     1 
ATOM   211  O O     . ASP A 1 27  ? -12.181 62.520  -18.885 1.00 41.01 ? 27  ASP A O     1 
ATOM   212  C CB    . ASP A 1 27  ? -11.257 64.870  -17.822 1.00 45.21 ? 27  ASP A CB    1 
ATOM   213  C CG    . ASP A 1 27  ? -10.171 63.914  -17.351 1.00 50.67 ? 27  ASP A CG    1 
ATOM   214  O OD1   . ASP A 1 27  ? -9.133  63.784  -18.042 1.00 53.35 ? 27  ASP A OD1   1 
ATOM   215  O OD2   . ASP A 1 27  ? -10.345 63.262  -16.291 1.00 53.34 ? 27  ASP A OD2   1 
ATOM   216  N N     . ALA A 1 28  ? -13.584 62.146  -17.174 1.00 40.27 ? 28  ALA A N     1 
ATOM   217  C CA    . ALA A 1 28  ? -13.890 60.785  -17.631 1.00 39.61 ? 28  ALA A CA    1 
ATOM   218  C C     . ALA A 1 28  ? -14.913 60.907  -18.760 1.00 39.13 ? 28  ALA A C     1 
ATOM   219  O O     . ALA A 1 28  ? -15.696 61.850  -18.788 1.00 39.11 ? 28  ALA A O     1 
ATOM   220  C CB    . ALA A 1 28  ? -14.473 59.953  -16.500 1.00 38.87 ? 28  ALA A CB    1 
ATOM   221  N N     . PRO A 1 29  ? -14.886 59.969  -19.690 1.00 38.88 ? 29  PRO A N     1 
ATOM   222  C CA    . PRO A 1 29  ? -15.821 59.914  -20.799 1.00 38.58 ? 29  PRO A CA    1 
ATOM   223  C C     . PRO A 1 29  ? -17.145 59.296  -20.370 1.00 38.48 ? 29  PRO A C     1 
ATOM   224  O O     . PRO A 1 29  ? -17.127 58.276  -19.679 1.00 38.52 ? 29  PRO A O     1 
ATOM   225  C CB    . PRO A 1 29  ? -15.153 58.991  -21.805 1.00 38.70 ? 29  PRO A CB    1 
ATOM   226  C CG    . PRO A 1 29  ? -13.882 58.512  -21.218 1.00 38.64 ? 29  PRO A CG    1 
ATOM   227  C CD    . PRO A 1 29  ? -13.913 58.847  -19.751 1.00 38.84 ? 29  PRO A CD    1 
ATOM   228  N N     . ALA A 1 30  ? -18.257 59.806  -20.889 1.00 38.57 ? 30  ALA A N     1 
ATOM   229  C CA    . ALA A 1 30  ? -19.571 59.316  -20.480 1.00 38.38 ? 30  ALA A CA    1 
ATOM   230  C C     . ALA A 1 30  ? -19.701 57.817  -20.693 1.00 38.33 ? 30  ALA A C     1 
ATOM   231  O O     . ALA A 1 30  ? -19.361 57.303  -21.751 1.00 38.78 ? 30  ALA A O     1 
ATOM   232  C CB    . ALA A 1 30  ? -20.694 60.010  -21.220 1.00 37.70 ? 30  ALA A CB    1 
ATOM   233  N N     . GLY A 1 31  ? -20.109 57.087  -19.670 1.00 38.44 ? 31  GLY A N     1 
ATOM   234  C CA    . GLY A 1 31  ? -20.324 55.656  -19.788 1.00 38.21 ? 31  GLY A CA    1 
ATOM   235  C C     . GLY A 1 31  ? -19.244 54.865  -19.083 1.00 38.29 ? 31  GLY A C     1 
ATOM   236  O O     . GLY A 1 31  ? -19.495 53.721  -18.707 1.00 38.56 ? 31  GLY A O     1 
ATOM   237  N N     . THR A 1 32  ? -18.048 55.406  -18.933 1.00 38.31 ? 32  THR A N     1 
ATOM   238  C CA    . THR A 1 32  ? -16.990 54.701  -18.201 1.00 38.29 ? 32  THR A CA    1 
ATOM   239  C C     . THR A 1 32  ? -17.411 54.541  -16.748 1.00 38.60 ? 32  THR A C     1 
ATOM   240  O O     . THR A 1 32  ? -18.488 55.012  -16.372 1.00 38.70 ? 32  THR A O     1 
ATOM   241  C CB    . THR A 1 32  ? -15.728 55.578  -18.294 1.00 38.23 ? 32  THR A CB    1 
ATOM   242  O OG1   . THR A 1 32  ? -16.130 56.878  -17.827 1.00 38.45 ? 32  THR A OG1   1 
ATOM   243  C CG2   . THR A 1 32  ? -15.294 55.678  -19.743 1.00 38.67 ? 32  THR A CG2   1 
ATOM   244  N N     . ASN A 1 33  ? -16.587 53.911  -15.914 1.00 38.78 ? 33  ASN A N     1 
ATOM   245  C CA    . ASN A 1 33  ? -16.944 53.672  -14.529 1.00 39.08 ? 33  ASN A CA    1 
ATOM   246  C C     . ASN A 1 33  ? -16.241 54.514  -13.481 1.00 38.50 ? 33  ASN A C     1 
ATOM   247  O O     . ASN A 1 33  ? -15.036 54.723  -13.557 1.00 38.63 ? 33  ASN A O     1 
ATOM   248  C CB    . ASN A 1 33  ? -16.675 52.203  -14.194 1.00 45.33 ? 33  ASN A CB    1 
ATOM   249  C CG    . ASN A 1 33  ? -17.192 51.209  -15.208 1.00 49.35 ? 33  ASN A CG    1 
ATOM   250  O OD1   . ASN A 1 33  ? -17.042 51.345  -16.424 1.00 51.94 ? 33  ASN A OD1   1 
ATOM   251  N ND2   . ASN A 1 33  ? -17.810 50.128  -14.732 1.00 51.43 ? 33  ASN A ND2   1 
ATOM   252  N N     . ILE A 1 34  ? -17.003 54.983  -12.491 1.00 38.12 ? 34  ILE A N     1 
ATOM   253  C CA    . ILE A 1 34  ? -16.429 55.744  -11.390 1.00 37.31 ? 34  ILE A CA    1 
ATOM   254  C C     . ILE A 1 34  ? -15.505 54.821  -10.599 1.00 36.98 ? 34  ILE A C     1 
ATOM   255  O O     . ILE A 1 34  ? -15.852 53.697  -10.243 1.00 37.06 ? 34  ILE A O     1 
ATOM   256  C CB    . ILE A 1 34  ? -17.457 56.344  -10.429 1.00 36.35 ? 34  ILE A CB    1 
ATOM   257  C CG1   . ILE A 1 34  ? -18.223 57.462  -11.141 1.00 36.56 ? 34  ILE A CG1   1 
ATOM   258  C CG2   . ILE A 1 34  ? -16.793 56.940  -9.194  1.00 36.84 ? 34  ILE A CG2   1 
ATOM   259  C CD1   . ILE A 1 34  ? -19.405 56.957  -11.910 1.00 34.84 ? 34  ILE A CD1   1 
ATOM   260  N N     . THR A 1 35  ? -14.244 55.229  -10.517 1.00 36.53 ? 35  THR A N     1 
ATOM   261  C CA    . THR A 1 35  ? -13.269 54.491  -9.719  1.00 36.09 ? 35  THR A CA    1 
ATOM   262  C C     . THR A 1 35  ? -12.435 55.505  -8.919  1.00 35.57 ? 35  THR A C     1 
ATOM   263  O O     . THR A 1 35  ? -12.543 56.704  -9.166  1.00 35.15 ? 35  THR A O     1 
ATOM   264  C CB    . THR A 1 35  ? -12.246 53.752  -10.598 1.00 35.66 ? 35  THR A CB    1 
ATOM   265  O OG1   . THR A 1 35  ? -11.654 54.765  -11.428 1.00 37.65 ? 35  THR A OG1   1 
ATOM   266  C CG2   . THR A 1 35  ? -12.845 52.687  -11.478 1.00 35.37 ? 35  THR A CG2   1 
ATOM   267  N N     . CYS A 1 36  ? -11.800 55.046  -7.850  1.00 35.01 ? 36  CYS A N     1 
ATOM   268  C CA    . CYS A 1 36  ? -10.943 55.914  -7.078  1.00 34.73 ? 36  CYS A CA    1 
ATOM   269  C C     . CYS A 1 36  ? -9.593  55.268  -6.814  1.00 35.25 ? 36  CYS A C     1 
ATOM   270  O O     . CYS A 1 36  ? -9.496  54.111  -6.411  1.00 35.30 ? 36  CYS A O     1 
ATOM   271  C CB    . CYS A 1 36  ? -11.600 56.283  -5.744  1.00 31.70 ? 36  CYS A CB    1 
ATOM   272  S SG    . CYS A 1 36  ? -13.247 56.955  -5.955  1.00 30.05 ? 36  CYS A SG    1 
ATOM   273  N N     . THR A 1 37  ? -8.557  56.096  -6.975  1.00 35.90 ? 37  THR A N     1 
ATOM   274  C CA    . THR A 1 37  ? -7.222  55.629  -6.575  1.00 36.51 ? 37  THR A CA    1 
ATOM   275  C C     . THR A 1 37  ? -7.271  55.406  -5.064  1.00 37.14 ? 37  THR A C     1 
ATOM   276  O O     . THR A 1 37  ? -8.167  55.893  -4.364  1.00 36.73 ? 37  THR A O     1 
ATOM   277  C CB    . THR A 1 37  ? -6.114  56.592  -6.987  1.00 35.73 ? 37  THR A CB    1 
ATOM   278  O OG1   . THR A 1 37  ? -6.269  57.822  -6.275  1.00 36.35 ? 37  THR A OG1   1 
ATOM   279  C CG2   . THR A 1 37  ? -6.195  56.868  -8.484  1.00 36.23 ? 37  THR A CG2   1 
ATOM   280  N N     . GLY A 1 38  ? -6.332  54.607  -4.568  1.00 38.02 ? 38  GLY A N     1 
ATOM   281  C CA    . GLY A 1 38  ? -6.346  54.281  -3.126  1.00 39.06 ? 38  GLY A CA    1 
ATOM   282  C C     . GLY A 1 38  ? -7.598  53.420  -2.907  1.00 40.01 ? 38  GLY A C     1 
ATOM   283  O O     . GLY A 1 38  ? -7.962  52.600  -3.760  1.00 40.42 ? 38  GLY A O     1 
ATOM   284  N N     . ASN A 1 39  ? -8.225  53.598  -1.752  1.00 40.72 ? 39  ASN A N     1 
ATOM   285  C CA    . ASN A 1 39  ? -9.547  52.990  -1.592  1.00 41.17 ? 39  ASN A CA    1 
ATOM   286  C C     . ASN A 1 39  ? -10.525 54.106  -1.270  1.00 40.81 ? 39  ASN A C     1 
ATOM   287  O O     . ASN A 1 39  ? -11.521 53.881  -0.597  1.00 41.57 ? 39  ASN A O     1 
ATOM   288  C CB    . ASN A 1 39  ? -9.563  51.869  -0.570  1.00 46.57 ? 39  ASN A CB    1 
ATOM   289  C CG    . ASN A 1 39  ? -10.021 50.577  -1.236  1.00 51.17 ? 39  ASN A CG    1 
ATOM   290  O OD1   . ASN A 1 39  ? -10.413 49.630  -0.536  1.00 54.73 ? 39  ASN A OD1   1 
ATOM   291  N ND2   . ASN A 1 39  ? -9.998  50.524  -2.569  1.00 50.96 ? 39  ASN A ND2   1 
ATOM   292  N N     . ALA A 1 40  ? -10.356 55.252  -1.919  1.00 39.91 ? 40  ALA A N     1 
ATOM   293  C CA    . ALA A 1 40  ? -11.223 56.390  -1.672  1.00 38.85 ? 40  ALA A CA    1 
ATOM   294  C C     . ALA A 1 40  ? -12.686 56.018  -1.820  1.00 38.14 ? 40  ALA A C     1 
ATOM   295  O O     . ALA A 1 40  ? -13.464 56.404  -0.947  1.00 38.59 ? 40  ALA A O     1 
ATOM   296  C CB    . ALA A 1 40  ? -10.838 57.544  -2.584  1.00 40.61 ? 40  ALA A CB    1 
ATOM   297  N N     . CYS A 1 41  ? -13.105 55.225  -2.797  1.00 37.14 ? 41  CYS A N     1 
ATOM   298  C CA    . CYS A 1 41  ? -14.501 54.857  -2.948  1.00 36.04 ? 41  CYS A CA    1 
ATOM   299  C C     . CYS A 1 41  ? -14.762 53.407  -3.324  1.00 36.03 ? 41  CYS A C     1 
ATOM   300  O O     . CYS A 1 41  ? -15.469 53.120  -4.309  1.00 35.76 ? 41  CYS A O     1 
ATOM   301  C CB    . CYS A 1 41  ? -15.139 55.735  -4.041  1.00 32.93 ? 41  CYS A CB    1 
ATOM   302  S SG    . CYS A 1 41  ? -14.537 55.422  -5.727  1.00 29.53 ? 41  CYS A SG    1 
ATOM   303  N N     . PRO A 1 42  ? -14.621 52.510  -2.351  1.00 36.06 ? 42  PRO A N     1 
ATOM   304  C CA    . PRO A 1 42  ? -14.849 51.088  -2.589  1.00 36.10 ? 42  PRO A CA    1 
ATOM   305  C C     . PRO A 1 42  ? -16.298 50.834  -2.966  1.00 36.51 ? 42  PRO A C     1 
ATOM   306  O O     . PRO A 1 42  ? -16.573 50.472  -4.113  1.00 36.32 ? 42  PRO A O     1 
ATOM   307  C CB    . PRO A 1 42  ? -14.405 50.402  -1.312  1.00 35.55 ? 42  PRO A CB    1 
ATOM   308  C CG    . PRO A 1 42  ? -14.530 51.447  -0.269  1.00 35.88 ? 42  PRO A CG    1 
ATOM   309  C CD    . PRO A 1 42  ? -14.245 52.764  -0.946  1.00 36.06 ? 42  PRO A CD    1 
ATOM   310  N N     . GLU A 1 43  ? -17.248 51.275  -2.135  1.00 37.03 ? 43  GLU A N     1 
ATOM   311  C CA    . GLU A 1 43  ? -18.667 51.069  -2.361  1.00 37.04 ? 43  GLU A CA    1 
ATOM   312  C C     . GLU A 1 43  ? -19.141 51.487  -3.746  1.00 36.35 ? 43  GLU A C     1 
ATOM   313  O O     . GLU A 1 43  ? -19.962 50.830  -4.374  1.00 36.00 ? 43  GLU A O     1 
ATOM   314  C CB    . GLU A 1 43  ? -19.554 51.831  -1.381  1.00 40.88 ? 43  GLU A CB    1 
ATOM   315  C CG    . GLU A 1 43  ? -19.633 51.331  0.039   1.00 45.94 ? 43  GLU A CG    1 
ATOM   316  C CD    . GLU A 1 43  ? -19.794 49.824  0.098   1.00 49.62 ? 43  GLU A CD    1 
ATOM   317  O OE1   . GLU A 1 43  ? -20.654 49.291  -0.637  1.00 51.42 ? 43  GLU A OE1   1 
ATOM   318  O OE2   . GLU A 1 43  ? -18.972 49.248  0.847   1.00 52.15 ? 43  GLU A OE2   1 
ATOM   319  N N     . VAL A 1 44  ? -18.825 52.724  -4.112  1.00 35.95 ? 44  VAL A N     1 
ATOM   320  C CA    . VAL A 1 44  ? -19.174 53.228  -5.442  1.00 35.24 ? 44  VAL A CA    1 
ATOM   321  C C     . VAL A 1 44  ? -18.620 52.332  -6.536  1.00 35.37 ? 44  VAL A C     1 
ATOM   322  O O     . VAL A 1 44  ? -19.322 52.092  -7.514  1.00 34.97 ? 44  VAL A O     1 
ATOM   323  C CB    . VAL A 1 44  ? -18.667 54.674  -5.592  1.00 33.27 ? 44  VAL A CB    1 
ATOM   324  C CG1   . VAL A 1 44  ? -19.015 55.263  -6.938  1.00 31.05 ? 44  VAL A CG1   1 
ATOM   325  C CG2   . VAL A 1 44  ? -19.209 55.520  -4.450  1.00 31.89 ? 44  VAL A CG2   1 
ATOM   326  N N     . GLU A 1 45  ? -17.394 51.822  -6.422  1.00 35.71 ? 45  GLU A N     1 
ATOM   327  C CA    . GLU A 1 45  ? -16.812 50.938  -7.421  1.00 36.30 ? 45  GLU A CA    1 
ATOM   328  C C     . GLU A 1 45  ? -17.553 49.602  -7.416  1.00 36.61 ? 45  GLU A C     1 
ATOM   329  O O     . GLU A 1 45  ? -17.865 48.985  -8.429  1.00 36.33 ? 45  GLU A O     1 
ATOM   330  C CB    . GLU A 1 45  ? -15.329 50.692  -7.152  1.00 37.99 ? 45  GLU A CB    1 
ATOM   331  C CG    . GLU A 1 45  ? -14.386 51.850  -7.402  1.00 42.15 ? 45  GLU A CG    1 
ATOM   332  C CD    . GLU A 1 45  ? -13.001 51.650  -6.811  1.00 43.73 ? 45  GLU A CD    1 
ATOM   333  O OE1   . GLU A 1 45  ? -12.870 51.202  -5.651  1.00 44.77 ? 45  GLU A OE1   1 
ATOM   334  O OE2   . GLU A 1 45  ? -12.021 51.950  -7.524  1.00 44.96 ? 45  GLU A OE2   1 
ATOM   335  N N     . LYS A 1 46  ? -17.945 49.179  -6.219  1.00 37.23 ? 46  LYS A N     1 
ATOM   336  C CA    . LYS A 1 46  ? -18.726 47.973  -5.996  1.00 37.79 ? 46  LYS A CA    1 
ATOM   337  C C     . LYS A 1 46  ? -20.069 48.067  -6.705  1.00 37.67 ? 46  LYS A C     1 
ATOM   338  O O     . LYS A 1 46  ? -20.509 47.087  -7.305  1.00 38.20 ? 46  LYS A O     1 
ATOM   339  C CB    . LYS A 1 46  ? -18.908 47.735  -4.503  1.00 40.06 ? 46  LYS A CB    1 
ATOM   340  C CG    . LYS A 1 46  ? -19.439 46.369  -4.119  1.00 43.31 ? 46  LYS A CG    1 
ATOM   341  C CD    . LYS A 1 46  ? -20.024 46.421  -2.705  1.00 47.26 ? 46  LYS A CD    1 
ATOM   342  C CE    . LYS A 1 46  ? -18.922 46.246  -1.675  1.00 49.73 ? 46  LYS A CE    1 
ATOM   343  N NZ    . LYS A 1 46  ? -19.256 46.873  -0.364  1.00 51.41 ? 46  LYS A NZ    1 
ATOM   344  N N     . ALA A 1 47  ? -20.740 49.204  -6.687  1.00 37.50 ? 47  ALA A N     1 
ATOM   345  C CA    . ALA A 1 47  ? -21.990 49.381  -7.408  1.00 37.44 ? 47  ALA A CA    1 
ATOM   346  C C     . ALA A 1 47  ? -21.748 49.466  -8.911  1.00 37.61 ? 47  ALA A C     1 
ATOM   347  O O     . ALA A 1 47  ? -20.617 49.602  -9.369  1.00 37.49 ? 47  ALA A O     1 
ATOM   348  C CB    . ALA A 1 47  ? -22.690 50.665  -6.976  1.00 37.65 ? 47  ALA A CB    1 
ATOM   349  N N     . ASP A 1 48  ? -22.843 49.457  -9.667  1.00 37.97 ? 48  ASP A N     1 
ATOM   350  C CA    . ASP A 1 48  ? -22.759 49.621  -11.125 1.00 38.98 ? 48  ASP A CA    1 
ATOM   351  C C     . ASP A 1 48  ? -22.886 51.115  -11.443 1.00 38.83 ? 48  ASP A C     1 
ATOM   352  O O     . ASP A 1 48  ? -23.972 51.566  -11.865 1.00 38.97 ? 48  ASP A O     1 
ATOM   353  C CB    . ASP A 1 48  ? -23.862 48.836  -11.824 1.00 44.22 ? 48  ASP A CB    1 
ATOM   354  C CG    . ASP A 1 48  ? -23.995 49.038  -13.321 1.00 48.18 ? 48  ASP A CG    1 
ATOM   355  O OD1   . ASP A 1 48  ? -24.875 48.394  -13.953 1.00 49.94 ? 48  ASP A OD1   1 
ATOM   356  O OD2   . ASP A 1 48  ? -23.273 49.865  -13.930 1.00 49.64 ? 48  ASP A OD2   1 
ATOM   357  N N     . ALA A 1 49  ? -21.823 51.884  -11.176 1.00 37.83 ? 49  ALA A N     1 
ATOM   358  C CA    . ALA A 1 49  ? -21.982 53.339  -11.295 1.00 36.97 ? 49  ALA A CA    1 
ATOM   359  C C     . ALA A 1 49  ? -21.173 53.860  -12.455 1.00 36.63 ? 49  ALA A C     1 
ATOM   360  O O     . ALA A 1 49  ? -19.996 53.519  -12.548 1.00 37.41 ? 49  ALA A O     1 
ATOM   361  C CB    . ALA A 1 49  ? -21.600 53.995  -9.984  1.00 36.42 ? 49  ALA A CB    1 
ATOM   362  N N     . THR A 1 50  ? -21.763 54.606  -13.372 1.00 36.01 ? 50  THR A N     1 
ATOM   363  C CA    . THR A 1 50  ? -21.044 55.072  -14.551 1.00 35.60 ? 50  THR A CA    1 
ATOM   364  C C     . THR A 1 50  ? -21.253 56.562  -14.794 1.00 35.59 ? 50  THR A C     1 
ATOM   365  O O     . THR A 1 50  ? -22.146 57.167  -14.188 1.00 36.20 ? 50  THR A O     1 
ATOM   366  C CB    . THR A 1 50  ? -21.537 54.316  -15.795 1.00 36.07 ? 50  THR A CB    1 
ATOM   367  O OG1   . THR A 1 50  ? -22.969 54.449  -15.877 1.00 36.55 ? 50  THR A OG1   1 
ATOM   368  C CG2   . THR A 1 50  ? -21.177 52.846  -15.780 1.00 35.60 ? 50  THR A CG2   1 
ATOM   369  N N     . PHE A 1 51  ? -20.315 57.194  -15.501 1.00 35.00 ? 51  PHE A N     1 
ATOM   370  C CA    . PHE A 1 51  ? -20.380 58.636  -15.679 1.00 34.15 ? 51  PHE A CA    1 
ATOM   371  C C     . PHE A 1 51  ? -21.480 59.029  -16.645 1.00 33.96 ? 51  PHE A C     1 
ATOM   372  O O     . PHE A 1 51  ? -21.549 58.507  -17.745 1.00 34.09 ? 51  PHE A O     1 
ATOM   373  C CB    . PHE A 1 51  ? -19.056 59.211  -16.192 1.00 32.51 ? 51  PHE A CB    1 
ATOM   374  C CG    . PHE A 1 51  ? -17.996 59.164  -15.129 1.00 32.63 ? 51  PHE A CG    1 
ATOM   375  C CD1   . PHE A 1 51  ? -17.908 60.165  -14.187 1.00 32.31 ? 51  PHE A CD1   1 
ATOM   376  C CD2   . PHE A 1 51  ? -17.105 58.102  -15.076 1.00 32.44 ? 51  PHE A CD2   1 
ATOM   377  C CE1   . PHE A 1 51  ? -16.935 60.117  -13.205 1.00 33.13 ? 51  PHE A CE1   1 
ATOM   378  C CE2   . PHE A 1 51  ? -16.139 58.060  -14.097 1.00 32.36 ? 51  PHE A CE2   1 
ATOM   379  C CZ    . PHE A 1 51  ? -16.044 59.065  -13.158 1.00 32.56 ? 51  PHE A CZ    1 
ATOM   380  N N     . LEU A 1 52  ? -22.312 59.977  -16.262 1.00 34.00 ? 52  LEU A N     1 
ATOM   381  C CA    . LEU A 1 52  ? -23.302 60.524  -17.185 1.00 34.16 ? 52  LEU A CA    1 
ATOM   382  C C     . LEU A 1 52  ? -22.710 61.816  -17.757 1.00 34.66 ? 52  LEU A C     1 
ATOM   383  O O     . LEU A 1 52  ? -22.880 62.131  -18.923 1.00 35.06 ? 52  LEU A O     1 
ATOM   384  C CB    . LEU A 1 52  ? -24.615 60.831  -16.501 1.00 31.90 ? 52  LEU A CB    1 
ATOM   385  C CG    . LEU A 1 52  ? -25.890 60.044  -16.734 1.00 28.61 ? 52  LEU A CG    1 
ATOM   386  C CD1   . LEU A 1 52  ? -25.701 58.739  -17.460 1.00 26.13 ? 52  LEU A CD1   1 
ATOM   387  C CD2   . LEU A 1 52  ? -26.579 59.784  -15.401 1.00 28.20 ? 52  LEU A CD2   1 
ATOM   388  N N     . TYR A 1 53  ? -22.053 62.582  -16.902 1.00 35.19 ? 53  TYR A N     1 
ATOM   389  C CA    . TYR A 1 53  ? -21.460 63.859  -17.264 1.00 35.78 ? 53  TYR A CA    1 
ATOM   390  C C     . TYR A 1 53  ? -20.331 64.130  -16.276 1.00 36.19 ? 53  TYR A C     1 
ATOM   391  O O     . TYR A 1 53  ? -20.575 64.108  -15.076 1.00 36.80 ? 53  TYR A O     1 
ATOM   392  C CB    . TYR A 1 53  ? -22.431 65.022  -17.095 1.00 36.52 ? 53  TYR A CB    1 
ATOM   393  C CG    . TYR A 1 53  ? -21.912 66.383  -17.476 1.00 37.78 ? 53  TYR A CG    1 
ATOM   394  C CD1   . TYR A 1 53  ? -21.246 66.583  -18.672 1.00 38.23 ? 53  TYR A CD1   1 
ATOM   395  C CD2   . TYR A 1 53  ? -22.146 67.496  -16.674 1.00 38.90 ? 53  TYR A CD2   1 
ATOM   396  C CE1   . TYR A 1 53  ? -20.812 67.835  -19.054 1.00 38.88 ? 53  TYR A CE1   1 
ATOM   397  C CE2   . TYR A 1 53  ? -21.719 68.761  -17.044 1.00 39.31 ? 53  TYR A CE2   1 
ATOM   398  C CZ    . TYR A 1 53  ? -21.050 68.917  -18.239 1.00 39.61 ? 53  TYR A CZ    1 
ATOM   399  O OH    . TYR A 1 53  ? -20.603 70.169  -18.601 1.00 40.64 ? 53  TYR A OH    1 
ATOM   400  N N     . SER A 1 54  ? -19.152 64.379  -16.784 1.00 36.58 ? 54  SER A N     1 
ATOM   401  C CA    . SER A 1 54  ? -17.975 64.651  -15.964 1.00 36.51 ? 54  SER A CA    1 
ATOM   402  C C     . SER A 1 54  ? -17.587 66.101  -16.238 1.00 36.63 ? 54  SER A C     1 
ATOM   403  O O     . SER A 1 54  ? -17.339 66.373  -17.417 1.00 37.19 ? 54  SER A O     1 
ATOM   404  C CB    . SER A 1 54  ? -16.838 63.778  -16.509 1.00 37.42 ? 54  SER A CB    1 
ATOM   405  O OG    . SER A 1 54  ? -15.952 63.334  -15.510 1.00 38.99 ? 54  SER A OG    1 
ATOM   406  N N     . PHE A 1 55  ? -17.535 66.964  -15.244 1.00 36.59 ? 55  PHE A N     1 
ATOM   407  C CA    . PHE A 1 55  ? -17.107 68.334  -15.523 1.00 36.64 ? 55  PHE A CA    1 
ATOM   408  C C     . PHE A 1 55  ? -15.993 68.809  -14.606 1.00 37.22 ? 55  PHE A C     1 
ATOM   409  O O     . PHE A 1 55  ? -15.776 68.359  -13.478 1.00 37.31 ? 55  PHE A O     1 
ATOM   410  C CB    . PHE A 1 55  ? -18.296 69.280  -15.477 1.00 34.70 ? 55  PHE A CB    1 
ATOM   411  C CG    . PHE A 1 55  ? -19.045 69.243  -14.174 1.00 33.21 ? 55  PHE A CG    1 
ATOM   412  C CD1   . PHE A 1 55  ? -20.053 68.329  -13.946 1.00 33.75 ? 55  PHE A CD1   1 
ATOM   413  C CD2   . PHE A 1 55  ? -18.746 70.135  -13.166 1.00 32.46 ? 55  PHE A CD2   1 
ATOM   414  C CE1   . PHE A 1 55  ? -20.752 68.318  -12.754 1.00 33.84 ? 55  PHE A CE1   1 
ATOM   415  C CE2   . PHE A 1 55  ? -19.455 70.153  -11.986 1.00 31.84 ? 55  PHE A CE2   1 
ATOM   416  C CZ    . PHE A 1 55  ? -20.453 69.232  -11.765 1.00 32.47 ? 55  PHE A CZ    1 
ATOM   417  N N     . GLU A 1 56  ? -15.178 69.700  -15.167 1.00 37.87 ? 56  GLU A N     1 
ATOM   418  C CA    . GLU A 1 56  ? -14.073 70.290  -14.421 1.00 38.27 ? 56  GLU A CA    1 
ATOM   419  C C     . GLU A 1 56  ? -13.786 71.697  -14.946 1.00 38.08 ? 56  GLU A C     1 
ATOM   420  O O     . GLU A 1 56  ? -14.004 72.033  -16.105 1.00 37.72 ? 56  GLU A O     1 
ATOM   421  C CB    . GLU A 1 56  ? -12.815 69.441  -14.520 1.00 40.57 ? 56  GLU A CB    1 
ATOM   422  C CG    . GLU A 1 56  ? -12.099 69.605  -15.854 1.00 44.46 ? 56  GLU A CG    1 
ATOM   423  C CD    . GLU A 1 56  ? -10.740 68.931  -15.836 1.00 47.01 ? 56  GLU A CD    1 
ATOM   424  O OE1   . GLU A 1 56  ? -10.148 68.855  -14.736 1.00 47.34 ? 56  GLU A OE1   1 
ATOM   425  O OE2   . GLU A 1 56  ? -10.285 68.486  -16.914 1.00 49.61 ? 56  GLU A OE2   1 
ATOM   426  N N     . ASP A 1 57  ? -13.446 72.541  -13.986 1.00 38.20 ? 57  ASP A N     1 
ATOM   427  C CA    . ASP A 1 57  ? -13.115 73.933  -14.263 1.00 38.20 ? 57  ASP A CA    1 
ATOM   428  C C     . ASP A 1 57  ? -14.221 74.617  -15.037 1.00 37.43 ? 57  ASP A C     1 
ATOM   429  O O     . ASP A 1 57  ? -13.994 75.192  -16.093 1.00 37.86 ? 57  ASP A O     1 
ATOM   430  C CB    . ASP A 1 57  ? -11.745 73.935  -14.930 1.00 41.70 ? 57  ASP A CB    1 
ATOM   431  C CG    . ASP A 1 57  ? -11.226 75.347  -15.129 1.00 45.22 ? 57  ASP A CG    1 
ATOM   432  O OD1   . ASP A 1 57  ? -11.556 76.188  -14.259 1.00 47.45 ? 57  ASP A OD1   1 
ATOM   433  O OD2   . ASP A 1 57  ? -10.579 75.559  -16.180 1.00 45.89 ? 57  ASP A OD2   1 
ATOM   434  N N     . SER A 1 58  ? -15.439 74.590  -14.508 1.00 36.66 ? 58  SER A N     1 
ATOM   435  C CA    . SER A 1 58  ? -16.600 75.144  -15.177 1.00 35.95 ? 58  SER A CA    1 
ATOM   436  C C     . SER A 1 58  ? -17.084 76.420  -14.513 1.00 35.28 ? 58  SER A C     1 
ATOM   437  O O     . SER A 1 58  ? -16.855 76.616  -13.319 1.00 35.54 ? 58  SER A O     1 
ATOM   438  C CB    . SER A 1 58  ? -17.758 74.134  -15.184 1.00 36.54 ? 58  SER A CB    1 
ATOM   439  O OG    . SER A 1 58  ? -17.626 73.281  -16.308 1.00 39.78 ? 58  SER A OG    1 
ATOM   440  N N     . GLY A 1 59  ? -17.839 77.210  -15.265 1.00 34.57 ? 59  GLY A N     1 
ATOM   441  C CA    . GLY A 1 59  ? -18.409 78.443  -14.731 1.00 33.73 ? 59  GLY A CA    1 
ATOM   442  C C     . GLY A 1 59  ? -17.351 79.261  -14.004 1.00 33.36 ? 59  GLY A C     1 
ATOM   443  O O     . GLY A 1 59  ? -16.245 79.457  -14.524 1.00 33.69 ? 59  GLY A O     1 
ATOM   444  N N     . VAL A 1 60  ? -17.753 79.911  -12.919 1.00 32.58 ? 60  VAL A N     1 
ATOM   445  C CA    . VAL A 1 60  ? -16.803 80.745  -12.188 1.00 32.14 ? 60  VAL A CA    1 
ATOM   446  C C     . VAL A 1 60  ? -16.469 80.079  -10.869 1.00 32.04 ? 60  VAL A C     1 
ATOM   447  O O     . VAL A 1 60  ? -17.335 79.514  -10.204 1.00 32.40 ? 60  VAL A O     1 
ATOM   448  C CB    . VAL A 1 60  ? -17.319 82.174  -11.988 1.00 31.21 ? 60  VAL A CB    1 
ATOM   449  C CG1   . VAL A 1 60  ? -17.929 82.711  -13.282 1.00 31.74 ? 60  VAL A CG1   1 
ATOM   450  C CG2   . VAL A 1 60  ? -18.356 82.280  -10.882 1.00 30.59 ? 60  VAL A CG2   1 
ATOM   451  N N     . GLY A 1 61  ? -15.202 80.067  -10.491 1.00 32.08 ? 61  GLY A N     1 
ATOM   452  C CA    . GLY A 1 61  ? -14.796 79.525  -9.195  1.00 31.59 ? 61  GLY A CA    1 
ATOM   453  C C     . GLY A 1 61  ? -14.406 78.062  -9.327  1.00 31.13 ? 61  GLY A C     1 
ATOM   454  O O     . GLY A 1 61  ? -14.456 77.300  -8.373  1.00 31.05 ? 61  GLY A O     1 
ATOM   455  N N     . ASP A 1 62  ? -14.150 77.641  -10.554 1.00 31.13 ? 62  ASP A N     1 
ATOM   456  C CA    . ASP A 1 62  ? -13.709 76.282  -10.837 1.00 31.08 ? 62  ASP A CA    1 
ATOM   457  C C     . ASP A 1 62  ? -14.673 75.233  -10.306 1.00 31.27 ? 62  ASP A C     1 
ATOM   458  O O     . ASP A 1 62  ? -14.397 74.530  -9.333  1.00 31.44 ? 62  ASP A O     1 
ATOM   459  C CB    . ASP A 1 62  ? -12.313 76.109  -10.256 1.00 30.89 ? 62  ASP A CB    1 
ATOM   460  C CG    . ASP A 1 62  ? -11.702 74.770  -10.583 1.00 33.03 ? 62  ASP A CG    1 
ATOM   461  O OD1   . ASP A 1 62  ? -12.056 74.136  -11.592 1.00 33.78 ? 62  ASP A OD1   1 
ATOM   462  O OD2   . ASP A 1 62  ? -10.846 74.328  -9.791  1.00 33.93 ? 62  ASP A OD2   1 
ATOM   463  N N     . VAL A 1 63  ? -15.875 75.189  -10.883 1.00 31.13 ? 63  VAL A N     1 
ATOM   464  C CA    . VAL A 1 63  ? -16.871 74.204  -10.474 1.00 30.91 ? 63  VAL A CA    1 
ATOM   465  C C     . VAL A 1 63  ? -16.551 72.866  -11.132 1.00 30.81 ? 63  VAL A C     1 
ATOM   466  O O     . VAL A 1 63  ? -16.482 72.728  -12.348 1.00 30.62 ? 63  VAL A O     1 
ATOM   467  C CB    . VAL A 1 63  ? -18.290 74.622  -10.867 1.00 30.72 ? 63  VAL A CB    1 
ATOM   468  C CG1   . VAL A 1 63  ? -19.270 73.516  -10.517 1.00 30.10 ? 63  VAL A CG1   1 
ATOM   469  C CG2   . VAL A 1 63  ? -18.604 75.955  -10.205 1.00 30.58 ? 63  VAL A CG2   1 
ATOM   470  N N     . THR A 1 64  ? -16.276 71.886  -10.283 1.00 30.67 ? 64  THR A N     1 
ATOM   471  C CA    . THR A 1 64  ? -15.821 70.573  -10.736 1.00 30.11 ? 64  THR A CA    1 
ATOM   472  C C     . THR A 1 64  ? -16.552 69.457  -10.015 1.00 29.68 ? 64  THR A C     1 
ATOM   473  O O     . THR A 1 64  ? -16.962 69.628  -8.867  1.00 29.35 ? 64  THR A O     1 
ATOM   474  C CB    . THR A 1 64  ? -14.313 70.528  -10.414 1.00 30.66 ? 64  THR A CB    1 
ATOM   475  O OG1   . THR A 1 64  ? -13.664 71.518  -11.231 1.00 31.05 ? 64  THR A OG1   1 
ATOM   476  C CG2   . THR A 1 64  ? -13.700 69.163  -10.619 1.00 29.82 ? 64  THR A CG2   1 
ATOM   477  N N     . GLY A 1 65  ? -16.820 68.368  -10.723 1.00 29.48 ? 65  GLY A N     1 
ATOM   478  C CA    . GLY A 1 65  ? -17.548 67.243  -10.134 1.00 29.65 ? 65  GLY A CA    1 
ATOM   479  C C     . GLY A 1 65  ? -18.086 66.326  -11.223 1.00 29.70 ? 65  GLY A C     1 
ATOM   480  O O     . GLY A 1 65  ? -17.699 66.496  -12.380 1.00 30.05 ? 65  GLY A O     1 
ATOM   481  N N     . PHE A 1 66  ? -19.013 65.430  -10.909 1.00 29.65 ? 66  PHE A N     1 
ATOM   482  C CA    . PHE A 1 66  ? -19.577 64.536  -11.906 1.00 29.45 ? 66  PHE A CA    1 
ATOM   483  C C     . PHE A 1 66  ? -21.053 64.242  -11.674 1.00 29.77 ? 66  PHE A C     1 
ATOM   484  O O     . PHE A 1 66  ? -21.629 64.421  -10.601 1.00 29.91 ? 66  PHE A O     1 
ATOM   485  C CB    . PHE A 1 66  ? -18.820 63.217  -12.014 1.00 27.81 ? 66  PHE A CB    1 
ATOM   486  C CG    . PHE A 1 66  ? -18.743 62.405  -10.760 1.00 27.93 ? 66  PHE A CG    1 
ATOM   487  C CD1   . PHE A 1 66  ? -19.798 61.620  -10.340 1.00 28.44 ? 66  PHE A CD1   1 
ATOM   488  C CD2   . PHE A 1 66  ? -17.589 62.400  -9.997  1.00 28.80 ? 66  PHE A CD2   1 
ATOM   489  C CE1   . PHE A 1 66  ? -19.720 60.871  -9.184  1.00 28.84 ? 66  PHE A CE1   1 
ATOM   490  C CE2   . PHE A 1 66  ? -17.493 61.656  -8.838  1.00 29.11 ? 66  PHE A CE2   1 
ATOM   491  C CZ    . PHE A 1 66  ? -18.565 60.890  -8.426  1.00 28.82 ? 66  PHE A CZ    1 
ATOM   492  N N     . LEU A 1 67  ? -21.679 63.761  -12.739 1.00 29.98 ? 67  LEU A N     1 
ATOM   493  C CA    . LEU A 1 67  ? -23.061 63.303  -12.682 1.00 30.41 ? 67  LEU A CA    1 
ATOM   494  C C     . LEU A 1 67  ? -23.065 61.811  -13.006 1.00 30.38 ? 67  LEU A C     1 
ATOM   495  O O     . LEU A 1 67  ? -22.655 61.445  -14.106 1.00 30.29 ? 67  LEU A O     1 
ATOM   496  C CB    . LEU A 1 67  ? -23.953 64.041  -13.675 1.00 31.20 ? 67  LEU A CB    1 
ATOM   497  C CG    . LEU A 1 67  ? -25.448 63.709  -13.574 1.00 32.16 ? 67  LEU A CG    1 
ATOM   498  C CD1   . LEU A 1 67  ? -26.029 64.124  -12.231 1.00 31.39 ? 67  LEU A CD1   1 
ATOM   499  C CD2   . LEU A 1 67  ? -26.200 64.386  -14.713 1.00 32.83 ? 67  LEU A CD2   1 
ATOM   500  N N     . ALA A 1 68  ? -23.335 60.974  -12.018 1.00 30.61 ? 68  ALA A N     1 
ATOM   501  C CA    . ALA A 1 68  ? -23.322 59.532  -12.242 1.00 30.73 ? 68  ALA A CA    1 
ATOM   502  C C     . ALA A 1 68  ? -24.710 58.907  -12.136 1.00 30.86 ? 68  ALA A C     1 
ATOM   503  O O     . ALA A 1 68  ? -25.578 59.335  -11.383 1.00 31.12 ? 68  ALA A O     1 
ATOM   504  C CB    . ALA A 1 68  ? -22.423 58.824  -11.237 1.00 30.34 ? 68  ALA A CB    1 
ATOM   505  N N     . LEU A 1 69  ? -24.851 57.810  -12.850 1.00 30.82 ? 69  LEU A N     1 
ATOM   506  C CA    . LEU A 1 69  ? -26.021 56.951  -12.857 1.00 30.89 ? 69  LEU A CA    1 
ATOM   507  C C     . LEU A 1 69  ? -25.650 55.669  -12.105 1.00 31.32 ? 69  LEU A C     1 
ATOM   508  O O     . LEU A 1 69  ? -24.726 54.977  -12.542 1.00 31.29 ? 69  LEU A O     1 
ATOM   509  C CB    . LEU A 1 69  ? -26.300 56.521  -14.285 1.00 31.31 ? 69  LEU A CB    1 
ATOM   510  C CG    . LEU A 1 69  ? -27.680 56.203  -14.829 1.00 31.94 ? 69  LEU A CG    1 
ATOM   511  C CD1   . LEU A 1 69  ? -27.659 54.868  -15.562 1.00 31.21 ? 69  LEU A CD1   1 
ATOM   512  C CD2   . LEU A 1 69  ? -28.785 56.236  -13.801 1.00 32.56 ? 69  LEU A CD2   1 
ATOM   513  N N     . ASP A 1 70  ? -26.252 55.419  -10.958 1.00 31.60 ? 70  ASP A N     1 
ATOM   514  C CA    . ASP A 1 70  ? -25.933 54.183  -10.226 1.00 31.65 ? 70  ASP A CA    1 
ATOM   515  C C     . ASP A 1 70  ? -27.059 53.186  -10.455 1.00 31.91 ? 70  ASP A C     1 
ATOM   516  O O     . ASP A 1 70  ? -28.148 53.278  -9.884  1.00 31.60 ? 70  ASP A O     1 
ATOM   517  C CB    . ASP A 1 70  ? -25.726 54.512  -8.755  1.00 31.18 ? 70  ASP A CB    1 
ATOM   518  C CG    . ASP A 1 70  ? -25.524 53.306  -7.872  1.00 31.36 ? 70  ASP A CG    1 
ATOM   519  O OD1   . ASP A 1 70  ? -25.711 52.169  -8.327  1.00 30.26 ? 70  ASP A OD1   1 
ATOM   520  O OD2   . ASP A 1 70  ? -25.157 53.463  -6.687  1.00 33.25 ? 70  ASP A OD2   1 
ATOM   521  N N     . ASN A 1 71  ? -26.797 52.143  -11.243 1.00 32.57 ? 71  ASN A N     1 
ATOM   522  C CA    . ASN A 1 71  ? -27.856 51.163  -11.525 1.00 32.85 ? 71  ASN A CA    1 
ATOM   523  C C     . ASN A 1 71  ? -28.090 50.218  -10.360 1.00 32.73 ? 71  ASN A C     1 
ATOM   524  O O     . ASN A 1 71  ? -29.151 49.619  -10.254 1.00 32.69 ? 71  ASN A O     1 
ATOM   525  C CB    . ASN A 1 71  ? -27.625 50.379  -12.814 1.00 33.33 ? 71  ASN A CB    1 
ATOM   526  C CG    . ASN A 1 71  ? -27.907 51.226  -14.031 1.00 34.16 ? 71  ASN A CG    1 
ATOM   527  O OD1   . ASN A 1 71  ? -27.240 51.151  -15.058 1.00 37.11 ? 71  ASN A OD1   1 
ATOM   528  N ND2   . ASN A 1 71  ? -28.914 52.073  -13.922 1.00 34.02 ? 71  ASN A ND2   1 
ATOM   529  N N     . THR A 1 72  ? -27.068 49.895  -9.590  1.00 32.86 ? 72  THR A N     1 
ATOM   530  C CA    . THR A 1 72  ? -27.177 49.089  -8.388  1.00 32.96 ? 72  THR A CA    1 
ATOM   531  C C     . THR A 1 72  ? -28.102 49.741  -7.369  1.00 33.17 ? 72  THR A C     1 
ATOM   532  O O     . THR A 1 72  ? -28.911 49.031  -6.770  1.00 33.67 ? 72  THR A O     1 
ATOM   533  C CB    . THR A 1 72  ? -25.806 48.908  -7.712  1.00 33.49 ? 72  THR A CB    1 
ATOM   534  O OG1   . THR A 1 72  ? -24.860 48.334  -8.625  1.00 35.41 ? 72  THR A OG1   1 
ATOM   535  C CG2   . THR A 1 72  ? -25.857 48.017  -6.494  1.00 32.71 ? 72  THR A CG2   1 
ATOM   536  N N     . ASN A 1 73  ? -27.915 51.013  -7.024  1.00 33.13 ? 73  ASN A N     1 
ATOM   537  C CA    . ASN A 1 73  ? -28.798 51.631  -6.041  1.00 33.00 ? 73  ASN A CA    1 
ATOM   538  C C     . ASN A 1 73  ? -29.944 52.420  -6.646  1.00 33.18 ? 73  ASN A C     1 
ATOM   539  O O     . ASN A 1 73  ? -30.693 53.014  -5.865  1.00 33.36 ? 73  ASN A O     1 
ATOM   540  C CB    . ASN A 1 73  ? -28.023 52.525  -5.072  1.00 31.07 ? 73  ASN A CB    1 
ATOM   541  C CG    . ASN A 1 73  ? -26.886 51.771  -4.415  1.00 29.15 ? 73  ASN A CG    1 
ATOM   542  O OD1   . ASN A 1 73  ? -25.775 51.715  -4.924  1.00 28.63 ? 73  ASN A OD1   1 
ATOM   543  N ND2   . ASN A 1 73  ? -27.161 51.169  -3.271  1.00 28.06 ? 73  ASN A ND2   1 
ATOM   544  N N     . LYS A 1 74  ? -30.092 52.402  -7.968  1.00 33.29 ? 74  LYS A N     1 
ATOM   545  C CA    . LYS A 1 74  ? -31.179 53.152  -8.595  1.00 33.06 ? 74  LYS A CA    1 
ATOM   546  C C     . LYS A 1 74  ? -31.053 54.610  -8.148  1.00 32.30 ? 74  LYS A C     1 
ATOM   547  O O     . LYS A 1 74  ? -31.989 55.141  -7.567  1.00 32.57 ? 74  LYS A O     1 
ATOM   548  C CB    . LYS A 1 74  ? -32.536 52.611  -8.161  1.00 35.34 ? 74  LYS A CB    1 
ATOM   549  C CG    . LYS A 1 74  ? -32.843 51.150  -8.383  1.00 36.65 ? 74  LYS A CG    1 
ATOM   550  C CD    . LYS A 1 74  ? -32.526 50.683  -9.787  1.00 38.90 ? 74  LYS A CD    1 
ATOM   551  C CE    . LYS A 1 74  ? -32.239 49.192  -9.828  1.00 42.34 ? 74  LYS A CE    1 
ATOM   552  N NZ    . LYS A 1 74  ? -31.410 48.817  -11.018 1.00 43.05 ? 74  LYS A NZ    1 
ATOM   553  N N     . LEU A 1 75  ? -29.994 55.250  -8.605  1.00 31.49 ? 75  LEU A N     1 
ATOM   554  C CA    . LEU A 1 75  ? -29.632 56.599  -8.204  1.00 30.30 ? 75  LEU A CA    1 
ATOM   555  C C     . LEU A 1 75  ? -29.061 57.430  -9.351  1.00 30.19 ? 75  LEU A C     1 
ATOM   556  O O     . LEU A 1 75  ? -28.370 56.988  -10.260 1.00 29.43 ? 75  LEU A O     1 
ATOM   557  C CB    . LEU A 1 75  ? -28.538 56.410  -7.158  1.00 28.28 ? 75  LEU A CB    1 
ATOM   558  C CG    . LEU A 1 75  ? -28.690 56.679  -5.680  1.00 27.12 ? 75  LEU A CG    1 
ATOM   559  C CD1   . LEU A 1 75  ? -30.079 56.451  -5.132  1.00 25.39 ? 75  LEU A CD1   1 
ATOM   560  C CD2   . LEU A 1 75  ? -27.664 55.862  -4.903  1.00 25.07 ? 75  LEU A CD2   1 
ATOM   561  N N     . ILE A 1 76  ? -29.430 58.701  -9.351  1.00 30.63 ? 76  ILE A N     1 
ATOM   562  C CA    . ILE A 1 76  ? -28.836 59.751  -10.175 1.00 30.84 ? 76  ILE A CA    1 
ATOM   563  C C     . ILE A 1 76  ? -28.107 60.711  -9.218  1.00 30.79 ? 76  ILE A C     1 
ATOM   564  O O     . ILE A 1 76  ? -28.773 61.383  -8.423  1.00 30.49 ? 76  ILE A O     1 
ATOM   565  C CB    . ILE A 1 76  ? -29.917 60.515  -10.938 1.00 31.20 ? 76  ILE A CB    1 
ATOM   566  C CG1   . ILE A 1 76  ? -30.524 59.601  -12.007 1.00 30.67 ? 76  ILE A CG1   1 
ATOM   567  C CG2   . ILE A 1 76  ? -29.355 61.796  -11.535 1.00 31.37 ? 76  ILE A CG2   1 
ATOM   568  C CD1   . ILE A 1 76  ? -31.857 60.097  -12.533 1.00 29.36 ? 76  ILE A CD1   1 
ATOM   569  N N     . VAL A 1 77  ? -26.782 60.570  -9.164  1.00 30.59 ? 77  VAL A N     1 
ATOM   570  C CA    . VAL A 1 77  ? -25.987 61.335  -8.209  1.00 30.33 ? 77  VAL A CA    1 
ATOM   571  C C     . VAL A 1 77  ? -25.226 62.474  -8.870  1.00 29.72 ? 77  VAL A C     1 
ATOM   572  O O     . VAL A 1 77  ? -24.807 62.301  -10.019 1.00 30.15 ? 77  VAL A O     1 
ATOM   573  C CB    . VAL A 1 77  ? -24.975 60.420  -7.485  1.00 30.75 ? 77  VAL A CB    1 
ATOM   574  C CG1   . VAL A 1 77  ? -24.326 61.148  -6.317  1.00 30.79 ? 77  VAL A CG1   1 
ATOM   575  C CG2   . VAL A 1 77  ? -25.681 59.163  -6.992  1.00 29.89 ? 77  VAL A CG2   1 
ATOM   576  N N     . LEU A 1 78  ? -25.332 63.668  -8.307  1.00 28.88 ? 78  LEU A N     1 
ATOM   577  C CA    . LEU A 1 78  ? -24.526 64.805  -8.755  1.00 28.00 ? 78  LEU A CA    1 
ATOM   578  C C     . LEU A 1 78  ? -23.593 65.168  -7.599  1.00 27.54 ? 78  LEU A C     1 
ATOM   579  O O     . LEU A 1 78  ? -24.066 65.578  -6.542  1.00 27.00 ? 78  LEU A O     1 
ATOM   580  C CB    . LEU A 1 78  ? -25.380 65.988  -9.162  1.00 27.45 ? 78  LEU A CB    1 
ATOM   581  C CG    . LEU A 1 78  ? -24.720 67.328  -9.479  1.00 27.35 ? 78  LEU A CG    1 
ATOM   582  C CD1   . LEU A 1 78  ? -23.768 67.231  -10.662 1.00 27.13 ? 78  LEU A CD1   1 
ATOM   583  C CD2   . LEU A 1 78  ? -25.763 68.409  -9.751  1.00 26.25 ? 78  LEU A CD2   1 
ATOM   584  N N     . SER A 1 79  ? -22.318 64.861  -7.775  1.00 27.37 ? 79  SER A N     1 
ATOM   585  C CA    . SER A 1 79  ? -21.307 65.078  -6.744  1.00 27.06 ? 79  SER A CA    1 
ATOM   586  C C     . SER A 1 79  ? -20.457 66.281  -7.123  1.00 27.12 ? 79  SER A C     1 
ATOM   587  O O     . SER A 1 79  ? -19.930 66.281  -8.234  1.00 27.04 ? 79  SER A O     1 
ATOM   588  C CB    . SER A 1 79  ? -20.335 63.888  -6.704  1.00 26.30 ? 79  SER A CB    1 
ATOM   589  O OG    . SER A 1 79  ? -19.462 63.928  -5.607  1.00 23.98 ? 79  SER A OG    1 
ATOM   590  N N     . PHE A 1 80  ? -20.244 67.187  -6.184  1.00 27.52 ? 80  PHE A N     1 
ATOM   591  C CA    . PHE A 1 80  ? -19.382 68.346  -6.437  1.00 27.32 ? 80  PHE A CA    1 
ATOM   592  C C     . PHE A 1 80  ? -18.049 68.181  -5.714  1.00 27.35 ? 80  PHE A C     1 
ATOM   593  O O     . PHE A 1 80  ? -18.057 67.842  -4.534  1.00 27.17 ? 80  PHE A O     1 
ATOM   594  C CB    . PHE A 1 80  ? -20.075 69.608  -5.938  1.00 26.41 ? 80  PHE A CB    1 
ATOM   595  C CG    . PHE A 1 80  ? -21.213 70.118  -6.759  1.00 27.58 ? 80  PHE A CG    1 
ATOM   596  C CD1   . PHE A 1 80  ? -22.521 70.047  -6.294  1.00 29.17 ? 80  PHE A CD1   1 
ATOM   597  C CD2   . PHE A 1 80  ? -20.994 70.686  -8.000  1.00 27.45 ? 80  PHE A CD2   1 
ATOM   598  C CE1   . PHE A 1 80  ? -23.577 70.532  -7.048  1.00 29.02 ? 80  PHE A CE1   1 
ATOM   599  C CE2   . PHE A 1 80  ? -22.048 71.173  -8.758  1.00 28.53 ? 80  PHE A CE2   1 
ATOM   600  C CZ    . PHE A 1 80  ? -23.345 71.099  -8.288  1.00 27.97 ? 80  PHE A CZ    1 
ATOM   601  N N     . ARG A 1 81  ? -16.934 68.351  -6.401  1.00 27.47 ? 81  ARG A N     1 
ATOM   602  C CA    . ARG A 1 81  ? -15.616 68.312  -5.763  1.00 27.81 ? 81  ARG A CA    1 
ATOM   603  C C     . ARG A 1 81  ? -15.502 69.488  -4.797  1.00 28.11 ? 81  ARG A C     1 
ATOM   604  O O     . ARG A 1 81  ? -15.926 70.577  -5.171  1.00 28.26 ? 81  ARG A O     1 
ATOM   605  C CB    . ARG A 1 81  ? -14.556 68.415  -6.845  1.00 28.82 ? 81  ARG A CB    1 
ATOM   606  C CG    . ARG A 1 81  ? -13.095 68.173  -6.646  1.00 29.16 ? 81  ARG A CG    1 
ATOM   607  C CD    . ARG A 1 81  ? -12.181 69.325  -6.534  1.00 31.24 ? 81  ARG A CD    1 
ATOM   608  N NE    . ARG A 1 81  ? -11.767 70.280  -7.510  1.00 32.49 ? 81  ARG A NE    1 
ATOM   609  C CZ    . ARG A 1 81  ? -10.851 70.198  -8.457  1.00 33.98 ? 81  ARG A CZ    1 
ATOM   610  N NH1   . ARG A 1 81  ? -10.186 69.061  -8.632  1.00 35.30 ? 81  ARG A NH1   1 
ATOM   611  N NH2   . ARG A 1 81  ? -10.623 71.271  -9.207  1.00 35.63 ? 81  ARG A NH2   1 
ATOM   612  N N     . GLY A 1 82  ? -14.945 69.303  -3.614  1.00 28.50 ? 82  GLY A N     1 
ATOM   613  C CA    . GLY A 1 82  ? -14.652 70.360  -2.660  1.00 28.99 ? 82  GLY A CA    1 
ATOM   614  C C     . GLY A 1 82  ? -13.493 71.230  -3.130  1.00 29.58 ? 82  GLY A C     1 
ATOM   615  O O     . GLY A 1 82  ? -13.080 71.130  -4.290  1.00 29.41 ? 82  GLY A O     1 
ATOM   616  N N     . SER A 1 83  ? -12.778 71.900  -2.235  1.00 30.54 ? 83  SER A N     1 
ATOM   617  C CA    . SER A 1 83  ? -11.735 72.844  -2.648  1.00 31.29 ? 83  SER A CA    1 
ATOM   618  C C     . SER A 1 83  ? -10.396 72.153  -2.903  1.00 31.62 ? 83  SER A C     1 
ATOM   619  O O     . SER A 1 83  ? -9.940  71.359  -2.081  1.00 32.20 ? 83  SER A O     1 
ATOM   620  C CB    . SER A 1 83  ? -11.550 73.995  -1.668  1.00 30.73 ? 83  SER A CB    1 
ATOM   621  O OG    . SER A 1 83  ? -12.454 73.898  -0.557  1.00 33.63 ? 83  SER A OG    1 
ATOM   622  N N     . ARG A 1 84  ? -9.828  72.528  -4.045  1.00 31.14 ? 84  ARG A N     1 
ATOM   623  C CA    . ARG A 1 84  ? -8.571  71.950  -4.481  1.00 30.80 ? 84  ARG A CA    1 
ATOM   624  C C     . ARG A 1 84  ? -7.697  72.985  -5.177  1.00 30.97 ? 84  ARG A C     1 
ATOM   625  O O     . ARG A 1 84  ? -6.536  73.116  -4.801  1.00 31.29 ? 84  ARG A O     1 
ATOM   626  C CB    . ARG A 1 84  ? -8.921  70.837  -5.471  1.00 29.92 ? 84  ARG A CB    1 
ATOM   627  C CG    . ARG A 1 84  ? -7.686  70.141  -6.012  1.00 29.74 ? 84  ARG A CG    1 
ATOM   628  C CD    . ARG A 1 84  ? -7.254  69.175  -4.906  1.00 29.92 ? 84  ARG A CD    1 
ATOM   629  N NE    . ARG A 1 84  ? -7.136  67.881  -5.531  1.00 30.32 ? 84  ARG A NE    1 
ATOM   630  C CZ    . ARG A 1 84  ? -7.286  66.699  -4.973  1.00 30.92 ? 84  ARG A CZ    1 
ATOM   631  N NH1   . ARG A 1 84  ? -7.581  66.569  -3.692  1.00 30.48 ? 84  ARG A NH1   1 
ATOM   632  N NH2   . ARG A 1 84  ? -7.113  65.637  -5.754  1.00 31.15 ? 84  ARG A NH2   1 
ATOM   633  N N     . SER A 1 85  ? -8.194  73.626  -6.218  1.00 30.58 ? 85  SER A N     1 
ATOM   634  C CA    . SER A 1 85  ? -7.440  74.645  -6.920  1.00 30.31 ? 85  SER A CA    1 
ATOM   635  C C     . SER A 1 85  ? -7.446  75.968  -6.168  1.00 30.88 ? 85  SER A C     1 
ATOM   636  O O     . SER A 1 85  ? -8.175  76.166  -5.205  1.00 31.06 ? 85  SER A O     1 
ATOM   637  C CB    . SER A 1 85  ? -8.145  74.857  -8.263  1.00 29.25 ? 85  SER A CB    1 
ATOM   638  O OG    . SER A 1 85  ? -9.492  75.154  -7.961  1.00 27.47 ? 85  SER A OG    1 
ATOM   639  N N     . ILE A 1 86  ? -6.711  76.939  -6.694  1.00 31.42 ? 86  ILE A N     1 
ATOM   640  C CA    . ILE A 1 86  ? -6.636  78.285  -6.137  1.00 31.40 ? 86  ILE A CA    1 
ATOM   641  C C     . ILE A 1 86  ? -7.906  79.052  -6.447  1.00 31.48 ? 86  ILE A C     1 
ATOM   642  O O     . ILE A 1 86  ? -8.316  79.824  -5.576  1.00 31.66 ? 86  ILE A O     1 
ATOM   643  C CB    . ILE A 1 86  ? -5.372  79.019  -6.627  1.00 31.57 ? 86  ILE A CB    1 
ATOM   644  C CG1   . ILE A 1 86  ? -4.164  78.446  -5.878  1.00 31.44 ? 86  ILE A CG1   1 
ATOM   645  C CG2   . ILE A 1 86  ? -5.403  80.524  -6.461  1.00 31.33 ? 86  ILE A CG2   1 
ATOM   646  C CD1   . ILE A 1 86  ? -2.833  78.867  -6.447  1.00 31.41 ? 86  ILE A CD1   1 
ATOM   647  N N     . GLU A 1 87  ? -8.564  78.829  -7.579  1.00 31.68 ? 87  GLU A N     1 
ATOM   648  C CA    . GLU A 1 87  ? -9.800  79.546  -7.874  1.00 32.96 ? 87  GLU A CA    1 
ATOM   649  C C     . GLU A 1 87  ? -10.905 79.115  -6.912  1.00 32.76 ? 87  GLU A C     1 
ATOM   650  O O     . GLU A 1 87  ? -11.640 79.916  -6.323  1.00 33.05 ? 87  GLU A O     1 
ATOM   651  C CB    . GLU A 1 87  ? -10.301 79.385  -9.304  1.00 37.95 ? 87  GLU A CB    1 
ATOM   652  C CG    . GLU A 1 87  ? -9.351  79.922  -10.349 1.00 46.20 ? 87  GLU A CG    1 
ATOM   653  C CD    . GLU A 1 87  ? -8.290  78.895  -10.729 1.00 51.67 ? 87  GLU A CD    1 
ATOM   654  O OE1   . GLU A 1 87  ? -7.375  78.530  -9.951  1.00 51.27 ? 87  GLU A OE1   1 
ATOM   655  O OE2   . GLU A 1 87  ? -8.408  78.440  -11.902 1.00 56.06 ? 87  GLU A OE2   1 
ATOM   656  N N     . ASN A 1 88  ? -10.900 77.820  -6.578  1.00 32.27 ? 88  ASN A N     1 
ATOM   657  C CA    . ASN A 1 88  ? -11.826 77.264  -5.600  1.00 31.83 ? 88  ASN A CA    1 
ATOM   658  C C     . ASN A 1 88  ? -11.692 78.065  -4.304  1.00 31.97 ? 88  ASN A C     1 
ATOM   659  O O     . ASN A 1 88  ? -12.619 78.486  -3.630  1.00 31.76 ? 88  ASN A O     1 
ATOM   660  C CB    . ASN A 1 88  ? -11.474 75.823  -5.263  1.00 30.50 ? 88  ASN A CB    1 
ATOM   661  C CG    . ASN A 1 88  ? -11.929 74.807  -6.279  1.00 31.48 ? 88  ASN A CG    1 
ATOM   662  O OD1   . ASN A 1 88  ? -11.338 73.720  -6.384  1.00 32.33 ? 88  ASN A OD1   1 
ATOM   663  N ND2   . ASN A 1 88  ? -12.965 75.116  -7.046  1.00 30.61 ? 88  ASN A ND2   1 
ATOM   664  N N     . TRP A 1 89  ? -10.423 78.208  -3.937  1.00 32.47 ? 89  TRP A N     1 
ATOM   665  C CA    . TRP A 1 89  ? -10.014 78.963  -2.782  1.00 32.96 ? 89  TRP A CA    1 
ATOM   666  C C     . TRP A 1 89  ? -10.314 80.448  -2.774  1.00 32.29 ? 89  TRP A C     1 
ATOM   667  O O     . TRP A 1 89  ? -10.846 81.027  -1.810  1.00 31.78 ? 89  TRP A O     1 
ATOM   668  C CB    . TRP A 1 89  ? -8.520  78.650  -2.559  1.00 39.18 ? 89  TRP A CB    1 
ATOM   669  C CG    . TRP A 1 89  ? -8.480  78.564  -1.058  1.00 47.57 ? 89  TRP A CG    1 
ATOM   670  C CD1   . TRP A 1 89  ? -9.076  77.600  -0.283  1.00 50.36 ? 89  TRP A CD1   1 
ATOM   671  C CD2   . TRP A 1 89  ? -8.043  79.600  -0.174  1.00 50.24 ? 89  TRP A CD2   1 
ATOM   672  N NE1   . TRP A 1 89  ? -8.953  77.927  1.056   1.00 52.46 ? 89  TRP A NE1   1 
ATOM   673  C CE2   . TRP A 1 89  ? -8.340  79.166  1.146   1.00 51.96 ? 89  TRP A CE2   1 
ATOM   674  C CE3   . TRP A 1 89  ? -7.302  80.769  -0.375  1.00 50.57 ? 89  TRP A CE3   1 
ATOM   675  C CZ2   . TRP A 1 89  ? -7.925  79.872  2.277   1.00 51.75 ? 89  TRP A CZ2   1 
ATOM   676  C CZ3   . TRP A 1 89  ? -6.923  81.488  0.747   1.00 53.16 ? 89  TRP A CZ3   1 
ATOM   677  C CH2   . TRP A 1 89  ? -7.214  81.016  2.051   1.00 53.14 ? 89  TRP A CH2   1 
ATOM   678  N N     . ILE A 1 90  ? -10.123 81.110  -3.914  1.00 31.36 ? 90  ILE A N     1 
ATOM   679  C CA    . ILE A 1 90  ? -10.461 82.530  -3.991  1.00 30.94 ? 90  ILE A CA    1 
ATOM   680  C C     . ILE A 1 90  ? -11.965 82.664  -3.826  1.00 30.75 ? 90  ILE A C     1 
ATOM   681  O O     . ILE A 1 90  ? -12.472 83.327  -2.925  1.00 30.74 ? 90  ILE A O     1 
ATOM   682  C CB    . ILE A 1 90  ? -9.954  83.148  -5.298  1.00 31.19 ? 90  ILE A CB    1 
ATOM   683  C CG1   . ILE A 1 90  ? -8.433  82.966  -5.408  1.00 30.35 ? 90  ILE A CG1   1 
ATOM   684  C CG2   . ILE A 1 90  ? -10.338 84.617  -5.404  1.00 29.70 ? 90  ILE A CG2   1 
ATOM   685  C CD1   . ILE A 1 90  ? -7.644  83.458  -4.220  1.00 27.29 ? 90  ILE A CD1   1 
ATOM   686  N N     . GLY A 1 91  ? -12.716 81.850  -4.558  1.00 30.58 ? 91  GLY A N     1 
ATOM   687  C CA    . GLY A 1 91  ? -14.163 81.813  -4.503  1.00 30.07 ? 91  GLY A CA    1 
ATOM   688  C C     . GLY A 1 91  ? -14.705 81.622  -3.102  1.00 29.86 ? 91  GLY A C     1 
ATOM   689  O O     . GLY A 1 91  ? -15.692 82.252  -2.710  1.00 30.18 ? 91  GLY A O     1 
ATOM   690  N N     . ASN A 1 92  ? -14.089 80.805  -2.251  1.00 29.48 ? 92  ASN A N     1 
ATOM   691  C CA    . ASN A 1 92  ? -14.549 80.651  -0.883  1.00 29.02 ? 92  ASN A CA    1 
ATOM   692  C C     . ASN A 1 92  ? -14.443 81.936  -0.075  1.00 28.73 ? 92  ASN A C     1 
ATOM   693  O O     . ASN A 1 92  ? -14.890 81.933  1.058   1.00 28.15 ? 92  ASN A O     1 
ATOM   694  C CB    . ASN A 1 92  ? -13.724 79.596  -0.141  1.00 30.61 ? 92  ASN A CB    1 
ATOM   695  C CG    . ASN A 1 92  ? -13.985 78.184  -0.567  1.00 32.11 ? 92  ASN A CG    1 
ATOM   696  O OD1   . ASN A 1 92  ? -13.173 77.315  -0.282  1.00 34.31 ? 92  ASN A OD1   1 
ATOM   697  N ND2   . ASN A 1 92  ? -15.060 77.860  -1.269  1.00 34.02 ? 92  ASN A ND2   1 
ATOM   698  N N     . LEU A 1 93  ? -13.501 82.804  -0.406  1.00 29.02 ? 93  LEU A N     1 
ATOM   699  C CA    . LEU A 1 93  ? -13.214 84.071  0.207   1.00 28.82 ? 93  LEU A CA    1 
ATOM   700  C C     . LEU A 1 93  ? -14.133 85.196  -0.224  1.00 29.03 ? 93  LEU A C     1 
ATOM   701  O O     . LEU A 1 93  ? -14.121 86.247  0.435   1.00 29.23 ? 93  LEU A O     1 
ATOM   702  C CB    . LEU A 1 93  ? -11.752 84.402  -0.092  1.00 29.01 ? 93  LEU A CB    1 
ATOM   703  C CG    . LEU A 1 93  ? -10.737 83.357  0.395   1.00 28.44 ? 93  LEU A CG    1 
ATOM   704  C CD1   . LEU A 1 93  ? -9.340  83.845  0.051   1.00 27.55 ? 93  LEU A CD1   1 
ATOM   705  C CD2   . LEU A 1 93  ? -10.864 83.209  1.905   1.00 29.34 ? 93  LEU A CD2   1 
ATOM   706  N N     . ASN A 1 94  ? -15.020 84.998  -1.204  1.00 28.99 ? 94  ASN A N     1 
ATOM   707  C CA    . ASN A 1 94  ? -16.082 85.988  -1.417  1.00 29.54 ? 94  ASN A CA    1 
ATOM   708  C C     . ASN A 1 94  ? -17.162 85.702  -0.368  1.00 29.51 ? 94  ASN A C     1 
ATOM   709  O O     . ASN A 1 94  ? -18.182 85.109  -0.705  1.00 29.36 ? 94  ASN A O     1 
ATOM   710  C CB    . ASN A 1 94  ? -16.674 85.991  -2.813  1.00 31.31 ? 94  ASN A CB    1 
ATOM   711  C CG    . ASN A 1 94  ? -15.702 86.462  -3.871  1.00 34.49 ? 94  ASN A CG    1 
ATOM   712  O OD1   . ASN A 1 94  ? -15.724 87.597  -4.353  1.00 37.09 ? 94  ASN A OD1   1 
ATOM   713  N ND2   . ASN A 1 94  ? -14.777 85.587  -4.263  1.00 36.09 ? 94  ASN A ND2   1 
ATOM   714  N N     . PHE A 1 95  ? -17.014 86.170  0.871   1.00 29.76 ? 95  PHE A N     1 
ATOM   715  C CA    . PHE A 1 95  ? -17.917 85.770  1.938   1.00 30.19 ? 95  PHE A CA    1 
ATOM   716  C C     . PHE A 1 95  ? -19.001 86.783  2.235   1.00 30.28 ? 95  PHE A C     1 
ATOM   717  O O     . PHE A 1 95  ? -19.833 86.559  3.111   1.00 29.75 ? 95  PHE A O     1 
ATOM   718  C CB    . PHE A 1 95  ? -17.161 85.347  3.202   1.00 31.38 ? 95  PHE A CB    1 
ATOM   719  C CG    . PHE A 1 95  ? -16.187 86.348  3.740   1.00 31.67 ? 95  PHE A CG    1 
ATOM   720  C CD1   . PHE A 1 95  ? -14.862 86.284  3.369   1.00 32.64 ? 95  PHE A CD1   1 
ATOM   721  C CD2   . PHE A 1 95  ? -16.595 87.352  4.602   1.00 31.91 ? 95  PHE A CD2   1 
ATOM   722  C CE1   . PHE A 1 95  ? -13.955 87.216  3.851   1.00 34.50 ? 95  PHE A CE1   1 
ATOM   723  C CE2   . PHE A 1 95  ? -15.692 88.279  5.077   1.00 33.07 ? 95  PHE A CE2   1 
ATOM   724  C CZ    . PHE A 1 95  ? -14.367 88.209  4.711   1.00 33.62 ? 95  PHE A CZ    1 
ATOM   725  N N     . ASP A 1 96  ? -19.020 87.894  1.515   1.00 31.01 ? 96  ASP A N     1 
ATOM   726  C CA    . ASP A 1 96  ? -20.089 88.896  1.623   1.00 31.95 ? 96  ASP A CA    1 
ATOM   727  C C     . ASP A 1 96  ? -21.420 88.268  1.205   1.00 32.26 ? 96  ASP A C     1 
ATOM   728  O O     . ASP A 1 96  ? -21.429 87.463  0.273   1.00 32.02 ? 96  ASP A O     1 
ATOM   729  C CB    . ASP A 1 96  ? -19.687 90.058  0.717   1.00 33.19 ? 96  ASP A CB    1 
ATOM   730  C CG    . ASP A 1 96  ? -19.840 89.655  -0.738  1.00 36.28 ? 96  ASP A CG    1 
ATOM   731  O OD1   . ASP A 1 96  ? -19.047 88.862  -1.292  1.00 39.27 ? 96  ASP A OD1   1 
ATOM   732  O OD2   . ASP A 1 96  ? -20.815 90.147  -1.338  1.00 37.80 ? 96  ASP A OD2   1 
ATOM   733  N N     . LEU A 1 97  ? -22.495 88.485  1.967   1.00 32.80 ? 97  LEU A N     1 
ATOM   734  C CA    . LEU A 1 97  ? -23.791 87.883  1.672   1.00 33.49 ? 97  LEU A CA    1 
ATOM   735  C C     . LEU A 1 97  ? -24.528 88.500  0.493   1.00 34.40 ? 97  LEU A C     1 
ATOM   736  O O     . LEU A 1 97  ? -24.907 89.662  0.508   1.00 34.56 ? 97  LEU A O     1 
ATOM   737  C CB    . LEU A 1 97  ? -24.708 87.967  2.901   1.00 31.05 ? 97  LEU A CB    1 
ATOM   738  C CG    . LEU A 1 97  ? -24.274 87.025  4.030   1.00 30.90 ? 97  LEU A CG    1 
ATOM   739  C CD1   . LEU A 1 97  ? -24.838 87.440  5.379   1.00 30.40 ? 97  LEU A CD1   1 
ATOM   740  C CD2   . LEU A 1 97  ? -24.663 85.593  3.726   1.00 29.00 ? 97  LEU A CD2   1 
ATOM   741  N N     . LYS A 1 98  ? -24.677 87.764  -0.594  1.00 35.48 ? 98  LYS A N     1 
ATOM   742  C CA    . LYS A 1 98  ? -25.397 88.216  -1.771  1.00 37.23 ? 98  LYS A CA    1 
ATOM   743  C C     . LYS A 1 98  ? -26.867 87.868  -1.581  1.00 38.63 ? 98  LYS A C     1 
ATOM   744  O O     . LYS A 1 98  ? -27.247 86.902  -0.903  1.00 39.26 ? 98  LYS A O     1 
ATOM   745  C CB    . LYS A 1 98  ? -24.826 87.537  -3.008  1.00 38.62 ? 98  LYS A CB    1 
ATOM   746  C CG    . LYS A 1 98  ? -25.012 88.316  -4.293  1.00 42.25 ? 98  LYS A CG    1 
ATOM   747  C CD    . LYS A 1 98  ? -24.343 87.602  -5.459  1.00 45.39 ? 98  LYS A CD    1 
ATOM   748  C CE    . LYS A 1 98  ? -25.166 86.396  -5.915  1.00 47.64 ? 98  LYS A CE    1 
ATOM   749  N NZ    . LYS A 1 98  ? -26.526 86.803  -6.393  1.00 47.93 ? 98  LYS A NZ    1 
ATOM   750  N N     . GLU A 1 99  ? -27.745 88.523  -2.304  1.00 39.55 ? 99  GLU A N     1 
ATOM   751  C CA    . GLU A 1 99  ? -29.191 88.394  -2.158  1.00 40.47 ? 99  GLU A CA    1 
ATOM   752  C C     . GLU A 1 99  ? -29.752 87.373  -3.132  1.00 40.54 ? 99  GLU A C     1 
ATOM   753  O O     . GLU A 1 99  ? -29.316 87.328  -4.284  1.00 40.88 ? 99  GLU A O     1 
ATOM   754  C CB    . GLU A 1 99  ? -29.773 89.791  -2.407  1.00 44.99 ? 99  GLU A CB    1 
ATOM   755  C CG    . GLU A 1 99  ? -28.943 90.927  -1.821  1.00 50.94 ? 99  GLU A CG    1 
ATOM   756  C CD    . GLU A 1 99  ? -27.691 91.381  -2.557  1.00 53.20 ? 99  GLU A CD    1 
ATOM   757  O OE1   . GLU A 1 99  ? -26.792 91.988  -1.912  1.00 53.56 ? 99  GLU A OE1   1 
ATOM   758  O OE2   . GLU A 1 99  ? -27.505 91.137  -3.780  1.00 53.04 ? 99  GLU A OE2   1 
ATOM   759  N N     . ILE A 1 100 ? -30.420 86.348  -2.615  1.00 40.50 ? 100 ILE A N     1 
ATOM   760  C CA    . ILE A 1 100 ? -30.934 85.264  -3.444  1.00 40.48 ? 100 ILE A CA    1 
ATOM   761  C C     . ILE A 1 100 ? -32.437 85.118  -3.243  1.00 40.74 ? 100 ILE A C     1 
ATOM   762  O O     . ILE A 1 100 ? -33.013 84.068  -2.957  1.00 40.66 ? 100 ILE A O     1 
ATOM   763  C CB    . ILE A 1 100 ? -30.204 83.935  -3.174  1.00 39.89 ? 100 ILE A CB    1 
ATOM   764  C CG1   . ILE A 1 100 ? -30.145 83.643  -1.671  1.00 38.26 ? 100 ILE A CG1   1 
ATOM   765  C CG2   . ILE A 1 100 ? -28.815 83.962  -3.787  1.00 38.72 ? 100 ILE A CG2   1 
ATOM   766  C CD1   . ILE A 1 100 ? -29.852 82.200  -1.346  1.00 37.37 ? 100 ILE A CD1   1 
ATOM   767  N N     . ASN A 1 101 ? -33.142 86.201  -3.569  1.00 41.04 ? 101 ASN A N     1 
ATOM   768  C CA    . ASN A 1 101 ? -34.597 86.233  -3.509  1.00 41.07 ? 101 ASN A CA    1 
ATOM   769  C C     . ASN A 1 101 ? -35.253 85.237  -4.445  1.00 40.66 ? 101 ASN A C     1 
ATOM   770  O O     . ASN A 1 101 ? -36.314 84.729  -4.091  1.00 41.11 ? 101 ASN A O     1 
ATOM   771  C CB    . ASN A 1 101 ? -35.129 87.638  -3.837  1.00 43.10 ? 101 ASN A CB    1 
ATOM   772  C CG    . ASN A 1 101 ? -34.887 88.503  -2.614  1.00 44.99 ? 101 ASN A CG    1 
ATOM   773  O OD1   . ASN A 1 101 ? -35.113 88.052  -1.488  1.00 46.46 ? 101 ASN A OD1   1 
ATOM   774  N ND2   . ASN A 1 101 ? -34.359 89.698  -2.805  1.00 47.25 ? 101 ASN A ND2   1 
ATOM   775  N N     . ASP A 1 102 ? -34.726 85.056  -5.645  1.00 40.13 ? 102 ASP A N     1 
ATOM   776  C CA    . ASP A 1 102 ? -35.215 84.057  -6.576  1.00 39.84 ? 102 ASP A CA    1 
ATOM   777  C C     . ASP A 1 102 ? -35.404 82.740  -5.836  1.00 39.25 ? 102 ASP A C     1 
ATOM   778  O O     . ASP A 1 102 ? -36.534 82.242  -5.791  1.00 39.54 ? 102 ASP A O     1 
ATOM   779  C CB    . ASP A 1 102 ? -34.293 83.902  -7.772  1.00 45.21 ? 102 ASP A CB    1 
ATOM   780  C CG    . ASP A 1 102 ? -32.819 83.815  -7.445  1.00 50.40 ? 102 ASP A CG    1 
ATOM   781  O OD1   . ASP A 1 102 ? -31.994 83.580  -8.371  1.00 51.46 ? 102 ASP A OD1   1 
ATOM   782  O OD2   . ASP A 1 102 ? -32.417 83.971  -6.264  1.00 52.92 ? 102 ASP A OD2   1 
ATOM   783  N N     . ILE A 1 103 ? -34.370 82.241  -5.169  1.00 38.44 ? 103 ILE A N     1 
ATOM   784  C CA    . ILE A 1 103 ? -34.494 81.088  -4.288  1.00 37.36 ? 103 ILE A CA    1 
ATOM   785  C C     . ILE A 1 103 ? -35.528 81.351  -3.195  1.00 37.10 ? 103 ILE A C     1 
ATOM   786  O O     . ILE A 1 103 ? -36.351 80.469  -2.942  1.00 37.34 ? 103 ILE A O     1 
ATOM   787  C CB    . ILE A 1 103 ? -33.163 80.706  -3.617  1.00 36.94 ? 103 ILE A CB    1 
ATOM   788  C CG1   . ILE A 1 103 ? -31.987 80.688  -4.583  1.00 36.81 ? 103 ILE A CG1   1 
ATOM   789  C CG2   . ILE A 1 103 ? -33.282 79.396  -2.849  1.00 35.92 ? 103 ILE A CG2   1 
ATOM   790  C CD1   . ILE A 1 103 ? -31.778 79.469  -5.428  1.00 35.36 ? 103 ILE A CD1   1 
ATOM   791  N N     . CYS A 1 104 ? -35.400 82.344  -2.327  1.00 37.06 ? 104 CYS A N     1 
ATOM   792  C CA    . CYS A 1 104 ? -36.386 82.601  -1.290  1.00 37.45 ? 104 CYS A CA    1 
ATOM   793  C C     . CYS A 1 104 ? -36.384 84.050  -0.792  1.00 38.32 ? 104 CYS A C     1 
ATOM   794  O O     . CYS A 1 104 ? -35.348 84.721  -0.718  1.00 38.60 ? 104 CYS A O     1 
ATOM   795  C CB    . CYS A 1 104 ? -36.333 81.676  -0.082  1.00 34.56 ? 104 CYS A CB    1 
ATOM   796  S SG    . CYS A 1 104 ? -34.749 81.163  0.565   1.00 33.70 ? 104 CYS A SG    1 
ATOM   797  N N     . SER A 1 105 ? -37.555 84.515  -0.345  1.00 38.67 ? 105 SER A N     1 
ATOM   798  C CA    . SER A 1 105 ? -37.673 85.898  0.069   1.00 39.48 ? 105 SER A CA    1 
ATOM   799  C C     . SER A 1 105 ? -36.971 86.154  1.394   1.00 39.54 ? 105 SER A C     1 
ATOM   800  O O     . SER A 1 105 ? -37.093 85.361  2.343   1.00 39.32 ? 105 SER A O     1 
ATOM   801  C CB    . SER A 1 105 ? -39.130 86.355  0.168   1.00 43.13 ? 105 SER A CB    1 
ATOM   802  O OG    . SER A 1 105 ? -39.706 86.187  -1.129  1.00 49.26 ? 105 SER A OG    1 
ATOM   803  N N     . GLY A 1 106 ? -36.121 87.202  1.350   1.00 39.07 ? 106 GLY A N     1 
ATOM   804  C CA    . GLY A 1 106 ? -35.346 87.567  2.532   1.00 38.37 ? 106 GLY A CA    1 
ATOM   805  C C     . GLY A 1 106 ? -34.001 86.846  2.551   1.00 38.17 ? 106 GLY A C     1 
ATOM   806  O O     . GLY A 1 106 ? -33.055 87.280  3.216   1.00 38.05 ? 106 GLY A O     1 
ATOM   807  N N     . CYS A 1 107 ? -33.938 85.680  1.923   1.00 37.71 ? 107 CYS A N     1 
ATOM   808  C CA    . CYS A 1 107 ? -32.757 84.854  1.898   1.00 37.33 ? 107 CYS A CA    1 
ATOM   809  C C     . CYS A 1 107 ? -31.570 85.563  1.244   1.00 37.04 ? 107 CYS A C     1 
ATOM   810  O O     . CYS A 1 107 ? -31.592 85.926  0.063   1.00 37.10 ? 107 CYS A O     1 
ATOM   811  C CB    . CYS A 1 107 ? -33.087 83.565  1.128   1.00 35.71 ? 107 CYS A CB    1 
ATOM   812  S SG    . CYS A 1 107 ? -34.220 82.480  2.002   1.00 33.20 ? 107 CYS A SG    1 
ATOM   813  N N     . ARG A 1 108 ? -30.457 85.461  1.959   1.00 36.66 ? 108 ARG A N     1 
ATOM   814  C CA    . ARG A 1 108 ? -29.182 85.967  1.443   1.00 36.63 ? 108 ARG A CA    1 
ATOM   815  C C     . ARG A 1 108 ? -28.122 84.862  1.450   1.00 35.83 ? 108 ARG A C     1 
ATOM   816  O O     . ARG A 1 108 ? -27.957 84.147  2.460   1.00 35.67 ? 108 ARG A O     1 
ATOM   817  C CB    . ARG A 1 108 ? -28.695 87.166  2.237   1.00 38.93 ? 108 ARG A CB    1 
ATOM   818  C CG    . ARG A 1 108 ? -29.312 88.457  1.751   1.00 43.37 ? 108 ARG A CG    1 
ATOM   819  C CD    . ARG A 1 108 ? -29.137 89.585  2.770   1.00 46.61 ? 108 ARG A CD    1 
ATOM   820  N NE    . ARG A 1 108 ? -27.891 90.254  2.372   1.00 51.85 ? 108 ARG A NE    1 
ATOM   821  C CZ    . ARG A 1 108 ? -27.095 90.831  3.272   1.00 55.19 ? 108 ARG A CZ    1 
ATOM   822  N NH1   . ARG A 1 108 ? -27.439 90.818  4.562   1.00 57.13 ? 108 ARG A NH1   1 
ATOM   823  N NH2   . ARG A 1 108 ? -25.956 91.421  2.913   1.00 56.01 ? 108 ARG A NH2   1 
ATOM   824  N N     . GLY A 1 109 ? -27.437 84.687  0.313   1.00 34.66 ? 109 GLY A N     1 
ATOM   825  C CA    . GLY A 1 109 ? -26.479 83.579  0.274   1.00 33.94 ? 109 GLY A CA    1 
ATOM   826  C C     . GLY A 1 109 ? -25.033 84.036  0.203   1.00 33.52 ? 109 GLY A C     1 
ATOM   827  O O     . GLY A 1 109 ? -24.732 85.131  -0.285  1.00 33.24 ? 109 GLY A O     1 
ATOM   828  N N     . HIS A 1 110 ? -24.119 83.203  0.714   1.00 32.82 ? 110 HIS A N     1 
ATOM   829  C CA    . HIS A 1 110 ? -22.691 83.496  0.519   1.00 32.08 ? 110 HIS A CA    1 
ATOM   830  C C     . HIS A 1 110 ? -22.467 83.761  -0.975  1.00 31.99 ? 110 HIS A C     1 
ATOM   831  O O     . HIS A 1 110 ? -22.619 82.856  -1.801  1.00 31.80 ? 110 HIS A O     1 
ATOM   832  C CB    . HIS A 1 110 ? -21.894 82.267  0.856   1.00 29.53 ? 110 HIS A CB    1 
ATOM   833  C CG    . HIS A 1 110 ? -20.428 82.221  0.622   1.00 27.97 ? 110 HIS A CG    1 
ATOM   834  N ND1   . HIS A 1 110 ? -19.830 81.900  -0.568  1.00 26.50 ? 110 HIS A ND1   1 
ATOM   835  C CD2   . HIS A 1 110 ? -19.391 82.391  1.495   1.00 27.37 ? 110 HIS A CD2   1 
ATOM   836  C CE1   . HIS A 1 110 ? -18.522 81.883  -0.409  1.00 26.85 ? 110 HIS A CE1   1 
ATOM   837  N NE2   . HIS A 1 110 ? -18.216 82.171  0.846   1.00 25.67 ? 110 HIS A NE2   1 
ATOM   838  N N     . ASP A 1 111 ? -21.785 84.852  -1.276  1.00 31.83 ? 111 ASP A N     1 
ATOM   839  C CA    . ASP A 1 111 ? -21.612 85.263  -2.651  1.00 31.52 ? 111 ASP A CA    1 
ATOM   840  C C     . ASP A 1 111 ? -21.080 84.229  -3.622  1.00 31.67 ? 111 ASP A C     1 
ATOM   841  O O     . ASP A 1 111 ? -21.714 83.864  -4.612  1.00 32.57 ? 111 ASP A O     1 
ATOM   842  C CB    . ASP A 1 111 ? -20.682 86.482  -2.694  1.00 30.02 ? 111 ASP A CB    1 
ATOM   843  C CG    . ASP A 1 111 ? -20.983 87.227  -3.978  1.00 30.91 ? 111 ASP A CG    1 
ATOM   844  O OD1   . ASP A 1 111 ? -20.878 88.462  -3.950  1.00 32.75 ? 111 ASP A OD1   1 
ATOM   845  O OD2   . ASP A 1 111 ? -21.360 86.611  -4.986  1.00 30.96 ? 111 ASP A OD2   1 
ATOM   846  N N     . GLY A 1 112 ? -19.843 83.793  -3.446  1.00 31.18 ? 112 GLY A N     1 
ATOM   847  C CA    . GLY A 1 112 ? -19.111 82.875  -4.264  1.00 30.22 ? 112 GLY A CA    1 
ATOM   848  C C     . GLY A 1 112 ? -19.791 81.559  -4.571  1.00 30.38 ? 112 GLY A C     1 
ATOM   849  O O     . GLY A 1 112 ? -19.933 81.097  -5.715  1.00 30.47 ? 112 GLY A O     1 
ATOM   850  N N     . PHE A 1 113 ? -20.314 80.949  -3.497  1.00 29.85 ? 113 PHE A N     1 
ATOM   851  C CA    . PHE A 1 113 ? -21.032 79.685  -3.640  1.00 28.94 ? 113 PHE A CA    1 
ATOM   852  C C     . PHE A 1 113 ? -22.203 79.914  -4.590  1.00 29.15 ? 113 PHE A C     1 
ATOM   853  O O     . PHE A 1 113 ? -22.357 79.201  -5.587  1.00 29.16 ? 113 PHE A O     1 
ATOM   854  C CB    . PHE A 1 113 ? -21.521 79.108  -2.326  1.00 25.28 ? 113 PHE A CB    1 
ATOM   855  C CG    . PHE A 1 113 ? -20.489 78.823  -1.283  1.00 22.39 ? 113 PHE A CG    1 
ATOM   856  C CD1   . PHE A 1 113 ? -19.193 78.513  -1.646  1.00 21.93 ? 113 PHE A CD1   1 
ATOM   857  C CD2   . PHE A 1 113 ? -20.801 78.863  0.070   1.00 21.66 ? 113 PHE A CD2   1 
ATOM   858  C CE1   . PHE A 1 113 ? -18.224 78.253  -0.686  1.00 21.32 ? 113 PHE A CE1   1 
ATOM   859  C CE2   . PHE A 1 113 ? -19.824 78.604  1.025   1.00 20.90 ? 113 PHE A CE2   1 
ATOM   860  C CZ    . PHE A 1 113 ? -18.537 78.289  0.652   1.00 19.60 ? 113 PHE A CZ    1 
ATOM   861  N N     . THR A 1 114 ? -22.965 80.966  -4.297  1.00 29.36 ? 114 THR A N     1 
ATOM   862  C CA    . THR A 1 114 ? -24.084 81.316  -5.156  1.00 30.26 ? 114 THR A CA    1 
ATOM   863  C C     . THR A 1 114 ? -23.686 81.624  -6.591  1.00 30.15 ? 114 THR A C     1 
ATOM   864  O O     . THR A 1 114 ? -24.248 81.070  -7.535  1.00 30.39 ? 114 THR A O     1 
ATOM   865  C CB    . THR A 1 114 ? -24.873 82.539  -4.661  1.00 32.49 ? 114 THR A CB    1 
ATOM   866  O OG1   . THR A 1 114 ? -24.676 82.738  -3.266  1.00 34.86 ? 114 THR A OG1   1 
ATOM   867  C CG2   . THR A 1 114 ? -26.343 82.187  -4.885  1.00 33.85 ? 114 THR A CG2   1 
ATOM   868  N N     . SER A 1 115 ? -22.699 82.487  -6.771  1.00 30.32 ? 115 SER A N     1 
ATOM   869  C CA    . SER A 1 115 ? -22.204 82.827  -8.101  1.00 30.57 ? 115 SER A CA    1 
ATOM   870  C C     . SER A 1 115 ? -21.698 81.613  -8.858  1.00 30.57 ? 115 SER A C     1 
ATOM   871  O O     . SER A 1 115 ? -22.042 81.468  -10.029 1.00 30.68 ? 115 SER A O     1 
ATOM   872  C CB    . SER A 1 115 ? -21.086 83.857  -7.997  1.00 30.95 ? 115 SER A CB    1 
ATOM   873  O OG    . SER A 1 115 ? -21.343 84.664  -6.863  1.00 31.95 ? 115 SER A OG    1 
ATOM   874  N N     . SER A 1 116 ? -20.894 80.785  -8.197  1.00 30.50 ? 116 SER A N     1 
ATOM   875  C CA    . SER A 1 116 ? -20.445 79.550  -8.834  1.00 30.39 ? 116 SER A CA    1 
ATOM   876  C C     . SER A 1 116 ? -21.660 78.745  -9.301  1.00 29.99 ? 116 SER A C     1 
ATOM   877  O O     . SER A 1 116 ? -21.797 78.485  -10.489 1.00 29.15 ? 116 SER A O     1 
ATOM   878  C CB    . SER A 1 116 ? -19.592 78.720  -7.873  1.00 30.26 ? 116 SER A CB    1 
ATOM   879  O OG    . SER A 1 116 ? -18.376 79.370  -7.587  1.00 30.59 ? 116 SER A OG    1 
ATOM   880  N N     . TRP A 1 117 ? -22.604 78.480  -8.404  1.00 30.12 ? 117 TRP A N     1 
ATOM   881  C CA    . TRP A 1 117 ? -23.752 77.672  -8.784  1.00 31.21 ? 117 TRP A CA    1 
ATOM   882  C C     . TRP A 1 117 ? -24.514 78.319  -9.932  1.00 31.83 ? 117 TRP A C     1 
ATOM   883  O O     . TRP A 1 117 ? -24.794 77.741  -10.987 1.00 31.76 ? 117 TRP A O     1 
ATOM   884  C CB    . TRP A 1 117 ? -24.697 77.402  -7.604  1.00 30.41 ? 117 TRP A CB    1 
ATOM   885  C CG    . TRP A 1 117 ? -26.024 76.898  -8.102  1.00 28.44 ? 117 TRP A CG    1 
ATOM   886  C CD1   . TRP A 1 117 ? -27.226 77.524  -8.005  1.00 27.46 ? 117 TRP A CD1   1 
ATOM   887  C CD2   . TRP A 1 117 ? -26.257 75.680  -8.814  1.00 28.53 ? 117 TRP A CD2   1 
ATOM   888  N NE1   . TRP A 1 117 ? -28.200 76.758  -8.600  1.00 26.69 ? 117 TRP A NE1   1 
ATOM   889  C CE2   . TRP A 1 117 ? -27.640 75.627  -9.105  1.00 27.59 ? 117 TRP A CE2   1 
ATOM   890  C CE3   . TRP A 1 117 ? -25.441 74.629  -9.241  1.00 28.45 ? 117 TRP A CE3   1 
ATOM   891  C CZ2   . TRP A 1 117 ? -28.218 74.567  -9.798  1.00 27.92 ? 117 TRP A CZ2   1 
ATOM   892  C CZ3   . TRP A 1 117 ? -26.025 73.573  -9.931  1.00 28.68 ? 117 TRP A CZ3   1 
ATOM   893  C CH2   . TRP A 1 117 ? -27.401 73.542  -10.202 1.00 28.07 ? 117 TRP A CH2   1 
ATOM   894  N N     . ARG A 1 118 ? -24.833 79.602  -9.772  1.00 32.44 ? 118 ARG A N     1 
ATOM   895  C CA    . ARG A 1 118 ? -25.559 80.329  -10.806 1.00 33.21 ? 118 ARG A CA    1 
ATOM   896  C C     . ARG A 1 118 ? -24.887 80.277  -12.159 1.00 32.93 ? 118 ARG A C     1 
ATOM   897  O O     . ARG A 1 118 ? -25.529 80.070  -13.192 1.00 33.08 ? 118 ARG A O     1 
ATOM   898  C CB    . ARG A 1 118 ? -25.879 81.742  -10.325 1.00 37.61 ? 118 ARG A CB    1 
ATOM   899  C CG    . ARG A 1 118 ? -27.377 81.964  -10.215 1.00 44.97 ? 118 ARG A CG    1 
ATOM   900  C CD    . ARG A 1 118 ? -27.824 82.612  -8.923  1.00 50.31 ? 118 ARG A CD    1 
ATOM   901  N NE    . ARG A 1 118 ? -29.157 82.269  -8.463  1.00 54.37 ? 118 ARG A NE    1 
ATOM   902  C CZ    . ARG A 1 118 ? -29.969 81.243  -8.661  1.00 55.27 ? 118 ARG A CZ    1 
ATOM   903  N NH1   . ARG A 1 118 ? -29.693 80.207  -9.452  1.00 53.64 ? 118 ARG A NH1   1 
ATOM   904  N NH2   . ARG A 1 118 ? -31.146 81.246  -8.020  1.00 55.77 ? 118 ARG A NH2   1 
ATOM   905  N N     . SER A 1 119 ? -23.568 80.230  -12.240 1.00 32.77 ? 119 SER A N     1 
ATOM   906  C CA    . SER A 1 119 ? -22.779 80.179  -13.439 1.00 32.43 ? 119 SER A CA    1 
ATOM   907  C C     . SER A 1 119 ? -22.790 78.844  -14.157 1.00 32.49 ? 119 SER A C     1 
ATOM   908  O O     . SER A 1 119 ? -22.314 78.745  -15.290 1.00 31.97 ? 119 SER A O     1 
ATOM   909  C CB    . SER A 1 119 ? -21.315 80.530  -13.132 1.00 32.92 ? 119 SER A CB    1 
ATOM   910  O OG    . SER A 1 119 ? -20.649 79.489  -12.457 1.00 32.85 ? 119 SER A OG    1 
ATOM   911  N N     . VAL A 1 120 ? -23.322 77.818  -13.513 1.00 33.03 ? 120 VAL A N     1 
ATOM   912  C CA    . VAL A 1 120 ? -23.307 76.462  -14.077 1.00 33.35 ? 120 VAL A CA    1 
ATOM   913  C C     . VAL A 1 120 ? -24.657 75.782  -13.907 1.00 33.92 ? 120 VAL A C     1 
ATOM   914  O O     . VAL A 1 120 ? -25.000 74.801  -14.579 1.00 34.12 ? 120 VAL A O     1 
ATOM   915  C CB    . VAL A 1 120 ? -22.123 75.749  -13.409 1.00 31.19 ? 120 VAL A CB    1 
ATOM   916  C CG1   . VAL A 1 120 ? -22.530 75.016  -12.149 1.00 30.83 ? 120 VAL A CG1   1 
ATOM   917  C CG2   . VAL A 1 120 ? -21.370 74.854  -14.360 1.00 32.63 ? 120 VAL A CG2   1 
ATOM   918  N N     . ALA A 1 121 ? -25.595 76.475  -13.252 1.00 34.19 ? 121 ALA A N     1 
ATOM   919  C CA    . ALA A 1 121 ? -26.940 76.000  -13.004 1.00 34.40 ? 121 ALA A CA    1 
ATOM   920  C C     . ALA A 1 121 ? -27.684 75.488  -14.219 1.00 35.01 ? 121 ALA A C     1 
ATOM   921  O O     . ALA A 1 121 ? -28.362 74.470  -14.057 1.00 35.13 ? 121 ALA A O     1 
ATOM   922  C CB    . ALA A 1 121 ? -27.792 77.016  -12.263 1.00 30.37 ? 121 ALA A CB    1 
ATOM   923  N N     . ASP A 1 122 ? -27.744 76.178  -15.349 1.00 36.21 ? 122 ASP A N     1 
ATOM   924  C CA    . ASP A 1 122 ? -28.508 75.697  -16.506 1.00 37.12 ? 122 ASP A CA    1 
ATOM   925  C C     . ASP A 1 122 ? -27.990 74.372  -17.042 1.00 37.16 ? 122 ASP A C     1 
ATOM   926  O O     . ASP A 1 122 ? -28.628 73.323  -16.956 1.00 37.73 ? 122 ASP A O     1 
ATOM   927  C CB    . ASP A 1 122 ? -28.510 76.682  -17.665 1.00 41.02 ? 122 ASP A CB    1 
ATOM   928  C CG    . ASP A 1 122 ? -29.302 77.949  -17.406 1.00 45.30 ? 122 ASP A CG    1 
ATOM   929  O OD1   . ASP A 1 122 ? -29.138 78.951  -18.156 1.00 46.79 ? 122 ASP A OD1   1 
ATOM   930  O OD2   . ASP A 1 122 ? -30.118 77.969  -16.456 1.00 46.50 ? 122 ASP A OD2   1 
ATOM   931  N N     . THR A 1 123 ? -26.758 74.357  -17.516 1.00 36.95 ? 123 THR A N     1 
ATOM   932  C CA    . THR A 1 123 ? -26.105 73.130  -17.958 1.00 36.93 ? 123 THR A CA    1 
ATOM   933  C C     . THR A 1 123 ? -26.415 71.941  -17.064 1.00 36.97 ? 123 THR A C     1 
ATOM   934  O O     . THR A 1 123 ? -26.941 70.925  -17.513 1.00 37.11 ? 123 THR A O     1 
ATOM   935  C CB    . THR A 1 123 ? -24.589 73.417  -17.981 1.00 36.36 ? 123 THR A CB    1 
ATOM   936  O OG1   . THR A 1 123 ? -24.429 74.461  -18.955 1.00 37.51 ? 123 THR A OG1   1 
ATOM   937  C CG2   . THR A 1 123 ? -23.796 72.183  -18.344 1.00 35.40 ? 123 THR A CG2   1 
ATOM   938  N N     . LEU A 1 124 ? -26.109 72.048  -15.774 1.00 36.76 ? 124 LEU A N     1 
ATOM   939  C CA    . LEU A 1 124 ? -26.340 70.971  -14.829 1.00 36.35 ? 124 LEU A CA    1 
ATOM   940  C C     . LEU A 1 124 ? -27.816 70.678  -14.660 1.00 36.56 ? 124 LEU A C     1 
ATOM   941  O O     . LEU A 1 124 ? -28.236 69.542  -14.939 1.00 36.82 ? 124 LEU A O     1 
ATOM   942  C CB    . LEU A 1 124 ? -25.613 71.288  -13.531 1.00 34.76 ? 124 LEU A CB    1 
ATOM   943  C CG    . LEU A 1 124 ? -24.341 70.542  -13.167 1.00 34.24 ? 124 LEU A CG    1 
ATOM   944  C CD1   . LEU A 1 124 ? -23.663 69.812  -14.320 1.00 34.76 ? 124 LEU A CD1   1 
ATOM   945  C CD2   . LEU A 1 124 ? -23.339 71.496  -12.540 1.00 33.68 ? 124 LEU A CD2   1 
ATOM   946  N N     . ARG A 1 125 ? -28.667 71.690  -14.471 1.00 36.53 ? 125 ARG A N     1 
ATOM   947  C CA    . ARG A 1 125 ? -30.106 71.469  -14.340 1.00 36.78 ? 125 ARG A CA    1 
ATOM   948  C C     . ARG A 1 125 ? -30.624 70.545  -15.440 1.00 36.24 ? 125 ARG A C     1 
ATOM   949  O O     . ARG A 1 125 ? -31.321 69.563  -15.220 1.00 35.71 ? 125 ARG A O     1 
ATOM   950  C CB    . ARG A 1 125 ? -30.933 72.754  -14.320 1.00 39.82 ? 125 ARG A CB    1 
ATOM   951  C CG    . ARG A 1 125 ? -32.435 72.553  -14.272 1.00 44.67 ? 125 ARG A CG    1 
ATOM   952  C CD    . ARG A 1 125 ? -33.266 73.784  -14.613 1.00 50.18 ? 125 ARG A CD    1 
ATOM   953  N NE    . ARG A 1 125 ? -33.305 74.775  -13.540 1.00 55.73 ? 125 ARG A NE    1 
ATOM   954  C CZ    . ARG A 1 125 ? -32.597 75.901  -13.430 1.00 58.29 ? 125 ARG A CZ    1 
ATOM   955  N NH1   . ARG A 1 125 ? -32.689 76.717  -12.373 1.00 58.15 ? 125 ARG A NH1   1 
ATOM   956  N NH2   . ARG A 1 125 ? -31.773 76.327  -14.392 1.00 58.99 ? 125 ARG A NH2   1 
ATOM   957  N N     . GLN A 1 126 ? -30.256 70.872  -16.673 1.00 36.23 ? 126 GLN A N     1 
ATOM   958  C CA    . GLN A 1 126 ? -30.596 70.069  -17.823 1.00 36.19 ? 126 GLN A CA    1 
ATOM   959  C C     . GLN A 1 126 ? -29.971 68.686  -17.843 1.00 35.48 ? 126 GLN A C     1 
ATOM   960  O O     . GLN A 1 126 ? -30.646 67.732  -18.258 1.00 35.62 ? 126 GLN A O     1 
ATOM   961  C CB    . GLN A 1 126 ? -30.242 70.850  -19.081 1.00 39.66 ? 126 GLN A CB    1 
ATOM   962  C CG    . GLN A 1 126 ? -30.799 70.152  -20.321 1.00 46.49 ? 126 GLN A CG    1 
ATOM   963  C CD    . GLN A 1 126 ? -29.775 70.268  -21.438 1.00 51.09 ? 126 GLN A CD    1 
ATOM   964  O OE1   . GLN A 1 126 ? -29.253 69.268  -21.937 1.00 53.43 ? 126 GLN A OE1   1 
ATOM   965  N NE2   . GLN A 1 126 ? -29.463 71.513  -21.805 1.00 53.87 ? 126 GLN A NE2   1 
ATOM   966  N N     . LYS A 1 127 ? -28.743 68.503  -17.369 1.00 34.64 ? 127 LYS A N     1 
ATOM   967  C CA    . LYS A 1 127 ? -28.153 67.167  -17.376 1.00 33.92 ? 127 LYS A CA    1 
ATOM   968  C C     . LYS A 1 127 ? -28.906 66.279  -16.398 1.00 33.83 ? 127 LYS A C     1 
ATOM   969  O O     . LYS A 1 127 ? -29.128 65.107  -16.659 1.00 33.93 ? 127 LYS A O     1 
ATOM   970  C CB    . LYS A 1 127 ? -26.676 67.233  -17.032 1.00 33.26 ? 127 LYS A CB    1 
ATOM   971  C CG    . LYS A 1 127 ? -25.894 68.027  -18.061 1.00 32.88 ? 127 LYS A CG    1 
ATOM   972  C CD    . LYS A 1 127 ? -25.422 67.141  -19.196 1.00 32.71 ? 127 LYS A CD    1 
ATOM   973  C CE    . LYS A 1 127 ? -24.748 67.982  -20.260 1.00 33.63 ? 127 LYS A CE    1 
ATOM   974  N NZ    . LYS A 1 127 ? -24.819 67.326  -21.597 1.00 37.04 ? 127 LYS A NZ    1 
ATOM   975  N N     . VAL A 1 128 ? -29.280 66.838  -15.256 1.00 33.77 ? 128 VAL A N     1 
ATOM   976  C CA    . VAL A 1 128 ? -30.078 66.131  -14.264 1.00 33.82 ? 128 VAL A CA    1 
ATOM   977  C C     . VAL A 1 128 ? -31.446 65.774  -14.831 1.00 34.45 ? 128 VAL A C     1 
ATOM   978  O O     . VAL A 1 128 ? -31.806 64.603  -14.906 1.00 34.56 ? 128 VAL A O     1 
ATOM   979  C CB    . VAL A 1 128 ? -30.280 67.021  -13.023 1.00 32.73 ? 128 VAL A CB    1 
ATOM   980  C CG1   . VAL A 1 128 ? -31.077 66.318  -11.941 1.00 30.03 ? 128 VAL A CG1   1 
ATOM   981  C CG2   . VAL A 1 128 ? -28.920 67.519  -12.558 1.00 31.69 ? 128 VAL A CG2   1 
ATOM   982  N N     . GLU A 1 129 ? -32.128 66.753  -15.424 1.00 35.01 ? 129 GLU A N     1 
ATOM   983  C CA    . GLU A 1 129 ? -33.435 66.540  -16.022 1.00 35.50 ? 129 GLU A CA    1 
ATOM   984  C C     . GLU A 1 129 ? -33.472 65.527  -17.146 1.00 35.62 ? 129 GLU A C     1 
ATOM   985  O O     . GLU A 1 129 ? -34.213 64.538  -16.999 1.00 35.69 ? 129 GLU A O     1 
ATOM   986  C CB    . GLU A 1 129 ? -34.110 67.877  -16.358 1.00 35.87 ? 129 GLU A CB    1 
ATOM   987  C CG    . GLU A 1 129 ? -34.497 68.549  -15.055 1.00 38.63 ? 129 GLU A CG    1 
ATOM   988  C CD    . GLU A 1 129 ? -35.240 69.858  -15.066 1.00 39.93 ? 129 GLU A CD    1 
ATOM   989  O OE1   . GLU A 1 129 ? -35.392 70.441  -13.961 1.00 37.05 ? 129 GLU A OE1   1 
ATOM   990  O OE2   . GLU A 1 129 ? -35.676 70.322  -16.146 1.00 42.25 ? 129 GLU A OE2   1 
ATOM   991  N N     . ASP A 1 130 ? -32.471 65.468  -18.024 1.00 35.89 ? 130 ASP A N     1 
ATOM   992  C CA    . ASP A 1 130 ? -32.465 64.382  -19.008 1.00 36.56 ? 130 ASP A CA    1 
ATOM   993  C C     . ASP A 1 130 ? -32.322 63.041  -18.279 1.00 35.81 ? 130 ASP A C     1 
ATOM   994  O O     . ASP A 1 130 ? -32.862 62.047  -18.756 1.00 35.69 ? 130 ASP A O     1 
ATOM   995  C CB    . ASP A 1 130 ? -31.364 64.466  -20.050 1.00 41.80 ? 130 ASP A CB    1 
ATOM   996  C CG    . ASP A 1 130 ? -31.353 65.742  -20.855 1.00 45.85 ? 130 ASP A CG    1 
ATOM   997  O OD1   . ASP A 1 130 ? -32.386 66.446  -20.901 1.00 49.06 ? 130 ASP A OD1   1 
ATOM   998  O OD2   . ASP A 1 130 ? -30.282 66.045  -21.436 1.00 48.09 ? 130 ASP A OD2   1 
ATOM   999  N N     . ALA A 1 131 ? -31.452 62.999  -17.278 1.00 35.01 ? 131 ALA A N     1 
ATOM   1000 C CA    . ALA A 1 131 ? -31.218 61.775  -16.526 1.00 34.55 ? 131 ALA A CA    1 
ATOM   1001 C C     . ALA A 1 131 ? -32.511 61.208  -15.950 1.00 34.31 ? 131 ALA A C     1 
ATOM   1002 O O     . ALA A 1 131 ? -32.866 60.057  -16.161 1.00 33.48 ? 131 ALA A O     1 
ATOM   1003 C CB    . ALA A 1 131 ? -30.230 62.037  -15.392 1.00 33.63 ? 131 ALA A CB    1 
ATOM   1004 N N     . VAL A 1 132 ? -33.242 62.056  -15.229 1.00 34.52 ? 132 VAL A N     1 
ATOM   1005 C CA    . VAL A 1 132 ? -34.499 61.720  -14.580 1.00 34.41 ? 132 VAL A CA    1 
ATOM   1006 C C     . VAL A 1 132 ? -35.508 61.222  -15.607 1.00 34.84 ? 132 VAL A C     1 
ATOM   1007 O O     . VAL A 1 132 ? -36.271 60.295  -15.380 1.00 34.69 ? 132 VAL A O     1 
ATOM   1008 C CB    . VAL A 1 132 ? -35.060 62.935  -13.825 1.00 32.17 ? 132 VAL A CB    1 
ATOM   1009 C CG1   . VAL A 1 132 ? -36.560 62.823  -13.602 1.00 33.19 ? 132 VAL A CG1   1 
ATOM   1010 C CG2   . VAL A 1 132 ? -34.365 63.122  -12.489 1.00 31.28 ? 132 VAL A CG2   1 
ATOM   1011 N N     . ARG A 1 133 ? -35.540 61.886  -16.754 1.00 35.22 ? 133 ARG A N     1 
ATOM   1012 C CA    . ARG A 1 133 ? -36.392 61.555  -17.872 1.00 35.51 ? 133 ARG A CA    1 
ATOM   1013 C C     . ARG A 1 133 ? -36.201 60.106  -18.282 1.00 35.67 ? 133 ARG A C     1 
ATOM   1014 O O     . ARG A 1 133 ? -37.176 59.409  -18.527 1.00 36.27 ? 133 ARG A O     1 
ATOM   1015 C CB    . ARG A 1 133 ? -36.058 62.452  -19.059 1.00 37.37 ? 133 ARG A CB    1 
ATOM   1016 C CG    . ARG A 1 133 ? -37.079 62.470  -20.184 1.00 39.49 ? 133 ARG A CG    1 
ATOM   1017 C CD    . ARG A 1 133 ? -36.870 63.688  -21.090 1.00 41.77 ? 133 ARG A CD    1 
ATOM   1018 N N     . GLU A 1 134 ? -34.967 59.660  -18.396 1.00 35.90 ? 134 GLU A N     1 
ATOM   1019 C CA    . GLU A 1 134 ? -34.612 58.319  -18.794 1.00 35.77 ? 134 GLU A CA    1 
ATOM   1020 C C     . GLU A 1 134 ? -34.714 57.297  -17.682 1.00 35.82 ? 134 GLU A C     1 
ATOM   1021 O O     . GLU A 1 134 ? -34.531 56.100  -17.967 1.00 36.45 ? 134 GLU A O     1 
ATOM   1022 C CB    . GLU A 1 134 ? -33.179 58.302  -19.350 1.00 36.23 ? 134 GLU A CB    1 
ATOM   1023 C CG    . GLU A 1 134 ? -32.999 59.083  -20.644 1.00 37.71 ? 134 GLU A CG    1 
ATOM   1024 N N     . HIS A 1 135 ? -34.621 57.671  -16.405 1.00 35.14 ? 135 HIS A N     1 
ATOM   1025 C CA    . HIS A 1 135 ? -34.695 56.780  -15.258 1.00 34.35 ? 135 HIS A CA    1 
ATOM   1026 C C     . HIS A 1 135 ? -35.539 57.440  -14.175 1.00 34.10 ? 135 HIS A C     1 
ATOM   1027 O O     . HIS A 1 135 ? -35.114 57.802  -13.076 1.00 34.61 ? 135 HIS A O     1 
ATOM   1028 C CB    . HIS A 1 135 ? -33.321 56.433  -14.690 1.00 35.42 ? 135 HIS A CB    1 
ATOM   1029 C CG    . HIS A 1 135 ? -32.327 56.007  -15.727 1.00 38.05 ? 135 HIS A CG    1 
ATOM   1030 N ND1   . HIS A 1 135 ? -32.402 54.781  -16.349 1.00 38.86 ? 135 HIS A ND1   1 
ATOM   1031 C CD2   . HIS A 1 135 ? -31.318 56.673  -16.342 1.00 39.13 ? 135 HIS A CD2   1 
ATOM   1032 C CE1   . HIS A 1 135 ? -31.442 54.677  -17.251 1.00 39.26 ? 135 HIS A CE1   1 
ATOM   1033 N NE2   . HIS A 1 135 ? -30.775 55.820  -17.271 1.00 39.94 ? 135 HIS A NE2   1 
ATOM   1034 N N     . PRO A 1 136 ? -36.821 57.639  -14.480 1.00 33.54 ? 136 PRO A N     1 
ATOM   1035 C CA    . PRO A 1 136 ? -37.799 58.297  -13.634 1.00 33.40 ? 136 PRO A CA    1 
ATOM   1036 C C     . PRO A 1 136 ? -38.103 57.657  -12.296 1.00 33.78 ? 136 PRO A C     1 
ATOM   1037 O O     . PRO A 1 136 ? -38.855 58.229  -11.506 1.00 33.52 ? 136 PRO A O     1 
ATOM   1038 C CB    . PRO A 1 136 ? -39.072 58.282  -14.493 1.00 32.92 ? 136 PRO A CB    1 
ATOM   1039 C CG    . PRO A 1 136 ? -38.892 57.006  -15.257 1.00 32.60 ? 136 PRO A CG    1 
ATOM   1040 C CD    . PRO A 1 136 ? -37.474 57.141  -15.726 1.00 32.93 ? 136 PRO A CD    1 
ATOM   1041 N N     . ASP A 1 137 ? -37.712 56.416  -12.094 1.00 34.49 ? 137 ASP A N     1 
ATOM   1042 C CA    . ASP A 1 137 ? -37.877 55.695  -10.856 1.00 35.86 ? 137 ASP A CA    1 
ATOM   1043 C C     . ASP A 1 137 ? -36.623 55.853  -9.996  1.00 36.33 ? 137 ASP A C     1 
ATOM   1044 O O     . ASP A 1 137 ? -36.665 55.582  -8.790  1.00 36.66 ? 137 ASP A O     1 
ATOM   1045 C CB    . ASP A 1 137 ? -38.162 54.219  -11.132 1.00 39.57 ? 137 ASP A CB    1 
ATOM   1046 C CG    . ASP A 1 137 ? -37.078 53.505  -11.921 1.00 42.32 ? 137 ASP A CG    1 
ATOM   1047 O OD1   . ASP A 1 137 ? -36.750 54.002  -13.027 1.00 43.00 ? 137 ASP A OD1   1 
ATOM   1048 O OD2   . ASP A 1 137 ? -36.587 52.460  -11.426 1.00 43.44 ? 137 ASP A OD2   1 
ATOM   1049 N N     . TYR A 1 138 ? -35.515 56.264  -10.615 1.00 36.31 ? 138 TYR A N     1 
ATOM   1050 C CA    . TYR A 1 138 ? -34.252 56.425  -9.885  1.00 35.39 ? 138 TYR A CA    1 
ATOM   1051 C C     . TYR A 1 138 ? -34.369 57.609  -8.946  1.00 34.27 ? 138 TYR A C     1 
ATOM   1052 O O     . TYR A 1 138 ? -35.237 58.439  -9.204  1.00 34.27 ? 138 TYR A O     1 
ATOM   1053 C CB    . TYR A 1 138 ? -33.106 56.629  -10.870 1.00 36.43 ? 138 TYR A CB    1 
ATOM   1054 C CG    . TYR A 1 138 ? -32.550 55.318  -11.382 1.00 38.16 ? 138 TYR A CG    1 
ATOM   1055 C CD1   . TYR A 1 138 ? -33.369 54.217  -11.595 1.00 38.55 ? 138 TYR A CD1   1 
ATOM   1056 C CD2   . TYR A 1 138 ? -31.198 55.180  -11.651 1.00 39.00 ? 138 TYR A CD2   1 
ATOM   1057 C CE1   . TYR A 1 138 ? -32.848 53.027  -12.051 1.00 38.94 ? 138 TYR A CE1   1 
ATOM   1058 C CE2   . TYR A 1 138 ? -30.671 53.987  -12.102 1.00 39.52 ? 138 TYR A CE2   1 
ATOM   1059 C CZ    . TYR A 1 138 ? -31.504 52.913  -12.305 1.00 39.45 ? 138 TYR A CZ    1 
ATOM   1060 O OH    . TYR A 1 138 ? -31.023 51.702  -12.743 1.00 40.01 ? 138 TYR A OH    1 
ATOM   1061 N N     . ARG A 1 139 ? -33.586 57.630  -7.889  1.00 32.93 ? 139 ARG A N     1 
ATOM   1062 C CA    . ARG A 1 139 ? -33.632 58.728  -6.926  1.00 31.80 ? 139 ARG A CA    1 
ATOM   1063 C C     . ARG A 1 139 ? -32.501 59.717  -7.165  1.00 31.85 ? 139 ARG A C     1 
ATOM   1064 O O     . ARG A 1 139 ? -31.400 59.347  -7.575  1.00 32.10 ? 139 ARG A O     1 
ATOM   1065 C CB    . ARG A 1 139 ? -33.673 58.183  -5.527  1.00 28.59 ? 139 ARG A CB    1 
ATOM   1066 C CG    . ARG A 1 139 ? -33.122 58.972  -4.358  1.00 27.75 ? 139 ARG A CG    1 
ATOM   1067 C CD    . ARG A 1 139 ? -33.421 58.174  -3.108  1.00 29.09 ? 139 ARG A CD    1 
ATOM   1068 N NE    . ARG A 1 139 ? -32.392 57.983  -2.088  1.00 29.00 ? 139 ARG A NE    1 
ATOM   1069 C CZ    . ARG A 1 139 ? -32.216 58.903  -1.131  1.00 29.70 ? 139 ARG A CZ    1 
ATOM   1070 N NH1   . ARG A 1 139 ? -31.321 58.737  -0.177  1.00 27.85 ? 139 ARG A NH1   1 
ATOM   1071 N NH2   . ARG A 1 139 ? -32.972 60.004  -1.142  1.00 30.39 ? 139 ARG A NH2   1 
ATOM   1072 N N     . VAL A 1 140 ? -32.809 61.010  -7.093  1.00 31.54 ? 140 VAL A N     1 
ATOM   1073 C CA    . VAL A 1 140 ? -31.836 62.061  -7.320  1.00 31.07 ? 140 VAL A CA    1 
ATOM   1074 C C     . VAL A 1 140 ? -31.217 62.549  -6.013  1.00 30.74 ? 140 VAL A C     1 
ATOM   1075 O O     . VAL A 1 140 ? -31.908 63.084  -5.144  1.00 30.63 ? 140 VAL A O     1 
ATOM   1076 C CB    . VAL A 1 140 ? -32.436 63.303  -8.013  1.00 30.86 ? 140 VAL A CB    1 
ATOM   1077 C CG1   . VAL A 1 140 ? -31.340 64.302  -8.356  1.00 28.41 ? 140 VAL A CG1   1 
ATOM   1078 C CG2   . VAL A 1 140 ? -33.222 62.913  -9.256  1.00 30.95 ? 140 VAL A CG2   1 
ATOM   1079 N N     . VAL A 1 141 ? -29.906 62.325  -5.907  1.00 30.20 ? 141 VAL A N     1 
ATOM   1080 C CA    . VAL A 1 141 ? -29.176 62.781  -4.725  1.00 29.24 ? 141 VAL A CA    1 
ATOM   1081 C C     . VAL A 1 141 ? -28.059 63.741  -5.136  1.00 28.54 ? 141 VAL A C     1 
ATOM   1082 O O     . VAL A 1 141 ? -27.541 63.563  -6.240  1.00 28.59 ? 141 VAL A O     1 
ATOM   1083 C CB    . VAL A 1 141 ? -28.510 61.630  -3.959  1.00 29.15 ? 141 VAL A CB    1 
ATOM   1084 C CG1   . VAL A 1 141 ? -28.177 62.111  -2.561  1.00 27.61 ? 141 VAL A CG1   1 
ATOM   1085 C CG2   . VAL A 1 141 ? -29.351 60.363  -3.939  1.00 27.42 ? 141 VAL A CG2   1 
ATOM   1086 N N     . PHE A 1 142 ? -27.997 64.900  -4.493  1.00 27.78 ? 142 PHE A N     1 
ATOM   1087 C CA    . PHE A 1 142 ? -26.906 65.843  -4.727  1.00 26.78 ? 142 PHE A CA    1 
ATOM   1088 C C     . PHE A 1 142 ? -25.953 65.719  -3.536  1.00 26.51 ? 142 PHE A C     1 
ATOM   1089 O O     . PHE A 1 142 ? -26.459 65.696  -2.407  1.00 26.41 ? 142 PHE A O     1 
ATOM   1090 C CB    . PHE A 1 142 ? -27.399 67.273  -4.837  1.00 24.44 ? 142 PHE A CB    1 
ATOM   1091 C CG    . PHE A 1 142 ? -28.146 67.652  -6.078  1.00 24.13 ? 142 PHE A CG    1 
ATOM   1092 C CD1   . PHE A 1 142 ? -28.319 66.766  -7.127  1.00 23.07 ? 142 PHE A CD1   1 
ATOM   1093 C CD2   . PHE A 1 142 ? -28.677 68.936  -6.208  1.00 23.16 ? 142 PHE A CD2   1 
ATOM   1094 C CE1   . PHE A 1 142 ? -29.005 67.123  -8.264  1.00 22.06 ? 142 PHE A CE1   1 
ATOM   1095 C CE2   . PHE A 1 142 ? -29.372 69.286  -7.347  1.00 22.30 ? 142 PHE A CE2   1 
ATOM   1096 C CZ    . PHE A 1 142 ? -29.533 68.386  -8.374  1.00 21.13 ? 142 PHE A CZ    1 
ATOM   1097 N N     . THR A 1 143 ? -24.656 65.552  -3.772  1.00 26.08 ? 143 THR A N     1 
ATOM   1098 C CA    . THR A 1 143 ? -23.750 65.459  -2.633  1.00 25.65 ? 143 THR A CA    1 
ATOM   1099 C C     . THR A 1 143 ? -22.407 66.151  -2.816  1.00 25.63 ? 143 THR A C     1 
ATOM   1100 O O     . THR A 1 143 ? -21.927 66.331  -3.940  1.00 25.82 ? 143 THR A O     1 
ATOM   1101 C CB    . THR A 1 143 ? -23.484 63.985  -2.273  1.00 24.33 ? 143 THR A CB    1 
ATOM   1102 O OG1   . THR A 1 143 ? -22.857 63.953  -0.978  1.00 25.35 ? 143 THR A OG1   1 
ATOM   1103 C CG2   . THR A 1 143 ? -22.602 63.312  -3.302  1.00 21.95 ? 143 THR A CG2   1 
ATOM   1104 N N     . GLY A 1 144 ? -21.678 66.254  -1.706  1.00 25.34 ? 144 GLY A N     1 
ATOM   1105 C CA    . GLY A 1 144 ? -20.335 66.813  -1.746  1.00 25.61 ? 144 GLY A CA    1 
ATOM   1106 C C     . GLY A 1 144 ? -19.770 67.078  -0.350  1.00 25.84 ? 144 GLY A C     1 
ATOM   1107 O O     . GLY A 1 144 ? -20.540 67.261  0.594   1.00 25.25 ? 144 GLY A O     1 
ATOM   1108 N N     . HIS A 1 145 ? -18.476 67.397  -0.326  1.00 26.00 ? 145 HIS A N     1 
ATOM   1109 C CA    . HIS A 1 145 ? -17.705 67.660  0.870   1.00 26.19 ? 145 HIS A CA    1 
ATOM   1110 C C     . HIS A 1 145 ? -17.128 69.067  0.847   1.00 26.92 ? 145 HIS A C     1 
ATOM   1111 O O     . HIS A 1 145 ? -16.741 69.588  -0.194  1.00 27.32 ? 145 HIS A O     1 
ATOM   1112 C CB    . HIS A 1 145 ? -16.513 66.700  0.847   1.00 25.58 ? 145 HIS A CB    1 
ATOM   1113 C CG    . HIS A 1 145 ? -15.425 66.923  1.857   1.00 25.28 ? 145 HIS A CG    1 
ATOM   1114 N ND1   . HIS A 1 145 ? -14.163 67.397  1.521   1.00 24.27 ? 145 HIS A ND1   1 
ATOM   1115 C CD2   . HIS A 1 145 ? -15.402 66.715  3.198   1.00 23.78 ? 145 HIS A CD2   1 
ATOM   1116 C CE1   . HIS A 1 145 ? -13.430 67.453  2.612   1.00 24.03 ? 145 HIS A CE1   1 
ATOM   1117 N NE2   . HIS A 1 145 ? -14.156 67.054  3.650   1.00 22.63 ? 145 HIS A NE2   1 
ATOM   1118 N N     . SER A 1 146 ? -17.257 69.749  1.968   1.00 27.54 ? 146 SER A N     1 
ATOM   1119 C CA    . SER A 1 146 ? -16.650 71.078  2.137   1.00 27.84 ? 146 SER A CA    1 
ATOM   1120 C C     . SER A 1 146 ? -17.258 71.998  1.111   1.00 27.89 ? 146 SER A C     1 
ATOM   1121 O O     . SER A 1 146 ? -18.482 72.041  1.080   1.00 27.90 ? 146 SER A O     1 
ATOM   1122 C CB    . SER A 1 146 ? -15.135 70.974  2.147   1.00 28.41 ? 146 SER A CB    1 
ATOM   1123 O OG    . SER A 1 146 ? -14.455 72.228  2.078   1.00 30.57 ? 146 SER A OG    1 
ATOM   1124 N N     . LEU A 1 147 ? -16.568 72.596  0.164   1.00 28.16 ? 147 LEU A N     1 
ATOM   1125 C CA    . LEU A 1 147 ? -17.119 73.547  -0.787  1.00 27.97 ? 147 LEU A CA    1 
ATOM   1126 C C     . LEU A 1 147 ? -18.214 72.864  -1.590  1.00 28.33 ? 147 LEU A C     1 
ATOM   1127 O O     . LEU A 1 147 ? -19.273 73.408  -1.888  1.00 28.60 ? 147 LEU A O     1 
ATOM   1128 C CB    . LEU A 1 147 ? -16.026 74.086  -1.707  1.00 27.16 ? 147 LEU A CB    1 
ATOM   1129 C CG    . LEU A 1 147 ? -16.451 74.584  -3.083  1.00 27.62 ? 147 LEU A CG    1 
ATOM   1130 C CD1   . LEU A 1 147 ? -17.364 75.789  -2.964  1.00 28.30 ? 147 LEU A CD1   1 
ATOM   1131 C CD2   . LEU A 1 147 ? -15.221 74.885  -3.916  1.00 28.41 ? 147 LEU A CD2   1 
ATOM   1132 N N     . GLY A 1 148 ? -17.938 71.613  -1.942  1.00 28.42 ? 148 GLY A N     1 
ATOM   1133 C CA    . GLY A 1 148 ? -18.846 70.757  -2.676  1.00 28.61 ? 148 GLY A CA    1 
ATOM   1134 C C     . GLY A 1 148 ? -20.192 70.581  -1.985  1.00 28.32 ? 148 GLY A C     1 
ATOM   1135 O O     . GLY A 1 148 ? -21.223 70.434  -2.645  1.00 28.44 ? 148 GLY A O     1 
ATOM   1136 N N     . GLY A 1 149 ? -20.206 70.430  -0.669  1.00 27.77 ? 149 GLY A N     1 
ATOM   1137 C CA    . GLY A 1 149 ? -21.434 70.355  0.105   1.00 27.35 ? 149 GLY A CA    1 
ATOM   1138 C C     . GLY A 1 149 ? -22.186 71.682  0.052   1.00 27.12 ? 149 GLY A C     1 
ATOM   1139 O O     . GLY A 1 149 ? -23.404 71.634  -0.145  1.00 27.25 ? 149 GLY A O     1 
ATOM   1140 N N     . ALA A 1 150 ? -21.509 72.821  0.154   1.00 26.46 ? 150 ALA A N     1 
ATOM   1141 C CA    . ALA A 1 150 ? -22.136 74.128  -0.030  1.00 25.89 ? 150 ALA A CA    1 
ATOM   1142 C C     . ALA A 1 150 ? -22.805 74.204  -1.396  1.00 25.64 ? 150 ALA A C     1 
ATOM   1143 O O     . ALA A 1 150 ? -23.981 74.518  -1.524  1.00 25.47 ? 150 ALA A O     1 
ATOM   1144 C CB    . ALA A 1 150 ? -21.058 75.183  0.123   1.00 24.27 ? 150 ALA A CB    1 
ATOM   1145 N N     . LEU A 1 151 ? -22.064 73.855  -2.443  1.00 25.68 ? 151 LEU A N     1 
ATOM   1146 C CA    . LEU A 1 151 ? -22.592 73.863  -3.799  1.00 25.85 ? 151 LEU A CA    1 
ATOM   1147 C C     . LEU A 1 151 ? -23.831 72.986  -3.908  1.00 25.38 ? 151 LEU A C     1 
ATOM   1148 O O     . LEU A 1 151 ? -24.922 73.416  -4.258  1.00 25.33 ? 151 LEU A O     1 
ATOM   1149 C CB    . LEU A 1 151 ? -21.515 73.450  -4.806  1.00 25.81 ? 151 LEU A CB    1 
ATOM   1150 C CG    . LEU A 1 151 ? -20.488 74.522  -5.177  1.00 24.70 ? 151 LEU A CG    1 
ATOM   1151 C CD1   . LEU A 1 151 ? -19.766 74.084  -6.444  1.00 26.31 ? 151 LEU A CD1   1 
ATOM   1152 C CD2   . LEU A 1 151 ? -21.123 75.883  -5.380  1.00 22.61 ? 151 LEU A CD2   1 
ATOM   1153 N N     . ALA A 1 152 ? -23.684 71.737  -3.510  1.00 25.29 ? 152 ALA A N     1 
ATOM   1154 C CA    . ALA A 1 152 ? -24.792 70.802  -3.425  1.00 25.98 ? 152 ALA A CA    1 
ATOM   1155 C C     . ALA A 1 152 ? -25.999 71.359  -2.673  1.00 26.08 ? 152 ALA A C     1 
ATOM   1156 O O     . ALA A 1 152 ? -27.118 71.288  -3.181  1.00 26.20 ? 152 ALA A O     1 
ATOM   1157 C CB    . ALA A 1 152 ? -24.319 69.513  -2.771  1.00 25.36 ? 152 ALA A CB    1 
ATOM   1158 N N     . THR A 1 153 ? -25.849 71.903  -1.479  1.00 26.01 ? 153 THR A N     1 
ATOM   1159 C CA    . THR A 1 153 ? -26.910 72.551  -0.743  1.00 25.85 ? 153 THR A CA    1 
ATOM   1160 C C     . THR A 1 153 ? -27.608 73.662  -1.514  1.00 26.88 ? 153 THR A C     1 
ATOM   1161 O O     . THR A 1 153 ? -28.848 73.633  -1.596  1.00 27.83 ? 153 THR A O     1 
ATOM   1162 C CB    . THR A 1 153 ? -26.360 73.100  0.573   1.00 23.44 ? 153 THR A CB    1 
ATOM   1163 O OG1   . THR A 1 153 ? -25.780 72.088  1.387   1.00 20.48 ? 153 THR A OG1   1 
ATOM   1164 C CG2   . THR A 1 153 ? -27.517 73.701  1.360   1.00 23.73 ? 153 THR A CG2   1 
ATOM   1165 N N     . VAL A 1 154 ? -26.944 74.641  -2.129  1.00 27.23 ? 154 VAL A N     1 
ATOM   1166 C CA    . VAL A 1 154 ? -27.689 75.656  -2.880  1.00 27.24 ? 154 VAL A CA    1 
ATOM   1167 C C     . VAL A 1 154 ? -28.270 75.072  -4.159  1.00 27.48 ? 154 VAL A C     1 
ATOM   1168 O O     . VAL A 1 154 ? -29.461 75.243  -4.429  1.00 27.22 ? 154 VAL A O     1 
ATOM   1169 C CB    . VAL A 1 154 ? -26.995 76.997  -3.084  1.00 25.19 ? 154 VAL A CB    1 
ATOM   1170 C CG1   . VAL A 1 154 ? -25.893 77.225  -2.060  1.00 24.27 ? 154 VAL A CG1   1 
ATOM   1171 C CG2   . VAL A 1 154 ? -26.482 77.229  -4.488  1.00 24.10 ? 154 VAL A CG2   1 
ATOM   1172 N N     . ALA A 1 155 ? -27.529 74.278  -4.926  1.00 27.72 ? 155 ALA A N     1 
ATOM   1173 C CA    . ALA A 1 155 ? -28.094 73.686  -6.140  1.00 28.22 ? 155 ALA A CA    1 
ATOM   1174 C C     . ALA A 1 155 ? -29.374 72.941  -5.754  1.00 28.94 ? 155 ALA A C     1 
ATOM   1175 O O     . ALA A 1 155 ? -30.416 73.043  -6.403  1.00 28.49 ? 155 ALA A O     1 
ATOM   1176 C CB    . ALA A 1 155 ? -27.121 72.776  -6.853  1.00 25.98 ? 155 ALA A CB    1 
ATOM   1177 N N     . GLY A 1 156 ? -29.303 72.131  -4.702  1.00 29.59 ? 156 GLY A N     1 
ATOM   1178 C CA    . GLY A 1 156 ? -30.440 71.435  -4.129  1.00 30.36 ? 156 GLY A CA    1 
ATOM   1179 C C     . GLY A 1 156 ? -31.657 72.328  -3.942  1.00 30.91 ? 156 GLY A C     1 
ATOM   1180 O O     . GLY A 1 156 ? -32.685 72.142  -4.584  1.00 30.46 ? 156 GLY A O     1 
ATOM   1181 N N     . ALA A 1 157 ? -31.563 73.373  -3.129  1.00 31.55 ? 157 ALA A N     1 
ATOM   1182 C CA    . ALA A 1 157 ? -32.628 74.350  -2.941  1.00 31.58 ? 157 ALA A CA    1 
ATOM   1183 C C     . ALA A 1 157 ? -33.036 75.006  -4.249  1.00 31.72 ? 157 ALA A C     1 
ATOM   1184 O O     . ALA A 1 157 ? -34.222 75.217  -4.459  1.00 32.26 ? 157 ALA A O     1 
ATOM   1185 C CB    . ALA A 1 157 ? -32.148 75.420  -1.970  1.00 30.99 ? 157 ALA A CB    1 
ATOM   1186 N N     . ASP A 1 158 ? -32.121 75.410  -5.108  1.00 32.03 ? 158 ASP A N     1 
ATOM   1187 C CA    . ASP A 1 158 ? -32.463 76.022  -6.380  1.00 32.32 ? 158 ASP A CA    1 
ATOM   1188 C C     . ASP A 1 158 ? -33.353 75.113  -7.210  1.00 32.60 ? 158 ASP A C     1 
ATOM   1189 O O     . ASP A 1 158 ? -34.439 75.519  -7.628  1.00 33.47 ? 158 ASP A O     1 
ATOM   1190 C CB    . ASP A 1 158 ? -31.196 76.385  -7.151  1.00 32.41 ? 158 ASP A CB    1 
ATOM   1191 C CG    . ASP A 1 158 ? -31.457 77.394  -8.241  1.00 31.41 ? 158 ASP A CG    1 
ATOM   1192 O OD1   . ASP A 1 158 ? -30.836 77.277  -9.305  1.00 32.65 ? 158 ASP A OD1   1 
ATOM   1193 O OD2   . ASP A 1 158 ? -32.283 78.288  -8.019  1.00 32.74 ? 158 ASP A OD2   1 
ATOM   1194 N N     . LEU A 1 159 ? -32.990 73.864  -7.432  1.00 32.50 ? 159 LEU A N     1 
ATOM   1195 C CA    . LEU A 1 159 ? -33.743 72.967  -8.290  1.00 32.32 ? 159 LEU A CA    1 
ATOM   1196 C C     . LEU A 1 159 ? -34.883 72.187  -7.676  1.00 32.68 ? 159 LEU A C     1 
ATOM   1197 O O     . LEU A 1 159 ? -35.586 71.495  -8.428  1.00 32.84 ? 159 LEU A O     1 
ATOM   1198 C CB    . LEU A 1 159 ? -32.766 71.994  -8.963  1.00 29.25 ? 159 LEU A CB    1 
ATOM   1199 C CG    . LEU A 1 159 ? -32.000 72.390  -10.213 1.00 26.71 ? 159 LEU A CG    1 
ATOM   1200 C CD1   . LEU A 1 159 ? -31.720 73.875  -10.333 1.00 27.24 ? 159 LEU A CD1   1 
ATOM   1201 C CD2   . LEU A 1 159 ? -30.688 71.623  -10.246 1.00 24.60 ? 159 LEU A CD2   1 
ATOM   1202 N N     . ARG A 1 160 ? -35.095 72.179  -6.368  1.00 33.37 ? 160 ARG A N     1 
ATOM   1203 C CA    . ARG A 1 160 ? -36.196 71.380  -5.811  1.00 34.21 ? 160 ARG A CA    1 
ATOM   1204 C C     . ARG A 1 160 ? -37.493 71.963  -6.335  1.00 35.23 ? 160 ARG A C     1 
ATOM   1205 O O     . ARG A 1 160 ? -37.464 73.146  -6.688  1.00 35.87 ? 160 ARG A O     1 
ATOM   1206 C CB    . ARG A 1 160 ? -36.177 71.290  -4.275  1.00 30.49 ? 160 ARG A CB    1 
ATOM   1207 C CG    . ARG A 1 160 ? -34.995 70.428  -3.899  1.00 31.50 ? 160 ARG A CG    1 
ATOM   1208 C CD    . ARG A 1 160 ? -34.966 69.584  -2.675  1.00 28.24 ? 160 ARG A CD    1 
ATOM   1209 N NE    . ARG A 1 160 ? -34.627 70.301  -1.474  1.00 25.23 ? 160 ARG A NE    1 
ATOM   1210 C CZ    . ARG A 1 160 ? -33.963 69.842  -0.437  1.00 23.68 ? 160 ARG A CZ    1 
ATOM   1211 N NH1   . ARG A 1 160 ? -33.790 70.681  0.576   1.00 25.09 ? 160 ARG A NH1   1 
ATOM   1212 N NH2   . ARG A 1 160 ? -33.483 68.624  -0.411  1.00 22.78 ? 160 ARG A NH2   1 
ATOM   1213 N N     . GLY A 1 161 ? -38.523 71.179  -6.616  1.00 36.06 ? 161 GLY A N     1 
ATOM   1214 C CA    . GLY A 1 161 ? -39.761 71.750  -7.098  1.00 36.65 ? 161 GLY A CA    1 
ATOM   1215 C C     . GLY A 1 161 ? -40.090 71.517  -8.549  1.00 37.43 ? 161 GLY A C     1 
ATOM   1216 O O     . GLY A 1 161 ? -41.126 72.054  -8.956  1.00 38.12 ? 161 GLY A O     1 
ATOM   1217 N N     . ASN A 1 162 ? -39.349 70.787  -9.367  1.00 37.89 ? 162 ASN A N     1 
ATOM   1218 C CA    . ASN A 1 162 ? -39.703 70.547  -10.756 1.00 38.10 ? 162 ASN A CA    1 
ATOM   1219 C C     . ASN A 1 162 ? -40.185 69.111  -10.962 1.00 37.74 ? 162 ASN A C     1 
ATOM   1220 O O     . ASN A 1 162 ? -39.927 68.467  -11.984 1.00 37.69 ? 162 ASN A O     1 
ATOM   1221 C CB    . ASN A 1 162 ? -38.571 70.860  -11.722 1.00 44.22 ? 162 ASN A CB    1 
ATOM   1222 C CG    . ASN A 1 162 ? -38.082 72.288  -11.686 1.00 49.36 ? 162 ASN A CG    1 
ATOM   1223 O OD1   . ASN A 1 162 ? -38.588 73.146  -10.954 1.00 52.12 ? 162 ASN A OD1   1 
ATOM   1224 N ND2   . ASN A 1 162 ? -37.067 72.639  -12.483 1.00 51.72 ? 162 ASN A ND2   1 
ATOM   1225 N N     . GLY A 1 163 ? -40.878 68.577  -9.960  1.00 36.94 ? 163 GLY A N     1 
ATOM   1226 C CA    . GLY A 1 163 ? -41.525 67.288  -10.072 1.00 36.29 ? 163 GLY A CA    1 
ATOM   1227 C C     . GLY A 1 163 ? -40.628 66.095  -9.819  1.00 36.16 ? 163 GLY A C     1 
ATOM   1228 O O     . GLY A 1 163 ? -40.942 64.994  -10.283 1.00 36.12 ? 163 GLY A O     1 
ATOM   1229 N N     . TYR A 1 164 ? -39.475 66.300  -9.192  1.00 35.87 ? 164 TYR A N     1 
ATOM   1230 C CA    . TYR A 1 164 ? -38.580 65.222  -8.800  1.00 35.24 ? 164 TYR A CA    1 
ATOM   1231 C C     . TYR A 1 164 ? -37.903 65.627  -7.491  1.00 35.21 ? 164 TYR A C     1 
ATOM   1232 O O     . TYR A 1 164 ? -37.617 66.813  -7.337  1.00 35.48 ? 164 TYR A O     1 
ATOM   1233 C CB    . TYR A 1 164 ? -37.530 64.884  -9.830  1.00 35.23 ? 164 TYR A CB    1 
ATOM   1234 C CG    . TYR A 1 164 ? -36.645 65.979  -10.361 1.00 35.78 ? 164 TYR A CG    1 
ATOM   1235 C CD1   . TYR A 1 164 ? -36.839 66.485  -11.639 1.00 35.50 ? 164 TYR A CD1   1 
ATOM   1236 C CD2   . TYR A 1 164 ? -35.564 66.478  -9.641  1.00 36.25 ? 164 TYR A CD2   1 
ATOM   1237 C CE1   . TYR A 1 164 ? -36.042 67.484  -12.147 1.00 35.31 ? 164 TYR A CE1   1 
ATOM   1238 C CE2   . TYR A 1 164 ? -34.743 67.477  -10.137 1.00 35.66 ? 164 TYR A CE2   1 
ATOM   1239 C CZ    . TYR A 1 164 ? -34.996 67.971  -11.397 1.00 35.58 ? 164 TYR A CZ    1 
ATOM   1240 O OH    . TYR A 1 164 ? -34.213 68.954  -11.960 1.00 35.79 ? 164 TYR A OH    1 
ATOM   1241 N N     . ASP A 1 165 ? -37.998 64.803  -6.457  1.00 34.88 ? 165 ASP A N     1 
ATOM   1242 C CA    . ASP A 1 165 ? -37.346 65.140  -5.202  1.00 34.30 ? 165 ASP A CA    1 
ATOM   1243 C C     . ASP A 1 165 ? -35.834 65.161  -5.348  1.00 34.45 ? 165 ASP A C     1 
ATOM   1244 O O     . ASP A 1 165 ? -35.280 64.726  -6.366  1.00 35.29 ? 165 ASP A O     1 
ATOM   1245 C CB    . ASP A 1 165 ? -37.730 64.121  -4.149  1.00 35.38 ? 165 ASP A CB    1 
ATOM   1246 C CG    . ASP A 1 165 ? -39.167 64.287  -3.719  1.00 36.52 ? 165 ASP A CG    1 
ATOM   1247 O OD1   . ASP A 1 165 ? -39.489 63.683  -2.677  1.00 37.16 ? 165 ASP A OD1   1 
ATOM   1248 O OD2   . ASP A 1 165 ? -39.932 65.009  -4.388  1.00 39.23 ? 165 ASP A OD2   1 
ATOM   1249 N N     . ILE A 1 166 ? -35.194 65.943  -4.480  1.00 33.71 ? 166 ILE A N     1 
ATOM   1250 C CA    . ILE A 1 166 ? -33.748 66.085  -4.494  1.00 32.36 ? 166 ILE A CA    1 
ATOM   1251 C C     . ILE A 1 166 ? -33.261 66.005  -3.046  1.00 31.85 ? 166 ILE A C     1 
ATOM   1252 O O     . ILE A 1 166 ? -33.586 66.832  -2.208  1.00 31.36 ? 166 ILE A O     1 
ATOM   1253 C CB    . ILE A 1 166 ? -33.217 67.366  -5.141  1.00 31.00 ? 166 ILE A CB    1 
ATOM   1254 C CG1   . ILE A 1 166 ? -33.623 67.508  -6.602  1.00 31.93 ? 166 ILE A CG1   1 
ATOM   1255 C CG2   . ILE A 1 166 ? -31.692 67.334  -5.055  1.00 30.65 ? 166 ILE A CG2   1 
ATOM   1256 C CD1   . ILE A 1 166 ? -33.228 68.792  -7.294  1.00 32.84 ? 166 ILE A CD1   1 
ATOM   1257 N N     . ASP A 1 167 ? -32.548 64.924  -2.777  1.00 31.61 ? 167 ASP A N     1 
ATOM   1258 C CA    . ASP A 1 167 ? -31.942 64.705  -1.467  1.00 31.11 ? 167 ASP A CA    1 
ATOM   1259 C C     . ASP A 1 167 ? -30.498 65.194  -1.518  1.00 30.16 ? 167 ASP A C     1 
ATOM   1260 O O     . ASP A 1 167 ? -29.873 65.206  -2.585  1.00 30.44 ? 167 ASP A O     1 
ATOM   1261 C CB    . ASP A 1 167 ? -31.998 63.213  -1.155  1.00 34.03 ? 167 ASP A CB    1 
ATOM   1262 C CG    . ASP A 1 167 ? -33.283 62.879  -0.438  1.00 36.74 ? 167 ASP A CG    1 
ATOM   1263 O OD1   . ASP A 1 167 ? -34.338 63.470  -0.703  1.00 38.77 ? 167 ASP A OD1   1 
ATOM   1264 O OD2   . ASP A 1 167 ? -33.225 61.987  0.428   1.00 40.75 ? 167 ASP A OD2   1 
ATOM   1265 N N     . VAL A 1 168 ? -30.014 65.761  -0.425  1.00 28.64 ? 168 VAL A N     1 
ATOM   1266 C CA    . VAL A 1 168 ? -28.703 66.378  -0.369  1.00 26.95 ? 168 VAL A CA    1 
ATOM   1267 C C     . VAL A 1 168 ? -27.959 65.822  0.840   1.00 26.74 ? 168 VAL A C     1 
ATOM   1268 O O     . VAL A 1 168 ? -28.412 65.932  1.988   1.00 26.42 ? 168 VAL A O     1 
ATOM   1269 C CB    . VAL A 1 168 ? -28.810 67.912  -0.198  1.00 24.18 ? 168 VAL A CB    1 
ATOM   1270 C CG1   . VAL A 1 168 ? -27.446 68.494  0.088   1.00 22.13 ? 168 VAL A CG1   1 
ATOM   1271 C CG2   . VAL A 1 168 ? -29.461 68.598  -1.380  1.00 23.75 ? 168 VAL A CG2   1 
ATOM   1272 N N     . PHE A 1 169 ? -26.827 65.182  0.595   1.00 26.34 ? 169 PHE A N     1 
ATOM   1273 C CA    . PHE A 1 169 ? -26.050 64.753  1.759   1.00 26.42 ? 169 PHE A CA    1 
ATOM   1274 C C     . PHE A 1 169 ? -24.822 65.671  1.733   1.00 26.00 ? 169 PHE A C     1 
ATOM   1275 O O     . PHE A 1 169 ? -24.093 65.587  0.735   1.00 25.85 ? 169 PHE A O     1 
ATOM   1276 C CB    . PHE A 1 169 ? -25.634 63.291  1.680   1.00 28.32 ? 169 PHE A CB    1 
ATOM   1277 C CG    . PHE A 1 169 ? -26.788 62.334  1.726   1.00 28.10 ? 169 PHE A CG    1 
ATOM   1278 C CD1   . PHE A 1 169 ? -27.557 62.151  0.597   1.00 27.98 ? 169 PHE A CD1   1 
ATOM   1279 C CD2   . PHE A 1 169 ? -27.085 61.637  2.887   1.00 28.61 ? 169 PHE A CD2   1 
ATOM   1280 C CE1   . PHE A 1 169 ? -28.654 61.311  0.625   1.00 28.37 ? 169 PHE A CE1   1 
ATOM   1281 C CE2   . PHE A 1 169 ? -28.143 60.755  2.919   1.00 28.57 ? 169 PHE A CE2   1 
ATOM   1282 C CZ    . PHE A 1 169 ? -28.947 60.648  1.797   1.00 29.63 ? 169 PHE A CZ    1 
ATOM   1283 N N     . SER A 1 170 ? -24.554 66.472  2.745   1.00 25.60 ? 170 SER A N     1 
ATOM   1284 C CA    . SER A 1 170 ? -23.339 67.281  2.718   1.00 26.01 ? 170 SER A CA    1 
ATOM   1285 C C     . SER A 1 170 ? -22.385 66.925  3.846   1.00 26.06 ? 170 SER A C     1 
ATOM   1286 O O     . SER A 1 170 ? -22.810 66.592  4.941   1.00 25.76 ? 170 SER A O     1 
ATOM   1287 C CB    . SER A 1 170 ? -23.659 68.769  2.704   1.00 25.81 ? 170 SER A CB    1 
ATOM   1288 O OG    . SER A 1 170 ? -23.859 69.290  4.002   1.00 23.42 ? 170 SER A OG    1 
ATOM   1289 N N     . TYR A 1 171 ? -21.095 66.868  3.552   1.00 26.58 ? 171 TYR A N     1 
ATOM   1290 C CA    . TYR A 1 171 ? -20.051 66.527  4.497   1.00 27.43 ? 171 TYR A CA    1 
ATOM   1291 C C     . TYR A 1 171 ? -19.058 67.665  4.747   1.00 28.01 ? 171 TYR A C     1 
ATOM   1292 O O     . TYR A 1 171 ? -18.354 68.118  3.842   1.00 27.73 ? 171 TYR A O     1 
ATOM   1293 C CB    . TYR A 1 171 ? -19.223 65.340  3.959   1.00 26.97 ? 171 TYR A CB    1 
ATOM   1294 C CG    . TYR A 1 171 ? -20.131 64.168  3.670   1.00 26.14 ? 171 TYR A CG    1 
ATOM   1295 C CD1   . TYR A 1 171 ? -20.717 64.036  2.422   1.00 26.09 ? 171 TYR A CD1   1 
ATOM   1296 C CD2   . TYR A 1 171 ? -20.478 63.283  4.678   1.00 25.74 ? 171 TYR A CD2   1 
ATOM   1297 C CE1   . TYR A 1 171 ? -21.670 63.061  2.176   1.00 26.32 ? 171 TYR A CE1   1 
ATOM   1298 C CE2   . TYR A 1 171 ? -21.332 62.232  4.426   1.00 25.48 ? 171 TYR A CE2   1 
ATOM   1299 C CZ    . TYR A 1 171 ? -21.928 62.139  3.186   1.00 26.26 ? 171 TYR A CZ    1 
ATOM   1300 O OH    . TYR A 1 171 ? -22.789 61.078  2.997   1.00 25.86 ? 171 TYR A OH    1 
ATOM   1301 N N     . GLY A 1 172 ? -18.983 68.078  6.007   1.00 28.32 ? 172 GLY A N     1 
ATOM   1302 C CA    . GLY A 1 172 ? -18.055 69.110  6.438   1.00 28.70 ? 172 GLY A CA    1 
ATOM   1303 C C     . GLY A 1 172 ? -18.262 70.389  5.646   1.00 29.15 ? 172 GLY A C     1 
ATOM   1304 O O     . GLY A 1 172 ? -17.270 71.048  5.319   1.00 29.68 ? 172 GLY A O     1 
ATOM   1305 N N     . ALA A 1 173 ? -19.516 70.756  5.398   1.00 29.24 ? 173 ALA A N     1 
ATOM   1306 C CA    . ALA A 1 173 ? -19.792 71.956  4.612   1.00 28.71 ? 173 ALA A CA    1 
ATOM   1307 C C     . ALA A 1 173 ? -19.938 73.161  5.533   1.00 27.62 ? 173 ALA A C     1 
ATOM   1308 O O     . ALA A 1 173 ? -20.356 72.978  6.668   1.00 27.55 ? 173 ALA A O     1 
ATOM   1309 C CB    . ALA A 1 173 ? -21.020 71.751  3.739   1.00 29.75 ? 173 ALA A CB    1 
ATOM   1310 N N     . PRO A 1 174 ? -19.508 74.306  5.041   1.00 26.87 ? 174 PRO A N     1 
ATOM   1311 C CA    . PRO A 1 174 ? -19.585 75.559  5.776   1.00 27.00 ? 174 PRO A CA    1 
ATOM   1312 C C     . PRO A 1 174 ? -20.989 76.135  5.810   1.00 26.73 ? 174 PRO A C     1 
ATOM   1313 O O     . PRO A 1 174 ? -21.867 75.530  5.195   1.00 27.17 ? 174 PRO A O     1 
ATOM   1314 C CB    . PRO A 1 174 ? -18.625 76.433  4.948   1.00 26.79 ? 174 PRO A CB    1 
ATOM   1315 C CG    . PRO A 1 174 ? -18.939 76.008  3.549   1.00 26.71 ? 174 PRO A CG    1 
ATOM   1316 C CD    . PRO A 1 174 ? -19.028 74.508  3.653   1.00 26.64 ? 174 PRO A CD    1 
ATOM   1317 N N     . ARG A 1 175 ? -21.264 77.211  6.535   1.00 26.50 ? 175 ARG A N     1 
ATOM   1318 C CA    . ARG A 1 175 ? -22.589 77.816  6.511   1.00 26.34 ? 175 ARG A CA    1 
ATOM   1319 C C     . ARG A 1 175 ? -22.725 78.422  5.115   1.00 27.05 ? 175 ARG A C     1 
ATOM   1320 O O     . ARG A 1 175 ? -21.702 78.915  4.630   1.00 27.04 ? 175 ARG A O     1 
ATOM   1321 C CB    . ARG A 1 175 ? -22.742 78.909  7.552   1.00 25.49 ? 175 ARG A CB    1 
ATOM   1322 C CG    . ARG A 1 175 ? -22.539 78.399  8.963   1.00 25.96 ? 175 ARG A CG    1 
ATOM   1323 C CD    . ARG A 1 175 ? -22.688 79.514  9.977   1.00 26.59 ? 175 ARG A CD    1 
ATOM   1324 N NE    . ARG A 1 175 ? -22.731 78.972  11.342  1.00 27.01 ? 175 ARG A NE    1 
ATOM   1325 C CZ    . ARG A 1 175 ? -21.677 78.966  12.146  1.00 27.16 ? 175 ARG A CZ    1 
ATOM   1326 N NH1   . ARG A 1 175 ? -21.760 78.460  13.367  1.00 26.56 ? 175 ARG A NH1   1 
ATOM   1327 N NH2   . ARG A 1 175 ? -20.532 79.474  11.704  1.00 28.17 ? 175 ARG A NH2   1 
ATOM   1328 N N     . VAL A 1 176 ? -23.947 78.495  4.614   1.00 27.44 ? 176 VAL A N     1 
ATOM   1329 C CA    . VAL A 1 176 ? -24.128 78.944  3.241   1.00 28.52 ? 176 VAL A CA    1 
ATOM   1330 C C     . VAL A 1 176 ? -24.976 80.183  3.132   1.00 29.09 ? 176 VAL A C     1 
ATOM   1331 O O     . VAL A 1 176 ? -25.023 80.805  2.063   1.00 29.41 ? 176 VAL A O     1 
ATOM   1332 C CB    . VAL A 1 176 ? -24.646 77.742  2.442   1.00 30.73 ? 176 VAL A CB    1 
ATOM   1333 C CG1   . VAL A 1 176 ? -26.063 77.381  2.861   1.00 32.15 ? 176 VAL A CG1   1 
ATOM   1334 C CG2   . VAL A 1 176 ? -24.602 77.951  0.939   1.00 33.75 ? 176 VAL A CG2   1 
ATOM   1335 N N     . GLY A 1 177 ? -25.469 80.750  4.232   1.00 29.93 ? 177 GLY A N     1 
ATOM   1336 C CA    . GLY A 1 177 ? -26.278 81.961  4.112   1.00 31.24 ? 177 GLY A CA    1 
ATOM   1337 C C     . GLY A 1 177 ? -26.843 82.469  5.422   1.00 32.42 ? 177 GLY A C     1 
ATOM   1338 O O     . GLY A 1 177 ? -26.552 81.965  6.508   1.00 32.46 ? 177 GLY A O     1 
ATOM   1339 N N     . ASN A 1 178 ? -27.652 83.528  5.327   1.00 33.45 ? 178 ASN A N     1 
ATOM   1340 C CA    . ASN A 1 178 ? -28.254 84.121  6.519   1.00 34.48 ? 178 ASN A CA    1 
ATOM   1341 C C     . ASN A 1 178 ? -29.208 83.140  7.196   1.00 35.03 ? 178 ASN A C     1 
ATOM   1342 O O     . ASN A 1 178 ? -29.735 82.217  6.569   1.00 35.52 ? 178 ASN A O     1 
ATOM   1343 C CB    . ASN A 1 178 ? -29.028 85.388  6.169   1.00 35.35 ? 178 ASN A CB    1 
ATOM   1344 C CG    . ASN A 1 178 ? -30.052 85.223  5.078   1.00 36.99 ? 178 ASN A CG    1 
ATOM   1345 O OD1   . ASN A 1 178 ? -30.671 86.207  4.649   1.00 38.67 ? 178 ASN A OD1   1 
ATOM   1346 N ND2   . ASN A 1 178 ? -30.260 84.013  4.573   1.00 37.94 ? 178 ASN A ND2   1 
ATOM   1347 N N     . ARG A 1 179 ? -29.775 83.584  8.312   1.00 35.46 ? 179 ARG A N     1 
ATOM   1348 C CA    . ARG A 1 179 ? -30.853 82.874  8.984   1.00 35.53 ? 179 ARG A CA    1 
ATOM   1349 C C     . ARG A 1 179 ? -32.072 82.687  8.092   1.00 35.54 ? 179 ARG A C     1 
ATOM   1350 O O     . ARG A 1 179 ? -32.684 81.615  8.143   1.00 35.53 ? 179 ARG A O     1 
ATOM   1351 C CB    . ARG A 1 179 ? -31.247 83.649  10.238  1.00 37.78 ? 179 ARG A CB    1 
ATOM   1352 C CG    . ARG A 1 179 ? -32.411 83.037  10.979  1.00 41.90 ? 179 ARG A CG    1 
ATOM   1353 C CD    . ARG A 1 179 ? -32.194 82.947  12.488  1.00 44.42 ? 179 ARG A CD    1 
ATOM   1354 N NE    . ARG A 1 179 ? -33.389 82.348  13.082  1.00 48.24 ? 179 ARG A NE    1 
ATOM   1355 C CZ    . ARG A 1 179 ? -33.472 81.556  14.138  1.00 49.32 ? 179 ARG A CZ    1 
ATOM   1356 N NH1   . ARG A 1 179 ? -32.406 81.189  14.836  1.00 49.96 ? 179 ARG A NH1   1 
ATOM   1357 N NH2   . ARG A 1 179 ? -34.656 81.094  14.525  1.00 50.40 ? 179 ARG A NH2   1 
ATOM   1358 N N     . ALA A 1 180 ? -32.499 83.680  7.308   1.00 35.36 ? 180 ALA A N     1 
ATOM   1359 C CA    . ALA A 1 180 ? -33.598 83.457  6.376   1.00 34.63 ? 180 ALA A CA    1 
ATOM   1360 C C     . ALA A 1 180 ? -33.277 82.220  5.542   1.00 34.56 ? 180 ALA A C     1 
ATOM   1361 O O     . ALA A 1 180 ? -34.088 81.284  5.572   1.00 34.96 ? 180 ALA A O     1 
ATOM   1362 C CB    . ALA A 1 180 ? -33.892 84.635  5.484   1.00 33.61 ? 180 ALA A CB    1 
ATOM   1363 N N     . PHE A 1 181 ? -32.093 82.112  4.935   1.00 34.05 ? 181 PHE A N     1 
ATOM   1364 C CA    . PHE A 1 181 ? -31.780 80.896  4.183   1.00 33.52 ? 181 PHE A CA    1 
ATOM   1365 C C     . PHE A 1 181 ? -31.779 79.664  5.095   1.00 33.26 ? 181 PHE A C     1 
ATOM   1366 O O     . PHE A 1 181 ? -32.403 78.644  4.809   1.00 32.28 ? 181 PHE A O     1 
ATOM   1367 C CB    . PHE A 1 181 ? -30.448 80.964  3.445   1.00 31.38 ? 181 PHE A CB    1 
ATOM   1368 C CG    . PHE A 1 181 ? -30.349 80.169  2.181   1.00 29.65 ? 181 PHE A CG    1 
ATOM   1369 C CD1   . PHE A 1 181 ? -31.471 79.709  1.530   1.00 29.63 ? 181 PHE A CD1   1 
ATOM   1370 C CD2   . PHE A 1 181 ? -29.117 79.902  1.596   1.00 29.71 ? 181 PHE A CD2   1 
ATOM   1371 C CE1   . PHE A 1 181 ? -31.381 79.001  0.345   1.00 28.82 ? 181 PHE A CE1   1 
ATOM   1372 C CE2   . PHE A 1 181 ? -29.005 79.209  0.410   1.00 28.00 ? 181 PHE A CE2   1 
ATOM   1373 C CZ    . PHE A 1 181 ? -30.149 78.748  -0.215  1.00 28.05 ? 181 PHE A CZ    1 
ATOM   1374 N N     . ALA A 1 182 ? -31.164 79.820  6.266   1.00 33.20 ? 182 ALA A N     1 
ATOM   1375 C CA    . ALA A 1 182 ? -31.085 78.739  7.230   1.00 34.02 ? 182 ALA A CA    1 
ATOM   1376 C C     . ALA A 1 182 ? -32.453 78.152  7.554   1.00 34.82 ? 182 ALA A C     1 
ATOM   1377 O O     . ALA A 1 182 ? -32.607 76.936  7.661   1.00 34.97 ? 182 ALA A O     1 
ATOM   1378 C CB    . ALA A 1 182 ? -30.367 79.186  8.488   1.00 33.48 ? 182 ALA A CB    1 
ATOM   1379 N N     . GLU A 1 183 ? -33.436 78.986  7.873   1.00 35.47 ? 183 GLU A N     1 
ATOM   1380 C CA    . GLU A 1 183 ? -34.809 78.585  8.110   1.00 35.29 ? 183 GLU A CA    1 
ATOM   1381 C C     . GLU A 1 183 ? -35.419 77.960  6.863   1.00 34.80 ? 183 GLU A C     1 
ATOM   1382 O O     . GLU A 1 183 ? -36.067 76.919  6.919   1.00 34.83 ? 183 GLU A O     1 
ATOM   1383 C CB    . GLU A 1 183 ? -35.612 79.833  8.476   1.00 38.55 ? 183 GLU A CB    1 
ATOM   1384 C CG    . GLU A 1 183 ? -36.109 79.815  9.908   1.00 43.39 ? 183 GLU A CG    1 
ATOM   1385 C CD    . GLU A 1 183 ? -35.861 81.139  10.606  1.00 46.63 ? 183 GLU A CD    1 
ATOM   1386 O OE1   . GLU A 1 183 ? -36.171 82.201  10.011  1.00 49.09 ? 183 GLU A OE1   1 
ATOM   1387 O OE2   . GLU A 1 183 ? -35.360 81.090  11.751  1.00 47.02 ? 183 GLU A OE2   1 
ATOM   1388 N N     . PHE A 1 184 ? -35.231 78.597  5.713   1.00 34.35 ? 184 PHE A N     1 
ATOM   1389 C CA    . PHE A 1 184 ? -35.740 78.038  4.465   1.00 33.81 ? 184 PHE A CA    1 
ATOM   1390 C C     . PHE A 1 184 ? -35.262 76.615  4.220   1.00 33.42 ? 184 PHE A C     1 
ATOM   1391 O O     . PHE A 1 184 ? -36.086 75.743  3.993   1.00 32.90 ? 184 PHE A O     1 
ATOM   1392 C CB    . PHE A 1 184 ? -35.330 78.956  3.306   1.00 33.45 ? 184 PHE A CB    1 
ATOM   1393 C CG    . PHE A 1 184 ? -35.825 78.393  2.005   1.00 33.32 ? 184 PHE A CG    1 
ATOM   1394 C CD1   . PHE A 1 184 ? -34.945 77.764  1.126   1.00 33.60 ? 184 PHE A CD1   1 
ATOM   1395 C CD2   . PHE A 1 184 ? -37.160 78.510  1.677   1.00 32.53 ? 184 PHE A CD2   1 
ATOM   1396 C CE1   . PHE A 1 184 ? -35.414 77.255  -0.077  1.00 33.07 ? 184 PHE A CE1   1 
ATOM   1397 C CE2   . PHE A 1 184 ? -37.619 77.998  0.469   1.00 32.01 ? 184 PHE A CE2   1 
ATOM   1398 C CZ    . PHE A 1 184 ? -36.751 77.377  -0.402  1.00 32.12 ? 184 PHE A CZ    1 
ATOM   1399 N N     . LEU A 1 185 ? -33.960 76.345  4.274   1.00 33.35 ? 185 LEU A N     1 
ATOM   1400 C CA    . LEU A 1 185 ? -33.361 75.049  4.034   1.00 32.86 ? 185 LEU A CA    1 
ATOM   1401 C C     . LEU A 1 185 ? -33.847 74.014  5.042   1.00 33.06 ? 185 LEU A C     1 
ATOM   1402 O O     . LEU A 1 185 ? -33.847 72.815  4.766   1.00 33.49 ? 185 LEU A O     1 
ATOM   1403 C CB    . LEU A 1 185 ? -31.826 75.063  4.104   1.00 30.01 ? 185 LEU A CB    1 
ATOM   1404 C CG    . LEU A 1 185 ? -31.104 75.746  2.947   1.00 29.38 ? 185 LEU A CG    1 
ATOM   1405 C CD1   . LEU A 1 185 ? -29.629 75.897  3.243   1.00 28.87 ? 185 LEU A CD1   1 
ATOM   1406 C CD2   . LEU A 1 185 ? -31.358 74.992  1.660   1.00 29.47 ? 185 LEU A CD2   1 
ATOM   1407 N N     . THR A 1 186 ? -34.107 74.434  6.264   1.00 32.73 ? 186 THR A N     1 
ATOM   1408 C CA    . THR A 1 186 ? -34.625 73.594  7.316   1.00 33.03 ? 186 THR A CA    1 
ATOM   1409 C C     . THR A 1 186 ? -36.017 73.040  7.047   1.00 33.61 ? 186 THR A C     1 
ATOM   1410 O O     . THR A 1 186 ? -36.396 71.964  7.528   1.00 34.08 ? 186 THR A O     1 
ATOM   1411 C CB    . THR A 1 186 ? -34.718 74.430  8.614   1.00 32.18 ? 186 THR A CB    1 
ATOM   1412 O OG1   . THR A 1 186 ? -33.414 74.905  8.966   1.00 34.26 ? 186 THR A OG1   1 
ATOM   1413 C CG2   . THR A 1 186 ? -35.226 73.615  9.780   1.00 31.12 ? 186 THR A CG2   1 
ATOM   1414 N N     . VAL A 1 187 ? -36.811 73.727  6.258   1.00 33.83 ? 187 VAL A N     1 
ATOM   1415 C CA    . VAL A 1 187 ? -38.230 73.483  6.061   1.00 33.57 ? 187 VAL A CA    1 
ATOM   1416 C C     . VAL A 1 187 ? -38.569 73.140  4.630   1.00 33.84 ? 187 VAL A C     1 
ATOM   1417 O O     . VAL A 1 187 ? -39.641 72.589  4.378   1.00 34.18 ? 187 VAL A O     1 
ATOM   1418 C CB    . VAL A 1 187 ? -38.881 74.817  6.506   1.00 32.02 ? 187 VAL A CB    1 
ATOM   1419 C CG1   . VAL A 1 187 ? -40.041 75.295  5.676   1.00 33.22 ? 187 VAL A CG1   1 
ATOM   1420 C CG2   . VAL A 1 187 ? -39.227 74.685  7.974   1.00 31.76 ? 187 VAL A CG2   1 
ATOM   1421 N N     . GLN A 1 188 ? -37.729 73.543  3.681   1.00 34.10 ? 188 GLN A N     1 
ATOM   1422 C CA    . GLN A 1 188 ? -38.059 73.313  2.281   1.00 34.29 ? 188 GLN A CA    1 
ATOM   1423 C C     . GLN A 1 188 ? -38.610 71.890  2.170   1.00 34.93 ? 188 GLN A C     1 
ATOM   1424 O O     . GLN A 1 188 ? -38.187 70.957  2.841   1.00 34.99 ? 188 GLN A O     1 
ATOM   1425 C CB    . GLN A 1 188 ? -36.872 73.517  1.349   1.00 31.50 ? 188 GLN A CB    1 
ATOM   1426 C CG    . GLN A 1 188 ? -37.218 73.597  -0.114  1.00 29.37 ? 188 GLN A CG    1 
ATOM   1427 C CD    . GLN A 1 188 ? -35.990 73.762  -0.974  1.00 29.38 ? 188 GLN A CD    1 
ATOM   1428 O OE1   . GLN A 1 188 ? -34.943 73.235  -0.582  1.00 30.86 ? 188 GLN A OE1   1 
ATOM   1429 N NE2   . GLN A 1 188 ? -36.131 74.462  -2.088  1.00 27.75 ? 188 GLN A NE2   1 
ATOM   1430 N N     . THR A 1 189 ? -39.427 71.752  1.154   1.00 35.67 ? 189 THR A N     1 
ATOM   1431 C CA    . THR A 1 189 ? -39.963 70.430  0.811   1.00 36.48 ? 189 THR A CA    1 
ATOM   1432 C C     . THR A 1 189 ? -39.521 69.970  -0.556  1.00 35.86 ? 189 THR A C     1 
ATOM   1433 O O     . THR A 1 189 ? -39.258 70.821  -1.414  1.00 36.62 ? 189 THR A O     1 
ATOM   1434 C CB    . THR A 1 189 ? -41.491 70.571  1.008   1.00 39.42 ? 189 THR A CB    1 
ATOM   1435 O OG1   . THR A 1 189 ? -41.672 69.880  2.265   1.00 41.50 ? 189 THR A OG1   1 
ATOM   1436 C CG2   . THR A 1 189 ? -42.367 70.160  -0.134  1.00 38.86 ? 189 THR A CG2   1 
ATOM   1437 N N     . GLY A 1 190 ? -39.587 68.664  -0.798  1.00 35.02 ? 190 GLY A N     1 
ATOM   1438 C CA    . GLY A 1 190 ? -39.203 68.191  -2.138  1.00 34.12 ? 190 GLY A CA    1 
ATOM   1439 C C     . GLY A 1 190 ? -37.936 67.354  -2.081  1.00 33.61 ? 190 GLY A C     1 
ATOM   1440 O O     . GLY A 1 190 ? -37.327 67.125  -3.115  1.00 33.53 ? 190 GLY A O     1 
ATOM   1441 N N     . GLY A 1 191 ? -37.570 66.910  -0.889  1.00 32.97 ? 191 GLY A N     1 
ATOM   1442 C CA    . GLY A 1 191 ? -36.412 66.079  -0.651  1.00 32.50 ? 191 GLY A CA    1 
ATOM   1443 C C     . GLY A 1 191 ? -35.825 66.378  0.724   1.00 32.28 ? 191 GLY A C     1 
ATOM   1444 O O     . GLY A 1 191 ? -36.301 67.344  1.317   1.00 32.21 ? 191 GLY A O     1 
ATOM   1445 N N     . THR A 1 192 ? -34.796 65.678  1.191   1.00 32.02 ? 192 THR A N     1 
ATOM   1446 C CA    . THR A 1 192 ? -34.198 66.056  2.468   1.00 31.93 ? 192 THR A CA    1 
ATOM   1447 C C     . THR A 1 192 ? -32.764 66.541  2.352   1.00 31.66 ? 192 THR A C     1 
ATOM   1448 O O     . THR A 1 192 ? -31.971 66.081  1.540   1.00 31.80 ? 192 THR A O     1 
ATOM   1449 C CB    . THR A 1 192 ? -34.296 64.811  3.365   1.00 33.21 ? 192 THR A CB    1 
ATOM   1450 O OG1   . THR A 1 192 ? -35.689 64.464  3.367   1.00 34.67 ? 192 THR A OG1   1 
ATOM   1451 C CG2   . THR A 1 192 ? -33.816 65.038  4.775   1.00 32.94 ? 192 THR A CG2   1 
ATOM   1452 N N     . LEU A 1 193 ? -32.366 67.385  3.294   1.00 31.35 ? 193 LEU A N     1 
ATOM   1453 C CA    . LEU A 1 193 ? -30.992 67.834  3.468   1.00 30.41 ? 193 LEU A CA    1 
ATOM   1454 C C     . LEU A 1 193 ? -30.359 67.094  4.649   1.00 29.55 ? 193 LEU A C     1 
ATOM   1455 O O     . LEU A 1 193 ? -30.837 67.151  5.783   1.00 28.83 ? 193 LEU A O     1 
ATOM   1456 C CB    . LEU A 1 193 ? -30.951 69.333  3.771   1.00 30.19 ? 193 LEU A CB    1 
ATOM   1457 C CG    . LEU A 1 193 ? -29.690 70.165  3.633   1.00 28.53 ? 193 LEU A CG    1 
ATOM   1458 C CD1   . LEU A 1 193 ? -29.452 70.948  4.914   1.00 28.77 ? 193 LEU A CD1   1 
ATOM   1459 C CD2   . LEU A 1 193 ? -28.471 69.382  3.204   1.00 25.94 ? 193 LEU A CD2   1 
ATOM   1460 N N     . TYR A 1 194 ? -29.258 66.400  4.380   1.00 29.06 ? 194 TYR A N     1 
ATOM   1461 C CA    . TYR A 1 194 ? -28.510 65.719  5.438   1.00 28.54 ? 194 TYR A CA    1 
ATOM   1462 C C     . TYR A 1 194 ? -27.189 66.436  5.701   1.00 28.00 ? 194 TYR A C     1 
ATOM   1463 O O     . TYR A 1 194 ? -26.299 66.335  4.870   1.00 28.09 ? 194 TYR A O     1 
ATOM   1464 C CB    . TYR A 1 194 ? -28.237 64.256  5.085   1.00 28.44 ? 194 TYR A CB    1 
ATOM   1465 C CG    . TYR A 1 194 ? -29.515 63.451  4.962   1.00 27.94 ? 194 TYR A CG    1 
ATOM   1466 C CD1   . TYR A 1 194 ? -30.173 62.961  6.074   1.00 27.84 ? 194 TYR A CD1   1 
ATOM   1467 C CD2   . TYR A 1 194 ? -30.080 63.247  3.713   1.00 28.34 ? 194 TYR A CD2   1 
ATOM   1468 C CE1   . TYR A 1 194 ? -31.358 62.263  5.936   1.00 28.87 ? 194 TYR A CE1   1 
ATOM   1469 C CE2   . TYR A 1 194 ? -31.265 62.571  3.550   1.00 28.95 ? 194 TYR A CE2   1 
ATOM   1470 C CZ    . TYR A 1 194 ? -31.908 62.094  4.679   1.00 29.73 ? 194 TYR A CZ    1 
ATOM   1471 O OH    . TYR A 1 194 ? -33.097 61.413  4.544   1.00 30.34 ? 194 TYR A OH    1 
ATOM   1472 N N     . ARG A 1 195 ? -27.100 67.277  6.707   1.00 27.75 ? 195 ARG A N     1 
ATOM   1473 C CA    . ARG A 1 195 ? -25.930 68.064  7.058   1.00 27.46 ? 195 ARG A CA    1 
ATOM   1474 C C     . ARG A 1 195 ? -25.071 67.320  8.084   1.00 27.48 ? 195 ARG A C     1 
ATOM   1475 O O     . ARG A 1 195 ? -25.358 67.320  9.280   1.00 26.79 ? 195 ARG A O     1 
ATOM   1476 C CB    . ARG A 1 195 ? -26.372 69.387  7.670   1.00 25.69 ? 195 ARG A CB    1 
ATOM   1477 C CG    . ARG A 1 195 ? -25.714 70.661  7.177   1.00 23.88 ? 195 ARG A CG    1 
ATOM   1478 C CD    . ARG A 1 195 ? -26.158 71.800  8.100   1.00 22.10 ? 195 ARG A CD    1 
ATOM   1479 N NE    . ARG A 1 195 ? -25.246 71.873  9.208   1.00 21.96 ? 195 ARG A NE    1 
ATOM   1480 C CZ    . ARG A 1 195 ? -25.473 72.117  10.476  1.00 24.52 ? 195 ARG A CZ    1 
ATOM   1481 N NH1   . ARG A 1 195 ? -24.423 72.136  11.316  1.00 29.44 ? 195 ARG A NH1   1 
ATOM   1482 N NH2   . ARG A 1 195 ? -26.696 72.328  10.908  1.00 22.68 ? 195 ARG A NH2   1 
ATOM   1483 N N     . ILE A 1 196 ? -24.023 66.663  7.601   1.00 27.69 ? 196 ILE A N     1 
ATOM   1484 C CA    . ILE A 1 196 ? -23.104 65.876  8.413   1.00 27.68 ? 196 ILE A CA    1 
ATOM   1485 C C     . ILE A 1 196 ? -21.808 66.621  8.707   1.00 28.21 ? 196 ILE A C     1 
ATOM   1486 O O     . ILE A 1 196 ? -21.204 67.294  7.865   1.00 28.01 ? 196 ILE A O     1 
ATOM   1487 C CB    . ILE A 1 196 ? -22.799 64.573  7.656   1.00 26.62 ? 196 ILE A CB    1 
ATOM   1488 C CG1   . ILE A 1 196 ? -24.126 63.852  7.416   1.00 26.79 ? 196 ILE A CG1   1 
ATOM   1489 C CG2   . ILE A 1 196 ? -21.831 63.624  8.325   1.00 26.48 ? 196 ILE A CG2   1 
ATOM   1490 C CD1   . ILE A 1 196 ? -24.137 62.966  6.195   1.00 27.11 ? 196 ILE A CD1   1 
ATOM   1491 N N     . THR A 1 197 ? -21.544 66.700  10.009  1.00 28.50 ? 197 THR A N     1 
ATOM   1492 C CA    . THR A 1 197 ? -20.367 67.390  10.531  1.00 29.13 ? 197 THR A CA    1 
ATOM   1493 C C     . THR A 1 197 ? -19.573 66.391  11.369  1.00 29.75 ? 197 THR A C     1 
ATOM   1494 O O     . THR A 1 197 ? -20.112 65.357  11.775  1.00 30.45 ? 197 THR A O     1 
ATOM   1495 C CB    . THR A 1 197 ? -20.776 68.547  11.458  1.00 27.82 ? 197 THR A CB    1 
ATOM   1496 O OG1   . THR A 1 197 ? -21.462 67.968  12.585  1.00 26.40 ? 197 THR A OG1   1 
ATOM   1497 C CG2   . THR A 1 197 ? -21.664 69.537  10.719  1.00 26.50 ? 197 THR A CG2   1 
ATOM   1498 N N     . HIS A 1 198 ? -18.294 66.648  11.553  1.00 29.91 ? 198 HIS A N     1 
ATOM   1499 C CA    . HIS A 1 198 ? -17.446 65.725  12.312  1.00 29.57 ? 198 HIS A CA    1 
ATOM   1500 C C     . HIS A 1 198 ? -16.721 66.457  13.421  1.00 29.41 ? 198 HIS A C     1 
ATOM   1501 O O     . HIS A 1 198 ? -16.050 67.462  13.221  1.00 29.53 ? 198 HIS A O     1 
ATOM   1502 C CB    . HIS A 1 198 ? -16.482 65.103  11.320  1.00 30.62 ? 198 HIS A CB    1 
ATOM   1503 C CG    . HIS A 1 198 ? -15.396 64.300  11.930  1.00 31.57 ? 198 HIS A CG    1 
ATOM   1504 N ND1   . HIS A 1 198 ? -15.560 63.659  13.127  1.00 32.60 ? 198 HIS A ND1   1 
ATOM   1505 C CD2   . HIS A 1 198 ? -14.139 64.026  11.529  1.00 32.72 ? 198 HIS A CD2   1 
ATOM   1506 C CE1   . HIS A 1 198 ? -14.444 63.025  13.440  1.00 33.31 ? 198 HIS A CE1   1 
ATOM   1507 N NE2   . HIS A 1 198 ? -13.563 63.229  12.482  1.00 34.12 ? 198 HIS A NE2   1 
ATOM   1508 N N     . THR A 1 199 ? -16.848 65.940  14.620  1.00 29.54 ? 199 THR A N     1 
ATOM   1509 C CA    . THR A 1 199 ? -16.347 66.477  15.862  1.00 29.78 ? 199 THR A CA    1 
ATOM   1510 C C     . THR A 1 199 ? -16.229 67.986  15.837  1.00 30.77 ? 199 THR A C     1 
ATOM   1511 O O     . THR A 1 199 ? -17.239 68.682  16.016  1.00 30.86 ? 199 THR A O     1 
ATOM   1512 C CB    . THR A 1 199 ? -15.042 65.777  16.216  1.00 29.05 ? 199 THR A CB    1 
ATOM   1513 O OG1   . THR A 1 199 ? -14.114 65.885  15.128  1.00 31.62 ? 199 THR A OG1   1 
ATOM   1514 C CG2   . THR A 1 199 ? -15.291 64.290  16.421  1.00 29.06 ? 199 THR A CG2   1 
ATOM   1515 N N     . ASN A 1 200 ? -15.026 68.503  15.628  1.00 31.30 ? 200 ASN A N     1 
ATOM   1516 C CA    . ASN A 1 200 ? -14.809 69.938  15.566  1.00 31.95 ? 200 ASN A CA    1 
ATOM   1517 C C     . ASN A 1 200 ? -14.027 70.303  14.314  1.00 31.76 ? 200 ASN A C     1 
ATOM   1518 O O     . ASN A 1 200 ? -13.081 71.089  14.312  1.00 31.93 ? 200 ASN A O     1 
ATOM   1519 C CB    . ASN A 1 200 ? -14.099 70.444  16.818  1.00 35.70 ? 200 ASN A CB    1 
ATOM   1520 C CG    . ASN A 1 200 ? -12.816 69.653  17.014  1.00 38.15 ? 200 ASN A CG    1 
ATOM   1521 O OD1   . ASN A 1 200 ? -12.672 68.552  16.476  1.00 38.05 ? 200 ASN A OD1   1 
ATOM   1522 N ND2   . ASN A 1 200 ? -11.842 70.168  17.756  1.00 39.80 ? 200 ASN A ND2   1 
ATOM   1523 N N     . ASP A 1 201 ? -14.483 69.702  13.218  1.00 31.62 ? 201 ASP A N     1 
ATOM   1524 C CA    . ASP A 1 201 ? -14.025 70.189  11.907  1.00 31.30 ? 201 ASP A CA    1 
ATOM   1525 C C     . ASP A 1 201 ? -14.241 71.706  11.918  1.00 31.32 ? 201 ASP A C     1 
ATOM   1526 O O     . ASP A 1 201 ? -15.332 72.192  12.272  1.00 30.30 ? 201 ASP A O     1 
ATOM   1527 C CB    . ASP A 1 201 ? -14.886 69.480  10.871  1.00 30.57 ? 201 ASP A CB    1 
ATOM   1528 C CG    . ASP A 1 201 ? -14.579 69.951  9.473   1.00 32.36 ? 201 ASP A CG    1 
ATOM   1529 O OD1   . ASP A 1 201 ? -13.751 70.872  9.284   1.00 33.51 ? 201 ASP A OD1   1 
ATOM   1530 O OD2   . ASP A 1 201 ? -15.191 69.357  8.562   1.00 33.86 ? 201 ASP A OD2   1 
ATOM   1531 N N     . ILE A 1 202 ? -13.202 72.443  11.517  1.00 31.30 ? 202 ILE A N     1 
ATOM   1532 C CA    . ILE A 1 202 ? -13.332 73.906  11.520  1.00 31.88 ? 202 ILE A CA    1 
ATOM   1533 C C     . ILE A 1 202 ? -14.317 74.402  10.470  1.00 31.69 ? 202 ILE A C     1 
ATOM   1534 O O     . ILE A 1 202 ? -15.092 75.328  10.728  1.00 31.93 ? 202 ILE A O     1 
ATOM   1535 C CB    . ILE A 1 202 ? -11.984 74.612  11.313  1.00 33.02 ? 202 ILE A CB    1 
ATOM   1536 C CG1   . ILE A 1 202 ? -12.100 76.130  11.490  1.00 32.70 ? 202 ILE A CG1   1 
ATOM   1537 C CG2   . ILE A 1 202 ? -11.407 74.263  9.946   1.00 33.15 ? 202 ILE A CG2   1 
ATOM   1538 C CD1   . ILE A 1 202 ? -10.707 76.749  11.557  1.00 32.40 ? 202 ILE A CD1   1 
ATOM   1539 N N     . VAL A 1 203 ? -14.383 73.725  9.326   1.00 31.26 ? 203 VAL A N     1 
ATOM   1540 C CA    . VAL A 1 203 ? -15.205 74.155  8.220   1.00 30.76 ? 203 VAL A CA    1 
ATOM   1541 C C     . VAL A 1 203 ? -16.651 74.435  8.443   1.00 30.77 ? 203 VAL A C     1 
ATOM   1542 O O     . VAL A 1 203 ? -17.077 75.583  8.204   1.00 30.97 ? 203 VAL A O     1 
ATOM   1543 C CB    . VAL A 1 203 ? -14.910 73.396  6.932   1.00 30.81 ? 203 VAL A CB    1 
ATOM   1544 C CG1   . VAL A 1 203 ? -15.720 73.943  5.766   1.00 30.96 ? 203 VAL A CG1   1 
ATOM   1545 C CG2   . VAL A 1 203 ? -13.422 73.556  6.597   1.00 31.16 ? 203 VAL A CG2   1 
ATOM   1546 N N     . PRO A 1 204 ? -17.407 73.621  9.169   1.00 31.02 ? 204 PRO A N     1 
ATOM   1547 C CA    . PRO A 1 204 ? -18.804 73.880  9.502   1.00 30.54 ? 204 PRO A CA    1 
ATOM   1548 C C     . PRO A 1 204 ? -18.953 75.052  10.460  1.00 30.31 ? 204 PRO A C     1 
ATOM   1549 O O     . PRO A 1 204 ? -20.082 75.340  10.853  1.00 30.49 ? 204 PRO A O     1 
ATOM   1550 C CB    . PRO A 1 204 ? -19.281 72.631  10.237  1.00 30.18 ? 204 PRO A CB    1 
ATOM   1551 C CG    . PRO A 1 204 ? -18.374 71.557  9.765   1.00 30.63 ? 204 PRO A CG    1 
ATOM   1552 C CD    . PRO A 1 204 ? -17.038 72.229  9.529   1.00 31.06 ? 204 PRO A CD    1 
ATOM   1553 N N     . ARG A 1 205 ? -17.855 75.623  10.953  1.00 29.63 ? 205 ARG A N     1 
ATOM   1554 C CA    . ARG A 1 205 ? -17.866 76.738  11.857  1.00 28.98 ? 205 ARG A CA    1 
ATOM   1555 C C     . ARG A 1 205 ? -17.607 78.066  11.156  1.00 28.91 ? 205 ARG A C     1 
ATOM   1556 O O     . ARG A 1 205 ? -17.562 79.093  11.838  1.00 28.61 ? 205 ARG A O     1 
ATOM   1557 C CB    . ARG A 1 205 ? -16.872 76.601  13.009  1.00 27.42 ? 205 ARG A CB    1 
ATOM   1558 C CG    . ARG A 1 205 ? -16.547 75.210  13.474  1.00 27.53 ? 205 ARG A CG    1 
ATOM   1559 C CD    . ARG A 1 205 ? -16.865 74.940  14.919  1.00 28.27 ? 205 ARG A CD    1 
ATOM   1560 N NE    . ARG A 1 205 ? -15.686 74.943  15.769  1.00 32.32 ? 205 ARG A NE    1 
ATOM   1561 C CZ    . ARG A 1 205 ? -15.484 74.108  16.789  1.00 33.65 ? 205 ARG A CZ    1 
ATOM   1562 N NH1   . ARG A 1 205 ? -14.381 74.156  17.530  1.00 35.75 ? 205 ARG A NH1   1 
ATOM   1563 N NH2   . ARG A 1 205 ? -16.328 73.150  17.127  1.00 32.13 ? 205 ARG A NH2   1 
ATOM   1564 N N     . LEU A 1 206 ? -17.484 78.082  9.841   1.00 28.87 ? 206 LEU A N     1 
ATOM   1565 C CA    . LEU A 1 206 ? -17.249 79.290  9.054   1.00 28.61 ? 206 LEU A CA    1 
ATOM   1566 C C     . LEU A 1 206 ? -18.290 79.480  7.947   1.00 28.49 ? 206 LEU A C     1 
ATOM   1567 O O     . LEU A 1 206 ? -18.794 78.483  7.439   1.00 28.33 ? 206 LEU A O     1 
ATOM   1568 C CB    . LEU A 1 206 ? -15.940 79.030  8.314   1.00 27.48 ? 206 LEU A CB    1 
ATOM   1569 C CG    . LEU A 1 206 ? -14.553 79.161  8.883   1.00 28.33 ? 206 LEU A CG    1 
ATOM   1570 C CD1   . LEU A 1 206 ? -14.470 79.481  10.359  1.00 28.06 ? 206 LEU A CD1   1 
ATOM   1571 C CD2   . LEU A 1 206 ? -13.756 77.898  8.549   1.00 26.82 ? 206 LEU A CD2   1 
ATOM   1572 N N     . PRO A 1 207 ? -18.513 80.706  7.487   1.00 28.39 ? 207 PRO A N     1 
ATOM   1573 C CA    . PRO A 1 207 ? -17.957 81.896  8.107   1.00 28.96 ? 207 PRO A CA    1 
ATOM   1574 C C     . PRO A 1 207 ? -18.492 82.071  9.521   1.00 30.19 ? 207 PRO A C     1 
ATOM   1575 O O     . PRO A 1 207 ? -19.464 81.430  9.922   1.00 30.35 ? 207 PRO A O     1 
ATOM   1576 C CB    . PRO A 1 207 ? -18.496 83.018  7.215   1.00 28.21 ? 207 PRO A CB    1 
ATOM   1577 C CG    . PRO A 1 207 ? -18.645 82.382  5.876   1.00 27.70 ? 207 PRO A CG    1 
ATOM   1578 C CD    . PRO A 1 207 ? -19.195 81.019  6.208   1.00 27.91 ? 207 PRO A CD    1 
ATOM   1579 N N     . PRO A 1 208 ? -17.850 82.887  10.338  1.00 31.59 ? 208 PRO A N     1 
ATOM   1580 C CA    . PRO A 1 208 ? -18.312 83.164  11.689  1.00 32.86 ? 208 PRO A CA    1 
ATOM   1581 C C     . PRO A 1 208 ? -19.761 83.620  11.650  1.00 34.25 ? 208 PRO A C     1 
ATOM   1582 O O     . PRO A 1 208 ? -20.223 84.103  10.607  1.00 35.08 ? 208 PRO A O     1 
ATOM   1583 C CB    . PRO A 1 208 ? -17.384 84.262  12.187  1.00 32.75 ? 208 PRO A CB    1 
ATOM   1584 C CG    . PRO A 1 208 ? -16.219 84.280  11.264  1.00 32.51 ? 208 PRO A CG    1 
ATOM   1585 C CD    . PRO A 1 208 ? -16.732 83.779  9.941   1.00 32.31 ? 208 PRO A CD    1 
ATOM   1586 N N     . ARG A 1 209 ? -20.481 83.571  12.769  1.00 35.33 ? 209 ARG A N     1 
ATOM   1587 C CA    . ARG A 1 209 ? -21.875 84.009  12.796  1.00 36.12 ? 209 ARG A CA    1 
ATOM   1588 C C     . ARG A 1 209 ? -22.036 85.516  12.856  1.00 36.34 ? 209 ARG A C     1 
ATOM   1589 O O     . ARG A 1 209 ? -23.036 86.068  12.399  1.00 36.59 ? 209 ARG A O     1 
ATOM   1590 C CB    . ARG A 1 209 ? -22.584 83.390  13.997  1.00 39.03 ? 209 ARG A CB    1 
ATOM   1591 C CG    . ARG A 1 209 ? -22.520 81.869  13.971  1.00 43.26 ? 209 ARG A CG    1 
ATOM   1592 C CD    . ARG A 1 209 ? -23.658 81.239  14.765  1.00 45.79 ? 209 ARG A CD    1 
ATOM   1593 N NE    . ARG A 1 209 ? -24.835 82.109  14.735  1.00 47.63 ? 209 ARG A NE    1 
ATOM   1594 C CZ    . ARG A 1 209 ? -25.650 82.267  15.772  1.00 49.01 ? 209 ARG A CZ    1 
ATOM   1595 N NH1   . ARG A 1 209 ? -25.439 81.620  16.917  1.00 49.59 ? 209 ARG A NH1   1 
ATOM   1596 N NH2   . ARG A 1 209 ? -26.688 83.082  15.657  1.00 48.87 ? 209 ARG A NH2   1 
ATOM   1597 N N     . GLU A 1 210 ? -20.962 86.208  13.219  1.00 36.53 ? 210 GLU A N     1 
ATOM   1598 C CA    . GLU A 1 210 ? -20.907 87.650  13.264  1.00 36.64 ? 210 GLU A CA    1 
ATOM   1599 C C     . GLU A 1 210 ? -20.975 88.235  11.867  1.00 36.33 ? 210 GLU A C     1 
ATOM   1600 O O     . GLU A 1 210 ? -21.469 89.352  11.738  1.00 37.07 ? 210 GLU A O     1 
ATOM   1601 C CB    . GLU A 1 210 ? -19.612 88.161  13.886  1.00 40.32 ? 210 GLU A CB    1 
ATOM   1602 C CG    . GLU A 1 210 ? -19.367 87.594  15.273  1.00 45.95 ? 210 GLU A CG    1 
ATOM   1603 C CD    . GLU A 1 210 ? -18.717 86.219  15.184  1.00 48.61 ? 210 GLU A CD    1 
ATOM   1604 O OE1   . GLU A 1 210 ? -19.418 85.241  15.526  1.00 49.25 ? 210 GLU A OE1   1 
ATOM   1605 O OE2   . GLU A 1 210 ? -17.537 86.180  14.757  1.00 50.54 ? 210 GLU A OE2   1 
ATOM   1606 N N     . PHE A 1 211 ? -20.610 87.465  10.843  1.00 35.50 ? 211 PHE A N     1 
ATOM   1607 C CA    . PHE A 1 211 ? -20.724 87.967  9.477   1.00 34.41 ? 211 PHE A CA    1 
ATOM   1608 C C     . PHE A 1 211 ? -22.159 87.838  9.012   1.00 34.14 ? 211 PHE A C     1 
ATOM   1609 O O     . PHE A 1 211 ? -22.494 88.345  7.945   1.00 35.09 ? 211 PHE A O     1 
ATOM   1610 C CB    . PHE A 1 211 ? -19.735 87.273  8.558   1.00 33.04 ? 211 PHE A CB    1 
ATOM   1611 C CG    . PHE A 1 211 ? -18.275 87.493  8.852   1.00 30.87 ? 211 PHE A CG    1 
ATOM   1612 C CD1   . PHE A 1 211 ? -17.301 87.023  7.984   1.00 28.40 ? 211 PHE A CD1   1 
ATOM   1613 C CD2   . PHE A 1 211 ? -17.866 88.186  9.980   1.00 29.30 ? 211 PHE A CD2   1 
ATOM   1614 C CE1   . PHE A 1 211 ? -15.968 87.246  8.272   1.00 28.79 ? 211 PHE A CE1   1 
ATOM   1615 C CE2   . PHE A 1 211 ? -16.548 88.414  10.263  1.00 27.91 ? 211 PHE A CE2   1 
ATOM   1616 C CZ    . PHE A 1 211 ? -15.590 87.943  9.399   1.00 27.74 ? 211 PHE A CZ    1 
ATOM   1617 N N     . GLY A 1 212 ? -23.030 87.250  9.817   1.00 33.54 ? 212 GLY A N     1 
ATOM   1618 C CA    . GLY A 1 212 ? -24.448 87.132  9.545   1.00 32.64 ? 212 GLY A CA    1 
ATOM   1619 C C     . GLY A 1 212 ? -24.805 85.760  8.977   1.00 32.10 ? 212 GLY A C     1 
ATOM   1620 O O     . GLY A 1 212 ? -25.754 85.625  8.196   1.00 32.28 ? 212 GLY A O     1 
ATOM   1621 N N     . TYR A 1 213 ? -24.038 84.727  9.340   1.00 30.79 ? 213 TYR A N     1 
ATOM   1622 C CA    . TYR A 1 213 ? -24.278 83.413  8.760   1.00 29.56 ? 213 TYR A CA    1 
ATOM   1623 C C     . TYR A 1 213 ? -24.955 82.484  9.756   1.00 28.93 ? 213 TYR A C     1 
ATOM   1624 O O     . TYR A 1 213 ? -24.622 82.506  10.940  1.00 28.64 ? 213 TYR A O     1 
ATOM   1625 C CB    . TYR A 1 213 ? -22.961 82.790  8.294   1.00 29.12 ? 213 TYR A CB    1 
ATOM   1626 C CG    . TYR A 1 213 ? -22.517 83.231  6.922   1.00 27.99 ? 213 TYR A CG    1 
ATOM   1627 C CD1   . TYR A 1 213 ? -22.852 82.481  5.800   1.00 27.56 ? 213 TYR A CD1   1 
ATOM   1628 C CD2   . TYR A 1 213 ? -21.802 84.412  6.755   1.00 27.43 ? 213 TYR A CD2   1 
ATOM   1629 C CE1   . TYR A 1 213 ? -22.453 82.885  4.538   1.00 27.34 ? 213 TYR A CE1   1 
ATOM   1630 C CE2   . TYR A 1 213 ? -21.414 84.835  5.496   1.00 27.20 ? 213 TYR A CE2   1 
ATOM   1631 C CZ    . TYR A 1 213 ? -21.731 84.053  4.405   1.00 27.55 ? 213 TYR A CZ    1 
ATOM   1632 O OH    . TYR A 1 213 ? -21.363 84.443  3.142   1.00 28.38 ? 213 TYR A OH    1 
ATOM   1633 N N     . SER A 1 214 ? -25.712 81.518  9.256   1.00 28.18 ? 214 SER A N     1 
ATOM   1634 C CA    . SER A 1 214 ? -26.401 80.578  10.121  1.00 27.51 ? 214 SER A CA    1 
ATOM   1635 C C     . SER A 1 214 ? -26.348 79.191  9.476   1.00 27.40 ? 214 SER A C     1 
ATOM   1636 O O     . SER A 1 214 ? -26.375 79.100  8.251   1.00 27.12 ? 214 SER A O     1 
ATOM   1637 C CB    . SER A 1 214 ? -27.879 80.928  10.308  1.00 26.71 ? 214 SER A CB    1 
ATOM   1638 O OG    . SER A 1 214 ? -28.069 81.920  11.277  1.00 25.75 ? 214 SER A OG    1 
ATOM   1639 N N     . HIS A 1 215 ? -26.694 78.208  10.291  1.00 27.40 ? 215 HIS A N     1 
ATOM   1640 C CA    . HIS A 1 215 ? -26.806 76.838  9.807   1.00 27.76 ? 215 HIS A CA    1 
ATOM   1641 C C     . HIS A 1 215 ? -28.236 76.307  9.843   1.00 27.86 ? 215 HIS A C     1 
ATOM   1642 O O     . HIS A 1 215 ? -28.943 76.459  10.838  1.00 28.13 ? 215 HIS A O     1 
ATOM   1643 C CB    . HIS A 1 215 ? -25.942 75.939  10.700  1.00 27.91 ? 215 HIS A CB    1 
ATOM   1644 C CG    . HIS A 1 215 ? -24.659 75.541  10.042  1.00 28.21 ? 215 HIS A CG    1 
ATOM   1645 N ND1   . HIS A 1 215 ? -24.597 75.232  8.700   1.00 27.18 ? 215 HIS A ND1   1 
ATOM   1646 C CD2   . HIS A 1 215 ? -23.406 75.394  10.541  1.00 27.96 ? 215 HIS A CD2   1 
ATOM   1647 C CE1   . HIS A 1 215 ? -23.353 74.908  8.401   1.00 27.81 ? 215 HIS A CE1   1 
ATOM   1648 N NE2   . HIS A 1 215 ? -22.610 74.999  9.496   1.00 27.86 ? 215 HIS A NE2   1 
ATOM   1649 N N     . SER A 1 216 ? -28.633 75.578  8.815   1.00 27.71 ? 216 SER A N     1 
ATOM   1650 C CA    . SER A 1 216 ? -29.938 74.935  8.790   1.00 28.24 ? 216 SER A CA    1 
ATOM   1651 C C     . SER A 1 216 ? -30.027 73.797  9.806   1.00 28.83 ? 216 SER A C     1 
ATOM   1652 O O     . SER A 1 216 ? -29.018 73.260  10.250  1.00 29.08 ? 216 SER A O     1 
ATOM   1653 C CB    . SER A 1 216 ? -30.106 74.323  7.391   1.00 27.63 ? 216 SER A CB    1 
ATOM   1654 O OG    . SER A 1 216 ? -29.192 73.229  7.323   1.00 25.95 ? 216 SER A OG    1 
ATOM   1655 N N     . SER A 1 217 ? -31.223 73.315  10.125  1.00 29.15 ? 217 SER A N     1 
ATOM   1656 C CA    . SER A 1 217 ? -31.420 72.240  11.094  1.00 29.33 ? 217 SER A CA    1 
ATOM   1657 C C     . SER A 1 217 ? -32.069 71.039  10.435  1.00 29.16 ? 217 SER A C     1 
ATOM   1658 O O     . SER A 1 217 ? -32.895 71.247  9.555   1.00 29.92 ? 217 SER A O     1 
ATOM   1659 C CB    . SER A 1 217 ? -32.387 72.746  12.169  1.00 30.43 ? 217 SER A CB    1 
ATOM   1660 O OG    . SER A 1 217 ? -32.448 71.880  13.293  1.00 29.89 ? 217 SER A OG    1 
ATOM   1661 N N     . PRO A 1 218 ? -31.784 69.836  10.872  1.00 28.82 ? 218 PRO A N     1 
ATOM   1662 C CA    . PRO A 1 218 ? -30.870 69.565  11.963  1.00 28.83 ? 218 PRO A CA    1 
ATOM   1663 C C     . PRO A 1 218 ? -29.452 69.223  11.526  1.00 28.83 ? 218 PRO A C     1 
ATOM   1664 O O     . PRO A 1 218 ? -29.104 69.348  10.349  1.00 28.45 ? 218 PRO A O     1 
ATOM   1665 C CB    . PRO A 1 218 ? -31.557 68.311  12.524  1.00 29.07 ? 218 PRO A CB    1 
ATOM   1666 C CG    . PRO A 1 218 ? -31.954 67.540  11.295  1.00 28.99 ? 218 PRO A CG    1 
ATOM   1667 C CD    . PRO A 1 218 ? -32.331 68.583  10.278  1.00 28.69 ? 218 PRO A CD    1 
ATOM   1668 N N     . GLU A 1 219 ? -28.625 68.714  12.430  1.00 28.83 ? 219 GLU A N     1 
ATOM   1669 C CA    . GLU A 1 219 ? -27.252 68.355  12.088  1.00 29.66 ? 219 GLU A CA    1 
ATOM   1670 C C     . GLU A 1 219 ? -26.964 66.945  12.577  1.00 29.86 ? 219 GLU A C     1 
ATOM   1671 O O     . GLU A 1 219 ? -27.179 66.670  13.752  1.00 29.68 ? 219 GLU A O     1 
ATOM   1672 C CB    . GLU A 1 219 ? -26.237 69.372  12.614  1.00 30.22 ? 219 GLU A CB    1 
ATOM   1673 C CG    . GLU A 1 219 ? -24.965 68.866  13.245  1.00 31.68 ? 219 GLU A CG    1 
ATOM   1674 C CD    . GLU A 1 219 ? -24.179 69.877  14.047  1.00 33.29 ? 219 GLU A CD    1 
ATOM   1675 O OE1   . GLU A 1 219 ? -24.724 70.911  14.488  1.00 34.74 ? 219 GLU A OE1   1 
ATOM   1676 O OE2   . GLU A 1 219 ? -22.966 69.624  14.247  1.00 32.94 ? 219 GLU A OE2   1 
ATOM   1677 N N     . TYR A 1 220 ? -26.456 66.088  11.708  1.00 30.34 ? 220 TYR A N     1 
ATOM   1678 C CA    . TYR A 1 220 ? -26.036 64.748  12.104  1.00 30.53 ? 220 TYR A CA    1 
ATOM   1679 C C     . TYR A 1 220 ? -24.551 64.812  12.437  1.00 30.37 ? 220 TYR A C     1 
ATOM   1680 O O     . TYR A 1 220 ? -23.725 65.021  11.550  1.00 30.77 ? 220 TYR A O     1 
ATOM   1681 C CB    . TYR A 1 220 ? -26.282 63.730  10.989  1.00 31.56 ? 220 TYR A CB    1 
ATOM   1682 C CG    . TYR A 1 220 ? -27.769 63.569  10.733  1.00 33.11 ? 220 TYR A CG    1 
ATOM   1683 C CD1   . TYR A 1 220 ? -28.413 64.290  9.740   1.00 33.76 ? 220 TYR A CD1   1 
ATOM   1684 C CD2   . TYR A 1 220 ? -28.521 62.714  11.525  1.00 33.63 ? 220 TYR A CD2   1 
ATOM   1685 C CE1   . TYR A 1 220 ? -29.773 64.132  9.530   1.00 34.38 ? 220 TYR A CE1   1 
ATOM   1686 C CE2   . TYR A 1 220 ? -29.880 62.561  11.325  1.00 34.18 ? 220 TYR A CE2   1 
ATOM   1687 C CZ    . TYR A 1 220 ? -30.506 63.273  10.323  1.00 34.31 ? 220 TYR A CZ    1 
ATOM   1688 O OH    . TYR A 1 220 ? -31.856 63.134  10.105  1.00 33.90 ? 220 TYR A OH    1 
ATOM   1689 N N     . TRP A 1 221 ? -24.257 64.783  13.722  1.00 30.02 ? 221 TRP A N     1 
ATOM   1690 C CA    . TRP A 1 221 ? -22.905 64.965  14.223  1.00 30.23 ? 221 TRP A CA    1 
ATOM   1691 C C     . TRP A 1 221 ? -22.180 63.644  14.444  1.00 30.09 ? 221 TRP A C     1 
ATOM   1692 O O     . TRP A 1 221 ? -22.588 62.832  15.272  1.00 29.23 ? 221 TRP A O     1 
ATOM   1693 C CB    . TRP A 1 221 ? -22.944 65.789  15.506  1.00 32.14 ? 221 TRP A CB    1 
ATOM   1694 C CG    . TRP A 1 221 ? -21.635 66.186  16.104  1.00 34.13 ? 221 TRP A CG    1 
ATOM   1695 C CD1   . TRP A 1 221 ? -20.578 66.788  15.483  1.00 34.86 ? 221 TRP A CD1   1 
ATOM   1696 C CD2   . TRP A 1 221 ? -21.265 66.061  17.482  1.00 35.41 ? 221 TRP A CD2   1 
ATOM   1697 N NE1   . TRP A 1 221 ? -19.578 67.040  16.385  1.00 34.95 ? 221 TRP A NE1   1 
ATOM   1698 C CE2   . TRP A 1 221 ? -19.960 66.576  17.615  1.00 36.05 ? 221 TRP A CE2   1 
ATOM   1699 C CE3   . TRP A 1 221 ? -21.902 65.546  18.617  1.00 35.83 ? 221 TRP A CE3   1 
ATOM   1700 C CZ2   . TRP A 1 221 ? -19.290 66.593  18.840  1.00 36.60 ? 221 TRP A CZ2   1 
ATOM   1701 C CZ3   . TRP A 1 221 ? -21.226 65.543  19.821  1.00 35.45 ? 221 TRP A CZ3   1 
ATOM   1702 C CH2   . TRP A 1 221 ? -19.930 66.063  19.923  1.00 35.92 ? 221 TRP A CH2   1 
ATOM   1703 N N     . ILE A 1 222 ? -21.136 63.411  13.641  1.00 30.05 ? 222 ILE A N     1 
ATOM   1704 C CA    . ILE A 1 222 ? -20.322 62.212  13.791  1.00 29.97 ? 222 ILE A CA    1 
ATOM   1705 C C     . ILE A 1 222 ? -19.361 62.450  14.952  1.00 30.57 ? 222 ILE A C     1 
ATOM   1706 O O     . ILE A 1 222 ? -18.470 63.278  14.821  1.00 30.75 ? 222 ILE A O     1 
ATOM   1707 C CB    . ILE A 1 222 ? -19.462 61.938  12.555  1.00 28.42 ? 222 ILE A CB    1 
ATOM   1708 C CG1   . ILE A 1 222 ? -20.273 61.814  11.279  1.00 28.65 ? 222 ILE A CG1   1 
ATOM   1709 C CG2   . ILE A 1 222 ? -18.640 60.689  12.844  1.00 28.51 ? 222 ILE A CG2   1 
ATOM   1710 C CD1   . ILE A 1 222 ? -19.479 61.405  10.053  1.00 26.91 ? 222 ILE A CD1   1 
ATOM   1711 N N     . LYS A 1 223 ? -19.375 61.642  15.996  1.00 31.29 ? 223 LYS A N     1 
ATOM   1712 C CA    . LYS A 1 223 ? -18.607 62.016  17.182  1.00 31.98 ? 223 LYS A CA    1 
ATOM   1713 C C     . LYS A 1 223 ? -17.377 61.176  17.460  1.00 32.05 ? 223 LYS A C     1 
ATOM   1714 O O     . LYS A 1 223 ? -16.668 61.394  18.445  1.00 31.85 ? 223 LYS A O     1 
ATOM   1715 C CB    . LYS A 1 223 ? -19.567 61.967  18.370  1.00 35.19 ? 223 LYS A CB    1 
ATOM   1716 C CG    . LYS A 1 223 ? -19.699 60.565  18.913  1.00 38.92 ? 223 LYS A CG    1 
ATOM   1717 C CD    . LYS A 1 223 ? -20.380 60.578  20.280  1.00 43.82 ? 223 LYS A CD    1 
ATOM   1718 C CE    . LYS A 1 223 ? -20.354 59.167  20.864  1.00 46.59 ? 223 LYS A CE    1 
ATOM   1719 N NZ    . LYS A 1 223 ? -20.988 58.134  19.981  1.00 46.70 ? 223 LYS A NZ    1 
ATOM   1720 N N     . SER A 1 224 ? -17.118 60.188  16.621  1.00 31.97 ? 224 SER A N     1 
ATOM   1721 C CA    . SER A 1 224 ? -15.963 59.314  16.709  1.00 31.28 ? 224 SER A CA    1 
ATOM   1722 C C     . SER A 1 224 ? -14.765 60.021  16.098  1.00 31.87 ? 224 SER A C     1 
ATOM   1723 O O     . SER A 1 224 ? -14.914 60.729  15.104  1.00 32.64 ? 224 SER A O     1 
ATOM   1724 C CB    . SER A 1 224 ? -16.276 58.026  15.962  1.00 29.39 ? 224 SER A CB    1 
ATOM   1725 O OG    . SER A 1 224 ? -16.686 58.272  14.637  1.00 29.39 ? 224 SER A OG    1 
ATOM   1726 N N     . GLY A 1 225 ? -13.567 59.800  16.604  1.00 32.09 ? 225 GLY A N     1 
ATOM   1727 C CA    . GLY A 1 225 ? -12.381 60.537  16.234  1.00 32.04 ? 225 GLY A CA    1 
ATOM   1728 C C     . GLY A 1 225 ? -11.878 60.424  14.813  1.00 32.05 ? 225 GLY A C     1 
ATOM   1729 O O     . GLY A 1 225 ? -12.251 59.506  14.085  1.00 32.34 ? 225 GLY A O     1 
ATOM   1730 N N     . THR A 1 226 ? -10.795 61.130  14.497  1.00 31.99 ? 226 THR A N     1 
ATOM   1731 C CA    . THR A 1 226 ? -10.219 61.032  13.161  1.00 32.14 ? 226 THR A CA    1 
ATOM   1732 C C     . THR A 1 226 ? -9.470  59.723  13.055  1.00 32.55 ? 226 THR A C     1 
ATOM   1733 O O     . THR A 1 226 ? -8.816  59.286  13.998  1.00 32.75 ? 226 THR A O     1 
ATOM   1734 C CB    . THR A 1 226 ? -9.271  62.216  12.914  1.00 32.14 ? 226 THR A CB    1 
ATOM   1735 O OG1   . THR A 1 226 ? -10.000 63.409  13.231  1.00 31.48 ? 226 THR A OG1   1 
ATOM   1736 C CG2   . THR A 1 226 ? -8.760  62.280  11.488  1.00 31.84 ? 226 THR A CG2   1 
ATOM   1737 N N     . LEU A 1 227 ? -9.638  58.999  11.961  1.00 33.04 ? 227 LEU A N     1 
ATOM   1738 C CA    . LEU A 1 227 ? -8.924  57.763  11.704  1.00 33.39 ? 227 LEU A CA    1 
ATOM   1739 C C     . LEU A 1 227 ? -9.566  56.560  12.366  1.00 33.73 ? 227 LEU A C     1 
ATOM   1740 O O     . LEU A 1 227 ? -9.139  55.438  12.070  1.00 34.34 ? 227 LEU A O     1 
ATOM   1741 C CB    . LEU A 1 227 ? -7.435  57.844  12.028  1.00 31.37 ? 227 LEU A CB    1 
ATOM   1742 C CG    . LEU A 1 227 ? -6.563  58.624  11.047  1.00 31.47 ? 227 LEU A CG    1 
ATOM   1743 C CD1   . LEU A 1 227 ? -5.100  58.473  11.430  1.00 31.80 ? 227 LEU A CD1   1 
ATOM   1744 C CD2   . LEU A 1 227 ? -6.785  58.225  9.601   1.00 31.09 ? 227 LEU A CD2   1 
ATOM   1745 N N     . VAL A 1 228 ? -10.520 56.760  13.253  1.00 33.89 ? 228 VAL A N     1 
ATOM   1746 C CA    . VAL A 1 228 ? -11.257 55.613  13.785  1.00 34.92 ? 228 VAL A CA    1 
ATOM   1747 C C     . VAL A 1 228 ? -12.508 55.528  12.909  1.00 35.84 ? 228 VAL A C     1 
ATOM   1748 O O     . VAL A 1 228 ? -12.967 56.524  12.342  1.00 35.83 ? 228 VAL A O     1 
ATOM   1749 C CB    . VAL A 1 228 ? -11.559 55.693  15.273  1.00 35.22 ? 228 VAL A CB    1 
ATOM   1750 C CG1   . VAL A 1 228 ? -11.377 57.099  15.832  1.00 34.53 ? 228 VAL A CG1   1 
ATOM   1751 C CG2   . VAL A 1 228 ? -12.952 55.168  15.616  1.00 35.37 ? 228 VAL A CG2   1 
ATOM   1752 N N     . PRO A 1 229 ? -12.976 54.304  12.674  1.00 36.10 ? 229 PRO A N     1 
ATOM   1753 C CA    . PRO A 1 229 ? -14.141 54.042  11.846  1.00 35.51 ? 229 PRO A CA    1 
ATOM   1754 C C     . PRO A 1 229 ? -15.438 54.365  12.566  1.00 35.22 ? 229 PRO A C     1 
ATOM   1755 O O     . PRO A 1 229 ? -15.552 54.210  13.773  1.00 34.80 ? 229 PRO A O     1 
ATOM   1756 C CB    . PRO A 1 229 ? -14.088 52.560  11.534  1.00 35.35 ? 229 PRO A CB    1 
ATOM   1757 C CG    . PRO A 1 229 ? -12.781 52.079  12.049  1.00 35.63 ? 229 PRO A CG    1 
ATOM   1758 C CD    . PRO A 1 229 ? -12.385 53.030  13.157  1.00 35.93 ? 229 PRO A CD    1 
ATOM   1759 N N     . VAL A 1 230 ? -16.400 54.814  11.775  1.00 35.53 ? 230 VAL A N     1 
ATOM   1760 C CA    . VAL A 1 230 ? -17.701 55.217  12.278  1.00 35.98 ? 230 VAL A CA    1 
ATOM   1761 C C     . VAL A 1 230 ? -18.692 54.066  12.364  1.00 36.36 ? 230 VAL A C     1 
ATOM   1762 O O     . VAL A 1 230 ? -18.692 53.159  11.542  1.00 36.30 ? 230 VAL A O     1 
ATOM   1763 C CB    . VAL A 1 230 ? -18.328 56.307  11.378  1.00 35.00 ? 230 VAL A CB    1 
ATOM   1764 C CG1   . VAL A 1 230 ? -19.511 56.948  12.086  1.00 34.60 ? 230 VAL A CG1   1 
ATOM   1765 C CG2   . VAL A 1 230 ? -17.302 57.356  10.996  1.00 35.33 ? 230 VAL A CG2   1 
ATOM   1766 N N     . THR A 1 231 ? -19.438 53.998  13.459  1.00 36.94 ? 231 THR A N     1 
ATOM   1767 C CA    . THR A 1 231 ? -20.585 53.109  13.589  1.00 37.81 ? 231 THR A CA    1 
ATOM   1768 C C     . THR A 1 231 ? -21.837 53.966  13.800  1.00 38.38 ? 231 THR A C     1 
ATOM   1769 O O     . THR A 1 231 ? -21.739 55.175  14.034  1.00 38.55 ? 231 THR A O     1 
ATOM   1770 C CB    . THR A 1 231 ? -20.481 52.123  14.758  1.00 37.46 ? 231 THR A CB    1 
ATOM   1771 O OG1   . THR A 1 231 ? -20.707 52.841  15.981  1.00 38.44 ? 231 THR A OG1   1 
ATOM   1772 C CG2   . THR A 1 231 ? -19.121 51.452  14.808  1.00 38.37 ? 231 THR A CG2   1 
ATOM   1773 N N     . ARG A 1 232 ? -23.032 53.403  13.630  1.00 38.61 ? 232 ARG A N     1 
ATOM   1774 C CA    . ARG A 1 232 ? -24.278 54.130  13.761  1.00 38.78 ? 232 ARG A CA    1 
ATOM   1775 C C     . ARG A 1 232 ? -24.591 54.636  15.161  1.00 38.76 ? 232 ARG A C     1 
ATOM   1776 O O     . ARG A 1 232 ? -25.557 55.395  15.339  1.00 38.46 ? 232 ARG A O     1 
ATOM   1777 C CB    . ARG A 1 232 ? -25.488 53.364  13.237  1.00 40.51 ? 232 ARG A CB    1 
ATOM   1778 C CG    . ARG A 1 232 ? -25.471 51.895  13.597  1.00 42.87 ? 232 ARG A CG    1 
ATOM   1779 C CD    . ARG A 1 232 ? -26.514 51.128  12.789  1.00 44.80 ? 232 ARG A CD    1 
ATOM   1780 N NE    . ARG A 1 232 ? -27.820 51.315  13.421  1.00 45.89 ? 232 ARG A NE    1 
ATOM   1781 C CZ    . ARG A 1 232 ? -28.142 50.790  14.593  1.00 45.65 ? 232 ARG A CZ    1 
ATOM   1782 N NH1   . ARG A 1 232 ? -29.336 50.981  15.137  1.00 44.80 ? 232 ARG A NH1   1 
ATOM   1783 N NH2   . ARG A 1 232 ? -27.250 50.054  15.240  1.00 47.41 ? 232 ARG A NH2   1 
ATOM   1784 N N     . ASN A 1 233 ? -23.777 54.278  16.145  1.00 38.78 ? 233 ASN A N     1 
ATOM   1785 C CA    . ASN A 1 233 ? -23.932 54.773  17.494  1.00 39.20 ? 233 ASN A CA    1 
ATOM   1786 C C     . ASN A 1 233 ? -23.097 56.030  17.691  1.00 38.58 ? 233 ASN A C     1 
ATOM   1787 O O     . ASN A 1 233 ? -23.087 56.583  18.792  1.00 39.15 ? 233 ASN A O     1 
ATOM   1788 C CB    . ASN A 1 233 ? -23.582 53.727  18.560  1.00 44.19 ? 233 ASN A CB    1 
ATOM   1789 C CG    . ASN A 1 233 ? -24.858 52.979  18.933  1.00 48.69 ? 233 ASN A CG    1 
ATOM   1790 O OD1   . ASN A 1 233 ? -25.174 51.955  18.313  1.00 50.65 ? 233 ASN A OD1   1 
ATOM   1791 N ND2   . ASN A 1 233 ? -25.600 53.523  19.899  1.00 50.70 ? 233 ASN A ND2   1 
ATOM   1792 N N     . ASP A 1 234 ? -22.336 56.411  16.674  1.00 37.57 ? 234 ASP A N     1 
ATOM   1793 C CA    . ASP A 1 234 ? -21.465 57.572  16.757  1.00 36.23 ? 234 ASP A CA    1 
ATOM   1794 C C     . ASP A 1 234 ? -22.126 58.798  16.167  1.00 35.68 ? 234 ASP A C     1 
ATOM   1795 O O     . ASP A 1 234 ? -21.722 59.917  16.456  1.00 36.17 ? 234 ASP A O     1 
ATOM   1796 C CB    . ASP A 1 234 ? -20.177 57.241  15.993  1.00 35.94 ? 234 ASP A CB    1 
ATOM   1797 C CG    . ASP A 1 234 ? -19.545 56.030  16.665  1.00 36.36 ? 234 ASP A CG    1 
ATOM   1798 O OD1   . ASP A 1 234 ? -19.244 55.034  15.991  1.00 35.62 ? 234 ASP A OD1   1 
ATOM   1799 O OD2   . ASP A 1 234 ? -19.399 56.098  17.901  1.00 38.36 ? 234 ASP A OD2   1 
ATOM   1800 N N     . ILE A 1 235 ? -23.039 58.580  15.238  1.00 35.15 ? 235 ILE A N     1 
ATOM   1801 C CA    . ILE A 1 235 ? -23.768 59.667  14.592  1.00 34.58 ? 235 ILE A CA    1 
ATOM   1802 C C     . ILE A 1 235 ? -24.888 60.141  15.504  1.00 35.05 ? 235 ILE A C     1 
ATOM   1803 O O     . ILE A 1 235 ? -25.580 59.339  16.125  1.00 34.89 ? 235 ILE A O     1 
ATOM   1804 C CB    . ILE A 1 235 ? -24.316 59.167  13.240  1.00 31.42 ? 235 ILE A CB    1 
ATOM   1805 C CG1   . ILE A 1 235 ? -23.143 58.668  12.411  1.00 30.88 ? 235 ILE A CG1   1 
ATOM   1806 C CG2   . ILE A 1 235 ? -25.119 60.265  12.572  1.00 31.50 ? 235 ILE A CG2   1 
ATOM   1807 C CD1   . ILE A 1 235 ? -23.342 58.453  10.937  1.00 30.98 ? 235 ILE A CD1   1 
ATOM   1808 N N     . VAL A 1 236 ? -24.878 61.399  15.923  1.00 35.67 ? 236 VAL A N     1 
ATOM   1809 C CA    . VAL A 1 236 ? -25.916 61.936  16.806  1.00 36.27 ? 236 VAL A CA    1 
ATOM   1810 C C     . VAL A 1 236 ? -26.714 63.002  16.057  1.00 36.31 ? 236 VAL A C     1 
ATOM   1811 O O     . VAL A 1 236 ? -26.142 63.748  15.264  1.00 36.59 ? 236 VAL A O     1 
ATOM   1812 C CB    . VAL A 1 236 ? -25.316 62.570  18.078  1.00 36.38 ? 236 VAL A CB    1 
ATOM   1813 C CG1   . VAL A 1 236 ? -26.420 63.018  19.021  1.00 36.69 ? 236 VAL A CG1   1 
ATOM   1814 C CG2   . VAL A 1 236 ? -24.395 61.593  18.791  1.00 36.43 ? 236 VAL A CG2   1 
ATOM   1815 N N     . LYS A 1 237 ? -28.011 63.103  16.274  1.00 36.38 ? 237 LYS A N     1 
ATOM   1816 C CA    . LYS A 1 237 ? -28.826 64.092  15.576  1.00 36.40 ? 237 LYS A CA    1 
ATOM   1817 C C     . LYS A 1 237 ? -29.113 65.306  16.453  1.00 36.32 ? 237 LYS A C     1 
ATOM   1818 O O     . LYS A 1 237 ? -29.534 65.157  17.603  1.00 36.81 ? 237 LYS A O     1 
ATOM   1819 C CB    . LYS A 1 237 ? -30.122 63.433  15.129  1.00 36.72 ? 237 LYS A CB    1 
ATOM   1820 C CG    . LYS A 1 237 ? -30.987 64.279  14.217  1.00 38.71 ? 237 LYS A CG    1 
ATOM   1821 C CD    . LYS A 1 237 ? -32.445 63.920  14.467  1.00 40.69 ? 237 LYS A CD    1 
ATOM   1822 C CE    . LYS A 1 237 ? -33.322 64.390  13.324  1.00 42.48 ? 237 LYS A CE    1 
ATOM   1823 N NZ    . LYS A 1 237 ? -34.754 64.225  13.704  1.00 44.51 ? 237 LYS A NZ    1 
ATOM   1824 N N     . ILE A 1 238 ? -28.588 66.465  16.067  1.00 35.98 ? 238 ILE A N     1 
ATOM   1825 C CA    . ILE A 1 238 ? -28.736 67.688  16.851  1.00 35.63 ? 238 ILE A CA    1 
ATOM   1826 C C     . ILE A 1 238 ? -29.720 68.608  16.140  1.00 35.60 ? 238 ILE A C     1 
ATOM   1827 O O     . ILE A 1 238 ? -29.587 68.876  14.949  1.00 35.57 ? 238 ILE A O     1 
ATOM   1828 C CB    . ILE A 1 238 ? -27.409 68.391  17.144  1.00 34.40 ? 238 ILE A CB    1 
ATOM   1829 C CG1   . ILE A 1 238 ? -26.552 67.538  18.080  1.00 33.21 ? 238 ILE A CG1   1 
ATOM   1830 C CG2   . ILE A 1 238 ? -27.605 69.740  17.807  1.00 34.09 ? 238 ILE A CG2   1 
ATOM   1831 C CD1   . ILE A 1 238 ? -25.781 66.457  17.353  1.00 34.84 ? 238 ILE A CD1   1 
ATOM   1832 N N     . GLU A 1 239 ? -30.712 69.066  16.902  1.00 35.74 ? 239 GLU A N     1 
ATOM   1833 C CA    . GLU A 1 239 ? -31.772 69.861  16.302  1.00 36.30 ? 239 GLU A CA    1 
ATOM   1834 C C     . GLU A 1 239 ? -31.858 71.311  16.720  1.00 35.95 ? 239 GLU A C     1 
ATOM   1835 O O     . GLU A 1 239 ? -31.506 71.661  17.840  1.00 35.80 ? 239 GLU A O     1 
ATOM   1836 C CB    . GLU A 1 239 ? -33.121 69.166  16.552  1.00 38.84 ? 239 GLU A CB    1 
ATOM   1837 C CG    . GLU A 1 239 ? -33.870 68.960  15.246  1.00 42.65 ? 239 GLU A CG    1 
ATOM   1838 C CD    . GLU A 1 239 ? -34.609 67.642  15.167  1.00 44.70 ? 239 GLU A CD    1 
ATOM   1839 O OE1   . GLU A 1 239 ? -34.519 66.852  16.132  1.00 45.02 ? 239 GLU A OE1   1 
ATOM   1840 O OE2   . GLU A 1 239 ? -35.292 67.409  14.139  1.00 46.55 ? 239 GLU A OE2   1 
ATOM   1841 N N     . GLY A 1 240 ? -32.272 72.160  15.777  1.00 35.62 ? 240 GLY A N     1 
ATOM   1842 C CA    . GLY A 1 240 ? -32.383 73.575  16.071  1.00 35.82 ? 240 GLY A CA    1 
ATOM   1843 C C     . GLY A 1 240 ? -31.380 74.441  15.330  1.00 35.82 ? 240 GLY A C     1 
ATOM   1844 O O     . GLY A 1 240 ? -30.166 74.278  15.427  1.00 36.10 ? 240 GLY A O     1 
ATOM   1845 N N     . ILE A 1 241 ? -31.912 75.406  14.590  1.00 35.54 ? 241 ILE A N     1 
ATOM   1846 C CA    . ILE A 1 241 ? -31.110 76.364  13.842  1.00 35.33 ? 241 ILE A CA    1 
ATOM   1847 C C     . ILE A 1 241 ? -30.048 77.006  14.709  1.00 35.86 ? 241 ILE A C     1 
ATOM   1848 O O     . ILE A 1 241 ? -30.304 77.326  15.876  1.00 36.29 ? 241 ILE A O     1 
ATOM   1849 C CB    . ILE A 1 241 ? -32.079 77.356  13.174  1.00 32.85 ? 241 ILE A CB    1 
ATOM   1850 C CG1   . ILE A 1 241 ? -32.536 76.624  11.913  1.00 32.60 ? 241 ILE A CG1   1 
ATOM   1851 C CG2   . ILE A 1 241 ? -31.470 78.708  12.914  1.00 31.96 ? 241 ILE A CG2   1 
ATOM   1852 C CD1   . ILE A 1 241 ? -33.557 77.269  11.028  1.00 33.38 ? 241 ILE A CD1   1 
ATOM   1853 N N     . ASP A 1 242 ? -28.790 76.910  14.278  1.00 35.74 ? 242 ASP A N     1 
ATOM   1854 C CA    . ASP A 1 242 ? -27.650 77.396  15.031  1.00 35.68 ? 242 ASP A CA    1 
ATOM   1855 C C     . ASP A 1 242 ? -27.534 76.739  16.400  1.00 35.64 ? 242 ASP A C     1 
ATOM   1856 O O     . ASP A 1 242 ? -26.922 77.284  17.314  1.00 35.42 ? 242 ASP A O     1 
ATOM   1857 C CB    . ASP A 1 242 ? -27.617 78.910  15.186  1.00 34.41 ? 242 ASP A CB    1 
ATOM   1858 C CG    . ASP A 1 242 ? -27.229 79.626  13.913  1.00 34.66 ? 242 ASP A CG    1 
ATOM   1859 O OD1   . ASP A 1 242 ? -27.685 80.787  13.849  1.00 35.33 ? 242 ASP A OD1   1 
ATOM   1860 O OD2   . ASP A 1 242 ? -26.536 79.034  13.065  1.00 34.88 ? 242 ASP A OD2   1 
ATOM   1861 N N     . ALA A 1 243 ? -27.875 75.461  16.485  1.00 36.20 ? 243 ALA A N     1 
ATOM   1862 C CA    . ALA A 1 243 ? -27.720 74.717  17.725  1.00 37.19 ? 243 ALA A CA    1 
ATOM   1863 C C     . ALA A 1 243 ? -26.244 74.567  18.094  1.00 37.90 ? 243 ALA A C     1 
ATOM   1864 O O     . ALA A 1 243 ? -25.370 74.531  17.230  1.00 38.44 ? 243 ALA A O     1 
ATOM   1865 C CB    . ALA A 1 243 ? -28.287 73.311  17.596  1.00 34.99 ? 243 ALA A CB    1 
ATOM   1866 N N     . THR A 1 244 ? -25.997 74.463  19.391  1.00 38.31 ? 244 THR A N     1 
ATOM   1867 C CA    . THR A 1 244 ? -24.647 74.156  19.883  1.00 38.52 ? 244 THR A CA    1 
ATOM   1868 C C     . THR A 1 244 ? -24.710 72.740  20.454  1.00 38.22 ? 244 THR A C     1 
ATOM   1869 O O     . THR A 1 244 ? -25.800 72.152  20.496  1.00 38.07 ? 244 THR A O     1 
ATOM   1870 C CB    . THR A 1 244 ? -24.205 75.149  20.960  1.00 40.17 ? 244 THR A CB    1 
ATOM   1871 O OG1   . THR A 1 244 ? -25.191 75.205  22.000  1.00 42.50 ? 244 THR A OG1   1 
ATOM   1872 C CG2   . THR A 1 244 ? -24.134 76.555  20.387  1.00 40.80 ? 244 THR A CG2   1 
ATOM   1873 N N     . GLY A 1 245 ? -23.593 72.137  20.822  1.00 38.06 ? 245 GLY A N     1 
ATOM   1874 C CA    . GLY A 1 245 ? -23.672 70.762  21.330  1.00 38.07 ? 245 GLY A CA    1 
ATOM   1875 C C     . GLY A 1 245 ? -23.174 69.794  20.269  1.00 38.11 ? 245 GLY A C     1 
ATOM   1876 O O     . GLY A 1 245 ? -22.483 68.826  20.593  1.00 38.78 ? 245 GLY A O     1 
ATOM   1877 N N     . GLY A 1 246 ? -23.470 70.066  19.005  1.00 37.85 ? 246 GLY A N     1 
ATOM   1878 C CA    . GLY A 1 246 ? -22.896 69.258  17.923  1.00 37.87 ? 246 GLY A CA    1 
ATOM   1879 C C     . GLY A 1 246 ? -21.499 69.801  17.600  1.00 37.67 ? 246 GLY A C     1 
ATOM   1880 O O     . GLY A 1 246 ? -20.703 70.095  18.493  1.00 37.74 ? 246 GLY A O     1 
ATOM   1881 N N     . ASN A 1 247 ? -21.237 69.981  16.307  1.00 37.38 ? 247 ASN A N     1 
ATOM   1882 C CA    . ASN A 1 247 ? -19.981 70.589  15.887  1.00 37.33 ? 247 ASN A CA    1 
ATOM   1883 C C     . ASN A 1 247 ? -19.853 72.004  16.435  1.00 37.44 ? 247 ASN A C     1 
ATOM   1884 O O     . ASN A 1 247 ? -18.770 72.448  16.795  1.00 37.50 ? 247 ASN A O     1 
ATOM   1885 C CB    . ASN A 1 247 ? -19.882 70.587  14.362  1.00 35.94 ? 247 ASN A CB    1 
ATOM   1886 C CG    . ASN A 1 247 ? -18.756 71.463  13.848  1.00 35.67 ? 247 ASN A CG    1 
ATOM   1887 O OD1   . ASN A 1 247 ? -17.621 70.991  13.733  1.00 36.69 ? 247 ASN A OD1   1 
ATOM   1888 N ND2   . ASN A 1 247 ? -19.076 72.716  13.570  1.00 33.85 ? 247 ASN A ND2   1 
ATOM   1889 N N     . ASN A 1 248 ? -20.937 72.762  16.464  1.00 38.02 ? 248 ASN A N     1 
ATOM   1890 C CA    . ASN A 1 248 ? -20.911 74.158  16.859  1.00 38.75 ? 248 ASN A CA    1 
ATOM   1891 C C     . ASN A 1 248 ? -20.736 74.351  18.348  1.00 39.24 ? 248 ASN A C     1 
ATOM   1892 O O     . ASN A 1 248 ? -21.674 74.591  19.110  1.00 39.52 ? 248 ASN A O     1 
ATOM   1893 C CB    . ASN A 1 248 ? -22.158 74.862  16.319  1.00 39.36 ? 248 ASN A CB    1 
ATOM   1894 C CG    . ASN A 1 248 ? -22.233 76.281  16.855  1.00 40.72 ? 248 ASN A CG    1 
ATOM   1895 O OD1   . ASN A 1 248 ? -21.187 76.896  17.058  1.00 42.40 ? 248 ASN A OD1   1 
ATOM   1896 N ND2   . ASN A 1 248 ? -23.453 76.721  17.112  1.00 41.29 ? 248 ASN A ND2   1 
ATOM   1897 N N     . GLN A 1 249 ? -19.510 74.222  18.834  1.00 39.90 ? 249 GLN A N     1 
ATOM   1898 C CA    . GLN A 1 249 ? -19.158 74.375  20.236  1.00 40.76 ? 249 GLN A CA    1 
ATOM   1899 C C     . GLN A 1 249 ? -17.976 75.336  20.397  1.00 41.15 ? 249 GLN A C     1 
ATOM   1900 O O     . GLN A 1 249 ? -17.149 75.524  19.493  1.00 41.22 ? 249 GLN A O     1 
ATOM   1901 C CB    . GLN A 1 249 ? -18.825 73.034  20.884  1.00 42.49 ? 249 GLN A CB    1 
ATOM   1902 C CG    . GLN A 1 249 ? -19.970 72.039  20.965  1.00 46.55 ? 249 GLN A CG    1 
ATOM   1903 C CD    . GLN A 1 249 ? -19.588 70.744  21.649  1.00 49.04 ? 249 GLN A CD    1 
ATOM   1904 O OE1   . GLN A 1 249 ? -19.650 70.618  22.879  1.00 50.92 ? 249 GLN A OE1   1 
ATOM   1905 N NE2   . GLN A 1 249 ? -19.158 69.738  20.890  1.00 50.44 ? 249 GLN A NE2   1 
ATOM   1906 N N     . PRO A 1 250 ? -17.937 76.016  21.543  1.00 41.08 ? 250 PRO A N     1 
ATOM   1907 C CA    . PRO A 1 250 ? -16.864 76.948  21.870  1.00 41.09 ? 250 PRO A CA    1 
ATOM   1908 C C     . PRO A 1 250 ? -15.599 76.173  22.199  1.00 41.52 ? 250 PRO A C     1 
ATOM   1909 O O     . PRO A 1 250 ? -15.409 75.799  23.363  1.00 42.16 ? 250 PRO A O     1 
ATOM   1910 C CB    . PRO A 1 250 ? -17.407 77.586  23.148  1.00 40.84 ? 250 PRO A CB    1 
ATOM   1911 C CG    . PRO A 1 250 ? -18.074 76.455  23.852  1.00 41.04 ? 250 PRO A CG    1 
ATOM   1912 C CD    . PRO A 1 250 ? -18.680 75.603  22.767  1.00 41.14 ? 250 PRO A CD    1 
ATOM   1913 N N     . ASN A 1 251 ? -14.754 75.846  21.228  1.00 41.40 ? 251 ASN A N     1 
ATOM   1914 C CA    . ASN A 1 251 ? -13.540 75.094  21.551  1.00 41.09 ? 251 ASN A CA    1 
ATOM   1915 C C     . ASN A 1 251 ? -12.586 75.102  20.374  1.00 40.92 ? 251 ASN A C     1 
ATOM   1916 O O     . ASN A 1 251 ? -12.931 75.654  19.323  1.00 41.31 ? 251 ASN A O     1 
ATOM   1917 C CB    . ASN A 1 251 ? -13.924 73.724  22.068  1.00 42.53 ? 251 ASN A CB    1 
ATOM   1918 C CG    . ASN A 1 251 ? -14.641 72.886  21.030  1.00 45.47 ? 251 ASN A CG    1 
ATOM   1919 O OD1   . ASN A 1 251 ? -15.099 73.451  20.027  1.00 46.98 ? 251 ASN A OD1   1 
ATOM   1920 N ND2   . ASN A 1 251 ? -14.744 71.579  21.257  1.00 46.02 ? 251 ASN A ND2   1 
ATOM   1921 N N     . ILE A 1 252 ? -11.372 74.593  20.549  1.00 40.45 ? 252 ILE A N     1 
ATOM   1922 C CA    . ILE A 1 252 ? -10.384 74.663  19.462  1.00 40.16 ? 252 ILE A CA    1 
ATOM   1923 C C     . ILE A 1 252 ? -10.836 73.810  18.287  1.00 38.91 ? 252 ILE A C     1 
ATOM   1924 O O     . ILE A 1 252 ? -11.256 72.668  18.483  1.00 38.91 ? 252 ILE A O     1 
ATOM   1925 C CB    . ILE A 1 252 ? -8.977  74.313  19.976  1.00 42.20 ? 252 ILE A CB    1 
ATOM   1926 C CG1   . ILE A 1 252 ? -8.393  75.477  20.782  1.00 43.30 ? 252 ILE A CG1   1 
ATOM   1927 C CG2   . ILE A 1 252 ? -7.992  74.001  18.857  1.00 42.91 ? 252 ILE A CG2   1 
ATOM   1928 C CD1   . ILE A 1 252 ? -9.193  75.951  21.976  1.00 45.92 ? 252 ILE A CD1   1 
ATOM   1929 N N     . PRO A 1 253 ? -11.004 74.444  17.134  1.00 37.81 ? 253 PRO A N     1 
ATOM   1930 C CA    . PRO A 1 253 ? -11.368 73.697  15.935  1.00 37.46 ? 253 PRO A CA    1 
ATOM   1931 C C     . PRO A 1 253 ? -10.137 72.892  15.538  1.00 36.97 ? 253 PRO A C     1 
ATOM   1932 O O     . PRO A 1 253 ? -9.063  73.120  16.093  1.00 36.79 ? 253 PRO A O     1 
ATOM   1933 C CB    . PRO A 1 253 ? -11.732 74.782  14.938  1.00 37.59 ? 253 PRO A CB    1 
ATOM   1934 C CG    . PRO A 1 253 ? -10.848 75.919  15.323  1.00 37.81 ? 253 PRO A CG    1 
ATOM   1935 C CD    . PRO A 1 253 ? -10.623 75.827  16.812  1.00 37.66 ? 253 PRO A CD    1 
ATOM   1936 N N     . ASP A 1 254 ? -10.289 71.998  14.575  1.00 36.40 ? 254 ASP A N     1 
ATOM   1937 C CA    . ASP A 1 254 ? -9.209  71.131  14.121  1.00 35.30 ? 254 ASP A CA    1 
ATOM   1938 C C     . ASP A 1 254 ? -9.208  70.961  12.605  1.00 34.23 ? 254 ASP A C     1 
ATOM   1939 O O     . ASP A 1 254 ? -10.289 70.759  12.049  1.00 34.18 ? 254 ASP A O     1 
ATOM   1940 C CB    . ASP A 1 254 ? -9.461  69.770  14.786  1.00 37.25 ? 254 ASP A CB    1 
ATOM   1941 C CG    . ASP A 1 254 ? -8.443  68.725  14.386  1.00 39.65 ? 254 ASP A CG    1 
ATOM   1942 O OD1   . ASP A 1 254 ? -7.387  68.632  15.050  1.00 40.71 ? 254 ASP A OD1   1 
ATOM   1943 O OD2   . ASP A 1 254 ? -8.676  67.983  13.406  1.00 40.86 ? 254 ASP A OD2   1 
ATOM   1944 N N     . ILE A 1 255 ? -8.044  70.833  11.964  1.00 33.03 ? 255 ILE A N     1 
ATOM   1945 C CA    . ILE A 1 255 ? -8.041  70.735  10.512  1.00 31.78 ? 255 ILE A CA    1 
ATOM   1946 C C     . ILE A 1 255 ? -8.239  69.325  10.003  1.00 31.20 ? 255 ILE A C     1 
ATOM   1947 O O     . ILE A 1 255 ? -9.240  69.041  9.323   1.00 31.07 ? 255 ILE A O     1 
ATOM   1948 C CB    . ILE A 1 255 ? -6.869  71.458  9.833   1.00 31.72 ? 255 ILE A CB    1 
ATOM   1949 C CG1   . ILE A 1 255 ? -6.623  72.868  10.383  1.00 31.37 ? 255 ILE A CG1   1 
ATOM   1950 C CG2   . ILE A 1 255 ? -7.013  71.529  8.316   1.00 29.13 ? 255 ILE A CG2   1 
ATOM   1951 C CD1   . ILE A 1 255 ? -7.804  73.792  10.424  1.00 32.66 ? 255 ILE A CD1   1 
ATOM   1952 N N     . PRO A 1 256 ? -7.448  68.348  10.434  1.00 30.46 ? 256 PRO A N     1 
ATOM   1953 C CA    . PRO A 1 256 ? -7.522  66.973  9.964   1.00 30.01 ? 256 PRO A CA    1 
ATOM   1954 C C     . PRO A 1 256 ? -8.854  66.273  10.149  1.00 29.57 ? 256 PRO A C     1 
ATOM   1955 O O     . PRO A 1 256 ? -9.308  65.472  9.318   1.00 29.53 ? 256 PRO A O     1 
ATOM   1956 C CB    . PRO A 1 256 ? -6.398  66.239  10.694  1.00 29.76 ? 256 PRO A CB    1 
ATOM   1957 C CG    . PRO A 1 256 ? -6.081  67.101  11.857  1.00 29.83 ? 256 PRO A CG    1 
ATOM   1958 C CD    . PRO A 1 256 ? -6.328  68.522  11.388  1.00 30.17 ? 256 PRO A CD    1 
ATOM   1959 N N     . ALA A 1 257 ? -9.623  66.677  11.155  1.00 28.91 ? 257 ALA A N     1 
ATOM   1960 C CA    . ALA A 1 257 ? -10.999 66.282  11.375  1.00 28.16 ? 257 ALA A CA    1 
ATOM   1961 C C     . ALA A 1 257 ? -11.861 66.500  10.139  1.00 27.65 ? 257 ALA A C     1 
ATOM   1962 O O     . ALA A 1 257 ? -12.595 65.616  9.702   1.00 27.49 ? 257 ALA A O     1 
ATOM   1963 C CB    . ALA A 1 257 ? -11.610 67.073  12.525  1.00 26.67 ? 257 ALA A CB    1 
ATOM   1964 N N     . HIS A 1 258 ? -11.646 67.590  9.422   1.00 27.37 ? 258 HIS A N     1 
ATOM   1965 C CA    . HIS A 1 258 ? -12.325 67.877  8.173   1.00 27.23 ? 258 HIS A CA    1 
ATOM   1966 C C     . HIS A 1 258 ? -12.034 66.825  7.114   1.00 27.91 ? 258 HIS A C     1 
ATOM   1967 O O     . HIS A 1 258 ? -12.834 66.655  6.190   1.00 28.25 ? 258 HIS A O     1 
ATOM   1968 C CB    . HIS A 1 258 ? -11.837 69.247  7.691   1.00 24.96 ? 258 HIS A CB    1 
ATOM   1969 C CG    . HIS A 1 258 ? -12.540 69.762  6.481   1.00 23.13 ? 258 HIS A CG    1 
ATOM   1970 N ND1   . HIS A 1 258 ? -13.862 70.120  6.477   1.00 21.61 ? 258 HIS A ND1   1 
ATOM   1971 C CD2   . HIS A 1 258 ? -12.072 69.976  5.224   1.00 22.69 ? 258 HIS A CD2   1 
ATOM   1972 C CE1   . HIS A 1 258 ? -14.198 70.527  5.269   1.00 22.31 ? 258 HIS A CE1   1 
ATOM   1973 N NE2   . HIS A 1 258 ? -13.130 70.454  4.490   1.00 22.93 ? 258 HIS A NE2   1 
ATOM   1974 N N     . LEU A 1 259 ? -10.897 66.147  7.180   1.00 28.21 ? 259 LEU A N     1 
ATOM   1975 C CA    . LEU A 1 259 ? -10.479 65.177  6.201   1.00 28.83 ? 259 LEU A CA    1 
ATOM   1976 C C     . LEU A 1 259 ? -11.022 63.793  6.500   1.00 29.54 ? 259 LEU A C     1 
ATOM   1977 O O     . LEU A 1 259 ? -10.820 62.885  5.688   1.00 30.08 ? 259 LEU A O     1 
ATOM   1978 C CB    . LEU A 1 259 ? -8.959  65.080  6.160   1.00 29.29 ? 259 LEU A CB    1 
ATOM   1979 C CG    . LEU A 1 259 ? -8.094  65.894  5.214   1.00 28.60 ? 259 LEU A CG    1 
ATOM   1980 C CD1   . LEU A 1 259 ? -8.881  67.006  4.545   1.00 30.13 ? 259 LEU A CD1   1 
ATOM   1981 C CD2   . LEU A 1 259 ? -6.928  66.476  6.009   1.00 29.60 ? 259 LEU A CD2   1 
ATOM   1982 N N     . TRP A 1 260 ? -11.626 63.595  7.662   1.00 30.04 ? 260 TRP A N     1 
ATOM   1983 C CA    . TRP A 1 260 ? -12.105 62.270  8.047   1.00 29.92 ? 260 TRP A CA    1 
ATOM   1984 C C     . TRP A 1 260 ? -13.611 62.139  8.158   1.00 29.85 ? 260 TRP A C     1 
ATOM   1985 O O     . TRP A 1 260 ? -14.172 62.285  9.238   1.00 30.30 ? 260 TRP A O     1 
ATOM   1986 C CB    . TRP A 1 260 ? -11.463 61.904  9.403   1.00 30.00 ? 260 TRP A CB    1 
ATOM   1987 C CG    . TRP A 1 260 ? -11.708 60.447  9.679   1.00 30.94 ? 260 TRP A CG    1 
ATOM   1988 C CD1   . TRP A 1 260 ? -12.625 59.938  10.549  1.00 31.19 ? 260 TRP A CD1   1 
ATOM   1989 C CD2   . TRP A 1 260 ? -11.086 59.330  9.046   1.00 30.89 ? 260 TRP A CD2   1 
ATOM   1990 N NE1   . TRP A 1 260 ? -12.602 58.568  10.494  1.00 31.58 ? 260 TRP A NE1   1 
ATOM   1991 C CE2   . TRP A 1 260 ? -11.670 58.170  9.577   1.00 31.14 ? 260 TRP A CE2   1 
ATOM   1992 C CE3   . TRP A 1 260 ? -10.092 59.195  8.078   1.00 33.04 ? 260 TRP A CE3   1 
ATOM   1993 C CZ2   . TRP A 1 260 ? -11.304 56.882  9.189   1.00 31.97 ? 260 TRP A CZ2   1 
ATOM   1994 C CZ3   . TRP A 1 260 ? -9.725  57.914  7.682   1.00 34.58 ? 260 TRP A CZ3   1 
ATOM   1995 C CH2   . TRP A 1 260 ? -10.327 56.771  8.238   1.00 33.35 ? 260 TRP A CH2   1 
ATOM   1996 N N     . TYR A 1 261 ? -14.330 61.856  7.084   1.00 29.73 ? 261 TYR A N     1 
ATOM   1997 C CA    . TYR A 1 261 ? -15.776 61.688  7.104   1.00 29.49 ? 261 TYR A CA    1 
ATOM   1998 C C     . TYR A 1 261 ? -16.121 60.291  6.621   1.00 29.40 ? 261 TYR A C     1 
ATOM   1999 O O     . TYR A 1 261 ? -16.099 60.016  5.422   1.00 28.84 ? 261 TYR A O     1 
ATOM   2000 C CB    . TYR A 1 261 ? -16.483 62.687  6.172   1.00 29.01 ? 261 TYR A CB    1 
ATOM   2001 C CG    . TYR A 1 261 ? -16.688 63.984  6.921   1.00 28.12 ? 261 TYR A CG    1 
ATOM   2002 C CD1   . TYR A 1 261 ? -15.666 64.917  7.036   1.00 27.26 ? 261 TYR A CD1   1 
ATOM   2003 C CD2   . TYR A 1 261 ? -17.905 64.223  7.534   1.00 28.41 ? 261 TYR A CD2   1 
ATOM   2004 C CE1   . TYR A 1 261 ? -15.866 66.089  7.735   1.00 26.74 ? 261 TYR A CE1   1 
ATOM   2005 C CE2   . TYR A 1 261 ? -18.104 65.406  8.240   1.00 28.17 ? 261 TYR A CE2   1 
ATOM   2006 C CZ    . TYR A 1 261 ? -17.079 66.326  8.334   1.00 26.83 ? 261 TYR A CZ    1 
ATOM   2007 O OH    . TYR A 1 261 ? -17.260 67.470  9.052   1.00 26.13 ? 261 TYR A OH    1 
ATOM   2008 N N     . PHE A 1 262 ? -16.173 59.343  7.539   1.00 29.64 ? 262 PHE A N     1 
ATOM   2009 C CA    . PHE A 1 262 ? -16.299 57.923  7.264   1.00 30.30 ? 262 PHE A CA    1 
ATOM   2010 C C     . PHE A 1 262 ? -14.969 57.336  6.822   1.00 30.71 ? 262 PHE A C     1 
ATOM   2011 O O     . PHE A 1 262 ? -14.575 56.277  7.309   1.00 31.36 ? 262 PHE A O     1 
ATOM   2012 C CB    . PHE A 1 262 ? -17.457 57.540  6.359   1.00 30.00 ? 262 PHE A CB    1 
ATOM   2013 C CG    . PHE A 1 262 ? -18.788 57.873  6.989   1.00 30.87 ? 262 PHE A CG    1 
ATOM   2014 C CD1   . PHE A 1 262 ? -19.390 56.961  7.829   1.00 29.94 ? 262 PHE A CD1   1 
ATOM   2015 C CD2   . PHE A 1 262 ? -19.427 59.088  6.752   1.00 30.04 ? 262 PHE A CD2   1 
ATOM   2016 C CE1   . PHE A 1 262 ? -20.602 57.268  8.414   1.00 31.38 ? 262 PHE A CE1   1 
ATOM   2017 C CE2   . PHE A 1 262 ? -20.632 59.391  7.330   1.00 28.52 ? 262 PHE A CE2   1 
ATOM   2018 C CZ    . PHE A 1 262 ? -21.226 58.480  8.166   1.00 29.87 ? 262 PHE A CZ    1 
ATOM   2019 N N     . GLY A 1 263 ? -14.195 57.975  5.981   1.00 30.69 ? 263 GLY A N     1 
ATOM   2020 C CA    . GLY A 1 263 ? -12.862 57.663  5.552   1.00 30.35 ? 263 GLY A CA    1 
ATOM   2021 C C     . GLY A 1 263 ? -12.185 58.959  5.093   1.00 30.35 ? 263 GLY A C     1 
ATOM   2022 O O     . GLY A 1 263 ? -12.749 60.043  5.215   1.00 30.54 ? 263 GLY A O     1 
ATOM   2023 N N     . LEU A 1 264 ? -10.952 58.840  4.627   1.00 30.44 ? 264 LEU A N     1 
ATOM   2024 C CA    . LEU A 1 264 ? -10.202 60.003  4.161   1.00 29.90 ? 264 LEU A CA    1 
ATOM   2025 C C     . LEU A 1 264 ? -10.951 60.601  2.976   1.00 29.23 ? 264 LEU A C     1 
ATOM   2026 O O     . LEU A 1 264 ? -11.494 59.821  2.212   1.00 28.48 ? 264 LEU A O     1 
ATOM   2027 C CB    . LEU A 1 264 ? -8.775  59.650  3.782   1.00 30.80 ? 264 LEU A CB    1 
ATOM   2028 C CG    . LEU A 1 264 ? -7.725  59.656  4.893   1.00 32.27 ? 264 LEU A CG    1 
ATOM   2029 C CD1   . LEU A 1 264 ? -6.348  59.647  4.237   1.00 33.58 ? 264 LEU A CD1   1 
ATOM   2030 C CD2   . LEU A 1 264 ? -7.872  60.845  5.835   1.00 33.28 ? 264 LEU A CD2   1 
ATOM   2031 N N     . ILE A 1 265 ? -11.228 61.891  3.060   1.00 29.18 ? 265 ILE A N     1 
ATOM   2032 C CA    . ILE A 1 265 ? -12.024 62.540  2.020   1.00 29.05 ? 265 ILE A CA    1 
ATOM   2033 C C     . ILE A 1 265 ? -11.371 63.883  1.702   1.00 29.11 ? 265 ILE A C     1 
ATOM   2034 O O     . ILE A 1 265 ? -10.748 64.495  2.575   1.00 28.93 ? 265 ILE A O     1 
ATOM   2035 C CB    . ILE A 1 265 ? -13.471 62.693  2.479   1.00 28.86 ? 265 ILE A CB    1 
ATOM   2036 C CG1   . ILE A 1 265 ? -14.337 63.295  1.368   1.00 29.94 ? 265 ILE A CG1   1 
ATOM   2037 C CG2   . ILE A 1 265 ? -13.529 63.507  3.762   1.00 28.34 ? 265 ILE A CG2   1 
ATOM   2038 C CD1   . ILE A 1 265 ? -15.796 62.832  1.521   1.00 31.00 ? 265 ILE A CD1   1 
ATOM   2039 N N     . GLY A 1 266 ? -11.136 64.102  0.411   1.00 28.97 ? 266 GLY A N     1 
ATOM   2040 C CA    . GLY A 1 266 ? -10.495 65.306  -0.073  1.00 28.91 ? 266 GLY A CA    1 
ATOM   2041 C C     . GLY A 1 266 ? -9.046  65.067  -0.461  1.00 29.27 ? 266 GLY A C     1 
ATOM   2042 O O     . GLY A 1 266 ? -8.417  65.864  -1.162  1.00 29.12 ? 266 GLY A O     1 
ATOM   2043 N N     . THR A 1 267 ? -8.509  63.906  -0.084  1.00 29.24 ? 267 THR A N     1 
ATOM   2044 C CA    . THR A 1 267 ? -7.104  63.606  -0.295  1.00 29.22 ? 267 THR A CA    1 
ATOM   2045 C C     . THR A 1 267 ? -6.900  62.717  -1.514  1.00 29.39 ? 267 THR A C     1 
ATOM   2046 O O     . THR A 1 267 ? -5.807  62.169  -1.723  1.00 29.62 ? 267 THR A O     1 
ATOM   2047 C CB    . THR A 1 267 ? -6.599  62.791  0.921   1.00 28.22 ? 267 THR A CB    1 
ATOM   2048 O OG1   . THR A 1 267 ? -7.379  61.598  0.885   1.00 28.61 ? 267 THR A OG1   1 
ATOM   2049 C CG2   . THR A 1 267 ? -6.830  63.574  2.186   1.00 28.87 ? 267 THR A CG2   1 
ATOM   2050 N N     . CYS A 1 268 ? -7.966  62.499  -2.276  1.00 29.01 ? 268 CYS A N     1 
ATOM   2051 C CA    . CYS A 1 268 ? -7.850  61.621  -3.422  1.00 29.43 ? 268 CYS A CA    1 
ATOM   2052 C C     . CYS A 1 268 ? -7.097  62.271  -4.566  1.00 30.45 ? 268 CYS A C     1 
ATOM   2053 O O     . CYS A 1 268 ? -7.700  63.090  -5.256  1.00 31.18 ? 268 CYS A O     1 
ATOM   2054 C CB    . CYS A 1 268 ? -9.186  61.083  -3.984  1.00 25.60 ? 268 CYS A CB    1 
ATOM   2055 S SG    . CYS A 1 268 ? -8.926  59.915  -5.341  1.00 23.29 ? 268 CYS A SG    1 
ATOM   2056 N N     . LEU A 1 269 ? -5.879  61.847  -4.830  1.00 31.73 ? 269 LEU A N     1 
ATOM   2057 C CA    . LEU A 1 269 ? -5.125  62.354  -5.969  1.00 33.12 ? 269 LEU A CA    1 
ATOM   2058 C C     . LEU A 1 269 ? -5.871  62.107  -7.287  1.00 33.63 ? 269 LEU A C     1 
ATOM   2059 O O     . LEU A 1 269 ? -5.987  63.123  -8.032  1.00 37.32 ? 269 LEU A O     1 
ATOM   2060 C CB    . LEU A 1 269 ? -3.735  61.719  -6.054  1.00 34.87 ? 269 LEU A CB    1 
ATOM   2061 C CG    . LEU A 1 269 ? -2.516  62.568  -5.693  1.00 35.61 ? 269 LEU A CG    1 
ATOM   2062 C CD1   . LEU A 1 269 ? -2.657  64.017  -6.149  1.00 36.31 ? 269 LEU A CD1   1 
ATOM   2063 C CD2   . LEU A 1 269 ? -2.206  62.476  -4.213  1.00 35.30 ? 269 LEU A CD2   1 
ATOM   2064 N N     . GLU B 1 1   ? -11.986 111.341 11.730  1.00 41.93 ? 1   GLU B N     1 
ATOM   2065 C CA    . GLU B 1 1   ? -10.522 111.549 11.766  1.00 41.22 ? 1   GLU B CA    1 
ATOM   2066 C C     . GLU B 1 1   ? -9.875  111.629 10.406  1.00 40.29 ? 1   GLU B C     1 
ATOM   2067 O O     . GLU B 1 1   ? -8.672  111.356 10.313  1.00 41.44 ? 1   GLU B O     1 
ATOM   2068 C CB    . GLU B 1 1   ? -9.903  110.439 12.610  1.00 46.36 ? 1   GLU B CB    1 
ATOM   2069 C CG    . GLU B 1 1   ? -9.522  110.910 14.001  1.00 53.59 ? 1   GLU B CG    1 
ATOM   2070 C CD    . GLU B 1 1   ? -8.023  111.120 14.158  1.00 58.16 ? 1   GLU B CD    1 
ATOM   2071 O OE1   . GLU B 1 1   ? -7.693  111.279 15.362  1.00 61.07 ? 1   GLU B OE1   1 
ATOM   2072 O OE2   . GLU B 1 1   ? -7.235  111.105 13.183  1.00 59.89 ? 1   GLU B OE2   1 
ATOM   2073 N N     . VAL B 1 2   ? -10.576 112.036 9.359   1.00 38.83 ? 2   VAL B N     1 
ATOM   2074 C CA    . VAL B 1 2   ? -9.972  112.153 8.032   1.00 36.81 ? 2   VAL B CA    1 
ATOM   2075 C C     . VAL B 1 2   ? -10.806 113.052 7.138   1.00 36.06 ? 2   VAL B C     1 
ATOM   2076 O O     . VAL B 1 2   ? -12.031 113.068 7.218   1.00 35.57 ? 2   VAL B O     1 
ATOM   2077 C CB    . VAL B 1 2   ? -9.677  110.768 7.449   1.00 36.05 ? 2   VAL B CB    1 
ATOM   2078 C CG1   . VAL B 1 2   ? -10.191 110.544 6.031   1.00 36.97 ? 2   VAL B CG1   1 
ATOM   2079 C CG2   . VAL B 1 2   ? -8.174  110.478 7.461   1.00 34.59 ? 2   VAL B CG2   1 
ATOM   2080 N N     . SER B 1 3   ? -10.120 113.863 6.336   1.00 36.03 ? 3   SER B N     1 
ATOM   2081 C CA    . SER B 1 3   ? -10.846 114.734 5.418   1.00 36.63 ? 3   SER B CA    1 
ATOM   2082 C C     . SER B 1 3   ? -11.626 113.853 4.446   1.00 37.25 ? 3   SER B C     1 
ATOM   2083 O O     . SER B 1 3   ? -11.206 112.788 3.984   1.00 37.11 ? 3   SER B O     1 
ATOM   2084 C CB    . SER B 1 3   ? -9.907  115.679 4.692   1.00 36.62 ? 3   SER B CB    1 
ATOM   2085 O OG    . SER B 1 3   ? -9.263  115.024 3.619   1.00 39.10 ? 3   SER B OG    1 
ATOM   2086 N N     . GLN B 1 4   ? -12.777 114.379 4.032   1.00 37.94 ? 4   GLN B N     1 
ATOM   2087 C CA    . GLN B 1 4   ? -13.647 113.712 3.075   1.00 38.20 ? 4   GLN B CA    1 
ATOM   2088 C C     . GLN B 1 4   ? -12.873 113.504 1.778   1.00 38.19 ? 4   GLN B C     1 
ATOM   2089 O O     . GLN B 1 4   ? -12.994 112.454 1.135   1.00 38.58 ? 4   GLN B O     1 
ATOM   2090 C CB    . GLN B 1 4   ? -14.879 114.569 2.795   1.00 40.66 ? 4   GLN B CB    1 
ATOM   2091 C CG    . GLN B 1 4   ? -15.778 113.917 1.757   1.00 43.79 ? 4   GLN B CG    1 
ATOM   2092 C CD    . GLN B 1 4   ? -16.551 112.767 2.358   1.00 45.46 ? 4   GLN B CD    1 
ATOM   2093 O OE1   . GLN B 1 4   ? -16.552 111.661 1.824   1.00 46.85 ? 4   GLN B OE1   1 
ATOM   2094 N NE2   . GLN B 1 4   ? -17.202 113.057 3.481   1.00 47.64 ? 4   GLN B NE2   1 
ATOM   2095 N N     . ASP B 1 5   ? -12.010 114.453 1.431   1.00 37.65 ? 5   ASP B N     1 
ATOM   2096 C CA    . ASP B 1 5   ? -11.119 114.251 0.298   1.00 37.68 ? 5   ASP B CA    1 
ATOM   2097 C C     . ASP B 1 5   ? -10.199 113.054 0.470   1.00 36.34 ? 5   ASP B C     1 
ATOM   2098 O O     . ASP B 1 5   ? -10.209 112.143 -0.369  1.00 36.37 ? 5   ASP B O     1 
ATOM   2099 C CB    . ASP B 1 5   ? -10.282 115.509 0.050   1.00 44.91 ? 5   ASP B CB    1 
ATOM   2100 C CG    . ASP B 1 5   ? -11.189 116.601 -0.510  1.00 51.96 ? 5   ASP B CG    1 
ATOM   2101 O OD1   . ASP B 1 5   ? -11.100 116.673 -1.763  1.00 56.36 ? 5   ASP B OD1   1 
ATOM   2102 O OD2   . ASP B 1 5   ? -11.933 117.303 0.224   1.00 54.96 ? 5   ASP B OD2   1 
ATOM   2103 N N     . LEU B 1 6   ? -9.462  112.964 1.569   1.00 34.83 ? 6   LEU B N     1 
ATOM   2104 C CA    . LEU B 1 6   ? -8.605  111.807 1.752   1.00 33.69 ? 6   LEU B CA    1 
ATOM   2105 C C     . LEU B 1 6   ? -9.437  110.525 1.665   1.00 33.44 ? 6   LEU B C     1 
ATOM   2106 O O     . LEU B 1 6   ? -9.126  109.536 1.002   1.00 33.01 ? 6   LEU B O     1 
ATOM   2107 C CB    . LEU B 1 6   ? -7.916  111.860 3.110   1.00 32.00 ? 6   LEU B CB    1 
ATOM   2108 C CG    . LEU B 1 6   ? -6.417  112.122 3.157   1.00 31.08 ? 6   LEU B CG    1 
ATOM   2109 C CD1   . LEU B 1 6   ? -5.879  111.595 4.486   1.00 32.05 ? 6   LEU B CD1   1 
ATOM   2110 C CD2   . LEU B 1 6   ? -5.658  111.512 1.996   1.00 29.17 ? 6   LEU B CD2   1 
ATOM   2111 N N     . PHE B 1 7   ? -10.563 110.583 2.396   1.00 33.10 ? 7   PHE B N     1 
ATOM   2112 C CA    . PHE B 1 7   ? -11.456 109.443 2.478   1.00 32.72 ? 7   PHE B CA    1 
ATOM   2113 C C     . PHE B 1 7   ? -11.788 109.053 1.052   1.00 32.64 ? 7   PHE B C     1 
ATOM   2114 O O     . PHE B 1 7   ? -11.731 107.871 0.726   1.00 32.60 ? 7   PHE B O     1 
ATOM   2115 C CB    . PHE B 1 7   ? -12.729 109.765 3.271   1.00 32.54 ? 7   PHE B CB    1 
ATOM   2116 C CG    . PHE B 1 7   ? -13.650 108.578 3.322   1.00 30.77 ? 7   PHE B CG    1 
ATOM   2117 C CD1   . PHE B 1 7   ? -13.537 107.671 4.352   1.00 31.82 ? 7   PHE B CD1   1 
ATOM   2118 C CD2   . PHE B 1 7   ? -14.566 108.335 2.315   1.00 30.47 ? 7   PHE B CD2   1 
ATOM   2119 C CE1   . PHE B 1 7   ? -14.333 106.539 4.376   1.00 31.85 ? 7   PHE B CE1   1 
ATOM   2120 C CE2   . PHE B 1 7   ? -15.350 107.194 2.338   1.00 30.33 ? 7   PHE B CE2   1 
ATOM   2121 C CZ    . PHE B 1 7   ? -15.278 106.316 3.400   1.00 30.23 ? 7   PHE B CZ    1 
ATOM   2122 N N     . ASN B 1 8   ? -12.131 110.019 0.199   1.00 32.92 ? 8   ASN B N     1 
ATOM   2123 C CA    . ASN B 1 8   ? -12.468 109.635 -1.177  1.00 33.26 ? 8   ASN B CA    1 
ATOM   2124 C C     . ASN B 1 8   ? -11.330 108.931 -1.887  1.00 33.19 ? 8   ASN B C     1 
ATOM   2125 O O     . ASN B 1 8   ? -11.569 107.958 -2.609  1.00 33.39 ? 8   ASN B O     1 
ATOM   2126 C CB    . ASN B 1 8   ? -12.967 110.862 -1.931  1.00 35.74 ? 8   ASN B CB    1 
ATOM   2127 C CG    . ASN B 1 8   ? -14.257 111.345 -1.291  1.00 38.05 ? 8   ASN B CG    1 
ATOM   2128 O OD1   . ASN B 1 8   ? -14.849 110.661 -0.455  1.00 40.42 ? 8   ASN B OD1   1 
ATOM   2129 N ND2   . ASN B 1 8   ? -14.697 112.532 -1.677  1.00 39.62 ? 8   ASN B ND2   1 
ATOM   2130 N N     . GLN B 1 9   ? -10.109 109.432 -1.738  1.00 32.82 ? 9   GLN B N     1 
ATOM   2131 C CA    . GLN B 1 9   ? -8.942  108.838 -2.358  1.00 32.41 ? 9   GLN B CA    1 
ATOM   2132 C C     . GLN B 1 9   ? -8.638  107.455 -1.804  1.00 32.12 ? 9   GLN B C     1 
ATOM   2133 O O     . GLN B 1 9   ? -8.645  106.502 -2.596  1.00 32.06 ? 9   GLN B O     1 
ATOM   2134 C CB    . GLN B 1 9   ? -7.738  109.754 -2.178  1.00 35.29 ? 9   GLN B CB    1 
ATOM   2135 C CG    . GLN B 1 9   ? -7.817  111.038 -2.979  1.00 39.83 ? 9   GLN B CG    1 
ATOM   2136 C CD    . GLN B 1 9   ? -6.494  111.779 -2.931  1.00 42.27 ? 9   GLN B CD    1 
ATOM   2137 O OE1   . GLN B 1 9   ? -5.799  111.958 -3.932  1.00 45.55 ? 9   GLN B OE1   1 
ATOM   2138 N NE2   . GLN B 1 9   ? -6.117  112.234 -1.744  1.00 42.46 ? 9   GLN B NE2   1 
ATOM   2139 N N     . PHE B 1 10  ? -8.552  107.295 -0.478  1.00 31.41 ? 10  PHE B N     1 
ATOM   2140 C CA    . PHE B 1 10  ? -8.421  105.986 0.135   1.00 30.49 ? 10  PHE B CA    1 
ATOM   2141 C C     . PHE B 1 10  ? -9.393  104.977 -0.467  1.00 30.48 ? 10  PHE B C     1 
ATOM   2142 O O     . PHE B 1 10  ? -9.024  103.823 -0.713  1.00 30.97 ? 10  PHE B O     1 
ATOM   2143 C CB    . PHE B 1 10  ? -8.647  106.008 1.635   1.00 28.66 ? 10  PHE B CB    1 
ATOM   2144 C CG    . PHE B 1 10  ? -7.546  106.600 2.461   1.00 28.68 ? 10  PHE B CG    1 
ATOM   2145 C CD1   . PHE B 1 10  ? -6.437  107.179 1.862   1.00 28.47 ? 10  PHE B CD1   1 
ATOM   2146 C CD2   . PHE B 1 10  ? -7.638  106.625 3.847   1.00 27.98 ? 10  PHE B CD2   1 
ATOM   2147 C CE1   . PHE B 1 10  ? -5.417  107.727 2.612   1.00 27.07 ? 10  PHE B CE1   1 
ATOM   2148 C CE2   . PHE B 1 10  ? -6.631  107.205 4.596   1.00 28.63 ? 10  PHE B CE2   1 
ATOM   2149 C CZ    . PHE B 1 10  ? -5.516  107.749 3.985   1.00 27.09 ? 10  PHE B CZ    1 
ATOM   2150 N N     . ASN B 1 11  ? -10.634 105.365 -0.674  1.00 30.08 ? 11  ASN B N     1 
ATOM   2151 C CA    . ASN B 1 11  ? -11.589 104.476 -1.313  1.00 29.99 ? 11  ASN B CA    1 
ATOM   2152 C C     . ASN B 1 11  ? -11.235 104.181 -2.759  1.00 29.10 ? 11  ASN B C     1 
ATOM   2153 O O     . ASN B 1 11  ? -11.340 103.035 -3.182  1.00 29.02 ? 11  ASN B O     1 
ATOM   2154 C CB    . ASN B 1 11  ? -12.965 105.153 -1.218  1.00 33.80 ? 11  ASN B CB    1 
ATOM   2155 C CG    . ASN B 1 11  ? -14.053 104.118 -1.368  1.00 35.49 ? 11  ASN B CG    1 
ATOM   2156 O OD1   . ASN B 1 11  ? -14.712 103.808 -0.385  1.00 39.10 ? 11  ASN B OD1   1 
ATOM   2157 N ND2   . ASN B 1 11  ? -14.148 103.557 -2.556  1.00 37.00 ? 11  ASN B ND2   1 
ATOM   2158 N N     . LEU B 1 12  ? -10.992 105.203 -3.569  1.00 28.57 ? 12  LEU B N     1 
ATOM   2159 C CA    . LEU B 1 12  ? -10.752 105.038 -4.995  1.00 27.88 ? 12  LEU B CA    1 
ATOM   2160 C C     . LEU B 1 12  ? -9.573  104.112 -5.263  1.00 28.05 ? 12  LEU B C     1 
ATOM   2161 O O     . LEU B 1 12  ? -9.625  103.224 -6.110  1.00 27.96 ? 12  LEU B O     1 
ATOM   2162 C CB    . LEU B 1 12  ? -10.521 106.397 -5.671  1.00 24.98 ? 12  LEU B CB    1 
ATOM   2163 C CG    . LEU B 1 12  ? -10.083 106.323 -7.135  1.00 23.32 ? 12  LEU B CG    1 
ATOM   2164 C CD1   . LEU B 1 12  ? -11.136 105.553 -7.923  1.00 22.03 ? 12  LEU B CD1   1 
ATOM   2165 C CD2   . LEU B 1 12  ? -9.808  107.687 -7.742  1.00 21.76 ? 12  LEU B CD2   1 
ATOM   2166 N N     . PHE B 1 13  ? -8.462  104.313 -4.555  1.00 28.04 ? 13  PHE B N     1 
ATOM   2167 C CA    . PHE B 1 13  ? -7.295  103.463 -4.697  1.00 27.85 ? 13  PHE B CA    1 
ATOM   2168 C C     . PHE B 1 13  ? -7.423  102.085 -4.077  1.00 27.30 ? 13  PHE B C     1 
ATOM   2169 O O     . PHE B 1 13  ? -6.677  101.188 -4.503  1.00 27.24 ? 13  PHE B O     1 
ATOM   2170 C CB    . PHE B 1 13  ? -6.026  104.197 -4.233  1.00 30.12 ? 13  PHE B CB    1 
ATOM   2171 C CG    . PHE B 1 13  ? -5.760  105.402 -5.106  1.00 32.41 ? 13  PHE B CG    1 
ATOM   2172 C CD1   . PHE B 1 13  ? -5.719  106.678 -4.562  1.00 32.22 ? 13  PHE B CD1   1 
ATOM   2173 C CD2   . PHE B 1 13  ? -5.594  105.264 -6.479  1.00 31.84 ? 13  PHE B CD2   1 
ATOM   2174 C CE1   . PHE B 1 13  ? -5.485  107.779 -5.367  1.00 30.84 ? 13  PHE B CE1   1 
ATOM   2175 C CE2   . PHE B 1 13  ? -5.389  106.366 -7.283  1.00 30.71 ? 13  PHE B CE2   1 
ATOM   2176 C CZ    . PHE B 1 13  ? -5.351  107.626 -6.730  1.00 29.95 ? 13  PHE B CZ    1 
ATOM   2177 N N     . ALA B 1 14  ? -8.298  101.846 -3.099  1.00 26.34 ? 14  ALA B N     1 
ATOM   2178 C CA    . ALA B 1 14  ? -8.574  100.504 -2.605  1.00 25.21 ? 14  ALA B CA    1 
ATOM   2179 C C     . ALA B 1 14  ? -9.187  99.704  -3.759  1.00 25.21 ? 14  ALA B C     1 
ATOM   2180 O O     . ALA B 1 14  ? -8.776  98.607  -4.146  1.00 24.93 ? 14  ALA B O     1 
ATOM   2181 C CB    . ALA B 1 14  ? -9.515  100.512 -1.424  1.00 23.04 ? 14  ALA B CB    1 
ATOM   2182 N N     . GLN B 1 15  ? -10.091 100.354 -4.489  1.00 25.14 ? 15  GLN B N     1 
ATOM   2183 C CA    . GLN B 1 15  ? -10.691 99.757  -5.660  1.00 25.47 ? 15  GLN B CA    1 
ATOM   2184 C C     . GLN B 1 15  ? -9.712  99.508  -6.784  1.00 25.80 ? 15  GLN B C     1 
ATOM   2185 O O     . GLN B 1 15  ? -9.797  98.442  -7.411  1.00 26.71 ? 15  GLN B O     1 
ATOM   2186 C CB    . GLN B 1 15  ? -11.898 100.545 -6.147  1.00 26.03 ? 15  GLN B CB    1 
ATOM   2187 C CG    . GLN B 1 15  ? -13.085 100.372 -5.204  1.00 27.32 ? 15  GLN B CG    1 
ATOM   2188 C CD    . GLN B 1 15  ? -14.303 101.159 -5.624  1.00 27.44 ? 15  GLN B CD    1 
ATOM   2189 O OE1   . GLN B 1 15  ? -14.983 101.715 -4.767  1.00 27.85 ? 15  GLN B OE1   1 
ATOM   2190 N NE2   . GLN B 1 15  ? -14.606 101.235 -6.909  1.00 27.24 ? 15  GLN B NE2   1 
ATOM   2191 N N     . TYR B 1 16  ? -8.763  100.386 -7.065  1.00 25.48 ? 16  TYR B N     1 
ATOM   2192 C CA    . TYR B 1 16  ? -7.748  100.116 -8.079  1.00 24.83 ? 16  TYR B CA    1 
ATOM   2193 C C     . TYR B 1 16  ? -6.892  98.922  -7.660  1.00 25.00 ? 16  TYR B C     1 
ATOM   2194 O O     . TYR B 1 16  ? -6.476  98.105  -8.489  1.00 24.48 ? 16  TYR B O     1 
ATOM   2195 C CB    . TYR B 1 16  ? -6.865  101.331 -8.320  1.00 24.54 ? 16  TYR B CB    1 
ATOM   2196 C CG    . TYR B 1 16  ? -7.339  102.276 -9.392  1.00 23.92 ? 16  TYR B CG    1 
ATOM   2197 C CD1   . TYR B 1 16  ? -7.217  101.941 -10.733 1.00 23.41 ? 16  TYR B CD1   1 
ATOM   2198 C CD2   . TYR B 1 16  ? -7.909  103.498 -9.064  1.00 24.23 ? 16  TYR B CD2   1 
ATOM   2199 C CE1   . TYR B 1 16  ? -7.652  102.812 -11.711 1.00 23.99 ? 16  TYR B CE1   1 
ATOM   2200 C CE2   . TYR B 1 16  ? -8.357  104.380 -10.033 1.00 24.02 ? 16  TYR B CE2   1 
ATOM   2201 C CZ    . TYR B 1 16  ? -8.223  104.023 -11.358 1.00 24.27 ? 16  TYR B CZ    1 
ATOM   2202 O OH    . TYR B 1 16  ? -8.655  104.886 -12.342 1.00 23.90 ? 16  TYR B OH    1 
ATOM   2203 N N     . SER B 1 17  ? -6.589  98.825  -6.363  1.00 25.04 ? 17  SER B N     1 
ATOM   2204 C CA    . SER B 1 17  ? -5.864  97.695  -5.808  1.00 25.09 ? 17  SER B CA    1 
ATOM   2205 C C     . SER B 1 17  ? -6.629  96.392  -6.002  1.00 24.87 ? 17  SER B C     1 
ATOM   2206 O O     . SER B 1 17  ? -6.132  95.401  -6.514  1.00 24.82 ? 17  SER B O     1 
ATOM   2207 C CB    . SER B 1 17  ? -5.630  97.891  -4.306  1.00 24.90 ? 17  SER B CB    1 
ATOM   2208 O OG    . SER B 1 17  ? -4.745  98.988  -4.129  1.00 26.70 ? 17  SER B OG    1 
ATOM   2209 N N     . ALA B 1 18  ? -7.899  96.412  -5.623  1.00 24.96 ? 18  ALA B N     1 
ATOM   2210 C CA    . ALA B 1 18  ? -8.799  95.274  -5.744  1.00 24.30 ? 18  ALA B CA    1 
ATOM   2211 C C     . ALA B 1 18  ? -8.981  94.824  -7.180  1.00 24.01 ? 18  ALA B C     1 
ATOM   2212 O O     . ALA B 1 18  ? -8.905  93.646  -7.532  1.00 24.22 ? 18  ALA B O     1 
ATOM   2213 C CB    . ALA B 1 18  ? -10.133 95.667  -5.140  1.00 23.37 ? 18  ALA B CB    1 
ATOM   2214 N N     . ALA B 1 19  ? -9.094  95.763  -8.097  1.00 23.79 ? 19  ALA B N     1 
ATOM   2215 C CA    . ALA B 1 19  ? -9.170  95.494  -9.522  1.00 24.02 ? 19  ALA B CA    1 
ATOM   2216 C C     . ALA B 1 19  ? -7.988  94.742  -10.104 1.00 24.06 ? 19  ALA B C     1 
ATOM   2217 O O     . ALA B 1 19  ? -8.185  94.078  -11.123 1.00 24.04 ? 19  ALA B O     1 
ATOM   2218 C CB    . ALA B 1 19  ? -9.381  96.811  -10.274 1.00 23.64 ? 19  ALA B CB    1 
ATOM   2219 N N     . ALA B 1 20  ? -6.780  94.815  -9.565  1.00 24.20 ? 20  ALA B N     1 
ATOM   2220 C CA    . ALA B 1 20  ? -5.600  94.133  -10.051 1.00 24.08 ? 20  ALA B CA    1 
ATOM   2221 C C     . ALA B 1 20  ? -5.680  92.615  -9.917  1.00 24.44 ? 20  ALA B C     1 
ATOM   2222 O O     . ALA B 1 20  ? -5.088  91.886  -10.727 1.00 24.28 ? 20  ALA B O     1 
ATOM   2223 C CB    . ALA B 1 20  ? -4.347  94.605  -9.327  1.00 22.71 ? 20  ALA B CB    1 
ATOM   2224 N N     . TYR B 1 21  ? -6.410  92.145  -8.915  1.00 24.58 ? 21  TYR B N     1 
ATOM   2225 C CA    . TYR B 1 21  ? -6.610  90.711  -8.805  1.00 25.52 ? 21  TYR B CA    1 
ATOM   2226 C C     . TYR B 1 21  ? -7.521  90.109  -9.872  1.00 25.95 ? 21  TYR B C     1 
ATOM   2227 O O     . TYR B 1 21  ? -7.654  88.878  -9.895  1.00 26.16 ? 21  TYR B O     1 
ATOM   2228 C CB    . TYR B 1 21  ? -7.235  90.456  -7.453  1.00 25.25 ? 21  TYR B CB    1 
ATOM   2229 C CG    . TYR B 1 21  ? -6.335  90.665  -6.266  1.00 24.74 ? 21  TYR B CG    1 
ATOM   2230 C CD1   . TYR B 1 21  ? -5.507  89.642  -5.819  1.00 24.07 ? 21  TYR B CD1   1 
ATOM   2231 C CD2   . TYR B 1 21  ? -6.357  91.861  -5.568  1.00 24.03 ? 21  TYR B CD2   1 
ATOM   2232 C CE1   . TYR B 1 21  ? -4.733  89.817  -4.686  1.00 23.04 ? 21  TYR B CE1   1 
ATOM   2233 C CE2   . TYR B 1 21  ? -5.570  92.041  -4.450  1.00 23.03 ? 21  TYR B CE2   1 
ATOM   2234 C CZ    . TYR B 1 21  ? -4.776  91.011  -4.016  1.00 22.58 ? 21  TYR B CZ    1 
ATOM   2235 O OH    . TYR B 1 21  ? -4.000  91.143  -2.894  1.00 22.97 ? 21  TYR B OH    1 
ATOM   2236 N N     . CYS B 1 22  ? -8.418  90.890  -10.463 1.00 26.39 ? 22  CYS B N     1 
ATOM   2237 C CA    . CYS B 1 22  ? -9.337  90.321  -11.442 1.00 26.59 ? 22  CYS B CA    1 
ATOM   2238 C C     . CYS B 1 22  ? -8.502  89.780  -12.593 1.00 27.40 ? 22  CYS B C     1 
ATOM   2239 O O     . CYS B 1 22  ? -7.614  90.487  -13.062 1.00 27.43 ? 22  CYS B O     1 
ATOM   2240 C CB    . CYS B 1 22  ? -10.349 91.336  -11.949 1.00 22.82 ? 22  CYS B CB    1 
ATOM   2241 S SG    . CYS B 1 22  ? -11.360 92.019  -10.666 1.00 20.25 ? 22  CYS B SG    1 
ATOM   2242 N N     . GLY B 1 23  ? -8.776  88.550  -12.995 1.00 28.28 ? 23  GLY B N     1 
ATOM   2243 C CA    . GLY B 1 23  ? -7.966  87.900  -14.015 1.00 29.63 ? 23  GLY B CA    1 
ATOM   2244 C C     . GLY B 1 23  ? -7.950  88.651  -15.330 1.00 30.83 ? 23  GLY B C     1 
ATOM   2245 O O     . GLY B 1 23  ? -6.915  89.110  -15.808 1.00 30.81 ? 23  GLY B O     1 
ATOM   2246 N N     . LYS B 1 24  ? -9.119  89.004  -15.851 1.00 31.98 ? 24  LYS B N     1 
ATOM   2247 C CA    . LYS B 1 24  ? -9.317  89.726  -17.080 1.00 33.33 ? 24  LYS B CA    1 
ATOM   2248 C C     . LYS B 1 24  ? -8.524  91.020  -17.173 1.00 34.00 ? 24  LYS B C     1 
ATOM   2249 O O     . LYS B 1 24  ? -8.142  91.418  -18.281 1.00 34.66 ? 24  LYS B O     1 
ATOM   2250 C CB    . LYS B 1 24  ? -10.813 89.996  -17.306 1.00 36.58 ? 24  LYS B CB    1 
ATOM   2251 C CG    . LYS B 1 24  ? -11.391 91.054  -16.382 1.00 40.93 ? 24  LYS B CG    1 
ATOM   2252 C CD    . LYS B 1 24  ? -12.873 91.325  -16.603 1.00 43.05 ? 24  LYS B CD    1 
ATOM   2253 C CE    . LYS B 1 24  ? -13.489 91.907  -15.330 1.00 44.18 ? 24  LYS B CE    1 
ATOM   2254 N NZ    . LYS B 1 24  ? -14.816 92.531  -15.592 1.00 47.07 ? 24  LYS B NZ    1 
ATOM   2255 N N     . ASN B 1 25  ? -8.201  91.686  -16.080 1.00 34.02 ? 25  ASN B N     1 
ATOM   2256 C CA    . ASN B 1 25  ? -7.410  92.881  -16.009 1.00 33.87 ? 25  ASN B CA    1 
ATOM   2257 C C     . ASN B 1 25  ? -5.913  92.643  -16.065 1.00 34.26 ? 25  ASN B C     1 
ATOM   2258 O O     . ASN B 1 25  ? -5.175  93.530  -15.618 1.00 34.10 ? 25  ASN B O     1 
ATOM   2259 C CB    . ASN B 1 25  ? -7.650  93.539  -14.629 1.00 31.90 ? 25  ASN B CB    1 
ATOM   2260 C CG    . ASN B 1 25  ? -9.065  94.043  -14.543 1.00 30.95 ? 25  ASN B CG    1 
ATOM   2261 O OD1   . ASN B 1 25  ? -9.738  94.111  -15.566 1.00 32.34 ? 25  ASN B OD1   1 
ATOM   2262 N ND2   . ASN B 1 25  ? -9.448  94.370  -13.324 1.00 31.96 ? 25  ASN B ND2   1 
ATOM   2263 N N     . ASN B 1 26  ? -5.457  91.432  -16.342 1.00 35.01 ? 26  ASN B N     1 
ATOM   2264 C CA    . ASN B 1 26  ? -4.014  91.196  -16.288 1.00 36.06 ? 26  ASN B CA    1 
ATOM   2265 C C     . ASN B 1 26  ? -3.468  90.879  -17.671 1.00 36.65 ? 26  ASN B C     1 
ATOM   2266 O O     . ASN B 1 26  ? -2.261  90.729  -17.810 1.00 36.87 ? 26  ASN B O     1 
ATOM   2267 C CB    . ASN B 1 26  ? -3.596  90.098  -15.330 1.00 35.79 ? 26  ASN B CB    1 
ATOM   2268 C CG    . ASN B 1 26  ? -3.941  90.324  -13.879 1.00 36.98 ? 26  ASN B CG    1 
ATOM   2269 O OD1   . ASN B 1 26  ? -4.127  89.309  -13.192 1.00 39.16 ? 26  ASN B OD1   1 
ATOM   2270 N ND2   . ASN B 1 26  ? -4.054  91.539  -13.360 1.00 35.99 ? 26  ASN B ND2   1 
ATOM   2271 N N     . ASP B 1 27  ? -4.368  90.782  -18.634 1.00 37.16 ? 27  ASP B N     1 
ATOM   2272 C CA    . ASP B 1 27  ? -3.964  90.490  -20.005 1.00 37.57 ? 27  ASP B CA    1 
ATOM   2273 C C     . ASP B 1 27  ? -4.876  91.317  -20.906 1.00 37.04 ? 27  ASP B C     1 
ATOM   2274 O O     . ASP B 1 27  ? -5.053  90.965  -22.066 1.00 37.61 ? 27  ASP B O     1 
ATOM   2275 C CB    . ASP B 1 27  ? -4.117  89.007  -20.311 1.00 43.17 ? 27  ASP B CB    1 
ATOM   2276 C CG    . ASP B 1 27  ? -5.537  88.500  -20.124 1.00 47.98 ? 27  ASP B CG    1 
ATOM   2277 O OD1   . ASP B 1 27  ? -5.788  87.411  -20.694 1.00 50.04 ? 27  ASP B OD1   1 
ATOM   2278 O OD2   . ASP B 1 27  ? -6.373  89.146  -19.453 1.00 50.74 ? 27  ASP B OD2   1 
ATOM   2279 N N     . ALA B 1 28  ? -5.478  92.338  -20.310 1.00 36.15 ? 28  ALA B N     1 
ATOM   2280 C CA    . ALA B 1 28  ? -6.380  93.184  -21.083 1.00 35.49 ? 28  ALA B CA    1 
ATOM   2281 C C     . ALA B 1 28  ? -5.566  93.908  -22.140 1.00 35.28 ? 28  ALA B C     1 
ATOM   2282 O O     . ALA B 1 28  ? -4.399  94.199  -21.908 1.00 35.71 ? 28  ALA B O     1 
ATOM   2283 C CB    . ALA B 1 28  ? -7.090  94.170  -20.180 1.00 33.76 ? 28  ALA B CB    1 
ATOM   2284 N N     . PRO B 1 29  ? -6.153  94.113  -23.311 1.00 34.95 ? 29  PRO B N     1 
ATOM   2285 C CA    . PRO B 1 29  ? -5.552  94.924  -24.354 1.00 34.97 ? 29  PRO B CA    1 
ATOM   2286 C C     . PRO B 1 29  ? -5.489  96.409  -23.992 1.00 34.98 ? 29  PRO B C     1 
ATOM   2287 O O     . PRO B 1 29  ? -6.491  96.952  -23.532 1.00 34.67 ? 29  PRO B O     1 
ATOM   2288 C CB    . PRO B 1 29  ? -6.522  94.760  -25.520 1.00 34.76 ? 29  PRO B CB    1 
ATOM   2289 C CG    . PRO B 1 29  ? -7.308  93.547  -25.210 1.00 34.32 ? 29  PRO B CG    1 
ATOM   2290 C CD    . PRO B 1 29  ? -7.460  93.552  -23.718 1.00 34.28 ? 29  PRO B CD    1 
ATOM   2291 N N     . ALA B 1 30  ? -4.378  97.056  -24.323 1.00 35.10 ? 30  ALA B N     1 
ATOM   2292 C CA    . ALA B 1 30  ? -4.199  98.480  -24.084 1.00 35.06 ? 30  ALA B CA    1 
ATOM   2293 C C     . ALA B 1 30  ? -5.328  99.247  -24.764 1.00 35.26 ? 30  ALA B C     1 
ATOM   2294 O O     . ALA B 1 30  ? -5.566  98.979  -25.937 1.00 35.23 ? 30  ALA B O     1 
ATOM   2295 C CB    . ALA B 1 30  ? -2.881  98.952  -24.662 1.00 33.77 ? 30  ALA B CB    1 
ATOM   2296 N N     . GLY B 1 31  ? -5.994  100.118 -24.022 1.00 35.39 ? 31  GLY B N     1 
ATOM   2297 C CA    . GLY B 1 31  ? -7.073  100.894 -24.594 1.00 35.65 ? 31  GLY B CA    1 
ATOM   2298 C C     . GLY B 1 31  ? -8.420  100.397 -24.135 1.00 36.16 ? 31  GLY B C     1 
ATOM   2299 O O     . GLY B 1 31  ? -9.394  101.135 -24.276 1.00 37.59 ? 31  GLY B O     1 
ATOM   2300 N N     . THR B 1 32  ? -8.522  99.187  -23.631 1.00 36.36 ? 32  THR B N     1 
ATOM   2301 C CA    . THR B 1 32  ? -9.818  98.692  -23.145 1.00 36.39 ? 32  THR B CA    1 
ATOM   2302 C C     . THR B 1 32  ? -10.057 99.294  -21.766 1.00 36.50 ? 32  THR B C     1 
ATOM   2303 O O     . THR B 1 32  ? -9.187  100.003 -21.251 1.00 36.18 ? 32  THR B O     1 
ATOM   2304 C CB    . THR B 1 32  ? -9.833  97.157  -23.176 1.00 35.57 ? 32  THR B CB    1 
ATOM   2305 O OG1   . THR B 1 32  ? -8.742  96.623  -22.417 1.00 34.64 ? 32  THR B OG1   1 
ATOM   2306 C CG2   . THR B 1 32  ? -9.638  96.694  -24.615 1.00 35.27 ? 32  THR B CG2   1 
ATOM   2307 N N     . ASN B 1 33  ? -11.211 99.045  -21.167 1.00 36.52 ? 33  ASN B N     1 
ATOM   2308 C CA    . ASN B 1 33  ? -11.601 99.657  -19.916 1.00 36.90 ? 33  ASN B CA    1 
ATOM   2309 C C     . ASN B 1 33  ? -11.491 98.775  -18.676 1.00 36.72 ? 33  ASN B C     1 
ATOM   2310 O O     . ASN B 1 33  ? -12.281 97.835  -18.527 1.00 36.78 ? 33  ASN B O     1 
ATOM   2311 C CB    . ASN B 1 33  ? -13.079 100.088 -19.983 1.00 39.23 ? 33  ASN B CB    1 
ATOM   2312 C CG    . ASN B 1 33  ? -13.387 100.941 -21.187 1.00 42.07 ? 33  ASN B CG    1 
ATOM   2313 O OD1   . ASN B 1 33  ? -12.938 100.641 -22.298 1.00 44.35 ? 33  ASN B OD1   1 
ATOM   2314 N ND2   . ASN B 1 33  ? -14.150 102.013 -20.998 1.00 42.32 ? 33  ASN B ND2   1 
ATOM   2315 N N     . ILE B 1 34  ? -10.831 99.310  -17.643 1.00 36.19 ? 34  ILE B N     1 
ATOM   2316 C CA    . ILE B 1 34  ? -10.823 98.619  -16.355 1.00 35.84 ? 34  ILE B CA    1 
ATOM   2317 C C     . ILE B 1 34  ? -12.278 98.327  -15.974 1.00 35.68 ? 34  ILE B C     1 
ATOM   2318 O O     . ILE B 1 34  ? -13.175 99.145  -16.155 1.00 35.36 ? 34  ILE B O     1 
ATOM   2319 C CB    . ILE B 1 34  ? -10.156 99.415  -15.236 1.00 36.09 ? 34  ILE B CB    1 
ATOM   2320 C CG1   . ILE B 1 34  ? -8.676  99.692  -15.416 1.00 36.62 ? 34  ILE B CG1   1 
ATOM   2321 C CG2   . ILE B 1 34  ? -10.328 98.683  -13.897 1.00 35.60 ? 34  ILE B CG2   1 
ATOM   2322 C CD1   . ILE B 1 34  ? -8.118  99.868  -16.781 1.00 37.38 ? 34  ILE B CD1   1 
ATOM   2323 N N     . THR B 1 35  ? -12.541 97.092  -15.574 1.00 35.83 ? 35  THR B N     1 
ATOM   2324 C CA    . THR B 1 35  ? -13.847 96.647  -15.102 1.00 35.43 ? 35  THR B CA    1 
ATOM   2325 C C     . THR B 1 35  ? -13.588 95.526  -14.079 1.00 34.79 ? 35  THR B C     1 
ATOM   2326 O O     . THR B 1 35  ? -12.530 94.920  -14.182 1.00 34.28 ? 35  THR B O     1 
ATOM   2327 C CB    . THR B 1 35  ? -14.690 95.931  -16.177 1.00 34.98 ? 35  THR B CB    1 
ATOM   2328 O OG1   . THR B 1 35  ? -13.798 95.029  -16.853 1.00 36.64 ? 35  THR B OG1   1 
ATOM   2329 C CG2   . THR B 1 35  ? -15.355 96.876  -17.136 1.00 32.80 ? 35  THR B CG2   1 
ATOM   2330 N N     . CYS B 1 36  ? -14.539 95.289  -13.197 1.00 34.37 ? 36  CYS B N     1 
ATOM   2331 C CA    . CYS B 1 36  ? -14.366 94.232  -12.217 1.00 34.31 ? 36  CYS B CA    1 
ATOM   2332 C C     . CYS B 1 36  ? -15.583 93.327  -12.165 1.00 35.12 ? 36  CYS B C     1 
ATOM   2333 O O     . CYS B 1 36  ? -16.709 93.804  -12.246 1.00 35.84 ? 36  CYS B O     1 
ATOM   2334 C CB    . CYS B 1 36  ? -14.112 94.820  -10.828 1.00 28.35 ? 36  CYS B CB    1 
ATOM   2335 S SG    . CYS B 1 36  ? -12.593 95.768  -10.771 1.00 25.19 ? 36  CYS B SG    1 
ATOM   2336 N N     . THR B 1 37  ? -15.338 92.030  -12.008 1.00 36.02 ? 37  THR B N     1 
ATOM   2337 C CA    . THR B 1 37  ? -16.503 91.134  -11.855 1.00 36.94 ? 37  THR B CA    1 
ATOM   2338 C C     . THR B 1 37  ? -17.093 91.431  -10.484 1.00 37.06 ? 37  THR B C     1 
ATOM   2339 O O     . THR B 1 37  ? -16.446 92.109  -9.683  1.00 36.98 ? 37  THR B O     1 
ATOM   2340 C CB    . THR B 1 37  ? -16.133 89.668  -12.063 1.00 37.80 ? 37  THR B CB    1 
ATOM   2341 O OG1   . THR B 1 37  ? -15.395 89.188  -10.931 1.00 39.89 ? 37  THR B OG1   1 
ATOM   2342 C CG2   . THR B 1 37  ? -15.292 89.520  -13.328 1.00 36.47 ? 37  THR B CG2   1 
ATOM   2343 N N     . GLY B 1 38  ? -18.368 91.151  -10.300 1.00 37.73 ? 38  GLY B N     1 
ATOM   2344 C CA    . GLY B 1 38  ? -19.029 91.543  -9.043  1.00 39.18 ? 38  GLY B CA    1 
ATOM   2345 C C     . GLY B 1 38  ? -18.999 93.072  -8.936  1.00 40.25 ? 38  GLY B C     1 
ATOM   2346 O O     . GLY B 1 38  ? -19.125 93.818  -9.930  1.00 40.49 ? 38  GLY B O     1 
ATOM   2347 N N     . ASN B 1 39  ? -18.944 93.577  -7.696  1.00 40.64 ? 39  ASN B N     1 
ATOM   2348 C CA    . ASN B 1 39  ? -18.769 95.025  -7.584  1.00 40.88 ? 39  ASN B CA    1 
ATOM   2349 C C     . ASN B 1 39  ? -17.435 95.351  -6.953  1.00 40.50 ? 39  ASN B C     1 
ATOM   2350 O O     . ASN B 1 39  ? -17.316 96.217  -6.089  1.00 41.06 ? 39  ASN B O     1 
ATOM   2351 C CB    . ASN B 1 39  ? -19.960 95.725  -6.948  1.00 46.55 ? 39  ASN B CB    1 
ATOM   2352 C CG    . ASN B 1 39  ? -20.596 96.647  -7.995  1.00 51.27 ? 39  ASN B CG    1 
ATOM   2353 O OD1   . ASN B 1 39  ? -21.236 97.662  -7.683  1.00 52.51 ? 39  ASN B OD1   1 
ATOM   2354 N ND2   . ASN B 1 39  ? -20.399 96.300  -9.274  1.00 51.45 ? 39  ASN B ND2   1 
ATOM   2355 N N     . ALA B 1 40  ? -16.382 94.696  -7.440  1.00 39.45 ? 40  ALA B N     1 
ATOM   2356 C CA    . ALA B 1 40  ? -15.042 94.861  -6.904  1.00 38.27 ? 40  ALA B CA    1 
ATOM   2357 C C     . ALA B 1 40  ? -14.514 96.284  -7.062  1.00 37.52 ? 40  ALA B C     1 
ATOM   2358 O O     . ALA B 1 40  ? -13.807 96.783  -6.178  1.00 37.01 ? 40  ALA B O     1 
ATOM   2359 C CB    . ALA B 1 40  ? -14.098 93.866  -7.571  1.00 38.87 ? 40  ALA B CB    1 
ATOM   2360 N N     . CYS B 1 41  ? -14.905 96.976  -8.133  1.00 36.49 ? 41  CYS B N     1 
ATOM   2361 C CA    . CYS B 1 41  ? -14.408 98.320  -8.383  1.00 35.57 ? 41  CYS B CA    1 
ATOM   2362 C C     . CYS B 1 41  ? -15.390 99.197  -9.142  1.00 36.12 ? 41  CYS B C     1 
ATOM   2363 O O     . CYS B 1 41  ? -15.154 99.643  -10.263 1.00 36.02 ? 41  CYS B O     1 
ATOM   2364 C CB    . CYS B 1 41  ? -13.080 98.215  -9.129  1.00 28.88 ? 41  CYS B CB    1 
ATOM   2365 S SG    . CYS B 1 41  ? -13.159 97.706  -10.856 1.00 24.65 ? 41  CYS B SG    1 
ATOM   2366 N N     . PRO B 1 42  ? -16.463 99.604  -8.464  1.00 36.63 ? 42  PRO B N     1 
ATOM   2367 C CA    . PRO B 1 42  ? -17.514 100.429 -9.049  1.00 36.81 ? 42  PRO B CA    1 
ATOM   2368 C C     . PRO B 1 42  ? -17.071 101.829 -9.417  1.00 36.94 ? 42  PRO B C     1 
ATOM   2369 O O     . PRO B 1 42  ? -17.236 102.290 -10.551 1.00 37.59 ? 42  PRO B O     1 
ATOM   2370 C CB    . PRO B 1 42  ? -18.590 100.460 -7.975  1.00 36.73 ? 42  PRO B CB    1 
ATOM   2371 C CG    . PRO B 1 42  ? -17.850 100.214 -6.701  1.00 36.63 ? 42  PRO B CG    1 
ATOM   2372 C CD    . PRO B 1 42  ? -16.821 99.180  -7.085  1.00 36.60 ? 42  PRO B CD    1 
ATOM   2373 N N     . GLU B 1 43  ? -16.300 102.474 -8.551  1.00 36.89 ? 43  GLU B N     1 
ATOM   2374 C CA    . GLU B 1 43  ? -15.787 103.808 -8.823  1.00 36.59 ? 43  GLU B CA    1 
ATOM   2375 C C     . GLU B 1 43  ? -14.842 103.809 -10.009 1.00 36.04 ? 43  GLU B C     1 
ATOM   2376 O O     . GLU B 1 43  ? -14.871 104.731 -10.815 1.00 36.49 ? 43  GLU B O     1 
ATOM   2377 C CB    . GLU B 1 43  ? -14.996 104.353 -7.630  1.00 40.26 ? 43  GLU B CB    1 
ATOM   2378 C CG    . GLU B 1 43  ? -15.843 104.636 -6.399  1.00 44.59 ? 43  GLU B CG    1 
ATOM   2379 C CD    . GLU B 1 43  ? -16.951 105.619 -6.728  1.00 47.38 ? 43  GLU B CD    1 
ATOM   2380 O OE1   . GLU B 1 43  ? -16.791 106.429 -7.667  1.00 49.19 ? 43  GLU B OE1   1 
ATOM   2381 O OE2   . GLU B 1 43  ? -18.014 105.615 -6.074  1.00 50.04 ? 43  GLU B OE2   1 
ATOM   2382 N N     . VAL B 1 44  ? -13.987 102.792 -10.105 1.00 35.41 ? 44  VAL B N     1 
ATOM   2383 C CA    . VAL B 1 44  ? -13.011 102.734 -11.194 1.00 34.34 ? 44  VAL B CA    1 
ATOM   2384 C C     . VAL B 1 44  ? -13.739 102.583 -12.514 1.00 34.54 ? 44  VAL B C     1 
ATOM   2385 O O     . VAL B 1 44  ? -13.479 103.371 -13.417 1.00 34.46 ? 44  VAL B O     1 
ATOM   2386 C CB    . VAL B 1 44  ? -11.980 101.624 -10.969 1.00 32.06 ? 44  VAL B CB    1 
ATOM   2387 C CG1   . VAL B 1 44  ? -10.960 101.490 -12.082 1.00 28.52 ? 44  VAL B CG1   1 
ATOM   2388 C CG2   . VAL B 1 44  ? -11.276 101.859 -9.631  1.00 30.65 ? 44  VAL B CG2   1 
ATOM   2389 N N     . GLU B 1 45  ? -14.829 101.822 -12.503 1.00 35.03 ? 45  GLU B N     1 
ATOM   2390 C CA    . GLU B 1 45  ? -15.665 101.615 -13.673 1.00 35.72 ? 45  GLU B CA    1 
ATOM   2391 C C     . GLU B 1 45  ? -16.410 102.889 -14.030 1.00 36.12 ? 45  GLU B C     1 
ATOM   2392 O O     . GLU B 1 45  ? -16.505 103.293 -15.182 1.00 36.30 ? 45  GLU B O     1 
ATOM   2393 C CB    . GLU B 1 45  ? -16.671 100.502 -13.398 1.00 36.29 ? 45  GLU B CB    1 
ATOM   2394 C CG    . GLU B 1 45  ? -16.018 99.132  -13.430 1.00 40.87 ? 45  GLU B CG    1 
ATOM   2395 C CD    . GLU B 1 45  ? -16.978 98.029  -13.017 1.00 42.83 ? 45  GLU B CD    1 
ATOM   2396 O OE1   . GLU B 1 45  ? -17.628 98.201  -11.966 1.00 44.45 ? 45  GLU B OE1   1 
ATOM   2397 O OE2   . GLU B 1 45  ? -17.046 97.024  -13.752 1.00 43.45 ? 45  GLU B OE2   1 
ATOM   2398 N N     . LYS B 1 46  ? -16.851 103.570 -12.988 1.00 36.65 ? 46  LYS B N     1 
ATOM   2399 C CA    . LYS B 1 46  ? -17.550 104.840 -13.170 1.00 38.21 ? 46  LYS B CA    1 
ATOM   2400 C C     . LYS B 1 46  ? -16.629 105.837 -13.856 1.00 38.72 ? 46  LYS B C     1 
ATOM   2401 O O     . LYS B 1 46  ? -17.054 106.499 -14.814 1.00 39.15 ? 46  LYS B O     1 
ATOM   2402 C CB    . LYS B 1 46  ? -18.060 105.263 -11.806 1.00 41.46 ? 46  LYS B CB    1 
ATOM   2403 C CG    . LYS B 1 46  ? -18.671 106.638 -11.688 1.00 45.27 ? 46  LYS B CG    1 
ATOM   2404 C CD    . LYS B 1 46  ? -18.704 107.049 -10.218 1.00 50.05 ? 46  LYS B CD    1 
ATOM   2405 C CE    . LYS B 1 46  ? -19.767 106.261 -9.452  1.00 51.69 ? 46  LYS B CE    1 
ATOM   2406 N NZ    . LYS B 1 46  ? -20.163 107.001 -8.213  1.00 54.52 ? 46  LYS B NZ    1 
ATOM   2407 N N     . ALA B 1 47  ? -15.367 105.932 -13.453 1.00 38.69 ? 47  ALA B N     1 
ATOM   2408 C CA    . ALA B 1 47  ? -14.398 106.782 -14.121 1.00 38.98 ? 47  ALA B CA    1 
ATOM   2409 C C     . ALA B 1 47  ? -14.246 106.457 -15.605 1.00 39.08 ? 47  ALA B C     1 
ATOM   2410 O O     . ALA B 1 47  ? -14.568 105.371 -16.077 1.00 39.27 ? 47  ALA B O     1 
ATOM   2411 C CB    . ALA B 1 47  ? -13.027 106.559 -13.468 1.00 40.28 ? 47  ALA B CB    1 
ATOM   2412 N N     . ASP B 1 48  ? -13.468 107.279 -16.300 1.00 39.36 ? 48  ASP B N     1 
ATOM   2413 C CA    . ASP B 1 48  ? -13.017 106.997 -17.667 1.00 39.21 ? 48  ASP B CA    1 
ATOM   2414 C C     . ASP B 1 48  ? -11.621 106.389 -17.521 1.00 38.38 ? 48  ASP B C     1 
ATOM   2415 O O     . ASP B 1 48  ? -10.632 107.136 -17.620 1.00 38.75 ? 48  ASP B O     1 
ATOM   2416 C CB    . ASP B 1 48  ? -12.960 108.279 -18.482 1.00 44.45 ? 48  ASP B CB    1 
ATOM   2417 C CG    . ASP B 1 48  ? -12.297 108.214 -19.837 1.00 48.78 ? 48  ASP B CG    1 
ATOM   2418 O OD1   . ASP B 1 48  ? -12.671 109.024 -20.725 1.00 50.80 ? 48  ASP B OD1   1 
ATOM   2419 O OD2   . ASP B 1 48  ? -11.384 107.399 -20.106 1.00 52.03 ? 48  ASP B OD2   1 
ATOM   2420 N N     . ALA B 1 49  ? -11.522 105.123 -17.124 1.00 37.01 ? 49  ALA B N     1 
ATOM   2421 C CA    . ALA B 1 49  ? -10.192 104.553 -16.898 1.00 35.42 ? 49  ALA B CA    1 
ATOM   2422 C C     . ALA B 1 49  ? -9.890  103.423 -17.859 1.00 34.46 ? 49  ALA B C     1 
ATOM   2423 O O     . ALA B 1 49  ? -10.686 102.497 -17.989 1.00 34.77 ? 49  ALA B O     1 
ATOM   2424 C CB    . ALA B 1 49  ? -10.027 104.074 -15.469 1.00 35.15 ? 49  ALA B CB    1 
ATOM   2425 N N     . THR B 1 50  ? -8.791  103.524 -18.590 1.00 33.42 ? 50  THR B N     1 
ATOM   2426 C CA    . THR B 1 50  ? -8.431  102.509 -19.565 1.00 32.53 ? 50  THR B CA    1 
ATOM   2427 C C     . THR B 1 50  ? -7.026  101.969 -19.330 1.00 32.10 ? 50  THR B C     1 
ATOM   2428 O O     . THR B 1 50  ? -6.264  102.519 -18.548 1.00 32.00 ? 50  THR B O     1 
ATOM   2429 C CB    . THR B 1 50  ? -8.527  103.043 -21.001 1.00 32.12 ? 50  THR B CB    1 
ATOM   2430 O OG1   . THR B 1 50  ? -7.709  104.215 -21.123 1.00 33.67 ? 50  THR B OG1   1 
ATOM   2431 C CG2   . THR B 1 50  ? -9.949  103.356 -21.411 1.00 30.93 ? 50  THR B CG2   1 
ATOM   2432 N N     . PHE B 1 51  ? -6.768  100.769 -19.835 1.00 31.88 ? 51  PHE B N     1 
ATOM   2433 C CA    . PHE B 1 51  ? -5.477  100.131 -19.672 1.00 31.72 ? 51  PHE B CA    1 
ATOM   2434 C C     . PHE B 1 51  ? -4.428  100.800 -20.555 1.00 31.99 ? 51  PHE B C     1 
ATOM   2435 O O     . PHE B 1 51  ? -4.607  100.893 -21.767 1.00 31.78 ? 51  PHE B O     1 
ATOM   2436 C CB    . PHE B 1 51  ? -5.562  98.650  -20.078 1.00 30.48 ? 51  PHE B CB    1 
ATOM   2437 C CG    . PHE B 1 51  ? -6.346  97.847  -19.085 1.00 29.84 ? 51  PHE B CG    1 
ATOM   2438 C CD1   . PHE B 1 51  ? -5.749  97.408  -17.913 1.00 28.50 ? 51  PHE B CD1   1 
ATOM   2439 C CD2   . PHE B 1 51  ? -7.685  97.559  -19.320 1.00 29.50 ? 51  PHE B CD2   1 
ATOM   2440 C CE1   . PHE B 1 51  ? -6.478  96.681  -16.987 1.00 28.34 ? 51  PHE B CE1   1 
ATOM   2441 C CE2   . PHE B 1 51  ? -8.404  96.827  -18.391 1.00 28.28 ? 51  PHE B CE2   1 
ATOM   2442 C CZ    . PHE B 1 51  ? -7.810  96.392  -17.222 1.00 27.46 ? 51  PHE B CZ    1 
ATOM   2443 N N     . LEU B 1 52  ? -3.289  101.138 -19.962 1.00 32.26 ? 52  LEU B N     1 
ATOM   2444 C CA    . LEU B 1 52  ? -2.136  101.602 -20.732 1.00 32.19 ? 52  LEU B CA    1 
ATOM   2445 C C     . LEU B 1 52  ? -1.250  100.386 -21.000 1.00 32.33 ? 52  LEU B C     1 
ATOM   2446 O O     . LEU B 1 52  ? -0.851  100.092 -22.111 1.00 32.06 ? 52  LEU B O     1 
ATOM   2447 C CB    . LEU B 1 52  ? -1.330  102.634 -19.972 1.00 32.00 ? 52  LEU B CB    1 
ATOM   2448 C CG    . LEU B 1 52  ? -1.365  104.117 -20.291 1.00 32.91 ? 52  LEU B CG    1 
ATOM   2449 C CD1   . LEU B 1 52  ? -2.429  104.516 -21.297 1.00 32.29 ? 52  LEU B CD1   1 
ATOM   2450 C CD2   . LEU B 1 52  ? -1.538  104.928 -19.010 1.00 32.29 ? 52  LEU B CD2   1 
ATOM   2451 N N     . TYR B 1 53  ? -1.038  99.631  -19.933 1.00 33.09 ? 53  TYR B N     1 
ATOM   2452 C CA    . TYR B 1 53  ? -0.191  98.447  -19.920 1.00 33.39 ? 53  TYR B CA    1 
ATOM   2453 C C     . TYR B 1 53  ? -0.744  97.450  -18.901 1.00 33.50 ? 53  TYR B C     1 
ATOM   2454 O O     . TYR B 1 53  ? -1.116  97.812  -17.784 1.00 33.43 ? 53  TYR B O     1 
ATOM   2455 C CB    . TYR B 1 53  ? 1.248   98.783  -19.536 1.00 33.25 ? 53  TYR B CB    1 
ATOM   2456 C CG    . TYR B 1 53  ? 2.236   97.641  -19.574 1.00 33.75 ? 53  TYR B CG    1 
ATOM   2457 C CD1   . TYR B 1 53  ? 2.392   96.898  -20.735 1.00 34.23 ? 53  TYR B CD1   1 
ATOM   2458 C CD2   . TYR B 1 53  ? 3.037   97.297  -18.493 1.00 33.84 ? 53  TYR B CD2   1 
ATOM   2459 C CE1   . TYR B 1 53  ? 3.293   95.859  -20.834 1.00 34.68 ? 53  TYR B CE1   1 
ATOM   2460 C CE2   . TYR B 1 53  ? 3.939   96.264  -18.558 1.00 34.58 ? 53  TYR B CE2   1 
ATOM   2461 C CZ    . TYR B 1 53  ? 4.065   95.539  -19.732 1.00 35.33 ? 53  TYR B CZ    1 
ATOM   2462 O OH    . TYR B 1 53  ? 4.947   94.479  -19.860 1.00 35.04 ? 53  TYR B OH    1 
ATOM   2463 N N     . SER B 1 54  ? -0.976  96.248  -19.397 1.00 33.60 ? 54  SER B N     1 
ATOM   2464 C CA    . SER B 1 54  ? -1.436  95.138  -18.566 1.00 33.50 ? 54  SER B CA    1 
ATOM   2465 C C     . SER B 1 54  ? -0.312  94.115  -18.447 1.00 33.66 ? 54  SER B C     1 
ATOM   2466 O O     . SER B 1 54  ? 0.284   93.746  -19.468 1.00 34.09 ? 54  SER B O     1 
ATOM   2467 C CB    . SER B 1 54  ? -2.605  94.462  -19.284 1.00 32.26 ? 54  SER B CB    1 
ATOM   2468 O OG    . SER B 1 54  ? -3.671  94.300  -18.380 1.00 34.49 ? 54  SER B OG    1 
ATOM   2469 N N     . PHE B 1 55  ? 0.016   93.653  -17.256 1.00 33.60 ? 55  PHE B N     1 
ATOM   2470 C CA    . PHE B 1 55  ? 1.080   92.666  -17.149 1.00 33.86 ? 55  PHE B CA    1 
ATOM   2471 C C     . PHE B 1 55  ? 0.785   91.591  -16.120 1.00 34.36 ? 55  PHE B C     1 
ATOM   2472 O O     . PHE B 1 55  ? 0.199   91.838  -15.071 1.00 34.40 ? 55  PHE B O     1 
ATOM   2473 C CB    . PHE B 1 55  ? 2.438   93.310  -16.889 1.00 32.86 ? 55  PHE B CB    1 
ATOM   2474 C CG    . PHE B 1 55  ? 2.475   94.134  -15.635 1.00 31.71 ? 55  PHE B CG    1 
ATOM   2475 C CD1   . PHE B 1 55  ? 2.057   95.455  -15.635 1.00 31.36 ? 55  PHE B CD1   1 
ATOM   2476 C CD2   . PHE B 1 55  ? 2.921   93.574  -14.457 1.00 31.00 ? 55  PHE B CD2   1 
ATOM   2477 C CE1   . PHE B 1 55  ? 2.092   96.209  -14.484 1.00 30.90 ? 55  PHE B CE1   1 
ATOM   2478 C CE2   . PHE B 1 55  ? 2.955   94.313  -13.297 1.00 30.98 ? 55  PHE B CE2   1 
ATOM   2479 C CZ    . PHE B 1 55  ? 2.535   95.624  -13.314 1.00 31.68 ? 55  PHE B CZ    1 
ATOM   2480 N N     . GLU B 1 56  ? 1.123   90.360  -16.485 1.00 35.07 ? 56  GLU B N     1 
ATOM   2481 C CA    . GLU B 1 56  ? 0.993   89.253  -15.561 1.00 36.26 ? 56  GLU B CA    1 
ATOM   2482 C C     . GLU B 1 56  ? 2.176   88.304  -15.708 1.00 36.98 ? 56  GLU B C     1 
ATOM   2483 O O     . GLU B 1 56  ? 2.785   88.121  -16.755 1.00 37.11 ? 56  GLU B O     1 
ATOM   2484 C CB    . GLU B 1 56  ? -0.271  88.434  -15.786 1.00 37.60 ? 56  GLU B CB    1 
ATOM   2485 C CG    . GLU B 1 56  ? -0.124  87.613  -17.051 1.00 39.76 ? 56  GLU B CG    1 
ATOM   2486 C CD    . GLU B 1 56  ? -1.399  86.901  -17.429 1.00 41.58 ? 56  GLU B CD    1 
ATOM   2487 O OE1   . GLU B 1 56  ? -2.087  86.406  -16.516 1.00 41.70 ? 56  GLU B OE1   1 
ATOM   2488 O OE2   . GLU B 1 56  ? -1.587  86.904  -18.665 1.00 43.52 ? 56  GLU B OE2   1 
ATOM   2489 N N     . ASP B 1 57  ? 2.480   87.667  -14.585 1.00 37.92 ? 57  ASP B N     1 
ATOM   2490 C CA    . ASP B 1 57  ? 3.574   86.704  -14.543 1.00 38.27 ? 57  ASP B CA    1 
ATOM   2491 C C     . ASP B 1 57  ? 4.827   87.285  -15.162 1.00 38.11 ? 57  ASP B C     1 
ATOM   2492 O O     . ASP B 1 57  ? 5.500   86.638  -15.963 1.00 38.74 ? 57  ASP B O     1 
ATOM   2493 C CB    . ASP B 1 57  ? 3.098   85.422  -15.206 1.00 42.06 ? 57  ASP B CB    1 
ATOM   2494 C CG    . ASP B 1 57  ? 4.048   84.269  -14.975 1.00 45.89 ? 57  ASP B CG    1 
ATOM   2495 O OD1   . ASP B 1 57  ? 4.786   84.256  -13.963 1.00 47.77 ? 57  ASP B OD1   1 
ATOM   2496 O OD2   . ASP B 1 57  ? 4.042   83.381  -15.854 1.00 48.52 ? 57  ASP B OD2   1 
ATOM   2497 N N     . SER B 1 58  ? 5.248   88.457  -14.682 1.00 37.47 ? 58  SER B N     1 
ATOM   2498 C CA    . SER B 1 58  ? 6.462   89.091  -15.157 1.00 36.59 ? 58  SER B CA    1 
ATOM   2499 C C     . SER B 1 58  ? 7.575   88.995  -14.126 1.00 36.13 ? 58  SER B C     1 
ATOM   2500 O O     . SER B 1 58  ? 7.275   88.768  -12.959 1.00 36.51 ? 58  SER B O     1 
ATOM   2501 C CB    . SER B 1 58  ? 6.217   90.568  -15.452 1.00 36.32 ? 58  SER B CB    1 
ATOM   2502 O OG    . SER B 1 58  ? 5.292   90.621  -16.522 1.00 39.17 ? 58  SER B OG    1 
ATOM   2503 N N     . GLY B 1 59  ? 8.791   89.285  -14.575 1.00 35.43 ? 59  GLY B N     1 
ATOM   2504 C CA    . GLY B 1 59  ? 9.958   89.274  -13.704 1.00 34.33 ? 59  GLY B CA    1 
ATOM   2505 C C     . GLY B 1 59  ? 10.047  87.985  -12.893 1.00 33.21 ? 59  GLY B C     1 
ATOM   2506 O O     . GLY B 1 59  ? 9.789   86.939  -13.470 1.00 33.28 ? 59  GLY B O     1 
ATOM   2507 N N     . VAL B 1 60  ? 10.573  88.057  -11.685 1.00 32.14 ? 60  VAL B N     1 
ATOM   2508 C CA    . VAL B 1 60  ? 10.644  86.892  -10.823 1.00 31.81 ? 60  VAL B CA    1 
ATOM   2509 C C     . VAL B 1 60  ? 9.617   87.085  -9.713  1.00 32.15 ? 60  VAL B C     1 
ATOM   2510 O O     . VAL B 1 60  ? 9.389   88.242  -9.352  1.00 32.75 ? 60  VAL B O     1 
ATOM   2511 C CB    . VAL B 1 60  ? 12.050  86.642  -10.265 1.00 30.09 ? 60  VAL B CB    1 
ATOM   2512 C CG1   . VAL B 1 60  ? 13.112  86.928  -11.318 1.00 28.59 ? 60  VAL B CG1   1 
ATOM   2513 C CG2   . VAL B 1 60  ? 12.389  87.408  -9.003  1.00 29.85 ? 60  VAL B CG2   1 
ATOM   2514 N N     . GLY B 1 61  ? 8.877   86.043  -9.354  1.00 32.12 ? 61  GLY B N     1 
ATOM   2515 C CA    . GLY B 1 61  ? 7.942   86.182  -8.239  1.00 32.05 ? 61  GLY B CA    1 
ATOM   2516 C C     . GLY B 1 61  ? 6.544   86.517  -8.734  1.00 31.82 ? 61  GLY B C     1 
ATOM   2517 O O     . GLY B 1 61  ? 5.722   87.004  -7.964  1.00 32.33 ? 61  GLY B O     1 
ATOM   2518 N N     . ASP B 1 62  ? 6.316   86.274  -10.012 1.00 31.49 ? 62  ASP B N     1 
ATOM   2519 C CA    . ASP B 1 62  ? 5.035   86.506  -10.655 1.00 31.40 ? 62  ASP B CA    1 
ATOM   2520 C C     . ASP B 1 62  ? 4.514   87.919  -10.468 1.00 31.03 ? 62  ASP B C     1 
ATOM   2521 O O     . ASP B 1 62  ? 3.478   88.148  -9.831  1.00 31.51 ? 62  ASP B O     1 
ATOM   2522 C CB    . ASP B 1 62  ? 4.056   85.435  -10.170 1.00 32.63 ? 62  ASP B CB    1 
ATOM   2523 C CG    . ASP B 1 62  ? 2.707   85.447  -10.858 1.00 35.55 ? 62  ASP B CG    1 
ATOM   2524 O OD1   . ASP B 1 62  ? 2.594   85.851  -12.036 1.00 34.14 ? 62  ASP B OD1   1 
ATOM   2525 O OD2   . ASP B 1 62  ? 1.693   85.069  -10.212 1.00 37.36 ? 62  ASP B OD2   1 
ATOM   2526 N N     . VAL B 1 63  ? 5.217   88.914  -10.996 1.00 30.34 ? 63  VAL B N     1 
ATOM   2527 C CA    . VAL B 1 63  ? 4.779   90.308  -10.834 1.00 30.07 ? 63  VAL B CA    1 
ATOM   2528 C C     . VAL B 1 63  ? 3.603   90.584  -11.766 1.00 29.85 ? 63  VAL B C     1 
ATOM   2529 O O     . VAL B 1 63  ? 3.635   90.325  -12.972 1.00 29.78 ? 63  VAL B O     1 
ATOM   2530 C CB    . VAL B 1 63  ? 5.923   91.295  -11.066 1.00 29.61 ? 63  VAL B CB    1 
ATOM   2531 C CG1   . VAL B 1 63  ? 5.615   92.609  -10.365 1.00 29.52 ? 63  VAL B CG1   1 
ATOM   2532 C CG2   . VAL B 1 63  ? 7.245   90.729  -10.566 1.00 28.19 ? 63  VAL B CG2   1 
ATOM   2533 N N     . THR B 1 64  ? 2.468   90.972  -11.194 1.00 29.31 ? 64  THR B N     1 
ATOM   2534 C CA    . THR B 1 64  ? 1.205   91.095  -11.919 1.00 28.33 ? 64  THR B CA    1 
ATOM   2535 C C     . THR B 1 64  ? 0.448   92.342  -11.509 1.00 27.94 ? 64  THR B C     1 
ATOM   2536 O O     . THR B 1 64  ? 0.387   92.715  -10.339 1.00 27.38 ? 64  THR B O     1 
ATOM   2537 C CB    . THR B 1 64  ? 0.394   89.817  -11.610 1.00 27.74 ? 64  THR B CB    1 
ATOM   2538 O OG1   . THR B 1 64  ? 1.147   88.668  -12.027 1.00 26.45 ? 64  THR B OG1   1 
ATOM   2539 C CG2   . THR B 1 64  ? -0.960  89.766  -12.276 1.00 28.09 ? 64  THR B CG2   1 
ATOM   2540 N N     . GLY B 1 65  ? -0.071  93.066  -12.494 1.00 28.08 ? 65  GLY B N     1 
ATOM   2541 C CA    . GLY B 1 65  ? -0.786  94.311  -12.204 1.00 28.66 ? 65  GLY B CA    1 
ATOM   2542 C C     . GLY B 1 65  ? -1.130  95.041  -13.495 1.00 28.66 ? 65  GLY B C     1 
ATOM   2543 O O     . GLY B 1 65  ? -1.041  94.448  -14.564 1.00 28.57 ? 65  GLY B O     1 
ATOM   2544 N N     . PHE B 1 66  ? -1.462  96.322  -13.402 1.00 28.82 ? 66  PHE B N     1 
ATOM   2545 C CA    . PHE B 1 66  ? -1.739  97.101  -14.598 1.00 28.71 ? 66  PHE B CA    1 
ATOM   2546 C C     . PHE B 1 66  ? -1.290  98.550  -14.415 1.00 28.92 ? 66  PHE B C     1 
ATOM   2547 O O     . PHE B 1 66  ? -0.982  99.042  -13.333 1.00 28.46 ? 66  PHE B O     1 
ATOM   2548 C CB    . PHE B 1 66  ? -3.188  97.095  -15.039 1.00 28.26 ? 66  PHE B CB    1 
ATOM   2549 C CG    . PHE B 1 66  ? -4.222  97.499  -14.033 1.00 28.35 ? 66  PHE B CG    1 
ATOM   2550 C CD1   . PHE B 1 66  ? -4.455  98.834  -13.768 1.00 28.62 ? 66  PHE B CD1   1 
ATOM   2551 C CD2   . PHE B 1 66  ? -4.989  96.550  -13.374 1.00 27.89 ? 66  PHE B CD2   1 
ATOM   2552 C CE1   . PHE B 1 66  ? -5.421  99.223  -12.858 1.00 29.57 ? 66  PHE B CE1   1 
ATOM   2553 C CE2   . PHE B 1 66  ? -5.957  96.937  -12.467 1.00 28.98 ? 66  PHE B CE2   1 
ATOM   2554 C CZ    . PHE B 1 66  ? -6.178  98.275  -12.204 1.00 29.01 ? 66  PHE B CZ    1 
ATOM   2555 N N     . LEU B 1 67  ? -1.163  99.181  -15.582 1.00 29.11 ? 67  LEU B N     1 
ATOM   2556 C CA    . LEU B 1 67  ? -0.895  100.620 -15.620 1.00 28.85 ? 67  LEU B CA    1 
ATOM   2557 C C     . LEU B 1 67  ? -2.069  101.271 -16.350 1.00 28.89 ? 67  LEU B C     1 
ATOM   2558 O O     . LEU B 1 67  ? -2.325  100.945 -17.506 1.00 28.56 ? 67  LEU B O     1 
ATOM   2559 C CB    . LEU B 1 67  ? 0.428   100.892 -16.288 1.00 28.32 ? 67  LEU B CB    1 
ATOM   2560 C CG    . LEU B 1 67  ? 0.822   102.370 -16.381 1.00 29.67 ? 67  LEU B CG    1 
ATOM   2561 C CD1   . LEU B 1 67  ? 1.227   102.931 -15.026 1.00 28.66 ? 67  LEU B CD1   1 
ATOM   2562 C CD2   . LEU B 1 67  ? 1.948   102.488 -17.409 1.00 29.64 ? 67  LEU B CD2   1 
ATOM   2563 N N     . ALA B 1 68  ? -2.842  102.063 -15.614 1.00 28.88 ? 68  ALA B N     1 
ATOM   2564 C CA    . ALA B 1 68  ? -4.029  102.699 -16.130 1.00 28.88 ? 68  ALA B CA    1 
ATOM   2565 C C     . ALA B 1 68  ? -3.886  104.207 -16.289 1.00 29.28 ? 68  ALA B C     1 
ATOM   2566 O O     . ALA B 1 68  ? -3.075  104.874 -15.663 1.00 29.19 ? 68  ALA B O     1 
ATOM   2567 C CB    . ALA B 1 68  ? -5.212  102.450 -15.208 1.00 27.69 ? 68  ALA B CB    1 
ATOM   2568 N N     . LEU B 1 69  ? -4.676  104.726 -17.216 1.00 29.69 ? 69  LEU B N     1 
ATOM   2569 C CA    . LEU B 1 69  ? -4.817  106.159 -17.446 1.00 30.08 ? 69  LEU B CA    1 
ATOM   2570 C C     . LEU B 1 69  ? -6.236  106.542 -17.016 1.00 30.28 ? 69  LEU B C     1 
ATOM   2571 O O     . LEU B 1 69  ? -7.175  106.017 -17.619 1.00 30.43 ? 69  LEU B O     1 
ATOM   2572 C CB    . LEU B 1 69  ? -4.700  106.459 -18.932 1.00 29.90 ? 69  LEU B CB    1 
ATOM   2573 C CG    . LEU B 1 69  ? -4.023  107.681 -19.528 1.00 28.99 ? 69  LEU B CG    1 
ATOM   2574 C CD1   . LEU B 1 69  ? -4.810  108.217 -20.714 1.00 26.78 ? 69  LEU B CD1   1 
ATOM   2575 C CD2   . LEU B 1 69  ? -3.674  108.788 -18.559 1.00 28.06 ? 69  LEU B CD2   1 
ATOM   2576 N N     . ASP B 1 70  ? -6.402  107.321 -15.961 1.00 30.44 ? 70  ASP B N     1 
ATOM   2577 C CA    . ASP B 1 70  ? -7.766  107.710 -15.553 1.00 30.08 ? 70  ASP B CA    1 
ATOM   2578 C C     . ASP B 1 70  ? -8.006  109.142 -16.006 1.00 29.97 ? 70  ASP B C     1 
ATOM   2579 O O     . ASP B 1 70  ? -7.463  110.076 -15.421 1.00 29.47 ? 70  ASP B O     1 
ATOM   2580 C CB    . ASP B 1 70  ? -7.904  107.550 -14.045 1.00 29.50 ? 70  ASP B CB    1 
ATOM   2581 C CG    . ASP B 1 70  ? -9.243  107.940 -13.469 1.00 29.52 ? 70  ASP B CG    1 
ATOM   2582 O OD1   . ASP B 1 70  ? -10.079 108.491 -14.209 1.00 29.79 ? 70  ASP B OD1   1 
ATOM   2583 O OD2   . ASP B 1 70  ? -9.473  107.694 -12.263 1.00 28.47 ? 70  ASP B OD2   1 
ATOM   2584 N N     . ASN B 1 71  ? -8.766  109.353 -17.079 1.00 30.51 ? 71  ASN B N     1 
ATOM   2585 C CA    . ASN B 1 71  ? -9.045  110.693 -17.584 1.00 30.69 ? 71  ASN B CA    1 
ATOM   2586 C C     . ASN B 1 71  ? -10.045 111.450 -16.725 1.00 31.22 ? 71  ASN B C     1 
ATOM   2587 O O     . ASN B 1 71  ? -10.004 112.675 -16.647 1.00 31.49 ? 71  ASN B O     1 
ATOM   2588 C CB    . ASN B 1 71  ? -9.529  110.739 -19.019 1.00 29.14 ? 71  ASN B CB    1 
ATOM   2589 C CG    . ASN B 1 71  ? -8.419  110.334 -19.961 1.00 32.22 ? 71  ASN B CG    1 
ATOM   2590 O OD1   . ASN B 1 71  ? -8.683  109.664 -20.965 1.00 36.02 ? 71  ASN B OD1   1 
ATOM   2591 N ND2   . ASN B 1 71  ? -7.179  110.681 -19.654 1.00 30.34 ? 71  ASN B ND2   1 
ATOM   2592 N N     . THR B 1 72  ? -10.904 110.742 -16.003 1.00 31.71 ? 72  THR B N     1 
ATOM   2593 C CA    . THR B 1 72  ? -11.812 111.396 -15.074 1.00 31.58 ? 72  THR B CA    1 
ATOM   2594 C C     . THR B 1 72  ? -11.061 111.980 -13.902 1.00 31.29 ? 72  THR B C     1 
ATOM   2595 O O     . THR B 1 72  ? -11.306 113.160 -13.664 1.00 32.14 ? 72  THR B O     1 
ATOM   2596 C CB    . THR B 1 72  ? -12.974 110.495 -14.644 1.00 31.57 ? 72  THR B CB    1 
ATOM   2597 O OG1   . THR B 1 72  ? -13.689 110.161 -15.839 1.00 30.99 ? 72  THR B OG1   1 
ATOM   2598 C CG2   . THR B 1 72  ? -13.920 111.202 -13.694 1.00 31.13 ? 72  THR B CG2   1 
ATOM   2599 N N     . ASN B 1 73  ? -10.157 111.287 -13.243 1.00 31.26 ? 73  ASN B N     1 
ATOM   2600 C CA    . ASN B 1 73  ? -9.415  111.919 -12.156 1.00 31.99 ? 73  ASN B CA    1 
ATOM   2601 C C     . ASN B 1 73  ? -8.030  112.411 -12.563 1.00 32.18 ? 73  ASN B C     1 
ATOM   2602 O O     . ASN B 1 73  ? -7.202  112.728 -11.711 1.00 31.74 ? 73  ASN B O     1 
ATOM   2603 C CB    . ASN B 1 73  ? -9.293  110.956 -10.984 1.00 33.38 ? 73  ASN B CB    1 
ATOM   2604 C CG    . ASN B 1 73  ? -10.616 110.341 -10.605 1.00 34.78 ? 73  ASN B CG    1 
ATOM   2605 O OD1   . ASN B 1 73  ? -10.995 109.318 -11.171 1.00 36.23 ? 73  ASN B OD1   1 
ATOM   2606 N ND2   . ASN B 1 73  ? -11.324 110.947 -9.665  1.00 35.84 ? 73  ASN B ND2   1 
ATOM   2607 N N     . LYS B 1 74  ? -7.747  112.561 -13.852 1.00 32.57 ? 74  LYS B N     1 
ATOM   2608 C CA    . LYS B 1 74  ? -6.426  112.961 -14.302 1.00 33.28 ? 74  LYS B CA    1 
ATOM   2609 C C     . LYS B 1 74  ? -5.370  112.219 -13.481 1.00 32.78 ? 74  LYS B C     1 
ATOM   2610 O O     . LYS B 1 74  ? -4.479  112.855 -12.924 1.00 33.12 ? 74  LYS B O     1 
ATOM   2611 C CB    . LYS B 1 74  ? -6.203  114.461 -14.120 1.00 38.41 ? 74  LYS B CB    1 
ATOM   2612 C CG    . LYS B 1 74  ? -7.307  115.394 -14.573 1.00 41.41 ? 74  LYS B CG    1 
ATOM   2613 C CD    . LYS B 1 74  ? -7.629  115.149 -16.030 1.00 45.02 ? 74  LYS B CD    1 
ATOM   2614 C CE    . LYS B 1 74  ? -8.795  115.987 -16.531 1.00 48.47 ? 74  LYS B CE    1 
ATOM   2615 N NZ    . LYS B 1 74  ? -9.175  115.503 -17.903 1.00 49.64 ? 74  LYS B NZ    1 
ATOM   2616 N N     . LEU B 1 75  ? -5.255  110.924 -13.702 1.00 32.11 ? 75  LEU B N     1 
ATOM   2617 C CA    . LEU B 1 75  ? -4.413  110.031 -12.930 1.00 30.75 ? 75  LEU B CA    1 
ATOM   2618 C C     . LEU B 1 75  ? -3.698  109.010 -13.806 1.00 30.34 ? 75  LEU B C     1 
ATOM   2619 O O     . LEU B 1 75  ? -4.221  108.490 -14.797 1.00 30.04 ? 75  LEU B O     1 
ATOM   2620 C CB    . LEU B 1 75  ? -5.382  109.252 -12.011 1.00 29.53 ? 75  LEU B CB    1 
ATOM   2621 C CG    . LEU B 1 75  ? -5.343  109.472 -10.512 1.00 28.37 ? 75  LEU B CG    1 
ATOM   2622 C CD1   . LEU B 1 75  ? -5.042  110.911 -10.139 1.00 28.30 ? 75  LEU B CD1   1 
ATOM   2623 C CD2   . LEU B 1 75  ? -6.616  109.013 -9.835  1.00 26.37 ? 75  LEU B CD2   1 
ATOM   2624 N N     . ILE B 1 76  ? -2.487  108.673 -13.376 1.00 29.85 ? 76  ILE B N     1 
ATOM   2625 C CA    . ILE B 1 76  ? -1.684  107.622 -14.005 1.00 29.06 ? 76  ILE B CA    1 
ATOM   2626 C C     . ILE B 1 76  ? -1.437  106.586 -12.901 1.00 28.83 ? 76  ILE B C     1 
ATOM   2627 O O     . ILE B 1 76  ? -0.748  106.917 -11.936 1.00 28.87 ? 76  ILE B O     1 
ATOM   2628 C CB    . ILE B 1 76  ? -0.354  108.105 -14.582 1.00 26.73 ? 76  ILE B CB    1 
ATOM   2629 C CG1   . ILE B 1 76  ? -0.593  109.170 -15.659 1.00 26.40 ? 76  ILE B CG1   1 
ATOM   2630 C CG2   . ILE B 1 76  ? 0.444   106.945 -15.157 1.00 24.48 ? 76  ILE B CG2   1 
ATOM   2631 C CD1   . ILE B 1 76  ? 0.647   109.957 -16.037 1.00 26.72 ? 76  ILE B CD1   1 
ATOM   2632 N N     . VAL B 1 77  ? -2.285  105.566 -12.856 1.00 28.64 ? 77  VAL B N     1 
ATOM   2633 C CA    . VAL B 1 77  ? -2.217  104.605 -11.766 1.00 28.52 ? 77  VAL B CA    1 
ATOM   2634 C C     . VAL B 1 77  ? -1.411  103.373 -12.136 1.00 28.30 ? 77  VAL B C     1 
ATOM   2635 O O     . VAL B 1 77  ? -1.600  102.862 -13.232 1.00 28.72 ? 77  VAL B O     1 
ATOM   2636 C CB    . VAL B 1 77  ? -3.614  104.121 -11.320 1.00 27.42 ? 77  VAL B CB    1 
ATOM   2637 C CG1   . VAL B 1 77  ? -3.451  103.315 -10.035 1.00 27.73 ? 77  VAL B CG1   1 
ATOM   2638 C CG2   . VAL B 1 77  ? -4.557  105.290 -11.101 1.00 26.41 ? 77  VAL B CG2   1 
ATOM   2639 N N     . LEU B 1 78  ? -0.570  102.905 -11.232 1.00 28.06 ? 78  LEU B N     1 
ATOM   2640 C CA    . LEU B 1 78  ? 0.140   101.642 -11.433 1.00 27.64 ? 78  LEU B CA    1 
ATOM   2641 C C     . LEU B 1 78  ? -0.195  100.757 -10.225 1.00 27.50 ? 78  LEU B C     1 
ATOM   2642 O O     . LEU B 1 78  ? 0.043   101.177 -9.092  1.00 27.34 ? 78  LEU B O     1 
ATOM   2643 C CB    . LEU B 1 78  ? 1.632   101.807 -11.597 1.00 26.26 ? 78  LEU B CB    1 
ATOM   2644 C CG    . LEU B 1 78  ? 2.502   100.569 -11.398 1.00 25.83 ? 78  LEU B CG    1 
ATOM   2645 C CD1   . LEU B 1 78  ? 2.403   99.624  -12.585 1.00 27.16 ? 78  LEU B CD1   1 
ATOM   2646 C CD2   . LEU B 1 78  ? 3.951   100.987 -11.187 1.00 27.20 ? 78  LEU B CD2   1 
ATOM   2647 N N     . SER B 1 79  ? -1.047  99.777  -10.478 1.00 27.23 ? 79  SER B N     1 
ATOM   2648 C CA    . SER B 1 79  ? -1.604  98.928  -9.442  1.00 26.69 ? 79  SER B CA    1 
ATOM   2649 C C     . SER B 1 79  ? -0.975  97.551  -9.543  1.00 26.61 ? 79  SER B C     1 
ATOM   2650 O O     . SER B 1 79  ? -0.974  96.950  -10.617 1.00 26.69 ? 79  SER B O     1 
ATOM   2651 C CB    . SER B 1 79  ? -3.114  98.780  -9.677  1.00 27.29 ? 79  SER B CB    1 
ATOM   2652 O OG    . SER B 1 79  ? -3.690  98.034  -8.627  1.00 29.04 ? 79  SER B OG    1 
ATOM   2653 N N     . PHE B 1 80  ? -0.450  97.083  -8.428  1.00 26.52 ? 80  PHE B N     1 
ATOM   2654 C CA    . PHE B 1 80  ? 0.165   95.760  -8.353  1.00 26.24 ? 80  PHE B CA    1 
ATOM   2655 C C     . PHE B 1 80  ? -0.783  94.755  -7.718  1.00 26.42 ? 80  PHE B C     1 
ATOM   2656 O O     . PHE B 1 80  ? -1.270  95.050  -6.624  1.00 26.54 ? 80  PHE B O     1 
ATOM   2657 C CB    . PHE B 1 80  ? 1.389   95.876  -7.437  1.00 25.34 ? 80  PHE B CB    1 
ATOM   2658 C CG    . PHE B 1 80  ? 2.585   96.507  -8.088  1.00 24.99 ? 80  PHE B CG    1 
ATOM   2659 C CD1   . PHE B 1 80  ? 3.010   97.769  -7.695  1.00 23.33 ? 80  PHE B CD1   1 
ATOM   2660 C CD2   . PHE B 1 80  ? 3.271   95.834  -9.095  1.00 23.89 ? 80  PHE B CD2   1 
ATOM   2661 C CE1   . PHE B 1 80  ? 4.119   98.337  -8.296  1.00 23.97 ? 80  PHE B CE1   1 
ATOM   2662 C CE2   . PHE B 1 80  ? 4.371   96.410  -9.707  1.00 23.74 ? 80  PHE B CE2   1 
ATOM   2663 C CZ    . PHE B 1 80  ? 4.806   97.658  -9.295  1.00 24.04 ? 80  PHE B CZ    1 
ATOM   2664 N N     . ARG B 1 81  ? -0.934  93.559  -8.279  1.00 26.50 ? 81  ARG B N     1 
ATOM   2665 C CA    . ARG B 1 81  ? -1.819  92.575  -7.644  1.00 26.15 ? 81  ARG B CA    1 
ATOM   2666 C C     . ARG B 1 81  ? -1.145  92.011  -6.404  1.00 26.08 ? 81  ARG B C     1 
ATOM   2667 O O     . ARG B 1 81  ? 0.082   91.899  -6.376  1.00 26.15 ? 81  ARG B O     1 
ATOM   2668 C CB    . ARG B 1 81  ? -2.192  91.479  -8.633  1.00 27.33 ? 81  ARG B CB    1 
ATOM   2669 C CG    . ARG B 1 81  ? -2.363  90.099  -8.061  1.00 29.48 ? 81  ARG B CG    1 
ATOM   2670 C CD    . ARG B 1 81  ? -3.331  89.214  -8.746  1.00 32.54 ? 81  ARG B CD    1 
ATOM   2671 N NE    . ARG B 1 81  ? -2.867  88.098  -9.523  1.00 35.86 ? 81  ARG B NE    1 
ATOM   2672 C CZ    . ARG B 1 81  ? -1.746  87.429  -9.582  1.00 36.50 ? 81  ARG B CZ    1 
ATOM   2673 N NH1   . ARG B 1 81  ? -1.611  86.401  -10.408 1.00 35.96 ? 81  ARG B NH1   1 
ATOM   2674 N NH2   . ARG B 1 81  ? -0.726  87.802  -8.819  1.00 39.72 ? 81  ARG B NH2   1 
ATOM   2675 N N     . GLY B 1 82  ? -1.918  91.626  -5.403  1.00 26.06 ? 82  GLY B N     1 
ATOM   2676 C CA    . GLY B 1 82  ? -1.330  91.002  -4.219  1.00 26.65 ? 82  GLY B CA    1 
ATOM   2677 C C     . GLY B 1 82  ? -0.970  89.562  -4.558  1.00 27.29 ? 82  GLY B C     1 
ATOM   2678 O O     . GLY B 1 82  ? -0.818  89.155  -5.711  1.00 26.93 ? 82  GLY B O     1 
ATOM   2679 N N     . SER B 1 83  ? -0.879  88.737  -3.524  1.00 28.30 ? 83  SER B N     1 
ATOM   2680 C CA    . SER B 1 83  ? -0.472  87.342  -3.744  1.00 29.69 ? 83  SER B CA    1 
ATOM   2681 C C     . SER B 1 83  ? -1.657  86.465  -4.108  1.00 30.00 ? 83  SER B C     1 
ATOM   2682 O O     . SER B 1 83  ? -2.718  86.496  -3.495  1.00 29.86 ? 83  SER B O     1 
ATOM   2683 C CB    . SER B 1 83  ? 0.273   86.815  -2.514  1.00 30.20 ? 83  SER B CB    1 
ATOM   2684 O OG    . SER B 1 83  ? -0.132  87.622  -1.405  1.00 33.97 ? 83  SER B OG    1 
ATOM   2685 N N     . ARG B 1 84  ? -1.472  85.662  -5.156  1.00 30.31 ? 84  ARG B N     1 
ATOM   2686 C CA    . ARG B 1 84  ? -2.518  84.763  -5.629  1.00 30.32 ? 84  ARG B CA    1 
ATOM   2687 C C     . ARG B 1 84  ? -1.899  83.447  -6.094  1.00 29.90 ? 84  ARG B C     1 
ATOM   2688 O O     . ARG B 1 84  ? -2.464  82.375  -5.945  1.00 30.04 ? 84  ARG B O     1 
ATOM   2689 C CB    . ARG B 1 84  ? -3.346  85.377  -6.767  1.00 28.95 ? 84  ARG B CB    1 
ATOM   2690 C CG    . ARG B 1 84  ? -4.151  84.342  -7.517  1.00 29.38 ? 84  ARG B CG    1 
ATOM   2691 C CD    . ARG B 1 84  ? -5.469  84.853  -8.037  1.00 31.31 ? 84  ARG B CD    1 
ATOM   2692 N NE    . ARG B 1 84  ? -6.257  85.523  -7.013  1.00 31.83 ? 84  ARG B NE    1 
ATOM   2693 C CZ    . ARG B 1 84  ? -7.419  86.119  -7.290  1.00 33.26 ? 84  ARG B CZ    1 
ATOM   2694 N NH1   . ARG B 1 84  ? -8.104  86.723  -6.318  1.00 33.64 ? 84  ARG B NH1   1 
ATOM   2695 N NH2   . ARG B 1 84  ? -7.893  86.110  -8.530  1.00 32.35 ? 84  ARG B NH2   1 
ATOM   2696 N N     . SER B 1 85  ? -0.780  83.542  -6.787  1.00 29.64 ? 85  SER B N     1 
ATOM   2697 C CA    . SER B 1 85  ? -0.141  82.335  -7.285  1.00 29.82 ? 85  SER B CA    1 
ATOM   2698 C C     . SER B 1 85  ? 0.813   81.758  -6.251  1.00 30.48 ? 85  SER B C     1 
ATOM   2699 O O     . SER B 1 85  ? 1.022   82.269  -5.151  1.00 30.92 ? 85  SER B O     1 
ATOM   2700 C CB    . SER B 1 85  ? 0.535   82.596  -8.622  1.00 27.94 ? 85  SER B CB    1 
ATOM   2701 O OG    . SER B 1 85  ? 1.728   83.306  -8.456  1.00 25.30 ? 85  SER B OG    1 
ATOM   2702 N N     . ILE B 1 86  ? 1.346   80.579  -6.532  1.00 30.57 ? 86  ILE B N     1 
ATOM   2703 C CA    . ILE B 1 86  ? 2.272   79.875  -5.657  1.00 30.95 ? 86  ILE B CA    1 
ATOM   2704 C C     . ILE B 1 86  ? 3.629   80.564  -5.670  1.00 31.34 ? 86  ILE B C     1 
ATOM   2705 O O     . ILE B 1 86  ? 4.360   80.623  -4.674  1.00 30.88 ? 86  ILE B O     1 
ATOM   2706 C CB    . ILE B 1 86  ? 2.395   78.435  -6.188  1.00 33.17 ? 86  ILE B CB    1 
ATOM   2707 C CG1   . ILE B 1 86  ? 1.143   77.614  -5.856  1.00 33.67 ? 86  ILE B CG1   1 
ATOM   2708 C CG2   . ILE B 1 86  ? 3.644   77.691  -5.752  1.00 33.15 ? 86  ILE B CG2   1 
ATOM   2709 C CD1   . ILE B 1 86  ? 1.147   76.276  -6.566  1.00 32.49 ? 86  ILE B CD1   1 
ATOM   2710 N N     . GLU B 1 87  ? 3.984   81.138  -6.829  1.00 31.50 ? 87  GLU B N     1 
ATOM   2711 C CA    . GLU B 1 87  ? 5.225   81.863  -7.007  1.00 31.66 ? 87  GLU B CA    1 
ATOM   2712 C C     . GLU B 1 87  ? 5.210   83.155  -6.199  1.00 31.51 ? 87  GLU B C     1 
ATOM   2713 O O     . GLU B 1 87  ? 6.236   83.585  -5.700  1.00 31.30 ? 87  GLU B O     1 
ATOM   2714 C CB    . GLU B 1 87  ? 5.477   82.301  -8.437  1.00 35.07 ? 87  GLU B CB    1 
ATOM   2715 C CG    . GLU B 1 87  ? 5.746   81.191  -9.422  1.00 41.39 ? 87  GLU B CG    1 
ATOM   2716 C CD    . GLU B 1 87  ? 4.443   80.619  -9.962  1.00 45.79 ? 87  GLU B CD    1 
ATOM   2717 O OE1   . GLU B 1 87  ? 3.557   80.119  -9.231  1.00 45.48 ? 87  GLU B OE1   1 
ATOM   2718 O OE2   . GLU B 1 87  ? 4.290   80.687  -11.209 1.00 48.85 ? 87  GLU B OE2   1 
ATOM   2719 N N     . ASN B 1 88  ? 4.021   83.761  -6.162  1.00 31.67 ? 88  ASN B N     1 
ATOM   2720 C CA    . ASN B 1 88  ? 3.808   84.956  -5.360  1.00 31.81 ? 88  ASN B CA    1 
ATOM   2721 C C     . ASN B 1 88  ? 4.162   84.569  -3.922  1.00 32.42 ? 88  ASN B C     1 
ATOM   2722 O O     . ASN B 1 88  ? 4.911   85.159  -3.167  1.00 32.20 ? 88  ASN B O     1 
ATOM   2723 C CB    . ASN B 1 88  ? 2.324   85.328  -5.339  1.00 30.20 ? 88  ASN B CB    1 
ATOM   2724 C CG    . ASN B 1 88  ? 1.932   86.057  -6.602  1.00 31.35 ? 88  ASN B CG    1 
ATOM   2725 O OD1   . ASN B 1 88  ? 0.749   86.003  -6.940  1.00 32.77 ? 88  ASN B OD1   1 
ATOM   2726 N ND2   . ASN B 1 88  ? 2.925   86.677  -7.228  1.00 29.85 ? 88  ASN B ND2   1 
ATOM   2727 N N     . TRP B 1 89  ? 3.511   83.464  -3.575  1.00 33.63 ? 89  TRP B N     1 
ATOM   2728 C CA    . TRP B 1 89  ? 3.629   82.925  -2.242  1.00 35.02 ? 89  TRP B CA    1 
ATOM   2729 C C     . TRP B 1 89  ? 5.034   82.534  -1.847  1.00 34.57 ? 89  TRP B C     1 
ATOM   2730 O O     . TRP B 1 89  ? 5.490   82.902  -0.755  1.00 34.87 ? 89  TRP B O     1 
ATOM   2731 C CB    . TRP B 1 89  ? 2.577   81.825  -2.051  1.00 41.41 ? 89  TRP B CB    1 
ATOM   2732 C CG    . TRP B 1 89  ? 2.206   82.036  -0.607  1.00 48.28 ? 89  TRP B CG    1 
ATOM   2733 C CD1   . TRP B 1 89  ? 1.564   83.111  -0.055  1.00 50.28 ? 89  TRP B CD1   1 
ATOM   2734 C CD2   . TRP B 1 89  ? 2.547   81.151  0.464   1.00 50.78 ? 89  TRP B CD2   1 
ATOM   2735 N NE1   . TRP B 1 89  ? 1.452   82.937  1.313   1.00 51.87 ? 89  TRP B NE1   1 
ATOM   2736 C CE2   . TRP B 1 89  ? 2.042   81.739  1.647   1.00 51.87 ? 89  TRP B CE2   1 
ATOM   2737 C CE3   . TRP B 1 89  ? 3.164   79.899  0.511   1.00 51.19 ? 89  TRP B CE3   1 
ATOM   2738 C CZ2   . TRP B 1 89  ? 2.165   81.129  2.885   1.00 52.38 ? 89  TRP B CZ2   1 
ATOM   2739 C CZ3   . TRP B 1 89  ? 3.292   79.296  1.751   1.00 53.06 ? 89  TRP B CZ3   1 
ATOM   2740 C CH2   . TRP B 1 89  ? 2.790   79.917  2.912   1.00 53.41 ? 89  TRP B CH2   1 
ATOM   2741 N N     . ILE B 1 90  ? 5.746   81.888  -2.770  1.00 33.60 ? 90  ILE B N     1 
ATOM   2742 C CA    . ILE B 1 90  ? 7.137   81.516  -2.503  1.00 32.75 ? 90  ILE B CA    1 
ATOM   2743 C C     . ILE B 1 90  ? 7.985   82.776  -2.332  1.00 31.77 ? 90  ILE B C     1 
ATOM   2744 O O     . ILE B 1 90  ? 8.793   82.904  -1.422  1.00 31.93 ? 90  ILE B O     1 
ATOM   2745 C CB    . ILE B 1 90  ? 7.717   80.644  -3.630  1.00 33.37 ? 90  ILE B CB    1 
ATOM   2746 C CG1   . ILE B 1 90  ? 7.067   79.269  -3.735  1.00 32.72 ? 90  ILE B CG1   1 
ATOM   2747 C CG2   . ILE B 1 90  ? 9.219   80.492  -3.459  1.00 32.89 ? 90  ILE B CG2   1 
ATOM   2748 C CD1   . ILE B 1 90  ? 6.972   78.502  -2.433  1.00 31.75 ? 90  ILE B CD1   1 
ATOM   2749 N N     . GLY B 1 91  ? 7.835   83.729  -3.234  1.00 30.90 ? 91  GLY B N     1 
ATOM   2750 C CA    . GLY B 1 91  ? 8.411   85.048  -3.153  1.00 30.37 ? 91  GLY B CA    1 
ATOM   2751 C C     . GLY B 1 91  ? 8.295   85.743  -1.813  1.00 29.88 ? 91  GLY B C     1 
ATOM   2752 O O     . GLY B 1 91  ? 9.309   85.989  -1.154  1.00 29.88 ? 91  GLY B O     1 
ATOM   2753 N N     . ASN B 1 92  ? 7.129   85.793  -1.177  1.00 29.77 ? 92  ASN B N     1 
ATOM   2754 C CA    . ASN B 1 92  ? 6.922   86.393  0.122   1.00 29.10 ? 92  ASN B CA    1 
ATOM   2755 C C     . ASN B 1 92  ? 7.754   85.662  1.150   1.00 28.57 ? 92  ASN B C     1 
ATOM   2756 O O     . ASN B 1 92  ? 8.100   86.247  2.164   1.00 28.19 ? 92  ASN B O     1 
ATOM   2757 C CB    . ASN B 1 92  ? 5.459   86.336  0.575   1.00 31.58 ? 92  ASN B CB    1 
ATOM   2758 C CG    . ASN B 1 92  ? 4.479   86.896  -0.422  1.00 33.37 ? 92  ASN B CG    1 
ATOM   2759 O OD1   . ASN B 1 92  ? 3.292   86.568  -0.457  1.00 35.56 ? 92  ASN B OD1   1 
ATOM   2760 N ND2   . ASN B 1 92  ? 4.954   87.763  -1.313  1.00 34.93 ? 92  ASN B ND2   1 
ATOM   2761 N N     . LEU B 1 93  ? 8.043   84.389  0.908   1.00 28.56 ? 93  LEU B N     1 
ATOM   2762 C CA    . LEU B 1 93  ? 8.843   83.619  1.844   1.00 27.97 ? 93  LEU B CA    1 
ATOM   2763 C C     . LEU B 1 93  ? 10.321  83.833  1.872   1.00 27.54 ? 93  LEU B C     1 
ATOM   2764 O O     . LEU B 1 93  ? 10.940  83.389  2.833   1.00 27.67 ? 93  LEU B O     1 
ATOM   2765 C CB    . LEU B 1 93  ? 8.510   82.123  1.663   1.00 26.39 ? 93  LEU B CB    1 
ATOM   2766 C CG    . LEU B 1 93  ? 7.056   81.888  2.087   1.00 23.80 ? 93  LEU B CG    1 
ATOM   2767 C CD1   . LEU B 1 93  ? 6.690   80.456  1.851   1.00 22.40 ? 93  LEU B CD1   1 
ATOM   2768 C CD2   . LEU B 1 93  ? 6.884   82.311  3.541   1.00 23.89 ? 93  LEU B CD2   1 
ATOM   2769 N N     . ASN B 1 94  ? 10.895  84.561  0.948   1.00 27.79 ? 94  ASN B N     1 
ATOM   2770 C CA    . ASN B 1 94  ? 12.285  84.995  1.034   1.00 28.15 ? 94  ASN B CA    1 
ATOM   2771 C C     . ASN B 1 94  ? 12.393  86.185  1.974   1.00 28.14 ? 94  ASN B C     1 
ATOM   2772 O O     . ASN B 1 94  ? 13.050  87.124  1.563   1.00 28.00 ? 94  ASN B O     1 
ATOM   2773 C CB    . ASN B 1 94  ? 12.713  85.412  -0.368  1.00 29.85 ? 94  ASN B CB    1 
ATOM   2774 C CG    . ASN B 1 94  ? 13.071  84.219  -1.229  1.00 32.57 ? 94  ASN B CG    1 
ATOM   2775 O OD1   . ASN B 1 94  ? 14.261  83.885  -1.293  1.00 35.32 ? 94  ASN B OD1   1 
ATOM   2776 N ND2   . ASN B 1 94  ? 12.155  83.537  -1.897  1.00 32.02 ? 94  ASN B ND2   1 
ATOM   2777 N N     . PHE B 1 95  ? 12.280  86.016  3.294   1.00 28.55 ? 95  PHE B N     1 
ATOM   2778 C CA    . PHE B 1 95  ? 12.158  87.155  4.184   1.00 28.80 ? 95  PHE B CA    1 
ATOM   2779 C C     . PHE B 1 95  ? 13.493  87.646  4.691   1.00 29.43 ? 95  PHE B C     1 
ATOM   2780 O O     . PHE B 1 95  ? 13.566  88.578  5.498   1.00 29.51 ? 95  PHE B O     1 
ATOM   2781 C CB    . PHE B 1 95  ? 11.186  86.883  5.323   1.00 28.47 ? 95  PHE B CB    1 
ATOM   2782 C CG    . PHE B 1 95  ? 11.442  85.602  6.056   1.00 29.81 ? 95  PHE B CG    1 
ATOM   2783 C CD1   . PHE B 1 95  ? 10.834  84.435  5.648   1.00 29.71 ? 95  PHE B CD1   1 
ATOM   2784 C CD2   . PHE B 1 95  ? 12.261  85.592  7.177   1.00 30.73 ? 95  PHE B CD2   1 
ATOM   2785 C CE1   . PHE B 1 95  ? 11.064  83.244  6.314   1.00 31.05 ? 95  PHE B CE1   1 
ATOM   2786 C CE2   . PHE B 1 95  ? 12.495  84.411  7.849   1.00 32.11 ? 95  PHE B CE2   1 
ATOM   2787 C CZ    . PHE B 1 95  ? 11.895  83.243  7.410   1.00 32.75 ? 95  PHE B CZ    1 
ATOM   2788 N N     . ASP B 1 96  ? 14.580  87.048  4.205   1.00 30.22 ? 96  ASP B N     1 
ATOM   2789 C CA    . ASP B 1 96  ? 15.892  87.541  4.636   1.00 31.59 ? 96  ASP B CA    1 
ATOM   2790 C C     . ASP B 1 96  ? 16.069  88.971  4.126   1.00 32.13 ? 96  ASP B C     1 
ATOM   2791 O O     . ASP B 1 96  ? 15.509  89.311  3.090   1.00 32.19 ? 96  ASP B O     1 
ATOM   2792 C CB    . ASP B 1 96  ? 17.009  86.647  4.132   1.00 33.29 ? 96  ASP B CB    1 
ATOM   2793 C CG    . ASP B 1 96  ? 17.049  86.666  2.616   1.00 35.79 ? 96  ASP B CG    1 
ATOM   2794 O OD1   . ASP B 1 96  ? 16.073  86.109  2.081   1.00 38.20 ? 96  ASP B OD1   1 
ATOM   2795 O OD2   . ASP B 1 96  ? 17.976  87.212  1.997   1.00 37.07 ? 96  ASP B OD2   1 
ATOM   2796 N N     . LEU B 1 97  ? 16.658  89.843  4.927   1.00 32.97 ? 97  LEU B N     1 
ATOM   2797 C CA    . LEU B 1 97  ? 16.912  91.223  4.557   1.00 33.73 ? 97  LEU B CA    1 
ATOM   2798 C C     . LEU B 1 97  ? 18.085  91.398  3.604   1.00 34.69 ? 97  LEU B C     1 
ATOM   2799 O O     . LEU B 1 97  ? 19.245  91.271  3.971   1.00 35.03 ? 97  LEU B O     1 
ATOM   2800 C CB    . LEU B 1 97  ? 17.188  92.073  5.807   1.00 30.70 ? 97  LEU B CB    1 
ATOM   2801 C CG    . LEU B 1 97  ? 15.940  92.431  6.605   1.00 29.98 ? 97  LEU B CG    1 
ATOM   2802 C CD1   . LEU B 1 97  ? 16.271  92.952  7.990   1.00 29.34 ? 97  LEU B CD1   1 
ATOM   2803 C CD2   . LEU B 1 97  ? 15.109  93.475  5.875   1.00 30.32 ? 97  LEU B CD2   1 
ATOM   2804 N N     . LYS B 1 98  ? 17.793  91.808  2.385   1.00 35.96 ? 98  LYS B N     1 
ATOM   2805 C CA    . LYS B 1 98  ? 18.769  92.101  1.359   1.00 37.60 ? 98  LYS B CA    1 
ATOM   2806 C C     . LYS B 1 98  ? 19.148  93.581  1.492   1.00 38.74 ? 98  LYS B C     1 
ATOM   2807 O O     . LYS B 1 98  ? 18.431  94.390  2.094   1.00 39.04 ? 98  LYS B O     1 
ATOM   2808 C CB    . LYS B 1 98  ? 18.189  91.884  -0.040  1.00 39.87 ? 98  LYS B CB    1 
ATOM   2809 C CG    . LYS B 1 98  ? 19.279  91.563  -1.051  1.00 43.49 ? 98  LYS B CG    1 
ATOM   2810 C CD    . LYS B 1 98  ? 18.749  91.122  -2.396  1.00 44.65 ? 98  LYS B CD    1 
ATOM   2811 C CE    . LYS B 1 98  ? 18.342  92.303  -3.253  1.00 45.96 ? 98  LYS B CE    1 
ATOM   2812 N NZ    . LYS B 1 98  ? 17.729  91.838  -4.537  1.00 48.40 ? 98  LYS B NZ    1 
ATOM   2813 N N     . GLU B 1 99  ? 20.157  93.971  0.732   1.00 39.38 ? 99  GLU B N     1 
ATOM   2814 C CA    . GLU B 1 99  ? 20.795  95.271  0.910   1.00 40.48 ? 99  GLU B CA    1 
ATOM   2815 C C     . GLU B 1 99  ? 20.440  96.175  -0.255  1.00 40.44 ? 99  GLU B C     1 
ATOM   2816 O O     . GLU B 1 99  ? 20.734  95.749  -1.376  1.00 40.66 ? 99  GLU B O     1 
ATOM   2817 C CB    . GLU B 1 99  ? 22.287  94.944  0.866   1.00 45.73 ? 99  GLU B CB    1 
ATOM   2818 C CG    . GLU B 1 99  ? 22.692  93.932  1.920   1.00 52.97 ? 99  GLU B CG    1 
ATOM   2819 C CD    . GLU B 1 99  ? 22.621  92.454  1.562   1.00 55.84 ? 99  GLU B CD    1 
ATOM   2820 O OE1   . GLU B 1 99  ? 22.730  91.661  2.551   1.00 57.42 ? 99  GLU B OE1   1 
ATOM   2821 O OE2   . GLU B 1 99  ? 22.428  92.074  0.379   1.00 57.26 ? 99  GLU B OE2   1 
ATOM   2822 N N     . ILE B 1 100 ? 19.721  97.265  0.001   1.00 39.96 ? 100 ILE B N     1 
ATOM   2823 C CA    . ILE B 1 100 ? 19.268  98.140  -1.078  1.00 39.18 ? 100 ILE B CA    1 
ATOM   2824 C C     . ILE B 1 100 ? 19.848  99.537  -0.905  1.00 39.23 ? 100 ILE B C     1 
ATOM   2825 O O     . ILE B 1 100 ? 19.158  100.548 -1.026  1.00 39.21 ? 100 ILE B O     1 
ATOM   2826 C CB    . ILE B 1 100 ? 17.728  98.192  -1.149  1.00 36.67 ? 100 ILE B CB    1 
ATOM   2827 C CG1   . ILE B 1 100 ? 17.132  98.446  0.236   1.00 35.36 ? 100 ILE B CG1   1 
ATOM   2828 C CG2   . ILE B 1 100 ? 17.133  96.909  -1.706  1.00 35.21 ? 100 ILE B CG2   1 
ATOM   2829 C CD1   . ILE B 1 100 ? 15.871  99.264  0.188   1.00 34.86 ? 100 ILE B CD1   1 
ATOM   2830 N N     . ASN B 1 101 ? 21.178  99.617  -0.929  1.00 39.64 ? 101 ASN B N     1 
ATOM   2831 C CA    . ASN B 1 101 ? 21.928  100.865 -0.791  1.00 39.69 ? 101 ASN B CA    1 
ATOM   2832 C C     . ASN B 1 101 ? 21.703  101.846 -1.930  1.00 39.48 ? 101 ASN B C     1 
ATOM   2833 O O     . ASN B 1 101 ? 21.650  103.053 -1.733  1.00 39.61 ? 101 ASN B O     1 
ATOM   2834 C CB    . ASN B 1 101 ? 23.441  100.636 -0.711  1.00 40.61 ? 101 ASN B CB    1 
ATOM   2835 C CG    . ASN B 1 101 ? 23.889  100.230 0.672   1.00 42.90 ? 101 ASN B CG    1 
ATOM   2836 O OD1   . ASN B 1 101 ? 23.401  100.741 1.691   1.00 45.46 ? 101 ASN B OD1   1 
ATOM   2837 N ND2   . ASN B 1 101 ? 24.823  99.295  0.775   1.00 42.76 ? 101 ASN B ND2   1 
ATOM   2838 N N     . ASP B 1 102 ? 21.559  101.316 -3.141  1.00 39.25 ? 102 ASP B N     1 
ATOM   2839 C CA    . ASP B 1 102 ? 21.122  102.092 -4.286  1.00 39.08 ? 102 ASP B CA    1 
ATOM   2840 C C     . ASP B 1 102 ? 19.900  102.923 -3.902  1.00 38.53 ? 102 ASP B C     1 
ATOM   2841 O O     . ASP B 1 102 ? 19.772  104.049 -4.395  1.00 38.67 ? 102 ASP B O     1 
ATOM   2842 C CB    . ASP B 1 102 ? 20.853  101.201 -5.490  1.00 43.15 ? 102 ASP B CB    1 
ATOM   2843 C CG    . ASP B 1 102 ? 20.075  99.934  -5.236  1.00 48.08 ? 102 ASP B CG    1 
ATOM   2844 O OD1   . ASP B 1 102 ? 19.623  99.289  -6.220  1.00 49.26 ? 102 ASP B OD1   1 
ATOM   2845 O OD2   . ASP B 1 102 ? 19.860  99.482  -4.086  1.00 50.96 ? 102 ASP B OD2   1 
ATOM   2846 N N     . ILE B 1 103 ? 18.911  102.323 -3.237  1.00 37.81 ? 103 ILE B N     1 
ATOM   2847 C CA    . ILE B 1 103 ? 17.740  103.057 -2.782  1.00 37.10 ? 103 ILE B CA    1 
ATOM   2848 C C     . ILE B 1 103 ? 18.197  104.047 -1.707  1.00 36.84 ? 103 ILE B C     1 
ATOM   2849 O O     . ILE B 1 103 ? 18.086  105.259 -1.906  1.00 36.93 ? 103 ILE B O     1 
ATOM   2850 C CB    . ILE B 1 103 ? 16.620  102.163 -2.228  1.00 36.62 ? 103 ILE B CB    1 
ATOM   2851 C CG1   . ILE B 1 103 ? 16.313  100.962 -3.109  1.00 36.97 ? 103 ILE B CG1   1 
ATOM   2852 C CG2   . ILE B 1 103 ? 15.401  103.002 -1.886  1.00 33.86 ? 103 ILE B CG2   1 
ATOM   2853 C CD1   . ILE B 1 103 ? 15.174  100.946 -4.078  1.00 36.68 ? 103 ILE B CD1   1 
ATOM   2854 N N     . CYS B 1 104 ? 18.701  103.576 -0.579  1.00 36.60 ? 104 CYS B N     1 
ATOM   2855 C CA    . CYS B 1 104 ? 19.182  104.460 0.468   1.00 37.12 ? 104 CYS B CA    1 
ATOM   2856 C C     . CYS B 1 104 ? 20.282  103.813 1.296   1.00 38.07 ? 104 CYS B C     1 
ATOM   2857 O O     . CYS B 1 104 ? 20.418  102.580 1.292   1.00 38.90 ? 104 CYS B O     1 
ATOM   2858 C CB    . CYS B 1 104 ? 18.104  105.003 1.379   1.00 35.66 ? 104 CYS B CB    1 
ATOM   2859 S SG    . CYS B 1 104 ? 16.789  103.906 1.916   1.00 35.54 ? 104 CYS B SG    1 
ATOM   2860 N N     . SER B 1 105 ? 21.105  104.604 1.975   1.00 38.35 ? 105 SER B N     1 
ATOM   2861 C CA    . SER B 1 105 ? 22.317  104.073 2.590   1.00 39.29 ? 105 SER B CA    1 
ATOM   2862 C C     . SER B 1 105 ? 22.027  103.465 3.942   1.00 39.26 ? 105 SER B C     1 
ATOM   2863 O O     . SER B 1 105 ? 21.324  104.073 4.748   1.00 39.87 ? 105 SER B O     1 
ATOM   2864 C CB    . SER B 1 105 ? 23.374  105.182 2.741   1.00 42.52 ? 105 SER B CB    1 
ATOM   2865 O OG    . SER B 1 105 ? 23.289  105.984 1.556   1.00 46.89 ? 105 SER B OG    1 
ATOM   2866 N N     . GLY B 1 106 ? 22.359  102.182 4.054   1.00 38.90 ? 106 GLY B N     1 
ATOM   2867 C CA    . GLY B 1 106 ? 22.101  101.468 5.300   1.00 38.97 ? 106 GLY B CA    1 
ATOM   2868 C C     . GLY B 1 106 ? 20.786  100.701 5.192   1.00 38.93 ? 106 GLY B C     1 
ATOM   2869 O O     . GLY B 1 106 ? 20.430  99.936  6.082   1.00 39.36 ? 106 GLY B O     1 
ATOM   2870 N N     . CYS B 1 107 ? 19.964  101.115 4.244   1.00 38.57 ? 107 CYS B N     1 
ATOM   2871 C CA    . CYS B 1 107 ? 18.671  100.542 3.986   1.00 37.89 ? 107 CYS B CA    1 
ATOM   2872 C C     . CYS B 1 107 ? 18.814  99.095  3.549   1.00 37.55 ? 107 CYS B C     1 
ATOM   2873 O O     . CYS B 1 107 ? 19.670  98.748  2.745   1.00 37.62 ? 107 CYS B O     1 
ATOM   2874 C CB    . CYS B 1 107 ? 18.003  101.365 2.874   1.00 36.07 ? 107 CYS B CB    1 
ATOM   2875 S SG    . CYS B 1 107 ? 17.462  102.956 3.565   1.00 35.24 ? 107 CYS B SG    1 
ATOM   2876 N N     . ARG B 1 108 ? 18.028  98.251  4.195   1.00 37.31 ? 108 ARG B N     1 
ATOM   2877 C CA    . ARG B 1 108 ? 17.960  96.854  3.781   1.00 37.19 ? 108 ARG B CA    1 
ATOM   2878 C C     . ARG B 1 108 ? 16.495  96.477  3.646   1.00 35.85 ? 108 ARG B C     1 
ATOM   2879 O O     . ARG B 1 108 ? 15.686  96.861  4.481   1.00 35.47 ? 108 ARG B O     1 
ATOM   2880 C CB    . ARG B 1 108 ? 18.741  95.944  4.728   1.00 41.85 ? 108 ARG B CB    1 
ATOM   2881 C CG    . ARG B 1 108 ? 20.194  95.872  4.257   1.00 45.42 ? 108 ARG B CG    1 
ATOM   2882 C CD    . ARG B 1 108 ? 21.053  95.431  5.429   1.00 49.73 ? 108 ARG B CD    1 
ATOM   2883 N NE    . ARG B 1 108 ? 21.114  93.972  5.378   1.00 53.66 ? 108 ARG B NE    1 
ATOM   2884 C CZ    . ARG B 1 108 ? 21.052  93.225  6.471   1.00 56.09 ? 108 ARG B CZ    1 
ATOM   2885 N NH1   . ARG B 1 108 ? 20.937  93.766  7.675   1.00 57.46 ? 108 ARG B NH1   1 
ATOM   2886 N NH2   . ARG B 1 108 ? 21.078  91.904  6.331   1.00 58.03 ? 108 ARG B NH2   1 
ATOM   2887 N N     . GLY B 1 109 ? 16.188  95.918  2.485   1.00 35.11 ? 109 GLY B N     1 
ATOM   2888 C CA    . GLY B 1 109 ? 14.800  95.540  2.229   1.00 34.45 ? 109 GLY B CA    1 
ATOM   2889 C C     . GLY B 1 109 ? 14.570  94.046  2.128   1.00 34.02 ? 109 GLY B C     1 
ATOM   2890 O O     . GLY B 1 109 ? 15.463  93.258  1.819   1.00 33.70 ? 109 GLY B O     1 
ATOM   2891 N N     . HIS B 1 110 ? 13.329  93.671  2.438   1.00 33.75 ? 110 HIS B N     1 
ATOM   2892 C CA    . HIS B 1 110 ? 12.903  92.275  2.247   1.00 33.20 ? 110 HIS B CA    1 
ATOM   2893 C C     . HIS B 1 110 ? 13.363  91.786  0.878   1.00 32.94 ? 110 HIS B C     1 
ATOM   2894 O O     . HIS B 1 110 ? 13.268  92.461  -0.132  1.00 32.66 ? 110 HIS B O     1 
ATOM   2895 C CB    . HIS B 1 110 ? 11.388  92.207  2.275   1.00 31.30 ? 110 HIS B CB    1 
ATOM   2896 C CG    . HIS B 1 110 ? 10.746  90.883  2.038   1.00 30.56 ? 110 HIS B CG    1 
ATOM   2897 N ND1   . HIS B 1 110 ? 10.457  90.332  0.804   1.00 29.24 ? 110 HIS B ND1   1 
ATOM   2898 C CD2   . HIS B 1 110 ? 10.190  90.025  2.941   1.00 29.72 ? 110 HIS B CD2   1 
ATOM   2899 C CE1   . HIS B 1 110 ? 9.762   89.228  0.959   1.00 27.51 ? 110 HIS B CE1   1 
ATOM   2900 N NE2   . HIS B 1 110 ? 9.596   89.004  2.251   1.00 27.42 ? 110 HIS B NE2   1 
ATOM   2901 N N     . ASP B 1 111 ? 13.837  90.563  0.855   1.00 33.19 ? 111 ASP B N     1 
ATOM   2902 C CA    . ASP B 1 111 ? 14.365  90.030  -0.413  1.00 33.67 ? 111 ASP B CA    1 
ATOM   2903 C C     . ASP B 1 111 ? 13.239  89.506  -1.271  1.00 33.60 ? 111 ASP B C     1 
ATOM   2904 O O     . ASP B 1 111 ? 12.191  89.101  -0.696  1.00 34.79 ? 111 ASP B O     1 
ATOM   2905 C CB    . ASP B 1 111 ? 15.334  88.922  0.009   1.00 35.86 ? 111 ASP B CB    1 
ATOM   2906 C CG    . ASP B 1 111 ? 16.190  88.497  -1.163  1.00 39.37 ? 111 ASP B CG    1 
ATOM   2907 O OD1   . ASP B 1 111 ? 17.103  87.685  -0.920  1.00 41.47 ? 111 ASP B OD1   1 
ATOM   2908 O OD2   . ASP B 1 111 ? 15.960  88.961  -2.304  1.00 40.60 ? 111 ASP B OD2   1 
ATOM   2909 N N     . GLY B 1 112 ? 13.222  89.568  -2.600  1.00 32.34 ? 112 GLY B N     1 
ATOM   2910 C CA    . GLY B 1 112 ? 11.970  89.017  -3.206  1.00 31.64 ? 112 GLY B CA    1 
ATOM   2911 C C     . GLY B 1 112 ? 10.960  90.129  -3.404  1.00 30.78 ? 112 GLY B C     1 
ATOM   2912 O O     . GLY B 1 112 ? 10.594  90.268  -4.581  1.00 30.84 ? 112 GLY B O     1 
ATOM   2913 N N     . PHE B 1 113 ? 10.585  90.949  -2.417  1.00 29.82 ? 113 PHE B N     1 
ATOM   2914 C CA    . PHE B 1 113 ? 9.807   92.148  -2.754  1.00 28.48 ? 113 PHE B CA    1 
ATOM   2915 C C     . PHE B 1 113 ? 10.779  92.998  -3.596  1.00 28.29 ? 113 PHE B C     1 
ATOM   2916 O O     . PHE B 1 113 ? 10.648  93.135  -4.811  1.00 28.42 ? 113 PHE B O     1 
ATOM   2917 C CB    . PHE B 1 113 ? 9.287   92.958  -1.589  1.00 24.93 ? 113 PHE B CB    1 
ATOM   2918 C CG    . PHE B 1 113 ? 8.332   92.312  -0.634  1.00 23.29 ? 113 PHE B CG    1 
ATOM   2919 C CD1   . PHE B 1 113 ? 7.548   91.239  -1.049  1.00 22.84 ? 113 PHE B CD1   1 
ATOM   2920 C CD2   . PHE B 1 113 ? 8.216   92.750  0.677   1.00 20.90 ? 113 PHE B CD2   1 
ATOM   2921 C CE1   . PHE B 1 113 ? 6.694   90.594  -0.178  1.00 20.16 ? 113 PHE B CE1   1 
ATOM   2922 C CE2   . PHE B 1 113 ? 7.389   92.098  1.564   1.00 19.81 ? 113 PHE B CE2   1 
ATOM   2923 C CZ    . PHE B 1 113 ? 6.599   91.061  1.119   1.00 20.24 ? 113 PHE B CZ    1 
ATOM   2924 N N     . THR B 1 114 ? 11.983  93.152  -3.064  1.00 28.10 ? 114 THR B N     1 
ATOM   2925 C CA    . THR B 1 114 ? 13.089  93.829  -3.718  1.00 28.38 ? 114 THR B CA    1 
ATOM   2926 C C     . THR B 1 114 ? 13.489  93.192  -5.039  1.00 28.95 ? 114 THR B C     1 
ATOM   2927 O O     . THR B 1 114 ? 13.867  93.857  -6.006  1.00 29.15 ? 114 THR B O     1 
ATOM   2928 C CB    . THR B 1 114 ? 14.293  93.902  -2.757  1.00 26.23 ? 114 THR B CB    1 
ATOM   2929 O OG1   . THR B 1 114 ? 14.046  94.916  -1.763  1.00 25.64 ? 114 THR B OG1   1 
ATOM   2930 C CG2   . THR B 1 114 ? 15.596  94.240  -3.429  1.00 24.61 ? 114 THR B CG2   1 
ATOM   2931 N N     . SER B 1 115 ? 13.592  91.875  -5.088  1.00 29.51 ? 115 SER B N     1 
ATOM   2932 C CA    . SER B 1 115 ? 14.001  91.154  -6.288  1.00 29.75 ? 115 SER B CA    1 
ATOM   2933 C C     . SER B 1 115 ? 12.927  91.192  -7.360  1.00 29.98 ? 115 SER B C     1 
ATOM   2934 O O     . SER B 1 115 ? 13.178  91.334  -8.555  1.00 28.95 ? 115 SER B O     1 
ATOM   2935 C CB    . SER B 1 115 ? 14.376  89.722  -5.887  1.00 29.78 ? 115 SER B CB    1 
ATOM   2936 O OG    . SER B 1 115 ? 15.424  89.790  -4.924  1.00 32.03 ? 115 SER B OG    1 
ATOM   2937 N N     . SER B 1 116 ? 11.669  91.015  -6.933  1.00 30.71 ? 116 SER B N     1 
ATOM   2938 C CA    . SER B 1 116 ? 10.544  91.112  -7.860  1.00 30.81 ? 116 SER B CA    1 
ATOM   2939 C C     . SER B 1 116 ? 10.569  92.506  -8.485  1.00 30.70 ? 116 SER B C     1 
ATOM   2940 O O     . SER B 1 116 ? 10.748  92.658  -9.688  1.00 30.00 ? 116 SER B O     1 
ATOM   2941 C CB    . SER B 1 116 ? 9.210   90.901  -7.150  1.00 31.40 ? 116 SER B CB    1 
ATOM   2942 O OG    . SER B 1 116 ? 9.128   89.560  -6.709  1.00 34.84 ? 116 SER B OG    1 
ATOM   2943 N N     . TRP B 1 117 ? 10.579  93.533  -7.626  1.00 30.85 ? 117 TRP B N     1 
ATOM   2944 C CA    . TRP B 1 117 ? 10.596  94.894  -8.145  1.00 31.04 ? 117 TRP B CA    1 
ATOM   2945 C C     . TRP B 1 117 ? 11.768  95.120  -9.088  1.00 31.37 ? 117 TRP B C     1 
ATOM   2946 O O     . TRP B 1 117 ? 11.622  95.533  -10.236 1.00 31.06 ? 117 TRP B O     1 
ATOM   2947 C CB    . TRP B 1 117 ? 10.559  95.966  -7.055  1.00 28.70 ? 117 TRP B CB    1 
ATOM   2948 C CG    . TRP B 1 117 ? 10.911  97.296  -7.668  1.00 27.58 ? 117 TRP B CG    1 
ATOM   2949 C CD1   . TRP B 1 117 ? 12.024  98.039  -7.426  1.00 26.59 ? 117 TRP B CD1   1 
ATOM   2950 C CD2   . TRP B 1 117 ? 10.199  97.958  -8.723  1.00 27.21 ? 117 TRP B CD2   1 
ATOM   2951 N NE1   . TRP B 1 117 ? 12.026  99.152  -8.223  1.00 26.14 ? 117 TRP B NE1   1 
ATOM   2952 C CE2   . TRP B 1 117 ? 10.922  99.134  -9.032  1.00 26.71 ? 117 TRP B CE2   1 
ATOM   2953 C CE3   . TRP B 1 117 ? 9.016   97.693  -9.422  1.00 24.91 ? 117 TRP B CE3   1 
ATOM   2954 C CZ2   . TRP B 1 117 ? 10.496  100.039 -10.008 1.00 24.61 ? 117 TRP B CZ2   1 
ATOM   2955 C CZ3   . TRP B 1 117 ? 8.610   98.594  -10.388 1.00 23.49 ? 117 TRP B CZ3   1 
ATOM   2956 C CH2   . TRP B 1 117 ? 9.342   99.750  -10.678 1.00 22.34 ? 117 TRP B CH2   1 
ATOM   2957 N N     . ARG B 1 118 ? 12.982  94.840  -8.628  1.00 32.05 ? 118 ARG B N     1 
ATOM   2958 C CA    . ARG B 1 118 ? 14.186  94.979  -9.430  1.00 32.33 ? 118 ARG B CA    1 
ATOM   2959 C C     . ARG B 1 118 ? 14.147  94.209  -10.729 1.00 31.89 ? 118 ARG B C     1 
ATOM   2960 O O     . ARG B 1 118 ? 14.559  94.755  -11.755 1.00 32.00 ? 118 ARG B O     1 
ATOM   2961 C CB    . ARG B 1 118 ? 15.444  94.647  -8.632  1.00 36.83 ? 118 ARG B CB    1 
ATOM   2962 C CG    . ARG B 1 118 ? 16.384  95.822  -8.436  1.00 43.78 ? 118 ARG B CG    1 
ATOM   2963 C CD    . ARG B 1 118 ? 16.855  96.025  -7.008  1.00 49.16 ? 118 ARG B CD    1 
ATOM   2964 N NE    . ARG B 1 118 ? 17.130  97.396  -6.619  1.00 53.53 ? 118 ARG B NE    1 
ATOM   2965 C CZ    . ARG B 1 118 ? 16.723  98.578  -7.064  1.00 54.77 ? 118 ARG B CZ    1 
ATOM   2966 N NH1   . ARG B 1 118 ? 15.909  98.784  -8.096  1.00 53.03 ? 118 ARG B NH1   1 
ATOM   2967 N NH2   . ARG B 1 118 ? 17.173  99.655  -6.410  1.00 55.04 ? 118 ARG B NH2   1 
ATOM   2968 N N     . SER B 1 119 ? 13.421  93.104  -10.839 1.00 32.02 ? 119 SER B N     1 
ATOM   2969 C CA    . SER B 1 119 ? 13.345  92.306  -12.048 1.00 31.51 ? 119 SER B CA    1 
ATOM   2970 C C     . SER B 1 119 ? 12.441  92.937  -13.089 1.00 31.72 ? 119 SER B C     1 
ATOM   2971 O O     . SER B 1 119 ? 12.480  92.539  -14.247 1.00 32.15 ? 119 SER B O     1 
ATOM   2972 C CB    . SER B 1 119 ? 12.854  90.881  -11.804 1.00 28.81 ? 119 SER B CB    1 
ATOM   2973 O OG    . SER B 1 119 ? 11.475  90.811  -11.553 1.00 28.17 ? 119 SER B OG    1 
ATOM   2974 N N     . VAL B 1 120 ? 11.593  93.869  -12.690 1.00 32.11 ? 120 VAL B N     1 
ATOM   2975 C CA    . VAL B 1 120 ? 10.631  94.456  -13.620 1.00 31.85 ? 120 VAL B CA    1 
ATOM   2976 C C     . VAL B 1 120 ? 10.723  95.968  -13.616 1.00 31.92 ? 120 VAL B C     1 
ATOM   2977 O O     . VAL B 1 120 ? 10.202  96.652  -14.494 1.00 32.25 ? 120 VAL B O     1 
ATOM   2978 C CB    . VAL B 1 120 ? 9.236   93.957  -13.215 1.00 30.26 ? 120 VAL B CB    1 
ATOM   2979 C CG1   . VAL B 1 120 ? 8.606   94.853  -12.172 1.00 29.04 ? 120 VAL B CG1   1 
ATOM   2980 C CG2   . VAL B 1 120 ? 8.373   93.756  -14.442 1.00 30.86 ? 120 VAL B CG2   1 
ATOM   2981 N N     . ALA B 1 121 ? 11.651  96.472  -12.814 1.00 32.00 ? 121 ALA B N     1 
ATOM   2982 C CA    . ALA B 1 121 ? 11.864  97.890  -12.625 1.00 32.25 ? 121 ALA B CA    1 
ATOM   2983 C C     . ALA B 1 121 ? 12.109  98.692  -13.877 1.00 32.63 ? 121 ALA B C     1 
ATOM   2984 O O     . ALA B 1 121 ? 11.582  99.792  -13.986 1.00 32.28 ? 121 ALA B O     1 
ATOM   2985 C CB    . ALA B 1 121 ? 12.936  98.155  -11.585 1.00 30.81 ? 121 ALA B CB    1 
ATOM   2986 N N     . ASP B 1 122 ? 12.872  98.231  -14.850 1.00 34.24 ? 122 ASP B N     1 
ATOM   2987 C CA    . ASP B 1 122 ? 13.102  98.979  -16.082 1.00 35.67 ? 122 ASP B CA    1 
ATOM   2988 C C     . ASP B 1 122 ? 11.871  99.134  -16.959 1.00 35.67 ? 122 ASP B C     1 
ATOM   2989 O O     . ASP B 1 122 ? 11.404  100.253 -17.140 1.00 36.63 ? 122 ASP B O     1 
ATOM   2990 C CB    . ASP B 1 122 ? 14.216  98.400  -16.949 1.00 38.93 ? 122 ASP B CB    1 
ATOM   2991 C CG    . ASP B 1 122 ? 15.577  98.558  -16.298 1.00 43.43 ? 122 ASP B CG    1 
ATOM   2992 O OD1   . ASP B 1 122 ? 16.513  97.783  -16.627 1.00 46.50 ? 122 ASP B OD1   1 
ATOM   2993 O OD2   . ASP B 1 122 ? 15.811  99.438  -15.430 1.00 43.73 ? 122 ASP B OD2   1 
ATOM   2994 N N     . THR B 1 123 ? 11.288  98.030  -17.382 1.00 35.33 ? 123 THR B N     1 
ATOM   2995 C CA    . THR B 1 123 ? 10.092  98.058  -18.212 1.00 34.69 ? 123 THR B CA    1 
ATOM   2996 C C     . THR B 1 123 ? 9.023   98.951  -17.613 1.00 34.23 ? 123 THR B C     1 
ATOM   2997 O O     . THR B 1 123 ? 8.530   99.829  -18.322 1.00 33.61 ? 123 THR B O     1 
ATOM   2998 C CB    . THR B 1 123 ? 9.624   96.603  -18.369 1.00 36.01 ? 123 THR B CB    1 
ATOM   2999 O OG1   . THR B 1 123 ? 10.733  95.873  -18.917 1.00 36.74 ? 123 THR B OG1   1 
ATOM   3000 C CG2   . THR B 1 123 ? 8.413   96.474  -19.263 1.00 35.04 ? 123 THR B CG2   1 
ATOM   3001 N N     . LEU B 1 124 ? 8.715   98.810  -16.327 1.00 33.78 ? 124 LEU B N     1 
ATOM   3002 C CA    . LEU B 1 124 ? 7.682   99.624  -15.706 1.00 33.39 ? 124 LEU B CA    1 
ATOM   3003 C C     . LEU B 1 124 ? 8.063   101.081 -15.619 1.00 33.57 ? 124 LEU B C     1 
ATOM   3004 O O     . LEU B 1 124 ? 7.327   101.954 -16.089 1.00 33.32 ? 124 LEU B O     1 
ATOM   3005 C CB    . LEU B 1 124 ? 7.264   99.041  -14.359 1.00 31.11 ? 124 LEU B CB    1 
ATOM   3006 C CG    . LEU B 1 124 ? 6.030   98.151  -14.314 1.00 29.55 ? 124 LEU B CG    1 
ATOM   3007 C CD1   . LEU B 1 124 ? 5.431   97.861  -15.682 1.00 29.37 ? 124 LEU B CD1   1 
ATOM   3008 C CD2   . LEU B 1 124 ? 6.370   96.815  -13.678 1.00 29.34 ? 124 LEU B CD2   1 
ATOM   3009 N N     . ARG B 1 125 ? 9.285   101.368 -15.190 1.00 34.20 ? 125 ARG B N     1 
ATOM   3010 C CA    . ARG B 1 125 ? 9.784   102.733 -15.090 1.00 35.35 ? 125 ARG B CA    1 
ATOM   3011 C C     . ARG B 1 125 ? 9.555   103.500 -16.395 1.00 35.44 ? 125 ARG B C     1 
ATOM   3012 O O     . ARG B 1 125 ? 9.275   104.701 -16.454 1.00 35.48 ? 125 ARG B O     1 
ATOM   3013 C CB    . ARG B 1 125 ? 11.281  102.810 -14.761 1.00 38.77 ? 125 ARG B CB    1 
ATOM   3014 C CG    . ARG B 1 125 ? 11.797  104.239 -14.749 1.00 43.36 ? 125 ARG B CG    1 
ATOM   3015 C CD    . ARG B 1 125 ? 13.300  104.369 -14.711 1.00 48.55 ? 125 ARG B CD    1 
ATOM   3016 N NE    . ARG B 1 125 ? 13.865  103.981 -13.426 1.00 55.12 ? 125 ARG B NE    1 
ATOM   3017 C CZ    . ARG B 1 125 ? 14.595  102.910 -13.115 1.00 57.61 ? 125 ARG B CZ    1 
ATOM   3018 N NH1   . ARG B 1 125 ? 15.036  102.684 -11.868 1.00 57.57 ? 125 ARG B NH1   1 
ATOM   3019 N NH2   . ARG B 1 125 ? 14.918  102.026 -14.064 1.00 57.34 ? 125 ARG B NH2   1 
ATOM   3020 N N     . GLN B 1 126 ? 9.899   102.858 -17.501 1.00 35.17 ? 126 GLN B N     1 
ATOM   3021 C CA    . GLN B 1 126 ? 9.641   103.371 -18.822 1.00 35.09 ? 126 GLN B CA    1 
ATOM   3022 C C     . GLN B 1 126 ? 8.190   103.577 -19.213 1.00 34.55 ? 126 GLN B C     1 
ATOM   3023 O O     . GLN B 1 126 ? 7.896   104.605 -19.831 1.00 34.51 ? 126 GLN B O     1 
ATOM   3024 C CB    . GLN B 1 126 ? 10.268  102.409 -19.831 1.00 38.41 ? 126 GLN B CB    1 
ATOM   3025 C CG    . GLN B 1 126 ? 10.483  103.148 -21.145 1.00 45.11 ? 126 GLN B CG    1 
ATOM   3026 C CD    . GLN B 1 126 ? 10.231  102.192 -22.298 1.00 49.33 ? 126 GLN B CD    1 
ATOM   3027 O OE1   . GLN B 1 126 ? 9.283   102.386 -23.066 1.00 51.19 ? 126 GLN B OE1   1 
ATOM   3028 N NE2   . GLN B 1 126 ? 11.073  101.166 -22.404 1.00 51.46 ? 126 GLN B NE2   1 
ATOM   3029 N N     . LYS B 1 127 ? 7.278   102.650 -18.951 1.00 34.01 ? 127 LYS B N     1 
ATOM   3030 C CA    . LYS B 1 127 ? 5.872   102.822 -19.291 1.00 32.77 ? 127 LYS B CA    1 
ATOM   3031 C C     . LYS B 1 127 ? 5.312   104.007 -18.502 1.00 32.81 ? 127 LYS B C     1 
ATOM   3032 O O     . LYS B 1 127 ? 4.582   104.832 -19.052 1.00 32.09 ? 127 LYS B O     1 
ATOM   3033 C CB    . LYS B 1 127 ? 5.089   101.554 -18.993 1.00 30.18 ? 127 LYS B CB    1 
ATOM   3034 C CG    . LYS B 1 127 ? 5.624   100.334 -19.719 1.00 28.21 ? 127 LYS B CG    1 
ATOM   3035 C CD    . LYS B 1 127 ? 4.949   100.207 -21.058 1.00 28.05 ? 127 LYS B CD    1 
ATOM   3036 C CE    . LYS B 1 127 ? 5.320   98.947  -21.814 1.00 28.89 ? 127 LYS B CE    1 
ATOM   3037 N NZ    . LYS B 1 127 ? 4.690   98.920  -23.179 1.00 28.14 ? 127 LYS B NZ    1 
ATOM   3038 N N     . VAL B 1 128 ? 5.706   104.126 -17.232 1.00 32.67 ? 128 VAL B N     1 
ATOM   3039 C CA    . VAL B 1 128 ? 5.231   105.240 -16.415 1.00 32.81 ? 128 VAL B CA    1 
ATOM   3040 C C     . VAL B 1 128 ? 5.732   106.560 -16.985 1.00 33.52 ? 128 VAL B C     1 
ATOM   3041 O O     . VAL B 1 128 ? 5.009   107.548 -17.122 1.00 33.39 ? 128 VAL B O     1 
ATOM   3042 C CB    . VAL B 1 128 ? 5.676   105.123 -14.951 1.00 30.46 ? 128 VAL B CB    1 
ATOM   3043 C CG1   . VAL B 1 128 ? 5.185   106.297 -14.128 1.00 28.53 ? 128 VAL B CG1   1 
ATOM   3044 C CG2   . VAL B 1 128 ? 5.216   103.803 -14.354 1.00 30.23 ? 128 VAL B CG2   1 
ATOM   3045 N N     . GLU B 1 129 ? 7.007   106.597 -17.372 1.00 34.36 ? 129 GLU B N     1 
ATOM   3046 C CA    . GLU B 1 129 ? 7.569   107.828 -17.926 1.00 34.88 ? 129 GLU B CA    1 
ATOM   3047 C C     . GLU B 1 129 ? 6.994   108.177 -19.277 1.00 34.92 ? 129 GLU B C     1 
ATOM   3048 O O     . GLU B 1 129 ? 6.537   109.315 -19.440 1.00 35.10 ? 129 GLU B O     1 
ATOM   3049 C CB    . GLU B 1 129 ? 9.094   107.844 -17.874 1.00 35.89 ? 129 GLU B CB    1 
ATOM   3050 C CG    . GLU B 1 129 ? 9.532   107.921 -16.415 1.00 38.41 ? 129 GLU B CG    1 
ATOM   3051 C CD    . GLU B 1 129 ? 11.033  107.891 -16.211 1.00 40.79 ? 129 GLU B CD    1 
ATOM   3052 O OE1   . GLU B 1 129 ? 11.416  107.989 -15.017 1.00 40.87 ? 129 GLU B OE1   1 
ATOM   3053 O OE2   . GLU B 1 129 ? 11.756  107.771 -17.231 1.00 40.60 ? 129 GLU B OE2   1 
ATOM   3054 N N     . ASP B 1 130 ? 6.733   107.227 -20.172 1.00 35.18 ? 130 ASP B N     1 
ATOM   3055 C CA    . ASP B 1 130 ? 6.011   107.584 -21.397 1.00 35.35 ? 130 ASP B CA    1 
ATOM   3056 C C     . ASP B 1 130 ? 4.636   108.159 -21.052 1.00 35.17 ? 130 ASP B C     1 
ATOM   3057 O O     . ASP B 1 130 ? 4.192   109.091 -21.711 1.00 35.52 ? 130 ASP B O     1 
ATOM   3058 C CB    . ASP B 1 130 ? 5.818   106.406 -22.330 1.00 37.56 ? 130 ASP B CB    1 
ATOM   3059 C CG    . ASP B 1 130 ? 7.085   105.769 -22.838 1.00 40.81 ? 130 ASP B CG    1 
ATOM   3060 O OD1   . ASP B 1 130 ? 8.184   106.348 -22.725 1.00 42.28 ? 130 ASP B OD1   1 
ATOM   3061 O OD2   . ASP B 1 130 ? 6.988   104.634 -23.366 1.00 43.69 ? 130 ASP B OD2   1 
ATOM   3062 N N     . ALA B 1 131 ? 3.901   107.588 -20.106 1.00 34.57 ? 131 ALA B N     1 
ATOM   3063 C CA    . ALA B 1 131 ? 2.593   108.052 -19.705 1.00 33.52 ? 131 ALA B CA    1 
ATOM   3064 C C     . ALA B 1 131 ? 2.687   109.487 -19.208 1.00 33.25 ? 131 ALA B C     1 
ATOM   3065 O O     . ALA B 1 131 ? 1.869   110.322 -19.573 1.00 33.20 ? 131 ALA B O     1 
ATOM   3066 C CB    . ALA B 1 131 ? 2.008   107.203 -18.585 1.00 32.86 ? 131 ALA B CB    1 
ATOM   3067 N N     . VAL B 1 132 ? 3.655   109.737 -18.330 1.00 33.16 ? 132 VAL B N     1 
ATOM   3068 C CA    . VAL B 1 132 ? 3.847   111.079 -17.775 1.00 32.58 ? 132 VAL B CA    1 
ATOM   3069 C C     . VAL B 1 132 ? 4.091   112.084 -18.889 1.00 32.52 ? 132 VAL B C     1 
ATOM   3070 O O     . VAL B 1 132 ? 3.467   113.126 -19.014 1.00 32.56 ? 132 VAL B O     1 
ATOM   3071 C CB    . VAL B 1 132 ? 5.024   111.129 -16.789 1.00 29.30 ? 132 VAL B CB    1 
ATOM   3072 C CG1   . VAL B 1 132 ? 5.174   112.545 -16.277 1.00 27.79 ? 132 VAL B CG1   1 
ATOM   3073 C CG2   . VAL B 1 132 ? 4.782   110.173 -15.634 1.00 29.14 ? 132 VAL B CG2   1 
ATOM   3074 N N     . ARG B 1 133 ? 4.993   111.722 -19.788 1.00 32.68 ? 133 ARG B N     1 
ATOM   3075 C CA    . ARG B 1 133 ? 5.320   112.483 -20.979 1.00 32.66 ? 133 ARG B CA    1 
ATOM   3076 C C     . ARG B 1 133 ? 4.083   112.892 -21.762 1.00 32.72 ? 133 ARG B C     1 
ATOM   3077 O O     . ARG B 1 133 ? 4.049   114.017 -22.248 1.00 33.18 ? 133 ARG B O     1 
ATOM   3078 C CB    . ARG B 1 133 ? 6.233   111.663 -21.884 1.00 31.18 ? 133 ARG B CB    1 
ATOM   3079 C CG    . ARG B 1 133 ? 7.069   112.461 -22.860 1.00 31.05 ? 133 ARG B CG    1 
ATOM   3080 C CD    . ARG B 1 133 ? 8.308   111.689 -23.306 1.00 31.83 ? 133 ARG B CD    1 
ATOM   3081 N N     . GLU B 1 134 ? 3.108   112.035 -21.990 1.00 32.91 ? 134 GLU B N     1 
ATOM   3082 C CA    . GLU B 1 134 ? 1.911   112.389 -22.721 1.00 33.04 ? 134 GLU B CA    1 
ATOM   3083 C C     . GLU B 1 134 ? 0.855   113.057 -21.872 1.00 33.20 ? 134 GLU B C     1 
ATOM   3084 O O     . GLU B 1 134 ? -0.018  113.717 -22.442 1.00 33.44 ? 134 GLU B O     1 
ATOM   3085 C CB    . GLU B 1 134 ? 1.305   111.201 -23.463 1.00 33.66 ? 134 GLU B CB    1 
ATOM   3086 C CG    . GLU B 1 134 ? 2.251   110.483 -24.413 1.00 33.24 ? 134 GLU B CG    1 
ATOM   3087 N N     . HIS B 1 135 ? 0.799   112.896 -20.555 1.00 33.12 ? 135 HIS B N     1 
ATOM   3088 C CA    . HIS B 1 135 ? -0.182  113.507 -19.672 1.00 32.53 ? 135 HIS B CA    1 
ATOM   3089 C C     . HIS B 1 135 ? 0.509   114.100 -18.448 1.00 32.48 ? 135 HIS B C     1 
ATOM   3090 O O     . HIS B 1 135 ? 0.260   113.706 -17.310 1.00 32.19 ? 135 HIS B O     1 
ATOM   3091 C CB    . HIS B 1 135 ? -1.220  112.490 -19.191 1.00 33.78 ? 135 HIS B CB    1 
ATOM   3092 C CG    . HIS B 1 135 ? -1.875  111.766 -20.325 1.00 36.06 ? 135 HIS B CG    1 
ATOM   3093 N ND1   . HIS B 1 135 ? -2.900  112.297 -21.078 1.00 37.16 ? 135 HIS B ND1   1 
ATOM   3094 C CD2   . HIS B 1 135 ? -1.583  110.559 -20.869 1.00 37.14 ? 135 HIS B CD2   1 
ATOM   3095 C CE1   . HIS B 1 135 ? -3.234  111.442 -22.030 1.00 37.21 ? 135 HIS B CE1   1 
ATOM   3096 N NE2   . HIS B 1 135 ? -2.455  110.379 -21.917 1.00 38.10 ? 135 HIS B NE2   1 
ATOM   3097 N N     . PRO B 1 136 ? 1.306   115.149 -18.674 1.00 32.34 ? 136 PRO B N     1 
ATOM   3098 C CA    . PRO B 1 136 ? 2.187   115.756 -17.699 1.00 32.15 ? 136 PRO B CA    1 
ATOM   3099 C C     . PRO B 1 136 ? 1.541   116.614 -16.638 1.00 32.15 ? 136 PRO B C     1 
ATOM   3100 O O     . PRO B 1 136 ? 2.168   117.091 -15.692 1.00 31.59 ? 136 PRO B O     1 
ATOM   3101 C CB    . PRO B 1 136 ? 3.154   116.547 -18.571 1.00 32.19 ? 136 PRO B CB    1 
ATOM   3102 C CG    . PRO B 1 136 ? 2.298   117.016 -19.698 1.00 32.15 ? 136 PRO B CG    1 
ATOM   3103 C CD    . PRO B 1 136 ? 1.360   115.890 -19.961 1.00 32.15 ? 136 PRO B CD    1 
ATOM   3104 N N     . ASP B 1 137 ? 0.224   116.743 -16.726 1.00 32.62 ? 137 ASP B N     1 
ATOM   3105 C CA    . ASP B 1 137 ? -0.615  117.379 -15.727 1.00 32.89 ? 137 ASP B CA    1 
ATOM   3106 C C     . ASP B 1 137 ? -1.379  116.321 -14.921 1.00 32.20 ? 137 ASP B C     1 
ATOM   3107 O O     . ASP B 1 137 ? -1.997  116.638 -13.907 1.00 31.06 ? 137 ASP B O     1 
ATOM   3108 C CB    . ASP B 1 137 ? -1.558  118.377 -16.381 1.00 36.00 ? 137 ASP B CB    1 
ATOM   3109 C CG    . ASP B 1 137 ? -2.537  117.709 -17.325 1.00 39.36 ? 137 ASP B CG    1 
ATOM   3110 O OD1   . ASP B 1 137 ? -2.087  116.927 -18.191 1.00 40.14 ? 137 ASP B OD1   1 
ATOM   3111 O OD2   . ASP B 1 137 ? -3.747  117.993 -17.151 1.00 42.14 ? 137 ASP B OD2   1 
ATOM   3112 N N     . TYR B 1 138 ? -1.177  115.055 -15.276 1.00 32.42 ? 138 TYR B N     1 
ATOM   3113 C CA    . TYR B 1 138 ? -1.820  113.947 -14.579 1.00 32.71 ? 138 TYR B CA    1 
ATOM   3114 C C     . TYR B 1 138 ? -0.983  113.550 -13.374 1.00 31.81 ? 138 TYR B C     1 
ATOM   3115 O O     . TYR B 1 138 ? 0.213   113.788 -13.395 1.00 32.13 ? 138 TYR B O     1 
ATOM   3116 C CB    . TYR B 1 138 ? -2.029  112.732 -15.482 1.00 34.23 ? 138 TYR B CB    1 
ATOM   3117 C CG    . TYR B 1 138 ? -3.251  112.783 -16.367 1.00 36.35 ? 138 TYR B CG    1 
ATOM   3118 C CD1   . TYR B 1 138 ? -3.711  113.993 -16.877 1.00 37.17 ? 138 TYR B CD1   1 
ATOM   3119 C CD2   . TYR B 1 138 ? -3.936  111.630 -16.701 1.00 37.30 ? 138 TYR B CD2   1 
ATOM   3120 C CE1   . TYR B 1 138 ? -4.817  114.047 -17.691 1.00 38.02 ? 138 TYR B CE1   1 
ATOM   3121 C CE2   . TYR B 1 138 ? -5.065  111.685 -17.499 1.00 38.44 ? 138 TYR B CE2   1 
ATOM   3122 C CZ    . TYR B 1 138 ? -5.490  112.889 -18.000 1.00 38.76 ? 138 TYR B CZ    1 
ATOM   3123 O OH    . TYR B 1 138 ? -6.599  112.988 -18.802 1.00 40.02 ? 138 TYR B OH    1 
ATOM   3124 N N     . ARG B 1 139 ? -1.598  113.085 -12.318 1.00 30.72 ? 139 ARG B N     1 
ATOM   3125 C CA    . ARG B 1 139 ? -0.923  112.676 -11.103 1.00 30.18 ? 139 ARG B CA    1 
ATOM   3126 C C     . ARG B 1 139 ? -0.525  111.211 -11.205 1.00 30.75 ? 139 ARG B C     1 
ATOM   3127 O O     . ARG B 1 139 ? -1.237  110.382 -11.777 1.00 31.26 ? 139 ARG B O     1 
ATOM   3128 C CB    . ARG B 1 139 ? -1.870  112.939 -9.949  1.00 26.52 ? 139 ARG B CB    1 
ATOM   3129 C CG    . ARG B 1 139 ? -1.479  112.488 -8.558  1.00 24.64 ? 139 ARG B CG    1 
ATOM   3130 C CD    . ARG B 1 139 ? -2.358  113.238 -7.583  1.00 25.86 ? 139 ARG B CD    1 
ATOM   3131 N NE    . ARG B 1 139 ? -3.198  112.435 -6.699  1.00 28.09 ? 139 ARG B NE    1 
ATOM   3132 C CZ    . ARG B 1 139 ? -2.757  111.978 -5.527  1.00 29.52 ? 139 ARG B CZ    1 
ATOM   3133 N NH1   . ARG B 1 139 ? -3.540  111.277 -4.732  1.00 29.03 ? 139 ARG B NH1   1 
ATOM   3134 N NH2   . ARG B 1 139 ? -1.501  112.225 -5.147  1.00 30.32 ? 139 ARG B NH2   1 
ATOM   3135 N N     . VAL B 1 140 ? 0.605   110.843 -10.620 1.00 30.76 ? 140 VAL B N     1 
ATOM   3136 C CA    . VAL B 1 140 ? 1.119   109.489 -10.643 1.00 30.62 ? 140 VAL B CA    1 
ATOM   3137 C C     . VAL B 1 140 ? 0.988   108.815 -9.282  1.00 30.59 ? 140 VAL B C     1 
ATOM   3138 O O     . VAL B 1 140 ? 1.646   109.142 -8.300  1.00 30.45 ? 140 VAL B O     1 
ATOM   3139 C CB    . VAL B 1 140 ? 2.593   109.429 -11.078 1.00 31.02 ? 140 VAL B CB    1 
ATOM   3140 C CG1   . VAL B 1 140 ? 3.120   108.001 -11.023 1.00 32.57 ? 140 VAL B CG1   1 
ATOM   3141 C CG2   . VAL B 1 140 ? 2.816   109.945 -12.495 1.00 31.17 ? 140 VAL B CG2   1 
ATOM   3142 N N     . VAL B 1 141 ? 0.035   107.894 -9.207  1.00 30.66 ? 141 VAL B N     1 
ATOM   3143 C CA    . VAL B 1 141 ? -0.197  107.099 -8.007  1.00 30.07 ? 141 VAL B CA    1 
ATOM   3144 C C     . VAL B 1 141 ? 0.251   105.655 -8.203  1.00 29.55 ? 141 VAL B C     1 
ATOM   3145 O O     . VAL B 1 141 ? 0.107   105.103 -9.300  1.00 30.07 ? 141 VAL B O     1 
ATOM   3146 C CB    . VAL B 1 141 ? -1.706  107.106 -7.696  1.00 29.26 ? 141 VAL B CB    1 
ATOM   3147 C CG1   . VAL B 1 141 ? -1.958  106.476 -6.339  1.00 30.77 ? 141 VAL B CG1   1 
ATOM   3148 C CG2   . VAL B 1 141 ? -2.227  108.533 -7.761  1.00 28.37 ? 141 VAL B CG2   1 
ATOM   3149 N N     . PHE B 1 142 ? 0.973   105.102 -7.239  1.00 28.21 ? 142 PHE B N     1 
ATOM   3150 C CA    . PHE B 1 142 ? 1.307   103.681 -7.260  1.00 26.74 ? 142 PHE B CA    1 
ATOM   3151 C C     . PHE B 1 142 ? 0.484   103.049 -6.131  1.00 26.30 ? 142 PHE B C     1 
ATOM   3152 O O     . PHE B 1 142 ? 0.280   103.794 -5.164  1.00 25.81 ? 142 PHE B O     1 
ATOM   3153 C CB    . PHE B 1 142 ? 2.768   103.411 -7.010  1.00 24.28 ? 142 PHE B CB    1 
ATOM   3154 C CG    . PHE B 1 142 ? 3.740   103.715 -8.098  1.00 21.51 ? 142 PHE B CG    1 
ATOM   3155 C CD1   . PHE B 1 142 ? 3.329   104.212 -9.317  1.00 21.87 ? 142 PHE B CD1   1 
ATOM   3156 C CD2   . PHE B 1 142 ? 5.091   103.505 -7.896  1.00 19.88 ? 142 PHE B CD2   1 
ATOM   3157 C CE1   . PHE B 1 142 ? 4.219   104.499 -10.334 1.00 21.33 ? 142 PHE B CE1   1 
ATOM   3158 C CE2   . PHE B 1 142 ? 5.992   103.790 -8.905  1.00 22.18 ? 142 PHE B CE2   1 
ATOM   3159 C CZ    . PHE B 1 142 ? 5.560   104.286 -10.127 1.00 21.55 ? 142 PHE B CZ    1 
ATOM   3160 N N     . THR B 1 143 ? -0.044  101.844 -6.343  1.00 25.45 ? 143 THR B N     1 
ATOM   3161 C CA    . THR B 1 143 ? -0.928  101.302 -5.315  1.00 24.51 ? 143 THR B CA    1 
ATOM   3162 C C     . THR B 1 143 ? -1.021  99.790  -5.358  1.00 24.25 ? 143 THR B C     1 
ATOM   3163 O O     . THR B 1 143 ? -0.746  99.153  -6.368  1.00 23.91 ? 143 THR B O     1 
ATOM   3164 C CB    . THR B 1 143 ? -2.319  101.963 -5.411  1.00 22.70 ? 143 THR B CB    1 
ATOM   3165 O OG1   . THR B 1 143 ? -3.110  101.544 -4.293  1.00 23.61 ? 143 THR B OG1   1 
ATOM   3166 C CG2   . THR B 1 143 ? -3.018  101.641 -6.715  1.00 21.61 ? 143 THR B CG2   1 
ATOM   3167 N N     . GLY B 1 144 ? -1.560  99.207  -4.295  1.00 24.33 ? 144 GLY B N     1 
ATOM   3168 C CA    . GLY B 1 144 ? -1.767  97.779  -4.221  1.00 24.69 ? 144 GLY B CA    1 
ATOM   3169 C C     . GLY B 1 144 ? -2.148  97.339  -2.809  1.00 25.30 ? 144 GLY B C     1 
ATOM   3170 O O     . GLY B 1 144 ? -1.758  97.981  -1.832  1.00 25.13 ? 144 GLY B O     1 
ATOM   3171 N N     . HIS B 1 145 ? -2.597  96.084  -2.731  1.00 25.39 ? 145 HIS B N     1 
ATOM   3172 C CA    . HIS B 1 145 ? -2.983  95.508  -1.445  1.00 25.50 ? 145 HIS B CA    1 
ATOM   3173 C C     . HIS B 1 145 ? -2.000  94.385  -1.140  1.00 26.08 ? 145 HIS B C     1 
ATOM   3174 O O     . HIS B 1 145 ? -1.492  93.767  -2.074  1.00 25.63 ? 145 HIS B O     1 
ATOM   3175 C CB    . HIS B 1 145 ? -4.406  94.992  -1.575  1.00 25.03 ? 145 HIS B CB    1 
ATOM   3176 C CG    . HIS B 1 145 ? -4.873  93.974  -0.596  1.00 24.84 ? 145 HIS B CG    1 
ATOM   3177 N ND1   . HIS B 1 145 ? -4.969  92.630  -0.881  1.00 24.99 ? 145 HIS B ND1   1 
ATOM   3178 C CD2   . HIS B 1 145 ? -5.260  94.101  0.697   1.00 25.40 ? 145 HIS B CD2   1 
ATOM   3179 C CE1   . HIS B 1 145 ? -5.365  91.977  0.202   1.00 25.56 ? 145 HIS B CE1   1 
ATOM   3180 N NE2   . HIS B 1 145 ? -5.575  92.849  1.183   1.00 25.30 ? 145 HIS B NE2   1 
ATOM   3181 N N     . SER B 1 146 ? -1.687  94.213  0.143   1.00 26.63 ? 146 SER B N     1 
ATOM   3182 C CA    . SER B 1 146 ? -0.809  93.097  0.546   1.00 27.05 ? 146 SER B CA    1 
ATOM   3183 C C     . SER B 1 146 ? 0.531   93.123  -0.152  1.00 27.07 ? 146 SER B C     1 
ATOM   3184 O O     . SER B 1 146 ? 1.168   94.160  -0.345  1.00 26.71 ? 146 SER B O     1 
ATOM   3185 C CB    . SER B 1 146 ? -1.609  91.834  0.210   1.00 27.81 ? 146 SER B CB    1 
ATOM   3186 O OG    . SER B 1 146 ? -1.293  90.740  1.028   1.00 30.38 ? 146 SER B OG    1 
ATOM   3187 N N     . LEU B 1 147 ? 0.876   92.067  -0.882  1.00 27.67 ? 147 LEU B N     1 
ATOM   3188 C CA    . LEU B 1 147 ? 2.137   91.930  -1.595  1.00 27.54 ? 147 LEU B CA    1 
ATOM   3189 C C     . LEU B 1 147 ? 2.277   93.078  -2.581  1.00 27.86 ? 147 LEU B C     1 
ATOM   3190 O O     . LEU B 1 147 ? 3.329   93.710  -2.683  1.00 28.33 ? 147 LEU B O     1 
ATOM   3191 C CB    . LEU B 1 147 ? 2.274   90.584  -2.294  1.00 25.90 ? 147 LEU B CB    1 
ATOM   3192 C CG    . LEU B 1 147 ? 3.214   90.524  -3.496  1.00 25.40 ? 147 LEU B CG    1 
ATOM   3193 C CD1   . LEU B 1 147 ? 4.643   90.800  -3.059  1.00 26.74 ? 147 LEU B CD1   1 
ATOM   3194 C CD2   . LEU B 1 147 ? 3.129   89.186  -4.198  1.00 23.84 ? 147 LEU B CD2   1 
ATOM   3195 N N     . GLY B 1 148 ? 1.195   93.379  -3.285  1.00 27.89 ? 148 GLY B N     1 
ATOM   3196 C CA    . GLY B 1 148 ? 1.133   94.524  -4.177  1.00 27.81 ? 148 GLY B CA    1 
ATOM   3197 C C     . GLY B 1 148 ? 1.401   95.855  -3.495  1.00 27.62 ? 148 GLY B C     1 
ATOM   3198 O O     . GLY B 1 148 ? 1.772   96.790  -4.205  1.00 27.65 ? 148 GLY B O     1 
ATOM   3199 N N     . GLY B 1 149 ? 1.015   96.074  -2.244  1.00 27.32 ? 149 GLY B N     1 
ATOM   3200 C CA    . GLY B 1 149 ? 1.342   97.291  -1.521  1.00 27.02 ? 149 GLY B CA    1 
ATOM   3201 C C     . GLY B 1 149 ? 2.826   97.380  -1.186  1.00 26.81 ? 149 GLY B C     1 
ATOM   3202 O O     . GLY B 1 149 ? 3.421   98.453  -1.232  1.00 26.56 ? 149 GLY B O     1 
ATOM   3203 N N     . ALA B 1 150 ? 3.463   96.242  -0.902  1.00 26.57 ? 150 ALA B N     1 
ATOM   3204 C CA    . ALA B 1 150 ? 4.901   96.185  -0.658  1.00 25.73 ? 150 ALA B CA    1 
ATOM   3205 C C     . ALA B 1 150 ? 5.615   96.528  -1.965  1.00 25.40 ? 150 ALA B C     1 
ATOM   3206 O O     . ALA B 1 150 ? 6.499   97.374  -1.981  1.00 25.14 ? 150 ALA B O     1 
ATOM   3207 C CB    . ALA B 1 150 ? 5.341   94.807  -0.207  1.00 23.47 ? 150 ALA B CB    1 
ATOM   3208 N N     . LEU B 1 151 ? 5.149   95.910  -3.053  1.00 25.17 ? 151 LEU B N     1 
ATOM   3209 C CA    . LEU B 1 151 ? 5.750   96.193  -4.345  1.00 25.28 ? 151 LEU B CA    1 
ATOM   3210 C C     . LEU B 1 151 ? 5.660   97.682  -4.658  1.00 25.38 ? 151 LEU B C     1 
ATOM   3211 O O     . LEU B 1 151 ? 6.643   98.326  -5.012  1.00 25.21 ? 151 LEU B O     1 
ATOM   3212 C CB    . LEU B 1 151 ? 5.117   95.366  -5.452  1.00 25.02 ? 151 LEU B CB    1 
ATOM   3213 C CG    . LEU B 1 151 ? 5.566   93.914  -5.537  1.00 26.51 ? 151 LEU B CG    1 
ATOM   3214 C CD1   . LEU B 1 151 ? 5.047   93.285  -6.825  1.00 27.76 ? 151 LEU B CD1   1 
ATOM   3215 C CD2   . LEU B 1 151 ? 7.083   93.793  -5.487  1.00 26.49 ? 151 LEU B CD2   1 
ATOM   3216 N N     . ALA B 1 152 ? 4.472   98.243  -4.458  1.00 25.36 ? 152 ALA B N     1 
ATOM   3217 C CA    . ALA B 1 152 ? 4.232   99.647  -4.739  1.00 25.57 ? 152 ALA B CA    1 
ATOM   3218 C C     . ALA B 1 152 ? 5.075   100.547 -3.845  1.00 26.00 ? 152 ALA B C     1 
ATOM   3219 O O     . ALA B 1 152 ? 5.542   101.616 -4.238  1.00 26.03 ? 152 ALA B O     1 
ATOM   3220 C CB    . ALA B 1 152 ? 2.750   99.929  -4.568  1.00 25.25 ? 152 ALA B CB    1 
ATOM   3221 N N     . THR B 1 153 ? 5.211   100.215 -2.565  1.00 26.07 ? 153 THR B N     1 
ATOM   3222 C CA    . THR B 1 153 ? 6.071   100.953 -1.665  1.00 25.95 ? 153 THR B CA    1 
ATOM   3223 C C     . THR B 1 153 ? 7.509   100.987 -2.149  1.00 26.78 ? 153 THR B C     1 
ATOM   3224 O O     . THR B 1 153 ? 8.101   102.065 -2.281  1.00 27.09 ? 153 THR B O     1 
ATOM   3225 C CB    . THR B 1 153 ? 5.978   100.379 -0.247  1.00 23.87 ? 153 THR B CB    1 
ATOM   3226 O OG1   . THR B 1 153 ? 4.601   100.384 0.131   1.00 23.75 ? 153 THR B OG1   1 
ATOM   3227 C CG2   . THR B 1 153 ? 6.727   101.246 0.743   1.00 24.05 ? 153 THR B CG2   1 
ATOM   3228 N N     . VAL B 1 154 ? 8.101   99.865  -2.547  1.00 27.54 ? 154 VAL B N     1 
ATOM   3229 C CA    . VAL B 1 154 ? 9.497   99.889  -2.970  1.00 28.32 ? 154 VAL B CA    1 
ATOM   3230 C C     . VAL B 1 154 ? 9.643   100.493 -4.358  1.00 28.72 ? 154 VAL B C     1 
ATOM   3231 O O     . VAL B 1 154 ? 10.443  101.411 -4.543  1.00 28.76 ? 154 VAL B O     1 
ATOM   3232 C CB    . VAL B 1 154 ? 10.248  98.568  -2.835  1.00 28.71 ? 154 VAL B CB    1 
ATOM   3233 C CG1   . VAL B 1 154 ? 9.655   97.669  -1.756  1.00 29.22 ? 154 VAL B CG1   1 
ATOM   3234 C CG2   . VAL B 1 154 ? 10.315  97.787  -4.132  1.00 29.82 ? 154 VAL B CG2   1 
ATOM   3235 N N     . ALA B 1 155 ? 8.695   100.207 -5.254  1.00 29.13 ? 155 ALA B N     1 
ATOM   3236 C CA    . ALA B 1 155 ? 8.705   100.800 -6.590  1.00 29.12 ? 155 ALA B CA    1 
ATOM   3237 C C     . ALA B 1 155 ? 8.611   102.314 -6.413  1.00 29.49 ? 155 ALA B C     1 
ATOM   3238 O O     . ALA B 1 155 ? 9.299   103.070 -7.089  1.00 29.80 ? 155 ALA B O     1 
ATOM   3239 C CB    . ALA B 1 155 ? 7.597   100.315 -7.501  1.00 26.27 ? 155 ALA B CB    1 
ATOM   3240 N N     . GLY B 1 156 ? 7.742   102.747 -5.511  1.00 29.88 ? 156 GLY B N     1 
ATOM   3241 C CA    . GLY B 1 156 ? 7.606   104.152 -5.173  1.00 30.42 ? 156 GLY B CA    1 
ATOM   3242 C C     . GLY B 1 156 ? 8.930   104.775 -4.756  1.00 30.72 ? 156 GLY B C     1 
ATOM   3243 O O     . GLY B 1 156 ? 9.496   105.592 -5.477  1.00 30.47 ? 156 GLY B O     1 
ATOM   3244 N N     . ALA B 1 157 ? 9.589   104.227 -3.740  1.00 31.19 ? 157 ALA B N     1 
ATOM   3245 C CA    . ALA B 1 157 ? 10.874  104.715 -3.269  1.00 31.12 ? 157 ALA B CA    1 
ATOM   3246 C C     . ALA B 1 157 ? 11.908  104.714 -4.380  1.00 31.09 ? 157 ALA B C     1 
ATOM   3247 O O     . ALA B 1 157 ? 12.782  105.568 -4.415  1.00 31.31 ? 157 ALA B O     1 
ATOM   3248 C CB    . ALA B 1 157 ? 11.389  103.843 -2.131  1.00 30.35 ? 157 ALA B CB    1 
ATOM   3249 N N     . ASP B 1 158 ? 11.957  103.645 -5.156  1.00 31.50 ? 158 ASP B N     1 
ATOM   3250 C CA    . ASP B 1 158 ? 12.945  103.515 -6.209  1.00 31.96 ? 158 ASP B CA    1 
ATOM   3251 C C     . ASP B 1 158 ? 12.854  104.624 -7.247  1.00 32.51 ? 158 ASP B C     1 
ATOM   3252 O O     . ASP B 1 158 ? 13.860  105.135 -7.739  1.00 32.91 ? 158 ASP B O     1 
ATOM   3253 C CB    . ASP B 1 158 ? 12.821  102.153 -6.920  1.00 31.26 ? 158 ASP B CB    1 
ATOM   3254 C CG    . ASP B 1 158 ? 14.112  101.874 -7.656  1.00 30.52 ? 158 ASP B CG    1 
ATOM   3255 O OD1   . ASP B 1 158 ? 14.212  101.194 -8.685  1.00 33.51 ? 158 ASP B OD1   1 
ATOM   3256 O OD2   . ASP B 1 158 ? 15.104  102.412 -7.147  1.00 31.22 ? 158 ASP B OD2   1 
ATOM   3257 N N     . LEU B 1 159 ? 11.652  104.966 -7.679  1.00 32.66 ? 159 LEU B N     1 
ATOM   3258 C CA    . LEU B 1 159 ? 11.431  105.879 -8.780  1.00 32.57 ? 159 LEU B CA    1 
ATOM   3259 C C     . LEU B 1 159 ? 11.196  107.328 -8.411  1.00 32.97 ? 159 LEU B C     1 
ATOM   3260 O O     . LEU B 1 159 ? 11.340  108.209 -9.282  1.00 33.09 ? 159 LEU B O     1 
ATOM   3261 C CB    . LEU B 1 159 ? 10.320  105.266 -9.637  1.00 30.82 ? 159 LEU B CB    1 
ATOM   3262 C CG    . LEU B 1 159 ? 10.708  104.513 -10.901 1.00 30.21 ? 159 LEU B CG    1 
ATOM   3263 C CD1   . LEU B 1 159 ? 11.974  103.709 -10.766 1.00 28.75 ? 159 LEU B CD1   1 
ATOM   3264 C CD2   . LEU B 1 159 ? 9.584   103.590 -11.377 1.00 31.36 ? 159 LEU B CD2   1 
ATOM   3265 N N     . ARG B 1 160 ? 10.949  107.660 -7.149  1.00 33.11 ? 160 ARG B N     1 
ATOM   3266 C CA    . ARG B 1 160 ? 10.713  109.055 -6.775  1.00 33.52 ? 160 ARG B CA    1 
ATOM   3267 C C     . ARG B 1 160 ? 11.951  109.865 -7.099  1.00 34.61 ? 160 ARG B C     1 
ATOM   3268 O O     . ARG B 1 160 ? 13.052  109.311 -7.186  1.00 34.98 ? 160 ARG B O     1 
ATOM   3269 C CB    . ARG B 1 160 ? 10.301  109.178 -5.306  1.00 31.37 ? 160 ARG B CB    1 
ATOM   3270 C CG    . ARG B 1 160 ? 9.001   108.437 -5.070  1.00 31.86 ? 160 ARG B CG    1 
ATOM   3271 C CD    . ARG B 1 160 ? 7.971   109.070 -4.185  1.00 29.34 ? 160 ARG B CD    1 
ATOM   3272 N NE    . ARG B 1 160 ? 8.135   108.643 -2.817  1.00 28.76 ? 160 ARG B NE    1 
ATOM   3273 C CZ    . ARG B 1 160 ? 7.150   108.390 -1.969  1.00 29.93 ? 160 ARG B CZ    1 
ATOM   3274 N NH1   . ARG B 1 160 ? 7.542   108.019 -0.748  1.00 31.39 ? 160 ARG B NH1   1 
ATOM   3275 N NH2   . ARG B 1 160 ? 5.879   108.497 -2.305  1.00 28.17 ? 160 ARG B NH2   1 
ATOM   3276 N N     . GLY B 1 161 ? 11.826  111.124 -7.499  1.00 35.49 ? 161 GLY B N     1 
ATOM   3277 C CA    . GLY B 1 161 ? 12.944  111.963 -7.848  1.00 35.92 ? 161 GLY B CA    1 
ATOM   3278 C C     . GLY B 1 161 ? 13.396  112.048 -9.282  1.00 36.67 ? 161 GLY B C     1 
ATOM   3279 O O     . GLY B 1 161 ? 14.601  112.256 -9.489  1.00 36.53 ? 161 GLY B O     1 
ATOM   3280 N N     . ASN B 1 162 ? 12.597  111.792 -10.312 1.00 37.55 ? 162 ASN B N     1 
ATOM   3281 C CA    . ASN B 1 162 ? 12.977  111.975 -11.706 1.00 38.01 ? 162 ASN B CA    1 
ATOM   3282 C C     . ASN B 1 162 ? 12.099  113.088 -12.297 1.00 37.48 ? 162 ASN B C     1 
ATOM   3283 O O     . ASN B 1 162 ? 11.784  113.114 -13.483 1.00 37.61 ? 162 ASN B O     1 
ATOM   3284 C CB    . ASN B 1 162 ? 12.876  110.745 -12.585 1.00 43.70 ? 162 ASN B CB    1 
ATOM   3285 C CG    . ASN B 1 162 ? 13.641  109.532 -12.114 1.00 48.19 ? 162 ASN B CG    1 
ATOM   3286 O OD1   . ASN B 1 162 ? 14.359  109.554 -11.111 1.00 50.08 ? 162 ASN B OD1   1 
ATOM   3287 N ND2   . ASN B 1 162 ? 13.523  108.391 -12.802 1.00 50.12 ? 162 ASN B ND2   1 
ATOM   3288 N N     . GLY B 1 163 ? 11.701  114.007 -11.422 1.00 36.66 ? 163 GLY B N     1 
ATOM   3289 C CA    . GLY B 1 163 ? 10.890  115.128 -11.848 1.00 36.10 ? 163 GLY B CA    1 
ATOM   3290 C C     . GLY B 1 163 ? 9.415   114.840 -12.012 1.00 35.31 ? 163 GLY B C     1 
ATOM   3291 O O     . GLY B 1 163 ? 8.819   115.396 -12.924 1.00 35.49 ? 163 GLY B O     1 
ATOM   3292 N N     . TYR B 1 164 ? 8.841   113.941 -11.245 1.00 34.72 ? 164 TYR B N     1 
ATOM   3293 C CA    . TYR B 1 164 ? 7.406   113.736 -11.186 1.00 34.24 ? 164 TYR B CA    1 
ATOM   3294 C C     . TYR B 1 164 ? 7.136   113.189 -9.789  1.00 34.13 ? 164 TYR B C     1 
ATOM   3295 O O     . TYR B 1 164 ? 7.972   112.429 -9.309  1.00 34.44 ? 164 TYR B O     1 
ATOM   3296 C CB    . TYR B 1 164 ? 6.875   112.847 -12.275 1.00 34.41 ? 164 TYR B CB    1 
ATOM   3297 C CG    . TYR B 1 164 ? 7.462   111.487 -12.507 1.00 35.19 ? 164 TYR B CG    1 
ATOM   3298 C CD1   . TYR B 1 164 ? 8.382   111.265 -13.513 1.00 35.61 ? 164 TYR B CD1   1 
ATOM   3299 C CD2   . TYR B 1 164 ? 7.087   110.386 -11.742 1.00 35.77 ? 164 TYR B CD2   1 
ATOM   3300 C CE1   . TYR B 1 164 ? 8.927   110.013 -13.732 1.00 36.29 ? 164 TYR B CE1   1 
ATOM   3301 C CE2   . TYR B 1 164 ? 7.607   109.127 -11.953 1.00 35.91 ? 164 TYR B CE2   1 
ATOM   3302 C CZ    . TYR B 1 164 ? 8.528   108.944 -12.959 1.00 36.69 ? 164 TYR B CZ    1 
ATOM   3303 O OH    . TYR B 1 164 ? 9.069   107.693 -13.190 1.00 37.49 ? 164 TYR B OH    1 
ATOM   3304 N N     . ASP B 1 165 ? 6.101   113.635 -9.113  1.00 33.90 ? 165 ASP B N     1 
ATOM   3305 C CA    . ASP B 1 165 ? 5.814   113.108 -7.782  1.00 33.40 ? 165 ASP B CA    1 
ATOM   3306 C C     . ASP B 1 165 ? 5.133   111.750 -7.895  1.00 33.15 ? 165 ASP B C     1 
ATOM   3307 O O     . ASP B 1 165 ? 4.742   111.377 -9.007  1.00 33.63 ? 165 ASP B O     1 
ATOM   3308 C CB    . ASP B 1 165 ? 4.889   114.079 -7.056  1.00 33.85 ? 165 ASP B CB    1 
ATOM   3309 C CG    . ASP B 1 165 ? 5.635   115.317 -6.616  1.00 34.48 ? 165 ASP B CG    1 
ATOM   3310 O OD1   . ASP B 1 165 ? 5.063   116.068 -5.802  1.00 34.60 ? 165 ASP B OD1   1 
ATOM   3311 O OD2   . ASP B 1 165 ? 6.791   115.521 -7.047  1.00 37.03 ? 165 ASP B OD2   1 
ATOM   3312 N N     . ILE B 1 166 ? 5.425   110.876 -6.933  1.00 32.36 ? 166 ILE B N     1 
ATOM   3313 C CA    . ILE B 1 166 ? 4.784   109.573 -6.879  1.00 31.19 ? 166 ILE B CA    1 
ATOM   3314 C C     . ILE B 1 166 ? 4.123   109.391 -5.514  1.00 31.15 ? 166 ILE B C     1 
ATOM   3315 O O     . ILE B 1 166 ? 4.799   109.453 -4.488  1.00 30.71 ? 166 ILE B O     1 
ATOM   3316 C CB    . ILE B 1 166 ? 5.747   108.413 -7.146  1.00 28.31 ? 166 ILE B CB    1 
ATOM   3317 C CG1   . ILE B 1 166 ? 6.411   108.548 -8.510  1.00 28.53 ? 166 ILE B CG1   1 
ATOM   3318 C CG2   . ILE B 1 166 ? 4.999   107.089 -7.097  1.00 27.06 ? 166 ILE B CG2   1 
ATOM   3319 C CD1   . ILE B 1 166 ? 7.531   107.566 -8.752  1.00 30.13 ? 166 ILE B CD1   1 
ATOM   3320 N N     . ASP B 1 167 ? 2.798   109.283 -5.524  1.00 31.22 ? 167 ASP B N     1 
ATOM   3321 C CA    . ASP B 1 167 ? 2.046   109.018 -4.299  1.00 30.79 ? 167 ASP B CA    1 
ATOM   3322 C C     . ASP B 1 167 ? 1.765   107.514 -4.253  1.00 29.67 ? 167 ASP B C     1 
ATOM   3323 O O     . ASP B 1 167 ? 1.765   106.883 -5.301  1.00 29.51 ? 167 ASP B O     1 
ATOM   3324 C CB    . ASP B 1 167 ? 0.709   109.741 -4.255  1.00 34.64 ? 167 ASP B CB    1 
ATOM   3325 C CG    . ASP B 1 167 ? 0.823   111.160 -3.764  1.00 36.92 ? 167 ASP B CG    1 
ATOM   3326 O OD1   . ASP B 1 167 ? 1.862   111.807 -3.989  1.00 38.33 ? 167 ASP B OD1   1 
ATOM   3327 O OD2   . ASP B 1 167 ? -0.169  111.628 -3.163  1.00 40.43 ? 167 ASP B OD2   1 
ATOM   3328 N N     . VAL B 1 168 ? 1.824   106.964 -3.054  1.00 28.84 ? 168 VAL B N     1 
ATOM   3329 C CA    . VAL B 1 168 ? 1.700   105.534 -2.843  1.00 28.07 ? 168 VAL B CA    1 
ATOM   3330 C C     . VAL B 1 168 ? 0.610   105.248 -1.820  1.00 27.90 ? 168 VAL B C     1 
ATOM   3331 O O     . VAL B 1 168 ? 0.708   105.758 -0.704  1.00 27.79 ? 168 VAL B O     1 
ATOM   3332 C CB    . VAL B 1 168 ? 3.034   104.931 -2.368  1.00 26.50 ? 168 VAL B CB    1 
ATOM   3333 C CG1   . VAL B 1 168 ? 2.899   103.478 -1.940  1.00 25.24 ? 168 VAL B CG1   1 
ATOM   3334 C CG2   . VAL B 1 168 ? 4.110   105.028 -3.450  1.00 25.13 ? 168 VAL B CG2   1 
ATOM   3335 N N     . PHE B 1 169 ? -0.473  104.609 -2.265  1.00 27.66 ? 169 PHE B N     1 
ATOM   3336 C CA    . PHE B 1 169 ? -1.482  104.182 -1.300  1.00 27.56 ? 169 PHE B CA    1 
ATOM   3337 C C     . PHE B 1 169 ? -1.381  102.657 -1.166  1.00 27.41 ? 169 PHE B C     1 
ATOM   3338 O O     . PHE B 1 169 ? -1.552  101.955 -2.165  1.00 26.71 ? 169 PHE B O     1 
ATOM   3339 C CB    . PHE B 1 169 ? -2.896  104.573 -1.666  1.00 28.23 ? 169 PHE B CB    1 
ATOM   3340 C CG    . PHE B 1 169 ? -3.153  106.041 -1.836  1.00 29.17 ? 169 PHE B CG    1 
ATOM   3341 C CD1   . PHE B 1 169 ? -2.682  106.692 -2.964  1.00 29.27 ? 169 PHE B CD1   1 
ATOM   3342 C CD2   . PHE B 1 169 ? -3.886  106.759 -0.899  1.00 29.10 ? 169 PHE B CD2   1 
ATOM   3343 C CE1   . PHE B 1 169 ? -2.909  108.037 -3.154  1.00 30.30 ? 169 PHE B CE1   1 
ATOM   3344 C CE2   . PHE B 1 169 ? -4.142  108.096 -1.092  1.00 29.85 ? 169 PHE B CE2   1 
ATOM   3345 C CZ    . PHE B 1 169 ? -3.642  108.736 -2.211  1.00 31.16 ? 169 PHE B CZ    1 
ATOM   3346 N N     . SER B 1 170 ? -0.935  102.226 0.025   1.00 27.32 ? 170 SER B N     1 
ATOM   3347 C CA    . SER B 1 170 ? -0.907  100.783 0.222   1.00 27.49 ? 170 SER B CA    1 
ATOM   3348 C C     . SER B 1 170 ? -1.892  100.216 1.232   1.00 28.01 ? 170 SER B C     1 
ATOM   3349 O O     . SER B 1 170 ? -2.213  100.859 2.240   1.00 28.67 ? 170 SER B O     1 
ATOM   3350 C CB    . SER B 1 170 ? 0.504   100.388 0.612   1.00 25.13 ? 170 SER B CB    1 
ATOM   3351 O OG    . SER B 1 170 ? 0.479   100.224 2.008   1.00 24.51 ? 170 SER B OG    1 
ATOM   3352 N N     . TYR B 1 171 ? -2.454  99.030  0.931   1.00 27.72 ? 171 TYR B N     1 
ATOM   3353 C CA    . TYR B 1 171 ? -3.500  98.447  1.761   1.00 27.62 ? 171 TYR B CA    1 
ATOM   3354 C C     . TYR B 1 171 ? -3.068  97.121  2.363   1.00 27.54 ? 171 TYR B C     1 
ATOM   3355 O O     . TYR B 1 171 ? -2.566  96.240  1.650   1.00 27.81 ? 171 TYR B O     1 
ATOM   3356 C CB    . TYR B 1 171 ? -4.863  98.243  1.063   1.00 27.17 ? 171 TYR B CB    1 
ATOM   3357 C CG    . TYR B 1 171 ? -5.369  99.571  0.529   1.00 26.34 ? 171 TYR B CG    1 
ATOM   3358 C CD1   . TYR B 1 171 ? -4.917  100.002 -0.705  1.00 26.10 ? 171 TYR B CD1   1 
ATOM   3359 C CD2   . TYR B 1 171 ? -6.221  100.384 1.240   1.00 26.26 ? 171 TYR B CD2   1 
ATOM   3360 C CE1   . TYR B 1 171 ? -5.307  101.209 -1.233  1.00 26.17 ? 171 TYR B CE1   1 
ATOM   3361 C CE2   . TYR B 1 171 ? -6.636  101.602 0.725   1.00 26.46 ? 171 TYR B CE2   1 
ATOM   3362 C CZ    . TYR B 1 171 ? -6.172  102.009 -0.519  1.00 26.06 ? 171 TYR B CZ    1 
ATOM   3363 O OH    . TYR B 1 171 ? -6.575  103.219 -1.015  1.00 24.61 ? 171 TYR B OH    1 
ATOM   3364 N N     . GLY B 1 172 ? -3.083  97.070  3.692   1.00 27.05 ? 172 GLY B N     1 
ATOM   3365 C CA    . GLY B 1 172 ? -2.726  95.854  4.412   1.00 26.82 ? 172 GLY B CA    1 
ATOM   3366 C C     . GLY B 1 172 ? -1.447  95.213  3.903   1.00 26.38 ? 172 GLY B C     1 
ATOM   3367 O O     . GLY B 1 172 ? -1.314  94.022  3.675   1.00 26.13 ? 172 GLY B O     1 
ATOM   3368 N N     . ALA B 1 173 ? -0.412  96.029  3.814   1.00 26.50 ? 173 ALA B N     1 
ATOM   3369 C CA    . ALA B 1 173 ? 0.905   95.671  3.338   1.00 25.87 ? 173 ALA B CA    1 
ATOM   3370 C C     . ALA B 1 173 ? 1.778   95.287  4.521   1.00 25.95 ? 173 ALA B C     1 
ATOM   3371 O O     . ALA B 1 173 ? 1.639   95.791  5.637   1.00 26.20 ? 173 ALA B O     1 
ATOM   3372 C CB    . ALA B 1 173 ? 1.484   96.838  2.557   1.00 23.29 ? 173 ALA B CB    1 
ATOM   3373 N N     . PRO B 1 174 ? 2.660   94.331  4.284   1.00 26.00 ? 174 PRO B N     1 
ATOM   3374 C CA    . PRO B 1 174 ? 3.608   93.878  5.289   1.00 26.27 ? 174 PRO B CA    1 
ATOM   3375 C C     . PRO B 1 174 ? 4.738   94.894  5.462   1.00 26.75 ? 174 PRO B C     1 
ATOM   3376 O O     . PRO B 1 174 ? 4.788   95.914  4.752   1.00 26.77 ? 174 PRO B O     1 
ATOM   3377 C CB    . PRO B 1 174 ? 4.135   92.586  4.691   1.00 25.81 ? 174 PRO B CB    1 
ATOM   3378 C CG    . PRO B 1 174 ? 4.088   92.798  3.220   1.00 25.66 ? 174 PRO B CG    1 
ATOM   3379 C CD    . PRO B 1 174 ? 2.911   93.692  2.969   1.00 25.94 ? 174 PRO B CD    1 
ATOM   3380 N N     . ARG B 1 175 ? 5.562   94.730  6.503   1.00 26.71 ? 175 ARG B N     1 
ATOM   3381 C CA    . ARG B 1 175 ? 6.736   95.604  6.623   1.00 26.62 ? 175 ARG B CA    1 
ATOM   3382 C C     . ARG B 1 175 ? 7.593   95.269  5.409   1.00 27.40 ? 175 ARG B C     1 
ATOM   3383 O O     . ARG B 1 175 ? 7.527   94.149  4.897   1.00 27.95 ? 175 ARG B O     1 
ATOM   3384 C CB    . ARG B 1 175 ? 7.506   95.348  7.899   1.00 24.98 ? 175 ARG B CB    1 
ATOM   3385 C CG    . ARG B 1 175 ? 6.632   95.260  9.133   1.00 25.31 ? 175 ARG B CG    1 
ATOM   3386 C CD    . ARG B 1 175 ? 7.455   95.247  10.398  1.00 24.40 ? 175 ARG B CD    1 
ATOM   3387 N NE    . ARG B 1 175 ? 6.663   95.568  11.572  1.00 25.84 ? 175 ARG B NE    1 
ATOM   3388 C CZ    . ARG B 1 175 ? 5.983   94.738  12.341  1.00 24.19 ? 175 ARG B CZ    1 
ATOM   3389 N NH1   . ARG B 1 175 ? 5.325   95.184  13.401  1.00 26.19 ? 175 ARG B NH1   1 
ATOM   3390 N NH2   . ARG B 1 175 ? 5.992   93.456  12.050  1.00 23.16 ? 175 ARG B NH2   1 
ATOM   3391 N N     . VAL B 1 176 ? 8.467   96.159  4.996   1.00 27.88 ? 176 VAL B N     1 
ATOM   3392 C CA    . VAL B 1 176 ? 9.145   95.961  3.702   1.00 28.30 ? 176 VAL B CA    1 
ATOM   3393 C C     . VAL B 1 176 ? 10.639  96.110  3.883   1.00 29.02 ? 176 VAL B C     1 
ATOM   3394 O O     . VAL B 1 176 ? 11.413  95.755  2.992   1.00 28.49 ? 176 VAL B O     1 
ATOM   3395 C CB    . VAL B 1 176 ? 8.490   96.961  2.741   1.00 27.82 ? 176 VAL B CB    1 
ATOM   3396 C CG1   . VAL B 1 176 ? 8.910   98.390  3.072   1.00 27.82 ? 176 VAL B CG1   1 
ATOM   3397 C CG2   . VAL B 1 176 ? 8.691   96.737  1.262   1.00 27.66 ? 176 VAL B CG2   1 
ATOM   3398 N N     . GLY B 1 177 ? 11.095  96.500  5.084   1.00 29.94 ? 177 GLY B N     1 
ATOM   3399 C CA    . GLY B 1 177 ? 12.535  96.641  5.294   1.00 31.06 ? 177 GLY B CA    1 
ATOM   3400 C C     . GLY B 1 177 ? 12.942  96.917  6.725   1.00 31.78 ? 177 GLY B C     1 
ATOM   3401 O O     . GLY B 1 177 ? 12.125  96.800  7.643   1.00 32.40 ? 177 GLY B O     1 
ATOM   3402 N N     . ASN B 1 178 ? 14.223  97.189  6.930   1.00 32.08 ? 178 ASN B N     1 
ATOM   3403 C CA    . ASN B 1 178 ? 14.774  97.491  8.241   1.00 32.94 ? 178 ASN B CA    1 
ATOM   3404 C C     . ASN B 1 178 ? 14.377  98.886  8.710   1.00 33.78 ? 178 ASN B C     1 
ATOM   3405 O O     . ASN B 1 178 ? 13.795  99.650  7.940   1.00 34.05 ? 178 ASN B O     1 
ATOM   3406 C CB    . ASN B 1 178 ? 16.297  97.428  8.198   1.00 33.74 ? 178 ASN B CB    1 
ATOM   3407 C CG    . ASN B 1 178 ? 16.913  98.302  7.135   1.00 34.80 ? 178 ASN B CG    1 
ATOM   3408 O OD1   . ASN B 1 178 ? 18.132  98.402  6.983   1.00 35.64 ? 178 ASN B OD1   1 
ATOM   3409 N ND2   . ASN B 1 178 ? 16.147  98.985  6.301   1.00 36.03 ? 178 ASN B ND2   1 
ATOM   3410 N N     . ARG B 1 179 ? 14.933  99.326  9.841   1.00 34.37 ? 179 ARG B N     1 
ATOM   3411 C CA    . ARG B 1 179 ? 14.591  100.619 10.414  1.00 34.85 ? 179 ARG B CA    1 
ATOM   3412 C C     . ARG B 1 179 ? 15.136  101.768 9.580   1.00 34.68 ? 179 ARG B C     1 
ATOM   3413 O O     . ARG B 1 179 ? 14.530  102.842 9.498   1.00 34.62 ? 179 ARG B O     1 
ATOM   3414 C CB    . ARG B 1 179 ? 15.014  100.722 11.878  1.00 37.04 ? 179 ARG B CB    1 
ATOM   3415 C CG    . ARG B 1 179 ? 14.979  102.125 12.455  1.00 38.81 ? 179 ARG B CG    1 
ATOM   3416 C CD    . ARG B 1 179 ? 14.310  102.202 13.819  1.00 40.93 ? 179 ARG B CD    1 
ATOM   3417 N NE    . ARG B 1 179 ? 14.109  103.603 14.155  1.00 44.89 ? 179 ARG B NE    1 
ATOM   3418 C CZ    . ARG B 1 179 ? 13.298  104.165 15.034  1.00 47.15 ? 179 ARG B CZ    1 
ATOM   3419 N NH1   . ARG B 1 179 ? 12.489  103.431 15.797  1.00 48.01 ? 179 ARG B NH1   1 
ATOM   3420 N NH2   . ARG B 1 179 ? 13.257  105.497 15.138  1.00 47.72 ? 179 ARG B NH2   1 
ATOM   3421 N N     . ALA B 1 180 ? 16.267  101.547 8.919   1.00 34.57 ? 180 ALA B N     1 
ATOM   3422 C CA    . ALA B 1 180 ? 16.816  102.556 8.023   1.00 34.50 ? 180 ALA B CA    1 
ATOM   3423 C C     . ALA B 1 180 ? 15.840  102.777 6.869   1.00 34.56 ? 180 ALA B C     1 
ATOM   3424 O O     . ALA B 1 180 ? 15.727  103.906 6.391   1.00 35.15 ? 180 ALA B O     1 
ATOM   3425 C CB    . ALA B 1 180 ? 18.168  102.205 7.438   1.00 34.48 ? 180 ALA B CB    1 
ATOM   3426 N N     . PHE B 1 181 ? 15.266  101.719 6.312   1.00 34.23 ? 181 PHE B N     1 
ATOM   3427 C CA    . PHE B 1 181 ? 14.316  101.864 5.210   1.00 33.88 ? 181 PHE B CA    1 
ATOM   3428 C C     . PHE B 1 181 ? 13.025  102.451 5.763   1.00 34.04 ? 181 PHE B C     1 
ATOM   3429 O O     . PHE B 1 181 ? 12.438  103.337 5.145   1.00 33.85 ? 181 PHE B O     1 
ATOM   3430 C CB    . PHE B 1 181 ? 14.156  100.553 4.456   1.00 32.63 ? 181 PHE B CB    1 
ATOM   3431 C CG    . PHE B 1 181 ? 13.638  100.616 3.053   1.00 31.89 ? 181 PHE B CG    1 
ATOM   3432 C CD1   . PHE B 1 181 ? 13.998  101.666 2.237   1.00 32.06 ? 181 PHE B CD1   1 
ATOM   3433 C CD2   . PHE B 1 181 ? 12.788  99.661  2.515   1.00 31.50 ? 181 PHE B CD2   1 
ATOM   3434 C CE1   . PHE B 1 181 ? 13.543  101.739 0.929   1.00 31.10 ? 181 PHE B CE1   1 
ATOM   3435 C CE2   . PHE B 1 181 ? 12.289  99.779  1.232   1.00 30.23 ? 181 PHE B CE2   1 
ATOM   3436 C CZ    . PHE B 1 181 ? 12.661  100.823 0.423   1.00 29.05 ? 181 PHE B CZ    1 
ATOM   3437 N N     . ALA B 1 182 ? 12.621  102.055 6.964   1.00 34.23 ? 182 ALA B N     1 
ATOM   3438 C CA    . ALA B 1 182 ? 11.443  102.612 7.615   1.00 34.72 ? 182 ALA B CA    1 
ATOM   3439 C C     . ALA B 1 182 ? 11.621  104.123 7.734   1.00 35.29 ? 182 ALA B C     1 
ATOM   3440 O O     . ALA B 1 182 ? 10.785  104.901 7.280   1.00 35.34 ? 182 ALA B O     1 
ATOM   3441 C CB    . ALA B 1 182 ? 11.224  102.010 8.996   1.00 33.89 ? 182 ALA B CB    1 
ATOM   3442 N N     . GLU B 1 183 ? 12.755  104.535 8.310   1.00 36.09 ? 183 GLU B N     1 
ATOM   3443 C CA    . GLU B 1 183 ? 13.065  105.954 8.465   1.00 36.49 ? 183 GLU B CA    1 
ATOM   3444 C C     . GLU B 1 183 ? 12.993  106.682 7.123   1.00 35.92 ? 183 GLU B C     1 
ATOM   3445 O O     . GLU B 1 183 ? 12.219  107.634 6.959   1.00 36.09 ? 183 GLU B O     1 
ATOM   3446 C CB    . GLU B 1 183 ? 14.429  106.128 9.123   1.00 40.51 ? 183 GLU B CB    1 
ATOM   3447 C CG    . GLU B 1 183 ? 14.344  106.753 10.505  1.00 46.68 ? 183 GLU B CG    1 
ATOM   3448 C CD    . GLU B 1 183 ? 15.130  105.974 11.551  1.00 50.28 ? 183 GLU B CD    1 
ATOM   3449 O OE1   . GLU B 1 183 ? 16.286  105.577 11.254  1.00 50.49 ? 183 GLU B OE1   1 
ATOM   3450 O OE2   . GLU B 1 183 ? 14.604  105.754 12.672  1.00 52.15 ? 183 GLU B OE2   1 
ATOM   3451 N N     . PHE B 1 184 ? 13.735  106.184 6.143   1.00 34.57 ? 184 PHE B N     1 
ATOM   3452 C CA    . PHE B 1 184 ? 13.723  106.718 4.802   1.00 33.85 ? 184 PHE B CA    1 
ATOM   3453 C C     . PHE B 1 184 ? 12.376  106.870 4.116   1.00 33.73 ? 184 PHE B C     1 
ATOM   3454 O O     . PHE B 1 184 ? 12.088  107.848 3.413   1.00 33.40 ? 184 PHE B O     1 
ATOM   3455 C CB    . PHE B 1 184 ? 14.590  105.775 3.958   1.00 33.84 ? 184 PHE B CB    1 
ATOM   3456 C CG    . PHE B 1 184 ? 14.710  106.312 2.561   1.00 34.02 ? 184 PHE B CG    1 
ATOM   3457 C CD1   . PHE B 1 184 ? 14.020  105.718 1.519   1.00 34.67 ? 184 PHE B CD1   1 
ATOM   3458 C CD2   . PHE B 1 184 ? 15.494  107.428 2.339   1.00 33.77 ? 184 PHE B CD2   1 
ATOM   3459 C CE1   . PHE B 1 184 ? 14.170  106.199 0.222   1.00 35.23 ? 184 PHE B CE1   1 
ATOM   3460 C CE2   . PHE B 1 184 ? 15.595  107.928 1.048   1.00 35.08 ? 184 PHE B CE2   1 
ATOM   3461 C CZ    . PHE B 1 184 ? 14.969  107.311 -0.018  1.00 35.08 ? 184 PHE B CZ    1 
ATOM   3462 N N     . LEU B 1 185 ? 11.493  105.882 4.214   1.00 33.57 ? 185 LEU B N     1 
ATOM   3463 C CA    . LEU B 1 185 ? 10.162  105.950 3.642   1.00 33.37 ? 185 LEU B CA    1 
ATOM   3464 C C     . LEU B 1 185 ? 9.319   106.978 4.379   1.00 33.69 ? 185 LEU B C     1 
ATOM   3465 O O     . LEU B 1 185 ? 8.350   107.469 3.805   1.00 34.33 ? 185 LEU B O     1 
ATOM   3466 C CB    . LEU B 1 185 ? 9.447   104.593 3.723   1.00 31.45 ? 185 LEU B CB    1 
ATOM   3467 C CG    . LEU B 1 185 ? 9.950   103.585 2.685   1.00 30.22 ? 185 LEU B CG    1 
ATOM   3468 C CD1   . LEU B 1 185 ? 9.471   102.198 3.049   1.00 29.15 ? 185 LEU B CD1   1 
ATOM   3469 C CD2   . LEU B 1 185 ? 9.512   104.064 1.311   1.00 29.59 ? 185 LEU B CD2   1 
ATOM   3470 N N     . THR B 1 186 ? 9.632   107.225 5.639   1.00 33.62 ? 186 THR B N     1 
ATOM   3471 C CA    . THR B 1 186 ? 8.903   108.172 6.463   1.00 34.16 ? 186 THR B CA    1 
ATOM   3472 C C     . THR B 1 186 ? 9.167   109.617 6.061   1.00 34.20 ? 186 THR B C     1 
ATOM   3473 O O     . THR B 1 186 ? 8.419   110.553 6.324   1.00 34.20 ? 186 THR B O     1 
ATOM   3474 C CB    . THR B 1 186 ? 9.330   108.005 7.938   1.00 34.63 ? 186 THR B CB    1 
ATOM   3475 O OG1   . THR B 1 186 ? 8.885   106.741 8.456   1.00 37.21 ? 186 THR B OG1   1 
ATOM   3476 C CG2   . THR B 1 186 ? 8.760   109.071 8.849   1.00 32.84 ? 186 THR B CG2   1 
ATOM   3477 N N     . VAL B 1 187 ? 10.311  109.871 5.458   1.00 34.58 ? 187 VAL B N     1 
ATOM   3478 C CA    . VAL B 1 187 ? 10.829  111.217 5.232   1.00 34.74 ? 187 VAL B CA    1 
ATOM   3479 C C     . VAL B 1 187 ? 11.077  111.528 3.769   1.00 34.95 ? 187 VAL B C     1 
ATOM   3480 O O     . VAL B 1 187 ? 11.203  112.700 3.393   1.00 34.55 ? 187 VAL B O     1 
ATOM   3481 C CB    . VAL B 1 187 ? 12.141  111.296 6.057   1.00 33.13 ? 187 VAL B CB    1 
ATOM   3482 C CG1   . VAL B 1 187 ? 13.082  112.388 5.628   1.00 34.41 ? 187 VAL B CG1   1 
ATOM   3483 C CG2   . VAL B 1 187 ? 11.802  111.505 7.525   1.00 32.96 ? 187 VAL B CG2   1 
ATOM   3484 N N     . GLN B 1 188 ? 11.174  110.492 2.933   1.00 35.18 ? 188 GLN B N     1 
ATOM   3485 C CA    . GLN B 1 188 ? 11.497  110.722 1.525   1.00 35.30 ? 188 GLN B CA    1 
ATOM   3486 C C     . GLN B 1 188 ? 10.599  111.840 1.017   1.00 35.86 ? 188 GLN B C     1 
ATOM   3487 O O     . GLN B 1 188 ? 9.500   112.045 1.545   1.00 36.25 ? 188 GLN B O     1 
ATOM   3488 C CB    . GLN B 1 188 ? 11.407  109.452 0.703   1.00 33.15 ? 188 GLN B CB    1 
ATOM   3489 C CG    . GLN B 1 188 ? 11.949  109.541 -0.708  1.00 31.81 ? 188 GLN B CG    1 
ATOM   3490 C CD    . GLN B 1 188 ? 11.597  108.319 -1.533  1.00 31.20 ? 188 GLN B CD    1 
ATOM   3491 O OE1   . GLN B 1 188 ? 10.568  107.698 -1.246  1.00 32.86 ? 188 GLN B OE1   1 
ATOM   3492 N NE2   . GLN B 1 188 ? 12.400  107.976 -2.527  1.00 28.20 ? 188 GLN B NE2   1 
ATOM   3493 N N     . THR B 1 189 ? 11.056  112.476 -0.050  1.00 36.33 ? 189 THR B N     1 
ATOM   3494 C CA    . THR B 1 189 ? 10.297  113.612 -0.619  1.00 36.43 ? 189 THR B CA    1 
ATOM   3495 C C     . THR B 1 189 ? 10.022  113.332 -2.081  1.00 35.69 ? 189 THR B C     1 
ATOM   3496 O O     . THR B 1 189 ? 10.844  112.642 -2.707  1.00 36.11 ? 189 THR B O     1 
ATOM   3497 C CB    . THR B 1 189 ? 11.221  114.831 -0.400  1.00 40.02 ? 189 THR B CB    1 
ATOM   3498 O OG1   . THR B 1 189 ? 10.499  116.055 -0.204  1.00 44.85 ? 189 THR B OG1   1 
ATOM   3499 C CG2   . THR B 1 189 ? 12.248  115.042 -1.495  1.00 38.39 ? 189 THR B CG2   1 
ATOM   3500 N N     . GLY B 1 190 ? 8.929   113.825 -2.643  1.00 34.86 ? 190 GLY B N     1 
ATOM   3501 C CA    . GLY B 1 190 ? 8.658   113.560 -4.065  1.00 33.87 ? 190 GLY B CA    1 
ATOM   3502 C C     . GLY B 1 190 ? 7.332   112.831 -4.229  1.00 33.48 ? 190 GLY B C     1 
ATOM   3503 O O     . GLY B 1 190 ? 7.122   112.130 -5.209  1.00 33.46 ? 190 GLY B O     1 
ATOM   3504 N N     . GLY B 1 191 ? 6.450   112.996 -3.256  1.00 32.96 ? 191 GLY B N     1 
ATOM   3505 C CA    . GLY B 1 191 ? 5.171   112.317 -3.207  1.00 32.49 ? 191 GLY B CA    1 
ATOM   3506 C C     . GLY B 1 191 ? 4.983   111.805 -1.775  1.00 32.29 ? 191 GLY B C     1 
ATOM   3507 O O     . GLY B 1 191 ? 5.995   111.673 -1.101  1.00 31.30 ? 191 GLY B O     1 
ATOM   3508 N N     . THR B 1 192 ? 3.786   111.321 -1.472  1.00 32.54 ? 192 THR B N     1 
ATOM   3509 C CA    . THR B 1 192 ? 3.490   110.826 -0.129  1.00 32.28 ? 192 THR B CA    1 
ATOM   3510 C C     . THR B 1 192 ? 3.277   109.333 -0.095  1.00 32.19 ? 192 THR B C     1 
ATOM   3511 O O     . THR B 1 192 ? 2.733   108.790 -1.052  1.00 32.69 ? 192 THR B O     1 
ATOM   3512 C CB    . THR B 1 192 ? 2.236   111.597 0.362   1.00 31.18 ? 192 THR B CB    1 
ATOM   3513 O OG1   . THR B 1 192 ? 2.780   112.829 0.846   1.00 30.46 ? 192 THR B OG1   1 
ATOM   3514 C CG2   . THR B 1 192 ? 1.452   110.994 1.505   1.00 30.70 ? 192 THR B CG2   1 
ATOM   3515 N N     . LEU B 1 193 ? 3.530   108.709 1.047   1.00 32.11 ? 193 LEU B N     1 
ATOM   3516 C CA    . LEU B 1 193 ? 3.120   107.315 1.253   1.00 31.70 ? 193 LEU B CA    1 
ATOM   3517 C C     . LEU B 1 193 ? 1.940   107.228 2.210   1.00 31.51 ? 193 LEU B C     1 
ATOM   3518 O O     . LEU B 1 193 ? 2.043   107.708 3.341   1.00 31.21 ? 193 LEU B O     1 
ATOM   3519 C CB    . LEU B 1 193 ? 4.291   106.484 1.728   1.00 31.64 ? 193 LEU B CB    1 
ATOM   3520 C CG    . LEU B 1 193 ? 4.229   104.989 1.907   1.00 32.88 ? 193 LEU B CG    1 
ATOM   3521 C CD1   . LEU B 1 193 ? 4.395   104.612 3.379   1.00 33.88 ? 193 LEU B CD1   1 
ATOM   3522 C CD2   . LEU B 1 193 ? 3.001   104.361 1.284   1.00 33.00 ? 193 LEU B CD2   1 
ATOM   3523 N N     . TYR B 1 194 ? 0.802   106.705 1.737   1.00 31.37 ? 194 TYR B N     1 
ATOM   3524 C CA    . TYR B 1 194 ? -0.303  106.375 2.637   1.00 30.95 ? 194 TYR B CA    1 
ATOM   3525 C C     . TYR B 1 194 ? -0.354  104.863 2.894   1.00 30.37 ? 194 TYR B C     1 
ATOM   3526 O O     . TYR B 1 194 ? -0.743  104.099 2.019   1.00 30.15 ? 194 TYR B O     1 
ATOM   3527 C CB    . TYR B 1 194 ? -1.670  106.808 2.097   1.00 30.90 ? 194 TYR B CB    1 
ATOM   3528 C CG    . TYR B 1 194 ? -1.701  108.256 1.686   1.00 30.53 ? 194 TYR B CG    1 
ATOM   3529 C CD1   . TYR B 1 194 ? -2.178  109.216 2.565   1.00 30.31 ? 194 TYR B CD1   1 
ATOM   3530 C CD2   . TYR B 1 194 ? -1.236  108.669 0.448   1.00 30.67 ? 194 TYR B CD2   1 
ATOM   3531 C CE1   . TYR B 1 194 ? -2.211  110.558 2.234   1.00 29.97 ? 194 TYR B CE1   1 
ATOM   3532 C CE2   . TYR B 1 194 ? -1.297  109.994 0.072   1.00 30.72 ? 194 TYR B CE2   1 
ATOM   3533 C CZ    . TYR B 1 194 ? -1.770  110.928 0.984   1.00 30.56 ? 194 TYR B CZ    1 
ATOM   3534 O OH    . TYR B 1 194 ? -1.797  112.244 0.575   1.00 30.61 ? 194 TYR B OH    1 
ATOM   3535 N N     . ARG B 1 195 ? -0.023  104.470 4.106   1.00 29.82 ? 195 ARG B N     1 
ATOM   3536 C CA    . ARG B 1 195 ? -0.010  103.080 4.553   1.00 29.08 ? 195 ARG B CA    1 
ATOM   3537 C C     . ARG B 1 195 ? -1.265  102.846 5.398   1.00 28.82 ? 195 ARG B C     1 
ATOM   3538 O O     . ARG B 1 195 ? -1.406  103.373 6.500   1.00 28.28 ? 195 ARG B O     1 
ATOM   3539 C CB    . ARG B 1 195 ? 1.264   102.868 5.341   1.00 27.35 ? 195 ARG B CB    1 
ATOM   3540 C CG    . ARG B 1 195 ? 2.023   101.577 5.392   1.00 26.43 ? 195 ARG B CG    1 
ATOM   3541 C CD    . ARG B 1 195 ? 2.985   101.549 6.586   1.00 25.72 ? 195 ARG B CD    1 
ATOM   3542 N NE    . ARG B 1 195 ? 2.399   100.836 7.709   1.00 26.57 ? 195 ARG B NE    1 
ATOM   3543 C CZ    . ARG B 1 195 ? 2.483   101.130 8.996   1.00 27.11 ? 195 ARG B CZ    1 
ATOM   3544 N NH1   . ARG B 1 195 ? 1.895   100.310 9.867   1.00 28.83 ? 195 ARG B NH1   1 
ATOM   3545 N NH2   . ARG B 1 195 ? 3.098   102.246 9.356   1.00 25.53 ? 195 ARG B NH2   1 
ATOM   3546 N N     . ILE B 1 196 ? -2.247  102.199 4.775   1.00 28.91 ? 196 ILE B N     1 
ATOM   3547 C CA    . ILE B 1 196 ? -3.522  101.910 5.419   1.00 28.63 ? 196 ILE B CA    1 
ATOM   3548 C C     . ILE B 1 196 ? -3.522  100.487 5.956   1.00 28.24 ? 196 ILE B C     1 
ATOM   3549 O O     . ILE B 1 196 ? -3.113  99.587  5.234   1.00 28.06 ? 196 ILE B O     1 
ATOM   3550 C CB    . ILE B 1 196 ? -4.702  102.078 4.445   1.00 29.10 ? 196 ILE B CB    1 
ATOM   3551 C CG1   . ILE B 1 196 ? -4.868  103.545 4.022   1.00 29.16 ? 196 ILE B CG1   1 
ATOM   3552 C CG2   . ILE B 1 196 ? -6.017  101.617 5.047   1.00 29.75 ? 196 ILE B CG2   1 
ATOM   3553 C CD1   . ILE B 1 196 ? -4.090  103.864 2.762   1.00 29.85 ? 196 ILE B CD1   1 
ATOM   3554 N N     . THR B 1 197 ? -3.882  100.353 7.223   1.00 28.37 ? 197 THR B N     1 
ATOM   3555 C CA    . THR B 1 197 ? -4.062  99.053  7.861   1.00 28.86 ? 197 THR B CA    1 
ATOM   3556 C C     . THR B 1 197 ? -5.491  98.879  8.364   1.00 29.18 ? 197 THR B C     1 
ATOM   3557 O O     . THR B 1 197 ? -6.196  99.879  8.534   1.00 29.84 ? 197 THR B O     1 
ATOM   3558 C CB    . THR B 1 197 ? -3.140  98.888  9.078   1.00 28.74 ? 197 THR B CB    1 
ATOM   3559 O OG1   . THR B 1 197 ? -3.429  99.909  10.050  1.00 30.36 ? 197 THR B OG1   1 
ATOM   3560 C CG2   . THR B 1 197 ? -1.687  98.997  8.647   1.00 28.35 ? 197 THR B CG2   1 
ATOM   3561 N N     . HIS B 1 198 ? -5.940  97.650  8.579   1.00 29.51 ? 198 HIS B N     1 
ATOM   3562 C CA    . HIS B 1 198 ? -7.322  97.461  9.044   1.00 29.64 ? 198 HIS B CA    1 
ATOM   3563 C C     . HIS B 1 198 ? -7.340  96.592  10.288  1.00 29.58 ? 198 HIS B C     1 
ATOM   3564 O O     . HIS B 1 198 ? -6.707  95.547  10.311  1.00 29.39 ? 198 HIS B O     1 
ATOM   3565 C CB    . HIS B 1 198 ? -8.193  96.945  7.921   1.00 30.78 ? 198 HIS B CB    1 
ATOM   3566 C CG    . HIS B 1 198 ? -9.495  96.351  8.320   1.00 30.81 ? 198 HIS B CG    1 
ATOM   3567 N ND1   . HIS B 1 198 ? -10.295 96.938  9.260   1.00 32.18 ? 198 HIS B ND1   1 
ATOM   3568 C CD2   . HIS B 1 198 ? -10.141 95.229  7.954   1.00 31.73 ? 198 HIS B CD2   1 
ATOM   3569 C CE1   . HIS B 1 198 ? -11.369 96.196  9.443   1.00 32.75 ? 198 HIS B CE1   1 
ATOM   3570 N NE2   . HIS B 1 198 ? -11.305 95.137  8.658   1.00 32.32 ? 198 HIS B NE2   1 
ATOM   3571 N N     . THR B 1 199 ? -7.938  97.137  11.334  1.00 29.81 ? 199 THR B N     1 
ATOM   3572 C CA    . THR B 1 199 ? -8.015  96.542  12.647  1.00 30.29 ? 199 THR B CA    1 
ATOM   3573 C C     . THR B 1 199 ? -6.772  95.723  12.962  1.00 30.95 ? 199 THR B C     1 
ATOM   3574 O O     . THR B 1 199 ? -5.672  96.262  13.165  1.00 31.12 ? 199 THR B O     1 
ATOM   3575 C CB    . THR B 1 199 ? -9.325  95.771  12.853  1.00 29.38 ? 199 THR B CB    1 
ATOM   3576 O OG1   . THR B 1 199 ? -9.428  94.684  11.926  1.00 30.96 ? 199 THR B OG1   1 
ATOM   3577 C CG2   . THR B 1 199 ? -10.524 96.686  12.653  1.00 28.52 ? 199 THR B CG2   1 
ATOM   3578 N N     . ASN B 1 200 ? -6.912  94.406  12.947  1.00 31.14 ? 200 ASN B N     1 
ATOM   3579 C CA    . ASN B 1 200 ? -5.796  93.540  13.278  1.00 31.86 ? 200 ASN B CA    1 
ATOM   3580 C C     . ASN B 1 200 ? -5.548  92.536  12.170  1.00 31.91 ? 200 ASN B C     1 
ATOM   3581 O O     . ASN B 1 200 ? -5.402  91.332  12.357  1.00 31.90 ? 200 ASN B O     1 
ATOM   3582 C CB    . ASN B 1 200 ? -6.056  92.868  14.619  1.00 35.99 ? 200 ASN B CB    1 
ATOM   3583 C CG    . ASN B 1 200 ? -7.360  92.108  14.617  1.00 36.87 ? 200 ASN B CG    1 
ATOM   3584 O OD1   . ASN B 1 200 ? -8.153  92.220  13.687  1.00 38.48 ? 200 ASN B OD1   1 
ATOM   3585 N ND2   . ASN B 1 200 ? -7.606  91.284  15.622  1.00 39.13 ? 200 ASN B ND2   1 
ATOM   3586 N N     . ASP B 1 201 ? -5.598  93.083  10.958  1.00 32.12 ? 201 ASP B N     1 
ATOM   3587 C CA    . ASP B 1 201 ? -5.105  92.323  9.808   1.00 32.34 ? 201 ASP B CA    1 
ATOM   3588 C C     . ASP B 1 201 ? -3.750  91.751  10.238  1.00 32.77 ? 201 ASP B C     1 
ATOM   3589 O O     . ASP B 1 201 ? -2.866  92.490  10.708  1.00 32.67 ? 201 ASP B O     1 
ATOM   3590 C CB    . ASP B 1 201 ? -4.872  93.300  8.647   1.00 32.55 ? 201 ASP B CB    1 
ATOM   3591 C CG    . ASP B 1 201 ? -4.421  92.550  7.408   1.00 33.10 ? 201 ASP B CG    1 
ATOM   3592 O OD1   . ASP B 1 201 ? -4.202  91.326  7.536   1.00 31.52 ? 201 ASP B OD1   1 
ATOM   3593 O OD2   . ASP B 1 201 ? -4.299  93.141  6.313   1.00 33.79 ? 201 ASP B OD2   1 
ATOM   3594 N N     . ILE B 1 202 ? -3.546  90.455  10.017  1.00 32.69 ? 202 ILE B N     1 
ATOM   3595 C CA    . ILE B 1 202 ? -2.273  89.860  10.407  1.00 32.57 ? 202 ILE B CA    1 
ATOM   3596 C C     . ILE B 1 202 ? -1.111  90.344  9.541   1.00 32.44 ? 202 ILE B C     1 
ATOM   3597 O O     . ILE B 1 202 ? 0.003   90.493  10.046  1.00 32.56 ? 202 ILE B O     1 
ATOM   3598 C CB    . ILE B 1 202 ? -2.294  88.323  10.345  1.00 32.77 ? 202 ILE B CB    1 
ATOM   3599 C CG1   . ILE B 1 202 ? -0.995  87.795  10.969  1.00 33.50 ? 202 ILE B CG1   1 
ATOM   3600 C CG2   . ILE B 1 202 ? -2.427  87.823  8.915   1.00 31.09 ? 202 ILE B CG2   1 
ATOM   3601 C CD1   . ILE B 1 202 ? -0.981  86.285  11.042  1.00 34.93 ? 202 ILE B CD1   1 
ATOM   3602 N N     . VAL B 1 203 ? -1.362  90.655  8.271   1.00 31.92 ? 203 VAL B N     1 
ATOM   3603 C CA    . VAL B 1 203 ? -0.337  90.967  7.308   1.00 31.34 ? 203 VAL B CA    1 
ATOM   3604 C C     . VAL B 1 203 ? 0.538   92.162  7.561   1.00 31.59 ? 203 VAL B C     1 
ATOM   3605 O O     . VAL B 1 203 ? 1.767   91.978  7.571   1.00 31.40 ? 203 VAL B O     1 
ATOM   3606 C CB    . VAL B 1 203 ? -0.769  90.888  5.842   1.00 29.71 ? 203 VAL B CB    1 
ATOM   3607 C CG1   . VAL B 1 203 ? 0.397   91.144  4.892   1.00 30.04 ? 203 VAL B CG1   1 
ATOM   3608 C CG2   . VAL B 1 203 ? -1.298  89.492  5.516   1.00 29.92 ? 203 VAL B CG2   1 
ATOM   3609 N N     . PRO B 1 204 ? 0.029   93.293  8.032   1.00 31.76 ? 204 PRO B N     1 
ATOM   3610 C CA    . PRO B 1 204 ? 0.856   94.432  8.398   1.00 31.51 ? 204 PRO B CA    1 
ATOM   3611 C C     . PRO B 1 204 ? 1.698   94.123  9.623   1.00 31.49 ? 204 PRO B C     1 
ATOM   3612 O O     . PRO B 1 204 ? 2.580   94.918  9.975   1.00 31.80 ? 204 PRO B O     1 
ATOM   3613 C CB    . PRO B 1 204 ? -0.117  95.571  8.624   1.00 31.47 ? 204 PRO B CB    1 
ATOM   3614 C CG    . PRO B 1 204 ? -1.408  95.152  8.023   1.00 31.63 ? 204 PRO B CG    1 
ATOM   3615 C CD    . PRO B 1 204 ? -1.411  93.640  8.053   1.00 31.88 ? 204 PRO B CD    1 
ATOM   3616 N N     . ARG B 1 205 ? 1.493   93.009  10.323  1.00 31.17 ? 205 ARG B N     1 
ATOM   3617 C CA    . ARG B 1 205 ? 2.284   92.585  11.461  1.00 30.56 ? 205 ARG B CA    1 
ATOM   3618 C C     . ARG B 1 205 ? 3.426   91.652  11.077  1.00 29.86 ? 205 ARG B C     1 
ATOM   3619 O O     . ARG B 1 205 ? 4.169   91.169  11.939  1.00 29.43 ? 205 ARG B O     1 
ATOM   3620 C CB    . ARG B 1 205 ? 1.448   92.005  12.615  1.00 29.38 ? 205 ARG B CB    1 
ATOM   3621 C CG    . ARG B 1 205 ? 0.003   92.422  12.673  1.00 31.05 ? 205 ARG B CG    1 
ATOM   3622 C CD    . ARG B 1 205 ? -0.494  93.037  13.967  1.00 31.30 ? 205 ARG B CD    1 
ATOM   3623 N NE    . ARG B 1 205 ? -1.270  92.125  14.773  1.00 32.13 ? 205 ARG B NE    1 
ATOM   3624 C CZ    . ARG B 1 205 ? -2.262  92.301  15.622  1.00 31.22 ? 205 ARG B CZ    1 
ATOM   3625 N NH1   . ARG B 1 205 ? -2.750  91.205  16.211  1.00 33.49 ? 205 ARG B NH1   1 
ATOM   3626 N NH2   . ARG B 1 205 ? -2.804  93.457  15.934  1.00 27.90 ? 205 ARG B NH2   1 
ATOM   3627 N N     . LEU B 1 206 ? 3.680   91.367  9.808   1.00 29.51 ? 206 LEU B N     1 
ATOM   3628 C CA    . LEU B 1 206 ? 4.784   90.499  9.398   1.00 29.42 ? 206 LEU B CA    1 
ATOM   3629 C C     . LEU B 1 206 ? 5.682   91.197  8.364   1.00 29.13 ? 206 LEU B C     1 
ATOM   3630 O O     . LEU B 1 206 ? 5.225   92.040  7.593   1.00 29.15 ? 206 LEU B O     1 
ATOM   3631 C CB    . LEU B 1 206 ? 4.303   89.257  8.663   1.00 29.24 ? 206 LEU B CB    1 
ATOM   3632 C CG    . LEU B 1 206 ? 3.667   88.004  9.190   1.00 28.59 ? 206 LEU B CG    1 
ATOM   3633 C CD1   . LEU B 1 206 ? 3.153   88.110  10.609  1.00 30.04 ? 206 LEU B CD1   1 
ATOM   3634 C CD2   . LEU B 1 206 ? 2.499   87.628  8.270   1.00 27.90 ? 206 LEU B CD2   1 
ATOM   3635 N N     . PRO B 1 207 ? 6.934   90.773  8.277   1.00 28.85 ? 207 PRO B N     1 
ATOM   3636 C CA    . PRO B 1 207 ? 7.522   89.800  9.172   1.00 29.29 ? 207 PRO B CA    1 
ATOM   3637 C C     . PRO B 1 207 ? 7.611   90.341  10.593  1.00 29.71 ? 207 PRO B C     1 
ATOM   3638 O O     . PRO B 1 207 ? 7.352   91.512  10.825  1.00 29.20 ? 207 PRO B O     1 
ATOM   3639 C CB    . PRO B 1 207 ? 8.936   89.589  8.621   1.00 28.89 ? 207 PRO B CB    1 
ATOM   3640 C CG    . PRO B 1 207 ? 8.881   90.046  7.207   1.00 28.37 ? 207 PRO B CG    1 
ATOM   3641 C CD    . PRO B 1 207 ? 7.914   91.203  7.248   1.00 28.65 ? 207 PRO B CD    1 
ATOM   3642 N N     . PRO B 1 208 ? 7.829   89.457  11.560  1.00 30.70 ? 208 PRO B N     1 
ATOM   3643 C CA    . PRO B 1 208 ? 8.001   89.874  12.943  1.00 31.59 ? 208 PRO B CA    1 
ATOM   3644 C C     . PRO B 1 208 ? 9.068   90.961  12.998  1.00 32.66 ? 208 PRO B C     1 
ATOM   3645 O O     . PRO B 1 208 ? 10.050  90.922  12.240  1.00 32.80 ? 208 PRO B O     1 
ATOM   3646 C CB    . PRO B 1 208 ? 8.492   88.618  13.651  1.00 31.30 ? 208 PRO B CB    1 
ATOM   3647 C CG    . PRO B 1 208 ? 8.149   87.488  12.746  1.00 31.10 ? 208 PRO B CG    1 
ATOM   3648 C CD    . PRO B 1 208 ? 8.204   88.036  11.350  1.00 30.76 ? 208 PRO B CD    1 
ATOM   3649 N N     . ARG B 1 209 ? 9.035   91.790  14.035  1.00 33.66 ? 209 ARG B N     1 
ATOM   3650 C CA    . ARG B 1 209 ? 10.092  92.781  14.226  1.00 34.68 ? 209 ARG B CA    1 
ATOM   3651 C C     . ARG B 1 209 ? 11.403  92.127  14.621  1.00 35.24 ? 209 ARG B C     1 
ATOM   3652 O O     . ARG B 1 209 ? 12.464  92.592  14.192  1.00 35.60 ? 209 ARG B O     1 
ATOM   3653 C CB    . ARG B 1 209 ? 9.675   93.779  15.304  1.00 37.52 ? 209 ARG B CB    1 
ATOM   3654 C CG    . ARG B 1 209 ? 8.350   94.434  14.935  1.00 41.49 ? 209 ARG B CG    1 
ATOM   3655 C CD    . ARG B 1 209 ? 8.275   95.867  15.414  1.00 44.07 ? 209 ARG B CD    1 
ATOM   3656 N NE    . ARG B 1 209 ? 9.611   96.450  15.613  1.00 45.26 ? 209 ARG B NE    1 
ATOM   3657 C CZ    . ARG B 1 209 ? 9.855   97.221  16.677  1.00 45.90 ? 209 ARG B CZ    1 
ATOM   3658 N NH1   . ARG B 1 209 ? 8.919   97.488  17.587  1.00 46.17 ? 209 ARG B NH1   1 
ATOM   3659 N NH2   . ARG B 1 209 ? 11.079  97.707  16.798  1.00 45.63 ? 209 ARG B NH2   1 
ATOM   3660 N N     . GLU B 1 210 ? 11.349  90.965  15.270  1.00 35.28 ? 210 GLU B N     1 
ATOM   3661 C CA    . GLU B 1 210 ? 12.499  90.173  15.620  1.00 35.01 ? 210 GLU B CA    1 
ATOM   3662 C C     . GLU B 1 210 ? 13.349  89.769  14.437  1.00 34.01 ? 210 GLU B C     1 
ATOM   3663 O O     . GLU B 1 210 ? 14.542  89.575  14.651  1.00 34.55 ? 210 GLU B O     1 
ATOM   3664 C CB    . GLU B 1 210 ? 12.122  88.906  16.382  1.00 39.40 ? 210 GLU B CB    1 
ATOM   3665 C CG    . GLU B 1 210 ? 11.252  89.276  17.584  1.00 45.61 ? 210 GLU B CG    1 
ATOM   3666 C CD    . GLU B 1 210 ? 9.794   89.312  17.148  1.00 49.16 ? 210 GLU B CD    1 
ATOM   3667 O OE1   . GLU B 1 210 ? 9.162   90.385  17.242  1.00 49.66 ? 210 GLU B OE1   1 
ATOM   3668 O OE2   . GLU B 1 210 ? 9.305   88.249  16.697  1.00 52.27 ? 210 GLU B OE2   1 
ATOM   3669 N N     . PHE B 1 211 ? 12.850  89.729  13.208  1.00 33.02 ? 211 PHE B N     1 
ATOM   3670 C CA    . PHE B 1 211 ? 13.710  89.432  12.074  1.00 32.16 ? 211 PHE B CA    1 
ATOM   3671 C C     . PHE B 1 211 ? 14.333  90.718  11.542  1.00 31.94 ? 211 PHE B C     1 
ATOM   3672 O O     . PHE B 1 211 ? 14.960  90.724  10.485  1.00 31.96 ? 211 PHE B O     1 
ATOM   3673 C CB    . PHE B 1 211 ? 13.071  88.633  10.958  1.00 30.87 ? 211 PHE B CB    1 
ATOM   3674 C CG    . PHE B 1 211 ? 12.349  87.370  11.324  1.00 30.40 ? 211 PHE B CG    1 
ATOM   3675 C CD1   . PHE B 1 211 ? 11.506  86.743  10.413  1.00 30.14 ? 211 PHE B CD1   1 
ATOM   3676 C CD2   . PHE B 1 211 ? 12.494  86.795  12.575  1.00 28.94 ? 211 PHE B CD2   1 
ATOM   3677 C CE1   . PHE B 1 211 ? 10.869  85.569  10.776  1.00 31.51 ? 211 PHE B CE1   1 
ATOM   3678 C CE2   . PHE B 1 211 ? 11.822  85.671  12.963  1.00 27.21 ? 211 PHE B CE2   1 
ATOM   3679 C CZ    . PHE B 1 211 ? 11.021  85.037  12.046  1.00 29.17 ? 211 PHE B CZ    1 
ATOM   3680 N N     . GLY B 1 212 ? 14.178  91.821  12.258  1.00 31.60 ? 212 GLY B N     1 
ATOM   3681 C CA    . GLY B 1 212 ? 14.785  93.087  11.927  1.00 31.06 ? 212 GLY B CA    1 
ATOM   3682 C C     . GLY B 1 212 ? 13.964  93.946  10.987  1.00 30.67 ? 212 GLY B C     1 
ATOM   3683 O O     . GLY B 1 212 ? 14.542  94.734  10.240  1.00 30.99 ? 212 GLY B O     1 
ATOM   3684 N N     . TYR B 1 213 ? 12.642  93.926  11.081  1.00 29.97 ? 213 TYR B N     1 
ATOM   3685 C CA    . TYR B 1 213 ? 11.806  94.708  10.192  1.00 28.97 ? 213 TYR B CA    1 
ATOM   3686 C C     . TYR B 1 213 ? 11.125  95.856  10.906  1.00 29.25 ? 213 TYR B C     1 
ATOM   3687 O O     . TYR B 1 213 ? 10.749  95.709  12.075  1.00 29.61 ? 213 TYR B O     1 
ATOM   3688 C CB    . TYR B 1 213 ? 10.722  93.799  9.614   1.00 28.38 ? 213 TYR B CB    1 
ATOM   3689 C CG    . TYR B 1 213 ? 11.229  93.027  8.420   1.00 27.39 ? 213 TYR B CG    1 
ATOM   3690 C CD1   . TYR B 1 213 ? 11.105  93.590  7.154   1.00 26.76 ? 213 TYR B CD1   1 
ATOM   3691 C CD2   . TYR B 1 213 ? 11.835  91.781  8.559   1.00 26.68 ? 213 TYR B CD2   1 
ATOM   3692 C CE1   . TYR B 1 213 ? 11.567  92.902  6.047   1.00 26.15 ? 213 TYR B CE1   1 
ATOM   3693 C CE2   . TYR B 1 213 ? 12.298  91.094  7.447   1.00 25.69 ? 213 TYR B CE2   1 
ATOM   3694 C CZ    . TYR B 1 213 ? 12.148  91.663  6.202   1.00 25.41 ? 213 TYR B CZ    1 
ATOM   3695 O OH    . TYR B 1 213 ? 12.574  91.025  5.071   1.00 25.15 ? 213 TYR B OH    1 
ATOM   3696 N N     . SER B 1 214 ? 10.798  96.889  10.125  1.00 29.18 ? 214 SER B N     1 
ATOM   3697 C CA    . SER B 1 214 ? 10.165  98.058  10.731  1.00 29.06 ? 214 SER B CA    1 
ATOM   3698 C C     . SER B 1 214 ? 9.141   98.730  9.843   1.00 28.75 ? 214 SER B C     1 
ATOM   3699 O O     . SER B 1 214 ? 9.277   98.667  8.626   1.00 28.87 ? 214 SER B O     1 
ATOM   3700 C CB    . SER B 1 214 ? 11.242  99.112  11.051  1.00 29.06 ? 214 SER B CB    1 
ATOM   3701 O OG    . SER B 1 214 ? 11.207  99.332  12.446  1.00 29.12 ? 214 SER B OG    1 
ATOM   3702 N N     . HIS B 1 215 ? 8.204   99.439  10.462  1.00 28.46 ? 215 HIS B N     1 
ATOM   3703 C CA    . HIS B 1 215 ? 7.194   100.131 9.657   1.00 27.93 ? 215 HIS B CA    1 
ATOM   3704 C C     . HIS B 1 215 ? 7.513   101.612 9.552   1.00 27.86 ? 215 HIS B C     1 
ATOM   3705 O O     . HIS B 1 215 ? 7.898   102.253 10.524  1.00 28.00 ? 215 HIS B O     1 
ATOM   3706 C CB    . HIS B 1 215 ? 5.798   99.891  10.241  1.00 25.24 ? 215 HIS B CB    1 
ATOM   3707 C CG    . HIS B 1 215 ? 5.028   98.825  9.529   1.00 24.48 ? 215 HIS B CG    1 
ATOM   3708 N ND1   . HIS B 1 215 ? 4.873   98.850  8.161   1.00 25.10 ? 215 HIS B ND1   1 
ATOM   3709 C CD2   . HIS B 1 215 ? 4.374   97.719  9.954   1.00 24.66 ? 215 HIS B CD2   1 
ATOM   3710 C CE1   . HIS B 1 215 ? 4.143   97.821  7.766   1.00 25.39 ? 215 HIS B CE1   1 
ATOM   3711 N NE2   . HIS B 1 215 ? 3.804   97.137  8.847   1.00 25.70 ? 215 HIS B NE2   1 
ATOM   3712 N N     . SER B 1 216 ? 7.358   102.194 8.376   1.00 27.93 ? 216 SER B N     1 
ATOM   3713 C CA    . SER B 1 216 ? 7.447   103.641 8.215   1.00 28.38 ? 216 SER B CA    1 
ATOM   3714 C C     . SER B 1 216 ? 6.310   104.323 8.963   1.00 28.81 ? 216 SER B C     1 
ATOM   3715 O O     . SER B 1 216 ? 5.383   103.656 9.418   1.00 29.29 ? 216 SER B O     1 
ATOM   3716 C CB    . SER B 1 216 ? 7.328   103.943 6.714   1.00 28.24 ? 216 SER B CB    1 
ATOM   3717 O OG    . SER B 1 216 ? 6.097   103.392 6.270   1.00 30.40 ? 216 SER B OG    1 
ATOM   3718 N N     . SER B 1 217 ? 6.280   105.649 9.006   1.00 29.09 ? 217 SER B N     1 
ATOM   3719 C CA    . SER B 1 217 ? 5.196   106.390 9.656   1.00 29.34 ? 217 SER B CA    1 
ATOM   3720 C C     . SER B 1 217 ? 4.664   107.452 8.715   1.00 29.35 ? 217 SER B C     1 
ATOM   3721 O O     . SER B 1 217 ? 5.433   107.896 7.866   1.00 29.62 ? 217 SER B O     1 
ATOM   3722 C CB    . SER B 1 217 ? 5.780   107.049 10.902  1.00 30.66 ? 217 SER B CB    1 
ATOM   3723 O OG    . SER B 1 217 ? 4.858   107.967 11.461  1.00 32.74 ? 217 SER B OG    1 
ATOM   3724 N N     . PRO B 1 218 ? 3.404   107.839 8.800   1.00 29.50 ? 218 PRO B N     1 
ATOM   3725 C CA    . PRO B 1 218 ? 2.476   107.322 9.785   1.00 29.84 ? 218 PRO B CA    1 
ATOM   3726 C C     . PRO B 1 218 ? 1.660   106.122 9.321   1.00 30.19 ? 218 PRO B C     1 
ATOM   3727 O O     . PRO B 1 218 ? 1.810   105.658 8.189   1.00 30.01 ? 218 PRO B O     1 
ATOM   3728 C CB    . PRO B 1 218 ? 1.504   108.512 9.919   1.00 29.62 ? 218 PRO B CB    1 
ATOM   3729 C CG    . PRO B 1 218 ? 1.419   109.048 8.531   1.00 29.07 ? 218 PRO B CG    1 
ATOM   3730 C CD    . PRO B 1 218 ? 2.777   108.866 7.924   1.00 28.92 ? 218 PRO B CD    1 
ATOM   3731 N N     . GLU B 1 219 ? 0.626   105.798 10.095  1.00 30.43 ? 219 GLU B N     1 
ATOM   3732 C CA    . GLU B 1 219 ? -0.275  104.715 9.695   1.00 31.02 ? 219 GLU B CA    1 
ATOM   3733 C C     . GLU B 1 219 ? -1.701  105.245 9.705   1.00 31.54 ? 219 GLU B C     1 
ATOM   3734 O O     . GLU B 1 219 ? -2.044  105.989 10.627  1.00 31.96 ? 219 GLU B O     1 
ATOM   3735 C CB    . GLU B 1 219 ? -0.055  103.529 10.626  1.00 30.18 ? 219 GLU B CB    1 
ATOM   3736 C CG    . GLU B 1 219 ? -1.246  102.672 10.970  1.00 31.52 ? 219 GLU B CG    1 
ATOM   3737 C CD    . GLU B 1 219 ? -0.987  101.518 11.916  1.00 32.10 ? 219 GLU B CD    1 
ATOM   3738 O OE1   . GLU B 1 219 ? -0.007  101.573 12.696  1.00 32.45 ? 219 GLU B OE1   1 
ATOM   3739 O OE2   . GLU B 1 219 ? -1.801  100.560 11.872  1.00 29.59 ? 219 GLU B OE2   1 
ATOM   3740 N N     . TYR B 1 220 ? -2.474  104.962 8.669   1.00 31.76 ? 220 TYR B N     1 
ATOM   3741 C CA    . TYR B 1 220 ? -3.892  105.311 8.653   1.00 32.29 ? 220 TYR B CA    1 
ATOM   3742 C C     . TYR B 1 220 ? -4.666  104.031 8.995   1.00 32.38 ? 220 TYR B C     1 
ATOM   3743 O O     . TYR B 1 220 ? -4.590  103.017 8.283   1.00 32.58 ? 220 TYR B O     1 
ATOM   3744 C CB    . TYR B 1 220 ? -4.354  105.915 7.328   1.00 32.77 ? 220 TYR B CB    1 
ATOM   3745 C CG    . TYR B 1 220 ? -3.728  107.275 7.080   1.00 33.51 ? 220 TYR B CG    1 
ATOM   3746 C CD1   . TYR B 1 220 ? -2.508  107.349 6.425   1.00 33.97 ? 220 TYR B CD1   1 
ATOM   3747 C CD2   . TYR B 1 220 ? -4.309  108.453 7.517   1.00 33.61 ? 220 TYR B CD2   1 
ATOM   3748 C CE1   . TYR B 1 220 ? -1.897  108.565 6.192   1.00 34.34 ? 220 TYR B CE1   1 
ATOM   3749 C CE2   . TYR B 1 220 ? -3.704  109.672 7.304   1.00 33.99 ? 220 TYR B CE2   1 
ATOM   3750 C CZ    . TYR B 1 220 ? -2.503  109.723 6.636   1.00 34.63 ? 220 TYR B CZ    1 
ATOM   3751 O OH    . TYR B 1 220 ? -1.841  110.901 6.373   1.00 35.25 ? 220 TYR B OH    1 
ATOM   3752 N N     . TRP B 1 221 ? -5.090  103.941 10.250  1.00 32.31 ? 221 TRP B N     1 
ATOM   3753 C CA    . TRP B 1 221 ? -5.708  102.731 10.789  1.00 31.96 ? 221 TRP B CA    1 
ATOM   3754 C C     . TRP B 1 221 ? -7.221  102.765 10.645  1.00 31.38 ? 221 TRP B C     1 
ATOM   3755 O O     . TRP B 1 221 ? -7.884  103.621 11.221  1.00 30.66 ? 221 TRP B O     1 
ATOM   3756 C CB    . TRP B 1 221 ? -5.293  102.566 12.246  1.00 34.05 ? 221 TRP B CB    1 
ATOM   3757 C CG    . TRP B 1 221 ? -5.688  101.320 12.954  1.00 37.01 ? 221 TRP B CG    1 
ATOM   3758 C CD1   . TRP B 1 221 ? -5.498  100.033 12.530  1.00 38.65 ? 221 TRP B CD1   1 
ATOM   3759 C CD2   . TRP B 1 221 ? -6.325  101.219 14.236  1.00 38.31 ? 221 TRP B CD2   1 
ATOM   3760 N NE1   . TRP B 1 221 ? -5.985  99.139  13.460  1.00 39.39 ? 221 TRP B NE1   1 
ATOM   3761 C CE2   . TRP B 1 221 ? -6.509  99.846  14.513  1.00 39.35 ? 221 TRP B CE2   1 
ATOM   3762 C CE3   . TRP B 1 221 ? -6.790  102.152 15.164  1.00 38.34 ? 221 TRP B CE3   1 
ATOM   3763 C CZ2   . TRP B 1 221 ? -7.083  99.388  15.695  1.00 39.43 ? 221 TRP B CZ2   1 
ATOM   3764 C CZ3   . TRP B 1 221 ? -7.389  101.706 16.324  1.00 37.88 ? 221 TRP B CZ3   1 
ATOM   3765 C CH2   . TRP B 1 221 ? -7.526  100.338 16.579  1.00 39.42 ? 221 TRP B CH2   1 
ATOM   3766 N N     . ILE B 1 222 ? -7.747  101.871 9.811   1.00 31.45 ? 222 ILE B N     1 
ATOM   3767 C CA    . ILE B 1 222 ? -9.195  101.726 9.643   1.00 31.65 ? 222 ILE B CA    1 
ATOM   3768 C C     . ILE B 1 222 ? -9.747  100.916 10.815  1.00 32.22 ? 222 ILE B C     1 
ATOM   3769 O O     . ILE B 1 222 ? -9.389  99.742  10.893  1.00 32.27 ? 222 ILE B O     1 
ATOM   3770 C CB    . ILE B 1 222 ? -9.538  100.965 8.343   1.00 29.50 ? 222 ILE B CB    1 
ATOM   3771 C CG1   . ILE B 1 222 ? -9.008  101.740 7.145   1.00 29.27 ? 222 ILE B CG1   1 
ATOM   3772 C CG2   . ILE B 1 222 ? -11.040 100.733 8.287   1.00 28.09 ? 222 ILE B CG2   1 
ATOM   3773 C CD1   . ILE B 1 222 ? -9.459  101.320 5.768   1.00 28.56 ? 222 ILE B CD1   1 
ATOM   3774 N N     . LYS B 1 223 ? -10.549 101.477 11.709  1.00 33.05 ? 223 LYS B N     1 
ATOM   3775 C CA    . LYS B 1 223 ? -10.949 100.723 12.898  1.00 34.09 ? 223 LYS B CA    1 
ATOM   3776 C C     . LYS B 1 223 ? -12.330 100.101 12.811  1.00 33.88 ? 223 LYS B C     1 
ATOM   3777 O O     . LYS B 1 223 ? -12.772 99.417  13.735  1.00 33.76 ? 223 LYS B O     1 
ATOM   3778 C CB    . LYS B 1 223 ? -10.815 101.618 14.143  1.00 38.89 ? 223 LYS B CB    1 
ATOM   3779 C CG    . LYS B 1 223 ? -11.702 102.839 14.059  1.00 43.95 ? 223 LYS B CG    1 
ATOM   3780 C CD    . LYS B 1 223 ? -11.861 103.646 15.331  1.00 48.57 ? 223 LYS B CD    1 
ATOM   3781 C CE    . LYS B 1 223 ? -13.346 103.816 15.670  1.00 52.47 ? 223 LYS B CE    1 
ATOM   3782 N NZ    . LYS B 1 223 ? -14.264 103.910 14.494  1.00 54.00 ? 223 LYS B NZ    1 
ATOM   3783 N N     . SER B 1 224 ? -13.107 100.372 11.771  1.00 33.81 ? 224 SER B N     1 
ATOM   3784 C CA    . SER B 1 224 ? -14.410 99.727  11.621  1.00 33.79 ? 224 SER B CA    1 
ATOM   3785 C C     . SER B 1 224 ? -14.204 98.252  11.315  1.00 34.31 ? 224 SER B C     1 
ATOM   3786 O O     . SER B 1 224 ? -13.308 97.938  10.520  1.00 34.93 ? 224 SER B O     1 
ATOM   3787 C CB    . SER B 1 224 ? -15.173 100.425 10.500  1.00 33.64 ? 224 SER B CB    1 
ATOM   3788 O OG    . SER B 1 224 ? -14.325 100.642 9.390   1.00 35.26 ? 224 SER B OG    1 
ATOM   3789 N N     . GLY B 1 225 ? -15.074 97.352  11.756  1.00 34.18 ? 225 GLY B N     1 
ATOM   3790 C CA    . GLY B 1 225 ? -14.836 95.929  11.526  1.00 33.78 ? 225 GLY B CA    1 
ATOM   3791 C C     . GLY B 1 225 ? -14.980 95.466  10.089  1.00 33.43 ? 225 GLY B C     1 
ATOM   3792 O O     . GLY B 1 225 ? -15.240 96.261  9.192   1.00 33.23 ? 225 GLY B O     1 
ATOM   3793 N N     . THR B 1 226 ? -14.902 94.153  9.888   1.00 33.21 ? 226 THR B N     1 
ATOM   3794 C CA    . THR B 1 226 ? -14.990 93.510  8.590   1.00 32.77 ? 226 THR B CA    1 
ATOM   3795 C C     . THR B 1 226 ? -16.427 93.363  8.124   1.00 32.76 ? 226 THR B C     1 
ATOM   3796 O O     . THR B 1 226 ? -17.259 92.774  8.817   1.00 33.07 ? 226 THR B O     1 
ATOM   3797 C CB    . THR B 1 226 ? -14.437 92.067  8.696   1.00 33.34 ? 226 THR B CB    1 
ATOM   3798 O OG1   . THR B 1 226 ? -13.253 92.072  9.493   1.00 32.00 ? 226 THR B OG1   1 
ATOM   3799 C CG2   . THR B 1 226 ? -14.179 91.430  7.344   1.00 34.05 ? 226 THR B CG2   1 
ATOM   3800 N N     . LEU B 1 227 ? -16.704 93.764  6.893   1.00 32.69 ? 227 LEU B N     1 
ATOM   3801 C CA    . LEU B 1 227 ? -18.022 93.717  6.296   1.00 32.68 ? 227 LEU B CA    1 
ATOM   3802 C C     . LEU B 1 227 ? -18.879 94.920  6.672   1.00 32.98 ? 227 LEU B C     1 
ATOM   3803 O O     . LEU B 1 227 ? -19.961 95.052  6.092   1.00 33.37 ? 227 LEU B O     1 
ATOM   3804 C CB    . LEU B 1 227 ? -18.788 92.422  6.527   1.00 30.43 ? 227 LEU B CB    1 
ATOM   3805 C CG    . LEU B 1 227 ? -18.287 91.163  5.826   1.00 29.23 ? 227 LEU B CG    1 
ATOM   3806 C CD1   . LEU B 1 227 ? -19.152 89.960  6.191   1.00 29.39 ? 227 LEU B CD1   1 
ATOM   3807 C CD2   . LEU B 1 227 ? -18.263 91.333  4.315   1.00 28.90 ? 227 LEU B CD2   1 
ATOM   3808 N N     . VAL B 1 228 ? -18.438 95.766  7.588   1.00 33.06 ? 228 VAL B N     1 
ATOM   3809 C CA    . VAL B 1 228 ? -19.175 96.994  7.895   1.00 33.69 ? 228 VAL B CA    1 
ATOM   3810 C C     . VAL B 1 228 ? -18.489 98.051  7.031   1.00 34.27 ? 228 VAL B C     1 
ATOM   3811 O O     . VAL B 1 228 ? -17.275 97.969  6.839   1.00 34.47 ? 228 VAL B O     1 
ATOM   3812 C CB    . VAL B 1 228 ? -19.171 97.366  9.377   1.00 33.07 ? 228 VAL B CB    1 
ATOM   3813 C CG1   . VAL B 1 228 ? -18.665 96.218  10.241  1.00 31.78 ? 228 VAL B CG1   1 
ATOM   3814 C CG2   . VAL B 1 228 ? -18.415 98.646  9.705   1.00 32.93 ? 228 VAL B CG2   1 
ATOM   3815 N N     . PRO B 1 229 ? -19.237 98.981  6.469   1.00 34.48 ? 229 PRO B N     1 
ATOM   3816 C CA    . PRO B 1 229 ? -18.662 100.016 5.627   1.00 34.71 ? 229 PRO B CA    1 
ATOM   3817 C C     . PRO B 1 229 ? -17.870 101.014 6.450   1.00 35.42 ? 229 PRO B C     1 
ATOM   3818 O O     . PRO B 1 229 ? -17.904 101.036 7.682   1.00 35.84 ? 229 PRO B O     1 
ATOM   3819 C CB    . PRO B 1 229 ? -19.857 100.655 4.966   1.00 34.63 ? 229 PRO B CB    1 
ATOM   3820 C CG    . PRO B 1 229 ? -21.048 99.862  5.341   1.00 34.61 ? 229 PRO B CG    1 
ATOM   3821 C CD    . PRO B 1 229 ? -20.700 99.106  6.595   1.00 34.37 ? 229 PRO B CD    1 
ATOM   3822 N N     . VAL B 1 230 ? -16.967 101.712 5.780   1.00 36.17 ? 230 VAL B N     1 
ATOM   3823 C CA    . VAL B 1 230 ? -16.041 102.642 6.422   1.00 36.66 ? 230 VAL B CA    1 
ATOM   3824 C C     . VAL B 1 230 ? -16.486 104.078 6.170   1.00 37.12 ? 230 VAL B C     1 
ATOM   3825 O O     . VAL B 1 230 ? -17.027 104.409 5.118   1.00 36.99 ? 230 VAL B O     1 
ATOM   3826 C CB    . VAL B 1 230 ? -14.617 102.470 5.858   1.00 36.15 ? 230 VAL B CB    1 
ATOM   3827 C CG1   . VAL B 1 230 ? -13.612 103.398 6.508   1.00 36.27 ? 230 VAL B CG1   1 
ATOM   3828 C CG2   . VAL B 1 230 ? -14.163 101.023 5.980   1.00 35.71 ? 230 VAL B CG2   1 
ATOM   3829 N N     . THR B 1 231 ? -16.387 104.879 7.220   1.00 37.67 ? 231 THR B N     1 
ATOM   3830 C CA    . THR B 1 231 ? -16.689 106.310 7.143   1.00 38.58 ? 231 THR B CA    1 
ATOM   3831 C C     . THR B 1 231 ? -15.439 107.080 7.559   1.00 38.99 ? 231 THR B C     1 
ATOM   3832 O O     . THR B 1 231 ? -14.519 106.510 8.166   1.00 38.91 ? 231 THR B O     1 
ATOM   3833 C CB    . THR B 1 231 ? -17.846 106.672 8.091   1.00 38.33 ? 231 THR B CB    1 
ATOM   3834 O OG1   . THR B 1 231 ? -17.379 106.377 9.418   1.00 39.54 ? 231 THR B OG1   1 
ATOM   3835 C CG2   . THR B 1 231 ? -19.113 105.884 7.815   1.00 37.51 ? 231 THR B CG2   1 
ATOM   3836 N N     . ARG B 1 232 ? -15.342 108.380 7.280   1.00 39.53 ? 232 ARG B N     1 
ATOM   3837 C CA    . ARG B 1 232 ? -14.132 109.133 7.600   1.00 40.09 ? 232 ARG B CA    1 
ATOM   3838 C C     . ARG B 1 232 ? -13.857 109.253 9.090   1.00 40.27 ? 232 ARG B C     1 
ATOM   3839 O O     . ARG B 1 232 ? -12.707 109.472 9.489   1.00 40.04 ? 232 ARG B O     1 
ATOM   3840 C CB    . ARG B 1 232 ? -14.047 110.503 6.942   1.00 40.83 ? 232 ARG B CB    1 
ATOM   3841 C CG    . ARG B 1 232 ? -15.403 111.124 6.645   1.00 43.89 ? 232 ARG B CG    1 
ATOM   3842 C CD    . ARG B 1 232 ? -15.226 112.366 5.776   1.00 45.84 ? 232 ARG B CD    1 
ATOM   3843 N NE    . ARG B 1 232 ? -14.647 113.453 6.570   1.00 47.66 ? 232 ARG B NE    1 
ATOM   3844 C CZ    . ARG B 1 232 ? -15.344 114.061 7.527   1.00 48.51 ? 232 ARG B CZ    1 
ATOM   3845 N NH1   . ARG B 1 232 ? -14.834 115.033 8.265   1.00 48.74 ? 232 ARG B NH1   1 
ATOM   3846 N NH2   . ARG B 1 232 ? -16.599 113.697 7.774   1.00 49.46 ? 232 ARG B NH2   1 
ATOM   3847 N N     . ASN B 1 233 ? -14.815 108.924 9.946   1.00 40.71 ? 233 ASN B N     1 
ATOM   3848 C CA    . ASN B 1 233 ? -14.604 108.900 11.379  1.00 41.33 ? 233 ASN B CA    1 
ATOM   3849 C C     . ASN B 1 233 ? -14.081 107.550 11.829  1.00 41.18 ? 233 ASN B C     1 
ATOM   3850 O O     . ASN B 1 233 ? -13.964 107.346 13.046  1.00 42.16 ? 233 ASN B O     1 
ATOM   3851 C CB    . ASN B 1 233 ? -15.893 109.263 12.130  1.00 46.33 ? 233 ASN B CB    1 
ATOM   3852 C CG    . ASN B 1 233 ? -15.964 110.773 12.326  1.00 50.35 ? 233 ASN B CG    1 
ATOM   3853 O OD1   . ASN B 1 233 ? -16.491 111.543 11.511  1.00 50.96 ? 233 ASN B OD1   1 
ATOM   3854 N ND2   . ASN B 1 233 ? -15.378 111.204 13.446  1.00 52.88 ? 233 ASN B ND2   1 
ATOM   3855 N N     . ASP B 1 234 ? -13.846 106.604 10.928  1.00 40.37 ? 234 ASP B N     1 
ATOM   3856 C CA    . ASP B 1 234 ? -13.315 105.301 11.307  1.00 39.62 ? 234 ASP B CA    1 
ATOM   3857 C C     . ASP B 1 234 ? -11.817 105.166 11.052  1.00 39.17 ? 234 ASP B C     1 
ATOM   3858 O O     . ASP B 1 234 ? -11.157 104.255 11.564  1.00 39.28 ? 234 ASP B O     1 
ATOM   3859 C CB    . ASP B 1 234 ? -14.051 104.206 10.530  1.00 41.11 ? 234 ASP B CB    1 
ATOM   3860 C CG    . ASP B 1 234 ? -15.519 104.182 10.933  1.00 43.40 ? 234 ASP B CG    1 
ATOM   3861 O OD1   . ASP B 1 234 ? -16.420 104.256 10.070  1.00 42.94 ? 234 ASP B OD1   1 
ATOM   3862 O OD2   . ASP B 1 234 ? -15.727 104.083 12.163  1.00 44.79 ? 234 ASP B OD2   1 
ATOM   3863 N N     . ILE B 1 235 ? -11.287 105.994 10.159  1.00 38.20 ? 235 ILE B N     1 
ATOM   3864 C CA    . ILE B 1 235 ? -9.864  105.975 9.833   1.00 37.12 ? 235 ILE B CA    1 
ATOM   3865 C C     . ILE B 1 235 ? -9.149  106.879 10.820  1.00 37.41 ? 235 ILE B C     1 
ATOM   3866 O O     . ILE B 1 235 ? -9.540  108.028 11.013  1.00 37.75 ? 235 ILE B O     1 
ATOM   3867 C CB    . ILE B 1 235 ? -9.710  106.456 8.383   1.00 35.21 ? 235 ILE B CB    1 
ATOM   3868 C CG1   . ILE B 1 235 ? -10.340 105.420 7.450   1.00 34.75 ? 235 ILE B CG1   1 
ATOM   3869 C CG2   . ILE B 1 235 ? -8.266  106.722 8.001   1.00 35.28 ? 235 ILE B CG2   1 
ATOM   3870 C CD1   . ILE B 1 235 ? -10.826 105.966 6.129   1.00 35.61 ? 235 ILE B CD1   1 
ATOM   3871 N N     . VAL B 1 236 ? -8.197  106.382 11.587  1.00 37.70 ? 236 VAL B N     1 
ATOM   3872 C CA    . VAL B 1 236 ? -7.443  107.169 12.565  1.00 38.13 ? 236 VAL B CA    1 
ATOM   3873 C C     . VAL B 1 236 ? -5.972  107.268 12.173  1.00 38.40 ? 236 VAL B C     1 
ATOM   3874 O O     . VAL B 1 236 ? -5.353  106.283 11.748  1.00 38.29 ? 236 VAL B O     1 
ATOM   3875 C CB    . VAL B 1 236 ? -7.606  106.497 13.943  1.00 38.64 ? 236 VAL B CB    1 
ATOM   3876 C CG1   . VAL B 1 236 ? -6.618  106.977 14.979  1.00 40.44 ? 236 VAL B CG1   1 
ATOM   3877 C CG2   . VAL B 1 236 ? -9.011  106.779 14.468  1.00 40.28 ? 236 VAL B CG2   1 
ATOM   3878 N N     . LYS B 1 237 ? -5.329  108.421 12.355  1.00 38.45 ? 237 LYS B N     1 
ATOM   3879 C CA    . LYS B 1 237 ? -3.932  108.563 11.946  1.00 38.47 ? 237 LYS B CA    1 
ATOM   3880 C C     . LYS B 1 237 ? -2.982  108.301 13.101  1.00 38.98 ? 237 LYS B C     1 
ATOM   3881 O O     . LYS B 1 237 ? -3.037  108.957 14.147  1.00 39.59 ? 237 LYS B O     1 
ATOM   3882 C CB    . LYS B 1 237 ? -3.698  109.958 11.385  1.00 38.34 ? 237 LYS B CB    1 
ATOM   3883 C CG    . LYS B 1 237 ? -2.338  110.176 10.760  1.00 38.66 ? 237 LYS B CG    1 
ATOM   3884 C CD    . LYS B 1 237 ? -2.203  111.596 10.235  1.00 39.79 ? 237 LYS B CD    1 
ATOM   3885 C CE    . LYS B 1 237 ? -0.829  111.816 9.626   1.00 41.77 ? 237 LYS B CE    1 
ATOM   3886 N NZ    . LYS B 1 237 ? -0.270  113.160 9.933   1.00 43.27 ? 237 LYS B NZ    1 
ATOM   3887 N N     . ILE B 1 238 ? -2.121  107.294 12.959  1.00 38.95 ? 238 ILE B N     1 
ATOM   3888 C CA    . ILE B 1 238 ? -1.210  106.935 14.052  1.00 38.58 ? 238 ILE B CA    1 
ATOM   3889 C C     . ILE B 1 238 ? 0.221   107.239 13.642  1.00 38.69 ? 238 ILE B C     1 
ATOM   3890 O O     . ILE B 1 238 ? 0.760   106.631 12.709  1.00 39.30 ? 238 ILE B O     1 
ATOM   3891 C CB    . ILE B 1 238 ? -1.380  105.467 14.469  1.00 37.74 ? 238 ILE B CB    1 
ATOM   3892 C CG1   . ILE B 1 238 ? -2.654  105.302 15.302  1.00 38.14 ? 238 ILE B CG1   1 
ATOM   3893 C CG2   . ILE B 1 238 ? -0.195  104.935 15.261  1.00 36.57 ? 238 ILE B CG2   1 
ATOM   3894 C CD1   . ILE B 1 238 ? -3.913  105.084 14.500  1.00 39.59 ? 238 ILE B CD1   1 
ATOM   3895 N N     . GLU B 1 239 ? 0.900   108.041 14.461  1.00 38.39 ? 239 GLU B N     1 
ATOM   3896 C CA    . GLU B 1 239 ? 2.236   108.487 14.101  1.00 37.86 ? 239 GLU B CA    1 
ATOM   3897 C C     . GLU B 1 239 ? 3.362   107.900 14.926  1.00 37.53 ? 239 GLU B C     1 
ATOM   3898 O O     . GLU B 1 239 ? 3.210   107.467 16.064  1.00 37.52 ? 239 GLU B O     1 
ATOM   3899 C CB    . GLU B 1 239 ? 2.303   110.003 14.172  1.00 40.43 ? 239 GLU B CB    1 
ATOM   3900 C CG    . GLU B 1 239 ? 2.855   110.606 12.888  1.00 45.24 ? 239 GLU B CG    1 
ATOM   3901 C CD    . GLU B 1 239 ? 2.178   111.938 12.585  1.00 48.49 ? 239 GLU B CD    1 
ATOM   3902 O OE1   . GLU B 1 239 ? 1.355   112.387 13.426  1.00 48.78 ? 239 GLU B OE1   1 
ATOM   3903 O OE2   . GLU B 1 239 ? 2.493   112.486 11.497  1.00 49.44 ? 239 GLU B OE2   1 
ATOM   3904 N N     . GLY B 1 240 ? 4.542   107.866 14.304  1.00 37.09 ? 240 GLY B N     1 
ATOM   3905 C CA    . GLY B 1 240 ? 5.727   107.295 14.900  1.00 36.63 ? 240 GLY B CA    1 
ATOM   3906 C C     . GLY B 1 240 ? 6.109   105.958 14.294  1.00 36.56 ? 240 GLY B C     1 
ATOM   3907 O O     . GLY B 1 240 ? 5.284   105.079 14.075  1.00 37.11 ? 240 GLY B O     1 
ATOM   3908 N N     . ILE B 1 241 ? 7.401   105.778 14.042  1.00 36.45 ? 241 ILE B N     1 
ATOM   3909 C CA    . ILE B 1 241 ? 7.927   104.536 13.486  1.00 36.01 ? 241 ILE B CA    1 
ATOM   3910 C C     . ILE B 1 241 ? 7.757   103.374 14.439  1.00 36.30 ? 241 ILE B C     1 
ATOM   3911 O O     . ILE B 1 241 ? 8.221   103.428 15.571  1.00 36.72 ? 241 ILE B O     1 
ATOM   3912 C CB    . ILE B 1 241 ? 9.414   104.711 13.104  1.00 33.71 ? 241 ILE B CB    1 
ATOM   3913 C CG1   . ILE B 1 241 ? 9.468   105.606 11.864  1.00 33.46 ? 241 ILE B CG1   1 
ATOM   3914 C CG2   . ILE B 1 241 ? 10.075  103.364 12.897  1.00 32.65 ? 241 ILE B CG2   1 
ATOM   3915 C CD1   . ILE B 1 241 ? 10.766  105.735 11.129  1.00 33.38 ? 241 ILE B CD1   1 
ATOM   3916 N N     . ASP B 1 242 ? 7.101   102.311 14.008  1.00 36.68 ? 242 ASP B N     1 
ATOM   3917 C CA    . ASP B 1 242 ? 6.824   101.118 14.782  1.00 36.75 ? 242 ASP B CA    1 
ATOM   3918 C C     . ASP B 1 242 ? 5.865   101.401 15.930  1.00 37.08 ? 242 ASP B C     1 
ATOM   3919 O O     . ASP B 1 242 ? 5.872   100.733 16.958  1.00 37.32 ? 242 ASP B O     1 
ATOM   3920 C CB    . ASP B 1 242 ? 8.046   100.392 15.302  1.00 35.49 ? 242 ASP B CB    1 
ATOM   3921 C CG    . ASP B 1 242 ? 8.797   99.626  14.240  1.00 37.28 ? 242 ASP B CG    1 
ATOM   3922 O OD1   . ASP B 1 242 ? 10.018  99.512  14.483  1.00 38.32 ? 242 ASP B OD1   1 
ATOM   3923 O OD2   . ASP B 1 242 ? 8.253   99.156  13.221  1.00 38.03 ? 242 ASP B OD2   1 
ATOM   3924 N N     . ALA B 1 243 ? 4.975   102.355 15.707  1.00 37.45 ? 243 ALA B N     1 
ATOM   3925 C CA    . ALA B 1 243 ? 3.972   102.763 16.669  1.00 37.79 ? 243 ALA B CA    1 
ATOM   3926 C C     . ALA B 1 243 ? 3.010   101.628 17.004  1.00 38.14 ? 243 ALA B C     1 
ATOM   3927 O O     . ALA B 1 243 ? 2.677   100.811 16.144  1.00 38.10 ? 243 ALA B O     1 
ATOM   3928 C CB    . ALA B 1 243 ? 3.157   103.898 16.059  1.00 38.55 ? 243 ALA B CB    1 
ATOM   3929 N N     . THR B 1 244 ? 2.569   101.621 18.260  1.00 38.32 ? 244 THR B N     1 
ATOM   3930 C CA    . THR B 1 244 ? 1.559   100.633 18.666  1.00 38.70 ? 244 THR B CA    1 
ATOM   3931 C C     . THR B 1 244 ? 0.227   101.346 18.830  1.00 38.89 ? 244 THR B C     1 
ATOM   3932 O O     . THR B 1 244 ? 0.221   102.577 18.728  1.00 39.59 ? 244 THR B O     1 
ATOM   3933 C CB    . THR B 1 244 ? 1.942   99.998  20.010  1.00 38.72 ? 244 THR B CB    1 
ATOM   3934 O OG1   . THR B 1 244 ? 1.710   100.958 21.055  1.00 40.21 ? 244 THR B OG1   1 
ATOM   3935 C CG2   . THR B 1 244 ? 3.401   99.585  20.019  1.00 36.54 ? 244 THR B CG2   1 
ATOM   3936 N N     . GLY B 1 245 ? -0.873  100.643 19.034  1.00 38.99 ? 245 GLY B N     1 
ATOM   3937 C CA    . GLY B 1 245 ? -2.129  101.390 19.199  1.00 39.68 ? 245 GLY B CA    1 
ATOM   3938 C C     . GLY B 1 245 ? -2.923  101.348 17.904  1.00 39.85 ? 245 GLY B C     1 
ATOM   3939 O O     . GLY B 1 245 ? -4.151  101.267 18.000  1.00 40.80 ? 245 GLY B O     1 
ATOM   3940 N N     . GLY B 1 246 ? -2.238  101.385 16.770  1.00 39.46 ? 246 GLY B N     1 
ATOM   3941 C CA    . GLY B 1 246 ? -2.933  101.178 15.497  1.00 39.18 ? 246 GLY B CA    1 
ATOM   3942 C C     . GLY B 1 246 ? -3.084  99.657  15.324  1.00 38.99 ? 246 GLY B C     1 
ATOM   3943 O O     . GLY B 1 246 ? -3.640  98.959  16.173  1.00 38.50 ? 246 GLY B O     1 
ATOM   3944 N N     . ASN B 1 247 ? -2.686  99.206  14.132  1.00 39.05 ? 247 ASN B N     1 
ATOM   3945 C CA    . ASN B 1 247 ? -2.775  97.784  13.809  1.00 39.16 ? 247 ASN B CA    1 
ATOM   3946 C C     . ASN B 1 247 ? -1.829  96.984  14.697  1.00 39.46 ? 247 ASN B C     1 
ATOM   3947 O O     . ASN B 1 247 ? -2.148  95.901  15.177  1.00 40.05 ? 247 ASN B O     1 
ATOM   3948 C CB    . ASN B 1 247 ? -2.413  97.540  12.350  1.00 37.91 ? 247 ASN B CB    1 
ATOM   3949 C CG    . ASN B 1 247 ? -2.170  96.093  11.986  1.00 36.76 ? 247 ASN B CG    1 
ATOM   3950 O OD1   . ASN B 1 247 ? -3.092  95.374  11.604  1.00 37.84 ? 247 ASN B OD1   1 
ATOM   3951 N ND2   . ASN B 1 247 ? -0.932  95.639  12.097  1.00 35.40 ? 247 ASN B ND2   1 
ATOM   3952 N N     . ASN B 1 248 ? -0.628  97.503  14.881  1.00 39.53 ? 248 ASN B N     1 
ATOM   3953 C CA    . ASN B 1 248 ? 0.437   96.853  15.626  1.00 39.62 ? 248 ASN B CA    1 
ATOM   3954 C C     . ASN B 1 248 ? 0.243   96.870  17.128  1.00 39.99 ? 248 ASN B C     1 
ATOM   3955 O O     . ASN B 1 248 ? 0.832   97.644  17.884  1.00 40.34 ? 248 ASN B O     1 
ATOM   3956 C CB    . ASN B 1 248 ? 1.749   97.545  15.236  1.00 39.18 ? 248 ASN B CB    1 
ATOM   3957 C CG    . ASN B 1 248 ? 2.933   97.160  16.080  1.00 38.65 ? 248 ASN B CG    1 
ATOM   3958 O OD1   . ASN B 1 248 ? 3.020   96.022  16.525  1.00 39.69 ? 248 ASN B OD1   1 
ATOM   3959 N ND2   . ASN B 1 248 ? 3.783   98.133  16.366  1.00 39.33 ? 248 ASN B ND2   1 
ATOM   3960 N N     . GLN B 1 249 ? -0.632  96.021  17.643  1.00 40.30 ? 249 GLN B N     1 
ATOM   3961 C CA    . GLN B 1 249 ? -0.890  95.856  19.059  1.00 40.51 ? 249 GLN B CA    1 
ATOM   3962 C C     . GLN B 1 249 ? -0.772  94.360  19.387  1.00 40.73 ? 249 GLN B C     1 
ATOM   3963 O O     . GLN B 1 249 ? -0.818  93.470  18.531  1.00 40.54 ? 249 GLN B O     1 
ATOM   3964 C CB    . GLN B 1 249 ? -2.267  96.358  19.470  1.00 41.92 ? 249 GLN B CB    1 
ATOM   3965 C CG    . GLN B 1 249 ? -2.750  97.687  18.926  1.00 44.74 ? 249 GLN B CG    1 
ATOM   3966 C CD    . GLN B 1 249 ? -4.122  98.054  19.461  1.00 46.82 ? 249 GLN B CD    1 
ATOM   3967 O OE1   . GLN B 1 249 ? -4.183  98.532  20.593  1.00 48.31 ? 249 GLN B OE1   1 
ATOM   3968 N NE2   . GLN B 1 249 ? -5.203  97.841  18.722  1.00 48.12 ? 249 GLN B NE2   1 
ATOM   3969 N N     . PRO B 1 250 ? -0.403  94.084  20.628  1.00 40.76 ? 250 PRO B N     1 
ATOM   3970 C CA    . PRO B 1 250 ? -0.343  92.713  21.116  1.00 41.04 ? 250 PRO B CA    1 
ATOM   3971 C C     . PRO B 1 250 ? -1.741  92.130  21.262  1.00 41.50 ? 250 PRO B C     1 
ATOM   3972 O O     . PRO B 1 250 ? -2.589  92.658  22.008  1.00 42.52 ? 250 PRO B O     1 
ATOM   3973 C CB    . PRO B 1 250 ? 0.377   92.905  22.436  1.00 40.92 ? 250 PRO B CB    1 
ATOM   3974 C CG    . PRO B 1 250 ? -0.121  94.222  22.943  1.00 40.93 ? 250 PRO B CG    1 
ATOM   3975 C CD    . PRO B 1 250 ? -0.237  95.078  21.716  1.00 40.99 ? 250 PRO B CD    1 
ATOM   3976 N N     . ASN B 1 251 ? -2.149  91.302  20.299  1.00 41.21 ? 251 ASN B N     1 
ATOM   3977 C CA    . ASN B 1 251 ? -3.465  90.677  20.338  1.00 40.79 ? 251 ASN B CA    1 
ATOM   3978 C C     . ASN B 1 251 ? -3.626  89.715  19.169  1.00 40.41 ? 251 ASN B C     1 
ATOM   3979 O O     . ASN B 1 251 ? -2.733  89.632  18.317  1.00 40.38 ? 251 ASN B O     1 
ATOM   3980 C CB    . ASN B 1 251 ? -4.594  91.684  20.425  1.00 43.40 ? 251 ASN B CB    1 
ATOM   3981 C CG    . ASN B 1 251 ? -4.716  92.675  19.293  1.00 46.06 ? 251 ASN B CG    1 
ATOM   3982 O OD1   . ASN B 1 251 ? -3.954  92.652  18.321  1.00 47.38 ? 251 ASN B OD1   1 
ATOM   3983 N ND2   . ASN B 1 251 ? -5.691  93.580  19.402  1.00 46.68 ? 251 ASN B ND2   1 
ATOM   3984 N N     . ILE B 1 252 ? -4.628  88.837  19.254  1.00 40.01 ? 252 ILE B N     1 
ATOM   3985 C CA    . ILE B 1 252 ? -4.808  87.824  18.213  1.00 39.04 ? 252 ILE B CA    1 
ATOM   3986 C C     . ILE B 1 252 ? -5.056  88.575  16.901  1.00 38.18 ? 252 ILE B C     1 
ATOM   3987 O O     . ILE B 1 252 ? -5.918  89.448  16.820  1.00 38.33 ? 252 ILE B O     1 
ATOM   3988 C CB    . ILE B 1 252 ? -5.972  86.850  18.448  1.00 39.67 ? 252 ILE B CB    1 
ATOM   3989 C CG1   . ILE B 1 252 ? -5.916  86.157  19.809  1.00 40.36 ? 252 ILE B CG1   1 
ATOM   3990 C CG2   . ILE B 1 252 ? -6.025  85.744  17.399  1.00 40.29 ? 252 ILE B CG2   1 
ATOM   3991 C CD1   . ILE B 1 252 ? -6.446  87.028  20.932  1.00 42.04 ? 252 ILE B CD1   1 
ATOM   3992 N N     . PRO B 1 253 ? -4.235  88.261  15.918  1.00 37.26 ? 253 PRO B N     1 
ATOM   3993 C CA    . PRO B 1 253 ? -4.403  88.837  14.585  1.00 36.70 ? 253 PRO B CA    1 
ATOM   3994 C C     . PRO B 1 253 ? -5.590  88.111  13.968  1.00 36.21 ? 253 PRO B C     1 
ATOM   3995 O O     . PRO B 1 253 ? -5.941  87.037  14.462  1.00 35.80 ? 253 PRO B O     1 
ATOM   3996 C CB    . PRO B 1 253 ? -3.099  88.464  13.890  1.00 36.97 ? 253 PRO B CB    1 
ATOM   3997 C CG    . PRO B 1 253 ? -2.708  87.166  14.517  1.00 36.95 ? 253 PRO B CG    1 
ATOM   3998 C CD    . PRO B 1 253 ? -3.168  87.237  15.954  1.00 37.00 ? 253 PRO B CD    1 
ATOM   3999 N N     . ASP B 1 254 ? -6.003  88.515  12.779  1.00 36.13 ? 254 ASP B N     1 
ATOM   4000 C CA    . ASP B 1 254 ? -7.196  87.930  12.160  1.00 35.67 ? 254 ASP B CA    1 
ATOM   4001 C C     . ASP B 1 254 ? -6.963  87.780  10.670  1.00 35.04 ? 254 ASP B C     1 
ATOM   4002 O O     . ASP B 1 254 ? -6.214  88.614  10.162  1.00 35.62 ? 254 ASP B O     1 
ATOM   4003 C CB    . ASP B 1 254 ? -8.371  88.874  12.418  1.00 37.47 ? 254 ASP B CB    1 
ATOM   4004 C CG    . ASP B 1 254 ? -9.641  88.356  11.787  1.00 40.62 ? 254 ASP B CG    1 
ATOM   4005 O OD1   . ASP B 1 254 ? -10.238 87.437  12.385  1.00 42.44 ? 254 ASP B OD1   1 
ATOM   4006 O OD2   . ASP B 1 254 ? -10.029 88.840  10.702  1.00 43.80 ? 254 ASP B OD2   1 
ATOM   4007 N N     . ILE B 1 255 ? -7.573  86.826  9.975   1.00 34.32 ? 255 ILE B N     1 
ATOM   4008 C CA    . ILE B 1 255 ? -7.274  86.716  8.554   1.00 32.93 ? 255 ILE B CA    1 
ATOM   4009 C C     . ILE B 1 255 ? -8.260  87.462  7.682   1.00 31.96 ? 255 ILE B C     1 
ATOM   4010 O O     . ILE B 1 255 ? -7.839  88.339  6.931   1.00 31.81 ? 255 ILE B O     1 
ATOM   4011 C CB    . ILE B 1 255 ? -7.121  85.289  8.011   1.00 34.30 ? 255 ILE B CB    1 
ATOM   4012 C CG1   . ILE B 1 255 ? -6.120  84.450  8.800   1.00 34.63 ? 255 ILE B CG1   1 
ATOM   4013 C CG2   . ILE B 1 255 ? -6.724  85.349  6.534   1.00 33.81 ? 255 ILE B CG2   1 
ATOM   4014 C CD1   . ILE B 1 255 ? -4.799  85.144  9.027   1.00 36.39 ? 255 ILE B CD1   1 
ATOM   4015 N N     . PRO B 1 256 ? -9.564  87.271  7.863   1.00 30.91 ? 256 PRO B N     1 
ATOM   4016 C CA    . PRO B 1 256 ? -10.569 87.901  7.026   1.00 30.26 ? 256 PRO B CA    1 
ATOM   4017 C C     . PRO B 1 256 ? -10.515 89.416  7.073   1.00 29.76 ? 256 PRO B C     1 
ATOM   4018 O O     . PRO B 1 256 ? -10.691 90.064  6.031   1.00 29.83 ? 256 PRO B O     1 
ATOM   4019 C CB    . PRO B 1 256 ? -11.898 87.345  7.514   1.00 30.02 ? 256 PRO B CB    1 
ATOM   4020 C CG    . PRO B 1 256 ? -11.606 86.859  8.889   1.00 29.85 ? 256 PRO B CG    1 
ATOM   4021 C CD    . PRO B 1 256 ? -10.187 86.353  8.839   1.00 30.30 ? 256 PRO B CD    1 
ATOM   4022 N N     . ALA B 1 257 ? -9.961  89.976  8.146   1.00 28.73 ? 257 ALA B N     1 
ATOM   4023 C CA    . ALA B 1 257 ? -9.726  91.397  8.272   1.00 28.37 ? 257 ALA B CA    1 
ATOM   4024 C C     . ALA B 1 257 ? -8.849  91.923  7.151   1.00 28.04 ? 257 ALA B C     1 
ATOM   4025 O O     . ALA B 1 257 ? -9.114  92.943  6.516   1.00 28.67 ? 257 ALA B O     1 
ATOM   4026 C CB    . ALA B 1 257 ? -9.137  91.761  9.621   1.00 28.10 ? 257 ALA B CB    1 
ATOM   4027 N N     . HIS B 1 258 ? -7.878  91.144  6.718   1.00 27.47 ? 258 HIS B N     1 
ATOM   4028 C CA    . HIS B 1 258 ? -7.037  91.462  5.576   1.00 26.71 ? 258 HIS B CA    1 
ATOM   4029 C C     . HIS B 1 258 ? -7.832  91.562  4.283   1.00 27.29 ? 258 HIS B C     1 
ATOM   4030 O O     . HIS B 1 258 ? -7.378  92.196  3.316   1.00 27.73 ? 258 HIS B O     1 
ATOM   4031 C CB    . HIS B 1 258 ? -6.021  90.326  5.483   1.00 22.42 ? 258 HIS B CB    1 
ATOM   4032 C CG    . HIS B 1 258 ? -4.964  90.536  4.461   1.00 20.59 ? 258 HIS B CG    1 
ATOM   4033 N ND1   . HIS B 1 258 ? -4.016  91.525  4.547   1.00 18.66 ? 258 HIS B ND1   1 
ATOM   4034 C CD2   . HIS B 1 258 ? -4.731  89.887  3.289   1.00 19.79 ? 258 HIS B CD2   1 
ATOM   4035 C CE1   . HIS B 1 258 ? -3.231  91.461  3.484   1.00 18.29 ? 258 HIS B CE1   1 
ATOM   4036 N NE2   . HIS B 1 258 ? -3.649  90.495  2.692   1.00 17.29 ? 258 HIS B NE2   1 
ATOM   4037 N N     . LEU B 1 259 ? -8.966  90.878  4.159   1.00 27.37 ? 259 LEU B N     1 
ATOM   4038 C CA    . LEU B 1 259 ? -9.734  90.957  2.933   1.00 27.93 ? 259 LEU B CA    1 
ATOM   4039 C C     . LEU B 1 259 ? -10.614 92.194  2.894   1.00 28.26 ? 259 LEU B C     1 
ATOM   4040 O O     . LEU B 1 259 ? -11.051 92.530  1.795   1.00 28.40 ? 259 LEU B O     1 
ATOM   4041 C CB    . LEU B 1 259 ? -10.564 89.702  2.706   1.00 28.46 ? 259 LEU B CB    1 
ATOM   4042 C CG    . LEU B 1 259 ? -9.883  88.406  2.269   1.00 29.03 ? 259 LEU B CG    1 
ATOM   4043 C CD1   . LEU B 1 259 ? -8.429  88.555  1.851   1.00 26.14 ? 259 LEU B CD1   1 
ATOM   4044 C CD2   . LEU B 1 259 ? -10.078 87.350  3.350   1.00 30.07 ? 259 LEU B CD2   1 
ATOM   4045 N N     . TRP B 1 260 ? -10.873 92.845  4.020   1.00 28.44 ? 260 TRP B N     1 
ATOM   4046 C CA    . TRP B 1 260 ? -11.818 93.946  4.036   1.00 28.65 ? 260 TRP B CA    1 
ATOM   4047 C C     . TRP B 1 260 ? -11.199 95.319  4.168   1.00 28.89 ? 260 TRP B C     1 
ATOM   4048 O O     . TRP B 1 260 ? -11.001 95.826  5.270   1.00 28.95 ? 260 TRP B O     1 
ATOM   4049 C CB    . TRP B 1 260 ? -12.826 93.720  5.172   1.00 29.52 ? 260 TRP B CB    1 
ATOM   4050 C CG    . TRP B 1 260 ? -13.976 94.689  5.099   1.00 29.80 ? 260 TRP B CG    1 
ATOM   4051 C CD1   . TRP B 1 260 ? -14.191 95.803  5.857   1.00 28.30 ? 260 TRP B CD1   1 
ATOM   4052 C CD2   . TRP B 1 260 ? -15.071 94.605  4.181   1.00 29.96 ? 260 TRP B CD2   1 
ATOM   4053 N NE1   . TRP B 1 260 ? -15.351 96.411  5.463   1.00 28.52 ? 260 TRP B NE1   1 
ATOM   4054 C CE2   . TRP B 1 260 ? -15.914 95.701  4.438   1.00 29.31 ? 260 TRP B CE2   1 
ATOM   4055 C CE3   . TRP B 1 260 ? -15.414 93.701  3.169   1.00 31.07 ? 260 TRP B CE3   1 
ATOM   4056 C CZ2   . TRP B 1 260 ? -17.082 95.916  3.713   1.00 29.57 ? 260 TRP B CZ2   1 
ATOM   4057 C CZ3   . TRP B 1 260 ? -16.572 93.906  2.440   1.00 30.20 ? 260 TRP B CZ3   1 
ATOM   4058 C CH2   . TRP B 1 260 ? -17.385 95.013  2.731   1.00 30.96 ? 260 TRP B CH2   1 
ATOM   4059 N N     . TYR B 1 261 ? -10.908 95.962  3.044   1.00 29.08 ? 261 TYR B N     1 
ATOM   4060 C CA    . TYR B 1 261 ? -10.360 97.316  3.041   1.00 29.41 ? 261 TYR B CA    1 
ATOM   4061 C C     . TYR B 1 261 ? -11.289 98.207  2.265   1.00 29.90 ? 261 TYR B C     1 
ATOM   4062 O O     . TYR B 1 261 ? -11.196 98.324  1.042   1.00 30.26 ? 261 TYR B O     1 
ATOM   4063 C CB    . TYR B 1 261 ? -8.971  97.346  2.383   1.00 28.62 ? 261 TYR B CB    1 
ATOM   4064 C CG    . TYR B 1 261 ? -7.920  97.026  3.424   1.00 27.32 ? 261 TYR B CG    1 
ATOM   4065 C CD1   . TYR B 1 261 ? -7.653  95.711  3.762   1.00 26.51 ? 261 TYR B CD1   1 
ATOM   4066 C CD2   . TYR B 1 261 ? -7.257  98.041  4.096   1.00 27.11 ? 261 TYR B CD2   1 
ATOM   4067 C CE1   . TYR B 1 261 ? -6.731  95.407  4.741   1.00 26.13 ? 261 TYR B CE1   1 
ATOM   4068 C CE2   . TYR B 1 261 ? -6.309  97.745  5.061   1.00 26.68 ? 261 TYR B CE2   1 
ATOM   4069 C CZ    . TYR B 1 261 ? -6.054  96.425  5.374   1.00 26.12 ? 261 TYR B CZ    1 
ATOM   4070 O OH    . TYR B 1 261 ? -5.143  96.093  6.342   1.00 25.32 ? 261 TYR B OH    1 
ATOM   4071 N N     . PHE B 1 262 ? -12.314 98.783  2.871   1.00 30.66 ? 262 PHE B N     1 
ATOM   4072 C CA    . PHE B 1 262 ? -13.322 99.591  2.200   1.00 31.34 ? 262 PHE B CA    1 
ATOM   4073 C C     . PHE B 1 262 ? -14.320 98.672  1.507   1.00 31.93 ? 262 PHE B C     1 
ATOM   4074 O O     . PHE B 1 262 ? -15.486 99.019  1.333   1.00 32.81 ? 262 PHE B O     1 
ATOM   4075 C CB    . PHE B 1 262 ? -12.788 100.623 1.196   1.00 30.14 ? 262 PHE B CB    1 
ATOM   4076 C CG    . PHE B 1 262 ? -12.058 101.718 1.921   1.00 30.02 ? 262 PHE B CG    1 
ATOM   4077 C CD1   . PHE B 1 262 ? -12.736 102.695 2.619   1.00 30.38 ? 262 PHE B CD1   1 
ATOM   4078 C CD2   . PHE B 1 262 ? -10.678 101.729 1.949   1.00 29.98 ? 262 PHE B CD2   1 
ATOM   4079 C CE1   . PHE B 1 262 ? -12.052 103.677 3.313   1.00 31.28 ? 262 PHE B CE1   1 
ATOM   4080 C CE2   . PHE B 1 262 ? -9.988  102.701 2.645   1.00 29.60 ? 262 PHE B CE2   1 
ATOM   4081 C CZ    . PHE B 1 262 ? -10.670 103.683 3.324   1.00 30.13 ? 262 PHE B CZ    1 
ATOM   4082 N N     . GLY B 1 263 ? -13.995 97.412  1.295   1.00 31.91 ? 263 GLY B N     1 
ATOM   4083 C CA    . GLY B 1 263 ? -14.723 96.382  0.630   1.00 31.46 ? 263 GLY B CA    1 
ATOM   4084 C C     . GLY B 1 263 ? -13.831 95.162  0.396   1.00 31.25 ? 263 GLY B C     1 
ATOM   4085 O O     . GLY B 1 263 ? -12.657 95.039  0.743   1.00 31.47 ? 263 GLY B O     1 
ATOM   4086 N N     . LEU B 1 264 ? -14.477 94.107  -0.091  1.00 31.07 ? 264 LEU B N     1 
ATOM   4087 C CA    . LEU B 1 264 ? -13.742 92.866  -0.323  1.00 30.19 ? 264 LEU B CA    1 
ATOM   4088 C C     . LEU B 1 264 ? -12.607 93.181  -1.297  1.00 29.45 ? 264 LEU B C     1 
ATOM   4089 O O     . LEU B 1 264 ? -12.813 93.738  -2.364  1.00 28.90 ? 264 LEU B O     1 
ATOM   4090 C CB    . LEU B 1 264 ? -14.513 91.657  -0.807  1.00 29.95 ? 264 LEU B CB    1 
ATOM   4091 C CG    . LEU B 1 264 ? -15.248 90.787  0.207   1.00 29.97 ? 264 LEU B CG    1 
ATOM   4092 C CD1   . LEU B 1 264 ? -15.695 89.505  -0.478  1.00 31.14 ? 264 LEU B CD1   1 
ATOM   4093 C CD2   . LEU B 1 264 ? -14.360 90.427  1.396   1.00 32.01 ? 264 LEU B CD2   1 
ATOM   4094 N N     . ILE B 1 265 ? -11.418 92.788  -0.863  1.00 29.14 ? 265 ILE B N     1 
ATOM   4095 C CA    . ILE B 1 265 ? -10.215 93.049  -1.650  1.00 28.60 ? 265 ILE B CA    1 
ATOM   4096 C C     . ILE B 1 265 ? -9.312  91.837  -1.670  1.00 28.17 ? 265 ILE B C     1 
ATOM   4097 O O     . ILE B 1 265 ? -9.198  91.095  -0.694  1.00 28.27 ? 265 ILE B O     1 
ATOM   4098 C CB    . ILE B 1 265 ? -9.599  94.373  -1.223  1.00 28.82 ? 265 ILE B CB    1 
ATOM   4099 C CG1   . ILE B 1 265 ? -8.229  94.652  -1.846  1.00 27.99 ? 265 ILE B CG1   1 
ATOM   4100 C CG2   . ILE B 1 265 ? -9.527  94.581  0.279   1.00 29.81 ? 265 ILE B CG2   1 
ATOM   4101 C CD1   . ILE B 1 265 ? -7.946  96.150  -1.766  1.00 27.84 ? 265 ILE B CD1   1 
ATOM   4102 N N     . GLY B 1 266 ? -8.914  91.433  -2.874  1.00 27.79 ? 266 GLY B N     1 
ATOM   4103 C CA    . GLY B 1 266 ? -8.131  90.244  -3.117  1.00 27.69 ? 266 GLY B CA    1 
ATOM   4104 C C     . GLY B 1 266 ? -8.931  88.996  -3.475  1.00 28.01 ? 266 GLY B C     1 
ATOM   4105 O O     . GLY B 1 266 ? -8.337  87.997  -3.899  1.00 27.16 ? 266 GLY B O     1 
ATOM   4106 N N     . THR B 1 267 ? -10.264 89.077  -3.383  1.00 28.05 ? 267 THR B N     1 
ATOM   4107 C CA    . THR B 1 267 ? -11.157 87.976  -3.658  1.00 27.64 ? 267 THR B CA    1 
ATOM   4108 C C     . THR B 1 267 ? -11.717 88.031  -5.071  1.00 27.60 ? 267 THR B C     1 
ATOM   4109 O O     . THR B 1 267 ? -12.621 87.259  -5.399  1.00 27.73 ? 267 THR B O     1 
ATOM   4110 C CB    . THR B 1 267 ? -12.361 88.019  -2.695  1.00 27.67 ? 267 THR B CB    1 
ATOM   4111 O OG1   . THR B 1 267 ? -13.183 89.099  -3.137  1.00 30.23 ? 267 THR B OG1   1 
ATOM   4112 C CG2   . THR B 1 267 ? -11.886 88.253  -1.277  1.00 28.53 ? 267 THR B CG2   1 
ATOM   4113 N N     . CYS B 1 268 ? -11.276 88.993  -5.875  1.00 27.53 ? 268 CYS B N     1 
ATOM   4114 C CA    . CYS B 1 268 ? -11.766 89.127  -7.231  1.00 27.67 ? 268 CYS B CA    1 
ATOM   4115 C C     . CYS B 1 268 ? -11.328 87.968  -8.114  1.00 28.66 ? 268 CYS B C     1 
ATOM   4116 O O     . CYS B 1 268 ? -10.158 87.896  -8.499  1.00 29.03 ? 268 CYS B O     1 
ATOM   4117 C CB    . CYS B 1 268 ? -11.363 90.424  -7.960  1.00 23.44 ? 268 CYS B CB    1 
ATOM   4118 S SG    . CYS B 1 268 ? -12.171 90.591  -9.567  1.00 20.98 ? 268 CYS B SG    1 
ATOM   4119 N N     . LEU B 1 269 ? -12.284 87.167  -8.573  1.00 29.74 ? 269 LEU B N     1 
ATOM   4120 C CA    . LEU B 1 269 ? -11.916 86.115  -9.524  1.00 30.65 ? 269 LEU B CA    1 
ATOM   4121 C C     . LEU B 1 269 ? -11.429 86.774  -10.821 1.00 31.31 ? 269 LEU B C     1 
ATOM   4122 O O     . LEU B 1 269 ? -10.256 86.453  -11.139 1.00 35.08 ? 269 LEU B O     1 
ATOM   4123 C CB    . LEU B 1 269 ? -13.045 85.164  -9.851  1.00 32.52 ? 269 LEU B CB    1 
ATOM   4124 C CG    . LEU B 1 269 ? -13.117 83.772  -9.252  1.00 31.66 ? 269 LEU B CG    1 
ATOM   4125 C CD1   . LEU B 1 269 ? -11.724 83.240  -8.962  1.00 33.89 ? 269 LEU B CD1   1 
ATOM   4126 C CD2   . LEU B 1 269 ? -13.976 83.749  -8.006  1.00 32.46 ? 269 LEU B CD2   1 
ATOM   4127 N N     . GLU C 1 1   ? 28.811  70.958  20.604  1.00 46.52 ? 1   GLU C N     1 
ATOM   4128 C CA    . GLU C 1 1   ? 27.994  69.712  20.559  1.00 45.75 ? 1   GLU C CA    1 
ATOM   4129 C C     . GLU C 1 1   ? 28.062  68.957  19.240  1.00 44.35 ? 1   GLU C C     1 
ATOM   4130 O O     . GLU C 1 1   ? 27.375  67.926  19.122  1.00 44.79 ? 1   GLU C O     1 
ATOM   4131 C CB    . GLU C 1 1   ? 26.539  70.018  20.937  1.00 50.30 ? 1   GLU C CB    1 
ATOM   4132 C CG    . GLU C 1 1   ? 26.178  69.634  22.356  1.00 56.18 ? 1   GLU C CG    1 
ATOM   4133 C CD    . GLU C 1 1   ? 25.235  68.436  22.466  1.00 59.80 ? 1   GLU C CD    1 
ATOM   4134 O OE1   . GLU C 1 1   ? 24.534  68.324  23.521  1.00 62.17 ? 1   GLU C OE1   1 
ATOM   4135 O OE2   . GLU C 1 1   ? 25.212  67.586  21.541  1.00 59.71 ? 1   GLU C OE2   1 
ATOM   4136 N N     . VAL C 1 2   ? 29.014  69.269  18.359  1.00 42.37 ? 2   VAL C N     1 
ATOM   4137 C CA    . VAL C 1 2   ? 29.126  68.507  17.112  1.00 39.67 ? 2   VAL C CA    1 
ATOM   4138 C C     . VAL C 1 2   ? 30.492  68.689  16.482  1.00 38.60 ? 2   VAL C C     1 
ATOM   4139 O O     . VAL C 1 2   ? 31.109  69.751  16.556  1.00 38.59 ? 2   VAL C O     1 
ATOM   4140 C CB    . VAL C 1 2   ? 27.949  68.838  16.188  1.00 38.05 ? 2   VAL C CB    1 
ATOM   4141 C CG1   . VAL C 1 2   ? 28.294  69.536  14.889  1.00 37.56 ? 2   VAL C CG1   1 
ATOM   4142 C CG2   . VAL C 1 2   ? 27.154  67.568  15.899  1.00 37.64 ? 2   VAL C CG2   1 
ATOM   4143 N N     . SER C 1 3   ? 31.018  67.620  15.899  1.00 37.65 ? 3   SER C N     1 
ATOM   4144 C CA    . SER C 1 3   ? 32.314  67.698  15.237  1.00 37.22 ? 3   SER C CA    1 
ATOM   4145 C C     . SER C 1 3   ? 32.250  68.678  14.071  1.00 37.28 ? 3   SER C C     1 
ATOM   4146 O O     . SER C 1 3   ? 31.362  68.546  13.219  1.00 37.09 ? 3   SER C O     1 
ATOM   4147 C CB    . SER C 1 3   ? 32.751  66.315  14.786  1.00 37.36 ? 3   SER C CB    1 
ATOM   4148 O OG    . SER C 1 3   ? 32.243  65.888  13.546  1.00 37.62 ? 3   SER C OG    1 
ATOM   4149 N N     . GLN C 1 4   ? 33.372  69.363  13.816  1.00 37.32 ? 4   GLN C N     1 
ATOM   4150 C CA    . GLN C 1 4   ? 33.468  70.292  12.707  1.00 37.20 ? 4   GLN C CA    1 
ATOM   4151 C C     . GLN C 1 4   ? 33.059  69.609  11.410  1.00 36.45 ? 4   GLN C C     1 
ATOM   4152 O O     . GLN C 1 4   ? 32.317  70.160  10.603  1.00 36.54 ? 4   GLN C O     1 
ATOM   4153 C CB    . GLN C 1 4   ? 34.852  70.899  12.506  1.00 41.69 ? 4   GLN C CB    1 
ATOM   4154 C CG    . GLN C 1 4   ? 34.906  71.975  11.419  1.00 46.02 ? 4   GLN C CG    1 
ATOM   4155 C CD    . GLN C 1 4   ? 34.046  73.179  11.785  1.00 49.13 ? 4   GLN C CD    1 
ATOM   4156 O OE1   . GLN C 1 4   ? 33.122  73.588  11.071  1.00 50.40 ? 4   GLN C OE1   1 
ATOM   4157 N NE2   . GLN C 1 4   ? 34.359  73.759  12.941  1.00 49.45 ? 4   GLN C NE2   1 
ATOM   4158 N N     . ASP C 1 5   ? 33.550  68.403  11.203  1.00 36.13 ? 5   ASP C N     1 
ATOM   4159 C CA    . ASP C 1 5   ? 33.182  67.598  10.040  1.00 35.60 ? 5   ASP C CA    1 
ATOM   4160 C C     . ASP C 1 5   ? 31.686  67.333  9.961   1.00 34.27 ? 5   ASP C C     1 
ATOM   4161 O O     . ASP C 1 5   ? 31.098  67.434  8.882   1.00 33.95 ? 5   ASP C O     1 
ATOM   4162 C CB    . ASP C 1 5   ? 33.913  66.250  10.094  1.00 39.99 ? 5   ASP C CB    1 
ATOM   4163 C CG    . ASP C 1 5   ? 35.419  66.460  10.076  1.00 43.96 ? 5   ASP C CG    1 
ATOM   4164 O OD1   . ASP C 1 5   ? 35.910  66.256  8.942   1.00 46.81 ? 5   ASP C OD1   1 
ATOM   4165 O OD2   . ASP C 1 5   ? 36.036  66.808  11.111  1.00 45.71 ? 5   ASP C OD2   1 
ATOM   4166 N N     . LEU C 1 6   ? 31.062  66.950  11.074  1.00 33.24 ? 6   LEU C N     1 
ATOM   4167 C CA    . LEU C 1 6   ? 29.625  66.690  11.061  1.00 31.94 ? 6   LEU C CA    1 
ATOM   4168 C C     . LEU C 1 6   ? 28.875  67.953  10.633  1.00 31.59 ? 6   LEU C C     1 
ATOM   4169 O O     . LEU C 1 6   ? 28.152  67.983  9.645   1.00 31.50 ? 6   LEU C O     1 
ATOM   4170 C CB    . LEU C 1 6   ? 29.119  66.228  12.426  1.00 28.13 ? 6   LEU C CB    1 
ATOM   4171 C CG    . LEU C 1 6   ? 28.259  64.969  12.415  1.00 26.77 ? 6   LEU C CG    1 
ATOM   4172 C CD1   . LEU C 1 6   ? 27.201  65.025  13.500  1.00 28.08 ? 6   LEU C CD1   1 
ATOM   4173 C CD2   . LEU C 1 6   ? 27.601  64.689  11.078  1.00 26.20 ? 6   LEU C CD2   1 
ATOM   4174 N N     . PHE C 1 7   ? 29.183  69.049  11.313  1.00 30.86 ? 7   PHE C N     1 
ATOM   4175 C CA    . PHE C 1 7   ? 28.680  70.355  10.982  1.00 30.85 ? 7   PHE C CA    1 
ATOM   4176 C C     . PHE C 1 7   ? 28.898  70.698  9.520   1.00 31.38 ? 7   PHE C C     1 
ATOM   4177 O O     . PHE C 1 7   ? 28.031  71.341  8.923   1.00 31.94 ? 7   PHE C O     1 
ATOM   4178 C CB    . PHE C 1 7   ? 29.438  71.394  11.822  1.00 32.60 ? 7   PHE C CB    1 
ATOM   4179 C CG    . PHE C 1 7   ? 28.952  72.790  11.559  1.00 32.45 ? 7   PHE C CG    1 
ATOM   4180 C CD1   . PHE C 1 7   ? 27.891  73.274  12.299  1.00 32.46 ? 7   PHE C CD1   1 
ATOM   4181 C CD2   . PHE C 1 7   ? 29.527  73.593  10.590  1.00 32.52 ? 7   PHE C CD2   1 
ATOM   4182 C CE1   . PHE C 1 7   ? 27.412  74.547  12.059  1.00 33.25 ? 7   PHE C CE1   1 
ATOM   4183 C CE2   . PHE C 1 7   ? 29.046  74.872  10.359  1.00 32.38 ? 7   PHE C CE2   1 
ATOM   4184 C CZ    . PHE C 1 7   ? 27.991  75.356  11.106  1.00 32.84 ? 7   PHE C CZ    1 
ATOM   4185 N N     . ASN C 1 8   ? 30.055  70.428  8.928   1.00 31.63 ? 8   ASN C N     1 
ATOM   4186 C CA    . ASN C 1 8   ? 30.265  70.756  7.521   1.00 31.49 ? 8   ASN C CA    1 
ATOM   4187 C C     . ASN C 1 8   ? 29.326  69.936  6.647   1.00 31.24 ? 8   ASN C C     1 
ATOM   4188 O O     . ASN C 1 8   ? 28.790  70.457  5.669   1.00 31.28 ? 8   ASN C O     1 
ATOM   4189 C CB    . ASN C 1 8   ? 31.716  70.530  7.119   1.00 34.13 ? 8   ASN C CB    1 
ATOM   4190 C CG    . ASN C 1 8   ? 32.666  71.473  7.827   1.00 36.68 ? 8   ASN C CG    1 
ATOM   4191 O OD1   . ASN C 1 8   ? 32.274  72.371  8.580   1.00 38.00 ? 8   ASN C OD1   1 
ATOM   4192 N ND2   . ASN C 1 8   ? 33.951  71.243  7.574   1.00 37.73 ? 8   ASN C ND2   1 
ATOM   4193 N N     . GLN C 1 9   ? 29.182  68.647  6.939   1.00 30.87 ? 9   GLN C N     1 
ATOM   4194 C CA    . GLN C 1 9   ? 28.291  67.807  6.161   1.00 30.64 ? 9   GLN C CA    1 
ATOM   4195 C C     . GLN C 1 9   ? 26.842  68.240  6.336   1.00 30.36 ? 9   GLN C C     1 
ATOM   4196 O O     . GLN C 1 9   ? 26.098  68.320  5.346   1.00 30.30 ? 9   GLN C O     1 
ATOM   4197 C CB    . GLN C 1 9   ? 28.511  66.349  6.535   1.00 33.87 ? 9   GLN C CB    1 
ATOM   4198 C CG    . GLN C 1 9   ? 29.763  65.721  5.951   1.00 37.52 ? 9   GLN C CG    1 
ATOM   4199 C CD    . GLN C 1 9   ? 29.862  64.244  6.262   1.00 40.34 ? 9   GLN C CD    1 
ATOM   4200 O OE1   . GLN C 1 9   ? 30.187  63.437  5.395   1.00 42.00 ? 9   GLN C OE1   1 
ATOM   4201 N NE2   . GLN C 1 9   ? 29.584  63.834  7.496   1.00 43.71 ? 9   GLN C NE2   1 
ATOM   4202 N N     . PHE C 1 10  ? 26.424  68.592  7.555   1.00 29.60 ? 10  PHE C N     1 
ATOM   4203 C CA    . PHE C 1 10  ? 25.065  69.042  7.819   1.00 28.84 ? 10  PHE C CA    1 
ATOM   4204 C C     . PHE C 1 10  ? 24.713  70.237  6.941   1.00 29.20 ? 10  PHE C C     1 
ATOM   4205 O O     . PHE C 1 10  ? 23.634  70.310  6.344   1.00 29.28 ? 10  PHE C O     1 
ATOM   4206 C CB    . PHE C 1 10  ? 24.829  69.417  9.272   1.00 24.90 ? 10  PHE C CB    1 
ATOM   4207 C CG    . PHE C 1 10  ? 24.554  68.282  10.207  1.00 23.98 ? 10  PHE C CG    1 
ATOM   4208 C CD1   . PHE C 1 10  ? 24.526  66.965  9.765   1.00 23.98 ? 10  PHE C CD1   1 
ATOM   4209 C CD2   . PHE C 1 10  ? 24.344  68.520  11.559  1.00 22.92 ? 10  PHE C CD2   1 
ATOM   4210 C CE1   . PHE C 1 10  ? 24.262  65.907  10.607  1.00 21.37 ? 10  PHE C CE1   1 
ATOM   4211 C CE2   . PHE C 1 10  ? 24.103  67.472  12.425  1.00 22.87 ? 10  PHE C CE2   1 
ATOM   4212 C CZ    . PHE C 1 10  ? 24.073  66.174  11.944  1.00 22.13 ? 10  PHE C CZ    1 
ATOM   4213 N N     . ASN C 1 11  ? 25.661  71.158  6.843   1.00 29.10 ? 11  ASN C N     1 
ATOM   4214 C CA    . ASN C 1 11  ? 25.509  72.313  5.977   1.00 28.96 ? 11  ASN C CA    1 
ATOM   4215 C C     . ASN C 1 11  ? 25.524  71.950  4.506   1.00 28.43 ? 11  ASN C C     1 
ATOM   4216 O O     . ASN C 1 11  ? 24.662  72.395  3.752   1.00 28.33 ? 11  ASN C O     1 
ATOM   4217 C CB    . ASN C 1 11  ? 26.644  73.285  6.308   1.00 31.54 ? 11  ASN C CB    1 
ATOM   4218 C CG    . ASN C 1 11  ? 26.254  74.669  5.851   1.00 33.66 ? 11  ASN C CG    1 
ATOM   4219 O OD1   . ASN C 1 11  ? 26.039  75.542  6.690   1.00 37.07 ? 11  ASN C OD1   1 
ATOM   4220 N ND2   . ASN C 1 11  ? 26.118  74.851  4.550   1.00 35.36 ? 11  ASN C ND2   1 
ATOM   4221 N N     . LEU C 1 12  ? 26.483  71.148  4.075   1.00 28.28 ? 12  LEU C N     1 
ATOM   4222 C CA    . LEU C 1 12  ? 26.555  70.771  2.668   1.00 28.30 ? 12  LEU C CA    1 
ATOM   4223 C C     . LEU C 1 12  ? 25.277  70.088  2.210   1.00 28.28 ? 12  LEU C C     1 
ATOM   4224 O O     . LEU C 1 12  ? 24.657  70.518  1.246   1.00 28.35 ? 12  LEU C O     1 
ATOM   4225 C CB    . LEU C 1 12  ? 27.761  69.854  2.449   1.00 27.06 ? 12  LEU C CB    1 
ATOM   4226 C CG    . LEU C 1 12  ? 27.898  69.348  1.006   1.00 24.21 ? 12  LEU C CG    1 
ATOM   4227 C CD1   . LEU C 1 12  ? 28.149  70.533  0.108   1.00 23.23 ? 12  LEU C CD1   1 
ATOM   4228 C CD2   . LEU C 1 12  ? 28.994  68.321  1.013   1.00 23.43 ? 12  LEU C CD2   1 
ATOM   4229 N N     . PHE C 1 13  ? 24.712  69.163  2.977   1.00 28.22 ? 13  PHE C N     1 
ATOM   4230 C CA    . PHE C 1 13  ? 23.463  68.543  2.517   1.00 28.11 ? 13  PHE C CA    1 
ATOM   4231 C C     . PHE C 1 13  ? 22.240  69.418  2.687   1.00 27.76 ? 13  PHE C C     1 
ATOM   4232 O O     . PHE C 1 13  ? 21.180  69.206  2.069   1.00 27.65 ? 13  PHE C O     1 
ATOM   4233 C CB    . PHE C 1 13  ? 23.353  67.123  3.068   1.00 27.91 ? 13  PHE C CB    1 
ATOM   4234 C CG    . PHE C 1 13  ? 24.500  66.258  2.605   1.00 28.95 ? 13  PHE C CG    1 
ATOM   4235 C CD1   . PHE C 1 13  ? 25.407  65.729  3.514   1.00 28.18 ? 13  PHE C CD1   1 
ATOM   4236 C CD2   . PHE C 1 13  ? 24.664  65.981  1.252   1.00 29.09 ? 13  PHE C CD2   1 
ATOM   4237 C CE1   . PHE C 1 13  ? 26.453  64.941  3.078   1.00 27.26 ? 13  PHE C CE1   1 
ATOM   4238 C CE2   . PHE C 1 13  ? 25.711  65.199  0.804   1.00 29.47 ? 13  PHE C CE2   1 
ATOM   4239 C CZ    . PHE C 1 13  ? 26.597  64.688  1.730   1.00 28.81 ? 13  PHE C CZ    1 
ATOM   4240 N N     . ALA C 1 14  ? 22.284  70.436  3.553   1.00 27.37 ? 14  ALA C N     1 
ATOM   4241 C CA    . ALA C 1 14  ? 21.153  71.351  3.702   1.00 26.69 ? 14  ALA C CA    1 
ATOM   4242 C C     . ALA C 1 14  ? 21.003  72.123  2.398   1.00 26.70 ? 14  ALA C C     1 
ATOM   4243 O O     . ALA C 1 14  ? 19.915  72.193  1.828   1.00 26.66 ? 14  ALA C O     1 
ATOM   4244 C CB    . ALA C 1 14  ? 21.271  72.234  4.914   1.00 24.56 ? 14  ALA C CB    1 
ATOM   4245 N N     . GLN C 1 15  ? 22.105  72.553  1.793   1.00 26.90 ? 15  GLN C N     1 
ATOM   4246 C CA    . GLN C 1 15  ? 22.066  73.187  0.473   1.00 26.98 ? 15  GLN C CA    1 
ATOM   4247 C C     . GLN C 1 15  ? 21.689  72.236  -0.653  1.00 27.19 ? 15  GLN C C     1 
ATOM   4248 O O     . GLN C 1 15  ? 20.992  72.638  -1.591  1.00 26.74 ? 15  GLN C O     1 
ATOM   4249 C CB    . GLN C 1 15  ? 23.442  73.794  0.210   1.00 26.16 ? 15  GLN C CB    1 
ATOM   4250 C CG    . GLN C 1 15  ? 23.793  74.823  1.277   1.00 27.67 ? 15  GLN C CG    1 
ATOM   4251 C CD    . GLN C 1 15  ? 25.031  75.629  0.948   1.00 28.61 ? 15  GLN C CD    1 
ATOM   4252 O OE1   . GLN C 1 15  ? 25.710  76.161  1.817   1.00 28.93 ? 15  GLN C OE1   1 
ATOM   4253 N NE2   . GLN C 1 15  ? 25.478  75.719  -0.296  1.00 29.37 ? 15  GLN C NE2   1 
ATOM   4254 N N     . TYR C 1 16  ? 22.118  70.969  -0.641  1.00 27.66 ? 16  TYR C N     1 
ATOM   4255 C CA    . TYR C 1 16  ? 21.695  70.026  -1.677  1.00 27.86 ? 16  TYR C CA    1 
ATOM   4256 C C     . TYR C 1 16  ? 20.176  69.887  -1.660  1.00 27.65 ? 16  TYR C C     1 
ATOM   4257 O O     . TYR C 1 16  ? 19.522  69.828  -2.698  1.00 26.99 ? 16  TYR C O     1 
ATOM   4258 C CB    . TYR C 1 16  ? 22.399  68.690  -1.557  1.00 29.23 ? 16  TYR C CB    1 
ATOM   4259 C CG    . TYR C 1 16  ? 23.679  68.511  -2.348  1.00 31.06 ? 16  TYR C CG    1 
ATOM   4260 C CD1   . TYR C 1 16  ? 23.638  68.294  -3.720  1.00 31.62 ? 16  TYR C CD1   1 
ATOM   4261 C CD2   . TYR C 1 16  ? 24.922  68.535  -1.726  1.00 31.44 ? 16  TYR C CD2   1 
ATOM   4262 C CE1   . TYR C 1 16  ? 24.806  68.111  -4.437  1.00 32.17 ? 16  TYR C CE1   1 
ATOM   4263 C CE2   . TYR C 1 16  ? 26.092  68.364  -2.438  1.00 31.76 ? 16  TYR C CE2   1 
ATOM   4264 C CZ    . TYR C 1 16  ? 26.024  68.151  -3.797  1.00 32.27 ? 16  TYR C CZ    1 
ATOM   4265 O OH    . TYR C 1 16  ? 27.172  67.989  -4.538  1.00 32.82 ? 16  TYR C OH    1 
ATOM   4266 N N     . SER C 1 17  ? 19.578  69.765  -0.478  1.00 27.53 ? 17  SER C N     1 
ATOM   4267 C CA    . SER C 1 17  ? 18.146  69.772  -0.244  1.00 26.80 ? 17  SER C CA    1 
ATOM   4268 C C     . SER C 1 17  ? 17.487  71.046  -0.779  1.00 26.38 ? 17  SER C C     1 
ATOM   4269 O O     . SER C 1 17  ? 16.654  71.014  -1.693  1.00 26.05 ? 17  SER C O     1 
ATOM   4270 C CB    . SER C 1 17  ? 17.813  69.724  1.255   1.00 26.27 ? 17  SER C CB    1 
ATOM   4271 O OG    . SER C 1 17  ? 18.121  68.451  1.781   1.00 27.08 ? 17  SER C OG    1 
ATOM   4272 N N     . ALA C 1 18  ? 17.988  72.200  -0.342  1.00 26.07 ? 18  ALA C N     1 
ATOM   4273 C CA    . ALA C 1 18  ? 17.511  73.496  -0.827  1.00 25.79 ? 18  ALA C CA    1 
ATOM   4274 C C     . ALA C 1 18  ? 17.579  73.637  -2.338  1.00 25.93 ? 18  ALA C C     1 
ATOM   4275 O O     . ALA C 1 18  ? 16.695  74.150  -3.016  1.00 25.29 ? 18  ALA C O     1 
ATOM   4276 C CB    . ALA C 1 18  ? 18.299  74.633  -0.207  1.00 24.44 ? 18  ALA C CB    1 
ATOM   4277 N N     . ALA C 1 19  ? 18.640  73.123  -2.951  1.00 26.77 ? 19  ALA C N     1 
ATOM   4278 C CA    . ALA C 1 19  ? 18.860  73.131  -4.385  1.00 27.01 ? 19  ALA C CA    1 
ATOM   4279 C C     . ALA C 1 19  ? 17.760  72.421  -5.152  1.00 27.33 ? 19  ALA C C     1 
ATOM   4280 O O     . ALA C 1 19  ? 17.547  72.710  -6.325  1.00 27.69 ? 19  ALA C O     1 
ATOM   4281 C CB    . ALA C 1 19  ? 20.187  72.436  -4.689  1.00 26.00 ? 19  ALA C CB    1 
ATOM   4282 N N     . ALA C 1 20  ? 17.056  71.464  -4.551  1.00 27.64 ? 20  ALA C N     1 
ATOM   4283 C CA    . ALA C 1 20  ? 16.066  70.657  -5.246  1.00 27.37 ? 20  ALA C CA    1 
ATOM   4284 C C     . ALA C 1 20  ? 14.798  71.452  -5.516  1.00 27.54 ? 20  ALA C C     1 
ATOM   4285 O O     . ALA C 1 20  ? 14.035  71.096  -6.412  1.00 27.35 ? 20  ALA C O     1 
ATOM   4286 C CB    . ALA C 1 20  ? 15.760  69.379  -4.492  1.00 25.24 ? 20  ALA C CB    1 
ATOM   4287 N N     . TYR C 1 21  ? 14.585  72.519  -4.754  1.00 27.69 ? 21  TYR C N     1 
ATOM   4288 C CA    . TYR C 1 21  ? 13.451  73.401  -4.925  1.00 27.98 ? 21  TYR C CA    1 
ATOM   4289 C C     . TYR C 1 21  ? 13.628  74.329  -6.122  1.00 28.61 ? 21  TYR C C     1 
ATOM   4290 O O     . TYR C 1 21  ? 12.647  74.884  -6.605  1.00 29.64 ? 21  TYR C O     1 
ATOM   4291 C CB    . TYR C 1 21  ? 13.257  74.308  -3.713  1.00 26.86 ? 21  TYR C CB    1 
ATOM   4292 C CG    . TYR C 1 21  ? 12.666  73.632  -2.499  1.00 26.18 ? 21  TYR C CG    1 
ATOM   4293 C CD1   . TYR C 1 21  ? 11.298  73.406  -2.374  1.00 25.99 ? 21  TYR C CD1   1 
ATOM   4294 C CD2   . TYR C 1 21  ? 13.471  73.221  -1.453  1.00 25.46 ? 21  TYR C CD2   1 
ATOM   4295 C CE1   . TYR C 1 21  ? 10.767  72.804  -1.248  1.00 25.07 ? 21  TYR C CE1   1 
ATOM   4296 C CE2   . TYR C 1 21  ? 12.960  72.597  -0.339  1.00 25.05 ? 21  TYR C CE2   1 
ATOM   4297 C CZ    . TYR C 1 21  ? 11.602  72.382  -0.234  1.00 24.70 ? 21  TYR C CZ    1 
ATOM   4298 O OH    . TYR C 1 21  ? 10.995  71.820  0.865   1.00 23.91 ? 21  TYR C OH    1 
ATOM   4299 N N     . CYS C 1 22  ? 14.859  74.604  -6.516  1.00 29.09 ? 22  CYS C N     1 
ATOM   4300 C CA    . CYS C 1 22  ? 15.095  75.499  -7.639  1.00 29.29 ? 22  CYS C CA    1 
ATOM   4301 C C     . CYS C 1 22  ? 14.512  74.903  -8.910  1.00 29.75 ? 22  CYS C C     1 
ATOM   4302 O O     . CYS C 1 22  ? 14.920  73.832  -9.345  1.00 29.60 ? 22  CYS C O     1 
ATOM   4303 C CB    . CYS C 1 22  ? 16.587  75.784  -7.794  1.00 27.40 ? 22  CYS C CB    1 
ATOM   4304 S SG    . CYS C 1 22  ? 17.336  76.653  -6.414  1.00 25.61 ? 22  CYS C SG    1 
ATOM   4305 N N     . GLY C 1 23  ? 13.645  75.665  -9.565  1.00 30.50 ? 23  GLY C N     1 
ATOM   4306 C CA    . GLY C 1 23  ? 12.995  75.222  -10.785 1.00 31.92 ? 23  GLY C CA    1 
ATOM   4307 C C     . GLY C 1 23  ? 13.928  74.636  -11.831 1.00 32.88 ? 23  GLY C C     1 
ATOM   4308 O O     . GLY C 1 23  ? 13.876  73.440  -12.127 1.00 32.86 ? 23  GLY C O     1 
ATOM   4309 N N     . LYS C 1 24  ? 14.963  75.388  -12.195 1.00 33.92 ? 24  LYS C N     1 
ATOM   4310 C CA    . LYS C 1 24  ? 15.955  74.992  -13.174 1.00 35.24 ? 24  LYS C CA    1 
ATOM   4311 C C     . LYS C 1 24  ? 16.684  73.693  -12.876 1.00 35.15 ? 24  LYS C C     1 
ATOM   4312 O O     . LYS C 1 24  ? 17.013  72.930  -13.788 1.00 35.22 ? 24  LYS C O     1 
ATOM   4313 C CB    . LYS C 1 24  ? 16.934  76.136  -13.459 1.00 39.66 ? 24  LYS C CB    1 
ATOM   4314 C CG    . LYS C 1 24  ? 17.358  76.969  -12.257 1.00 44.02 ? 24  LYS C CG    1 
ATOM   4315 C CD    . LYS C 1 24  ? 18.805  77.445  -12.405 1.00 47.06 ? 24  LYS C CD    1 
ATOM   4316 C CE    . LYS C 1 24  ? 19.318  78.038  -11.101 1.00 48.87 ? 24  LYS C CE    1 
ATOM   4317 N NZ    . LYS C 1 24  ? 20.708  78.571  -11.225 1.00 51.30 ? 24  LYS C NZ    1 
ATOM   4318 N N     . ASN C 1 25  ? 16.772  73.282  -11.620 1.00 35.40 ? 25  ASN C N     1 
ATOM   4319 C CA    . ASN C 1 25  ? 17.343  72.017  -11.207 1.00 35.81 ? 25  ASN C CA    1 
ATOM   4320 C C     . ASN C 1 25  ? 16.451  70.796  -11.350 1.00 35.99 ? 25  ASN C C     1 
ATOM   4321 O O     . ASN C 1 25  ? 16.775  69.761  -10.763 1.00 35.75 ? 25  ASN C O     1 
ATOM   4322 C CB    . ASN C 1 25  ? 17.771  72.112  -9.721  1.00 33.45 ? 25  ASN C CB    1 
ATOM   4323 C CG    . ASN C 1 25  ? 18.849  73.166  -9.614  1.00 31.41 ? 25  ASN C CG    1 
ATOM   4324 O OD1   . ASN C 1 25  ? 19.513  73.398  -10.620 1.00 32.95 ? 25  ASN C OD1   1 
ATOM   4325 N ND2   . ASN C 1 25  ? 19.008  73.809  -8.478  1.00 31.65 ? 25  ASN C ND2   1 
ATOM   4326 N N     . ASN C 1 26  ? 15.300  70.896  -11.989 1.00 36.69 ? 26  ASN C N     1 
ATOM   4327 C CA    . ASN C 1 26  ? 14.375  69.777  -12.061 1.00 37.87 ? 26  ASN C CA    1 
ATOM   4328 C C     . ASN C 1 26  ? 14.104  69.305  -13.483 1.00 38.59 ? 26  ASN C C     1 
ATOM   4329 O O     . ASN C 1 26  ? 13.589  68.204  -13.665 1.00 38.87 ? 26  ASN C O     1 
ATOM   4330 C CB    . ASN C 1 26  ? 13.061  70.167  -11.398 1.00 38.03 ? 26  ASN C CB    1 
ATOM   4331 C CG    . ASN C 1 26  ? 13.107  70.552  -9.943  1.00 36.59 ? 26  ASN C CG    1 
ATOM   4332 O OD1   . ASN C 1 26  ? 12.175  71.227  -9.496  1.00 37.05 ? 26  ASN C OD1   1 
ATOM   4333 N ND2   . ASN C 1 26  ? 14.101  70.175  -9.163  1.00 36.09 ? 26  ASN C ND2   1 
ATOM   4334 N N     . ASP C 1 27  ? 14.757  69.929  -14.443 1.00 39.55 ? 27  ASP C N     1 
ATOM   4335 C CA    . ASP C 1 27  ? 14.660  69.540  -15.848 1.00 40.82 ? 27  ASP C CA    1 
ATOM   4336 C C     . ASP C 1 27  ? 16.023  69.759  -16.518 1.00 40.96 ? 27  ASP C C     1 
ATOM   4337 O O     . ASP C 1 27  ? 16.102  70.019  -17.723 1.00 41.32 ? 27  ASP C O     1 
ATOM   4338 C CB    . ASP C 1 27  ? 13.606  70.406  -16.550 1.00 44.78 ? 27  ASP C CB    1 
ATOM   4339 C CG    . ASP C 1 27  ? 13.906  71.890  -16.445 1.00 47.70 ? 27  ASP C CG    1 
ATOM   4340 O OD1   . ASP C 1 27  ? 13.449  72.677  -17.309 1.00 49.82 ? 27  ASP C OD1   1 
ATOM   4341 O OD2   . ASP C 1 27  ? 14.606  72.339  -15.507 1.00 48.54 ? 27  ASP C OD2   1 
ATOM   4342 N N     . ALA C 1 28  ? 17.038  69.948  -15.679 1.00 40.47 ? 28  ALA C N     1 
ATOM   4343 C CA    . ALA C 1 28  ? 18.385  70.211  -16.164 1.00 40.15 ? 28  ALA C CA    1 
ATOM   4344 C C     . ALA C 1 28  ? 18.926  68.981  -16.879 1.00 39.96 ? 28  ALA C C     1 
ATOM   4345 O O     . ALA C 1 28  ? 18.791  67.868  -16.400 1.00 40.23 ? 28  ALA C O     1 
ATOM   4346 C CB    . ALA C 1 28  ? 19.287  70.570  -14.996 1.00 40.88 ? 28  ALA C CB    1 
ATOM   4347 N N     . PRO C 1 29  ? 19.562  69.182  -18.022 1.00 40.11 ? 29  PRO C N     1 
ATOM   4348 C CA    . PRO C 1 29  ? 20.127  68.108  -18.818 1.00 39.94 ? 29  PRO C CA    1 
ATOM   4349 C C     . PRO C 1 29  ? 21.264  67.413  -18.082 1.00 40.12 ? 29  PRO C C     1 
ATOM   4350 O O     . PRO C 1 29  ? 21.975  68.081  -17.318 1.00 40.38 ? 29  PRO C O     1 
ATOM   4351 C CB    . PRO C 1 29  ? 20.640  68.808  -20.066 1.00 40.00 ? 29  PRO C CB    1 
ATOM   4352 C CG    . PRO C 1 29  ? 20.094  70.195  -20.066 1.00 39.91 ? 29  PRO C CG    1 
ATOM   4353 C CD    . PRO C 1 29  ? 19.815  70.526  -18.627 1.00 40.11 ? 29  PRO C CD    1 
ATOM   4354 N N     . ALA C 1 30  ? 21.425  66.107  -18.310 1.00 40.14 ? 30  ALA C N     1 
ATOM   4355 C CA    . ALA C 1 30  ? 22.501  65.378  -17.626 1.00 40.03 ? 30  ALA C CA    1 
ATOM   4356 C C     . ALA C 1 30  ? 23.845  65.988  -18.010 1.00 40.09 ? 30  ALA C C     1 
ATOM   4357 O O     . ALA C 1 30  ? 23.990  66.524  -19.113 1.00 40.43 ? 30  ALA C O     1 
ATOM   4358 C CB    . ALA C 1 30  ? 22.489  63.901  -17.975 1.00 39.59 ? 30  ALA C CB    1 
ATOM   4359 N N     . GLY C 1 31  ? 24.733  66.198  -17.051 1.00 40.05 ? 31  GLY C N     1 
ATOM   4360 C CA    . GLY C 1 31  ? 26.071  66.688  -17.341 1.00 39.78 ? 31  GLY C CA    1 
ATOM   4361 C C     . GLY C 1 31  ? 26.191  68.161  -16.994 1.00 40.43 ? 31  GLY C C     1 
ATOM   4362 O O     . GLY C 1 31  ? 27.319  68.615  -16.754 1.00 40.65 ? 31  GLY C O     1 
ATOM   4363 N N     . THR C 1 32  ? 25.061  68.871  -16.928 1.00 40.48 ? 32  THR C N     1 
ATOM   4364 C CA    . THR C 1 32  ? 25.119  70.304  -16.617 1.00 40.68 ? 32  THR C CA    1 
ATOM   4365 C C     . THR C 1 32  ? 25.419  70.520  -15.146 1.00 40.80 ? 32  THR C C     1 
ATOM   4366 O O     . THR C 1 32  ? 25.511  69.545  -14.394 1.00 40.76 ? 32  THR C O     1 
ATOM   4367 C CB    . THR C 1 32  ? 23.847  71.015  -17.088 1.00 41.99 ? 32  THR C CB    1 
ATOM   4368 O OG1   . THR C 1 32  ? 22.707  70.774  -16.262 1.00 42.38 ? 32  THR C OG1   1 
ATOM   4369 C CG2   . THR C 1 32  ? 23.494  70.515  -18.489 1.00 43.14 ? 32  THR C CG2   1 
ATOM   4370 N N     . ASN C 1 33  ? 25.569  71.757  -14.681 1.00 41.24 ? 33  ASN C N     1 
ATOM   4371 C CA    . ASN C 1 33  ? 25.993  71.977  -13.310 1.00 42.18 ? 33  ASN C CA    1 
ATOM   4372 C C     . ASN C 1 33  ? 24.899  72.413  -12.342 1.00 41.90 ? 33  ASN C C     1 
ATOM   4373 O O     . ASN C 1 33  ? 24.300  73.464  -12.607 1.00 42.27 ? 33  ASN C O     1 
ATOM   4374 C CB    . ASN C 1 33  ? 27.074  73.058  -13.207 1.00 47.04 ? 33  ASN C CB    1 
ATOM   4375 C CG    . ASN C 1 33  ? 28.237  72.867  -14.144 1.00 51.29 ? 33  ASN C CG    1 
ATOM   4376 O OD1   . ASN C 1 33  ? 28.014  72.666  -15.341 1.00 55.09 ? 33  ASN C OD1   1 
ATOM   4377 N ND2   . ASN C 1 33  ? 29.460  72.932  -13.627 1.00 52.89 ? 33  ASN C ND2   1 
ATOM   4378 N N     . ILE C 1 34  ? 24.820  71.739  -11.188 1.00 41.01 ? 34  ILE C N     1 
ATOM   4379 C CA    . ILE C 1 34  ? 23.888  72.201  -10.154 1.00 39.94 ? 34  ILE C CA    1 
ATOM   4380 C C     . ILE C 1 34  ? 24.229  73.673  -9.897  1.00 39.67 ? 34  ILE C C     1 
ATOM   4381 O O     . ILE C 1 34  ? 25.377  74.109  -10.053 1.00 39.62 ? 34  ILE C O     1 
ATOM   4382 C CB    . ILE C 1 34  ? 23.998  71.396  -8.856  1.00 38.65 ? 34  ILE C CB    1 
ATOM   4383 C CG1   . ILE C 1 34  ? 23.355  70.014  -8.929  1.00 39.29 ? 34  ILE C CG1   1 
ATOM   4384 C CG2   . ILE C 1 34  ? 23.335  72.143  -7.700  1.00 37.51 ? 34  ILE C CG2   1 
ATOM   4385 C CD1   . ILE C 1 34  ? 23.725  69.157  -10.103 1.00 40.20 ? 34  ILE C CD1   1 
ATOM   4386 N N     . THR C 1 35  ? 23.219  74.523  -9.784  1.00 39.16 ? 35  THR C N     1 
ATOM   4387 C CA    . THR C 1 35  ? 23.382  75.932  -9.452  1.00 38.79 ? 35  THR C CA    1 
ATOM   4388 C C     . THR C 1 35  ? 22.096  76.416  -8.756  1.00 37.86 ? 35  THR C C     1 
ATOM   4389 O O     . THR C 1 35  ? 21.028  75.842  -8.962  1.00 37.49 ? 35  THR C O     1 
ATOM   4390 C CB    . THR C 1 35  ? 23.496  76.875  -10.663 1.00 41.00 ? 35  THR C CB    1 
ATOM   4391 O OG1   . THR C 1 35  ? 22.386  76.576  -11.530 1.00 44.32 ? 35  THR C OG1   1 
ATOM   4392 C CG2   . THR C 1 35  ? 24.798  76.807  -11.420 1.00 41.17 ? 35  THR C CG2   1 
ATOM   4393 N N     . CYS C 1 36  ? 22.172  77.516  -8.022  1.00 37.06 ? 36  CYS C N     1 
ATOM   4394 C CA    . CYS C 1 36  ? 21.020  78.031  -7.311  1.00 36.28 ? 36  CYS C CA    1 
ATOM   4395 C C     . CYS C 1 36  ? 20.790  79.530  -7.437  1.00 36.42 ? 36  CYS C C     1 
ATOM   4396 O O     . CYS C 1 36  ? 21.556  80.327  -6.880  1.00 36.64 ? 36  CYS C O     1 
ATOM   4397 C CB    . CYS C 1 36  ? 21.123  77.763  -5.801  1.00 33.47 ? 36  CYS C CB    1 
ATOM   4398 S SG    . CYS C 1 36  ? 21.032  76.014  -5.411  1.00 33.37 ? 36  CYS C SG    1 
ATOM   4399 N N     . THR C 1 37  ? 19.586  79.909  -7.866  1.00 36.62 ? 37  THR C N     1 
ATOM   4400 C CA    . THR C 1 37  ? 19.283  81.340  -7.893  1.00 37.19 ? 37  THR C CA    1 
ATOM   4401 C C     . THR C 1 37  ? 19.388  81.885  -6.469  1.00 37.52 ? 37  THR C C     1 
ATOM   4402 O O     . THR C 1 37  ? 19.114  81.215  -5.480  1.00 37.05 ? 37  THR C O     1 
ATOM   4403 C CB    . THR C 1 37  ? 17.960  81.715  -8.545  1.00 37.56 ? 37  THR C CB    1 
ATOM   4404 O OG1   . THR C 1 37  ? 16.847  81.123  -7.874  1.00 39.53 ? 37  THR C OG1   1 
ATOM   4405 C CG2   . THR C 1 37  ? 17.889  81.237  -9.993  1.00 39.13 ? 37  THR C CG2   1 
ATOM   4406 N N     . GLY C 1 38  ? 19.794  83.148  -6.374  1.00 38.52 ? 38  GLY C N     1 
ATOM   4407 C CA    . GLY C 1 38  ? 20.134  83.749  -5.079  1.00 39.54 ? 38  GLY C CA    1 
ATOM   4408 C C     . GLY C 1 38  ? 21.392  83.006  -4.609  1.00 40.52 ? 38  GLY C C     1 
ATOM   4409 O O     . GLY C 1 38  ? 22.184  82.552  -5.443  1.00 40.82 ? 38  GLY C O     1 
ATOM   4410 N N     . ASN C 1 39  ? 21.539  82.855  -3.299  1.00 41.18 ? 39  ASN C N     1 
ATOM   4411 C CA    . ASN C 1 39  ? 22.696  82.096  -2.819  1.00 41.46 ? 39  ASN C CA    1 
ATOM   4412 C C     . ASN C 1 39  ? 22.174  80.867  -2.076  1.00 40.95 ? 39  ASN C C     1 
ATOM   4413 O O     . ASN C 1 39  ? 22.753  80.466  -1.061  1.00 41.37 ? 39  ASN C O     1 
ATOM   4414 C CB    . ASN C 1 39  ? 23.631  82.982  -2.020  1.00 46.07 ? 39  ASN C CB    1 
ATOM   4415 C CG    . ASN C 1 39  ? 25.040  82.929  -2.600  1.00 50.67 ? 39  ASN C CG    1 
ATOM   4416 O OD1   . ASN C 1 39  ? 26.002  83.160  -1.852  1.00 53.16 ? 39  ASN C OD1   1 
ATOM   4417 N ND2   . ASN C 1 39  ? 25.186  82.633  -3.893  1.00 51.55 ? 39  ASN C ND2   1 
ATOM   4418 N N     . ALA C 1 40  ? 21.255  80.165  -2.748  1.00 39.36 ? 40  ALA C N     1 
ATOM   4419 C CA    . ALA C 1 40  ? 20.606  79.017  -2.150  1.00 38.58 ? 40  ALA C CA    1 
ATOM   4420 C C     . ALA C 1 40  ? 21.564  77.864  -1.884  1.00 38.36 ? 40  ALA C C     1 
ATOM   4421 O O     . ALA C 1 40  ? 21.373  77.100  -0.926  1.00 38.49 ? 40  ALA C O     1 
ATOM   4422 C CB    . ALA C 1 40  ? 19.449  78.582  -3.039  1.00 39.00 ? 40  ALA C CB    1 
ATOM   4423 N N     . CYS C 1 41  ? 22.587  77.698  -2.719  1.00 37.66 ? 41  CYS C N     1 
ATOM   4424 C CA    . CYS C 1 41  ? 23.560  76.637  -2.542  1.00 36.85 ? 41  CYS C CA    1 
ATOM   4425 C C     . CYS C 1 41  ? 24.939  77.020  -3.067  1.00 37.15 ? 41  CYS C C     1 
ATOM   4426 O O     . CYS C 1 41  ? 25.560  76.245  -3.806  1.00 37.59 ? 41  CYS C O     1 
ATOM   4427 C CB    . CYS C 1 41  ? 23.053  75.380  -3.257  1.00 34.04 ? 41  CYS C CB    1 
ATOM   4428 S SG    . CYS C 1 41  ? 22.976  75.556  -5.050  1.00 33.41 ? 41  CYS C SG    1 
ATOM   4429 N N     . PRO C 1 42  ? 25.653  77.840  -2.298  1.00 37.33 ? 42  PRO C N     1 
ATOM   4430 C CA    . PRO C 1 42  ? 26.995  78.279  -2.639  1.00 37.37 ? 42  PRO C CA    1 
ATOM   4431 C C     . PRO C 1 42  ? 28.013  77.158  -2.655  1.00 37.63 ? 42  PRO C C     1 
ATOM   4432 O O     . PRO C 1 42  ? 28.684  76.915  -3.669  1.00 37.77 ? 42  PRO C O     1 
ATOM   4433 C CB    . PRO C 1 42  ? 27.340  79.355  -1.620  1.00 37.34 ? 42  PRO C CB    1 
ATOM   4434 C CG    . PRO C 1 42  ? 26.373  79.183  -0.506  1.00 37.73 ? 42  PRO C CG    1 
ATOM   4435 C CD    . PRO C 1 42  ? 25.122  78.609  -1.141  1.00 37.76 ? 42  PRO C CD    1 
ATOM   4436 N N     . GLU C 1 43  ? 28.075  76.367  -1.583  1.00 38.03 ? 43  GLU C N     1 
ATOM   4437 C CA    . GLU C 1 43  ? 28.967  75.218  -1.510  1.00 38.23 ? 43  GLU C CA    1 
ATOM   4438 C C     . GLU C 1 43  ? 28.712  74.209  -2.629  1.00 38.05 ? 43  GLU C C     1 
ATOM   4439 O O     . GLU C 1 43  ? 29.639  73.511  -3.032  1.00 38.24 ? 43  GLU C O     1 
ATOM   4440 C CB    . GLU C 1 43  ? 28.766  74.415  -0.230  1.00 41.45 ? 43  GLU C CB    1 
ATOM   4441 C CG    . GLU C 1 43  ? 29.053  75.109  1.076   1.00 45.95 ? 43  GLU C CG    1 
ATOM   4442 C CD    . GLU C 1 43  ? 30.436  75.739  1.100   1.00 48.55 ? 43  GLU C CD    1 
ATOM   4443 O OE1   . GLU C 1 43  ? 31.363  75.242  0.422   1.00 50.74 ? 43  GLU C OE1   1 
ATOM   4444 O OE2   . GLU C 1 43  ? 30.604  76.778  1.781   1.00 49.30 ? 43  GLU C OE2   1 
ATOM   4445 N N     . VAL C 1 44  ? 27.446  74.009  -3.010  1.00 37.70 ? 44  VAL C N     1 
ATOM   4446 C CA    . VAL C 1 44  ? 27.187  73.030  -4.060  1.00 37.86 ? 44  VAL C CA    1 
ATOM   4447 C C     . VAL C 1 44  ? 27.786  73.504  -5.376  1.00 38.49 ? 44  VAL C C     1 
ATOM   4448 O O     . VAL C 1 44  ? 28.481  72.768  -6.079  1.00 38.42 ? 44  VAL C O     1 
ATOM   4449 C CB    . VAL C 1 44  ? 25.708  72.654  -4.185  1.00 35.66 ? 44  VAL C CB    1 
ATOM   4450 C CG1   . VAL C 1 44  ? 25.512  71.668  -5.324  1.00 33.13 ? 44  VAL C CG1   1 
ATOM   4451 C CG2   . VAL C 1 44  ? 25.248  72.005  -2.879  1.00 35.00 ? 44  VAL C CG2   1 
ATOM   4452 N N     . GLU C 1 45  ? 27.640  74.807  -5.615  1.00 39.16 ? 45  GLU C N     1 
ATOM   4453 C CA    . GLU C 1 45  ? 28.159  75.443  -6.818  1.00 40.16 ? 45  GLU C CA    1 
ATOM   4454 C C     . GLU C 1 45  ? 29.683  75.458  -6.768  1.00 40.68 ? 45  GLU C C     1 
ATOM   4455 O O     . GLU C 1 45  ? 30.368  75.171  -7.751  1.00 41.14 ? 45  GLU C O     1 
ATOM   4456 C CB    . GLU C 1 45  ? 27.643  76.874  -6.928  1.00 42.05 ? 45  GLU C CB    1 
ATOM   4457 C CG    . GLU C 1 45  ? 26.155  76.958  -7.259  1.00 46.59 ? 45  GLU C CG    1 
ATOM   4458 C CD    . GLU C 1 45  ? 25.678  78.398  -7.178  1.00 48.57 ? 45  GLU C CD    1 
ATOM   4459 O OE1   . GLU C 1 45  ? 26.153  79.104  -6.258  1.00 50.65 ? 45  GLU C OE1   1 
ATOM   4460 O OE2   . GLU C 1 45  ? 24.859  78.849  -8.003  1.00 48.50 ? 45  GLU C OE2   1 
ATOM   4461 N N     . LYS C 1 46  ? 30.191  75.676  -5.555  1.00 40.77 ? 46  LYS C N     1 
ATOM   4462 C CA    . LYS C 1 46  ? 31.635  75.639  -5.338  1.00 41.15 ? 46  LYS C CA    1 
ATOM   4463 C C     . LYS C 1 46  ? 32.201  74.258  -5.629  1.00 40.78 ? 46  LYS C C     1 
ATOM   4464 O O     . LYS C 1 46  ? 33.290  74.219  -6.213  1.00 41.70 ? 46  LYS C O     1 
ATOM   4465 C CB    . LYS C 1 46  ? 31.918  76.142  -3.934  1.00 44.76 ? 46  LYS C CB    1 
ATOM   4466 C CG    . LYS C 1 46  ? 33.306  75.895  -3.390  1.00 49.11 ? 46  LYS C CG    1 
ATOM   4467 C CD    . LYS C 1 46  ? 33.293  76.031  -1.866  1.00 52.76 ? 46  LYS C CD    1 
ATOM   4468 C CE    . LYS C 1 46  ? 33.179  77.500  -1.477  1.00 55.00 ? 46  LYS C CE    1 
ATOM   4469 N NZ    . LYS C 1 46  ? 32.400  77.725  -0.221  1.00 57.30 ? 46  LYS C NZ    1 
ATOM   4470 N N     . ALA C 1 47  ? 31.503  73.163  -5.376  1.00 40.05 ? 47  ALA C N     1 
ATOM   4471 C CA    . ALA C 1 47  ? 31.987  71.835  -5.701  1.00 39.59 ? 47  ALA C CA    1 
ATOM   4472 C C     . ALA C 1 47  ? 31.886  71.555  -7.198  1.00 39.66 ? 47  ALA C C     1 
ATOM   4473 O O     . ALA C 1 47  ? 31.414  72.406  -7.953  1.00 39.15 ? 47  ALA C O     1 
ATOM   4474 C CB    . ALA C 1 47  ? 31.172  70.782  -4.965  1.00 40.24 ? 47  ALA C CB    1 
ATOM   4475 N N     . ASP C 1 48  ? 32.454  70.426  -7.616  1.00 40.00 ? 48  ASP C N     1 
ATOM   4476 C CA    . ASP C 1 48  ? 32.339  69.999  -9.020  1.00 40.98 ? 48  ASP C CA    1 
ATOM   4477 C C     . ASP C 1 48  ? 31.095  69.094  -9.022  1.00 40.74 ? 48  ASP C C     1 
ATOM   4478 O O     . ASP C 1 48  ? 31.237  67.882  -8.772  1.00 41.35 ? 48  ASP C O     1 
ATOM   4479 C CB    . ASP C 1 48  ? 33.568  69.243  -9.494  1.00 46.50 ? 48  ASP C CB    1 
ATOM   4480 C CG    . ASP C 1 48  ? 33.480  68.515  -10.822 1.00 50.34 ? 48  ASP C CG    1 
ATOM   4481 O OD1   . ASP C 1 48  ? 34.554  68.335  -11.461 1.00 51.70 ? 48  ASP C OD1   1 
ATOM   4482 O OD2   . ASP C 1 48  ? 32.385  68.084  -11.265 1.00 51.93 ? 48  ASP C OD2   1 
ATOM   4483 N N     . ALA C 1 49  ? 29.920  69.706  -9.166  1.00 39.60 ? 49  ALA C N     1 
ATOM   4484 C CA    . ALA C 1 49  ? 28.695  68.929  -8.981  1.00 38.52 ? 49  ALA C CA    1 
ATOM   4485 C C     . ALA C 1 49  ? 27.782  68.968  -10.187 1.00 38.09 ? 49  ALA C C     1 
ATOM   4486 O O     . ALA C 1 49  ? 27.262  70.036  -10.524 1.00 38.65 ? 49  ALA C O     1 
ATOM   4487 C CB    . ALA C 1 49  ? 28.006  69.481  -7.739  1.00 38.47 ? 49  ALA C CB    1 
ATOM   4488 N N     . THR C 1 50  ? 27.572  67.843  -10.856 1.00 37.47 ? 50  THR C N     1 
ATOM   4489 C CA    . THR C 1 50  ? 26.789  67.802  -12.072 1.00 36.90 ? 50  THR C CA    1 
ATOM   4490 C C     . THR C 1 50  ? 25.623  66.826  -12.010 1.00 37.19 ? 50  THR C C     1 
ATOM   4491 O O     . THR C 1 50  ? 25.537  65.939  -11.156 1.00 37.20 ? 50  THR C O     1 
ATOM   4492 C CB    . THR C 1 50  ? 27.647  67.449  -13.302 1.00 36.76 ? 50  THR C CB    1 
ATOM   4493 O OG1   . THR C 1 50  ? 28.533  66.366  -13.013 1.00 34.78 ? 50  THR C OG1   1 
ATOM   4494 C CG2   . THR C 1 50  ? 28.415  68.695  -13.732 1.00 37.61 ? 50  THR C CG2   1 
ATOM   4495 N N     . PHE C 1 51  ? 24.615  67.155  -12.828 1.00 37.06 ? 51  PHE C N     1 
ATOM   4496 C CA    . PHE C 1 51  ? 23.393  66.366  -12.871 1.00 36.69 ? 51  PHE C CA    1 
ATOM   4497 C C     . PHE C 1 51  ? 23.657  64.995  -13.482 1.00 36.87 ? 51  PHE C C     1 
ATOM   4498 O O     . PHE C 1 51  ? 24.567  64.808  -14.286 1.00 37.12 ? 51  PHE C O     1 
ATOM   4499 C CB    . PHE C 1 51  ? 22.334  67.118  -13.655 1.00 35.76 ? 51  PHE C CB    1 
ATOM   4500 C CG    . PHE C 1 51  ? 21.773  68.309  -12.946 1.00 36.79 ? 51  PHE C CG    1 
ATOM   4501 C CD1   . PHE C 1 51  ? 20.815  68.175  -11.963 1.00 37.54 ? 51  PHE C CD1   1 
ATOM   4502 C CD2   . PHE C 1 51  ? 22.191  69.590  -13.277 1.00 38.49 ? 51  PHE C CD2   1 
ATOM   4503 C CE1   . PHE C 1 51  ? 20.278  69.279  -11.324 1.00 37.81 ? 51  PHE C CE1   1 
ATOM   4504 C CE2   . PHE C 1 51  ? 21.670  70.708  -12.655 1.00 38.00 ? 51  PHE C CE2   1 
ATOM   4505 C CZ    . PHE C 1 51  ? 20.701  70.544  -11.681 1.00 38.62 ? 51  PHE C CZ    1 
ATOM   4506 N N     . LEU C 1 52  ? 23.146  63.966  -12.831 1.00 37.00 ? 52  LEU C N     1 
ATOM   4507 C CA    . LEU C 1 52  ? 23.231  62.617  -13.378 1.00 37.54 ? 52  LEU C CA    1 
ATOM   4508 C C     . LEU C 1 52  ? 21.833  62.322  -13.924 1.00 38.05 ? 52  LEU C C     1 
ATOM   4509 O O     . LEU C 1 52  ? 21.653  61.832  -15.031 1.00 38.72 ? 52  LEU C O     1 
ATOM   4510 C CB    . LEU C 1 52  ? 23.613  61.612  -12.307 1.00 37.86 ? 52  LEU C CB    1 
ATOM   4511 C CG    . LEU C 1 52  ? 24.955  60.893  -12.374 1.00 37.34 ? 52  LEU C CG    1 
ATOM   4512 C CD1   . LEU C 1 52  ? 26.039  61.813  -12.903 1.00 37.14 ? 52  LEU C CD1   1 
ATOM   4513 C CD2   . LEU C 1 52  ? 25.354  60.338  -11.008 1.00 37.24 ? 52  LEU C CD2   1 
ATOM   4514 N N     . TYR C 1 53  ? 20.851  62.730  -13.135 1.00 38.12 ? 53  TYR C N     1 
ATOM   4515 C CA    . TYR C 1 53  ? 19.445  62.527  -13.457 1.00 38.28 ? 53  TYR C CA    1 
ATOM   4516 C C     . TYR C 1 53  ? 18.683  63.678  -12.804 1.00 38.49 ? 53  TYR C C     1 
ATOM   4517 O O     . TYR C 1 53  ? 18.975  64.078  -11.677 1.00 38.75 ? 53  TYR C O     1 
ATOM   4518 C CB    . TYR C 1 53  ? 18.901  61.214  -12.922 1.00 38.68 ? 53  TYR C CB    1 
ATOM   4519 C CG    . TYR C 1 53  ? 17.486  60.847  -13.304 1.00 39.09 ? 53  TYR C CG    1 
ATOM   4520 C CD1   . TYR C 1 53  ? 17.038  61.010  -14.605 1.00 39.42 ? 53  TYR C CD1   1 
ATOM   4521 C CD2   . TYR C 1 53  ? 16.611  60.285  -12.383 1.00 39.14 ? 53  TYR C CD2   1 
ATOM   4522 C CE1   . TYR C 1 53  ? 15.757  60.640  -14.964 1.00 40.07 ? 53  TYR C CE1   1 
ATOM   4523 C CE2   . TYR C 1 53  ? 15.326  59.929  -12.730 1.00 39.46 ? 53  TYR C CE2   1 
ATOM   4524 C CZ    . TYR C 1 53  ? 14.898  60.102  -14.026 1.00 39.95 ? 53  TYR C CZ    1 
ATOM   4525 O OH    . TYR C 1 53  ? 13.620  59.758  -14.424 1.00 39.72 ? 53  TYR C OH    1 
ATOM   4526 N N     . SER C 1 54  ? 17.751  64.226  -13.559 1.00 38.58 ? 54  SER C N     1 
ATOM   4527 C CA    . SER C 1 54  ? 16.964  65.368  -13.089 1.00 38.17 ? 54  SER C CA    1 
ATOM   4528 C C     . SER C 1 54  ? 15.500  65.017  -13.299 1.00 37.88 ? 54  SER C C     1 
ATOM   4529 O O     . SER C 1 54  ? 15.184  64.537  -14.391 1.00 38.36 ? 54  SER C O     1 
ATOM   4530 C CB    . SER C 1 54  ? 17.338  66.578  -13.937 1.00 38.48 ? 54  SER C CB    1 
ATOM   4531 O OG    . SER C 1 54  ? 16.997  67.761  -13.249 1.00 40.70 ? 54  SER C OG    1 
ATOM   4532 N N     . PHE C 1 55  ? 14.687  64.994  -12.257 1.00 37.72 ? 55  PHE C N     1 
ATOM   4533 C CA    . PHE C 1 55  ? 13.316  64.522  -12.435 1.00 37.65 ? 55  PHE C CA    1 
ATOM   4534 C C     . PHE C 1 55  ? 12.302  65.403  -11.740 1.00 37.80 ? 55  PHE C C     1 
ATOM   4535 O O     . PHE C 1 55  ? 12.465  65.873  -10.622 1.00 37.77 ? 55  PHE C O     1 
ATOM   4536 C CB    . PHE C 1 55  ? 13.137  63.069  -11.972 1.00 36.73 ? 55  PHE C CB    1 
ATOM   4537 C CG    . PHE C 1 55  ? 13.486  62.872  -10.523 1.00 35.69 ? 55  PHE C CG    1 
ATOM   4538 C CD1   . PHE C 1 55  ? 14.788  62.589  -10.147 1.00 35.88 ? 55  PHE C CD1   1 
ATOM   4539 C CD2   . PHE C 1 55  ? 12.521  62.982  -9.539  1.00 34.40 ? 55  PHE C CD2   1 
ATOM   4540 C CE1   . PHE C 1 55  ? 15.108  62.415  -8.814  1.00 35.98 ? 55  PHE C CE1   1 
ATOM   4541 C CE2   . PHE C 1 55  ? 12.843  62.809  -8.210  1.00 33.86 ? 55  PHE C CE2   1 
ATOM   4542 C CZ    . PHE C 1 55  ? 14.136  62.530  -7.836  1.00 34.48 ? 55  PHE C CZ    1 
ATOM   4543 N N     . GLU C 1 56  ? 11.192  65.606  -12.438 1.00 38.59 ? 56  GLU C N     1 
ATOM   4544 C CA    . GLU C 1 56  ? 10.121  66.431  -11.868 1.00 39.40 ? 56  GLU C CA    1 
ATOM   4545 C C     . GLU C 1 56  ? 8.777   65.847  -12.288 1.00 39.32 ? 56  GLU C C     1 
ATOM   4546 O O     . GLU C 1 56  ? 8.632   65.194  -13.313 1.00 38.95 ? 56  GLU C O     1 
ATOM   4547 C CB    . GLU C 1 56  ? 10.223  67.885  -12.334 1.00 40.91 ? 56  GLU C CB    1 
ATOM   4548 C CG    . GLU C 1 56  ? 9.910   67.980  -13.821 1.00 43.57 ? 56  GLU C CG    1 
ATOM   4549 C CD    . GLU C 1 56  ? 9.766   69.396  -14.323 1.00 45.46 ? 56  GLU C CD    1 
ATOM   4550 O OE1   . GLU C 1 56  ? 9.342   70.269  -13.538 1.00 45.56 ? 56  GLU C OE1   1 
ATOM   4551 O OE2   . GLU C 1 56  ? 10.079  69.613  -15.520 1.00 47.76 ? 56  GLU C OE2   1 
ATOM   4552 N N     . ASP C 1 57  ? 7.827   65.979  -11.381 1.00 39.99 ? 57  ASP C N     1 
ATOM   4553 C CA    . ASP C 1 57  ? 6.477   65.481  -11.605 1.00 40.24 ? 57  ASP C CA    1 
ATOM   4554 C C     . ASP C 1 57  ? 6.439   64.021  -12.005 1.00 39.59 ? 57  ASP C C     1 
ATOM   4555 O O     . ASP C 1 57  ? 5.868   63.671  -13.032 1.00 39.69 ? 57  ASP C O     1 
ATOM   4556 C CB    . ASP C 1 57  ? 5.820   66.349  -12.679 1.00 44.65 ? 57  ASP C CB    1 
ATOM   4557 C CG    . ASP C 1 57  ? 4.316   66.132  -12.649 1.00 47.80 ? 57  ASP C CG    1 
ATOM   4558 O OD1   . ASP C 1 57  ? 3.816   65.721  -11.580 1.00 50.02 ? 57  ASP C OD1   1 
ATOM   4559 O OD2   . ASP C 1 57  ? 3.690   66.365  -13.704 1.00 50.58 ? 57  ASP C OD2   1 
ATOM   4560 N N     . SER C 1 58  ? 7.074   63.172  -11.207 1.00 39.00 ? 58  SER C N     1 
ATOM   4561 C CA    . SER C 1 58  ? 7.168   61.749  -11.487 1.00 37.66 ? 58  SER C CA    1 
ATOM   4562 C C     . SER C 1 58  ? 6.310   60.982  -10.493 1.00 37.05 ? 58  SER C C     1 
ATOM   4563 O O     . SER C 1 58  ? 6.111   61.479  -9.383  1.00 37.23 ? 58  SER C O     1 
ATOM   4564 C CB    . SER C 1 58  ? 8.622   61.307  -11.279 1.00 37.38 ? 58  SER C CB    1 
ATOM   4565 O OG    . SER C 1 58  ? 9.434   62.314  -11.863 1.00 40.10 ? 58  SER C OG    1 
ATOM   4566 N N     . GLY C 1 59  ? 6.059   59.722  -10.826 1.00 36.30 ? 59  GLY C N     1 
ATOM   4567 C CA    . GLY C 1 59  ? 5.326   58.862  -9.897  1.00 35.14 ? 59  GLY C CA    1 
ATOM   4568 C C     . GLY C 1 59  ? 4.006   59.513  -9.525  1.00 34.31 ? 59  GLY C C     1 
ATOM   4569 O O     . GLY C 1 59  ? 3.392   60.170  -10.351 1.00 34.59 ? 59  GLY C O     1 
ATOM   4570 N N     . VAL C 1 60  ? 3.537   59.247  -8.322  1.00 33.95 ? 60  VAL C N     1 
ATOM   4571 C CA    . VAL C 1 60  ? 2.284   59.809  -7.828  1.00 33.36 ? 60  VAL C CA    1 
ATOM   4572 C C     . VAL C 1 60  ? 2.660   60.737  -6.670  1.00 33.30 ? 60  VAL C C     1 
ATOM   4573 O O     . VAL C 1 60  ? 3.532   60.384  -5.867  1.00 33.29 ? 60  VAL C O     1 
ATOM   4574 C CB    . VAL C 1 60  ? 1.238   58.788  -7.379  1.00 31.65 ? 60  VAL C CB    1 
ATOM   4575 C CG1   . VAL C 1 60  ? 1.363   57.519  -8.216  1.00 32.63 ? 60  VAL C CG1   1 
ATOM   4576 C CG2   . VAL C 1 60  ? 1.268   58.390  -5.921  1.00 30.53 ? 60  VAL C CG2   1 
ATOM   4577 N N     . GLY C 1 61  ? 2.080   61.925  -6.693  1.00 33.08 ? 61  GLY C N     1 
ATOM   4578 C CA    . GLY C 1 61  ? 2.328   62.880  -5.615  1.00 33.20 ? 61  GLY C CA    1 
ATOM   4579 C C     . GLY C 1 61  ? 3.365   63.915  -6.021  1.00 33.09 ? 61  GLY C C     1 
ATOM   4580 O O     . GLY C 1 61  ? 3.834   64.701  -5.198  1.00 33.25 ? 61  GLY C O     1 
ATOM   4581 N N     . ASP C 1 62  ? 3.702   63.897  -7.304  1.00 33.02 ? 62  ASP C N     1 
ATOM   4582 C CA    . ASP C 1 62  ? 4.657   64.844  -7.880  1.00 32.94 ? 62  ASP C CA    1 
ATOM   4583 C C     . ASP C 1 62  ? 6.053   64.693  -7.292  1.00 32.29 ? 62  ASP C C     1 
ATOM   4584 O O     . ASP C 1 62  ? 6.571   65.585  -6.616  1.00 32.29 ? 62  ASP C O     1 
ATOM   4585 C CB    . ASP C 1 62  ? 4.052   66.242  -7.735  1.00 34.03 ? 62  ASP C CB    1 
ATOM   4586 C CG    . ASP C 1 62  ? 4.862   67.341  -8.384  1.00 36.39 ? 62  ASP C CG    1 
ATOM   4587 O OD1   . ASP C 1 62  ? 5.613   67.063  -9.342  1.00 36.09 ? 62  ASP C OD1   1 
ATOM   4588 O OD2   . ASP C 1 62  ? 4.776   68.495  -7.897  1.00 37.67 ? 62  ASP C OD2   1 
ATOM   4589 N N     . VAL C 1 63  ? 6.682   63.539  -7.509  1.00 31.69 ? 63  VAL C N     1 
ATOM   4590 C CA    . VAL C 1 63  ? 8.026   63.297  -6.995  1.00 31.52 ? 63  VAL C CA    1 
ATOM   4591 C C     . VAL C 1 63  ? 9.068   64.035  -7.838  1.00 31.43 ? 63  VAL C C     1 
ATOM   4592 O O     . VAL C 1 63  ? 9.083   63.991  -9.068  1.00 31.16 ? 63  VAL C O     1 
ATOM   4593 C CB    . VAL C 1 63  ? 8.383   61.812  -6.884  1.00 30.88 ? 63  VAL C CB    1 
ATOM   4594 C CG1   . VAL C 1 63  ? 9.794   61.654  -6.326  1.00 30.52 ? 63  VAL C CG1   1 
ATOM   4595 C CG2   . VAL C 1 63  ? 7.380   61.088  -6.001  1.00 30.31 ? 63  VAL C CG2   1 
ATOM   4596 N N     . THR C 1 64  ? 9.793   64.936  -7.177  1.00 31.25 ? 64  THR C N     1 
ATOM   4597 C CA    . THR C 1 64  ? 10.680  65.891  -7.830  1.00 31.30 ? 64  THR C CA    1 
ATOM   4598 C C     . THR C 1 64  ? 11.994  66.082  -7.088  1.00 31.53 ? 64  THR C C     1 
ATOM   4599 O O     . THR C 1 64  ? 12.061  66.113  -5.861  1.00 31.40 ? 64  THR C O     1 
ATOM   4600 C CB    . THR C 1 64  ? 9.924   67.234  -7.884  1.00 31.86 ? 64  THR C CB    1 
ATOM   4601 O OG1   . THR C 1 64  ? 8.714   67.075  -8.643  1.00 33.46 ? 64  THR C OG1   1 
ATOM   4602 C CG2   . THR C 1 64  ? 10.724  68.369  -8.484  1.00 32.15 ? 64  THR C CG2   1 
ATOM   4603 N N     . GLY C 1 65  ? 13.099  66.114  -7.822  1.00 31.95 ? 65  GLY C N     1 
ATOM   4604 C CA    . GLY C 1 65  ? 14.438  66.304  -7.300  1.00 32.51 ? 65  GLY C CA    1 
ATOM   4605 C C     . GLY C 1 65  ? 15.499  65.931  -8.331  1.00 33.02 ? 65  GLY C C     1 
ATOM   4606 O O     . GLY C 1 65  ? 15.191  65.687  -9.495  1.00 33.34 ? 65  GLY C O     1 
ATOM   4607 N N     . PHE C 1 66  ? 16.730  65.666  -7.899  1.00 33.35 ? 66  PHE C N     1 
ATOM   4608 C CA    . PHE C 1 66  ? 17.792  65.296  -8.818  1.00 33.02 ? 66  PHE C CA    1 
ATOM   4609 C C     . PHE C 1 66  ? 18.763  64.294  -8.209  1.00 33.07 ? 66  PHE C C     1 
ATOM   4610 O O     . PHE C 1 66  ? 18.775  64.093  -7.001  1.00 32.67 ? 66  PHE C O     1 
ATOM   4611 C CB    . PHE C 1 66  ? 18.553  66.545  -9.245  1.00 32.37 ? 66  PHE C CB    1 
ATOM   4612 C CG    . PHE C 1 66  ? 19.211  67.330  -8.150  1.00 31.73 ? 66  PHE C CG    1 
ATOM   4613 C CD1   . PHE C 1 66  ? 20.420  66.951  -7.600  1.00 31.72 ? 66  PHE C CD1   1 
ATOM   4614 C CD2   . PHE C 1 66  ? 18.618  68.487  -7.680  1.00 31.71 ? 66  PHE C CD2   1 
ATOM   4615 C CE1   . PHE C 1 66  ? 21.023  67.701  -6.608  1.00 31.94 ? 66  PHE C CE1   1 
ATOM   4616 C CE2   . PHE C 1 66  ? 19.210  69.244  -6.684  1.00 31.78 ? 66  PHE C CE2   1 
ATOM   4617 C CZ    . PHE C 1 66  ? 20.419  68.850  -6.146  1.00 31.89 ? 66  PHE C CZ    1 
ATOM   4618 N N     . LEU C 1 67  ? 19.539  63.691  -9.101  1.00 33.29 ? 67  LEU C N     1 
ATOM   4619 C CA    . LEU C 1 67  ? 20.576  62.735  -8.751  1.00 33.38 ? 67  LEU C CA    1 
ATOM   4620 C C     . LEU C 1 67  ? 21.895  63.372  -9.210  1.00 33.87 ? 67  LEU C C     1 
ATOM   4621 O O     . LEU C 1 67  ? 21.856  64.015  -10.263 1.00 34.08 ? 67  LEU C O     1 
ATOM   4622 C CB    . LEU C 1 67  ? 20.403  61.380  -9.424  1.00 31.38 ? 67  LEU C CB    1 
ATOM   4623 C CG    . LEU C 1 67  ? 21.344  60.289  -8.904  1.00 32.45 ? 67  LEU C CG    1 
ATOM   4624 C CD1   . LEU C 1 67  ? 21.277  60.182  -7.384  1.00 33.01 ? 67  LEU C CD1   1 
ATOM   4625 C CD2   . LEU C 1 67  ? 21.073  58.911  -9.484  1.00 31.38 ? 67  LEU C CD2   1 
ATOM   4626 N N     . ALA C 1 68  ? 22.788  63.639  -8.263  1.00 34.35 ? 68  ALA C N     1 
ATOM   4627 C CA    . ALA C 1 68  ? 24.012  64.370  -8.564  1.00 34.52 ? 68  ALA C CA    1 
ATOM   4628 C C     . ALA C 1 68  ? 25.276  63.553  -8.313  1.00 34.53 ? 68  ALA C C     1 
ATOM   4629 O O     . ALA C 1 68  ? 25.354  62.663  -7.476  1.00 34.35 ? 68  ALA C O     1 
ATOM   4630 C CB    . ALA C 1 68  ? 24.098  65.631  -7.714  1.00 34.88 ? 68  ALA C CB    1 
ATOM   4631 N N     . LEU C 1 69  ? 26.314  63.923  -9.047  1.00 34.70 ? 69  LEU C N     1 
ATOM   4632 C CA    . LEU C 1 69  ? 27.629  63.287  -8.958  1.00 34.50 ? 69  LEU C CA    1 
ATOM   4633 C C     . LEU C 1 69  ? 28.605  64.407  -8.582  1.00 34.46 ? 69  LEU C C     1 
ATOM   4634 O O     . LEU C 1 69  ? 28.464  65.511  -9.124  1.00 34.19 ? 69  LEU C O     1 
ATOM   4635 C CB    . LEU C 1 69  ? 27.944  62.609  -10.270 1.00 35.19 ? 69  LEU C CB    1 
ATOM   4636 C CG    . LEU C 1 69  ? 29.118  61.673  -10.494 1.00 36.23 ? 69  LEU C CG    1 
ATOM   4637 C CD1   . LEU C 1 69  ? 30.332  62.468  -10.967 1.00 36.83 ? 69  LEU C CD1   1 
ATOM   4638 C CD2   . LEU C 1 69  ? 29.505  60.849  -9.280  1.00 34.51 ? 69  LEU C CD2   1 
ATOM   4639 N N     . ASP C 1 70  ? 29.056  64.355  -7.325  1.00 34.50 ? 70  ASP C N     1 
ATOM   4640 C CA    . ASP C 1 70  ? 29.922  65.402  -6.788  1.00 34.30 ? 70  ASP C CA    1 
ATOM   4641 C C     . ASP C 1 70  ? 31.353  64.876  -6.758  1.00 34.69 ? 70  ASP C C     1 
ATOM   4642 O O     . ASP C 1 70  ? 31.792  64.208  -5.820  1.00 34.39 ? 70  ASP C O     1 
ATOM   4643 C CB    . ASP C 1 70  ? 29.443  65.844  -5.414  1.00 32.84 ? 70  ASP C CB    1 
ATOM   4644 C CG    . ASP C 1 70  ? 30.350  66.862  -4.753  1.00 32.82 ? 70  ASP C CG    1 
ATOM   4645 O OD1   . ASP C 1 70  ? 31.495  67.058  -5.205  1.00 32.10 ? 70  ASP C OD1   1 
ATOM   4646 O OD2   . ASP C 1 70  ? 29.918  67.468  -3.748  1.00 32.70 ? 70  ASP C OD2   1 
ATOM   4647 N N     . ASN C 1 71  ? 32.143  65.265  -7.765  1.00 35.29 ? 71  ASN C N     1 
ATOM   4648 C CA    . ASN C 1 71  ? 33.524  64.793  -7.854  1.00 35.11 ? 71  ASN C CA    1 
ATOM   4649 C C     . ASN C 1 71  ? 34.389  65.432  -6.781  1.00 35.13 ? 71  ASN C C     1 
ATOM   4650 O O     . ASN C 1 71  ? 35.286  64.756  -6.276  1.00 35.18 ? 71  ASN C O     1 
ATOM   4651 C CB    . ASN C 1 71  ? 34.152  65.034  -9.225  1.00 34.84 ? 71  ASN C CB    1 
ATOM   4652 C CG    . ASN C 1 71  ? 33.332  64.286  -10.263 1.00 35.65 ? 71  ASN C CG    1 
ATOM   4653 O OD1   . ASN C 1 71  ? 32.828  64.952  -11.169 1.00 37.38 ? 71  ASN C OD1   1 
ATOM   4654 N ND2   . ASN C 1 71  ? 33.218  62.998  -10.003 1.00 33.97 ? 71  ASN C ND2   1 
ATOM   4655 N N     . THR C 1 72  ? 34.151  66.693  -6.425  1.00 34.71 ? 72  THR C N     1 
ATOM   4656 C CA    . THR C 1 72  ? 34.919  67.294  -5.338  1.00 34.36 ? 72  THR C CA    1 
ATOM   4657 C C     . THR C 1 72  ? 34.771  66.488  -4.052  1.00 34.79 ? 72  THR C C     1 
ATOM   4658 O O     . THR C 1 72  ? 35.778  66.258  -3.383  1.00 34.80 ? 72  THR C O     1 
ATOM   4659 C CB    . THR C 1 72  ? 34.468  68.726  -5.038  1.00 33.91 ? 72  THR C CB    1 
ATOM   4660 O OG1   . THR C 1 72  ? 34.686  69.594  -6.151  1.00 36.55 ? 72  THR C OG1   1 
ATOM   4661 C CG2   . THR C 1 72  ? 35.164  69.334  -3.840  1.00 32.90 ? 72  THR C CG2   1 
ATOM   4662 N N     . ASN C 1 73  ? 33.553  66.123  -3.641  1.00 35.12 ? 73  ASN C N     1 
ATOM   4663 C CA    . ASN C 1 73  ? 33.401  65.381  -2.395  1.00 35.39 ? 73  ASN C CA    1 
ATOM   4664 C C     . ASN C 1 73  ? 33.233  63.885  -2.600  1.00 35.51 ? 73  ASN C C     1 
ATOM   4665 O O     . ASN C 1 73  ? 33.049  63.174  -1.606  1.00 35.56 ? 73  ASN C O     1 
ATOM   4666 C CB    . ASN C 1 73  ? 32.256  65.932  -1.553  1.00 35.87 ? 73  ASN C CB    1 
ATOM   4667 C CG    . ASN C 1 73  ? 32.257  67.430  -1.366  1.00 36.06 ? 73  ASN C CG    1 
ATOM   4668 O OD1   . ASN C 1 73  ? 31.589  68.155  -2.106  1.00 34.60 ? 73  ASN C OD1   1 
ATOM   4669 N ND2   . ASN C 1 73  ? 32.991  67.958  -0.385  1.00 36.99 ? 73  ASN C ND2   1 
ATOM   4670 N N     . LYS C 1 74  ? 33.430  63.384  -3.817  1.00 35.70 ? 74  LYS C N     1 
ATOM   4671 C CA    . LYS C 1 74  ? 33.288  61.948  -4.065  1.00 36.21 ? 74  LYS C CA    1 
ATOM   4672 C C     . LYS C 1 74  ? 31.947  61.503  -3.466  1.00 35.49 ? 74  LYS C C     1 
ATOM   4673 O O     . LYS C 1 74  ? 31.847  60.538  -2.715  1.00 35.90 ? 74  LYS C O     1 
ATOM   4674 C CB    . LYS C 1 74  ? 34.415  61.119  -3.467  1.00 40.22 ? 74  LYS C CB    1 
ATOM   4675 C CG    . LYS C 1 74  ? 35.837  61.599  -3.645  1.00 43.33 ? 74  LYS C CG    1 
ATOM   4676 C CD    . LYS C 1 74  ? 36.206  61.765  -5.107  1.00 47.40 ? 74  LYS C CD    1 
ATOM   4677 C CE    . LYS C 1 74  ? 37.360  62.738  -5.316  1.00 50.52 ? 74  LYS C CE    1 
ATOM   4678 N NZ    . LYS C 1 74  ? 37.541  63.020  -6.778  1.00 52.87 ? 74  LYS C NZ    1 
ATOM   4679 N N     . LEU C 1 75  ? 30.893  62.065  -4.044  1.00 34.42 ? 75  LEU C N     1 
ATOM   4680 C CA    . LEU C 1 75  ? 29.537  61.854  -3.594  1.00 32.86 ? 75  LEU C CA    1 
ATOM   4681 C C     . LEU C 1 75  ? 28.538  61.587  -4.703  1.00 32.62 ? 75  LEU C C     1 
ATOM   4682 O O     . LEU C 1 75  ? 28.617  62.206  -5.760  1.00 32.74 ? 75  LEU C O     1 
ATOM   4683 C CB    . LEU C 1 75  ? 29.121  63.179  -2.946  1.00 30.84 ? 75  LEU C CB    1 
ATOM   4684 C CG    . LEU C 1 75  ? 28.890  63.190  -1.444  1.00 30.53 ? 75  LEU C CG    1 
ATOM   4685 C CD1   . LEU C 1 75  ? 29.627  62.089  -0.706  1.00 29.64 ? 75  LEU C CD1   1 
ATOM   4686 C CD2   . LEU C 1 75  ? 29.230  64.561  -0.885  1.00 29.07 ? 75  LEU C CD2   1 
ATOM   4687 N N     . ILE C 1 76  ? 27.648  60.647  -4.436  1.00 32.25 ? 76  ILE C N     1 
ATOM   4688 C CA    . ILE C 1 76  ? 26.472  60.433  -5.290  1.00 31.63 ? 76  ILE C CA    1 
ATOM   4689 C C     . ILE C 1 76  ? 25.296  60.883  -4.418  1.00 31.24 ? 76  ILE C C     1 
ATOM   4690 O O     . ILE C 1 76  ? 25.074  60.295  -3.350  1.00 31.68 ? 76  ILE C O     1 
ATOM   4691 C CB    . ILE C 1 76  ? 26.323  58.968  -5.710  1.00 30.92 ? 76  ILE C CB    1 
ATOM   4692 C CG1   . ILE C 1 76  ? 27.432  58.592  -6.696  1.00 31.41 ? 76  ILE C CG1   1 
ATOM   4693 C CG2   . ILE C 1 76  ? 24.950  58.713  -6.300  1.00 29.46 ? 76  ILE C CG2   1 
ATOM   4694 C CD1   . ILE C 1 76  ? 27.596  57.098  -6.884  1.00 32.97 ? 76  ILE C CD1   1 
ATOM   4695 N N     . VAL C 1 77  ? 24.753  62.053  -4.707  1.00 30.50 ? 77  VAL C N     1 
ATOM   4696 C CA    . VAL C 1 77  ? 23.665  62.600  -3.910  1.00 30.06 ? 77  VAL C CA    1 
ATOM   4697 C C     . VAL C 1 77  ? 22.307  62.525  -4.607  1.00 29.88 ? 77  VAL C C     1 
ATOM   4698 O O     . VAL C 1 77  ? 22.141  63.015  -5.730  1.00 29.76 ? 77  VAL C O     1 
ATOM   4699 C CB    . VAL C 1 77  ? 23.909  64.086  -3.600  1.00 30.65 ? 77  VAL C CB    1 
ATOM   4700 C CG1   . VAL C 1 77  ? 22.895  64.629  -2.603  1.00 30.73 ? 77  VAL C CG1   1 
ATOM   4701 C CG2   . VAL C 1 77  ? 25.322  64.345  -3.110  1.00 31.15 ? 77  VAL C CG2   1 
ATOM   4702 N N     . LEU C 1 78  ? 21.325  61.965  -3.911  1.00 29.34 ? 78  LEU C N     1 
ATOM   4703 C CA    . LEU C 1 78  ? 19.948  61.963  -4.409  1.00 29.01 ? 78  LEU C CA    1 
ATOM   4704 C C     . LEU C 1 78  ? 19.167  62.944  -3.537  1.00 28.95 ? 78  LEU C C     1 
ATOM   4705 O O     . LEU C 1 78  ? 19.023  62.700  -2.336  1.00 29.28 ? 78  LEU C O     1 
ATOM   4706 C CB    . LEU C 1 78  ? 19.318  60.583  -4.318  1.00 28.16 ? 78  LEU C CB    1 
ATOM   4707 C CG    . LEU C 1 78  ? 17.846  60.443  -4.701  1.00 26.66 ? 78  LEU C CG    1 
ATOM   4708 C CD1   . LEU C 1 78  ? 17.673  60.753  -6.176  1.00 26.60 ? 78  LEU C CD1   1 
ATOM   4709 C CD2   . LEU C 1 78  ? 17.348  59.048  -4.358  1.00 25.45 ? 78  LEU C CD2   1 
ATOM   4710 N N     . SER C 1 79  ? 18.791  64.085  -4.089  1.00 28.70 ? 79  SER C N     1 
ATOM   4711 C CA    . SER C 1 79  ? 18.082  65.108  -3.325  1.00 28.01 ? 79  SER C CA    1 
ATOM   4712 C C     . SER C 1 79  ? 16.621  65.251  -3.736  1.00 27.61 ? 79  SER C C     1 
ATOM   4713 O O     . SER C 1 79  ? 16.307  65.565  -4.884  1.00 27.24 ? 79  SER C O     1 
ATOM   4714 C CB    . SER C 1 79  ? 18.826  66.429  -3.538  1.00 27.65 ? 79  SER C CB    1 
ATOM   4715 O OG    . SER C 1 79  ? 18.181  67.468  -2.820  1.00 28.10 ? 79  SER C OG    1 
ATOM   4716 N N     . PHE C 1 80  ? 15.691  65.038  -2.810  1.00 27.27 ? 80  PHE C N     1 
ATOM   4717 C CA    . PHE C 1 80  ? 14.265  65.141  -3.076  1.00 26.82 ? 80  PHE C CA    1 
ATOM   4718 C C     . PHE C 1 80  ? 13.753  66.544  -2.751  1.00 26.56 ? 80  PHE C C     1 
ATOM   4719 O O     . PHE C 1 80  ? 14.174  67.166  -1.784  1.00 25.67 ? 80  PHE C O     1 
ATOM   4720 C CB    . PHE C 1 80  ? 13.413  64.138  -2.293  1.00 27.05 ? 80  PHE C CB    1 
ATOM   4721 C CG    . PHE C 1 80  ? 13.570  62.704  -2.712  1.00 27.85 ? 80  PHE C CG    1 
ATOM   4722 C CD1   . PHE C 1 80  ? 14.358  61.823  -1.986  1.00 26.95 ? 80  PHE C CD1   1 
ATOM   4723 C CD2   . PHE C 1 80  ? 12.925  62.242  -3.855  1.00 27.34 ? 80  PHE C CD2   1 
ATOM   4724 C CE1   . PHE C 1 80  ? 14.491  60.509  -2.383  1.00 26.91 ? 80  PHE C CE1   1 
ATOM   4725 C CE2   . PHE C 1 80  ? 13.068  60.936  -4.265  1.00 26.82 ? 80  PHE C CE2   1 
ATOM   4726 C CZ    . PHE C 1 80  ? 13.853  60.069  -3.522  1.00 27.21 ? 80  PHE C CZ    1 
ATOM   4727 N N     . ARG C 1 81  ? 12.845  67.037  -3.589  1.00 26.66 ? 81  ARG C N     1 
ATOM   4728 C CA    . ARG C 1 81  ? 12.279  68.355  -3.359  1.00 26.89 ? 81  ARG C CA    1 
ATOM   4729 C C     . ARG C 1 81  ? 11.214  68.271  -2.275  1.00 27.25 ? 81  ARG C C     1 
ATOM   4730 O O     . ARG C 1 81  ? 10.569  67.247  -2.095  1.00 27.10 ? 81  ARG C O     1 
ATOM   4731 C CB    . ARG C 1 81  ? 11.719  68.989  -4.630  1.00 27.03 ? 81  ARG C CB    1 
ATOM   4732 C CG    . ARG C 1 81  ? 10.866  70.207  -4.358  1.00 28.93 ? 81  ARG C CG    1 
ATOM   4733 C CD    . ARG C 1 81  ? 10.744  71.194  -5.465  1.00 32.09 ? 81  ARG C CD    1 
ATOM   4734 N NE    . ARG C 1 81  ? 9.665   71.125  -6.409  1.00 34.48 ? 81  ARG C NE    1 
ATOM   4735 C CZ    . ARG C 1 81  ? 8.509   70.525  -6.545  1.00 34.29 ? 81  ARG C CZ    1 
ATOM   4736 N NH1   . ARG C 1 81  ? 7.751   70.770  -7.608  1.00 34.17 ? 81  ARG C NH1   1 
ATOM   4737 N NH2   . ARG C 1 81  ? 8.107   69.619  -5.659  1.00 36.11 ? 81  ARG C NH2   1 
ATOM   4738 N N     . GLY C 1 82  ? 11.140  69.275  -1.410  1.00 27.82 ? 82  GLY C N     1 
ATOM   4739 C CA    . GLY C 1 82  ? 10.048  69.341  -0.448  1.00 28.78 ? 82  GLY C CA    1 
ATOM   4740 C C     . GLY C 1 82  ? 8.744   69.626  -1.214  1.00 29.62 ? 82  GLY C C     1 
ATOM   4741 O O     . GLY C 1 82  ? 8.684   69.613  -2.449  1.00 29.30 ? 82  GLY C O     1 
ATOM   4742 N N     . SER C 1 83  ? 7.691   69.936  -0.449  1.00 30.10 ? 83  SER C N     1 
ATOM   4743 C CA    . SER C 1 83  ? 6.394   70.210  -1.063  1.00 30.74 ? 83  SER C CA    1 
ATOM   4744 C C     . SER C 1 83  ? 6.356   71.609  -1.655  1.00 30.43 ? 83  SER C C     1 
ATOM   4745 O O     . SER C 1 83  ? 6.813   72.580  -1.070  1.00 30.09 ? 83  SER C O     1 
ATOM   4746 C CB    . SER C 1 83  ? 5.195   69.977  -0.132  1.00 31.83 ? 83  SER C CB    1 
ATOM   4747 O OG    . SER C 1 83  ? 5.536   70.271  1.218   1.00 33.89 ? 83  SER C OG    1 
ATOM   4748 N N     . ARG C 1 84  ? 5.869   71.689  -2.886  1.00 30.72 ? 84  ARG C N     1 
ATOM   4749 C CA    . ARG C 1 84  ? 5.731   72.982  -3.542  1.00 31.02 ? 84  ARG C CA    1 
ATOM   4750 C C     . ARG C 1 84  ? 4.440   73.073  -4.351  1.00 31.03 ? 84  ARG C C     1 
ATOM   4751 O O     . ARG C 1 84  ? 3.849   74.148  -4.397  1.00 30.91 ? 84  ARG C O     1 
ATOM   4752 C CB    . ARG C 1 84  ? 6.941   73.309  -4.417  1.00 31.09 ? 84  ARG C CB    1 
ATOM   4753 C CG    . ARG C 1 84  ? 6.596   74.339  -5.472  1.00 32.76 ? 84  ARG C CG    1 
ATOM   4754 C CD    . ARG C 1 84  ? 7.639   75.368  -5.780  1.00 32.96 ? 84  ARG C CD    1 
ATOM   4755 N NE    . ARG C 1 84  ? 8.428   75.819  -4.651  1.00 31.42 ? 84  ARG C NE    1 
ATOM   4756 C CZ    . ARG C 1 84  ? 9.623   76.390  -4.799  1.00 32.30 ? 84  ARG C CZ    1 
ATOM   4757 N NH1   . ARG C 1 84  ? 10.294  76.753  -3.707  1.00 32.81 ? 84  ARG C NH1   1 
ATOM   4758 N NH2   . ARG C 1 84  ? 10.180  76.614  -5.983  1.00 30.81 ? 84  ARG C NH2   1 
ATOM   4759 N N     . SER C 1 85  ? 4.087   71.997  -5.038  1.00 31.12 ? 85  SER C N     1 
ATOM   4760 C CA    . SER C 1 85  ? 2.888   71.968  -5.859  1.00 31.04 ? 85  SER C CA    1 
ATOM   4761 C C     . SER C 1 85  ? 1.692   71.574  -5.011  1.00 31.26 ? 85  SER C C     1 
ATOM   4762 O O     . SER C 1 85  ? 1.835   71.192  -3.858  1.00 31.70 ? 85  SER C O     1 
ATOM   4763 C CB    . SER C 1 85  ? 3.037   70.901  -6.950  1.00 31.28 ? 85  SER C CB    1 
ATOM   4764 O OG    . SER C 1 85  ? 3.174   69.647  -6.320  1.00 30.45 ? 85  SER C OG    1 
ATOM   4765 N N     . ILE C 1 86  ? 0.515   71.560  -5.612  1.00 31.78 ? 86  ILE C N     1 
ATOM   4766 C CA    . ILE C 1 86  ? -0.706  71.143  -4.924  1.00 31.74 ? 86  ILE C CA    1 
ATOM   4767 C C     . ILE C 1 86  ? -0.807  69.640  -4.763  1.00 31.92 ? 86  ILE C C     1 
ATOM   4768 O O     . ILE C 1 86  ? -1.091  69.225  -3.634  1.00 32.34 ? 86  ILE C O     1 
ATOM   4769 C CB    . ILE C 1 86  ? -1.942  71.702  -5.643  1.00 31.43 ? 86  ILE C CB    1 
ATOM   4770 C CG1   . ILE C 1 86  ? -1.885  73.230  -5.527  1.00 32.29 ? 86  ILE C CG1   1 
ATOM   4771 C CG2   . ILE C 1 86  ? -3.222  71.204  -5.004  1.00 33.07 ? 86  ILE C CG2   1 
ATOM   4772 C CD1   . ILE C 1 86  ? -2.965  73.971  -6.260  1.00 31.12 ? 86  ILE C CD1   1 
ATOM   4773 N N     . GLU C 1 87  ? -0.312  68.856  -5.716  1.00 31.95 ? 87  GLU C N     1 
ATOM   4774 C CA    . GLU C 1 87  ? -0.248  67.418  -5.584  1.00 32.34 ? 87  GLU C CA    1 
ATOM   4775 C C     . GLU C 1 87  ? 0.657   67.009  -4.435  1.00 32.39 ? 87  GLU C C     1 
ATOM   4776 O O     . GLU C 1 87  ? 0.190   66.398  -3.461  1.00 32.86 ? 87  GLU C O     1 
ATOM   4777 C CB    . GLU C 1 87  ? 0.268   66.764  -6.860  1.00 36.64 ? 87  GLU C CB    1 
ATOM   4778 C CG    . GLU C 1 87  ? -0.736  66.942  -7.990  1.00 43.58 ? 87  GLU C CG    1 
ATOM   4779 C CD    . GLU C 1 87  ? -0.379  68.160  -8.828  1.00 48.04 ? 87  GLU C CD    1 
ATOM   4780 O OE1   . GLU C 1 87  ? -0.601  69.336  -8.468  1.00 48.43 ? 87  GLU C OE1   1 
ATOM   4781 O OE2   . GLU C 1 87  ? 0.184   67.865  -9.916  1.00 52.54 ? 87  GLU C OE2   1 
ATOM   4782 N N     . ASN C 1 88  ? 1.793   67.712  -4.315  1.00 31.97 ? 88  ASN C N     1 
ATOM   4783 C CA    . ASN C 1 88  ? 2.709   67.444  -3.215  1.00 31.59 ? 88  ASN C CA    1 
ATOM   4784 C C     . ASN C 1 88  ? 1.894   67.491  -1.919  1.00 31.95 ? 88  ASN C C     1 
ATOM   4785 O O     . ASN C 1 88  ? 1.925   66.636  -1.049  1.00 31.80 ? 88  ASN C O     1 
ATOM   4786 C CB    . ASN C 1 88  ? 3.802   68.486  -3.059  1.00 29.07 ? 88  ASN C CB    1 
ATOM   4787 C CG    . ASN C 1 88  ? 4.903   68.373  -4.078  1.00 29.50 ? 88  ASN C CG    1 
ATOM   4788 O OD1   . ASN C 1 88  ? 5.481   69.421  -4.365  1.00 30.51 ? 88  ASN C OD1   1 
ATOM   4789 N ND2   . ASN C 1 88  ? 5.155   67.192  -4.621  1.00 29.15 ? 88  ASN C ND2   1 
ATOM   4790 N N     . TRP C 1 89  ? 1.167   68.593  -1.856  1.00 32.80 ? 89  TRP C N     1 
ATOM   4791 C CA    . TRP C 1 89  ? 0.383   68.895  -0.677  1.00 34.31 ? 89  TRP C CA    1 
ATOM   4792 C C     . TRP C 1 89  ? -0.746  67.942  -0.355  1.00 33.90 ? 89  TRP C C     1 
ATOM   4793 O O     . TRP C 1 89  ? -0.764  67.328  0.727   1.00 33.26 ? 89  TRP C O     1 
ATOM   4794 C CB    . TRP C 1 89  ? 0.014   70.377  -0.837  1.00 42.13 ? 89  TRP C CB    1 
ATOM   4795 C CG    . TRP C 1 89  ? -0.004  70.835  0.588   1.00 49.27 ? 89  TRP C CG    1 
ATOM   4796 C CD1   . TRP C 1 89  ? 1.048   71.010  1.443   1.00 52.00 ? 89  TRP C CD1   1 
ATOM   4797 C CD2   . TRP C 1 89  ? -1.196  71.097  1.333   1.00 52.69 ? 89  TRP C CD2   1 
ATOM   4798 N NE1   . TRP C 1 89  ? 0.606   71.405  2.700   1.00 53.63 ? 89  TRP C NE1   1 
ATOM   4799 C CE2   . TRP C 1 89  ? -0.771  71.464  2.644   1.00 54.61 ? 89  TRP C CE2   1 
ATOM   4800 C CE3   . TRP C 1 89  ? -2.557  71.096  1.019   1.00 53.02 ? 89  TRP C CE3   1 
ATOM   4801 C CZ2   . TRP C 1 89  ? -1.674  71.812  3.646   1.00 55.53 ? 89  TRP C CZ2   1 
ATOM   4802 C CZ3   . TRP C 1 89  ? -3.436  71.441  2.027   1.00 55.16 ? 89  TRP C CZ3   1 
ATOM   4803 C CH2   . TRP C 1 89  ? -3.003  71.793  3.317   1.00 56.35 ? 89  TRP C CH2   1 
ATOM   4804 N N     . ILE C 1 90  ? -1.502  67.591  -1.397  1.00 33.44 ? 90  ILE C N     1 
ATOM   4805 C CA    . ILE C 1 90  ? -2.530  66.560  -1.300  1.00 33.22 ? 90  ILE C CA    1 
ATOM   4806 C C     . ILE C 1 90  ? -1.871  65.295  -0.765  1.00 33.22 ? 90  ILE C C     1 
ATOM   4807 O O     . ILE C 1 90  ? -2.158  64.899  0.364   1.00 33.66 ? 90  ILE C O     1 
ATOM   4808 C CB    . ILE C 1 90  ? -3.154  66.274  -2.673  1.00 33.42 ? 90  ILE C CB    1 
ATOM   4809 C CG1   . ILE C 1 90  ? -3.930  67.475  -3.212  1.00 34.43 ? 90  ILE C CG1   1 
ATOM   4810 C CG2   . ILE C 1 90  ? -4.033  65.033  -2.619  1.00 33.82 ? 90  ILE C CG2   1 
ATOM   4811 C CD1   . ILE C 1 90  ? -5.031  68.042  -2.346  1.00 33.78 ? 90  ILE C CD1   1 
ATOM   4812 N N     . GLY C 1 91  ? -0.869  64.742  -1.441  1.00 32.63 ? 91  GLY C N     1 
ATOM   4813 C CA    . GLY C 1 91  ? -0.116  63.604  -0.966  1.00 31.86 ? 91  GLY C CA    1 
ATOM   4814 C C     . GLY C 1 91  ? 0.278   63.626  0.497   1.00 31.58 ? 91  GLY C C     1 
ATOM   4815 O O     . GLY C 1 91  ? -0.252  62.815  1.264   1.00 31.55 ? 91  GLY C O     1 
ATOM   4816 N N     . ASN C 1 92  ? 0.682   64.752  1.082   1.00 31.50 ? 92  ASN C N     1 
ATOM   4817 C CA    . ASN C 1 92  ? 0.989   64.864  2.495   1.00 31.20 ? 92  ASN C CA    1 
ATOM   4818 C C     . ASN C 1 92  ? -0.251  64.544  3.322   1.00 30.87 ? 92  ASN C C     1 
ATOM   4819 O O     . ASN C 1 92  ? -0.176  63.973  4.408   1.00 30.85 ? 92  ASN C O     1 
ATOM   4820 C CB    . ASN C 1 92  ? 1.542   66.223  2.900   1.00 32.89 ? 92  ASN C CB    1 
ATOM   4821 C CG    . ASN C 1 92  ? 2.848   66.648  2.291   1.00 35.15 ? 92  ASN C CG    1 
ATOM   4822 O OD1   . ASN C 1 92  ? 3.087   67.857  2.169   1.00 36.17 ? 92  ASN C OD1   1 
ATOM   4823 N ND2   . ASN C 1 92  ? 3.725   65.740  1.853   1.00 36.31 ? 92  ASN C ND2   1 
ATOM   4824 N N     . LEU C 1 93  ? -1.429  64.868  2.805   1.00 30.77 ? 93  LEU C N     1 
ATOM   4825 C CA    . LEU C 1 93  ? -2.707  64.647  3.439   1.00 29.98 ? 93  LEU C CA    1 
ATOM   4826 C C     . LEU C 1 93  ? -3.252  63.242  3.487   1.00 29.66 ? 93  LEU C C     1 
ATOM   4827 O O     . LEU C 1 93  ? -4.166  63.020  4.296   1.00 29.72 ? 93  LEU C O     1 
ATOM   4828 C CB    . LEU C 1 93  ? -3.778  65.588  2.866   1.00 27.96 ? 93  LEU C CB    1 
ATOM   4829 C CG    . LEU C 1 93  ? -3.421  67.054  3.159   1.00 27.33 ? 93  LEU C CG    1 
ATOM   4830 C CD1   . LEU C 1 93  ? -4.346  67.975  2.395   1.00 28.51 ? 93  LEU C CD1   1 
ATOM   4831 C CD2   . LEU C 1 93  ? -3.505  67.338  4.645   1.00 27.67 ? 93  LEU C CD2   1 
ATOM   4832 N N     . ASN C 1 94  ? -2.666  62.277  2.810   1.00 29.41 ? 94  ASN C N     1 
ATOM   4833 C CA    . ASN C 1 94  ? -3.003  60.871  3.042   1.00 29.72 ? 94  ASN C CA    1 
ATOM   4834 C C     . ASN C 1 94  ? -2.224  60.422  4.273   1.00 29.72 ? 94  ASN C C     1 
ATOM   4835 O O     . ASN C 1 94  ? -1.227  59.713  4.136   1.00 29.90 ? 94  ASN C O     1 
ATOM   4836 C CB    . ASN C 1 94  ? -2.483  60.113  1.823   1.00 33.18 ? 94  ASN C CB    1 
ATOM   4837 C CG    . ASN C 1 94  ? -3.436  60.232  0.656   1.00 37.06 ? 94  ASN C CG    1 
ATOM   4838 O OD1   . ASN C 1 94  ? -4.289  59.328  0.604   1.00 40.27 ? 94  ASN C OD1   1 
ATOM   4839 N ND2   . ASN C 1 94  ? -3.355  61.204  -0.247  1.00 37.75 ? 94  ASN C ND2   1 
ATOM   4840 N N     . PHE C 1 95  ? -2.631  60.777  5.483   1.00 29.58 ? 95  PHE C N     1 
ATOM   4841 C CA    . PHE C 1 95  ? -1.850  60.452  6.658   1.00 29.74 ? 95  PHE C CA    1 
ATOM   4842 C C     . PHE C 1 95  ? -2.242  59.153  7.322   1.00 30.02 ? 95  PHE C C     1 
ATOM   4843 O O     . PHE C 1 95  ? -1.742  58.859  8.414   1.00 29.97 ? 95  PHE C O     1 
ATOM   4844 C CB    . PHE C 1 95  ? -1.855  61.615  7.652   1.00 29.09 ? 95  PHE C CB    1 
ATOM   4845 C CG    . PHE C 1 95  ? -3.234  62.074  8.011   1.00 27.74 ? 95  PHE C CG    1 
ATOM   4846 C CD1   . PHE C 1 95  ? -3.872  63.007  7.228   1.00 27.71 ? 95  PHE C CD1   1 
ATOM   4847 C CD2   . PHE C 1 95  ? -3.880  61.572  9.131   1.00 27.87 ? 95  PHE C CD2   1 
ATOM   4848 C CE1   . PHE C 1 95  ? -5.149  63.433  7.558   1.00 29.56 ? 95  PHE C CE1   1 
ATOM   4849 C CE2   . PHE C 1 95  ? -5.148  61.997  9.467   1.00 27.39 ? 95  PHE C CE2   1 
ATOM   4850 C CZ    . PHE C 1 95  ? -5.788  62.931  8.680   1.00 27.97 ? 95  PHE C CZ    1 
ATOM   4851 N N     . ASP C 1 96  ? -3.040  58.352  6.627   1.00 30.38 ? 96  ASP C N     1 
ATOM   4852 C CA    . ASP C 1 96  ? -3.393  57.041  7.180   1.00 31.00 ? 96  ASP C CA    1 
ATOM   4853 C C     . ASP C 1 96  ? -2.150  56.163  7.112   1.00 31.46 ? 96  ASP C C     1 
ATOM   4854 O O     . ASP C 1 96  ? -1.293  56.393  6.261   1.00 31.51 ? 96  ASP C O     1 
ATOM   4855 C CB    . ASP C 1 96  ? -4.569  56.447  6.431   1.00 31.27 ? 96  ASP C CB    1 
ATOM   4856 C CG    . ASP C 1 96  ? -4.178  56.132  5.005   1.00 33.42 ? 96  ASP C CG    1 
ATOM   4857 O OD1   . ASP C 1 96  ? -3.994  57.092  4.231   1.00 35.52 ? 96  ASP C OD1   1 
ATOM   4858 O OD2   . ASP C 1 96  ? -4.004  54.937  4.694   1.00 35.30 ? 96  ASP C OD2   1 
ATOM   4859 N N     . LEU C 1 97  ? -2.012  55.236  8.047   1.00 32.28 ? 97  LEU C N     1 
ATOM   4860 C CA    . LEU C 1 97  ? -0.845  54.378  8.128   1.00 33.08 ? 97  LEU C CA    1 
ATOM   4861 C C     . LEU C 1 97  ? -0.985  53.151  7.246   1.00 34.14 ? 97  LEU C C     1 
ATOM   4862 O O     . LEU C 1 97  ? -1.876  52.347  7.492   1.00 34.29 ? 97  LEU C O     1 
ATOM   4863 C CB    . LEU C 1 97  ? -0.550  53.931  9.567   1.00 31.03 ? 97  LEU C CB    1 
ATOM   4864 C CG    . LEU C 1 97  ? 0.098   55.065  10.385  1.00 31.16 ? 97  LEU C CG    1 
ATOM   4865 C CD1   . LEU C 1 97  ? -0.014  54.817  11.875  1.00 28.74 ? 97  LEU C CD1   1 
ATOM   4866 C CD2   . LEU C 1 97  ? 1.530   55.268  9.908   1.00 29.83 ? 97  LEU C CD2   1 
ATOM   4867 N N     . LYS C 1 98  ? -0.252  53.160  6.139   1.00 35.26 ? 98  LYS C N     1 
ATOM   4868 C CA    . LYS C 1 98  ? -0.239  52.004  5.252   1.00 37.04 ? 98  LYS C CA    1 
ATOM   4869 C C     . LYS C 1 98  ? 0.766   50.999  5.785   1.00 38.35 ? 98  LYS C C     1 
ATOM   4870 O O     . LYS C 1 98  ? 1.611   51.339  6.611   1.00 39.07 ? 98  LYS C O     1 
ATOM   4871 C CB    . LYS C 1 98  ? 0.083   52.425  3.829   1.00 39.19 ? 98  LYS C CB    1 
ATOM   4872 C CG    . LYS C 1 98  ? -0.280  51.388  2.793   1.00 43.43 ? 98  LYS C CG    1 
ATOM   4873 C CD    . LYS C 1 98  ? -0.193  51.854  1.353   1.00 46.05 ? 98  LYS C CD    1 
ATOM   4874 C CE    . LYS C 1 98  ? 1.240   52.156  0.938   1.00 49.26 ? 98  LYS C CE    1 
ATOM   4875 N NZ    . LYS C 1 98  ? 1.794   51.299  -0.158  1.00 52.27 ? 98  LYS C NZ    1 
ATOM   4876 N N     . GLU C 1 99  ? 0.746   49.772  5.299   1.00 39.52 ? 99  GLU C N     1 
ATOM   4877 C CA    . GLU C 1 99  ? 1.545   48.678  5.848   1.00 40.85 ? 99  GLU C CA    1 
ATOM   4878 C C     . GLU C 1 99  ? 2.747   48.339  4.980   1.00 41.19 ? 99  GLU C C     1 
ATOM   4879 O O     . GLU C 1 99  ? 2.578   47.989  3.805   1.00 41.75 ? 99  GLU C O     1 
ATOM   4880 C CB    . GLU C 1 99  ? 0.639   47.457  6.010   1.00 45.18 ? 99  GLU C CB    1 
ATOM   4881 C CG    . GLU C 1 99  ? -0.757  47.732  6.527   1.00 51.72 ? 99  GLU C CG    1 
ATOM   4882 C CD    . GLU C 1 99  ? -1.782  48.366  5.602   1.00 55.42 ? 99  GLU C CD    1 
ATOM   4883 O OE1   . GLU C 1 99  ? -2.798  48.901  6.136   1.00 57.28 ? 99  GLU C OE1   1 
ATOM   4884 O OE2   . GLU C 1 99  ? -1.675  48.393  4.347   1.00 55.37 ? 99  GLU C OE2   1 
ATOM   4885 N N     . ILE C 1 100 ? 3.956   48.525  5.516   1.00 40.90 ? 100 ILE C N     1 
ATOM   4886 C CA    . ILE C 1 100 ? 5.175   48.303  4.754   1.00 40.40 ? 100 ILE C CA    1 
ATOM   4887 C C     . ILE C 1 100 ? 6.051   47.196  5.319   1.00 40.49 ? 100 ILE C C     1 
ATOM   4888 O O     . ILE C 1 100 ? 7.274   47.310  5.457   1.00 40.39 ? 100 ILE C O     1 
ATOM   4889 C CB    . ILE C 1 100 ? 5.983   49.607  4.592   1.00 39.81 ? 100 ILE C CB    1 
ATOM   4890 C CG1   . ILE C 1 100 ? 6.158   50.328  5.928   1.00 37.65 ? 100 ILE C CG1   1 
ATOM   4891 C CG2   . ILE C 1 100 ? 5.292   50.471  3.547   1.00 39.50 ? 100 ILE C CG2   1 
ATOM   4892 C CD1   . ILE C 1 100 ? 7.323   51.287  5.965   1.00 35.69 ? 100 ILE C CD1   1 
ATOM   4893 N N     . ASN C 1 101 ? 5.478   45.993  5.353   1.00 40.77 ? 101 ASN C N     1 
ATOM   4894 C CA    . ASN C 1 101 ? 6.144   44.759  5.747   1.00 40.78 ? 101 ASN C CA    1 
ATOM   4895 C C     . ASN C 1 101 ? 7.337   44.422  4.872   1.00 40.82 ? 101 ASN C C     1 
ATOM   4896 O O     . ASN C 1 101 ? 8.414   44.110  5.392   1.00 41.38 ? 101 ASN C O     1 
ATOM   4897 C CB    . ASN C 1 101 ? 5.169   43.587  5.699   1.00 41.94 ? 101 ASN C CB    1 
ATOM   4898 C CG    . ASN C 1 101 ? 4.256   43.629  6.908   1.00 43.94 ? 101 ASN C CG    1 
ATOM   4899 O OD1   . ASN C 1 101 ? 4.645   44.171  7.950   1.00 46.56 ? 101 ASN C OD1   1 
ATOM   4900 N ND2   . ASN C 1 101 ? 3.072   43.061  6.749   1.00 43.27 ? 101 ASN C ND2   1 
ATOM   4901 N N     . ASP C 1 102 ? 7.214   44.547  3.554   1.00 40.30 ? 102 ASP C N     1 
ATOM   4902 C CA    . ASP C 1 102 ? 8.395   44.413  2.702   1.00 40.60 ? 102 ASP C CA    1 
ATOM   4903 C C     . ASP C 1 102 ? 9.570   45.160  3.339   1.00 40.23 ? 102 ASP C C     1 
ATOM   4904 O O     . ASP C 1 102 ? 10.605  44.533  3.594   1.00 40.83 ? 102 ASP C O     1 
ATOM   4905 C CB    . ASP C 1 102 ? 8.142   44.896  1.278   1.00 43.39 ? 102 ASP C CB    1 
ATOM   4906 C CG    . ASP C 1 102 ? 7.413   46.220  1.234   1.00 47.20 ? 102 ASP C CG    1 
ATOM   4907 O OD1   . ASP C 1 102 ? 7.333   46.847  0.145   1.00 49.23 ? 102 ASP C OD1   1 
ATOM   4908 O OD2   . ASP C 1 102 ? 6.872   46.654  2.283   1.00 48.61 ? 102 ASP C OD2   1 
ATOM   4909 N N     . ILE C 1 103 ? 9.460   46.437  3.683   1.00 39.55 ? 103 ILE C N     1 
ATOM   4910 C CA    . ILE C 1 103 ? 10.509  47.159  4.375   1.00 38.79 ? 103 ILE C CA    1 
ATOM   4911 C C     . ILE C 1 103 ? 10.858  46.550  5.731   1.00 38.71 ? 103 ILE C C     1 
ATOM   4912 O O     . ILE C 1 103 ? 12.043  46.431  6.071   1.00 38.76 ? 103 ILE C O     1 
ATOM   4913 C CB    . ILE C 1 103 ? 10.138  48.637  4.576   1.00 37.98 ? 103 ILE C CB    1 
ATOM   4914 C CG1   . ILE C 1 103 ? 9.466   49.252  3.358   1.00 37.04 ? 103 ILE C CG1   1 
ATOM   4915 C CG2   . ILE C 1 103 ? 11.388  49.404  4.995   1.00 38.11 ? 103 ILE C CG2   1 
ATOM   4916 C CD1   . ILE C 1 103 ? 10.334  49.764  2.239   1.00 35.95 ? 103 ILE C CD1   1 
ATOM   4917 N N     . CYS C 1 104 ? 9.893   46.283  6.598   1.00 38.56 ? 104 CYS C N     1 
ATOM   4918 C CA    . CYS C 1 104 ? 10.160  45.643  7.881   1.00 39.19 ? 104 CYS C CA    1 
ATOM   4919 C C     . CYS C 1 104 ? 8.873   45.100  8.505   1.00 39.93 ? 104 CYS C C     1 
ATOM   4920 O O     . CYS C 1 104 ? 7.779   45.581  8.195   1.00 40.14 ? 104 CYS C O     1 
ATOM   4921 C CB    . CYS C 1 104 ? 10.933  46.480  8.888   1.00 37.05 ? 104 CYS C CB    1 
ATOM   4922 S SG    . CYS C 1 104 ? 10.562  48.248  8.907   1.00 37.09 ? 104 CYS C SG    1 
ATOM   4923 N N     . SER C 1 105 ? 8.995   44.002  9.249   1.00 40.46 ? 105 SER C N     1 
ATOM   4924 C CA    . SER C 1 105 ? 7.841   43.337  9.831   1.00 41.01 ? 105 SER C CA    1 
ATOM   4925 C C     . SER C 1 105 ? 7.169   44.189  10.899  1.00 40.74 ? 105 SER C C     1 
ATOM   4926 O O     . SER C 1 105 ? 7.819   44.692  11.817  1.00 40.98 ? 105 SER C O     1 
ATOM   4927 C CB    . SER C 1 105 ? 8.172   41.983  10.472  1.00 43.92 ? 105 SER C CB    1 
ATOM   4928 O OG    . SER C 1 105 ? 8.420   40.981  9.495   1.00 48.63 ? 105 SER C OG    1 
ATOM   4929 N N     . GLY C 1 106 ? 5.876   44.434  10.673  1.00 40.25 ? 106 GLY C N     1 
ATOM   4930 C CA    . GLY C 1 106 ? 5.071   45.201  11.610  1.00 40.05 ? 106 GLY C CA    1 
ATOM   4931 C C     . GLY C 1 106 ? 5.174   46.703  11.404  1.00 39.87 ? 106 GLY C C     1 
ATOM   4932 O O     . GLY C 1 106 ? 4.575   47.490  12.139  1.00 40.22 ? 106 GLY C O     1 
ATOM   4933 N N     . CYS C 1 107 ? 6.054   47.100  10.503  1.00 39.16 ? 107 CYS C N     1 
ATOM   4934 C CA    . CYS C 1 107 ? 6.315   48.470  10.147  1.00 38.15 ? 107 CYS C CA    1 
ATOM   4935 C C     . CYS C 1 107 ? 5.161   49.015  9.319   1.00 37.82 ? 107 CYS C C     1 
ATOM   4936 O O     . CYS C 1 107 ? 4.667   48.394  8.379   1.00 37.90 ? 107 CYS C O     1 
ATOM   4937 C CB    . CYS C 1 107 ? 7.609   48.490  9.324   1.00 37.15 ? 107 CYS C CB    1 
ATOM   4938 S SG    . CYS C 1 107 ? 9.123   48.465  10.317  1.00 36.13 ? 107 CYS C SG    1 
ATOM   4939 N N     . ARG C 1 108 ? 4.627   50.153  9.742   1.00 37.50 ? 108 ARG C N     1 
ATOM   4940 C CA    . ARG C 1 108 ? 3.568   50.814  8.983   1.00 37.21 ? 108 ARG C CA    1 
ATOM   4941 C C     . ARG C 1 108 ? 3.923   52.281  8.766   1.00 35.79 ? 108 ARG C C     1 
ATOM   4942 O O     . ARG C 1 108 ? 4.371   52.986  9.649   1.00 35.01 ? 108 ARG C O     1 
ATOM   4943 C CB    . ARG C 1 108 ? 2.198   50.629  9.620   1.00 41.92 ? 108 ARG C CB    1 
ATOM   4944 C CG    . ARG C 1 108 ? 1.627   49.261  9.309   1.00 46.49 ? 108 ARG C CG    1 
ATOM   4945 C CD    . ARG C 1 108 ? 0.478   48.947  10.256  1.00 51.41 ? 108 ARG C CD    1 
ATOM   4946 N NE    . ARG C 1 108 ? -0.722  49.639  9.772   1.00 56.08 ? 108 ARG C NE    1 
ATOM   4947 C CZ    . ARG C 1 108 ? -1.531  50.258  10.632  1.00 59.37 ? 108 ARG C CZ    1 
ATOM   4948 N NH1   . ARG C 1 108 ? -1.257  50.252  11.937  1.00 60.42 ? 108 ARG C NH1   1 
ATOM   4949 N NH2   . ARG C 1 108 ? -2.627  50.898  10.232  1.00 60.20 ? 108 ARG C NH2   1 
ATOM   4950 N N     . GLY C 1 109 ? 3.910   52.657  7.499   1.00 35.29 ? 109 GLY C N     1 
ATOM   4951 C CA    . GLY C 1 109 ? 4.428   53.934  7.048   1.00 34.74 ? 109 GLY C CA    1 
ATOM   4952 C C     . GLY C 1 109 ? 3.327   54.818  6.487   1.00 34.28 ? 109 GLY C C     1 
ATOM   4953 O O     . GLY C 1 109 ? 2.269   54.381  6.053   1.00 34.34 ? 109 GLY C O     1 
ATOM   4954 N N     . HIS C 1 110 ? 3.540   56.116  6.657   1.00 33.83 ? 110 HIS C N     1 
ATOM   4955 C CA    . HIS C 1 110 ? 2.604   57.115  6.157   1.00 33.04 ? 110 HIS C CA    1 
ATOM   4956 C C     . HIS C 1 110 ? 2.336   56.841  4.686   1.00 33.48 ? 110 HIS C C     1 
ATOM   4957 O O     . HIS C 1 110 ? 3.258   56.695  3.892   1.00 33.85 ? 110 HIS C O     1 
ATOM   4958 C CB    . HIS C 1 110 ? 3.243   58.480  6.289   1.00 28.67 ? 110 HIS C CB    1 
ATOM   4959 C CG    . HIS C 1 110 ? 2.506   59.627  5.700   1.00 26.03 ? 110 HIS C CG    1 
ATOM   4960 N ND1   . HIS C 1 110 ? 2.517   59.915  4.361   1.00 24.06 ? 110 HIS C ND1   1 
ATOM   4961 C CD2   . HIS C 1 110 ? 1.748   60.583  6.298   1.00 25.57 ? 110 HIS C CD2   1 
ATOM   4962 C CE1   . HIS C 1 110 ? 1.797   61.005  4.161   1.00 24.86 ? 110 HIS C CE1   1 
ATOM   4963 N NE2   . HIS C 1 110 ? 1.313   61.432  5.316   1.00 24.68 ? 110 HIS C NE2   1 
ATOM   4964 N N     . ASP C 1 111 ? 1.093   56.548  4.363   1.00 33.91 ? 111 ASP C N     1 
ATOM   4965 C CA    . ASP C 1 111 ? 0.671   56.342  2.972   1.00 33.96 ? 111 ASP C CA    1 
ATOM   4966 C C     . ASP C 1 111 ? 0.969   57.592  2.158   1.00 33.79 ? 111 ASP C C     1 
ATOM   4967 O O     . ASP C 1 111 ? 0.764   58.671  2.777   1.00 34.33 ? 111 ASP C O     1 
ATOM   4968 C CB    . ASP C 1 111 ? -0.861  56.241  3.098   1.00 36.06 ? 111 ASP C CB    1 
ATOM   4969 C CG    . ASP C 1 111 ? -1.491  55.575  1.901   1.00 39.27 ? 111 ASP C CG    1 
ATOM   4970 O OD1   . ASP C 1 111 ? -2.663  55.177  2.060   1.00 40.35 ? 111 ASP C OD1   1 
ATOM   4971 O OD2   . ASP C 1 111 ? -0.862  55.453  0.822   1.00 41.16 ? 111 ASP C OD2   1 
ATOM   4972 N N     . GLY C 1 112 ? 1.222   57.606  0.864   1.00 32.70 ? 112 GLY C N     1 
ATOM   4973 C CA    . GLY C 1 112 ? 1.430   58.994  0.326   1.00 31.83 ? 112 GLY C CA    1 
ATOM   4974 C C     . GLY C 1 112 ? 2.946   59.143  0.267   1.00 31.33 ? 112 GLY C C     1 
ATOM   4975 O O     . GLY C 1 112 ? 3.440   59.052  -0.861  1.00 31.86 ? 112 GLY C O     1 
ATOM   4976 N N     . PHE C 1 113 ? 3.641   59.282  1.394   1.00 30.41 ? 113 PHE C N     1 
ATOM   4977 C CA    . PHE C 1 113 ? 5.089   59.188  1.335   1.00 29.58 ? 113 PHE C CA    1 
ATOM   4978 C C     . PHE C 1 113 ? 5.477   57.850  0.697   1.00 29.95 ? 113 PHE C C     1 
ATOM   4979 O O     . PHE C 1 113 ? 5.942   57.795  -0.445  1.00 29.67 ? 113 PHE C O     1 
ATOM   4980 C CB    . PHE C 1 113 ? 5.743   59.350  2.700   1.00 25.77 ? 113 PHE C CB    1 
ATOM   4981 C CG    . PHE C 1 113 ? 5.425   60.647  3.381   1.00 22.18 ? 113 PHE C CG    1 
ATOM   4982 C CD1   . PHE C 1 113 ? 5.008   61.746  2.652   1.00 19.92 ? 113 PHE C CD1   1 
ATOM   4983 C CD2   . PHE C 1 113 ? 5.557   60.760  4.762   1.00 20.57 ? 113 PHE C CD2   1 
ATOM   4984 C CE1   . PHE C 1 113 ? 4.699   62.938  3.288   1.00 18.82 ? 113 PHE C CE1   1 
ATOM   4985 C CE2   . PHE C 1 113 ? 5.252   61.951  5.393   1.00 19.48 ? 113 PHE C CE2   1 
ATOM   4986 C CZ    . PHE C 1 113 ? 4.837   63.042  4.655   1.00 18.20 ? 113 PHE C CZ    1 
ATOM   4987 N N     . THR C 1 114 ? 5.133   56.775  1.385   1.00 30.29 ? 114 THR C N     1 
ATOM   4988 C CA    . THR C 1 114 ? 5.318   55.415  0.925   1.00 30.83 ? 114 THR C CA    1 
ATOM   4989 C C     . THR C 1 114 ? 4.848   55.223  -0.515  1.00 31.19 ? 114 THR C C     1 
ATOM   4990 O O     . THR C 1 114 ? 5.578   54.609  -1.301  1.00 31.43 ? 114 THR C O     1 
ATOM   4991 C CB    . THR C 1 114 ? 4.432   54.501  1.793   1.00 31.76 ? 114 THR C CB    1 
ATOM   4992 O OG1   . THR C 1 114 ? 4.846   54.556  3.157   1.00 32.27 ? 114 THR C OG1   1 
ATOM   4993 C CG2   . THR C 1 114 ? 4.566   53.079  1.295   1.00 33.45 ? 114 THR C CG2   1 
ATOM   4994 N N     . SER C 1 115 ? 3.633   55.671  -0.825  1.00 31.34 ? 115 SER C N     1 
ATOM   4995 C CA    . SER C 1 115 ? 3.091   55.537  -2.170  1.00 32.04 ? 115 SER C CA    1 
ATOM   4996 C C     . SER C 1 115 ? 3.952   56.262  -3.204  1.00 32.62 ? 115 SER C C     1 
ATOM   4997 O O     . SER C 1 115 ? 4.282   55.715  -4.258  1.00 32.69 ? 115 SER C O     1 
ATOM   4998 C CB    . SER C 1 115 ? 1.664   56.062  -2.293  1.00 31.53 ? 115 SER C CB    1 
ATOM   4999 O OG    . SER C 1 115 ? 0.962   56.006  -1.066  1.00 32.88 ? 115 SER C OG    1 
ATOM   5000 N N     . SER C 1 116 ? 4.203   57.542  -2.940  1.00 33.11 ? 116 SER C N     1 
ATOM   5001 C CA    . SER C 1 116 ? 5.113   58.342  -3.751  1.00 33.69 ? 116 SER C CA    1 
ATOM   5002 C C     . SER C 1 116 ? 6.418   57.563  -3.969  1.00 33.87 ? 116 SER C C     1 
ATOM   5003 O O     . SER C 1 116 ? 6.809   57.300  -5.103  1.00 34.04 ? 116 SER C O     1 
ATOM   5004 C CB    . SER C 1 116 ? 5.461   59.660  -3.066  1.00 35.00 ? 116 SER C CB    1 
ATOM   5005 O OG    . SER C 1 116 ? 4.553   60.731  -3.115  1.00 33.83 ? 116 SER C OG    1 
ATOM   5006 N N     . TRP C 1 117 ? 7.095   57.181  -2.888  1.00 34.08 ? 117 TRP C N     1 
ATOM   5007 C CA    . TRP C 1 117 ? 8.346   56.448  -3.026  1.00 34.82 ? 117 TRP C CA    1 
ATOM   5008 C C     . TRP C 1 117 ? 8.180   55.218  -3.903  1.00 35.13 ? 117 TRP C C     1 
ATOM   5009 O O     . TRP C 1 117 ? 8.728   55.154  -5.003  1.00 35.04 ? 117 TRP C O     1 
ATOM   5010 C CB    . TRP C 1 117 ? 9.008   56.064  -1.691  1.00 34.28 ? 117 TRP C CB    1 
ATOM   5011 C CG    . TRP C 1 117 ? 10.140  55.114  -1.941  1.00 34.23 ? 117 TRP C CG    1 
ATOM   5012 C CD1   . TRP C 1 117 ? 10.188  53.833  -1.487  1.00 35.44 ? 117 TRP C CD1   1 
ATOM   5013 C CD2   . TRP C 1 117 ? 11.314  55.309  -2.732  1.00 35.18 ? 117 TRP C CD2   1 
ATOM   5014 N NE1   . TRP C 1 117 ? 11.340  53.225  -1.929  1.00 36.34 ? 117 TRP C NE1   1 
ATOM   5015 C CE2   . TRP C 1 117 ? 12.051  54.108  -2.693  1.00 34.68 ? 117 TRP C CE2   1 
ATOM   5016 C CE3   . TRP C 1 117 ? 11.831  56.382  -3.471  1.00 36.29 ? 117 TRP C CE3   1 
ATOM   5017 C CZ2   . TRP C 1 117 ? 13.264  53.937  -3.350  1.00 34.13 ? 117 TRP C CZ2   1 
ATOM   5018 C CZ3   . TRP C 1 117 ? 13.054  56.203  -4.125  1.00 36.59 ? 117 TRP C CZ3   1 
ATOM   5019 C CH2   . TRP C 1 117 ? 13.758  54.991  -4.062  1.00 34.25 ? 117 TRP C CH2   1 
ATOM   5020 N N     . ARG C 1 118 ? 7.298   54.310  -3.502  1.00 35.77 ? 118 ARG C N     1 
ATOM   5021 C CA    . ARG C 1 118 ? 7.045   53.086  -4.251  1.00 36.51 ? 118 ARG C CA    1 
ATOM   5022 C C     . ARG C 1 118 ? 6.751   53.339  -5.712  1.00 36.28 ? 118 ARG C C     1 
ATOM   5023 O O     . ARG C 1 118 ? 7.223   52.601  -6.583  1.00 36.86 ? 118 ARG C O     1 
ATOM   5024 C CB    . ARG C 1 118 ? 5.933   52.283  -3.564  1.00 41.61 ? 118 ARG C CB    1 
ATOM   5025 C CG    . ARG C 1 118 ? 6.347   50.920  -3.052  1.00 48.93 ? 118 ARG C CG    1 
ATOM   5026 C CD    . ARG C 1 118 ? 6.022   50.602  -1.605  1.00 53.44 ? 118 ARG C CD    1 
ATOM   5027 N NE    . ARG C 1 118 ? 6.958   49.761  -0.869  1.00 57.51 ? 118 ARG C NE    1 
ATOM   5028 C CZ    . ARG C 1 118 ? 8.241   49.498  -1.071  1.00 60.23 ? 118 ARG C CZ    1 
ATOM   5029 N NH1   . ARG C 1 118 ? 8.962   49.989  -2.083  1.00 60.89 ? 118 ARG C NH1   1 
ATOM   5030 N NH2   . ARG C 1 118 ? 8.918   48.692  -0.246  1.00 61.54 ? 118 ARG C NH2   1 
ATOM   5031 N N     . SER C 1 119 ? 6.133   54.444  -6.111  1.00 35.87 ? 119 SER C N     1 
ATOM   5032 C CA    . SER C 1 119 ? 5.808   54.764  -7.483  1.00 35.32 ? 119 SER C CA    1 
ATOM   5033 C C     . SER C 1 119 ? 6.981   55.210  -8.341  1.00 35.27 ? 119 SER C C     1 
ATOM   5034 O O     . SER C 1 119 ? 6.830   55.496  -9.535  1.00 35.09 ? 119 SER C O     1 
ATOM   5035 C CB    . SER C 1 119 ? 4.735   55.870  -7.500  1.00 34.08 ? 119 SER C CB    1 
ATOM   5036 O OG    . SER C 1 119 ? 5.352   57.136  -7.379  1.00 34.09 ? 119 SER C OG    1 
ATOM   5037 N N     . VAL C 1 120 ? 8.158   55.353  -7.751  1.00 35.42 ? 120 VAL C N     1 
ATOM   5038 C CA    . VAL C 1 120 ? 9.329   55.861  -8.457  1.00 35.57 ? 120 VAL C CA    1 
ATOM   5039 C C     . VAL C 1 120 ? 10.588  55.111  -8.069  1.00 35.45 ? 120 VAL C C     1 
ATOM   5040 O O     . VAL C 1 120 ? 11.650  55.235  -8.673  1.00 35.10 ? 120 VAL C O     1 
ATOM   5041 C CB    . VAL C 1 120 ? 9.442   57.373  -8.179  1.00 36.57 ? 120 VAL C CB    1 
ATOM   5042 C CG1   . VAL C 1 120 ? 10.161  57.670  -6.876  1.00 36.55 ? 120 VAL C CG1   1 
ATOM   5043 C CG2   . VAL C 1 120 ? 10.086  58.103  -9.347  1.00 38.20 ? 120 VAL C CG2   1 
ATOM   5044 N N     . ALA C 1 121 ? 10.425  54.212  -7.107  1.00 36.02 ? 121 ALA C N     1 
ATOM   5045 C CA    . ALA C 1 121 ? 11.486  53.405  -6.544  1.00 36.79 ? 121 ALA C CA    1 
ATOM   5046 C C     . ALA C 1 121 ? 12.311  52.614  -7.540  1.00 37.54 ? 121 ALA C C     1 
ATOM   5047 O O     . ALA C 1 121 ? 13.528  52.536  -7.344  1.00 37.33 ? 121 ALA C O     1 
ATOM   5048 C CB    . ALA C 1 121 ? 10.941  52.492  -5.459  1.00 36.44 ? 121 ALA C CB    1 
ATOM   5049 N N     . ASP C 1 122 ? 11.708  51.981  -8.542  1.00 38.63 ? 122 ASP C N     1 
ATOM   5050 C CA    . ASP C 1 122 ? 12.513  51.245  -9.521  1.00 39.84 ? 122 ASP C CA    1 
ATOM   5051 C C     . ASP C 1 122 ? 13.429  52.214  -10.258 1.00 40.17 ? 122 ASP C C     1 
ATOM   5052 O O     . ASP C 1 122 ? 14.598  52.345  -9.883  1.00 41.25 ? 122 ASP C O     1 
ATOM   5053 C CB    . ASP C 1 122 ? 11.685  50.479  -10.536 1.00 42.77 ? 122 ASP C CB    1 
ATOM   5054 C CG    . ASP C 1 122 ? 10.935  49.309  -9.922  1.00 46.20 ? 122 ASP C CG    1 
ATOM   5055 O OD1   . ASP C 1 122 ? 9.901   48.933  -10.531 1.00 47.40 ? 122 ASP C OD1   1 
ATOM   5056 O OD2   . ASP C 1 122 ? 11.350  48.796  -8.851  1.00 46.79 ? 122 ASP C OD2   1 
ATOM   5057 N N     . THR C 1 123 ? 12.855  53.045  -11.117 1.00 39.60 ? 123 THR C N     1 
ATOM   5058 C CA    . THR C 1 123 ? 13.629  54.038  -11.848 1.00 39.05 ? 123 THR C CA    1 
ATOM   5059 C C     . THR C 1 123 ? 14.820  54.578  -11.073 1.00 38.88 ? 123 THR C C     1 
ATOM   5060 O O     . THR C 1 123 ? 15.974  54.335  -11.439 1.00 38.80 ? 123 THR C O     1 
ATOM   5061 C CB    . THR C 1 123 ? 12.658  55.187  -12.186 1.00 39.80 ? 123 THR C CB    1 
ATOM   5062 O OG1   . THR C 1 123 ? 11.418  54.569  -12.566 1.00 40.75 ? 123 THR C OG1   1 
ATOM   5063 C CG2   . THR C 1 123 ? 13.253  56.038  -13.288 1.00 39.53 ? 123 THR C CG2   1 
ATOM   5064 N N     . LEU C 1 124 ? 14.564  55.214  -9.933  1.00 38.47 ? 124 LEU C N     1 
ATOM   5065 C CA    . LEU C 1 124 ? 15.606  55.772  -9.082  1.00 37.83 ? 124 LEU C CA    1 
ATOM   5066 C C     . LEU C 1 124 ? 16.594  54.744  -8.563  1.00 37.43 ? 124 LEU C C     1 
ATOM   5067 O O     . LEU C 1 124 ? 17.794  54.896  -8.804  1.00 36.92 ? 124 LEU C O     1 
ATOM   5068 C CB    . LEU C 1 124 ? 14.940  56.576  -7.968  1.00 37.17 ? 124 LEU C CB    1 
ATOM   5069 C CG    . LEU C 1 124 ? 14.806  58.087  -8.048  1.00 36.30 ? 124 LEU C CG    1 
ATOM   5070 C CD1   . LEU C 1 124 ? 14.774  58.651  -9.453  1.00 36.81 ? 124 LEU C CD1   1 
ATOM   5071 C CD2   . LEU C 1 124 ? 13.537  58.533  -7.328  1.00 36.30 ? 124 LEU C CD2   1 
ATOM   5072 N N     . ARG C 1 125 ? 16.167  53.609  -8.026  1.00 37.62 ? 125 ARG C N     1 
ATOM   5073 C CA    . ARG C 1 125 ? 17.059  52.560  -7.558  1.00 38.72 ? 125 ARG C CA    1 
ATOM   5074 C C     . ARG C 1 125 ? 18.124  52.244  -8.610  1.00 39.07 ? 125 ARG C C     1 
ATOM   5075 O O     . ARG C 1 125 ? 19.314  52.056  -8.326  1.00 39.69 ? 125 ARG C O     1 
ATOM   5076 C CB    . ARG C 1 125 ? 16.343  51.240  -7.231  1.00 41.79 ? 125 ARG C CB    1 
ATOM   5077 C CG    . ARG C 1 125 ? 17.261  50.037  -7.105  1.00 44.64 ? 125 ARG C CG    1 
ATOM   5078 C CD    . ARG C 1 125 ? 16.568  48.725  -6.827  1.00 49.77 ? 125 ARG C CD    1 
ATOM   5079 N NE    . ARG C 1 125 ? 15.802  48.654  -5.592  1.00 54.04 ? 125 ARG C NE    1 
ATOM   5080 C CZ    . ARG C 1 125 ? 14.481  48.507  -5.490  1.00 56.23 ? 125 ARG C CZ    1 
ATOM   5081 N NH1   . ARG C 1 125 ? 13.928  48.466  -4.276  1.00 56.46 ? 125 ARG C NH1   1 
ATOM   5082 N NH2   . ARG C 1 125 ? 13.729  48.389  -6.583  1.00 57.70 ? 125 ARG C NH2   1 
ATOM   5083 N N     . GLN C 1 126 ? 17.679  52.070  -9.849  1.00 38.80 ? 126 GLN C N     1 
ATOM   5084 C CA    . GLN C 1 126 ? 18.563  51.778  -10.956 1.00 38.43 ? 126 GLN C CA    1 
ATOM   5085 C C     . GLN C 1 126 ? 19.471  52.925  -11.356 1.00 37.81 ? 126 GLN C C     1 
ATOM   5086 O O     . GLN C 1 126 ? 20.579  52.651  -11.812 1.00 37.61 ? 126 GLN C O     1 
ATOM   5087 C CB    . GLN C 1 126 ? 17.684  51.341  -12.126 1.00 42.34 ? 126 GLN C CB    1 
ATOM   5088 C CG    . GLN C 1 126 ? 18.484  50.683  -13.240 1.00 48.00 ? 126 GLN C CG    1 
ATOM   5089 C CD    . GLN C 1 126 ? 18.014  51.260  -14.571 1.00 51.35 ? 126 GLN C CD    1 
ATOM   5090 O OE1   . GLN C 1 126 ? 18.804  51.970  -15.205 1.00 54.28 ? 126 GLN C OE1   1 
ATOM   5091 N NE2   . GLN C 1 126 ? 16.758  50.950  -14.883 1.00 51.38 ? 126 GLN C NE2   1 
ATOM   5092 N N     . LYS C 1 127 ? 19.067  54.183  -11.206 1.00 37.44 ? 127 LYS C N     1 
ATOM   5093 C CA    . LYS C 1 127 ? 19.902  55.327  -11.546 1.00 36.70 ? 127 LYS C CA    1 
ATOM   5094 C C     . LYS C 1 127 ? 21.004  55.425  -10.493 1.00 36.46 ? 127 LYS C C     1 
ATOM   5095 O O     . LYS C 1 127 ? 22.150  55.751  -10.784 1.00 36.46 ? 127 LYS C O     1 
ATOM   5096 C CB    . LYS C 1 127 ? 19.101  56.625  -11.578 1.00 37.57 ? 127 LYS C CB    1 
ATOM   5097 C CG    . LYS C 1 127 ? 17.993  56.661  -12.618 1.00 39.10 ? 127 LYS C CG    1 
ATOM   5098 C CD    . LYS C 1 127 ? 18.557  56.992  -13.988 1.00 41.68 ? 127 LYS C CD    1 
ATOM   5099 C CE    . LYS C 1 127 ? 17.467  57.367  -14.978 1.00 43.10 ? 127 LYS C CE    1 
ATOM   5100 N NZ    . LYS C 1 127 ? 17.762  56.863  -16.356 1.00 45.68 ? 127 LYS C NZ    1 
ATOM   5101 N N     . VAL C 1 128 ? 20.646  55.120  -9.248  1.00 36.09 ? 128 VAL C N     1 
ATOM   5102 C CA    . VAL C 1 128 ? 21.614  55.114  -8.158  1.00 36.23 ? 128 VAL C CA    1 
ATOM   5103 C C     . VAL C 1 128 ? 22.652  54.021  -8.423  1.00 36.91 ? 128 VAL C C     1 
ATOM   5104 O O     . VAL C 1 128 ? 23.868  54.237  -8.453  1.00 36.74 ? 128 VAL C O     1 
ATOM   5105 C CB    . VAL C 1 128 ? 20.946  54.809  -6.807  1.00 35.07 ? 128 VAL C CB    1 
ATOM   5106 C CG1   . VAL C 1 128 ? 21.898  55.093  -5.657  1.00 36.22 ? 128 VAL C CG1   1 
ATOM   5107 C CG2   . VAL C 1 128 ? 19.707  55.659  -6.597  1.00 37.09 ? 128 VAL C CG2   1 
ATOM   5108 N N     . GLU C 1 129 ? 22.123  52.821  -8.701  1.00 37.45 ? 129 GLU C N     1 
ATOM   5109 C CA    . GLU C 1 129 ? 22.993  51.671  -8.924  1.00 38.17 ? 129 GLU C CA    1 
ATOM   5110 C C     . GLU C 1 129 ? 23.960  51.828  -10.077 1.00 38.25 ? 129 GLU C C     1 
ATOM   5111 O O     . GLU C 1 129 ? 25.160  51.543  -9.883  1.00 37.63 ? 129 GLU C O     1 
ATOM   5112 C CB    . GLU C 1 129 ? 22.144  50.398  -8.910  1.00 40.60 ? 129 GLU C CB    1 
ATOM   5113 C CG    . GLU C 1 129 ? 21.748  50.116  -7.472  1.00 43.58 ? 129 GLU C CG    1 
ATOM   5114 C CD    . GLU C 1 129 ? 20.916  48.881  -7.236  1.00 47.19 ? 129 GLU C CD    1 
ATOM   5115 O OE1   . GLU C 1 129 ? 20.463  48.794  -6.062  1.00 49.03 ? 129 GLU C OE1   1 
ATOM   5116 O OE2   . GLU C 1 129 ? 20.734  48.042  -8.150  1.00 47.78 ? 129 GLU C OE2   1 
ATOM   5117 N N     . ASP C 1 130 ? 23.517  52.372  -11.219 1.00 38.30 ? 130 ASP C N     1 
ATOM   5118 C CA    . ASP C 1 130 ? 24.456  52.638  -12.307 1.00 38.99 ? 130 ASP C CA    1 
ATOM   5119 C C     . ASP C 1 130 ? 25.556  53.576  -11.793 1.00 39.11 ? 130 ASP C C     1 
ATOM   5120 O O     . ASP C 1 130 ? 26.744  53.229  -11.827 1.00 39.00 ? 130 ASP C O     1 
ATOM   5121 C CB    . ASP C 1 130 ? 23.819  53.235  -13.547 1.00 42.48 ? 130 ASP C CB    1 
ATOM   5122 C CG    . ASP C 1 130 ? 22.851  52.304  -14.248 1.00 47.46 ? 130 ASP C CG    1 
ATOM   5123 O OD1   . ASP C 1 130 ? 22.896  51.066  -14.047 1.00 49.24 ? 130 ASP C OD1   1 
ATOM   5124 O OD2   . ASP C 1 130 ? 22.002  52.827  -15.014 1.00 50.52 ? 130 ASP C OD2   1 
ATOM   5125 N N     . ALA C 1 131 ? 25.156  54.670  -11.133 1.00 38.82 ? 131 ALA C N     1 
ATOM   5126 C CA    . ALA C 1 131 ? 26.114  55.611  -10.585 1.00 38.52 ? 131 ALA C CA    1 
ATOM   5127 C C     . ALA C 1 131 ? 27.142  54.915  -9.703  1.00 38.66 ? 131 ALA C C     1 
ATOM   5128 O O     . ALA C 1 131 ? 28.351  55.167  -9.831  1.00 38.99 ? 131 ALA C O     1 
ATOM   5129 C CB    . ALA C 1 131 ? 25.467  56.713  -9.771  1.00 39.23 ? 131 ALA C CB    1 
ATOM   5130 N N     . VAL C 1 132 ? 26.666  54.132  -8.738  1.00 38.43 ? 132 VAL C N     1 
ATOM   5131 C CA    . VAL C 1 132 ? 27.602  53.421  -7.852  1.00 38.80 ? 132 VAL C CA    1 
ATOM   5132 C C     . VAL C 1 132 ? 28.581  52.573  -8.659  1.00 39.86 ? 132 VAL C C     1 
ATOM   5133 O O     . VAL C 1 132 ? 29.803  52.643  -8.506  1.00 39.74 ? 132 VAL C O     1 
ATOM   5134 C CB    . VAL C 1 132 ? 26.786  52.568  -6.872  1.00 36.20 ? 132 VAL C CB    1 
ATOM   5135 C CG1   . VAL C 1 132 ? 27.592  51.529  -6.136  1.00 33.01 ? 132 VAL C CG1   1 
ATOM   5136 C CG2   . VAL C 1 132 ? 26.058  53.491  -5.904  1.00 36.59 ? 132 VAL C CG2   1 
ATOM   5137 N N     . ARG C 1 133 ? 28.045  51.815  -9.626  1.00 40.71 ? 133 ARG C N     1 
ATOM   5138 C CA    . ARG C 1 133 ? 28.829  50.986  -10.527 1.00 41.28 ? 133 ARG C CA    1 
ATOM   5139 C C     . ARG C 1 133 ? 29.956  51.809  -11.144 1.00 41.66 ? 133 ARG C C     1 
ATOM   5140 O O     . ARG C 1 133 ? 31.110  51.409  -10.992 1.00 42.33 ? 133 ARG C O     1 
ATOM   5141 C CB    . ARG C 1 133 ? 27.984  50.423  -11.668 1.00 43.53 ? 133 ARG C CB    1 
ATOM   5142 C CG    . ARG C 1 133 ? 27.928  48.901  -11.753 1.00 44.85 ? 133 ARG C CG    1 
ATOM   5143 C CD    . ARG C 1 133 ? 26.736  48.444  -12.604 1.00 44.72 ? 133 ARG C CD    1 
ATOM   5144 N N     . GLU C 1 134 ? 29.662  52.965  -11.730 1.00 41.71 ? 134 GLU C N     1 
ATOM   5145 C CA    . GLU C 1 134 ? 30.711  53.791  -12.301 1.00 41.94 ? 134 GLU C CA    1 
ATOM   5146 C C     . GLU C 1 134 ? 31.629  54.453  -11.291 1.00 41.85 ? 134 GLU C C     1 
ATOM   5147 O O     . GLU C 1 134 ? 32.502  55.201  -11.786 1.00 42.35 ? 134 GLU C O     1 
ATOM   5148 C CB    . GLU C 1 134 ? 30.142  54.885  -13.225 1.00 42.82 ? 134 GLU C CB    1 
ATOM   5149 C CG    . GLU C 1 134 ? 29.787  54.399  -14.624 1.00 43.61 ? 134 GLU C CG    1 
ATOM   5150 N N     . HIS C 1 135 ? 31.235  54.671  -10.028 1.00 41.35 ? 135 HIS C N     1 
ATOM   5151 C CA    . HIS C 1 135 ? 32.068  55.417  -9.071  1.00 40.96 ? 135 HIS C CA    1 
ATOM   5152 C C     . HIS C 1 135 ? 31.969  54.747  -7.699  1.00 40.05 ? 135 HIS C C     1 
ATOM   5153 O O     . HIS C 1 135 ? 31.469  55.258  -6.697  1.00 40.25 ? 135 HIS C O     1 
ATOM   5154 C CB    . HIS C 1 135 ? 31.672  56.886  -8.905  1.00 42.40 ? 135 HIS C CB    1 
ATOM   5155 C CG    . HIS C 1 135 ? 31.599  57.654  -10.181 1.00 45.20 ? 135 HIS C CG    1 
ATOM   5156 N ND1   . HIS C 1 135 ? 32.710  58.164  -10.798 1.00 46.29 ? 135 HIS C ND1   1 
ATOM   5157 C CD2   . HIS C 1 135 ? 30.542  57.930  -10.988 1.00 47.78 ? 135 HIS C CD2   1 
ATOM   5158 C CE1   . HIS C 1 135 ? 32.342  58.767  -11.919 1.00 48.52 ? 135 HIS C CE1   1 
ATOM   5159 N NE2   . HIS C 1 135 ? 31.028  58.643  -12.061 1.00 49.56 ? 135 HIS C NE2   1 
ATOM   5160 N N     . PRO C 1 136 ? 32.420  53.495  -7.657  1.00 39.23 ? 136 PRO C N     1 
ATOM   5161 C CA    . PRO C 1 136 ? 32.295  52.607  -6.516  1.00 38.74 ? 136 PRO C CA    1 
ATOM   5162 C C     . PRO C 1 136 ? 32.955  53.079  -5.241  1.00 38.62 ? 136 PRO C C     1 
ATOM   5163 O O     . PRO C 1 136 ? 32.779  52.462  -4.191  1.00 38.34 ? 136 PRO C O     1 
ATOM   5164 C CB    . PRO C 1 136 ? 32.945  51.300  -6.991  1.00 38.57 ? 136 PRO C CB    1 
ATOM   5165 C CG    . PRO C 1 136 ? 33.969  51.776  -7.979  1.00 38.59 ? 136 PRO C CG    1 
ATOM   5166 C CD    . PRO C 1 136 ? 33.220  52.848  -8.735  1.00 38.82 ? 136 PRO C CD    1 
ATOM   5167 N N     . ASP C 1 137 ? 33.914  53.994  -5.342  1.00 38.91 ? 137 ASP C N     1 
ATOM   5168 C CA    . ASP C 1 137 ? 34.530  54.617  -4.187  1.00 39.52 ? 137 ASP C CA    1 
ATOM   5169 C C     . ASP C 1 137 ? 33.804  55.893  -3.764  1.00 39.44 ? 137 ASP C C     1 
ATOM   5170 O O     . ASP C 1 137 ? 34.289  56.577  -2.851  1.00 40.04 ? 137 ASP C O     1 
ATOM   5171 C CB    . ASP C 1 137 ? 35.990  54.997  -4.472  1.00 42.79 ? 137 ASP C CB    1 
ATOM   5172 C CG    . ASP C 1 137 ? 36.050  56.042  -5.577  1.00 46.24 ? 137 ASP C CG    1 
ATOM   5173 O OD1   . ASP C 1 137 ? 35.551  55.756  -6.687  1.00 48.42 ? 137 ASP C OD1   1 
ATOM   5174 O OD2   . ASP C 1 137 ? 36.569  57.134  -5.266  1.00 48.34 ? 137 ASP C OD2   1 
ATOM   5175 N N     . TYR C 1 138 ? 32.781  56.317  -4.496  1.00 38.91 ? 138 TYR C N     1 
ATOM   5176 C CA    . TYR C 1 138 ? 32.009  57.493  -4.097  1.00 38.22 ? 138 TYR C CA    1 
ATOM   5177 C C     . TYR C 1 138 ? 31.022  57.128  -2.999  1.00 37.38 ? 138 TYR C C     1 
ATOM   5178 O O     . TYR C 1 138 ? 30.746  55.948  -2.789  1.00 37.39 ? 138 TYR C O     1 
ATOM   5179 C CB    . TYR C 1 138 ? 31.299  58.079  -5.314  1.00 39.44 ? 138 TYR C CB    1 
ATOM   5180 C CG    . TYR C 1 138 ? 32.164  59.068  -6.073  1.00 41.16 ? 138 TYR C CG    1 
ATOM   5181 C CD1   . TYR C 1 138 ? 33.535  58.885  -6.221  1.00 41.60 ? 138 TYR C CD1   1 
ATOM   5182 C CD2   . TYR C 1 138 ? 31.587  60.191  -6.651  1.00 41.42 ? 138 TYR C CD2   1 
ATOM   5183 C CE1   . TYR C 1 138 ? 34.305  59.786  -6.924  1.00 41.54 ? 138 TYR C CE1   1 
ATOM   5184 C CE2   . TYR C 1 138 ? 32.365  61.100  -7.337  1.00 41.96 ? 138 TYR C CE2   1 
ATOM   5185 C CZ    . TYR C 1 138 ? 33.720  60.895  -7.475  1.00 41.83 ? 138 TYR C CZ    1 
ATOM   5186 O OH    . TYR C 1 138 ? 34.467  61.824  -8.158  1.00 42.44 ? 138 TYR C OH    1 
ATOM   5187 N N     . ARG C 1 139 ? 30.578  58.105  -2.227  1.00 36.38 ? 139 ARG C N     1 
ATOM   5188 C CA    . ARG C 1 139 ? 29.689  57.884  -1.090  1.00 35.64 ? 139 ARG C CA    1 
ATOM   5189 C C     . ARG C 1 139 ? 28.244  58.199  -1.455  1.00 35.68 ? 139 ARG C C     1 
ATOM   5190 O O     . ARG C 1 139 ? 28.002  59.208  -2.136  1.00 36.16 ? 139 ARG C O     1 
ATOM   5191 C CB    . ARG C 1 139 ? 30.173  58.737  0.077   1.00 33.97 ? 139 ARG C CB    1 
ATOM   5192 C CG    . ARG C 1 139 ? 29.330  58.741  1.330   1.00 34.58 ? 139 ARG C CG    1 
ATOM   5193 C CD    . ARG C 1 139 ? 30.115  59.033  2.583   1.00 34.54 ? 139 ARG C CD    1 
ATOM   5194 N NE    . ARG C 1 139 ? 29.811  60.317  3.228   1.00 36.80 ? 139 ARG C NE    1 
ATOM   5195 C CZ    . ARG C 1 139 ? 28.867  60.440  4.160   1.00 37.13 ? 139 ARG C CZ    1 
ATOM   5196 N NH1   . ARG C 1 139 ? 28.622  61.591  4.752   1.00 35.38 ? 139 ARG C NH1   1 
ATOM   5197 N NH2   . ARG C 1 139 ? 28.146  59.370  4.496   1.00 39.68 ? 139 ARG C NH2   1 
ATOM   5198 N N     . VAL C 1 140 ? 27.287  57.343  -1.086  1.00 35.14 ? 140 VAL C N     1 
ATOM   5199 C CA    . VAL C 1 140 ? 25.897  57.607  -1.450  1.00 34.72 ? 140 VAL C CA    1 
ATOM   5200 C C     . VAL C 1 140 ? 25.074  58.205  -0.307  1.00 34.26 ? 140 VAL C C     1 
ATOM   5201 O O     . VAL C 1 140 ? 24.692  57.560  0.687   1.00 34.21 ? 140 VAL C O     1 
ATOM   5202 C CB    . VAL C 1 140 ? 25.155  56.388  -2.020  1.00 34.72 ? 140 VAL C CB    1 
ATOM   5203 C CG1   . VAL C 1 140 ? 23.741  56.794  -2.414  1.00 33.42 ? 140 VAL C CG1   1 
ATOM   5204 C CG2   . VAL C 1 140 ? 25.876  55.793  -3.219  1.00 35.09 ? 140 VAL C CG2   1 
ATOM   5205 N N     . VAL C 1 141 ? 24.683  59.457  -0.548  1.00 33.45 ? 141 VAL C N     1 
ATOM   5206 C CA    . VAL C 1 141 ? 23.861  60.203  0.410   1.00 32.53 ? 141 VAL C CA    1 
ATOM   5207 C C     . VAL C 1 141 ? 22.481  60.486  -0.188  1.00 31.94 ? 141 VAL C C     1 
ATOM   5208 O O     . VAL C 1 141 ? 22.356  60.951  -1.328  1.00 32.28 ? 141 VAL C O     1 
ATOM   5209 C CB    . VAL C 1 141 ? 24.583  61.519  0.752   1.00 32.35 ? 141 VAL C CB    1 
ATOM   5210 C CG1   . VAL C 1 141 ? 23.685  62.593  1.339   1.00 32.19 ? 141 VAL C CG1   1 
ATOM   5211 C CG2   . VAL C 1 141 ? 25.780  61.299  1.657   1.00 32.15 ? 141 VAL C CG2   1 
ATOM   5212 N N     . PHE C 1 142 ? 21.420  60.122  0.535   1.00 30.74 ? 142 PHE C N     1 
ATOM   5213 C CA    . PHE C 1 142 ? 20.069  60.538  0.178   1.00 29.64 ? 142 PHE C CA    1 
ATOM   5214 C C     . PHE C 1 142 ? 19.663  61.739  1.040   1.00 28.94 ? 142 PHE C C     1 
ATOM   5215 O O     . PHE C 1 142 ? 19.880  61.726  2.264   1.00 29.02 ? 142 PHE C O     1 
ATOM   5216 C CB    . PHE C 1 142 ? 19.022  59.441  0.320   1.00 29.50 ? 142 PHE C CB    1 
ATOM   5217 C CG    . PHE C 1 142 ? 19.076  58.311  -0.668  1.00 29.39 ? 142 PHE C CG    1 
ATOM   5218 C CD1   . PHE C 1 142 ? 19.925  58.338  -1.763  1.00 28.02 ? 142 PHE C CD1   1 
ATOM   5219 C CD2   . PHE C 1 142 ? 18.236  57.214  -0.488  1.00 28.27 ? 142 PHE C CD2   1 
ATOM   5220 C CE1   . PHE C 1 142 ? 19.962  57.305  -2.673  1.00 27.00 ? 142 PHE C CE1   1 
ATOM   5221 C CE2   . PHE C 1 142 ? 18.281  56.183  -1.415  1.00 28.85 ? 142 PHE C CE2   1 
ATOM   5222 C CZ    . PHE C 1 142 ? 19.130  56.229  -2.509  1.00 27.13 ? 142 PHE C CZ    1 
ATOM   5223 N N     . THR C 1 143 ? 19.134  62.812  0.442   1.00 28.04 ? 143 THR C N     1 
ATOM   5224 C CA    . THR C 1 143 ? 18.752  63.962  1.263   1.00 26.77 ? 143 THR C CA    1 
ATOM   5225 C C     . THR C 1 143 ? 17.449  64.636  0.875   1.00 26.52 ? 143 THR C C     1 
ATOM   5226 O O     . THR C 1 143 ? 16.809  64.363  -0.139  1.00 26.58 ? 143 THR C O     1 
ATOM   5227 C CB    . THR C 1 143 ? 19.907  64.969  1.308   1.00 23.18 ? 143 THR C CB    1 
ATOM   5228 O OG1   . THR C 1 143 ? 19.710  65.862  2.413   1.00 22.78 ? 143 THR C OG1   1 
ATOM   5229 C CG2   . THR C 1 143 ? 20.028  65.812  0.074   1.00 20.74 ? 143 THR C CG2   1 
ATOM   5230 N N     . GLY C 1 144 ? 17.029  65.604  1.683   1.00 25.79 ? 144 GLY C N     1 
ATOM   5231 C CA    . GLY C 1 144 ? 15.852  66.381  1.404   1.00 25.51 ? 144 GLY C CA    1 
ATOM   5232 C C     . GLY C 1 144 ? 15.287  67.121  2.598   1.00 25.70 ? 144 GLY C C     1 
ATOM   5233 O O     . GLY C 1 144 ? 15.450  66.700  3.745   1.00 25.84 ? 144 GLY C O     1 
ATOM   5234 N N     . HIS C 1 145 ? 14.449  68.113  2.288   1.00 25.46 ? 145 HIS C N     1 
ATOM   5235 C CA    . HIS C 1 145 ? 13.835  68.952  3.319   1.00 25.42 ? 145 HIS C CA    1 
ATOM   5236 C C     . HIS C 1 145 ? 12.341  68.716  3.419   1.00 25.96 ? 145 HIS C C     1 
ATOM   5237 O O     . HIS C 1 145 ? 11.680  68.510  2.403   1.00 26.30 ? 145 HIS C O     1 
ATOM   5238 C CB    . HIS C 1 145 ? 14.123  70.398  2.937   1.00 23.07 ? 145 HIS C CB    1 
ATOM   5239 C CG    . HIS C 1 145 ? 13.346  71.451  3.642   1.00 23.30 ? 145 HIS C CG    1 
ATOM   5240 N ND1   . HIS C 1 145 ? 12.358  72.194  3.022   1.00 23.00 ? 145 HIS C ND1   1 
ATOM   5241 C CD2   . HIS C 1 145 ? 13.399  71.905  4.914   1.00 24.01 ? 145 HIS C CD2   1 
ATOM   5242 C CE1   . HIS C 1 145 ? 11.842  73.047  3.877   1.00 23.36 ? 145 HIS C CE1   1 
ATOM   5243 N NE2   . HIS C 1 145 ? 12.457  72.904  5.043   1.00 23.63 ? 145 HIS C NE2   1 
ATOM   5244 N N     . SER C 1 146 ? 11.768  68.693  4.616   1.00 26.49 ? 146 SER C N     1 
ATOM   5245 C CA    . SER C 1 146 ? 10.311  68.535  4.755   1.00 26.95 ? 146 SER C CA    1 
ATOM   5246 C C     . SER C 1 146 ? 9.831   67.228  4.147   1.00 27.18 ? 146 SER C C     1 
ATOM   5247 O O     . SER C 1 146 ? 10.362  66.152  4.434   1.00 27.27 ? 146 SER C O     1 
ATOM   5248 C CB    . SER C 1 146 ? 9.721   69.775  4.091   1.00 27.76 ? 146 SER C CB    1 
ATOM   5249 O OG    . SER C 1 146 ? 8.389   70.071  4.430   1.00 30.21 ? 146 SER C OG    1 
ATOM   5250 N N     . LEU C 1 147 ? 8.891   67.256  3.216   1.00 27.20 ? 147 LEU C N     1 
ATOM   5251 C CA    . LEU C 1 147 ? 8.408   66.114  2.475   1.00 27.16 ? 147 LEU C CA    1 
ATOM   5252 C C     . LEU C 1 147 ? 9.570   65.377  1.828   1.00 27.58 ? 147 LEU C C     1 
ATOM   5253 O O     . LEU C 1 147 ? 9.584   64.142  1.824   1.00 27.87 ? 147 LEU C O     1 
ATOM   5254 C CB    . LEU C 1 147 ? 7.455   66.613  1.394   1.00 26.78 ? 147 LEU C CB    1 
ATOM   5255 C CG    . LEU C 1 147 ? 7.088   65.659  0.267   1.00 27.53 ? 147 LEU C CG    1 
ATOM   5256 C CD1   . LEU C 1 147 ? 6.484   64.378  0.813   1.00 28.33 ? 147 LEU C CD1   1 
ATOM   5257 C CD2   . LEU C 1 147 ? 6.203   66.384  -0.725  1.00 27.33 ? 147 LEU C CD2   1 
ATOM   5258 N N     . GLY C 1 148 ? 10.520  66.108  1.237   1.00 27.48 ? 148 GLY C N     1 
ATOM   5259 C CA    . GLY C 1 148 ? 11.696  65.506  0.652   1.00 27.63 ? 148 GLY C CA    1 
ATOM   5260 C C     . GLY C 1 148 ? 12.481  64.710  1.678   1.00 28.03 ? 148 GLY C C     1 
ATOM   5261 O O     . GLY C 1 148 ? 13.171  63.753  1.316   1.00 28.42 ? 148 GLY C O     1 
ATOM   5262 N N     . GLY C 1 149 ? 12.560  65.130  2.937   1.00 27.84 ? 149 GLY C N     1 
ATOM   5263 C CA    . GLY C 1 149 ? 13.283  64.407  3.979   1.00 27.57 ? 149 GLY C CA    1 
ATOM   5264 C C     . GLY C 1 149 ? 12.591  63.086  4.290   1.00 27.57 ? 149 GLY C C     1 
ATOM   5265 O O     . GLY C 1 149 ? 13.228  62.060  4.521   1.00 27.90 ? 149 GLY C O     1 
ATOM   5266 N N     . ALA C 1 150 ? 11.262  63.103  4.260   1.00 27.13 ? 150 ALA C N     1 
ATOM   5267 C CA    . ALA C 1 150 ? 10.464  61.899  4.437   1.00 26.59 ? 150 ALA C CA    1 
ATOM   5268 C C     . ALA C 1 150 ? 10.758  60.904  3.317   1.00 26.45 ? 150 ALA C C     1 
ATOM   5269 O O     . ALA C 1 150 ? 11.021  59.740  3.586   1.00 26.14 ? 150 ALA C O     1 
ATOM   5270 C CB    . ALA C 1 150 ? 8.989   62.274  4.434   1.00 25.02 ? 150 ALA C CB    1 
ATOM   5271 N N     . LEU C 1 151 ? 10.754  61.380  2.079   1.00 26.42 ? 151 LEU C N     1 
ATOM   5272 C CA    . LEU C 1 151 ? 10.944  60.537  0.917   1.00 26.73 ? 151 LEU C CA    1 
ATOM   5273 C C     . LEU C 1 151 ? 12.327  59.910  0.906   1.00 26.92 ? 151 LEU C C     1 
ATOM   5274 O O     . LEU C 1 151 ? 12.513  58.710  0.713   1.00 27.15 ? 151 LEU C O     1 
ATOM   5275 C CB    . LEU C 1 151 ? 10.762  61.388  -0.344  1.00 28.26 ? 151 LEU C CB    1 
ATOM   5276 C CG    . LEU C 1 151 ? 9.330   61.626  -0.816  1.00 28.39 ? 151 LEU C CG    1 
ATOM   5277 C CD1   . LEU C 1 151 ? 9.319   61.996  -2.291  1.00 28.39 ? 151 LEU C CD1   1 
ATOM   5278 C CD2   . LEU C 1 151 ? 8.497   60.367  -0.615  1.00 28.21 ? 151 LEU C CD2   1 
ATOM   5279 N N     . ALA C 1 152 ? 13.330  60.725  1.223   1.00 26.87 ? 152 ALA C N     1 
ATOM   5280 C CA    . ALA C 1 152 ? 14.687  60.235  1.390   1.00 26.79 ? 152 ALA C CA    1 
ATOM   5281 C C     . ALA C 1 152 ? 14.759  59.243  2.541   1.00 26.84 ? 152 ALA C C     1 
ATOM   5282 O O     . ALA C 1 152 ? 15.314  58.160  2.347   1.00 27.46 ? 152 ALA C O     1 
ATOM   5283 C CB    . ALA C 1 152 ? 15.575  61.436  1.657   1.00 27.61 ? 152 ALA C CB    1 
ATOM   5284 N N     . THR C 1 153 ? 14.131  59.511  3.678   1.00 26.61 ? 153 THR C N     1 
ATOM   5285 C CA    . THR C 1 153 ? 14.121  58.528  4.752   1.00 26.89 ? 153 THR C CA    1 
ATOM   5286 C C     . THR C 1 153 ? 13.619  57.166  4.306   1.00 27.57 ? 153 THR C C     1 
ATOM   5287 O O     . THR C 1 153 ? 14.370  56.185  4.408   1.00 28.01 ? 153 THR C O     1 
ATOM   5288 C CB    . THR C 1 153 ? 13.337  59.041  5.963   1.00 26.25 ? 153 THR C CB    1 
ATOM   5289 O OG1   . THR C 1 153 ? 13.964  60.269  6.369   1.00 26.69 ? 153 THR C OG1   1 
ATOM   5290 C CG2   . THR C 1 153 ? 13.357  58.060  7.116   1.00 25.81 ? 153 THR C CG2   1 
ATOM   5291 N N     . VAL C 1 154 ? 12.439  57.077  3.693   1.00 27.90 ? 154 VAL C N     1 
ATOM   5292 C CA    . VAL C 1 154 ? 11.900  55.792  3.290   1.00 28.07 ? 154 VAL C CA    1 
ATOM   5293 C C     . VAL C 1 154 ? 12.671  55.239  2.107   1.00 28.51 ? 154 VAL C C     1 
ATOM   5294 O O     . VAL C 1 154 ? 13.153  54.092  2.202   1.00 28.68 ? 154 VAL C O     1 
ATOM   5295 C CB    . VAL C 1 154 ? 10.393  55.745  3.046   1.00 28.37 ? 154 VAL C CB    1 
ATOM   5296 C CG1   . VAL C 1 154 ? 9.671   56.802  3.866   1.00 27.62 ? 154 VAL C CG1   1 
ATOM   5297 C CG2   . VAL C 1 154 ? 9.992   55.816  1.584   1.00 28.30 ? 154 VAL C CG2   1 
ATOM   5298 N N     . ALA C 1 155 ? 13.052  56.113  1.170   1.00 28.37 ? 155 ALA C N     1 
ATOM   5299 C CA    . ALA C 1 155 ? 13.886  55.596  0.073   1.00 28.90 ? 155 ALA C CA    1 
ATOM   5300 C C     . ALA C 1 155 ? 15.142  54.937  0.645   1.00 29.35 ? 155 ALA C C     1 
ATOM   5301 O O     . ALA C 1 155 ? 15.572  53.934  0.095   1.00 29.53 ? 155 ALA C O     1 
ATOM   5302 C CB    . ALA C 1 155 ? 14.318  56.658  -0.918  1.00 28.09 ? 155 ALA C CB    1 
ATOM   5303 N N     . GLY C 1 156 ? 15.793  55.542  1.628   1.00 29.76 ? 156 GLY C N     1 
ATOM   5304 C CA    . GLY C 1 156 ? 16.975  55.001  2.250   1.00 30.47 ? 156 GLY C CA    1 
ATOM   5305 C C     . GLY C 1 156 ? 16.697  53.659  2.888   1.00 31.20 ? 156 GLY C C     1 
ATOM   5306 O O     . GLY C 1 156 ? 17.153  52.630  2.395   1.00 31.33 ? 156 GLY C O     1 
ATOM   5307 N N     . ALA C 1 157 ? 15.796  53.573  3.856   1.00 32.02 ? 157 ALA C N     1 
ATOM   5308 C CA    . ALA C 1 157 ? 15.372  52.300  4.423   1.00 32.62 ? 157 ALA C CA    1 
ATOM   5309 C C     . ALA C 1 157 ? 15.087  51.253  3.351   1.00 33.50 ? 157 ALA C C     1 
ATOM   5310 O O     . ALA C 1 157 ? 15.623  50.148  3.443   1.00 33.90 ? 157 ALA C O     1 
ATOM   5311 C CB    . ALA C 1 157 ? 14.110  52.547  5.226   1.00 32.04 ? 157 ALA C CB    1 
ATOM   5312 N N     . ASP C 1 158 ? 14.291  51.563  2.333   1.00 34.12 ? 158 ASP C N     1 
ATOM   5313 C CA    . ASP C 1 158 ? 14.026  50.654  1.239   1.00 35.00 ? 158 ASP C CA    1 
ATOM   5314 C C     . ASP C 1 158 ? 15.271  50.210  0.486   1.00 35.40 ? 158 ASP C C     1 
ATOM   5315 O O     . ASP C 1 158 ? 15.141  49.169  -0.176  1.00 36.60 ? 158 ASP C O     1 
ATOM   5316 C CB    . ASP C 1 158 ? 13.092  51.247  0.166   1.00 35.81 ? 158 ASP C CB    1 
ATOM   5317 C CG    . ASP C 1 158 ? 12.385  50.222  -0.703  1.00 35.91 ? 158 ASP C CG    1 
ATOM   5318 O OD1   . ASP C 1 158 ? 12.008  50.546  -1.858  1.00 36.25 ? 158 ASP C OD1   1 
ATOM   5319 O OD2   . ASP C 1 158 ? 12.180  49.081  -0.235  1.00 35.19 ? 158 ASP C OD2   1 
ATOM   5320 N N     . LEU C 1 159 ? 16.349  50.943  0.336   1.00 35.39 ? 159 LEU C N     1 
ATOM   5321 C CA    . LEU C 1 159 ? 17.378  50.559  -0.615  1.00 35.95 ? 159 LEU C CA    1 
ATOM   5322 C C     . LEU C 1 159 ? 18.662  50.166  0.093   1.00 36.58 ? 159 LEU C C     1 
ATOM   5323 O O     . LEU C 1 159 ? 19.632  49.782  -0.575  1.00 36.93 ? 159 LEU C O     1 
ATOM   5324 C CB    . LEU C 1 159 ? 17.627  51.702  -1.605  1.00 36.21 ? 159 LEU C CB    1 
ATOM   5325 C CG    . LEU C 1 159 ? 16.999  51.629  -2.997  1.00 35.78 ? 159 LEU C CG    1 
ATOM   5326 C CD1   . LEU C 1 159 ? 15.512  51.342  -2.951  1.00 35.55 ? 159 LEU C CD1   1 
ATOM   5327 C CD2   . LEU C 1 159 ? 17.271  52.913  -3.765  1.00 34.03 ? 159 LEU C CD2   1 
ATOM   5328 N N     . ARG C 1 160 ? 18.678  50.330  1.422   1.00 36.66 ? 160 ARG C N     1 
ATOM   5329 C CA    . ARG C 1 160 ? 19.882  49.925  2.136   1.00 36.84 ? 160 ARG C CA    1 
ATOM   5330 C C     . ARG C 1 160 ? 20.027  48.418  2.005   1.00 37.56 ? 160 ARG C C     1 
ATOM   5331 O O     . ARG C 1 160 ? 19.007  47.740  2.046   1.00 37.38 ? 160 ARG C O     1 
ATOM   5332 C CB    . ARG C 1 160 ? 19.787  50.374  3.602   1.00 35.07 ? 160 ARG C CB    1 
ATOM   5333 C CG    . ARG C 1 160 ? 19.915  51.888  3.597   1.00 37.29 ? 160 ARG C CG    1 
ATOM   5334 C CD    . ARG C 1 160 ? 20.670  52.539  4.723   1.00 35.61 ? 160 ARG C CD    1 
ATOM   5335 N NE    . ARG C 1 160 ? 19.811  52.938  5.819   1.00 33.25 ? 160 ARG C NE    1 
ATOM   5336 C CZ    . ARG C 1 160 ? 19.901  54.054  6.519   1.00 33.32 ? 160 ARG C CZ    1 
ATOM   5337 N NH1   . ARG C 1 160 ? 19.035  54.225  7.518   1.00 34.98 ? 160 ARG C NH1   1 
ATOM   5338 N NH2   . ARG C 1 160 ? 20.783  54.995  6.241   1.00 31.82 ? 160 ARG C NH2   1 
ATOM   5339 N N     . GLY C 1 161 ? 21.216  47.894  1.744   1.00 38.51 ? 161 GLY C N     1 
ATOM   5340 C CA    . GLY C 1 161 ? 21.387  46.453  1.808   1.00 39.80 ? 161 GLY C CA    1 
ATOM   5341 C C     . GLY C 1 161 ? 21.724  45.816  0.482   1.00 40.69 ? 161 GLY C C     1 
ATOM   5342 O O     . GLY C 1 161 ? 21.728  44.581  0.405   1.00 41.33 ? 161 GLY C O     1 
ATOM   5343 N N     . ASN C 1 162 ? 22.030  46.581  -0.565  1.00 41.20 ? 162 ASN C N     1 
ATOM   5344 C CA    . ASN C 1 162 ? 22.423  46.006  -1.842  1.00 41.39 ? 162 ASN C CA    1 
ATOM   5345 C C     . ASN C 1 162 ? 23.924  46.153  -2.055  1.00 41.26 ? 162 ASN C C     1 
ATOM   5346 O O     . ASN C 1 162 ? 24.400  46.191  -3.191  1.00 41.72 ? 162 ASN C O     1 
ATOM   5347 C CB    . ASN C 1 162 ? 21.654  46.621  -3.006  1.00 44.28 ? 162 ASN C CB    1 
ATOM   5348 C CG    . ASN C 1 162 ? 20.167  46.350  -2.896  1.00 46.60 ? 162 ASN C CG    1 
ATOM   5349 O OD1   . ASN C 1 162 ? 19.711  45.656  -1.989  1.00 46.76 ? 162 ASN C OD1   1 
ATOM   5350 N ND2   . ASN C 1 162 ? 19.375  46.895  -3.818  1.00 48.85 ? 162 ASN C ND2   1 
ATOM   5351 N N     . GLY C 1 163 ? 24.672  46.187  -0.958  1.00 40.76 ? 163 GLY C N     1 
ATOM   5352 C CA    . GLY C 1 163 ? 26.123  46.241  -1.049  1.00 40.19 ? 163 GLY C CA    1 
ATOM   5353 C C     . GLY C 1 163 ? 26.631  47.643  -1.325  1.00 39.59 ? 163 GLY C C     1 
ATOM   5354 O O     . GLY C 1 163 ? 27.579  47.821  -2.082  1.00 39.80 ? 163 GLY C O     1 
ATOM   5355 N N     . TYR C 1 164 ? 25.951  48.632  -0.757  1.00 39.11 ? 164 TYR C N     1 
ATOM   5356 C CA    . TYR C 1 164 ? 26.452  50.004  -0.786  1.00 38.27 ? 164 TYR C CA    1 
ATOM   5357 C C     . TYR C 1 164 ? 25.824  50.797  0.345   1.00 37.59 ? 164 TYR C C     1 
ATOM   5358 O O     . TYR C 1 164 ? 24.613  50.869  0.436   1.00 37.77 ? 164 TYR C O     1 
ATOM   5359 C CB    . TYR C 1 164 ? 26.281  50.713  -2.108  1.00 38.29 ? 164 TYR C CB    1 
ATOM   5360 C CG    . TYR C 1 164 ? 24.908  50.772  -2.716  1.00 39.11 ? 164 TYR C CG    1 
ATOM   5361 C CD1   . TYR C 1 164 ? 24.570  49.935  -3.769  1.00 39.62 ? 164 TYR C CD1   1 
ATOM   5362 C CD2   . TYR C 1 164 ? 23.941  51.667  -2.271  1.00 39.37 ? 164 TYR C CD2   1 
ATOM   5363 C CE1   . TYR C 1 164 ? 23.310  49.985  -4.347  1.00 40.19 ? 164 TYR C CE1   1 
ATOM   5364 C CE2   . TYR C 1 164 ? 22.684  51.729  -2.834  1.00 39.48 ? 164 TYR C CE2   1 
ATOM   5365 C CZ    . TYR C 1 164 ? 22.375  50.885  -3.875  1.00 40.26 ? 164 TYR C CZ    1 
ATOM   5366 O OH    . TYR C 1 164 ? 21.134  50.892  -4.479  1.00 41.01 ? 164 TYR C OH    1 
ATOM   5367 N N     . ASP C 1 165 ? 26.595  51.396  1.226   1.00 37.15 ? 165 ASP C N     1 
ATOM   5368 C CA    . ASP C 1 165 ? 25.957  52.191  2.275   1.00 36.75 ? 165 ASP C CA    1 
ATOM   5369 C C     . ASP C 1 165 ? 25.191  53.407  1.790   1.00 36.48 ? 165 ASP C C     1 
ATOM   5370 O O     . ASP C 1 165 ? 25.560  54.106  0.844   1.00 36.98 ? 165 ASP C O     1 
ATOM   5371 C CB    . ASP C 1 165 ? 27.028  52.633  3.266   1.00 38.97 ? 165 ASP C CB    1 
ATOM   5372 C CG    . ASP C 1 165 ? 27.528  51.430  4.042   1.00 39.96 ? 165 ASP C CG    1 
ATOM   5373 O OD1   . ASP C 1 165 ? 28.270  51.687  5.003   1.00 40.28 ? 165 ASP C OD1   1 
ATOM   5374 O OD2   . ASP C 1 165 ? 27.166  50.280  3.716   1.00 42.81 ? 165 ASP C OD2   1 
ATOM   5375 N N     . ILE C 1 166 ? 24.039  53.666  2.427   1.00 35.87 ? 166 ILE C N     1 
ATOM   5376 C CA    . ILE C 1 166 ? 23.246  54.848  2.111   1.00 34.77 ? 166 ILE C CA    1 
ATOM   5377 C C     . ILE C 1 166 ? 23.081  55.718  3.352   1.00 34.33 ? 166 ILE C C     1 
ATOM   5378 O O     . ILE C 1 166 ? 22.575  55.239  4.365   1.00 34.24 ? 166 ILE C O     1 
ATOM   5379 C CB    . ILE C 1 166 ? 21.868  54.512  1.545   1.00 34.40 ? 166 ILE C CB    1 
ATOM   5380 C CG1   . ILE C 1 166 ? 22.030  53.852  0.170   1.00 34.83 ? 166 ILE C CG1   1 
ATOM   5381 C CG2   . ILE C 1 166 ? 21.055  55.794  1.393   1.00 33.92 ? 166 ILE C CG2   1 
ATOM   5382 C CD1   . ILE C 1 166 ? 20.774  53.189  -0.357  1.00 35.33 ? 166 ILE C CD1   1 
ATOM   5383 N N     . ASP C 1 167 ? 23.688  56.900  3.327   1.00 34.08 ? 167 ASP C N     1 
ATOM   5384 C CA    . ASP C 1 167 ? 23.499  57.841  4.443   1.00 33.23 ? 167 ASP C CA    1 
ATOM   5385 C C     . ASP C 1 167 ? 22.316  58.732  4.078   1.00 32.06 ? 167 ASP C C     1 
ATOM   5386 O O     . ASP C 1 167 ? 22.047  58.934  2.888   1.00 32.24 ? 167 ASP C O     1 
ATOM   5387 C CB    . ASP C 1 167 ? 24.740  58.682  4.716   1.00 35.92 ? 167 ASP C CB    1 
ATOM   5388 C CG    . ASP C 1 167 ? 25.689  57.976  5.665   1.00 38.69 ? 167 ASP C CG    1 
ATOM   5389 O OD1   . ASP C 1 167 ? 25.661  56.726  5.711   1.00 40.08 ? 167 ASP C OD1   1 
ATOM   5390 O OD2   . ASP C 1 167 ? 26.463  58.662  6.375   1.00 40.60 ? 167 ASP C OD2   1 
ATOM   5391 N N     . VAL C 1 168 ? 21.563  59.183  5.070   1.00 30.45 ? 168 VAL C N     1 
ATOM   5392 C CA    . VAL C 1 168 ? 20.401  60.024  4.816   1.00 28.54 ? 168 VAL C CA    1 
ATOM   5393 C C     . VAL C 1 168 ? 20.413  61.236  5.734   1.00 27.98 ? 168 VAL C C     1 
ATOM   5394 O O     . VAL C 1 168 ? 20.450  61.083  6.956   1.00 27.99 ? 168 VAL C O     1 
ATOM   5395 C CB    . VAL C 1 168 ? 19.099  59.246  5.035   1.00 27.50 ? 168 VAL C CB    1 
ATOM   5396 C CG1   . VAL C 1 168 ? 17.884  60.158  5.176   1.00 26.90 ? 168 VAL C CG1   1 
ATOM   5397 C CG2   . VAL C 1 168 ? 18.827  58.263  3.903   1.00 27.45 ? 168 VAL C CG2   1 
ATOM   5398 N N     . PHE C 1 169 ? 20.519  62.427  5.156   1.00 27.31 ? 169 PHE C N     1 
ATOM   5399 C CA    . PHE C 1 169 ? 20.416  63.635  5.979   1.00 26.86 ? 169 PHE C CA    1 
ATOM   5400 C C     . PHE C 1 169 ? 19.063  64.299  5.687   1.00 26.72 ? 169 PHE C C     1 
ATOM   5401 O O     . PHE C 1 169 ? 18.832  64.715  4.551   1.00 26.64 ? 169 PHE C O     1 
ATOM   5402 C CB    . PHE C 1 169 ? 21.544  64.611  5.707   1.00 25.85 ? 169 PHE C CB    1 
ATOM   5403 C CG    . PHE C 1 169 ? 22.939  64.121  5.945   1.00 25.39 ? 169 PHE C CG    1 
ATOM   5404 C CD1   . PHE C 1 169 ? 23.502  63.188  5.096   1.00 25.92 ? 169 PHE C CD1   1 
ATOM   5405 C CD2   . PHE C 1 169 ? 23.690  64.607  6.998   1.00 25.46 ? 169 PHE C CD2   1 
ATOM   5406 C CE1   . PHE C 1 169 ? 24.776  62.722  5.290   1.00 27.46 ? 169 PHE C CE1   1 
ATOM   5407 C CE2   . PHE C 1 169 ? 24.973  64.166  7.212   1.00 27.62 ? 169 PHE C CE2   1 
ATOM   5408 C CZ    . PHE C 1 169 ? 25.508  63.218  6.354   1.00 29.73 ? 169 PHE C CZ    1 
ATOM   5409 N N     . SER C 1 170 ? 18.167  64.379  6.661   1.00 26.25 ? 170 SER C N     1 
ATOM   5410 C CA    . SER C 1 170 ? 16.871  64.987  6.462   1.00 26.40 ? 170 SER C CA    1 
ATOM   5411 C C     . SER C 1 170 ? 16.665  66.215  7.343   1.00 26.97 ? 170 SER C C     1 
ATOM   5412 O O     . SER C 1 170 ? 16.966  66.229  8.529   1.00 26.57 ? 170 SER C O     1 
ATOM   5413 C CB    . SER C 1 170 ? 15.720  64.016  6.717   1.00 26.08 ? 170 SER C CB    1 
ATOM   5414 O OG    . SER C 1 170 ? 15.308  64.060  8.077   1.00 23.03 ? 170 SER C OG    1 
ATOM   5415 N N     . TYR C 1 171 ? 16.102  67.251  6.715   1.00 27.56 ? 171 TYR C N     1 
ATOM   5416 C CA    . TYR C 1 171 ? 15.916  68.544  7.348   1.00 27.98 ? 171 TYR C CA    1 
ATOM   5417 C C     . TYR C 1 171 ? 14.449  68.911  7.492   1.00 28.26 ? 171 TYR C C     1 
ATOM   5418 O O     . TYR C 1 171 ? 13.731  69.006  6.501   1.00 28.25 ? 171 TYR C O     1 
ATOM   5419 C CB    . TYR C 1 171 ? 16.561  69.666  6.506   1.00 27.63 ? 171 TYR C CB    1 
ATOM   5420 C CG    . TYR C 1 171 ? 18.034  69.364  6.313   1.00 26.53 ? 171 TYR C CG    1 
ATOM   5421 C CD1   . TYR C 1 171 ? 18.462  68.661  5.199   1.00 26.06 ? 171 TYR C CD1   1 
ATOM   5422 C CD2   . TYR C 1 171 ? 18.943  69.765  7.277   1.00 26.05 ? 171 TYR C CD2   1 
ATOM   5423 C CE1   . TYR C 1 171 ? 19.807  68.373  5.060   1.00 26.35 ? 171 TYR C CE1   1 
ATOM   5424 C CE2   . TYR C 1 171 ? 20.287  69.486  7.124   1.00 26.14 ? 171 TYR C CE2   1 
ATOM   5425 C CZ    . TYR C 1 171 ? 20.709  68.790  6.015   1.00 26.18 ? 171 TYR C CZ    1 
ATOM   5426 O OH    . TYR C 1 171 ? 22.050  68.542  5.916   1.00 26.01 ? 171 TYR C OH    1 
ATOM   5427 N N     . GLY C 1 172 ? 14.048  69.150  8.732   1.00 28.56 ? 172 GLY C N     1 
ATOM   5428 C CA    . GLY C 1 172 ? 12.674  69.509  9.067   1.00 28.40 ? 172 GLY C CA    1 
ATOM   5429 C C     . GLY C 1 172 ? 11.666  68.520  8.520   1.00 28.14 ? 172 GLY C C     1 
ATOM   5430 O O     . GLY C 1 172 ? 10.710  68.911  7.864   1.00 28.31 ? 172 GLY C O     1 
ATOM   5431 N N     . ALA C 1 173 ? 11.908  67.228  8.694   1.00 28.30 ? 173 ALA C N     1 
ATOM   5432 C CA    . ALA C 1 173 ? 11.060  66.197  8.120   1.00 27.86 ? 173 ALA C CA    1 
ATOM   5433 C C     . ALA C 1 173 ? 10.037  65.729  9.147   1.00 27.73 ? 173 ALA C C     1 
ATOM   5434 O O     . ALA C 1 173 ? 10.296  65.707  10.348  1.00 28.18 ? 173 ALA C O     1 
ATOM   5435 C CB    . ALA C 1 173 ? 11.867  65.045  7.561   1.00 25.17 ? 173 ALA C CB    1 
ATOM   5436 N N     . PRO C 1 174 ? 8.819   65.493  8.676   1.00 27.26 ? 174 PRO C N     1 
ATOM   5437 C CA    . PRO C 1 174 ? 7.761   64.974  9.514   1.00 27.29 ? 174 PRO C CA    1 
ATOM   5438 C C     . PRO C 1 174 ? 7.998   63.534  9.947   1.00 27.39 ? 174 PRO C C     1 
ATOM   5439 O O     . PRO C 1 174 ? 8.940   62.873  9.493   1.00 27.73 ? 174 PRO C O     1 
ATOM   5440 C CB    . PRO C 1 174 ? 6.573   65.047  8.557   1.00 27.54 ? 174 PRO C CB    1 
ATOM   5441 C CG    . PRO C 1 174 ? 7.163   64.758  7.211   1.00 27.07 ? 174 PRO C CG    1 
ATOM   5442 C CD    . PRO C 1 174 ? 8.442   65.534  7.241   1.00 27.06 ? 174 PRO C CD    1 
ATOM   5443 N N     . ARG C 1 175 ? 7.128   63.029  10.829  1.00 26.99 ? 175 ARG C N     1 
ATOM   5444 C CA    . ARG C 1 175 ? 7.199   61.630  11.258  1.00 26.26 ? 175 ARG C CA    1 
ATOM   5445 C C     . ARG C 1 175 ? 6.767   60.798  10.053  1.00 26.83 ? 175 ARG C C     1 
ATOM   5446 O O     . ARG C 1 175 ? 5.890   61.300  9.343   1.00 27.34 ? 175 ARG C O     1 
ATOM   5447 C CB    . ARG C 1 175 ? 6.265   61.316  12.412  1.00 20.65 ? 175 ARG C CB    1 
ATOM   5448 C CG    . ARG C 1 175 ? 6.738   61.960  13.693  1.00 19.11 ? 175 ARG C CG    1 
ATOM   5449 C CD    . ARG C 1 175 ? 5.765   61.714  14.824  1.00 20.27 ? 175 ARG C CD    1 
ATOM   5450 N NE    . ARG C 1 175 ? 6.204   62.333  16.074  1.00 20.76 ? 175 ARG C NE    1 
ATOM   5451 C CZ    . ARG C 1 175 ? 5.658   63.420  16.596  1.00 20.93 ? 175 ARG C CZ    1 
ATOM   5452 N NH1   . ARG C 1 175 ? 6.099   63.939  17.732  1.00 21.87 ? 175 ARG C NH1   1 
ATOM   5453 N NH2   . ARG C 1 175 ? 4.636   64.010  15.995  1.00 20.66 ? 175 ARG C NH2   1 
ATOM   5454 N N     . VAL C 1 176 ? 7.388   59.662  9.822   1.00 26.95 ? 176 VAL C N     1 
ATOM   5455 C CA    . VAL C 1 176 ? 7.110   58.900  8.609   1.00 27.03 ? 176 VAL C CA    1 
ATOM   5456 C C     . VAL C 1 176 ? 6.440   57.560  8.839   1.00 27.10 ? 176 VAL C C     1 
ATOM   5457 O O     . VAL C 1 176 ? 5.852   57.010  7.905   1.00 26.35 ? 176 VAL C O     1 
ATOM   5458 C CB    . VAL C 1 176 ? 8.423   58.805  7.815   1.00 26.46 ? 176 VAL C CB    1 
ATOM   5459 C CG1   . VAL C 1 176 ? 9.537   58.174  8.643   1.00 27.73 ? 176 VAL C CG1   1 
ATOM   5460 C CG2   . VAL C 1 176 ? 8.250   58.003  6.545   1.00 28.02 ? 176 VAL C CG2   1 
ATOM   5461 N N     . GLY C 1 177 ? 6.197   57.146  10.080  1.00 27.66 ? 177 GLY C N     1 
ATOM   5462 C CA    . GLY C 1 177 ? 5.571   55.862  10.346  1.00 28.64 ? 177 GLY C CA    1 
ATOM   5463 C C     . GLY C 1 177 ? 5.375   55.562  11.819  1.00 29.63 ? 177 GLY C C     1 
ATOM   5464 O O     . GLY C 1 177 ? 5.538   56.419  12.690  1.00 30.05 ? 177 GLY C O     1 
ATOM   5465 N N     . ASN C 1 178 ? 4.815   54.397  12.123  1.00 30.43 ? 178 ASN C N     1 
ATOM   5466 C CA    . ASN C 1 178 ? 4.614   53.917  13.477  1.00 31.17 ? 178 ASN C CA    1 
ATOM   5467 C C     . ASN C 1 178 ? 5.919   53.632  14.214  1.00 31.83 ? 178 ASN C C     1 
ATOM   5468 O O     . ASN C 1 178 ? 6.979   53.476  13.608  1.00 31.86 ? 178 ASN C O     1 
ATOM   5469 C CB    . ASN C 1 178 ? 3.846   52.599  13.479  1.00 30.86 ? 178 ASN C CB    1 
ATOM   5470 C CG    . ASN C 1 178 ? 4.465   51.488  12.684  1.00 31.55 ? 178 ASN C CG    1 
ATOM   5471 O OD1   . ASN C 1 178 ? 3.800   50.465  12.520  1.00 33.12 ? 178 ASN C OD1   1 
ATOM   5472 N ND2   . ASN C 1 178 ? 5.664   51.597  12.142  1.00 34.03 ? 178 ASN C ND2   1 
ATOM   5473 N N     . ARG C 1 179 ? 5.787   53.277  15.490  1.00 32.50 ? 179 ARG C N     1 
ATOM   5474 C CA    . ARG C 1 179 ? 6.917   52.939  16.337  1.00 33.04 ? 179 ARG C CA    1 
ATOM   5475 C C     . ARG C 1 179 ? 7.738   51.767  15.836  1.00 33.40 ? 179 ARG C C     1 
ATOM   5476 O O     . ARG C 1 179 ? 8.953   51.714  16.036  1.00 33.55 ? 179 ARG C O     1 
ATOM   5477 C CB    . ARG C 1 179 ? 6.463   52.705  17.773  1.00 33.83 ? 179 ARG C CB    1 
ATOM   5478 C CG    . ARG C 1 179 ? 7.611   52.379  18.697  1.00 37.16 ? 179 ARG C CG    1 
ATOM   5479 C CD    . ARG C 1 179 ? 7.495   52.948  20.109  1.00 38.71 ? 179 ARG C CD    1 
ATOM   5480 N NE    . ARG C 1 179 ? 8.633   52.455  20.870  1.00 43.49 ? 179 ARG C NE    1 
ATOM   5481 C CZ    . ARG C 1 179 ? 9.314   53.032  21.845  1.00 46.24 ? 179 ARG C CZ    1 
ATOM   5482 N NH1   . ARG C 1 179 ? 8.949   54.247  22.246  1.00 47.90 ? 179 ARG C NH1   1 
ATOM   5483 N NH2   . ARG C 1 179 ? 10.355  52.424  22.426  1.00 47.30 ? 179 ARG C NH2   1 
ATOM   5484 N N     . ALA C 1 180 ? 7.143   50.777  15.175  1.00 33.88 ? 180 ALA C N     1 
ATOM   5485 C CA    . ALA C 1 180 ? 7.897   49.673  14.592  1.00 33.60 ? 180 ALA C CA    1 
ATOM   5486 C C     . ALA C 1 180 ? 8.858   50.284  13.573  1.00 33.99 ? 180 ALA C C     1 
ATOM   5487 O O     . ALA C 1 180 ? 10.067  50.111  13.723  1.00 34.43 ? 180 ALA C O     1 
ATOM   5488 C CB    . ALA C 1 180 ? 7.027   48.628  13.938  1.00 31.48 ? 180 ALA C CB    1 
ATOM   5489 N N     . PHE C 1 181 ? 8.366   51.127  12.664  1.00 33.94 ? 181 PHE C N     1 
ATOM   5490 C CA    . PHE C 1 181 ? 9.238   51.785  11.703  1.00 33.66 ? 181 PHE C CA    1 
ATOM   5491 C C     . PHE C 1 181 ? 10.240  52.703  12.400  1.00 33.61 ? 181 PHE C C     1 
ATOM   5492 O O     . PHE C 1 181 ? 11.375  52.788  11.945  1.00 33.29 ? 181 PHE C O     1 
ATOM   5493 C CB    . PHE C 1 181 ? 8.459   52.585  10.658  1.00 32.94 ? 181 PHE C CB    1 
ATOM   5494 C CG    . PHE C 1 181 ? 9.169   52.788  9.348   1.00 32.51 ? 181 PHE C CG    1 
ATOM   5495 C CD1   . PHE C 1 181 ? 10.246  51.994  8.983   1.00 32.46 ? 181 PHE C CD1   1 
ATOM   5496 C CD2   . PHE C 1 181 ? 8.760   53.773  8.458   1.00 31.08 ? 181 PHE C CD2   1 
ATOM   5497 C CE1   . PHE C 1 181 ? 10.899  52.169  7.778   1.00 30.69 ? 181 PHE C CE1   1 
ATOM   5498 C CE2   . PHE C 1 181 ? 9.413   53.950  7.252   1.00 29.10 ? 181 PHE C CE2   1 
ATOM   5499 C CZ    . PHE C 1 181 ? 10.476  53.145  6.910   1.00 28.71 ? 181 PHE C CZ    1 
ATOM   5500 N N     . ALA C 1 182 ? 9.790   53.416  13.434  1.00 33.45 ? 182 ALA C N     1 
ATOM   5501 C CA    . ALA C 1 182 ? 10.656  54.286  14.209  1.00 33.33 ? 182 ALA C CA    1 
ATOM   5502 C C     . ALA C 1 182 ? 11.862  53.498  14.718  1.00 33.65 ? 182 ALA C C     1 
ATOM   5503 O O     . ALA C 1 182 ? 12.999  53.869  14.426  1.00 33.43 ? 182 ALA C O     1 
ATOM   5504 C CB    . ALA C 1 182 ? 9.904   54.921  15.363  1.00 31.23 ? 182 ALA C CB    1 
ATOM   5505 N N     . GLU C 1 183 ? 11.598  52.386  15.397  1.00 33.96 ? 183 GLU C N     1 
ATOM   5506 C CA    . GLU C 1 183 ? 12.617  51.506  15.936  1.00 33.99 ? 183 GLU C CA    1 
ATOM   5507 C C     . GLU C 1 183 ? 13.555  50.953  14.876  1.00 33.39 ? 183 GLU C C     1 
ATOM   5508 O O     . GLU C 1 183 ? 14.782  51.048  14.955  1.00 32.78 ? 183 GLU C O     1 
ATOM   5509 C CB    . GLU C 1 183 ? 11.920  50.360  16.674  1.00 37.81 ? 183 GLU C CB    1 
ATOM   5510 C CG    . GLU C 1 183 ? 11.980  50.639  18.169  1.00 43.52 ? 183 GLU C CG    1 
ATOM   5511 C CD    . GLU C 1 183 ? 10.703  50.234  18.882  1.00 46.27 ? 183 GLU C CD    1 
ATOM   5512 O OE1   . GLU C 1 183 ? 10.039  49.278  18.414  1.00 47.58 ? 183 GLU C OE1   1 
ATOM   5513 O OE2   . GLU C 1 183 ? 10.383  50.852  19.923  1.00 46.35 ? 183 GLU C OE2   1 
ATOM   5514 N N     . PHE C 1 184 ? 12.964  50.474  13.790  1.00 32.81 ? 184 PHE C N     1 
ATOM   5515 C CA    . PHE C 1 184 ? 13.714  49.987  12.650  1.00 32.76 ? 184 PHE C CA    1 
ATOM   5516 C C     . PHE C 1 184 ? 14.673  50.997  12.046  1.00 33.19 ? 184 PHE C C     1 
ATOM   5517 O O     . PHE C 1 184 ? 15.801  50.669  11.669  1.00 33.30 ? 184 PHE C O     1 
ATOM   5518 C CB    . PHE C 1 184 ? 12.716  49.546  11.561  1.00 32.02 ? 184 PHE C CB    1 
ATOM   5519 C CG    . PHE C 1 184 ? 13.480  49.010  10.388  1.00 31.60 ? 184 PHE C CG    1 
ATOM   5520 C CD1   . PHE C 1 184 ? 13.588  49.744  9.221   1.00 32.72 ? 184 PHE C CD1   1 
ATOM   5521 C CD2   . PHE C 1 184 ? 14.123  47.787  10.493  1.00 31.52 ? 184 PHE C CD2   1 
ATOM   5522 C CE1   . PHE C 1 184 ? 14.316  49.249  8.146   1.00 32.62 ? 184 PHE C CE1   1 
ATOM   5523 C CE2   . PHE C 1 184 ? 14.855  47.302  9.421   1.00 31.84 ? 184 PHE C CE2   1 
ATOM   5524 C CZ    . PHE C 1 184 ? 14.952  48.026  8.248   1.00 31.52 ? 184 PHE C CZ    1 
ATOM   5525 N N     . LEU C 1 185 ? 14.257  52.252  11.863  1.00 33.51 ? 185 LEU C N     1 
ATOM   5526 C CA    . LEU C 1 185 ? 15.076  53.303  11.285  1.00 33.21 ? 185 LEU C CA    1 
ATOM   5527 C C     . LEU C 1 185 ? 16.178  53.721  12.251  1.00 33.43 ? 185 LEU C C     1 
ATOM   5528 O O     . LEU C 1 185 ? 17.204  54.244  11.822  1.00 33.58 ? 185 LEU C O     1 
ATOM   5529 C CB    . LEU C 1 185 ? 14.266  54.540  10.877  1.00 30.47 ? 185 LEU C CB    1 
ATOM   5530 C CG    . LEU C 1 185 ? 13.343  54.373  9.665   1.00 29.48 ? 185 LEU C CG    1 
ATOM   5531 C CD1   . LEU C 1 185 ? 12.417  55.570  9.537   1.00 29.44 ? 185 LEU C CD1   1 
ATOM   5532 C CD2   . LEU C 1 185 ? 14.082  54.156  8.363   1.00 27.34 ? 185 LEU C CD2   1 
ATOM   5533 N N     . THR C 1 186 ? 15.972  53.459  13.532  1.00 33.52 ? 186 THR C N     1 
ATOM   5534 C CA    . THR C 1 186 ? 16.903  53.818  14.581  1.00 33.95 ? 186 THR C CA    1 
ATOM   5535 C C     . THR C 1 186 ? 18.099  52.882  14.605  1.00 34.43 ? 186 THR C C     1 
ATOM   5536 O O     . THR C 1 186 ? 19.215  53.241  14.931  1.00 34.83 ? 186 THR C O     1 
ATOM   5537 C CB    . THR C 1 186 ? 16.190  53.715  15.949  1.00 33.82 ? 186 THR C CB    1 
ATOM   5538 O OG1   . THR C 1 186 ? 15.041  54.578  15.964  1.00 34.29 ? 186 THR C OG1   1 
ATOM   5539 C CG2   . THR C 1 186 ? 17.110  54.083  17.098  1.00 33.04 ? 186 THR C CG2   1 
ATOM   5540 N N     . VAL C 1 187 ? 17.896  51.658  14.195  1.00 35.06 ? 187 VAL C N     1 
ATOM   5541 C CA    . VAL C 1 187 ? 18.799  50.529  14.297  1.00 34.92 ? 187 VAL C CA    1 
ATOM   5542 C C     . VAL C 1 187 ? 19.286  50.029  12.954  1.00 35.35 ? 187 VAL C C     1 
ATOM   5543 O O     . VAL C 1 187 ? 20.361  49.420  12.937  1.00 36.17 ? 187 VAL C O     1 
ATOM   5544 C CB    . VAL C 1 187 ? 17.914  49.453  14.991  1.00 33.43 ? 187 VAL C CB    1 
ATOM   5545 C CG1   . VAL C 1 187 ? 18.112  48.047  14.514  1.00 34.24 ? 187 VAL C CG1   1 
ATOM   5546 C CG2   . VAL C 1 187 ? 18.043  49.596  16.493  1.00 33.37 ? 187 VAL C CG2   1 
ATOM   5547 N N     . GLN C 1 188 ? 18.533  50.204  11.877  1.00 35.15 ? 188 GLN C N     1 
ATOM   5548 C CA    . GLN C 1 188 ? 18.944  49.691  10.583  1.00 35.53 ? 188 GLN C CA    1 
ATOM   5549 C C     . GLN C 1 188 ? 20.419  49.928  10.324  1.00 35.80 ? 188 GLN C C     1 
ATOM   5550 O O     . GLN C 1 188 ? 20.990  50.938  10.704  1.00 36.45 ? 188 GLN C O     1 
ATOM   5551 C CB    . GLN C 1 188 ? 18.086  50.225  9.439   1.00 36.23 ? 188 GLN C CB    1 
ATOM   5552 C CG    . GLN C 1 188 ? 18.388  49.578  8.088   1.00 34.80 ? 188 GLN C CG    1 
ATOM   5553 C CD    . GLN C 1 188 ? 17.610  50.281  7.002   1.00 34.76 ? 188 GLN C CD    1 
ATOM   5554 O OE1   . GLN C 1 188 ? 17.614  51.515  6.973   1.00 36.14 ? 188 GLN C OE1   1 
ATOM   5555 N NE2   . GLN C 1 188 ? 16.949  49.534  6.137   1.00 34.86 ? 188 GLN C NE2   1 
ATOM   5556 N N     . THR C 1 189 ? 21.029  49.034  9.584   1.00 36.26 ? 189 THR C N     1 
ATOM   5557 C CA    . THR C 1 189 ? 22.474  48.992  9.333   1.00 36.63 ? 189 THR C CA    1 
ATOM   5558 C C     . THR C 1 189 ? 22.767  49.124  7.856   1.00 36.16 ? 189 THR C C     1 
ATOM   5559 O O     . THR C 1 189 ? 21.923  48.719  7.055   1.00 36.97 ? 189 THR C O     1 
ATOM   5560 C CB    . THR C 1 189 ? 22.855  47.601  9.896   1.00 39.03 ? 189 THR C CB    1 
ATOM   5561 O OG1   . THR C 1 189 ? 23.385  47.780  11.216  1.00 40.66 ? 189 THR C OG1   1 
ATOM   5562 C CG2   . THR C 1 189 ? 23.712  46.765  8.980   1.00 38.97 ? 189 THR C CG2   1 
ATOM   5563 N N     . GLY C 1 190 ? 23.815  49.791  7.426   1.00 35.87 ? 190 GLY C N     1 
ATOM   5564 C CA    . GLY C 1 190 ? 24.068  49.920  5.987   1.00 35.88 ? 190 GLY C CA    1 
ATOM   5565 C C     . GLY C 1 190 ? 24.150  51.395  5.609   1.00 35.93 ? 190 GLY C C     1 
ATOM   5566 O O     . GLY C 1 190 ? 24.068  51.720  4.431   1.00 36.21 ? 190 GLY C O     1 
ATOM   5567 N N     . GLY C 1 191 ? 24.139  52.247  6.623   1.00 35.56 ? 191 GLY C N     1 
ATOM   5568 C CA    . GLY C 1 191 ? 24.225  53.687  6.415   1.00 35.55 ? 191 GLY C CA    1 
ATOM   5569 C C     . GLY C 1 191 ? 23.730  54.376  7.693   1.00 35.49 ? 191 GLY C C     1 
ATOM   5570 O O     . GLY C 1 191 ? 23.189  53.670  8.549   1.00 35.19 ? 191 GLY C O     1 
ATOM   5571 N N     . THR C 1 192 ? 23.842  55.700  7.739   1.00 35.17 ? 192 THR C N     1 
ATOM   5572 C CA    . THR C 1 192 ? 23.272  56.415  8.881   1.00 34.95 ? 192 THR C CA    1 
ATOM   5573 C C     . THR C 1 192 ? 22.129  57.345  8.509   1.00 34.58 ? 192 THR C C     1 
ATOM   5574 O O     . THR C 1 192 ? 22.003  57.826  7.376   1.00 35.23 ? 192 THR C O     1 
ATOM   5575 C CB    . THR C 1 192 ? 24.409  57.148  9.606   1.00 35.07 ? 192 THR C CB    1 
ATOM   5576 O OG1   . THR C 1 192 ? 25.135  56.108  10.300  1.00 37.62 ? 192 THR C OG1   1 
ATOM   5577 C CG2   . THR C 1 192 ? 23.937  58.169  10.615  1.00 33.69 ? 192 THR C CG2   1 
ATOM   5578 N N     . LEU C 1 193 ? 21.265  57.623  9.483   1.00 33.41 ? 193 LEU C N     1 
ATOM   5579 C CA    . LEU C 1 193 ? 20.148  58.545  9.316   1.00 31.56 ? 193 LEU C CA    1 
ATOM   5580 C C     . LEU C 1 193 ? 20.348  59.749  10.237  1.00 30.74 ? 193 LEU C C     1 
ATOM   5581 O O     . LEU C 1 193 ? 20.389  59.621  11.453  1.00 29.81 ? 193 LEU C O     1 
ATOM   5582 C CB    . LEU C 1 193 ? 18.822  57.892  9.630   1.00 29.74 ? 193 LEU C CB    1 
ATOM   5583 C CG    . LEU C 1 193 ? 17.480  58.547  9.387   1.00 29.34 ? 193 LEU C CG    1 
ATOM   5584 C CD1   . LEU C 1 193 ? 16.706  58.754  10.679  1.00 28.61 ? 193 LEU C CD1   1 
ATOM   5585 C CD2   . LEU C 1 193 ? 17.546  59.843  8.600   1.00 29.03 ? 193 LEU C CD2   1 
ATOM   5586 N N     . TYR C 1 194 ? 20.591  60.900  9.619   1.00 30.48 ? 194 TYR C N     1 
ATOM   5587 C CA    . TYR C 1 194 ? 20.754  62.150  10.357  1.00 29.85 ? 194 TYR C CA    1 
ATOM   5588 C C     . TYR C 1 194 ? 19.465  62.964  10.299  1.00 28.86 ? 194 TYR C C     1 
ATOM   5589 O O     . TYR C 1 194 ? 19.178  63.525  9.252   1.00 28.61 ? 194 TYR C O     1 
ATOM   5590 C CB    . TYR C 1 194 ? 21.918  62.951  9.792   1.00 30.23 ? 194 TYR C CB    1 
ATOM   5591 C CG    . TYR C 1 194 ? 23.243  62.226  9.848   1.00 30.77 ? 194 TYR C CG    1 
ATOM   5592 C CD1   . TYR C 1 194 ? 24.005  62.259  11.004  1.00 30.96 ? 194 TYR C CD1   1 
ATOM   5593 C CD2   . TYR C 1 194 ? 23.731  61.521  8.753   1.00 30.98 ? 194 TYR C CD2   1 
ATOM   5594 C CE1   . TYR C 1 194 ? 25.223  61.608  11.060  1.00 31.32 ? 194 TYR C CE1   1 
ATOM   5595 C CE2   . TYR C 1 194 ? 24.944  60.872  8.807   1.00 31.07 ? 194 TYR C CE2   1 
ATOM   5596 C CZ    . TYR C 1 194 ? 25.682  60.921  9.963   1.00 31.56 ? 194 TYR C CZ    1 
ATOM   5597 O OH    . TYR C 1 194 ? 26.892  60.267  10.043  1.00 32.79 ? 194 TYR C OH    1 
ATOM   5598 N N     . ARG C 1 195 ? 18.727  63.004  11.397  1.00 27.90 ? 195 ARG C N     1 
ATOM   5599 C CA    . ARG C 1 195 ? 17.437  63.676  11.468  1.00 27.17 ? 195 ARG C CA    1 
ATOM   5600 C C     . ARG C 1 195 ? 17.543  65.057  12.088  1.00 26.40 ? 195 ARG C C     1 
ATOM   5601 O O     . ARG C 1 195 ? 17.557  65.147  13.305  1.00 26.18 ? 195 ARG C O     1 
ATOM   5602 C CB    . ARG C 1 195 ? 16.437  62.893  12.318  1.00 26.17 ? 195 ARG C CB    1 
ATOM   5603 C CG    . ARG C 1 195 ? 15.011  62.823  11.807  1.00 24.90 ? 195 ARG C CG    1 
ATOM   5604 C CD    . ARG C 1 195 ? 14.127  62.121  12.849  1.00 23.03 ? 195 ARG C CD    1 
ATOM   5605 N NE    . ARG C 1 195 ? 13.665  63.076  13.814  1.00 22.72 ? 195 ARG C NE    1 
ATOM   5606 C CZ    . ARG C 1 195 ? 13.492  63.089  15.116  1.00 22.81 ? 195 ARG C CZ    1 
ATOM   5607 N NH1   . ARG C 1 195 ? 13.009  64.224  15.647  1.00 23.83 ? 195 ARG C NH1   1 
ATOM   5608 N NH2   . ARG C 1 195 ? 13.768  62.060  15.891  1.00 19.35 ? 195 ARG C NH2   1 
ATOM   5609 N N     . ILE C 1 196 ? 17.667  66.079  11.260  1.00 26.37 ? 196 ILE C N     1 
ATOM   5610 C CA    . ILE C 1 196 ? 17.908  67.432  11.752  1.00 26.01 ? 196 ILE C CA    1 
ATOM   5611 C C     . ILE C 1 196 ? 16.604  68.211  11.880  1.00 26.30 ? 196 ILE C C     1 
ATOM   5612 O O     . ILE C 1 196 ? 15.733  68.231  11.006  1.00 26.59 ? 196 ILE C O     1 
ATOM   5613 C CB    . ILE C 1 196 ? 18.917  68.197  10.886  1.00 23.51 ? 196 ILE C CB    1 
ATOM   5614 C CG1   . ILE C 1 196 ? 20.298  67.538  10.867  1.00 21.94 ? 196 ILE C CG1   1 
ATOM   5615 C CG2   . ILE C 1 196 ? 19.115  69.634  11.339  1.00 24.11 ? 196 ILE C CG2   1 
ATOM   5616 C CD1   . ILE C 1 196 ? 20.460  66.563  9.721   1.00 21.95 ? 196 ILE C CD1   1 
ATOM   5617 N N     . THR C 1 197 ? 16.429  68.813  13.051  1.00 26.05 ? 197 THR C N     1 
ATOM   5618 C CA    . THR C 1 197 ? 15.256  69.608  13.341  1.00 26.46 ? 197 THR C CA    1 
ATOM   5619 C C     . THR C 1 197 ? 15.698  70.985  13.828  1.00 26.94 ? 197 THR C C     1 
ATOM   5620 O O     . THR C 1 197 ? 16.791  71.153  14.358  1.00 26.91 ? 197 THR C O     1 
ATOM   5621 C CB    . THR C 1 197 ? 14.377  68.999  14.439  1.00 26.40 ? 197 THR C CB    1 
ATOM   5622 O OG1   . THR C 1 197 ? 15.113  69.022  15.670  1.00 26.95 ? 197 THR C OG1   1 
ATOM   5623 C CG2   . THR C 1 197 ? 13.945  67.586  14.112  1.00 26.74 ? 197 THR C CG2   1 
ATOM   5624 N N     . HIS C 1 198 ? 14.863  71.991  13.586  1.00 27.42 ? 198 HIS C N     1 
ATOM   5625 C CA    . HIS C 1 198 ? 15.194  73.352  14.004  1.00 27.43 ? 198 HIS C CA    1 
ATOM   5626 C C     . HIS C 1 198 ? 14.203  73.905  15.011  1.00 27.93 ? 198 HIS C C     1 
ATOM   5627 O O     . HIS C 1 198 ? 13.005  73.975  14.771  1.00 27.49 ? 198 HIS C O     1 
ATOM   5628 C CB    . HIS C 1 198 ? 15.286  74.197  12.747  1.00 27.19 ? 198 HIS C CB    1 
ATOM   5629 C CG    . HIS C 1 198 ? 15.408  75.654  13.009  1.00 29.14 ? 198 HIS C CG    1 
ATOM   5630 N ND1   . HIS C 1 198 ? 16.111  76.163  14.084  1.00 29.79 ? 198 HIS C ND1   1 
ATOM   5631 C CD2   . HIS C 1 198 ? 14.917  76.723  12.348  1.00 29.22 ? 198 HIS C CD2   1 
ATOM   5632 C CE1   . HIS C 1 198 ? 16.006  77.478  14.073  1.00 29.27 ? 198 HIS C CE1   1 
ATOM   5633 N NE2   . HIS C 1 198 ? 15.290  77.849  13.024  1.00 30.23 ? 198 HIS C NE2   1 
ATOM   5634 N N     . THR C 1 199 ? 14.699  74.360  16.158  1.00 28.49 ? 199 THR C N     1 
ATOM   5635 C CA    . THR C 1 199 ? 13.930  74.899  17.256  1.00 29.35 ? 199 THR C CA    1 
ATOM   5636 C C     . THR C 1 199 ? 12.543  74.278  17.376  1.00 29.38 ? 199 THR C C     1 
ATOM   5637 O O     . THR C 1 199 ? 12.377  73.157  17.874  1.00 29.98 ? 199 THR C O     1 
ATOM   5638 C CB    . THR C 1 199 ? 13.768  76.422  17.186  1.00 31.13 ? 199 THR C CB    1 
ATOM   5639 O OG1   . THR C 1 199 ? 13.182  76.792  15.931  1.00 34.02 ? 199 THR C OG1   1 
ATOM   5640 C CG2   . THR C 1 199 ? 15.089  77.154  17.316  1.00 32.16 ? 199 THR C CG2   1 
ATOM   5641 N N     . ASN C 1 200 ? 11.528  75.028  16.988  1.00 29.01 ? 200 ASN C N     1 
ATOM   5642 C CA    . ASN C 1 200 ? 10.178  74.502  17.020  1.00 29.73 ? 200 ASN C CA    1 
ATOM   5643 C C     . ASN C 1 200 ? 9.469   74.558  15.680  1.00 29.11 ? 200 ASN C C     1 
ATOM   5644 O O     . ASN C 1 200 ? 8.363   75.043  15.567  1.00 28.56 ? 200 ASN C O     1 
ATOM   5645 C CB    . ASN C 1 200 ? 9.318   75.170  18.084  1.00 34.45 ? 200 ASN C CB    1 
ATOM   5646 C CG    . ASN C 1 200 ? 9.409   76.672  17.974  1.00 37.19 ? 200 ASN C CG    1 
ATOM   5647 O OD1   . ASN C 1 200 ? 10.260  77.220  17.263  1.00 40.54 ? 200 ASN C OD1   1 
ATOM   5648 N ND2   . ASN C 1 200 ? 8.552   77.421  18.654  1.00 36.98 ? 200 ASN C ND2   1 
ATOM   5649 N N     . ASP C 1 201 ? 10.154  74.057  14.672  1.00 29.38 ? 201 ASP C N     1 
ATOM   5650 C CA    . ASP C 1 201 ? 9.590   73.890  13.340  1.00 29.23 ? 201 ASP C CA    1 
ATOM   5651 C C     . ASP C 1 201 ? 8.370   72.998  13.612  1.00 29.65 ? 201 ASP C C     1 
ATOM   5652 O O     . ASP C 1 201 ? 8.498   71.968  14.295  1.00 29.41 ? 201 ASP C O     1 
ATOM   5653 C CB    . ASP C 1 201 ? 10.584  73.079  12.505  1.00 28.38 ? 201 ASP C CB    1 
ATOM   5654 C CG    . ASP C 1 201 ? 10.123  72.839  11.090  1.00 29.42 ? 201 ASP C CG    1 
ATOM   5655 O OD1   . ASP C 1 201 ? 8.935   73.063  10.762  1.00 29.19 ? 201 ASP C OD1   1 
ATOM   5656 O OD2   . ASP C 1 201 ? 10.999  72.418  10.303  1.00 30.27 ? 201 ASP C OD2   1 
ATOM   5657 N N     . ILE C 1 202 ? 7.218   73.400  13.106  1.00 29.69 ? 202 ILE C N     1 
ATOM   5658 C CA    . ILE C 1 202 ? 6.017   72.598  13.303  1.00 29.92 ? 202 ILE C CA    1 
ATOM   5659 C C     . ILE C 1 202 ? 6.039   71.273  12.552  1.00 30.38 ? 202 ILE C C     1 
ATOM   5660 O O     . ILE C 1 202 ? 5.575   70.238  13.061  1.00 30.18 ? 202 ILE C O     1 
ATOM   5661 C CB    . ILE C 1 202 ? 4.795   73.446  12.915  1.00 29.90 ? 202 ILE C CB    1 
ATOM   5662 C CG1   . ILE C 1 202 ? 3.522   72.600  13.038  1.00 30.57 ? 202 ILE C CG1   1 
ATOM   5663 C CG2   . ILE C 1 202 ? 4.889   74.009  11.513  1.00 29.31 ? 202 ILE C CG2   1 
ATOM   5664 C CD1   . ILE C 1 202 ? 2.301   73.425  13.344  1.00 31.65 ? 202 ILE C CD1   1 
ATOM   5665 N N     . VAL C 1 203 ? 6.724   71.174  11.409  1.00 30.59 ? 203 VAL C N     1 
ATOM   5666 C CA    . VAL C 1 203 ? 6.736   69.978  10.603  1.00 30.83 ? 203 VAL C CA    1 
ATOM   5667 C C     . VAL C 1 203 ? 7.273   68.702  11.188  1.00 31.37 ? 203 VAL C C     1 
ATOM   5668 O O     . VAL C 1 203 ? 6.494   67.723  11.203  1.00 31.49 ? 203 VAL C O     1 
ATOM   5669 C CB    . VAL C 1 203 ? 7.190   70.177  9.154   1.00 30.94 ? 203 VAL C CB    1 
ATOM   5670 C CG1   . VAL C 1 203 ? 6.908   68.928  8.323   1.00 29.90 ? 203 VAL C CG1   1 
ATOM   5671 C CG2   . VAL C 1 203 ? 6.449   71.353  8.520   1.00 31.19 ? 203 VAL C CG2   1 
ATOM   5672 N N     . PRO C 1 204 ? 8.325   68.693  12.006  1.00 31.56 ? 204 PRO C N     1 
ATOM   5673 C CA    . PRO C 1 204 ? 8.773   67.476  12.675  1.00 31.31 ? 204 PRO C CA    1 
ATOM   5674 C C     . PRO C 1 204 ? 7.815   67.049  13.775  1.00 31.09 ? 204 PRO C C     1 
ATOM   5675 O O     . PRO C 1 204 ? 7.928   65.976  14.385  1.00 31.03 ? 204 PRO C O     1 
ATOM   5676 C CB    . PRO C 1 204 ? 10.172  67.787  13.169  1.00 31.16 ? 204 PRO C CB    1 
ATOM   5677 C CG    . PRO C 1 204 ? 10.328  69.248  13.074  1.00 31.48 ? 204 PRO C CG    1 
ATOM   5678 C CD    . PRO C 1 204 ? 9.357   69.749  12.041  1.00 31.50 ? 204 PRO C CD    1 
ATOM   5679 N N     . ARG C 1 205 ? 6.794   67.854  14.068  1.00 30.79 ? 205 ARG C N     1 
ATOM   5680 C CA    . ARG C 1 205 ? 5.783   67.584  15.058  1.00 30.44 ? 205 ARG C CA    1 
ATOM   5681 C C     . ARG C 1 205 ? 4.529   66.959  14.461  1.00 30.19 ? 205 ARG C C     1 
ATOM   5682 O O     . ARG C 1 205 ? 3.537   66.791  15.180  1.00 30.24 ? 205 ARG C O     1 
ATOM   5683 C CB    . ARG C 1 205 ? 5.334   68.792  15.877  1.00 29.74 ? 205 ARG C CB    1 
ATOM   5684 C CG    . ARG C 1 205 ? 6.303   69.905  16.138  1.00 31.07 ? 205 ARG C CG    1 
ATOM   5685 C CD    . ARG C 1 205 ? 6.687   70.065  17.595  1.00 31.17 ? 205 ARG C CD    1 
ATOM   5686 N NE    . ARG C 1 205 ? 6.152   71.305  18.127  1.00 32.53 ? 205 ARG C NE    1 
ATOM   5687 C CZ    . ARG C 1 205 ? 6.769   72.148  18.941  1.00 33.49 ? 205 ARG C CZ    1 
ATOM   5688 N NH1   . ARG C 1 205 ? 6.112   73.243  19.319  1.00 36.05 ? 205 ARG C NH1   1 
ATOM   5689 N NH2   . ARG C 1 205 ? 7.992   72.005  19.410  1.00 31.41 ? 205 ARG C NH2   1 
ATOM   5690 N N     . LEU C 1 206 ? 4.461   66.668  13.179  1.00 30.07 ? 206 LEU C N     1 
ATOM   5691 C CA    . LEU C 1 206 ? 3.313   66.049  12.526  1.00 29.46 ? 206 LEU C CA    1 
ATOM   5692 C C     . LEU C 1 206 ? 3.739   64.795  11.751  1.00 29.70 ? 206 LEU C C     1 
ATOM   5693 O O     . LEU C 1 206 ? 4.807   64.803  11.125  1.00 29.91 ? 206 LEU C O     1 
ATOM   5694 C CB    . LEU C 1 206 ? 2.796   66.975  11.431  1.00 26.96 ? 206 LEU C CB    1 
ATOM   5695 C CG    . LEU C 1 206 ? 1.871   68.142  11.649  1.00 27.33 ? 206 LEU C CG    1 
ATOM   5696 C CD1   . LEU C 1 206 ? 1.621   68.481  13.098  1.00 26.62 ? 206 LEU C CD1   1 
ATOM   5697 C CD2   . LEU C 1 206 ? 2.425   69.359  10.902  1.00 26.78 ? 206 LEU C CD2   1 
ATOM   5698 N N     . PRO C 1 207 ? 2.802   63.872  11.537  1.00 29.52 ? 207 PRO C N     1 
ATOM   5699 C CA    . PRO C 1 207 ? 1.471   63.927  12.109  1.00 29.54 ? 207 PRO C CA    1 
ATOM   5700 C C     . PRO C 1 207 ? 1.529   63.766  13.620  1.00 30.05 ? 207 PRO C C     1 
ATOM   5701 O O     . PRO C 1 207 ? 2.573   63.369  14.133  1.00 30.15 ? 207 PRO C O     1 
ATOM   5702 C CB    . PRO C 1 207 ? 0.773   62.717  11.500  1.00 29.07 ? 207 PRO C CB    1 
ATOM   5703 C CG    . PRO C 1 207 ? 1.487   62.452  10.231  1.00 28.67 ? 207 PRO C CG    1 
ATOM   5704 C CD    . PRO C 1 207 ? 2.921   62.757  10.562  1.00 29.07 ? 207 PRO C CD    1 
ATOM   5705 N N     . PRO C 1 208 ? 0.443   64.079  14.306  1.00 30.61 ? 208 PRO C N     1 
ATOM   5706 C CA    . PRO C 1 208 ? 0.384   63.978  15.752  1.00 31.50 ? 208 PRO C CA    1 
ATOM   5707 C C     . PRO C 1 208 ? 0.743   62.567  16.182  1.00 32.44 ? 208 PRO C C     1 
ATOM   5708 O O     . PRO C 1 208 ? 0.422   61.621  15.452  1.00 33.00 ? 208 PRO C O     1 
ATOM   5709 C CB    . PRO C 1 208 ? -1.056  64.302  16.113  1.00 31.19 ? 208 PRO C CB    1 
ATOM   5710 C CG    . PRO C 1 208 ? -1.700  64.858  14.909  1.00 30.82 ? 208 PRO C CG    1 
ATOM   5711 C CD    . PRO C 1 208 ? -0.839  64.529  13.727  1.00 30.88 ? 208 PRO C CD    1 
ATOM   5712 N N     . ARG C 1 209 ? 1.110   62.354  17.438  1.00 33.39 ? 209 ARG C N     1 
ATOM   5713 C CA    . ARG C 1 209 ? 1.448   60.989  17.856  1.00 34.56 ? 209 ARG C CA    1 
ATOM   5714 C C     . ARG C 1 209 ? 0.198   60.154  18.064  1.00 35.11 ? 209 ARG C C     1 
ATOM   5715 O O     . ARG C 1 209 ? 0.110   58.955  17.789  1.00 35.24 ? 209 ARG C O     1 
ATOM   5716 C CB    . ARG C 1 209 ? 2.343   61.030  19.089  1.00 35.70 ? 209 ARG C CB    1 
ATOM   5717 C CG    . ARG C 1 209 ? 3.679   61.680  18.770  1.00 39.18 ? 209 ARG C CG    1 
ATOM   5718 C CD    . ARG C 1 209 ? 4.706   61.373  19.848  1.00 43.34 ? 209 ARG C CD    1 
ATOM   5719 N NE    . ARG C 1 209 ? 4.599   59.959  20.202  1.00 47.24 ? 209 ARG C NE    1 
ATOM   5720 C CZ    . ARG C 1 209 ? 4.748   59.480  21.434  1.00 49.42 ? 209 ARG C CZ    1 
ATOM   5721 N NH1   . ARG C 1 209 ? 5.032   60.217  22.503  1.00 49.39 ? 209 ARG C NH1   1 
ATOM   5722 N NH2   . ARG C 1 209 ? 4.567   58.166  21.553  1.00 50.22 ? 209 ARG C NH2   1 
ATOM   5723 N N     . GLU C 1 210 ? -0.918  60.815  18.329  1.00 35.55 ? 210 GLU C N     1 
ATOM   5724 C CA    . GLU C 1 210 ? -2.227  60.243  18.513  1.00 35.76 ? 210 GLU C CA    1 
ATOM   5725 C C     . GLU C 1 210 ? -2.685  59.506  17.275  1.00 35.26 ? 210 GLU C C     1 
ATOM   5726 O O     . GLU C 1 210 ? -3.312  58.457  17.425  1.00 36.15 ? 210 GLU C O     1 
ATOM   5727 C CB    . GLU C 1 210 ? -3.264  61.318  18.865  1.00 40.08 ? 210 GLU C CB    1 
ATOM   5728 C CG    . GLU C 1 210 ? -2.848  62.141  20.084  1.00 46.82 ? 210 GLU C CG    1 
ATOM   5729 C CD    . GLU C 1 210 ? -2.005  63.338  19.665  1.00 51.59 ? 210 GLU C CD    1 
ATOM   5730 O OE1   . GLU C 1 210 ? -0.800  63.450  20.003  1.00 52.41 ? 210 GLU C OE1   1 
ATOM   5731 O OE2   . GLU C 1 210 ? -2.568  64.199  18.937  1.00 54.18 ? 210 GLU C OE2   1 
ATOM   5732 N N     . PHE C 1 211 ? -2.239  59.848  16.077  1.00 34.53 ? 211 PHE C N     1 
ATOM   5733 C CA    . PHE C 1 211 ? -2.603  59.104  14.880  1.00 33.68 ? 211 PHE C CA    1 
ATOM   5734 C C     . PHE C 1 211 ? -1.732  57.863  14.752  1.00 33.33 ? 211 PHE C C     1 
ATOM   5735 O O     . PHE C 1 211 ? -1.807  57.175  13.731  1.00 34.14 ? 211 PHE C O     1 
ATOM   5736 C CB    . PHE C 1 211 ? -2.502  59.968  13.627  1.00 33.45 ? 211 PHE C CB    1 
ATOM   5737 C CG    . PHE C 1 211 ? -3.372  61.186  13.577  1.00 33.59 ? 211 PHE C CG    1 
ATOM   5738 C CD1   . PHE C 1 211 ? -3.375  62.019  12.464  1.00 33.30 ? 211 PHE C CD1   1 
ATOM   5739 C CD2   . PHE C 1 211 ? -4.207  61.519  14.631  1.00 33.15 ? 211 PHE C CD2   1 
ATOM   5740 C CE1   . PHE C 1 211 ? -4.180  63.144  12.432  1.00 33.77 ? 211 PHE C CE1   1 
ATOM   5741 C CE2   . PHE C 1 211 ? -5.014  62.631  14.613  1.00 32.55 ? 211 PHE C CE2   1 
ATOM   5742 C CZ    . PHE C 1 211 ? -5.005  63.449  13.505  1.00 33.02 ? 211 PHE C CZ    1 
ATOM   5743 N N     . GLY C 1 212 ? -0.853  57.576  15.694  1.00 32.48 ? 212 GLY C N     1 
ATOM   5744 C CA    . GLY C 1 212 ? 0.001   56.421  15.660  1.00 31.68 ? 212 GLY C CA    1 
ATOM   5745 C C     . GLY C 1 212 ? 1.351   56.641  14.994  1.00 31.09 ? 212 GLY C C     1 
ATOM   5746 O O     . GLY C 1 212 ? 1.946   55.637  14.576  1.00 31.11 ? 212 GLY C O     1 
ATOM   5747 N N     . TYR C 1 213 ? 1.941   57.830  15.095  1.00 30.10 ? 213 TYR C N     1 
ATOM   5748 C CA    . TYR C 1 213 ? 3.242   58.067  14.493  1.00 29.10 ? 213 TYR C CA    1 
ATOM   5749 C C     . TYR C 1 213 ? 4.366   58.237  15.505  1.00 28.65 ? 213 TYR C C     1 
ATOM   5750 O O     . TYR C 1 213 ? 4.129   58.766  16.585  1.00 28.71 ? 213 TYR C O     1 
ATOM   5751 C CB    . TYR C 1 213 ? 3.192   59.347  13.658  1.00 29.02 ? 213 TYR C CB    1 
ATOM   5752 C CG    . TYR C 1 213 ? 2.584   59.105  12.297  1.00 28.23 ? 213 TYR C CG    1 
ATOM   5753 C CD1   . TYR C 1 213 ? 3.389   58.836  11.205  1.00 27.96 ? 213 TYR C CD1   1 
ATOM   5754 C CD2   . TYR C 1 213 ? 1.215   59.147  12.119  1.00 28.04 ? 213 TYR C CD2   1 
ATOM   5755 C CE1   . TYR C 1 213 ? 2.856   58.613  9.955   1.00 27.19 ? 213 TYR C CE1   1 
ATOM   5756 C CE2   . TYR C 1 213 ? 0.668   58.920  10.872  1.00 27.79 ? 213 TYR C CE2   1 
ATOM   5757 C CZ    . TYR C 1 213 ? 1.497   58.657  9.807   1.00 27.47 ? 213 TYR C CZ    1 
ATOM   5758 O OH    . TYR C 1 213 ? 0.921   58.437  8.580   1.00 28.38 ? 213 TYR C OH    1 
ATOM   5759 N N     . SER C 1 214 ? 5.582   57.894  15.085  1.00 27.87 ? 214 SER C N     1 
ATOM   5760 C CA    . SER C 1 214 ? 6.740   57.996  15.950  1.00 26.75 ? 214 SER C CA    1 
ATOM   5761 C C     . SER C 1 214 ? 7.968   58.514  15.221  1.00 26.33 ? 214 SER C C     1 
ATOM   5762 O O     . SER C 1 214 ? 8.150   58.219  14.044  1.00 25.95 ? 214 SER C O     1 
ATOM   5763 C CB    . SER C 1 214 ? 7.063   56.600  16.494  1.00 26.26 ? 214 SER C CB    1 
ATOM   5764 O OG    . SER C 1 214 ? 6.827   56.595  17.886  1.00 28.23 ? 214 SER C OG    1 
ATOM   5765 N N     . HIS C 1 215 ? 8.906   59.038  16.007  1.00 26.03 ? 215 HIS C N     1 
ATOM   5766 C CA    . HIS C 1 215 ? 10.175  59.487  15.450  1.00 25.48 ? 215 HIS C CA    1 
ATOM   5767 C C     . HIS C 1 215 ? 11.319  58.532  15.779  1.00 25.33 ? 215 HIS C C     1 
ATOM   5768 O O     . HIS C 1 215 ? 11.454  58.029  16.881  1.00 24.64 ? 215 HIS C O     1 
ATOM   5769 C CB    . HIS C 1 215 ? 10.483  60.894  15.975  1.00 23.19 ? 215 HIS C CB    1 
ATOM   5770 C CG    . HIS C 1 215 ? 10.191  61.968  14.978  1.00 23.11 ? 215 HIS C CG    1 
ATOM   5771 N ND1   . HIS C 1 215 ? 10.494  61.812  13.645  1.00 24.33 ? 215 HIS C ND1   1 
ATOM   5772 C CD2   . HIS C 1 215 ? 9.640   63.203  15.101  1.00 23.18 ? 215 HIS C CD2   1 
ATOM   5773 C CE1   . HIS C 1 215 ? 10.142  62.912  12.984  1.00 24.77 ? 215 HIS C CE1   1 
ATOM   5774 N NE2   . HIS C 1 215 ? 9.616   63.765  13.850  1.00 23.66 ? 215 HIS C NE2   1 
ATOM   5775 N N     . SER C 1 216 ? 12.180  58.292  14.805  1.00 25.61 ? 216 SER C N     1 
ATOM   5776 C CA    . SER C 1 216 ? 13.376  57.487  14.985  1.00 26.45 ? 216 SER C CA    1 
ATOM   5777 C C     . SER C 1 216 ? 14.395  58.269  15.817  1.00 26.80 ? 216 SER C C     1 
ATOM   5778 O O     . SER C 1 216 ? 14.239  59.473  15.986  1.00 26.66 ? 216 SER C O     1 
ATOM   5779 C CB    . SER C 1 216 ? 13.932  57.207  13.580  1.00 26.24 ? 216 SER C CB    1 
ATOM   5780 O OG    . SER C 1 216 ? 14.412  58.432  13.068  1.00 25.67 ? 216 SER C OG    1 
ATOM   5781 N N     . SER C 1 217 ? 15.422  57.632  16.350  1.00 27.13 ? 217 SER C N     1 
ATOM   5782 C CA    . SER C 1 217 ? 16.446  58.278  17.160  1.00 27.69 ? 217 SER C CA    1 
ATOM   5783 C C     . SER C 1 217 ? 17.820  58.136  16.513  1.00 27.91 ? 217 SER C C     1 
ATOM   5784 O O     . SER C 1 217 ? 18.073  57.168  15.798  1.00 28.13 ? 217 SER C O     1 
ATOM   5785 C CB    . SER C 1 217 ? 16.462  57.584  18.520  1.00 28.34 ? 217 SER C CB    1 
ATOM   5786 O OG    . SER C 1 217 ? 17.536  58.020  19.333  1.00 28.81 ? 217 SER C OG    1 
ATOM   5787 N N     . PRO C 1 218 ? 18.711  59.085  16.728  1.00 27.73 ? 218 PRO C N     1 
ATOM   5788 C CA    . PRO C 1 218 ? 18.466  60.267  17.530  1.00 27.99 ? 218 PRO C CA    1 
ATOM   5789 C C     . PRO C 1 218 ? 17.943  61.439  16.711  1.00 27.98 ? 218 PRO C C     1 
ATOM   5790 O O     . PRO C 1 218 ? 17.621  61.313  15.530  1.00 27.73 ? 218 PRO C O     1 
ATOM   5791 C CB    . PRO C 1 218 ? 19.884  60.576  18.029  1.00 27.90 ? 218 PRO C CB    1 
ATOM   5792 C CG    . PRO C 1 218 ? 20.748  60.250  16.862  1.00 27.78 ? 218 PRO C CG    1 
ATOM   5793 C CD    . PRO C 1 218 ? 20.068  59.124  16.139  1.00 27.78 ? 218 PRO C CD    1 
ATOM   5794 N N     . GLU C 1 219 ? 18.107  62.651  17.216  1.00 27.94 ? 219 GLU C N     1 
ATOM   5795 C CA    . GLU C 1 219 ? 17.662  63.869  16.558  1.00 27.44 ? 219 GLU C CA    1 
ATOM   5796 C C     . GLU C 1 219 ? 18.735  64.920  16.780  1.00 27.71 ? 219 GLU C C     1 
ATOM   5797 O O     . GLU C 1 219 ? 19.204  65.063  17.910  1.00 27.83 ? 219 GLU C O     1 
ATOM   5798 C CB    . GLU C 1 219 ? 16.324  64.303  17.142  1.00 26.89 ? 219 GLU C CB    1 
ATOM   5799 C CG    . GLU C 1 219 ? 16.143  65.742  17.507  1.00 28.45 ? 219 GLU C CG    1 
ATOM   5800 C CD    . GLU C 1 219 ? 14.804  66.195  18.025  1.00 29.28 ? 219 GLU C CD    1 
ATOM   5801 O OE1   . GLU C 1 219 ? 14.146  65.429  18.761  1.00 30.53 ? 219 GLU C OE1   1 
ATOM   5802 O OE2   . GLU C 1 219 ? 14.376  67.337  17.729  1.00 27.93 ? 219 GLU C OE2   1 
ATOM   5803 N N     . TYR C 1 220 ? 19.229  65.482  15.685  1.00 27.96 ? 220 TYR C N     1 
ATOM   5804 C CA    . TYR C 1 220 ? 20.194  66.582  15.818  1.00 28.04 ? 220 TYR C CA    1 
ATOM   5805 C C     . TYR C 1 220 ? 19.381  67.872  15.825  1.00 27.85 ? 220 TYR C C     1 
ATOM   5806 O O     . TYR C 1 220 ? 18.747  68.234  14.841  1.00 27.76 ? 220 TYR C O     1 
ATOM   5807 C CB    . TYR C 1 220 ? 21.264  66.518  14.746  1.00 28.53 ? 220 TYR C CB    1 
ATOM   5808 C CG    . TYR C 1 220 ? 22.168  65.310  14.870  1.00 30.22 ? 220 TYR C CG    1 
ATOM   5809 C CD1   . TYR C 1 220 ? 21.817  64.123  14.233  1.00 30.63 ? 220 TYR C CD1   1 
ATOM   5810 C CD2   . TYR C 1 220 ? 23.350  65.317  15.594  1.00 30.52 ? 220 TYR C CD2   1 
ATOM   5811 C CE1   . TYR C 1 220 ? 22.620  63.010  14.315  1.00 30.64 ? 220 TYR C CE1   1 
ATOM   5812 C CE2   . TYR C 1 220 ? 24.156  64.204  15.681  1.00 30.24 ? 220 TYR C CE2   1 
ATOM   5813 C CZ    . TYR C 1 220 ? 23.788  63.059  15.038  1.00 30.92 ? 220 TYR C CZ    1 
ATOM   5814 O OH    . TYR C 1 220 ? 24.521  61.892  15.059  1.00 32.60 ? 220 TYR C OH    1 
ATOM   5815 N N     . TRP C 1 221 ? 19.235  68.484  16.987  1.00 27.53 ? 221 TRP C N     1 
ATOM   5816 C CA    . TRP C 1 221 ? 18.408  69.666  17.149  1.00 27.99 ? 221 TRP C CA    1 
ATOM   5817 C C     . TRP C 1 221 ? 19.140  70.997  17.030  1.00 27.92 ? 221 TRP C C     1 
ATOM   5818 O O     . TRP C 1 221 ? 19.941  71.373  17.883  1.00 27.89 ? 221 TRP C O     1 
ATOM   5819 C CB    . TRP C 1 221 ? 17.659  69.520  18.474  1.00 28.33 ? 221 TRP C CB    1 
ATOM   5820 C CG    . TRP C 1 221 ? 16.707  70.626  18.804  1.00 29.21 ? 221 TRP C CG    1 
ATOM   5821 C CD1   . TRP C 1 221 ? 15.623  71.015  18.068  1.00 28.44 ? 221 TRP C CD1   1 
ATOM   5822 C CD2   . TRP C 1 221 ? 16.744  71.489  19.947  1.00 29.61 ? 221 TRP C CD2   1 
ATOM   5823 N NE1   . TRP C 1 221 ? 14.989  72.063  18.690  1.00 28.11 ? 221 TRP C NE1   1 
ATOM   5824 C CE2   . TRP C 1 221 ? 15.657  72.377  19.842  1.00 28.94 ? 221 TRP C CE2   1 
ATOM   5825 C CE3   . TRP C 1 221 ? 17.597  71.601  21.049  1.00 31.17 ? 221 TRP C CE3   1 
ATOM   5826 C CZ2   . TRP C 1 221 ? 15.405  73.353  20.800  1.00 29.13 ? 221 TRP C CZ2   1 
ATOM   5827 C CZ3   . TRP C 1 221 ? 17.353  72.589  21.994  1.00 30.84 ? 221 TRP C CZ3   1 
ATOM   5828 C CH2   . TRP C 1 221 ? 16.261  73.436  21.868  1.00 28.87 ? 221 TRP C CH2   1 
ATOM   5829 N N     . ILE C 1 222 ? 18.799  71.793  16.018  1.00 27.72 ? 222 ILE C N     1 
ATOM   5830 C CA    . ILE C 1 222 ? 19.420  73.093  15.796  1.00 27.91 ? 222 ILE C CA    1 
ATOM   5831 C C     . ILE C 1 222 ? 18.717  74.116  16.683  1.00 28.69 ? 222 ILE C C     1 
ATOM   5832 O O     . ILE C 1 222 ? 17.556  74.499  16.506  1.00 28.70 ? 222 ILE C O     1 
ATOM   5833 C CB    . ILE C 1 222 ? 19.344  73.550  14.330  1.00 26.11 ? 222 ILE C CB    1 
ATOM   5834 C CG1   . ILE C 1 222 ? 19.896  72.528  13.344  1.00 25.78 ? 222 ILE C CG1   1 
ATOM   5835 C CG2   . ILE C 1 222 ? 20.026  74.901  14.194  1.00 23.93 ? 222 ILE C CG2   1 
ATOM   5836 C CD1   . ILE C 1 222 ? 19.764  72.924  11.894  1.00 25.84 ? 222 ILE C CD1   1 
ATOM   5837 N N     . LYS C 1 223 ? 19.375  74.622  17.716  1.00 29.31 ? 223 LYS C N     1 
ATOM   5838 C CA    . LYS C 1 223 ? 18.723  75.530  18.649  1.00 29.35 ? 223 LYS C CA    1 
ATOM   5839 C C     . LYS C 1 223 ? 18.875  77.006  18.347  1.00 29.51 ? 223 LYS C C     1 
ATOM   5840 O O     . LYS C 1 223 ? 18.351  77.819  19.109  1.00 29.17 ? 223 LYS C O     1 
ATOM   5841 C CB    . LYS C 1 223 ? 19.235  75.253  20.069  1.00 30.44 ? 223 LYS C CB    1 
ATOM   5842 C CG    . LYS C 1 223 ? 20.715  75.572  20.211  1.00 31.69 ? 223 LYS C CG    1 
ATOM   5843 C CD    . LYS C 1 223 ? 21.138  75.411  21.665  1.00 34.78 ? 223 LYS C CD    1 
ATOM   5844 C CE    . LYS C 1 223 ? 22.019  76.589  22.049  1.00 37.41 ? 223 LYS C CE    1 
ATOM   5845 N NZ    . LYS C 1 223 ? 23.311  76.539  21.303  1.00 39.35 ? 223 LYS C NZ    1 
ATOM   5846 N N     . SER C 1 224 ? 19.691  77.410  17.388  1.00 29.70 ? 224 SER C N     1 
ATOM   5847 C CA    . SER C 1 224 ? 19.899  78.813  17.068  1.00 29.38 ? 224 SER C CA    1 
ATOM   5848 C C     . SER C 1 224 ? 18.629  79.310  16.399  1.00 30.33 ? 224 SER C C     1 
ATOM   5849 O O     . SER C 1 224 ? 17.850  78.513  15.879  1.00 30.71 ? 224 SER C O     1 
ATOM   5850 C CB    . SER C 1 224 ? 21.107  78.979  16.164  1.00 27.46 ? 224 SER C CB    1 
ATOM   5851 O OG    . SER C 1 224 ? 21.084  78.050  15.100  1.00 27.63 ? 224 SER C OG    1 
ATOM   5852 N N     . GLY C 1 225 ? 18.411  80.617  16.376  1.00 30.85 ? 225 GLY C N     1 
ATOM   5853 C CA    . GLY C 1 225 ? 17.161  81.168  15.874  1.00 30.71 ? 225 GLY C CA    1 
ATOM   5854 C C     . GLY C 1 225 ? 17.078  81.202  14.359  1.00 30.67 ? 225 GLY C C     1 
ATOM   5855 O O     . GLY C 1 225 ? 18.028  80.827  13.690  1.00 29.98 ? 225 GLY C O     1 
ATOM   5856 N N     . THR C 1 226 ? 15.941  81.685  13.864  1.00 31.01 ? 226 THR C N     1 
ATOM   5857 C CA    . THR C 1 226 ? 15.711  81.823  12.435  1.00 31.23 ? 226 THR C CA    1 
ATOM   5858 C C     . THR C 1 226 ? 16.410  83.069  11.915  1.00 31.95 ? 226 THR C C     1 
ATOM   5859 O O     . THR C 1 226 ? 16.176  84.160  12.437  1.00 32.50 ? 226 THR C O     1 
ATOM   5860 C CB    . THR C 1 226 ? 14.212  82.076  12.182  1.00 29.99 ? 226 THR C CB    1 
ATOM   5861 O OG1   . THR C 1 226 ? 13.520  80.959  12.731  1.00 29.60 ? 226 THR C OG1   1 
ATOM   5862 C CG2   . THR C 1 226 ? 13.913  82.285  10.710  1.00 30.11 ? 226 THR C CG2   1 
ATOM   5863 N N     . LEU C 1 227 ? 17.207  82.921  10.873  1.00 32.19 ? 227 LEU C N     1 
ATOM   5864 C CA    . LEU C 1 227 ? 17.947  84.022  10.287  1.00 32.53 ? 227 LEU C CA    1 
ATOM   5865 C C     . LEU C 1 227 ? 19.302  84.198  10.966  1.00 33.01 ? 227 LEU C C     1 
ATOM   5866 O O     . LEU C 1 227 ? 20.228  84.593  10.238  1.00 34.13 ? 227 LEU C O     1 
ATOM   5867 C CB    . LEU C 1 227 ? 17.173  85.323  10.173  1.00 29.50 ? 227 LEU C CB    1 
ATOM   5868 C CG    . LEU C 1 227 ? 16.057  85.431  9.138   1.00 27.56 ? 227 LEU C CG    1 
ATOM   5869 C CD1   . LEU C 1 227 ? 15.378  86.786  9.267   1.00 27.28 ? 227 LEU C CD1   1 
ATOM   5870 C CD2   . LEU C 1 227 ? 16.516  85.242  7.709   1.00 26.76 ? 227 LEU C CD2   1 
ATOM   5871 N N     . VAL C 1 228 ? 19.531  83.653  12.151  1.00 32.55 ? 228 VAL C N     1 
ATOM   5872 C CA    . VAL C 1 228 ? 20.881  83.671  12.711  1.00 32.43 ? 228 VAL C CA    1 
ATOM   5873 C C     . VAL C 1 228 ? 21.622  82.462  12.161  1.00 32.45 ? 228 VAL C C     1 
ATOM   5874 O O     . VAL C 1 228 ? 21.042  81.399  11.969  1.00 32.34 ? 228 VAL C O     1 
ATOM   5875 C CB    . VAL C 1 228 ? 20.915  83.798  14.235  1.00 31.52 ? 228 VAL C CB    1 
ATOM   5876 C CG1   . VAL C 1 228 ? 19.532  83.769  14.859  1.00 29.30 ? 228 VAL C CG1   1 
ATOM   5877 C CG2   . VAL C 1 228 ? 21.826  82.805  14.949  1.00 29.82 ? 228 VAL C CG2   1 
ATOM   5878 N N     . PRO C 1 229 ? 22.910  82.608  11.881  1.00 32.56 ? 229 PRO C N     1 
ATOM   5879 C CA    . PRO C 1 229 ? 23.730  81.513  11.389  1.00 32.53 ? 229 PRO C CA    1 
ATOM   5880 C C     . PRO C 1 229 ? 24.104  80.500  12.456  1.00 32.50 ? 229 PRO C C     1 
ATOM   5881 O O     . PRO C 1 229 ? 24.206  80.760  13.651  1.00 32.30 ? 229 PRO C O     1 
ATOM   5882 C CB    . PRO C 1 229 ? 24.937  82.178  10.774  1.00 32.31 ? 229 PRO C CB    1 
ATOM   5883 C CG    . PRO C 1 229 ? 24.795  83.631  11.001  1.00 32.32 ? 229 PRO C CG    1 
ATOM   5884 C CD    . PRO C 1 229 ? 23.680  83.866  11.976  1.00 32.27 ? 229 PRO C CD    1 
ATOM   5885 N N     . VAL C 1 230 ? 24.228  79.253  12.014  1.00 32.75 ? 230 VAL C N     1 
ATOM   5886 C CA    . VAL C 1 230 ? 24.458  78.117  12.891  1.00 32.91 ? 230 VAL C CA    1 
ATOM   5887 C C     . VAL C 1 230 ? 25.951  77.847  13.026  1.00 33.75 ? 230 VAL C C     1 
ATOM   5888 O O     . VAL C 1 230 ? 26.766  78.021  12.123  1.00 33.90 ? 230 VAL C O     1 
ATOM   5889 C CB    . VAL C 1 230 ? 23.705  76.866  12.408  1.00 29.58 ? 230 VAL C CB    1 
ATOM   5890 C CG1   . VAL C 1 230 ? 23.920  75.684  13.339  1.00 29.71 ? 230 VAL C CG1   1 
ATOM   5891 C CG2   . VAL C 1 230 ? 22.219  77.116  12.274  1.00 27.53 ? 230 VAL C CG2   1 
ATOM   5892 N N     . THR C 1 231 ? 26.339  77.500  14.241  1.00 34.18 ? 231 THR C N     1 
ATOM   5893 C CA    . THR C 1 231 ? 27.694  77.151  14.629  1.00 34.97 ? 231 THR C CA    1 
ATOM   5894 C C     . THR C 1 231 ? 27.656  75.753  15.241  1.00 35.96 ? 231 THR C C     1 
ATOM   5895 O O     . THR C 1 231 ? 26.564  75.343  15.672  1.00 36.34 ? 231 THR C O     1 
ATOM   5896 C CB    . THR C 1 231 ? 28.221  78.137  15.679  1.00 33.78 ? 231 THR C CB    1 
ATOM   5897 O OG1   . THR C 1 231 ? 27.533  77.945  16.924  1.00 33.17 ? 231 THR C OG1   1 
ATOM   5898 C CG2   . THR C 1 231 ? 28.028  79.591  15.296  1.00 32.72 ? 231 THR C CG2   1 
ATOM   5899 N N     . ARG C 1 232 ? 28.762  75.015  15.335  1.00 36.38 ? 232 ARG C N     1 
ATOM   5900 C CA    . ARG C 1 232 ? 28.712  73.647  15.825  1.00 36.78 ? 232 ARG C CA    1 
ATOM   5901 C C     . ARG C 1 232 ? 28.306  73.538  17.281  1.00 36.62 ? 232 ARG C C     1 
ATOM   5902 O O     . ARG C 1 232 ? 27.785  72.499  17.720  1.00 36.75 ? 232 ARG C O     1 
ATOM   5903 C CB    . ARG C 1 232 ? 29.972  72.837  15.579  1.00 40.08 ? 232 ARG C CB    1 
ATOM   5904 C CG    . ARG C 1 232 ? 31.253  73.640  15.617  1.00 45.16 ? 232 ARG C CG    1 
ATOM   5905 C CD    . ARG C 1 232 ? 32.396  72.864  14.967  1.00 49.88 ? 232 ARG C CD    1 
ATOM   5906 N NE    . ARG C 1 232 ? 32.972  71.879  15.874  1.00 53.95 ? 232 ARG C NE    1 
ATOM   5907 C CZ    . ARG C 1 232 ? 33.500  72.184  17.059  1.00 55.44 ? 232 ARG C CZ    1 
ATOM   5908 N NH1   . ARG C 1 232 ? 33.977  71.194  17.808  1.00 55.63 ? 232 ARG C NH1   1 
ATOM   5909 N NH2   . ARG C 1 232 ? 33.550  73.438  17.495  1.00 56.26 ? 232 ARG C NH2   1 
ATOM   5910 N N     . ASN C 1 233 ? 28.337  74.654  17.995  1.00 36.33 ? 233 ASN C N     1 
ATOM   5911 C CA    . ASN C 1 233 ? 27.842  74.678  19.355  1.00 36.69 ? 233 ASN C CA    1 
ATOM   5912 C C     . ASN C 1 233 ? 26.342  74.840  19.449  1.00 35.91 ? 233 ASN C C     1 
ATOM   5913 O O     . ASN C 1 233 ? 25.835  74.871  20.570  1.00 35.77 ? 233 ASN C O     1 
ATOM   5914 C CB    . ASN C 1 233 ? 28.589  75.745  20.170  1.00 42.13 ? 233 ASN C CB    1 
ATOM   5915 C CG    . ASN C 1 233 ? 29.769  75.059  20.864  1.00 47.12 ? 233 ASN C CG    1 
ATOM   5916 O OD1   . ASN C 1 233 ? 30.899  74.976  20.359  1.00 48.15 ? 233 ASN C OD1   1 
ATOM   5917 N ND2   . ASN C 1 233 ? 29.440  74.543  22.062  1.00 48.86 ? 233 ASN C ND2   1 
ATOM   5918 N N     . ASP C 1 234 ? 25.607  74.909  18.352  1.00 35.46 ? 234 ASP C N     1 
ATOM   5919 C CA    . ASP C 1 234 ? 24.171  75.112  18.387  1.00 35.16 ? 234 ASP C CA    1 
ATOM   5920 C C     . ASP C 1 234 ? 23.418  73.810  18.131  1.00 34.76 ? 234 ASP C C     1 
ATOM   5921 O O     . ASP C 1 234 ? 22.207  73.759  18.339  1.00 34.54 ? 234 ASP C O     1 
ATOM   5922 C CB    . ASP C 1 234 ? 23.684  76.141  17.368  1.00 35.54 ? 234 ASP C CB    1 
ATOM   5923 C CG    . ASP C 1 234 ? 24.296  77.511  17.542  1.00 36.13 ? 234 ASP C CG    1 
ATOM   5924 O OD1   . ASP C 1 234 ? 24.912  77.989  16.566  1.00 37.73 ? 234 ASP C OD1   1 
ATOM   5925 O OD2   . ASP C 1 234 ? 24.175  78.090  18.637  1.00 36.28 ? 234 ASP C OD2   1 
ATOM   5926 N N     . ILE C 1 235 ? 24.090  72.895  17.445  1.00 34.45 ? 235 ILE C N     1 
ATOM   5927 C CA    . ILE C 1 235 ? 23.461  71.614  17.133  1.00 33.93 ? 235 ILE C CA    1 
ATOM   5928 C C     . ILE C 1 235 ? 23.591  70.683  18.334  1.00 33.85 ? 235 ILE C C     1 
ATOM   5929 O O     . ILE C 1 235 ? 24.694  70.294  18.704  1.00 34.17 ? 235 ILE C O     1 
ATOM   5930 C CB    . ILE C 1 235 ? 24.111  70.941  15.917  1.00 31.84 ? 235 ILE C CB    1 
ATOM   5931 C CG1   . ILE C 1 235 ? 24.053  71.842  14.694  1.00 31.94 ? 235 ILE C CG1   1 
ATOM   5932 C CG2   . ILE C 1 235 ? 23.410  69.611  15.700  1.00 31.65 ? 235 ILE C CG2   1 
ATOM   5933 C CD1   . ILE C 1 235 ? 24.653  71.226  13.442  1.00 32.31 ? 235 ILE C CD1   1 
ATOM   5934 N N     . VAL C 1 236 ? 22.483  70.272  18.910  1.00 33.79 ? 236 VAL C N     1 
ATOM   5935 C CA    . VAL C 1 236 ? 22.498  69.388  20.070  1.00 34.14 ? 236 VAL C CA    1 
ATOM   5936 C C     . VAL C 1 236 ? 22.056  67.980  19.705  1.00 34.07 ? 236 VAL C C     1 
ATOM   5937 O O     . VAL C 1 236 ? 21.043  67.902  19.003  1.00 34.54 ? 236 VAL C O     1 
ATOM   5938 C CB    . VAL C 1 236 ? 21.512  69.946  21.119  1.00 35.11 ? 236 VAL C CB    1 
ATOM   5939 C CG1   . VAL C 1 236 ? 21.416  68.975  22.285  1.00 34.83 ? 236 VAL C CG1   1 
ATOM   5940 C CG2   . VAL C 1 236 ? 21.914  71.328  21.603  1.00 35.10 ? 236 VAL C CG2   1 
ATOM   5941 N N     . LYS C 1 237 ? 22.603  66.904  20.252  1.00 33.84 ? 237 LYS C N     1 
ATOM   5942 C CA    . LYS C 1 237 ? 22.148  65.563  19.859  1.00 33.37 ? 237 LYS C CA    1 
ATOM   5943 C C     . LYS C 1 237 ? 21.178  64.984  20.873  1.00 33.26 ? 237 LYS C C     1 
ATOM   5944 O O     . LYS C 1 237 ? 21.448  64.931  22.067  1.00 33.01 ? 237 LYS C O     1 
ATOM   5945 C CB    . LYS C 1 237 ? 23.348  64.657  19.665  1.00 32.83 ? 237 LYS C CB    1 
ATOM   5946 C CG    . LYS C 1 237 ? 23.156  63.389  18.860  1.00 33.96 ? 237 LYS C CG    1 
ATOM   5947 C CD    . LYS C 1 237 ? 23.857  62.234  19.556  1.00 35.71 ? 237 LYS C CD    1 
ATOM   5948 C CE    . LYS C 1 237 ? 24.491  61.248  18.595  1.00 36.40 ? 237 LYS C CE    1 
ATOM   5949 N NZ    . LYS C 1 237 ? 25.494  60.420  19.345  1.00 38.28 ? 237 LYS C NZ    1 
ATOM   5950 N N     . ILE C 1 238 ? 19.918  64.776  20.498  1.00 33.52 ? 238 ILE C N     1 
ATOM   5951 C CA    . ILE C 1 238 ? 18.928  64.270  21.455  1.00 33.82 ? 238 ILE C CA    1 
ATOM   5952 C C     . ILE C 1 238 ? 18.650  62.802  21.161  1.00 34.23 ? 238 ILE C C     1 
ATOM   5953 O O     . ILE C 1 238 ? 18.364  62.417  20.029  1.00 34.42 ? 238 ILE C O     1 
ATOM   5954 C CB    . ILE C 1 238 ? 17.660  65.122  21.548  1.00 33.25 ? 238 ILE C CB    1 
ATOM   5955 C CG1   . ILE C 1 238 ? 17.836  66.452  22.300  1.00 32.38 ? 238 ILE C CG1   1 
ATOM   5956 C CG2   . ILE C 1 238 ? 16.579  64.366  22.319  1.00 31.55 ? 238 ILE C CG2   1 
ATOM   5957 C CD1   . ILE C 1 238 ? 18.624  67.505  21.584  1.00 33.82 ? 238 ILE C CD1   1 
ATOM   5958 N N     . GLU C 1 239 ? 18.654  61.957  22.192  1.00 34.56 ? 239 GLU C N     1 
ATOM   5959 C CA    . GLU C 1 239 ? 18.594  60.521  22.026  1.00 34.56 ? 239 GLU C CA    1 
ATOM   5960 C C     . GLU C 1 239 ? 17.345  59.864  22.568  1.00 34.41 ? 239 GLU C C     1 
ATOM   5961 O O     . GLU C 1 239 ? 16.592  60.406  23.386  1.00 34.76 ? 239 GLU C O     1 
ATOM   5962 C CB    . GLU C 1 239 ? 19.863  59.922  22.617  1.00 37.48 ? 239 GLU C CB    1 
ATOM   5963 C CG    . GLU C 1 239 ? 20.356  58.747  21.770  1.00 43.26 ? 239 GLU C CG    1 
ATOM   5964 C CD    . GLU C 1 239 ? 21.865  58.822  21.597  1.00 47.23 ? 239 GLU C CD    1 
ATOM   5965 O OE1   . GLU C 1 239 ? 22.499  59.298  22.584  1.00 49.71 ? 239 GLU C OE1   1 
ATOM   5966 O OE2   . GLU C 1 239 ? 22.349  58.431  20.510  1.00 49.29 ? 239 GLU C OE2   1 
ATOM   5967 N N     . GLY C 1 240 ? 16.903  58.823  21.873  1.00 33.86 ? 240 GLY C N     1 
ATOM   5968 C CA    . GLY C 1 240 ? 15.778  58.044  22.316  1.00 33.86 ? 240 GLY C CA    1 
ATOM   5969 C C     . GLY C 1 240 ? 14.527  58.321  21.504  1.00 34.19 ? 240 GLY C C     1 
ATOM   5970 O O     . GLY C 1 240 ? 14.291  59.426  21.023  1.00 34.87 ? 240 GLY C O     1 
ATOM   5971 N N     . ILE C 1 241 ? 13.848  57.230  21.174  1.00 34.00 ? 241 ILE C N     1 
ATOM   5972 C CA    . ILE C 1 241 ? 12.640  57.289  20.362  1.00 34.07 ? 241 ILE C CA    1 
ATOM   5973 C C     . ILE C 1 241 ? 11.568  58.164  20.976  1.00 34.55 ? 241 ILE C C     1 
ATOM   5974 O O     . ILE C 1 241 ? 11.299  58.138  22.179  1.00 34.61 ? 241 ILE C O     1 
ATOM   5975 C CB    . ILE C 1 241 ? 12.183  55.845  20.078  1.00 31.87 ? 241 ILE C CB    1 
ATOM   5976 C CG1   . ILE C 1 241 ? 13.249  55.215  19.183  1.00 31.74 ? 241 ILE C CG1   1 
ATOM   5977 C CG2   . ILE C 1 241 ? 10.799  55.821  19.470  1.00 30.81 ? 241 ILE C CG2   1 
ATOM   5978 C CD1   . ILE C 1 241 ? 12.885  54.003  18.368  1.00 33.51 ? 241 ILE C CD1   1 
ATOM   5979 N N     . ASP C 1 242 ? 11.017  59.091  20.198  1.00 34.71 ? 242 ASP C N     1 
ATOM   5980 C CA    . ASP C 1 242 ? 9.990   60.035  20.591  1.00 35.00 ? 242 ASP C CA    1 
ATOM   5981 C C     . ASP C 1 242 ? 10.408  60.869  21.790  1.00 35.45 ? 242 ASP C C     1 
ATOM   5982 O O     . ASP C 1 242 ? 9.601   61.160  22.657  1.00 35.67 ? 242 ASP C O     1 
ATOM   5983 C CB    . ASP C 1 242 ? 8.634   59.408  20.873  1.00 32.60 ? 242 ASP C CB    1 
ATOM   5984 C CG    . ASP C 1 242 ? 7.836   58.915  19.697  1.00 32.65 ? 242 ASP C CG    1 
ATOM   5985 O OD1   . ASP C 1 242 ? 7.045   57.965  19.910  1.00 31.85 ? 242 ASP C OD1   1 
ATOM   5986 O OD2   . ASP C 1 242 ? 7.929   59.432  18.561  1.00 33.76 ? 242 ASP C OD2   1 
ATOM   5987 N N     . ALA C 1 243 ? 11.681  61.199  21.907  1.00 36.18 ? 243 ALA C N     1 
ATOM   5988 C CA    . ALA C 1 243 ? 12.234  61.926  23.036  1.00 36.31 ? 243 ALA C CA    1 
ATOM   5989 C C     . ALA C 1 243 ? 11.652  63.329  23.049  1.00 36.48 ? 243 ALA C C     1 
ATOM   5990 O O     . ALA C 1 243 ? 11.122  63.754  22.026  1.00 36.92 ? 243 ALA C O     1 
ATOM   5991 C CB    . ALA C 1 243 ? 13.734  62.076  22.866  1.00 37.45 ? 243 ALA C CB    1 
ATOM   5992 N N     . THR C 1 244 ? 11.816  64.004  24.167  1.00 36.42 ? 244 THR C N     1 
ATOM   5993 C CA    . THR C 1 244 ? 11.346  65.394  24.279  1.00 36.31 ? 244 THR C CA    1 
ATOM   5994 C C     . THR C 1 244 ? 12.574  66.211  24.675  1.00 36.20 ? 244 THR C C     1 
ATOM   5995 O O     . THR C 1 244 ? 13.552  65.569  25.052  1.00 36.37 ? 244 THR C O     1 
ATOM   5996 C CB    . THR C 1 244 ? 10.258  65.649  25.323  1.00 34.84 ? 244 THR C CB    1 
ATOM   5997 O OG1   . THR C 1 244 ? 10.716  65.149  26.592  1.00 36.77 ? 244 THR C OG1   1 
ATOM   5998 C CG2   . THR C 1 244 ? 8.969   64.910  25.036  1.00 34.56 ? 244 THR C CG2   1 
ATOM   5999 N N     . GLY C 1 245 ? 12.543  67.522  24.592  1.00 36.15 ? 245 GLY C N     1 
ATOM   6000 C CA    . GLY C 1 245 ? 13.724  68.332  24.879  1.00 36.02 ? 245 GLY C CA    1 
ATOM   6001 C C     . GLY C 1 245 ? 14.284  68.922  23.585  1.00 36.13 ? 245 GLY C C     1 
ATOM   6002 O O     . GLY C 1 245 ? 14.994  69.935  23.559  1.00 36.45 ? 245 GLY C O     1 
ATOM   6003 N N     . GLY C 1 246 ? 14.086  68.197  22.490  1.00 35.79 ? 246 GLY C N     1 
ATOM   6004 C CA    . GLY C 1 246 ? 14.590  68.621  21.194  1.00 35.86 ? 246 GLY C CA    1 
ATOM   6005 C C     . GLY C 1 246 ? 13.490  69.488  20.584  1.00 36.03 ? 246 GLY C C     1 
ATOM   6006 O O     . GLY C 1 246 ? 13.034  70.465  21.172  1.00 36.06 ? 246 GLY C O     1 
ATOM   6007 N N     . ASN C 1 247 ? 13.117  69.108  19.368  1.00 36.11 ? 247 ASN C N     1 
ATOM   6008 C CA    . ASN C 1 247 ? 12.065  69.852  18.674  1.00 36.38 ? 247 ASN C CA    1 
ATOM   6009 C C     . ASN C 1 247 ? 10.722  69.524  19.313  1.00 36.84 ? 247 ASN C C     1 
ATOM   6010 O O     . ASN C 1 247 ? 9.825   70.340  19.473  1.00 37.31 ? 247 ASN C O     1 
ATOM   6011 C CB    . ASN C 1 247 ? 12.047  69.464  17.198  1.00 35.31 ? 247 ASN C CB    1 
ATOM   6012 C CG    . ASN C 1 247 ? 10.802  69.955  16.487  1.00 34.92 ? 247 ASN C CG    1 
ATOM   6013 O OD1   . ASN C 1 247 ? 10.737  71.137  16.139  1.00 33.71 ? 247 ASN C OD1   1 
ATOM   6014 N ND2   . ASN C 1 247 ? 9.816   69.081  16.300  1.00 33.79 ? 247 ASN C ND2   1 
ATOM   6015 N N     . ASN C 1 248 ? 10.490  68.246  19.559  1.00 37.23 ? 248 ASN C N     1 
ATOM   6016 C CA    . ASN C 1 248 ? 9.292   67.758  20.219  1.00 37.37 ? 248 ASN C CA    1 
ATOM   6017 C C     . ASN C 1 248 ? 9.264   68.184  21.679  1.00 37.81 ? 248 ASN C C     1 
ATOM   6018 O O     . ASN C 1 248 ? 9.835   67.589  22.583  1.00 37.71 ? 248 ASN C O     1 
ATOM   6019 C CB    . ASN C 1 248 ? 9.267   66.231  20.153  1.00 37.57 ? 248 ASN C CB    1 
ATOM   6020 C CG    . ASN C 1 248 ? 8.237   65.585  21.046  1.00 37.23 ? 248 ASN C CG    1 
ATOM   6021 O OD1   . ASN C 1 248 ? 7.119   66.051  21.252  1.00 37.47 ? 248 ASN C OD1   1 
ATOM   6022 N ND2   . ASN C 1 248 ? 8.607   64.454  21.625  1.00 37.79 ? 248 ASN C ND2   1 
ATOM   6023 N N     . GLN C 1 249 ? 8.597   69.275  21.957  1.00 38.46 ? 249 GLN C N     1 
ATOM   6024 C CA    . GLN C 1 249 ? 8.379   69.885  23.245  1.00 39.46 ? 249 GLN C CA    1 
ATOM   6025 C C     . GLN C 1 249 ? 7.001   70.565  23.232  1.00 39.85 ? 249 GLN C C     1 
ATOM   6026 O O     . GLN C 1 249 ? 6.534   71.081  22.213  1.00 39.95 ? 249 GLN C O     1 
ATOM   6027 C CB    . GLN C 1 249 ? 9.354   71.000  23.557  1.00 42.12 ? 249 GLN C CB    1 
ATOM   6028 C CG    . GLN C 1 249 ? 10.804  70.638  23.695  1.00 46.29 ? 249 GLN C CG    1 
ATOM   6029 C CD    . GLN C 1 249 ? 11.610  71.810  24.230  1.00 50.41 ? 249 GLN C CD    1 
ATOM   6030 O OE1   . GLN C 1 249 ? 11.620  71.965  25.461  1.00 53.71 ? 249 GLN C OE1   1 
ATOM   6031 N NE2   . GLN C 1 249 ? 12.256  72.591  23.362  1.00 50.94 ? 249 GLN C NE2   1 
ATOM   6032 N N     . PRO C 1 250 ? 6.364   70.612  24.388  1.00 40.19 ? 250 PRO C N     1 
ATOM   6033 C CA    . PRO C 1 250 ? 5.041   71.213  24.524  1.00 40.66 ? 250 PRO C CA    1 
ATOM   6034 C C     . PRO C 1 250 ? 5.070   72.729  24.425  1.00 41.12 ? 250 PRO C C     1 
ATOM   6035 O O     . PRO C 1 250 ? 5.427   73.401  25.404  1.00 41.69 ? 250 PRO C O     1 
ATOM   6036 C CB    . PRO C 1 250 ? 4.626   70.778  25.928  1.00 40.54 ? 250 PRO C CB    1 
ATOM   6037 C CG    . PRO C 1 250 ? 5.931   70.717  26.672  1.00 40.22 ? 250 PRO C CG    1 
ATOM   6038 C CD    . PRO C 1 250 ? 6.872   70.079  25.677  1.00 40.20 ? 250 PRO C CD    1 
ATOM   6039 N N     . ASN C 1 251 ? 4.871   73.284  23.227  1.00 41.07 ? 251 ASN C N     1 
ATOM   6040 C CA    . ASN C 1 251 ? 4.900   74.737  23.076  1.00 40.99 ? 251 ASN C CA    1 
ATOM   6041 C C     . ASN C 1 251 ? 4.450   75.117  21.675  1.00 40.62 ? 251 ASN C C     1 
ATOM   6042 O O     . ASN C 1 251 ? 4.109   74.246  20.872  1.00 41.04 ? 251 ASN C O     1 
ATOM   6043 C CB    . ASN C 1 251 ? 6.264   75.275  23.474  1.00 42.80 ? 251 ASN C CB    1 
ATOM   6044 C CG    . ASN C 1 251 ? 7.455   74.817  22.667  1.00 44.36 ? 251 ASN C CG    1 
ATOM   6045 O OD1   . ASN C 1 251 ? 7.328   74.227  21.589  1.00 45.27 ? 251 ASN C OD1   1 
ATOM   6046 N ND2   . ASN C 1 251 ? 8.641   75.089  23.222  1.00 44.88 ? 251 ASN C ND2   1 
ATOM   6047 N N     . ILE C 1 252 ? 4.242   76.397  21.433  1.00 40.06 ? 252 ILE C N     1 
ATOM   6048 C CA    . ILE C 1 252 ? 3.701   76.874  20.167  1.00 39.10 ? 252 ILE C CA    1 
ATOM   6049 C C     . ILE C 1 252 ? 4.730   76.563  19.094  1.00 37.82 ? 252 ILE C C     1 
ATOM   6050 O O     . ILE C 1 252 ? 5.855   77.005  19.257  1.00 38.41 ? 252 ILE C O     1 
ATOM   6051 C CB    . ILE C 1 252 ? 3.450   78.395  20.201  1.00 41.11 ? 252 ILE C CB    1 
ATOM   6052 C CG1   . ILE C 1 252 ? 2.305   78.715  21.166  1.00 40.78 ? 252 ILE C CG1   1 
ATOM   6053 C CG2   . ILE C 1 252 ? 3.105   78.973  18.837  1.00 42.67 ? 252 ILE C CG2   1 
ATOM   6054 C CD1   . ILE C 1 252 ? 2.709   78.545  22.616  1.00 42.77 ? 252 ILE C CD1   1 
ATOM   6055 N N     . PRO C 1 253 ? 4.360   75.782  18.103  1.00 36.81 ? 253 PRO C N     1 
ATOM   6056 C CA    . PRO C 1 253 ? 5.220   75.554  16.950  1.00 35.93 ? 253 PRO C CA    1 
ATOM   6057 C C     . PRO C 1 253 ? 5.277   76.827  16.112  1.00 34.94 ? 253 PRO C C     1 
ATOM   6058 O O     . PRO C 1 253 ? 4.435   77.706  16.265  1.00 34.69 ? 253 PRO C O     1 
ATOM   6059 C CB    . PRO C 1 253 ? 4.504   74.433  16.209  1.00 36.13 ? 253 PRO C CB    1 
ATOM   6060 C CG    . PRO C 1 253 ? 3.062   74.693  16.492  1.00 36.50 ? 253 PRO C CG    1 
ATOM   6061 C CD    . PRO C 1 253 ? 3.001   75.228  17.902  1.00 36.66 ? 253 PRO C CD    1 
ATOM   6062 N N     . ASP C 1 254 ? 6.222   76.893  15.188  1.00 34.02 ? 254 ASP C N     1 
ATOM   6063 C CA    . ASP C 1 254 ? 6.439   78.076  14.368  1.00 32.80 ? 254 ASP C CA    1 
ATOM   6064 C C     . ASP C 1 254 ? 6.534   77.743  12.895  1.00 31.84 ? 254 ASP C C     1 
ATOM   6065 O O     . ASP C 1 254 ? 6.843   76.586  12.640  1.00 31.83 ? 254 ASP C O     1 
ATOM   6066 C CB    . ASP C 1 254 ? 7.755   78.681  14.858  1.00 33.91 ? 254 ASP C CB    1 
ATOM   6067 C CG    . ASP C 1 254 ? 8.102   79.940  14.100  1.00 35.80 ? 254 ASP C CG    1 
ATOM   6068 O OD1   . ASP C 1 254 ? 7.577   80.998  14.496  1.00 36.88 ? 254 ASP C OD1   1 
ATOM   6069 O OD2   . ASP C 1 254 ? 8.869   79.865  13.120  1.00 38.04 ? 254 ASP C OD2   1 
ATOM   6070 N N     . ILE C 1 255 ? 6.197   78.637  11.974  1.00 31.36 ? 255 ILE C N     1 
ATOM   6071 C CA    . ILE C 1 255 ? 6.264   78.308  10.555  1.00 30.80 ? 255 ILE C CA    1 
ATOM   6072 C C     . ILE C 1 255 ? 7.580   78.658  9.883   1.00 30.16 ? 255 ILE C C     1 
ATOM   6073 O O     . ILE C 1 255 ? 8.261   77.783  9.346   1.00 30.01 ? 255 ILE C O     1 
ATOM   6074 C CB    . ILE C 1 255 ? 5.089   78.872  9.737   1.00 30.52 ? 255 ILE C CB    1 
ATOM   6075 C CG1   . ILE C 1 255 ? 3.748   78.478  10.340  1.00 31.11 ? 255 ILE C CG1   1 
ATOM   6076 C CG2   . ILE C 1 255 ? 5.182   78.421  8.287   1.00 30.27 ? 255 ILE C CG2   1 
ATOM   6077 C CD1   . ILE C 1 255 ? 3.590   77.058  10.797  1.00 32.68 ? 255 ILE C CD1   1 
ATOM   6078 N N     . PRO C 1 256 ? 8.059   79.891  10.020  1.00 29.52 ? 256 PRO C N     1 
ATOM   6079 C CA    . PRO C 1 256 ? 9.285   80.343  9.398   1.00 29.43 ? 256 PRO C CA    1 
ATOM   6080 C C     . PRO C 1 256 ? 10.506  79.552  9.822   1.00 29.52 ? 256 PRO C C     1 
ATOM   6081 O O     . PRO C 1 256 ? 11.404  79.281  9.019   1.00 29.68 ? 256 PRO C O     1 
ATOM   6082 C CB    . PRO C 1 256 ? 9.416   81.805  9.762   1.00 29.31 ? 256 PRO C CB    1 
ATOM   6083 C CG    . PRO C 1 256 ? 8.308   82.142  10.669  1.00 29.04 ? 256 PRO C CG    1 
ATOM   6084 C CD    . PRO C 1 256 ? 7.336   81.005  10.664  1.00 29.28 ? 256 PRO C CD    1 
ATOM   6085 N N     . ALA C 1 257 ? 10.502  79.026  11.046  1.00 29.11 ? 257 ALA C N     1 
ATOM   6086 C CA    . ALA C 1 257 ? 11.547  78.163  11.558  1.00 28.73 ? 257 ALA C CA    1 
ATOM   6087 C C     . ALA C 1 257 ? 11.738  76.954  10.658  1.00 28.36 ? 257 ALA C C     1 
ATOM   6088 O O     . ALA C 1 257 ? 12.840  76.449  10.476  1.00 28.72 ? 257 ALA C O     1 
ATOM   6089 C CB    . ALA C 1 257 ? 11.267  77.731  12.988  1.00 27.88 ? 257 ALA C CB    1 
ATOM   6090 N N     . HIS C 1 258 ? 10.724  76.490  9.958   1.00 28.19 ? 258 HIS C N     1 
ATOM   6091 C CA    . HIS C 1 258 ? 10.833  75.431  8.968   1.00 28.07 ? 258 HIS C CA    1 
ATOM   6092 C C     . HIS C 1 258 ? 11.640  75.874  7.745   1.00 28.63 ? 258 HIS C C     1 
ATOM   6093 O O     . HIS C 1 258 ? 12.185  75.038  6.999   1.00 28.83 ? 258 HIS C O     1 
ATOM   6094 C CB    . HIS C 1 258 ? 9.422   75.081  8.499   1.00 23.51 ? 258 HIS C CB    1 
ATOM   6095 C CG    . HIS C 1 258 ? 9.351   73.881  7.623   1.00 21.34 ? 258 HIS C CG    1 
ATOM   6096 N ND1   . HIS C 1 258 ? 9.696   72.616  8.026   1.00 20.17 ? 258 HIS C ND1   1 
ATOM   6097 C CD2   . HIS C 1 258 ? 8.921   73.774  6.341   1.00 20.96 ? 258 HIS C CD2   1 
ATOM   6098 C CE1   . HIS C 1 258 ? 9.485   71.779  7.024   1.00 20.72 ? 258 HIS C CE1   1 
ATOM   6099 N NE2   . HIS C 1 258 ? 9.016   72.451  5.984   1.00 20.42 ? 258 HIS C NE2   1 
ATOM   6100 N N     . LEU C 1 259 ? 11.638  77.187  7.491   1.00 28.26 ? 259 LEU C N     1 
ATOM   6101 C CA    . LEU C 1 259 ? 12.367  77.696  6.348   1.00 28.57 ? 259 LEU C CA    1 
ATOM   6102 C C     . LEU C 1 259 ? 13.840  77.964  6.600   1.00 28.62 ? 259 LEU C C     1 
ATOM   6103 O O     . LEU C 1 259 ? 14.583  78.114  5.624   1.00 28.56 ? 259 LEU C O     1 
ATOM   6104 C CB    . LEU C 1 259 ? 11.694  78.950  5.811   1.00 29.53 ? 259 LEU C CB    1 
ATOM   6105 C CG    . LEU C 1 259 ? 10.452  78.874  4.930   1.00 28.64 ? 259 LEU C CG    1 
ATOM   6106 C CD1   . LEU C 1 259 ? 10.095  77.448  4.559   1.00 26.05 ? 259 LEU C CD1   1 
ATOM   6107 C CD2   . LEU C 1 259 ? 9.273   79.599  5.564   1.00 28.79 ? 259 LEU C CD2   1 
ATOM   6108 N N     . TRP C 1 260 ? 14.302  77.867  7.834   1.00 28.72 ? 260 TRP C N     1 
ATOM   6109 C CA    . TRP C 1 260 ? 15.672  78.205  8.176   1.00 28.92 ? 260 TRP C CA    1 
ATOM   6110 C C     . TRP C 1 260 ? 16.500  77.036  8.685   1.00 29.25 ? 260 TRP C C     1 
ATOM   6111 O O     . TRP C 1 260 ? 16.584  76.799  9.894   1.00 29.14 ? 260 TRP C O     1 
ATOM   6112 C CB    . TRP C 1 260 ? 15.640  79.337  9.220   1.00 28.84 ? 260 TRP C CB    1 
ATOM   6113 C CG    . TRP C 1 260 ? 17.017  79.897  9.424   1.00 29.00 ? 260 TRP C CG    1 
ATOM   6114 C CD1   . TRP C 1 260 ? 17.892  79.617  10.435  1.00 28.90 ? 260 TRP C CD1   1 
ATOM   6115 C CD2   . TRP C 1 260 ? 17.693  80.781  8.532   1.00 29.18 ? 260 TRP C CD2   1 
ATOM   6116 N NE1   . TRP C 1 260 ? 19.077  80.277  10.225  1.00 29.22 ? 260 TRP C NE1   1 
ATOM   6117 C CE2   . TRP C 1 260 ? 18.981  81.004  9.068   1.00 29.73 ? 260 TRP C CE2   1 
ATOM   6118 C CE3   . TRP C 1 260 ? 17.331  81.418  7.343   1.00 29.38 ? 260 TRP C CE3   1 
ATOM   6119 C CZ2   . TRP C 1 260 ? 19.914  81.830  8.444   1.00 29.22 ? 260 TRP C CZ2   1 
ATOM   6120 C CZ3   . TRP C 1 260 ? 18.251  82.249  6.732   1.00 30.05 ? 260 TRP C CZ3   1 
ATOM   6121 C CH2   . TRP C 1 260 ? 19.524  82.447  7.289   1.00 30.07 ? 260 TRP C CH2   1 
ATOM   6122 N N     . TYR C 1 261 ? 17.147  76.311  7.775   1.00 29.34 ? 261 TYR C N     1 
ATOM   6123 C CA    . TYR C 1 261 ? 17.983  75.179  8.143   1.00 29.67 ? 261 TYR C CA    1 
ATOM   6124 C C     . TYR C 1 261 ? 19.383  75.407  7.629   1.00 30.28 ? 261 TYR C C     1 
ATOM   6125 O O     . TYR C 1 261 ? 19.628  75.174  6.443   1.00 30.42 ? 261 TYR C O     1 
ATOM   6126 C CB    . TYR C 1 261 ? 17.485  73.860  7.539   1.00 28.93 ? 261 TYR C CB    1 
ATOM   6127 C CG    . TYR C 1 261 ? 16.490  73.249  8.502   1.00 27.77 ? 261 TYR C CG    1 
ATOM   6128 C CD1   . TYR C 1 261 ? 15.149  73.569  8.405   1.00 27.21 ? 261 TYR C CD1   1 
ATOM   6129 C CD2   . TYR C 1 261 ? 16.911  72.401  9.509   1.00 27.36 ? 261 TYR C CD2   1 
ATOM   6130 C CE1   . TYR C 1 261 ? 14.224  73.033  9.279   1.00 26.63 ? 261 TYR C CE1   1 
ATOM   6131 C CE2   . TYR C 1 261 ? 15.986  71.849  10.375  1.00 26.91 ? 261 TYR C CE2   1 
ATOM   6132 C CZ    . TYR C 1 261 ? 14.653  72.166  10.254  1.00 26.39 ? 261 TYR C CZ    1 
ATOM   6133 O OH    . TYR C 1 261 ? 13.756  71.632  11.138  1.00 26.02 ? 261 TYR C OH    1 
ATOM   6134 N N     . PHE C 1 262 ? 20.206  76.112  8.399   1.00 31.18 ? 262 PHE C N     1 
ATOM   6135 C CA    . PHE C 1 262 ? 21.531  76.556  7.982   1.00 31.68 ? 262 PHE C CA    1 
ATOM   6136 C C     . PHE C 1 262 ? 21.383  77.819  7.145   1.00 31.75 ? 262 PHE C C     1 
ATOM   6137 O O     . PHE C 1 262 ? 21.951  78.842  7.527   1.00 32.54 ? 262 PHE C O     1 
ATOM   6138 C CB    . PHE C 1 262 ? 22.417  75.490  7.347   1.00 32.48 ? 262 PHE C CB    1 
ATOM   6139 C CG    . PHE C 1 262 ? 22.764  74.422  8.358   1.00 33.36 ? 262 PHE C CG    1 
ATOM   6140 C CD1   . PHE C 1 262 ? 23.761  74.645  9.286   1.00 34.67 ? 262 PHE C CD1   1 
ATOM   6141 C CD2   . PHE C 1 262 ? 22.060  73.232  8.427   1.00 33.20 ? 262 PHE C CD2   1 
ATOM   6142 C CE1   . PHE C 1 262 ? 24.057  73.699  10.254  1.00 34.83 ? 262 PHE C CE1   1 
ATOM   6143 C CE2   . PHE C 1 262 ? 22.344  72.289  9.387   1.00 33.04 ? 262 PHE C CE2   1 
ATOM   6144 C CZ    . PHE C 1 262 ? 23.348  72.517  10.306  1.00 33.72 ? 262 PHE C CZ    1 
ATOM   6145 N N     . GLY C 1 263 ? 20.393  77.918  6.290   1.00 31.62 ? 263 GLY C N     1 
ATOM   6146 C CA    . GLY C 1 263 ? 19.936  79.130  5.649   1.00 31.80 ? 263 GLY C CA    1 
ATOM   6147 C C     . GLY C 1 263 ? 18.521  78.903  5.111   1.00 31.61 ? 263 GLY C C     1 
ATOM   6148 O O     . GLY C 1 263 ? 17.823  77.989  5.544   1.00 32.06 ? 263 GLY C O     1 
ATOM   6149 N N     . LEU C 1 264 ? 18.012  79.846  4.339   1.00 31.36 ? 264 LEU C N     1 
ATOM   6150 C CA    . LEU C 1 264 ? 16.697  79.710  3.735   1.00 30.93 ? 264 LEU C CA    1 
ATOM   6151 C C     . LEU C 1 264 ? 16.661  78.467  2.841   1.00 30.84 ? 264 LEU C C     1 
ATOM   6152 O O     . LEU C 1 264 ? 17.434  78.261  1.908   1.00 30.83 ? 264 LEU C O     1 
ATOM   6153 C CB    . LEU C 1 264 ? 16.257  80.921  2.934   1.00 30.08 ? 264 LEU C CB    1 
ATOM   6154 C CG    . LEU C 1 264 ? 15.644  82.112  3.654   1.00 29.68 ? 264 LEU C CG    1 
ATOM   6155 C CD1   . LEU C 1 264 ? 15.138  83.095  2.603   1.00 31.25 ? 264 LEU C CD1   1 
ATOM   6156 C CD2   . LEU C 1 264 ? 14.496  81.706  4.567   1.00 30.24 ? 264 LEU C CD2   1 
ATOM   6157 N N     . ILE C 1 265 ? 15.632  77.672  3.107   1.00 30.45 ? 265 ILE C N     1 
ATOM   6158 C CA    . ILE C 1 265 ? 15.470  76.383  2.416   1.00 30.16 ? 265 ILE C CA    1 
ATOM   6159 C C     . ILE C 1 265 ? 13.992  76.228  2.132   1.00 30.21 ? 265 ILE C C     1 
ATOM   6160 O O     . ILE C 1 265 ? 13.159  76.633  2.958   1.00 30.65 ? 265 ILE C O     1 
ATOM   6161 C CB    . ILE C 1 265 ? 16.116  75.305  3.284   1.00 29.58 ? 265 ILE C CB    1 
ATOM   6162 C CG1   . ILE C 1 265 ? 15.928  73.880  2.784   1.00 29.14 ? 265 ILE C CG1   1 
ATOM   6163 C CG2   . ILE C 1 265 ? 15.667  75.396  4.739   1.00 30.50 ? 265 ILE C CG2   1 
ATOM   6164 C CD1   . ILE C 1 265 ? 16.766  72.893  3.589   1.00 27.48 ? 265 ILE C CD1   1 
ATOM   6165 N N     . GLY C 1 266 ? 13.590  75.857  0.916   1.00 29.88 ? 266 GLY C N     1 
ATOM   6166 C CA    . GLY C 1 266 ? 12.174  75.840  0.584   1.00 29.24 ? 266 GLY C CA    1 
ATOM   6167 C C     . GLY C 1 266 ? 11.763  77.060  -0.219  1.00 29.20 ? 266 GLY C C     1 
ATOM   6168 O O     . GLY C 1 266 ? 10.849  76.992  -1.053  1.00 28.91 ? 266 GLY C O     1 
ATOM   6169 N N     . THR C 1 267 ? 12.546  78.134  -0.159  1.00 29.10 ? 267 THR C N     1 
ATOM   6170 C CA    . THR C 1 267 ? 12.171  79.373  -0.809  1.00 28.89 ? 267 THR C CA    1 
ATOM   6171 C C     . THR C 1 267 ? 12.885  79.562  -2.136  1.00 29.04 ? 267 THR C C     1 
ATOM   6172 O O     . THR C 1 267 ? 12.884  80.707  -2.614  1.00 29.67 ? 267 THR C O     1 
ATOM   6173 C CB    . THR C 1 267 ? 12.561  80.573  0.082   1.00 27.67 ? 267 THR C CB    1 
ATOM   6174 O OG1   . THR C 1 267 ? 13.990  80.576  0.031   1.00 28.70 ? 267 THR C OG1   1 
ATOM   6175 C CG2   . THR C 1 267 ? 12.116  80.389  1.513   1.00 27.90 ? 267 THR C CG2   1 
ATOM   6176 N N     . CYS C 1 268 ? 13.616  78.602  -2.664  1.00 29.08 ? 268 CYS C N     1 
ATOM   6177 C CA    . CYS C 1 268 ? 14.274  78.845  -3.942  1.00 30.28 ? 268 CYS C CA    1 
ATOM   6178 C C     . CYS C 1 268 ? 13.260  78.862  -5.079  1.00 31.55 ? 268 CYS C C     1 
ATOM   6179 O O     . CYS C 1 268 ? 12.766  77.791  -5.455  1.00 32.26 ? 268 CYS C O     1 
ATOM   6180 C CB    . CYS C 1 268 ? 15.416  77.870  -4.270  1.00 27.66 ? 268 CYS C CB    1 
ATOM   6181 S SG    . CYS C 1 268 ? 16.167  78.151  -5.882  1.00 26.54 ? 268 CYS C SG    1 
ATOM   6182 N N     . LEU C 1 269 ? 13.168  79.975  -5.811  1.00 32.88 ? 269 LEU C N     1 
ATOM   6183 C CA    . LEU C 1 269 ? 12.392  80.002  -7.051  1.00 33.65 ? 269 LEU C CA    1 
ATOM   6184 C C     . LEU C 1 269 ? 13.048  79.091  -8.113  1.00 34.24 ? 269 LEU C C     1 
ATOM   6185 O O     . LEU C 1 269 ? 12.217  78.371  -8.727  1.00 37.79 ? 269 LEU C O     1 
ATOM   6186 C CB    . LEU C 1 269 ? 12.218  81.358  -7.701  1.00 33.54 ? 269 LEU C CB    1 
ATOM   6187 C CG    . LEU C 1 269 ? 10.988  82.208  -7.436  1.00 34.47 ? 269 LEU C CG    1 
ATOM   6188 C CD1   . LEU C 1 269 ? 9.740   81.406  -7.098  1.00 35.65 ? 269 LEU C CD1   1 
ATOM   6189 C CD2   . LEU C 1 269 ? 11.243  83.258  -6.368  1.00 34.26 ? 269 LEU C CD2   1 
HETATM 6190 C C1    . PLC D 2 .   ? -10.180 76.420  6.358   1.00 38.44 ? 601 PLC A C1    1 
HETATM 6191 C C2    . PLC D 2 .   ? -10.939 75.666  5.260   1.00 37.51 ? 601 PLC A C2    1 
HETATM 6192 C C3    . PLC D 2 .   ? -11.805 76.583  4.407   1.00 36.52 ? 601 PLC A C3    1 
HETATM 6193 C C4    . PLC D 2 .   ? -6.090  79.072  6.972   1.00 39.74 ? 601 PLC A C4    1 
HETATM 6194 C C5    . PLC D 2 .   ? -4.773  79.062  6.169   1.00 39.01 ? 601 PLC A C5    1 
HETATM 6195 C C6    . PLC D 2 .   ? -3.201  80.299  4.818   1.00 38.64 ? 601 PLC A C6    1 
HETATM 6196 C C7    . PLC D 2 .   ? -4.260  81.260  6.834   1.00 38.39 ? 601 PLC A C7    1 
HETATM 6197 C C8    . PLC D 2 .   ? -5.480  80.984  4.918   1.00 38.43 ? 601 PLC A C8    1 
HETATM 6198 C "C'"  . PLC D 2 .   ? -9.499  73.898  5.427   1.00 36.36 ? 601 PLC A "C'"  1 
HETATM 6199 C "C1'" . PLC D 2 .   ? -8.197  73.241  4.942   1.00 35.39 ? 601 PLC A "C1'" 1 
HETATM 6200 C "C2'" . PLC D 2 .   ? -8.556  72.069  4.020   1.00 34.07 ? 601 PLC A "C2'" 1 
HETATM 6201 C "C3'" . PLC D 2 .   ? -7.358  71.247  3.557   1.00 33.72 ? 601 PLC A "C3'" 1 
HETATM 6202 C "C4'" . PLC D 2 .   ? -7.524  70.626  2.160   1.00 33.18 ? 601 PLC A "C4'" 1 
HETATM 6203 C "C5'" . PLC D 2 .   ? -6.508  71.215  1.181   1.00 33.13 ? 601 PLC A "C5'" 1 
HETATM 6204 C "C6'" . PLC D 2 .   ? -6.935  72.402  0.313   1.00 32.70 ? 601 PLC A "C6'" 1 
HETATM 6205 C "C7'" . PLC D 2 .   ? -6.000  72.465  -0.920  1.00 32.29 ? 601 PLC A "C7'" 1 
HETATM 6206 C "C8'" . PLC D 2 .   ? -6.421  73.572  -1.866  1.00 32.94 ? 601 PLC A "C8'" 1 
HETATM 6207 C "C9'" . PLC D 2 .   ? -6.125  75.011  -1.409  1.00 33.33 ? 601 PLC A "C9'" 1 
HETATM 6208 C "CA'" . PLC D 2 .   ? -4.622  75.274  -1.170  1.00 32.86 ? 601 PLC A "CA'" 1 
HETATM 6209 C "CB'" . PLC D 2 .   ? -4.268  76.762  -1.125  1.00 32.87 ? 601 PLC A "CB'" 1 
HETATM 6210 C CB    . PLC D 2 .   ? -13.584 75.928  3.032   1.00 35.39 ? 601 PLC A CB    1 
HETATM 6211 C C1B   . PLC D 2 .   ? -14.287 76.921  3.947   1.00 34.06 ? 601 PLC A C1B   1 
HETATM 6212 C C2B   . PLC D 2 .   ? -14.603 78.246  3.242   1.00 32.83 ? 601 PLC A C2B   1 
HETATM 6213 C C3B   . PLC D 2 .   ? -14.170 79.374  4.200   1.00 31.61 ? 601 PLC A C3B   1 
HETATM 6214 C C4B   . PLC D 2 .   ? -15.154 80.532  4.241   1.00 29.88 ? 601 PLC A C4B   1 
HETATM 6215 C C5B   . PLC D 2 .   ? -14.387 81.849  4.415   1.00 29.42 ? 601 PLC A C5B   1 
HETATM 6216 C C6B   . PLC D 2 .   ? -14.270 82.364  5.846   1.00 28.93 ? 601 PLC A C6B   1 
HETATM 6217 C C7B   . PLC D 2 .   ? -12.888 82.942  6.143   1.00 29.29 ? 601 PLC A C7B   1 
HETATM 6218 C C8B   . PLC D 2 .   ? -11.747 81.922  6.212   1.00 29.32 ? 601 PLC A C8B   1 
HETATM 6219 C C9B   . PLC D 2 .   ? -10.494 82.451  6.923   1.00 29.23 ? 601 PLC A C9B   1 
HETATM 6220 C CAA   . PLC D 2 .   ? -9.804  81.398  7.790   1.00 29.50 ? 601 PLC A CAA   1 
HETATM 6221 C CBA   . PLC D 2 .   ? -9.822  81.691  9.300   1.00 29.18 ? 601 PLC A CBA   1 
HETATM 6222 O "O'"  . PLC D 2 .   ? -9.797  73.907  6.605   1.00 36.57 ? 601 PLC A "O'"  1 
HETATM 6223 O OB    . PLC D 2 .   ? -14.169 75.009  2.484   1.00 36.35 ? 601 PLC A OB    1 
HETATM 6224 O O2    . PLC D 2 .   ? -10.076 74.759  4.562   1.00 36.91 ? 601 PLC A O2    1 
HETATM 6225 O O3    . PLC D 2 .   ? -12.274 75.910  3.258   1.00 36.02 ? 601 PLC A O3    1 
HETATM 6226 O O1P   . PLC D 2 .   ? -7.428  76.216  8.179   1.00 42.01 ? 601 PLC A O1P   1 
HETATM 6227 O O2P   . PLC D 2 .   ? -8.848  78.418  7.581   1.00 42.11 ? 601 PLC A O2P   1 
HETATM 6228 O O3P   . PLC D 2 .   ? -8.777  76.350  6.053   1.00 40.71 ? 601 PLC A O3P   1 
HETATM 6229 O O4P   . PLC D 2 .   ? -6.857  78.042  6.374   1.00 41.34 ? 601 PLC A O4P   1 
HETATM 6230 N N     . PLC D 2 .   ? -4.383  80.378  5.679   1.00 38.89 ? 601 PLC A N     1 
HETATM 6231 P P     . PLC D 2 .   ? -7.919  77.163  7.115   1.00 42.98 ? 601 PLC A P     1 
HETATM 6232 C C1    . PLC E 2 .   ? -1.513  85.118  6.174   1.00 39.72 ? 701 PLC B C1    1 
HETATM 6233 C C2    . PLC E 2 .   ? -1.314  86.007  4.949   1.00 38.14 ? 701 PLC B C2    1 
HETATM 6234 C C3    . PLC E 2 .   ? 0.167   86.041  4.551   1.00 36.85 ? 701 PLC B C3    1 
HETATM 6235 C C4    . PLC E 2 .   ? -0.891  80.284  7.327   1.00 42.07 ? 701 PLC B C4    1 
HETATM 6236 C C5    . PLC E 2 .   ? 0.094   79.512  6.400   1.00 41.09 ? 701 PLC B C5    1 
HETATM 6237 C C6    . PLC E 2 .   ? 0.696   77.194  6.099   1.00 40.91 ? 701 PLC B C6    1 
HETATM 6238 C C7    . PLC E 2 .   ? -1.017  77.875  7.728   1.00 40.70 ? 701 PLC B C7    1 
HETATM 6239 C C8    . PLC E 2 .   ? 1.189   78.355  8.198   1.00 40.76 ? 701 PLC B C8    1 
HETATM 6240 C "C'"  . PLC E 2 .   ? -3.446  85.473  4.177   1.00 36.99 ? 701 PLC B "C'"  1 
HETATM 6241 C "C1'" . PLC E 2 .   ? -4.302  84.722  3.146   1.00 36.18 ? 701 PLC B "C1'" 1 
HETATM 6242 C "C2'" . PLC E 2 .   ? -5.234  85.735  2.484   1.00 35.03 ? 701 PLC B "C2'" 1 
HETATM 6243 C "C3'" . PLC E 2 .   ? -5.182  85.674  0.948   1.00 34.47 ? 701 PLC B "C3'" 1 
HETATM 6244 C "C4'" . PLC E 2 .   ? -4.263  84.531  0.449   1.00 34.11 ? 701 PLC B "C4'" 1 
HETATM 6245 C "C5'" . PLC E 2 .   ? -4.301  84.449  -1.072  1.00 34.05 ? 701 PLC B "C5'" 1 
HETATM 6246 C "C6'" . PLC E 2 .   ? -4.874  83.156  -1.637  1.00 33.66 ? 701 PLC B "C6'" 1 
HETATM 6247 C "C7'" . PLC E 2 .   ? -3.762  82.448  -2.444  1.00 33.36 ? 701 PLC B "C7'" 1 
HETATM 6248 C "C8'" . PLC E 2 .   ? -3.383  81.156  -1.691  1.00 33.69 ? 701 PLC B "C8'" 1 
HETATM 6249 C "C9'" . PLC E 2 .   ? -2.308  80.307  -2.372  1.00 33.25 ? 701 PLC B "C9'" 1 
HETATM 6250 C "CA'" . PLC E 2 .   ? -1.741  79.276  -1.391  1.00 33.15 ? 701 PLC B "CA'" 1 
HETATM 6251 C "CB'" . PLC E 2 .   ? -0.385  78.722  -1.850  1.00 33.02 ? 701 PLC B "CB'" 1 
HETATM 6252 C CB    . PLC E 2 .   ? 1.399   87.272  2.966   1.00 35.62 ? 701 PLC B CB    1 
HETATM 6253 C C1B   . PLC E 2 .   ? 2.564   86.880  3.911   1.00 34.23 ? 701 PLC B C1B   1 
HETATM 6254 C C2B   . PLC E 2 .   ? 3.554   88.051  3.840   1.00 32.99 ? 701 PLC B C2B   1 
HETATM 6255 C C3B   . PLC E 2 .   ? 5.033   87.703  3.788   1.00 31.82 ? 701 PLC B C3B   1 
HETATM 6256 C C4B   . PLC E 2 .   ? 5.714   87.650  5.152   1.00 30.75 ? 701 PLC B C4B   1 
HETATM 6257 C C5B   . PLC E 2 .   ? 6.174   86.247  5.521   1.00 30.17 ? 701 PLC B C5B   1 
HETATM 6258 C C6B   . PLC E 2 .   ? 6.396   85.926  6.995   1.00 29.71 ? 701 PLC B C6B   1 
HETATM 6259 C C7B   . PLC E 2 .   ? 6.270   84.413  7.233   1.00 29.87 ? 701 PLC B C7B   1 
HETATM 6260 C C8B   . PLC E 2 .   ? 4.841   83.841  7.274   1.00 29.59 ? 701 PLC B C8B   1 
HETATM 6261 C C9B   . PLC E 2 .   ? 4.474   83.387  8.691   1.00 29.95 ? 701 PLC B C9B   1 
HETATM 6262 C CAA   . PLC E 2 .   ? 3.013   82.983  8.904   1.00 30.51 ? 701 PLC B CAA   1 
HETATM 6263 C CBA   . PLC E 2 .   ? 2.615   82.992  10.401  1.00 30.55 ? 701 PLC B CBA   1 
HETATM 6264 O "O'"  . PLC E 2 .   ? -3.907  85.775  5.248   1.00 37.39 ? 701 PLC B "O'"  1 
HETATM 6265 O OB    . PLC E 2 .   ? 1.580   88.284  2.291   1.00 36.21 ? 701 PLC B OB    1 
HETATM 6266 O O2    . PLC E 2 .   ? -2.158  85.621  3.856   1.00 37.60 ? 701 PLC B O2    1 
HETATM 6267 O O3    . PLC E 2 .   ? 0.241   86.733  3.309   1.00 36.31 ? 701 PLC B O3    1 
HETATM 6268 O O1P   . PLC E 2 .   ? -2.534  83.382  7.773   1.00 43.80 ? 701 PLC B O1P   1 
HETATM 6269 O O2P   . PLC E 2 .   ? -0.014  82.734  8.178   1.00 43.40 ? 701 PLC B O2P   1 
HETATM 6270 O O3P   . PLC E 2 .   ? -0.858  83.853  5.958   1.00 42.13 ? 701 PLC B O3P   1 
HETATM 6271 O O4P   . PLC E 2 .   ? -1.321  81.407  6.591   1.00 43.17 ? 701 PLC B O4P   1 
HETATM 6272 N N     . PLC E 2 .   ? 0.261   78.192  7.070   1.00 41.44 ? 701 PLC B N     1 
HETATM 6273 P P     . PLC E 2 .   ? -1.254  82.862  7.144   1.00 44.57 ? 701 PLC B P     1 
HETATM 6274 C C1    . PLC F 2 .   ? 2.690   73.549  7.904   1.00 38.13 ? 801 PLC C C1    1 
HETATM 6275 C C2    . PLC F 2 .   ? 3.642   72.849  6.944   1.00 36.75 ? 801 PLC C C2    1 
HETATM 6276 C C3    . PLC F 2 .   ? 3.093   71.486  6.532   1.00 35.47 ? 801 PLC C C3    1 
HETATM 6277 C C4    . PLC F 2 .   ? -2.107  74.505  7.552   1.00 40.45 ? 801 PLC C C4    1 
HETATM 6278 C C5    . PLC F 2 .   ? -2.964  75.041  6.389   1.00 39.83 ? 801 PLC C C5    1 
HETATM 6279 C C6    . PLC F 2 .   ? -5.142  75.830  5.782   1.00 39.46 ? 801 PLC C C6    1 
HETATM 6280 C C7    . PLC F 2 .   ? -4.175  76.454  7.939   1.00 39.08 ? 801 PLC C C7    1 
HETATM 6281 C C8    . PLC F 2 .   ? -4.866  74.267  7.597   1.00 39.73 ? 801 PLC C C8    1 
HETATM 6282 C "C'"  . PLC F 2 .   ? 4.344   74.886  6.050   1.00 35.93 ? 801 PLC C "C'"  1 
HETATM 6283 C "C1'" . PLC F 2 .   ? 4.353   75.747  4.773   1.00 34.97 ? 801 PLC C "C1'" 1 
HETATM 6284 C "C2'" . PLC F 2 .   ? 5.787   76.164  4.464   1.00 34.18 ? 801 PLC C "C2'" 1 
HETATM 6285 C "C3'" . PLC F 2 .   ? 6.074   76.371  2.972   1.00 33.64 ? 801 PLC C "C3'" 1 
HETATM 6286 C "C4'" . PLC F 2 .   ? 4.890   75.984  2.082   1.00 33.65 ? 801 PLC C "C4'" 1 
HETATM 6287 C "C5'" . PLC F 2 .   ? 5.290   75.474  0.683   1.00 33.20 ? 801 PLC C "C5'" 1 
HETATM 6288 C "C6'" . PLC F 2 .   ? 4.617   76.335  -0.407  1.00 32.51 ? 801 PLC C "C6'" 1 
HETATM 6289 C "C7'" . PLC F 2 .   ? 3.608   75.521  -1.211  1.00 32.28 ? 801 PLC C "C7'" 1 
HETATM 6290 C "C8'" . PLC F 2 .   ? 2.186   76.054  -1.031  1.00 32.45 ? 801 PLC C "C8'" 1 
HETATM 6291 C "C9'" . PLC F 2 .   ? 1.104   75.007  -1.312  1.00 32.45 ? 801 PLC C "C9'" 1 
HETATM 6292 C "CA'" . PLC F 2 .   ? -0.313  75.499  -0.965  1.00 32.27 ? 801 PLC C "CA'" 1 
HETATM 6293 C "CB'" . PLC F 2 .   ? -1.371  74.747  -1.780  1.00 32.31 ? 801 PLC C "CB'" 1 
HETATM 6294 C CB    . PLC F 2 .   ? 3.918   69.643  5.502   1.00 32.91 ? 801 PLC C CB    1 
HETATM 6295 C C1B   . PLC F 2 .   ? 2.850   69.049  6.457   1.00 31.37 ? 801 PLC C C1B   1 
HETATM 6296 C C2B   . PLC F 2 .   ? 3.128   67.540  6.438   1.00 30.57 ? 801 PLC C C2B   1 
HETATM 6297 C C3B   . PLC F 2 .   ? 1.906   66.650  6.411   1.00 29.66 ? 801 PLC C C3B   1 
HETATM 6298 C C4B   . PLC F 2 .   ? 1.560   65.992  7.744   1.00 28.65 ? 801 PLC C C4B   1 
HETATM 6299 C C5B   . PLC F 2 .   ? 0.049   65.802  7.840   1.00 28.74 ? 801 PLC C C5B   1 
HETATM 6300 C C6B   . PLC F 2 .   ? -0.671  66.312  9.075   1.00 28.41 ? 801 PLC C C6B   1 
HETATM 6301 C C7B   . PLC F 2 .   ? -1.826  67.258  8.756   1.00 28.77 ? 801 PLC C C7B   1 
HETATM 6302 C C8B   . PLC F 2 .   ? -1.471  68.732  8.975   1.00 29.35 ? 801 PLC C C8B   1 
HETATM 6303 C C9B   . PLC F 2 .   ? -2.627  69.610  9.483   1.00 29.82 ? 801 PLC C C9B   1 
HETATM 6304 C CAA   . PLC F 2 .   ? -2.164  71.008  9.926   1.00 30.25 ? 801 PLC C CAA   1 
HETATM 6305 C CBA   . PLC F 2 .   ? -2.405  71.314  11.417  1.00 30.21 ? 801 PLC C CBA   1 
HETATM 6306 O "O'"  . PLC F 2 .   ? 4.162   75.366  7.148   1.00 36.40 ? 801 PLC C "O'"  1 
HETATM 6307 O OB    . PLC F 2 .   ? 4.649   68.886  4.910   1.00 32.97 ? 801 PLC C OB    1 
HETATM 6308 O O2    . PLC F 2 .   ? 3.991   73.619  5.795   1.00 36.49 ? 801 PLC C O2    1 
HETATM 6309 O O3    . PLC F 2 .   ? 3.869   70.968  5.443   1.00 33.78 ? 801 PLC C O3    1 
HETATM 6310 O O1P   . PLC F 2 .   ? 1.175   75.604  8.965   1.00 42.91 ? 801 PLC C O1P   1 
HETATM 6311 O O2P   . PLC F 2 .   ? -0.386  73.516  9.179   1.00 42.72 ? 801 PLC C O2P   1 
HETATM 6312 O O3P   . PLC F 2 .   ? 1.403   73.686  7.294   1.00 40.83 ? 801 PLC C O3P   1 
HETATM 6313 O O4P   . PLC F 2 .   ? -0.819  75.068  7.385   1.00 41.86 ? 801 PLC C O4P   1 
HETATM 6314 N N     . PLC F 2 .   ? -4.288  75.434  6.904   1.00 39.93 ? 801 PLC C N     1 
HETATM 6315 P P     . PLC F 2 .   ? 0.407   74.542  8.205   1.00 43.74 ? 801 PLC C P     1 
HETATM 6316 O O     . HOH G 3 .   ? -16.911 66.302  -2.818  1.00 11.39 ? 602 HOH A O     1 
HETATM 6317 O O     . HOH G 3 .   ? -24.524 76.903  13.512  1.00 16.93 ? 603 HOH A O     1 
HETATM 6318 O O     . HOH G 3 .   ? -22.544 71.542  8.428   1.00 16.47 ? 604 HOH A O     1 
HETATM 6319 O O     . HOH G 3 .   ? -10.474 59.960  -0.477  1.00 31.18 ? 605 HOH A O     1 
HETATM 6320 O O     . HOH G 3 .   ? -23.895 72.072  16.783  1.00 28.39 ? 606 HOH A O     1 
HETATM 6321 O O     . HOH G 3 .   ? -23.551 91.125  -1.422  1.00 53.17 ? 607 HOH A O     1 
HETATM 6322 O O     . HOH G 3 .   ? -22.441 83.531  -12.203 1.00 76.23 ? 608 HOH A O     1 
HETATM 6323 O O     . HOH G 3 .   ? -27.552 63.534  -18.450 1.00 36.45 ? 609 HOH A O     1 
HETATM 6324 O O     . HOH G 3 .   ? -16.838 72.525  -7.138  1.00 23.90 ? 610 HOH A O     1 
HETATM 6325 O O     . HOH G 3 .   ? -37.535 69.033  -8.332  1.00 19.49 ? 611 HOH A O     1 
HETATM 6326 O O     . HOH G 3 .   ? -38.228 68.571  -5.379  1.00 36.33 ? 612 HOH A O     1 
HETATM 6327 O O     . HOH G 3 .   ? -24.155 73.669  5.198   1.00 32.87 ? 613 HOH A O     1 
HETATM 6328 O O     . HOH G 3 .   ? -24.626 52.208  -14.419 1.00 41.92 ? 614 HOH A O     1 
HETATM 6329 O O     . HOH G 3 .   ? -10.995 62.291  -1.657  1.00 17.73 ? 615 HOH A O     1 
HETATM 6330 O O     . HOH G 3 .   ? -29.607 70.550  8.026   1.00 37.81 ? 616 HOH A O     1 
HETATM 6331 O O     . HOH G 3 .   ? -25.241 74.449  14.517  1.00 38.64 ? 617 HOH A O     1 
HETATM 6332 O O     . HOH G 3 .   ? -28.939 67.283  8.768   1.00 44.88 ? 618 HOH A O     1 
HETATM 6333 O O     . HOH G 3 .   ? -33.284 65.430  8.212   1.00 57.79 ? 619 HOH A O     1 
HETATM 6334 O O     . HOH G 3 .   ? -13.287 56.946  1.735   1.00 46.03 ? 620 HOH A O     1 
HETATM 6335 O O     . HOH G 3 .   ? -22.606 50.062  -3.803  1.00 46.08 ? 621 HOH A O     1 
HETATM 6336 O O     . HOH G 3 .   ? -15.844 59.996  10.544  1.00 48.17 ? 622 HOH A O     1 
HETATM 6337 O O     . HOH G 3 .   ? -29.244 54.077  17.813  1.00 56.57 ? 623 HOH A O     1 
HETATM 6338 O O     . HOH G 3 .   ? -9.822  68.562  -11.534 1.00 59.41 ? 624 HOH A O     1 
HETATM 6339 O O     . HOH G 3 .   ? -12.854 56.726  -12.902 1.00 55.53 ? 625 HOH A O     1 
HETATM 6340 O O     . HOH G 3 .   ? -28.097 84.965  10.375  1.00 45.82 ? 626 HOH A O     1 
HETATM 6341 O O     . HOH G 3 .   ? -11.664 52.831  -4.009  1.00 50.53 ? 627 HOH A O     1 
HETATM 6342 O O     . HOH G 3 .   ? -18.170 49.064  -11.171 1.00 59.75 ? 628 HOH A O     1 
HETATM 6343 O O     . HOH G 3 .   ? -23.159 55.910  -18.253 1.00 54.94 ? 629 HOH A O     1 
HETATM 6344 O O     . HOH G 3 .   ? -14.047 68.068  -18.280 1.00 51.39 ? 630 HOH A O     1 
HETATM 6345 O O     . HOH G 3 .   ? -20.586 72.356  -16.890 1.00 40.13 ? 631 HOH A O     1 
HETATM 6346 O O     . HOH G 3 .   ? -13.745 78.385  -13.490 1.00 35.24 ? 632 HOH A O     1 
HETATM 6347 O O     . HOH G 3 .   ? -10.063 72.515  -12.425 1.00 79.12 ? 633 HOH A O     1 
HETATM 6348 O O     . HOH G 3 .   ? -17.219 77.645  -5.800  1.00 50.49 ? 634 HOH A O     1 
HETATM 6349 O O     . HOH G 3 .   ? -16.335 75.413  -7.340  1.00 22.17 ? 635 HOH A O     1 
HETATM 6350 O O     . HOH G 3 .   ? -34.682 80.085  -7.753  1.00 83.13 ? 636 HOH A O     1 
HETATM 6351 O O     . HOH G 3 .   ? -25.406 71.693  3.881   1.00 19.50 ? 637 HOH A O     1 
HETATM 6352 O O     . HOH G 3 .   ? -26.300 74.971  6.552   1.00 26.05 ? 638 HOH A O     1 
HETATM 6353 O O     . HOH G 3 .   ? -26.176 77.945  5.973   1.00 23.20 ? 639 HOH A O     1 
HETATM 6354 O O     . HOH G 3 .   ? -34.805 70.174  3.174   1.00 62.64 ? 640 HOH A O     1 
HETATM 6355 O O     . HOH G 3 .   ? -20.826 74.532  13.396  1.00 43.85 ? 641 HOH A O     1 
HETATM 6356 O O     . HOH G 3 .   ? -12.025 64.326  15.271  1.00 78.84 ? 642 HOH A O     1 
HETATM 6357 O O     . HOH G 3 .   ? -34.863 70.181  12.459  1.00 35.89 ? 643 HOH A O     1 
HETATM 6358 O O     . HOH G 3 .   ? -26.835 72.404  13.980  1.00 28.15 ? 644 HOH A O     1 
HETATM 6359 O O     . HOH G 3 .   ? -32.273 70.783  6.953   1.00 53.04 ? 645 HOH A O     1 
HETATM 6360 O O     . HOH G 3 .   ? -14.764 58.487  12.651  1.00 27.90 ? 646 HOH A O     1 
HETATM 6361 O O     . HOH G 3 .   ? -8.126  53.792  9.912   1.00 53.17 ? 647 HOH A O     1 
HETATM 6362 O O     . HOH G 3 .   ? -16.355 54.513  16.533  1.00 49.93 ? 648 HOH A O     1 
HETATM 6363 O O     . HOH G 3 .   ? -16.108 54.569  8.914   1.00 33.10 ? 649 HOH A O     1 
HETATM 6364 O O     . HOH G 3 .   ? -20.803 77.216  20.113  1.00 65.34 ? 650 HOH A O     1 
HETATM 6365 O O     . HOH G 3 .   ? -21.619 73.157  24.188  1.00 67.39 ? 651 HOH A O     1 
HETATM 6366 O O     . HOH G 3 .   ? -19.970 67.486  22.627  1.00 66.16 ? 652 HOH A O     1 
HETATM 6367 O O     . HOH G 3 .   ? -16.320 68.600  19.094  1.00 40.13 ? 653 HOH A O     1 
HETATM 6368 O O     . HOH G 3 .   ? -16.682 55.509  3.433   1.00 51.59 ? 654 HOH A O     1 
HETATM 6369 O O     . HOH G 3 .   ? -22.302 69.461  6.174   1.00 33.71 ? 655 HOH A O     1 
HETATM 6370 O O     . HOH G 3 .   ? -40.812 68.603  -7.180  1.00 62.71 ? 656 HOH A O     1 
HETATM 6371 O O     . HOH G 3 .   ? -11.811 70.965  1.925   1.00 30.11 ? 657 HOH A O     1 
HETATM 6372 O O     . HOH G 3 .   ? -6.511  67.274  -8.105  1.00 53.82 ? 658 HOH A O     1 
HETATM 6373 O O     . HOH G 3 .   ? -8.450  68.881  -2.155  1.00 28.04 ? 659 HOH A O     1 
HETATM 6374 O O     . HOH G 3 .   ? -18.469 52.170  -10.340 1.00 58.14 ? 660 HOH A O     1 
HETATM 6375 O O     . HOH G 3 .   ? -14.145 72.040  -6.814  1.00 27.79 ? 661 HOH A O     1 
HETATM 6376 O O     . HOH G 3 .   ? -15.407 78.230  -4.052  1.00 57.27 ? 662 HOH A O     1 
HETATM 6377 O O     . HOH G 3 .   ? -27.628 65.094  -21.336 1.00 54.91 ? 663 HOH A O     1 
HETATM 6378 O O     . HOH G 3 .   ? -37.065 60.700  -9.721  1.00 52.39 ? 664 HOH A O     1 
HETATM 6379 O O     . HOH G 3 .   ? -35.263 71.253  -11.044 1.00 58.43 ? 665 HOH A O     1 
HETATM 6380 O O     . HOH G 3 .   ? -26.171 83.460  12.913  1.00 70.76 ? 666 HOH A O     1 
HETATM 6381 O O     . HOH G 3 .   ? -29.428 71.496  14.107  1.00 32.39 ? 667 HOH A O     1 
HETATM 6382 O O     . HOH G 3 .   ? -17.455 70.734  18.469  1.00 55.24 ? 668 HOH A O     1 
HETATM 6383 O O     . HOH G 3 .   ? -15.644 58.638  2.811   1.00 58.85 ? 669 HOH A O     1 
HETATM 6384 O O     . HOH H 3 .   ? -3.572  95.051  -5.393  1.00 17.05 ? 702 HOH B O     1 
HETATM 6385 O O     . HOH H 3 .   ? 5.332   98.220  13.366  1.00 31.79 ? 703 HOH B O     1 
HETATM 6386 O O     . HOH H 3 .   ? 1.009   98.616  6.660   1.00 28.53 ? 704 HOH B O     1 
HETATM 6387 O O     . HOH H 3 .   ? -12.548 92.081  -5.035  1.00 41.55 ? 705 HOH B O     1 
HETATM 6388 O O     . HOH H 3 .   ? 0.119   100.483 15.153  1.00 45.17 ? 706 HOH B O     1 
HETATM 6389 O O     . HOH H 3 .   ? 20.910  89.075  3.052   1.00 60.98 ? 707 HOH B O     1 
HETATM 6390 O O     . HOH H 3 .   ? 15.891  90.200  -10.117 1.00 30.68 ? 708 HOH B O     1 
HETATM 6391 O O     . HOH H 3 .   ? 2.946   103.559 -21.253 1.00 36.26 ? 709 HOH B O     1 
HETATM 6392 O O     . HOH H 3 .   ? 2.383   91.247  -8.213  1.00 18.60 ? 710 HOH B O     1 
HETATM 6393 O O     . HOH H 3 .   ? 10.044  110.667 -10.137 1.00 17.24 ? 711 HOH B O     1 
HETATM 6394 O O     . HOH H 3 .   ? 9.321   112.102 -7.193  1.00 37.14 ? 712 HOH B O     1 
HETATM 6395 O O     . HOH H 3 .   ? 4.665   98.890  4.037   1.00 43.51 ? 713 HOH B O     1 
HETATM 6396 O O     . HOH H 3 .   ? -7.694  107.359 -23.491 1.00 63.10 ? 714 HOH B O     1 
HETATM 6397 O O     . HOH H 3 .   ? -9.744  91.921  -5.339  1.00 22.26 ? 715 HOH B O     1 
HETATM 6398 O O     . HOH H 3 .   ? 3.965   105.263 6.329   1.00 35.16 ? 716 HOH B O     1 
HETATM 6399 O O     . HOH H 3 .   ? 3.588   100.307 13.606  1.00 47.35 ? 717 HOH B O     1 
HETATM 6400 O O     . HOH H 3 .   ? 1.402   106.443 5.716   1.00 37.17 ? 718 HOH B O     1 
HETATM 6401 O O     . HOH H 3 .   ? 0.857   110.560 5.330   1.00 63.23 ? 719 HOH B O     1 
HETATM 6402 O O     . HOH H 3 .   ? -13.243 96.877  -3.268  1.00 67.70 ? 720 HOH B O     1 
HETATM 6403 O O     . HOH H 3 .   ? -13.948 107.306 -10.280 1.00 59.91 ? 721 HOH B O     1 
HETATM 6404 O O     . HOH H 3 .   ? -12.088 98.824  5.719   1.00 34.24 ? 722 HOH B O     1 
HETATM 6405 O O     . HOH H 3 .   ? -12.755 113.830 11.605  1.00 40.52 ? 723 HOH B O     1 
HETATM 6406 O O     . HOH H 3 .   ? -3.647  86.963  -14.432 1.00 74.84 ? 724 HOH B O     1 
HETATM 6407 O O     . HOH H 3 .   ? -11.167 95.536  -20.982 1.00 72.79 ? 725 HOH B O     1 
HETATM 6408 O O     . HOH H 3 .   ? 15.421  97.385  11.761  1.00 61.71 ? 726 HOH B O     1 
HETATM 6409 O O     . HOH H 3 .   ? -16.765 96.385  -10.097 1.00 43.09 ? 727 HOH B O     1 
HETATM 6410 O O     . HOH H 3 .   ? -14.758 102.871 -17.117 1.00 46.26 ? 728 HOH B O     1 
HETATM 6411 O O     . HOH H 3 .   ? -0.879  90.087  -20.079 1.00 67.50 ? 729 HOH B O     1 
HETATM 6412 O O     . HOH H 3 .   ? 6.601   93.501  -17.473 1.00 54.85 ? 730 HOH B O     1 
HETATM 6413 O O     . HOH H 3 .   ? 8.259   84.956  -11.892 1.00 58.20 ? 731 HOH B O     1 
HETATM 6414 O O     . HOH H 3 .   ? 0.320   84.890  -13.070 1.00 74.03 ? 732 HOH B O     1 
HETATM 6415 O O     . HOH H 3 .   ? 6.925   89.238  -4.988  1.00 45.11 ? 733 HOH B O     1 
HETATM 6416 O O     . HOH H 3 .   ? 4.809   89.744  -7.329  1.00 28.92 ? 734 HOH B O     1 
HETATM 6417 O O     . HOH H 3 .   ? 17.463  102.159 -5.705  1.00 62.81 ? 735 HOH B O     1 
HETATM 6418 O O     . HOH H 3 .   ? 3.333   100.486 2.326   1.00 23.22 ? 736 HOH B O     1 
HETATM 6419 O O     . HOH H 3 .   ? 6.706   100.312 6.086   1.00 21.82 ? 737 HOH B O     1 
HETATM 6420 O O     . HOH H 3 .   ? 9.018   98.648  5.975   1.00 29.35 ? 738 HOH B O     1 
HETATM 6421 O O     . HOH H 3 .   ? 7.376   109.076 1.620   1.00 58.55 ? 739 HOH B O     1 
HETATM 6422 O O     . HOH H 3 .   ? 1.649   96.003  12.194  1.00 31.57 ? 740 HOH B O     1 
HETATM 6423 O O     . HOH H 3 .   ? -11.801 93.156  12.083  1.00 62.78 ? 741 HOH B O     1 
HETATM 6424 O O     . HOH H 3 .   ? 5.044   110.771 10.630  1.00 43.94 ? 742 HOH B O     1 
HETATM 6425 O O     . HOH H 3 .   ? 2.523   102.470 12.261  1.00 46.92 ? 743 HOH B O     1 
HETATM 6426 O O     . HOH H 3 .   ? 5.368   107.263 5.318   1.00 50.62 ? 744 HOH B O     1 
HETATM 6427 O O     . HOH H 3 .   ? -15.077 98.817  7.690   1.00 32.33 ? 745 HOH B O     1 
HETATM 6428 O O     . HOH H 3 .   ? -21.568 94.590  3.176   1.00 56.74 ? 746 HOH B O     1 
HETATM 6429 O O     . HOH H 3 .   ? -18.615 101.804 10.322  1.00 59.28 ? 747 HOH B O     1 
HETATM 6430 O O     . HOH H 3 .   ? -16.621 101.158 2.877   1.00 38.32 ? 748 HOH B O     1 
HETATM 6431 O O     . HOH H 3 .   ? 2.438   95.795  19.328  1.00 60.44 ? 749 HOH B O     1 
HETATM 6432 O O     . HOH H 3 .   ? -1.654  98.331  22.974  1.00 81.67 ? 750 HOH B O     1 
HETATM 6433 O O     . HOH H 3 .   ? -6.845  101.382 20.154  1.00 60.55 ? 751 HOH B O     1 
HETATM 6434 O O     . HOH H 3 .   ? -5.237  95.666  16.257  1.00 44.73 ? 752 HOH B O     1 
HETATM 6435 O O     . HOH H 3 .   ? -14.028 100.738 -2.180  1.00 52.11 ? 753 HOH B O     1 
HETATM 6436 O O     . HOH H 3 .   ? -0.344  99.010  4.336   1.00 28.32 ? 754 HOH B O     1 
HETATM 6437 O O     . HOH H 3 .   ? 11.182  114.589 -8.231  1.00 49.34 ? 755 HOH B O     1 
HETATM 6438 O O     . HOH H 3 .   ? -2.935  88.337  0.049   1.00 39.75 ? 756 HOH B O     1 
HETATM 6439 O O     . HOH H 3 .   ? -7.000  84.825  -10.985 1.00 47.05 ? 757 HOH B O     1 
HETATM 6440 O O     . HOH H 3 .   ? -5.767  86.163  -4.328  1.00 38.25 ? 758 HOH B O     1 
HETATM 6441 O O     . HOH I 3 .   ? 24.681  70.016  26.426  1.00 63.85 ? 802 HOH C O     1 
HETATM 6442 O O     . HOH I 3 .   ? 14.477  69.440  -0.534  1.00 19.57 ? 803 HOH C O     1 
HETATM 6443 O O     . HOH I 3 .   ? 8.569   62.646  18.488  1.00 16.22 ? 804 HOH C O     1 
HETATM 6444 O O     . HOH I 3 .   ? 12.651  65.157  12.362  1.00 29.66 ? 805 HOH C O     1 
HETATM 6445 O O     . HOH I 3 .   ? 16.752  78.241  -0.803  1.00 41.19 ? 806 HOH C O     1 
HETATM 6446 O O     . HOH I 3 .   ? 12.548  66.177  20.857  1.00 45.52 ? 807 HOH C O     1 
HETATM 6447 O O     . HOH I 3 .   ? -3.351  52.178  4.683   1.00 70.90 ? 808 HOH C O     1 
HETATM 6448 O O     . HOH I 3 .   ? 2.150   53.215  -6.870  1.00 58.90 ? 809 HOH C O     1 
HETATM 6449 O O     . HOH I 3 .   ? 23.038  57.116  -12.872 1.00 57.11 ? 810 HOH C O     1 
HETATM 6450 O O     . HOH I 3 .   ? 8.819   66.554  -4.086  1.00 27.00 ? 811 HOH C O     1 
HETATM 6451 O O     . HOH I 3 .   ? 22.686  49.352  -0.453  1.00 27.25 ? 812 HOH C O     1 
HETATM 6452 O O     . HOH I 3 .   ? 23.276  49.842  2.314   1.00 36.95 ? 813 HOH C O     1 
HETATM 6453 O O     . HOH I 3 .   ? 11.826  61.393  9.861   1.00 39.01 ? 814 HOH C O     1 
HETATM 6454 O O     . HOH I 3 .   ? 32.931  62.629  -14.045 1.00 78.95 ? 815 HOH C O     1 
HETATM 6455 O O     . HOH I 3 .   ? 15.302  76.081  -1.749  1.00 26.52 ? 816 HOH C O     1 
HETATM 6456 O O     . HOH I 3 .   ? 16.943  59.704  13.552  1.00 20.50 ? 817 HOH C O     1 
HETATM 6457 O O     . HOH I 3 .   ? 10.995  63.151  19.378  1.00 45.88 ? 818 HOH C O     1 
HETATM 6458 O O     . HOH I 3 .   ? 19.587  61.390  13.390  1.00 35.07 ? 819 HOH C O     1 
HETATM 6459 O O     . HOH I 3 .   ? 22.730  59.051  14.217  1.00 56.66 ? 820 HOH C O     1 
HETATM 6460 O O     . HOH I 3 .   ? 21.070  76.721  1.997   1.00 52.60 ? 821 HOH C O     1 
HETATM 6461 O O     . HOH I 3 .   ? 31.704  71.463  -1.815  1.00 55.69 ? 822 HOH C O     1 
HETATM 6462 O O     . HOH I 3 .   ? 19.124  76.493  11.200  1.00 30.87 ? 823 HOH C O     1 
HETATM 6463 O O     . HOH I 3 .   ? 31.375  71.478  19.975  1.00 53.37 ? 824 HOH C O     1 
HETATM 6464 O O     . HOH I 3 .   ? 10.658  71.819  -11.798 1.00 65.54 ? 825 HOH C O     1 
HETATM 6465 O O     . HOH I 3 .   ? 22.406  73.793  -14.917 1.00 67.31 ? 826 HOH C O     1 
HETATM 6466 O O     . HOH I 3 .   ? 3.043   53.911  16.399  1.00 71.78 ? 827 HOH C O     1 
HETATM 6467 O O     . HOH I 3 .   ? 23.936  79.806  -4.638  1.00 58.15 ? 828 HOH C O     1 
HETATM 6468 O O     . HOH I 3 .   ? 30.024  73.704  -10.350 1.00 63.44 ? 829 HOH C O     1 
HETATM 6469 O O     . HOH I 3 .   ? 27.858  63.451  -14.883 1.00 61.17 ? 830 HOH C O     1 
HETATM 6470 O O     . HOH I 3 .   ? 12.463  66.177  -15.668 1.00 60.21 ? 831 HOH C O     1 
HETATM 6471 O O     . HOH I 3 .   ? 11.498  59.228  -12.335 1.00 56.71 ? 832 HOH C O     1 
HETATM 6472 O O     . HOH I 3 .   ? 2.797   63.225  -10.027 1.00 71.46 ? 833 HOH C O     1 
HETATM 6473 O O     . HOH I 3 .   ? 5.844   69.907  -10.573 1.00 66.91 ? 834 HOH C O     1 
HETATM 6474 O O     . HOH I 3 .   ? 4.321   63.597  -1.670  1.00 45.80 ? 835 HOH C O     1 
HETATM 6475 O O     . HOH I 3 .   ? 6.451   64.120  -3.819  1.00 38.00 ? 836 HOH C O     1 
HETATM 6476 O O     . HOH I 3 .   ? 12.183  45.834  1.458   1.00 85.06 ? 837 HOH C O     1 
HETATM 6477 O O     . HOH I 3 .   ? 13.872  61.818  8.295   1.00 24.61 ? 838 HOH C O     1 
HETATM 6478 O O     . HOH I 3 .   ? 11.244  59.459  12.154  1.00 21.31 ? 839 HOH C O     1 
HETATM 6479 O O     . HOH I 3 .   ? 8.946   58.442  11.541  1.00 14.53 ? 840 HOH C O     1 
HETATM 6480 O O     . HOH I 3 .   ? 19.432  53.813  10.064  1.00 54.73 ? 841 HOH C O     1 
HETATM 6481 O O     . HOH I 3 .   ? 9.328   66.532  16.709  1.00 38.90 ? 842 HOH C O     1 
HETATM 6482 O O     . HOH I 3 .   ? 13.642  80.014  15.598  1.00 72.86 ? 843 HOH C O     1 
HETATM 6483 O O     . HOH I 3 .   ? 19.814  56.778  19.364  1.00 40.56 ? 844 HOH C O     1 
HETATM 6484 O O     . HOH I 3 .   ? 13.723  62.615  18.562  1.00 32.62 ? 845 HOH C O     1 
HETATM 6485 O O     . HOH I 3 .   ? 18.070  57.178  13.212  1.00 41.09 ? 846 HOH C O     1 
HETATM 6486 O O     . HOH I 3 .   ? 19.822  79.041  12.812  1.00 31.03 ? 847 HOH C O     1 
HETATM 6487 O O     . HOH I 3 .   ? 20.780  85.999  7.027   1.00 71.64 ? 848 HOH C O     1 
HETATM 6488 O O     . HOH I 3 .   ? 24.221  81.024  16.613  1.00 47.10 ? 849 HOH C O     1 
HETATM 6489 O O     . HOH I 3 .   ? 24.354  78.801  9.206   1.00 41.11 ? 850 HOH C O     1 
HETATM 6490 O O     . HOH I 3 .   ? 6.781   67.073  23.908  1.00 69.91 ? 851 HOH C O     1 
HETATM 6491 O O     . HOH I 3 .   ? 10.263  68.062  27.613  1.00 62.12 ? 852 HOH C O     1 
HETATM 6492 O O     . HOH I 3 .   ? 15.785  72.120  25.297  1.00 52.67 ? 853 HOH C O     1 
HETATM 6493 O O     . HOH I 3 .   ? 11.217  73.680  20.844  1.00 62.65 ? 854 HOH C O     1 
HETATM 6494 O O     . HOH I 3 .   ? 23.718  76.541  3.832   1.00 68.41 ? 855 HOH C O     1 
HETATM 6495 O O     . HOH I 3 .   ? 13.936  65.778  10.068  1.00 34.51 ? 856 HOH C O     1 
HETATM 6496 O O     . HOH I 3 .   ? 24.701  46.339  1.699   1.00 45.90 ? 857 HOH C O     1 
HETATM 6497 O O     . HOH I 3 .   ? 7.951   72.551  2.809   1.00 45.00 ? 858 HOH C O     1 
HETATM 6498 O O     . HOH I 3 .   ? 8.670   76.469  -8.310  1.00 58.26 ? 859 HOH C O     1 
HETATM 6499 O O     . HOH I 3 .   ? 7.845   75.471  -1.715  1.00 32.49 ? 860 HOH C O     1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLU 1   1   1   GLU GLU A . n 
A 1 2   VAL 2   2   2   VAL VAL A . n 
A 1 3   SER 3   3   3   SER SER A . n 
A 1 4   GLN 4   4   4   GLN GLN A . n 
A 1 5   ASP 5   5   5   ASP ASP A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   ASN 8   8   8   ASN ASN A . n 
A 1 9   GLN 9   9   9   GLN GLN A . n 
A 1 10  PHE 10  10  10  PHE PHE A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  PHE 13  13  13  PHE PHE A . n 
A 1 14  ALA 14  14  14  ALA ALA A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  TYR 16  16  16  TYR TYR A . n 
A 1 17  SER 17  17  17  SER SER A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  TYR 21  21  21  TYR TYR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  ASN 25  25  25  ASN ASN A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  GLY 31  31  31  GLY GLY A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  ASN 33  33  33  ASN ASN A . n 
A 1 34  ILE 34  34  34  ILE ILE A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  CYS 36  36  36  CYS CYS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  ASN 39  39  39  ASN ASN A . n 
A 1 40  ALA 40  40  40  ALA ALA A . n 
A 1 41  CYS 41  41  41  CYS CYS A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  VAL 44  44  44  VAL VAL A . n 
A 1 45  GLU 45  45  45  GLU GLU A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  ALA 49  49  49  ALA ALA A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  PHE 51  51  51  PHE PHE A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  TYR 53  53  53  TYR TYR A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  PHE 55  55  55  PHE PHE A . n 
A 1 56  GLU 56  56  56  GLU GLU A . n 
A 1 57  ASP 57  57  57  ASP ASP A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  VAL 60  60  60  VAL VAL A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  ASP 62  62  62  ASP ASP A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  ASP 70  70  70  ASP ASP A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  THR 72  72  72  THR THR A . n 
A 1 73  ASN 73  73  73  ASN ASN A . n 
A 1 74  LYS 74  74  74  LYS LYS A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ILE 76  76  76  ILE ILE A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  PHE 80  80  80  PHE PHE A . n 
A 1 81  ARG 81  81  81  ARG ARG A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  ILE 86  86  86  ILE ILE A . n 
A 1 87  GLU 87  87  87  GLU GLU A . n 
A 1 88  ASN 88  88  88  ASN ASN A . n 
A 1 89  TRP 89  89  89  TRP TRP A . n 
A 1 90  ILE 90  90  90  ILE ILE A . n 
A 1 91  GLY 91  91  91  GLY GLY A . n 
A 1 92  ASN 92  92  92  ASN ASN A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  ASN 94  94  94  ASN ASN A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  LYS 98  98  98  LYS LYS A . n 
A 1 99  GLU 99  99  99  GLU GLU A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 ILE 103 103 103 ILE ILE A . n 
A 1 104 CYS 104 104 104 CYS CYS A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 CYS 107 107 107 CYS CYS A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 ASP 111 111 111 ASP ASP A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 PHE 113 113 113 PHE PHE A . n 
A 1 114 THR 114 114 114 THR THR A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 SER 116 116 116 SER SER A . n 
A 1 117 TRP 117 117 117 TRP TRP A . n 
A 1 118 ARG 118 118 118 ARG ARG A . n 
A 1 119 SER 119 119 119 SER SER A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 ARG 125 125 125 ARG ARG A . n 
A 1 126 GLN 126 126 126 GLN GLN A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 ASP 130 130 130 ASP ASP A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 ARG 133 133 133 ARG ARG A . n 
A 1 134 GLU 134 134 134 GLU GLU A . n 
A 1 135 HIS 135 135 135 HIS HIS A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ASP 137 137 137 ASP ASP A . n 
A 1 138 TYR 138 138 138 TYR TYR A . n 
A 1 139 ARG 139 139 139 ARG ARG A . n 
A 1 140 VAL 140 140 140 VAL VAL A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 PHE 142 142 142 PHE PHE A . n 
A 1 143 THR 143 143 143 THR THR A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 HIS 145 145 145 HIS HIS A . n 
A 1 146 SER 146 146 146 SER SER A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 GLY 148 148 148 GLY GLY A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 THR 153 153 153 THR THR A . n 
A 1 154 VAL 154 154 154 VAL VAL A . n 
A 1 155 ALA 155 155 155 ALA ALA A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 ALA 157 157 157 ALA ALA A . n 
A 1 158 ASP 158 158 158 ASP ASP A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 ARG 160 160 160 ARG ARG A . n 
A 1 161 GLY 161 161 161 GLY GLY A . n 
A 1 162 ASN 162 162 162 ASN ASN A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 TYR 164 164 164 TYR TYR A . n 
A 1 165 ASP 165 165 165 ASP ASP A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 ASP 167 167 167 ASP ASP A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 PHE 169 169 169 PHE PHE A . n 
A 1 170 SER 170 170 170 SER SER A . n 
A 1 171 TYR 171 171 171 TYR TYR A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 PRO 174 174 174 PRO PRO A . n 
A 1 175 ARG 175 175 175 ARG ARG A . n 
A 1 176 VAL 176 176 176 VAL VAL A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 ARG 179 179 179 ARG ARG A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 PHE 184 184 184 PHE PHE A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 THR 186 186 186 THR THR A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 GLN 188 188 188 GLN GLN A . n 
A 1 189 THR 189 189 189 THR THR A . n 
A 1 190 GLY 190 190 190 GLY GLY A . n 
A 1 191 GLY 191 191 191 GLY GLY A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 LEU 193 193 193 LEU LEU A . n 
A 1 194 TYR 194 194 194 TYR TYR A . n 
A 1 195 ARG 195 195 195 ARG ARG A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 THR 197 197 197 THR THR A . n 
A 1 198 HIS 198 198 198 HIS HIS A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ASN 200 200 200 ASN ASN A . n 
A 1 201 ASP 201 201 201 ASP ASP A . n 
A 1 202 ILE 202 202 202 ILE ILE A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 ARG 205 205 205 ARG ARG A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 PRO 207 207 207 PRO PRO A . n 
A 1 208 PRO 208 208 208 PRO PRO A . n 
A 1 209 ARG 209 209 209 ARG ARG A . n 
A 1 210 GLU 210 210 210 GLU GLU A . n 
A 1 211 PHE 211 211 211 PHE PHE A . n 
A 1 212 GLY 212 212 212 GLY GLY A . n 
A 1 213 TYR 213 213 213 TYR TYR A . n 
A 1 214 SER 214 214 214 SER SER A . n 
A 1 215 HIS 215 215 215 HIS HIS A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 SER 217 217 217 SER SER A . n 
A 1 218 PRO 218 218 218 PRO PRO A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 TYR 220 220 220 TYR TYR A . n 
A 1 221 TRP 221 221 221 TRP TRP A . n 
A 1 222 ILE 222 222 222 ILE ILE A . n 
A 1 223 LYS 223 223 223 LYS LYS A . n 
A 1 224 SER 224 224 224 SER SER A . n 
A 1 225 GLY 225 225 225 GLY GLY A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 VAL 228 228 228 VAL VAL A . n 
A 1 229 PRO 229 229 229 PRO PRO A . n 
A 1 230 VAL 230 230 230 VAL VAL A . n 
A 1 231 THR 231 231 231 THR THR A . n 
A 1 232 ARG 232 232 232 ARG ARG A . n 
A 1 233 ASN 233 233 233 ASN ASN A . n 
A 1 234 ASP 234 234 234 ASP ASP A . n 
A 1 235 ILE 235 235 235 ILE ILE A . n 
A 1 236 VAL 236 236 236 VAL VAL A . n 
A 1 237 LYS 237 237 237 LYS LYS A . n 
A 1 238 ILE 238 238 238 ILE ILE A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 GLY 240 240 240 GLY GLY A . n 
A 1 241 ILE 241 241 241 ILE ILE A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 ALA 243 243 243 ALA ALA A . n 
A 1 244 THR 244 244 244 THR THR A . n 
A 1 245 GLY 245 245 245 GLY GLY A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 ASN 247 247 247 ASN ASN A . n 
A 1 248 ASN 248 248 248 ASN ASN A . n 
A 1 249 GLN 249 249 249 GLN GLN A . n 
A 1 250 PRO 250 250 250 PRO PRO A . n 
A 1 251 ASN 251 251 251 ASN ASN A . n 
A 1 252 ILE 252 252 252 ILE ILE A . n 
A 1 253 PRO 253 253 253 PRO PRO A . n 
A 1 254 ASP 254 254 254 ASP ASP A . n 
A 1 255 ILE 255 255 255 ILE ILE A . n 
A 1 256 PRO 256 256 256 PRO PRO A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 HIS 258 258 258 HIS HIS A . n 
A 1 259 LEU 259 259 259 LEU LEU A . n 
A 1 260 TRP 260 260 260 TRP TRP A . n 
A 1 261 TYR 261 261 261 TYR TYR A . n 
A 1 262 PHE 262 262 262 PHE PHE A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 ILE 265 265 265 ILE ILE A . n 
A 1 266 GLY 266 266 266 GLY GLY A . n 
A 1 267 THR 267 267 267 THR THR A . n 
A 1 268 CYS 268 268 268 CYS CYS A . n 
A 1 269 LEU 269 269 269 LEU LEU A . n 
B 1 1   GLU 1   1   1   GLU GLU B . n 
B 1 2   VAL 2   2   2   VAL VAL B . n 
B 1 3   SER 3   3   3   SER SER B . n 
B 1 4   GLN 4   4   4   GLN GLN B . n 
B 1 5   ASP 5   5   5   ASP ASP B . n 
B 1 6   LEU 6   6   6   LEU LEU B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   ASN 8   8   8   ASN ASN B . n 
B 1 9   GLN 9   9   9   GLN GLN B . n 
B 1 10  PHE 10  10  10  PHE PHE B . n 
B 1 11  ASN 11  11  11  ASN ASN B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  PHE 13  13  13  PHE PHE B . n 
B 1 14  ALA 14  14  14  ALA ALA B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  TYR 16  16  16  TYR TYR B . n 
B 1 17  SER 17  17  17  SER SER B . n 
B 1 18  ALA 18  18  18  ALA ALA B . n 
B 1 19  ALA 19  19  19  ALA ALA B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  TYR 21  21  21  TYR TYR B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  LYS 24  24  24  LYS LYS B . n 
B 1 25  ASN 25  25  25  ASN ASN B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  ASP 27  27  27  ASP ASP B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  PRO 29  29  29  PRO PRO B . n 
B 1 30  ALA 30  30  30  ALA ALA B . n 
B 1 31  GLY 31  31  31  GLY GLY B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  ASN 33  33  33  ASN ASN B . n 
B 1 34  ILE 34  34  34  ILE ILE B . n 
B 1 35  THR 35  35  35  THR THR B . n 
B 1 36  CYS 36  36  36  CYS CYS B . n 
B 1 37  THR 37  37  37  THR THR B . n 
B 1 38  GLY 38  38  38  GLY GLY B . n 
B 1 39  ASN 39  39  39  ASN ASN B . n 
B 1 40  ALA 40  40  40  ALA ALA B . n 
B 1 41  CYS 41  41  41  CYS CYS B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  GLU 43  43  43  GLU GLU B . n 
B 1 44  VAL 44  44  44  VAL VAL B . n 
B 1 45  GLU 45  45  45  GLU GLU B . n 
B 1 46  LYS 46  46  46  LYS LYS B . n 
B 1 47  ALA 47  47  47  ALA ALA B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  ALA 49  49  49  ALA ALA B . n 
B 1 50  THR 50  50  50  THR THR B . n 
B 1 51  PHE 51  51  51  PHE PHE B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  TYR 53  53  53  TYR TYR B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  PHE 55  55  55  PHE PHE B . n 
B 1 56  GLU 56  56  56  GLU GLU B . n 
B 1 57  ASP 57  57  57  ASP ASP B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  GLY 59  59  59  GLY GLY B . n 
B 1 60  VAL 60  60  60  VAL VAL B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  ASP 62  62  62  ASP ASP B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  THR 64  64  64  THR THR B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  ALA 68  68  68  ALA ALA B . n 
B 1 69  LEU 69  69  69  LEU LEU B . n 
B 1 70  ASP 70  70  70  ASP ASP B . n 
B 1 71  ASN 71  71  71  ASN ASN B . n 
B 1 72  THR 72  72  72  THR THR B . n 
B 1 73  ASN 73  73  73  ASN ASN B . n 
B 1 74  LYS 74  74  74  LYS LYS B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  ILE 76  76  76  ILE ILE B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  LEU 78  78  78  LEU LEU B . n 
B 1 79  SER 79  79  79  SER SER B . n 
B 1 80  PHE 80  80  80  PHE PHE B . n 
B 1 81  ARG 81  81  81  ARG ARG B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  SER 85  85  85  SER SER B . n 
B 1 86  ILE 86  86  86  ILE ILE B . n 
B 1 87  GLU 87  87  87  GLU GLU B . n 
B 1 88  ASN 88  88  88  ASN ASN B . n 
B 1 89  TRP 89  89  89  TRP TRP B . n 
B 1 90  ILE 90  90  90  ILE ILE B . n 
B 1 91  GLY 91  91  91  GLY GLY B . n 
B 1 92  ASN 92  92  92  ASN ASN B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  ASN 94  94  94  ASN ASN B . n 
B 1 95  PHE 95  95  95  PHE PHE B . n 
B 1 96  ASP 96  96  96  ASP ASP B . n 
B 1 97  LEU 97  97  97  LEU LEU B . n 
B 1 98  LYS 98  98  98  LYS LYS B . n 
B 1 99  GLU 99  99  99  GLU GLU B . n 
B 1 100 ILE 100 100 100 ILE ILE B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 ASP 102 102 102 ASP ASP B . n 
B 1 103 ILE 103 103 103 ILE ILE B . n 
B 1 104 CYS 104 104 104 CYS CYS B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 GLY 106 106 106 GLY GLY B . n 
B 1 107 CYS 107 107 107 CYS CYS B . n 
B 1 108 ARG 108 108 108 ARG ARG B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 HIS 110 110 110 HIS HIS B . n 
B 1 111 ASP 111 111 111 ASP ASP B . n 
B 1 112 GLY 112 112 112 GLY GLY B . n 
B 1 113 PHE 113 113 113 PHE PHE B . n 
B 1 114 THR 114 114 114 THR THR B . n 
B 1 115 SER 115 115 115 SER SER B . n 
B 1 116 SER 116 116 116 SER SER B . n 
B 1 117 TRP 117 117 117 TRP TRP B . n 
B 1 118 ARG 118 118 118 ARG ARG B . n 
B 1 119 SER 119 119 119 SER SER B . n 
B 1 120 VAL 120 120 120 VAL VAL B . n 
B 1 121 ALA 121 121 121 ALA ALA B . n 
B 1 122 ASP 122 122 122 ASP ASP B . n 
B 1 123 THR 123 123 123 THR THR B . n 
B 1 124 LEU 124 124 124 LEU LEU B . n 
B 1 125 ARG 125 125 125 ARG ARG B . n 
B 1 126 GLN 126 126 126 GLN GLN B . n 
B 1 127 LYS 127 127 127 LYS LYS B . n 
B 1 128 VAL 128 128 128 VAL VAL B . n 
B 1 129 GLU 129 129 129 GLU GLU B . n 
B 1 130 ASP 130 130 130 ASP ASP B . n 
B 1 131 ALA 131 131 131 ALA ALA B . n 
B 1 132 VAL 132 132 132 VAL VAL B . n 
B 1 133 ARG 133 133 133 ARG ARG B . n 
B 1 134 GLU 134 134 134 GLU GLU B . n 
B 1 135 HIS 135 135 135 HIS HIS B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ASP 137 137 137 ASP ASP B . n 
B 1 138 TYR 138 138 138 TYR TYR B . n 
B 1 139 ARG 139 139 139 ARG ARG B . n 
B 1 140 VAL 140 140 140 VAL VAL B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 PHE 142 142 142 PHE PHE B . n 
B 1 143 THR 143 143 143 THR THR B . n 
B 1 144 GLY 144 144 144 GLY GLY B . n 
B 1 145 HIS 145 145 145 HIS HIS B . n 
B 1 146 SER 146 146 146 SER SER B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 GLY 148 148 148 GLY GLY B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 ALA 150 150 150 ALA ALA B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 THR 153 153 153 THR THR B . n 
B 1 154 VAL 154 154 154 VAL VAL B . n 
B 1 155 ALA 155 155 155 ALA ALA B . n 
B 1 156 GLY 156 156 156 GLY GLY B . n 
B 1 157 ALA 157 157 157 ALA ALA B . n 
B 1 158 ASP 158 158 158 ASP ASP B . n 
B 1 159 LEU 159 159 159 LEU LEU B . n 
B 1 160 ARG 160 160 160 ARG ARG B . n 
B 1 161 GLY 161 161 161 GLY GLY B . n 
B 1 162 ASN 162 162 162 ASN ASN B . n 
B 1 163 GLY 163 163 163 GLY GLY B . n 
B 1 164 TYR 164 164 164 TYR TYR B . n 
B 1 165 ASP 165 165 165 ASP ASP B . n 
B 1 166 ILE 166 166 166 ILE ILE B . n 
B 1 167 ASP 167 167 167 ASP ASP B . n 
B 1 168 VAL 168 168 168 VAL VAL B . n 
B 1 169 PHE 169 169 169 PHE PHE B . n 
B 1 170 SER 170 170 170 SER SER B . n 
B 1 171 TYR 171 171 171 TYR TYR B . n 
B 1 172 GLY 172 172 172 GLY GLY B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 PRO 174 174 174 PRO PRO B . n 
B 1 175 ARG 175 175 175 ARG ARG B . n 
B 1 176 VAL 176 176 176 VAL VAL B . n 
B 1 177 GLY 177 177 177 GLY GLY B . n 
B 1 178 ASN 178 178 178 ASN ASN B . n 
B 1 179 ARG 179 179 179 ARG ARG B . n 
B 1 180 ALA 180 180 180 ALA ALA B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 ALA 182 182 182 ALA ALA B . n 
B 1 183 GLU 183 183 183 GLU GLU B . n 
B 1 184 PHE 184 184 184 PHE PHE B . n 
B 1 185 LEU 185 185 185 LEU LEU B . n 
B 1 186 THR 186 186 186 THR THR B . n 
B 1 187 VAL 187 187 187 VAL VAL B . n 
B 1 188 GLN 188 188 188 GLN GLN B . n 
B 1 189 THR 189 189 189 THR THR B . n 
B 1 190 GLY 190 190 190 GLY GLY B . n 
B 1 191 GLY 191 191 191 GLY GLY B . n 
B 1 192 THR 192 192 192 THR THR B . n 
B 1 193 LEU 193 193 193 LEU LEU B . n 
B 1 194 TYR 194 194 194 TYR TYR B . n 
B 1 195 ARG 195 195 195 ARG ARG B . n 
B 1 196 ILE 196 196 196 ILE ILE B . n 
B 1 197 THR 197 197 197 THR THR B . n 
B 1 198 HIS 198 198 198 HIS HIS B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 ASN 200 200 200 ASN ASN B . n 
B 1 201 ASP 201 201 201 ASP ASP B . n 
B 1 202 ILE 202 202 202 ILE ILE B . n 
B 1 203 VAL 203 203 203 VAL VAL B . n 
B 1 204 PRO 204 204 204 PRO PRO B . n 
B 1 205 ARG 205 205 205 ARG ARG B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 PRO 207 207 207 PRO PRO B . n 
B 1 208 PRO 208 208 208 PRO PRO B . n 
B 1 209 ARG 209 209 209 ARG ARG B . n 
B 1 210 GLU 210 210 210 GLU GLU B . n 
B 1 211 PHE 211 211 211 PHE PHE B . n 
B 1 212 GLY 212 212 212 GLY GLY B . n 
B 1 213 TYR 213 213 213 TYR TYR B . n 
B 1 214 SER 214 214 214 SER SER B . n 
B 1 215 HIS 215 215 215 HIS HIS B . n 
B 1 216 SER 216 216 216 SER SER B . n 
B 1 217 SER 217 217 217 SER SER B . n 
B 1 218 PRO 218 218 218 PRO PRO B . n 
B 1 219 GLU 219 219 219 GLU GLU B . n 
B 1 220 TYR 220 220 220 TYR TYR B . n 
B 1 221 TRP 221 221 221 TRP TRP B . n 
B 1 222 ILE 222 222 222 ILE ILE B . n 
B 1 223 LYS 223 223 223 LYS LYS B . n 
B 1 224 SER 224 224 224 SER SER B . n 
B 1 225 GLY 225 225 225 GLY GLY B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 VAL 228 228 228 VAL VAL B . n 
B 1 229 PRO 229 229 229 PRO PRO B . n 
B 1 230 VAL 230 230 230 VAL VAL B . n 
B 1 231 THR 231 231 231 THR THR B . n 
B 1 232 ARG 232 232 232 ARG ARG B . n 
B 1 233 ASN 233 233 233 ASN ASN B . n 
B 1 234 ASP 234 234 234 ASP ASP B . n 
B 1 235 ILE 235 235 235 ILE ILE B . n 
B 1 236 VAL 236 236 236 VAL VAL B . n 
B 1 237 LYS 237 237 237 LYS LYS B . n 
B 1 238 ILE 238 238 238 ILE ILE B . n 
B 1 239 GLU 239 239 239 GLU GLU B . n 
B 1 240 GLY 240 240 240 GLY GLY B . n 
B 1 241 ILE 241 241 241 ILE ILE B . n 
B 1 242 ASP 242 242 242 ASP ASP B . n 
B 1 243 ALA 243 243 243 ALA ALA B . n 
B 1 244 THR 244 244 244 THR THR B . n 
B 1 245 GLY 245 245 245 GLY GLY B . n 
B 1 246 GLY 246 246 246 GLY GLY B . n 
B 1 247 ASN 247 247 247 ASN ASN B . n 
B 1 248 ASN 248 248 248 ASN ASN B . n 
B 1 249 GLN 249 249 249 GLN GLN B . n 
B 1 250 PRO 250 250 250 PRO PRO B . n 
B 1 251 ASN 251 251 251 ASN ASN B . n 
B 1 252 ILE 252 252 252 ILE ILE B . n 
B 1 253 PRO 253 253 253 PRO PRO B . n 
B 1 254 ASP 254 254 254 ASP ASP B . n 
B 1 255 ILE 255 255 255 ILE ILE B . n 
B 1 256 PRO 256 256 256 PRO PRO B . n 
B 1 257 ALA 257 257 257 ALA ALA B . n 
B 1 258 HIS 258 258 258 HIS HIS B . n 
B 1 259 LEU 259 259 259 LEU LEU B . n 
B 1 260 TRP 260 260 260 TRP TRP B . n 
B 1 261 TYR 261 261 261 TYR TYR B . n 
B 1 262 PHE 262 262 262 PHE PHE B . n 
B 1 263 GLY 263 263 263 GLY GLY B . n 
B 1 264 LEU 264 264 264 LEU LEU B . n 
B 1 265 ILE 265 265 265 ILE ILE B . n 
B 1 266 GLY 266 266 266 GLY GLY B . n 
B 1 267 THR 267 267 267 THR THR B . n 
B 1 268 CYS 268 268 268 CYS CYS B . n 
B 1 269 LEU 269 269 269 LEU LEU B . n 
C 1 1   GLU 1   1   1   GLU GLU C . n 
C 1 2   VAL 2   2   2   VAL VAL C . n 
C 1 3   SER 3   3   3   SER SER C . n 
C 1 4   GLN 4   4   4   GLN GLN C . n 
C 1 5   ASP 5   5   5   ASP ASP C . n 
C 1 6   LEU 6   6   6   LEU LEU C . n 
C 1 7   PHE 7   7   7   PHE PHE C . n 
C 1 8   ASN 8   8   8   ASN ASN C . n 
C 1 9   GLN 9   9   9   GLN GLN C . n 
C 1 10  PHE 10  10  10  PHE PHE C . n 
C 1 11  ASN 11  11  11  ASN ASN C . n 
C 1 12  LEU 12  12  12  LEU LEU C . n 
C 1 13  PHE 13  13  13  PHE PHE C . n 
C 1 14  ALA 14  14  14  ALA ALA C . n 
C 1 15  GLN 15  15  15  GLN GLN C . n 
C 1 16  TYR 16  16  16  TYR TYR C . n 
C 1 17  SER 17  17  17  SER SER C . n 
C 1 18  ALA 18  18  18  ALA ALA C . n 
C 1 19  ALA 19  19  19  ALA ALA C . n 
C 1 20  ALA 20  20  20  ALA ALA C . n 
C 1 21  TYR 21  21  21  TYR TYR C . n 
C 1 22  CYS 22  22  22  CYS CYS C . n 
C 1 23  GLY 23  23  23  GLY GLY C . n 
C 1 24  LYS 24  24  24  LYS LYS C . n 
C 1 25  ASN 25  25  25  ASN ASN C . n 
C 1 26  ASN 26  26  26  ASN ASN C . n 
C 1 27  ASP 27  27  27  ASP ASP C . n 
C 1 28  ALA 28  28  28  ALA ALA C . n 
C 1 29  PRO 29  29  29  PRO PRO C . n 
C 1 30  ALA 30  30  30  ALA ALA C . n 
C 1 31  GLY 31  31  31  GLY GLY C . n 
C 1 32  THR 32  32  32  THR THR C . n 
C 1 33  ASN 33  33  33  ASN ASN C . n 
C 1 34  ILE 34  34  34  ILE ILE C . n 
C 1 35  THR 35  35  35  THR THR C . n 
C 1 36  CYS 36  36  36  CYS CYS C . n 
C 1 37  THR 37  37  37  THR THR C . n 
C 1 38  GLY 38  38  38  GLY GLY C . n 
C 1 39  ASN 39  39  39  ASN ASN C . n 
C 1 40  ALA 40  40  40  ALA ALA C . n 
C 1 41  CYS 41  41  41  CYS CYS C . n 
C 1 42  PRO 42  42  42  PRO PRO C . n 
C 1 43  GLU 43  43  43  GLU GLU C . n 
C 1 44  VAL 44  44  44  VAL VAL C . n 
C 1 45  GLU 45  45  45  GLU GLU C . n 
C 1 46  LYS 46  46  46  LYS LYS C . n 
C 1 47  ALA 47  47  47  ALA ALA C . n 
C 1 48  ASP 48  48  48  ASP ASP C . n 
C 1 49  ALA 49  49  49  ALA ALA C . n 
C 1 50  THR 50  50  50  THR THR C . n 
C 1 51  PHE 51  51  51  PHE PHE C . n 
C 1 52  LEU 52  52  52  LEU LEU C . n 
C 1 53  TYR 53  53  53  TYR TYR C . n 
C 1 54  SER 54  54  54  SER SER C . n 
C 1 55  PHE 55  55  55  PHE PHE C . n 
C 1 56  GLU 56  56  56  GLU GLU C . n 
C 1 57  ASP 57  57  57  ASP ASP C . n 
C 1 58  SER 58  58  58  SER SER C . n 
C 1 59  GLY 59  59  59  GLY GLY C . n 
C 1 60  VAL 60  60  60  VAL VAL C . n 
C 1 61  GLY 61  61  61  GLY GLY C . n 
C 1 62  ASP 62  62  62  ASP ASP C . n 
C 1 63  VAL 63  63  63  VAL VAL C . n 
C 1 64  THR 64  64  64  THR THR C . n 
C 1 65  GLY 65  65  65  GLY GLY C . n 
C 1 66  PHE 66  66  66  PHE PHE C . n 
C 1 67  LEU 67  67  67  LEU LEU C . n 
C 1 68  ALA 68  68  68  ALA ALA C . n 
C 1 69  LEU 69  69  69  LEU LEU C . n 
C 1 70  ASP 70  70  70  ASP ASP C . n 
C 1 71  ASN 71  71  71  ASN ASN C . n 
C 1 72  THR 72  72  72  THR THR C . n 
C 1 73  ASN 73  73  73  ASN ASN C . n 
C 1 74  LYS 74  74  74  LYS LYS C . n 
C 1 75  LEU 75  75  75  LEU LEU C . n 
C 1 76  ILE 76  76  76  ILE ILE C . n 
C 1 77  VAL 77  77  77  VAL VAL C . n 
C 1 78  LEU 78  78  78  LEU LEU C . n 
C 1 79  SER 79  79  79  SER SER C . n 
C 1 80  PHE 80  80  80  PHE PHE C . n 
C 1 81  ARG 81  81  81  ARG ARG C . n 
C 1 82  GLY 82  82  82  GLY GLY C . n 
C 1 83  SER 83  83  83  SER SER C . n 
C 1 84  ARG 84  84  84  ARG ARG C . n 
C 1 85  SER 85  85  85  SER SER C . n 
C 1 86  ILE 86  86  86  ILE ILE C . n 
C 1 87  GLU 87  87  87  GLU GLU C . n 
C 1 88  ASN 88  88  88  ASN ASN C . n 
C 1 89  TRP 89  89  89  TRP TRP C . n 
C 1 90  ILE 90  90  90  ILE ILE C . n 
C 1 91  GLY 91  91  91  GLY GLY C . n 
C 1 92  ASN 92  92  92  ASN ASN C . n 
C 1 93  LEU 93  93  93  LEU LEU C . n 
C 1 94  ASN 94  94  94  ASN ASN C . n 
C 1 95  PHE 95  95  95  PHE PHE C . n 
C 1 96  ASP 96  96  96  ASP ASP C . n 
C 1 97  LEU 97  97  97  LEU LEU C . n 
C 1 98  LYS 98  98  98  LYS LYS C . n 
C 1 99  GLU 99  99  99  GLU GLU C . n 
C 1 100 ILE 100 100 100 ILE ILE C . n 
C 1 101 ASN 101 101 101 ASN ASN C . n 
C 1 102 ASP 102 102 102 ASP ASP C . n 
C 1 103 ILE 103 103 103 ILE ILE C . n 
C 1 104 CYS 104 104 104 CYS CYS C . n 
C 1 105 SER 105 105 105 SER SER C . n 
C 1 106 GLY 106 106 106 GLY GLY C . n 
C 1 107 CYS 107 107 107 CYS CYS C . n 
C 1 108 ARG 108 108 108 ARG ARG C . n 
C 1 109 GLY 109 109 109 GLY GLY C . n 
C 1 110 HIS 110 110 110 HIS HIS C . n 
C 1 111 ASP 111 111 111 ASP ASP C . n 
C 1 112 GLY 112 112 112 GLY GLY C . n 
C 1 113 PHE 113 113 113 PHE PHE C . n 
C 1 114 THR 114 114 114 THR THR C . n 
C 1 115 SER 115 115 115 SER SER C . n 
C 1 116 SER 116 116 116 SER SER C . n 
C 1 117 TRP 117 117 117 TRP TRP C . n 
C 1 118 ARG 118 118 118 ARG ARG C . n 
C 1 119 SER 119 119 119 SER SER C . n 
C 1 120 VAL 120 120 120 VAL VAL C . n 
C 1 121 ALA 121 121 121 ALA ALA C . n 
C 1 122 ASP 122 122 122 ASP ASP C . n 
C 1 123 THR 123 123 123 THR THR C . n 
C 1 124 LEU 124 124 124 LEU LEU C . n 
C 1 125 ARG 125 125 125 ARG ARG C . n 
C 1 126 GLN 126 126 126 GLN GLN C . n 
C 1 127 LYS 127 127 127 LYS LYS C . n 
C 1 128 VAL 128 128 128 VAL VAL C . n 
C 1 129 GLU 129 129 129 GLU GLU C . n 
C 1 130 ASP 130 130 130 ASP ASP C . n 
C 1 131 ALA 131 131 131 ALA ALA C . n 
C 1 132 VAL 132 132 132 VAL VAL C . n 
C 1 133 ARG 133 133 133 ARG ARG C . n 
C 1 134 GLU 134 134 134 GLU GLU C . n 
C 1 135 HIS 135 135 135 HIS HIS C . n 
C 1 136 PRO 136 136 136 PRO PRO C . n 
C 1 137 ASP 137 137 137 ASP ASP C . n 
C 1 138 TYR 138 138 138 TYR TYR C . n 
C 1 139 ARG 139 139 139 ARG ARG C . n 
C 1 140 VAL 140 140 140 VAL VAL C . n 
C 1 141 VAL 141 141 141 VAL VAL C . n 
C 1 142 PHE 142 142 142 PHE PHE C . n 
C 1 143 THR 143 143 143 THR THR C . n 
C 1 144 GLY 144 144 144 GLY GLY C . n 
C 1 145 HIS 145 145 145 HIS HIS C . n 
C 1 146 SER 146 146 146 SER SER C . n 
C 1 147 LEU 147 147 147 LEU LEU C . n 
C 1 148 GLY 148 148 148 GLY GLY C . n 
C 1 149 GLY 149 149 149 GLY GLY C . n 
C 1 150 ALA 150 150 150 ALA ALA C . n 
C 1 151 LEU 151 151 151 LEU LEU C . n 
C 1 152 ALA 152 152 152 ALA ALA C . n 
C 1 153 THR 153 153 153 THR THR C . n 
C 1 154 VAL 154 154 154 VAL VAL C . n 
C 1 155 ALA 155 155 155 ALA ALA C . n 
C 1 156 GLY 156 156 156 GLY GLY C . n 
C 1 157 ALA 157 157 157 ALA ALA C . n 
C 1 158 ASP 158 158 158 ASP ASP C . n 
C 1 159 LEU 159 159 159 LEU LEU C . n 
C 1 160 ARG 160 160 160 ARG ARG C . n 
C 1 161 GLY 161 161 161 GLY GLY C . n 
C 1 162 ASN 162 162 162 ASN ASN C . n 
C 1 163 GLY 163 163 163 GLY GLY C . n 
C 1 164 TYR 164 164 164 TYR TYR C . n 
C 1 165 ASP 165 165 165 ASP ASP C . n 
C 1 166 ILE 166 166 166 ILE ILE C . n 
C 1 167 ASP 167 167 167 ASP ASP C . n 
C 1 168 VAL 168 168 168 VAL VAL C . n 
C 1 169 PHE 169 169 169 PHE PHE C . n 
C 1 170 SER 170 170 170 SER SER C . n 
C 1 171 TYR 171 171 171 TYR TYR C . n 
C 1 172 GLY 172 172 172 GLY GLY C . n 
C 1 173 ALA 173 173 173 ALA ALA C . n 
C 1 174 PRO 174 174 174 PRO PRO C . n 
C 1 175 ARG 175 175 175 ARG ARG C . n 
C 1 176 VAL 176 176 176 VAL VAL C . n 
C 1 177 GLY 177 177 177 GLY GLY C . n 
C 1 178 ASN 178 178 178 ASN ASN C . n 
C 1 179 ARG 179 179 179 ARG ARG C . n 
C 1 180 ALA 180 180 180 ALA ALA C . n 
C 1 181 PHE 181 181 181 PHE PHE C . n 
C 1 182 ALA 182 182 182 ALA ALA C . n 
C 1 183 GLU 183 183 183 GLU GLU C . n 
C 1 184 PHE 184 184 184 PHE PHE C . n 
C 1 185 LEU 185 185 185 LEU LEU C . n 
C 1 186 THR 186 186 186 THR THR C . n 
C 1 187 VAL 187 187 187 VAL VAL C . n 
C 1 188 GLN 188 188 188 GLN GLN C . n 
C 1 189 THR 189 189 189 THR THR C . n 
C 1 190 GLY 190 190 190 GLY GLY C . n 
C 1 191 GLY 191 191 191 GLY GLY C . n 
C 1 192 THR 192 192 192 THR THR C . n 
C 1 193 LEU 193 193 193 LEU LEU C . n 
C 1 194 TYR 194 194 194 TYR TYR C . n 
C 1 195 ARG 195 195 195 ARG ARG C . n 
C 1 196 ILE 196 196 196 ILE ILE C . n 
C 1 197 THR 197 197 197 THR THR C . n 
C 1 198 HIS 198 198 198 HIS HIS C . n 
C 1 199 THR 199 199 199 THR THR C . n 
C 1 200 ASN 200 200 200 ASN ASN C . n 
C 1 201 ASP 201 201 201 ASP ASP C . n 
C 1 202 ILE 202 202 202 ILE ILE C . n 
C 1 203 VAL 203 203 203 VAL VAL C . n 
C 1 204 PRO 204 204 204 PRO PRO C . n 
C 1 205 ARG 205 205 205 ARG ARG C . n 
C 1 206 LEU 206 206 206 LEU LEU C . n 
C 1 207 PRO 207 207 207 PRO PRO C . n 
C 1 208 PRO 208 208 208 PRO PRO C . n 
C 1 209 ARG 209 209 209 ARG ARG C . n 
C 1 210 GLU 210 210 210 GLU GLU C . n 
C 1 211 PHE 211 211 211 PHE PHE C . n 
C 1 212 GLY 212 212 212 GLY GLY C . n 
C 1 213 TYR 213 213 213 TYR TYR C . n 
C 1 214 SER 214 214 214 SER SER C . n 
C 1 215 HIS 215 215 215 HIS HIS C . n 
C 1 216 SER 216 216 216 SER SER C . n 
C 1 217 SER 217 217 217 SER SER C . n 
C 1 218 PRO 218 218 218 PRO PRO C . n 
C 1 219 GLU 219 219 219 GLU GLU C . n 
C 1 220 TYR 220 220 220 TYR TYR C . n 
C 1 221 TRP 221 221 221 TRP TRP C . n 
C 1 222 ILE 222 222 222 ILE ILE C . n 
C 1 223 LYS 223 223 223 LYS LYS C . n 
C 1 224 SER 224 224 224 SER SER C . n 
C 1 225 GLY 225 225 225 GLY GLY C . n 
C 1 226 THR 226 226 226 THR THR C . n 
C 1 227 LEU 227 227 227 LEU LEU C . n 
C 1 228 VAL 228 228 228 VAL VAL C . n 
C 1 229 PRO 229 229 229 PRO PRO C . n 
C 1 230 VAL 230 230 230 VAL VAL C . n 
C 1 231 THR 231 231 231 THR THR C . n 
C 1 232 ARG 232 232 232 ARG ARG C . n 
C 1 233 ASN 233 233 233 ASN ASN C . n 
C 1 234 ASP 234 234 234 ASP ASP C . n 
C 1 235 ILE 235 235 235 ILE ILE C . n 
C 1 236 VAL 236 236 236 VAL VAL C . n 
C 1 237 LYS 237 237 237 LYS LYS C . n 
C 1 238 ILE 238 238 238 ILE ILE C . n 
C 1 239 GLU 239 239 239 GLU GLU C . n 
C 1 240 GLY 240 240 240 GLY GLY C . n 
C 1 241 ILE 241 241 241 ILE ILE C . n 
C 1 242 ASP 242 242 242 ASP ASP C . n 
C 1 243 ALA 243 243 243 ALA ALA C . n 
C 1 244 THR 244 244 244 THR THR C . n 
C 1 245 GLY 245 245 245 GLY GLY C . n 
C 1 246 GLY 246 246 246 GLY GLY C . n 
C 1 247 ASN 247 247 247 ASN ASN C . n 
C 1 248 ASN 248 248 248 ASN ASN C . n 
C 1 249 GLN 249 249 249 GLN GLN C . n 
C 1 250 PRO 250 250 250 PRO PRO C . n 
C 1 251 ASN 251 251 251 ASN ASN C . n 
C 1 252 ILE 252 252 252 ILE ILE C . n 
C 1 253 PRO 253 253 253 PRO PRO C . n 
C 1 254 ASP 254 254 254 ASP ASP C . n 
C 1 255 ILE 255 255 255 ILE ILE C . n 
C 1 256 PRO 256 256 256 PRO PRO C . n 
C 1 257 ALA 257 257 257 ALA ALA C . n 
C 1 258 HIS 258 258 258 HIS HIS C . n 
C 1 259 LEU 259 259 259 LEU LEU C . n 
C 1 260 TRP 260 260 260 TRP TRP C . n 
C 1 261 TYR 261 261 261 TYR TYR C . n 
C 1 262 PHE 262 262 262 PHE PHE C . n 
C 1 263 GLY 263 263 263 GLY GLY C . n 
C 1 264 LEU 264 264 264 LEU LEU C . n 
C 1 265 ILE 265 265 265 ILE ILE C . n 
C 1 266 GLY 266 266 266 GLY GLY C . n 
C 1 267 THR 267 267 267 THR THR C . n 
C 1 268 CYS 268 268 268 CYS CYS C . n 
C 1 269 LEU 269 269 269 LEU LEU C . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 PLC 1  601 1   PLC PHC A . 
E 2 PLC 1  701 1   PLC PHC B . 
F 2 PLC 1  801 1   PLC PHC C . 
G 3 HOH 1  602 1   HOH WAT A . 
G 3 HOH 2  603 2   HOH WAT A . 
G 3 HOH 3  604 3   HOH WAT A . 
G 3 HOH 4  605 4   HOH WAT A . 
G 3 HOH 5  606 5   HOH WAT A . 
G 3 HOH 6  607 6   HOH WAT A . 
G 3 HOH 7  608 7   HOH WAT A . 
G 3 HOH 8  609 8   HOH WAT A . 
G 3 HOH 9  610 9   HOH WAT A . 
G 3 HOH 10 611 10  HOH WAT A . 
G 3 HOH 11 612 11  HOH WAT A . 
G 3 HOH 12 613 12  HOH WAT A . 
G 3 HOH 13 614 13  HOH WAT A . 
G 3 HOH 14 615 14  HOH WAT A . 
G 3 HOH 15 616 15  HOH WAT A . 
G 3 HOH 16 617 16  HOH WAT A . 
G 3 HOH 17 618 17  HOH WAT A . 
G 3 HOH 18 619 18  HOH WAT A . 
G 3 HOH 19 620 19  HOH WAT A . 
G 3 HOH 20 621 20  HOH WAT A . 
G 3 HOH 21 622 21  HOH WAT A . 
G 3 HOH 22 623 22  HOH WAT A . 
G 3 HOH 23 624 23  HOH WAT A . 
G 3 HOH 24 625 24  HOH WAT A . 
G 3 HOH 25 626 25  HOH WAT A . 
G 3 HOH 26 627 26  HOH WAT A . 
G 3 HOH 27 628 27  HOH WAT A . 
G 3 HOH 28 629 28  HOH WAT A . 
G 3 HOH 29 630 29  HOH WAT A . 
G 3 HOH 30 631 30  HOH WAT A . 
G 3 HOH 31 632 31  HOH WAT A . 
G 3 HOH 32 633 32  HOH WAT A . 
G 3 HOH 33 634 33  HOH WAT A . 
G 3 HOH 34 635 34  HOH WAT A . 
G 3 HOH 35 636 35  HOH WAT A . 
G 3 HOH 36 637 36  HOH WAT A . 
G 3 HOH 37 638 37  HOH WAT A . 
G 3 HOH 38 639 38  HOH WAT A . 
G 3 HOH 39 640 39  HOH WAT A . 
G 3 HOH 40 641 40  HOH WAT A . 
G 3 HOH 41 642 41  HOH WAT A . 
G 3 HOH 42 643 42  HOH WAT A . 
G 3 HOH 43 644 43  HOH WAT A . 
G 3 HOH 44 645 44  HOH WAT A . 
G 3 HOH 45 646 45  HOH WAT A . 
G 3 HOH 46 647 46  HOH WAT A . 
G 3 HOH 47 648 47  HOH WAT A . 
G 3 HOH 48 649 48  HOH WAT A . 
G 3 HOH 49 650 49  HOH WAT A . 
G 3 HOH 50 651 50  HOH WAT A . 
G 3 HOH 51 652 51  HOH WAT A . 
G 3 HOH 52 653 52  HOH WAT A . 
G 3 HOH 53 654 53  HOH WAT A . 
G 3 HOH 54 655 54  HOH WAT A . 
G 3 HOH 55 656 55  HOH WAT A . 
G 3 HOH 56 657 101 HOH WAT A . 
G 3 HOH 57 658 102 HOH WAT A . 
G 3 HOH 58 659 103 HOH WAT A . 
G 3 HOH 59 660 104 HOH WAT A . 
G 3 HOH 60 661 105 HOH WAT A . 
G 3 HOH 61 662 106 HOH WAT A . 
G 3 HOH 62 663 107 HOH WAT A . 
G 3 HOH 63 664 108 HOH WAT A . 
G 3 HOH 64 665 109 HOH WAT A . 
G 3 HOH 65 666 110 HOH WAT A . 
G 3 HOH 66 667 111 HOH WAT A . 
G 3 HOH 67 668 112 HOH WAT A . 
G 3 HOH 68 669 113 HOH WAT A . 
H 3 HOH 1  702 1   HOH WAT B . 
H 3 HOH 2  703 2   HOH WAT B . 
H 3 HOH 3  704 3   HOH WAT B . 
H 3 HOH 4  705 4   HOH WAT B . 
H 3 HOH 5  706 5   HOH WAT B . 
H 3 HOH 6  707 6   HOH WAT B . 
H 3 HOH 7  708 7   HOH WAT B . 
H 3 HOH 8  709 8   HOH WAT B . 
H 3 HOH 9  710 9   HOH WAT B . 
H 3 HOH 10 711 10  HOH WAT B . 
H 3 HOH 11 712 11  HOH WAT B . 
H 3 HOH 12 713 12  HOH WAT B . 
H 3 HOH 13 714 13  HOH WAT B . 
H 3 HOH 14 715 14  HOH WAT B . 
H 3 HOH 15 716 15  HOH WAT B . 
H 3 HOH 16 717 16  HOH WAT B . 
H 3 HOH 17 718 17  HOH WAT B . 
H 3 HOH 18 719 18  HOH WAT B . 
H 3 HOH 19 720 19  HOH WAT B . 
H 3 HOH 20 721 20  HOH WAT B . 
H 3 HOH 21 722 21  HOH WAT B . 
H 3 HOH 22 723 22  HOH WAT B . 
H 3 HOH 23 724 23  HOH WAT B . 
H 3 HOH 24 725 24  HOH WAT B . 
H 3 HOH 25 726 25  HOH WAT B . 
H 3 HOH 26 727 26  HOH WAT B . 
H 3 HOH 27 728 27  HOH WAT B . 
H 3 HOH 28 729 29  HOH WAT B . 
H 3 HOH 29 730 30  HOH WAT B . 
H 3 HOH 30 731 31  HOH WAT B . 
H 3 HOH 31 732 32  HOH WAT B . 
H 3 HOH 32 733 33  HOH WAT B . 
H 3 HOH 33 734 34  HOH WAT B . 
H 3 HOH 34 735 35  HOH WAT B . 
H 3 HOH 35 736 36  HOH WAT B . 
H 3 HOH 36 737 37  HOH WAT B . 
H 3 HOH 37 738 38  HOH WAT B . 
H 3 HOH 38 739 39  HOH WAT B . 
H 3 HOH 39 740 40  HOH WAT B . 
H 3 HOH 40 741 41  HOH WAT B . 
H 3 HOH 41 742 42  HOH WAT B . 
H 3 HOH 42 743 43  HOH WAT B . 
H 3 HOH 43 744 44  HOH WAT B . 
H 3 HOH 44 745 45  HOH WAT B . 
H 3 HOH 45 746 46  HOH WAT B . 
H 3 HOH 46 747 47  HOH WAT B . 
H 3 HOH 47 748 48  HOH WAT B . 
H 3 HOH 48 749 49  HOH WAT B . 
H 3 HOH 49 750 50  HOH WAT B . 
H 3 HOH 50 751 51  HOH WAT B . 
H 3 HOH 51 752 52  HOH WAT B . 
H 3 HOH 52 753 53  HOH WAT B . 
H 3 HOH 53 754 54  HOH WAT B . 
H 3 HOH 54 755 55  HOH WAT B . 
H 3 HOH 55 756 101 HOH WAT B . 
H 3 HOH 56 757 102 HOH WAT B . 
H 3 HOH 57 758 103 HOH WAT B . 
I 3 HOH 1  802 28  HOH WAT C . 
I 3 HOH 2  803 1   HOH WAT C . 
I 3 HOH 3  804 2   HOH WAT C . 
I 3 HOH 4  805 3   HOH WAT C . 
I 3 HOH 5  806 4   HOH WAT C . 
I 3 HOH 6  807 5   HOH WAT C . 
I 3 HOH 7  808 6   HOH WAT C . 
I 3 HOH 8  809 7   HOH WAT C . 
I 3 HOH 9  810 8   HOH WAT C . 
I 3 HOH 10 811 9   HOH WAT C . 
I 3 HOH 11 812 10  HOH WAT C . 
I 3 HOH 12 813 11  HOH WAT C . 
I 3 HOH 13 814 12  HOH WAT C . 
I 3 HOH 14 815 13  HOH WAT C . 
I 3 HOH 15 816 14  HOH WAT C . 
I 3 HOH 16 817 15  HOH WAT C . 
I 3 HOH 17 818 16  HOH WAT C . 
I 3 HOH 18 819 17  HOH WAT C . 
I 3 HOH 19 820 18  HOH WAT C . 
I 3 HOH 20 821 19  HOH WAT C . 
I 3 HOH 21 822 20  HOH WAT C . 
I 3 HOH 22 823 21  HOH WAT C . 
I 3 HOH 23 824 22  HOH WAT C . 
I 3 HOH 24 825 23  HOH WAT C . 
I 3 HOH 25 826 24  HOH WAT C . 
I 3 HOH 26 827 25  HOH WAT C . 
I 3 HOH 27 828 26  HOH WAT C . 
I 3 HOH 28 829 27  HOH WAT C . 
I 3 HOH 29 830 28  HOH WAT C . 
I 3 HOH 30 831 29  HOH WAT C . 
I 3 HOH 31 832 30  HOH WAT C . 
I 3 HOH 32 833 31  HOH WAT C . 
I 3 HOH 33 834 32  HOH WAT C . 
I 3 HOH 34 835 33  HOH WAT C . 
I 3 HOH 35 836 34  HOH WAT C . 
I 3 HOH 36 837 35  HOH WAT C . 
I 3 HOH 37 838 36  HOH WAT C . 
I 3 HOH 38 839 37  HOH WAT C . 
I 3 HOH 39 840 38  HOH WAT C . 
I 3 HOH 40 841 39  HOH WAT C . 
I 3 HOH 41 842 40  HOH WAT C . 
I 3 HOH 42 843 41  HOH WAT C . 
I 3 HOH 43 844 42  HOH WAT C . 
I 3 HOH 44 845 43  HOH WAT C . 
I 3 HOH 45 846 44  HOH WAT C . 
I 3 HOH 46 847 45  HOH WAT C . 
I 3 HOH 47 848 46  HOH WAT C . 
I 3 HOH 48 849 47  HOH WAT C . 
I 3 HOH 49 850 48  HOH WAT C . 
I 3 HOH 50 851 49  HOH WAT C . 
I 3 HOH 51 852 50  HOH WAT C . 
I 3 HOH 52 853 51  HOH WAT C . 
I 3 HOH 53 854 52  HOH WAT C . 
I 3 HOH 54 855 53  HOH WAT C . 
I 3 HOH 55 856 54  HOH WAT C . 
I 3 HOH 56 857 55  HOH WAT C . 
I 3 HOH 57 858 101 HOH WAT C . 
I 3 HOH 58 859 102 HOH WAT C . 
I 3 HOH 59 860 103 HOH WAT C . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,G 
2 1 B,E,H 
3 1 C,F,I 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2000-12-20 
2 'Structure model' 1 1 2008-04-27 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2017-10-04 
5 'Structure model' 1 4 2018-01-31 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' 'Refinement description'    
4 5 'Structure model' 'Experimental preparation'  
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' software           
2 5 'Structure model' exptl_crystal_grow 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 5 'Structure model' '_exptl_crystal_grow.pdbx_details' 
2 5 'Structure model' '_exptl_crystal_grow.temp'         
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
ROTAVATA 'data reduction' .           ? 1 
AMoRE    phasing          .           ? 2 
REFMAC   refinement       .           ? 3 
CCP4     'data scaling'   '(AGROVATA' ? 4 
ROTAVATA 'data scaling'   .           ? 5 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CG A ARG 81  ? ? CD A ARG 81  ? ? NE  A ARG 81  ? ? 130.59 111.80 18.79  2.10 N 
2  1 NE A ARG 84  ? ? CZ A ARG 84  ? ? NH2 A ARG 84  ? ? 116.98 120.30 -3.32  0.50 N 
3  1 CA A TRP 89  ? ? CB A TRP 89  ? ? CG  A TRP 89  ? ? 100.46 113.70 -13.24 1.90 N 
4  1 CD A ARG 118 ? ? NE A ARG 118 ? ? CZ  A ARG 118 ? ? 134.38 123.60 10.78  1.40 N 
5  1 NE A ARG 118 ? ? CZ A ARG 118 ? ? NH1 A ARG 118 ? ? 124.37 120.30 4.07   0.50 N 
6  1 NE A ARG 160 ? ? CZ A ARG 160 ? ? NH1 A ARG 160 ? ? 116.59 120.30 -3.71  0.50 N 
7  1 NE A ARG 205 ? ? CZ A ARG 205 ? ? NH2 A ARG 205 ? ? 123.58 120.30 3.28   0.50 N 
8  1 CB B ASP 5   ? ? CG B ASP 5   ? ? OD1 B ASP 5   ? ? 111.37 118.30 -6.93  0.90 N 
9  1 CD B ARG 81  ? ? NE B ARG 81  ? ? CZ  B ARG 81  ? ? 134.35 123.60 10.75  1.40 N 
10 1 CA B TRP 89  ? ? CB B TRP 89  ? ? CG  B TRP 89  ? ? 100.83 113.70 -12.87 1.90 N 
11 1 CD B ARG 118 ? ? NE B ARG 118 ? ? CZ  B ARG 118 ? ? 133.90 123.60 10.30  1.40 N 
12 1 NE B ARG 118 ? ? CZ B ARG 118 ? ? NH1 B ARG 118 ? ? 125.85 120.30 5.55   0.50 N 
13 1 NE B ARG 118 ? ? CZ B ARG 118 ? ? NH2 B ARG 118 ? ? 116.74 120.30 -3.56  0.50 N 
14 1 CB B ASP 158 ? ? CG B ASP 158 ? ? OD1 B ASP 158 ? ? 125.11 118.30 6.81   0.90 N 
15 1 NE B ARG 160 ? ? CZ B ARG 160 ? ? NH1 B ARG 160 ? ? 114.86 120.30 -5.44  0.50 N 
16 1 CD B ARG 205 ? ? NE B ARG 205 ? ? CZ  B ARG 205 ? ? 132.86 123.60 9.26   1.40 N 
17 1 NE B ARG 205 ? ? CZ B ARG 205 ? ? NH1 B ARG 205 ? ? 116.70 120.30 -3.60  0.50 N 
18 1 NE B ARG 205 ? ? CZ B ARG 205 ? ? NH2 B ARG 205 ? ? 125.52 120.30 5.22   0.50 N 
19 1 CA B LEU 206 ? ? CB B LEU 206 ? ? CG  B LEU 206 ? ? 130.24 115.30 14.94  2.30 N 
20 1 NE B ARG 209 ? ? CZ B ARG 209 ? ? NH2 B ARG 209 ? ? 116.99 120.30 -3.31  0.50 N 
21 1 CB C ASP 5   ? ? CG C ASP 5   ? ? OD1 C ASP 5   ? ? 112.12 118.30 -6.18  0.90 N 
22 1 CD C ARG 81  ? ? NE C ARG 81  ? ? CZ  C ARG 81  ? ? 138.93 123.60 15.33  1.40 N 
23 1 CA C TRP 89  ? ? CB C TRP 89  ? ? CG  C TRP 89  ? ? 101.48 113.70 -12.22 1.90 N 
24 1 NE C ARG 118 ? ? CZ C ARG 118 ? ? NH1 C ARG 118 ? ? 124.40 120.30 4.10   0.50 N 
25 1 CD C ARG 195 ? ? NE C ARG 195 ? ? CZ  C ARG 195 ? ? 135.73 123.60 12.13  1.40 N 
26 1 NE C ARG 195 ? ? CZ C ARG 195 ? ? NH1 C ARG 195 ? ? 116.59 120.30 -3.71  0.50 N 
27 1 NE C ARG 205 ? ? CZ C ARG 205 ? ? NH2 C ARG 205 ? ? 125.60 120.30 5.30   0.50 N 
28 1 NE C ARG 209 ? ? CZ C ARG 209 ? ? NH1 C ARG 209 ? ? 124.69 120.30 4.39   0.50 N 
29 1 NE C ARG 209 ? ? CZ C ARG 209 ? ? NH2 C ARG 209 ? ? 115.01 120.30 -5.29  0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 27  ? ? -143.79 24.51   
2  1 ARG A 84  ? ? -143.54 -56.26  
3  1 SER A 146 ? ? 61.64   -118.20 
4  1 GLN A 188 ? ? -43.15  153.37  
5  1 THR A 199 ? ? 28.01   -100.35 
6  1 LEU A 227 ? ? 83.43   -11.13  
7  1 PHE A 262 ? ? 77.61   -42.40  
8  1 ASP B 27  ? ? -142.45 19.28   
9  1 CYS B 41  ? ? -150.60 71.83   
10 1 ALA B 47  ? ? -56.93  173.96  
11 1 LYS B 74  ? ? 41.57   70.23   
12 1 ARG B 84  ? ? -142.70 -41.48  
13 1 ILE B 100 ? ? -118.92 60.92   
14 1 SER B 146 ? ? 57.12   -121.30 
15 1 GLN B 188 ? ? -47.64  157.64  
16 1 THR B 199 ? ? 33.18   -106.86 
17 1 LEU B 227 ? ? 83.25   -8.03   
18 1 PHE B 262 ? ? 78.90   -17.22  
19 1 ASP C 27  ? ? -144.87 14.25   
20 1 ASP C 62  ? ? 63.73   63.83   
21 1 ARG C 84  ? ? -140.53 -40.43  
22 1 ILE C 100 ? ? -117.42 61.04   
23 1 ASP C 122 ? ? -62.73  -71.23  
24 1 SER C 146 ? ? 60.03   -124.10 
25 1 THR C 199 ? ? 30.96   -105.73 
26 1 PRO C 218 ? ? -91.17  -157.98 
27 1 LEU C 227 ? ? 88.27   -17.56  
28 1 ASN C 248 ? ? -68.34  95.30   
29 1 PHE C 262 ? ? 81.35   -39.49  
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1  1 SER A 3   ? ? -10.84 
2  1 CYS A 41  ? ? -12.09 
3  1 ASN A 92  ? ? 13.01  
4  1 GLU A 129 ? ? -11.72 
5  1 GLU A 134 ? ? 10.51  
6  1 VAL A 141 ? ? 10.83  
7  1 TYR A 164 ? ? 10.47  
8  1 ASN A 178 ? ? -11.51 
9  1 SER A 214 ? ? -10.74 
10 1 ILE A 235 ? ? 10.22  
11 1 ILE A 265 ? ? 11.39  
12 1 TYR B 21  ? ? 10.78  
13 1 ASN B 33  ? ? -10.74 
14 1 ILE B 76  ? ? 10.62  
15 1 ASN B 94  ? ? -15.00 
16 1 PHE B 113 ? ? -12.27 
17 1 ASP B 165 ? ? 12.64  
18 1 PRO B 250 ? ? 10.23  
19 1 SER C 3   ? ? -10.55 
20 1 CYS C 41  ? ? -15.20 
21 1 PHE C 51  ? ? 10.22  
22 1 LEU C 67  ? ? 14.14  
23 1 LEU C 69  ? ? 17.08  
24 1 GLU C 87  ? ? -11.79 
25 1 GLY C 91  ? ? -16.14 
26 1 GLU C 134 ? ? 14.93  
27 1 VAL C 203 ? ? -11.61 
28 1 PHE C 262 ? ? -10.80 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ARG 133 ? NE  ? A ARG 133 NE  
2  1 Y 1 A ARG 133 ? CZ  ? A ARG 133 CZ  
3  1 Y 1 A ARG 133 ? NH1 ? A ARG 133 NH1 
4  1 Y 1 A ARG 133 ? NH2 ? A ARG 133 NH2 
5  1 Y 1 A GLU 134 ? CD  ? A GLU 134 CD  
6  1 Y 1 A GLU 134 ? OE1 ? A GLU 134 OE1 
7  1 Y 1 A GLU 134 ? OE2 ? A GLU 134 OE2 
8  1 Y 1 B ARG 133 ? NE  ? B ARG 133 NE  
9  1 Y 1 B ARG 133 ? CZ  ? B ARG 133 CZ  
10 1 Y 1 B ARG 133 ? NH1 ? B ARG 133 NH1 
11 1 Y 1 B ARG 133 ? NH2 ? B ARG 133 NH2 
12 1 Y 1 B GLU 134 ? CD  ? B GLU 134 CD  
13 1 Y 1 B GLU 134 ? OE1 ? B GLU 134 OE1 
14 1 Y 1 B GLU 134 ? OE2 ? B GLU 134 OE2 
15 1 Y 1 C ARG 133 ? NE  ? C ARG 133 NE  
16 1 Y 1 C ARG 133 ? CZ  ? C ARG 133 CZ  
17 1 Y 1 C ARG 133 ? NH1 ? C ARG 133 NH1 
18 1 Y 1 C ARG 133 ? NH2 ? C ARG 133 NH2 
19 1 Y 1 C GLU 134 ? CD  ? C GLU 134 CD  
20 1 Y 1 C GLU 134 ? OE1 ? C GLU 134 OE1 
21 1 Y 1 C GLU 134 ? OE2 ? C GLU 134 OE2 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'DIUNDECYL PHOSPHATIDYL CHOLINE' PLC 
3 water                            HOH 
# 


A second structure was input as follows:


data_1DT3
# 
_entry.id   1DT3 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.289 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1DT3         
RCSB  RCSB010343   
WWPDB D_1000010343 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1DT3 
_pdbx_database_status.recvd_initial_deposition_date   2000-01-11 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Brozozowski, A.M.' 1 
'Savage, H.'        2 
# 
_citation.id                        primary 
_citation.title                     'Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase.' 
_citation.journal_abbrev            Biochemistry 
_citation.journal_volume            39 
_citation.page_first                15071 
_citation.page_last                 15082 
_citation.year                      2000 
_citation.journal_id_ASTM           BICHAW 
_citation.country                   US 
_citation.journal_id_ISSN           0006-2960 
_citation.journal_id_CSD            0033 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   11106485 
_citation.pdbx_database_id_DOI      10.1021/bi0013905 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Brzozowski, A.M.' 1 
primary 'Savage, H.'       2 
primary 'Verma, C.S.'      3 
primary 'Turkenburg, J.P.' 4 
primary 'Lawson, D.M.'     5 
primary 'Svendsen, A.'     6 
primary 'Patkar, S.'       7 
# 
_cell.entry_id           1DT3 
_cell.length_a           139.920 
_cell.length_b           139.920 
_cell.length_c           80.680 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1DT3 
_symmetry.space_group_name_H-M             'P 61' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                169 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer nat LIPASE 29342.484 2   3.1.1.3 ? ? ? 
2 water   nat water  18.015    242 ?       ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;EVSQDLFNQFNLFAQYSAAAYCGKNNDAPAGTNITCTGNACPEVEKADATFLYSFEDSGVGDVTGFLALDNTNKLIVLSF
RGSRSIENWIGNLNFDLKEINDICSGCRGHDGFTSSWRSVADTLRQKVEDAVREHPDYRVVFTGHSLGGALATVAGADLR
GNGYDIDVFSYGAPRVGNRAFAEFLTVQTGGTLYRITHTNDIVPRLPPREFGYSHSSPEYWIKSGTLVPVTRNDIVKIEG
IDATGGNNQPNIPDIPAHLWYFGLIGTCL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;EVSQDLFNQFNLFAQYSAAAYCGKNNDAPAGTNITCTGNACPEVEKADATFLYSFEDSGVGDVTGFLALDNTNKLIVLSF
RGSRSIENWIGNLNFDLKEINDICSGCRGHDGFTSSWRSVADTLRQKVEDAVREHPDYRVVFTGHSLGGALATVAGADLR
GNGYDIDVFSYGAPRVGNRAFAEFLTVQTGGTLYRITHTNDIVPRLPPREFGYSHSSPEYWIKSGTLVPVTRNDIVKIEG
IDATGGNNQPNIPDIPAHLWYFGLIGTCL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLU n 
1 2   VAL n 
1 3   SER n 
1 4   GLN n 
1 5   ASP n 
1 6   LEU n 
1 7   PHE n 
1 8   ASN n 
1 9   GLN n 
1 10  PHE n 
1 11  ASN n 
1 12  LEU n 
1 13  PHE n 
1 14  ALA n 
1 15  GLN n 
1 16  TYR n 
1 17  SER n 
1 18  ALA n 
1 19  ALA n 
1 20  ALA n 
1 21  TYR n 
1 22  CYS n 
1 23  GLY n 
1 24  LYS n 
1 25  ASN n 
1 26  ASN n 
1 27  ASP n 
1 28  ALA n 
1 29  PRO n 
1 30  ALA n 
1 31  GLY n 
1 32  THR n 
1 33  ASN n 
1 34  ILE n 
1 35  THR n 
1 36  CYS n 
1 37  THR n 
1 38  GLY n 
1 39  ASN n 
1 40  ALA n 
1 41  CYS n 
1 42  PRO n 
1 43  GLU n 
1 44  VAL n 
1 45  GLU n 
1 46  LYS n 
1 47  ALA n 
1 48  ASP n 
1 49  ALA n 
1 50  THR n 
1 51  PHE n 
1 52  LEU n 
1 53  TYR n 
1 54  SER n 
1 55  PHE n 
1 56  GLU n 
1 57  ASP n 
1 58  SER n 
1 59  GLY n 
1 60  VAL n 
1 61  GLY n 
1 62  ASP n 
1 63  VAL n 
1 64  THR n 
1 65  GLY n 
1 66  PHE n 
1 67  LEU n 
1 68  ALA n 
1 69  LEU n 
1 70  ASP n 
1 71  ASN n 
1 72  THR n 
1 73  ASN n 
1 74  LYS n 
1 75  LEU n 
1 76  ILE n 
1 77  VAL n 
1 78  LEU n 
1 79  SER n 
1 80  PHE n 
1 81  ARG n 
1 82  GLY n 
1 83  SER n 
1 84  ARG n 
1 85  SER n 
1 86  ILE n 
1 87  GLU n 
1 88  ASN n 
1 89  TRP n 
1 90  ILE n 
1 91  GLY n 
1 92  ASN n 
1 93  LEU n 
1 94  ASN n 
1 95  PHE n 
1 96  ASP n 
1 97  LEU n 
1 98  LYS n 
1 99  GLU n 
1 100 ILE n 
1 101 ASN n 
1 102 ASP n 
1 103 ILE n 
1 104 CYS n 
1 105 SER n 
1 106 GLY n 
1 107 CYS n 
1 108 ARG n 
1 109 GLY n 
1 110 HIS n 
1 111 ASP n 
1 112 GLY n 
1 113 PHE n 
1 114 THR n 
1 115 SER n 
1 116 SER n 
1 117 TRP n 
1 118 ARG n 
1 119 SER n 
1 120 VAL n 
1 121 ALA n 
1 122 ASP n 
1 123 THR n 
1 124 LEU n 
1 125 ARG n 
1 126 GLN n 
1 127 LYS n 
1 128 VAL n 
1 129 GLU n 
1 130 ASP n 
1 131 ALA n 
1 132 VAL n 
1 133 ARG n 
1 134 GLU n 
1 135 HIS n 
1 136 PRO n 
1 137 ASP n 
1 138 TYR n 
1 139 ARG n 
1 140 VAL n 
1 141 VAL n 
1 142 PHE n 
1 143 THR n 
1 144 GLY n 
1 145 HIS n 
1 146 SER n 
1 147 LEU n 
1 148 GLY n 
1 149 GLY n 
1 150 ALA n 
1 151 LEU n 
1 152 ALA n 
1 153 THR n 
1 154 VAL n 
1 155 ALA n 
1 156 GLY n 
1 157 ALA n 
1 158 ASP n 
1 159 LEU n 
1 160 ARG n 
1 161 GLY n 
1 162 ASN n 
1 163 GLY n 
1 164 TYR n 
1 165 ASP n 
1 166 ILE n 
1 167 ASP n 
1 168 VAL n 
1 169 PHE n 
1 170 SER n 
1 171 TYR n 
1 172 GLY n 
1 173 ALA n 
1 174 PRO n 
1 175 ARG n 
1 176 VAL n 
1 177 GLY n 
1 178 ASN n 
1 179 ARG n 
1 180 ALA n 
1 181 PHE n 
1 182 ALA n 
1 183 GLU n 
1 184 PHE n 
1 185 LEU n 
1 186 THR n 
1 187 VAL n 
1 188 GLN n 
1 189 THR n 
1 190 GLY n 
1 191 GLY n 
1 192 THR n 
1 193 LEU n 
1 194 TYR n 
1 195 ARG n 
1 196 ILE n 
1 197 THR n 
1 198 HIS n 
1 199 THR n 
1 200 ASN n 
1 201 ASP n 
1 202 ILE n 
1 203 VAL n 
1 204 PRO n 
1 205 ARG n 
1 206 LEU n 
1 207 PRO n 
1 208 PRO n 
1 209 ARG n 
1 210 GLU n 
1 211 PHE n 
1 212 GLY n 
1 213 TYR n 
1 214 SER n 
1 215 HIS n 
1 216 SER n 
1 217 SER n 
1 218 PRO n 
1 219 GLU n 
1 220 TYR n 
1 221 TRP n 
1 222 ILE n 
1 223 LYS n 
1 224 SER n 
1 225 GLY n 
1 226 THR n 
1 227 LEU n 
1 228 VAL n 
1 229 PRO n 
1 230 VAL n 
1 231 THR n 
1 232 ARG n 
1 233 ASN n 
1 234 ASP n 
1 235 ILE n 
1 236 VAL n 
1 237 LYS n 
1 238 ILE n 
1 239 GLU n 
1 240 GLY n 
1 241 ILE n 
1 242 ASP n 
1 243 ALA n 
1 244 THR n 
1 245 GLY n 
1 246 GLY n 
1 247 ASN n 
1 248 ASN n 
1 249 GLN n 
1 250 PRO n 
1 251 ASN n 
1 252 ILE n 
1 253 PRO n 
1 254 ASP n 
1 255 ILE n 
1 256 PRO n 
1 257 ALA n 
1 258 HIS n 
1 259 LEU n 
1 260 TRP n 
1 261 TYR n 
1 262 PHE n 
1 263 GLY n 
1 264 LEU n 
1 265 ILE n 
1 266 GLY n 
1 267 THR n 
1 268 CYS n 
1 269 LEU n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           ? 
_entity_src_nat.pdbx_end_seq_num           ? 
_entity_src_nat.common_name                ? 
_entity_src_nat.pdbx_organism_scientific   'Thermomyces lanuginosus' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      5541 
_entity_src_nat.genus                      Thermomyces 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    LIP_THELA 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          O59952 
_struct_ref.pdbx_align_begin           23 
_struct_ref.pdbx_seq_one_letter_code   
;EVSQDLFNQFNLFAQYSAAAYCGKNNDAPAGTNITCTGNACPEVEKADATFLYSFEDSGVGDVTGFLALDNTNKLIVLSF
RGSRSIENWIGNLNFDLKEINDICSGCRGHDGFTSSWRSVADTLRQKVEDAVREHPDYRVVFTGHSLGGALATVAGADLR
GNGYDIDVFSYGAPRVGNRAFAEFLTVQTGGTLYRITHTNDIVPRLPPREFGYSHSSPEYWIKSGTLVPVTRNDIVKIEG
IDATGGNNQPNIPDIPAHLWYFGLIGTCL
;
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 1DT3 A 1 ? 269 ? O59952 23 ? 291 ? 1 269 
2 1 1DT3 B 1 ? 269 ? O59952 23 ? 291 ? 1 269 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          1DT3 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.88 
_exptl_crystal.density_percent_sol   68.33 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            279.0 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              8.1 
_exptl_crystal_grow.pdbx_details    'PEG 5000, magnesium chloride, , pH 8.1, VAPOR DIFFUSION, HANGING DROP, temperature 6K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           110 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   1999-03-06 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'RIGAKU RU200' 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             1.5418 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     1DT3 
_reflns.observed_criterion_sigma_I   2.0 
_reflns.observed_criterion_sigma_F   2.0 
_reflns.d_resolution_low             20 
_reflns.d_resolution_high            2.6 
_reflns.number_obs                   26160 
_reflns.number_all                   27814 
_reflns.percent_possible_obs         94 
_reflns.pdbx_Rmerge_I_obs            0.052 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        26 
_reflns.B_iso_Wilson_estimate        55 
_reflns.pdbx_redundancy              5 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             2.6 
_reflns_shell.d_res_low              20.0 
_reflns_shell.percent_possible_all   99.6 
_reflns_shell.Rmerge_I_obs           0.048 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        26 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      26160 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1DT3 
_refine.ls_number_reflns_obs                     26160 
_refine.ls_number_reflns_all                     27814 
_refine.pdbx_ls_sigma_I                          0.0 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_d_res_low                             20.0 
_refine.ls_d_res_high                            2.6 
_refine.ls_percent_reflns_obs                    99.4 
_refine.ls_R_factor_obs                          0.228 
_refine.ls_R_factor_all                          0.228 
_refine.ls_R_factor_R_work                       0.228 
_refine.ls_R_factor_R_free                       0.288 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  1390 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  
;rms bond  = 0.013A 
rms angle = 0.041A
;
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       
;rms bond = 0.02A 
rms angle = 0.06A
;
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            '5% of total data set used' 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4142 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             242 
_refine_hist.number_atoms_total               4384 
_refine_hist.d_res_high                       2.6 
_refine_hist.d_res_low                        20.0 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
x_bond_d    0.02 ? ? ? 'X-RAY DIFFRACTION' ? 
t_angle_deg 0.06 ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_struct.entry_id                  1DT3 
_struct.title                     'THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE' 
_struct.pdbx_descriptor           'LIPASE (E.C.3.1.1.3)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1DT3 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            'lipase, thermomyces linuginosa, interfacial activation, HYDROLASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
# 
loop_
_struct_biol.id 
_struct_biol.details 
_struct_biol.pdbx_parent_biol_id 
1 'The biological assembly is a monomer' ? 
2 ?                                      ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  SER A 3   ? CYS A 22  ? SER A 3   CYS A 22  1 ? 20 
HELX_P HELX_P2  2  CYS A 41  ? ALA A 47  ? CYS A 41  ALA A 47  1 ? 7  
HELX_P HELX_P3  3  SER A 85  ? ASN A 92  ? SER A 85  ASN A 92  1 ? 8  
HELX_P HELX_P4  4  ASP A 111 ? SER A 119 ? ASP A 111 SER A 119 1 ? 9  
HELX_P HELX_P5  5  VAL A 120 ? HIS A 135 ? VAL A 120 HIS A 135 1 ? 16 
HELX_P HELX_P6  6  SER A 146 ? ARG A 160 ? SER A 146 ARG A 160 1 ? 15 
HELX_P HELX_P7  7  ASN A 178 ? GLN A 188 ? ASN A 178 GLN A 188 1 ? 11 
HELX_P HELX_P8  8  ILE A 202 ? LEU A 206 ? ILE A 202 LEU A 206 5 ? 5  
HELX_P HELX_P9  9  PRO A 208 ? GLY A 212 ? PRO A 208 GLY A 212 5 ? 5  
HELX_P HELX_P10 10 THR A 231 ? ASN A 233 ? THR A 231 ASN A 233 5 ? 3  
HELX_P HELX_P11 11 ASP A 254 ? LEU A 259 ? ASP A 254 LEU A 259 1 ? 6  
HELX_P HELX_P12 12 SER B 3   ? ALA B 20  ? SER B 3   ALA B 20  1 ? 18 
HELX_P HELX_P13 13 CYS B 41  ? ALA B 47  ? CYS B 41  ALA B 47  1 ? 7  
HELX_P HELX_P14 14 SER B 85  ? ASN B 92  ? SER B 85  ASN B 92  1 ? 8  
HELX_P HELX_P15 15 ASN B 101 ? CYS B 104 ? ASN B 101 CYS B 104 5 ? 4  
HELX_P HELX_P16 16 ASP B 111 ? HIS B 135 ? ASP B 111 HIS B 135 1 ? 25 
HELX_P HELX_P17 17 SER B 146 ? ARG B 160 ? SER B 146 ARG B 160 1 ? 15 
HELX_P HELX_P18 18 ASN B 178 ? GLN B 188 ? ASN B 178 GLN B 188 1 ? 11 
HELX_P HELX_P19 19 ILE B 202 ? LEU B 206 ? ILE B 202 LEU B 206 5 ? 5  
HELX_P HELX_P20 20 PRO B 208 ? GLY B 212 ? PRO B 208 GLY B 212 5 ? 5  
HELX_P HELX_P21 21 THR B 231 ? ASN B 233 ? THR B 231 ASN B 233 5 ? 3  
HELX_P HELX_P22 22 ILE B 255 ? LEU B 259 ? ILE B 255 LEU B 259 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1 disulf ? ? A CYS 22  SG ? ? ? 1_555 A CYS 268 SG ? ? A CYS 22  A CYS 268 1_555 ? ? ? ? ? ? ? 2.009 ? 
disulf2 disulf ? ? A CYS 36  SG ? ? ? 1_555 A CYS 41  SG ? ? A CYS 36  A CYS 41  1_555 ? ? ? ? ? ? ? 2.056 ? 
disulf3 disulf ? ? A CYS 104 SG ? ? ? 1_555 A CYS 107 SG ? ? A CYS 104 A CYS 107 1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf4 disulf ? ? B CYS 22  SG ? ? ? 1_555 B CYS 268 SG ? ? B CYS 22  B CYS 268 1_555 ? ? ? ? ? ? ? 1.970 ? 
disulf5 disulf ? ? B CYS 36  SG ? ? ? 1_555 B CYS 41  SG ? ? B CYS 36  B CYS 41  1_555 ? ? ? ? ? ? ? 2.055 ? 
disulf6 disulf ? ? B CYS 104 SG ? ? ? 1_555 B CYS 107 SG ? ? B CYS 104 B CYS 107 1_555 ? ? ? ? ? ? ? 2.044 ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LEU 206 A . ? LEU 206 A PRO 207 A ? PRO 207 A 1 -8.75 
2 SER 217 A . ? SER 217 A PRO 218 A ? PRO 218 A 1 4.21  
3 LEU 206 B . ? LEU 206 B PRO 207 B ? PRO 207 B 1 -7.30 
4 SER 217 B . ? SER 217 B PRO 218 B ? PRO 218 B 1 -2.31 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 8 ? 
B ? 2 ? 
C ? 8 ? 
D ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? parallel      
A 4 5 ? parallel      
A 5 6 ? parallel      
A 6 7 ? parallel      
A 7 8 ? anti-parallel 
B 1 2 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? parallel      
C 4 5 ? parallel      
C 5 6 ? parallel      
C 6 7 ? parallel      
C 7 8 ? anti-parallel 
D 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ALA A 49  ? SER A 58  ? ALA A 49  SER A 58  
A 2 VAL A 63  ? ASP A 70  ? VAL A 63  ASP A 70  
A 3 LEU A 75  ? PHE A 80  ? LEU A 75  PHE A 80  
A 4 ARG A 139 ? HIS A 145 ? ARG A 139 HIS A 145 
A 5 ASP A 167 ? TYR A 171 ? ASP A 167 TYR A 171 
A 6 LEU A 193 ? HIS A 198 ? LEU A 193 HIS A 198 
A 7 GLU A 219 ? ILE A 222 ? GLU A 219 ILE A 222 
A 8 ILE A 235 ? ILE A 238 ? ILE A 235 ILE A 238 
B 1 LEU A 97  ? GLU A 99  ? LEU A 97  GLU A 99  
B 2 ARG A 108 ? HIS A 110 ? ARG A 108 HIS A 110 
C 1 ALA B 49  ? SER B 58  ? ALA B 49  SER B 58  
C 2 VAL B 63  ? ASP B 70  ? VAL B 63  ASP B 70  
C 3 LEU B 75  ? PHE B 80  ? LEU B 75  PHE B 80  
C 4 ARG B 139 ? HIS B 145 ? ARG B 139 HIS B 145 
C 5 ILE B 166 ? TYR B 171 ? ILE B 166 TYR B 171 
C 6 LEU B 193 ? HIS B 198 ? LEU B 193 HIS B 198 
C 7 GLU B 219 ? ILE B 222 ? GLU B 219 ILE B 222 
C 8 ILE B 235 ? ILE B 238 ? ILE B 235 ILE B 238 
D 1 LEU B 97  ? GLU B 99  ? LEU B 97  GLU B 99  
D 2 ARG B 108 ? HIS B 110 ? ARG B 108 HIS B 110 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 N SER A 58  ? N SER A 58  O VAL A 63  ? O VAL A 63  
A 2 3 N ASP A 70  ? N ASP A 70  O LEU A 75  ? O LEU A 75  
A 3 4 N ILE A 76  ? N ILE A 76  O ARG A 139 ? O ARG A 139 
A 4 5 N PHE A 142 ? N PHE A 142 O ASP A 167 ? O ASP A 167 
A 5 6 O VAL A 168 ? O VAL A 168 N TYR A 194 ? N TYR A 194 
A 6 7 N THR A 197 ? N THR A 197 O TYR A 220 ? O TYR A 220 
A 7 8 N TRP A 221 ? N TRP A 221 O VAL A 236 ? O VAL A 236 
B 1 2 O LYS A 98  ? O LYS A 98  N GLY A 109 ? N GLY A 109 
C 1 2 N SER B 58  ? N SER B 58  O VAL B 63  ? O VAL B 63  
C 2 3 N ASP B 70  ? N ASP B 70  O LEU B 75  ? O LEU B 75  
C 3 4 N ILE B 76  ? N ILE B 76  O ARG B 139 ? O ARG B 139 
C 4 5 N PHE B 142 ? N PHE B 142 O ASP B 167 ? O ASP B 167 
C 5 6 O VAL B 168 ? O VAL B 168 N TYR B 194 ? N TYR B 194 
C 6 7 O ARG B 195 ? O ARG B 195 N TYR B 220 ? N TYR B 220 
C 7 8 O TRP B 221 ? O TRP B 221 N VAL B 236 ? N VAL B 236 
D 1 2 O LYS B 98  ? O LYS B 98  N GLY B 109 ? N GLY B 109 
# 
_database_PDB_matrix.entry_id          1DT3 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    1DT3 
_atom_sites.fract_transf_matrix[1][1]   0.007147 
_atom_sites.fract_transf_matrix[1][2]   0.004126 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008253 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.012395 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLU A 1 1   ? 71.730 9.217   54.158 1.00 49.98  ? 1   GLU A N   1 
ATOM   2    C CA  . GLU A 1 1   ? 71.310 10.231  55.142 1.00 49.84  ? 1   GLU A CA  1 
ATOM   3    C C   . GLU A 1 1   ? 70.703 9.809   56.467 1.00 47.97  ? 1   GLU A C   1 
ATOM   4    O O   . GLU A 1 1   ? 70.713 10.725  57.317 1.00 49.31  ? 1   GLU A O   1 
ATOM   5    C CB  . GLU A 1 1   ? 70.505 11.362  54.526 1.00 54.70  ? 1   GLU A CB  1 
ATOM   6    C CG  . GLU A 1 1   ? 70.854 11.669  53.097 1.00 64.91  ? 1   GLU A CG  1 
ATOM   7    C CD  . GLU A 1 1   ? 72.326 11.852  52.782 1.00 69.62  ? 1   GLU A CD  1 
ATOM   8    O OE1 . GLU A 1 1   ? 73.093 12.209  53.705 1.00 71.59  ? 1   GLU A OE1 1 
ATOM   9    O OE2 . GLU A 1 1   ? 72.662 11.626  51.585 1.00 71.70  ? 1   GLU A OE2 1 
ATOM   10   N N   . VAL A 1 2   ? 70.267 8.630   56.824 1.00 45.27  ? 2   VAL A N   1 
ATOM   11   C CA  . VAL A 1 2   ? 70.037 8.340   58.244 1.00 43.07  ? 2   VAL A CA  1 
ATOM   12   C C   . VAL A 1 2   ? 70.957 7.142   58.579 1.00 42.30  ? 2   VAL A C   1 
ATOM   13   O O   . VAL A 1 2   ? 71.496 6.548   57.636 1.00 42.75  ? 2   VAL A O   1 
ATOM   14   C CB  . VAL A 1 2   ? 68.601 8.099   58.682 1.00 39.40  ? 2   VAL A CB  1 
ATOM   15   C CG1 . VAL A 1 2   ? 67.713 9.259   58.282 1.00 40.78  ? 2   VAL A CG1 1 
ATOM   16   C CG2 . VAL A 1 2   ? 67.951 6.795   58.219 1.00 36.28  ? 2   VAL A CG2 1 
ATOM   17   N N   . SER A 1 3   ? 70.992 6.662   59.802 1.00 39.75  ? 3   SER A N   1 
ATOM   18   C CA  . SER A 1 3   ? 71.811 5.533   60.127 1.00 39.24  ? 3   SER A CA  1 
ATOM   19   C C   . SER A 1 3   ? 71.130 4.202   59.830 1.00 39.51  ? 3   SER A C   1 
ATOM   20   O O   . SER A 1 3   ? 69.908 3.998   59.969 1.00 39.71  ? 3   SER A O   1 
ATOM   21   C CB  . SER A 1 3   ? 72.218 5.652   61.601 1.00 38.00  ? 3   SER A CB  1 
ATOM   22   O OG  . SER A 1 3   ? 71.130 5.216   62.424 1.00 41.99  ? 3   SER A OG  1 
ATOM   23   N N   . GLN A 1 4   ? 71.951 3.148   59.723 1.00 38.94  ? 4   GLN A N   1 
ATOM   24   C CA  . GLN A 1 4   ? 71.505 1.790   59.478 1.00 38.61  ? 4   GLN A CA  1 
ATOM   25   C C   . GLN A 1 4   ? 70.564 1.293   60.563 1.00 38.16  ? 4   GLN A C   1 
ATOM   26   O O   . GLN A 1 4   ? 69.542 0.618   60.389 1.00 37.18  ? 4   GLN A O   1 
ATOM   27   C CB  . GLN A 1 4   ? 72.730 0.885   59.308 1.00 38.34  ? 4   GLN A CB  1 
ATOM   28   C CG  . GLN A 1 4   ? 72.443 -0.529  58.876 1.00 39.64  ? 4   GLN A CG  1 
ATOM   29   C CD  . GLN A 1 4   ? 71.639 -0.720  57.617 1.00 41.25  ? 4   GLN A CD  1 
ATOM   30   O OE1 . GLN A 1 4   ? 71.204 -1.837  57.335 1.00 42.74  ? 4   GLN A OE1 1 
ATOM   31   N NE2 . GLN A 1 4   ? 71.422 0.252   56.735 1.00 40.11  ? 4   GLN A NE2 1 
ATOM   32   N N   . ASP A 1 5   ? 70.880 1.688   61.790 1.00 38.16  ? 5   ASP A N   1 
ATOM   33   C CA  . ASP A 1 5   ? 70.044 1.307   62.912 1.00 38.98  ? 5   ASP A CA  1 
ATOM   34   C C   . ASP A 1 5   ? 68.687 2.004   62.860 1.00 38.66  ? 5   ASP A C   1 
ATOM   35   O O   . ASP A 1 5   ? 67.620 1.386   62.970 1.00 38.26  ? 5   ASP A O   1 
ATOM   36   C CB  . ASP A 1 5   ? 70.774 1.557   64.213 1.00 42.89  ? 5   ASP A CB  1 
ATOM   37   C CG  . ASP A 1 5   ? 69.820 1.120   65.304 1.00 48.05  ? 5   ASP A CG  1 
ATOM   38   O OD1 . ASP A 1 5   ? 69.623 -0.084  65.529 1.00 51.02  ? 5   ASP A OD1 1 
ATOM   39   O OD2 . ASP A 1 5   ? 69.267 2.087   65.830 1.00 53.14  ? 5   ASP A OD2 1 
ATOM   40   N N   . LEU A 1 6   ? 68.728 3.274   62.448 1.00 37.65  ? 6   LEU A N   1 
ATOM   41   C CA  . LEU A 1 6   ? 67.399 3.891   62.287 1.00 37.21  ? 6   LEU A CA  1 
ATOM   42   C C   . LEU A 1 6   ? 66.701 3.276   61.090 1.00 36.39  ? 6   LEU A C   1 
ATOM   43   O O   . LEU A 1 6   ? 65.514 2.973   61.178 1.00 37.02  ? 6   LEU A O   1 
ATOM   44   C CB  . LEU A 1 6   ? 67.628 5.373   62.318 1.00 35.38  ? 6   LEU A CB  1 
ATOM   45   C CG  . LEU A 1 6   ? 66.658 6.264   63.049 1.00 35.84  ? 6   LEU A CG  1 
ATOM   46   C CD1 . LEU A 1 6   ? 66.093 5.692   64.320 1.00 33.23  ? 6   LEU A CD1 1 
ATOM   47   C CD2 . LEU A 1 6   ? 67.322 7.620   63.277 1.00 37.16  ? 6   LEU A CD2 1 
ATOM   48   N N   . PHE A 1 7   ? 67.341 3.072   59.962 1.00 35.12  ? 7   PHE A N   1 
ATOM   49   C CA  . PHE A 1 7   ? 66.736 2.446   58.801 1.00 35.09  ? 7   PHE A CA  1 
ATOM   50   C C   . PHE A 1 7   ? 66.067 1.134   59.125 1.00 34.48  ? 7   PHE A C   1 
ATOM   51   O O   . PHE A 1 7   ? 64.943 0.855   58.713 1.00 35.59  ? 7   PHE A O   1 
ATOM   52   C CB  . PHE A 1 7   ? 67.792 2.247   57.690 1.00 36.63  ? 7   PHE A CB  1 
ATOM   53   C CG  . PHE A 1 7   ? 67.345 1.388   56.562 1.00 39.60  ? 7   PHE A CG  1 
ATOM   54   C CD1 . PHE A 1 7   ? 66.691 1.970   55.491 1.00 42.84  ? 7   PHE A CD1 1 
ATOM   55   C CD2 . PHE A 1 7   ? 67.565 0.005   56.535 1.00 40.79  ? 7   PHE A CD2 1 
ATOM   56   C CE1 . PHE A 1 7   ? 66.285 1.193   54.390 1.00 42.11  ? 7   PHE A CE1 1 
ATOM   57   C CE2 . PHE A 1 7   ? 67.106 -0.771  55.470 1.00 39.02  ? 7   PHE A CE2 1 
ATOM   58   C CZ  . PHE A 1 7   ? 66.467 -0.174  54.418 1.00 39.95  ? 7   PHE A CZ  1 
ATOM   59   N N   . ASN A 1 8   ? 66.746 0.187   59.756 1.00 34.47  ? 8   ASN A N   1 
ATOM   60   C CA  . ASN A 1 8   ? 66.197 -1.069  60.199 1.00 32.74  ? 8   ASN A CA  1 
ATOM   61   C C   . ASN A 1 8   ? 64.965 -0.842  61.024 1.00 32.42  ? 8   ASN A C   1 
ATOM   62   O O   . ASN A 1 8   ? 63.973 -1.510  60.738 1.00 33.05  ? 8   ASN A O   1 
ATOM   63   C CB  . ASN A 1 8   ? 67.191 -1.916  60.970 1.00 35.40  ? 8   ASN A CB  1 
ATOM   64   C CG  . ASN A 1 8   ? 68.308 -2.451  60.091 1.00 36.24  ? 8   ASN A CG  1 
ATOM   65   O OD1 . ASN A 1 8   ? 68.092 -2.633  58.882 1.00 40.15  ? 8   ASN A OD1 1 
ATOM   66   N ND2 . ASN A 1 8   ? 69.487 -2.683  60.649 1.00 34.58  ? 8   ASN A ND2 1 
ATOM   67   N N   . GLN A 1 9   ? 64.956 0.140   61.927 1.00 32.33  ? 9   GLN A N   1 
ATOM   68   C CA  . GLN A 1 9   ? 63.737 0.358   62.714 1.00 32.26  ? 9   GLN A CA  1 
ATOM   69   C C   . GLN A 1 9   ? 62.583 0.832   61.845 1.00 31.97  ? 9   GLN A C   1 
ATOM   70   O O   . GLN A 1 9   ? 61.426 0.399   61.966 1.00 32.22  ? 9   GLN A O   1 
ATOM   71   C CB  . GLN A 1 9   ? 63.989 1.388   63.806 1.00 33.71  ? 9   GLN A CB  1 
ATOM   72   C CG  . GLN A 1 9   ? 64.795 0.874   64.964 1.00 37.50  ? 9   GLN A CG  1 
ATOM   73   C CD  . GLN A 1 9   ? 65.019 1.903   66.064 1.00 38.15  ? 9   GLN A CD  1 
ATOM   74   O OE1 . GLN A 1 9   ? 64.086 2.169   66.838 1.00 36.50  ? 9   GLN A OE1 1 
ATOM   75   N NE2 . GLN A 1 9   ? 66.274 2.373   66.126 1.00 36.79  ? 9   GLN A NE2 1 
ATOM   76   N N   . PHE A 1 10  ? 62.896 1.787   60.969 1.00 31.50  ? 10  PHE A N   1 
ATOM   77   C CA  . PHE A 1 10  ? 61.893 2.368   60.068 1.00 31.30  ? 10  PHE A CA  1 
ATOM   78   C C   . PHE A 1 10  ? 61.236 1.272   59.233 1.00 31.37  ? 10  PHE A C   1 
ATOM   79   O O   . PHE A 1 10  ? 60.009 1.241   59.208 1.00 30.34  ? 10  PHE A O   1 
ATOM   80   C CB  . PHE A 1 10  ? 62.514 3.439   59.206 1.00 30.24  ? 10  PHE A CB  1 
ATOM   81   C CG  . PHE A 1 10  ? 62.812 4.740   59.926 1.00 31.75  ? 10  PHE A CG  1 
ATOM   82   C CD1 . PHE A 1 10  ? 62.489 4.962   61.238 1.00 30.00  ? 10  PHE A CD1 1 
ATOM   83   C CD2 . PHE A 1 10  ? 63.392 5.780   59.226 1.00 28.32  ? 10  PHE A CD2 1 
ATOM   84   C CE1 . PHE A 1 10  ? 62.827 6.131   61.861 1.00 34.27  ? 10  PHE A CE1 1 
ATOM   85   C CE2 . PHE A 1 10  ? 63.678 6.970   59.841 1.00 32.13  ? 10  PHE A CE2 1 
ATOM   86   C CZ  . PHE A 1 10  ? 63.394 7.183   61.167 1.00 31.95  ? 10  PHE A CZ  1 
ATOM   87   N N   . ASN A 1 11  ? 62.042 0.290   58.839 1.00 31.08  ? 11  ASN A N   1 
ATOM   88   C CA  . ASN A 1 11  ? 61.632 -0.825  58.049 1.00 31.74  ? 11  ASN A CA  1 
ATOM   89   C C   . ASN A 1 11  ? 60.719 -1.841  58.721 1.00 31.51  ? 11  ASN A C   1 
ATOM   90   O O   . ASN A 1 11  ? 59.628 -2.163  58.218 1.00 31.26  ? 11  ASN A O   1 
ATOM   91   C CB  . ASN A 1 11  ? 62.920 -1.489  57.524 1.00 35.54  ? 11  ASN A CB  1 
ATOM   92   C CG  . ASN A 1 11  ? 62.574 -2.481  56.425 1.00 36.22  ? 11  ASN A CG  1 
ATOM   93   O OD1 . ASN A 1 11  ? 61.552 -2.346  55.777 1.00 39.20  ? 11  ASN A OD1 1 
ATOM   94   N ND2 . ASN A 1 11  ? 63.381 -3.491  56.209 1.00 38.01  ? 11  ASN A ND2 1 
ATOM   95   N N   . LEU A 1 12  ? 61.177 -2.358  59.847 1.00 30.11  ? 12  LEU A N   1 
ATOM   96   C CA  . LEU A 1 12  ? 60.347 -3.139  60.738 1.00 29.77  ? 12  LEU A CA  1 
ATOM   97   C C   . LEU A 1 12  ? 58.980 -2.515  60.971 1.00 30.07  ? 12  LEU A C   1 
ATOM   98   O O   . LEU A 1 12  ? 57.948 -3.068  60.567 1.00 28.81  ? 12  LEU A O   1 
ATOM   99   C CB  . LEU A 1 12  ? 61.136 -3.309  62.043 1.00 28.18  ? 12  LEU A CB  1 
ATOM   100  C CG  . LEU A 1 12  ? 60.610 -4.363  63.009 1.00 30.12  ? 12  LEU A CG  1 
ATOM   101  C CD1 . LEU A 1 12  ? 60.790 -5.762  62.426 1.00 31.43  ? 12  LEU A CD1 1 
ATOM   102  C CD2 . LEU A 1 12  ? 61.295 -4.367  64.363 1.00 27.85  ? 12  LEU A CD2 1 
ATOM   103  N N   . PHE A 1 13  ? 58.927 -1.266  61.476 1.00 30.79  ? 13  PHE A N   1 
ATOM   104  C CA  . PHE A 1 13  ? 57.623 -0.672  61.837 1.00 30.92  ? 13  PHE A CA  1 
ATOM   105  C C   . PHE A 1 13  ? 56.736 -0.367  60.642 1.00 30.33  ? 13  PHE A C   1 
ATOM   106  O O   . PHE A 1 13  ? 55.509 -0.523  60.738 1.00 28.41  ? 13  PHE A O   1 
ATOM   107  C CB  . PHE A 1 13  ? 57.801 0.442   62.876 1.00 32.24  ? 13  PHE A CB  1 
ATOM   108  C CG  . PHE A 1 13  ? 58.418 -0.068  64.166 1.00 34.02  ? 13  PHE A CG  1 
ATOM   109  C CD1 . PHE A 1 13  ? 57.747 -1.050  64.900 1.00 32.34  ? 13  PHE A CD1 1 
ATOM   110  C CD2 . PHE A 1 13  ? 59.657 0.394   64.602 1.00 32.37  ? 13  PHE A CD2 1 
ATOM   111  C CE1 . PHE A 1 13  ? 58.350 -1.545  66.039 1.00 34.06  ? 13  PHE A CE1 1 
ATOM   112  C CE2 . PHE A 1 13  ? 60.248 -0.083  65.733 1.00 30.83  ? 13  PHE A CE2 1 
ATOM   113  C CZ  . PHE A 1 13  ? 59.573 -1.050  66.466 1.00 33.25  ? 13  PHE A CZ  1 
ATOM   114  N N   . ALA A 1 14  ? 57.298 -0.152  59.440 1.00 29.91  ? 14  ALA A N   1 
ATOM   115  C CA  . ALA A 1 14  ? 56.450 -0.081  58.248 1.00 30.28  ? 14  ALA A CA  1 
ATOM   116  C C   . ALA A 1 14  ? 55.727 -1.426  58.091 1.00 31.85  ? 14  ALA A C   1 
ATOM   117  O O   . ALA A 1 14  ? 54.587 -1.462  57.646 1.00 30.90  ? 14  ALA A O   1 
ATOM   118  C CB  . ALA A 1 14  ? 57.257 0.190   57.006 1.00 31.09  ? 14  ALA A CB  1 
ATOM   119  N N   . GLN A 1 15  ? 56.470 -2.542  58.256 1.00 32.79  ? 15  GLN A N   1 
ATOM   120  C CA  . GLN A 1 15  ? 55.848 -3.839  58.184 1.00 34.01  ? 15  GLN A CA  1 
ATOM   121  C C   . GLN A 1 15  ? 54.870 -4.146  59.293 1.00 34.99  ? 15  GLN A C   1 
ATOM   122  O O   . GLN A 1 15  ? 53.762 -4.582  58.943 1.00 35.11  ? 15  GLN A O   1 
ATOM   123  C CB  . GLN A 1 15  ? 56.882 -4.949  58.035 1.00 35.96  ? 15  GLN A CB  1 
ATOM   124  C CG  . GLN A 1 15  ? 57.640 -4.674  56.750 1.00 33.29  ? 15  GLN A CG  1 
ATOM   125  C CD  . GLN A 1 15  ? 58.643 -5.748  56.438 1.00 33.50  ? 15  GLN A CD  1 
ATOM   126  O OE1 . GLN A 1 15  ? 58.717 -6.804  57.027 1.00 34.65  ? 15  GLN A OE1 1 
ATOM   127  N NE2 . GLN A 1 15  ? 59.463 -5.420  55.443 1.00 37.01  ? 15  GLN A NE2 1 
ATOM   128  N N   . TYR A 1 16  ? 55.126 -3.748  60.546 1.00 35.32  ? 16  TYR A N   1 
ATOM   129  C CA  . TYR A 1 16  ? 54.080 -3.850  61.555 1.00 35.65  ? 16  TYR A CA  1 
ATOM   130  C C   . TYR A 1 16  ? 52.884 -3.034  61.092 1.00 36.20  ? 16  TYR A C   1 
ATOM   131  O O   . TYR A 1 16  ? 51.770 -3.475  61.297 1.00 37.08  ? 16  TYR A O   1 
ATOM   132  C CB  . TYR A 1 16  ? 54.415 -3.394  62.985 1.00 35.71  ? 16  TYR A CB  1 
ATOM   133  C CG  . TYR A 1 16  ? 55.051 -4.504  63.807 1.00 32.62  ? 16  TYR A CG  1 
ATOM   134  C CD1 . TYR A 1 16  ? 54.339 -5.547  64.394 1.00 32.22  ? 16  TYR A CD1 1 
ATOM   135  C CD2 . TYR A 1 16  ? 56.423 -4.433  63.953 1.00 30.22  ? 16  TYR A CD2 1 
ATOM   136  C CE1 . TYR A 1 16  ? 55.015 -6.559  65.082 1.00 31.50  ? 16  TYR A CE1 1 
ATOM   137  C CE2 . TYR A 1 16  ? 57.086 -5.363  64.699 1.00 29.79  ? 16  TYR A CE2 1 
ATOM   138  C CZ  . TYR A 1 16  ? 56.389 -6.423  65.216 1.00 31.17  ? 16  TYR A CZ  1 
ATOM   139  O OH  . TYR A 1 16  ? 57.103 -7.356  65.900 1.00 30.39  ? 16  TYR A OH  1 
ATOM   140  N N   . SER A 1 17  ? 53.050 -1.840  60.579 1.00 37.07  ? 17  SER A N   1 
ATOM   141  C CA  . SER A 1 17  ? 52.006 -1.053  59.959 1.00 37.53  ? 17  SER A CA  1 
ATOM   142  C C   . SER A 1 17  ? 51.392 -1.740  58.756 1.00 38.13  ? 17  SER A C   1 
ATOM   143  O O   . SER A 1 17  ? 50.170 -1.935  58.655 1.00 38.96  ? 17  SER A O   1 
ATOM   144  C CB  . SER A 1 17  ? 52.564 0.327   59.558 1.00 37.59  ? 17  SER A CB  1 
ATOM   145  O OG  . SER A 1 17  ? 52.910 1.038   60.753 1.00 38.61  ? 17  SER A OG  1 
ATOM   146  N N   . ALA A 1 18  ? 52.181 -2.434  57.943 1.00 38.91  ? 18  ALA A N   1 
ATOM   147  C CA  . ALA A 1 18  ? 51.602 -3.119  56.774 1.00 39.36  ? 18  ALA A CA  1 
ATOM   148  C C   . ALA A 1 18  ? 50.818 -4.333  57.216 1.00 40.45  ? 18  ALA A C   1 
ATOM   149  O O   . ALA A 1 18  ? 49.661 -4.510  56.775 1.00 41.65  ? 18  ALA A O   1 
ATOM   150  C CB  . ALA A 1 18  ? 52.646 -3.408  55.727 1.00 37.65  ? 18  ALA A CB  1 
ATOM   151  N N   . ALA A 1 19  ? 51.228 -4.989  58.304 1.00 40.68  ? 19  ALA A N   1 
ATOM   152  C CA  . ALA A 1 19  ? 50.485 -6.106  58.862 1.00 40.68  ? 19  ALA A CA  1 
ATOM   153  C C   . ALA A 1 19  ? 49.141 -5.697  59.410 1.00 41.41  ? 19  ALA A C   1 
ATOM   154  O O   . ALA A 1 19  ? 48.215 -6.463  59.263 1.00 40.73  ? 19  ALA A O   1 
ATOM   155  C CB  . ALA A 1 19  ? 51.254 -6.814  59.957 1.00 39.56  ? 19  ALA A CB  1 
ATOM   156  N N   . ALA A 1 20  ? 48.881 -4.441  59.780 1.00 43.29  ? 20  ALA A N   1 
ATOM   157  C CA  . ALA A 1 20  ? 47.542 -4.034  60.217 1.00 44.52  ? 20  ALA A CA  1 
ATOM   158  C C   . ALA A 1 20  ? 46.506 -4.346  59.132 1.00 45.53  ? 20  ALA A C   1 
ATOM   159  O O   . ALA A 1 20  ? 45.301 -4.354  59.364 1.00 45.14  ? 20  ALA A O   1 
ATOM   160  C CB  . ALA A 1 20  ? 47.434 -2.558  60.541 1.00 37.28  ? 20  ALA A CB  1 
ATOM   161  N N   . TYR A 1 21  ? 46.913 -4.051  57.891 1.00 47.50  ? 21  TYR A N   1 
ATOM   162  C CA  . TYR A 1 21  ? 46.034 -4.337  56.771 1.00 49.03  ? 21  TYR A CA  1 
ATOM   163  C C   . TYR A 1 21  ? 46.080 -5.793  56.299 1.00 51.25  ? 21  TYR A C   1 
ATOM   164  O O   . TYR A 1 21  ? 45.080 -6.252  55.768 1.00 50.65  ? 21  TYR A O   1 
ATOM   165  C CB  . TYR A 1 21  ? 46.457 -3.523  55.544 1.00 45.16  ? 21  TYR A CB  1 
ATOM   166  C CG  . TYR A 1 21  ? 46.283 -2.030  55.631 1.00 40.21  ? 21  TYR A CG  1 
ATOM   167  C CD1 . TYR A 1 21  ? 45.146 -1.266  55.362 1.00 36.28  ? 21  TYR A CD1 1 
ATOM   168  C CD2 . TYR A 1 21  ? 47.452 -1.394  56.101 1.00 38.71  ? 21  TYR A CD2 1 
ATOM   169  C CE1 . TYR A 1 21  ? 45.217 0.110   55.487 1.00 36.14  ? 21  TYR A CE1 1 
ATOM   170  C CE2 . TYR A 1 21  ? 47.559 -0.016  56.228 1.00 35.86  ? 21  TYR A CE2 1 
ATOM   171  C CZ  . TYR A 1 21  ? 46.421 0.671   55.965 1.00 35.01  ? 21  TYR A CZ  1 
ATOM   172  O OH  . TYR A 1 21  ? 46.474 2.014   56.010 1.00 33.68  ? 21  TYR A OH  1 
ATOM   173  N N   . CYS A 1 22  ? 47.268 -6.421  56.338 1.00 54.64  ? 22  CYS A N   1 
ATOM   174  C CA  . CYS A 1 22  ? 47.437 -7.602  55.521 1.00 58.75  ? 22  CYS A CA  1 
ATOM   175  C C   . CYS A 1 22  ? 47.469 -8.988  56.161 1.00 63.51  ? 22  CYS A C   1 
ATOM   176  O O   . CYS A 1 22  ? 48.126 -9.955  55.742 1.00 63.22  ? 22  CYS A O   1 
ATOM   177  C CB  . CYS A 1 22  ? 48.457 -7.566  54.383 1.00 50.09  ? 22  CYS A CB  1 
ATOM   178  S SG  . CYS A 1 22  ? 48.282 -6.192  53.280 1.00 43.87  ? 22  CYS A SG  1 
ATOM   179  N N   . GLY A 1 23  ? 46.232 -9.107  56.654 1.00 68.53  ? 23  GLY A N   1 
ATOM   180  C CA  . GLY A 1 23  ? 45.465 -10.263 56.968 1.00 74.61  ? 23  GLY A CA  1 
ATOM   181  C C   . GLY A 1 23  ? 45.881 -11.081 58.149 1.00 78.80  ? 23  GLY A C   1 
ATOM   182  O O   . GLY A 1 23  ? 46.841 -10.808 58.849 1.00 78.31  ? 23  GLY A O   1 
ATOM   183  N N   . LYS A 1 24  ? 44.919 -11.900 58.581 1.00 83.70  ? 24  LYS A N   1 
ATOM   184  C CA  . LYS A 1 24  ? 44.983 -12.830 59.693 1.00 88.58  ? 24  LYS A CA  1 
ATOM   185  C C   . LYS A 1 24  ? 44.784 -12.145 61.040 1.00 91.63  ? 24  LYS A C   1 
ATOM   186  O O   . LYS A 1 24  ? 43.883 -12.474 61.818 1.00 91.83  ? 24  LYS A O   1 
ATOM   187  C CB  . LYS A 1 24  ? 46.252 -13.683 59.653 1.00 90.53  ? 24  LYS A CB  1 
ATOM   188  C CG  . LYS A 1 24  ? 46.214 -14.809 58.632 1.00 93.98  ? 24  LYS A CG  1 
ATOM   189  C CD  . LYS A 1 24  ? 46.363 -14.439 57.171 1.00 94.49  ? 24  LYS A CD  1 
ATOM   190  C CE  . LYS A 1 24  ? 47.756 -14.724 56.638 1.00 94.77  ? 24  LYS A CE  1 
ATOM   191  N NZ  . LYS A 1 24  ? 48.242 -16.058 57.096 1.00 96.25  ? 24  LYS A NZ  1 
ATOM   192  N N   . ASN A 1 25  ? 45.229 -10.900 61.116 1.00 94.64  ? 25  ASN A N   1 
ATOM   193  C CA  . ASN A 1 25  ? 45.343 -10.032 62.246 1.00 97.87  ? 25  ASN A CA  1 
ATOM   194  C C   . ASN A 1 25  ? 44.302 -8.931  62.399 1.00 99.64  ? 25  ASN A C   1 
ATOM   195  O O   . ASN A 1 25  ? 44.479 -8.055  63.261 1.00 99.53  ? 25  ASN A O   1 
ATOM   196  C CB  . ASN A 1 25  ? 46.704 -9.347  62.266 1.00 100.24 ? 25  ASN A CB  1 
ATOM   197  C CG  . ASN A 1 25  ? 47.194 -8.551  61.106 1.00 101.21 ? 25  ASN A CG  1 
ATOM   198  O OD1 . ASN A 1 25  ? 48.185 -8.921  60.471 1.00 101.96 ? 25  ASN A OD1 1 
ATOM   199  N ND2 . ASN A 1 25  ? 46.493 -7.446  60.861 1.00 102.65 ? 25  ASN A ND2 1 
ATOM   200  N N   . ASN A 1 26  ? 43.223 -9.015  61.607 1.00 101.23 ? 26  ASN A N   1 
ATOM   201  C CA  . ASN A 1 26  ? 42.143 -8.032  61.806 1.00 102.70 ? 26  ASN A CA  1 
ATOM   202  C C   . ASN A 1 26  ? 41.373 -8.526  63.041 1.00 103.35 ? 26  ASN A C   1 
ATOM   203  O O   . ASN A 1 26  ? 41.255 -7.726  63.972 1.00 103.58 ? 26  ASN A O   1 
ATOM   204  C CB  . ASN A 1 26  ? 41.305 -7.736  60.590 1.00 103.88 ? 26  ASN A CB  1 
ATOM   205  C CG  . ASN A 1 26  ? 42.021 -7.113  59.405 1.00 104.93 ? 26  ASN A CG  1 
ATOM   206  O OD1 . ASN A 1 26  ? 42.543 -5.996  59.438 1.00 103.51 ? 26  ASN A OD1 1 
ATOM   207  N ND2 . ASN A 1 26  ? 42.052 -7.806  58.261 1.00 105.60 ? 26  ASN A ND2 1 
ATOM   208  N N   . ASP A 1 27  ? 41.349 -9.855  63.211 1.00 103.88 ? 27  ASP A N   1 
ATOM   209  C CA  . ASP A 1 27  ? 40.932 -10.505 64.441 1.00 104.41 ? 27  ASP A CA  1 
ATOM   210  C C   . ASP A 1 27  ? 41.272 -11.997 64.499 1.00 103.96 ? 27  ASP A C   1 
ATOM   211  O O   . ASP A 1 27  ? 40.448 -12.842 64.153 1.00 104.02 ? 27  ASP A O   1 
ATOM   212  C CB  . ASP A 1 27  ? 39.440 -10.303 64.705 1.00 107.34 ? 27  ASP A CB  1 
ATOM   213  C CG  . ASP A 1 27  ? 39.090 -9.637  66.026 1.00 109.11 ? 27  ASP A CG  1 
ATOM   214  O OD1 . ASP A 1 27  ? 39.094 -8.383  66.124 1.00 109.47 ? 27  ASP A OD1 1 
ATOM   215  O OD2 . ASP A 1 27  ? 38.744 -10.369 66.981 1.00 110.38 ? 27  ASP A OD2 1 
ATOM   216  N N   . ALA A 1 28  ? 42.393 -12.342 65.134 1.00 103.36 ? 28  ALA A N   1 
ATOM   217  C CA  . ALA A 1 28  ? 42.842 -13.723 65.306 1.00 101.83 ? 28  ALA A CA  1 
ATOM   218  C C   . ALA A 1 28  ? 43.324 -13.967 66.727 1.00 100.49 ? 28  ALA A C   1 
ATOM   219  O O   . ALA A 1 28  ? 43.809 -13.059 67.399 1.00 100.77 ? 28  ALA A O   1 
ATOM   220  C CB  . ALA A 1 28  ? 43.909 -14.085 64.293 1.00 102.60 ? 28  ALA A CB  1 
ATOM   221  N N   . PRO A 1 29  ? 43.226 -15.208 67.174 1.00 99.12  ? 29  PRO A N   1 
ATOM   222  C CA  . PRO A 1 29  ? 43.463 -15.584 68.555 1.00 97.37  ? 29  PRO A CA  1 
ATOM   223  C C   . PRO A 1 29  ? 44.777 -15.138 69.158 1.00 95.25  ? 29  PRO A C   1 
ATOM   224  O O   . PRO A 1 29  ? 45.837 -15.215 68.543 1.00 95.07  ? 29  PRO A O   1 
ATOM   225  C CB  . PRO A 1 29  ? 43.322 -17.104 68.573 1.00 97.93  ? 29  PRO A CB  1 
ATOM   226  C CG  . PRO A 1 29  ? 43.380 -17.545 67.158 1.00 98.54  ? 29  PRO A CG  1 
ATOM   227  C CD  . PRO A 1 29  ? 42.914 -16.384 66.322 1.00 99.04  ? 29  PRO A CD  1 
ATOM   228  N N   . ALA A 1 30  ? 44.782 -14.814 70.451 1.00 92.58  ? 30  ALA A N   1 
ATOM   229  C CA  . ALA A 1 30  ? 45.971 -14.351 71.151 1.00 89.09  ? 30  ALA A CA  1 
ATOM   230  C C   . ALA A 1 30  ? 47.080 -15.388 71.236 1.00 86.67  ? 30  ALA A C   1 
ATOM   231  O O   . ALA A 1 30  ? 46.817 -16.555 71.511 1.00 86.44  ? 30  ALA A O   1 
ATOM   232  C CB  . ALA A 1 30  ? 45.543 -13.914 72.544 1.00 87.42  ? 30  ALA A CB  1 
ATOM   233  N N   . GLY A 1 31  ? 48.328 -14.995 70.981 1.00 83.85  ? 31  GLY A N   1 
ATOM   234  C CA  . GLY A 1 31  ? 49.460 -15.900 71.098 1.00 80.40  ? 31  GLY A CA  1 
ATOM   235  C C   . GLY A 1 31  ? 49.871 -16.556 69.789 1.00 77.65  ? 31  GLY A C   1 
ATOM   236  O O   . GLY A 1 31  ? 50.889 -17.207 69.593 1.00 77.22  ? 31  GLY A O   1 
ATOM   237  N N   . THR A 1 32  ? 49.026 -16.363 68.809 1.00 75.30  ? 32  THR A N   1 
ATOM   238  C CA  . THR A 1 32  ? 49.132 -16.808 67.436 1.00 72.76  ? 32  THR A CA  1 
ATOM   239  C C   . THR A 1 32  ? 50.251 -16.076 66.712 1.00 70.52  ? 32  THR A C   1 
ATOM   240  O O   . THR A 1 32  ? 50.682 -15.020 67.175 1.00 70.40  ? 32  THR A O   1 
ATOM   241  C CB  . THR A 1 32  ? 47.780 -16.438 66.791 1.00 73.23  ? 32  THR A CB  1 
ATOM   242  O OG1 . THR A 1 32  ? 46.753 -17.232 67.411 1.00 73.97  ? 32  THR A OG1 1 
ATOM   243  C CG2 . THR A 1 32  ? 47.821 -16.604 65.300 1.00 72.67  ? 32  THR A CG2 1 
ATOM   244  N N   . ASN A 1 33  ? 50.944 -16.747 65.815 1.00 68.07  ? 33  ASN A N   1 
ATOM   245  C CA  . ASN A 1 33  ? 52.077 -16.132 65.110 1.00 64.54  ? 33  ASN A CA  1 
ATOM   246  C C   . ASN A 1 33  ? 51.523 -15.060 64.189 1.00 61.50  ? 33  ASN A C   1 
ATOM   247  O O   . ASN A 1 33  ? 50.371 -15.151 63.768 1.00 60.81  ? 33  ASN A O   1 
ATOM   248  C CB  . ASN A 1 33  ? 52.844 -17.264 64.430 1.00 67.60  ? 33  ASN A CB  1 
ATOM   249  C CG  . ASN A 1 33  ? 53.783 -17.997 65.369 1.00 70.77  ? 33  ASN A CG  1 
ATOM   250  O OD1 . ASN A 1 33  ? 54.450 -19.026 65.133 1.00 72.39  ? 33  ASN A OD1 1 
ATOM   251  N ND2 . ASN A 1 33  ? 53.866 -17.381 66.543 1.00 72.01  ? 33  ASN A ND2 1 
ATOM   252  N N   . ILE A 1 34  ? 52.098 -13.857 64.173 1.00 58.72  ? 34  ILE A N   1 
ATOM   253  C CA  . ILE A 1 34  ? 51.636 -12.779 63.288 1.00 56.09  ? 34  ILE A CA  1 
ATOM   254  C C   . ILE A 1 34  ? 52.141 -13.019 61.857 1.00 53.67  ? 34  ILE A C   1 
ATOM   255  O O   . ILE A 1 34  ? 53.325 -13.300 61.713 1.00 51.14  ? 34  ILE A O   1 
ATOM   256  C CB  . ILE A 1 34  ? 52.092 -11.378 63.753 1.00 56.77  ? 34  ILE A CB  1 
ATOM   257  C CG1 . ILE A 1 34  ? 51.346 -10.891 65.003 1.00 54.43  ? 34  ILE A CG1 1 
ATOM   258  C CG2 . ILE A 1 34  ? 52.001 -10.347 62.632 1.00 52.63  ? 34  ILE A CG2 1 
ATOM   259  C CD1 . ILE A 1 34  ? 51.848 -9.524  65.473 1.00 52.33  ? 34  ILE A CD1 1 
ATOM   260  N N   . THR A 1 35  ? 51.237 -13.086 60.868 1.00 52.77  ? 35  THR A N   1 
ATOM   261  C CA  . THR A 1 35  ? 51.643 -13.372 59.498 1.00 52.49  ? 35  THR A CA  1 
ATOM   262  C C   . THR A 1 35  ? 50.876 -12.537 58.471 1.00 51.59  ? 35  THR A C   1 
ATOM   263  O O   . THR A 1 35  ? 49.668 -12.393 58.629 1.00 52.69  ? 35  THR A O   1 
ATOM   264  C CB  . THR A 1 35  ? 51.448 -14.799 58.943 1.00 53.10  ? 35  THR A CB  1 
ATOM   265  O OG1 . THR A 1 35  ? 50.048 -15.134 58.943 1.00 56.05  ? 35  THR A OG1 1 
ATOM   266  C CG2 . THR A 1 35  ? 52.282 -15.834 59.649 1.00 52.24  ? 35  THR A CG2 1 
ATOM   267  N N   . CYS A 1 36  ? 51.495 -12.228 57.341 1.00 50.05  ? 36  CYS A N   1 
ATOM   268  C CA  . CYS A 1 36  ? 50.754 -11.488 56.321 1.00 49.17  ? 36  CYS A CA  1 
ATOM   269  C C   . CYS A 1 36  ? 50.569 -12.204 55.001 1.00 48.90  ? 36  CYS A C   1 
ATOM   270  O O   . CYS A 1 36  ? 51.324 -13.098 54.572 1.00 48.69  ? 36  CYS A O   1 
ATOM   271  C CB  . CYS A 1 36  ? 51.539 -10.178 56.031 1.00 44.85  ? 36  CYS A CB  1 
ATOM   272  S SG  . CYS A 1 36  ? 51.764 -9.133  57.479 1.00 45.88  ? 36  CYS A SG  1 
ATOM   273  N N   . THR A 1 37  ? 49.660 -11.666 54.175 1.00 48.59  ? 37  THR A N   1 
ATOM   274  C CA  . THR A 1 37  ? 49.641 -12.270 52.825 1.00 48.19  ? 37  THR A CA  1 
ATOM   275  C C   . THR A 1 37  ? 50.561 -11.460 51.936 1.00 47.61  ? 37  THR A C   1 
ATOM   276  O O   . THR A 1 37  ? 51.114 -10.428 52.332 1.00 47.12  ? 37  THR A O   1 
ATOM   277  C CB  . THR A 1 37  ? 48.216 -12.252 52.266 1.00 50.44  ? 37  THR A CB  1 
ATOM   278  O OG1 . THR A 1 37  ? 47.642 -10.997 52.677 1.00 52.56  ? 37  THR A OG1 1 
ATOM   279  C CG2 . THR A 1 37  ? 47.460 -13.402 52.899 1.00 47.64  ? 37  THR A CG2 1 
ATOM   280  N N   . GLY A 1 38  ? 50.956 -12.057 50.811 1.00 46.74  ? 38  GLY A N   1 
ATOM   281  C CA  . GLY A 1 38  ? 51.659 -11.392 49.755 1.00 45.18  ? 38  GLY A CA  1 
ATOM   282  C C   . GLY A 1 38  ? 52.918 -10.662 50.109 1.00 45.03  ? 38  GLY A C   1 
ATOM   283  O O   . GLY A 1 38  ? 53.204 -9.591  49.568 1.00 45.39  ? 38  GLY A O   1 
ATOM   284  N N   . ASN A 1 39  ? 53.667 -11.129 51.089 1.00 44.54  ? 39  ASN A N   1 
ATOM   285  C CA  . ASN A 1 39  ? 54.950 -10.602 51.476 1.00 43.87  ? 39  ASN A CA  1 
ATOM   286  C C   . ASN A 1 39  ? 54.979 -9.196  52.045 1.00 43.57  ? 39  ASN A C   1 
ATOM   287  O O   . ASN A 1 39  ? 56.079 -8.620  52.154 1.00 43.08  ? 39  ASN A O   1 
ATOM   288  C CB  . ASN A 1 39  ? 55.931 -10.829 50.316 1.00 44.37  ? 39  ASN A CB  1 
ATOM   289  C CG  . ASN A 1 39  ? 57.329 -11.074 50.842 1.00 47.78  ? 39  ASN A CG  1 
ATOM   290  O OD1 . ASN A 1 39  ? 57.577 -11.775 51.833 1.00 51.93  ? 39  ASN A OD1 1 
ATOM   291  N ND2 . ASN A 1 39  ? 58.338 -10.466 50.254 1.00 48.04  ? 39  ASN A ND2 1 
ATOM   292  N N   . ALA A 1 40  ? 53.897 -8.708  52.658 1.00 42.78  ? 40  ALA A N   1 
ATOM   293  C CA  . ALA A 1 40  ? 53.867 -7.440  53.353 1.00 42.79  ? 40  ALA A CA  1 
ATOM   294  C C   . ALA A 1 40  ? 54.743 -7.288  54.598 1.00 42.76  ? 40  ALA A C   1 
ATOM   295  O O   . ALA A 1 40  ? 55.317 -6.201  54.761 1.00 42.34  ? 40  ALA A O   1 
ATOM   296  C CB  . ALA A 1 40  ? 52.491 -6.969  53.826 1.00 40.92  ? 40  ALA A CB  1 
ATOM   297  N N   . CYS A 1 41  ? 54.898 -8.364  55.379 1.00 42.93  ? 41  CYS A N   1 
ATOM   298  C CA  . CYS A 1 41  ? 55.666 -8.252  56.600 1.00 42.56  ? 41  CYS A CA  1 
ATOM   299  C C   . CYS A 1 41  ? 56.660 -9.331  56.890 1.00 42.37  ? 41  CYS A C   1 
ATOM   300  O O   . CYS A 1 41  ? 56.565 -9.872  57.985 1.00 43.31  ? 41  CYS A O   1 
ATOM   301  C CB  . CYS A 1 41  ? 54.621 -8.135  57.709 1.00 43.77  ? 41  CYS A CB  1 
ATOM   302  S SG  . CYS A 1 41  ? 53.664 -9.580  58.125 1.00 42.61  ? 41  CYS A SG  1 
ATOM   303  N N   . PRO A 1 42  ? 57.646 -9.611  56.059 1.00 42.10  ? 42  PRO A N   1 
ATOM   304  C CA  . PRO A 1 42  ? 58.613 -10.640 56.261 1.00 41.79  ? 42  PRO A CA  1 
ATOM   305  C C   . PRO A 1 42  ? 59.542 -10.372 57.439 1.00 43.26  ? 42  PRO A C   1 
ATOM   306  O O   . PRO A 1 42  ? 60.004 -11.397 58.031 1.00 43.29  ? 42  PRO A O   1 
ATOM   307  C CB  . PRO A 1 42  ? 59.460 -10.769 55.002 1.00 41.85  ? 42  PRO A CB  1 
ATOM   308  C CG  . PRO A 1 42  ? 59.020 -9.699  54.058 1.00 41.62  ? 42  PRO A CG  1 
ATOM   309  C CD  . PRO A 1 42  ? 57.847 -8.985  54.710 1.00 42.12  ? 42  PRO A CD  1 
ATOM   310  N N   . GLU A 1 43  ? 59.815 -9.086  57.795 1.00 42.33  ? 43  GLU A N   1 
ATOM   311  C CA  . GLU A 1 43  ? 60.610 -8.963  59.036 1.00 42.71  ? 43  GLU A CA  1 
ATOM   312  C C   . GLU A 1 43  ? 59.785 -9.284  60.280 1.00 42.20  ? 43  GLU A C   1 
ATOM   313  O O   . GLU A 1 43  ? 60.379 -9.642  61.289 1.00 41.82  ? 43  GLU A O   1 
ATOM   314  C CB  . GLU A 1 43  ? 61.385 -7.682  59.204 1.00 42.46  ? 43  GLU A CB  1 
ATOM   315  C CG  . GLU A 1 43  ? 62.039 -7.211  57.929 1.00 47.03  ? 43  GLU A CG  1 
ATOM   316  C CD  . GLU A 1 43  ? 63.359 -7.877  57.605 1.00 49.67  ? 43  GLU A CD  1 
ATOM   317  O OE1 . GLU A 1 43  ? 64.011 -8.392  58.544 1.00 47.76  ? 43  GLU A OE1 1 
ATOM   318  O OE2 . GLU A 1 43  ? 63.719 -7.866  56.379 1.00 51.78  ? 43  GLU A OE2 1 
ATOM   319  N N   . VAL A 1 44  ? 58.467 -9.226  60.228 1.00 42.07  ? 44  VAL A N   1 
ATOM   320  C CA  . VAL A 1 44  ? 57.608 -9.561  61.345 1.00 43.07  ? 44  VAL A CA  1 
ATOM   321  C C   . VAL A 1 44  ? 57.479 -11.065 61.532 1.00 44.38  ? 44  VAL A C   1 
ATOM   322  O O   . VAL A 1 44  ? 57.974 -11.588 62.544 1.00 43.76  ? 44  VAL A O   1 
ATOM   323  C CB  . VAL A 1 44  ? 56.236 -8.921  61.140 1.00 41.83  ? 44  VAL A CB  1 
ATOM   324  C CG1 . VAL A 1 44  ? 55.273 -9.312  62.234 1.00 40.68  ? 44  VAL A CG1 1 
ATOM   325  C CG2 . VAL A 1 44  ? 56.449 -7.417  61.037 1.00 40.32  ? 44  VAL A CG2 1 
ATOM   326  N N   . GLU A 1 45  ? 57.358 -11.755 60.392 1.00 46.03  ? 45  GLU A N   1 
ATOM   327  C CA  . GLU A 1 45  ? 57.368 -13.220 60.424 1.00 47.86  ? 45  GLU A CA  1 
ATOM   328  C C   . GLU A 1 45  ? 58.711 -13.790 60.842 1.00 48.44  ? 45  GLU A C   1 
ATOM   329  O O   . GLU A 1 45  ? 58.768 -14.755 61.590 1.00 47.99  ? 45  GLU A O   1 
ATOM   330  C CB  . GLU A 1 45  ? 56.890 -13.787 59.100 1.00 46.45  ? 45  GLU A CB  1 
ATOM   331  C CG  . GLU A 1 45  ? 55.433 -13.480 58.829 1.00 49.87  ? 45  GLU A CG  1 
ATOM   332  C CD  . GLU A 1 45  ? 54.981 -13.879 57.440 1.00 52.46  ? 45  GLU A CD  1 
ATOM   333  O OE1 . GLU A 1 45  ? 55.756 -14.496 56.684 1.00 52.86  ? 45  GLU A OE1 1 
ATOM   334  O OE2 . GLU A 1 45  ? 53.827 -13.571 57.083 1.00 54.29  ? 45  GLU A OE2 1 
ATOM   335  N N   . LYS A 1 46  ? 59.825 -13.130 60.563 1.00 50.21  ? 46  LYS A N   1 
ATOM   336  C CA  . LYS A 1 46  ? 61.168 -13.613 60.913 1.00 51.19  ? 46  LYS A CA  1 
ATOM   337  C C   . LYS A 1 46  ? 61.264 -13.721 62.438 1.00 52.80  ? 46  LYS A C   1 
ATOM   338  O O   . LYS A 1 46  ? 61.704 -14.740 62.957 1.00 52.82  ? 46  LYS A O   1 
ATOM   339  C CB  . LYS A 1 46  ? 62.202 -12.669 60.361 1.00 51.36  ? 46  LYS A CB  1 
ATOM   340  C CG  . LYS A 1 46  ? 63.400 -13.080 59.573 1.00 54.27  ? 46  LYS A CG  1 
ATOM   341  C CD  . LYS A 1 46  ? 63.420 -12.451 58.180 1.00 60.10  ? 46  LYS A CD  1 
ATOM   342  C CE  . LYS A 1 46  ? 64.456 -11.386 57.917 1.00 63.57  ? 46  LYS A CE  1 
ATOM   343  N NZ  . LYS A 1 46  ? 64.179 -10.527 56.708 1.00 64.04  ? 46  LYS A NZ  1 
ATOM   344  N N   . ALA A 1 47  ? 60.685 -12.785 63.170 1.00 53.76  ? 47  ALA A N   1 
ATOM   345  C CA  . ALA A 1 47  ? 60.619 -12.748 64.602 1.00 54.73  ? 47  ALA A CA  1 
ATOM   346  C C   . ALA A 1 47  ? 59.638 -13.719 65.265 1.00 55.82  ? 47  ALA A C   1 
ATOM   347  O O   . ALA A 1 47  ? 58.546 -14.097 64.837 1.00 54.96  ? 47  ALA A O   1 
ATOM   348  C CB  . ALA A 1 47  ? 60.278 -11.317 65.014 1.00 54.09  ? 47  ALA A CB  1 
ATOM   349  N N   . ASP A 1 48  ? 59.797 -13.785 66.604 1.00 56.45  ? 48  ASP A N   1 
ATOM   350  C CA  . ASP A 1 48  ? 58.880 -14.553 67.452 1.00 57.38  ? 48  ASP A CA  1 
ATOM   351  C C   . ASP A 1 48  ? 57.821 -13.503 67.807 1.00 56.86  ? 48  ASP A C   1 
ATOM   352  O O   . ASP A 1 48  ? 58.016 -12.901 68.887 1.00 56.90  ? 48  ASP A O   1 
ATOM   353  C CB  . ASP A 1 48  ? 59.594 -15.074 68.707 1.00 59.92  ? 48  ASP A CB  1 
ATOM   354  C CG  . ASP A 1 48  ? 58.666 -15.743 69.715 1.00 62.06  ? 48  ASP A CG  1 
ATOM   355  O OD1 . ASP A 1 48  ? 57.466 -15.908 69.393 1.00 61.14  ? 48  ASP A OD1 1 
ATOM   356  O OD2 . ASP A 1 48  ? 59.096 -16.110 70.845 1.00 62.81  ? 48  ASP A OD2 1 
ATOM   357  N N   . ALA A 1 49  ? 56.967 -13.180 66.835 1.00 55.69  ? 49  ALA A N   1 
ATOM   358  C CA  . ALA A 1 49  ? 56.013 -12.092 67.132 1.00 55.22  ? 49  ALA A CA  1 
ATOM   359  C C   . ALA A 1 49  ? 54.582 -12.581 67.112 1.00 54.78  ? 49  ALA A C   1 
ATOM   360  O O   . ALA A 1 49  ? 54.163 -13.236 66.119 1.00 56.13  ? 49  ALA A O   1 
ATOM   361  C CB  . ALA A 1 49  ? 56.241 -10.939 66.168 1.00 52.80  ? 49  ALA A CB  1 
ATOM   362  N N   . THR A 1 50  ? 53.875 -12.397 68.208 1.00 53.77  ? 50  THR A N   1 
ATOM   363  C CA  . THR A 1 50  ? 52.513 -12.928 68.299 1.00 53.17  ? 50  THR A CA  1 
ATOM   364  C C   . THR A 1 50  ? 51.549 -11.843 68.782 1.00 53.30  ? 50  THR A C   1 
ATOM   365  O O   . THR A 1 50  ? 51.989 -10.790 69.245 1.00 51.95  ? 50  THR A O   1 
ATOM   366  C CB  . THR A 1 50  ? 52.490 -14.085 69.323 1.00 50.23  ? 50  THR A CB  1 
ATOM   367  O OG1 . THR A 1 50  ? 52.967 -13.526 70.542 1.00 49.30  ? 50  THR A OG1 1 
ATOM   368  C CG2 . THR A 1 50  ? 53.372 -15.265 68.962 1.00 45.07  ? 50  THR A CG2 1 
ATOM   369  N N   . PHE A 1 51  ? 50.254 -12.121 68.646 1.00 53.46  ? 51  PHE A N   1 
ATOM   370  C CA  . PHE A 1 51  ? 49.201 -11.233 69.050 1.00 54.00  ? 51  PHE A CA  1 
ATOM   371  C C   . PHE A 1 51  ? 48.925 -11.322 70.562 1.00 55.55  ? 51  PHE A C   1 
ATOM   372  O O   . PHE A 1 51  ? 48.475 -12.389 71.006 1.00 56.17  ? 51  PHE A O   1 
ATOM   373  C CB  . PHE A 1 51  ? 47.815 -11.660 68.500 1.00 53.40  ? 51  PHE A CB  1 
ATOM   374  C CG  . PHE A 1 51  ? 47.824 -11.526 67.017 1.00 52.56  ? 51  PHE A CG  1 
ATOM   375  C CD1 . PHE A 1 51  ? 47.768 -10.267 66.442 1.00 52.03  ? 51  PHE A CD1 1 
ATOM   376  C CD2 . PHE A 1 51  ? 48.025 -12.655 66.231 1.00 52.79  ? 51  PHE A CD2 1 
ATOM   377  C CE1 . PHE A 1 51  ? 47.884 -10.120 65.080 1.00 52.39  ? 51  PHE A CE1 1 
ATOM   378  C CE2 . PHE A 1 51  ? 48.072 -12.513 64.850 1.00 51.98  ? 51  PHE A CE2 1 
ATOM   379  C CZ  . PHE A 1 51  ? 48.036 -11.252 64.301 1.00 51.44  ? 51  PHE A CZ  1 
ATOM   380  N N   . LEU A 1 52  ? 48.573 -10.152 71.070 1.00 55.61  ? 52  LEU A N   1 
ATOM   381  C CA  . LEU A 1 52  ? 48.170 -10.001 72.441 1.00 55.98  ? 52  LEU A CA  1 
ATOM   382  C C   . LEU A 1 52  ? 46.682 -9.699  72.454 1.00 56.75  ? 52  LEU A C   1 
ATOM   383  O O   . LEU A 1 52  ? 45.953 -10.262 73.263 1.00 57.38  ? 52  LEU A O   1 
ATOM   384  C CB  . LEU A 1 52  ? 48.980 -8.890  73.117 1.00 54.29  ? 52  LEU A CB  1 
ATOM   385  C CG  . LEU A 1 52  ? 50.439 -9.253  73.437 1.00 54.37  ? 52  LEU A CG  1 
ATOM   386  C CD1 . LEU A 1 52  ? 51.053 -8.257  74.402 1.00 52.04  ? 52  LEU A CD1 1 
ATOM   387  C CD2 . LEU A 1 52  ? 50.611 -10.649 74.005 1.00 51.08  ? 52  LEU A CD2 1 
ATOM   388  N N   . TYR A 1 53  ? 46.260 -8.833  71.548 1.00 56.95  ? 53  TYR A N   1 
ATOM   389  C CA  . TYR A 1 53  ? 44.875 -8.393  71.460 1.00 56.81  ? 53  TYR A CA  1 
ATOM   390  C C   . TYR A 1 53  ? 44.653 -7.892  70.032 1.00 57.67  ? 53  TYR A C   1 
ATOM   391  O O   . TYR A 1 53  ? 45.651 -7.449  69.457 1.00 58.33  ? 53  TYR A O   1 
ATOM   392  C CB  . TYR A 1 53  ? 44.605 -7.268  72.451 1.00 56.05  ? 53  TYR A CB  1 
ATOM   393  C CG  . TYR A 1 53  ? 43.207 -6.697  72.406 1.00 56.05  ? 53  TYR A CG  1 
ATOM   394  C CD1 . TYR A 1 53  ? 42.075 -7.495  72.526 1.00 56.09  ? 53  TYR A CD1 1 
ATOM   395  C CD2 . TYR A 1 53  ? 43.020 -5.332  72.254 1.00 56.10  ? 53  TYR A CD2 1 
ATOM   396  C CE1 . TYR A 1 53  ? 40.805 -6.960  72.458 1.00 56.97  ? 53  TYR A CE1 1 
ATOM   397  C CE2 . TYR A 1 53  ? 41.763 -4.777  72.217 1.00 57.15  ? 53  TYR A CE2 1 
ATOM   398  C CZ  . TYR A 1 53  ? 40.648 -5.596  72.309 1.00 58.30  ? 53  TYR A CZ  1 
ATOM   399  O OH  . TYR A 1 53  ? 39.386 -5.019  72.236 1.00 58.77  ? 53  TYR A OH  1 
ATOM   400  N N   . SER A 1 54  ? 43.633 -8.397  69.361 1.00 57.96  ? 54  SER A N   1 
ATOM   401  C CA  . SER A 1 54  ? 43.238 -7.993  68.028 1.00 58.07  ? 54  SER A CA  1 
ATOM   402  C C   . SER A 1 54  ? 41.924 -7.215  68.162 1.00 58.66  ? 54  SER A C   1 
ATOM   403  O O   . SER A 1 54  ? 41.061 -7.628  68.943 1.00 59.38  ? 54  SER A O   1 
ATOM   404  C CB  . SER A 1 54  ? 42.938 -9.202  67.133 1.00 55.05  ? 54  SER A CB  1 
ATOM   405  O OG  . SER A 1 54  ? 43.907 -10.201 67.403 1.00 62.08  ? 54  SER A OG  1 
ATOM   406  N N   . PHE A 1 55  ? 41.750 -6.108  67.484 1.00 58.33  ? 55  PHE A N   1 
ATOM   407  C CA  . PHE A 1 55  ? 40.533 -5.320  67.516 1.00 58.29  ? 55  PHE A CA  1 
ATOM   408  C C   . PHE A 1 55  ? 40.080 -4.929  66.125 1.00 59.61  ? 55  PHE A C   1 
ATOM   409  O O   . PHE A 1 55  ? 40.851 -4.894  65.160 1.00 60.07  ? 55  PHE A O   1 
ATOM   410  C CB  . PHE A 1 55  ? 40.640 -4.136  68.466 1.00 51.80  ? 55  PHE A CB  1 
ATOM   411  C CG  . PHE A 1 55  ? 41.873 -3.291  68.332 1.00 46.41  ? 55  PHE A CG  1 
ATOM   412  C CD1 . PHE A 1 55  ? 41.815 -2.086  67.672 1.00 42.14  ? 55  PHE A CD1 1 
ATOM   413  C CD2 . PHE A 1 55  ? 43.092 -3.705  68.836 1.00 44.70  ? 55  PHE A CD2 1 
ATOM   414  C CE1 . PHE A 1 55  ? 42.957 -1.329  67.547 1.00 43.00  ? 55  PHE A CE1 1 
ATOM   415  C CE2 . PHE A 1 55  ? 44.224 -2.923  68.716 1.00 44.00  ? 55  PHE A CE2 1 
ATOM   416  C CZ  . PHE A 1 55  ? 44.183 -1.734  68.029 1.00 41.09  ? 55  PHE A CZ  1 
ATOM   417  N N   . GLU A 1 56  ? 38.796 -4.704  65.921 1.00 61.30  ? 56  GLU A N   1 
ATOM   418  C CA  . GLU A 1 56  ? 38.351 -4.442  64.548 1.00 63.52  ? 56  GLU A CA  1 
ATOM   419  C C   . GLU A 1 56  ? 37.049 -3.677  64.557 1.00 64.85  ? 56  GLU A C   1 
ATOM   420  O O   . GLU A 1 56  ? 36.095 -4.083  65.200 1.00 64.99  ? 56  GLU A O   1 
ATOM   421  C CB  . GLU A 1 56  ? 38.182 -5.760  63.809 1.00 63.34  ? 56  GLU A CB  1 
ATOM   422  C CG  . GLU A 1 56  ? 37.484 -5.498  62.485 1.00 64.91  ? 56  GLU A CG  1 
ATOM   423  C CD  . GLU A 1 56  ? 37.747 -6.639  61.526 1.00 67.47  ? 56  GLU A CD  1 
ATOM   424  O OE1 . GLU A 1 56  ? 37.775 -7.778  62.030 1.00 67.00  ? 56  GLU A OE1 1 
ATOM   425  O OE2 . GLU A 1 56  ? 37.915 -6.284  60.335 1.00 70.64  ? 56  GLU A OE2 1 
ATOM   426  N N   . ASP A 1 57  ? 37.050 -2.490  63.970 1.00 66.31  ? 57  ASP A N   1 
ATOM   427  C CA  . ASP A 1 57  ? 35.832 -1.678  64.057 1.00 68.32  ? 57  ASP A CA  1 
ATOM   428  C C   . ASP A 1 57  ? 35.450 -1.501  65.536 1.00 69.46  ? 57  ASP A C   1 
ATOM   429  O O   . ASP A 1 57  ? 34.350 -1.879  65.981 1.00 69.34  ? 57  ASP A O   1 
ATOM   430  C CB  . ASP A 1 57  ? 34.683 -2.356  63.338 1.00 70.02  ? 57  ASP A CB  1 
ATOM   431  C CG  . ASP A 1 57  ? 34.825 -2.494  61.842 1.00 74.31  ? 57  ASP A CG  1 
ATOM   432  O OD1 . ASP A 1 57  ? 35.393 -1.594  61.178 1.00 76.24  ? 57  ASP A OD1 1 
ATOM   433  O OD2 . ASP A 1 57  ? 34.304 -3.513  61.315 1.00 75.33  ? 57  ASP A OD2 1 
ATOM   434  N N   . SER A 1 58  ? 36.437 -1.077  66.330 1.00 70.12  ? 58  SER A N   1 
ATOM   435  C CA  . SER A 1 58  ? 36.222 -0.779  67.737 1.00 70.79  ? 58  SER A CA  1 
ATOM   436  C C   . SER A 1 58  ? 36.050 0.734   67.914 1.00 70.90  ? 58  SER A C   1 
ATOM   437  O O   . SER A 1 58  ? 36.269 1.520   66.980 1.00 70.78  ? 58  SER A O   1 
ATOM   438  C CB  . SER A 1 58  ? 37.371 -1.309  68.585 1.00 72.43  ? 58  SER A CB  1 
ATOM   439  O OG  . SER A 1 58  ? 37.210 -1.044  69.967 1.00 76.12  ? 58  SER A OG  1 
ATOM   440  N N   . GLY A 1 59  ? 35.299 1.097   68.958 1.00 70.62  ? 59  GLY A N   1 
ATOM   441  C CA  . GLY A 1 59  ? 35.166 2.504   69.292 1.00 70.63  ? 59  GLY A CA  1 
ATOM   442  C C   . GLY A 1 59  ? 34.266 3.255   68.335 1.00 70.40  ? 59  GLY A C   1 
ATOM   443  O O   . GLY A 1 59  ? 33.662 2.706   67.426 1.00 70.92  ? 59  GLY A O   1 
ATOM   444  N N   . VAL A 1 60  ? 34.175 4.552   68.587 1.00 70.04  ? 60  VAL A N   1 
ATOM   445  C CA  . VAL A 1 60  ? 33.257 5.417   67.868 1.00 69.36  ? 60  VAL A CA  1 
ATOM   446  C C   . VAL A 1 60  ? 33.682 5.573   66.423 1.00 69.39  ? 60  VAL A C   1 
ATOM   447  O O   . VAL A 1 60  ? 32.845 5.222   65.585 1.00 70.03  ? 60  VAL A O   1 
ATOM   448  C CB  . VAL A 1 60  ? 33.067 6.723   68.644 1.00 66.49  ? 60  VAL A CB  1 
ATOM   449  C CG1 . VAL A 1 60  ? 33.805 7.910   68.054 1.00 64.25  ? 60  VAL A CG1 1 
ATOM   450  C CG2 . VAL A 1 60  ? 31.583 7.032   68.771 1.00 67.33  ? 60  VAL A CG2 1 
ATOM   451  N N   . GLY A 1 61  ? 34.954 5.827   66.141 1.00 68.74  ? 61  GLY A N   1 
ATOM   452  C CA  . GLY A 1 61  ? 35.437 6.018   64.786 1.00 68.13  ? 61  GLY A CA  1 
ATOM   453  C C   . GLY A 1 61  ? 36.005 4.802   64.066 1.00 67.52  ? 61  GLY A C   1 
ATOM   454  O O   . GLY A 1 61  ? 36.778 4.885   63.117 1.00 67.54  ? 61  GLY A O   1 
ATOM   455  N N   . ASP A 1 62  ? 35.666 3.613   64.525 1.00 67.19  ? 62  ASP A N   1 
ATOM   456  C CA  . ASP A 1 62  ? 36.000 2.314   64.005 1.00 66.59  ? 62  ASP A CA  1 
ATOM   457  C C   . ASP A 1 62  ? 37.498 2.200   63.757 1.00 64.89  ? 62  ASP A C   1 
ATOM   458  O O   . ASP A 1 62  ? 38.026 2.673   62.761 1.00 65.65  ? 62  ASP A O   1 
ATOM   459  C CB  . ASP A 1 62  ? 35.227 1.947   62.730 1.00 72.12  ? 62  ASP A CB  1 
ATOM   460  C CG  . ASP A 1 62  ? 33.761 1.631   62.976 1.00 75.24  ? 62  ASP A CG  1 
ATOM   461  O OD1 . ASP A 1 62  ? 32.939 2.551   63.208 1.00 77.61  ? 62  ASP A OD1 1 
ATOM   462  O OD2 . ASP A 1 62  ? 33.348 0.450   62.935 1.00 75.75  ? 62  ASP A OD2 1 
ATOM   463  N N   . VAL A 1 63  ? 38.195 1.716   64.753 1.00 62.27  ? 63  VAL A N   1 
ATOM   464  C CA  . VAL A 1 63  ? 39.616 1.548   64.887 1.00 58.38  ? 63  VAL A CA  1 
ATOM   465  C C   . VAL A 1 63  ? 39.898 0.049   64.825 1.00 55.98  ? 63  VAL A C   1 
ATOM   466  O O   . VAL A 1 63  ? 39.303 -0.790  65.460 1.00 54.77  ? 63  VAL A O   1 
ATOM   467  C CB  . VAL A 1 63  ? 40.106 2.048   66.262 1.00 59.12  ? 63  VAL A CB  1 
ATOM   468  C CG1 . VAL A 1 63  ? 41.567 1.757   66.543 1.00 60.50  ? 63  VAL A CG1 1 
ATOM   469  C CG2 . VAL A 1 63  ? 39.772 3.531   66.387 1.00 59.19  ? 63  VAL A CG2 1 
ATOM   470  N N   . THR A 1 64  ? 40.853 -0.219  63.941 1.00 53.80  ? 64  THR A N   1 
ATOM   471  C CA  . THR A 1 64  ? 41.189 -1.608  63.617 1.00 50.58  ? 64  THR A CA  1 
ATOM   472  C C   . THR A 1 64  ? 42.680 -1.724  63.855 1.00 49.39  ? 64  THR A C   1 
ATOM   473  O O   . THR A 1 64  ? 43.344 -0.692  63.723 1.00 49.43  ? 64  THR A O   1 
ATOM   474  C CB  . THR A 1 64  ? 40.778 -1.829  62.144 1.00 45.67  ? 64  THR A CB  1 
ATOM   475  O OG1 . THR A 1 64  ? 39.348 -1.705  62.043 1.00 41.56  ? 64  THR A OG1 1 
ATOM   476  C CG2 . THR A 1 64  ? 41.214 -3.170  61.606 1.00 42.80  ? 64  THR A CG2 1 
ATOM   477  N N   . GLY A 1 65  ? 43.186 -2.809  64.426 1.00 47.80  ? 65  GLY A N   1 
ATOM   478  C CA  . GLY A 1 65  ? 44.598 -2.927  64.640 1.00 46.12  ? 65  GLY A CA  1 
ATOM   479  C C   . GLY A 1 65  ? 44.904 -4.183  65.426 1.00 45.34  ? 65  GLY A C   1 
ATOM   480  O O   . GLY A 1 65  ? 43.999 -4.898  65.805 1.00 44.42  ? 65  GLY A O   1 
ATOM   481  N N   . PHE A 1 66  ? 46.154 -4.198  65.896 1.00 44.99  ? 66  PHE A N   1 
ATOM   482  C CA  . PHE A 1 66  ? 46.536 -5.309  66.766 1.00 44.50  ? 66  PHE A CA  1 
ATOM   483  C C   . PHE A 1 66  ? 47.647 -4.804  67.696 1.00 44.26  ? 66  PHE A C   1 
ATOM   484  O O   . PHE A 1 66  ? 48.101 -3.675  67.547 1.00 44.40  ? 66  PHE A O   1 
ATOM   485  C CB  . PHE A 1 66  ? 46.856 -6.553  65.963 1.00 41.61  ? 66  PHE A CB  1 
ATOM   486  C CG  . PHE A 1 66  ? 48.077 -6.325  65.108 1.00 40.20  ? 66  PHE A CG  1 
ATOM   487  C CD1 . PHE A 1 66  ? 49.314 -6.479  65.680 1.00 39.89  ? 66  PHE A CD1 1 
ATOM   488  C CD2 . PHE A 1 66  ? 48.001 -5.929  63.794 1.00 38.94  ? 66  PHE A CD2 1 
ATOM   489  C CE1 . PHE A 1 66  ? 50.467 -6.245  64.933 1.00 40.06  ? 66  PHE A CE1 1 
ATOM   490  C CE2 . PHE A 1 66  ? 49.161 -5.690  63.070 1.00 38.12  ? 66  PHE A CE2 1 
ATOM   491  C CZ  . PHE A 1 66  ? 50.413 -5.876  63.610 1.00 36.02  ? 66  PHE A CZ  1 
ATOM   492  N N   . LEU A 1 67  ? 47.634 -5.345  68.908 1.00 43.57  ? 67  LEU A N   1 
ATOM   493  C CA  . LEU A 1 67  ? 48.671 -5.179  69.891 1.00 43.44  ? 67  LEU A CA  1 
ATOM   494  C C   . LEU A 1 67  ? 49.529 -6.454  69.881 1.00 43.29  ? 67  LEU A C   1 
ATOM   495  O O   . LEU A 1 67  ? 48.927 -7.501  70.072 1.00 43.29  ? 67  LEU A O   1 
ATOM   496  C CB  . LEU A 1 67  ? 48.156 -4.950  71.325 1.00 39.16  ? 67  LEU A CB  1 
ATOM   497  C CG  . LEU A 1 67  ? 49.283 -4.851  72.363 1.00 39.07  ? 67  LEU A CG  1 
ATOM   498  C CD1 . LEU A 1 67  ? 50.048 -3.541  72.249 1.00 38.75  ? 67  LEU A CD1 1 
ATOM   499  C CD2 . LEU A 1 67  ? 48.760 -4.975  73.777 1.00 41.17  ? 67  LEU A CD2 1 
ATOM   500  N N   . ALA A 1 68  ? 50.835 -6.343  69.693 1.00 43.18  ? 68  ALA A N   1 
ATOM   501  C CA  . ALA A 1 68  ? 51.706 -7.474  69.579 1.00 43.55  ? 68  ALA A CA  1 
ATOM   502  C C   . ALA A 1 68  ? 52.885 -7.579  70.551 1.00 44.71  ? 68  ALA A C   1 
ATOM   503  O O   . ALA A 1 68  ? 53.638 -6.647  70.861 1.00 44.19  ? 68  ALA A O   1 
ATOM   504  C CB  . ALA A 1 68  ? 52.410 -7.484  68.216 1.00 40.22  ? 68  ALA A CB  1 
ATOM   505  N N   . LEU A 1 69  ? 53.317 -8.855  70.601 1.00 45.37  ? 69  LEU A N   1 
ATOM   506  C CA  . LEU A 1 69  ? 54.451 -9.235  71.407 1.00 45.07  ? 69  LEU A CA  1 
ATOM   507  C C   . LEU A 1 69  ? 55.579 -9.674  70.494 1.00 45.57  ? 69  LEU A C   1 
ATOM   508  O O   . LEU A 1 69  ? 55.410 -10.552 69.648 1.00 45.84  ? 69  LEU A O   1 
ATOM   509  C CB  . LEU A 1 69  ? 54.152 -10.352 72.397 1.00 44.13  ? 69  LEU A CB  1 
ATOM   510  C CG  . LEU A 1 69  ? 55.300 -10.446 73.428 1.00 47.87  ? 69  LEU A CG  1 
ATOM   511  C CD1 . LEU A 1 69  ? 55.247 -9.214  74.339 1.00 46.28  ? 69  LEU A CD1 1 
ATOM   512  C CD2 . LEU A 1 69  ? 55.223 -11.756 74.191 1.00 45.52  ? 69  LEU A CD2 1 
ATOM   513  N N   . ASP A 1 70  ? 56.728 -9.017  70.650 1.00 45.85  ? 70  ASP A N   1 
ATOM   514  C CA  . ASP A 1 70  ? 57.831 -9.408  69.753 1.00 45.21  ? 70  ASP A CA  1 
ATOM   515  C C   . ASP A 1 70  ? 58.957 -9.746  70.712 1.00 45.67  ? 70  ASP A C   1 
ATOM   516  O O   . ASP A 1 70  ? 59.685 -8.832  71.068 1.00 45.88  ? 70  ASP A O   1 
ATOM   517  C CB  . ASP A 1 70  ? 58.130 -8.357  68.721 1.00 40.15  ? 70  ASP A CB  1 
ATOM   518  C CG  . ASP A 1 70  ? 59.314 -8.542  67.817 1.00 39.46  ? 70  ASP A CG  1 
ATOM   519  O OD1 . ASP A 1 70  ? 60.205 -9.365  68.140 1.00 38.46  ? 70  ASP A OD1 1 
ATOM   520  O OD2 . ASP A 1 70  ? 59.412 -7.864  66.751 1.00 39.03  ? 70  ASP A OD2 1 
ATOM   521  N N   . ASN A 1 71  ? 59.115 -11.039 71.009 1.00 45.89  ? 71  ASN A N   1 
ATOM   522  C CA  . ASN A 1 71  ? 60.226 -11.455 71.829 1.00 45.90  ? 71  ASN A CA  1 
ATOM   523  C C   . ASN A 1 71  ? 61.538 -11.406 71.081 1.00 46.42  ? 71  ASN A C   1 
ATOM   524  O O   . ASN A 1 71  ? 62.500 -11.600 71.831 1.00 48.02  ? 71  ASN A O   1 
ATOM   525  C CB  . ASN A 1 71  ? 60.113 -12.883 72.376 1.00 44.23  ? 71  ASN A CB  1 
ATOM   526  C CG  . ASN A 1 71  ? 58.818 -13.039 73.151 1.00 44.58  ? 71  ASN A CG  1 
ATOM   527  O OD1 . ASN A 1 71  ? 58.500 -12.297 74.068 1.00 45.58  ? 71  ASN A OD1 1 
ATOM   528  N ND2 . ASN A 1 71  ? 58.045 -14.023 72.745 1.00 45.03  ? 71  ASN A ND2 1 
ATOM   529  N N   . THR A 1 72  ? 61.667 -11.227 69.790 1.00 46.10  ? 72  THR A N   1 
ATOM   530  C CA  . THR A 1 72  ? 63.017 -11.303 69.199 1.00 46.17  ? 72  THR A CA  1 
ATOM   531  C C   . THR A 1 72  ? 63.696 -9.949  69.325 1.00 46.23  ? 72  THR A C   1 
ATOM   532  O O   . THR A 1 72  ? 64.832 -9.802  69.738 1.00 45.39  ? 72  THR A O   1 
ATOM   533  C CB  . THR A 1 72  ? 62.829 -11.715 67.730 1.00 47.44  ? 72  THR A CB  1 
ATOM   534  O OG1 . THR A 1 72  ? 62.479 -13.109 67.745 1.00 50.22  ? 72  THR A OG1 1 
ATOM   535  C CG2 . THR A 1 72  ? 63.998 -11.493 66.830 1.00 42.62  ? 72  THR A CG2 1 
ATOM   536  N N   . ASN A 1 73  ? 62.884 -8.932  69.052 1.00 46.11  ? 73  ASN A N   1 
ATOM   537  C CA  . ASN A 1 73  ? 63.250 -7.533  69.069 1.00 45.97  ? 73  ASN A CA  1 
ATOM   538  C C   . ASN A 1 73  ? 62.945 -6.916  70.445 1.00 46.28  ? 73  ASN A C   1 
ATOM   539  O O   . ASN A 1 73  ? 63.283 -5.762  70.750 1.00 45.68  ? 73  ASN A O   1 
ATOM   540  C CB  . ASN A 1 73  ? 62.448 -6.795  67.993 1.00 44.04  ? 73  ASN A CB  1 
ATOM   541  C CG  . ASN A 1 73  ? 62.923 -7.196  66.594 1.00 43.96  ? 73  ASN A CG  1 
ATOM   542  O OD1 . ASN A 1 73  ? 64.018 -6.752  66.246 1.00 39.86  ? 73  ASN A OD1 1 
ATOM   543  N ND2 . ASN A 1 73  ? 62.076 -7.957  65.901 1.00 40.72  ? 73  ASN A ND2 1 
ATOM   544  N N   . LYS A 1 74  ? 62.233 -7.693  71.257 1.00 45.47  ? 74  LYS A N   1 
ATOM   545  C CA  . LYS A 1 74  ? 61.962 -7.237  72.617 1.00 46.40  ? 74  LYS A CA  1 
ATOM   546  C C   . LYS A 1 74  ? 61.100 -5.976  72.560 1.00 45.28  ? 74  LYS A C   1 
ATOM   547  O O   . LYS A 1 74  ? 61.499 -4.919  73.031 1.00 45.24  ? 74  LYS A O   1 
ATOM   548  C CB  . LYS A 1 74  ? 63.268 -6.923  73.348 1.00 50.90  ? 74  LYS A CB  1 
ATOM   549  C CG  . LYS A 1 74  ? 63.998 -8.111  73.946 1.00 55.44  ? 74  LYS A CG  1 
ATOM   550  C CD  . LYS A 1 74  ? 65.435 -7.698  74.231 1.00 59.96  ? 74  LYS A CD  1 
ATOM   551  C CE  . LYS A 1 74  ? 65.947 -8.213  75.567 1.00 65.53  ? 74  LYS A CE  1 
ATOM   552  N NZ  . LYS A 1 74  ? 65.571 -7.313  76.712 1.00 67.27  ? 74  LYS A NZ  1 
ATOM   553  N N   . LEU A 1 75  ? 59.951 -6.106  71.920 1.00 43.87  ? 75  LEU A N   1 
ATOM   554  C CA  . LEU A 1 75  ? 59.000 -5.052  71.742 1.00 42.89  ? 75  LEU A CA  1 
ATOM   555  C C   . LEU A 1 75  ? 57.575 -5.395  72.183 1.00 42.03  ? 75  LEU A C   1 
ATOM   556  O O   . LEU A 1 75  ? 57.170 -6.551  72.130 1.00 40.44  ? 75  LEU A O   1 
ATOM   557  C CB  . LEU A 1 75  ? 58.849 -4.713  70.236 1.00 42.33  ? 75  LEU A CB  1 
ATOM   558  C CG  . LEU A 1 75  ? 60.162 -4.397  69.519 1.00 43.23  ? 75  LEU A CG  1 
ATOM   559  C CD1 . LEU A 1 75  ? 59.895 -4.247  68.029 1.00 41.45  ? 75  LEU A CD1 1 
ATOM   560  C CD2 . LEU A 1 75  ? 60.865 -3.162  70.084 1.00 39.65  ? 75  LEU A CD2 1 
ATOM   561  N N   . ILE A 1 76  ? 56.845 -4.311  72.446 1.00 41.47  ? 76  ILE A N   1 
ATOM   562  C CA  . ILE A 1 76  ? 55.422 -4.352  72.724 1.00 41.33  ? 76  ILE A CA  1 
ATOM   563  C C   . ILE A 1 76  ? 54.865 -3.267  71.776 1.00 42.27  ? 76  ILE A C   1 
ATOM   564  O O   . ILE A 1 76  ? 55.322 -2.127  71.887 1.00 42.51  ? 76  ILE A O   1 
ATOM   565  C CB  . ILE A 1 76  ? 55.027 -3.938  74.141 1.00 41.01  ? 76  ILE A CB  1 
ATOM   566  C CG1 . ILE A 1 76  ? 55.613 -4.944  75.147 1.00 36.63  ? 76  ILE A CG1 1 
ATOM   567  C CG2 . ILE A 1 76  ? 53.503 -3.800  74.257 1.00 40.27  ? 76  ILE A CG2 1 
ATOM   568  C CD1 . ILE A 1 76  ? 55.484 -4.493  76.561 1.00 32.53  ? 76  ILE A CD1 1 
ATOM   569  N N   . VAL A 1 77  ? 54.279 -3.740  70.686 1.00 42.03  ? 77  VAL A N   1 
ATOM   570  C CA  . VAL A 1 77  ? 53.849 -2.968  69.566 1.00 41.42  ? 77  VAL A CA  1 
ATOM   571  C C   . VAL A 1 77  ? 52.328 -2.910  69.432 1.00 42.11  ? 77  VAL A C   1 
ATOM   572  O O   . VAL A 1 77  ? 51.679 -3.925  69.173 1.00 41.23  ? 77  VAL A O   1 
ATOM   573  C CB  . VAL A 1 77  ? 54.268 -3.612  68.219 1.00 40.45  ? 77  VAL A CB  1 
ATOM   574  C CG1 . VAL A 1 77  ? 53.879 -2.639  67.095 1.00 40.65  ? 77  VAL A CG1 1 
ATOM   575  C CG2 . VAL A 1 77  ? 55.722 -3.932  68.144 1.00 37.91  ? 77  VAL A CG2 1 
ATOM   576  N N   . LEU A 1 78  ? 51.843 -1.674  69.372 1.00 42.69  ? 78  LEU A N   1 
ATOM   577  C CA  . LEU A 1 78  ? 50.413 -1.424  69.191 1.00 42.61  ? 78  LEU A CA  1 
ATOM   578  C C   . LEU A 1 78  ? 50.231 -0.842  67.778 1.00 43.70  ? 78  LEU A C   1 
ATOM   579  O O   . LEU A 1 78  ? 50.556 0.334   67.556 1.00 43.21  ? 78  LEU A O   1 
ATOM   580  C CB  . LEU A 1 78  ? 49.898 -0.387  70.154 1.00 40.89  ? 78  LEU A CB  1 
ATOM   581  C CG  . LEU A 1 78  ? 48.429 -0.011  70.203 1.00 42.38  ? 78  LEU A CG  1 
ATOM   582  C CD1 . LEU A 1 78  ? 47.623 -1.289  70.460 1.00 42.26  ? 78  LEU A CD1 1 
ATOM   583  C CD2 . LEU A 1 78  ? 48.139 1.001   71.333 1.00 40.34  ? 78  LEU A CD2 1 
ATOM   584  N N   . SER A 1 79  ? 49.647 -1.663  66.889 1.00 43.53  ? 79  SER A N   1 
ATOM   585  C CA  . SER A 1 79  ? 49.519 -1.180  65.534 1.00 43.37  ? 79  SER A CA  1 
ATOM   586  C C   . SER A 1 79  ? 48.099 -0.851  65.151 1.00 43.44  ? 79  SER A C   1 
ATOM   587  O O   . SER A 1 79  ? 47.180 -1.660  65.145 1.00 43.75  ? 79  SER A O   1 
ATOM   588  C CB  . SER A 1 79  ? 50.248 -2.182  64.645 1.00 42.33  ? 79  SER A CB  1 
ATOM   589  O OG  . SER A 1 79  ? 50.107 -1.929  63.263 1.00 41.73  ? 79  SER A OG  1 
ATOM   590  N N   . PHE A 1 80  ? 47.946 0.256   64.451 1.00 43.82  ? 80  PHE A N   1 
ATOM   591  C CA  . PHE A 1 80  ? 46.699 0.730   63.901 1.00 43.94  ? 80  PHE A CA  1 
ATOM   592  C C   . PHE A 1 80  ? 46.708 0.682   62.379 1.00 44.89  ? 80  PHE A C   1 
ATOM   593  O O   . PHE A 1 80  ? 47.539 1.234   61.678 1.00 45.31  ? 80  PHE A O   1 
ATOM   594  C CB  . PHE A 1 80  ? 46.528 2.195   64.261 1.00 43.63  ? 80  PHE A CB  1 
ATOM   595  C CG  . PHE A 1 80  ? 46.480 2.451   65.720 1.00 43.82  ? 80  PHE A CG  1 
ATOM   596  C CD1 . PHE A 1 80  ? 45.256 2.511   66.366 1.00 42.94  ? 80  PHE A CD1 1 
ATOM   597  C CD2 . PHE A 1 80  ? 47.639 2.621   66.445 1.00 43.88  ? 80  PHE A CD2 1 
ATOM   598  C CE1 . PHE A 1 80  ? 45.188 2.742   67.721 1.00 41.65  ? 80  PHE A CE1 1 
ATOM   599  C CE2 . PHE A 1 80  ? 47.569 2.836   67.818 1.00 43.26  ? 80  PHE A CE2 1 
ATOM   600  C CZ  . PHE A 1 80  ? 46.350 2.911   68.455 1.00 43.04  ? 80  PHE A CZ  1 
ATOM   601  N N   . ARG A 1 81  ? 45.580 0.256   61.833 1.00 45.84  ? 81  ARG A N   1 
ATOM   602  C CA  . ARG A 1 81  ? 45.363 0.157   60.397 1.00 45.28  ? 81  ARG A CA  1 
ATOM   603  C C   . ARG A 1 81  ? 44.773 1.486   59.956 1.00 45.16  ? 81  ARG A C   1 
ATOM   604  O O   . ARG A 1 81  ? 44.006 2.079   60.697 1.00 43.93  ? 81  ARG A O   1 
ATOM   605  C CB  . ARG A 1 81  ? 44.344 -0.948  60.157 1.00 45.60  ? 81  ARG A CB  1 
ATOM   606  C CG  . ARG A 1 81  ? 44.316 -1.550  58.777 1.00 46.02  ? 81  ARG A CG  1 
ATOM   607  C CD  . ARG A 1 81  ? 42.987 -1.335  58.099 1.00 47.35  ? 81  ARG A CD  1 
ATOM   608  N NE  . ARG A 1 81  ? 41.985 -2.347  58.312 1.00 42.22  ? 81  ARG A NE  1 
ATOM   609  C CZ  . ARG A 1 81  ? 40.694 -2.112  58.454 1.00 43.03  ? 81  ARG A CZ  1 
ATOM   610  N NH1 . ARG A 1 81  ? 40.078 -0.943  58.450 1.00 40.73  ? 81  ARG A NH1 1 
ATOM   611  N NH2 . ARG A 1 81  ? 39.899 -3.160  58.662 1.00 46.53  ? 81  ARG A NH2 1 
ATOM   612  N N   . GLY A 1 82  ? 45.152 1.874   58.764 1.00 46.06  ? 82  GLY A N   1 
ATOM   613  C CA  . GLY A 1 82  ? 44.595 3.103   58.197 1.00 47.63  ? 82  GLY A CA  1 
ATOM   614  C C   . GLY A 1 82  ? 43.236 2.697   57.589 1.00 49.08  ? 82  GLY A C   1 
ATOM   615  O O   . GLY A 1 82  ? 42.763 1.585   57.865 1.00 48.10  ? 82  GLY A O   1 
ATOM   616  N N   . SER A 1 83  ? 42.649 3.594   56.797 1.00 50.45  ? 83  SER A N   1 
ATOM   617  C CA  . SER A 1 83  ? 41.343 3.230   56.275 1.00 52.96  ? 83  SER A CA  1 
ATOM   618  C C   . SER A 1 83  ? 41.398 2.108   55.252 1.00 55.27  ? 83  SER A C   1 
ATOM   619  O O   . SER A 1 83  ? 42.203 1.884   54.305 1.00 55.20  ? 83  SER A O   1 
ATOM   620  C CB  . SER A 1 83  ? 40.627 4.453   55.742 1.00 52.87  ? 83  SER A CB  1 
ATOM   621  O OG  . SER A 1 83  ? 40.068 4.051   54.514 1.00 54.69  ? 83  SER A OG  1 
ATOM   622  N N   . ARG A 1 84  ? 40.399 1.233   55.463 1.00 56.75  ? 84  ARG A N   1 
ATOM   623  C CA  . ARG A 1 84  ? 40.094 0.143   54.507 1.00 58.75  ? 84  ARG A CA  1 
ATOM   624  C C   . ARG A 1 84  ? 40.030 0.565   53.055 1.00 58.39  ? 84  ARG A C   1 
ATOM   625  O O   . ARG A 1 84  ? 40.258 -0.328  52.236 1.00 59.41  ? 84  ARG A O   1 
ATOM   626  C CB  . ARG A 1 84  ? 38.725 -0.507  54.794 1.00 63.72  ? 84  ARG A CB  1 
ATOM   627  C CG  . ARG A 1 84  ? 38.959 -2.001  55.002 1.00 68.52  ? 84  ARG A CG  1 
ATOM   628  C CD  . ARG A 1 84  ? 37.658 -2.678  54.586 1.00 75.79  ? 84  ARG A CD  1 
ATOM   629  N NE  . ARG A 1 84  ? 36.876 -3.061  55.753 1.00 80.90  ? 84  ARG A NE  1 
ATOM   630  C CZ  . ARG A 1 84  ? 36.336 -2.267  56.671 1.00 83.74  ? 84  ARG A CZ  1 
ATOM   631  N NH1 . ARG A 1 84  ? 36.404 -0.936  56.680 1.00 84.74  ? 84  ARG A NH1 1 
ATOM   632  N NH2 . ARG A 1 84  ? 35.674 -2.882  57.658 1.00 84.49  ? 84  ARG A NH2 1 
ATOM   633  N N   . SER A 1 85  ? 39.506 1.732   52.705 1.00 58.02  ? 85  SER A N   1 
ATOM   634  C CA  . SER A 1 85  ? 39.638 2.215   51.333 1.00 58.14  ? 85  SER A CA  1 
ATOM   635  C C   . SER A 1 85  ? 40.002 3.689   51.355 1.00 57.32  ? 85  SER A C   1 
ATOM   636  O O   . SER A 1 85  ? 39.171 4.578   51.482 1.00 57.78  ? 85  SER A O   1 
ATOM   637  C CB  . SER A 1 85  ? 38.397 1.911   50.499 1.00 60.61  ? 85  SER A CB  1 
ATOM   638  O OG  . SER A 1 85  ? 37.296 2.672   50.933 1.00 63.26  ? 85  SER A OG  1 
ATOM   639  N N   . ILE A 1 86  ? 41.269 3.987   51.219 1.00 56.89  ? 86  ILE A N   1 
ATOM   640  C CA  . ILE A 1 86  ? 41.901 5.268   51.455 1.00 57.22  ? 86  ILE A CA  1 
ATOM   641  C C   . ILE A 1 86  ? 41.510 6.404   50.563 1.00 58.19  ? 86  ILE A C   1 
ATOM   642  O O   . ILE A 1 86  ? 41.404 7.573   50.959 1.00 58.67  ? 86  ILE A O   1 
ATOM   643  C CB  . ILE A 1 86  ? 43.447 5.061   51.489 1.00 53.83  ? 86  ILE A CB  1 
ATOM   644  C CG1 . ILE A 1 86  ? 43.708 4.169   52.711 1.00 50.54  ? 86  ILE A CG1 1 
ATOM   645  C CG2 . ILE A 1 86  ? 44.258 6.329   51.531 1.00 48.00  ? 86  ILE A CG2 1 
ATOM   646  C CD1 . ILE A 1 86  ? 45.002 3.440   52.794 1.00 49.34  ? 86  ILE A CD1 1 
ATOM   647  N N   . GLU A 1 87  ? 41.289 6.116   49.297 1.00 58.95  ? 87  GLU A N   1 
ATOM   648  C CA  . GLU A 1 87  ? 40.924 7.144   48.331 1.00 59.98  ? 87  GLU A CA  1 
ATOM   649  C C   . GLU A 1 87  ? 39.653 7.842   48.794 1.00 60.38  ? 87  GLU A C   1 
ATOM   650  O O   . GLU A 1 87  ? 39.520 9.069   48.774 1.00 59.89  ? 87  GLU A O   1 
ATOM   651  C CB  . GLU A 1 87  ? 40.759 6.443   46.982 1.00 63.08  ? 87  GLU A CB  1 
ATOM   652  C CG  . GLU A 1 87  ? 41.546 7.113   45.873 1.00 65.23  ? 87  GLU A CG  1 
ATOM   653  C CD  . GLU A 1 87  ? 40.688 7.448   44.671 1.00 66.40  ? 87  GLU A CD  1 
ATOM   654  O OE1 . GLU A 1 87  ? 39.451 7.340   44.812 1.00 67.45  ? 87  GLU A OE1 1 
ATOM   655  O OE2 . GLU A 1 87  ? 41.279 7.826   43.639 1.00 65.57  ? 87  GLU A OE2 1 
ATOM   656  N N   . ASN A 1 88  ? 38.678 7.041   49.224 1.00 60.80  ? 88  ASN A N   1 
ATOM   657  C CA  . ASN A 1 88  ? 37.446 7.595   49.764 1.00 61.75  ? 88  ASN A CA  1 
ATOM   658  C C   . ASN A 1 88  ? 37.684 8.401   51.036 1.00 60.97  ? 88  ASN A C   1 
ATOM   659  O O   . ASN A 1 88  ? 37.179 9.516   51.202 1.00 60.40  ? 88  ASN A O   1 
ATOM   660  C CB  . ASN A 1 88  ? 36.410 6.501   50.022 1.00 67.73  ? 88  ASN A CB  1 
ATOM   661  C CG  . ASN A 1 88  ? 35.839 5.950   48.730 1.00 70.50  ? 88  ASN A CG  1 
ATOM   662  O OD1 . ASN A 1 88  ? 35.178 4.908   48.783 1.00 73.97  ? 88  ASN A OD1 1 
ATOM   663  N ND2 . ASN A 1 88  ? 36.097 6.613   47.606 1.00 70.27  ? 88  ASN A ND2 1 
ATOM   664  N N   . TRP A 1 89  ? 38.432 7.834   51.965 1.00 60.16  ? 89  TRP A N   1 
ATOM   665  C CA  . TRP A 1 89  ? 38.776 8.523   53.218 1.00 58.58  ? 89  TRP A CA  1 
ATOM   666  C C   . TRP A 1 89  ? 39.341 9.912   52.952 1.00 57.75  ? 89  TRP A C   1 
ATOM   667  O O   . TRP A 1 89  ? 38.904 10.939  53.485 1.00 56.70  ? 89  TRP A O   1 
ATOM   668  C CB  . TRP A 1 89  ? 39.744 7.566   53.921 1.00 56.42  ? 89  TRP A CB  1 
ATOM   669  C CG  . TRP A 1 89  ? 40.313 8.176   55.147 1.00 55.76  ? 89  TRP A CG  1 
ATOM   670  C CD1 . TRP A 1 89  ? 39.707 8.252   56.357 1.00 56.56  ? 89  TRP A CD1 1 
ATOM   671  C CD2 . TRP A 1 89  ? 41.581 8.817   55.289 1.00 55.76  ? 89  TRP A CD2 1 
ATOM   672  N NE1 . TRP A 1 89  ? 40.477 8.970   57.236 1.00 56.31  ? 89  TRP A NE1 1 
ATOM   673  C CE2 . TRP A 1 89  ? 41.642 9.316   56.600 1.00 57.14  ? 89  TRP A CE2 1 
ATOM   674  C CE3 . TRP A 1 89  ? 42.677 8.968   54.436 1.00 54.87  ? 89  TRP A CE3 1 
ATOM   675  C CZ2 . TRP A 1 89  ? 42.774 9.957   57.125 1.00 56.14  ? 89  TRP A CZ2 1 
ATOM   676  C CZ3 . TRP A 1 89  ? 43.760 9.655   54.927 1.00 55.77  ? 89  TRP A CZ3 1 
ATOM   677  C CH2 . TRP A 1 89  ? 43.797 10.150  56.262 1.00 56.40  ? 89  TRP A CH2 1 
ATOM   678  N N   . ILE A 1 90  ? 40.352 10.025  52.100 1.00 57.75  ? 90  ILE A N   1 
ATOM   679  C CA  . ILE A 1 90  ? 40.954 11.299  51.768 1.00 58.78  ? 90  ILE A CA  1 
ATOM   680  C C   . ILE A 1 90  ? 39.886 12.295  51.329 1.00 60.24  ? 90  ILE A C   1 
ATOM   681  O O   . ILE A 1 90  ? 39.768 13.376  51.887 1.00 60.69  ? 90  ILE A O   1 
ATOM   682  C CB  . ILE A 1 90  ? 41.981 11.195  50.630 1.00 55.90  ? 90  ILE A CB  1 
ATOM   683  C CG1 . ILE A 1 90  ? 43.264 10.546  51.131 1.00 56.34  ? 90  ILE A CG1 1 
ATOM   684  C CG2 . ILE A 1 90  ? 42.262 12.549  50.010 1.00 54.67  ? 90  ILE A CG2 1 
ATOM   685  C CD1 . ILE A 1 90  ? 43.815 9.458   50.233 1.00 57.09  ? 90  ILE A CD1 1 
ATOM   686  N N   . GLY A 1 91  ? 39.094 11.919  50.331 1.00 60.96  ? 91  GLY A N   1 
ATOM   687  C CA  . GLY A 1 91  ? 38.084 12.780  49.769 1.00 61.75  ? 91  GLY A CA  1 
ATOM   688  C C   . GLY A 1 91  ? 37.007 13.238  50.715 1.00 62.52  ? 91  GLY A C   1 
ATOM   689  O O   . GLY A 1 91  ? 36.547 14.376  50.684 1.00 63.10  ? 91  GLY A O   1 
ATOM   690  N N   . ASN A 1 92  ? 36.609 12.381  51.637 1.00 63.31  ? 92  ASN A N   1 
ATOM   691  C CA  . ASN A 1 92  ? 35.606 12.633  52.642 1.00 63.59  ? 92  ASN A CA  1 
ATOM   692  C C   . ASN A 1 92  ? 36.265 13.303  53.847 1.00 63.66  ? 92  ASN A C   1 
ATOM   693  O O   . ASN A 1 92  ? 35.569 13.484  54.852 1.00 63.89  ? 92  ASN A O   1 
ATOM   694  C CB  . ASN A 1 92  ? 35.007 11.322  53.133 1.00 68.04  ? 92  ASN A CB  1 
ATOM   695  C CG  . ASN A 1 92  ? 34.184 10.520  52.165 1.00 72.21  ? 92  ASN A CG  1 
ATOM   696  O OD1 . ASN A 1 92  ? 32.995 10.289  52.426 1.00 74.48  ? 92  ASN A OD1 1 
ATOM   697  N ND2 . ASN A 1 92  ? 34.738 10.058  51.053 1.00 76.33  ? 92  ASN A ND2 1 
ATOM   698  N N   . LEU A 1 93  ? 37.575 13.526  53.807 1.00 63.24  ? 93  LEU A N   1 
ATOM   699  C CA  . LEU A 1 93  ? 38.209 14.069  54.996 1.00 63.10  ? 93  LEU A CA  1 
ATOM   700  C C   . LEU A 1 93  ? 37.679 15.465  55.303 1.00 63.62  ? 93  LEU A C   1 
ATOM   701  O O   . LEU A 1 93  ? 38.178 16.395  54.678 1.00 63.91  ? 93  LEU A O   1 
ATOM   702  C CB  . LEU A 1 93  ? 39.727 14.061  54.865 1.00 59.29  ? 93  LEU A CB  1 
ATOM   703  C CG  . LEU A 1 93  ? 40.517 14.165  56.171 1.00 55.96  ? 93  LEU A CG  1 
ATOM   704  C CD1 . LEU A 1 93  ? 40.193 13.002  57.075 1.00 57.16  ? 93  LEU A CD1 1 
ATOM   705  C CD2 . LEU A 1 93  ? 42.006 14.235  55.862 1.00 55.33  ? 93  LEU A CD2 1 
ATOM   706  N N   . ASN A 1 94  ? 37.127 15.637  56.496 1.00 64.29  ? 94  ASN A N   1 
ATOM   707  C CA  . ASN A 1 94  ? 36.786 16.901  57.123 1.00 64.43  ? 94  ASN A CA  1 
ATOM   708  C C   . ASN A 1 94  ? 37.960 17.398  57.968 1.00 64.38  ? 94  ASN A C   1 
ATOM   709  O O   . ASN A 1 94  ? 38.767 16.672  58.548 1.00 63.54  ? 94  ASN A O   1 
ATOM   710  C CB  . ASN A 1 94  ? 35.491 16.804  57.896 1.00 68.37  ? 94  ASN A CB  1 
ATOM   711  C CG  . ASN A 1 94  ? 35.368 17.053  59.363 1.00 71.47  ? 94  ASN A CG  1 
ATOM   712  O OD1 . ASN A 1 94  ? 36.005 16.453  60.234 1.00 76.07  ? 94  ASN A OD1 1 
ATOM   713  N ND2 . ASN A 1 94  ? 34.486 17.988  59.727 1.00 72.43  ? 94  ASN A ND2 1 
ATOM   714  N N   . PHE A 1 95  ? 38.176 18.714  57.917 1.00 64.45  ? 95  PHE A N   1 
ATOM   715  C CA  . PHE A 1 95  ? 39.236 19.428  58.579 1.00 64.26  ? 95  PHE A CA  1 
ATOM   716  C C   . PHE A 1 95  ? 38.814 20.105  59.874 1.00 64.81  ? 95  PHE A C   1 
ATOM   717  O O   . PHE A 1 95  ? 39.626 20.854  60.434 1.00 64.61  ? 95  PHE A O   1 
ATOM   718  C CB  . PHE A 1 95  ? 39.823 20.521  57.683 1.00 61.27  ? 95  PHE A CB  1 
ATOM   719  C CG  . PHE A 1 95  ? 40.054 20.104  56.263 1.00 61.51  ? 95  PHE A CG  1 
ATOM   720  C CD1 . PHE A 1 95  ? 40.498 18.817  55.954 1.00 61.20  ? 95  PHE A CD1 1 
ATOM   721  C CD2 . PHE A 1 95  ? 39.881 21.004  55.233 1.00 59.31  ? 95  PHE A CD2 1 
ATOM   722  C CE1 . PHE A 1 95  ? 40.753 18.423  54.674 1.00 60.13  ? 95  PHE A CE1 1 
ATOM   723  C CE2 . PHE A 1 95  ? 40.120 20.604  53.949 1.00 60.54  ? 95  PHE A CE2 1 
ATOM   724  C CZ  . PHE A 1 95  ? 40.555 19.336  53.656 1.00 58.89  ? 95  PHE A CZ  1 
ATOM   725  N N   . ASP A 1 96  ? 37.755 19.612  60.505 1.00 65.93  ? 96  ASP A N   1 
ATOM   726  C CA  . ASP A 1 96  ? 37.350 20.234  61.759 1.00 67.01  ? 96  ASP A CA  1 
ATOM   727  C C   . ASP A 1 96  ? 38.274 19.997  62.934 1.00 66.94  ? 96  ASP A C   1 
ATOM   728  O O   . ASP A 1 96  ? 38.633 18.860  63.230 1.00 67.28  ? 96  ASP A O   1 
ATOM   729  C CB  . ASP A 1 96  ? 35.897 19.892  62.080 1.00 70.63  ? 96  ASP A CB  1 
ATOM   730  C CG  . ASP A 1 96  ? 34.988 20.891  61.372 1.00 74.38  ? 96  ASP A CG  1 
ATOM   731  O OD1 . ASP A 1 96  ? 35.475 21.803  60.656 1.00 77.15  ? 96  ASP A OD1 1 
ATOM   732  O OD2 . ASP A 1 96  ? 33.772 20.708  61.565 1.00 75.59  ? 96  ASP A OD2 1 
ATOM   733  N N   . LEU A 1 97  ? 38.683 21.087  63.593 1.00 66.58  ? 97  LEU A N   1 
ATOM   734  C CA  . LEU A 1 97  ? 39.385 21.021  64.854 1.00 66.93  ? 97  LEU A CA  1 
ATOM   735  C C   . LEU A 1 97  ? 38.369 20.942  66.016 1.00 67.67  ? 97  LEU A C   1 
ATOM   736  O O   . LEU A 1 97  ? 37.135 21.050  65.976 1.00 66.66  ? 97  LEU A O   1 
ATOM   737  C CB  . LEU A 1 97  ? 40.487 22.032  65.143 1.00 66.11  ? 97  LEU A CB  1 
ATOM   738  C CG  . LEU A 1 97  ? 41.627 22.265  64.161 1.00 68.06  ? 97  LEU A CG  1 
ATOM   739  C CD1 . LEU A 1 97  ? 41.075 22.386  62.717 1.00 70.02  ? 97  LEU A CD1 1 
ATOM   740  C CD2 . LEU A 1 97  ? 42.415 23.567  64.227 1.00 66.91  ? 97  LEU A CD2 1 
ATOM   741  N N   . LYS A 1 98  ? 38.972 20.493  67.114 1.00 68.61  ? 98  LYS A N   1 
ATOM   742  C CA  . LYS A 1 98  ? 38.296 20.303  68.406 1.00 69.59  ? 98  LYS A CA  1 
ATOM   743  C C   . LYS A 1 98  ? 39.351 20.302  69.494 1.00 69.61  ? 98  LYS A C   1 
ATOM   744  O O   . LYS A 1 98  ? 40.517 19.965  69.268 1.00 69.92  ? 98  LYS A O   1 
ATOM   745  C CB  . LYS A 1 98  ? 37.450 19.063  68.261 1.00 73.26  ? 98  LYS A CB  1 
ATOM   746  C CG  . LYS A 1 98  ? 36.599 18.653  69.427 1.00 77.20  ? 98  LYS A CG  1 
ATOM   747  C CD  . LYS A 1 98  ? 37.425 17.858  70.430 1.00 80.86  ? 98  LYS A CD  1 
ATOM   748  C CE  . LYS A 1 98  ? 37.272 16.356  70.259 1.00 83.24  ? 98  LYS A CE  1 
ATOM   749  N NZ  . LYS A 1 98  ? 37.708 15.602  71.478 1.00 85.02  ? 98  LYS A NZ  1 
ATOM   750  N N   . GLU A 1 99  ? 39.071 20.815  70.681 1.00 70.18  ? 99  GLU A N   1 
ATOM   751  C CA  . GLU A 1 99  ? 40.092 20.959  71.714 1.00 70.17  ? 99  GLU A CA  1 
ATOM   752  C C   . GLU A 1 99  ? 40.515 19.633  72.316 1.00 69.78  ? 99  GLU A C   1 
ATOM   753  O O   . GLU A 1 99  ? 39.723 18.712  72.489 1.00 69.42  ? 99  GLU A O   1 
ATOM   754  C CB  . GLU A 1 99  ? 39.725 21.971  72.791 1.00 69.56  ? 99  GLU A CB  1 
ATOM   755  C CG  . GLU A 1 99  ? 38.567 21.583  73.678 1.00 70.68  ? 99  GLU A CG  1 
ATOM   756  C CD  . GLU A 1 99  ? 38.863 20.559  74.752 1.00 72.43  ? 99  GLU A CD  1 
ATOM   757  O OE1 . GLU A 1 99  ? 39.967 20.464  75.334 1.00 71.60  ? 99  GLU A OE1 1 
ATOM   758  O OE2 . GLU A 1 99  ? 37.937 19.749  75.005 1.00 74.77  ? 99  GLU A OE2 1 
ATOM   759  N N   . ILE A 1 100 ? 41.763 19.598  72.757 1.00 69.77  ? 100 ILE A N   1 
ATOM   760  C CA  . ILE A 1 100 ? 42.327 18.427  73.410 1.00 70.07  ? 100 ILE A CA  1 
ATOM   761  C C   . ILE A 1 100 ? 43.238 18.888  74.539 1.00 70.66  ? 100 ILE A C   1 
ATOM   762  O O   . ILE A 1 100 ? 44.414 18.593  74.629 1.00 70.87  ? 100 ILE A O   1 
ATOM   763  C CB  . ILE A 1 100 ? 43.040 17.452  72.469 1.00 68.19  ? 100 ILE A CB  1 
ATOM   764  C CG1 . ILE A 1 100 ? 43.788 18.175  71.358 1.00 68.68  ? 100 ILE A CG1 1 
ATOM   765  C CG2 . ILE A 1 100 ? 42.086 16.438  71.849 1.00 65.34  ? 100 ILE A CG2 1 
ATOM   766  C CD1 . ILE A 1 100 ? 45.108 17.567  70.939 1.00 68.88  ? 100 ILE A CD1 1 
ATOM   767  N N   . ASN A 1 101 ? 42.645 19.588  75.496 1.00 71.57  ? 101 ASN A N   1 
ATOM   768  C CA  . ASN A 1 101 ? 43.320 20.089  76.677 1.00 72.14  ? 101 ASN A CA  1 
ATOM   769  C C   . ASN A 1 101 ? 43.793 19.010  77.625 1.00 71.75  ? 101 ASN A C   1 
ATOM   770  O O   . ASN A 1 101 ? 44.913 19.092  78.144 1.00 71.70  ? 101 ASN A O   1 
ATOM   771  C CB  . ASN A 1 101 ? 42.438 21.176  77.306 1.00 75.86  ? 101 ASN A CB  1 
ATOM   772  C CG  . ASN A 1 101 ? 43.075 22.532  77.020 1.00 79.80  ? 101 ASN A CG  1 
ATOM   773  O OD1 . ASN A 1 101 ? 43.834 22.985  77.890 1.00 83.27  ? 101 ASN A OD1 1 
ATOM   774  N ND2 . ASN A 1 101 ? 42.897 23.115  75.841 1.00 79.56  ? 101 ASN A ND2 1 
ATOM   775  N N   . ASP A 1 102 ? 43.176 17.837  77.664 1.00 71.43  ? 102 ASP A N   1 
ATOM   776  C CA  . ASP A 1 102 ? 43.656 16.687  78.393 1.00 71.54  ? 102 ASP A CA  1 
ATOM   777  C C   . ASP A 1 102 ? 45.007 16.165  77.894 1.00 71.17  ? 102 ASP A C   1 
ATOM   778  O O   . ASP A 1 102 ? 45.711 15.474  78.632 1.00 70.97  ? 102 ASP A O   1 
ATOM   779  C CB  . ASP A 1 102 ? 42.751 15.460  78.313 1.00 76.30  ? 102 ASP A CB  1 
ATOM   780  C CG  . ASP A 1 102 ? 41.285 15.768  78.098 1.00 81.68  ? 102 ASP A CG  1 
ATOM   781  O OD1 . ASP A 1 102 ? 40.628 16.109  79.113 1.00 81.03  ? 102 ASP A OD1 1 
ATOM   782  O OD2 . ASP A 1 102 ? 40.873 15.646  76.914 1.00 84.74  ? 102 ASP A OD2 1 
ATOM   783  N N   . ILE A 1 103 ? 45.336 16.367  76.623 1.00 70.36  ? 103 ILE A N   1 
ATOM   784  C CA  . ILE A 1 103 ? 46.635 15.926  76.129 1.00 69.02  ? 103 ILE A CA  1 
ATOM   785  C C   . ILE A 1 103 ? 47.654 17.017  76.390 1.00 68.31  ? 103 ILE A C   1 
ATOM   786  O O   . ILE A 1 103 ? 48.655 16.766  77.061 1.00 67.77  ? 103 ILE A O   1 
ATOM   787  C CB  . ILE A 1 103 ? 46.531 15.490  74.657 1.00 68.70  ? 103 ILE A CB  1 
ATOM   788  C CG1 . ILE A 1 103 ? 45.389 14.460  74.601 1.00 67.58  ? 103 ILE A CG1 1 
ATOM   789  C CG2 . ILE A 1 103 ? 47.836 14.911  74.153 1.00 65.18  ? 103 ILE A CG2 1 
ATOM   790  C CD1 . ILE A 1 103 ? 45.080 13.866  73.261 1.00 67.67  ? 103 ILE A CD1 1 
ATOM   791  N N   . CYS A 1 104 ? 47.312 18.267  76.090 1.00 67.83  ? 104 CYS A N   1 
ATOM   792  C CA  . CYS A 1 104 ? 48.269 19.366  76.233 1.00 67.14  ? 104 CYS A CA  1 
ATOM   793  C C   . CYS A 1 104 ? 47.547 20.704  76.170 1.00 66.75  ? 104 CYS A C   1 
ATOM   794  O O   . CYS A 1 104 ? 46.751 20.930  75.263 1.00 67.28  ? 104 CYS A O   1 
ATOM   795  C CB  . CYS A 1 104 ? 49.436 19.343  75.236 1.00 62.32  ? 104 CYS A CB  1 
ATOM   796  S SG  . CYS A 1 104 ? 49.077 19.140  73.479 1.00 57.88  ? 104 CYS A SG  1 
ATOM   797  N N   . SER A 1 105 ? 48.021 21.654  76.957 1.00 66.82  ? 105 SER A N   1 
ATOM   798  C CA  . SER A 1 105 ? 47.416 22.965  77.064 1.00 66.21  ? 105 SER A CA  1 
ATOM   799  C C   . SER A 1 105 ? 47.412 23.739  75.749 1.00 64.87  ? 105 SER A C   1 
ATOM   800  O O   . SER A 1 105 ? 48.419 24.090  75.152 1.00 63.73  ? 105 SER A O   1 
ATOM   801  C CB  . SER A 1 105 ? 48.005 23.861  78.158 1.00 67.48  ? 105 SER A CB  1 
ATOM   802  O OG  . SER A 1 105 ? 48.881 24.852  77.622 1.00 69.67  ? 105 SER A OG  1 
ATOM   803  N N   . GLY A 1 106 ? 46.177 24.132  75.442 1.00 64.33  ? 106 GLY A N   1 
ATOM   804  C CA  . GLY A 1 106 ? 45.964 24.952  74.248 1.00 64.25  ? 106 GLY A CA  1 
ATOM   805  C C   . GLY A 1 106 ? 46.159 24.155  72.962 1.00 62.89  ? 106 GLY A C   1 
ATOM   806  O O   . GLY A 1 106 ? 46.821 24.667  72.072 1.00 63.22  ? 106 GLY A O   1 
ATOM   807  N N   . CYS A 1 107 ? 45.887 22.864  72.988 1.00 61.84  ? 107 CYS A N   1 
ATOM   808  C CA  . CYS A 1 107 ? 46.113 22.033  71.830 1.00 60.53  ? 107 CYS A CA  1 
ATOM   809  C C   . CYS A 1 107 ? 44.724 21.647  71.299 1.00 59.54  ? 107 CYS A C   1 
ATOM   810  O O   . CYS A 1 107 ? 43.768 21.399  72.017 1.00 58.02  ? 107 CYS A O   1 
ATOM   811  C CB  . CYS A 1 107 ? 46.980 20.809  72.044 1.00 58.19  ? 107 CYS A CB  1 
ATOM   812  S SG  . CYS A 1 107 ? 48.606 20.987  72.764 1.00 57.20  ? 107 CYS A SG  1 
ATOM   813  N N   . ARG A 1 108 ? 44.639 21.877  69.984 1.00 59.31  ? 108 ARG A N   1 
ATOM   814  C CA  . ARG A 1 108 ? 43.476 21.414  69.226 1.00 58.15  ? 108 ARG A CA  1 
ATOM   815  C C   . ARG A 1 108 ? 43.990 20.328  68.266 1.00 56.71  ? 108 ARG A C   1 
ATOM   816  O O   . ARG A 1 108 ? 45.131 20.455  67.825 1.00 56.18  ? 108 ARG A O   1 
ATOM   817  C CB  . ARG A 1 108 ? 42.802 22.560  68.494 1.00 56.76  ? 108 ARG A CB  1 
ATOM   818  C CG  . ARG A 1 108 ? 42.697 23.830  69.318 1.00 59.87  ? 108 ARG A CG  1 
ATOM   819  C CD  . ARG A 1 108 ? 41.844 24.892  68.626 1.00 61.15  ? 108 ARG A CD  1 
ATOM   820  N NE  . ARG A 1 108 ? 40.444 24.481  68.792 1.00 62.03  ? 108 ARG A NE  1 
ATOM   821  C CZ  . ARG A 1 108 ? 39.519 24.713  67.874 1.00 65.07  ? 108 ARG A CZ  1 
ATOM   822  N NH1 . ARG A 1 108 ? 39.803 25.336  66.713 1.00 68.15  ? 108 ARG A NH1 1 
ATOM   823  N NH2 . ARG A 1 108 ? 38.302 24.258  68.156 1.00 65.89  ? 108 ARG A NH2 1 
ATOM   824  N N   . GLY A 1 109 ? 43.223 19.262  68.092 1.00 55.06  ? 109 GLY A N   1 
ATOM   825  C CA  . GLY A 1 109 ? 43.562 18.254  67.114 1.00 54.61  ? 109 GLY A CA  1 
ATOM   826  C C   . GLY A 1 109 ? 42.368 17.789  66.273 1.00 53.97  ? 109 GLY A C   1 
ATOM   827  O O   . GLY A 1 109 ? 41.249 18.160  66.593 1.00 53.68  ? 109 GLY A O   1 
ATOM   828  N N   . HIS A 1 110 ? 42.606 17.147  65.142 1.00 53.20  ? 110 HIS A N   1 
ATOM   829  C CA  . HIS A 1 110 ? 41.578 16.616  64.292 1.00 53.05  ? 110 HIS A CA  1 
ATOM   830  C C   . HIS A 1 110 ? 40.559 15.871  65.174 1.00 53.22  ? 110 HIS A C   1 
ATOM   831  O O   . HIS A 1 110 ? 40.700 14.806  65.750 1.00 52.55  ? 110 HIS A O   1 
ATOM   832  C CB  . HIS A 1 110 ? 42.097 15.633  63.247 1.00 49.39  ? 110 HIS A CB  1 
ATOM   833  C CG  . HIS A 1 110 ? 41.115 15.243  62.197 1.00 48.01  ? 110 HIS A CG  1 
ATOM   834  N ND1 . HIS A 1 110 ? 40.298 14.134  62.272 1.00 47.44  ? 110 HIS A ND1 1 
ATOM   835  C CD2 . HIS A 1 110 ? 40.844 15.810  60.985 1.00 48.20  ? 110 HIS A CD2 1 
ATOM   836  C CE1 . HIS A 1 110 ? 39.566 14.038  61.179 1.00 45.38  ? 110 HIS A CE1 1 
ATOM   837  N NE2 . HIS A 1 110 ? 39.891 15.044  60.373 1.00 45.23  ? 110 HIS A NE2 1 
ATOM   838  N N   . ASP A 1 111 ? 39.406 16.517  65.062 1.00 53.10  ? 111 ASP A N   1 
ATOM   839  C CA  . ASP A 1 111 ? 38.246 16.128  65.808 1.00 53.86  ? 111 ASP A CA  1 
ATOM   840  C C   . ASP A 1 111 ? 37.980 14.653  65.655 1.00 53.69  ? 111 ASP A C   1 
ATOM   841  O O   . ASP A 1 111 ? 37.823 13.975  66.678 1.00 54.09  ? 111 ASP A O   1 
ATOM   842  C CB  . ASP A 1 111 ? 37.117 17.088  65.468 1.00 56.87  ? 111 ASP A CB  1 
ATOM   843  C CG  . ASP A 1 111 ? 35.835 16.780  66.173 1.00 58.61  ? 111 ASP A CG  1 
ATOM   844  O OD1 . ASP A 1 111 ? 35.761 15.750  66.870 1.00 60.75  ? 111 ASP A OD1 1 
ATOM   845  O OD2 . ASP A 1 111 ? 34.850 17.534  66.077 1.00 63.15  ? 111 ASP A OD2 1 
ATOM   846  N N   . GLY A 1 112 ? 37.934 14.045  64.472 1.00 53.82  ? 112 GLY A N   1 
ATOM   847  C CA  . GLY A 1 112 ? 37.756 12.616  64.260 1.00 52.67  ? 112 GLY A CA  1 
ATOM   848  C C   . GLY A 1 112 ? 38.889 11.740  64.768 1.00 52.86  ? 112 GLY A C   1 
ATOM   849  O O   . GLY A 1 112 ? 38.702 10.762  65.497 1.00 52.08  ? 112 GLY A O   1 
ATOM   850  N N   . PHE A 1 113 ? 40.146 12.166  64.540 1.00 52.77  ? 113 PHE A N   1 
ATOM   851  C CA  . PHE A 1 113 ? 41.292 11.350  64.962 1.00 52.52  ? 113 PHE A CA  1 
ATOM   852  C C   . PHE A 1 113 ? 41.241 11.274  66.474 1.00 53.40  ? 113 PHE A C   1 
ATOM   853  O O   . PHE A 1 113 ? 41.088 10.238  67.103 1.00 53.64  ? 113 PHE A O   1 
ATOM   854  C CB  . PHE A 1 113 ? 42.629 11.856  64.443 1.00 46.49  ? 113 PHE A CB  1 
ATOM   855  C CG  . PHE A 1 113 ? 42.721 12.072  62.936 1.00 41.11  ? 113 PHE A CG  1 
ATOM   856  C CD1 . PHE A 1 113 ? 41.915 11.433  62.005 1.00 36.34  ? 113 PHE A CD1 1 
ATOM   857  C CD2 . PHE A 1 113 ? 43.685 12.947  62.458 1.00 35.99  ? 113 PHE A CD2 1 
ATOM   858  C CE1 . PHE A 1 113 ? 42.103 11.702  60.660 1.00 36.57  ? 113 PHE A CE1 1 
ATOM   859  C CE2 . PHE A 1 113 ? 43.871 13.209  61.131 1.00 33.34  ? 113 PHE A CE2 1 
ATOM   860  C CZ  . PHE A 1 113 ? 43.042 12.618  60.204 1.00 33.22  ? 113 PHE A CZ  1 
ATOM   861  N N   . THR A 1 114 ? 41.108 12.466  67.016 1.00 54.53  ? 114 THR A N   1 
ATOM   862  C CA  . THR A 1 114 ? 40.949 12.732  68.438 1.00 55.05  ? 114 THR A CA  1 
ATOM   863  C C   . THR A 1 114 ? 39.766 12.023  69.054 1.00 55.45  ? 114 THR A C   1 
ATOM   864  O O   . THR A 1 114 ? 39.968 11.361  70.074 1.00 55.21  ? 114 THR A O   1 
ATOM   865  C CB  . THR A 1 114 ? 40.778 14.259  68.528 1.00 55.30  ? 114 THR A CB  1 
ATOM   866  O OG1 . THR A 1 114 ? 42.066 14.843  68.286 1.00 56.46  ? 114 THR A OG1 1 
ATOM   867  C CG2 . THR A 1 114 ? 40.186 14.691  69.830 1.00 59.22  ? 114 THR A CG2 1 
ATOM   868  N N   . SER A 1 115 ? 38.569 11.987  68.455 1.00 55.97  ? 115 SER A N   1 
ATOM   869  C CA  . SER A 1 115 ? 37.467 11.263  69.099 1.00 56.09  ? 115 SER A CA  1 
ATOM   870  C C   . SER A 1 115 ? 37.556 9.740   68.957 1.00 56.49  ? 115 SER A C   1 
ATOM   871  O O   . SER A 1 115 ? 36.940 9.077   69.794 1.00 56.09  ? 115 SER A O   1 
ATOM   872  C CB  . SER A 1 115 ? 36.084 11.654  68.585 1.00 53.43  ? 115 SER A CB  1 
ATOM   873  O OG  . SER A 1 115 ? 36.043 12.983  68.150 1.00 54.03  ? 115 SER A OG  1 
ATOM   874  N N   . SER A 1 116 ? 38.154 9.229   67.880 1.00 56.28  ? 116 SER A N   1 
ATOM   875  C CA  . SER A 1 116 ? 38.248 7.799   67.677 1.00 56.89  ? 116 SER A CA  1 
ATOM   876  C C   . SER A 1 116 ? 39.169 7.192   68.726 1.00 57.00  ? 116 SER A C   1 
ATOM   877  O O   . SER A 1 116 ? 38.801 6.166   69.278 1.00 57.36  ? 116 SER A O   1 
ATOM   878  C CB  . SER A 1 116 ? 38.835 7.362   66.317 1.00 59.21  ? 116 SER A CB  1 
ATOM   879  O OG  . SER A 1 116 ? 37.983 7.852   65.294 1.00 60.81  ? 116 SER A OG  1 
ATOM   880  N N   . TRP A 1 117 ? 40.322 7.832   68.903 1.00 56.83  ? 117 TRP A N   1 
ATOM   881  C CA  . TRP A 1 117 ? 41.290 7.320   69.858 1.00 56.95  ? 117 TRP A CA  1 
ATOM   882  C C   . TRP A 1 117 ? 40.672 7.453   71.245 1.00 57.46  ? 117 TRP A C   1 
ATOM   883  O O   . TRP A 1 117 ? 40.383 6.457   71.887 1.00 56.81  ? 117 TRP A O   1 
ATOM   884  C CB  . TRP A 1 117 ? 42.614 8.102   69.871 1.00 53.72  ? 117 TRP A CB  1 
ATOM   885  C CG  . TRP A 1 117 ? 43.369 7.781   71.134 1.00 52.98  ? 117 TRP A CG  1 
ATOM   886  C CD1 . TRP A 1 117 ? 43.644 8.633   72.162 1.00 52.11  ? 117 TRP A CD1 1 
ATOM   887  C CD2 . TRP A 1 117 ? 43.838 6.488   71.540 1.00 51.49  ? 117 TRP A CD2 1 
ATOM   888  N NE1 . TRP A 1 117 ? 44.271 7.943   73.178 1.00 52.17  ? 117 TRP A NE1 1 
ATOM   889  C CE2 . TRP A 1 117 ? 44.431 6.637   72.809 1.00 50.43  ? 117 TRP A CE2 1 
ATOM   890  C CE3 . TRP A 1 117 ? 43.844 5.229   70.944 1.00 51.35  ? 117 TRP A CE3 1 
ATOM   891  C CZ2 . TRP A 1 117 ? 45.036 5.584   73.476 1.00 51.40  ? 117 TRP A CZ2 1 
ATOM   892  C CZ3 . TRP A 1 117 ? 44.416 4.159   71.627 1.00 51.39  ? 117 TRP A CZ3 1 
ATOM   893  C CH2 . TRP A 1 117 ? 45.011 4.341   72.887 1.00 51.50  ? 117 TRP A CH2 1 
ATOM   894  N N   . ARG A 1 118 ? 40.135 8.647   71.507 1.00 58.43  ? 118 ARG A N   1 
ATOM   895  C CA  . ARG A 1 118 ? 39.535 8.960   72.793 1.00 59.59  ? 118 ARG A CA  1 
ATOM   896  C C   . ARG A 1 118 ? 38.558 7.873   73.225 1.00 59.58  ? 118 ARG A C   1 
ATOM   897  O O   . ARG A 1 118 ? 38.490 7.549   74.412 1.00 59.73  ? 118 ARG A O   1 
ATOM   898  C CB  . ARG A 1 118 ? 38.875 10.335  72.840 1.00 62.99  ? 118 ARG A CB  1 
ATOM   899  C CG  . ARG A 1 118 ? 37.988 10.640  74.023 1.00 66.79  ? 118 ARG A CG  1 
ATOM   900  C CD  . ARG A 1 118 ? 38.662 10.981  75.328 1.00 70.78  ? 118 ARG A CD  1 
ATOM   901  N NE  . ARG A 1 118 ? 39.823 10.183  75.704 1.00 74.17  ? 118 ARG A NE  1 
ATOM   902  C CZ  . ARG A 1 118 ? 41.078 10.476  75.348 1.00 75.72  ? 118 ARG A CZ  1 
ATOM   903  N NH1 . ARG A 1 118 ? 41.366 11.534  74.603 1.00 75.08  ? 118 ARG A NH1 1 
ATOM   904  N NH2 . ARG A 1 118 ? 42.079 9.684   75.721 1.00 78.86  ? 118 ARG A NH2 1 
ATOM   905  N N   . SER A 1 119 ? 37.888 7.277   72.261 1.00 59.04  ? 119 SER A N   1 
ATOM   906  C CA  . SER A 1 119 ? 36.907 6.243   72.419 1.00 58.83  ? 119 SER A CA  1 
ATOM   907  C C   . SER A 1 119 ? 37.433 4.850   72.665 1.00 58.68  ? 119 SER A C   1 
ATOM   908  O O   . SER A 1 119 ? 36.615 4.019   73.093 1.00 59.68  ? 119 SER A O   1 
ATOM   909  C CB  . SER A 1 119 ? 36.062 6.240   71.128 1.00 59.11  ? 119 SER A CB  1 
ATOM   910  O OG  . SER A 1 119 ? 35.335 5.037   71.024 1.00 61.54  ? 119 SER A OG  1 
ATOM   911  N N   . VAL A 1 120 ? 38.688 4.550   72.331 1.00 57.87  ? 120 VAL A N   1 
ATOM   912  C CA  . VAL A 1 120 ? 39.235 3.213   72.567 1.00 56.32  ? 120 VAL A CA  1 
ATOM   913  C C   . VAL A 1 120 ? 40.384 3.326   73.567 1.00 55.74  ? 120 VAL A C   1 
ATOM   914  O O   . VAL A 1 120 ? 40.956 2.328   73.999 1.00 55.65  ? 120 VAL A O   1 
ATOM   915  C CB  . VAL A 1 120 ? 39.780 2.459   71.337 1.00 54.34  ? 120 VAL A CB  1 
ATOM   916  C CG1 . VAL A 1 120 ? 38.693 2.154   70.328 1.00 53.24  ? 120 VAL A CG1 1 
ATOM   917  C CG2 . VAL A 1 120 ? 40.920 3.223   70.670 1.00 50.76  ? 120 VAL A CG2 1 
ATOM   918  N N   . ALA A 1 121 ? 40.690 4.554   73.945 1.00 55.71  ? 121 ALA A N   1 
ATOM   919  C CA  . ALA A 1 121 ? 41.788 4.843   74.855 1.00 56.13  ? 121 ALA A CA  1 
ATOM   920  C C   . ALA A 1 121 ? 41.815 3.962   76.080 1.00 55.99  ? 121 ALA A C   1 
ATOM   921  O O   . ALA A 1 121 ? 42.849 3.335   76.288 1.00 57.05  ? 121 ALA A O   1 
ATOM   922  C CB  . ALA A 1 121 ? 41.816 6.305   75.283 1.00 55.84  ? 121 ALA A CB  1 
ATOM   923  N N   . ASP A 1 122 ? 40.753 3.879   76.849 1.00 56.21  ? 122 ASP A N   1 
ATOM   924  C CA  . ASP A 1 122 ? 40.759 3.057   78.054 1.00 56.37  ? 122 ASP A CA  1 
ATOM   925  C C   . ASP A 1 122 ? 40.931 1.579   77.794 1.00 56.44  ? 122 ASP A C   1 
ATOM   926  O O   . ASP A 1 122 ? 41.800 1.031   78.478 1.00 56.38  ? 122 ASP A O   1 
ATOM   927  C CB  . ASP A 1 122 ? 39.568 3.347   78.958 1.00 56.93  ? 122 ASP A CB  1 
ATOM   928  C CG  . ASP A 1 122 ? 39.536 4.799   79.408 1.00 57.76  ? 122 ASP A CG  1 
ATOM   929  O OD1 . ASP A 1 122 ? 40.604 5.444   79.541 1.00 60.37  ? 122 ASP A OD1 1 
ATOM   930  O OD2 . ASP A 1 122 ? 38.423 5.310   79.635 1.00 57.60  ? 122 ASP A OD2 1 
ATOM   931  N N   . THR A 1 123 ? 40.237 0.931   76.859 1.00 56.67  ? 123 THR A N   1 
ATOM   932  C CA  . THR A 1 123 ? 40.583 -0.481  76.636 1.00 57.10  ? 123 THR A CA  1 
ATOM   933  C C   . THR A 1 123 ? 42.032 -0.591  76.176 1.00 57.17  ? 123 THR A C   1 
ATOM   934  O O   . THR A 1 123 ? 42.824 -1.216  76.854 1.00 57.28  ? 123 THR A O   1 
ATOM   935  C CB  . THR A 1 123 ? 39.652 -1.209  75.659 1.00 56.92  ? 123 THR A CB  1 
ATOM   936  O OG1 . THR A 1 123 ? 38.370 -1.347  76.310 1.00 59.07  ? 123 THR A OG1 1 
ATOM   937  C CG2 . THR A 1 123 ? 40.136 -2.606  75.297 1.00 53.02  ? 123 THR A CG2 1 
ATOM   938  N N   . LEU A 1 124 ? 42.453 0.105   75.118 1.00 57.36  ? 124 LEU A N   1 
ATOM   939  C CA  . LEU A 1 124 ? 43.829 -0.036  74.667 1.00 56.89  ? 124 LEU A CA  1 
ATOM   940  C C   . LEU A 1 124 ? 44.836 0.367   75.725 1.00 56.49  ? 124 LEU A C   1 
ATOM   941  O O   . LEU A 1 124 ? 45.770 -0.422  75.937 1.00 55.78  ? 124 LEU A O   1 
ATOM   942  C CB  . LEU A 1 124 ? 44.050 0.491   73.243 1.00 51.57  ? 124 LEU A CB  1 
ATOM   943  C CG  . LEU A 1 124 ? 43.151 -0.161  72.191 1.00 50.02  ? 124 LEU A CG  1 
ATOM   944  C CD1 . LEU A 1 124 ? 43.146 0.625   70.887 1.00 49.00  ? 124 LEU A CD1 1 
ATOM   945  C CD2 . LEU A 1 124 ? 43.475 -1.624  71.900 1.00 47.05  ? 124 LEU A CD2 1 
ATOM   946  N N   . ARG A 1 125 ? 44.659 1.439   76.484 1.00 56.52  ? 125 ARG A N   1 
ATOM   947  C CA  . ARG A 1 125 ? 45.622 1.855   77.521 1.00 56.98  ? 125 ARG A CA  1 
ATOM   948  C C   . ARG A 1 125 ? 45.831 0.719   78.527 1.00 56.17  ? 125 ARG A C   1 
ATOM   949  O O   . ARG A 1 125 ? 46.908 0.227   78.846 1.00 55.09  ? 125 ARG A O   1 
ATOM   950  C CB  . ARG A 1 125 ? 45.101 3.090   78.232 1.00 61.31  ? 125 ARG A CB  1 
ATOM   951  C CG  . ARG A 1 125 ? 45.941 3.763   79.297 1.00 69.18  ? 125 ARG A CG  1 
ATOM   952  C CD  . ARG A 1 125 ? 45.209 4.925   79.945 1.00 75.65  ? 125 ARG A CD  1 
ATOM   953  N NE  . ARG A 1 125 ? 45.825 5.795   80.918 1.00 83.22  ? 125 ARG A NE  1 
ATOM   954  C CZ  . ARG A 1 125 ? 46.726 5.579   81.879 1.00 88.08  ? 125 ARG A CZ  1 
ATOM   955  N NH1 . ARG A 1 125 ? 47.198 4.323   81.983 1.00 90.48  ? 125 ARG A NH1 1 
ATOM   956  N NH2 . ARG A 1 125 ? 47.187 6.483   82.771 1.00 89.34  ? 125 ARG A NH2 1 
ATOM   957  N N   . GLN A 1 126 ? 44.690 0.116   78.884 1.00 55.82  ? 126 GLN A N   1 
ATOM   958  C CA  . GLN A 1 126 ? 44.673 -1.041  79.751 1.00 55.41  ? 126 GLN A CA  1 
ATOM   959  C C   . GLN A 1 126 ? 45.523 -2.171  79.193 1.00 53.79  ? 126 GLN A C   1 
ATOM   960  O O   . GLN A 1 126 ? 46.394 -2.715  79.890 1.00 53.03  ? 126 GLN A O   1 
ATOM   961  C CB  . GLN A 1 126 ? 43.263 -1.477  80.120 1.00 59.76  ? 126 GLN A CB  1 
ATOM   962  C CG  . GLN A 1 126 ? 43.160 -2.904  80.629 1.00 65.48  ? 126 GLN A CG  1 
ATOM   963  C CD  . GLN A 1 126 ? 42.667 -3.909  79.595 1.00 69.35  ? 126 GLN A CD  1 
ATOM   964  O OE1 . GLN A 1 126 ? 42.179 -3.504  78.526 1.00 67.50  ? 126 GLN A OE1 1 
ATOM   965  N NE2 . GLN A 1 126 ? 42.763 -5.209  79.946 1.00 69.76  ? 126 GLN A NE2 1 
ATOM   966  N N   . LYS A 1 127 ? 45.271 -2.539  77.939 1.00 52.44  ? 127 LYS A N   1 
ATOM   967  C CA  . LYS A 1 127 ? 45.970 -3.669  77.336 1.00 50.64  ? 127 LYS A CA  1 
ATOM   968  C C   . LYS A 1 127 ? 47.456 -3.471  77.207 1.00 50.55  ? 127 LYS A C   1 
ATOM   969  O O   . LYS A 1 127 ? 48.242 -4.340  77.594 1.00 50.66  ? 127 LYS A O   1 
ATOM   970  C CB  . LYS A 1 127 ? 45.243 -4.039  76.052 1.00 49.55  ? 127 LYS A CB  1 
ATOM   971  C CG  . LYS A 1 127 ? 44.105 -4.964  76.443 1.00 48.52  ? 127 LYS A CG  1 
ATOM   972  C CD  . LYS A 1 127 ? 42.950 -4.992  75.479 1.00 48.30  ? 127 LYS A CD  1 
ATOM   973  C CE  . LYS A 1 127 ? 41.928 -6.045  75.917 1.00 48.89  ? 127 LYS A CE  1 
ATOM   974  N NZ  . LYS A 1 127 ? 42.556 -7.345  76.287 1.00 48.35  ? 127 LYS A NZ  1 
ATOM   975  N N   . VAL A 1 128 ? 47.881 -2.238  76.941 1.00 49.99  ? 128 VAL A N   1 
ATOM   976  C CA  . VAL A 1 128 ? 49.259 -1.836  76.904 1.00 49.31  ? 128 VAL A CA  1 
ATOM   977  C C   . VAL A 1 128 ? 49.853 -1.926  78.296 1.00 50.24  ? 128 VAL A C   1 
ATOM   978  O O   . VAL A 1 128 ? 51.001 -2.328  78.483 1.00 49.82  ? 128 VAL A O   1 
ATOM   979  C CB  . VAL A 1 128 ? 49.412 -0.420  76.327 1.00 45.76  ? 128 VAL A CB  1 
ATOM   980  C CG1 . VAL A 1 128 ? 50.862 0.084   76.345 1.00 40.99  ? 128 VAL A CG1 1 
ATOM   981  C CG2 . VAL A 1 128 ? 48.953 -0.487  74.883 1.00 45.05  ? 128 VAL A CG2 1 
ATOM   982  N N   . GLU A 1 129 ? 49.055 -1.574  79.303 1.00 51.37  ? 129 GLU A N   1 
ATOM   983  C CA  . GLU A 1 129 ? 49.553 -1.683  80.669 1.00 52.23  ? 129 GLU A CA  1 
ATOM   984  C C   . GLU A 1 129 ? 49.841 -3.100  81.090 1.00 52.92  ? 129 GLU A C   1 
ATOM   985  O O   . GLU A 1 129 ? 50.918 -3.370  81.636 1.00 53.17  ? 129 GLU A O   1 
ATOM   986  C CB  . GLU A 1 129 ? 48.613 -0.987  81.642 1.00 52.42  ? 129 GLU A CB  1 
ATOM   987  C CG  . GLU A 1 129 ? 49.209 0.374   81.834 1.00 53.15  ? 129 GLU A CG  1 
ATOM   988  C CD  . GLU A 1 129 ? 48.358 1.604   82.060 1.00 54.01  ? 129 GLU A CD  1 
ATOM   989  O OE1 . GLU A 1 129 ? 47.303 1.306   82.623 1.00 50.06  ? 129 GLU A OE1 1 
ATOM   990  O OE2 . GLU A 1 129 ? 49.005 2.619   81.580 1.00 57.16  ? 129 GLU A OE2 1 
ATOM   991  N N   . ASP A 1 130 ? 48.970 -4.045  80.758 1.00 53.57  ? 130 ASP A N   1 
ATOM   992  C CA  . ASP A 1 130 ? 49.283 -5.401  81.191 1.00 54.53  ? 130 ASP A CA  1 
ATOM   993  C C   . ASP A 1 130 ? 50.539 -5.883  80.504 1.00 54.60  ? 130 ASP A C   1 
ATOM   994  O O   . ASP A 1 130 ? 51.245 -6.616  81.188 1.00 55.66  ? 130 ASP A O   1 
ATOM   995  C CB  . ASP A 1 130 ? 48.124 -6.345  80.956 1.00 56.66  ? 130 ASP A CB  1 
ATOM   996  C CG  . ASP A 1 130 ? 46.846 -5.810  81.554 1.00 58.59  ? 130 ASP A CG  1 
ATOM   997  O OD1 . ASP A 1 130 ? 46.849 -5.056  82.558 1.00 60.68  ? 130 ASP A OD1 1 
ATOM   998  O OD2 . ASP A 1 130 ? 45.813 -6.181  80.955 1.00 62.23  ? 130 ASP A OD2 1 
ATOM   999  N N   . ALA A 1 131 ? 50.793 -5.553  79.258 1.00 54.11  ? 131 ALA A N   1 
ATOM   1000 C CA  . ALA A 1 131 ? 51.978 -6.000  78.541 1.00 53.04  ? 131 ALA A CA  1 
ATOM   1001 C C   . ALA A 1 131 ? 53.231 -5.429  79.192 1.00 51.89  ? 131 ALA A C   1 
ATOM   1002 O O   . ALA A 1 131 ? 54.220 -6.121  79.441 1.00 51.38  ? 131 ALA A O   1 
ATOM   1003 C CB  . ALA A 1 131 ? 51.866 -5.607  77.067 1.00 50.32  ? 131 ALA A CB  1 
ATOM   1004 N N   . VAL A 1 132 ? 53.186 -4.140  79.493 1.00 51.28  ? 132 VAL A N   1 
ATOM   1005 C CA  . VAL A 1 132 ? 54.299 -3.514  80.212 1.00 52.33  ? 132 VAL A CA  1 
ATOM   1006 C C   . VAL A 1 132 ? 54.604 -4.301  81.493 1.00 53.44  ? 132 VAL A C   1 
ATOM   1007 O O   . VAL A 1 132 ? 55.775 -4.600  81.700 1.00 52.62  ? 132 VAL A O   1 
ATOM   1008 C CB  . VAL A 1 132 ? 53.946 -2.048  80.418 1.00 49.06  ? 132 VAL A CB  1 
ATOM   1009 C CG1 . VAL A 1 132 ? 54.927 -1.337  81.322 1.00 49.82  ? 132 VAL A CG1 1 
ATOM   1010 C CG2 . VAL A 1 132 ? 53.960 -1.299  79.087 1.00 47.54  ? 132 VAL A CG2 1 
ATOM   1011 N N   . ARG A 1 133 ? 53.572 -4.658  82.280 1.00 54.59  ? 133 ARG A N   1 
ATOM   1012 C CA  . ARG A 1 133 ? 53.751 -5.410  83.460 1.00 55.50  ? 133 ARG A CA  1 
ATOM   1013 C C   . ARG A 1 133 ? 54.511 -6.691  83.214 1.00 56.36  ? 133 ARG A C   1 
ATOM   1014 O O   . ARG A 1 133 ? 55.505 -7.021  83.843 1.00 56.13  ? 133 ARG A O   1 
ATOM   1015 C CB  . ARG A 1 133 ? 52.449 -5.731  84.171 1.00 58.22  ? 133 ARG A CB  1 
ATOM   1016 C CG  . ARG A 1 133 ? 52.719 -6.293  85.575 1.00 56.85  ? 133 ARG A CG  1 
ATOM   1017 C CD  . ARG A 1 133 ? 51.386 -6.615  86.197 1.00 59.47  ? 133 ARG A CD  1 
ATOM   1018 N NE  . ARG A 1 133 ? 50.867 -7.941  85.823 1.00 64.13  ? 133 ARG A NE  1 
ATOM   1019 C CZ  . ARG A 1 133 ? 49.720 -8.018  85.130 1.00 67.18  ? 133 ARG A CZ  1 
ATOM   1020 N NH1 . ARG A 1 133 ? 49.066 -6.894  84.812 1.00 66.91  ? 133 ARG A NH1 1 
ATOM   1021 N NH2 . ARG A 1 133 ? 49.236 -9.203  84.800 1.00 68.98  ? 133 ARG A NH2 1 
ATOM   1022 N N   . GLU A 1 134 ? 53.922 -7.559  82.408 1.00 57.87  ? 134 GLU A N   1 
ATOM   1023 C CA  . GLU A 1 134 ? 54.488 -8.836  82.009 1.00 58.48  ? 134 GLU A CA  1 
ATOM   1024 C C   . GLU A 1 134 ? 55.898 -8.681  81.470 1.00 58.42  ? 134 GLU A C   1 
ATOM   1025 O O   . GLU A 1 134 ? 56.517 -9.715  81.161 1.00 59.48  ? 134 GLU A O   1 
ATOM   1026 C CB  . GLU A 1 134 ? 53.664 -9.487  80.932 1.00 63.45  ? 134 GLU A CB  1 
ATOM   1027 C CG  . GLU A 1 134 ? 52.658 -10.578 81.167 1.00 69.96  ? 134 GLU A CG  1 
ATOM   1028 C CD  . GLU A 1 134 ? 51.301 -10.162 81.668 1.00 72.94  ? 134 GLU A CD  1 
ATOM   1029 O OE1 . GLU A 1 134 ? 50.845 -9.042  81.368 1.00 75.28  ? 134 GLU A OE1 1 
ATOM   1030 O OE2 . GLU A 1 134 ? 50.595 -10.895 82.405 1.00 75.60  ? 134 GLU A OE2 1 
ATOM   1031 N N   . HIS A 1 135 ? 56.283 -7.621  80.773 1.00 57.83  ? 135 HIS A N   1 
ATOM   1032 C CA  . HIS A 1 135 ? 57.564 -7.450  80.120 1.00 57.07  ? 135 HIS A CA  1 
ATOM   1033 C C   . HIS A 1 135 ? 58.140 -6.053  80.305 1.00 57.13  ? 135 HIS A C   1 
ATOM   1034 O O   . HIS A 1 135 ? 58.369 -5.251  79.408 1.00 57.69  ? 135 HIS A O   1 
ATOM   1035 C CB  . HIS A 1 135 ? 57.463 -7.710  78.599 1.00 51.72  ? 135 HIS A CB  1 
ATOM   1036 C CG  . HIS A 1 135 ? 56.741 -8.975  78.264 1.00 51.77  ? 135 HIS A CG  1 
ATOM   1037 N ND1 . HIS A 1 135 ? 57.326 -10.226 78.269 1.00 49.65  ? 135 HIS A ND1 1 
ATOM   1038 C CD2 . HIS A 1 135 ? 55.409 -9.149  78.005 1.00 50.55  ? 135 HIS A CD2 1 
ATOM   1039 C CE1 . HIS A 1 135 ? 56.377 -11.102 77.988 1.00 50.38  ? 135 HIS A CE1 1 
ATOM   1040 N NE2 . HIS A 1 135 ? 55.207 -10.497 77.850 1.00 48.68  ? 135 HIS A NE2 1 
ATOM   1041 N N   . PRO A 1 136 ? 58.591 -5.730  81.503 1.00 56.93  ? 136 PRO A N   1 
ATOM   1042 C CA  . PRO A 1 136 ? 59.034 -4.416  81.920 1.00 56.33  ? 136 PRO A CA  1 
ATOM   1043 C C   . PRO A 1 136 ? 60.213 -3.881  81.107 1.00 55.38  ? 136 PRO A C   1 
ATOM   1044 O O   . PRO A 1 136 ? 60.446 -2.688  80.929 1.00 53.62  ? 136 PRO A O   1 
ATOM   1045 C CB  . PRO A 1 136 ? 59.408 -4.616  83.407 1.00 56.05  ? 136 PRO A CB  1 
ATOM   1046 C CG  . PRO A 1 136 ? 59.589 -6.086  83.583 1.00 55.92  ? 136 PRO A CG  1 
ATOM   1047 C CD  . PRO A 1 136 ? 58.555 -6.693  82.676 1.00 56.71  ? 136 PRO A CD  1 
ATOM   1048 N N   . ASP A 1 137 ? 61.010 -4.844  80.694 1.00 54.76  ? 137 ASP A N   1 
ATOM   1049 C CA  . ASP A 1 137 ? 62.225 -4.659  79.933 1.00 55.25  ? 137 ASP A CA  1 
ATOM   1050 C C   . ASP A 1 137 ? 61.957 -4.351  78.461 1.00 54.03  ? 137 ASP A C   1 
ATOM   1051 O O   . ASP A 1 137 ? 62.690 -3.573  77.856 1.00 54.22  ? 137 ASP A O   1 
ATOM   1052 C CB  . ASP A 1 137 ? 63.105 -5.904  80.153 1.00 57.61  ? 137 ASP A CB  1 
ATOM   1053 C CG  . ASP A 1 137 ? 62.447 -7.206  79.701 1.00 62.20  ? 137 ASP A CG  1 
ATOM   1054 O OD1 . ASP A 1 137 ? 61.200 -7.414  79.761 1.00 57.57  ? 137 ASP A OD1 1 
ATOM   1055 O OD2 . ASP A 1 137 ? 63.218 -8.118  79.260 1.00 65.75  ? 137 ASP A OD2 1 
ATOM   1056 N N   . TYR A 1 138 ? 60.772 -4.623  77.937 1.00 52.80  ? 138 TYR A N   1 
ATOM   1057 C CA  . TYR A 1 138 ? 60.462 -4.512  76.518 1.00 51.55  ? 138 TYR A CA  1 
ATOM   1058 C C   . TYR A 1 138 ? 60.155 -3.081  76.108 1.00 50.48  ? 138 TYR A C   1 
ATOM   1059 O O   . TYR A 1 138 ? 59.486 -2.388  76.856 1.00 50.64  ? 138 TYR A O   1 
ATOM   1060 C CB  . TYR A 1 138 ? 59.283 -5.422  76.151 1.00 49.90  ? 138 TYR A CB  1 
ATOM   1061 C CG  . TYR A 1 138 ? 59.594 -6.884  75.954 1.00 47.56  ? 138 TYR A CG  1 
ATOM   1062 C CD1 . TYR A 1 138 ? 60.732 -7.507  76.441 1.00 46.89  ? 138 TYR A CD1 1 
ATOM   1063 C CD2 . TYR A 1 138 ? 58.696 -7.667  75.235 1.00 46.66  ? 138 TYR A CD2 1 
ATOM   1064 C CE1 . TYR A 1 138 ? 60.978 -8.860  76.215 1.00 46.05  ? 138 TYR A CE1 1 
ATOM   1065 C CE2 . TYR A 1 138 ? 58.901 -9.011  75.004 1.00 45.52  ? 138 TYR A CE2 1 
ATOM   1066 C CZ  . TYR A 1 138 ? 60.045 -9.598  75.508 1.00 45.48  ? 138 TYR A CZ  1 
ATOM   1067 O OH  . TYR A 1 138 ? 60.244 -10.929 75.258 1.00 44.12  ? 138 TYR A OH  1 
ATOM   1068 N N   . ARG A 1 139 ? 60.497 -2.692  74.900 1.00 49.41  ? 139 ARG A N   1 
ATOM   1069 C CA  . ARG A 1 139 ? 60.195 -1.361  74.379 1.00 48.07  ? 139 ARG A CA  1 
ATOM   1070 C C   . ARG A 1 139 ? 58.763 -1.257  73.854 1.00 47.50  ? 139 ARG A C   1 
ATOM   1071 O O   . ARG A 1 139 ? 58.243 -2.174  73.200 1.00 48.49  ? 139 ARG A O   1 
ATOM   1072 C CB  . ARG A 1 139 ? 61.207 -1.034  73.312 1.00 45.77  ? 139 ARG A CB  1 
ATOM   1073 C CG  . ARG A 1 139 ? 61.275 0.338   72.710 1.00 46.45  ? 139 ARG A CG  1 
ATOM   1074 C CD  . ARG A 1 139 ? 61.583 0.232   71.203 1.00 46.21  ? 139 ARG A CD  1 
ATOM   1075 N NE  . ARG A 1 139 ? 61.910 1.496   70.599 1.00 44.62  ? 139 ARG A NE  1 
ATOM   1076 C CZ  . ARG A 1 139 ? 62.513 1.693   69.452 1.00 47.60  ? 139 ARG A CZ  1 
ATOM   1077 N NH1 . ARG A 1 139 ? 62.883 0.734   68.616 1.00 49.97  ? 139 ARG A NH1 1 
ATOM   1078 N NH2 . ARG A 1 139 ? 62.831 2.920   69.060 1.00 49.09  ? 139 ARG A NH2 1 
ATOM   1079 N N   . VAL A 1 140 ? 58.072 -0.199  74.249 1.00 45.40  ? 140 VAL A N   1 
ATOM   1080 C CA  . VAL A 1 140 ? 56.723 0.089   73.898 1.00 44.28  ? 140 VAL A CA  1 
ATOM   1081 C C   . VAL A 1 140 ? 56.706 1.062   72.721 1.00 44.33  ? 140 VAL A C   1 
ATOM   1082 O O   . VAL A 1 140 ? 57.244 2.168   72.738 1.00 43.90  ? 140 VAL A O   1 
ATOM   1083 C CB  . VAL A 1 140 ? 55.824 0.664   75.002 1.00 45.08  ? 140 VAL A CB  1 
ATOM   1084 C CG1 . VAL A 1 140 ? 54.424 1.025   74.496 1.00 40.19  ? 140 VAL A CG1 1 
ATOM   1085 C CG2 . VAL A 1 140 ? 55.714 -0.341  76.151 1.00 43.61  ? 140 VAL A CG2 1 
ATOM   1086 N N   . VAL A 1 141 ? 56.089 0.530   71.650 1.00 43.50  ? 141 VAL A N   1 
ATOM   1087 C CA  . VAL A 1 141 ? 56.109 1.195   70.356 1.00 41.66  ? 141 VAL A CA  1 
ATOM   1088 C C   . VAL A 1 141 ? 54.728 1.232   69.718 1.00 40.98  ? 141 VAL A C   1 
ATOM   1089 O O   . VAL A 1 141 ? 54.030 0.219   69.593 1.00 40.58  ? 141 VAL A O   1 
ATOM   1090 C CB  . VAL A 1 141 ? 57.059 0.397   69.446 1.00 40.71  ? 141 VAL A CB  1 
ATOM   1091 C CG1 . VAL A 1 141 ? 56.979 0.899   68.015 1.00 43.00  ? 141 VAL A CG1 1 
ATOM   1092 C CG2 . VAL A 1 141 ? 58.512 0.521   69.903 1.00 40.28  ? 141 VAL A CG2 1 
ATOM   1093 N N   . PHE A 1 142 ? 54.287 2.447   69.388 1.00 39.56  ? 142 PHE A N   1 
ATOM   1094 C CA  . PHE A 1 142 ? 53.048 2.606   68.649 1.00 38.47  ? 142 PHE A CA  1 
ATOM   1095 C C   . PHE A 1 142 ? 53.412 2.943   67.196 1.00 38.29  ? 142 PHE A C   1 
ATOM   1096 O O   . PHE A 1 142 ? 54.263 3.781   66.937 1.00 38.11  ? 142 PHE A O   1 
ATOM   1097 C CB  . PHE A 1 142 ? 52.182 3.692   69.230 1.00 39.45  ? 142 PHE A CB  1 
ATOM   1098 C CG  . PHE A 1 142 ? 51.615 3.524   70.603 1.00 39.18  ? 142 PHE A CG  1 
ATOM   1099 C CD1 . PHE A 1 142 ? 51.825 2.417   71.391 1.00 38.24  ? 142 PHE A CD1 1 
ATOM   1100 C CD2 . PHE A 1 142 ? 50.837 4.545   71.134 1.00 39.04  ? 142 PHE A CD2 1 
ATOM   1101 C CE1 . PHE A 1 142 ? 51.326 2.324   72.658 1.00 37.18  ? 142 PHE A CE1 1 
ATOM   1102 C CE2 . PHE A 1 142 ? 50.313 4.469   72.396 1.00 36.78  ? 142 PHE A CE2 1 
ATOM   1103 C CZ  . PHE A 1 142 ? 50.543 3.343   73.156 1.00 37.82  ? 142 PHE A CZ  1 
ATOM   1104 N N   . THR A 1 143 ? 52.630 2.472   66.251 1.00 37.50  ? 143 THR A N   1 
ATOM   1105 C CA  . THR A 1 143 ? 52.921 2.612   64.845 1.00 36.68  ? 143 THR A CA  1 
ATOM   1106 C C   . THR A 1 143 ? 51.650 2.486   64.005 1.00 36.37  ? 143 THR A C   1 
ATOM   1107 O O   . THR A 1 143 ? 50.604 2.018   64.401 1.00 35.36  ? 143 THR A O   1 
ATOM   1108 C CB  . THR A 1 143 ? 53.852 1.473   64.406 1.00 37.95  ? 143 THR A CB  1 
ATOM   1109 O OG1 . THR A 1 143 ? 54.297 1.804   63.066 1.00 40.20  ? 143 THR A OG1 1 
ATOM   1110 C CG2 . THR A 1 143 ? 53.127 0.129   64.335 1.00 36.34  ? 143 THR A CG2 1 
ATOM   1111 N N   . GLY A 1 144 ? 51.687 3.094   62.825 1.00 36.99  ? 144 GLY A N   1 
ATOM   1112 C CA  . GLY A 1 144 ? 50.595 2.983   61.864 1.00 36.67  ? 144 GLY A CA  1 
ATOM   1113 C C   . GLY A 1 144 ? 50.973 3.779   60.614 1.00 37.09  ? 144 GLY A C   1 
ATOM   1114 O O   . GLY A 1 144 ? 51.723 4.757   60.574 1.00 36.10  ? 144 GLY A O   1 
ATOM   1115 N N   . HIS A 1 145 ? 50.235 3.395   59.580 1.00 37.45  ? 145 HIS A N   1 
ATOM   1116 C CA  . HIS A 1 145 ? 50.354 4.044   58.266 1.00 36.47  ? 145 HIS A CA  1 
ATOM   1117 C C   . HIS A 1 145 ? 49.091 4.872   58.047 1.00 36.33  ? 145 HIS A C   1 
ATOM   1118 O O   . HIS A 1 145 ? 48.025 4.435   58.509 1.00 35.83  ? 145 HIS A O   1 
ATOM   1119 C CB  . HIS A 1 145 ? 50.384 2.879   57.258 1.00 35.33  ? 145 HIS A CB  1 
ATOM   1120 C CG  . HIS A 1 145 ? 50.102 3.299   55.855 1.00 32.28  ? 145 HIS A CG  1 
ATOM   1121 N ND1 . HIS A 1 145 ? 48.879 3.214   55.256 1.00 31.14  ? 145 HIS A ND1 1 
ATOM   1122 C CD2 . HIS A 1 145 ? 51.003 3.897   55.003 1.00 30.65  ? 145 HIS A CD2 1 
ATOM   1123 C CE1 . HIS A 1 145 ? 49.034 3.728   53.997 1.00 29.71  ? 145 HIS A CE1 1 
ATOM   1124 N NE2 . HIS A 1 145 ? 50.273 4.153   53.862 1.00 32.64  ? 145 HIS A NE2 1 
ATOM   1125 N N   . SER A 1 146 ? 49.218 6.026   57.415 1.00 35.93  ? 146 SER A N   1 
ATOM   1126 C CA  . SER A 1 146 ? 48.015 6.774   57.046 1.00 38.21  ? 146 SER A CA  1 
ATOM   1127 C C   . SER A 1 146 ? 47.176 7.261   58.222 1.00 38.40  ? 146 SER A C   1 
ATOM   1128 O O   . SER A 1 146 ? 47.709 7.488   59.296 1.00 39.13  ? 146 SER A O   1 
ATOM   1129 C CB  . SER A 1 146 ? 47.107 5.920   56.105 1.00 36.24  ? 146 SER A CB  1 
ATOM   1130 O OG  . SER A 1 146 ? 46.406 6.860   55.299 1.00 39.14  ? 146 SER A OG  1 
ATOM   1131 N N   . LEU A 1 147 ? 45.867 7.105   58.166 1.00 38.33  ? 147 LEU A N   1 
ATOM   1132 C CA  . LEU A 1 147 ? 44.967 7.320   59.276 1.00 39.15  ? 147 LEU A CA  1 
ATOM   1133 C C   . LEU A 1 147 ? 45.447 6.639   60.557 1.00 38.95  ? 147 LEU A C   1 
ATOM   1134 O O   . LEU A 1 147 ? 45.389 7.234   61.646 1.00 39.43  ? 147 LEU A O   1 
ATOM   1135 C CB  . LEU A 1 147 ? 43.556 6.836   58.908 1.00 38.63  ? 147 LEU A CB  1 
ATOM   1136 C CG  . LEU A 1 147 ? 42.584 6.727   60.089 1.00 40.86  ? 147 LEU A CG  1 
ATOM   1137 C CD1 . LEU A 1 147 ? 42.384 8.080   60.768 1.00 38.22  ? 147 LEU A CD1 1 
ATOM   1138 C CD2 . LEU A 1 147 ? 41.309 5.984   59.737 1.00 35.06  ? 147 LEU A CD2 1 
ATOM   1139 N N   . GLY A 1 148 ? 45.998 5.448   60.470 1.00 38.24  ? 148 GLY A N   1 
ATOM   1140 C CA  . GLY A 1 148 ? 46.619 4.753   61.585 1.00 38.44  ? 148 GLY A CA  1 
ATOM   1141 C C   . GLY A 1 148 ? 47.872 5.488   62.092 1.00 38.31  ? 148 GLY A C   1 
ATOM   1142 O O   . GLY A 1 148 ? 48.368 5.091   63.138 1.00 37.65  ? 148 GLY A O   1 
ATOM   1143 N N   . GLY A 1 149 ? 48.574 6.258   61.282 1.00 37.67  ? 149 GLY A N   1 
ATOM   1144 C CA  . GLY A 1 149 ? 49.713 7.038   61.719 1.00 39.00  ? 149 GLY A CA  1 
ATOM   1145 C C   . GLY A 1 149 ? 49.165 8.142   62.658 1.00 40.13  ? 149 GLY A C   1 
ATOM   1146 O O   . GLY A 1 149 ? 49.747 8.405   63.727 1.00 40.37  ? 149 GLY A O   1 
ATOM   1147 N N   . ALA A 1 150 ? 48.064 8.765   62.233 1.00 38.69  ? 150 ALA A N   1 
ATOM   1148 C CA  . ALA A 1 150 ? 47.358 9.713   63.062 1.00 39.11  ? 150 ALA A CA  1 
ATOM   1149 C C   . ALA A 1 150 ? 47.008 9.086   64.442 1.00 39.08  ? 150 ALA A C   1 
ATOM   1150 O O   . ALA A 1 150 ? 47.399 9.632   65.454 1.00 38.49  ? 150 ALA A O   1 
ATOM   1151 C CB  . ALA A 1 150 ? 46.050 10.147  62.410 1.00 32.88  ? 150 ALA A CB  1 
ATOM   1152 N N   . LEU A 1 151 ? 46.203 8.024   64.388 1.00 38.87  ? 151 LEU A N   1 
ATOM   1153 C CA  . LEU A 1 151 ? 45.758 7.434   65.605 1.00 40.11  ? 151 LEU A CA  1 
ATOM   1154 C C   . LEU A 1 151 ? 46.928 7.038   66.502 1.00 40.82  ? 151 LEU A C   1 
ATOM   1155 O O   . LEU A 1 151 ? 46.774 7.159   67.737 1.00 42.05  ? 151 LEU A O   1 
ATOM   1156 C CB  . LEU A 1 151 ? 44.795 6.277   65.519 1.00 39.14  ? 151 LEU A CB  1 
ATOM   1157 C CG  . LEU A 1 151 ? 43.474 6.394   64.710 1.00 40.41  ? 151 LEU A CG  1 
ATOM   1158 C CD1 . LEU A 1 151 ? 43.034 5.016   64.208 1.00 39.76  ? 151 LEU A CD1 1 
ATOM   1159 C CD2 . LEU A 1 151 ? 42.342 6.973   65.552 1.00 38.36  ? 151 LEU A CD2 1 
ATOM   1160 N N   . ALA A 1 152 ? 48.043 6.576   65.999 1.00 39.88  ? 152 ALA A N   1 
ATOM   1161 C CA  . ALA A 1 152 ? 49.153 6.120   66.770 1.00 39.03  ? 152 ALA A CA  1 
ATOM   1162 C C   . ALA A 1 152 ? 49.881 7.339   67.322 1.00 39.63  ? 152 ALA A C   1 
ATOM   1163 O O   . ALA A 1 152 ? 50.454 7.204   68.420 1.00 39.91  ? 152 ALA A O   1 
ATOM   1164 C CB  . ALA A 1 152 ? 50.141 5.266   66.042 1.00 34.49  ? 152 ALA A CB  1 
ATOM   1165 N N   . THR A 1 153 ? 49.923 8.391   66.519 1.00 39.40  ? 153 THR A N   1 
ATOM   1166 C CA  . THR A 1 153 ? 50.445 9.657   67.043 1.00 39.77  ? 153 THR A CA  1 
ATOM   1167 C C   . THR A 1 153 ? 49.544 10.232  68.138 1.00 40.29  ? 153 THR A C   1 
ATOM   1168 O O   . THR A 1 153 ? 50.110 10.623  69.165 1.00 40.21  ? 153 THR A O   1 
ATOM   1169 C CB  . THR A 1 153 ? 50.614 10.720  65.970 1.00 39.19  ? 153 THR A CB  1 
ATOM   1170 O OG1 . THR A 1 153 ? 51.330 10.145  64.850 1.00 41.61  ? 153 THR A OG1 1 
ATOM   1171 C CG2 . THR A 1 153 ? 51.264 11.971  66.499 1.00 36.48  ? 153 THR A CG2 1 
ATOM   1172 N N   . VAL A 1 154 ? 48.228 10.251  68.003 1.00 40.36  ? 154 VAL A N   1 
ATOM   1173 C CA  . VAL A 1 154 ? 47.357 10.763  69.051 1.00 41.85  ? 154 VAL A CA  1 
ATOM   1174 C C   . VAL A 1 154 ? 47.332 9.931   70.327 1.00 42.91  ? 154 VAL A C   1 
ATOM   1175 O O   . VAL A 1 154 ? 47.737 10.421  71.397 1.00 42.95  ? 154 VAL A O   1 
ATOM   1176 C CB  . VAL A 1 154 ? 45.965 11.093  68.514 1.00 41.67  ? 154 VAL A CB  1 
ATOM   1177 C CG1 . VAL A 1 154 ? 44.954 11.355  69.605 1.00 40.91  ? 154 VAL A CG1 1 
ATOM   1178 C CG2 . VAL A 1 154 ? 46.112 12.311  67.585 1.00 42.30  ? 154 VAL A CG2 1 
ATOM   1179 N N   . ALA A 1 155 ? 47.308 8.618   70.214 1.00 43.46  ? 155 ALA A N   1 
ATOM   1180 C CA  . ALA A 1 155 ? 47.491 7.699   71.318 1.00 44.53  ? 155 ALA A CA  1 
ATOM   1181 C C   . ALA A 1 155 ? 48.867 7.830   71.981 1.00 45.14  ? 155 ALA A C   1 
ATOM   1182 O O   . ALA A 1 155 ? 48.944 7.914   73.218 1.00 45.02  ? 155 ALA A O   1 
ATOM   1183 C CB  . ALA A 1 155 ? 47.227 6.278   70.864 1.00 41.74  ? 155 ALA A CB  1 
ATOM   1184 N N   . GLY A 1 156 ? 49.901 8.169   71.218 1.00 45.05  ? 156 GLY A N   1 
ATOM   1185 C CA  . GLY A 1 156 ? 51.224 8.300   71.812 1.00 45.72  ? 156 GLY A CA  1 
ATOM   1186 C C   . GLY A 1 156 ? 51.334 9.558   72.643 1.00 46.31  ? 156 GLY A C   1 
ATOM   1187 O O   . GLY A 1 156 ? 51.578 9.487   73.851 1.00 46.83  ? 156 GLY A O   1 
ATOM   1188 N N   . ALA A 1 157 ? 50.759 10.649  72.143 1.00 47.17  ? 157 ALA A N   1 
ATOM   1189 C CA  . ALA A 1 157 ? 50.773 11.922  72.853 1.00 47.26  ? 157 ALA A CA  1 
ATOM   1190 C C   . ALA A 1 157 ? 49.959 11.853  74.146 1.00 47.42  ? 157 ALA A C   1 
ATOM   1191 O O   . ALA A 1 157 ? 50.304 12.493  75.139 1.00 47.49  ? 157 ALA A O   1 
ATOM   1192 C CB  . ALA A 1 157 ? 50.288 13.058  71.990 1.00 44.90  ? 157 ALA A CB  1 
ATOM   1193 N N   . ASP A 1 158 ? 48.932 11.058  74.177 1.00 47.07  ? 158 ASP A N   1 
ATOM   1194 C CA  . ASP A 1 158 ? 48.051 10.908  75.299 1.00 48.02  ? 158 ASP A CA  1 
ATOM   1195 C C   . ASP A 1 158 ? 48.524 9.903   76.332 1.00 49.20  ? 158 ASP A C   1 
ATOM   1196 O O   . ASP A 1 158 ? 47.953 9.897   77.426 1.00 50.18  ? 158 ASP A O   1 
ATOM   1197 C CB  . ASP A 1 158 ? 46.733 10.343  74.708 1.00 48.02  ? 158 ASP A CB  1 
ATOM   1198 C CG  . ASP A 1 158 ? 45.564 10.433  75.660 1.00 47.23  ? 158 ASP A CG  1 
ATOM   1199 O OD1 . ASP A 1 158 ? 45.654 11.365  76.491 1.00 50.25  ? 158 ASP A OD1 1 
ATOM   1200 O OD2 . ASP A 1 158 ? 44.625 9.623   75.566 1.00 45.39  ? 158 ASP A OD2 1 
ATOM   1201 N N   . LEU A 1 159 ? 49.311 8.884   75.995 1.00 49.46  ? 159 LEU A N   1 
ATOM   1202 C CA  . LEU A 1 159 ? 49.586 7.843   76.969 1.00 49.37  ? 159 LEU A CA  1 
ATOM   1203 C C   . LEU A 1 159 ? 50.951 7.983   77.582 1.00 50.23  ? 159 LEU A C   1 
ATOM   1204 O O   . LEU A 1 159 ? 51.331 7.160   78.413 1.00 50.58  ? 159 LEU A O   1 
ATOM   1205 C CB  . LEU A 1 159 ? 49.342 6.470   76.365 1.00 48.25  ? 159 LEU A CB  1 
ATOM   1206 C CG  . LEU A 1 159 ? 47.924 6.000   76.107 1.00 48.59  ? 159 LEU A CG  1 
ATOM   1207 C CD1 . LEU A 1 159 ? 47.856 4.474   76.059 1.00 49.10  ? 159 LEU A CD1 1 
ATOM   1208 C CD2 . LEU A 1 159 ? 46.868 6.502   77.094 1.00 44.40  ? 159 LEU A CD2 1 
ATOM   1209 N N   . ARG A 1 160 ? 51.799 8.785   76.973 1.00 51.53  ? 160 ARG A N   1 
ATOM   1210 C CA  . ARG A 1 160 ? 53.150 9.021   77.484 1.00 53.41  ? 160 ARG A CA  1 
ATOM   1211 C C   . ARG A 1 160 ? 53.089 9.652   78.861 1.00 53.96  ? 160 ARG A C   1 
ATOM   1212 O O   . ARG A 1 160 ? 52.065 10.273  79.123 1.00 54.15  ? 160 ARG A O   1 
ATOM   1213 C CB  . ARG A 1 160 ? 53.882 9.923   76.477 1.00 56.68  ? 160 ARG A CB  1 
ATOM   1214 C CG  . ARG A 1 160 ? 54.322 9.153   75.225 1.00 58.37  ? 160 ARG A CG  1 
ATOM   1215 C CD  . ARG A 1 160 ? 54.738 10.072  74.113 1.00 56.57  ? 160 ARG A CD  1 
ATOM   1216 N NE  . ARG A 1 160 ? 55.700 9.525   73.150 1.00 55.17  ? 160 ARG A NE  1 
ATOM   1217 C CZ  . ARG A 1 160 ? 55.986 10.275  72.079 1.00 52.83  ? 160 ARG A CZ  1 
ATOM   1218 N NH1 . ARG A 1 160 ? 55.360 11.433  72.003 1.00 53.75  ? 160 ARG A NH1 1 
ATOM   1219 N NH2 . ARG A 1 160 ? 56.826 9.973   71.128 1.00 50.63  ? 160 ARG A NH2 1 
ATOM   1220 N N   . GLY A 1 161 ? 54.059 9.454   79.748 1.00 54.97  ? 161 GLY A N   1 
ATOM   1221 C CA  . GLY A 1 161 ? 54.063 10.034  81.056 1.00 54.58  ? 161 GLY A CA  1 
ATOM   1222 C C   . GLY A 1 161 ? 53.750 9.103   82.199 1.00 55.24  ? 161 GLY A C   1 
ATOM   1223 O O   . GLY A 1 161 ? 53.883 9.535   83.348 1.00 55.68  ? 161 GLY A O   1 
ATOM   1224 N N   . ASN A 1 162 ? 53.257 7.900   82.027 1.00 55.55  ? 162 ASN A N   1 
ATOM   1225 C CA  . ASN A 1 162 ? 52.752 6.997   83.048 1.00 55.90  ? 162 ASN A CA  1 
ATOM   1226 C C   . ASN A 1 162 ? 53.843 5.970   83.339 1.00 55.24  ? 162 ASN A C   1 
ATOM   1227 O O   . ASN A 1 162 ? 53.592 4.803   83.670 1.00 55.39  ? 162 ASN A O   1 
ATOM   1228 C CB  . ASN A 1 162 ? 51.320 6.469   82.800 1.00 60.93  ? 162 ASN A CB  1 
ATOM   1229 C CG  . ASN A 1 162 ? 50.496 7.362   81.876 1.00 67.28  ? 162 ASN A CG  1 
ATOM   1230 O OD1 . ASN A 1 162 ? 49.673 6.971   80.992 1.00 71.53  ? 162 ASN A OD1 1 
ATOM   1231 N ND2 . ASN A 1 162 ? 50.590 8.709   81.890 1.00 67.62  ? 162 ASN A ND2 1 
ATOM   1232 N N   . GLY A 1 163 ? 55.100 6.427   83.241 1.00 53.96  ? 163 GLY A N   1 
ATOM   1233 C CA  . GLY A 1 163 ? 56.229 5.592   83.553 1.00 53.45  ? 163 GLY A CA  1 
ATOM   1234 C C   . GLY A 1 163 ? 56.702 4.734   82.391 1.00 53.47  ? 163 GLY A C   1 
ATOM   1235 O O   . GLY A 1 163 ? 57.627 3.912   82.597 1.00 54.21  ? 163 GLY A O   1 
ATOM   1236 N N   . TYR A 1 164 ? 56.128 4.768   81.181 1.00 51.80  ? 164 TYR A N   1 
ATOM   1237 C CA  . TYR A 1 164 ? 56.810 3.920   80.181 1.00 50.55  ? 164 TYR A CA  1 
ATOM   1238 C C   . TYR A 1 164 ? 56.973 4.703   78.900 1.00 49.18  ? 164 TYR A C   1 
ATOM   1239 O O   . TYR A 1 164 ? 56.051 5.450   78.590 1.00 49.71  ? 164 TYR A O   1 
ATOM   1240 C CB  . TYR A 1 164 ? 56.160 2.562   80.077 1.00 50.20  ? 164 TYR A CB  1 
ATOM   1241 C CG  . TYR A 1 164 ? 54.697 2.668   79.723 1.00 49.60  ? 164 TYR A CG  1 
ATOM   1242 C CD1 . TYR A 1 164 ? 53.740 2.666   80.715 1.00 47.90  ? 164 TYR A CD1 1 
ATOM   1243 C CD2 . TYR A 1 164 ? 54.306 2.802   78.392 1.00 49.31  ? 164 TYR A CD2 1 
ATOM   1244 C CE1 . TYR A 1 164 ? 52.400 2.732   80.428 1.00 47.95  ? 164 TYR A CE1 1 
ATOM   1245 C CE2 . TYR A 1 164 ? 52.953 2.899   78.096 1.00 49.36  ? 164 TYR A CE2 1 
ATOM   1246 C CZ  . TYR A 1 164 ? 52.027 2.871   79.111 1.00 49.42  ? 164 TYR A CZ  1 
ATOM   1247 O OH  . TYR A 1 164 ? 50.697 2.984   78.777 1.00 51.38  ? 164 TYR A OH  1 
ATOM   1248 N N   . ASP A 1 165 ? 58.183 4.739   78.384 1.00 47.84  ? 165 ASP A N   1 
ATOM   1249 C CA  . ASP A 1 165 ? 58.474 5.523   77.182 1.00 46.27  ? 165 ASP A CA  1 
ATOM   1250 C C   . ASP A 1 165 ? 57.649 4.977   76.031 1.00 45.03  ? 165 ASP A C   1 
ATOM   1251 O O   . ASP A 1 165 ? 57.409 3.766   76.008 1.00 44.41  ? 165 ASP A O   1 
ATOM   1252 C CB  . ASP A 1 165 ? 59.951 5.411   76.791 1.00 47.57  ? 165 ASP A CB  1 
ATOM   1253 C CG  . ASP A 1 165 ? 60.853 6.358   77.537 1.00 51.05  ? 165 ASP A CG  1 
ATOM   1254 O OD1 . ASP A 1 165 ? 60.330 7.176   78.331 1.00 52.02  ? 165 ASP A OD1 1 
ATOM   1255 O OD2 . ASP A 1 165 ? 62.086 6.308   77.325 1.00 53.59  ? 165 ASP A OD2 1 
ATOM   1256 N N   . ILE A 1 166 ? 57.048 5.878   75.257 1.00 44.30  ? 166 ILE A N   1 
ATOM   1257 C CA  . ILE A 1 166 ? 56.350 5.439   74.042 1.00 44.06  ? 166 ILE A CA  1 
ATOM   1258 C C   . ILE A 1 166 ? 56.968 5.957   72.756 1.00 44.37  ? 166 ILE A C   1 
ATOM   1259 O O   . ILE A 1 166 ? 57.099 7.164   72.479 1.00 44.92  ? 166 ILE A O   1 
ATOM   1260 C CB  . ILE A 1 166 ? 54.856 5.790   74.056 1.00 43.24  ? 166 ILE A CB  1 
ATOM   1261 C CG1 . ILE A 1 166 ? 54.240 5.334   75.403 1.00 42.19  ? 166 ILE A CG1 1 
ATOM   1262 C CG2 . ILE A 1 166 ? 54.139 5.196   72.861 1.00 39.19  ? 166 ILE A CG2 1 
ATOM   1263 C CD1 . ILE A 1 166 ? 52.809 5.711   75.640 1.00 40.33  ? 166 ILE A CD1 1 
ATOM   1264 N N   . ASP A 1 167 ? 57.522 5.017   71.990 1.00 44.35  ? 167 ASP A N   1 
ATOM   1265 C CA  . ASP A 1 167 ? 58.048 5.383   70.657 1.00 43.38  ? 167 ASP A CA  1 
ATOM   1266 C C   . ASP A 1 167 ? 56.923 5.309   69.635 1.00 42.54  ? 167 ASP A C   1 
ATOM   1267 O O   . ASP A 1 167 ? 56.041 4.452   69.782 1.00 43.38  ? 167 ASP A O   1 
ATOM   1268 C CB  . ASP A 1 167 ? 59.231 4.508   70.276 1.00 43.79  ? 167 ASP A CB  1 
ATOM   1269 C CG  . ASP A 1 167 ? 60.526 4.969   70.923 1.00 46.90  ? 167 ASP A CG  1 
ATOM   1270 O OD1 . ASP A 1 167 ? 60.515 6.127   71.383 1.00 45.82  ? 167 ASP A OD1 1 
ATOM   1271 O OD2 . ASP A 1 167 ? 61.534 4.215   70.991 1.00 48.62  ? 167 ASP A OD2 1 
ATOM   1272 N N   . VAL A 1 168 ? 56.739 6.328   68.822 1.00 41.78  ? 168 VAL A N   1 
ATOM   1273 C CA  . VAL A 1 168 ? 55.765 6.350   67.743 1.00 40.69  ? 168 VAL A CA  1 
ATOM   1274 C C   . VAL A 1 168 ? 56.506 6.333   66.399 1.00 39.34  ? 168 VAL A C   1 
ATOM   1275 O O   . VAL A 1 168 ? 57.340 7.244   66.231 1.00 39.95  ? 168 VAL A O   1 
ATOM   1276 C CB  . VAL A 1 168 ? 54.864 7.594   67.681 1.00 40.42  ? 168 VAL A CB  1 
ATOM   1277 C CG1 . VAL A 1 168 ? 53.869 7.423   66.539 1.00 40.66  ? 168 VAL A CG1 1 
ATOM   1278 C CG2 . VAL A 1 168 ? 54.114 7.802   68.989 1.00 42.16  ? 168 VAL A CG2 1 
ATOM   1279 N N   . PHE A 1 169 ? 56.041 5.504   65.489 1.00 37.64  ? 169 PHE A N   1 
ATOM   1280 C CA  . PHE A 1 169 ? 56.543 5.450   64.129 1.00 36.37  ? 169 PHE A CA  1 
ATOM   1281 C C   . PHE A 1 169 ? 55.311 5.526   63.225 1.00 36.73  ? 169 PHE A C   1 
ATOM   1282 O O   . PHE A 1 169 ? 54.430 4.662   63.363 1.00 37.63  ? 169 PHE A O   1 
ATOM   1283 C CB  . PHE A 1 169 ? 57.276 4.152   63.821 1.00 33.50  ? 169 PHE A CB  1 
ATOM   1284 C CG  . PHE A 1 169 ? 58.635 3.971   64.424 1.00 29.46  ? 169 PHE A CG  1 
ATOM   1285 C CD1 . PHE A 1 169 ? 58.684 3.645   65.764 1.00 25.88  ? 169 PHE A CD1 1 
ATOM   1286 C CD2 . PHE A 1 169 ? 59.821 4.075   63.742 1.00 31.10  ? 169 PHE A CD2 1 
ATOM   1287 C CE1 . PHE A 1 169 ? 59.875 3.473   66.421 1.00 26.62  ? 169 PHE A CE1 1 
ATOM   1288 C CE2 . PHE A 1 169 ? 61.048 3.874   64.405 1.00 32.46  ? 169 PHE A CE2 1 
ATOM   1289 C CZ  . PHE A 1 169 ? 61.061 3.556   65.771 1.00 28.13  ? 169 PHE A CZ  1 
ATOM   1290 N N   . SER A 1 170 ? 55.182 6.638   62.513 1.00 35.49  ? 170 SER A N   1 
ATOM   1291 C CA  . SER A 1 170 ? 53.980 6.797   61.712 1.00 35.09  ? 170 SER A CA  1 
ATOM   1292 C C   . SER A 1 170 ? 54.330 6.951   60.235 1.00 34.17  ? 170 SER A C   1 
ATOM   1293 O O   . SER A 1 170 ? 55.493 7.308   59.972 1.00 34.96  ? 170 SER A O   1 
ATOM   1294 C CB  . SER A 1 170 ? 53.225 8.035   62.221 1.00 34.17  ? 170 SER A CB  1 
ATOM   1295 O OG  . SER A 1 170 ? 54.135 9.095   61.849 1.00 38.66  ? 170 SER A OG  1 
ATOM   1296 N N   . TYR A 1 171 ? 53.601 6.268   59.346 1.00 32.13  ? 171 TYR A N   1 
ATOM   1297 C CA  . TYR A 1 171 ? 53.983 6.272   57.938 1.00 31.29  ? 171 TYR A CA  1 
ATOM   1298 C C   . TYR A 1 171 ? 52.903 7.004   57.170 1.00 31.03  ? 171 TYR A C   1 
ATOM   1299 O O   . TYR A 1 171 ? 51.716 6.682   57.305 1.00 31.23  ? 171 TYR A O   1 
ATOM   1300 C CB  . TYR A 1 171 ? 54.260 4.838   57.419 1.00 30.85  ? 171 TYR A CB  1 
ATOM   1301 C CG  . TYR A 1 171 ? 55.396 4.236   58.211 1.00 30.25  ? 171 TYR A CG  1 
ATOM   1302 C CD1 . TYR A 1 171 ? 55.155 3.711   59.484 1.00 30.77  ? 171 TYR A CD1 1 
ATOM   1303 C CD2 . TYR A 1 171 ? 56.695 4.234   57.704 1.00 30.34  ? 171 TYR A CD2 1 
ATOM   1304 C CE1 . TYR A 1 171 ? 56.200 3.222   60.249 1.00 31.08  ? 171 TYR A CE1 1 
ATOM   1305 C CE2 . TYR A 1 171 ? 57.748 3.742   58.464 1.00 30.81  ? 171 TYR A CE2 1 
ATOM   1306 C CZ  . TYR A 1 171 ? 57.474 3.235   59.718 1.00 31.47  ? 171 TYR A CZ  1 
ATOM   1307 O OH  . TYR A 1 171 ? 58.482 2.692   60.461 1.00 32.91  ? 171 TYR A OH  1 
ATOM   1308 N N   . GLY A 1 172 ? 53.270 8.000   56.377 1.00 30.95  ? 172 GLY A N   1 
ATOM   1309 C CA  . GLY A 1 172 ? 52.368 8.880   55.670 1.00 31.40  ? 172 GLY A CA  1 
ATOM   1310 C C   . GLY A 1 172 ? 51.135 9.324   56.422 1.00 31.95  ? 172 GLY A C   1 
ATOM   1311 O O   . GLY A 1 172 ? 50.044 9.308   55.839 1.00 31.21  ? 172 GLY A O   1 
ATOM   1312 N N   . ALA A 1 173 ? 51.337 9.736   57.682 1.00 32.72  ? 173 ALA A N   1 
ATOM   1313 C CA  . ALA A 1 173 ? 50.193 10.208  58.460 1.00 33.98  ? 173 ALA A CA  1 
ATOM   1314 C C   . ALA A 1 173 ? 49.885 11.658  58.076 1.00 34.94  ? 173 ALA A C   1 
ATOM   1315 O O   . ALA A 1 173 ? 50.782 12.408  57.692 1.00 34.55  ? 173 ALA A O   1 
ATOM   1316 C CB  . ALA A 1 173 ? 50.542 10.110  59.929 1.00 32.86  ? 173 ALA A CB  1 
ATOM   1317 N N   . PRO A 1 174 ? 48.631 12.036  58.211 1.00 36.20  ? 174 PRO A N   1 
ATOM   1318 C CA  . PRO A 1 174 ? 48.167 13.397  58.003 1.00 37.42  ? 174 PRO A CA  1 
ATOM   1319 C C   . PRO A 1 174 ? 48.507 14.246  59.221 1.00 38.62  ? 174 PRO A C   1 
ATOM   1320 O O   . PRO A 1 174 ? 48.993 13.754  60.248 1.00 39.41  ? 174 PRO A O   1 
ATOM   1321 C CB  . PRO A 1 174 ? 46.642 13.278  57.908 1.00 36.96  ? 174 PRO A CB  1 
ATOM   1322 C CG  . PRO A 1 174 ? 46.282 12.002  58.545 1.00 36.95  ? 174 PRO A CG  1 
ATOM   1323 C CD  . PRO A 1 174 ? 47.536 11.196  58.757 1.00 36.71  ? 174 PRO A CD  1 
ATOM   1324 N N   . ARG A 1 175 ? 48.413 15.559  59.059 1.00 39.57  ? 175 ARG A N   1 
ATOM   1325 C CA  . ARG A 1 175 ? 48.594 16.483  60.185 1.00 38.81  ? 175 ARG A CA  1 
ATOM   1326 C C   . ARG A 1 175 ? 47.544 16.075  61.215 1.00 39.24  ? 175 ARG A C   1 
ATOM   1327 O O   . ARG A 1 175 ? 46.482 15.523  60.853 1.00 38.46  ? 175 ARG A O   1 
ATOM   1328 C CB  . ARG A 1 175 ? 48.433 17.953  59.773 1.00 35.13  ? 175 ARG A CB  1 
ATOM   1329 C CG  . ARG A 1 175 ? 49.610 18.395  58.902 1.00 35.25  ? 175 ARG A CG  1 
ATOM   1330 C CD  . ARG A 1 175 ? 49.565 19.856  58.496 1.00 35.37  ? 175 ARG A CD  1 
ATOM   1331 N NE  . ARG A 1 175 ? 50.530 20.120  57.456 1.00 36.70  ? 175 ARG A NE  1 
ATOM   1332 C CZ  . ARG A 1 175 ? 50.313 20.229  56.135 1.00 34.91  ? 175 ARG A CZ  1 
ATOM   1333 N NH1 . ARG A 1 175 ? 51.411 20.371  55.366 1.00 33.53  ? 175 ARG A NH1 1 
ATOM   1334 N NH2 . ARG A 1 175 ? 49.057 20.085  55.708 1.00 30.72  ? 175 ARG A NH2 1 
ATOM   1335 N N   . VAL A 1 176 ? 47.783 16.465  62.466 1.00 39.70  ? 176 VAL A N   1 
ATOM   1336 C CA  . VAL A 1 176 ? 46.860 15.913  63.492 1.00 40.72  ? 176 VAL A CA  1 
ATOM   1337 C C   . VAL A 1 176 ? 46.236 17.006  64.341 1.00 42.35  ? 176 VAL A C   1 
ATOM   1338 O O   . VAL A 1 176 ? 45.273 16.733  65.106 1.00 41.64  ? 176 VAL A O   1 
ATOM   1339 C CB  . VAL A 1 176 ? 47.700 14.785  64.096 0.50 36.39  ? 176 VAL A CB  1 
ATOM   1340 C CG1 . VAL A 1 176 ? 48.215 15.101  65.468 0.50 29.95  ? 176 VAL A CG1 1 
ATOM   1341 C CG2 . VAL A 1 176 ? 47.032 13.440  63.864 0.50 32.52  ? 176 VAL A CG2 1 
ATOM   1342 N N   . GLY A 1 177 ? 46.784 18.233  64.143 1.00 42.36  ? 177 GLY A N   1 
ATOM   1343 C CA  . GLY A 1 177 ? 46.217 19.333  64.911 1.00 43.88  ? 177 GLY A CA  1 
ATOM   1344 C C   . GLY A 1 177 ? 47.057 20.596  64.791 1.00 44.59  ? 177 GLY A C   1 
ATOM   1345 O O   . GLY A 1 177 ? 47.534 20.865  63.684 1.00 44.98  ? 177 GLY A O   1 
ATOM   1346 N N   . ASN A 1 178 ? 46.970 21.464  65.794 1.00 45.54  ? 178 ASN A N   1 
ATOM   1347 C CA  . ASN A 1 178 ? 47.481 22.816  65.660 1.00 46.68  ? 178 ASN A CA  1 
ATOM   1348 C C   . ASN A 1 178 ? 48.938 22.884  66.047 1.00 47.13  ? 178 ASN A C   1 
ATOM   1349 O O   . ASN A 1 178 ? 49.503 21.847  66.358 1.00 47.36  ? 178 ASN A O   1 
ATOM   1350 C CB  . ASN A 1 178 ? 46.686 23.892  66.339 1.00 46.92  ? 178 ASN A CB  1 
ATOM   1351 C CG  . ASN A 1 178 ? 46.530 23.739  67.825 1.00 49.08  ? 178 ASN A CG  1 
ATOM   1352 O OD1 . ASN A 1 178 ? 47.281 23.052  68.513 1.00 48.90  ? 178 ASN A OD1 1 
ATOM   1353 N ND2 . ASN A 1 178 ? 45.500 24.437  68.269 1.00 51.16  ? 178 ASN A ND2 1 
ATOM   1354 N N   . ARG A 1 179 ? 49.415 24.107  65.927 1.00 47.66  ? 179 ARG A N   1 
ATOM   1355 C CA  . ARG A 1 179 ? 50.791 24.506  66.180 1.00 49.07  ? 179 ARG A CA  1 
ATOM   1356 C C   . ARG A 1 179 ? 51.130 24.074  67.570 1.00 49.79  ? 179 ARG A C   1 
ATOM   1357 O O   . ARG A 1 179 ? 52.121 23.386  67.757 1.00 51.55  ? 179 ARG A O   1 
ATOM   1358 C CB  . ARG A 1 179 ? 51.024 26.016  66.096 1.00 53.20  ? 179 ARG A CB  1 
ATOM   1359 C CG  . ARG A 1 179 ? 52.386 26.530  66.436 1.00 55.29  ? 179 ARG A CG  1 
ATOM   1360 C CD  . ARG A 1 179 ? 53.371 26.213  65.350 1.00 58.68  ? 179 ARG A CD  1 
ATOM   1361 N NE  . ARG A 1 179 ? 54.710 26.712  65.721 1.00 62.87  ? 179 ARG A NE  1 
ATOM   1362 C CZ  . ARG A 1 179 ? 55.532 27.263  64.811 1.00 65.97  ? 179 ARG A CZ  1 
ATOM   1363 N NH1 . ARG A 1 179 ? 55.148 27.417  63.535 1.00 64.73  ? 179 ARG A NH1 1 
ATOM   1364 N NH2 . ARG A 1 179 ? 56.774 27.652  65.151 1.00 66.71  ? 179 ARG A NH2 1 
ATOM   1365 N N   . ALA A 1 180 ? 50.253 24.452  68.504 1.00 49.47  ? 180 ALA A N   1 
ATOM   1366 C CA  . ALA A 1 180 ? 50.543 24.015  69.873 1.00 48.70  ? 180 ALA A CA  1 
ATOM   1367 C C   . ALA A 1 180 ? 50.625 22.496  69.866 1.00 47.67  ? 180 ALA A C   1 
ATOM   1368 O O   . ALA A 1 180 ? 51.599 21.971  70.412 1.00 48.07  ? 180 ALA A O   1 
ATOM   1369 C CB  . ALA A 1 180 ? 49.541 24.580  70.865 1.00 47.71  ? 180 ALA A CB  1 
ATOM   1370 N N   . PHE A 1 181 ? 49.717 21.758  69.233 1.00 46.32  ? 181 PHE A N   1 
ATOM   1371 C CA  . PHE A 1 181 ? 49.828 20.307  69.256 1.00 45.71  ? 181 PHE A CA  1 
ATOM   1372 C C   . PHE A 1 181 ? 51.114 19.800  68.613 1.00 46.24  ? 181 PHE A C   1 
ATOM   1373 O O   . PHE A 1 181 ? 51.776 18.875  69.112 1.00 46.09  ? 181 PHE A O   1 
ATOM   1374 C CB  . PHE A 1 181 ? 48.623 19.623  68.644 1.00 45.88  ? 181 PHE A CB  1 
ATOM   1375 C CG  . PHE A 1 181 ? 48.497 18.179  69.035 1.00 46.62  ? 181 PHE A CG  1 
ATOM   1376 C CD1 . PHE A 1 181 ? 49.059 17.685  70.205 1.00 44.03  ? 181 PHE A CD1 1 
ATOM   1377 C CD2 . PHE A 1 181 ? 47.740 17.338  68.239 1.00 44.43  ? 181 PHE A CD2 1 
ATOM   1378 C CE1 . PHE A 1 181 ? 48.907 16.357  70.538 1.00 45.12  ? 181 PHE A CE1 1 
ATOM   1379 C CE2 . PHE A 1 181 ? 47.589 16.011  68.611 1.00 45.43  ? 181 PHE A CE2 1 
ATOM   1380 C CZ  . PHE A 1 181 ? 48.175 15.491  69.729 1.00 43.63  ? 181 PHE A CZ  1 
ATOM   1381 N N   . ALA A 1 182 ? 51.539 20.492  67.573 1.00 45.51  ? 182 ALA A N   1 
ATOM   1382 C CA  . ALA A 1 182 ? 52.787 20.297  66.901 1.00 46.21  ? 182 ALA A CA  1 
ATOM   1383 C C   . ALA A 1 182 ? 53.966 20.501  67.830 1.00 47.42  ? 182 ALA A C   1 
ATOM   1384 O O   . ALA A 1 182 ? 54.980 19.789  67.815 1.00 47.64  ? 182 ALA A O   1 
ATOM   1385 C CB  . ALA A 1 182 ? 52.838 21.293  65.730 1.00 46.60  ? 182 ALA A CB  1 
ATOM   1386 N N   . GLU A 1 183 ? 53.857 21.549  68.670 1.00 47.65  ? 183 GLU A N   1 
ATOM   1387 C CA  . GLU A 1 183 ? 54.970 21.866  69.565 1.00 47.58  ? 183 GLU A CA  1 
ATOM   1388 C C   . GLU A 1 183 ? 55.060 20.823  70.645 1.00 46.53  ? 183 GLU A C   1 
ATOM   1389 O O   . GLU A 1 183 ? 56.112 20.230  70.906 1.00 46.49  ? 183 GLU A O   1 
ATOM   1390 C CB  . GLU A 1 183 ? 54.859 23.310  70.031 1.00 53.85  ? 183 GLU A CB  1 
ATOM   1391 C CG  . GLU A 1 183 ? 55.258 24.215  68.865 1.00 59.62  ? 183 GLU A CG  1 
ATOM   1392 C CD  . GLU A 1 183 ? 54.815 25.645  69.039 1.00 63.73  ? 183 GLU A CD  1 
ATOM   1393 O OE1 . GLU A 1 183 ? 54.155 25.938  70.063 1.00 65.97  ? 183 GLU A OE1 1 
ATOM   1394 O OE2 . GLU A 1 183 ? 55.172 26.425  68.120 1.00 66.19  ? 183 GLU A OE2 1 
ATOM   1395 N N   . PHE A 1 184 ? 53.888 20.398  71.082 1.00 46.09  ? 184 PHE A N   1 
ATOM   1396 C CA  . PHE A 1 184 ? 53.867 19.366  72.119 1.00 47.67  ? 184 PHE A CA  1 
ATOM   1397 C C   . PHE A 1 184 ? 54.548 18.128  71.559 1.00 48.67  ? 184 PHE A C   1 
ATOM   1398 O O   . PHE A 1 184 ? 55.586 17.699  72.043 1.00 49.28  ? 184 PHE A O   1 
ATOM   1399 C CB  . PHE A 1 184 ? 52.471 19.119  72.648 1.00 43.45  ? 184 PHE A CB  1 
ATOM   1400 C CG  . PHE A 1 184 ? 52.405 18.082  73.721 1.00 43.08  ? 184 PHE A CG  1 
ATOM   1401 C CD1 . PHE A 1 184 ? 52.770 18.417  75.034 1.00 44.27  ? 184 PHE A CD1 1 
ATOM   1402 C CD2 . PHE A 1 184 ? 51.828 16.844  73.481 1.00 38.87  ? 184 PHE A CD2 1 
ATOM   1403 C CE1 . PHE A 1 184 ? 52.619 17.478  76.057 1.00 41.91  ? 184 PHE A CE1 1 
ATOM   1404 C CE2 . PHE A 1 184 ? 51.667 15.926  74.498 1.00 40.09  ? 184 PHE A CE2 1 
ATOM   1405 C CZ  . PHE A 1 184 ? 52.099 16.214  75.790 1.00 40.60  ? 184 PHE A CZ  1 
ATOM   1406 N N   . LEU A 1 185 ? 54.067 17.603  70.430 1.00 49.59  ? 185 LEU A N   1 
ATOM   1407 C CA  . LEU A 1 185 ? 54.656 16.446  69.794 1.00 48.85  ? 185 LEU A CA  1 
ATOM   1408 C C   . LEU A 1 185 ? 56.103 16.676  69.399 1.00 48.66  ? 185 LEU A C   1 
ATOM   1409 O O   . LEU A 1 185 ? 56.857 15.697  69.318 1.00 48.36  ? 185 LEU A O   1 
ATOM   1410 C CB  . LEU A 1 185 ? 53.780 16.048  68.605 1.00 50.28  ? 185 LEU A CB  1 
ATOM   1411 C CG  . LEU A 1 185 ? 52.467 15.357  69.005 1.00 52.46  ? 185 LEU A CG  1 
ATOM   1412 C CD1 . LEU A 1 185 ? 51.626 15.170  67.748 1.00 50.87  ? 185 LEU A CD1 1 
ATOM   1413 C CD2 . LEU A 1 185 ? 52.720 14.039  69.722 1.00 51.47  ? 185 LEU A CD2 1 
ATOM   1414 N N   . THR A 1 186 ? 56.565 17.892  69.125 1.00 48.58  ? 186 THR A N   1 
ATOM   1415 C CA  . THR A 1 186 ? 57.994 18.020  68.869 1.00 49.28  ? 186 THR A CA  1 
ATOM   1416 C C   . THR A 1 186 ? 58.786 17.796  70.160 1.00 51.26  ? 186 THR A C   1 
ATOM   1417 O O   . THR A 1 186 ? 59.868 17.203  70.083 1.00 51.60  ? 186 THR A O   1 
ATOM   1418 C CB  . THR A 1 186 ? 58.405 19.366  68.275 1.00 43.36  ? 186 THR A CB  1 
ATOM   1419 O OG1 . THR A 1 186 ? 57.825 19.602  67.000 1.00 43.78  ? 186 THR A OG1 1 
ATOM   1420 C CG2 . THR A 1 186 ? 59.906 19.446  68.125 1.00 38.27  ? 186 THR A CG2 1 
ATOM   1421 N N   . VAL A 1 187 ? 58.346 18.324  71.308 1.00 52.27  ? 187 VAL A N   1 
ATOM   1422 C CA  . VAL A 1 187 ? 59.140 18.269  72.534 1.00 53.16  ? 187 VAL A CA  1 
ATOM   1423 C C   . VAL A 1 187 ? 58.644 17.328  73.607 1.00 53.88  ? 187 VAL A C   1 
ATOM   1424 O O   . VAL A 1 187 ? 59.102 17.317  74.747 1.00 53.99  ? 187 VAL A O   1 
ATOM   1425 C CB  . VAL A 1 187 ? 59.283 19.681  73.178 1.00 52.41  ? 187 VAL A CB  1 
ATOM   1426 C CG1 . VAL A 1 187 ? 59.828 20.716  72.205 1.00 51.74  ? 187 VAL A CG1 1 
ATOM   1427 C CG2 . VAL A 1 187 ? 57.937 20.168  73.709 1.00 50.82  ? 187 VAL A CG2 1 
ATOM   1428 N N   . GLN A 1 188 ? 57.554 16.616  73.377 1.00 54.85  ? 188 GLN A N   1 
ATOM   1429 C CA  . GLN A 1 188 ? 57.016 15.787  74.454 1.00 55.80  ? 188 GLN A CA  1 
ATOM   1430 C C   . GLN A 1 188 ? 57.974 14.665  74.844 1.00 56.22  ? 188 GLN A C   1 
ATOM   1431 O O   . GLN A 1 188 ? 58.061 13.616  74.186 1.00 56.62  ? 188 GLN A O   1 
ATOM   1432 C CB  . GLN A 1 188 ? 55.620 15.303  74.084 1.00 53.80  ? 188 GLN A CB  1 
ATOM   1433 C CG  . GLN A 1 188 ? 55.206 14.164  75.015 1.00 53.71  ? 188 GLN A CG  1 
ATOM   1434 C CD  . GLN A 1 188 ? 54.042 13.465  74.340 1.00 58.94  ? 188 GLN A CD  1 
ATOM   1435 O OE1 . GLN A 1 188 ? 54.130 13.138  73.157 1.00 53.23  ? 188 GLN A OE1 1 
ATOM   1436 N NE2 . GLN A 1 188 ? 52.994 13.308  75.163 1.00 60.99  ? 188 GLN A NE2 1 
ATOM   1437 N N   . THR A 1 189 ? 58.530 14.770  76.044 1.00 56.00  ? 189 THR A N   1 
ATOM   1438 C CA  . THR A 1 189 ? 59.450 13.712  76.500 1.00 56.18  ? 189 THR A CA  1 
ATOM   1439 C C   . THR A 1 189 ? 58.809 12.361  76.768 1.00 55.13  ? 189 THR A C   1 
ATOM   1440 O O   . THR A 1 189 ? 57.609 12.274  76.999 1.00 55.35  ? 189 THR A O   1 
ATOM   1441 C CB  . THR A 1 189 ? 60.100 14.218  77.818 1.00 57.34  ? 189 THR A CB  1 
ATOM   1442 O OG1 . THR A 1 189 ? 59.042 14.836  78.570 1.00 55.94  ? 189 THR A OG1 1 
ATOM   1443 C CG2 . THR A 1 189 ? 61.253 15.136  77.448 1.00 55.37  ? 189 THR A CG2 1 
ATOM   1444 N N   . GLY A 1 190 ? 59.616 11.332  77.022 1.00 54.44  ? 190 GLY A N   1 
ATOM   1445 C CA  . GLY A 1 190 ? 59.071 10.015  77.334 1.00 53.57  ? 190 GLY A CA  1 
ATOM   1446 C C   . GLY A 1 190 ? 58.807 9.219   76.055 1.00 53.10  ? 190 GLY A C   1 
ATOM   1447 O O   . GLY A 1 190 ? 57.961 8.321   76.061 1.00 53.12  ? 190 GLY A O   1 
ATOM   1448 N N   . GLY A 1 191 ? 59.612 9.475   75.020 1.00 51.72  ? 191 GLY A N   1 
ATOM   1449 C CA  . GLY A 1 191 ? 59.463 8.740   73.777 1.00 50.45  ? 191 GLY A CA  1 
ATOM   1450 C C   . GLY A 1 191 ? 59.802 9.612   72.585 1.00 49.42  ? 191 GLY A C   1 
ATOM   1451 O O   . GLY A 1 191 ? 59.842 10.835  72.696 1.00 50.61  ? 191 GLY A O   1 
ATOM   1452 N N   . THR A 1 192 ? 60.119 9.000   71.443 1.00 47.57  ? 192 THR A N   1 
ATOM   1453 C CA  . THR A 1 192 ? 60.456 9.755   70.250 1.00 44.08  ? 192 THR A CA  1 
ATOM   1454 C C   . THR A 1 192 ? 59.474 9.425   69.135 1.00 42.77  ? 192 THR A C   1 
ATOM   1455 O O   . THR A 1 192 ? 58.929 8.334   69.118 1.00 41.34  ? 192 THR A O   1 
ATOM   1456 C CB  . THR A 1 192 ? 61.887 9.479   69.849 1.00 43.19  ? 192 THR A CB  1 
ATOM   1457 O OG1 . THR A 1 192 ? 62.822 10.012  70.820 1.00 47.13  ? 192 THR A OG1 1 
ATOM   1458 C CG2 . THR A 1 192 ? 62.197 10.035  68.484 1.00 38.84  ? 192 THR A CG2 1 
ATOM   1459 N N   . LEU A 1 193 ? 58.923 10.477  68.501 1.00 41.51  ? 193 LEU A N   1 
ATOM   1460 C CA  . LEU A 1 193 ? 58.044 10.275  67.373 1.00 40.36  ? 193 LEU A CA  1 
ATOM   1461 C C   . LEU A 1 193 ? 58.841 10.347  66.054 1.00 39.97  ? 193 LEU A C   1 
ATOM   1462 O O   . LEU A 1 193 ? 59.750 11.154  65.846 1.00 39.37  ? 193 LEU A O   1 
ATOM   1463 C CB  . LEU A 1 193 ? 56.810 11.143  67.469 1.00 39.84  ? 193 LEU A CB  1 
ATOM   1464 C CG  . LEU A 1 193 ? 56.335 11.822  66.169 1.00 40.66  ? 193 LEU A CG  1 
ATOM   1465 C CD1 . LEU A 1 193 ? 55.847 10.756  65.198 1.00 43.51  ? 193 LEU A CD1 1 
ATOM   1466 C CD2 . LEU A 1 193 ? 55.295 12.866  66.452 1.00 40.18  ? 193 LEU A CD2 1 
ATOM   1467 N N   . TYR A 1 194 ? 58.699 9.254   65.280 1.00 38.84  ? 194 TYR A N   1 
ATOM   1468 C CA  . TYR A 1 194 ? 59.370 9.235   63.994 1.00 38.68  ? 194 TYR A CA  1 
ATOM   1469 C C   . TYR A 1 194 ? 58.360 9.399   62.859 1.00 38.27  ? 194 TYR A C   1 
ATOM   1470 O O   . TYR A 1 194 ? 57.601 8.458   62.620 1.00 39.24  ? 194 TYR A O   1 
ATOM   1471 C CB  . TYR A 1 194 ? 60.209 8.012   63.739 1.00 37.93  ? 194 TYR A CB  1 
ATOM   1472 C CG  . TYR A 1 194 ? 61.261 7.827   64.786 1.00 36.30  ? 194 TYR A CG  1 
ATOM   1473 C CD1 . TYR A 1 194 ? 62.518 8.334   64.567 1.00 35.95  ? 194 TYR A CD1 1 
ATOM   1474 C CD2 . TYR A 1 194 ? 61.037 7.131   65.957 1.00 36.09  ? 194 TYR A CD2 1 
ATOM   1475 C CE1 . TYR A 1 194 ? 63.551 8.203   65.476 1.00 34.49  ? 194 TYR A CE1 1 
ATOM   1476 C CE2 . TYR A 1 194 ? 62.047 6.926   66.870 1.00 35.00  ? 194 TYR A CE2 1 
ATOM   1477 C CZ  . TYR A 1 194 ? 63.268 7.503   66.619 1.00 35.61  ? 194 TYR A CZ  1 
ATOM   1478 O OH  . TYR A 1 194 ? 64.299 7.373   67.532 1.00 37.27  ? 194 TYR A OH  1 
ATOM   1479 N N   . ARG A 1 195 ? 58.183 10.634  62.421 1.00 37.00  ? 195 ARG A N   1 
ATOM   1480 C CA  . ARG A 1 195 ? 57.176 10.941  61.448 1.00 35.80  ? 195 ARG A CA  1 
ATOM   1481 C C   . ARG A 1 195 ? 57.833 10.748  60.090 1.00 37.37  ? 195 ARG A C   1 
ATOM   1482 O O   . ARG A 1 195 ? 58.589 11.619  59.628 1.00 38.51  ? 195 ARG A O   1 
ATOM   1483 C CB  . ARG A 1 195 ? 56.657 12.353  61.570 1.00 32.56  ? 195 ARG A CB  1 
ATOM   1484 C CG  . ARG A 1 195 ? 55.228 12.504  61.086 1.00 30.31  ? 195 ARG A CG  1 
ATOM   1485 C CD  . ARG A 1 195 ? 54.725 13.911  61.205 1.00 29.56  ? 195 ARG A CD  1 
ATOM   1486 N NE  . ARG A 1 195 ? 55.784 14.900  61.000 1.00 32.83  ? 195 ARG A NE  1 
ATOM   1487 C CZ  . ARG A 1 195 ? 56.019 15.474  59.816 1.00 33.10  ? 195 ARG A CZ  1 
ATOM   1488 N NH1 . ARG A 1 195 ? 57.021 16.344  59.820 1.00 34.97  ? 195 ARG A NH1 1 
ATOM   1489 N NH2 . ARG A 1 195 ? 55.310 15.212  58.712 1.00 28.95  ? 195 ARG A NH2 1 
ATOM   1490 N N   . ILE A 1 196 ? 57.361 9.692   59.419 1.00 37.14  ? 196 ILE A N   1 
ATOM   1491 C CA  . ILE A 1 196 ? 58.070 9.268   58.213 1.00 35.81  ? 196 ILE A CA  1 
ATOM   1492 C C   . ILE A 1 196 ? 57.265 9.655   57.009 1.00 35.36  ? 196 ILE A C   1 
ATOM   1493 O O   . ILE A 1 196 ? 56.070 9.364   56.934 1.00 35.70  ? 196 ILE A O   1 
ATOM   1494 C CB  . ILE A 1 196 ? 58.325 7.745   58.272 1.00 34.39  ? 196 ILE A CB  1 
ATOM   1495 C CG1 . ILE A 1 196 ? 59.500 7.523   59.241 1.00 31.66  ? 196 ILE A CG1 1 
ATOM   1496 C CG2 . ILE A 1 196 ? 58.672 7.168   56.901 1.00 31.22  ? 196 ILE A CG2 1 
ATOM   1497 C CD1 . ILE A 1 196 ? 59.334 6.378   60.176 1.00 29.09  ? 196 ILE A CD1 1 
ATOM   1498 N N   . THR A 1 197 ? 57.929 10.303  56.065 1.00 34.58  ? 197 THR A N   1 
ATOM   1499 C CA  . THR A 1 197 ? 57.139 10.672  54.881 1.00 33.89  ? 197 THR A CA  1 
ATOM   1500 C C   . THR A 1 197 ? 57.791 10.149  53.600 1.00 33.98  ? 197 THR A C   1 
ATOM   1501 O O   . THR A 1 197 ? 58.964 9.730   53.675 1.00 34.26  ? 197 THR A O   1 
ATOM   1502 C CB  . THR A 1 197 ? 56.893 12.166  54.722 1.00 30.93  ? 197 THR A CB  1 
ATOM   1503 O OG1 . THR A 1 197 ? 58.033 12.949  54.663 1.00 28.68  ? 197 THR A OG1 1 
ATOM   1504 C CG2 . THR A 1 197 ? 55.948 12.686  55.740 1.00 24.80  ? 197 THR A CG2 1 
ATOM   1505 N N   . HIS A 1 198 ? 57.002 10.126  52.533 1.00 32.99  ? 198 HIS A N   1 
ATOM   1506 C CA  . HIS A 1 198 ? 57.541 9.627   51.270 1.00 34.51  ? 198 HIS A CA  1 
ATOM   1507 C C   . HIS A 1 198 ? 57.278 10.567  50.082 1.00 35.68  ? 198 HIS A C   1 
ATOM   1508 O O   . HIS A 1 198 ? 56.145 10.861  49.667 1.00 35.25  ? 198 HIS A O   1 
ATOM   1509 C CB  . HIS A 1 198 ? 56.924 8.228   50.985 1.00 32.91  ? 198 HIS A CB  1 
ATOM   1510 C CG  . HIS A 1 198 ? 57.341 7.690   49.657 1.00 31.37  ? 198 HIS A CG  1 
ATOM   1511 N ND1 . HIS A 1 198 ? 56.471 7.275   48.681 1.00 31.95  ? 198 HIS A ND1 1 
ATOM   1512 C CD2 . HIS A 1 198 ? 58.601 7.592   49.139 1.00 31.50  ? 198 HIS A CD2 1 
ATOM   1513 C CE1 . HIS A 1 198 ? 57.193 6.880   47.638 1.00 31.94  ? 198 HIS A CE1 1 
ATOM   1514 N NE2 . HIS A 1 198 ? 58.478 7.092   47.872 1.00 30.42  ? 198 HIS A NE2 1 
ATOM   1515 N N   . THR A 1 199 ? 58.338 10.889  49.342 1.00 35.24  ? 199 THR A N   1 
ATOM   1516 C CA  . THR A 1 199 ? 58.298 11.767  48.198 1.00 36.50  ? 199 THR A CA  1 
ATOM   1517 C C   . THR A 1 199 ? 57.126 12.738  48.228 1.00 37.49  ? 199 THR A C   1 
ATOM   1518 O O   . THR A 1 199 ? 57.023 13.486  49.189 1.00 38.10  ? 199 THR A O   1 
ATOM   1519 C CB  . THR A 1 199 ? 58.257 10.968  46.858 1.00 31.90  ? 199 THR A CB  1 
ATOM   1520 O OG1 . THR A 1 199 ? 57.313 9.918   47.082 1.00 30.15  ? 199 THR A OG1 1 
ATOM   1521 C CG2 . THR A 1 199 ? 59.633 10.395  46.628 1.00 25.36  ? 199 THR A CG2 1 
ATOM   1522 N N   . ASN A 1 200 ? 56.220 12.676  47.261 1.00 38.28  ? 200 ASN A N   1 
ATOM   1523 C CA  . ASN A 1 200 ? 55.077 13.562  47.188 1.00 38.96  ? 200 ASN A CA  1 
ATOM   1524 C C   . ASN A 1 200 ? 53.820 12.930  47.713 1.00 38.46  ? 200 ASN A C   1 
ATOM   1525 O O   . ASN A 1 200 ? 52.735 13.229  47.213 1.00 39.42  ? 200 ASN A O   1 
ATOM   1526 C CB  . ASN A 1 200 ? 54.892 14.163  45.786 1.00 45.97  ? 200 ASN A CB  1 
ATOM   1527 C CG  . ASN A 1 200 ? 54.534 13.211  44.667 1.00 53.54  ? 200 ASN A CG  1 
ATOM   1528 O OD1 . ASN A 1 200 ? 54.848 12.000  44.769 1.00 56.55  ? 200 ASN A OD1 1 
ATOM   1529 N ND2 . ASN A 1 200 ? 53.904 13.650  43.559 1.00 53.86  ? 200 ASN A ND2 1 
ATOM   1530 N N   . ASP A 1 201 ? 53.879 12.049  48.697 1.00 38.25  ? 201 ASP A N   1 
ATOM   1531 C CA  . ASP A 1 201 ? 52.648 11.473  49.262 1.00 37.91  ? 201 ASP A CA  1 
ATOM   1532 C C   . ASP A 1 201 ? 51.716 12.641  49.593 1.00 39.32  ? 201 ASP A C   1 
ATOM   1533 O O   . ASP A 1 201 ? 52.143 13.725  50.009 1.00 38.88  ? 201 ASP A O   1 
ATOM   1534 C CB  . ASP A 1 201 ? 53.006 10.641  50.458 1.00 35.79  ? 201 ASP A CB  1 
ATOM   1535 C CG  . ASP A 1 201 ? 51.944 9.984   51.300 1.00 34.09  ? 201 ASP A CG  1 
ATOM   1536 O OD1 . ASP A 1 201 ? 50.754 10.043  50.917 1.00 36.31  ? 201 ASP A OD1 1 
ATOM   1537 O OD2 . ASP A 1 201 ? 52.282 9.366   52.331 1.00 26.13  ? 201 ASP A OD2 1 
ATOM   1538 N N   . ILE A 1 202 ? 50.432 12.463  49.302 1.00 39.99  ? 202 ILE A N   1 
ATOM   1539 C CA  . ILE A 1 202 ? 49.386 13.433  49.517 1.00 39.94  ? 202 ILE A CA  1 
ATOM   1540 C C   . ILE A 1 202 ? 48.892 13.447  50.958 1.00 40.92  ? 202 ILE A C   1 
ATOM   1541 O O   . ILE A 1 202 ? 48.577 14.543  51.431 1.00 40.88  ? 202 ILE A O   1 
ATOM   1542 C CB  . ILE A 1 202 ? 48.175 13.193  48.590 1.00 37.80  ? 202 ILE A CB  1 
ATOM   1543 C CG1 . ILE A 1 202 ? 47.123 14.306  48.696 1.00 37.82  ? 202 ILE A CG1 1 
ATOM   1544 C CG2 . ILE A 1 202 ? 47.486 11.860  48.871 1.00 35.60  ? 202 ILE A CG2 1 
ATOM   1545 C CD1 . ILE A 1 202 ? 45.955 14.208  47.713 1.00 33.20  ? 202 ILE A CD1 1 
ATOM   1546 N N   . VAL A 1 203 ? 48.879 12.315  51.678 1.00 40.94  ? 203 VAL A N   1 
ATOM   1547 C CA  . VAL A 1 203 ? 48.279 12.301  53.001 1.00 40.57  ? 203 VAL A CA  1 
ATOM   1548 C C   . VAL A 1 203 ? 48.893 13.280  53.980 1.00 40.78  ? 203 VAL A C   1 
ATOM   1549 O O   . VAL A 1 203 ? 48.111 14.111  54.434 1.00 39.16  ? 203 VAL A O   1 
ATOM   1550 C CB  . VAL A 1 203 ? 47.934 10.926  53.583 1.00 41.48  ? 203 VAL A CB  1 
ATOM   1551 C CG1 . VAL A 1 203 ? 47.154 11.090  54.920 1.00 40.01  ? 203 VAL A CG1 1 
ATOM   1552 C CG2 . VAL A 1 203 ? 47.130 10.112  52.562 1.00 38.68  ? 203 VAL A CG2 1 
ATOM   1553 N N   . PRO A 1 204 ? 50.210 13.455  54.031 1.00 41.22  ? 204 PRO A N   1 
ATOM   1554 C CA  . PRO A 1 204 ? 50.887 14.382  54.884 1.00 41.96  ? 204 PRO A CA  1 
ATOM   1555 C C   . PRO A 1 204 ? 50.613 15.823  54.596 1.00 42.62  ? 204 PRO A C   1 
ATOM   1556 O O   . PRO A 1 204 ? 51.359 16.655  55.131 1.00 43.65  ? 204 PRO A O   1 
ATOM   1557 C CB  . PRO A 1 204 ? 52.399 14.166  54.671 1.00 42.28  ? 204 PRO A CB  1 
ATOM   1558 C CG  . PRO A 1 204 ? 52.356 12.682  54.418 1.00 43.19  ? 204 PRO A CG  1 
ATOM   1559 C CD  . PRO A 1 204 ? 51.117 12.374  53.636 1.00 41.84  ? 204 PRO A CD  1 
ATOM   1560 N N   . ARG A 1 205 ? 49.952 16.134  53.517 1.00 43.23  ? 205 ARG A N   1 
ATOM   1561 C CA  . ARG A 1 205 ? 49.673 17.481  53.007 1.00 42.51  ? 205 ARG A CA  1 
ATOM   1562 C C   . ARG A 1 205 ? 48.284 17.837  53.495 1.00 42.50  ? 205 ARG A C   1 
ATOM   1563 O O   . ARG A 1 205 ? 47.649 18.856  53.343 1.00 44.45  ? 205 ARG A O   1 
ATOM   1564 C CB  . ARG A 1 205 ? 49.779 17.274  51.506 1.00 39.78  ? 205 ARG A CB  1 
ATOM   1565 C CG  . ARG A 1 205 ? 50.844 17.840  50.665 1.00 40.75  ? 205 ARG A CG  1 
ATOM   1566 C CD  . ARG A 1 205 ? 52.165 17.243  50.351 1.00 39.38  ? 205 ARG A CD  1 
ATOM   1567 N NE  . ARG A 1 205 ? 52.641 17.536  49.049 1.00 37.59  ? 205 ARG A NE  1 
ATOM   1568 C CZ  . ARG A 1 205 ? 53.535 17.546  48.121 1.00 40.44  ? 205 ARG A CZ  1 
ATOM   1569 N NH1 . ARG A 1 205 ? 54.778 17.077  48.237 1.00 43.05  ? 205 ARG A NH1 1 
ATOM   1570 N NH2 . ARG A 1 205 ? 53.263 18.043  46.909 1.00 37.80  ? 205 ARG A NH2 1 
ATOM   1571 N N   . LEU A 1 206 ? 47.682 16.905  54.176 1.00 42.35  ? 206 LEU A N   1 
ATOM   1572 C CA  . LEU A 1 206 ? 46.353 17.023  54.730 1.00 42.77  ? 206 LEU A CA  1 
ATOM   1573 C C   . LEU A 1 206 ? 46.261 16.734  56.230 1.00 42.47  ? 206 LEU A C   1 
ATOM   1574 O O   . LEU A 1 206 ? 46.980 15.862  56.732 1.00 42.82  ? 206 LEU A O   1 
ATOM   1575 C CB  . LEU A 1 206 ? 45.544 15.929  54.012 1.00 43.92  ? 206 LEU A CB  1 
ATOM   1576 C CG  . LEU A 1 206 ? 45.189 16.091  52.546 1.00 45.35  ? 206 LEU A CG  1 
ATOM   1577 C CD1 . LEU A 1 206 ? 44.209 14.975  52.160 1.00 43.58  ? 206 LEU A CD1 1 
ATOM   1578 C CD2 . LEU A 1 206 ? 44.659 17.495  52.286 1.00 44.95  ? 206 LEU A CD2 1 
ATOM   1579 N N   . PRO A 1 207 ? 45.417 17.415  56.963 1.00 41.64  ? 207 PRO A N   1 
ATOM   1580 C CA  . PRO A 1 207 ? 44.705 18.552  56.442 1.00 41.86  ? 207 PRO A CA  1 
ATOM   1581 C C   . PRO A 1 207 ? 45.667 19.709  56.228 1.00 42.04  ? 207 PRO A C   1 
ATOM   1582 O O   . PRO A 1 207 ? 46.876 19.534  56.469 1.00 40.79  ? 207 PRO A O   1 
ATOM   1583 C CB  . PRO A 1 207 ? 43.689 18.909  57.523 1.00 42.24  ? 207 PRO A CB  1 
ATOM   1584 C CG  . PRO A 1 207 ? 43.591 17.642  58.323 1.00 42.60  ? 207 PRO A CG  1 
ATOM   1585 C CD  . PRO A 1 207 ? 45.049 17.193  58.372 1.00 41.79  ? 207 PRO A CD  1 
ATOM   1586 N N   . PRO A 1 208 ? 45.290 20.591  55.292 1.00 42.54  ? 208 PRO A N   1 
ATOM   1587 C CA  . PRO A 1 208 ? 46.104 21.734  54.920 1.00 42.34  ? 208 PRO A CA  1 
ATOM   1588 C C   . PRO A 1 208 ? 46.427 22.612  56.100 1.00 42.80  ? 208 PRO A C   1 
ATOM   1589 O O   . PRO A 1 208 ? 45.570 22.755  56.988 1.00 43.58  ? 208 PRO A O   1 
ATOM   1590 C CB  . PRO A 1 208 ? 45.161 22.523  54.014 1.00 42.14  ? 208 PRO A CB  1 
ATOM   1591 C CG  . PRO A 1 208 ? 44.147 21.583  53.483 1.00 41.24  ? 208 PRO A CG  1 
ATOM   1592 C CD  . PRO A 1 208 ? 43.994 20.535  54.541 1.00 42.28  ? 208 PRO A CD  1 
ATOM   1593 N N   . ARG A 1 209 ? 47.563 23.263  56.119 1.00 43.00  ? 209 ARG A N   1 
ATOM   1594 C CA  . ARG A 1 209 ? 47.873 24.317  57.063 1.00 44.05  ? 209 ARG A CA  1 
ATOM   1595 C C   . ARG A 1 209 ? 46.847 25.433  57.099 1.00 44.76  ? 209 ARG A C   1 
ATOM   1596 O O   . ARG A 1 209 ? 46.342 25.890  58.144 1.00 45.31  ? 209 ARG A O   1 
ATOM   1597 C CB  . ARG A 1 209 ? 49.205 24.949  56.615 1.00 45.20  ? 209 ARG A CB  1 
ATOM   1598 C CG  . ARG A 1 209 ? 50.318 23.908  56.758 1.00 49.55  ? 209 ARG A CG  1 
ATOM   1599 C CD  . ARG A 1 209 ? 51.656 24.555  56.570 1.00 53.18  ? 209 ARG A CD  1 
ATOM   1600 N NE  . ARG A 1 209 ? 52.025 25.602  57.471 1.00 62.28  ? 209 ARG A NE  1 
ATOM   1601 C CZ  . ARG A 1 209 ? 51.657 26.128  58.627 1.00 65.44  ? 209 ARG A CZ  1 
ATOM   1602 N NH1 . ARG A 1 209 ? 50.637 25.697  59.375 1.00 63.93  ? 209 ARG A NH1 1 
ATOM   1603 N NH2 . ARG A 1 209 ? 52.366 27.157  59.127 1.00 66.26  ? 209 ARG A NH2 1 
ATOM   1604 N N   . GLU A 1 210 ? 46.347 25.884  55.960 1.00 44.91  ? 210 GLU A N   1 
ATOM   1605 C CA  . GLU A 1 210 ? 45.321 26.912  55.862 1.00 45.34  ? 210 GLU A CA  1 
ATOM   1606 C C   . GLU A 1 210 ? 44.158 26.640  56.801 1.00 45.41  ? 210 GLU A C   1 
ATOM   1607 O O   . GLU A 1 210 ? 43.662 27.628  57.342 1.00 45.44  ? 210 GLU A O   1 
ATOM   1608 C CB  . GLU A 1 210 ? 44.861 27.060  54.420 1.00 45.77  ? 210 GLU A CB  1 
ATOM   1609 C CG  . GLU A 1 210 ? 45.941 27.597  53.500 1.00 48.40  ? 210 GLU A CG  1 
ATOM   1610 C CD  . GLU A 1 210 ? 46.970 26.596  53.018 1.00 49.14  ? 210 GLU A CD  1 
ATOM   1611 O OE1 . GLU A 1 210 ? 48.050 27.002  52.552 1.00 51.59  ? 210 GLU A OE1 1 
ATOM   1612 O OE2 . GLU A 1 210 ? 46.750 25.367  53.108 1.00 50.40  ? 210 GLU A OE2 1 
ATOM   1613 N N   . PHE A 1 211 ? 43.845 25.401  57.181 1.00 44.68  ? 211 PHE A N   1 
ATOM   1614 C CA  . PHE A 1 211 ? 42.804 25.158  58.149 1.00 44.65  ? 211 PHE A CA  1 
ATOM   1615 C C   . PHE A 1 211 ? 43.273 25.064  59.594 1.00 45.12  ? 211 PHE A C   1 
ATOM   1616 O O   . PHE A 1 211 ? 42.543 24.533  60.438 1.00 45.18  ? 211 PHE A O   1 
ATOM   1617 C CB  . PHE A 1 211 ? 42.008 23.910  57.791 1.00 44.19  ? 211 PHE A CB  1 
ATOM   1618 C CG  . PHE A 1 211 ? 41.217 24.110  56.535 1.00 46.60  ? 211 PHE A CG  1 
ATOM   1619 C CD1 . PHE A 1 211 ? 41.752 23.871  55.281 1.00 47.62  ? 211 PHE A CD1 1 
ATOM   1620 C CD2 . PHE A 1 211 ? 39.897 24.524  56.608 1.00 43.56  ? 211 PHE A CD2 1 
ATOM   1621 C CE1 . PHE A 1 211 ? 40.983 24.058  54.132 1.00 48.50  ? 211 PHE A CE1 1 
ATOM   1622 C CE2 . PHE A 1 211 ? 39.148 24.708  55.463 1.00 45.78  ? 211 PHE A CE2 1 
ATOM   1623 C CZ  . PHE A 1 211 ? 39.677 24.480  54.215 1.00 46.98  ? 211 PHE A CZ  1 
ATOM   1624 N N   . GLY A 1 212 ? 44.429 25.615  59.942 1.00 44.75  ? 212 GLY A N   1 
ATOM   1625 C CA  . GLY A 1 212 ? 44.946 25.687  61.277 1.00 43.92  ? 212 GLY A CA  1 
ATOM   1626 C C   . GLY A 1 212 ? 45.839 24.522  61.673 1.00 44.59  ? 212 GLY A C   1 
ATOM   1627 O O   . GLY A 1 212 ? 45.968 24.257  62.882 1.00 43.92  ? 212 GLY A O   1 
ATOM   1628 N N   . TYR A 1 213 ? 46.337 23.760  60.682 1.00 44.30  ? 213 TYR A N   1 
ATOM   1629 C CA  . TYR A 1 213 ? 47.126 22.592  61.008 1.00 44.21  ? 213 TYR A CA  1 
ATOM   1630 C C   . TYR A 1 213 ? 48.626 22.742  60.806 1.00 43.87  ? 213 TYR A C   1 
ATOM   1631 O O   . TYR A 1 213 ? 49.119 23.369  59.874 1.00 44.51  ? 213 TYR A O   1 
ATOM   1632 C CB  . TYR A 1 213 ? 46.708 21.329  60.286 1.00 44.05  ? 213 TYR A CB  1 
ATOM   1633 C CG  . TYR A 1 213 ? 45.359 20.794  60.680 1.00 43.77  ? 213 TYR A CG  1 
ATOM   1634 C CD1 . TYR A 1 213 ? 44.230 21.422  60.166 1.00 43.76  ? 213 TYR A CD1 1 
ATOM   1635 C CD2 . TYR A 1 213 ? 45.189 19.697  61.510 1.00 42.62  ? 213 TYR A CD2 1 
ATOM   1636 C CE1 . TYR A 1 213 ? 42.972 20.928  60.467 1.00 42.61  ? 213 TYR A CE1 1 
ATOM   1637 C CE2 . TYR A 1 213 ? 43.938 19.200  61.800 1.00 41.59  ? 213 TYR A CE2 1 
ATOM   1638 C CZ  . TYR A 1 213 ? 42.838 19.835  61.278 1.00 41.73  ? 213 TYR A CZ  1 
ATOM   1639 O OH  . TYR A 1 213 ? 41.559 19.411  61.543 1.00 42.33  ? 213 TYR A OH  1 
ATOM   1640 N N   . SER A 1 214 ? 49.328 22.021  61.668 1.00 42.63  ? 214 SER A N   1 
ATOM   1641 C CA  . SER A 1 214 ? 50.783 22.068  61.656 1.00 42.04  ? 214 SER A CA  1 
ATOM   1642 C C   . SER A 1 214 ? 51.326 20.645  61.791 1.00 40.55  ? 214 SER A C   1 
ATOM   1643 O O   . SER A 1 214 ? 50.620 19.771  62.286 1.00 40.42  ? 214 SER A O   1 
ATOM   1644 C CB  . SER A 1 214 ? 51.224 22.890  62.884 1.00 43.70  ? 214 SER A CB  1 
ATOM   1645 O OG  . SER A 1 214 ? 51.782 24.130  62.492 1.00 47.26  ? 214 SER A OG  1 
ATOM   1646 N N   . HIS A 1 215 ? 52.560 20.446  61.382 1.00 39.23  ? 215 HIS A N   1 
ATOM   1647 C CA  . HIS A 1 215 ? 53.235 19.187  61.568 1.00 38.45  ? 215 HIS A CA  1 
ATOM   1648 C C   . HIS A 1 215 ? 54.275 19.284  62.687 1.00 37.84  ? 215 HIS A C   1 
ATOM   1649 O O   . HIS A 1 215 ? 55.107 20.190  62.697 1.00 37.70  ? 215 HIS A O   1 
ATOM   1650 C CB  . HIS A 1 215 ? 53.917 18.702  60.289 1.00 38.74  ? 215 HIS A CB  1 
ATOM   1651 C CG  . HIS A 1 215 ? 53.156 17.731  59.451 1.00 39.43  ? 215 HIS A CG  1 
ATOM   1652 N ND1 . HIS A 1 215 ? 52.396 16.705  60.000 1.00 39.41  ? 215 HIS A ND1 1 
ATOM   1653 C CD2 . HIS A 1 215 ? 53.115 17.556  58.101 1.00 37.87  ? 215 HIS A CD2 1 
ATOM   1654 C CE1 . HIS A 1 215 ? 51.891 15.963  59.039 1.00 37.80  ? 215 HIS A CE1 1 
ATOM   1655 N NE2 . HIS A 1 215 ? 52.338 16.450  57.869 1.00 38.20  ? 215 HIS A NE2 1 
ATOM   1656 N N   . SER A 1 216 ? 54.426 18.176  63.388 1.00 37.89  ? 216 SER A N   1 
ATOM   1657 C CA  . SER A 1 216 ? 55.486 17.904  64.344 1.00 38.02  ? 216 SER A CA  1 
ATOM   1658 C C   . SER A 1 216 ? 56.832 18.114  63.663 1.00 37.15  ? 216 SER A C   1 
ATOM   1659 O O   . SER A 1 216 ? 56.947 17.798  62.487 1.00 37.13  ? 216 SER A O   1 
ATOM   1660 C CB  . SER A 1 216 ? 55.320 16.404  64.770 1.00 39.61  ? 216 SER A CB  1 
ATOM   1661 O OG  . SER A 1 216 ? 56.382 15.669  64.022 1.00 50.59  ? 216 SER A OG  1 
ATOM   1662 N N   . SER A 1 217 ? 57.922 18.138  64.396 1.00 37.76  ? 217 SER A N   1 
ATOM   1663 C CA  . SER A 1 217 ? 59.292 18.117  63.835 1.00 37.70  ? 217 SER A CA  1 
ATOM   1664 C C   . SER A 1 217 ? 60.143 17.155  64.668 1.00 36.88  ? 217 SER A C   1 
ATOM   1665 O O   . SER A 1 217 ? 59.832 17.122  65.821 1.00 37.83  ? 217 SER A O   1 
ATOM   1666 C CB  . SER A 1 217 ? 59.894 19.511  63.924 1.00 36.53  ? 217 SER A CB  1 
ATOM   1667 O OG  . SER A 1 217 ? 61.149 19.529  63.305 1.00 35.66  ? 217 SER A OG  1 
ATOM   1668 N N   . PRO A 1 218 ? 61.070 16.362  64.178 1.00 36.34  ? 218 PRO A N   1 
ATOM   1669 C CA  . PRO A 1 218 ? 61.372 16.472  62.734 1.00 36.86  ? 218 PRO A CA  1 
ATOM   1670 C C   . PRO A 1 218 ? 60.616 15.569  61.789 1.00 37.50  ? 218 PRO A C   1 
ATOM   1671 O O   . PRO A 1 218 ? 59.654 14.914  62.168 1.00 38.65  ? 218 PRO A O   1 
ATOM   1672 C CB  . PRO A 1 218 ? 62.848 16.084  62.725 1.00 36.93  ? 218 PRO A CB  1 
ATOM   1673 C CG  . PRO A 1 218 ? 62.952 15.083  63.851 1.00 35.92  ? 218 PRO A CG  1 
ATOM   1674 C CD  . PRO A 1 218 ? 61.842 15.336  64.834 1.00 34.53  ? 218 PRO A CD  1 
ATOM   1675 N N   . GLU A 1 219 ? 61.007 15.553  60.512 1.00 38.01  ? 219 GLU A N   1 
ATOM   1676 C CA  . GLU A 1 219 ? 60.404 14.732  59.479 1.00 37.20  ? 219 GLU A CA  1 
ATOM   1677 C C   . GLU A 1 219 ? 61.428 13.802  58.837 1.00 36.09  ? 219 GLU A C   1 
ATOM   1678 O O   . GLU A 1 219 ? 62.566 14.252  58.691 1.00 35.79  ? 219 GLU A O   1 
ATOM   1679 C CB  . GLU A 1 219 ? 59.723 15.614  58.441 1.00 37.90  ? 219 GLU A CB  1 
ATOM   1680 C CG  . GLU A 1 219 ? 59.319 14.895  57.149 1.00 37.39  ? 219 GLU A CG  1 
ATOM   1681 C CD  . GLU A 1 219 ? 58.910 15.819  56.035 1.00 38.56  ? 219 GLU A CD  1 
ATOM   1682 O OE1 . GLU A 1 219 ? 58.998 17.050  56.171 1.00 40.30  ? 219 GLU A OE1 1 
ATOM   1683 O OE2 . GLU A 1 219 ? 58.395 15.430  54.963 1.00 40.45  ? 219 GLU A OE2 1 
ATOM   1684 N N   . TYR A 1 220 ? 61.099 12.538  58.624 1.00 35.50  ? 220 TYR A N   1 
ATOM   1685 C CA  . TYR A 1 220 ? 62.050 11.646  57.942 1.00 36.20  ? 220 TYR A CA  1 
ATOM   1686 C C   . TYR A 1 220 ? 61.574 11.334  56.530 1.00 36.43  ? 220 TYR A C   1 
ATOM   1687 O O   . TYR A 1 220 ? 60.539 10.682  56.362 1.00 36.65  ? 220 TYR A O   1 
ATOM   1688 C CB  . TYR A 1 220 ? 62.278 10.313  58.663 1.00 36.54  ? 220 TYR A CB  1 
ATOM   1689 C CG  . TYR A 1 220 ? 63.045 10.559  59.944 1.00 37.86  ? 220 TYR A CG  1 
ATOM   1690 C CD1 . TYR A 1 220 ? 64.430 10.594  59.972 1.00 37.85  ? 220 TYR A CD1 1 
ATOM   1691 C CD2 . TYR A 1 220 ? 62.312 10.824  61.112 1.00 38.05  ? 220 TYR A CD2 1 
ATOM   1692 C CE1 . TYR A 1 220 ? 65.080 10.922  61.147 1.00 38.56  ? 220 TYR A CE1 1 
ATOM   1693 C CE2 . TYR A 1 220 ? 62.961 11.082  62.301 1.00 37.64  ? 220 TYR A CE2 1 
ATOM   1694 C CZ  . TYR A 1 220 ? 64.332 11.128  62.295 1.00 39.51  ? 220 TYR A CZ  1 
ATOM   1695 O OH  . TYR A 1 220 ? 64.987 11.404  63.483 1.00 43.11  ? 220 TYR A OH  1 
ATOM   1696 N N   . TRP A 1 221 ? 62.090 12.094  55.577 1.00 36.55  ? 221 TRP A N   1 
ATOM   1697 C CA  . TRP A 1 221 ? 61.650 11.978  54.190 1.00 36.54  ? 221 TRP A CA  1 
ATOM   1698 C C   . TRP A 1 221 ? 62.312 10.968  53.250 1.00 36.73  ? 221 TRP A C   1 
ATOM   1699 O O   . TRP A 1 221 ? 63.519 11.073  52.931 1.00 36.53  ? 221 TRP A O   1 
ATOM   1700 C CB  . TRP A 1 221 ? 61.850 13.354  53.541 1.00 29.96  ? 221 TRP A CB  1 
ATOM   1701 C CG  . TRP A 1 221 ? 61.167 13.526  52.220 1.00 25.13  ? 221 TRP A CG  1 
ATOM   1702 C CD1 . TRP A 1 221 ? 59.854 13.228  51.954 1.00 19.56  ? 221 TRP A CD1 1 
ATOM   1703 C CD2 . TRP A 1 221 ? 61.725 14.174  51.072 1.00 20.84  ? 221 TRP A CD2 1 
ATOM   1704 N NE1 . TRP A 1 221 ? 59.601 13.612  50.660 1.00 23.57  ? 221 TRP A NE1 1 
ATOM   1705 C CE2 . TRP A 1 221 ? 60.722 14.193  50.101 1.00 22.54  ? 221 TRP A CE2 1 
ATOM   1706 C CE3 . TRP A 1 221 ? 62.940 14.746  50.770 1.00 25.31  ? 221 TRP A CE3 1 
ATOM   1707 C CZ2 . TRP A 1 221 ? 60.912 14.717  48.825 1.00 25.38  ? 221 TRP A CZ2 1 
ATOM   1708 C CZ3 . TRP A 1 221 ? 63.170 15.255  49.467 1.00 28.48  ? 221 TRP A CZ3 1 
ATOM   1709 C CH2 . TRP A 1 221 ? 62.144 15.247  48.506 1.00 24.82  ? 221 TRP A CH2 1 
ATOM   1710 N N   . ILE A 1 222 ? 61.525 10.014  52.732 1.00 36.63  ? 222 ILE A N   1 
ATOM   1711 C CA  . ILE A 1 222 ? 62.110 8.992   51.815 1.00 36.07  ? 222 ILE A CA  1 
ATOM   1712 C C   . ILE A 1 222 ? 62.137 9.542   50.401 1.00 36.25  ? 222 ILE A C   1 
ATOM   1713 O O   . ILE A 1 222 ? 61.066 9.974   49.931 1.00 37.56  ? 222 ILE A O   1 
ATOM   1714 C CB  . ILE A 1 222 ? 61.225 7.725   51.870 1.00 32.96  ? 222 ILE A CB  1 
ATOM   1715 C CG1 . ILE A 1 222 ? 61.199 7.167   53.280 1.00 31.11  ? 222 ILE A CG1 1 
ATOM   1716 C CG2 . ILE A 1 222 ? 61.639 6.661   50.859 1.00 32.80  ? 222 ILE A CG2 1 
ATOM   1717 C CD1 . ILE A 1 222 ? 60.057 6.242   53.594 1.00 28.29  ? 222 ILE A CD1 1 
ATOM   1718 N N   . LYS A 1 223 ? 63.230 9.623   49.680 1.00 36.17  ? 223 LYS A N   1 
ATOM   1719 C CA  . LYS A 1 223 ? 63.210 10.242  48.357 1.00 36.60  ? 223 LYS A CA  1 
ATOM   1720 C C   . LYS A 1 223 ? 63.070 9.209   47.239 1.00 36.22  ? 223 LYS A C   1 
ATOM   1721 O O   . LYS A 1 223 ? 62.845 9.587   46.076 1.00 38.02  ? 223 LYS A O   1 
ATOM   1722 C CB  . LYS A 1 223 ? 64.519 10.948  48.042 1.00 41.42  ? 223 LYS A CB  1 
ATOM   1723 C CG  . LYS A 1 223 ? 65.182 11.804  49.097 1.00 46.84  ? 223 LYS A CG  1 
ATOM   1724 C CD  . LYS A 1 223 ? 66.497 12.381  48.564 1.00 50.93  ? 223 LYS A CD  1 
ATOM   1725 C CE  . LYS A 1 223 ? 67.597 11.304  48.569 1.00 53.86  ? 223 LYS A CE  1 
ATOM   1726 N NZ  . LYS A 1 223 ? 68.924 11.923  48.926 1.00 56.32  ? 223 LYS A NZ  1 
ATOM   1727 N N   . SER A 1 224 ? 63.403 7.965   47.453 1.00 33.99  ? 224 SER A N   1 
ATOM   1728 C CA  . SER A 1 224 ? 63.297 6.992   46.384 1.00 33.49  ? 224 SER A CA  1 
ATOM   1729 C C   . SER A 1 224 ? 61.845 6.985   45.962 1.00 34.17  ? 224 SER A C   1 
ATOM   1730 O O   . SER A 1 224 ? 60.945 7.353   46.725 1.00 33.66  ? 224 SER A O   1 
ATOM   1731 C CB  . SER A 1 224 ? 63.895 5.678   46.843 1.00 31.92  ? 224 SER A CB  1 
ATOM   1732 O OG  . SER A 1 224 ? 63.879 5.593   48.250 1.00 33.65  ? 224 SER A OG  1 
ATOM   1733 N N   . GLY A 1 225 ? 61.590 6.548   44.742 1.00 35.15  ? 225 GLY A N   1 
ATOM   1734 C CA  . GLY A 1 225 ? 60.300 6.638   44.123 1.00 35.93  ? 225 GLY A CA  1 
ATOM   1735 C C   . GLY A 1 225 ? 59.347 5.530   44.483 1.00 37.62  ? 225 GLY A C   1 
ATOM   1736 O O   . GLY A 1 225 ? 59.767 4.591   45.175 1.00 39.53  ? 225 GLY A O   1 
ATOM   1737 N N   . THR A 1 226 ? 58.117 5.623   43.965 1.00 37.30  ? 226 THR A N   1 
ATOM   1738 C CA  . THR A 1 226 ? 57.173 4.539   44.140 1.00 36.58  ? 226 THR A CA  1 
ATOM   1739 C C   . THR A 1 226 ? 57.727 3.240   43.578 1.00 36.26  ? 226 THR A C   1 
ATOM   1740 O O   . THR A 1 226 ? 58.347 3.202   42.512 1.00 35.90  ? 226 THR A O   1 
ATOM   1741 C CB  . THR A 1 226 ? 55.828 4.835   43.440 1.00 34.26  ? 226 THR A CB  1 
ATOM   1742 O OG1 . THR A 1 226 ? 55.368 5.990   44.124 1.00 39.82  ? 226 THR A OG1 1 
ATOM   1743 C CG2 . THR A 1 226 ? 54.826 3.753   43.762 1.00 35.92  ? 226 THR A CG2 1 
ATOM   1744 N N   . LEU A 1 227 ? 57.538 2.165   44.335 1.00 35.58  ? 227 LEU A N   1 
ATOM   1745 C CA  . LEU A 1 227 ? 58.043 0.891   43.854 1.00 36.00  ? 227 LEU A CA  1 
ATOM   1746 C C   . LEU A 1 227 ? 59.547 0.909   43.750 1.00 36.14  ? 227 LEU A C   1 
ATOM   1747 O O   . LEU A 1 227 ? 60.064 -0.068  43.172 1.00 36.98  ? 227 LEU A O   1 
ATOM   1748 C CB  . LEU A 1 227 ? 57.345 0.496   42.544 1.00 34.85  ? 227 LEU A CB  1 
ATOM   1749 C CG  . LEU A 1 227 ? 55.842 0.192   42.715 1.00 36.78  ? 227 LEU A CG  1 
ATOM   1750 C CD1 . LEU A 1 227 ? 55.062 0.592   41.485 1.00 37.96  ? 227 LEU A CD1 1 
ATOM   1751 C CD2 . LEU A 1 227 ? 55.639 -1.271  43.093 1.00 36.33  ? 227 LEU A CD2 1 
ATOM   1752 N N   . VAL A 1 228 ? 60.286 1.784   44.422 1.00 35.86  ? 228 VAL A N   1 
ATOM   1753 C CA  . VAL A 1 228 ? 61.740 1.651   44.485 1.00 36.10  ? 228 VAL A CA  1 
ATOM   1754 C C   . VAL A 1 228 ? 62.207 1.215   45.857 1.00 36.85  ? 228 VAL A C   1 
ATOM   1755 O O   . VAL A 1 228 ? 61.711 1.613   46.892 1.00 37.72  ? 228 VAL A O   1 
ATOM   1756 C CB  . VAL A 1 228 ? 62.431 2.977   44.147 1.00 36.47  ? 228 VAL A CB  1 
ATOM   1757 C CG1 . VAL A 1 228 ? 63.960 2.825   44.136 1.00 30.02  ? 228 VAL A CG1 1 
ATOM   1758 C CG2 . VAL A 1 228 ? 61.883 3.413   42.764 1.00 36.58  ? 228 VAL A CG2 1 
ATOM   1759 N N   . PRO A 1 229 ? 63.082 0.227   45.937 1.00 38.10  ? 229 PRO A N   1 
ATOM   1760 C CA  . PRO A 1 229 ? 63.607 -0.219  47.232 1.00 37.69  ? 229 PRO A CA  1 
ATOM   1761 C C   . PRO A 1 229 ? 64.125 0.995   47.998 1.00 37.69  ? 229 PRO A C   1 
ATOM   1762 O O   . PRO A 1 229 ? 64.622 1.918   47.359 1.00 35.88  ? 229 PRO A O   1 
ATOM   1763 C CB  . PRO A 1 229 ? 64.792 -1.102  46.880 1.00 36.62  ? 229 PRO A CB  1 
ATOM   1764 C CG  . PRO A 1 229 ? 64.586 -1.478  45.475 1.00 36.62  ? 229 PRO A CG  1 
ATOM   1765 C CD  . PRO A 1 229 ? 63.684 -0.498  44.780 1.00 36.80  ? 229 PRO A CD  1 
ATOM   1766 N N   . VAL A 1 230 ? 64.052 0.950   49.346 1.00 38.11  ? 230 VAL A N   1 
ATOM   1767 C CA  . VAL A 1 230 ? 64.587 2.098   50.079 1.00 37.78  ? 230 VAL A CA  1 
ATOM   1768 C C   . VAL A 1 230 ? 65.924 1.721   50.719 1.00 37.85  ? 230 VAL A C   1 
ATOM   1769 O O   . VAL A 1 230 ? 66.050 0.543   51.024 1.00 36.89  ? 230 VAL A O   1 
ATOM   1770 C CB  . VAL A 1 230 ? 63.597 2.551   51.155 1.00 37.71  ? 230 VAL A CB  1 
ATOM   1771 C CG1 . VAL A 1 230 ? 64.153 3.737   51.927 1.00 35.23  ? 230 VAL A CG1 1 
ATOM   1772 C CG2 . VAL A 1 230 ? 62.219 2.786   50.611 1.00 34.85  ? 230 VAL A CG2 1 
ATOM   1773 N N   . THR A 1 231 ? 66.944 2.572   50.736 1.00 37.98  ? 231 THR A N   1 
ATOM   1774 C CA  . THR A 1 231 ? 68.129 2.248   51.510 1.00 39.72  ? 231 THR A CA  1 
ATOM   1775 C C   . THR A 1 231 ? 68.361 3.349   52.562 1.00 41.23  ? 231 THR A C   1 
ATOM   1776 O O   . THR A 1 231 ? 67.834 4.454   52.445 1.00 41.36  ? 231 THR A O   1 
ATOM   1777 C CB  . THR A 1 231 ? 69.479 2.185   50.779 1.00 35.61  ? 231 THR A CB  1 
ATOM   1778 O OG1 . THR A 1 231 ? 69.698 3.581   50.504 1.00 41.74  ? 231 THR A OG1 1 
ATOM   1779 C CG2 . THR A 1 231 ? 69.470 1.396   49.499 1.00 34.29  ? 231 THR A CG2 1 
ATOM   1780 N N   . ARG A 1 232 ? 69.319 3.113   53.473 1.00 42.09  ? 232 ARG A N   1 
ATOM   1781 C CA  . ARG A 1 232 ? 69.692 4.195   54.357 1.00 42.75  ? 232 ARG A CA  1 
ATOM   1782 C C   . ARG A 1 232 ? 70.125 5.478   53.655 1.00 43.00  ? 232 ARG A C   1 
ATOM   1783 O O   . ARG A 1 232 ? 69.906 6.517   54.284 1.00 42.81  ? 232 ARG A O   1 
ATOM   1784 C CB  . ARG A 1 232 ? 70.691 3.810   55.404 1.00 43.70  ? 232 ARG A CB  1 
ATOM   1785 C CG  . ARG A 1 232 ? 71.831 2.897   55.192 1.00 48.19  ? 232 ARG A CG  1 
ATOM   1786 C CD  . ARG A 1 232 ? 73.108 3.548   54.821 1.00 51.25  ? 232 ARG A CD  1 
ATOM   1787 N NE  . ARG A 1 232 ? 73.572 4.461   55.845 1.00 59.57  ? 232 ARG A NE  1 
ATOM   1788 C CZ  . ARG A 1 232 ? 74.864 4.535   56.240 1.00 62.22  ? 232 ARG A CZ  1 
ATOM   1789 N NH1 . ARG A 1 232 ? 75.856 3.822   55.722 1.00 58.30  ? 232 ARG A NH1 1 
ATOM   1790 N NH2 . ARG A 1 232 ? 75.058 5.431   57.230 1.00 62.16  ? 232 ARG A NH2 1 
ATOM   1791 N N   . ASN A 1 233 ? 70.575 5.553   52.414 1.00 43.24  ? 233 ASN A N   1 
ATOM   1792 C CA  . ASN A 1 233 ? 70.949 6.799   51.786 1.00 43.92  ? 233 ASN A CA  1 
ATOM   1793 C C   . ASN A 1 233 ? 69.773 7.525   51.146 1.00 43.98  ? 233 ASN A C   1 
ATOM   1794 O O   . ASN A 1 233 ? 69.866 8.726   50.811 1.00 44.17  ? 233 ASN A O   1 
ATOM   1795 C CB  . ASN A 1 233 ? 72.147 6.616   50.865 1.00 46.32  ? 233 ASN A CB  1 
ATOM   1796 C CG  . ASN A 1 233 ? 73.314 5.946   51.582 1.00 52.73  ? 233 ASN A CG  1 
ATOM   1797 O OD1 . ASN A 1 233 ? 73.800 4.834   51.305 1.00 52.44  ? 233 ASN A OD1 1 
ATOM   1798 N ND2 . ASN A 1 233 ? 73.836 6.611   52.626 1.00 54.73  ? 233 ASN A ND2 1 
ATOM   1799 N N   . ASP A 1 234 ? 68.595 6.897   51.130 1.00 42.81  ? 234 ASP A N   1 
ATOM   1800 C CA  . ASP A 1 234 ? 67.448 7.566   50.546 1.00 42.41  ? 234 ASP A CA  1 
ATOM   1801 C C   . ASP A 1 234 ? 66.586 8.313   51.553 1.00 41.63  ? 234 ASP A C   1 
ATOM   1802 O O   . ASP A 1 234 ? 65.557 8.798   51.050 1.00 42.19  ? 234 ASP A O   1 
ATOM   1803 C CB  . ASP A 1 234 ? 66.495 6.670   49.726 1.00 40.06  ? 234 ASP A CB  1 
ATOM   1804 C CG  . ASP A 1 234 ? 67.365 5.888   48.762 1.00 41.61  ? 234 ASP A CG  1 
ATOM   1805 O OD1 . ASP A 1 234 ? 67.961 6.638   47.962 1.00 44.12  ? 234 ASP A OD1 1 
ATOM   1806 O OD2 . ASP A 1 234 ? 67.496 4.654   48.884 1.00 39.94  ? 234 ASP A OD2 1 
ATOM   1807 N N   . ILE A 1 235 ? 66.922 8.371   52.819 1.00 40.38  ? 235 ILE A N   1 
ATOM   1808 C CA  . ILE A 1 235 ? 66.058 9.038   53.790 1.00 40.56  ? 235 ILE A CA  1 
ATOM   1809 C C   . ILE A 1 235 ? 66.847 10.227  54.331 1.00 41.77  ? 235 ILE A C   1 
ATOM   1810 O O   . ILE A 1 235 ? 68.045 10.152  54.602 1.00 41.94  ? 235 ILE A O   1 
ATOM   1811 C CB  . ILE A 1 235 ? 65.690 8.042   54.878 1.00 35.98  ? 235 ILE A CB  1 
ATOM   1812 C CG1 . ILE A 1 235 ? 65.144 6.707   54.314 1.00 34.82  ? 235 ILE A CG1 1 
ATOM   1813 C CG2 . ILE A 1 235 ? 64.650 8.658   55.816 1.00 34.01  ? 235 ILE A CG2 1 
ATOM   1814 C CD1 . ILE A 1 235 ? 65.169 5.546   55.338 1.00 29.05  ? 235 ILE A CD1 1 
ATOM   1815 N N   . VAL A 1 236 ? 66.197 11.372  54.403 1.00 42.55  ? 236 VAL A N   1 
ATOM   1816 C CA  . VAL A 1 236 ? 66.931 12.586  54.902 1.00 43.45  ? 236 VAL A CA  1 
ATOM   1817 C C   . VAL A 1 236 ? 66.140 13.227  56.027 1.00 43.06  ? 236 VAL A C   1 
ATOM   1818 O O   . VAL A 1 236 ? 64.902 13.221  55.994 1.00 43.15  ? 236 VAL A O   1 
ATOM   1819 C CB  . VAL A 1 236 ? 66.944 13.493  53.659 1.00 45.49  ? 236 VAL A CB  1 
ATOM   1820 C CG1 . VAL A 1 236 ? 66.488 14.882  53.992 1.00 44.54  ? 236 VAL A CG1 1 
ATOM   1821 C CG2 . VAL A 1 236 ? 68.179 13.458  52.803 1.00 46.62  ? 236 VAL A CG2 1 
ATOM   1822 N N   . LYS A 1 237 ? 66.736 13.614  57.129 1.00 43.44  ? 237 LYS A N   1 
ATOM   1823 C CA  . LYS A 1 237 ? 65.991 14.167  58.251 1.00 42.68  ? 237 LYS A CA  1 
ATOM   1824 C C   . LYS A 1 237 ? 65.816 15.661  57.992 1.00 42.93  ? 237 LYS A C   1 
ATOM   1825 O O   . LYS A 1 237 ? 66.633 16.227  57.267 1.00 42.59  ? 237 LYS A O   1 
ATOM   1826 C CB  . LYS A 1 237 ? 66.774 14.028  59.527 1.00 41.82  ? 237 LYS A CB  1 
ATOM   1827 C CG  . LYS A 1 237 ? 65.917 14.239  60.777 1.00 44.55  ? 237 LYS A CG  1 
ATOM   1828 C CD  . LYS A 1 237 ? 66.923 14.202  61.924 1.00 49.03  ? 237 LYS A CD  1 
ATOM   1829 C CE  . LYS A 1 237 ? 66.305 14.168  63.304 1.00 49.08  ? 237 LYS A CE  1 
ATOM   1830 N NZ  . LYS A 1 237 ? 67.444 14.506  64.225 1.00 55.86  ? 237 LYS A NZ  1 
ATOM   1831 N N   . ILE A 1 238 ? 64.626 16.133  58.287 1.00 43.14  ? 238 ILE A N   1 
ATOM   1832 C CA  . ILE A 1 238 ? 64.237 17.504  58.039 1.00 44.71  ? 238 ILE A CA  1 
ATOM   1833 C C   . ILE A 1 238 ? 63.672 18.159  59.287 1.00 45.80  ? 238 ILE A C   1 
ATOM   1834 O O   . ILE A 1 238 ? 62.630 17.824  59.839 1.00 45.91  ? 238 ILE A O   1 
ATOM   1835 C CB  . ILE A 1 238 ? 63.251 17.538  56.862 1.00 45.76  ? 238 ILE A CB  1 
ATOM   1836 C CG1 . ILE A 1 238 ? 64.069 17.393  55.572 1.00 45.65  ? 238 ILE A CG1 1 
ATOM   1837 C CG2 . ILE A 1 238 ? 62.435 18.811  56.889 1.00 43.96  ? 238 ILE A CG2 1 
ATOM   1838 C CD1 . ILE A 1 238 ? 63.299 17.230  54.309 1.00 45.86  ? 238 ILE A CD1 1 
ATOM   1839 N N   . GLU A 1 239 ? 64.326 19.260  59.640 1.00 46.25  ? 239 GLU A N   1 
ATOM   1840 C CA  . GLU A 1 239 ? 64.147 19.866  60.969 1.00 45.68  ? 239 GLU A CA  1 
ATOM   1841 C C   . GLU A 1 239 ? 63.279 21.092  60.816 1.00 44.68  ? 239 GLU A C   1 
ATOM   1842 O O   . GLU A 1 239 ? 63.402 21.713  59.761 1.00 43.82  ? 239 GLU A O   1 
ATOM   1843 C CB  . GLU A 1 239 ? 65.610 20.095  61.374 1.00 50.03  ? 239 GLU A CB  1 
ATOM   1844 C CG  . GLU A 1 239 ? 65.924 19.897  62.823 1.00 57.98  ? 239 GLU A CG  1 
ATOM   1845 C CD  . GLU A 1 239 ? 66.118 18.498  63.328 1.00 60.91  ? 239 GLU A CD  1 
ATOM   1846 O OE1 . GLU A 1 239 ? 67.091 17.895  62.833 1.00 63.63  ? 239 GLU A OE1 1 
ATOM   1847 O OE2 . GLU A 1 239 ? 65.353 17.992  64.202 1.00 65.98  ? 239 GLU A OE2 1 
ATOM   1848 N N   . GLY A 1 240 ? 62.395 21.408  61.754 1.00 43.87  ? 240 GLY A N   1 
ATOM   1849 C CA  . GLY A 1 240 ? 61.552 22.567  61.721 1.00 42.63  ? 240 GLY A CA  1 
ATOM   1850 C C   . GLY A 1 240 ? 60.059 22.316  61.668 1.00 43.09  ? 240 GLY A C   1 
ATOM   1851 O O   . GLY A 1 240 ? 59.610 21.671  60.698 1.00 43.16  ? 240 GLY A O   1 
ATOM   1852 N N   . ILE A 1 241 ? 59.252 22.893  62.572 1.00 42.26  ? 241 ILE A N   1 
ATOM   1853 C CA  . ILE A 1 241 ? 57.807 22.762  62.465 1.00 42.35  ? 241 ILE A CA  1 
ATOM   1854 C C   . ILE A 1 241 ? 57.390 23.419  61.148 1.00 42.72  ? 241 ILE A C   1 
ATOM   1855 O O   . ILE A 1 241 ? 58.052 24.380  60.790 1.00 43.41  ? 241 ILE A O   1 
ATOM   1856 C CB  . ILE A 1 241 ? 56.925 23.493  63.470 1.00 41.38  ? 241 ILE A CB  1 
ATOM   1857 C CG1 . ILE A 1 241 ? 56.725 22.605  64.682 1.00 41.70  ? 241 ILE A CG1 1 
ATOM   1858 C CG2 . ILE A 1 241 ? 55.551 23.889  62.981 1.00 40.25  ? 241 ILE A CG2 1 
ATOM   1859 C CD1 . ILE A 1 241 ? 57.593 22.916  65.850 1.00 38.70  ? 241 ILE A CD1 1 
ATOM   1860 N N   . ASP A 1 242 ? 56.625 22.677  60.364 1.00 42.98  ? 242 ASP A N   1 
ATOM   1861 C CA  . ASP A 1 242 ? 56.098 23.204  59.106 1.00 41.84  ? 242 ASP A CA  1 
ATOM   1862 C C   . ASP A 1 242 ? 57.205 23.392  58.078 1.00 41.78  ? 242 ASP A C   1 
ATOM   1863 O O   . ASP A 1 242 ? 57.095 24.059  57.045 1.00 40.97  ? 242 ASP A O   1 
ATOM   1864 C CB  . ASP A 1 242 ? 55.236 24.391  59.457 1.00 40.96  ? 242 ASP A CB  1 
ATOM   1865 C CG  . ASP A 1 242 ? 53.921 23.995  60.103 1.00 45.29  ? 242 ASP A CG  1 
ATOM   1866 O OD1 . ASP A 1 242 ? 53.552 22.805  60.082 1.00 44.89  ? 242 ASP A OD1 1 
ATOM   1867 O OD2 . ASP A 1 242 ? 53.231 24.849  60.723 1.00 48.05  ? 242 ASP A OD2 1 
ATOM   1868 N N   . ALA A 1 243 ? 58.333 22.691  58.282 1.00 40.43  ? 243 ALA A N   1 
ATOM   1869 C CA  . ALA A 1 243 ? 59.447 22.734  57.385 1.00 40.46  ? 243 ALA A CA  1 
ATOM   1870 C C   . ALA A 1 243 ? 59.029 22.460  55.931 1.00 40.57  ? 243 ALA A C   1 
ATOM   1871 O O   . ALA A 1 243 ? 58.179 21.626  55.716 1.00 39.26  ? 243 ALA A O   1 
ATOM   1872 C CB  . ALA A 1 243 ? 60.491 21.755  57.882 1.00 39.46  ? 243 ALA A CB  1 
ATOM   1873 N N   . THR A 1 244 ? 59.877 22.906  55.002 1.00 41.50  ? 244 THR A N   1 
ATOM   1874 C CA  . THR A 1 244 ? 59.555 22.714  53.585 1.00 43.76  ? 244 THR A CA  1 
ATOM   1875 C C   . THR A 1 244 ? 60.580 21.893  52.813 1.00 43.98  ? 244 THR A C   1 
ATOM   1876 O O   . THR A 1 244 ? 61.701 21.560  53.240 1.00 43.49  ? 244 THR A O   1 
ATOM   1877 C CB  . THR A 1 244 ? 59.159 23.987  52.827 1.00 43.94  ? 244 THR A CB  1 
ATOM   1878 O OG1 . THR A 1 244 ? 60.161 24.998  52.886 1.00 43.10  ? 244 THR A OG1 1 
ATOM   1879 C CG2 . THR A 1 244 ? 57.889 24.617  53.387 1.00 44.10  ? 244 THR A CG2 1 
ATOM   1880 N N   . GLY A 1 245 ? 60.235 21.338  51.658 1.00 44.75  ? 245 GLY A N   1 
ATOM   1881 C CA  . GLY A 1 245 ? 61.360 20.549  51.074 1.00 48.38  ? 245 GLY A CA  1 
ATOM   1882 C C   . GLY A 1 245 ? 61.791 19.306  51.851 1.00 48.83  ? 245 GLY A C   1 
ATOM   1883 O O   . GLY A 1 245 ? 62.940 18.911  51.937 1.00 48.95  ? 245 GLY A O   1 
ATOM   1884 N N   . GLY A 1 246 ? 60.850 18.415  52.013 1.00 48.70  ? 246 GLY A N   1 
ATOM   1885 C CA  . GLY A 1 246 ? 60.573 17.099  52.462 1.00 47.39  ? 246 GLY A CA  1 
ATOM   1886 C C   . GLY A 1 246 ? 59.199 16.828  51.818 1.00 46.42  ? 246 GLY A C   1 
ATOM   1887 O O   . GLY A 1 246 ? 59.031 17.339  50.719 1.00 46.98  ? 246 GLY A O   1 
ATOM   1888 N N   . ASN A 1 247 ? 58.183 16.249  52.392 1.00 45.73  ? 247 ASN A N   1 
ATOM   1889 C CA  . ASN A 1 247 ? 56.878 16.151  51.746 1.00 45.19  ? 247 ASN A CA  1 
ATOM   1890 C C   . ASN A 1 247 ? 56.140 17.467  51.490 1.00 45.73  ? 247 ASN A C   1 
ATOM   1891 O O   . ASN A 1 247 ? 55.334 17.622  50.560 1.00 43.47  ? 247 ASN A O   1 
ATOM   1892 C CB  . ASN A 1 247 ? 56.056 15.240  52.652 1.00 38.71  ? 247 ASN A CB  1 
ATOM   1893 C CG  . ASN A 1 247 ? 54.618 15.178  52.186 1.00 40.45  ? 247 ASN A CG  1 
ATOM   1894 O OD1 . ASN A 1 247 ? 53.765 15.907  52.728 1.00 40.36  ? 247 ASN A OD1 1 
ATOM   1895 N ND2 . ASN A 1 247 ? 54.438 14.327  51.182 1.00 37.26  ? 247 ASN A ND2 1 
ATOM   1896 N N   . ASN A 1 248 ? 56.313 18.434  52.398 1.00 46.93  ? 248 ASN A N   1 
ATOM   1897 C CA  . ASN A 1 248 ? 55.669 19.737  52.332 1.00 48.29  ? 248 ASN A CA  1 
ATOM   1898 C C   . ASN A 1 248 ? 56.314 20.712  51.343 1.00 48.22  ? 248 ASN A C   1 
ATOM   1899 O O   . ASN A 1 248 ? 56.944 21.705  51.697 1.00 48.13  ? 248 ASN A O   1 
ATOM   1900 C CB  . ASN A 1 248 ? 55.588 20.344  53.723 1.00 50.44  ? 248 ASN A CB  1 
ATOM   1901 C CG  . ASN A 1 248 ? 54.780 21.610  53.784 1.00 55.80  ? 248 ASN A CG  1 
ATOM   1902 O OD1 . ASN A 1 248 ? 53.690 21.674  53.184 1.00 60.61  ? 248 ASN A OD1 1 
ATOM   1903 N ND2 . ASN A 1 248 ? 55.301 22.652  54.443 1.00 55.99  ? 248 ASN A ND2 1 
ATOM   1904 N N   . GLN A 1 249 ? 56.074 20.486  50.062 1.00 47.96  ? 249 GLN A N   1 
ATOM   1905 C CA  . GLN A 1 249 ? 56.600 21.250  48.967 1.00 48.38  ? 249 GLN A CA  1 
ATOM   1906 C C   . GLN A 1 249 ? 55.486 21.545  47.972 1.00 48.42  ? 249 GLN A C   1 
ATOM   1907 O O   . GLN A 1 249 ? 54.516 20.805  47.910 1.00 48.43  ? 249 GLN A O   1 
ATOM   1908 C CB  . GLN A 1 249 ? 57.699 20.514  48.229 1.00 52.34  ? 249 GLN A CB  1 
ATOM   1909 C CG  . GLN A 1 249 ? 59.062 20.717  48.869 1.00 56.53  ? 249 GLN A CG  1 
ATOM   1910 C CD  . GLN A 1 249 ? 60.055 19.838  48.135 1.00 58.56  ? 249 GLN A CD  1 
ATOM   1911 O OE1 . GLN A 1 249 ? 60.348 20.141  46.985 1.00 61.48  ? 249 GLN A OE1 1 
ATOM   1912 N NE2 . GLN A 1 249 ? 60.520 18.789  48.796 1.00 60.02  ? 249 GLN A NE2 1 
ATOM   1913 N N   . PRO A 1 250 ? 55.626 22.660  47.286 1.00 48.45  ? 250 PRO A N   1 
ATOM   1914 C CA  . PRO A 1 250 ? 54.626 23.144  46.353 1.00 48.55  ? 250 PRO A CA  1 
ATOM   1915 C C   . PRO A 1 250 ? 54.699 22.463  44.993 1.00 48.22  ? 250 PRO A C   1 
ATOM   1916 O O   . PRO A 1 250 ? 55.457 22.929  44.142 1.00 48.87  ? 250 PRO A O   1 
ATOM   1917 C CB  . PRO A 1 250 ? 55.031 24.616  46.185 1.00 48.62  ? 250 PRO A CB  1 
ATOM   1918 C CG  . PRO A 1 250 ? 56.509 24.613  46.330 1.00 48.47  ? 250 PRO A CG  1 
ATOM   1919 C CD  . PRO A 1 250 ? 56.874 23.476  47.246 1.00 48.62  ? 250 PRO A CD  1 
ATOM   1920 N N   . ASN A 1 251 ? 54.175 21.264  44.876 1.00 46.98  ? 251 ASN A N   1 
ATOM   1921 C CA  . ASN A 1 251 ? 54.095 20.525  43.619 1.00 45.62  ? 251 ASN A CA  1 
ATOM   1922 C C   . ASN A 1 251 ? 52.859 19.652  43.684 1.00 45.46  ? 251 ASN A C   1 
ATOM   1923 O O   . ASN A 1 251 ? 52.137 19.788  44.680 1.00 46.20  ? 251 ASN A O   1 
ATOM   1924 C CB  . ASN A 1 251 ? 55.388 19.798  43.399 1.00 41.45  ? 251 ASN A CB  1 
ATOM   1925 C CG  . ASN A 1 251 ? 55.707 18.739  44.441 1.00 41.17  ? 251 ASN A CG  1 
ATOM   1926 O OD1 . ASN A 1 251 ? 54.794 18.071  44.922 1.00 42.50  ? 251 ASN A OD1 1 
ATOM   1927 N ND2 . ASN A 1 251 ? 56.969 18.523  44.805 1.00 35.51  ? 251 ASN A ND2 1 
ATOM   1928 N N   . ILE A 1 252 ? 52.488 18.846  42.740 1.00 46.56  ? 252 ILE A N   1 
ATOM   1929 C CA  . ILE A 1 252 ? 51.277 18.032  42.819 1.00 48.47  ? 252 ILE A CA  1 
ATOM   1930 C C   . ILE A 1 252 ? 51.495 16.700  43.554 1.00 48.82  ? 252 ILE A C   1 
ATOM   1931 O O   . ILE A 1 252 ? 52.443 15.954  43.357 1.00 47.84  ? 252 ILE A O   1 
ATOM   1932 C CB  . ILE A 1 252 ? 50.607 17.792  41.464 1.00 51.08  ? 252 ILE A CB  1 
ATOM   1933 C CG1 . ILE A 1 252 ? 50.441 19.150  40.746 1.00 51.82  ? 252 ILE A CG1 1 
ATOM   1934 C CG2 . ILE A 1 252 ? 49.219 17.162  41.574 1.00 50.03  ? 252 ILE A CG2 1 
ATOM   1935 C CD1 . ILE A 1 252 ? 50.301 18.957  39.245 1.00 52.07  ? 252 ILE A CD1 1 
ATOM   1936 N N   . PRO A 1 253 ? 50.648 16.503  44.575 1.00 49.05  ? 253 PRO A N   1 
ATOM   1937 C CA  . PRO A 1 253 ? 50.708 15.312  45.406 1.00 48.58  ? 253 PRO A CA  1 
ATOM   1938 C C   . PRO A 1 253 ? 50.269 14.080  44.629 1.00 47.76  ? 253 PRO A C   1 
ATOM   1939 O O   . PRO A 1 253 ? 49.547 14.194  43.626 1.00 48.12  ? 253 PRO A O   1 
ATOM   1940 C CB  . PRO A 1 253 ? 49.747 15.630  46.555 1.00 48.83  ? 253 PRO A CB  1 
ATOM   1941 C CG  . PRO A 1 253 ? 48.781 16.620  45.993 1.00 49.16  ? 253 PRO A CG  1 
ATOM   1942 C CD  . PRO A 1 253 ? 49.488 17.372  44.910 1.00 48.46  ? 253 PRO A CD  1 
ATOM   1943 N N   . ASP A 1 254 ? 50.228 12.941  45.325 1.00 46.98  ? 254 ASP A N   1 
ATOM   1944 C CA  . ASP A 1 254 ? 49.927 11.698  44.585 1.00 44.90  ? 254 ASP A CA  1 
ATOM   1945 C C   . ASP A 1 254 ? 49.477 10.592  45.503 1.00 43.12  ? 254 ASP A C   1 
ATOM   1946 O O   . ASP A 1 254 ? 50.214 10.236  46.403 1.00 42.36  ? 254 ASP A O   1 
ATOM   1947 C CB  . ASP A 1 254 ? 51.336 11.447  44.007 1.00 49.41  ? 254 ASP A CB  1 
ATOM   1948 C CG  . ASP A 1 254 ? 51.447 10.121  43.319 1.00 51.25  ? 254 ASP A CG  1 
ATOM   1949 O OD1 . ASP A 1 254 ? 50.859 10.168  42.216 1.00 53.52  ? 254 ASP A OD1 1 
ATOM   1950 O OD2 . ASP A 1 254 ? 52.026 9.152   43.852 1.00 52.96  ? 254 ASP A OD2 1 
ATOM   1951 N N   . ILE A 1 255 ? 48.568 9.733   45.107 1.00 42.87  ? 255 ILE A N   1 
ATOM   1952 C CA  . ILE A 1 255 ? 48.154 8.579   45.883 1.00 42.57  ? 255 ILE A CA  1 
ATOM   1953 C C   . ILE A 1 255 ? 49.057 7.374   45.913 1.00 42.23  ? 255 ILE A C   1 
ATOM   1954 O O   . ILE A 1 255 ? 49.372 6.852   46.989 1.00 42.34  ? 255 ILE A O   1 
ATOM   1955 C CB  . ILE A 1 255 ? 46.683 8.226   45.620 1.00 40.10  ? 255 ILE A CB  1 
ATOM   1956 C CG1 . ILE A 1 255 ? 45.843 9.487   45.884 1.00 43.23  ? 255 ILE A CG1 1 
ATOM   1957 C CG2 . ILE A 1 255 ? 46.181 7.160   46.566 1.00 38.47  ? 255 ILE A CG2 1 
ATOM   1958 C CD1 . ILE A 1 255 ? 44.414 9.304   45.383 1.00 45.18  ? 255 ILE A CD1 1 
ATOM   1959 N N   . PRO A 1 256 ? 49.602 6.880   44.813 1.00 42.36  ? 256 PRO A N   1 
ATOM   1960 C CA  . PRO A 1 256 ? 50.482 5.722   44.769 1.00 41.37  ? 256 PRO A CA  1 
ATOM   1961 C C   . PRO A 1 256 ? 51.728 5.939   45.605 1.00 40.74  ? 256 PRO A C   1 
ATOM   1962 O O   . PRO A 1 256 ? 52.211 5.021   46.252 1.00 40.18  ? 256 PRO A O   1 
ATOM   1963 C CB  . PRO A 1 256 ? 50.871 5.555   43.298 1.00 41.33  ? 256 PRO A CB  1 
ATOM   1964 C CG  . PRO A 1 256 ? 49.815 6.289   42.540 1.00 40.95  ? 256 PRO A CG  1 
ATOM   1965 C CD  . PRO A 1 256 ? 49.359 7.411   43.430 1.00 41.83  ? 256 PRO A CD  1 
ATOM   1966 N N   . ALA A 1 257 ? 52.179 7.179   45.729 1.00 40.40  ? 257 ALA A N   1 
ATOM   1967 C CA  . ALA A 1 257 ? 53.265 7.584   46.601 1.00 39.89  ? 257 ALA A CA  1 
ATOM   1968 C C   . ALA A 1 257 ? 52.947 7.241   48.061 1.00 40.03  ? 257 ALA A C   1 
ATOM   1969 O O   . ALA A 1 257 ? 53.873 6.871   48.783 1.00 40.70  ? 257 ALA A O   1 
ATOM   1970 C CB  . ALA A 1 257 ? 53.580 9.063   46.443 1.00 33.53  ? 257 ALA A CB  1 
ATOM   1971 N N   . HIS A 1 258 ? 51.710 7.303   48.494 1.00 39.22  ? 258 HIS A N   1 
ATOM   1972 C CA  . HIS A 1 258 ? 51.242 6.939   49.817 1.00 38.93  ? 258 HIS A CA  1 
ATOM   1973 C C   . HIS A 1 258 ? 51.253 5.440   50.103 1.00 38.88  ? 258 HIS A C   1 
ATOM   1974 O O   . HIS A 1 258 ? 51.180 5.046   51.264 1.00 38.32  ? 258 HIS A O   1 
ATOM   1975 C CB  . HIS A 1 258 ? 49.751 7.344   49.921 1.00 35.92  ? 258 HIS A CB  1 
ATOM   1976 C CG  . HIS A 1 258 ? 49.121 7.248   51.264 1.00 33.72  ? 258 HIS A CG  1 
ATOM   1977 N ND1 . HIS A 1 258 ? 49.708 7.791   52.383 1.00 33.17  ? 258 HIS A ND1 1 
ATOM   1978 C CD2 . HIS A 1 258 ? 47.956 6.655   51.671 1.00 32.49  ? 258 HIS A CD2 1 
ATOM   1979 C CE1 . HIS A 1 258 ? 48.897 7.504   53.408 1.00 34.27  ? 258 HIS A CE1 1 
ATOM   1980 N NE2 . HIS A 1 258 ? 47.867 6.783   53.035 1.00 30.20  ? 258 HIS A NE2 1 
ATOM   1981 N N   . LEU A 1 259 ? 51.318 4.596   49.079 1.00 38.87  ? 259 LEU A N   1 
ATOM   1982 C CA  . LEU A 1 259 ? 51.133 3.159   49.310 1.00 38.85  ? 259 LEU A CA  1 
ATOM   1983 C C   . LEU A 1 259 ? 52.472 2.428   49.253 1.00 39.03  ? 259 LEU A C   1 
ATOM   1984 O O   . LEU A 1 259 ? 52.451 1.196   49.323 1.00 38.67  ? 259 LEU A O   1 
ATOM   1985 C CB  . LEU A 1 259 ? 50.207 2.566   48.251 1.00 34.14  ? 259 LEU A CB  1 
ATOM   1986 C CG  . LEU A 1 259 ? 48.813 3.207   48.173 1.00 33.80  ? 259 LEU A CG  1 
ATOM   1987 C CD1 . LEU A 1 259 ? 47.969 2.467   47.156 1.00 26.00  ? 259 LEU A CD1 1 
ATOM   1988 C CD2 . LEU A 1 259 ? 48.127 3.242   49.541 1.00 29.76  ? 259 LEU A CD2 1 
ATOM   1989 N N   . TRP A 1 260 ? 53.526 3.247   49.060 1.00 38.24  ? 260 TRP A N   1 
ATOM   1990 C CA  . TRP A 1 260 ? 54.845 2.667   48.982 1.00 37.36  ? 260 TRP A CA  1 
ATOM   1991 C C   . TRP A 1 260 ? 55.695 3.223   50.117 1.00 37.56  ? 260 TRP A C   1 
ATOM   1992 O O   . TRP A 1 260 ? 56.036 4.395   50.028 1.00 38.45  ? 260 TRP A O   1 
ATOM   1993 C CB  . TRP A 1 260 ? 55.521 2.934   47.636 1.00 33.71  ? 260 TRP A CB  1 
ATOM   1994 C CG  . TRP A 1 260 ? 56.799 2.146   47.510 1.00 32.36  ? 260 TRP A CG  1 
ATOM   1995 C CD1 . TRP A 1 260 ? 58.070 2.572   47.661 1.00 31.84  ? 260 TRP A CD1 1 
ATOM   1996 C CD2 . TRP A 1 260 ? 56.898 0.745   47.222 1.00 33.13  ? 260 TRP A CD2 1 
ATOM   1997 N NE1 . TRP A 1 260 ? 58.976 1.541   47.511 1.00 30.20  ? 260 TRP A NE1 1 
ATOM   1998 C CE2 . TRP A 1 260 ? 58.274 0.405   47.244 1.00 33.95  ? 260 TRP A CE2 1 
ATOM   1999 C CE3 . TRP A 1 260 ? 55.965 -0.251  46.938 1.00 32.07  ? 260 TRP A CE3 1 
ATOM   2000 C CZ2 . TRP A 1 260 ? 58.722 -0.889  46.968 1.00 31.37  ? 260 TRP A CZ2 1 
ATOM   2001 C CZ3 . TRP A 1 260 ? 56.397 -1.533  46.707 1.00 33.53  ? 260 TRP A CZ3 1 
ATOM   2002 C CH2 . TRP A 1 260 ? 57.775 -1.836  46.736 1.00 32.00  ? 260 TRP A CH2 1 
ATOM   2003 N N   . TYR A 1 261 ? 55.748 2.563   51.269 1.00 36.62  ? 261 TYR A N   1 
ATOM   2004 C CA  . TYR A 1 261 ? 56.647 2.963   52.346 1.00 35.28  ? 261 TYR A CA  1 
ATOM   2005 C C   . TYR A 1 261 ? 57.567 1.776   52.596 1.00 34.75  ? 261 TYR A C   1 
ATOM   2006 O O   . TYR A 1 261 ? 57.240 0.817   53.330 1.00 34.99  ? 261 TYR A O   1 
ATOM   2007 C CB  . TYR A 1 261 ? 55.896 3.305   53.644 1.00 35.91  ? 261 TYR A CB  1 
ATOM   2008 C CG  . TYR A 1 261 ? 55.508 4.766   53.663 1.00 36.04  ? 261 TYR A CG  1 
ATOM   2009 C CD1 . TYR A 1 261 ? 54.355 5.157   52.967 1.00 34.82  ? 261 TYR A CD1 1 
ATOM   2010 C CD2 . TYR A 1 261 ? 56.342 5.704   54.290 1.00 35.36  ? 261 TYR A CD2 1 
ATOM   2011 C CE1 . TYR A 1 261 ? 54.026 6.490   52.912 1.00 33.93  ? 261 TYR A CE1 1 
ATOM   2012 C CE2 . TYR A 1 261 ? 56.046 7.061   54.190 1.00 33.67  ? 261 TYR A CE2 1 
ATOM   2013 C CZ  . TYR A 1 261 ? 54.880 7.417   53.560 1.00 33.25  ? 261 TYR A CZ  1 
ATOM   2014 O OH  . TYR A 1 261 ? 54.450 8.688   53.378 1.00 31.29  ? 261 TYR A OH  1 
ATOM   2015 N N   . PHE A 1 262 ? 58.775 1.776   52.072 1.00 33.59  ? 262 PHE A N   1 
ATOM   2016 C CA  . PHE A 1 262 ? 59.707 0.673   52.154 1.00 34.10  ? 262 PHE A CA  1 
ATOM   2017 C C   . PHE A 1 262 ? 59.297 -0.556  51.352 1.00 33.69  ? 262 PHE A C   1 
ATOM   2018 O O   . PHE A 1 262 ? 60.150 -1.359  51.038 1.00 33.30  ? 262 PHE A O   1 
ATOM   2019 C CB  . PHE A 1 262 ? 60.095 0.149   53.545 1.00 33.20  ? 262 PHE A CB  1 
ATOM   2020 C CG  . PHE A 1 262 ? 60.838 1.235   54.301 1.00 32.71  ? 262 PHE A CG  1 
ATOM   2021 C CD1 . PHE A 1 262 ? 62.189 1.320   54.406 1.00 31.00  ? 262 PHE A CD1 1 
ATOM   2022 C CD2 . PHE A 1 262 ? 60.071 2.218   54.900 1.00 32.17  ? 262 PHE A CD2 1 
ATOM   2023 C CE1 . PHE A 1 262 ? 62.810 2.369   55.036 1.00 30.46  ? 262 PHE A CE1 1 
ATOM   2024 C CE2 . PHE A 1 262 ? 60.671 3.251   55.576 1.00 33.50  ? 262 PHE A CE2 1 
ATOM   2025 C CZ  . PHE A 1 262 ? 62.043 3.329   55.673 1.00 30.68  ? 262 PHE A CZ  1 
ATOM   2026 N N   . GLY A 1 263 ? 58.042 -0.839  51.200 1.00 34.01  ? 263 GLY A N   1 
ATOM   2027 C CA  . GLY A 1 263 ? 57.308 -1.804  50.487 1.00 34.62  ? 263 GLY A CA  1 
ATOM   2028 C C   . GLY A 1 263 ? 55.813 -1.483  50.393 1.00 34.90  ? 263 GLY A C   1 
ATOM   2029 O O   . GLY A 1 263 ? 55.351 -0.442  50.861 1.00 36.02  ? 263 GLY A O   1 
ATOM   2030 N N   . LEU A 1 264 ? 55.025 -2.411  49.883 1.00 34.70  ? 264 LEU A N   1 
ATOM   2031 C CA  . LEU A 1 264 ? 53.609 -2.199  49.639 1.00 35.03  ? 264 LEU A CA  1 
ATOM   2032 C C   . LEU A 1 264 ? 52.904 -1.947  50.945 1.00 34.69  ? 264 LEU A C   1 
ATOM   2033 O O   . LEU A 1 264 ? 53.165 -2.766  51.816 1.00 35.21  ? 264 LEU A O   1 
ATOM   2034 C CB  . LEU A 1 264 ? 52.989 -3.446  48.962 1.00 34.70  ? 264 LEU A CB  1 
ATOM   2035 C CG  . LEU A 1 264 ? 51.669 -3.151  48.266 1.00 33.92  ? 264 LEU A CG  1 
ATOM   2036 C CD1 . LEU A 1 264 ? 51.843 -1.947  47.315 1.00 36.18  ? 264 LEU A CD1 1 
ATOM   2037 C CD2 . LEU A 1 264 ? 51.221 -4.326  47.397 1.00 36.62  ? 264 LEU A CD2 1 
ATOM   2038 N N   . ILE A 1 265 ? 52.046 -0.978  51.084 1.00 35.33  ? 265 ILE A N   1 
ATOM   2039 C CA  . ILE A 1 265 ? 51.414 -0.655  52.368 1.00 36.38  ? 265 ILE A CA  1 
ATOM   2040 C C   . ILE A 1 265 ? 50.121 0.107   52.092 1.00 38.09  ? 265 ILE A C   1 
ATOM   2041 O O   . ILE A 1 265 ? 50.098 0.877   51.127 1.00 36.82  ? 265 ILE A O   1 
ATOM   2042 C CB  . ILE A 1 265 ? 52.354 0.190   53.234 1.00 34.06  ? 265 ILE A CB  1 
ATOM   2043 C CG1 . ILE A 1 265 ? 52.017 0.248   54.729 1.00 33.27  ? 265 ILE A CG1 1 
ATOM   2044 C CG2 . ILE A 1 265 ? 52.561 1.610   52.673 1.00 32.58  ? 265 ILE A CG2 1 
ATOM   2045 C CD1 . ILE A 1 265 ? 53.203 0.809   55.571 1.00 29.00  ? 265 ILE A CD1 1 
ATOM   2046 N N   . GLY A 1 266 ? 49.051 -0.310  52.803 1.00 40.23  ? 266 GLY A N   1 
ATOM   2047 C CA  . GLY A 1 266 ? 47.752 0.357   52.647 1.00 41.71  ? 266 GLY A CA  1 
ATOM   2048 C C   . GLY A 1 266 ? 46.887 -0.453  51.699 1.00 43.06  ? 266 GLY A C   1 
ATOM   2049 O O   . GLY A 1 266 ? 45.914 0.028   51.137 1.00 44.37  ? 266 GLY A O   1 
ATOM   2050 N N   . THR A 1 267 ? 47.399 -1.629  51.345 1.00 42.96  ? 267 THR A N   1 
ATOM   2051 C CA  . THR A 1 267 ? 46.755 -2.408  50.302 1.00 42.99  ? 267 THR A CA  1 
ATOM   2052 C C   . THR A 1 267 ? 47.412 -3.767  50.261 1.00 43.17  ? 267 THR A C   1 
ATOM   2053 O O   . THR A 1 267 ? 48.543 -3.896  50.722 1.00 43.22  ? 267 THR A O   1 
ATOM   2054 C CB  . THR A 1 267 ? 46.859 -1.684  48.949 1.00 44.52  ? 267 THR A CB  1 
ATOM   2055 O OG1 . THR A 1 267 ? 46.203 -2.525  47.990 1.00 44.60  ? 267 THR A OG1 1 
ATOM   2056 C CG2 . THR A 1 267 ? 48.301 -1.395  48.511 1.00 40.28  ? 267 THR A CG2 1 
ATOM   2057 N N   . CYS A 1 268 ? 46.646 -4.805  49.967 1.00 44.03  ? 268 CYS A N   1 
ATOM   2058 C CA  . CYS A 1 268 ? 47.206 -6.159  50.046 1.00 44.59  ? 268 CYS A CA  1 
ATOM   2059 C C   . CYS A 1 268 ? 47.180 -6.833  48.701 1.00 45.30  ? 268 CYS A C   1 
ATOM   2060 O O   . CYS A 1 268 ? 46.130 -6.784  48.052 1.00 46.11  ? 268 CYS A O   1 
ATOM   2061 C CB  . CYS A 1 268 ? 46.365 -6.921  51.073 1.00 45.02  ? 268 CYS A CB  1 
ATOM   2062 S SG  . CYS A 1 268 ? 46.360 -6.089  52.704 1.00 45.65  ? 268 CYS A SG  1 
ATOM   2063 N N   . LEU A 1 269 ? 48.295 -7.372  48.239 1.00 45.56  ? 269 LEU A N   1 
ATOM   2064 C CA  . LEU A 1 269 ? 48.316 -8.088  46.974 1.00 45.98  ? 269 LEU A CA  1 
ATOM   2065 C C   . LEU A 1 269 ? 47.402 -9.314  47.108 1.00 47.28  ? 269 LEU A C   1 
ATOM   2066 O O   . LEU A 1 269 ? 47.477 -9.966  48.183 1.00 47.90  ? 269 LEU A O   1 
ATOM   2067 C CB  . LEU A 1 269 ? 49.724 -8.577  46.677 1.00 43.67  ? 269 LEU A CB  1 
ATOM   2068 C CG  . LEU A 1 269 ? 50.763 -7.641  46.098 1.00 41.56  ? 269 LEU A CG  1 
ATOM   2069 C CD1 . LEU A 1 269 ? 51.895 -8.486  45.522 1.00 39.08  ? 269 LEU A CD1 1 
ATOM   2070 C CD2 . LEU A 1 269 ? 50.216 -6.727  45.004 1.00 40.04  ? 269 LEU A CD2 1 
ATOM   2071 O OXT . LEU A 1 269 ? 46.778 -9.724  46.101 1.00 48.55  ? 269 LEU A OXT 1 
ATOM   2072 N N   . GLU B 1 1   ? 50.878 54.212  47.595 1.00 55.87  ? 1   GLU B N   1 
ATOM   2073 C CA  . GLU B 1 1   ? 50.559 52.717  47.669 1.00 54.74  ? 1   GLU B CA  1 
ATOM   2074 C C   . GLU B 1 1   ? 49.767 52.367  46.439 1.00 52.43  ? 1   GLU B C   1 
ATOM   2075 O O   . GLU B 1 1   ? 50.361 51.756  45.538 1.00 52.80  ? 1   GLU B O   1 
ATOM   2076 C CB  . GLU B 1 1   ? 49.993 52.464  49.036 1.00 64.23  ? 1   GLU B CB  1 
ATOM   2077 C CG  . GLU B 1 1   ? 50.761 53.175  50.148 1.00 72.51  ? 1   GLU B CG  1 
ATOM   2078 C CD  . GLU B 1 1   ? 50.417 54.636  50.425 1.00 77.23  ? 1   GLU B CD  1 
ATOM   2079 O OE1 . GLU B 1 1   ? 50.024 55.428  49.522 1.00 78.03  ? 1   GLU B OE1 1 
ATOM   2080 O OE2 . GLU B 1 1   ? 50.497 55.040  51.630 1.00 76.25  ? 1   GLU B OE2 1 
ATOM   2081 N N   . VAL B 1 2   ? 48.557 52.861  46.251 1.00 49.69  ? 2   VAL B N   1 
ATOM   2082 C CA  . VAL B 1 2   ? 47.906 52.728  44.951 1.00 46.94  ? 2   VAL B CA  1 
ATOM   2083 C C   . VAL B 1 2   ? 47.323 54.129  44.684 1.00 46.46  ? 2   VAL B C   1 
ATOM   2084 O O   . VAL B 1 2   ? 47.154 54.884  45.653 1.00 46.55  ? 2   VAL B O   1 
ATOM   2085 C CB  . VAL B 1 2   ? 46.847 51.686  44.681 1.00 43.43  ? 2   VAL B CB  1 
ATOM   2086 C CG1 . VAL B 1 2   ? 47.388 50.275  44.644 1.00 39.71  ? 2   VAL B CG1 1 
ATOM   2087 C CG2 . VAL B 1 2   ? 45.629 51.832  45.590 1.00 40.55  ? 2   VAL B CG2 1 
ATOM   2088 N N   . SER B 1 3   ? 47.050 54.462  43.422 1.00 44.77  ? 3   SER B N   1 
ATOM   2089 C CA  . SER B 1 3   ? 46.543 55.814  43.148 1.00 42.30  ? 3   SER B CA  1 
ATOM   2090 C C   . SER B 1 3   ? 45.078 56.021  43.514 1.00 41.93  ? 3   SER B C   1 
ATOM   2091 O O   . SER B 1 3   ? 44.301 55.056  43.606 1.00 41.96  ? 3   SER B O   1 
ATOM   2092 C CB  . SER B 1 3   ? 46.698 56.111  41.665 1.00 36.01  ? 3   SER B CB  1 
ATOM   2093 O OG  . SER B 1 3   ? 45.780 55.362  40.897 1.00 31.69  ? 3   SER B OG  1 
ATOM   2094 N N   . GLN B 1 4   ? 44.669 57.280  43.665 1.00 40.38  ? 4   GLN B N   1 
ATOM   2095 C CA  . GLN B 1 4   ? 43.271 57.566  43.903 1.00 40.43  ? 4   GLN B CA  1 
ATOM   2096 C C   . GLN B 1 4   ? 42.418 56.981  42.768 1.00 39.44  ? 4   GLN B C   1 
ATOM   2097 O O   . GLN B 1 4   ? 41.406 56.312  42.976 1.00 38.02  ? 4   GLN B O   1 
ATOM   2098 C CB  . GLN B 1 4   ? 43.018 59.065  44.096 1.00 44.73  ? 4   GLN B CB  1 
ATOM   2099 C CG  . GLN B 1 4   ? 41.644 59.443  44.611 1.00 49.62  ? 4   GLN B CG  1 
ATOM   2100 C CD  . GLN B 1 4   ? 41.213 58.766  45.894 1.00 52.37  ? 4   GLN B CD  1 
ATOM   2101 O OE1 . GLN B 1 4   ? 40.098 58.266  46.070 1.00 53.29  ? 4   GLN B OE1 1 
ATOM   2102 N NE2 . GLN B 1 4   ? 42.073 58.671  46.909 1.00 55.10  ? 4   GLN B NE2 1 
ATOM   2103 N N   . ASP B 1 5   ? 42.819 57.172  41.508 1.00 38.83  ? 5   ASP B N   1 
ATOM   2104 C CA  . ASP B 1 5   ? 42.079 56.585  40.414 1.00 38.32  ? 5   ASP B CA  1 
ATOM   2105 C C   . ASP B 1 5   ? 41.983 55.078  40.623 1.00 37.61  ? 5   ASP B C   1 
ATOM   2106 O O   . ASP B 1 5   ? 40.863 54.601  40.806 1.00 36.58  ? 5   ASP B O   1 
ATOM   2107 C CB  . ASP B 1 5   ? 42.382 56.981  38.950 1.00 39.17  ? 5   ASP B CB  1 
ATOM   2108 C CG  . ASP B 1 5   ? 41.523 56.158  37.979 1.00 41.94  ? 5   ASP B CG  1 
ATOM   2109 O OD1 . ASP B 1 5   ? 40.267 56.261  37.941 1.00 40.30  ? 5   ASP B OD1 1 
ATOM   2110 O OD2 . ASP B 1 5   ? 42.164 55.330  37.290 1.00 43.82  ? 5   ASP B OD2 1 
ATOM   2111 N N   . LEU B 1 6   ? 43.060 54.320  40.760 1.00 37.69  ? 6   LEU B N   1 
ATOM   2112 C CA  . LEU B 1 6   ? 42.930 52.880  40.967 1.00 37.21  ? 6   LEU B CA  1 
ATOM   2113 C C   . LEU B 1 6   ? 42.143 52.516  42.214 1.00 36.39  ? 6   LEU B C   1 
ATOM   2114 O O   . LEU B 1 6   ? 41.338 51.577  42.160 1.00 36.58  ? 6   LEU B O   1 
ATOM   2115 C CB  . LEU B 1 6   ? 44.296 52.224  41.011 1.00 40.97  ? 6   LEU B CB  1 
ATOM   2116 C CG  . LEU B 1 6   ? 44.369 50.707  40.740 1.00 41.76  ? 6   LEU B CG  1 
ATOM   2117 C CD1 . LEU B 1 6   ? 43.607 50.301  39.488 1.00 39.08  ? 6   LEU B CD1 1 
ATOM   2118 C CD2 . LEU B 1 6   ? 45.860 50.378  40.567 1.00 36.23  ? 6   LEU B CD2 1 
ATOM   2119 N N   . PHE B 1 7   ? 42.294 53.259  43.305 1.00 35.03  ? 7   PHE B N   1 
ATOM   2120 C CA  . PHE B 1 7   ? 41.484 52.961  44.492 1.00 34.39  ? 7   PHE B CA  1 
ATOM   2121 C C   . PHE B 1 7   ? 40.001 53.125  44.181 1.00 34.01  ? 7   PHE B C   1 
ATOM   2122 O O   . PHE B 1 7   ? 39.213 52.205  44.440 1.00 34.70  ? 7   PHE B O   1 
ATOM   2123 C CB  . PHE B 1 7   ? 41.985 53.814  45.655 1.00 33.42  ? 7   PHE B CB  1 
ATOM   2124 C CG  . PHE B 1 7   ? 41.027 53.834  46.813 1.00 37.14  ? 7   PHE B CG  1 
ATOM   2125 C CD1 . PHE B 1 7   ? 41.236 52.950  47.878 1.00 37.25  ? 7   PHE B CD1 1 
ATOM   2126 C CD2 . PHE B 1 7   ? 39.926 54.697  46.843 1.00 33.57  ? 7   PHE B CD2 1 
ATOM   2127 C CE1 . PHE B 1 7   ? 40.370 52.947  48.954 1.00 36.58  ? 7   PHE B CE1 1 
ATOM   2128 C CE2 . PHE B 1 7   ? 39.072 54.658  47.922 1.00 33.06  ? 7   PHE B CE2 1 
ATOM   2129 C CZ  . PHE B 1 7   ? 39.284 53.796  48.981 1.00 32.93  ? 7   PHE B CZ  1 
ATOM   2130 N N   . ASN B 1 8   ? 39.568 54.179  43.503 1.00 33.16  ? 8   ASN B N   1 
ATOM   2131 C CA  . ASN B 1 8   ? 38.198 54.389  43.072 1.00 33.45  ? 8   ASN B CA  1 
ATOM   2132 C C   . ASN B 1 8   ? 37.672 53.191  42.288 1.00 33.87  ? 8   ASN B C   1 
ATOM   2133 O O   . ASN B 1 8   ? 36.616 52.618  42.620 1.00 34.92  ? 8   ASN B O   1 
ATOM   2134 C CB  . ASN B 1 8   ? 38.010 55.708  42.297 1.00 29.03  ? 8   ASN B CB  1 
ATOM   2135 C CG  . ASN B 1 8   ? 38.184 56.865  43.241 1.00 31.27  ? 8   ASN B CG  1 
ATOM   2136 O OD1 . ASN B 1 8   ? 38.030 56.678  44.459 1.00 35.47  ? 8   ASN B OD1 1 
ATOM   2137 N ND2 . ASN B 1 8   ? 38.610 58.068  42.885 1.00 31.84  ? 8   ASN B ND2 1 
ATOM   2138 N N   . GLN B 1 9   ? 38.455 52.663  41.355 1.00 33.02  ? 9   GLN B N   1 
ATOM   2139 C CA  . GLN B 1 9   ? 38.047 51.529  40.579 1.00 32.87  ? 9   GLN B CA  1 
ATOM   2140 C C   . GLN B 1 9   ? 38.075 50.194  41.356 1.00 32.16  ? 9   GLN B C   1 
ATOM   2141 O O   . GLN B 1 9   ? 37.156 49.369  41.245 1.00 29.50  ? 9   GLN B O   1 
ATOM   2142 C CB  . GLN B 1 9   ? 38.795 51.411  39.293 1.00 32.40  ? 9   GLN B CB  1 
ATOM   2143 C CG  . GLN B 1 9   ? 39.504 52.442  38.537 1.00 35.42  ? 9   GLN B CG  1 
ATOM   2144 C CD  . GLN B 1 9   ? 40.110 51.969  37.227 1.00 39.08  ? 9   GLN B CD  1 
ATOM   2145 O OE1 . GLN B 1 9   ? 39.796 50.900  36.702 1.00 41.51  ? 9   GLN B OE1 1 
ATOM   2146 N NE2 . GLN B 1 9   ? 40.916 52.814  36.587 1.00 41.53  ? 9   GLN B NE2 1 
ATOM   2147 N N   . PHE B 1 10  ? 39.037 50.021  42.253 1.00 32.23  ? 10  PHE B N   1 
ATOM   2148 C CA  . PHE B 1 10  ? 39.001 48.833  43.130 1.00 33.07  ? 10  PHE B CA  1 
ATOM   2149 C C   . PHE B 1 10  ? 37.703 48.814  43.927 1.00 33.52  ? 10  PHE B C   1 
ATOM   2150 O O   . PHE B 1 10  ? 36.987 47.795  43.992 1.00 31.81  ? 10  PHE B O   1 
ATOM   2151 C CB  . PHE B 1 10  ? 40.247 48.809  44.049 1.00 34.28  ? 10  PHE B CB  1 
ATOM   2152 C CG  . PHE B 1 10  ? 41.530 48.353  43.379 1.00 30.90  ? 10  PHE B CG  1 
ATOM   2153 C CD1 . PHE B 1 10  ? 41.606 48.003  42.055 1.00 31.11  ? 10  PHE B CD1 1 
ATOM   2154 C CD2 . PHE B 1 10  ? 42.706 48.277  44.094 1.00 30.78  ? 10  PHE B CD2 1 
ATOM   2155 C CE1 . PHE B 1 10  ? 42.793 47.598  41.448 1.00 31.48  ? 10  PHE B CE1 1 
ATOM   2156 C CE2 . PHE B 1 10  ? 43.904 47.863  43.555 1.00 28.49  ? 10  PHE B CE2 1 
ATOM   2157 C CZ  . PHE B 1 10  ? 43.950 47.531  42.204 1.00 29.76  ? 10  PHE B CZ  1 
ATOM   2158 N N   . ASN B 1 11  ? 37.341 49.996  44.488 1.00 33.36  ? 11  ASN B N   1 
ATOM   2159 C CA  . ASN B 1 11  ? 36.118 50.113  45.293 1.00 33.12  ? 11  ASN B CA  1 
ATOM   2160 C C   . ASN B 1 11  ? 34.797 49.902  44.613 1.00 32.87  ? 11  ASN B C   1 
ATOM   2161 O O   . ASN B 1 11  ? 33.809 49.320  45.067 1.00 32.41  ? 11  ASN B O   1 
ATOM   2162 C CB  . ASN B 1 11  ? 36.203 51.492  45.944 1.00 38.24  ? 11  ASN B CB  1 
ATOM   2163 C CG  . ASN B 1 11  ? 35.134 51.801  46.965 1.00 39.72  ? 11  ASN B CG  1 
ATOM   2164 O OD1 . ASN B 1 11  ? 34.872 51.080  47.930 1.00 41.78  ? 11  ASN B OD1 1 
ATOM   2165 N ND2 . ASN B 1 11  ? 34.464 52.924  46.720 1.00 38.81  ? 11  ASN B ND2 1 
ATOM   2166 N N   . LEU B 1 12  ? 34.725 50.341  43.359 1.00 34.00  ? 12  LEU B N   1 
ATOM   2167 C CA  . LEU B 1 12  ? 33.551 50.203  42.513 1.00 34.05  ? 12  LEU B CA  1 
ATOM   2168 C C   . LEU B 1 12  ? 33.405 48.772  41.993 1.00 35.31  ? 12  LEU B C   1 
ATOM   2169 O O   . LEU B 1 12  ? 32.255 48.284  41.969 1.00 35.72  ? 12  LEU B O   1 
ATOM   2170 C CB  . LEU B 1 12  ? 33.641 51.184  41.352 1.00 31.20  ? 12  LEU B CB  1 
ATOM   2171 C CG  . LEU B 1 12  ? 32.490 51.048  40.325 1.00 30.84  ? 12  LEU B CG  1 
ATOM   2172 C CD1 . LEU B 1 12  ? 31.173 51.433  40.972 1.00 27.33  ? 12  LEU B CD1 1 
ATOM   2173 C CD2 . LEU B 1 12  ? 32.823 51.814  39.080 1.00 22.85  ? 12  LEU B CD2 1 
ATOM   2174 N N   . PHE B 1 13  ? 34.513 48.032  41.843 1.00 35.03  ? 13  PHE B N   1 
ATOM   2175 C CA  . PHE B 1 13  ? 34.325 46.644  41.393 1.00 35.95  ? 13  PHE B CA  1 
ATOM   2176 C C   . PHE B 1 13  ? 34.089 45.718  42.587 1.00 36.12  ? 13  PHE B C   1 
ATOM   2177 O O   . PHE B 1 13  ? 33.354 44.716  42.542 1.00 35.44  ? 13  PHE B O   1 
ATOM   2178 C CB  . PHE B 1 13  ? 35.371 46.205  40.372 1.00 34.14  ? 13  PHE B CB  1 
ATOM   2179 C CG  . PHE B 1 13  ? 35.309 47.042  39.105 1.00 32.73  ? 13  PHE B CG  1 
ATOM   2180 C CD1 . PHE B 1 13  ? 34.219 46.993  38.266 1.00 32.64  ? 13  PHE B CD1 1 
ATOM   2181 C CD2 . PHE B 1 13  ? 36.354 47.896  38.823 1.00 30.83  ? 13  PHE B CD2 1 
ATOM   2182 C CE1 . PHE B 1 13  ? 34.125 47.813  37.140 1.00 33.93  ? 13  PHE B CE1 1 
ATOM   2183 C CE2 . PHE B 1 13  ? 36.262 48.725  37.734 1.00 35.21  ? 13  PHE B CE2 1 
ATOM   2184 C CZ  . PHE B 1 13  ? 35.167 48.676  36.852 1.00 34.04  ? 13  PHE B CZ  1 
ATOM   2185 N N   . ALA B 1 14  ? 34.405 46.247  43.776 1.00 36.25  ? 14  ALA B N   1 
ATOM   2186 C CA  . ALA B 1 14  ? 34.045 45.518  45.001 1.00 37.29  ? 14  ALA B CA  1 
ATOM   2187 C C   . ALA B 1 14  ? 32.546 45.624  45.239 1.00 37.77  ? 14  ALA B C   1 
ATOM   2188 O O   . ALA B 1 14  ? 31.916 44.602  45.516 1.00 36.81  ? 14  ALA B O   1 
ATOM   2189 C CB  . ALA B 1 14  ? 34.875 45.931  46.182 1.00 36.32  ? 14  ALA B CB  1 
ATOM   2190 N N   . GLN B 1 15  ? 31.931 46.767  44.853 1.00 38.72  ? 15  GLN B N   1 
ATOM   2191 C CA  . GLN B 1 15  ? 30.477 46.871  45.042 1.00 37.89  ? 15  GLN B CA  1 
ATOM   2192 C C   . GLN B 1 15  ? 29.696 46.147  43.974 1.00 37.57  ? 15  GLN B C   1 
ATOM   2193 O O   . GLN B 1 15  ? 28.636 45.580  44.253 1.00 37.83  ? 15  GLN B O   1 
ATOM   2194 C CB  . GLN B 1 15  ? 30.030 48.319  45.202 1.00 37.89  ? 15  GLN B CB  1 
ATOM   2195 C CG  . GLN B 1 15  ? 30.714 48.988  46.372 1.00 38.74  ? 15  GLN B CG  1 
ATOM   2196 C CD  . GLN B 1 15  ? 30.413 50.437  46.577 1.00 38.80  ? 15  GLN B CD  1 
ATOM   2197 O OE1 . GLN B 1 15  ? 29.506 51.041  46.010 1.00 42.12  ? 15  GLN B OE1 1 
ATOM   2198 N NE2 . GLN B 1 15  ? 31.222 51.074  47.402 1.00 39.87  ? 15  GLN B NE2 1 
ATOM   2199 N N   . TYR B 1 16  ? 30.187 46.155  42.741 1.00 37.37  ? 16  TYR B N   1 
ATOM   2200 C CA  . TYR B 1 16  ? 29.579 45.372  41.646 1.00 36.47  ? 16  TYR B CA  1 
ATOM   2201 C C   . TYR B 1 16  ? 29.726 43.894  42.038 1.00 36.01  ? 16  TYR B C   1 
ATOM   2202 O O   . TYR B 1 16  ? 28.741 43.150  41.957 1.00 35.52  ? 16  TYR B O   1 
ATOM   2203 C CB  . TYR B 1 16  ? 30.133 45.663  40.241 1.00 35.23  ? 16  TYR B CB  1 
ATOM   2204 C CG  . TYR B 1 16  ? 29.602 46.836  39.421 1.00 33.21  ? 16  TYR B CG  1 
ATOM   2205 C CD1 . TYR B 1 16  ? 28.404 46.738  38.699 1.00 33.58  ? 16  TYR B CD1 1 
ATOM   2206 C CD2 . TYR B 1 16  ? 30.377 47.956  39.187 1.00 32.07  ? 16  TYR B CD2 1 
ATOM   2207 C CE1 . TYR B 1 16  ? 27.951 47.780  37.946 1.00 33.36  ? 16  TYR B CE1 1 
ATOM   2208 C CE2 . TYR B 1 16  ? 29.967 49.063  38.469 1.00 32.78  ? 16  TYR B CE2 1 
ATOM   2209 C CZ  . TYR B 1 16  ? 28.729 48.922  37.798 1.00 33.84  ? 16  TYR B CZ  1 
ATOM   2210 O OH  . TYR B 1 16  ? 28.286 49.979  37.029 1.00 31.99  ? 16  TYR B OH  1 
ATOM   2211 N N   . SER B 1 17  ? 30.844 43.490  42.655 1.00 35.31  ? 17  SER B N   1 
ATOM   2212 C CA  . SER B 1 17  ? 30.955 42.131  43.181 1.00 36.04  ? 17  SER B CA  1 
ATOM   2213 C C   . SER B 1 17  ? 30.040 41.897  44.400 1.00 36.61  ? 17  SER B C   1 
ATOM   2214 O O   . SER B 1 17  ? 29.080 41.115  44.270 1.00 36.29  ? 17  SER B O   1 
ATOM   2215 C CB  . SER B 1 17  ? 32.432 41.879  43.519 1.00 36.24  ? 17  SER B CB  1 
ATOM   2216 O OG  . SER B 1 17  ? 33.192 41.659  42.347 1.00 32.44  ? 17  SER B OG  1 
ATOM   2217 N N   . ALA B 1 18  ? 29.829 42.926  45.240 1.00 36.78  ? 18  ALA B N   1 
ATOM   2218 C CA  . ALA B 1 18  ? 28.875 42.794  46.322 1.00 39.44  ? 18  ALA B CA  1 
ATOM   2219 C C   . ALA B 1 18  ? 27.439 42.688  45.818 1.00 40.28  ? 18  ALA B C   1 
ATOM   2220 O O   . ALA B 1 18  ? 26.670 41.789  46.245 1.00 41.32  ? 18  ALA B O   1 
ATOM   2221 C CB  . ALA B 1 18  ? 28.940 43.802  47.457 1.00 40.26  ? 18  ALA B CB  1 
ATOM   2222 N N   . ALA B 1 19  ? 27.119 43.463  44.800 1.00 39.58  ? 19  ALA B N   1 
ATOM   2223 C CA  . ALA B 1 19  ? 25.760 43.483  44.232 1.00 38.68  ? 19  ALA B CA  1 
ATOM   2224 C C   . ALA B 1 19  ? 25.296 42.134  43.721 1.00 38.60  ? 19  ALA B C   1 
ATOM   2225 O O   . ALA B 1 19  ? 24.106 41.855  43.633 1.00 36.99  ? 19  ALA B O   1 
ATOM   2226 C CB  . ALA B 1 19  ? 25.703 44.460  43.058 1.00 34.13  ? 19  ALA B CB  1 
ATOM   2227 N N   . ALA B 1 20  ? 26.259 41.284  43.333 1.00 39.99  ? 20  ALA B N   1 
ATOM   2228 C CA  . ALA B 1 20  ? 25.962 39.929  42.880 1.00 40.64  ? 20  ALA B CA  1 
ATOM   2229 C C   . ALA B 1 20  ? 25.336 39.130  44.023 1.00 41.57  ? 20  ALA B C   1 
ATOM   2230 O O   . ALA B 1 20  ? 24.708 38.126  43.734 1.00 40.92  ? 20  ALA B O   1 
ATOM   2231 C CB  . ALA B 1 20  ? 27.184 39.191  42.385 1.00 36.26  ? 20  ALA B CB  1 
ATOM   2232 N N   . TYR B 1 21  ? 25.689 39.411  45.286 1.00 43.16  ? 21  TYR B N   1 
ATOM   2233 C CA  . TYR B 1 21  ? 24.945 38.709  46.325 1.00 44.78  ? 21  TYR B CA  1 
ATOM   2234 C C   . TYR B 1 21  ? 23.727 39.487  46.841 1.00 47.02  ? 21  TYR B C   1 
ATOM   2235 O O   . TYR B 1 21  ? 22.822 38.820  47.327 1.00 46.18  ? 21  TYR B O   1 
ATOM   2236 C CB  . TYR B 1 21  ? 25.789 38.339  47.500 1.00 41.15  ? 21  TYR B CB  1 
ATOM   2237 C CG  . TYR B 1 21  ? 27.122 37.698  47.380 1.00 38.19  ? 21  TYR B CG  1 
ATOM   2238 C CD1 . TYR B 1 21  ? 27.274 36.330  47.591 1.00 36.86  ? 21  TYR B CD1 1 
ATOM   2239 C CD2 . TYR B 1 21  ? 28.250 38.436  47.056 1.00 37.26  ? 21  TYR B CD2 1 
ATOM   2240 C CE1 . TYR B 1 21  ? 28.507 35.725  47.511 1.00 35.89  ? 21  TYR B CE1 1 
ATOM   2241 C CE2 . TYR B 1 21  ? 29.491 37.850  46.960 1.00 36.61  ? 21  TYR B CE2 1 
ATOM   2242 C CZ  . TYR B 1 21  ? 29.609 36.493  47.211 1.00 36.92  ? 21  TYR B CZ  1 
ATOM   2243 O OH  . TYR B 1 21  ? 30.856 35.893  47.135 1.00 36.57  ? 21  TYR B OH  1 
ATOM   2244 N N   . CYS B 1 22  ? 23.756 40.809  46.853 1.00 50.68  ? 22  CYS B N   1 
ATOM   2245 C CA  . CYS B 1 22  ? 22.898 41.588  47.687 1.00 55.86  ? 22  CYS B CA  1 
ATOM   2246 C C   . CYS B 1 22  ? 21.938 42.559  47.069 1.00 60.63  ? 22  CYS B C   1 
ATOM   2247 O O   . CYS B 1 22  ? 21.765 43.658  47.629 1.00 61.24  ? 22  CYS B O   1 
ATOM   2248 C CB  . CYS B 1 22  ? 23.681 42.443  48.730 1.00 48.90  ? 22  CYS B CB  1 
ATOM   2249 S SG  . CYS B 1 22  ? 24.646 41.479  49.831 1.00 46.21  ? 22  CYS B SG  1 
ATOM   2250 N N   . GLY B 1 23  ? 21.167 42.154  46.065 1.00 66.24  ? 23  GLY B N   1 
ATOM   2251 C CA  . GLY B 1 23  ? 20.120 43.152  45.788 1.00 73.37  ? 23  GLY B CA  1 
ATOM   2252 C C   . GLY B 1 23  ? 19.332 42.921  44.571 1.00 77.69  ? 23  GLY B C   1 
ATOM   2253 O O   . GLY B 1 23  ? 19.840 43.358  43.531 1.00 78.36  ? 23  GLY B O   1 
ATOM   2254 N N   . LYS B 1 24  ? 18.279 42.115  44.566 1.00 82.10  ? 24  LYS B N   1 
ATOM   2255 C CA  . LYS B 1 24  ? 17.387 41.979  43.409 1.00 87.14  ? 24  LYS B CA  1 
ATOM   2256 C C   . LYS B 1 24  ? 18.009 41.457  42.127 1.00 90.14  ? 24  LYS B C   1 
ATOM   2257 O O   . LYS B 1 24  ? 17.439 41.016  41.124 1.00 90.60  ? 24  LYS B O   1 
ATOM   2258 C CB  . LYS B 1 24  ? 16.640 43.302  43.170 1.00 88.22  ? 24  LYS B CB  1 
ATOM   2259 C CG  . LYS B 1 24  ? 15.867 43.812  44.391 1.00 89.47  ? 24  LYS B CG  1 
ATOM   2260 C CD  . LYS B 1 24  ? 16.520 45.068  44.950 1.00 89.98  ? 24  LYS B CD  1 
ATOM   2261 C CE  . LYS B 1 24  ? 16.021 45.424  46.334 1.00 90.54  ? 24  LYS B CE  1 
ATOM   2262 N NZ  . LYS B 1 24  ? 16.818 46.537  46.932 1.00 90.97  ? 24  LYS B NZ  1 
ATOM   2263 N N   . ASN B 1 25  ? 19.299 41.357  42.067 1.00 93.21  ? 25  ASN B N   1 
ATOM   2264 C CA  . ASN B 1 25  ? 20.387 40.945  41.280 1.00 96.50  ? 25  ASN B CA  1 
ATOM   2265 C C   . ASN B 1 25  ? 20.118 39.699  40.432 1.00 98.12  ? 25  ASN B C   1 
ATOM   2266 O O   . ASN B 1 25  ? 20.126 39.607  39.221 1.00 97.91  ? 25  ASN B O   1 
ATOM   2267 C CB  . ASN B 1 25  ? 21.464 40.498  42.341 1.00 100.06 ? 25  ASN B CB  1 
ATOM   2268 C CG  . ASN B 1 25  ? 22.707 40.073  41.575 1.00 102.38 ? 25  ASN B CG  1 
ATOM   2269 O OD1 . ASN B 1 25  ? 23.212 41.027  40.992 1.00 104.81 ? 25  ASN B OD1 1 
ATOM   2270 N ND2 . ASN B 1 25  ? 23.096 38.811  41.571 1.00 102.15 ? 25  ASN B ND2 1 
ATOM   2271 N N   . ASN B 1 26  ? 19.898 38.670  41.245 1.00 99.63  ? 26  ASN B N   1 
ATOM   2272 C CA  . ASN B 1 26  ? 19.746 37.276  40.872 1.00 100.68 ? 26  ASN B CA  1 
ATOM   2273 C C   . ASN B 1 26  ? 18.794 37.184  39.695 1.00 100.90 ? 26  ASN B C   1 
ATOM   2274 O O   . ASN B 1 26  ? 19.286 36.734  38.633 1.00 100.50 ? 26  ASN B O   1 
ATOM   2275 C CB  . ASN B 1 26  ? 19.522 36.504  42.175 1.00 102.55 ? 26  ASN B CB  1 
ATOM   2276 C CG  . ASN B 1 26  ? 20.276 37.045  43.387 1.00 103.68 ? 26  ASN B CG  1 
ATOM   2277 O OD1 . ASN B 1 26  ? 21.375 36.632  43.783 1.00 103.34 ? 26  ASN B OD1 1 
ATOM   2278 N ND2 . ASN B 1 26  ? 19.715 38.037  44.080 1.00 103.84 ? 26  ASN B ND2 1 
ATOM   2279 N N   . ASP B 1 27  ? 17.547 37.684  39.736 1.00 100.85 ? 27  ASP B N   1 
ATOM   2280 C CA  . ASP B 1 27  ? 16.688 37.609  38.564 1.00 100.82 ? 27  ASP B CA  1 
ATOM   2281 C C   . ASP B 1 27  ? 15.599 38.664  38.376 1.00 100.49 ? 27  ASP B C   1 
ATOM   2282 O O   . ASP B 1 27  ? 14.534 38.427  37.775 1.00 100.21 ? 27  ASP B O   1 
ATOM   2283 C CB  . ASP B 1 27  ? 16.117 36.200  38.337 1.00 101.36 ? 27  ASP B CB  1 
ATOM   2284 C CG  . ASP B 1 27  ? 16.784 35.520  37.150 1.00 101.09 ? 27  ASP B CG  1 
ATOM   2285 O OD1 . ASP B 1 27  ? 18.019 35.322  37.195 1.00 100.38 ? 27  ASP B OD1 1 
ATOM   2286 O OD2 . ASP B 1 27  ? 16.037 35.213  36.203 1.00 101.48 ? 27  ASP B OD2 1 
ATOM   2287 N N   . ALA B 1 28  ? 15.986 39.915  38.684 1.00 99.67  ? 28  ALA B N   1 
ATOM   2288 C CA  . ALA B 1 28  ? 15.194 41.096  38.369 1.00 98.46  ? 28  ALA B CA  1 
ATOM   2289 C C   . ALA B 1 28  ? 15.086 41.265  36.850 1.00 97.26  ? 28  ALA B C   1 
ATOM   2290 O O   . ALA B 1 28  ? 15.895 40.760  36.066 1.00 97.99  ? 28  ALA B O   1 
ATOM   2291 C CB  . ALA B 1 28  ? 15.858 42.360  38.917 1.00 98.08  ? 28  ALA B CB  1 
ATOM   2292 N N   . PRO B 1 29  ? 14.107 42.041  36.405 1.00 95.76  ? 29  PRO B N   1 
ATOM   2293 C CA  . PRO B 1 29  ? 13.858 42.288  34.996 1.00 94.00  ? 29  PRO B CA  1 
ATOM   2294 C C   . PRO B 1 29  ? 14.873 43.169  34.290 1.00 91.84  ? 29  PRO B C   1 
ATOM   2295 O O   . PRO B 1 29  ? 15.223 44.274  34.714 1.00 91.43  ? 29  PRO B O   1 
ATOM   2296 C CB  . PRO B 1 29  ? 12.466 42.908  34.965 1.00 94.44  ? 29  PRO B CB  1 
ATOM   2297 C CG  . PRO B 1 29  ? 12.208 43.414  36.332 1.00 95.28  ? 29  PRO B CG  1 
ATOM   2298 C CD  . PRO B 1 29  ? 13.102 42.679  37.295 1.00 95.68  ? 29  PRO B CD  1 
ATOM   2299 N N   . ALA B 1 30  ? 15.140 42.874  33.019 1.00 89.20  ? 30  ALA B N   1 
ATOM   2300 C CA  . ALA B 1 30  ? 16.139 43.552  32.206 1.00 85.90  ? 30  ALA B CA  1 
ATOM   2301 C C   . ALA B 1 30  ? 15.891 45.009  31.849 1.00 83.32  ? 30  ALA B C   1 
ATOM   2302 O O   . ALA B 1 30  ? 14.874 45.408  31.283 1.00 83.50  ? 30  ALA B O   1 
ATOM   2303 C CB  . ALA B 1 30  ? 16.386 42.740  30.939 1.00 84.69  ? 30  ALA B CB  1 
ATOM   2304 N N   . GLY B 1 31  ? 16.896 45.861  32.062 1.00 80.27  ? 31  GLY B N   1 
ATOM   2305 C CA  . GLY B 1 31  ? 16.853 47.294  31.862 1.00 75.62  ? 31  GLY B CA  1 
ATOM   2306 C C   . GLY B 1 31  ? 16.656 48.041  33.180 1.00 72.86  ? 31  GLY B C   1 
ATOM   2307 O O   . GLY B 1 31  ? 16.546 49.263  33.262 1.00 72.25  ? 31  GLY B O   1 
ATOM   2308 N N   . THR B 1 32  ? 16.506 47.301  34.261 1.00 69.98  ? 32  THR B N   1 
ATOM   2309 C CA  . THR B 1 32  ? 16.292 47.830  35.607 1.00 67.16  ? 32  THR B CA  1 
ATOM   2310 C C   . THR B 1 32  ? 17.551 48.409  36.229 1.00 64.34  ? 32  THR B C   1 
ATOM   2311 O O   . THR B 1 32  ? 18.661 48.035  35.862 1.00 63.79  ? 32  THR B O   1 
ATOM   2312 C CB  . THR B 1 32  ? 15.769 46.605  36.398 1.00 68.83  ? 32  THR B CB  1 
ATOM   2313 O OG1 . THR B 1 32  ? 14.425 46.338  35.954 1.00 70.44  ? 32  THR B OG1 1 
ATOM   2314 C CG2 . THR B 1 32  ? 15.882 46.649  37.892 1.00 66.30  ? 32  THR B CG2 1 
ATOM   2315 N N   . ASN B 1 33  ? 17.462 49.398  37.085 1.00 61.63  ? 33  ASN B N   1 
ATOM   2316 C CA  . ASN B 1 33  ? 18.529 49.945  37.891 1.00 59.46  ? 33  ASN B CA  1 
ATOM   2317 C C   . ASN B 1 33  ? 19.070 48.992  38.951 1.00 56.71  ? 33  ASN B C   1 
ATOM   2318 O O   . ASN B 1 33  ? 18.209 48.456  39.651 1.00 57.01  ? 33  ASN B O   1 
ATOM   2319 C CB  . ASN B 1 33  ? 18.151 51.226  38.707 1.00 58.85  ? 33  ASN B CB  1 
ATOM   2320 C CG  . ASN B 1 33  ? 18.025 52.266  37.604 1.00 62.12  ? 33  ASN B CG  1 
ATOM   2321 O OD1 . ASN B 1 33  ? 17.217 51.963  36.712 1.00 64.22  ? 33  ASN B OD1 1 
ATOM   2322 N ND2 . ASN B 1 33  ? 18.802 53.316  37.405 1.00 63.02  ? 33  ASN B ND2 1 
ATOM   2323 N N   . ILE B 1 34  ? 20.353 48.712  38.916 1.00 53.62  ? 34  ILE B N   1 
ATOM   2324 C CA  . ILE B 1 34  ? 20.965 47.807  39.868 1.00 51.68  ? 34  ILE B CA  1 
ATOM   2325 C C   . ILE B 1 34  ? 21.025 48.501  41.229 1.00 50.38  ? 34  ILE B C   1 
ATOM   2326 O O   . ILE B 1 34  ? 21.270 49.710  41.265 1.00 49.29  ? 34  ILE B O   1 
ATOM   2327 C CB  . ILE B 1 34  ? 22.411 47.395  39.466 1.00 49.21  ? 34  ILE B CB  1 
ATOM   2328 C CG1 . ILE B 1 34  ? 22.349 46.847  38.052 1.00 49.78  ? 34  ILE B CG1 1 
ATOM   2329 C CG2 . ILE B 1 34  ? 22.995 46.361  40.398 1.00 45.68  ? 34  ILE B CG2 1 
ATOM   2330 C CD1 . ILE B 1 34  ? 23.617 46.262  37.475 1.00 49.77  ? 34  ILE B CD1 1 
ATOM   2331 N N   . THR B 1 35  ? 20.318 47.965  42.229 1.00 49.78  ? 35  THR B N   1 
ATOM   2332 C CA  . THR B 1 35  ? 20.377 48.521  43.588 1.00 48.84  ? 35  THR B CA  1 
ATOM   2333 C C   . THR B 1 35  ? 20.571 47.360  44.570 1.00 47.95  ? 35  THR B C   1 
ATOM   2334 O O   . THR B 1 35  ? 20.418 46.182  44.212 1.00 48.03  ? 35  THR B O   1 
ATOM   2335 C CB  . THR B 1 35  ? 19.106 49.286  43.973 1.00 48.75  ? 35  THR B CB  1 
ATOM   2336 O OG1 . THR B 1 35  ? 18.056 48.303  43.980 1.00 48.54  ? 35  THR B OG1 1 
ATOM   2337 C CG2 . THR B 1 35  ? 18.750 50.380  42.982 1.00 46.24  ? 35  THR B CG2 1 
ATOM   2338 N N   . CYS B 1 36  ? 21.123 47.646  45.747 1.00 46.31  ? 36  CYS B N   1 
ATOM   2339 C CA  . CYS B 1 36  ? 21.365 46.546  46.688 1.00 44.36  ? 36  CYS B CA  1 
ATOM   2340 C C   . CYS B 1 36  ? 20.617 46.763  47.992 1.00 43.60  ? 36  CYS B C   1 
ATOM   2341 O O   . CYS B 1 36  ? 20.225 47.872  48.363 1.00 43.76  ? 36  CYS B O   1 
ATOM   2342 C CB  . CYS B 1 36  ? 22.885 46.462  46.959 1.00 39.91  ? 36  CYS B CB  1 
ATOM   2343 S SG  . CYS B 1 36  ? 23.959 46.223  45.549 1.00 38.52  ? 36  CYS B SG  1 
ATOM   2344 N N   . THR B 1 37  ? 20.603 45.766  48.872 1.00 43.31  ? 37  THR B N   1 
ATOM   2345 C CA  . THR B 1 37  ? 20.042 46.034  50.213 1.00 42.53  ? 37  THR B CA  1 
ATOM   2346 C C   . THR B 1 37  ? 21.223 46.406  51.086 1.00 44.05  ? 37  THR B C   1 
ATOM   2347 O O   . THR B 1 37  ? 22.378 46.319  50.609 1.00 44.43  ? 37  THR B O   1 
ATOM   2348 C CB  . THR B 1 37  ? 19.347 44.781  50.719 1.00 38.00  ? 37  THR B CB  1 
ATOM   2349 O OG1 . THR B 1 37  ? 20.305 43.728  50.503 1.00 36.28  ? 37  THR B OG1 1 
ATOM   2350 C CG2 . THR B 1 37  ? 18.026 44.505  50.017 1.00 28.69  ? 37  THR B CG2 1 
ATOM   2351 N N   . GLY B 1 38  ? 20.970 46.923  52.286 1.00 44.14  ? 38  GLY B N   1 
ATOM   2352 C CA  . GLY B 1 38  ? 21.988 47.265  53.244 1.00 44.22  ? 38  GLY B CA  1 
ATOM   2353 C C   . GLY B 1 38  ? 23.205 48.063  52.921 1.00 45.00  ? 38  GLY B C   1 
ATOM   2354 O O   . GLY B 1 38  ? 24.347 47.807  53.366 1.00 46.60  ? 38  GLY B O   1 
ATOM   2355 N N   . ASN B 1 39  ? 23.076 49.029  52.016 1.00 45.11  ? 39  ASN B N   1 
ATOM   2356 C CA  . ASN B 1 39  ? 24.121 49.941  51.587 1.00 43.30  ? 39  ASN B CA  1 
ATOM   2357 C C   . ASN B 1 39  ? 25.338 49.214  51.033 1.00 42.21  ? 39  ASN B C   1 
ATOM   2358 O O   . ASN B 1 39  ? 26.478 49.673  51.151 1.00 41.74  ? 39  ASN B O   1 
ATOM   2359 C CB  . ASN B 1 39  ? 24.491 50.825  52.759 1.00 47.07  ? 39  ASN B CB  1 
ATOM   2360 C CG  . ASN B 1 39  ? 24.956 52.210  52.418 1.00 50.47  ? 39  ASN B CG  1 
ATOM   2361 O OD1 . ASN B 1 39  ? 24.272 52.929  51.690 1.00 56.67  ? 39  ASN B OD1 1 
ATOM   2362 N ND2 . ASN B 1 39  ? 26.092 52.720  52.873 1.00 51.61  ? 39  ASN B ND2 1 
ATOM   2363 N N   . ALA B 1 40  ? 25.117 48.060  50.417 1.00 40.72  ? 40  ALA B N   1 
ATOM   2364 C CA  . ALA B 1 40  ? 26.153 47.265  49.808 1.00 39.93  ? 40  ALA B CA  1 
ATOM   2365 C C   . ALA B 1 40  ? 26.685 47.782  48.494 1.00 39.56  ? 40  ALA B C   1 
ATOM   2366 O O   . ALA B 1 40  ? 27.833 47.514  48.202 1.00 41.39  ? 40  ALA B O   1 
ATOM   2367 C CB  . ALA B 1 40  ? 25.684 45.842  49.642 1.00 40.37  ? 40  ALA B CB  1 
ATOM   2368 N N   . CYS B 1 41  ? 26.071 48.610  47.698 1.00 39.63  ? 41  CYS B N   1 
ATOM   2369 C CA  . CYS B 1 41  ? 26.590 49.127  46.463 1.00 38.93  ? 41  CYS B CA  1 
ATOM   2370 C C   . CYS B 1 41  ? 26.068 50.516  46.096 1.00 39.08  ? 41  CYS B C   1 
ATOM   2371 O O   . CYS B 1 41  ? 25.675 50.765  44.953 1.00 38.07  ? 41  CYS B O   1 
ATOM   2372 C CB  . CYS B 1 41  ? 26.287 48.143  45.337 1.00 37.77  ? 41  CYS B CB  1 
ATOM   2373 S SG  . CYS B 1 41  ? 24.556 48.087  44.924 1.00 33.88  ? 41  CYS B SG  1 
ATOM   2374 N N   . PRO B 1 42  ? 26.465 51.498  46.922 1.00 39.44  ? 42  PRO B N   1 
ATOM   2375 C CA  . PRO B 1 42  ? 26.148 52.893  46.684 1.00 38.90  ? 42  PRO B CA  1 
ATOM   2376 C C   . PRO B 1 42  ? 26.811 53.423  45.435 1.00 39.63  ? 42  PRO B C   1 
ATOM   2377 O O   . PRO B 1 42  ? 26.174 54.109  44.632 1.00 39.99  ? 42  PRO B O   1 
ATOM   2378 C CB  . PRO B 1 42  ? 26.627 53.617  47.932 1.00 38.41  ? 42  PRO B CB  1 
ATOM   2379 C CG  . PRO B 1 42  ? 27.244 52.637  48.869 1.00 37.87  ? 42  PRO B CG  1 
ATOM   2380 C CD  . PRO B 1 42  ? 27.090 51.282  48.270 1.00 38.71  ? 42  PRO B CD  1 
ATOM   2381 N N   . GLU B 1 43  ? 28.080 53.142  45.140 1.00 40.09  ? 43  GLU B N   1 
ATOM   2382 C CA  . GLU B 1 43  ? 28.695 53.726  43.931 1.00 39.95  ? 43  GLU B CA  1 
ATOM   2383 C C   . GLU B 1 43  ? 28.004 53.196  42.688 1.00 39.50  ? 43  GLU B C   1 
ATOM   2384 O O   . GLU B 1 43  ? 27.915 53.889  41.694 1.00 38.37  ? 43  GLU B O   1 
ATOM   2385 C CB  . GLU B 1 43  ? 30.193 53.476  43.831 1.00 39.25  ? 43  GLU B CB  1 
ATOM   2386 C CG  . GLU B 1 43  ? 30.982 54.099  44.957 1.00 43.86  ? 43  GLU B CG  1 
ATOM   2387 C CD  . GLU B 1 43  ? 30.727 55.589  45.049 1.00 48.48  ? 43  GLU B CD  1 
ATOM   2388 O OE1 . GLU B 1 43  ? 30.734 56.239  43.969 1.00 48.75  ? 43  GLU B OE1 1 
ATOM   2389 O OE2 . GLU B 1 43  ? 30.505 56.061  46.196 1.00 52.44  ? 43  GLU B OE2 1 
ATOM   2390 N N   . VAL B 1 44  ? 27.545 51.938  42.728 1.00 40.58  ? 44  VAL B N   1 
ATOM   2391 C CA  . VAL B 1 44  ? 26.771 51.405  41.615 1.00 41.18  ? 44  VAL B CA  1 
ATOM   2392 C C   . VAL B 1 44  ? 25.403 52.082  41.612 1.00 41.73  ? 44  VAL B C   1 
ATOM   2393 O O   . VAL B 1 44  ? 24.919 52.450  40.555 1.00 41.50  ? 44  VAL B O   1 
ATOM   2394 C CB  . VAL B 1 44  ? 26.604 49.904  41.563 1.00 39.79  ? 44  VAL B CB  1 
ATOM   2395 C CG1 . VAL B 1 44  ? 25.781 49.495  40.357 1.00 41.12  ? 44  VAL B CG1 1 
ATOM   2396 C CG2 . VAL B 1 44  ? 27.953 49.206  41.518 1.00 40.81  ? 44  VAL B CG2 1 
ATOM   2397 N N   . GLU B 1 45  ? 24.863 52.415  42.774 1.00 42.50  ? 45  GLU B N   1 
ATOM   2398 C CA  . GLU B 1 45  ? 23.571 53.072  42.814 1.00 43.15  ? 45  GLU B CA  1 
ATOM   2399 C C   . GLU B 1 45  ? 23.628 54.490  42.323 1.00 43.25  ? 45  GLU B C   1 
ATOM   2400 O O   . GLU B 1 45  ? 22.639 55.008  41.840 1.00 43.72  ? 45  GLU B O   1 
ATOM   2401 C CB  . GLU B 1 45  ? 22.934 52.951  44.187 1.00 43.55  ? 45  GLU B CB  1 
ATOM   2402 C CG  . GLU B 1 45  ? 22.235 51.624  44.350 1.00 48.39  ? 45  GLU B CG  1 
ATOM   2403 C CD  . GLU B 1 45  ? 21.527 51.498  45.680 1.00 53.28  ? 45  GLU B CD  1 
ATOM   2404 O OE1 . GLU B 1 45  ? 21.196 52.572  46.222 1.00 54.75  ? 45  GLU B OE1 1 
ATOM   2405 O OE2 . GLU B 1 45  ? 21.284 50.339  46.105 1.00 56.67  ? 45  GLU B OE2 1 
ATOM   2406 N N   . LYS B 1 46  ? 24.761 55.118  42.331 1.00 43.93  ? 46  LYS B N   1 
ATOM   2407 C CA  . LYS B 1 46  ? 24.927 56.506  41.933 1.00 45.70  ? 46  LYS B CA  1 
ATOM   2408 C C   . LYS B 1 46  ? 25.245 56.577  40.455 1.00 47.23  ? 46  LYS B C   1 
ATOM   2409 O O   . LYS B 1 46  ? 25.137 57.614  39.811 1.00 47.48  ? 46  LYS B O   1 
ATOM   2410 C CB  . LYS B 1 46  ? 25.944 57.020  42.914 1.00 50.03  ? 46  LYS B CB  1 
ATOM   2411 C CG  . LYS B 1 46  ? 26.671 58.318  42.761 1.00 57.07  ? 46  LYS B CG  1 
ATOM   2412 C CD  . LYS B 1 46  ? 27.091 58.972  44.064 1.00 60.16  ? 46  LYS B CD  1 
ATOM   2413 C CE  . LYS B 1 46  ? 27.614 57.996  45.093 1.00 64.71  ? 46  LYS B CE  1 
ATOM   2414 N NZ  . LYS B 1 46  ? 27.635 58.533  46.485 1.00 68.02  ? 46  LYS B NZ  1 
ATOM   2415 N N   . ALA B 1 47  ? 25.510 55.443  39.789 1.00 48.16  ? 47  ALA B N   1 
ATOM   2416 C CA  . ALA B 1 47  ? 25.807 55.441  38.365 1.00 48.03  ? 47  ALA B CA  1 
ATOM   2417 C C   . ALA B 1 47  ? 24.546 55.077  37.604 1.00 48.66  ? 47  ALA B C   1 
ATOM   2418 O O   . ALA B 1 47  ? 23.627 54.404  38.069 1.00 47.56  ? 47  ALA B O   1 
ATOM   2419 C CB  . ALA B 1 47  ? 27.024 54.570  38.054 1.00 42.79  ? 47  ALA B CB  1 
ATOM   2420 N N   . ASP B 1 48  ? 24.472 55.557  36.347 1.00 49.62  ? 48  ASP B N   1 
ATOM   2421 C CA  . ASP B 1 48  ? 23.338 55.135  35.496 1.00 50.86  ? 48  ASP B CA  1 
ATOM   2422 C C   . ASP B 1 48  ? 23.613 53.663  35.164 1.00 50.37  ? 48  ASP B C   1 
ATOM   2423 O O   . ASP B 1 48  ? 24.330 53.456  34.155 1.00 51.35  ? 48  ASP B O   1 
ATOM   2424 C CB  . ASP B 1 48  ? 23.272 56.032  34.261 1.00 53.97  ? 48  ASP B CB  1 
ATOM   2425 C CG  . ASP B 1 48  ? 22.257 55.609  33.216 1.00 56.86  ? 48  ASP B CG  1 
ATOM   2426 O OD1 . ASP B 1 48  ? 21.347 54.814  33.539 1.00 59.16  ? 48  ASP B OD1 1 
ATOM   2427 O OD2 . ASP B 1 48  ? 22.312 56.021  32.035 1.00 58.54  ? 48  ASP B OD2 1 
ATOM   2428 N N   . ALA B 1 49  ? 23.245 52.745  36.047 1.00 48.87  ? 49  ALA B N   1 
ATOM   2429 C CA  . ALA B 1 49  ? 23.741 51.375  35.919 1.00 48.51  ? 49  ALA B CA  1 
ATOM   2430 C C   . ALA B 1 49  ? 22.646 50.333  36.038 1.00 48.16  ? 49  ALA B C   1 
ATOM   2431 O O   . ALA B 1 49  ? 21.996 50.121  37.048 1.00 47.59  ? 49  ALA B O   1 
ATOM   2432 C CB  . ALA B 1 49  ? 24.870 51.135  36.909 1.00 47.81  ? 49  ALA B CB  1 
ATOM   2433 N N   . THR B 1 50  ? 22.400 49.639  34.927 1.00 48.32  ? 50  THR B N   1 
ATOM   2434 C CA  . THR B 1 50  ? 21.241 48.774  34.793 1.00 48.51  ? 50  THR B CA  1 
ATOM   2435 C C   . THR B 1 50  ? 21.638 47.375  34.357 1.00 48.82  ? 50  THR B C   1 
ATOM   2436 O O   . THR B 1 50  ? 22.641 47.194  33.664 1.00 48.26  ? 50  THR B O   1 
ATOM   2437 C CB  . THR B 1 50  ? 20.261 49.373  33.751 1.00 44.01  ? 50  THR B CB  1 
ATOM   2438 O OG1 . THR B 1 50  ? 21.097 49.581  32.603 1.00 48.97  ? 50  THR B OG1 1 
ATOM   2439 C CG2 . THR B 1 50  ? 19.799 50.767  34.122 1.00 39.75  ? 50  THR B CG2 1 
ATOM   2440 N N   . PHE B 1 51  ? 20.729 46.455  34.652 1.00 49.36  ? 51  PHE B N   1 
ATOM   2441 C CA  . PHE B 1 51  ? 20.895 45.066  34.261 1.00 50.46  ? 51  PHE B CA  1 
ATOM   2442 C C   . PHE B 1 51  ? 20.757 44.908  32.744 1.00 51.26  ? 51  PHE B C   1 
ATOM   2443 O O   . PHE B 1 51  ? 19.867 45.514  32.156 1.00 50.52  ? 51  PHE B O   1 
ATOM   2444 C CB  . PHE B 1 51  ? 19.790 44.243  34.935 1.00 51.55  ? 51  PHE B CB  1 
ATOM   2445 C CG  . PHE B 1 51  ? 19.946 43.982  36.404 1.00 53.21  ? 51  PHE B CG  1 
ATOM   2446 C CD1 . PHE B 1 51  ? 21.034 43.265  36.885 1.00 53.41  ? 51  PHE B CD1 1 
ATOM   2447 C CD2 . PHE B 1 51  ? 18.990 44.460  37.312 1.00 52.42  ? 51  PHE B CD2 1 
ATOM   2448 C CE1 . PHE B 1 51  ? 21.191 43.019  38.238 1.00 52.25  ? 51  PHE B CE1 1 
ATOM   2449 C CE2 . PHE B 1 51  ? 19.163 44.203  38.645 1.00 53.40  ? 51  PHE B CE2 1 
ATOM   2450 C CZ  . PHE B 1 51  ? 20.260 43.491  39.106 1.00 52.16  ? 51  PHE B CZ  1 
ATOM   2451 N N   . LEU B 1 52  ? 21.614 44.101  32.132 1.00 51.78  ? 52  LEU B N   1 
ATOM   2452 C CA  . LEU B 1 52  ? 21.532 43.781  30.713 1.00 52.19  ? 52  LEU B CA  1 
ATOM   2453 C C   . LEU B 1 52  ? 21.091 42.315  30.608 1.00 53.32  ? 52  LEU B C   1 
ATOM   2454 O O   . LEU B 1 52  ? 20.256 41.923  29.787 1.00 54.26  ? 52  LEU B O   1 
ATOM   2455 C CB  . LEU B 1 52  ? 22.851 43.961  29.956 1.00 48.10  ? 52  LEU B CB  1 
ATOM   2456 C CG  . LEU B 1 52  ? 23.317 45.377  29.605 1.00 47.01  ? 52  LEU B CG  1 
ATOM   2457 C CD1 . LEU B 1 52  ? 24.748 45.436  29.099 1.00 46.23  ? 52  LEU B CD1 1 
ATOM   2458 C CD2 . LEU B 1 52  ? 22.462 46.097  28.574 1.00 40.16  ? 52  LEU B CD2 1 
ATOM   2459 N N   . TYR B 1 53  ? 21.596 41.497  31.526 1.00 53.46  ? 53  TYR B N   1 
ATOM   2460 C CA  . TYR B 1 53  ? 21.240 40.080  31.586 1.00 53.46  ? 53  TYR B CA  1 
ATOM   2461 C C   . TYR B 1 53  ? 21.433 39.599  33.021 1.00 53.39  ? 53  TYR B C   1 
ATOM   2462 O O   . TYR B 1 53  ? 22.404 40.046  33.643 1.00 53.78  ? 53  TYR B O   1 
ATOM   2463 C CB  . TYR B 1 53  ? 22.134 39.283  30.630 1.00 53.56  ? 53  TYR B CB  1 
ATOM   2464 C CG  . TYR B 1 53  ? 21.890 37.795  30.646 1.00 55.14  ? 53  TYR B CG  1 
ATOM   2465 C CD1 . TYR B 1 53  ? 20.592 37.312  30.480 1.00 56.10  ? 53  TYR B CD1 1 
ATOM   2466 C CD2 . TYR B 1 53  ? 22.896 36.855  30.812 1.00 55.93  ? 53  TYR B CD2 1 
ATOM   2467 C CE1 . TYR B 1 53  ? 20.303 35.963  30.490 1.00 57.35  ? 53  TYR B CE1 1 
ATOM   2468 C CE2 . TYR B 1 53  ? 22.636 35.492  30.822 1.00 56.75  ? 53  TYR B CE2 1 
ATOM   2469 C CZ  . TYR B 1 53  ? 21.333 35.058  30.674 1.00 58.45  ? 53  TYR B CZ  1 
ATOM   2470 O OH  . TYR B 1 53  ? 21.000 33.715  30.705 1.00 59.96  ? 53  TYR B OH  1 
ATOM   2471 N N   . SER B 1 54  ? 20.600 38.741  33.567 1.00 53.07  ? 54  SER B N   1 
ATOM   2472 C CA  . SER B 1 54  ? 20.819 38.228  34.911 1.00 53.44  ? 54  SER B CA  1 
ATOM   2473 C C   . SER B 1 54  ? 20.899 36.708  34.820 1.00 54.36  ? 54  SER B C   1 
ATOM   2474 O O   . SER B 1 54  ? 19.969 36.148  34.262 1.00 54.57  ? 54  SER B O   1 
ATOM   2475 C CB  . SER B 1 54  ? 19.717 38.522  35.904 1.00 52.25  ? 54  SER B CB  1 
ATOM   2476 O OG  . SER B 1 54  ? 19.398 39.853  36.202 1.00 53.35  ? 54  SER B OG  1 
ATOM   2477 N N   . PHE B 1 55  ? 21.807 36.077  35.538 1.00 55.35  ? 55  PHE B N   1 
ATOM   2478 C CA  . PHE B 1 55  ? 21.786 34.619  35.649 1.00 56.29  ? 55  PHE B CA  1 
ATOM   2479 C C   . PHE B 1 55  ? 21.915 34.094  37.087 1.00 58.38  ? 55  PHE B C   1 
ATOM   2480 O O   . PHE B 1 55  ? 22.214 34.777  38.090 1.00 58.11  ? 55  PHE B O   1 
ATOM   2481 C CB  . PHE B 1 55  ? 22.850 34.015  34.759 1.00 50.83  ? 55  PHE B CB  1 
ATOM   2482 C CG  . PHE B 1 55  ? 24.203 34.645  34.915 1.00 49.46  ? 55  PHE B CG  1 
ATOM   2483 C CD1 . PHE B 1 55  ? 25.197 33.981  35.607 1.00 46.47  ? 55  PHE B CD1 1 
ATOM   2484 C CD2 . PHE B 1 55  ? 24.498 35.895  34.384 1.00 48.48  ? 55  PHE B CD2 1 
ATOM   2485 C CE1 . PHE B 1 55  ? 26.459 34.513  35.749 1.00 46.15  ? 55  PHE B CE1 1 
ATOM   2486 C CE2 . PHE B 1 55  ? 25.758 36.440  34.516 1.00 46.53  ? 55  PHE B CE2 1 
ATOM   2487 C CZ  . PHE B 1 55  ? 26.721 35.753  35.215 1.00 47.30  ? 55  PHE B CZ  1 
ATOM   2488 N N   . GLU B 1 56  ? 21.368 32.884  37.226 1.00 60.15  ? 56  GLU B N   1 
ATOM   2489 C CA  . GLU B 1 56  ? 21.209 32.251  38.524 1.00 62.42  ? 56  GLU B CA  1 
ATOM   2490 C C   . GLU B 1 56  ? 21.233 30.738  38.489 1.00 63.31  ? 56  GLU B C   1 
ATOM   2491 O O   . GLU B 1 56  ? 20.200 30.191  38.170 1.00 62.90  ? 56  GLU B O   1 
ATOM   2492 C CB  . GLU B 1 56  ? 19.854 32.752  39.078 1.00 63.57  ? 56  GLU B CB  1 
ATOM   2493 C CG  . GLU B 1 56  ? 19.516 32.029  40.381 1.00 66.50  ? 56  GLU B CG  1 
ATOM   2494 C CD  . GLU B 1 56  ? 18.555 32.837  41.231 1.00 68.77  ? 56  GLU B CD  1 
ATOM   2495 O OE1 . GLU B 1 56  ? 17.462 33.131  40.704 1.00 68.86  ? 56  GLU B OE1 1 
ATOM   2496 O OE2 . GLU B 1 56  ? 18.939 33.149  42.384 1.00 70.30  ? 56  GLU B OE2 1 
ATOM   2497 N N   . ASP B 1 57  ? 22.247 30.066  38.971 1.00 65.12  ? 57  ASP B N   1 
ATOM   2498 C CA  . ASP B 1 57  ? 22.323 28.624  39.114 1.00 67.31  ? 57  ASP B CA  1 
ATOM   2499 C C   . ASP B 1 57  ? 22.376 28.043  37.712 1.00 68.71  ? 57  ASP B C   1 
ATOM   2500 O O   . ASP B 1 57  ? 21.845 26.986  37.397 1.00 69.67  ? 57  ASP B O   1 
ATOM   2501 C CB  . ASP B 1 57  ? 21.113 28.081  39.846 1.00 67.97  ? 57  ASP B CB  1 
ATOM   2502 C CG  . ASP B 1 57  ? 21.236 28.110  41.346 1.00 70.76  ? 57  ASP B CG  1 
ATOM   2503 O OD1 . ASP B 1 57  ? 22.363 28.006  41.875 1.00 72.75  ? 57  ASP B OD1 1 
ATOM   2504 O OD2 . ASP B 1 57  ? 20.169 28.233  41.987 1.00 73.61  ? 57  ASP B OD2 1 
ATOM   2505 N N   . SER B 1 58  ? 23.121 28.739  36.868 1.00 69.51  ? 58  SER B N   1 
ATOM   2506 C CA  . SER B 1 58  ? 23.130 28.472  35.435 1.00 69.59  ? 58  SER B CA  1 
ATOM   2507 C C   . SER B 1 58  ? 24.209 27.450  35.151 1.00 69.78  ? 58  SER B C   1 
ATOM   2508 O O   . SER B 1 58  ? 25.323 27.524  35.666 1.00 69.54  ? 58  SER B O   1 
ATOM   2509 C CB  . SER B 1 58  ? 23.266 29.806  34.716 1.00 68.93  ? 58  SER B CB  1 
ATOM   2510 O OG  . SER B 1 58  ? 23.740 29.744  33.392 1.00 70.62  ? 58  SER B OG  1 
ATOM   2511 N N   . GLY B 1 59  ? 23.830 26.415  34.412 1.00 70.18  ? 59  GLY B N   1 
ATOM   2512 C CA  . GLY B 1 59  ? 24.756 25.370  34.031 1.00 70.76  ? 59  GLY B CA  1 
ATOM   2513 C C   . GLY B 1 59  ? 25.218 24.442  35.143 1.00 70.89  ? 59  GLY B C   1 
ATOM   2514 O O   . GLY B 1 59  ? 24.708 24.325  36.242 1.00 70.36  ? 59  GLY B O   1 
ATOM   2515 N N   . VAL B 1 60  ? 26.299 23.742  34.834 1.00 71.13  ? 60  VAL B N   1 
ATOM   2516 C CA  . VAL B 1 60  ? 26.941 22.745  35.648 1.00 71.31  ? 60  VAL B CA  1 
ATOM   2517 C C   . VAL B 1 60  ? 27.465 23.181  36.993 1.00 71.27  ? 60  VAL B C   1 
ATOM   2518 O O   . VAL B 1 60  ? 27.267 22.409  37.946 1.00 72.23  ? 60  VAL B O   1 
ATOM   2519 C CB  . VAL B 1 60  ? 28.027 22.004  34.832 1.00 71.06  ? 60  VAL B CB  1 
ATOM   2520 C CG1 . VAL B 1 60  ? 28.965 21.194  35.716 1.00 70.10  ? 60  VAL B CG1 1 
ATOM   2521 C CG2 . VAL B 1 60  ? 27.346 21.076  33.822 1.00 71.94  ? 60  VAL B CG2 1 
ATOM   2522 N N   . GLY B 1 61  ? 28.087 24.324  37.231 1.00 70.63  ? 61  GLY B N   1 
ATOM   2523 C CA  . GLY B 1 61  ? 28.669 24.641  38.531 1.00 68.59  ? 61  GLY B CA  1 
ATOM   2524 C C   . GLY B 1 61  ? 27.771 25.614  39.268 1.00 67.80  ? 61  GLY B C   1 
ATOM   2525 O O   . GLY B 1 61  ? 28.188 26.226  40.247 1.00 68.16  ? 61  GLY B O   1 
ATOM   2526 N N   . ASP B 1 62  ? 26.519 25.705  38.839 1.00 66.30  ? 62  ASP B N   1 
ATOM   2527 C CA  . ASP B 1 62  ? 25.526 26.599  39.379 1.00 64.72  ? 62  ASP B CA  1 
ATOM   2528 C C   . ASP B 1 62  ? 26.073 28.007  39.574 1.00 62.75  ? 62  ASP B C   1 
ATOM   2529 O O   . ASP B 1 62  ? 26.378 28.495  40.650 1.00 63.60  ? 62  ASP B O   1 
ATOM   2530 C CB  . ASP B 1 62  ? 24.904 26.036  40.646 1.00 68.93  ? 62  ASP B CB  1 
ATOM   2531 C CG  . ASP B 1 62  ? 23.746 25.073  40.417 1.00 72.77  ? 62  ASP B CG  1 
ATOM   2532 O OD1 . ASP B 1 62  ? 23.569 24.510  39.310 1.00 71.46  ? 62  ASP B OD1 1 
ATOM   2533 O OD2 . ASP B 1 62  ? 23.002 24.884  41.422 1.00 73.30  ? 62  ASP B OD2 1 
ATOM   2534 N N   . VAL B 1 63  ? 26.278 28.717  38.496 1.00 59.80  ? 63  VAL B N   1 
ATOM   2535 C CA  . VAL B 1 63  ? 26.808 30.024  38.252 1.00 55.94  ? 63  VAL B CA  1 
ATOM   2536 C C   . VAL B 1 63  ? 25.743 31.120  38.230 1.00 52.88  ? 63  VAL B C   1 
ATOM   2537 O O   . VAL B 1 63  ? 24.822 31.078  37.446 1.00 50.68  ? 63  VAL B O   1 
ATOM   2538 C CB  . VAL B 1 63  ? 27.583 29.981  36.924 1.00 56.43  ? 63  VAL B CB  1 
ATOM   2539 C CG1 . VAL B 1 63  ? 27.817 31.356  36.340 1.00 56.83  ? 63  VAL B CG1 1 
ATOM   2540 C CG2 . VAL B 1 63  ? 28.874 29.205  37.205 1.00 56.68  ? 63  VAL B CG2 1 
ATOM   2541 N N   . THR B 1 64  ? 25.985 32.121  39.079 1.00 50.50  ? 64  THR B N   1 
ATOM   2542 C CA  . THR B 1 64  ? 25.038 33.209  39.321 1.00 49.00  ? 64  THR B CA  1 
ATOM   2543 C C   . THR B 1 64  ? 25.715 34.568  39.245 1.00 47.53  ? 64  THR B C   1 
ATOM   2544 O O   . THR B 1 64  ? 26.928 34.532  39.381 1.00 48.02  ? 64  THR B O   1 
ATOM   2545 C CB  . THR B 1 64  ? 24.434 33.066  40.730 1.00 47.55  ? 64  THR B CB  1 
ATOM   2546 O OG1 . THR B 1 64  ? 23.821 31.778  40.926 1.00 44.60  ? 64  THR B OG1 1 
ATOM   2547 C CG2 . THR B 1 64  ? 23.416 34.140  41.026 1.00 46.67  ? 64  THR B CG2 1 
ATOM   2548 N N   . GLY B 1 65  ? 25.048 35.607  38.824 1.00 46.52  ? 65  GLY B N   1 
ATOM   2549 C CA  . GLY B 1 65  ? 25.466 36.975  38.771 1.00 45.22  ? 65  GLY B CA  1 
ATOM   2550 C C   . GLY B 1 65  ? 24.733 37.816  37.725 1.00 44.99  ? 65  GLY B C   1 
ATOM   2551 O O   . GLY B 1 65  ? 23.645 37.464  37.212 1.00 44.57  ? 65  GLY B O   1 
ATOM   2552 N N   . PHE B 1 66  ? 25.404 38.888  37.285 1.00 44.62  ? 66  PHE B N   1 
ATOM   2553 C CA  . PHE B 1 66  ? 24.765 39.690  36.225 1.00 44.63  ? 66  PHE B CA  1 
ATOM   2554 C C   . PHE B 1 66  ? 25.746 40.320  35.260 1.00 44.38  ? 66  PHE B C   1 
ATOM   2555 O O   . PHE B 1 66  ? 26.971 40.267  35.334 1.00 44.01  ? 66  PHE B O   1 
ATOM   2556 C CB  . PHE B 1 66  ? 23.834 40.784  36.776 1.00 45.35  ? 66  PHE B CB  1 
ATOM   2557 C CG  . PHE B 1 66  ? 24.590 41.755  37.660 1.00 44.99  ? 66  PHE B CG  1 
ATOM   2558 C CD1 . PHE B 1 66  ? 25.212 42.874  37.098 1.00 41.32  ? 66  PHE B CD1 1 
ATOM   2559 C CD2 . PHE B 1 66  ? 24.923 41.393  38.966 1.00 42.35  ? 66  PHE B CD2 1 
ATOM   2560 C CE1 . PHE B 1 66  ? 25.963 43.691  37.907 1.00 39.47  ? 66  PHE B CE1 1 
ATOM   2561 C CE2 . PHE B 1 66  ? 25.643 42.243  39.783 1.00 40.27  ? 66  PHE B CE2 1 
ATOM   2562 C CZ  . PHE B 1 66  ? 26.179 43.388  39.239 1.00 41.05  ? 66  PHE B CZ  1 
ATOM   2563 N N   . LEU B 1 67  ? 25.154 40.860  34.193 1.00 45.26  ? 67  LEU B N   1 
ATOM   2564 C CA  . LEU B 1 67  ? 25.886 41.625  33.173 1.00 43.56  ? 67  LEU B CA  1 
ATOM   2565 C C   . LEU B 1 67  ? 25.203 42.989  33.134 1.00 42.41  ? 67  LEU B C   1 
ATOM   2566 O O   . LEU B 1 67  ? 24.004 43.005  32.928 1.00 41.22  ? 67  LEU B O   1 
ATOM   2567 C CB  . LEU B 1 67  ? 25.855 41.003  31.795 1.00 44.81  ? 67  LEU B CB  1 
ATOM   2568 C CG  . LEU B 1 67  ? 26.468 41.878  30.657 1.00 48.35  ? 67  LEU B CG  1 
ATOM   2569 C CD1 . LEU B 1 67  ? 27.982 41.925  30.842 1.00 46.67  ? 67  LEU B CD1 1 
ATOM   2570 C CD2 . LEU B 1 67  ? 26.092 41.363  29.270 1.00 43.99  ? 67  LEU B CD2 1 
ATOM   2571 N N   . ALA B 1 68  ? 25.978 44.041  33.391 1.00 42.80  ? 68  ALA B N   1 
ATOM   2572 C CA  . ALA B 1 68  ? 25.383 45.371  33.459 1.00 42.17  ? 68  ALA B CA  1 
ATOM   2573 C C   . ALA B 1 68  ? 25.921 46.461  32.552 1.00 42.39  ? 68  ALA B C   1 
ATOM   2574 O O   . ALA B 1 68  ? 27.086 46.510  32.150 1.00 42.66  ? 68  ALA B O   1 
ATOM   2575 C CB  . ALA B 1 68  ? 25.626 45.866  34.880 1.00 41.14  ? 68  ALA B CB  1 
ATOM   2576 N N   . LEU B 1 69  ? 25.096 47.500  32.363 1.00 41.83  ? 69  LEU B N   1 
ATOM   2577 C CA  . LEU B 1 69  ? 25.506 48.626  31.524 1.00 40.62  ? 69  LEU B CA  1 
ATOM   2578 C C   . LEU B 1 69  ? 25.625 49.855  32.416 1.00 40.64  ? 69  LEU B C   1 
ATOM   2579 O O   . LEU B 1 69  ? 24.777 50.123  33.275 1.00 40.68  ? 69  LEU B O   1 
ATOM   2580 C CB  . LEU B 1 69  ? 24.589 48.817  30.345 1.00 37.50  ? 69  LEU B CB  1 
ATOM   2581 C CG  . LEU B 1 69  ? 24.946 49.940  29.327 1.00 39.91  ? 69  LEU B CG  1 
ATOM   2582 C CD1 . LEU B 1 69  ? 26.123 49.557  28.418 1.00 32.49  ? 69  LEU B CD1 1 
ATOM   2583 C CD2 . LEU B 1 69  ? 23.647 50.314  28.633 1.00 34.89  ? 69  LEU B CD2 1 
ATOM   2584 N N   . ASP B 1 70  ? 26.821 50.433  32.421 1.00 40.17  ? 70  ASP B N   1 
ATOM   2585 C CA  . ASP B 1 70  ? 27.079 51.570  33.311 1.00 39.62  ? 70  ASP B CA  1 
ATOM   2586 C C   . ASP B 1 70  ? 27.422 52.749  32.402 1.00 39.92  ? 70  ASP B C   1 
ATOM   2587 O O   . ASP B 1 70  ? 28.611 52.914  32.110 1.00 39.58  ? 70  ASP B O   1 
ATOM   2588 C CB  . ASP B 1 70  ? 28.198 51.297  34.286 1.00 36.07  ? 70  ASP B CB  1 
ATOM   2589 C CG  . ASP B 1 70  ? 28.667 52.429  35.162 1.00 36.94  ? 70  ASP B CG  1 
ATOM   2590 O OD1 . ASP B 1 70  ? 28.450 53.606  34.787 1.00 35.49  ? 70  ASP B OD1 1 
ATOM   2591 O OD2 . ASP B 1 70  ? 29.310 52.191  36.232 1.00 34.88  ? 70  ASP B OD2 1 
ATOM   2592 N N   . ASN B 1 71  ? 26.425 53.614  32.195 1.00 39.80  ? 71  ASN B N   1 
ATOM   2593 C CA  . ASN B 1 71  ? 26.680 54.766  31.361 1.00 39.92  ? 71  ASN B CA  1 
ATOM   2594 C C   . ASN B 1 71  ? 27.507 55.841  32.056 1.00 39.62  ? 71  ASN B C   1 
ATOM   2595 O O   . ASN B 1 71  ? 27.834 56.809  31.363 1.00 41.02  ? 71  ASN B O   1 
ATOM   2596 C CB  . ASN B 1 71  ? 25.451 55.464  30.784 1.00 39.54  ? 71  ASN B CB  1 
ATOM   2597 C CG  . ASN B 1 71  ? 24.671 54.526  29.899 1.00 40.19  ? 71  ASN B CG  1 
ATOM   2598 O OD1 . ASN B 1 71  ? 25.188 53.736  29.117 1.00 42.92  ? 71  ASN B OD1 1 
ATOM   2599 N ND2 . ASN B 1 71  ? 23.380 54.639  30.115 1.00 41.25  ? 71  ASN B ND2 1 
ATOM   2600 N N   . THR B 1 72  ? 27.571 55.853  33.366 1.00 38.39  ? 72  THR B N   1 
ATOM   2601 C CA  . THR B 1 72  ? 28.288 56.914  34.035 1.00 37.46  ? 72  THR B CA  1 
ATOM   2602 C C   . THR B 1 72  ? 29.764 56.633  33.842 1.00 37.47  ? 72  THR B C   1 
ATOM   2603 O O   . THR B 1 72  ? 30.481 57.524  33.401 1.00 37.86  ? 72  THR B O   1 
ATOM   2604 C CB  . THR B 1 72  ? 27.896 57.025  35.523 1.00 36.99  ? 72  THR B CB  1 
ATOM   2605 O OG1 . THR B 1 72  ? 26.484 57.243  35.583 1.00 39.68  ? 72  THR B OG1 1 
ATOM   2606 C CG2 . THR B 1 72  ? 28.643 58.167  36.156 1.00 34.59  ? 72  THR B CG2 1 
ATOM   2607 N N   . ASN B 1 73  ? 30.206 55.423  34.172 1.00 37.41  ? 73  ASN B N   1 
ATOM   2608 C CA  . ASN B 1 73  ? 31.593 55.036  34.028 1.00 37.32  ? 73  ASN B CA  1 
ATOM   2609 C C   . ASN B 1 73  ? 31.931 54.450  32.672 1.00 38.52  ? 73  ASN B C   1 
ATOM   2610 O O   . ASN B 1 73  ? 33.116 54.164  32.451 1.00 38.71  ? 73  ASN B O   1 
ATOM   2611 C CB  . ASN B 1 73  ? 31.995 54.036  35.126 1.00 36.20  ? 73  ASN B CB  1 
ATOM   2612 C CG  . ASN B 1 73  ? 31.736 54.668  36.470 1.00 36.25  ? 73  ASN B CG  1 
ATOM   2613 O OD1 . ASN B 1 73  ? 32.509 55.561  36.814 1.00 40.60  ? 73  ASN B OD1 1 
ATOM   2614 N ND2 . ASN B 1 73  ? 30.637 54.305  37.082 1.00 35.84  ? 73  ASN B ND2 1 
ATOM   2615 N N   . LYS B 1 74  ? 30.976 54.283  31.753 1.00 38.91  ? 74  LYS B N   1 
ATOM   2616 C CA  . LYS B 1 74  ? 31.284 53.842  30.390 1.00 40.23  ? 74  LYS B CA  1 
ATOM   2617 C C   . LYS B 1 74  ? 31.740 52.384  30.403 1.00 41.21  ? 74  LYS B C   1 
ATOM   2618 O O   . LYS B 1 74  ? 32.692 51.979  29.733 1.00 42.10  ? 74  LYS B O   1 
ATOM   2619 C CB  . LYS B 1 74  ? 32.336 54.681  29.678 1.00 35.69  ? 74  LYS B CB  1 
ATOM   2620 C CG  . LYS B 1 74  ? 32.144 56.183  29.665 1.00 38.69  ? 74  LYS B CG  1 
ATOM   2621 C CD  . LYS B 1 74  ? 31.094 56.562  28.620 1.00 42.76  ? 74  LYS B CD  1 
ATOM   2622 C CE  . LYS B 1 74  ? 29.867 57.180  29.259 1.00 47.81  ? 74  LYS B CE  1 
ATOM   2623 N NZ  . LYS B 1 74  ? 29.152 58.081  28.266 1.00 50.70  ? 74  LYS B NZ  1 
ATOM   2624 N N   . LEU B 1 75  ? 31.048 51.594  31.239 1.00 40.53  ? 75  LEU B N   1 
ATOM   2625 C CA  . LEU B 1 75  ? 31.358 50.193  31.336 1.00 38.47  ? 75  LEU B CA  1 
ATOM   2626 C C   . LEU B 1 75  ? 30.278 49.241  30.846 1.00 37.88  ? 75  LEU B C   1 
ATOM   2627 O O   . LEU B 1 75  ? 29.082 49.493  30.859 1.00 37.06  ? 75  LEU B O   1 
ATOM   2628 C CB  . LEU B 1 75  ? 31.546 49.850  32.844 1.00 34.45  ? 75  LEU B CB  1 
ATOM   2629 C CG  . LEU B 1 75  ? 32.520 50.801  33.579 1.00 33.80  ? 75  LEU B CG  1 
ATOM   2630 C CD1 . LEU B 1 75  ? 32.412 50.407  35.058 1.00 29.69  ? 75  LEU B CD1 1 
ATOM   2631 C CD2 . LEU B 1 75  ? 33.958 50.831  33.047 1.00 23.87  ? 75  LEU B CD2 1 
ATOM   2632 N N   . ILE B 1 76  ? 30.790 48.048  30.567 1.00 37.46  ? 76  ILE B N   1 
ATOM   2633 C CA  . ILE B 1 76  ? 30.024 46.832  30.467 1.00 37.68  ? 76  ILE B CA  1 
ATOM   2634 C C   . ILE B 1 76  ? 30.636 45.872  31.483 1.00 38.86  ? 76  ILE B C   1 
ATOM   2635 O O   . ILE B 1 76  ? 31.812 45.534  31.365 1.00 40.71  ? 76  ILE B O   1 
ATOM   2636 C CB  . ILE B 1 76  ? 30.151 46.203  29.113 1.00 37.46  ? 76  ILE B CB  1 
ATOM   2637 C CG1 . ILE B 1 76  ? 29.252 46.919  28.076 1.00 35.75  ? 76  ILE B CG1 1 
ATOM   2638 C CG2 . ILE B 1 76  ? 29.791 44.739  29.082 1.00 38.32  ? 76  ILE B CG2 1 
ATOM   2639 C CD1 . ILE B 1 76  ? 29.918 46.836  26.717 1.00 33.52  ? 76  ILE B CD1 1 
ATOM   2640 N N   . VAL B 1 77  ? 29.948 45.534  32.555 1.00 39.52  ? 77  VAL B N   1 
ATOM   2641 C CA  . VAL B 1 77  ? 30.396 44.687  33.634 1.00 38.00  ? 77  VAL B CA  1 
ATOM   2642 C C   . VAL B 1 77  ? 29.611 43.382  33.759 1.00 38.28  ? 77  VAL B C   1 
ATOM   2643 O O   . VAL B 1 77  ? 28.383 43.247  33.754 1.00 37.31  ? 77  VAL B O   1 
ATOM   2644 C CB  . VAL B 1 77  ? 30.208 45.487  34.941 1.00 35.43  ? 77  VAL B CB  1 
ATOM   2645 C CG1 . VAL B 1 77  ? 30.598 44.698  36.182 1.00 33.92  ? 77  VAL B CG1 1 
ATOM   2646 C CG2 . VAL B 1 77  ? 30.957 46.781  34.882 1.00 34.18  ? 77  VAL B CG2 1 
ATOM   2647 N N   . LEU B 1 78  ? 30.411 42.342  33.914 1.00 38.51  ? 78  LEU B N   1 
ATOM   2648 C CA  . LEU B 1 78  ? 29.977 40.965  34.080 1.00 38.97  ? 78  LEU B CA  1 
ATOM   2649 C C   . LEU B 1 78  ? 30.418 40.545  35.481 1.00 39.28  ? 78  LEU B C   1 
ATOM   2650 O O   . LEU B 1 78  ? 31.599 40.542  35.803 1.00 38.22  ? 78  LEU B O   1 
ATOM   2651 C CB  . LEU B 1 78  ? 30.556 40.054  33.025 1.00 40.51  ? 78  LEU B CB  1 
ATOM   2652 C CG  . LEU B 1 78  ? 30.404 38.547  33.147 1.00 45.33  ? 78  LEU B CG  1 
ATOM   2653 C CD1 . LEU B 1 78  ? 29.001 38.066  32.818 1.00 43.98  ? 78  LEU B CD1 1 
ATOM   2654 C CD2 . LEU B 1 78  ? 31.440 37.812  32.275 1.00 47.24  ? 78  LEU B CD2 1 
ATOM   2655 N N   . SER B 1 79  ? 29.396 40.502  36.346 1.00 40.31  ? 79  SER B N   1 
ATOM   2656 C CA  . SER B 1 79  ? 29.659 40.236  37.755 1.00 40.71  ? 79  SER B CA  1 
ATOM   2657 C C   . SER B 1 79  ? 29.298 38.829  38.158 1.00 41.50  ? 79  SER B C   1 
ATOM   2658 O O   . SER B 1 79  ? 28.169 38.373  38.008 1.00 40.77  ? 79  SER B O   1 
ATOM   2659 C CB  . SER B 1 79  ? 29.045 41.377  38.508 1.00 41.10  ? 79  SER B CB  1 
ATOM   2660 O OG  . SER B 1 79  ? 29.092 41.240  39.919 1.00 40.48  ? 79  SER B OG  1 
ATOM   2661 N N   . PHE B 1 80  ? 30.333 38.127  38.649 1.00 42.09  ? 80  PHE B N   1 
ATOM   2662 C CA  . PHE B 1 80  ? 30.113 36.720  39.080 1.00 43.54  ? 80  PHE B CA  1 
ATOM   2663 C C   . PHE B 1 80  ? 29.869 36.585  40.574 1.00 43.53  ? 80  PHE B C   1 
ATOM   2664 O O   . PHE B 1 80  ? 30.711 36.991  41.392 1.00 43.20  ? 80  PHE B O   1 
ATOM   2665 C CB  . PHE B 1 80  ? 31.276 35.748  38.787 1.00 45.75  ? 80  PHE B CB  1 
ATOM   2666 C CG  . PHE B 1 80  ? 31.312 35.406  37.316 1.00 48.04  ? 80  PHE B CG  1 
ATOM   2667 C CD1 . PHE B 1 80  ? 30.474 34.402  36.855 1.00 48.37  ? 80  PHE B CD1 1 
ATOM   2668 C CD2 . PHE B 1 80  ? 32.138 36.066  36.424 1.00 48.74  ? 80  PHE B CD2 1 
ATOM   2669 C CE1 . PHE B 1 80  ? 30.486 34.031  35.537 1.00 50.36  ? 80  PHE B CE1 1 
ATOM   2670 C CE2 . PHE B 1 80  ? 32.091 35.707  35.078 1.00 50.88  ? 80  PHE B CE2 1 
ATOM   2671 C CZ  . PHE B 1 80  ? 31.270 34.699  34.626 1.00 49.17  ? 80  PHE B CZ  1 
ATOM   2672 N N   . ARG B 1 81  ? 28.755 35.974  40.948 1.00 43.85  ? 81  ARG B N   1 
ATOM   2673 C CA  . ARG B 1 81  ? 28.513 35.791  42.394 1.00 44.46  ? 81  ARG B CA  1 
ATOM   2674 C C   . ARG B 1 81  ? 29.319 34.647  43.002 1.00 44.45  ? 81  ARG B C   1 
ATOM   2675 O O   . ARG B 1 81  ? 29.335 33.556  42.459 1.00 44.89  ? 81  ARG B O   1 
ATOM   2676 C CB  . ARG B 1 81  ? 27.042 35.548  42.693 1.00 40.91  ? 81  ARG B CB  1 
ATOM   2677 C CG  . ARG B 1 81  ? 26.683 35.777  44.155 1.00 39.65  ? 81  ARG B CG  1 
ATOM   2678 C CD  . ARG B 1 81  ? 26.107 34.539  44.772 1.00 41.29  ? 81  ARG B CD  1 
ATOM   2679 N NE  . ARG B 1 81  ? 24.745 34.160  44.634 1.00 45.12  ? 81  ARG B NE  1 
ATOM   2680 C CZ  . ARG B 1 81  ? 24.191 32.944  44.482 1.00 48.10  ? 81  ARG B CZ  1 
ATOM   2681 N NH1 . ARG B 1 81  ? 24.845 31.785  44.391 1.00 42.98  ? 81  ARG B NH1 1 
ATOM   2682 N NH2 . ARG B 1 81  ? 22.843 32.862  44.370 1.00 46.74  ? 81  ARG B NH2 1 
ATOM   2683 N N   . GLY B 1 82  ? 29.818 34.764  44.206 1.00 45.31  ? 82  GLY B N   1 
ATOM   2684 C CA  . GLY B 1 82  ? 30.476 33.650  44.879 1.00 47.44  ? 82  GLY B CA  1 
ATOM   2685 C C   . GLY B 1 82  ? 29.439 32.697  45.485 1.00 48.47  ? 82  GLY B C   1 
ATOM   2686 O O   . GLY B 1 82  ? 28.240 32.834  45.251 1.00 47.17  ? 82  GLY B O   1 
ATOM   2687 N N   . SER B 1 83  ? 29.899 31.850  46.426 1.00 49.33  ? 83  SER B N   1 
ATOM   2688 C CA  . SER B 1 83  ? 28.921 30.891  46.946 1.00 51.48  ? 83  SER B CA  1 
ATOM   2689 C C   . SER B 1 83  ? 27.903 31.504  47.890 1.00 51.98  ? 83  SER B C   1 
ATOM   2690 O O   . SER B 1 83  ? 28.109 32.381  48.725 1.00 51.68  ? 83  SER B O   1 
ATOM   2691 C CB  . SER B 1 83  ? 29.688 29.660  47.419 1.00 51.50  ? 83  SER B CB  1 
ATOM   2692 O OG  . SER B 1 83  ? 28.949 28.986  48.436 1.00 54.92  ? 83  SER B OG  1 
ATOM   2693 N N   . ARG B 1 84  ? 26.668 30.996  47.849 1.00 52.89  ? 84  ARG B N   1 
ATOM   2694 C CA  . ARG B 1 84  ? 25.610 31.365  48.801 1.00 53.71  ? 84  ARG B CA  1 
ATOM   2695 C C   . ARG B 1 84  ? 25.920 30.975  50.238 1.00 52.82  ? 84  ARG B C   1 
ATOM   2696 O O   . ARG B 1 84  ? 25.248 31.465  51.125 1.00 53.01  ? 84  ARG B O   1 
ATOM   2697 C CB  . ARG B 1 84  ? 24.316 30.677  48.375 1.00 59.49  ? 84  ARG B CB  1 
ATOM   2698 C CG  . ARG B 1 84  ? 23.025 31.405  48.695 1.00 66.09  ? 84  ARG B CG  1 
ATOM   2699 C CD  . ARG B 1 84  ? 21.894 30.863  47.816 1.00 72.10  ? 84  ARG B CD  1 
ATOM   2700 N NE  . ARG B 1 84  ? 21.836 29.397  47.929 1.00 79.32  ? 84  ARG B NE  1 
ATOM   2701 C CZ  . ARG B 1 84  ? 20.906 28.793  48.676 1.00 82.90  ? 84  ARG B CZ  1 
ATOM   2702 N NH1 . ARG B 1 84  ? 19.982 29.508  49.321 1.00 83.02  ? 84  ARG B NH1 1 
ATOM   2703 N NH2 . ARG B 1 84  ? 20.909 27.465  48.751 1.00 84.65  ? 84  ARG B NH2 1 
ATOM   2704 N N   . SER B 1 85  ? 26.747 30.003  50.530 1.00 52.56  ? 85  SER B N   1 
ATOM   2705 C CA  . SER B 1 85  ? 27.197 29.631  51.834 1.00 53.33  ? 85  SER B CA  1 
ATOM   2706 C C   . SER B 1 85  ? 28.722 29.480  51.701 1.00 53.71  ? 85  SER B C   1 
ATOM   2707 O O   . SER B 1 85  ? 29.247 28.390  51.463 1.00 53.68  ? 85  SER B O   1 
ATOM   2708 C CB  . SER B 1 85  ? 26.613 28.380  52.463 1.00 53.64  ? 85  SER B CB  1 
ATOM   2709 O OG  . SER B 1 85  ? 25.216 28.314  52.378 1.00 57.56  ? 85  SER B OG  1 
ATOM   2710 N N   . ILE B 1 86  ? 29.441 30.530  52.058 1.00 53.54  ? 86  ILE B N   1 
ATOM   2711 C CA  . ILE B 1 86  ? 30.899 30.464  51.980 1.00 54.09  ? 86  ILE B CA  1 
ATOM   2712 C C   . ILE B 1 86  ? 31.572 29.512  52.938 1.00 54.66  ? 86  ILE B C   1 
ATOM   2713 O O   . ILE B 1 86  ? 32.584 28.851  52.631 1.00 53.26  ? 86  ILE B O   1 
ATOM   2714 C CB  . ILE B 1 86  ? 31.424 31.917  51.944 1.00 51.58  ? 86  ILE B CB  1 
ATOM   2715 C CG1 . ILE B 1 86  ? 30.870 32.581  50.670 1.00 48.74  ? 86  ILE B CG1 1 
ATOM   2716 C CG2 . ILE B 1 86  ? 32.936 31.979  52.055 1.00 49.90  ? 86  ILE B CG2 1 
ATOM   2717 C CD1 . ILE B 1 86  ? 31.258 33.988  50.337 1.00 43.98  ? 86  ILE B CD1 1 
ATOM   2718 N N   . GLU B 1 87  ? 31.129 29.367  54.188 1.00 56.38  ? 87  GLU B N   1 
ATOM   2719 C CA  . GLU B 1 87  ? 31.716 28.483  55.194 1.00 57.75  ? 87  GLU B CA  1 
ATOM   2720 C C   . GLU B 1 87  ? 31.810 27.066  54.604 1.00 58.22  ? 87  GLU B C   1 
ATOM   2721 O O   . GLU B 1 87  ? 32.841 26.399  54.597 1.00 57.53  ? 87  GLU B O   1 
ATOM   2722 C CB  . GLU B 1 87  ? 30.874 28.297  56.443 1.00 63.12  ? 87  GLU B CB  1 
ATOM   2723 C CG  . GLU B 1 87  ? 29.393 27.979  56.485 1.00 69.05  ? 87  GLU B CG  1 
ATOM   2724 C CD  . GLU B 1 87  ? 28.452 28.227  55.353 1.00 70.16  ? 87  GLU B CD  1 
ATOM   2725 O OE1 . GLU B 1 87  ? 28.812 27.846  54.230 1.00 71.57  ? 87  GLU B OE1 1 
ATOM   2726 O OE2 . GLU B 1 87  ? 27.340 28.764  55.467 1.00 73.78  ? 87  GLU B OE2 1 
ATOM   2727 N N   . ASN B 1 88  ? 30.688 26.569  54.084 1.00 57.87  ? 88  ASN B N   1 
ATOM   2728 C CA  . ASN B 1 88  ? 30.690 25.170  53.681 1.00 58.80  ? 88  ASN B CA  1 
ATOM   2729 C C   . ASN B 1 88  ? 31.300 24.957  52.325 1.00 58.26  ? 88  ASN B C   1 
ATOM   2730 O O   . ASN B 1 88  ? 32.013 23.980  52.066 1.00 58.27  ? 88  ASN B O   1 
ATOM   2731 C CB  . ASN B 1 88  ? 29.313 24.662  54.094 1.00 62.41  ? 88  ASN B CB  1 
ATOM   2732 C CG  . ASN B 1 88  ? 29.251 24.395  55.613 1.00 65.26  ? 88  ASN B CG  1 
ATOM   2733 O OD1 . ASN B 1 88  ? 30.110 24.580  56.510 1.00 63.19  ? 88  ASN B OD1 1 
ATOM   2734 N ND2 . ASN B 1 88  ? 28.139 23.757  56.005 1.00 67.40  ? 88  ASN B ND2 1 
ATOM   2735 N N   . TRP B 1 89  ? 31.360 26.000  51.510 1.00 57.25  ? 89  TRP B N   1 
ATOM   2736 C CA  . TRP B 1 89  ? 32.092 25.971  50.265 1.00 56.69  ? 89  TRP B CA  1 
ATOM   2737 C C   . TRP B 1 89  ? 33.585 25.848  50.505 1.00 57.36  ? 89  TRP B C   1 
ATOM   2738 O O   . TRP B 1 89  ? 34.241 25.101  49.771 1.00 57.27  ? 89  TRP B O   1 
ATOM   2739 C CB  . TRP B 1 89  ? 31.693 27.198  49.449 1.00 53.79  ? 89  TRP B CB  1 
ATOM   2740 C CG  . TRP B 1 89  ? 32.506 27.375  48.202 1.00 49.87  ? 89  TRP B CG  1 
ATOM   2741 C CD1 . TRP B 1 89  ? 32.192 26.898  46.967 1.00 50.07  ? 89  TRP B CD1 1 
ATOM   2742 C CD2 . TRP B 1 89  ? 33.729 28.090  48.063 1.00 46.65  ? 89  TRP B CD2 1 
ATOM   2743 N NE1 . TRP B 1 89  ? 33.189 27.223  46.071 1.00 51.66  ? 89  TRP B NE1 1 
ATOM   2744 C CE2 . TRP B 1 89  ? 34.150 27.944  46.737 1.00 50.20  ? 89  TRP B CE2 1 
ATOM   2745 C CE3 . TRP B 1 89  ? 34.521 28.842  48.918 1.00 47.19  ? 89  TRP B CE3 1 
ATOM   2746 C CZ2 . TRP B 1 89  ? 35.307 28.552  46.237 1.00 49.74  ? 89  TRP B CZ2 1 
ATOM   2747 C CZ3 . TRP B 1 89  ? 35.702 29.377  48.451 1.00 46.43  ? 89  TRP B CZ3 1 
ATOM   2748 C CH2 . TRP B 1 89  ? 36.087 29.232  47.130 1.00 46.39  ? 89  TRP B CH2 1 
ATOM   2749 N N   . ILE B 1 90  ? 34.178 26.498  51.498 1.00 58.37  ? 90  ILE B N   1 
ATOM   2750 C CA  . ILE B 1 90  ? 35.612 26.432  51.750 1.00 59.84  ? 90  ILE B CA  1 
ATOM   2751 C C   . ILE B 1 90  ? 36.108 25.037  52.094 1.00 61.73  ? 90  ILE B C   1 
ATOM   2752 O O   . ILE B 1 90  ? 37.094 24.516  51.565 1.00 61.57  ? 90  ILE B O   1 
ATOM   2753 C CB  . ILE B 1 90  ? 36.037 27.449  52.813 1.00 56.75  ? 90  ILE B CB  1 
ATOM   2754 C CG1 . ILE B 1 90  ? 36.278 28.792  52.096 1.00 58.19  ? 90  ILE B CG1 1 
ATOM   2755 C CG2 . ILE B 1 90  ? 37.256 27.124  53.650 1.00 56.32  ? 90  ILE B CG2 1 
ATOM   2756 C CD1 . ILE B 1 90  ? 36.038 30.032  52.936 1.00 53.59  ? 90  ILE B CD1 1 
ATOM   2757 N N   . GLY B 1 91  ? 35.397 24.398  53.009 1.00 63.13  ? 91  GLY B N   1 
ATOM   2758 C CA  . GLY B 1 91  ? 35.736 23.121  53.598 1.00 64.75  ? 91  GLY B CA  1 
ATOM   2759 C C   . GLY B 1 91  ? 35.327 21.923  52.759 1.00 65.62  ? 91  GLY B C   1 
ATOM   2760 O O   . GLY B 1 91  ? 35.864 20.828  52.984 1.00 66.59  ? 91  GLY B O   1 
ATOM   2761 N N   . ASN B 1 92  ? 34.494 22.168  51.752 1.00 65.51  ? 92  ASN B N   1 
ATOM   2762 C CA  . ASN B 1 92  ? 34.085 21.106  50.857 1.00 66.08  ? 92  ASN B CA  1 
ATOM   2763 C C   . ASN B 1 92  ? 34.739 21.210  49.493 1.00 66.14  ? 92  ASN B C   1 
ATOM   2764 O O   . ASN B 1 92  ? 34.327 20.554  48.529 1.00 66.82  ? 92  ASN B O   1 
ATOM   2765 C CB  . ASN B 1 92  ? 32.558 21.091  50.705 1.00 69.12  ? 92  ASN B CB  1 
ATOM   2766 C CG  . ASN B 1 92  ? 31.987 20.443  51.960 1.00 73.35  ? 92  ASN B CG  1 
ATOM   2767 O OD1 . ASN B 1 92  ? 31.640 19.268  51.907 1.00 74.84  ? 92  ASN B OD1 1 
ATOM   2768 N ND2 . ASN B 1 92  ? 32.035 21.171  53.076 1.00 76.73  ? 92  ASN B ND2 1 
ATOM   2769 N N   . LEU B 1 93  ? 35.802 21.977  49.392 1.00 65.56  ? 93  LEU B N   1 
ATOM   2770 C CA  . LEU B 1 93  ? 36.454 22.281  48.134 1.00 65.19  ? 93  LEU B CA  1 
ATOM   2771 C C   . LEU B 1 93  ? 37.463 21.234  47.708 1.00 66.30  ? 93  LEU B C   1 
ATOM   2772 O O   . LEU B 1 93  ? 38.486 21.043  48.369 1.00 67.15  ? 93  LEU B O   1 
ATOM   2773 C CB  . LEU B 1 93  ? 37.221 23.591  48.333 1.00 61.23  ? 93  LEU B CB  1 
ATOM   2774 C CG  . LEU B 1 93  ? 37.847 24.237  47.116 1.00 57.58  ? 93  LEU B CG  1 
ATOM   2775 C CD1 . LEU B 1 93  ? 36.760 24.945  46.339 1.00 56.38  ? 93  LEU B CD1 1 
ATOM   2776 C CD2 . LEU B 1 93  ? 38.938 25.191  47.574 1.00 59.22  ? 93  LEU B CD2 1 
ATOM   2777 N N   . ASN B 1 94  ? 37.271 20.659  46.543 1.00 67.07  ? 94  ASN B N   1 
ATOM   2778 C CA  . ASN B 1 94  ? 38.109 19.660  45.917 1.00 67.46  ? 94  ASN B CA  1 
ATOM   2779 C C   . ASN B 1 94  ? 39.258 20.235  45.100 1.00 66.93  ? 94  ASN B C   1 
ATOM   2780 O O   . ASN B 1 94  ? 39.226 20.136  43.845 1.00 68.41  ? 94  ASN B O   1 
ATOM   2781 C CB  . ASN B 1 94  ? 37.137 18.887  45.007 1.00 72.18  ? 94  ASN B CB  1 
ATOM   2782 C CG  . ASN B 1 94  ? 37.762 17.802  44.174 1.00 77.89  ? 94  ASN B CG  1 
ATOM   2783 O OD1 . ASN B 1 94  ? 38.927 17.433  44.369 1.00 81.90  ? 94  ASN B OD1 1 
ATOM   2784 N ND2 . ASN B 1 94  ? 36.996 17.286  43.217 1.00 81.89  ? 94  ASN B ND2 1 
ATOM   2785 N N   . PHE B 1 95  ? 40.474 20.191  45.609 1.00 65.61  ? 95  PHE B N   1 
ATOM   2786 C CA  . PHE B 1 95  ? 41.703 20.605  44.966 1.00 64.41  ? 95  PHE B CA  1 
ATOM   2787 C C   . PHE B 1 95  ? 42.084 20.038  43.613 1.00 63.40  ? 95  PHE B C   1 
ATOM   2788 O O   . PHE B 1 95  ? 43.055 20.526  43.023 1.00 63.01  ? 95  PHE B O   1 
ATOM   2789 C CB  . PHE B 1 95  ? 42.872 20.422  45.968 1.00 61.25  ? 95  PHE B CB  1 
ATOM   2790 C CG  . PHE B 1 95  ? 42.546 20.924  47.343 1.00 59.81  ? 95  PHE B CG  1 
ATOM   2791 C CD1 . PHE B 1 95  ? 41.748 22.034  47.569 1.00 60.18  ? 95  PHE B CD1 1 
ATOM   2792 C CD2 . PHE B 1 95  ? 43.061 20.265  48.448 1.00 61.04  ? 95  PHE B CD2 1 
ATOM   2793 C CE1 . PHE B 1 95  ? 41.453 22.468  48.844 1.00 61.37  ? 95  PHE B CE1 1 
ATOM   2794 C CE2 . PHE B 1 95  ? 42.788 20.693  49.734 1.00 61.38  ? 95  PHE B CE2 1 
ATOM   2795 C CZ  . PHE B 1 95  ? 41.974 21.792  49.935 1.00 61.79  ? 95  PHE B CZ  1 
ATOM   2796 N N   . ASP B 1 96  ? 41.365 19.114  43.005 1.00 63.30  ? 96  ASP B N   1 
ATOM   2797 C CA  . ASP B 1 96  ? 41.718 18.532  41.726 1.00 63.35  ? 96  ASP B CA  1 
ATOM   2798 C C   . ASP B 1 96  ? 41.929 19.559  40.624 1.00 63.19  ? 96  ASP B C   1 
ATOM   2799 O O   . ASP B 1 96  ? 41.197 20.537  40.490 1.00 64.20  ? 96  ASP B O   1 
ATOM   2800 C CB  . ASP B 1 96  ? 40.717 17.476  41.271 1.00 62.04  ? 96  ASP B CB  1 
ATOM   2801 C CG  . ASP B 1 96  ? 40.670 16.321  42.251 1.00 61.52  ? 96  ASP B CG  1 
ATOM   2802 O OD1 . ASP B 1 96  ? 41.717 15.992  42.831 1.00 63.73  ? 96  ASP B OD1 1 
ATOM   2803 O OD2 . ASP B 1 96  ? 39.572 15.779  42.444 1.00 60.26  ? 96  ASP B OD2 1 
ATOM   2804 N N   . LEU B 1 97  ? 43.033 19.378  39.941 1.00 62.27  ? 97  LEU B N   1 
ATOM   2805 C CA  . LEU B 1 97  ? 43.542 20.113  38.822 1.00 62.03  ? 97  LEU B CA  1 
ATOM   2806 C C   . LEU B 1 97  ? 43.173 19.400  37.510 1.00 63.06  ? 97  LEU B C   1 
ATOM   2807 O O   . LEU B 1 97  ? 42.843 18.200  37.501 1.00 62.76  ? 97  LEU B O   1 
ATOM   2808 C CB  . LEU B 1 97  ? 45.055 20.086  38.969 1.00 57.24  ? 97  LEU B CB  1 
ATOM   2809 C CG  . LEU B 1 97  ? 45.729 21.199  39.739 1.00 57.90  ? 97  LEU B CG  1 
ATOM   2810 C CD1 . LEU B 1 97  ? 47.233 21.064  39.813 1.00 54.99  ? 97  LEU B CD1 1 
ATOM   2811 C CD2 . LEU B 1 97  ? 45.319 22.587  39.244 1.00 56.57  ? 97  LEU B CD2 1 
ATOM   2812 N N   . LYS B 1 98  ? 43.374 20.064  36.374 1.00 63.87  ? 98  LYS B N   1 
ATOM   2813 C CA  . LYS B 1 98  ? 42.932 19.535  35.085 1.00 64.24  ? 98  LYS B CA  1 
ATOM   2814 C C   . LYS B 1 98  ? 43.413 20.367  33.904 1.00 64.65  ? 98  LYS B C   1 
ATOM   2815 O O   . LYS B 1 98  ? 43.440 21.589  33.952 1.00 65.25  ? 98  LYS B O   1 
ATOM   2816 C CB  . LYS B 1 98  ? 41.429 19.427  35.038 1.00 63.22  ? 98  LYS B CB  1 
ATOM   2817 C CG  . LYS B 1 98  ? 40.680 19.813  33.789 1.00 63.57  ? 98  LYS B CG  1 
ATOM   2818 C CD  . LYS B 1 98  ? 39.227 19.376  34.009 1.00 65.29  ? 98  LYS B CD  1 
ATOM   2819 C CE  . LYS B 1 98  ? 38.288 20.490  33.587 1.00 66.30  ? 98  LYS B CE  1 
ATOM   2820 N NZ  . LYS B 1 98  ? 38.496 20.765  32.125 1.00 69.93  ? 98  LYS B NZ  1 
ATOM   2821 N N   . GLU B 1 99  ? 43.561 19.683  32.777 1.00 64.82  ? 99  GLU B N   1 
ATOM   2822 C CA  . GLU B 1 99  ? 44.050 20.267  31.548 1.00 64.57  ? 99  GLU B CA  1 
ATOM   2823 C C   . GLU B 1 99  ? 43.258 21.466  31.055 1.00 64.14  ? 99  GLU B C   1 
ATOM   2824 O O   . GLU B 1 99  ? 42.043 21.387  30.845 1.00 63.62  ? 99  GLU B O   1 
ATOM   2825 C CB  . GLU B 1 99  ? 44.205 19.194  30.471 1.00 63.90  ? 99  GLU B CB  1 
ATOM   2826 C CG  . GLU B 1 99  ? 43.156 18.949  29.419 1.00 61.38  ? 99  GLU B CG  1 
ATOM   2827 C CD  . GLU B 1 99  ? 43.036 19.963  28.304 1.00 59.62  ? 99  GLU B CD  1 
ATOM   2828 O OE1 . GLU B 1 99  ? 43.878 20.851  28.080 1.00 59.32  ? 99  GLU B OE1 1 
ATOM   2829 O OE2 . GLU B 1 99  ? 41.989 19.885  27.643 1.00 60.25  ? 99  GLU B OE2 1 
ATOM   2830 N N   . ILE B 1 100 ? 43.956 22.588  30.904 1.00 64.20  ? 100 ILE B N   1 
ATOM   2831 C CA  . ILE B 1 100 ? 43.347 23.756  30.277 1.00 65.50  ? 100 ILE B CA  1 
ATOM   2832 C C   . ILE B 1 100 ? 44.268 24.238  29.154 1.00 67.03  ? 100 ILE B C   1 
ATOM   2833 O O   . ILE B 1 100 ? 44.398 25.419  28.795 1.00 66.98  ? 100 ILE B O   1 
ATOM   2834 C CB  . ILE B 1 100 ? 42.895 24.900  31.189 1.00 62.13  ? 100 ILE B CB  1 
ATOM   2835 C CG1 . ILE B 1 100 ? 43.957 25.319  32.192 1.00 61.11  ? 100 ILE B CG1 1 
ATOM   2836 C CG2 . ILE B 1 100 ? 41.607 24.586  31.924 1.00 57.17  ? 100 ILE B CG2 1 
ATOM   2837 C CD1 . ILE B 1 100 ? 43.844 26.716  32.750 1.00 60.25  ? 100 ILE B CD1 1 
ATOM   2838 N N   . ASN B 1 101 ? 44.602 23.259  28.283 1.00 68.55  ? 101 ASN B N   1 
ATOM   2839 C CA  . ASN B 1 101 ? 45.397 23.516  27.087 1.00 69.82  ? 101 ASN B CA  1 
ATOM   2840 C C   . ASN B 1 101 ? 44.601 24.502  26.226 1.00 70.44  ? 101 ASN B C   1 
ATOM   2841 O O   . ASN B 1 101 ? 45.041 25.600  25.912 1.00 69.40  ? 101 ASN B O   1 
ATOM   2842 C CB  . ASN B 1 101 ? 45.736 22.300  26.265 1.00 72.23  ? 101 ASN B CB  1 
ATOM   2843 C CG  . ASN B 1 101 ? 46.607 21.271  26.958 1.00 74.90  ? 101 ASN B CG  1 
ATOM   2844 O OD1 . ASN B 1 101 ? 47.714 21.588  27.443 1.00 75.86  ? 101 ASN B OD1 1 
ATOM   2845 N ND2 . ASN B 1 101 ? 46.065 20.041  26.988 1.00 73.19  ? 101 ASN B ND2 1 
ATOM   2846 N N   . ASP B 1 102 ? 43.297 24.267  26.212 1.00 71.55  ? 102 ASP B N   1 
ATOM   2847 C CA  . ASP B 1 102 ? 42.322 25.139  25.602 1.00 73.19  ? 102 ASP B CA  1 
ATOM   2848 C C   . ASP B 1 102 ? 42.553 26.631  25.790 1.00 73.38  ? 102 ASP B C   1 
ATOM   2849 O O   . ASP B 1 102 ? 42.068 27.386  24.931 1.00 73.45  ? 102 ASP B O   1 
ATOM   2850 C CB  . ASP B 1 102 ? 40.942 24.713  26.071 1.00 77.83  ? 102 ASP B CB  1 
ATOM   2851 C CG  . ASP B 1 102 ? 40.823 23.781  27.266 1.00 81.87  ? 102 ASP B CG  1 
ATOM   2852 O OD1 . ASP B 1 102 ? 41.032 22.537  27.083 1.00 83.25  ? 102 ASP B OD1 1 
ATOM   2853 O OD2 . ASP B 1 102 ? 40.390 24.240  28.375 1.00 80.85  ? 102 ASP B OD2 1 
ATOM   2854 N N   . ILE B 1 103 ? 43.064 27.107  26.912 1.00 72.80  ? 103 ILE B N   1 
ATOM   2855 C CA  . ILE B 1 103 ? 43.223 28.505  27.238 1.00 72.25  ? 103 ILE B CA  1 
ATOM   2856 C C   . ILE B 1 103 ? 44.684 28.877  27.349 1.00 72.11  ? 103 ILE B C   1 
ATOM   2857 O O   . ILE B 1 103 ? 45.010 30.037  27.604 1.00 72.99  ? 103 ILE B O   1 
ATOM   2858 C CB  . ILE B 1 103 ? 42.542 28.803  28.585 1.00 72.21  ? 103 ILE B CB  1 
ATOM   2859 C CG1 . ILE B 1 103 ? 41.038 28.526  28.385 1.00 71.60  ? 103 ILE B CG1 1 
ATOM   2860 C CG2 . ILE B 1 103 ? 42.720 30.124  29.260 1.00 70.54  ? 103 ILE B CG2 1 
ATOM   2861 C CD1 . ILE B 1 103 ? 40.809 27.153  28.981 1.00 74.83  ? 103 ILE B CD1 1 
ATOM   2862 N N   . CYS B 1 104 ? 45.611 27.951  27.447 1.00 71.50  ? 104 CYS B N   1 
ATOM   2863 C CA  . CYS B 1 104 ? 47.036 28.187  27.386 1.00 70.57  ? 104 CYS B CA  1 
ATOM   2864 C C   . CYS B 1 104 ? 47.688 26.799  27.402 1.00 70.65  ? 104 CYS B C   1 
ATOM   2865 O O   . CYS B 1 104 ? 47.072 25.872  27.920 1.00 70.78  ? 104 CYS B O   1 
ATOM   2866 C CB  . CYS B 1 104 ? 47.825 28.988  28.384 1.00 67.13  ? 104 CYS B CB  1 
ATOM   2867 S SG  . CYS B 1 104 ? 47.351 28.926  30.116 1.00 66.14  ? 104 CYS B SG  1 
ATOM   2868 N N   . SER B 1 105 ? 48.971 26.767  27.086 1.00 70.77  ? 105 SER B N   1 
ATOM   2869 C CA  . SER B 1 105 ? 49.517 25.438  26.858 1.00 70.37  ? 105 SER B CA  1 
ATOM   2870 C C   . SER B 1 105 ? 50.363 24.879  27.955 1.00 69.81  ? 105 SER B C   1 
ATOM   2871 O O   . SER B 1 105 ? 51.200 25.522  28.550 1.00 69.79  ? 105 SER B O   1 
ATOM   2872 C CB  . SER B 1 105 ? 50.141 25.319  25.468 1.00 71.72  ? 105 SER B CB  1 
ATOM   2873 O OG  . SER B 1 105 ? 49.180 24.667  24.635 1.00 72.56  ? 105 SER B OG  1 
ATOM   2874 N N   . GLY B 1 106 ? 49.975 23.650  28.289 1.00 69.45  ? 106 GLY B N   1 
ATOM   2875 C CA  . GLY B 1 106 ? 50.494 22.914  29.440 1.00 68.87  ? 106 GLY B CA  1 
ATOM   2876 C C   . GLY B 1 106 ? 49.921 23.453  30.758 1.00 68.32  ? 106 GLY B C   1 
ATOM   2877 O O   . GLY B 1 106 ? 50.387 23.152  31.857 1.00 68.36  ? 106 GLY B O   1 
ATOM   2878 N N   . CYS B 1 107 ? 48.903 24.298  30.696 1.00 67.18  ? 107 CYS B N   1 
ATOM   2879 C CA  . CYS B 1 107 ? 48.285 24.937  31.825 1.00 65.76  ? 107 CYS B CA  1 
ATOM   2880 C C   . CYS B 1 107 ? 47.257 23.972  32.427 1.00 64.66  ? 107 CYS B C   1 
ATOM   2881 O O   . CYS B 1 107 ? 46.562 23.328  31.637 1.00 63.65  ? 107 CYS B O   1 
ATOM   2882 C CB  . CYS B 1 107 ? 47.583 26.223  31.389 1.00 65.49  ? 107 CYS B CB  1 
ATOM   2883 S SG  . CYS B 1 107 ? 48.638 27.639  31.046 1.00 63.58  ? 107 CYS B SG  1 
ATOM   2884 N N   . ARG B 1 108 ? 47.148 24.003  33.762 1.00 62.80  ? 108 ARG B N   1 
ATOM   2885 C CA  . ARG B 1 108 ? 46.145 23.161  34.398 1.00 61.65  ? 108 ARG B CA  1 
ATOM   2886 C C   . ARG B 1 108 ? 45.371 24.053  35.375 1.00 60.71  ? 108 ARG B C   1 
ATOM   2887 O O   . ARG B 1 108 ? 45.938 24.862  36.119 1.00 60.81  ? 108 ARG B O   1 
ATOM   2888 C CB  . ARG B 1 108 ? 46.688 21.917  35.065 1.00 62.12  ? 108 ARG B CB  1 
ATOM   2889 C CG  . ARG B 1 108 ? 47.806 21.097  34.475 1.00 62.00  ? 108 ARG B CG  1 
ATOM   2890 C CD  . ARG B 1 108 ? 48.114 19.822  35.277 1.00 62.24  ? 108 ARG B CD  1 
ATOM   2891 N NE  . ARG B 1 108 ? 47.168 18.782  34.897 1.00 63.63  ? 108 ARG B NE  1 
ATOM   2892 C CZ  . ARG B 1 108 ? 46.487 18.005  35.723 1.00 65.02  ? 108 ARG B CZ  1 
ATOM   2893 N NH1 . ARG B 1 108 ? 46.695 18.064  37.037 1.00 68.79  ? 108 ARG B NH1 1 
ATOM   2894 N NH2 . ARG B 1 108 ? 45.573 17.170  35.247 1.00 64.50  ? 108 ARG B NH2 1 
ATOM   2895 N N   . GLY B 1 109 ? 44.050 23.907  35.367 1.00 59.27  ? 109 GLY B N   1 
ATOM   2896 C CA  . GLY B 1 109 ? 43.231 24.739  36.229 1.00 57.74  ? 109 GLY B CA  1 
ATOM   2897 C C   . GLY B 1 109 ? 42.404 23.889  37.185 1.00 57.10  ? 109 GLY B C   1 
ATOM   2898 O O   . GLY B 1 109 ? 42.048 22.761  36.848 1.00 56.66  ? 109 GLY B O   1 
ATOM   2899 N N   . HIS B 1 110 ? 41.963 24.546  38.266 1.00 56.01  ? 110 HIS B N   1 
ATOM   2900 C CA  . HIS B 1 110 ? 41.045 23.908  39.209 1.00 55.47  ? 110 HIS B CA  1 
ATOM   2901 C C   . HIS B 1 110 ? 39.946 23.259  38.397 1.00 55.35  ? 110 HIS B C   1 
ATOM   2902 O O   . HIS B 1 110 ? 39.424 23.940  37.531 1.00 55.35  ? 110 HIS B O   1 
ATOM   2903 C CB  . HIS B 1 110 ? 40.508 24.945  40.209 1.00 50.91  ? 110 HIS B CB  1 
ATOM   2904 C CG  . HIS B 1 110 ? 39.566 24.358  41.222 1.00 47.57  ? 110 HIS B CG  1 
ATOM   2905 N ND1 . HIS B 1 110 ? 38.194 24.308  40.990 1.00 45.19  ? 110 HIS B ND1 1 
ATOM   2906 C CD2 . HIS B 1 110 ? 39.795 23.779  42.423 1.00 46.00  ? 110 HIS B CD2 1 
ATOM   2907 C CE1 . HIS B 1 110 ? 37.614 23.703  42.005 1.00 47.94  ? 110 HIS B CE1 1 
ATOM   2908 N NE2 . HIS B 1 110 ? 38.567 23.366  42.890 1.00 49.05  ? 110 HIS B NE2 1 
ATOM   2909 N N   . ASP B 1 111 ? 39.355 22.136  38.720 1.00 56.07  ? 111 ASP B N   1 
ATOM   2910 C CA  . ASP B 1 111 ? 38.511 21.472  37.725 1.00 56.33  ? 111 ASP B CA  1 
ATOM   2911 C C   . ASP B 1 111 ? 37.076 21.874  37.893 1.00 55.11  ? 111 ASP B C   1 
ATOM   2912 O O   . ASP B 1 111 ? 36.404 22.075  36.872 1.00 55.50  ? 111 ASP B O   1 
ATOM   2913 C CB  . ASP B 1 111 ? 38.899 19.999  37.548 1.00 59.29  ? 111 ASP B CB  1 
ATOM   2914 C CG  . ASP B 1 111 ? 37.669 19.179  37.227 1.00 61.79  ? 111 ASP B CG  1 
ATOM   2915 O OD1 . ASP B 1 111 ? 37.147 19.066  36.089 1.00 64.25  ? 111 ASP B OD1 1 
ATOM   2916 O OD2 . ASP B 1 111 ? 36.958 18.713  38.130 1.00 64.06  ? 111 ASP B OD2 1 
ATOM   2917 N N   . GLY B 1 112 ? 36.617 22.218  39.061 1.00 54.80  ? 112 GLY B N   1 
ATOM   2918 C CA  . GLY B 1 112 ? 35.214 22.693  39.107 1.00 54.32  ? 112 GLY B CA  1 
ATOM   2919 C C   . GLY B 1 112 ? 35.171 24.080  38.482 1.00 53.97  ? 112 GLY B C   1 
ATOM   2920 O O   . GLY B 1 112 ? 34.183 24.409  37.827 1.00 54.22  ? 112 GLY B O   1 
ATOM   2921 N N   . PHE B 1 113 ? 36.087 24.992  38.808 1.00 53.20  ? 113 PHE B N   1 
ATOM   2922 C CA  . PHE B 1 113 ? 36.045 26.363  38.332 1.00 52.07  ? 113 PHE B CA  1 
ATOM   2923 C C   . PHE B 1 113 ? 36.043 26.360  36.819 1.00 53.17  ? 113 PHE B C   1 
ATOM   2924 O O   . PHE B 1 113 ? 35.103 26.817  36.176 1.00 54.34  ? 113 PHE B O   1 
ATOM   2925 C CB  . PHE B 1 113 ? 37.199 27.224  38.814 1.00 42.47  ? 113 PHE B CB  1 
ATOM   2926 C CG  . PHE B 1 113 ? 37.392 27.294  40.307 1.00 34.29  ? 113 PHE B CG  1 
ATOM   2927 C CD1 . PHE B 1 113 ? 36.336 27.050  41.181 1.00 30.20  ? 113 PHE B CD1 1 
ATOM   2928 C CD2 . PHE B 1 113 ? 38.635 27.639  40.809 1.00 28.90  ? 113 PHE B CD2 1 
ATOM   2929 C CE1 . PHE B 1 113 ? 36.554 27.117  42.537 1.00 28.80  ? 113 PHE B CE1 1 
ATOM   2930 C CE2 . PHE B 1 113 ? 38.846 27.733  42.168 1.00 27.03  ? 113 PHE B CE2 1 
ATOM   2931 C CZ  . PHE B 1 113 ? 37.802 27.426  43.028 1.00 28.49  ? 113 PHE B CZ  1 
ATOM   2932 N N   . THR B 1 114 ? 37.108 25.792  36.282 1.00 53.65  ? 114 THR B N   1 
ATOM   2933 C CA  . THR B 1 114 ? 37.244 25.650  34.830 1.00 53.82  ? 114 THR B CA  1 
ATOM   2934 C C   . THR B 1 114 ? 35.982 25.085  34.198 1.00 53.82  ? 114 THR B C   1 
ATOM   2935 O O   . THR B 1 114 ? 35.477 25.600  33.214 1.00 53.54  ? 114 THR B O   1 
ATOM   2936 C CB  . THR B 1 114 ? 38.437 24.687  34.609 1.00 53.64  ? 114 THR B CB  1 
ATOM   2937 O OG1 . THR B 1 114 ? 39.642 25.386  34.948 1.00 52.15  ? 114 THR B OG1 1 
ATOM   2938 C CG2 . THR B 1 114 ? 38.512 24.224  33.163 1.00 56.02  ? 114 THR B CG2 1 
ATOM   2939 N N   . SER B 1 115 ? 35.467 23.965  34.692 1.00 54.16  ? 115 SER B N   1 
ATOM   2940 C CA  . SER B 1 115 ? 34.292 23.323  34.175 1.00 54.40  ? 115 SER B CA  1 
ATOM   2941 C C   . SER B 1 115 ? 33.065 24.196  34.329 1.00 54.29  ? 115 SER B C   1 
ATOM   2942 O O   . SER B 1 115 ? 32.174 24.030  33.517 1.00 55.13  ? 115 SER B O   1 
ATOM   2943 C CB  . SER B 1 115 ? 33.912 22.023  34.920 1.00 54.61  ? 115 SER B CB  1 
ATOM   2944 O OG  . SER B 1 115 ? 34.993 21.123  34.968 1.00 52.52  ? 115 SER B OG  1 
ATOM   2945 N N   . SER B 1 116 ? 32.972 24.913  35.433 1.00 54.86  ? 116 SER B N   1 
ATOM   2946 C CA  . SER B 1 116 ? 31.778 25.713  35.665 1.00 55.04  ? 116 SER B CA  1 
ATOM   2947 C C   . SER B 1 116 ? 31.734 26.788  34.579 1.00 55.12  ? 116 SER B C   1 
ATOM   2948 O O   . SER B 1 116 ? 30.691 26.976  33.952 1.00 54.44  ? 116 SER B O   1 
ATOM   2949 C CB  . SER B 1 116 ? 31.729 26.358  37.037 1.00 55.06  ? 116 SER B CB  1 
ATOM   2950 O OG  . SER B 1 116 ? 31.845 25.447  38.088 1.00 53.55  ? 116 SER B OG  1 
ATOM   2951 N N   . TRP B 1 117 ? 32.861 27.486  34.447 1.00 55.42  ? 117 TRP B N   1 
ATOM   2952 C CA  . TRP B 1 117 ? 32.912 28.535  33.433 1.00 57.00  ? 117 TRP B CA  1 
ATOM   2953 C C   . TRP B 1 117 ? 32.530 27.969  32.062 1.00 57.93  ? 117 TRP B C   1 
ATOM   2954 O O   . TRP B 1 117 ? 31.618 28.474  31.410 1.00 57.94  ? 117 TRP B O   1 
ATOM   2955 C CB  . TRP B 1 117 ? 34.264 29.208  33.299 1.00 54.08  ? 117 TRP B CB  1 
ATOM   2956 C CG  . TRP B 1 117 ? 34.327 30.111  32.093 1.00 54.72  ? 117 TRP B CG  1 
ATOM   2957 C CD1 . TRP B 1 117 ? 35.255 30.040  31.086 1.00 52.98  ? 117 TRP B CD1 1 
ATOM   2958 C CD2 . TRP B 1 117 ? 33.455 31.192  31.770 1.00 53.65  ? 117 TRP B CD2 1 
ATOM   2959 N NE1 . TRP B 1 117 ? 35.008 31.022  30.170 1.00 54.23  ? 117 TRP B NE1 1 
ATOM   2960 C CE2 . TRP B 1 117 ? 33.908 31.748  30.565 1.00 55.70  ? 117 TRP B CE2 1 
ATOM   2961 C CE3 . TRP B 1 117 ? 32.342 31.764  32.374 1.00 55.55  ? 117 TRP B CE3 1 
ATOM   2962 C CZ2 . TRP B 1 117 ? 33.283 32.853  29.962 1.00 55.69  ? 117 TRP B CZ2 1 
ATOM   2963 C CZ3 . TRP B 1 117 ? 31.724 32.851  31.788 1.00 54.39  ? 117 TRP B CZ3 1 
ATOM   2964 C CH2 . TRP B 1 117 ? 32.197 33.381  30.584 1.00 54.10  ? 117 TRP B CH2 1 
ATOM   2965 N N   . ARG B 1 118 ? 33.263 26.928  31.686 1.00 58.65  ? 118 ARG B N   1 
ATOM   2966 C CA  . ARG B 1 118 ? 33.087 26.225  30.423 1.00 60.49  ? 118 ARG B CA  1 
ATOM   2967 C C   . ARG B 1 118 ? 31.640 25.853  30.152 1.00 60.66  ? 118 ARG B C   1 
ATOM   2968 O O   . ARG B 1 118 ? 31.128 26.219  29.083 1.00 61.15  ? 118 ARG B O   1 
ATOM   2969 C CB  . ARG B 1 118 ? 34.063 25.068  30.336 1.00 64.34  ? 118 ARG B CB  1 
ATOM   2970 C CG  . ARG B 1 118 ? 33.939 23.945  29.369 1.00 68.93  ? 118 ARG B CG  1 
ATOM   2971 C CD  . ARG B 1 118 ? 34.203 24.272  27.906 1.00 76.70  ? 118 ARG B CD  1 
ATOM   2972 N NE  . ARG B 1 118 ? 34.453 25.664  27.584 1.00 81.72  ? 118 ARG B NE  1 
ATOM   2973 C CZ  . ARG B 1 118 ? 35.576 26.373  27.541 1.00 83.12  ? 118 ARG B CZ  1 
ATOM   2974 N NH1 . ARG B 1 118 ? 36.799 25.915  27.761 1.00 83.36  ? 118 ARG B NH1 1 
ATOM   2975 N NH2 . ARG B 1 118 ? 35.428 27.673  27.251 1.00 85.49  ? 118 ARG B NH2 1 
ATOM   2976 N N   . SER B 1 119 ? 30.844 25.460  31.136 1.00 60.18  ? 119 SER B N   1 
ATOM   2977 C CA  . SER B 1 119 ? 29.442 25.175  30.905 1.00 59.90  ? 119 SER B CA  1 
ATOM   2978 C C   . SER B 1 119 ? 28.623 26.410  30.570 1.00 59.62  ? 119 SER B C   1 
ATOM   2979 O O   . SER B 1 119 ? 27.574 26.306  29.929 1.00 59.39  ? 119 SER B O   1 
ATOM   2980 C CB  . SER B 1 119 ? 28.843 24.469  32.125 1.00 61.58  ? 119 SER B CB  1 
ATOM   2981 O OG  . SER B 1 119 ? 27.423 24.614  32.094 1.00 64.38  ? 119 SER B OG  1 
ATOM   2982 N N   . VAL B 1 120 ? 29.020 27.581  31.041 1.00 59.47  ? 120 VAL B N   1 
ATOM   2983 C CA  . VAL B 1 120 ? 28.225 28.786  30.862 1.00 59.45  ? 120 VAL B CA  1 
ATOM   2984 C C   . VAL B 1 120 ? 28.945 29.735  29.913 1.00 59.50  ? 120 VAL B C   1 
ATOM   2985 O O   . VAL B 1 120 ? 28.377 30.741  29.513 1.00 59.46  ? 120 VAL B O   1 
ATOM   2986 C CB  . VAL B 1 120 ? 27.925 29.515  32.179 1.00 60.06  ? 120 VAL B CB  1 
ATOM   2987 C CG1 . VAL B 1 120 ? 27.075 28.694  33.132 1.00 57.79  ? 120 VAL B CG1 1 
ATOM   2988 C CG2 . VAL B 1 120 ? 29.219 29.937  32.868 1.00 61.00  ? 120 VAL B CG2 1 
ATOM   2989 N N   . ALA B 1 121 ? 30.097 29.312  29.436 1.00 59.73  ? 121 ALA B N   1 
ATOM   2990 C CA  . ALA B 1 121 ? 30.961 30.056  28.548 1.00 60.44  ? 121 ALA B CA  1 
ATOM   2991 C C   . ALA B 1 121 ? 30.307 30.617  27.321 1.00 61.25  ? 121 ALA B C   1 
ATOM   2992 O O   . ALA B 1 121 ? 30.083 31.845  27.326 1.00 61.61  ? 121 ALA B O   1 
ATOM   2993 C CB  . ALA B 1 121 ? 32.283 29.317  28.357 1.00 56.76  ? 121 ALA B CB  1 
ATOM   2994 N N   . ASP B 1 122 ? 30.083 29.941  26.211 1.00 62.26  ? 122 ASP B N   1 
ATOM   2995 C CA  . ASP B 1 122 ? 29.386 30.398  25.024 1.00 62.28  ? 122 ASP B CA  1 
ATOM   2996 C C   . ASP B 1 122 ? 28.239 31.365  25.268 1.00 62.08  ? 122 ASP B C   1 
ATOM   2997 O O   . ASP B 1 122 ? 28.227 32.396  24.600 1.00 62.19  ? 122 ASP B O   1 
ATOM   2998 C CB  . ASP B 1 122 ? 28.790 29.220  24.244 1.00 65.87  ? 122 ASP B CB  1 
ATOM   2999 C CG  . ASP B 1 122 ? 29.793 28.241  23.678 1.00 70.25  ? 122 ASP B CG  1 
ATOM   3000 O OD1 . ASP B 1 122 ? 30.969 28.597  23.415 1.00 72.20  ? 122 ASP B OD1 1 
ATOM   3001 O OD2 . ASP B 1 122 ? 29.417 27.060  23.471 1.00 72.59  ? 122 ASP B OD2 1 
ATOM   3002 N N   . THR B 1 123 ? 27.240 31.069  26.102 1.00 61.72  ? 123 THR B N   1 
ATOM   3003 C CA  . THR B 1 123 ? 26.191 32.060  26.356 1.00 61.63  ? 123 THR B CA  1 
ATOM   3004 C C   . THR B 1 123 ? 26.791 33.368  26.871 1.00 61.45  ? 123 THR B C   1 
ATOM   3005 O O   . THR B 1 123 ? 26.377 34.418  26.395 1.00 60.42  ? 123 THR B O   1 
ATOM   3006 C CB  . THR B 1 123 ? 25.131 31.520  27.333 1.00 60.67  ? 123 THR B CB  1 
ATOM   3007 O OG1 . THR B 1 123 ? 24.757 30.263  26.784 1.00 59.39  ? 123 THR B OG1 1 
ATOM   3008 C CG2 . THR B 1 123 ? 23.921 32.402  27.589 1.00 60.22  ? 123 THR B CG2 1 
ATOM   3009 N N   . LEU B 1 124 ? 27.618 33.329  27.921 1.00 61.44  ? 124 LEU B N   1 
ATOM   3010 C CA  . LEU B 1 124 ? 28.062 34.607  28.486 1.00 61.71  ? 124 LEU B CA  1 
ATOM   3011 C C   . LEU B 1 124 ? 28.849 35.511  27.566 1.00 61.57  ? 124 LEU B C   1 
ATOM   3012 O O   . LEU B 1 124 ? 28.352 36.584  27.193 1.00 61.48  ? 124 LEU B O   1 
ATOM   3013 C CB  . LEU B 1 124 ? 28.627 34.344  29.881 1.00 59.17  ? 124 LEU B CB  1 
ATOM   3014 C CG  . LEU B 1 124 ? 27.545 33.940  30.901 1.00 57.38  ? 124 LEU B CG  1 
ATOM   3015 C CD1 . LEU B 1 124 ? 28.117 33.985  32.313 1.00 55.99  ? 124 LEU B CD1 1 
ATOM   3016 C CD2 . LEU B 1 124 ? 26.282 34.781  30.795 1.00 55.02  ? 124 LEU B CD2 1 
ATOM   3017 N N   . ARG B 1 125 ? 29.810 34.999  26.839 1.00 61.82  ? 125 ARG B N   1 
ATOM   3018 C CA  . ARG B 1 125 ? 30.552 35.630  25.787 1.00 62.24  ? 125 ARG B CA  1 
ATOM   3019 C C   . ARG B 1 125 ? 29.608 36.138  24.706 1.00 61.26  ? 125 ARG B C   1 
ATOM   3020 O O   . ARG B 1 125 ? 29.807 37.277  24.277 1.00 60.73  ? 125 ARG B O   1 
ATOM   3021 C CB  . ARG B 1 125 ? 31.600 34.631  25.326 1.00 67.33  ? 125 ARG B CB  1 
ATOM   3022 C CG  . ARG B 1 125 ? 31.474 34.012  23.957 1.00 72.47  ? 125 ARG B CG  1 
ATOM   3023 C CD  . ARG B 1 125 ? 32.539 34.513  23.027 1.00 76.05  ? 125 ARG B CD  1 
ATOM   3024 N NE  . ARG B 1 125 ? 33.633 33.600  22.713 1.00 82.42  ? 125 ARG B NE  1 
ATOM   3025 C CZ  . ARG B 1 125 ? 34.591 33.951  21.836 1.00 85.99  ? 125 ARG B CZ  1 
ATOM   3026 N NH1 . ARG B 1 125 ? 34.527 35.159  21.258 1.00 89.40  ? 125 ARG B NH1 1 
ATOM   3027 N NH2 . ARG B 1 125 ? 35.621 33.197  21.481 1.00 85.42  ? 125 ARG B NH2 1 
ATOM   3028 N N   . GLN B 1 126 ? 28.469 35.487  24.507 1.00 60.32  ? 126 GLN B N   1 
ATOM   3029 C CA  . GLN B 1 126 ? 27.428 35.906  23.595 1.00 59.55  ? 126 GLN B CA  1 
ATOM   3030 C C   . GLN B 1 126 ? 26.738 37.166  24.082 1.00 57.74  ? 126 GLN B C   1 
ATOM   3031 O O   . GLN B 1 126 ? 26.697 38.183  23.407 1.00 56.87  ? 126 GLN B O   1 
ATOM   3032 C CB  . GLN B 1 126 ? 26.381 34.812  23.372 1.00 66.85  ? 126 GLN B CB  1 
ATOM   3033 C CG  . GLN B 1 126 ? 25.256 35.023  22.386 1.00 71.35  ? 126 GLN B CG  1 
ATOM   3034 C CD  . GLN B 1 126 ? 23.866 35.252  22.951 1.00 74.38  ? 126 GLN B CD  1 
ATOM   3035 O OE1 . GLN B 1 126 ? 23.421 34.580  23.896 1.00 75.61  ? 126 GLN B OE1 1 
ATOM   3036 N NE2 . GLN B 1 126 ? 23.150 36.212  22.354 1.00 72.74  ? 126 GLN B NE2 1 
ATOM   3037 N N   . LYS B 1 127 ? 26.491 37.220  25.387 1.00 57.35  ? 127 LYS B N   1 
ATOM   3038 C CA  . LYS B 1 127 ? 25.786 38.366  25.947 1.00 55.25  ? 127 LYS B CA  1 
ATOM   3039 C C   . LYS B 1 127 ? 26.727 39.548  25.943 1.00 54.30  ? 127 LYS B C   1 
ATOM   3040 O O   . LYS B 1 127 ? 26.447 40.662  25.474 1.00 53.91  ? 127 LYS B O   1 
ATOM   3041 C CB  . LYS B 1 127 ? 25.169 37.941  27.247 1.00 56.37  ? 127 LYS B CB  1 
ATOM   3042 C CG  . LYS B 1 127 ? 23.687 37.649  27.160 1.00 55.83  ? 127 LYS B CG  1 
ATOM   3043 C CD  . LYS B 1 127 ? 23.478 36.143  27.263 1.00 57.53  ? 127 LYS B CD  1 
ATOM   3044 C CE  . LYS B 1 127 ? 21.950 35.964  27.207 1.00 58.96  ? 127 LYS B CE  1 
ATOM   3045 N NZ  . LYS B 1 127 ? 21.342 36.766  26.107 1.00 57.88  ? 127 LYS B NZ  1 
ATOM   3046 N N   . VAL B 1 128 ? 28.001 39.251  26.192 1.00 53.36  ? 128 VAL B N   1 
ATOM   3047 C CA  . VAL B 1 128 ? 29.050 40.267  26.265 1.00 52.40  ? 128 VAL B CA  1 
ATOM   3048 C C   . VAL B 1 128 ? 29.289 40.895  24.898 1.00 52.33  ? 128 VAL B C   1 
ATOM   3049 O O   . VAL B 1 128 ? 29.570 42.084  24.790 1.00 51.13  ? 128 VAL B O   1 
ATOM   3050 C CB  . VAL B 1 128 ? 30.363 39.766  26.856 1.00 49.75  ? 128 VAL B CB  1 
ATOM   3051 C CG1 . VAL B 1 128 ? 31.539 40.737  26.720 1.00 47.15  ? 128 VAL B CG1 1 
ATOM   3052 C CG2 . VAL B 1 128 ? 30.143 39.404  28.320 1.00 48.15  ? 128 VAL B CG2 1 
ATOM   3053 N N   . GLU B 1 129 ? 29.452 40.010  23.921 1.00 52.86  ? 129 GLU B N   1 
ATOM   3054 C CA  . GLU B 1 129 ? 29.534 40.408  22.521 1.00 53.87  ? 129 GLU B CA  1 
ATOM   3055 C C   . GLU B 1 129 ? 28.394 41.339  22.104 1.00 54.34  ? 129 GLU B C   1 
ATOM   3056 O O   . GLU B 1 129 ? 28.676 42.426  21.570 1.00 54.29  ? 129 GLU B O   1 
ATOM   3057 C CB  . GLU B 1 129 ? 29.611 39.184  21.607 1.00 52.15  ? 129 GLU B CB  1 
ATOM   3058 C CG  . GLU B 1 129 ? 31.014 38.901  21.106 1.00 53.13  ? 129 GLU B CG  1 
ATOM   3059 C CD  . GLU B 1 129 ? 31.236 37.425  20.812 1.00 55.36  ? 129 GLU B CD  1 
ATOM   3060 O OE1 . GLU B 1 129 ? 30.274 36.858  20.255 1.00 54.98  ? 129 GLU B OE1 1 
ATOM   3061 O OE2 . GLU B 1 129 ? 32.325 36.901  21.155 1.00 56.72  ? 129 GLU B OE2 1 
ATOM   3062 N N   . ASP B 1 130 ? 27.147 41.045  22.469 1.00 54.39  ? 130 ASP B N   1 
ATOM   3063 C CA  . ASP B 1 130 ? 26.030 41.914  22.163 1.00 54.80  ? 130 ASP B CA  1 
ATOM   3064 C C   . ASP B 1 130 ? 26.144 43.241  22.901 1.00 55.73  ? 130 ASP B C   1 
ATOM   3065 O O   . ASP B 1 130 ? 25.929 44.298  22.294 1.00 56.98  ? 130 ASP B O   1 
ATOM   3066 C CB  . ASP B 1 130 ? 24.678 41.272  22.389 1.00 52.38  ? 130 ASP B CB  1 
ATOM   3067 C CG  . ASP B 1 130 ? 24.410 40.005  21.599 1.00 53.82  ? 130 ASP B CG  1 
ATOM   3068 O OD1 . ASP B 1 130 ? 24.585 39.937  20.359 1.00 51.97  ? 130 ASP B OD1 1 
ATOM   3069 O OD2 . ASP B 1 130 ? 24.007 38.993  22.224 1.00 52.42  ? 130 ASP B OD2 1 
ATOM   3070 N N   . ALA B 1 131 ? 26.768 43.271  24.077 1.00 55.55  ? 131 ALA B N   1 
ATOM   3071 C CA  . ALA B 1 131 ? 26.968 44.557  24.746 1.00 54.74  ? 131 ALA B CA  1 
ATOM   3072 C C   . ALA B 1 131 ? 28.102 45.312  24.083 1.00 54.80  ? 131 ALA B C   1 
ATOM   3073 O O   . ALA B 1 131 ? 28.080 46.539  23.960 1.00 54.33  ? 131 ALA B O   1 
ATOM   3074 C CB  . ALA B 1 131 ? 27.151 44.277  26.226 1.00 52.63  ? 131 ALA B CB  1 
ATOM   3075 N N   . VAL B 1 132 ? 29.164 44.604  23.689 1.00 55.34  ? 132 VAL B N   1 
ATOM   3076 C CA  . VAL B 1 132 ? 30.330 45.172  23.028 1.00 55.09  ? 132 VAL B CA  1 
ATOM   3077 C C   . VAL B 1 132 ? 30.002 45.806  21.687 1.00 55.66  ? 132 VAL B C   1 
ATOM   3078 O O   . VAL B 1 132 ? 30.512 46.897  21.397 1.00 55.23  ? 132 VAL B O   1 
ATOM   3079 C CB  . VAL B 1 132 ? 31.525 44.221  22.928 1.00 54.43  ? 132 VAL B CB  1 
ATOM   3080 C CG1 . VAL B 1 132 ? 32.682 44.793  22.105 1.00 51.56  ? 132 VAL B CG1 1 
ATOM   3081 C CG2 . VAL B 1 132 ? 32.073 43.786  24.291 1.00 51.47  ? 132 VAL B CG2 1 
ATOM   3082 N N   . ARG B 1 133 ? 29.057 45.280  20.920 1.00 56.85  ? 133 ARG B N   1 
ATOM   3083 C CA  . ARG B 1 133 ? 28.610 45.870  19.655 1.00 57.28  ? 133 ARG B CA  1 
ATOM   3084 C C   . ARG B 1 133 ? 27.802 47.124  19.904 1.00 57.24  ? 133 ARG B C   1 
ATOM   3085 O O   . ARG B 1 133 ? 28.163 48.160  19.379 1.00 57.44  ? 133 ARG B O   1 
ATOM   3086 C CB  . ARG B 1 133 ? 27.730 44.898  18.901 1.00 59.90  ? 133 ARG B CB  1 
ATOM   3087 C CG  . ARG B 1 133 ? 27.361 45.226  17.464 1.00 59.87  ? 133 ARG B CG  1 
ATOM   3088 C CD  . ARG B 1 133 ? 26.216 44.293  17.121 1.00 62.24  ? 133 ARG B CD  1 
ATOM   3089 N NE  . ARG B 1 133 ? 24.895 44.914  17.118 1.00 63.31  ? 133 ARG B NE  1 
ATOM   3090 C CZ  . ARG B 1 133 ? 23.868 44.332  17.734 1.00 65.49  ? 133 ARG B CZ  1 
ATOM   3091 N NH1 . ARG B 1 133 ? 24.059 43.183  18.373 1.00 66.65  ? 133 ARG B NH1 1 
ATOM   3092 N NH2 . ARG B 1 133 ? 22.712 44.967  17.646 1.00 67.46  ? 133 ARG B NH2 1 
ATOM   3093 N N   . GLU B 1 134 ? 26.716 47.071  20.644 1.00 58.11  ? 134 GLU B N   1 
ATOM   3094 C CA  . GLU B 1 134 ? 26.002 48.271  21.053 1.00 59.26  ? 134 GLU B CA  1 
ATOM   3095 C C   . GLU B 1 134 ? 26.899 49.376  21.572 1.00 58.59  ? 134 GLU B C   1 
ATOM   3096 O O   . GLU B 1 134 ? 26.670 50.546  21.325 1.00 59.06  ? 134 GLU B O   1 
ATOM   3097 C CB  . GLU B 1 134 ? 25.033 47.975  22.207 1.00 63.23  ? 134 GLU B CB  1 
ATOM   3098 C CG  . GLU B 1 134 ? 23.563 48.009  21.809 1.00 68.49  ? 134 GLU B CG  1 
ATOM   3099 C CD  . GLU B 1 134 ? 23.285 46.727  21.013 1.00 72.31  ? 134 GLU B CD  1 
ATOM   3100 O OE1 . GLU B 1 134 ? 23.295 45.680  21.702 1.00 71.87  ? 134 GLU B OE1 1 
ATOM   3101 O OE2 . GLU B 1 134 ? 23.125 46.861  19.773 1.00 74.38  ? 134 GLU B OE2 1 
ATOM   3102 N N   . HIS B 1 135 ? 27.818 49.125  22.492 1.00 58.68  ? 135 HIS B N   1 
ATOM   3103 C CA  . HIS B 1 135 ? 28.672 50.109  23.132 1.00 58.45  ? 135 HIS B CA  1 
ATOM   3104 C C   . HIS B 1 135 ? 30.136 49.802  22.906 1.00 58.48  ? 135 HIS B C   1 
ATOM   3105 O O   . HIS B 1 135 ? 30.882 49.394  23.800 1.00 59.55  ? 135 HIS B O   1 
ATOM   3106 C CB  . HIS B 1 135 ? 28.410 50.164  24.646 1.00 56.92  ? 135 HIS B CB  1 
ATOM   3107 C CG  . HIS B 1 135 ? 26.951 50.324  24.952 1.00 57.11  ? 135 HIS B CG  1 
ATOM   3108 N ND1 . HIS B 1 135 ? 26.338 51.558  25.063 1.00 57.42  ? 135 HIS B ND1 1 
ATOM   3109 C CD2 . HIS B 1 135 ? 25.998 49.371  25.108 1.00 56.85  ? 135 HIS B CD2 1 
ATOM   3110 C CE1 . HIS B 1 135 ? 25.052 51.343  25.299 1.00 59.13  ? 135 HIS B CE1 1 
ATOM   3111 N NE2 . HIS B 1 135 ? 24.811 50.027  25.340 1.00 58.09  ? 135 HIS B NE2 1 
ATOM   3112 N N   . PRO B 1 136 ? 30.599 49.995  21.677 1.00 57.80  ? 136 PRO B N   1 
ATOM   3113 C CA  . PRO B 1 136 ? 31.954 49.701  21.279 1.00 56.58  ? 136 PRO B CA  1 
ATOM   3114 C C   . PRO B 1 136 ? 32.980 50.452  22.094 1.00 55.12  ? 136 PRO B C   1 
ATOM   3115 O O   . PRO B 1 136 ? 34.105 50.003  22.219 1.00 54.73  ? 136 PRO B O   1 
ATOM   3116 C CB  . PRO B 1 136 ? 32.042 50.169  19.824 1.00 57.21  ? 136 PRO B CB  1 
ATOM   3117 C CG  . PRO B 1 136 ? 30.868 51.045  19.590 1.00 56.83  ? 136 PRO B CG  1 
ATOM   3118 C CD  . PRO B 1 136 ? 29.827 50.583  20.542 1.00 57.66  ? 136 PRO B CD  1 
ATOM   3119 N N   . ASP B 1 137 ? 32.656 51.683  22.426 1.00 54.21  ? 137 ASP B N   1 
ATOM   3120 C CA  . ASP B 1 137 ? 33.545 52.544  23.182 1.00 53.13  ? 137 ASP B CA  1 
ATOM   3121 C C   . ASP B 1 137 ? 33.834 51.976  24.569 1.00 50.68  ? 137 ASP B C   1 
ATOM   3122 O O   . ASP B 1 137 ? 34.902 52.292  25.024 1.00 51.13  ? 137 ASP B O   1 
ATOM   3123 C CB  . ASP B 1 137 ? 33.010 53.964  23.289 1.00 58.86  ? 137 ASP B CB  1 
ATOM   3124 C CG  . ASP B 1 137 ? 31.502 54.210  23.340 1.00 62.40  ? 137 ASP B CG  1 
ATOM   3125 O OD1 . ASP B 1 137 ? 30.759 53.425  22.675 1.00 57.33  ? 137 ASP B OD1 1 
ATOM   3126 O OD2 . ASP B 1 137 ? 31.075 55.216  24.028 1.00 63.24  ? 137 ASP B OD2 1 
ATOM   3127 N N   . TYR B 1 138 ? 32.846 51.566  25.309 1.00 48.28  ? 138 TYR B N   1 
ATOM   3128 C CA  . TYR B 1 138 ? 32.757 51.159  26.678 1.00 46.40  ? 138 TYR B CA  1 
ATOM   3129 C C   . TYR B 1 138 ? 33.642 49.952  26.960 1.00 46.59  ? 138 TYR B C   1 
ATOM   3130 O O   . TYR B 1 138 ? 33.781 49.083  26.112 1.00 47.49  ? 138 TYR B O   1 
ATOM   3131 C CB  . TYR B 1 138 ? 31.290 50.758  26.913 1.00 44.08  ? 138 TYR B CB  1 
ATOM   3132 C CG  . TYR B 1 138 ? 30.273 51.868  27.079 1.00 40.84  ? 138 TYR B CG  1 
ATOM   3133 C CD1 . TYR B 1 138 ? 30.297 53.139  26.460 1.00 38.28  ? 138 TYR B CD1 1 
ATOM   3134 C CD2 . TYR B 1 138 ? 29.244 51.574  27.952 1.00 39.08  ? 138 TYR B CD2 1 
ATOM   3135 C CE1 . TYR B 1 138 ? 29.322 54.056  26.770 1.00 36.61  ? 138 TYR B CE1 1 
ATOM   3136 C CE2 . TYR B 1 138 ? 28.236 52.473  28.189 1.00 37.88  ? 138 TYR B CE2 1 
ATOM   3137 C CZ  . TYR B 1 138 ? 28.293 53.714  27.604 1.00 36.95  ? 138 TYR B CZ  1 
ATOM   3138 O OH  . TYR B 1 138 ? 27.239 54.518  27.915 1.00 36.86  ? 138 TYR B OH  1 
ATOM   3139 N N   . ARG B 1 139 ? 34.380 49.883  28.037 1.00 45.78  ? 139 ARG B N   1 
ATOM   3140 C CA  . ARG B 1 139 ? 35.296 48.980  28.628 1.00 44.59  ? 139 ARG B CA  1 
ATOM   3141 C C   . ARG B 1 139 ? 34.557 47.802  29.304 1.00 44.36  ? 139 ARG B C   1 
ATOM   3142 O O   . ARG B 1 139 ? 33.670 47.991  30.139 1.00 44.51  ? 139 ARG B O   1 
ATOM   3143 C CB  . ARG B 1 139 ? 36.007 49.733  29.737 1.00 42.72  ? 139 ARG B CB  1 
ATOM   3144 C CG  . ARG B 1 139 ? 37.240 49.141  30.367 1.00 47.14  ? 139 ARG B CG  1 
ATOM   3145 C CD  . ARG B 1 139 ? 37.419 49.864  31.705 1.00 53.64  ? 139 ARG B CD  1 
ATOM   3146 N NE  . ARG B 1 139 ? 38.344 49.305  32.690 1.00 52.52  ? 139 ARG B NE  1 
ATOM   3147 C CZ  . ARG B 1 139 ? 38.651 50.004  33.785 1.00 55.09  ? 139 ARG B CZ  1 
ATOM   3148 N NH1 . ARG B 1 139 ? 38.107 51.206  34.007 1.00 55.70  ? 139 ARG B NH1 1 
ATOM   3149 N NH2 . ARG B 1 139 ? 39.527 49.471  34.634 1.00 55.79  ? 139 ARG B NH2 1 
ATOM   3150 N N   . VAL B 1 140 ? 34.924 46.603  28.883 1.00 42.40  ? 140 VAL B N   1 
ATOM   3151 C CA  . VAL B 1 140 ? 34.521 45.387  29.487 1.00 41.46  ? 140 VAL B CA  1 
ATOM   3152 C C   . VAL B 1 140 ? 35.333 45.075  30.741 1.00 41.90  ? 140 VAL B C   1 
ATOM   3153 O O   . VAL B 1 140 ? 36.559 44.972  30.645 1.00 41.10  ? 140 VAL B O   1 
ATOM   3154 C CB  . VAL B 1 140 ? 34.662 44.131  28.592 1.00 41.58  ? 140 VAL B CB  1 
ATOM   3155 C CG1 . VAL B 1 140 ? 33.995 42.995  29.385 1.00 39.95  ? 140 VAL B CG1 1 
ATOM   3156 C CG2 . VAL B 1 140 ? 34.067 44.430  27.219 1.00 35.85  ? 140 VAL B CG2 1 
ATOM   3157 N N   . VAL B 1 141 ? 34.561 44.855  31.813 1.00 40.83  ? 141 VAL B N   1 
ATOM   3158 C CA  . VAL B 1 141 ? 35.169 44.535  33.100 1.00 39.67  ? 141 VAL B CA  1 
ATOM   3159 C C   . VAL B 1 141 ? 34.508 43.269  33.640 1.00 38.95  ? 141 VAL B C   1 
ATOM   3160 O O   . VAL B 1 141 ? 33.281 43.164  33.660 1.00 38.63  ? 141 VAL B O   1 
ATOM   3161 C CB  . VAL B 1 141 ? 34.981 45.631  34.193 1.00 38.58  ? 141 VAL B CB  1 
ATOM   3162 C CG1 . VAL B 1 141 ? 35.750 45.202  35.447 1.00 36.12  ? 141 VAL B CG1 1 
ATOM   3163 C CG2 . VAL B 1 141 ? 35.572 46.970  33.755 1.00 37.46  ? 141 VAL B CG2 1 
ATOM   3164 N N   . PHE B 1 142 ? 35.309 42.258  33.932 1.00 38.96  ? 142 PHE B N   1 
ATOM   3165 C CA  . PHE B 1 142 ? 34.798 41.089  34.654 1.00 38.22  ? 142 PHE B CA  1 
ATOM   3166 C C   . PHE B 1 142 ? 35.228 41.228  36.113 1.00 37.37  ? 142 PHE B C   1 
ATOM   3167 O O   . PHE B 1 142 ? 36.368 41.585  36.445 1.00 36.84  ? 142 PHE B O   1 
ATOM   3168 C CB  . PHE B 1 142 ? 35.192 39.725  34.120 1.00 39.89  ? 142 PHE B CB  1 
ATOM   3169 C CG  . PHE B 1 142 ? 34.777 39.394  32.718 1.00 43.07  ? 142 PHE B CG  1 
ATOM   3170 C CD1 . PHE B 1 142 ? 33.872 40.158  31.995 1.00 43.22  ? 142 PHE B CD1 1 
ATOM   3171 C CD2 . PHE B 1 142 ? 35.325 38.275  32.089 1.00 43.82  ? 142 PHE B CD2 1 
ATOM   3172 C CE1 . PHE B 1 142 ? 33.524 39.843  30.696 1.00 42.91  ? 142 PHE B CE1 1 
ATOM   3173 C CE2 . PHE B 1 142 ? 34.979 37.935  30.798 1.00 42.57  ? 142 PHE B CE2 1 
ATOM   3174 C CZ  . PHE B 1 142 ? 34.072 38.715  30.113 1.00 43.56  ? 142 PHE B CZ  1 
ATOM   3175 N N   . THR B 1 143 ? 34.279 40.939  37.004 1.00 36.98  ? 143 THR B N   1 
ATOM   3176 C CA  . THR B 1 143 ? 34.600 41.031  38.437 1.00 35.55  ? 143 THR B CA  1 
ATOM   3177 C C   . THR B 1 143 ? 33.903 39.954  39.209 1.00 35.91  ? 143 THR B C   1 
ATOM   3178 O O   . THR B 1 143 ? 32.956 39.290  38.754 1.00 36.45  ? 143 THR B O   1 
ATOM   3179 C CB  . THR B 1 143 ? 34.155 42.390  38.985 1.00 32.09  ? 143 THR B CB  1 
ATOM   3180 O OG1 . THR B 1 143 ? 34.801 42.577  40.268 1.00 36.62  ? 143 THR B OG1 1 
ATOM   3181 C CG2 . THR B 1 143 ? 32.688 42.555  39.245 1.00 28.07  ? 143 THR B CG2 1 
ATOM   3182 N N   . GLY B 1 144 ? 34.361 39.766  40.452 1.00 36.50  ? 144 GLY B N   1 
ATOM   3183 C CA  . GLY B 1 144 ? 33.718 38.850  41.403 1.00 35.65  ? 144 GLY B CA  1 
ATOM   3184 C C   . GLY B 1 144 ? 34.492 38.688  42.700 1.00 36.56  ? 144 GLY B C   1 
ATOM   3185 O O   . GLY B 1 144 ? 35.707 38.960  42.789 1.00 35.19  ? 144 GLY B O   1 
ATOM   3186 N N   . HIS B 1 145 ? 33.747 38.213  43.729 1.00 36.90  ? 145 HIS B N   1 
ATOM   3187 C CA  . HIS B 1 145 ? 34.447 37.945  45.002 1.00 37.21  ? 145 HIS B CA  1 
ATOM   3188 C C   . HIS B 1 145 ? 34.386 36.455  45.274 1.00 37.81  ? 145 HIS B C   1 
ATOM   3189 O O   . HIS B 1 145 ? 33.499 35.792  44.746 1.00 37.73  ? 145 HIS B O   1 
ATOM   3190 C CB  . HIS B 1 145 ? 33.784 38.723  46.116 1.00 37.39  ? 145 HIS B CB  1 
ATOM   3191 C CG  . HIS B 1 145 ? 33.931 38.177  47.510 1.00 34.61  ? 145 HIS B CG  1 
ATOM   3192 N ND1 . HIS B 1 145 ? 33.013 37.291  48.014 1.00 31.56  ? 145 HIS B ND1 1 
ATOM   3193 C CD2 . HIS B 1 145 ? 34.832 38.439  48.491 1.00 32.68  ? 145 HIS B CD2 1 
ATOM   3194 C CE1 . HIS B 1 145 ? 33.368 37.005  49.278 1.00 35.23  ? 145 HIS B CE1 1 
ATOM   3195 N NE2 . HIS B 1 145 ? 34.471 37.667  49.567 1.00 35.00  ? 145 HIS B NE2 1 
ATOM   3196 N N   . SER B 1 146 ? 35.418 35.893  45.882 1.00 38.53  ? 146 SER B N   1 
ATOM   3197 C CA  . SER B 1 146 ? 35.398 34.476  46.243 1.00 39.31  ? 146 SER B CA  1 
ATOM   3198 C C   . SER B 1 146 ? 35.345 33.572  45.042 1.00 39.92  ? 146 SER B C   1 
ATOM   3199 O O   . SER B 1 146 ? 36.211 33.653  44.154 1.00 40.98  ? 146 SER B O   1 
ATOM   3200 C CB  . SER B 1 146 ? 34.192 34.195  47.165 1.00 40.90  ? 146 SER B CB  1 
ATOM   3201 O OG  . SER B 1 146 ? 34.598 33.297  48.184 1.00 42.94  ? 146 SER B OG  1 
ATOM   3202 N N   . LEU B 1 147 ? 34.563 32.497  45.055 1.00 40.06  ? 147 LEU B N   1 
ATOM   3203 C CA  . LEU B 1 147 ? 34.370 31.694  43.831 1.00 39.85  ? 147 LEU B CA  1 
ATOM   3204 C C   . LEU B 1 147 ? 34.081 32.541  42.605 1.00 39.15  ? 147 LEU B C   1 
ATOM   3205 O O   . LEU B 1 147 ? 34.671 32.369  41.533 1.00 39.41  ? 147 LEU B O   1 
ATOM   3206 C CB  . LEU B 1 147 ? 33.257 30.663  44.117 1.00 40.74  ? 147 LEU B CB  1 
ATOM   3207 C CG  . LEU B 1 147 ? 32.536 30.014  42.948 1.00 39.06  ? 147 LEU B CG  1 
ATOM   3208 C CD1 . LEU B 1 147 ? 33.461 29.179  42.071 1.00 34.31  ? 147 LEU B CD1 1 
ATOM   3209 C CD2 . LEU B 1 147 ? 31.307 29.240  43.377 1.00 34.65  ? 147 LEU B CD2 1 
ATOM   3210 N N   . GLY B 1 148 ? 33.253 33.575  42.684 1.00 38.27  ? 148 GLY B N   1 
ATOM   3211 C CA  . GLY B 1 148 ? 32.889 34.479  41.627 1.00 37.80  ? 148 GLY B CA  1 
ATOM   3212 C C   . GLY B 1 148 ? 34.129 35.161  41.069 1.00 38.27  ? 148 GLY B C   1 
ATOM   3213 O O   . GLY B 1 148 ? 34.294 35.337  39.879 1.00 37.12  ? 148 GLY B O   1 
ATOM   3214 N N   . GLY B 1 149 ? 35.083 35.482  41.954 1.00 38.21  ? 149 GLY B N   1 
ATOM   3215 C CA  . GLY B 1 149 ? 36.374 36.006  41.572 1.00 38.51  ? 149 GLY B CA  1 
ATOM   3216 C C   . GLY B 1 149 ? 37.128 34.967  40.745 1.00 40.23  ? 149 GLY B C   1 
ATOM   3217 O O   . GLY B 1 149 ? 37.898 35.340  39.841 1.00 40.21  ? 149 GLY B O   1 
ATOM   3218 N N   . ALA B 1 150 ? 36.915 33.672  41.082 1.00 39.49  ? 150 ALA B N   1 
ATOM   3219 C CA  . ALA B 1 150 ? 37.551 32.591  40.372 1.00 38.62  ? 150 ALA B CA  1 
ATOM   3220 C C   . ALA B 1 150 ? 36.853 32.523  39.008 1.00 38.73  ? 150 ALA B C   1 
ATOM   3221 O O   . ALA B 1 150 ? 37.611 32.422  38.052 1.00 38.40  ? 150 ALA B O   1 
ATOM   3222 C CB  . ALA B 1 150 ? 37.569 31.248  41.067 1.00 34.22  ? 150 ALA B CB  1 
ATOM   3223 N N   . LEU B 1 151 ? 35.559 32.766  38.947 1.00 39.00  ? 151 LEU B N   1 
ATOM   3224 C CA  . LEU B 1 151 ? 34.962 32.751  37.636 1.00 39.74  ? 151 LEU B CA  1 
ATOM   3225 C C   . LEU B 1 151 ? 35.363 33.971  36.846 1.00 41.19  ? 151 LEU B C   1 
ATOM   3226 O O   . LEU B 1 151 ? 35.921 33.695  35.754 1.00 43.47  ? 151 LEU B O   1 
ATOM   3227 C CB  . LEU B 1 151 ? 33.446 32.662  37.720 1.00 38.84  ? 151 LEU B CB  1 
ATOM   3228 C CG  . LEU B 1 151 ? 33.103 31.350  38.474 1.00 39.58  ? 151 LEU B CG  1 
ATOM   3229 C CD1 . LEU B 1 151 ? 31.619 31.265  38.800 1.00 39.03  ? 151 LEU B CD1 1 
ATOM   3230 C CD2 . LEU B 1 151 ? 33.512 30.170  37.576 1.00 36.68  ? 151 LEU B CD2 1 
ATOM   3231 N N   . ALA B 1 152 ? 35.408 35.176  37.420 1.00 40.66  ? 152 ALA B N   1 
ATOM   3232 C CA  . ALA B 1 152 ? 35.854 36.277  36.582 1.00 40.92  ? 152 ALA B CA  1 
ATOM   3233 C C   . ALA B 1 152 ? 37.230 35.949  35.973 1.00 41.02  ? 152 ALA B C   1 
ATOM   3234 O O   . ALA B 1 152 ? 37.448 36.263  34.798 1.00 40.32  ? 152 ALA B O   1 
ATOM   3235 C CB  . ALA B 1 152 ? 35.932 37.645  37.232 1.00 36.23  ? 152 ALA B CB  1 
ATOM   3236 N N   . THR B 1 153 ? 38.138 35.448  36.811 1.00 40.98  ? 153 THR B N   1 
ATOM   3237 C CA  . THR B 1 153 ? 39.497 35.232  36.375 1.00 41.73  ? 153 THR B CA  1 
ATOM   3238 C C   . THR B 1 153 ? 39.577 34.203  35.271 1.00 42.72  ? 153 THR B C   1 
ATOM   3239 O O   . THR B 1 153 ? 40.204 34.531  34.257 1.00 43.65  ? 153 THR B O   1 
ATOM   3240 C CB  . THR B 1 153 ? 40.401 34.806  37.520 1.00 43.51  ? 153 THR B CB  1 
ATOM   3241 O OG1 . THR B 1 153 ? 40.383 35.842  38.528 1.00 40.50  ? 153 THR B OG1 1 
ATOM   3242 C CG2 . THR B 1 153 ? 41.822 34.518  37.064 1.00 39.93  ? 153 THR B CG2 1 
ATOM   3243 N N   . VAL B 1 154 ? 38.935 33.067  35.418 1.00 42.82  ? 154 VAL B N   1 
ATOM   3244 C CA  . VAL B 1 154 ? 39.024 32.051  34.356 1.00 43.69  ? 154 VAL B CA  1 
ATOM   3245 C C   . VAL B 1 154 ? 38.422 32.580  33.061 1.00 44.76  ? 154 VAL B C   1 
ATOM   3246 O O   . VAL B 1 154 ? 39.025 32.542  31.994 1.00 44.57  ? 154 VAL B O   1 
ATOM   3247 C CB  . VAL B 1 154 ? 38.328 30.737  34.756 1.00 41.52  ? 154 VAL B CB  1 
ATOM   3248 C CG1 . VAL B 1 154 ? 38.395 29.715  33.631 1.00 39.50  ? 154 VAL B CG1 1 
ATOM   3249 C CG2 . VAL B 1 154 ? 38.951 30.164  36.020 1.00 37.05  ? 154 VAL B CG2 1 
ATOM   3250 N N   . ALA B 1 155 ? 37.182 33.060  33.178 1.00 45.53  ? 155 ALA B N   1 
ATOM   3251 C CA  . ALA B 1 155 ? 36.459 33.628  32.045 1.00 46.57  ? 155 ALA B CA  1 
ATOM   3252 C C   . ALA B 1 155 ? 37.201 34.765  31.344 1.00 46.73  ? 155 ALA B C   1 
ATOM   3253 O O   . ALA B 1 155 ? 37.191 34.869  30.115 1.00 46.58  ? 155 ALA B O   1 
ATOM   3254 C CB  . ALA B 1 155 ? 35.086 34.123  32.493 1.00 44.59  ? 155 ALA B CB  1 
ATOM   3255 N N   . GLY B 1 156 ? 37.948 35.564  32.094 1.00 46.85  ? 156 GLY B N   1 
ATOM   3256 C CA  . GLY B 1 156 ? 38.676 36.659  31.454 1.00 47.75  ? 156 GLY B CA  1 
ATOM   3257 C C   . GLY B 1 156 ? 39.903 36.067  30.768 1.00 48.23  ? 156 GLY B C   1 
ATOM   3258 O O   . GLY B 1 156 ? 40.258 36.479  29.678 1.00 48.13  ? 156 GLY B O   1 
ATOM   3259 N N   . ALA B 1 157 ? 40.479 35.000  31.319 1.00 48.56  ? 157 ALA B N   1 
ATOM   3260 C CA  . ALA B 1 157 ? 41.612 34.346  30.691 1.00 48.28  ? 157 ALA B CA  1 
ATOM   3261 C C   . ALA B 1 157 ? 41.084 33.803  29.383 1.00 48.59  ? 157 ALA B C   1 
ATOM   3262 O O   . ALA B 1 157 ? 41.831 33.794  28.400 1.00 49.30  ? 157 ALA B O   1 
ATOM   3263 C CB  . ALA B 1 157 ? 42.258 33.263  31.519 1.00 48.29  ? 157 ALA B CB  1 
ATOM   3264 N N   . ASP B 1 158 ? 39.915 33.230  29.339 1.00 48.78  ? 158 ASP B N   1 
ATOM   3265 C CA  . ASP B 1 158 ? 39.304 32.696  28.157 1.00 49.30  ? 158 ASP B CA  1 
ATOM   3266 C C   . ASP B 1 158 ? 38.774 33.591  27.040 1.00 50.02  ? 158 ASP B C   1 
ATOM   3267 O O   . ASP B 1 158 ? 38.475 33.039  25.973 1.00 50.50  ? 158 ASP B O   1 
ATOM   3268 C CB  . ASP B 1 158 ? 37.998 32.003  28.641 1.00 50.14  ? 158 ASP B CB  1 
ATOM   3269 C CG  . ASP B 1 158 ? 37.868 30.809  27.737 1.00 51.68  ? 158 ASP B CG  1 
ATOM   3270 O OD1 . ASP B 1 158 ? 38.853 30.596  26.987 1.00 56.93  ? 158 ASP B OD1 1 
ATOM   3271 O OD2 . ASP B 1 158 ? 36.828 30.164  27.821 1.00 50.17  ? 158 ASP B OD2 1 
ATOM   3272 N N   . LEU B 1 159 ? 38.285 34.805  27.298 1.00 49.40  ? 159 LEU B N   1 
ATOM   3273 C CA  . LEU B 1 159 ? 37.532 35.540  26.283 1.00 48.95  ? 159 LEU B CA  1 
ATOM   3274 C C   . LEU B 1 159 ? 38.386 36.604  25.636 1.00 48.42  ? 159 LEU B C   1 
ATOM   3275 O O   . LEU B 1 159 ? 38.071 37.259  24.674 1.00 48.49  ? 159 LEU B O   1 
ATOM   3276 C CB  . LEU B 1 159 ? 36.197 36.042  26.864 1.00 45.51  ? 159 LEU B CB  1 
ATOM   3277 C CG  . LEU B 1 159 ? 35.309 34.891  27.299 1.00 45.72  ? 159 LEU B CG  1 
ATOM   3278 C CD1 . LEU B 1 159 ? 33.873 35.364  27.545 1.00 46.92  ? 159 LEU B CD1 1 
ATOM   3279 C CD2 . LEU B 1 159 ? 35.256 33.737  26.294 1.00 43.08  ? 159 LEU B CD2 1 
ATOM   3280 N N   . ARG B 1 160 ? 39.417 36.987  26.334 1.00 49.05  ? 160 ARG B N   1 
ATOM   3281 C CA  . ARG B 1 160 ? 40.428 37.942  25.950 1.00 50.28  ? 160 ARG B CA  1 
ATOM   3282 C C   . ARG B 1 160 ? 40.884 37.538  24.556 1.00 50.70  ? 160 ARG B C   1 
ATOM   3283 O O   . ARG B 1 160 ? 40.760 36.382  24.206 1.00 50.62  ? 160 ARG B O   1 
ATOM   3284 C CB  . ARG B 1 160 ? 41.585 37.846  26.958 1.00 50.23  ? 160 ARG B CB  1 
ATOM   3285 C CG  . ARG B 1 160 ? 41.525 38.936  28.011 1.00 49.62  ? 160 ARG B CG  1 
ATOM   3286 C CD  . ARG B 1 160 ? 42.243 38.523  29.292 1.00 48.85  ? 160 ARG B CD  1 
ATOM   3287 N NE  . ARG B 1 160 ? 42.164 39.589  30.275 1.00 46.38  ? 160 ARG B NE  1 
ATOM   3288 C CZ  . ARG B 1 160 ? 42.963 39.643  31.328 1.00 44.07  ? 160 ARG B CZ  1 
ATOM   3289 N NH1 . ARG B 1 160 ? 43.841 38.672  31.467 1.00 43.72  ? 160 ARG B NH1 1 
ATOM   3290 N NH2 . ARG B 1 160 ? 42.871 40.629  32.190 1.00 43.00  ? 160 ARG B NH2 1 
ATOM   3291 N N   . GLY B 1 161 ? 41.482 38.433  23.790 1.00 52.09  ? 161 GLY B N   1 
ATOM   3292 C CA  . GLY B 1 161 ? 41.903 38.208  22.432 1.00 51.76  ? 161 GLY B CA  1 
ATOM   3293 C C   . GLY B 1 161 ? 40.839 38.234  21.354 1.00 51.99  ? 161 GLY B C   1 
ATOM   3294 O O   . GLY B 1 161 ? 41.247 37.843  20.253 1.00 52.74  ? 161 GLY B O   1 
ATOM   3295 N N   . ASN B 1 162 ? 39.554 38.489  21.507 1.00 51.53  ? 162 ASN B N   1 
ATOM   3296 C CA  . ASN B 1 162 ? 38.618 38.542  20.394 1.00 51.90  ? 162 ASN B CA  1 
ATOM   3297 C C   . ASN B 1 162 ? 38.331 39.994  19.988 1.00 49.89  ? 162 ASN B C   1 
ATOM   3298 O O   . ASN B 1 162 ? 37.231 40.325  19.553 1.00 48.88  ? 162 ASN B O   1 
ATOM   3299 C CB  . ASN B 1 162 ? 37.284 37.796  20.547 1.00 60.60  ? 162 ASN B CB  1 
ATOM   3300 C CG  . ASN B 1 162 ? 37.425 36.495  21.314 1.00 71.74  ? 162 ASN B CG  1 
ATOM   3301 O OD1 . ASN B 1 162 ? 36.659 36.138  22.244 1.00 76.22  ? 162 ASN B OD1 1 
ATOM   3302 N ND2 . ASN B 1 162 ? 38.445 35.682  20.993 1.00 76.70  ? 162 ASN B ND2 1 
ATOM   3303 N N   . GLY B 1 163 ? 39.233 40.936  20.270 1.00 48.91  ? 163 GLY B N   1 
ATOM   3304 C CA  . GLY B 1 163 ? 39.036 42.297  19.825 1.00 48.52  ? 163 GLY B CA  1 
ATOM   3305 C C   . GLY B 1 163 ? 38.677 43.409  20.778 1.00 47.50  ? 163 GLY B C   1 
ATOM   3306 O O   . GLY B 1 163 ? 38.929 44.588  20.498 1.00 47.37  ? 163 GLY B O   1 
ATOM   3307 N N   . TYR B 1 164 ? 38.248 43.124  21.976 1.00 46.63  ? 164 TYR B N   1 
ATOM   3308 C CA  . TYR B 1 164 ? 38.012 44.085  23.047 1.00 46.16  ? 164 TYR B CA  1 
ATOM   3309 C C   . TYR B 1 164 ? 38.811 43.661  24.272 1.00 45.75  ? 164 TYR B C   1 
ATOM   3310 O O   . TYR B 1 164 ? 38.920 42.464  24.556 1.00 46.63  ? 164 TYR B O   1 
ATOM   3311 C CB  . TYR B 1 164 ? 36.500 44.099  23.314 1.00 44.52  ? 164 TYR B CB  1 
ATOM   3312 C CG  . TYR B 1 164 ? 35.912 42.728  23.598 1.00 43.52  ? 164 TYR B CG  1 
ATOM   3313 C CD1 . TYR B 1 164 ? 35.480 41.878  22.583 1.00 43.72  ? 164 TYR B CD1 1 
ATOM   3314 C CD2 . TYR B 1 164 ? 35.810 42.264  24.893 1.00 41.97  ? 164 TYR B CD2 1 
ATOM   3315 C CE1 . TYR B 1 164 ? 34.895 40.662  22.860 1.00 44.09  ? 164 TYR B CE1 1 
ATOM   3316 C CE2 . TYR B 1 164 ? 35.181 41.092  25.209 1.00 42.67  ? 164 TYR B CE2 1 
ATOM   3317 C CZ  . TYR B 1 164 ? 34.766 40.271  24.184 1.00 44.72  ? 164 TYR B CZ  1 
ATOM   3318 O OH  . TYR B 1 164 ? 34.247 39.037  24.507 1.00 45.01  ? 164 TYR B OH  1 
ATOM   3319 N N   . ASP B 1 165 ? 39.510 44.551  24.924 1.00 45.78  ? 165 ASP B N   1 
ATOM   3320 C CA  . ASP B 1 165 ? 40.230 44.320  26.166 1.00 46.15  ? 165 ASP B CA  1 
ATOM   3321 C C   . ASP B 1 165 ? 39.279 43.888  27.272 1.00 46.49  ? 165 ASP B C   1 
ATOM   3322 O O   . ASP B 1 165 ? 38.126 44.348  27.169 1.00 45.89  ? 165 ASP B O   1 
ATOM   3323 C CB  . ASP B 1 165 ? 40.804 45.694  26.605 1.00 49.00  ? 165 ASP B CB  1 
ATOM   3324 C CG  . ASP B 1 165 ? 42.169 45.909  25.989 1.00 51.39  ? 165 ASP B CG  1 
ATOM   3325 O OD1 . ASP B 1 165 ? 42.652 44.950  25.352 1.00 51.43  ? 165 ASP B OD1 1 
ATOM   3326 O OD2 . ASP B 1 165 ? 42.806 46.975  26.135 1.00 53.43  ? 165 ASP B OD2 1 
ATOM   3327 N N   . ILE B 1 166 ? 39.648 42.977  28.199 1.00 46.24  ? 166 ILE B N   1 
ATOM   3328 C CA  . ILE B 1 166 ? 38.810 42.570  29.336 1.00 45.23  ? 166 ILE B CA  1 
ATOM   3329 C C   . ILE B 1 166 ? 39.637 42.695  30.601 1.00 44.96  ? 166 ILE B C   1 
ATOM   3330 O O   . ILE B 1 166 ? 40.687 42.063  30.694 1.00 45.21  ? 166 ILE B O   1 
ATOM   3331 C CB  . ILE B 1 166 ? 38.406 41.091  29.294 1.00 44.79  ? 166 ILE B CB  1 
ATOM   3332 C CG1 . ILE B 1 166 ? 37.712 40.883  27.913 1.00 43.32  ? 166 ILE B CG1 1 
ATOM   3333 C CG2 . ILE B 1 166 ? 37.487 40.779  30.453 1.00 43.90  ? 166 ILE B CG2 1 
ATOM   3334 C CD1 . ILE B 1 166 ? 37.255 39.534  27.507 1.00 42.28  ? 166 ILE B CD1 1 
ATOM   3335 N N   . ASP B 1 167 ? 39.179 43.600  31.468 1.00 44.49  ? 167 ASP B N   1 
ATOM   3336 C CA  . ASP B 1 167 ? 39.910 43.761  32.725 1.00 42.63  ? 167 ASP B CA  1 
ATOM   3337 C C   . ASP B 1 167 ? 39.205 42.854  33.735 1.00 41.48  ? 167 ASP B C   1 
ATOM   3338 O O   . ASP B 1 167 ? 38.038 42.453  33.593 1.00 40.41  ? 167 ASP B O   1 
ATOM   3339 C CB  . ASP B 1 167 ? 39.965 45.193  33.185 1.00 45.83  ? 167 ASP B CB  1 
ATOM   3340 C CG  . ASP B 1 167 ? 40.938 46.093  32.437 1.00 50.16  ? 167 ASP B CG  1 
ATOM   3341 O OD1 . ASP B 1 167 ? 41.892 45.646  31.751 1.00 47.19  ? 167 ASP B OD1 1 
ATOM   3342 O OD2 . ASP B 1 167 ? 40.720 47.331  32.608 1.00 51.09  ? 167 ASP B OD2 1 
ATOM   3343 N N   . VAL B 1 168 ? 40.038 42.347  34.646 1.00 39.78  ? 168 VAL B N   1 
ATOM   3344 C CA  . VAL B 1 168 ? 39.521 41.484  35.692 1.00 38.26  ? 168 VAL B CA  1 
ATOM   3345 C C   . VAL B 1 168 ? 39.888 42.151  37.026 1.00 38.39  ? 168 VAL B C   1 
ATOM   3346 O O   . VAL B 1 168 ? 41.020 42.647  37.195 1.00 38.77  ? 168 VAL B O   1 
ATOM   3347 C CB  . VAL B 1 168 ? 40.117 40.078  35.683 1.00 37.99  ? 168 VAL B CB  1 
ATOM   3348 C CG1 . VAL B 1 168 ? 39.501 39.183  36.755 1.00 35.50  ? 168 VAL B CG1 1 
ATOM   3349 C CG2 . VAL B 1 168 ? 39.999 39.434  34.305 1.00 38.67  ? 168 VAL B CG2 1 
ATOM   3350 N N   . PHE B 1 169 ? 38.825 42.264  37.830 1.00 36.45  ? 169 PHE B N   1 
ATOM   3351 C CA  . PHE B 1 169 ? 38.985 42.709  39.205 1.00 34.49  ? 169 PHE B CA  1 
ATOM   3352 C C   . PHE B 1 169 ? 38.341 41.650  40.099 1.00 33.46  ? 169 PHE B C   1 
ATOM   3353 O O   . PHE B 1 169 ? 37.210 41.157  39.862 1.00 32.64  ? 169 PHE B O   1 
ATOM   3354 C CB  . PHE B 1 169 ? 38.251 44.025  39.368 1.00 33.15  ? 169 PHE B CB  1 
ATOM   3355 C CG  . PHE B 1 169 ? 38.837 45.227  38.697 1.00 30.93  ? 169 PHE B CG  1 
ATOM   3356 C CD1 . PHE B 1 169 ? 38.532 45.490  37.376 1.00 30.07  ? 169 PHE B CD1 1 
ATOM   3357 C CD2 . PHE B 1 169 ? 39.471 46.207  39.453 1.00 29.77  ? 169 PHE B CD2 1 
ATOM   3358 C CE1 . PHE B 1 169 ? 38.910 46.669  36.777 1.00 26.55  ? 169 PHE B CE1 1 
ATOM   3359 C CE2 . PHE B 1 169 ? 39.950 47.357  38.832 1.00 31.58  ? 169 PHE B CE2 1 
ATOM   3360 C CZ  . PHE B 1 169 ? 39.675 47.554  37.458 1.00 28.45  ? 169 PHE B CZ  1 
ATOM   3361 N N   . SER B 1 170 ? 39.249 40.961  40.796 1.00 33.24  ? 170 SER B N   1 
ATOM   3362 C CA  . SER B 1 170 ? 38.821 39.767  41.591 1.00 32.67  ? 170 SER B CA  1 
ATOM   3363 C C   . SER B 1 170 ? 39.009 40.013  43.059 1.00 30.81  ? 170 SER B C   1 
ATOM   3364 O O   . SER B 1 170 ? 39.881 40.811  43.425 1.00 31.43  ? 170 SER B O   1 
ATOM   3365 C CB  . SER B 1 170 ? 39.582 38.498  41.140 1.00 31.64  ? 170 SER B CB  1 
ATOM   3366 O OG  . SER B 1 170 ? 40.892 38.440  41.767 1.00 32.24  ? 170 SER B OG  1 
ATOM   3367 N N   . TYR B 1 171 ? 38.075 39.656  43.913 1.00 31.52  ? 171 TYR B N   1 
ATOM   3368 C CA  . TYR B 1 171 ? 38.147 39.973  45.362 1.00 31.24  ? 171 TYR B CA  1 
ATOM   3369 C C   . TYR B 1 171 ? 38.136 38.728  46.233 1.00 31.85  ? 171 TYR B C   1 
ATOM   3370 O O   . TYR B 1 171 ? 37.198 37.903  46.227 1.00 32.16  ? 171 TYR B O   1 
ATOM   3371 C CB  . TYR B 1 171 ? 37.008 40.893  45.846 1.00 30.29  ? 171 TYR B CB  1 
ATOM   3372 C CG  . TYR B 1 171 ? 37.105 42.207  45.065 1.00 30.97  ? 171 TYR B CG  1 
ATOM   3373 C CD1 . TYR B 1 171 ? 36.542 42.279  43.807 1.00 29.92  ? 171 TYR B CD1 1 
ATOM   3374 C CD2 . TYR B 1 171 ? 37.730 43.339  45.592 1.00 31.94  ? 171 TYR B CD2 1 
ATOM   3375 C CE1 . TYR B 1 171 ? 36.694 43.424  43.071 1.00 31.88  ? 171 TYR B CE1 1 
ATOM   3376 C CE2 . TYR B 1 171 ? 37.830 44.508  44.881 1.00 31.87  ? 171 TYR B CE2 1 
ATOM   3377 C CZ  . TYR B 1 171 ? 37.326 44.520  43.597 1.00 33.23  ? 171 TYR B CZ  1 
ATOM   3378 O OH  . TYR B 1 171 ? 37.407 45.657  42.809 1.00 35.39  ? 171 TYR B OH  1 
ATOM   3379 N N   . GLY B 1 172 ? 39.249 38.598  46.954 1.00 31.69  ? 172 GLY B N   1 
ATOM   3380 C CA  . GLY B 1 172 ? 39.557 37.374  47.635 1.00 32.93  ? 172 GLY B CA  1 
ATOM   3381 C C   . GLY B 1 172 ? 39.354 36.114  46.814 1.00 33.78  ? 172 GLY B C   1 
ATOM   3382 O O   . GLY B 1 172 ? 38.803 35.140  47.354 1.00 33.50  ? 172 GLY B O   1 
ATOM   3383 N N   . ALA B 1 173 ? 39.796 36.061  45.559 1.00 35.23  ? 173 ALA B N   1 
ATOM   3384 C CA  . ALA B 1 173 ? 39.738 34.795  44.800 1.00 36.67  ? 173 ALA B CA  1 
ATOM   3385 C C   . ALA B 1 173 ? 40.766 33.769  45.286 1.00 37.20  ? 173 ALA B C   1 
ATOM   3386 O O   . ALA B 1 173 ? 41.890 34.106  45.656 1.00 38.28  ? 173 ALA B O   1 
ATOM   3387 C CB  . ALA B 1 173 ? 40.057 35.044  43.332 1.00 33.01  ? 173 ALA B CB  1 
ATOM   3388 N N   . PRO B 1 174 ? 40.407 32.509  45.216 1.00 37.74  ? 174 PRO B N   1 
ATOM   3389 C CA  . PRO B 1 174 ? 41.354 31.416  45.413 1.00 39.39  ? 174 PRO B CA  1 
ATOM   3390 C C   . PRO B 1 174 ? 42.249 31.223  44.173 1.00 40.86  ? 174 PRO B C   1 
ATOM   3391 O O   . PRO B 1 174 ? 41.983 31.681  43.064 1.00 41.45  ? 174 PRO B O   1 
ATOM   3392 C CB  . PRO B 1 174 ? 40.460 30.167  45.474 1.00 37.83  ? 174 PRO B CB  1 
ATOM   3393 C CG  . PRO B 1 174 ? 39.241 30.541  44.713 1.00 37.71  ? 174 PRO B CG  1 
ATOM   3394 C CD  . PRO B 1 174 ? 39.085 32.036  44.734 1.00 37.25  ? 174 PRO B CD  1 
ATOM   3395 N N   . ARG B 1 175 ? 43.229 30.330  44.289 1.00 42.39  ? 175 ARG B N   1 
ATOM   3396 C CA  . ARG B 1 175 ? 44.103 29.930  43.172 1.00 41.56  ? 175 ARG B CA  1 
ATOM   3397 C C   . ARG B 1 175 ? 43.248 29.147  42.196 1.00 40.97  ? 175 ARG B C   1 
ATOM   3398 O O   . ARG B 1 175 ? 42.208 28.626  42.584 1.00 40.41  ? 175 ARG B O   1 
ATOM   3399 C CB  . ARG B 1 175 ? 45.329 29.172  43.709 1.00 39.51  ? 175 ARG B CB  1 
ATOM   3400 C CG  . ARG B 1 175 ? 46.350 30.120  44.312 1.00 38.22  ? 175 ARG B CG  1 
ATOM   3401 C CD  . ARG B 1 175 ? 47.555 29.543  45.010 1.00 41.52  ? 175 ARG B CD  1 
ATOM   3402 N NE  . ARG B 1 175 ? 47.342 29.101  46.368 1.00 44.25  ? 175 ARG B NE  1 
ATOM   3403 C CZ  . ARG B 1 175 ? 48.080 29.429  47.425 1.00 42.09  ? 175 ARG B CZ  1 
ATOM   3404 N NH1 . ARG B 1 175 ? 49.126 30.240  47.313 1.00 41.17  ? 175 ARG B NH1 1 
ATOM   3405 N NH2 . ARG B 1 175 ? 47.753 28.891  48.592 1.00 39.68  ? 175 ARG B NH2 1 
ATOM   3406 N N   . VAL B 1 176 ? 43.445 29.380  40.904 1.00 42.32  ? 176 VAL B N   1 
ATOM   3407 C CA  . VAL B 1 176 ? 42.556 28.843  39.845 1.00 42.95  ? 176 VAL B CA  1 
ATOM   3408 C C   . VAL B 1 176 ? 43.301 27.789  39.042 1.00 44.04  ? 176 VAL B C   1 
ATOM   3409 O O   . VAL B 1 176 ? 42.771 26.986  38.233 1.00 43.45  ? 176 VAL B O   1 
ATOM   3410 C CB  . VAL B 1 176 ? 42.132 30.075  39.047 0.50 41.32  ? 176 VAL B CB  1 
ATOM   3411 C CG1 . VAL B 1 176 ? 41.724 29.770  37.639 0.50 42.53  ? 176 VAL B CG1 1 
ATOM   3412 C CG2 . VAL B 1 176 ? 40.916 30.652  39.778 0.50 40.55  ? 176 VAL B CG2 1 
ATOM   3413 N N   . GLY B 1 177 ? 44.611 27.704  39.364 1.00 44.42  ? 177 GLY B N   1 
ATOM   3414 C CA  . GLY B 1 177 ? 45.450 26.790  38.670 1.00 45.97  ? 177 GLY B CA  1 
ATOM   3415 C C   . GLY B 1 177 ? 46.924 26.691  38.891 1.00 47.16  ? 177 GLY B C   1 
ATOM   3416 O O   . GLY B 1 177 ? 47.569 27.065  39.863 1.00 46.29  ? 177 GLY B O   1 
ATOM   3417 N N   . ASN B 1 178 ? 47.539 26.061  37.862 1.00 49.40  ? 178 ASN B N   1 
ATOM   3418 C CA  . ASN B 1 178 ? 48.966 25.754  37.896 1.00 51.35  ? 178 ASN B CA  1 
ATOM   3419 C C   . ASN B 1 178 ? 49.978 26.826  37.658 1.00 51.82  ? 178 ASN B C   1 
ATOM   3420 O O   . ASN B 1 178 ? 49.621 28.005  37.821 1.00 52.74  ? 178 ASN B O   1 
ATOM   3421 C CB  . ASN B 1 178 ? 49.192 24.474  37.107 1.00 55.44  ? 178 ASN B CB  1 
ATOM   3422 C CG  . ASN B 1 178 ? 49.486 24.679  35.641 1.00 59.13  ? 178 ASN B CG  1 
ATOM   3423 O OD1 . ASN B 1 178 ? 49.450 25.813  35.129 1.00 60.29  ? 178 ASN B OD1 1 
ATOM   3424 N ND2 . ASN B 1 178 ? 49.739 23.487  35.089 1.00 57.24  ? 178 ASN B ND2 1 
ATOM   3425 N N   . ARG B 1 179 ? 51.266 26.516  37.519 1.00 52.95  ? 179 ARG B N   1 
ATOM   3426 C CA  . ARG B 1 179 ? 52.226 27.630  37.455 1.00 53.71  ? 179 ARG B CA  1 
ATOM   3427 C C   . ARG B 1 179 ? 52.199 28.242  36.069 1.00 54.44  ? 179 ARG B C   1 
ATOM   3428 O O   . ARG B 1 179 ? 52.613 29.371  35.905 1.00 55.17  ? 179 ARG B O   1 
ATOM   3429 C CB  . ARG B 1 179 ? 53.695 27.416  37.761 1.00 54.57  ? 179 ARG B CB  1 
ATOM   3430 C CG  . ARG B 1 179 ? 54.307 28.665  38.407 1.00 56.24  ? 179 ARG B CG  1 
ATOM   3431 C CD  . ARG B 1 179 ? 55.777 28.517  38.687 1.00 59.03  ? 179 ARG B CD  1 
ATOM   3432 N NE  . ARG B 1 179 ? 56.498 29.545  37.910 1.00 63.69  ? 179 ARG B NE  1 
ATOM   3433 C CZ  . ARG B 1 179 ? 57.178 30.561  38.436 1.00 64.79  ? 179 ARG B CZ  1 
ATOM   3434 N NH1 . ARG B 1 179 ? 57.289 30.649  39.770 1.00 65.77  ? 179 ARG B NH1 1 
ATOM   3435 N NH2 . ARG B 1 179 ? 57.703 31.501  37.660 1.00 63.79  ? 179 ARG B NH2 1 
ATOM   3436 N N   . ALA B 1 180 ? 51.986 27.349  35.113 1.00 55.03  ? 180 ALA B N   1 
ATOM   3437 C CA  . ALA B 1 180 ? 51.920 27.788  33.725 1.00 54.93  ? 180 ALA B CA  1 
ATOM   3438 C C   . ALA B 1 180 ? 50.785 28.812  33.627 1.00 53.80  ? 180 ALA B C   1 
ATOM   3439 O O   . ALA B 1 180 ? 51.014 29.904  33.127 1.00 53.26  ? 180 ALA B O   1 
ATOM   3440 C CB  . ALA B 1 180 ? 51.743 26.533  32.871 1.00 56.06  ? 180 ALA B CB  1 
ATOM   3441 N N   . PHE B 1 181 ? 49.665 28.499  34.252 1.00 53.06  ? 181 PHE B N   1 
ATOM   3442 C CA  . PHE B 1 181 ? 48.480 29.347  34.264 1.00 52.65  ? 181 PHE B CA  1 
ATOM   3443 C C   . PHE B 1 181 ? 48.669 30.637  35.043 1.00 51.78  ? 181 PHE B C   1 
ATOM   3444 O O   . PHE B 1 181 ? 48.430 31.721  34.531 1.00 51.01  ? 181 PHE B O   1 
ATOM   3445 C CB  . PHE B 1 181 ? 47.262 28.591  34.804 1.00 52.41  ? 181 PHE B CB  1 
ATOM   3446 C CG  . PHE B 1 181 ? 45.932 29.173  34.446 1.00 54.66  ? 181 PHE B CG  1 
ATOM   3447 C CD1 . PHE B 1 181 ? 45.764 30.006  33.350 1.00 54.48  ? 181 PHE B CD1 1 
ATOM   3448 C CD2 . PHE B 1 181 ? 44.811 28.882  35.222 1.00 53.20  ? 181 PHE B CD2 1 
ATOM   3449 C CE1 . PHE B 1 181 ? 44.529 30.536  33.019 1.00 53.41  ? 181 PHE B CE1 1 
ATOM   3450 C CE2 . PHE B 1 181 ? 43.586 29.406  34.880 1.00 52.59  ? 181 PHE B CE2 1 
ATOM   3451 C CZ  . PHE B 1 181 ? 43.437 30.239  33.798 1.00 52.85  ? 181 PHE B CZ  1 
ATOM   3452 N N   . ALA B 1 182 ? 49.364 30.550  36.162 1.00 51.65  ? 182 ALA B N   1 
ATOM   3453 C CA  . ALA B 1 182 ? 49.789 31.684  36.956 1.00 52.17  ? 182 ALA B CA  1 
ATOM   3454 C C   . ALA B 1 182 ? 50.619 32.641  36.099 1.00 52.99  ? 182 ALA B C   1 
ATOM   3455 O O   . ALA B 1 182 ? 50.578 33.875  36.131 1.00 51.50  ? 182 ALA B O   1 
ATOM   3456 C CB  . ALA B 1 182 ? 50.581 31.159  38.157 1.00 48.64  ? 182 ALA B CB  1 
ATOM   3457 N N   . GLU B 1 183 ? 51.463 32.023  35.274 1.00 54.50  ? 183 GLU B N   1 
ATOM   3458 C CA  . GLU B 1 183 ? 52.378 32.668  34.350 1.00 55.36  ? 183 GLU B CA  1 
ATOM   3459 C C   . GLU B 1 183 ? 51.642 33.304  33.172 1.00 54.70  ? 183 GLU B C   1 
ATOM   3460 O O   . GLU B 1 183 ? 51.901 34.476  32.904 1.00 53.64  ? 183 GLU B O   1 
ATOM   3461 C CB  . GLU B 1 183 ? 53.389 31.608  33.874 1.00 58.98  ? 183 GLU B CB  1 
ATOM   3462 C CG  . GLU B 1 183 ? 54.821 32.066  34.143 1.00 63.58  ? 183 GLU B CG  1 
ATOM   3463 C CD  . GLU B 1 183 ? 55.724 30.906  34.509 1.00 67.60  ? 183 GLU B CD  1 
ATOM   3464 O OE1 . GLU B 1 183 ? 55.697 29.886  33.768 1.00 69.74  ? 183 GLU B OE1 1 
ATOM   3465 O OE2 . GLU B 1 183 ? 56.458 31.028  35.518 1.00 68.48  ? 183 GLU B OE2 1 
ATOM   3466 N N   . PHE B 1 184 ? 50.641 32.597  32.664 1.00 54.29  ? 184 PHE B N   1 
ATOM   3467 C CA  . PHE B 1 184 ? 49.805 33.078  31.590 1.00 55.75  ? 184 PHE B CA  1 
ATOM   3468 C C   . PHE B 1 184 ? 49.036 34.309  32.058 1.00 57.13  ? 184 PHE B C   1 
ATOM   3469 O O   . PHE B 1 184 ? 49.309 35.410  31.554 1.00 58.10  ? 184 PHE B O   1 
ATOM   3470 C CB  . PHE B 1 184 ? 48.796 32.037  31.114 1.00 57.00  ? 184 PHE B CB  1 
ATOM   3471 C CG  . PHE B 1 184 ? 47.885 32.389  29.981 1.00 59.73  ? 184 PHE B CG  1 
ATOM   3472 C CD1 . PHE B 1 184 ? 48.385 32.575  28.677 1.00 60.57  ? 184 PHE B CD1 1 
ATOM   3473 C CD2 . PHE B 1 184 ? 46.518 32.512  30.142 1.00 59.29  ? 184 PHE B CD2 1 
ATOM   3474 C CE1 . PHE B 1 184 ? 47.528 32.896  27.635 1.00 60.63  ? 184 PHE B CE1 1 
ATOM   3475 C CE2 . PHE B 1 184 ? 45.685 32.814  29.075 1.00 59.60  ? 184 PHE B CE2 1 
ATOM   3476 C CZ  . PHE B 1 184 ? 46.166 33.014  27.809 1.00 57.69  ? 184 PHE B CZ  1 
ATOM   3477 N N   . LEU B 1 185 ? 48.359 34.193  33.215 1.00 56.79  ? 185 LEU B N   1 
ATOM   3478 C CA  . LEU B 1 185 ? 47.618 35.312  33.749 1.00 55.88  ? 185 LEU B CA  1 
ATOM   3479 C C   . LEU B 1 185 ? 48.472 36.531  34.009 1.00 56.19  ? 185 LEU B C   1 
ATOM   3480 O O   . LEU B 1 185 ? 47.904 37.629  33.958 1.00 57.02  ? 185 LEU B O   1 
ATOM   3481 C CB  . LEU B 1 185 ? 46.889 34.875  35.028 1.00 52.22  ? 185 LEU B CB  1 
ATOM   3482 C CG  . LEU B 1 185 ? 45.854 33.777  34.689 1.00 50.85  ? 185 LEU B CG  1 
ATOM   3483 C CD1 . LEU B 1 185 ? 45.479 33.050  35.953 1.00 44.76  ? 185 LEU B CD1 1 
ATOM   3484 C CD2 . LEU B 1 185 ? 44.690 34.376  33.912 1.00 50.67  ? 185 LEU B CD2 1 
ATOM   3485 N N   . THR B 1 186 ? 49.747 36.384  34.323 1.00 55.73  ? 186 THR B N   1 
ATOM   3486 C CA  . THR B 1 186 ? 50.635 37.484  34.623 1.00 55.79  ? 186 THR B CA  1 
ATOM   3487 C C   . THR B 1 186 ? 51.083 38.293  33.407 1.00 56.70  ? 186 THR B C   1 
ATOM   3488 O O   . THR B 1 186 ? 51.440 39.469  33.579 1.00 56.61  ? 186 THR B O   1 
ATOM   3489 C CB  . THR B 1 186 ? 51.900 36.939  35.317 1.00 52.93  ? 186 THR B CB  1 
ATOM   3490 O OG1 . THR B 1 186 ? 51.487 36.057  36.371 1.00 53.80  ? 186 THR B OG1 1 
ATOM   3491 C CG2 . THR B 1 186 ? 52.823 38.004  35.860 1.00 47.71  ? 186 THR B CG2 1 
ATOM   3492 N N   . VAL B 1 187 ? 51.263 37.620  32.271 1.00 56.57  ? 187 VAL B N   1 
ATOM   3493 C CA  . VAL B 1 187 ? 51.810 38.270  31.091 1.00 56.78  ? 187 VAL B CA  1 
ATOM   3494 C C   . VAL B 1 187 ? 50.875 38.383  29.885 1.00 57.09  ? 187 VAL B C   1 
ATOM   3495 O O   . VAL B 1 187 ? 51.267 38.899  28.845 1.00 56.49  ? 187 VAL B O   1 
ATOM   3496 C CB  . VAL B 1 187 ? 53.110 37.564  30.629 1.00 55.82  ? 187 VAL B CB  1 
ATOM   3497 C CG1 . VAL B 1 187 ? 54.169 37.602  31.725 1.00 54.45  ? 187 VAL B CG1 1 
ATOM   3498 C CG2 . VAL B 1 187 ? 52.853 36.159  30.131 1.00 50.43  ? 187 VAL B CG2 1 
ATOM   3499 N N   . GLN B 1 188 ? 49.652 37.833  30.017 1.00 57.01  ? 188 GLN B N   1 
ATOM   3500 C CA  . GLN B 1 188 ? 48.634 37.886  28.967 1.00 55.46  ? 188 GLN B CA  1 
ATOM   3501 C C   . GLN B 1 188 ? 48.390 39.392  28.749 1.00 55.31  ? 188 GLN B C   1 
ATOM   3502 O O   . GLN B 1 188 ? 48.492 40.209  29.703 1.00 55.00  ? 188 GLN B O   1 
ATOM   3503 C CB  . GLN B 1 188 ? 47.315 37.190  29.337 1.00 51.28  ? 188 GLN B CB  1 
ATOM   3504 C CG  . GLN B 1 188 ? 46.331 36.885  28.231 1.00 48.62  ? 188 GLN B CG  1 
ATOM   3505 C CD  . GLN B 1 188 ? 44.990 36.366  28.705 1.00 51.97  ? 188 GLN B CD  1 
ATOM   3506 O OE1 . GLN B 1 188 ? 44.605 36.695  29.865 1.00 50.47  ? 188 GLN B OE1 1 
ATOM   3507 N NE2 . GLN B 1 188 ? 44.229 35.662  27.867 1.00 49.61  ? 188 GLN B NE2 1 
ATOM   3508 N N   . THR B 1 189 ? 48.047 39.658  27.499 1.00 54.17  ? 189 THR B N   1 
ATOM   3509 C CA  . THR B 1 189 ? 47.772 41.038  27.104 1.00 52.95  ? 189 THR B CA  1 
ATOM   3510 C C   . THR B 1 189 ? 46.269 41.032  26.793 1.00 52.51  ? 189 THR B C   1 
ATOM   3511 O O   . THR B 1 189 ? 45.614 39.988  26.740 1.00 51.76  ? 189 THR B O   1 
ATOM   3512 C CB  . THR B 1 189 ? 48.549 41.266  25.775 1.00 54.24  ? 189 THR B CB  1 
ATOM   3513 O OG1 . THR B 1 189 ? 48.136 40.211  24.860 1.00 49.16  ? 189 THR B OG1 1 
ATOM   3514 C CG2 . THR B 1 189 ? 50.053 41.226  26.034 1.00 52.39  ? 189 THR B CG2 1 
ATOM   3515 N N   . GLY B 1 190 ? 45.840 42.239  26.430 1.00 51.72  ? 190 GLY B N   1 
ATOM   3516 C CA  . GLY B 1 190 ? 44.440 42.429  26.059 1.00 50.96  ? 190 GLY B CA  1 
ATOM   3517 C C   . GLY B 1 190 ? 43.591 42.625  27.318 1.00 51.02  ? 190 GLY B C   1 
ATOM   3518 O O   . GLY B 1 190 ? 42.453 42.140  27.293 1.00 50.99  ? 190 GLY B O   1 
ATOM   3519 N N   . GLY B 1 191 ? 44.094 43.358  28.317 1.00 50.06  ? 191 GLY B N   1 
ATOM   3520 C CA  . GLY B 1 191 ? 43.312 43.453  29.536 1.00 50.04  ? 191 GLY B CA  1 
ATOM   3521 C C   . GLY B 1 191 ? 44.256 43.175  30.713 1.00 50.20  ? 191 GLY B C   1 
ATOM   3522 O O   . GLY B 1 191 ? 45.200 42.398  30.577 1.00 50.28  ? 191 GLY B O   1 
ATOM   3523 N N   . THR B 1 192 ? 44.003 43.812  31.852 1.00 49.36  ? 192 THR B N   1 
ATOM   3524 C CA  . THR B 1 192 ? 44.808 43.666  33.036 1.00 48.44  ? 192 THR B CA  1 
ATOM   3525 C C   . THR B 1 192 ? 43.982 43.000  34.134 1.00 48.91  ? 192 THR B C   1 
ATOM   3526 O O   . THR B 1 192 ? 42.798 43.301  34.307 1.00 49.87  ? 192 THR B O   1 
ATOM   3527 C CB  . THR B 1 192 ? 45.213 45.048  33.570 1.00 47.88  ? 192 THR B CB  1 
ATOM   3528 O OG1 . THR B 1 192 ? 46.015 45.707  32.584 1.00 51.45  ? 192 THR B OG1 1 
ATOM   3529 C CG2 . THR B 1 192 ? 46.020 45.006  34.845 1.00 42.96  ? 192 THR B CG2 1 
ATOM   3530 N N   . LEU B 1 193 ? 44.637 42.160  34.924 1.00 47.70  ? 193 LEU B N   1 
ATOM   3531 C CA  . LEU B 1 193 ? 43.951 41.497  36.006 1.00 45.97  ? 193 LEU B CA  1 
ATOM   3532 C C   . LEU B 1 193 ? 44.336 42.066  37.358 1.00 45.57  ? 193 LEU B C   1 
ATOM   3533 O O   . LEU B 1 193 ? 45.474 41.961  37.803 1.00 45.64  ? 193 LEU B O   1 
ATOM   3534 C CB  . LEU B 1 193 ? 44.302 40.027  35.953 1.00 43.94  ? 193 LEU B CB  1 
ATOM   3535 C CG  . LEU B 1 193 ? 44.185 39.336  37.317 1.00 42.58  ? 193 LEU B CG  1 
ATOM   3536 C CD1 . LEU B 1 193 ? 42.711 39.242  37.670 1.00 41.70  ? 193 LEU B CD1 1 
ATOM   3537 C CD2 . LEU B 1 193 ? 44.924 38.031  37.139 1.00 42.11  ? 193 LEU B CD2 1 
ATOM   3538 N N   . TYR B 1 194 ? 43.288 42.405  38.134 1.00 44.39  ? 194 TYR B N   1 
ATOM   3539 C CA  . TYR B 1 194 ? 43.597 43.023  39.438 1.00 43.32  ? 194 TYR B CA  1 
ATOM   3540 C C   . TYR B 1 194 ? 43.145 42.128  40.584 1.00 42.90  ? 194 TYR B C   1 
ATOM   3541 O O   . TYR B 1 194 ? 41.950 41.853  40.759 1.00 43.35  ? 194 TYR B O   1 
ATOM   3542 C CB  . TYR B 1 194 ? 43.061 44.428  39.469 1.00 42.67  ? 194 TYR B CB  1 
ATOM   3543 C CG  . TYR B 1 194 ? 43.544 45.400  38.448 1.00 40.67  ? 194 TYR B CG  1 
ATOM   3544 C CD1 . TYR B 1 194 ? 44.651 46.177  38.608 1.00 39.68  ? 194 TYR B CD1 1 
ATOM   3545 C CD2 . TYR B 1 194 ? 42.721 45.651  37.347 1.00 41.13  ? 194 TYR B CD2 1 
ATOM   3546 C CE1 . TYR B 1 194 ? 44.960 47.160  37.687 1.00 38.88  ? 194 TYR B CE1 1 
ATOM   3547 C CE2 . TYR B 1 194 ? 43.010 46.632  36.419 1.00 40.21  ? 194 TYR B CE2 1 
ATOM   3548 C CZ  . TYR B 1 194 ? 44.162 47.346  36.600 1.00 40.14  ? 194 TYR B CZ  1 
ATOM   3549 O OH  . TYR B 1 194 ? 44.520 48.261  35.653 1.00 43.26  ? 194 TYR B OH  1 
ATOM   3550 N N   . ARG B 1 195 ? 44.118 41.419  41.169 1.00 41.76  ? 195 ARG B N   1 
ATOM   3551 C CA  . ARG B 1 195 ? 43.865 40.375  42.146 1.00 40.63  ? 195 ARG B CA  1 
ATOM   3552 C C   . ARG B 1 195 ? 44.036 40.989  43.531 1.00 40.23  ? 195 ARG B C   1 
ATOM   3553 O O   . ARG B 1 195 ? 45.186 41.123  43.959 1.00 41.70  ? 195 ARG B O   1 
ATOM   3554 C CB  . ARG B 1 195 ? 44.828 39.200  42.015 1.00 37.28  ? 195 ARG B CB  1 
ATOM   3555 C CG  . ARG B 1 195 ? 44.196 37.836  42.123 1.00 38.78  ? 195 ARG B CG  1 
ATOM   3556 C CD  . ARG B 1 195 ? 45.135 36.635  42.113 1.00 36.62  ? 195 ARG B CD  1 
ATOM   3557 N NE  . ARG B 1 195 ? 46.154 36.689  43.056 1.00 35.71  ? 195 ARG B NE  1 
ATOM   3558 C CZ  . ARG B 1 195 ? 47.145 36.789  43.845 1.00 39.50  ? 195 ARG B CZ  1 
ATOM   3559 N NH1 . ARG B 1 195 ? 48.294 37.312  43.432 1.00 41.21  ? 195 ARG B NH1 1 
ATOM   3560 N NH2 . ARG B 1 195 ? 47.074 36.466  45.152 1.00 41.91  ? 195 ARG B NH2 1 
ATOM   3561 N N   . ILE B 1 196 ? 42.945 41.422  44.124 1.00 38.43  ? 196 ILE B N   1 
ATOM   3562 C CA  . ILE B 1 196 ? 42.954 42.063  45.428 1.00 37.12  ? 196 ILE B CA  1 
ATOM   3563 C C   . ILE B 1 196 ? 42.683 41.041  46.519 1.00 36.60  ? 196 ILE B C   1 
ATOM   3564 O O   . ILE B 1 196 ? 41.848 40.139  46.426 1.00 36.71  ? 196 ILE B O   1 
ATOM   3565 C CB  . ILE B 1 196 ? 41.786 43.097  45.423 1.00 38.21  ? 196 ILE B CB  1 
ATOM   3566 C CG1 . ILE B 1 196 ? 42.046 44.198  44.387 1.00 37.99  ? 196 ILE B CG1 1 
ATOM   3567 C CG2 . ILE B 1 196 ? 41.529 43.744  46.765 1.00 32.76  ? 196 ILE B CG2 1 
ATOM   3568 C CD1 . ILE B 1 196 ? 41.096 44.048  43.228 1.00 41.75  ? 196 ILE B CD1 1 
ATOM   3569 N N   . THR B 1 197 ? 43.543 40.972  47.498 1.00 36.54  ? 197 THR B N   1 
ATOM   3570 C CA  . THR B 1 197 ? 43.493 40.120  48.658 1.00 35.92  ? 197 THR B CA  1 
ATOM   3571 C C   . THR B 1 197 ? 43.404 40.939  49.950 1.00 36.27  ? 197 THR B C   1 
ATOM   3572 O O   . THR B 1 197 ? 43.628 42.169  49.988 1.00 35.19  ? 197 THR B O   1 
ATOM   3573 C CB  . THR B 1 197 ? 44.762 39.245  48.700 1.00 35.35  ? 197 THR B CB  1 
ATOM   3574 O OG1 . THR B 1 197 ? 45.929 40.046  48.796 1.00 34.71  ? 197 THR B OG1 1 
ATOM   3575 C CG2 . THR B 1 197 ? 44.867 38.333  47.511 1.00 31.33  ? 197 THR B CG2 1 
ATOM   3576 N N   . HIS B 1 198 ? 42.668 40.334  50.902 1.00 36.74  ? 198 HIS B N   1 
ATOM   3577 C CA  . HIS B 1 198 ? 42.516 40.982  52.222 1.00 37.62  ? 198 HIS B CA  1 
ATOM   3578 C C   . HIS B 1 198 ? 43.246 40.212  53.345 1.00 38.44  ? 198 HIS B C   1 
ATOM   3579 O O   . HIS B 1 198 ? 43.061 39.054  53.769 1.00 37.51  ? 198 HIS B O   1 
ATOM   3580 C CB  . HIS B 1 198 ? 41.123 41.442  52.595 1.00 31.60  ? 198 HIS B CB  1 
ATOM   3581 C CG  . HIS B 1 198 ? 40.950 42.223  53.838 1.00 32.71  ? 198 HIS B CG  1 
ATOM   3582 N ND1 . HIS B 1 198 ? 40.101 41.844  54.880 1.00 32.25  ? 198 HIS B ND1 1 
ATOM   3583 C CD2 . HIS B 1 198 ? 41.593 43.355  54.284 1.00 34.97  ? 198 HIS B CD2 1 
ATOM   3584 C CE1 . HIS B 1 198 ? 40.300 42.685  55.902 1.00 31.12  ? 198 HIS B CE1 1 
ATOM   3585 N NE2 . HIS B 1 198 ? 41.198 43.597  55.606 1.00 31.01  ? 198 HIS B NE2 1 
ATOM   3586 N N   . THR B 1 199 ? 44.007 41.097  53.999 1.00 38.44  ? 199 THR B N   1 
ATOM   3587 C CA  . THR B 1 199 ? 44.819 40.796  55.144 1.00 40.75  ? 199 THR B CA  1 
ATOM   3588 C C   . THR B 1 199 ? 45.262 39.343  55.081 1.00 42.37  ? 199 THR B C   1 
ATOM   3589 O O   . THR B 1 199 ? 46.108 39.036  54.214 1.00 43.99  ? 199 THR B O   1 
ATOM   3590 C CB  . THR B 1 199 ? 44.114 41.043  56.489 1.00 38.37  ? 199 THR B CB  1 
ATOM   3591 O OG1 . THR B 1 199 ? 42.703 40.734  56.338 1.00 38.77  ? 199 THR B OG1 1 
ATOM   3592 C CG2 . THR B 1 199 ? 44.438 42.469  56.876 1.00 33.94  ? 199 THR B CG2 1 
ATOM   3593 N N   . ASN B 1 200 ? 44.741 38.472  55.893 1.00 42.50  ? 200 ASN B N   1 
ATOM   3594 C CA  . ASN B 1 200 ? 45.083 37.092  55.982 1.00 43.45  ? 200 ASN B CA  1 
ATOM   3595 C C   . ASN B 1 200 ? 43.836 36.240  55.644 1.00 43.37  ? 200 ASN B C   1 
ATOM   3596 O O   . ASN B 1 200 ? 43.588 35.184  56.299 1.00 43.02  ? 200 ASN B O   1 
ATOM   3597 C CB  . ASN B 1 200 ? 45.556 36.726  57.409 1.00 48.12  ? 200 ASN B CB  1 
ATOM   3598 C CG  . ASN B 1 200 ? 44.461 36.854  58.444 1.00 55.72  ? 200 ASN B CG  1 
ATOM   3599 O OD1 . ASN B 1 200 ? 43.430 37.503  58.155 1.00 56.89  ? 200 ASN B OD1 1 
ATOM   3600 N ND2 . ASN B 1 200 ? 44.614 36.276  59.648 1.00 57.84  ? 200 ASN B ND2 1 
ATOM   3601 N N   . ASP B 1 201 ? 42.983 36.784  54.766 1.00 41.99  ? 201 ASP B N   1 
ATOM   3602 C CA  . ASP B 1 201 ? 41.866 35.982  54.293 1.00 40.88  ? 201 ASP B CA  1 
ATOM   3603 C C   . ASP B 1 201 ? 42.360 34.610  53.889 1.00 41.58  ? 201 ASP B C   1 
ATOM   3604 O O   . ASP B 1 201 ? 43.330 34.558  53.164 1.00 42.17  ? 201 ASP B O   1 
ATOM   3605 C CB  . ASP B 1 201 ? 41.217 36.736  53.156 1.00 36.90  ? 201 ASP B CB  1 
ATOM   3606 C CG  . ASP B 1 201 ? 40.200 36.063  52.276 1.00 32.63  ? 201 ASP B CG  1 
ATOM   3607 O OD1 . ASP B 1 201 ? 39.723 34.968  52.618 1.00 29.11  ? 201 ASP B OD1 1 
ATOM   3608 O OD2 . ASP B 1 201 ? 39.811 36.644  51.218 1.00 29.36  ? 201 ASP B OD2 1 
ATOM   3609 N N   . ILE B 1 202 ? 41.439 33.637  53.947 1.00 42.53  ? 202 ILE B N   1 
ATOM   3610 C CA  . ILE B 1 202 ? 41.762 32.259  53.703 1.00 42.51  ? 202 ILE B CA  1 
ATOM   3611 C C   . ILE B 1 202 ? 41.604 31.808  52.270 1.00 43.60  ? 202 ILE B C   1 
ATOM   3612 O O   . ILE B 1 202 ? 42.337 30.909  51.829 1.00 43.86  ? 202 ILE B O   1 
ATOM   3613 C CB  . ILE B 1 202 ? 40.877 31.307  54.562 1.00 41.80  ? 202 ILE B CB  1 
ATOM   3614 C CG1 . ILE B 1 202 ? 41.319 29.851  54.360 1.00 39.16  ? 202 ILE B CG1 1 
ATOM   3615 C CG2 . ILE B 1 202 ? 39.388 31.493  54.256 1.00 38.54  ? 202 ILE B CG2 1 
ATOM   3616 C CD1 . ILE B 1 202 ? 40.756 28.762  55.216 1.00 39.81  ? 202 ILE B CD1 1 
ATOM   3617 N N   . VAL B 1 203 ? 40.680 32.421  51.536 1.00 43.74  ? 203 VAL B N   1 
ATOM   3618 C CA  . VAL B 1 203 ? 40.352 31.944  50.207 1.00 43.88  ? 203 VAL B CA  1 
ATOM   3619 C C   . VAL B 1 203 ? 41.477 31.985  49.199 1.00 44.40  ? 203 VAL B C   1 
ATOM   3620 O O   . VAL B 1 203 ? 41.871 30.913  48.706 1.00 43.62  ? 203 VAL B O   1 
ATOM   3621 C CB  . VAL B 1 203 ? 38.985 32.491  49.763 1.00 43.12  ? 203 VAL B CB  1 
ATOM   3622 C CG1 . VAL B 1 203 ? 38.457 31.890  48.452 1.00 39.72  ? 203 VAL B CG1 1 
ATOM   3623 C CG2 . VAL B 1 203 ? 37.977 32.188  50.882 1.00 37.77  ? 203 VAL B CG2 1 
ATOM   3624 N N   . PRO B 1 204 ? 42.335 33.008  49.216 1.00 44.84  ? 204 PRO B N   1 
ATOM   3625 C CA  . PRO B 1 204 ? 43.414 33.158  48.257 1.00 45.10  ? 204 PRO B CA  1 
ATOM   3626 C C   . PRO B 1 204 ? 44.643 32.331  48.566 1.00 45.65  ? 204 PRO B C   1 
ATOM   3627 O O   . PRO B 1 204 ? 45.708 32.333  47.948 1.00 45.54  ? 204 PRO B O   1 
ATOM   3628 C CB  . PRO B 1 204 ? 43.785 34.635  48.319 1.00 44.94  ? 204 PRO B CB  1 
ATOM   3629 C CG  . PRO B 1 204 ? 42.537 35.307  48.784 1.00 45.45  ? 204 PRO B CG  1 
ATOM   3630 C CD  . PRO B 1 204 ? 41.945 34.331  49.788 1.00 45.20  ? 204 PRO B CD  1 
ATOM   3631 N N   . ARG B 1 205 ? 44.499 31.559  49.602 1.00 46.10  ? 205 ARG B N   1 
ATOM   3632 C CA  . ARG B 1 205 ? 45.375 30.652  50.272 1.00 46.51  ? 205 ARG B CA  1 
ATOM   3633 C C   . ARG B 1 205 ? 44.919 29.228  49.945 1.00 47.60  ? 205 ARG B C   1 
ATOM   3634 O O   . ARG B 1 205 ? 45.656 28.293  50.267 1.00 48.05  ? 205 ARG B O   1 
ATOM   3635 C CB  . ARG B 1 205 ? 45.171 30.923  51.753 1.00 47.20  ? 205 ARG B CB  1 
ATOM   3636 C CG  . ARG B 1 205 ? 46.268 31.098  52.736 1.00 44.95  ? 205 ARG B CG  1 
ATOM   3637 C CD  . ARG B 1 205 ? 46.489 32.536  53.190 1.00 43.01  ? 205 ARG B CD  1 
ATOM   3638 N NE  . ARG B 1 205 ? 46.883 32.415  54.564 1.00 46.56  ? 205 ARG B NE  1 
ATOM   3639 C CZ  . ARG B 1 205 ? 47.283 33.234  55.478 1.00 50.08  ? 205 ARG B CZ  1 
ATOM   3640 N NH1 . ARG B 1 205 ? 47.415 34.543  55.288 1.00 52.11  ? 205 ARG B NH1 1 
ATOM   3641 N NH2 . ARG B 1 205 ? 47.657 32.754  56.646 1.00 50.94  ? 205 ARG B NH2 1 
ATOM   3642 N N   . LEU B 1 206 ? 43.835 29.087  49.204 1.00 47.74  ? 206 LEU B N   1 
ATOM   3643 C CA  . LEU B 1 206 ? 43.331 27.830  48.709 1.00 47.81  ? 206 LEU B CA  1 
ATOM   3644 C C   . LEU B 1 206 ? 43.006 27.906  47.229 1.00 49.12  ? 206 LEU B C   1 
ATOM   3645 O O   . LEU B 1 206 ? 42.738 28.966  46.667 1.00 50.60  ? 206 LEU B O   1 
ATOM   3646 C CB  . LEU B 1 206 ? 42.011 27.448  49.376 1.00 44.71  ? 206 LEU B CB  1 
ATOM   3647 C CG  . LEU B 1 206 ? 41.980 27.330  50.899 1.00 43.61  ? 206 LEU B CG  1 
ATOM   3648 C CD1 . LEU B 1 206 ? 40.572 27.043  51.399 1.00 40.25  ? 206 LEU B CD1 1 
ATOM   3649 C CD2 . LEU B 1 206 ? 42.988 26.309  51.425 1.00 44.38  ? 206 LEU B CD2 1 
ATOM   3650 N N   . PRO B 1 207 ? 43.104 26.791  46.525 1.00 49.50  ? 207 PRO B N   1 
ATOM   3651 C CA  . PRO B 1 207 ? 43.658 25.574  47.108 1.00 49.45  ? 207 PRO B CA  1 
ATOM   3652 C C   . PRO B 1 207 ? 45.165 25.821  47.293 1.00 48.92  ? 207 PRO B C   1 
ATOM   3653 O O   . PRO B 1 207 ? 45.728 26.876  46.958 1.00 48.09  ? 207 PRO B O   1 
ATOM   3654 C CB  . PRO B 1 207 ? 43.331 24.525  46.069 1.00 50.01  ? 207 PRO B CB  1 
ATOM   3655 C CG  . PRO B 1 207 ? 42.238 25.132  45.222 1.00 49.79  ? 207 PRO B CG  1 
ATOM   3656 C CD  . PRO B 1 207 ? 42.688 26.577  45.114 1.00 49.24  ? 207 PRO B CD  1 
ATOM   3657 N N   . PRO B 1 208 ? 45.763 24.980  48.134 1.00 47.65  ? 208 PRO B N   1 
ATOM   3658 C CA  . PRO B 1 208 ? 47.145 25.095  48.495 1.00 47.14  ? 208 PRO B CA  1 
ATOM   3659 C C   . PRO B 1 208 ? 48.155 24.913  47.373 1.00 46.77  ? 208 PRO B C   1 
ATOM   3660 O O   . PRO B 1 208 ? 48.062 24.067  46.497 1.00 45.09  ? 208 PRO B O   1 
ATOM   3661 C CB  . PRO B 1 208 ? 47.344 24.023  49.559 1.00 47.22  ? 208 PRO B CB  1 
ATOM   3662 C CG  . PRO B 1 208 ? 45.958 23.690  50.004 1.00 47.81  ? 208 PRO B CG  1 
ATOM   3663 C CD  . PRO B 1 208 ? 45.153 23.759  48.718 1.00 47.67  ? 208 PRO B CD  1 
ATOM   3664 N N   . ARG B 1 209 ? 49.308 25.526  47.625 1.00 47.01  ? 209 ARG B N   1 
ATOM   3665 C CA  . ARG B 1 209 ? 50.535 25.420  46.883 1.00 48.22  ? 209 ARG B CA  1 
ATOM   3666 C C   . ARG B 1 209 ? 51.083 24.002  46.812 1.00 48.24  ? 209 ARG B C   1 
ATOM   3667 O O   . ARG B 1 209 ? 51.439 23.541  45.722 1.00 49.45  ? 209 ARG B O   1 
ATOM   3668 C CB  . ARG B 1 209 ? 51.638 26.309  47.493 1.00 47.99  ? 209 ARG B CB  1 
ATOM   3669 C CG  . ARG B 1 209 ? 51.248 27.775  47.343 1.00 46.77  ? 209 ARG B CG  1 
ATOM   3670 C CD  . ARG B 1 209 ? 51.885 28.353  46.095 1.00 50.01  ? 209 ARG B CD  1 
ATOM   3671 N NE  . ARG B 1 209 ? 53.329 28.509  46.235 1.00 51.27  ? 209 ARG B NE  1 
ATOM   3672 C CZ  . ARG B 1 209 ? 54.176 28.012  45.324 1.00 52.27  ? 209 ARG B CZ  1 
ATOM   3673 N NH1 . ARG B 1 209 ? 53.667 27.369  44.268 1.00 50.98  ? 209 ARG B NH1 1 
ATOM   3674 N NH2 . ARG B 1 209 ? 55.475 28.197  45.521 1.00 49.63  ? 209 ARG B NH2 1 
ATOM   3675 N N   . GLU B 1 210 ? 50.873 23.229  47.845 1.00 48.04  ? 210 GLU B N   1 
ATOM   3676 C CA  . GLU B 1 210 ? 51.279 21.838  47.922 1.00 48.37  ? 210 GLU B CA  1 
ATOM   3677 C C   . GLU B 1 210 ? 50.269 20.886  47.309 1.00 47.42  ? 210 GLU B C   1 
ATOM   3678 O O   . GLU B 1 210 ? 50.260 19.681  47.561 1.00 48.21  ? 210 GLU B O   1 
ATOM   3679 C CB  . GLU B 1 210 ? 51.706 21.449  49.327 1.00 48.95  ? 210 GLU B CB  1 
ATOM   3680 C CG  . GLU B 1 210 ? 51.368 22.479  50.376 1.00 55.40  ? 210 GLU B CG  1 
ATOM   3681 C CD  . GLU B 1 210 ? 52.319 23.635  50.541 1.00 58.00  ? 210 GLU B CD  1 
ATOM   3682 O OE1 . GLU B 1 210 ? 53.482 23.590  50.074 1.00 61.68  ? 210 GLU B OE1 1 
ATOM   3683 O OE2 . GLU B 1 210 ? 51.882 24.614  51.189 1.00 58.40  ? 210 GLU B OE2 1 
ATOM   3684 N N   . PHE B 1 211 ? 49.260 21.413  46.623 1.00 45.89  ? 211 PHE B N   1 
ATOM   3685 C CA  . PHE B 1 211 ? 48.457 20.622  45.714 1.00 44.28  ? 211 PHE B CA  1 
ATOM   3686 C C   . PHE B 1 211 ? 48.844 21.107  44.318 1.00 44.15  ? 211 PHE B C   1 
ATOM   3687 O O   . PHE B 1 211 ? 48.093 20.864  43.411 1.00 44.51  ? 211 PHE B O   1 
ATOM   3688 C CB  . PHE B 1 211 ? 46.943 20.606  45.851 1.00 40.22  ? 211 PHE B CB  1 
ATOM   3689 C CG  . PHE B 1 211 ? 46.558 19.745  47.023 1.00 40.14  ? 211 PHE B CG  1 
ATOM   3690 C CD1 . PHE B 1 211 ? 46.840 20.173  48.323 1.00 39.10  ? 211 PHE B CD1 1 
ATOM   3691 C CD2 . PHE B 1 211 ? 45.984 18.506  46.816 1.00 37.84  ? 211 PHE B CD2 1 
ATOM   3692 C CE1 . PHE B 1 211 ? 46.555 19.342  49.393 1.00 39.91  ? 211 PHE B CE1 1 
ATOM   3693 C CE2 . PHE B 1 211 ? 45.683 17.696  47.890 1.00 38.25  ? 211 PHE B CE2 1 
ATOM   3694 C CZ  . PHE B 1 211 ? 45.973 18.104  49.177 1.00 40.08  ? 211 PHE B CZ  1 
ATOM   3695 N N   . GLY B 1 212 ? 49.880 21.924  44.231 1.00 44.41  ? 212 GLY B N   1 
ATOM   3696 C CA  . GLY B 1 212 ? 50.455 22.328  42.979 1.00 45.09  ? 212 GLY B CA  1 
ATOM   3697 C C   . GLY B 1 212 ? 49.737 23.504  42.343 1.00 45.83  ? 212 GLY B C   1 
ATOM   3698 O O   . GLY B 1 212 ? 49.548 23.555  41.120 1.00 46.11  ? 212 GLY B O   1 
ATOM   3699 N N   . TYR B 1 213 ? 49.476 24.518  43.185 1.00 45.23  ? 213 TYR B N   1 
ATOM   3700 C CA  . TYR B 1 213 ? 48.748 25.669  42.649 1.00 43.77  ? 213 TYR B CA  1 
ATOM   3701 C C   . TYR B 1 213 ? 49.646 26.874  42.819 1.00 43.33  ? 213 TYR B C   1 
ATOM   3702 O O   . TYR B 1 213 ? 50.490 26.883  43.707 1.00 44.54  ? 213 TYR B O   1 
ATOM   3703 C CB  . TYR B 1 213 ? 47.430 25.871  43.342 1.00 42.66  ? 213 TYR B CB  1 
ATOM   3704 C CG  . TYR B 1 213 ? 46.270 25.020  42.911 1.00 40.48  ? 213 TYR B CG  1 
ATOM   3705 C CD1 . TYR B 1 213 ? 46.206 23.679  43.268 1.00 40.52  ? 213 TYR B CD1 1 
ATOM   3706 C CD2 . TYR B 1 213 ? 45.207 25.573  42.215 1.00 39.30  ? 213 TYR B CD2 1 
ATOM   3707 C CE1 . TYR B 1 213 ? 45.104 22.904  42.877 1.00 39.94  ? 213 TYR B CE1 1 
ATOM   3708 C CE2 . TYR B 1 213 ? 44.102 24.828  41.859 1.00 39.08  ? 213 TYR B CE2 1 
ATOM   3709 C CZ  . TYR B 1 213 ? 44.064 23.487  42.195 1.00 39.07  ? 213 TYR B CZ  1 
ATOM   3710 O OH  . TYR B 1 213 ? 43.015 22.703  41.798 1.00 38.44  ? 213 TYR B OH  1 
ATOM   3711 N N   . SER B 1 214 ? 49.400 27.880  42.017 1.00 42.58  ? 214 SER B N   1 
ATOM   3712 C CA  . SER B 1 214 ? 50.154 29.116  42.207 1.00 41.93  ? 214 SER B CA  1 
ATOM   3713 C C   . SER B 1 214 ? 49.237 30.317  41.964 1.00 40.74  ? 214 SER B C   1 
ATOM   3714 O O   . SER B 1 214 ? 48.216 30.140  41.319 1.00 39.51  ? 214 SER B O   1 
ATOM   3715 C CB  . SER B 1 214 ? 51.178 29.090  41.042 1.00 44.64  ? 214 SER B CB  1 
ATOM   3716 O OG  . SER B 1 214 ? 52.401 28.668  41.570 1.00 46.95  ? 214 SER B OG  1 
ATOM   3717 N N   . HIS B 1 215 ? 49.732 31.489  42.304 1.00 40.57  ? 215 HIS B N   1 
ATOM   3718 C CA  . HIS B 1 215 ? 49.068 32.736  42.040 1.00 40.39  ? 215 HIS B CA  1 
ATOM   3719 C C   . HIS B 1 215 ? 49.812 33.566  40.978 1.00 41.10  ? 215 HIS B C   1 
ATOM   3720 O O   . HIS B 1 215 ? 51.025 33.810  40.992 1.00 41.11  ? 215 HIS B O   1 
ATOM   3721 C CB  . HIS B 1 215 ? 49.003 33.639  43.290 1.00 39.68  ? 215 HIS B CB  1 
ATOM   3722 C CG  . HIS B 1 215 ? 47.715 33.514  44.031 1.00 39.22  ? 215 HIS B CG  1 
ATOM   3723 N ND1 . HIS B 1 215 ? 46.498 33.391  43.373 1.00 38.66  ? 215 HIS B ND1 1 
ATOM   3724 C CD2 . HIS B 1 215 ? 47.436 33.483  45.350 1.00 39.49  ? 215 HIS B CD2 1 
ATOM   3725 C CE1 . HIS B 1 215 ? 45.522 33.284  44.258 1.00 36.69  ? 215 HIS B CE1 1 
ATOM   3726 N NE2 . HIS B 1 215 ? 46.066 33.344  45.457 1.00 37.90  ? 215 HIS B NE2 1 
ATOM   3727 N N   . SER B 1 216 ? 48.943 34.299  40.273 1.00 41.31  ? 216 SER B N   1 
ATOM   3728 C CA  . SER B 1 216 ? 49.347 35.211  39.232 1.00 40.36  ? 216 SER B CA  1 
ATOM   3729 C C   . SER B 1 216 ? 49.998 36.405  39.943 1.00 40.43  ? 216 SER B C   1 
ATOM   3730 O O   . SER B 1 216 ? 49.744 36.489  41.156 1.00 38.50  ? 216 SER B O   1 
ATOM   3731 C CB  . SER B 1 216 ? 48.237 35.717  38.360 1.00 39.56  ? 216 SER B CB  1 
ATOM   3732 O OG  . SER B 1 216 ? 47.111 36.069  39.139 1.00 46.54  ? 216 SER B OG  1 
ATOM   3733 N N   . SER B 1 217 ? 50.655 37.244  39.118 1.00 39.97  ? 217 SER B N   1 
ATOM   3734 C CA  . SER B 1 217 ? 51.243 38.406  39.870 1.00 40.42  ? 217 SER B CA  1 
ATOM   3735 C C   . SER B 1 217 ? 50.787 39.625  39.087 1.00 39.77  ? 217 SER B C   1 
ATOM   3736 O O   . SER B 1 217 ? 50.667 39.377  37.885 1.00 41.53  ? 217 SER B O   1 
ATOM   3737 C CB  . SER B 1 217 ? 52.756 38.225  39.748 1.00 42.62  ? 217 SER B CB  1 
ATOM   3738 O OG  . SER B 1 217 ? 53.546 39.347  40.065 1.00 41.65  ? 217 SER B OG  1 
ATOM   3739 N N   . PRO B 1 218 ? 50.635 40.784  39.608 1.00 38.52  ? 218 PRO B N   1 
ATOM   3740 C CA  . PRO B 1 218 ? 50.845 41.007  41.018 1.00 39.13  ? 218 PRO B CA  1 
ATOM   3741 C C   . PRO B 1 218 ? 49.612 40.872  41.904 1.00 39.54  ? 218 PRO B C   1 
ATOM   3742 O O   . PRO B 1 218 ? 48.709 40.061  41.668 1.00 39.20  ? 218 PRO B O   1 
ATOM   3743 C CB  . PRO B 1 218 ? 51.370 42.439  40.992 1.00 38.71  ? 218 PRO B CB  1 
ATOM   3744 C CG  . PRO B 1 218 ? 50.489 43.096  39.957 1.00 38.87  ? 218 PRO B CG  1 
ATOM   3745 C CD  . PRO B 1 218 ? 50.273 42.016  38.913 1.00 38.27  ? 218 PRO B CD  1 
ATOM   3746 N N   . GLU B 1 219 ? 49.793 41.230  43.178 1.00 40.39  ? 219 GLU B N   1 
ATOM   3747 C CA  . GLU B 1 219 ? 48.779 41.136  44.225 1.00 40.94  ? 219 GLU B CA  1 
ATOM   3748 C C   . GLU B 1 219 ? 48.553 42.530  44.842 1.00 40.56  ? 219 GLU B C   1 
ATOM   3749 O O   . GLU B 1 219 ? 49.487 43.256  45.216 1.00 38.09  ? 219 GLU B O   1 
ATOM   3750 C CB  . GLU B 1 219 ? 49.126 40.130  45.307 1.00 44.36  ? 219 GLU B CB  1 
ATOM   3751 C CG  . GLU B 1 219 ? 48.305 40.034  46.562 1.00 48.44  ? 219 GLU B CG  1 
ATOM   3752 C CD  . GLU B 1 219 ? 48.892 39.247  47.713 1.00 51.19  ? 219 GLU B CD  1 
ATOM   3753 O OE1 . GLU B 1 219 ? 49.823 38.428  47.529 1.00 55.41  ? 219 GLU B OE1 1 
ATOM   3754 O OE2 . GLU B 1 219 ? 48.456 39.390  48.878 1.00 49.78  ? 219 GLU B OE2 1 
ATOM   3755 N N   . TYR B 1 220 ? 47.265 42.929  44.763 1.00 40.03  ? 220 TYR B N   1 
ATOM   3756 C CA  . TYR B 1 220 ? 46.977 44.226  45.440 1.00 40.04  ? 220 TYR B CA  1 
ATOM   3757 C C   . TYR B 1 220 ? 46.479 43.804  46.808 1.00 39.84  ? 220 TYR B C   1 
ATOM   3758 O O   . TYR B 1 220 ? 45.470 43.124  46.781 1.00 39.98  ? 220 TYR B O   1 
ATOM   3759 C CB  . TYR B 1 220 ? 45.942 45.060  44.700 1.00 39.06  ? 220 TYR B CB  1 
ATOM   3760 C CG  . TYR B 1 220 ? 46.553 45.596  43.421 1.00 37.09  ? 220 TYR B CG  1 
ATOM   3761 C CD1 . TYR B 1 220 ? 47.265 46.784  43.498 1.00 36.76  ? 220 TYR B CD1 1 
ATOM   3762 C CD2 . TYR B 1 220 ? 46.506 44.906  42.217 1.00 35.40  ? 220 TYR B CD2 1 
ATOM   3763 C CE1 . TYR B 1 220 ? 47.913 47.279  42.378 1.00 35.78  ? 220 TYR B CE1 1 
ATOM   3764 C CE2 . TYR B 1 220 ? 47.119 45.409  41.097 1.00 34.22  ? 220 TYR B CE2 1 
ATOM   3765 C CZ  . TYR B 1 220 ? 47.839 46.576  41.193 1.00 35.46  ? 220 TYR B CZ  1 
ATOM   3766 O OH  . TYR B 1 220 ? 48.491 47.129  40.110 1.00 37.05  ? 220 TYR B OH  1 
ATOM   3767 N N   . TRP B 1 221 ? 47.263 44.014  47.852 1.00 40.51  ? 221 TRP B N   1 
ATOM   3768 C CA  . TRP B 1 221 ? 46.980 43.497  49.189 1.00 39.87  ? 221 TRP B CA  1 
ATOM   3769 C C   . TRP B 1 221 ? 46.522 44.598  50.132 1.00 39.63  ? 221 TRP B C   1 
ATOM   3770 O O   . TRP B 1 221 ? 47.189 45.622  50.207 1.00 40.00  ? 221 TRP B O   1 
ATOM   3771 C CB  . TRP B 1 221 ? 48.179 42.756  49.783 1.00 36.93  ? 221 TRP B CB  1 
ATOM   3772 C CG  . TRP B 1 221 ? 48.026 42.140  51.135 1.00 35.07  ? 221 TRP B CG  1 
ATOM   3773 C CD1 . TRP B 1 221 ? 47.083 41.250  51.551 1.00 35.34  ? 221 TRP B CD1 1 
ATOM   3774 C CD2 . TRP B 1 221 ? 48.912 42.305  52.255 1.00 34.47  ? 221 TRP B CD2 1 
ATOM   3775 N NE1 . TRP B 1 221 ? 47.283 40.891  52.882 1.00 34.54  ? 221 TRP B NE1 1 
ATOM   3776 C CE2 . TRP B 1 221 ? 48.388 41.547  53.322 1.00 34.34  ? 221 TRP B CE2 1 
ATOM   3777 C CE3 . TRP B 1 221 ? 50.096 43.028  52.449 1.00 33.18  ? 221 TRP B CE3 1 
ATOM   3778 C CZ2 . TRP B 1 221 ? 49.006 41.486  54.574 1.00 36.08  ? 221 TRP B CZ2 1 
ATOM   3779 C CZ3 . TRP B 1 221 ? 50.670 42.985  53.739 1.00 36.14  ? 221 TRP B CZ3 1 
ATOM   3780 C CH2 . TRP B 1 221 ? 50.149 42.226  54.793 1.00 34.75  ? 221 TRP B CH2 1 
ATOM   3781 N N   . ILE B 1 222 ? 45.448 44.304  50.890 1.00 39.28  ? 222 ILE B N   1 
ATOM   3782 C CA  . ILE B 1 222 ? 44.792 45.288  51.732 1.00 37.57  ? 222 ILE B CA  1 
ATOM   3783 C C   . ILE B 1 222 ? 45.258 44.968  53.154 1.00 38.81  ? 222 ILE B C   1 
ATOM   3784 O O   . ILE B 1 222 ? 44.905 43.962  53.782 1.00 38.45  ? 222 ILE B O   1 
ATOM   3785 C CB  . ILE B 1 222 ? 43.256 45.305  51.625 1.00 31.32  ? 222 ILE B CB  1 
ATOM   3786 C CG1 . ILE B 1 222 ? 42.689 45.655  50.247 1.00 26.67  ? 222 ILE B CG1 1 
ATOM   3787 C CG2 . ILE B 1 222 ? 42.596 46.243  52.657 1.00 28.79  ? 222 ILE B CG2 1 
ATOM   3788 C CD1 . ILE B 1 222 ? 41.270 45.124  49.976 1.00 18.53  ? 222 ILE B CD1 1 
ATOM   3789 N N   . LYS B 1 223 ? 45.925 45.947  53.772 1.00 38.92  ? 223 LYS B N   1 
ATOM   3790 C CA  . LYS B 1 223 ? 46.445 45.682  55.096 1.00 39.56  ? 223 LYS B CA  1 
ATOM   3791 C C   . LYS B 1 223 ? 45.476 46.084  56.209 1.00 39.26  ? 223 LYS B C   1 
ATOM   3792 O O   . LYS B 1 223 ? 45.728 45.773  57.369 1.00 39.67  ? 223 LYS B O   1 
ATOM   3793 C CB  . LYS B 1 223 ? 47.646 46.570  55.343 1.00 43.95  ? 223 LYS B CB  1 
ATOM   3794 C CG  . LYS B 1 223 ? 48.882 46.428  54.509 1.00 49.41  ? 223 LYS B CG  1 
ATOM   3795 C CD  . LYS B 1 223 ? 50.060 47.175  55.150 1.00 52.68  ? 223 LYS B CD  1 
ATOM   3796 C CE  . LYS B 1 223 ? 49.746 48.532  55.793 1.00 54.32  ? 223 LYS B CE  1 
ATOM   3797 N NZ  . LYS B 1 223 ? 50.751 49.583  55.443 1.00 54.95  ? 223 LYS B NZ  1 
ATOM   3798 N N   . SER B 1 224 ? 44.441 46.842  55.913 1.00 38.53  ? 224 SER B N   1 
ATOM   3799 C CA  . SER B 1 224 ? 43.584 47.320  57.007 1.00 37.64  ? 224 SER B CA  1 
ATOM   3800 C C   . SER B 1 224 ? 42.748 46.142  57.481 1.00 36.80  ? 224 SER B C   1 
ATOM   3801 O O   . SER B 1 224 ? 42.470 45.207  56.716 1.00 37.28  ? 224 SER B O   1 
ATOM   3802 C CB  . SER B 1 224 ? 42.878 48.617  56.563 1.00 33.74  ? 224 SER B CB  1 
ATOM   3803 O OG  . SER B 1 224 ? 42.511 48.448  55.184 1.00 35.65  ? 224 SER B OG  1 
ATOM   3804 N