data_2YP1
# 
_entry.id   2YP1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   2YP1         
PDBE  EBI-54580    
WWPDB D_1290054580 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          2YOR 
_pdbx_database_related.content_type   unspecified 
_pdbx_database_related.details        
;CRYSTALLIZATION OF A 45 KDA PEROXYGENASE- PEROXIDASE FROM THE MUSHROOM AGROCYBE AEGERITA AND STRUCTURE DETERMINATION BY SAD UTILIZING ONLY THE HAEM IRON
;
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2YP1 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2012-10-29 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Piontek, K.'      1 
'Strittmatter, E.' 2 
'Ullrich, R.'      3 
'Plattner, D.A.'   4 
'Hofrichter, M.'   5 
# 
loop_
_citation.id 
_citation.title 
_citation.journal_abbrev 
_citation.journal_volume 
_citation.page_first 
_citation.page_last 
_citation.year 
_citation.journal_id_ASTM 
_citation.country 
_citation.journal_id_ISSN 
_citation.journal_id_CSD 
_citation.book_publisher 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_DOI 
primary 'Structural Basis of Substrate Conversion in a New Aromatic Peroxygenase: P450 Functionality with Benefits' J.Biol.Chem. 
288 34767 ? 2013 JBCHA3 US 0021-9258 0071 ? 24126915 10.1074/JBC.M113.514521   
1       
;Crystallization of a 45 kDa Peroxygenase/Peroxidase from the Mushroom Agrocybe Aegerita and Structure Determination by Sad Utilizing Only the Haem Iron.
;
'Acta Crystallogr.,Sect.F' 66  693   ? 2010 ?      DK 1744-3091 ?    ? 20516602 10.1107/S1744309110013515 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Piontek, K.'      1  
primary 'Strittmatter, E.' 2  
primary 'Ullrich, R.'      3  
primary 'Grobe, G.'        4  
primary 'Pecyna, M.J.'     5  
primary 'Kluge, M.'        6  
primary 'Scheibner, K.'    7  
primary 'Hofrichter, M.'   8  
primary 'Plattner, D.A.'   9  
1       'Piontek, K.'      10 
1       'Ullrich, R.'      11 
1       'Liers, C.'        12 
1       'Diederichs, K.'   13 
1       'Plattner, D.A.'   14 
1       'Hofrichter, M.'   15 
# 
_cell.entry_id           2YP1 
_cell.length_a           112.750 
_cell.length_b           144.880 
_cell.length_c           134.460 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              16 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         2YP1 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
# 
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 'AROMATIC PEROXYGENASE'           35692.707 4    1.11.2.1 ? ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   4    ?        ? ? ? 
3 non-polymer syn 'MAGNESIUM ION'                   24.305    4    ?        ? ? ? 
4 non-polymer man N-ACETYL-D-GLUCOSAMINE            221.208   36   ?        ? ? ? 
5 non-polymer man BETA-D-MANNOSE                    180.156   7    ?        ? ? ? 
6 non-polymer man ALPHA-D-MANNOSE                   180.156   17   ?        ? ? ? 
7 non-polymer syn 'ACETATE ION'                     59.044    5    ?        ? ? ? 
8 non-polymer syn 'SULFATE ION'                     96.063    13   ?        ? ? ? 
9 water       nat water                             18.015    1185 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        AAP 
# 
_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       
;LPPGPLENSSAKLVNDEAHPWKPLRPGDIRGPCPGLNTLASHGYLPRNGVATPVQIINAVQEGLNFDNQAAVFATYAAHL
VDGNLITDLLSIGRKTRLTGPDPPPPASVGGLNEHGTFEGDASMTRGDAFFGNNHDFNETLFEQLVDYSNRFGGGKYNLT
VAGELRFKRIQDSIATNPNFSFVDFRFFTAYGETTFPANLFVDGRRDDGQLDMDAARSFFQFSRMPDDFFRAPSPRSGTG
VEVVIQAHPMQPGRNVGKINSYTVDPTSSDFSTPCLMYEKFVNITVKSLYPNPTVQLRKALNTNLDFFFQGVAAGCTQVF
PYGRD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;LPPGPLENSSAKLVNDEAHPWKPLRPGDIRGPCPGLNTLASHGYLPRNGVATPVQIINAVQEGLNFDNQAAVFATYAAHL
VDGNLITDLLSIGRKTRLTGPDPPPPASVGGLNEHGTFEGDASMTRGDAFFGNNHDFNETLFEQLVDYSNRFGGGKYNLT
VAGELRFKRIQDSIATNPNFSFVDFRFFTAYGETTFPANLFVDGRRDDGQLDMDAARSFFQFSRMPDDFFRAPSPRSGTG
VEVVIQAHPMQPGRNVGKINSYTVDPTSSDFSTPCLMYEKFVNITVKSLYPNPTVQLRKALNTNLDFFFQGVAAGCTQVF
PYGRD
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_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   LEU n 
1 2   PRO n 
1 3   PRO n 
1 4   GLY n 
1 5   PRO n 
1 6   LEU n 
1 7   GLU n 
1 8   ASN n 
1 9   SER n 
1 10  SER n 
1 11  ALA n 
1 12  LYS n 
1 13  LEU n 
1 14  VAL n 
1 15  ASN n 
1 16  ASP n 
1 17  GLU n 
1 18  ALA n 
1 19  HIS n 
1 20  PRO n 
1 21  TRP n 
1 22  LYS n 
1 23  PRO n 
1 24  LEU n 
1 25  ARG n 
1 26  PRO n 
1 27  GLY n 
1 28  ASP n 
1 29  ILE n 
1 30  ARG n 
1 31  GLY n 
1 32  PRO n 
1 33  CYS n 
1 34  PRO n 
1 35  GLY n 
1 36  LEU n 
1 37  ASN n 
1 38  THR n 
1 39  LEU n 
1 40  ALA n 
1 41  SER n 
1 42  HIS n 
1 43  GLY n 
1 44  TYR n 
1 45  LEU n 
1 46  PRO n 
1 47  ARG n 
1 48  ASN n 
1 49  GLY n 
1 50  VAL n 
1 51  ALA n 
1 52  THR n 
1 53  PRO n 
1 54  VAL n 
1 55  GLN n 
1 56  ILE n 
1 57  ILE n 
1 58  ASN n 
1 59  ALA n 
1 60  VAL n 
1 61  GLN n 
1 62  GLU n 
1 63  GLY n 
1 64  LEU n 
1 65  ASN n 
1 66  PHE n 
1 67  ASP n 
1 68  ASN n 
1 69  GLN n 
1 70  ALA n 
1 71  ALA n 
1 72  VAL n 
1 73  PHE n 
1 74  ALA n 
1 75  THR n 
1 76  TYR n 
1 77  ALA n 
1 78  ALA n 
1 79  HIS n 
1 80  LEU n 
1 81  VAL n 
1 82  ASP n 
1 83  GLY n 
1 84  ASN n 
1 85  LEU n 
1 86  ILE n 
1 87  THR n 
1 88  ASP n 
1 89  LEU n 
1 90  LEU n 
1 91  SER n 
1 92  ILE n 
1 93  GLY n 
1 94  ARG n 
1 95  LYS n 
1 96  THR n 
1 97  ARG n 
1 98  LEU n 
1 99  THR n 
1 100 GLY n 
1 101 PRO n 
1 102 ASP n 
1 103 PRO n 
1 104 PRO n 
1 105 PRO n 
1 106 PRO n 
1 107 ALA n 
1 108 SER n 
1 109 VAL n 
1 110 GLY n 
1 111 GLY n 
1 112 LEU n 
1 113 ASN n 
1 114 GLU n 
1 115 HIS n 
1 116 GLY n 
1 117 THR n 
1 118 PHE n 
1 119 GLU n 
1 120 GLY n 
1 121 ASP n 
1 122 ALA n 
1 123 SER n 
1 124 MET n 
1 125 THR n 
1 126 ARG n 
1 127 GLY n 
1 128 ASP n 
1 129 ALA n 
1 130 PHE n 
1 131 PHE n 
1 132 GLY n 
1 133 ASN n 
1 134 ASN n 
1 135 HIS n 
1 136 ASP n 
1 137 PHE n 
1 138 ASN n 
1 139 GLU n 
1 140 THR n 
1 141 LEU n 
1 142 PHE n 
1 143 GLU n 
1 144 GLN n 
1 145 LEU n 
1 146 VAL n 
1 147 ASP n 
1 148 TYR n 
1 149 SER n 
1 150 ASN n 
1 151 ARG n 
1 152 PHE n 
1 153 GLY n 
1 154 GLY n 
1 155 GLY n 
1 156 LYS n 
1 157 TYR n 
1 158 ASN n 
1 159 LEU n 
1 160 THR n 
1 161 VAL n 
1 162 ALA n 
1 163 GLY n 
1 164 GLU n 
1 165 LEU n 
1 166 ARG n 
1 167 PHE n 
1 168 LYS n 
1 169 ARG n 
1 170 ILE n 
1 171 GLN n 
1 172 ASP n 
1 173 SER n 
1 174 ILE n 
1 175 ALA n 
1 176 THR n 
1 177 ASN n 
1 178 PRO n 
1 179 ASN n 
1 180 PHE n 
1 181 SER n 
1 182 PHE n 
1 183 VAL n 
1 184 ASP n 
1 185 PHE n 
1 186 ARG n 
1 187 PHE n 
1 188 PHE n 
1 189 THR n 
1 190 ALA n 
1 191 TYR n 
1 192 GLY n 
1 193 GLU n 
1 194 THR n 
1 195 THR n 
1 196 PHE n 
1 197 PRO n 
1 198 ALA n 
1 199 ASN n 
1 200 LEU n 
1 201 PHE n 
1 202 VAL n 
1 203 ASP n 
1 204 GLY n 
1 205 ARG n 
1 206 ARG n 
1 207 ASP n 
1 208 ASP n 
1 209 GLY n 
1 210 GLN n 
1 211 LEU n 
1 212 ASP n 
1 213 MET n 
1 214 ASP n 
1 215 ALA n 
1 216 ALA n 
1 217 ARG n 
1 218 SER n 
1 219 PHE n 
1 220 PHE n 
1 221 GLN n 
1 222 PHE n 
1 223 SER n 
1 224 ARG n 
1 225 MET n 
1 226 PRO n 
1 227 ASP n 
1 228 ASP n 
1 229 PHE n 
1 230 PHE n 
1 231 ARG n 
1 232 ALA n 
1 233 PRO n 
1 234 SER n 
1 235 PRO n 
1 236 ARG n 
1 237 SER n 
1 238 GLY n 
1 239 THR n 
1 240 GLY n 
1 241 VAL n 
1 242 GLU n 
1 243 VAL n 
1 244 VAL n 
1 245 ILE n 
1 246 GLN n 
1 247 ALA n 
1 248 HIS n 
1 249 PRO n 
1 250 MET n 
1 251 GLN n 
1 252 PRO n 
1 253 GLY n 
1 254 ARG n 
1 255 ASN n 
1 256 VAL n 
1 257 GLY n 
1 258 LYS n 
1 259 ILE n 
1 260 ASN n 
1 261 SER n 
1 262 TYR n 
1 263 THR n 
1 264 VAL n 
1 265 ASP n 
1 266 PRO n 
1 267 THR n 
1 268 SER n 
1 269 SER n 
1 270 ASP n 
1 271 PHE n 
1 272 SER n 
1 273 THR n 
1 274 PRO n 
1 275 CYS n 
1 276 LEU n 
1 277 MET n 
1 278 TYR n 
1 279 GLU n 
1 280 LYS n 
1 281 PHE n 
1 282 VAL n 
1 283 ASN n 
1 284 ILE n 
1 285 THR n 
1 286 VAL n 
1 287 LYS n 
1 288 SER n 
1 289 LEU n 
1 290 TYR n 
1 291 PRO n 
1 292 ASN n 
1 293 PRO n 
1 294 THR n 
1 295 VAL n 
1 296 GLN n 
1 297 LEU n 
1 298 ARG n 
1 299 LYS n 
1 300 ALA n 
1 301 LEU n 
1 302 ASN n 
1 303 THR n 
1 304 ASN n 
1 305 LEU n 
1 306 ASP n 
1 307 PHE n 
1 308 PHE n 
1 309 PHE n 
1 310 GLN n 
1 311 GLY n 
1 312 VAL n 
1 313 ALA n 
1 314 ALA n 
1 315 GLY n 
1 316 CYS n 
1 317 THR n 
1 318 GLN n 
1 319 VAL n 
1 320 PHE n 
1 321 PRO n 
1 322 TYR n 
1 323 GLY n 
1 324 ARG n 
1 325 ASP 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   'AGROCYBE AEGERITA' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      5400 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     TM-A1 
_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                    'GERMAN COLLECTION OF MICROORGANISMS (DSM), ACCESS NUMBER DSMZ 22459' 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    APO1_AGRAE 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_db_accession          B9W4V6 
_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 2YP1 A 1 ? 325 ? B9W4V6 47 ? 371 ? 4 328 
2 1 2YP1 B 1 ? 325 ? B9W4V6 47 ? 371 ? 4 328 
3 1 2YP1 C 1 ? 325 ? B9W4V6 47 ? 371 ? 4 328 
4 1 2YP1 D 1 ? 325 ? B9W4V6 47 ? 371 ? 4 328 
# 
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 
ACT non-polymer         . 'ACETATE ION'                     ?    'C2 H3 O2 -1'      59.044  
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 
BMA D-saccharide        . BETA-D-MANNOSE                    ?    'C6 H12 O6'        180.156 
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  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 
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 
MAN D-saccharide        . ALPHA-D-MANNOSE                   ?    'C6 H12 O6'        180.156 
MET 'L-peptide linking' y METHIONINE                        ?    'C5 H11 N O2 S'    149.211 
MG  non-polymer         . 'MAGNESIUM ION'                   ?    'Mg 2'             24.305  
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE            ?    'C8 H15 N O6'      221.208 
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 
SO4 non-polymer         . 'SULFATE ION'                     ?    'O4 S -2'          96.063  
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          2YP1 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.29 
_exptl_crystal.density_percent_sol   46 
_exptl_crystal.description           NONE 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              4.6 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '2.0M AMMONIUM SULFATE, 200MM SODIUM ACETATE, PH 4.6' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC CCD' 
_diffrn_detector.pdbx_collection_date   2007-12-15 
_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   0.976 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.pdbx_synchrotron_site       ESRF 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_wavelength             0.976 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     2YP1 
_reflns.observed_criterion_sigma_I   -3.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             48.90 
_reflns.d_resolution_high            2.31 
_reflns.number_obs                   97006 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.4 
_reflns.pdbx_Rmerge_I_obs            0.06 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        15.40 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              4.8 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             2.31 
_reflns_shell.d_res_low              2.37 
_reflns_shell.percent_possible_all   95.7 
_reflns_shell.Rmerge_I_obs           0.22 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    5.50 
_reflns_shell.pdbx_redundancy        4.8 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 2YP1 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     92154 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          . 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             48.91 
_refine.ls_d_res_high                            2.31 
_refine.ls_percent_reflns_obs                    100.00 
_refine.ls_R_factor_obs                          0.18006 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.17740 
_refine.ls_R_factor_R_free                       0.23039 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  4851 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.946 
_refine.correlation_coeff_Fo_to_Fc_free          0.914 
_refine.B_iso_mean                               29.918 
_refine.aniso_B[1][1]                            -0.93 
_refine.aniso_B[2][2]                            2.22 
_refine.aniso_B[3][3]                            -1.29 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.223 
_refine.pdbx_overall_ESU_R_Free                  0.197 
_refine.overall_SU_ML                            0.087 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             3.465 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_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        10035 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         1029 
_refine_hist.number_atoms_solvent             1185 
_refine_hist.number_atoms_total               12249 
_refine_hist.d_res_high                       2.31 
_refine_hist.d_res_low                        48.91 
# 
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 
r_bond_refined_d             0.010  0.022  ? 11482 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.206  2.084  ? 15754 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.721  5.000  ? 1305  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       35.138 23.878 ? 526   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       16.553 15.000 ? 1511  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       19.436 15.000 ? 75    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.091  0.200  ? 1774  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.015  0.021  ? 8823  'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcbond_it                  2.056  2.000  ? 6500  'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcangle_it                 2.983  3.000  ? 10482 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.366  2.000  ? 4982  'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_it                 3.434  3.000  ? 5265  'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.306 
_refine_ls_shell.d_res_low                        2.366 
_refine_ls_shell.number_reflns_R_work             6460 
_refine_ls_shell.R_factor_R_work                  0.224 
_refine_ls_shell.percent_reflns_obs               100.00 
_refine_ls_shell.R_factor_R_free                  0.333 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             340 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
loop_
_struct_ncs_oper.id 
_struct_ncs_oper.code 
_struct_ncs_oper.details 
_struct_ncs_oper.matrix[1][1] 
_struct_ncs_oper.matrix[1][2] 
_struct_ncs_oper.matrix[1][3] 
_struct_ncs_oper.matrix[2][1] 
_struct_ncs_oper.matrix[2][2] 
_struct_ncs_oper.matrix[2][3] 
_struct_ncs_oper.matrix[3][1] 
_struct_ncs_oper.matrix[3][2] 
_struct_ncs_oper.matrix[3][3] 
_struct_ncs_oper.vector[1] 
_struct_ncs_oper.vector[2] 
_struct_ncs_oper.vector[3] 
1 given ? -0.962320 -0.271870 -0.005540 -0.271910 0.961800 0.031660  -0.003280 0.031970  -0.999480 51.18112 6.46248  48.83316  
2 given ? 0.981920  -0.187960 0.022270  0.188570  0.981600 -0.029900 -0.016240 0.033550  0.999310  51.49788 2.90069  -18.88594 
3 given ? -0.995740 -0.089190 -0.023500 -0.089090 0.996010 -0.004890 0.023850  -0.002770 -0.999710 1.11668  -5.56625 67.75539  
# 
_struct.entry_id                  2YP1 
_struct.title                     
;Crystallization of a 45 kDa peroxygenase- peroxidase from the mushroom Agrocybe aegerita and structure determination by SAD utilizing only the haem iron
;
_struct.pdbx_descriptor           'AROMATIC PEROXYGENASE (E.C.1.11.2.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2YP1 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'OXIDOREDUCTASE, PEROXIDASE/PEROXYGENASE, UNSPECIFIC/AROMATIC PEROXYGENASE, HEME, GLYCOPROTEIN' 
# 
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 1 ? 
E  N N 2 ? 
F  N N 3 ? 
G  N N 4 ? 
H  N N 4 ? 
I  N N 5 ? 
J  N N 6 ? 
K  N N 6 ? 
L  N N 6 ? 
M  N N 4 ? 
N  N N 4 ? 
O  N N 5 ? 
P  N N 6 ? 
Q  N N 6 ? 
R  N N 4 ? 
S  N N 4 ? 
T  N N 4 ? 
U  N N 4 ? 
V  N N 5 ? 
W  N N 6 ? 
X  N N 6 ? 
Y  N N 6 ? 
Z  N N 6 ? 
AA N N 6 ? 
BA N N 4 ? 
CA N N 4 ? 
DA N N 7 ? 
EA N N 8 ? 
FA N N 8 ? 
GA N N 8 ? 
HA N N 8 ? 
IA N N 2 ? 
JA N N 3 ? 
KA N N 4 ? 
LA N N 4 ? 
MA N N 5 ? 
NA N N 6 ? 
OA N N 6 ? 
PA N N 4 ? 
QA N N 4 ? 
RA N N 4 ? 
SA N N 4 ? 
TA N N 4 ? 
UA N N 4 ? 
VA N N 5 ? 
WA N N 6 ? 
XA N N 6 ? 
YA N N 6 ? 
ZA N N 6 ? 
AB N N 6 ? 
BB N N 4 ? 
CB N N 4 ? 
DB N N 7 ? 
EB N N 8 ? 
FB N N 8 ? 
GB N N 8 ? 
HB N N 2 ? 
IB N N 3 ? 
JB N N 4 ? 
KB N N 4 ? 
LB N N 5 ? 
MB N N 4 ? 
NB N N 4 ? 
OB N N 4 ? 
PB N N 4 ? 
QB N N 4 ? 
RB N N 4 ? 
SB N N 4 ? 
TB N N 7 ? 
UB N N 8 ? 
VB N N 8 ? 
WB N N 8 ? 
XB N N 8 ? 
YB N N 7 ? 
ZB N N 2 ? 
AC N N 3 ? 
BC N N 4 ? 
CC N N 4 ? 
DC N N 4 ? 
EC N N 4 ? 
FC N N 5 ? 
GC N N 4 ? 
HC N N 4 ? 
IC N N 4 ? 
JC N N 7 ? 
KC N N 8 ? 
LC N N 8 ? 
MC N N 9 ? 
NC N N 9 ? 
OC N N 9 ? 
PC N N 9 ? 
# 
_struct_biol.id   1 
# 
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  CYS A 33  ? SER A 41  ? CYS A 36  SER A 44  1 ? 9  
HELX_P HELX_P2  2  THR A 52  ? ASN A 65  ? THR A 55  ASN A 68  1 ? 14 
HELX_P HELX_P3  3  ASP A 67  ? GLY A 83  ? ASP A 70  GLY A 86  1 ? 17 
HELX_P HELX_P4  4  THR A 96  ? GLY A 100 ? THR A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  5  ASP A 128 ? GLY A 132 ? ASP A 131 GLY A 135 5 ? 5  
HELX_P HELX_P6  6  ASN A 138 ? GLY A 153 ? ASN A 141 GLY A 156 1 ? 16 
HELX_P HELX_P7  7  ASN A 158 ? ASN A 177 ? ASN A 161 ASN A 180 1 ? 20 
HELX_P HELX_P8  8  VAL A 183 ? GLU A 193 ? VAL A 186 GLU A 196 1 ? 11 
HELX_P HELX_P9  9  THR A 195 ? PHE A 201 ? THR A 198 PHE A 204 1 ? 7  
HELX_P HELX_P10 10 ASP A 212 ? SER A 223 ? ASP A 215 SER A 226 1 ? 12 
HELX_P HELX_P11 11 GLY A 240 ? HIS A 248 ? GLY A 243 HIS A 251 1 ? 9  
HELX_P HELX_P12 12 THR A 273 ? ILE A 284 ? THR A 276 ILE A 287 1 ? 12 
HELX_P HELX_P13 13 ILE A 284 ? TYR A 290 ? ILE A 287 TYR A 293 1 ? 7  
HELX_P HELX_P14 14 THR A 294 ? GLY A 311 ? THR A 297 GLY A 314 1 ? 18 
HELX_P HELX_P15 15 CYS B 33  ? HIS B 42  ? CYS B 36  HIS B 45  1 ? 10 
HELX_P HELX_P16 16 THR B 52  ? ASN B 65  ? THR B 55  ASN B 68  1 ? 14 
HELX_P HELX_P17 17 ASP B 67  ? GLY B 83  ? ASP B 70  GLY B 86  1 ? 17 
HELX_P HELX_P18 18 THR B 96  ? GLY B 100 ? THR B 99  GLY B 103 5 ? 5  
HELX_P HELX_P19 19 ASP B 128 ? GLY B 132 ? ASP B 131 GLY B 135 5 ? 5  
HELX_P HELX_P20 20 ASN B 138 ? GLY B 153 ? ASN B 141 GLY B 156 1 ? 16 
HELX_P HELX_P21 21 ASN B 158 ? ASN B 177 ? ASN B 161 ASN B 180 1 ? 20 
HELX_P HELX_P22 22 VAL B 183 ? PHE B 201 ? VAL B 186 PHE B 204 1 ? 19 
HELX_P HELX_P23 23 ASP B 212 ? SER B 223 ? ASP B 215 SER B 226 1 ? 12 
HELX_P HELX_P24 24 GLY B 240 ? HIS B 248 ? GLY B 243 HIS B 251 1 ? 9  
HELX_P HELX_P25 25 THR B 273 ? ILE B 284 ? THR B 276 ILE B 287 1 ? 12 
HELX_P HELX_P26 26 ILE B 284 ? TYR B 290 ? ILE B 287 TYR B 293 1 ? 7  
HELX_P HELX_P27 27 THR B 294 ? GLY B 311 ? THR B 297 GLY B 314 1 ? 18 
HELX_P HELX_P28 28 CYS C 33  ? HIS C 42  ? CYS C 36  HIS C 45  1 ? 10 
HELX_P HELX_P29 29 THR C 52  ? ASN C 65  ? THR C 55  ASN C 68  1 ? 14 
HELX_P HELX_P30 30 ASP C 67  ? GLY C 83  ? ASP C 70  GLY C 86  1 ? 17 
HELX_P HELX_P31 31 THR C 96  ? GLY C 100 ? THR C 99  GLY C 103 5 ? 5  
HELX_P HELX_P32 32 ASP C 128 ? GLY C 132 ? ASP C 131 GLY C 135 5 ? 5  
HELX_P HELX_P33 33 ASN C 138 ? GLY C 153 ? ASN C 141 GLY C 156 1 ? 16 
HELX_P HELX_P34 34 ASN C 158 ? ASN C 177 ? ASN C 161 ASN C 180 1 ? 20 
HELX_P HELX_P35 35 VAL C 183 ? THR C 194 ? VAL C 186 THR C 197 1 ? 12 
HELX_P HELX_P36 36 THR C 195 ? PHE C 201 ? THR C 198 PHE C 204 1 ? 7  
HELX_P HELX_P37 37 ASP C 212 ? SER C 223 ? ASP C 215 SER C 226 1 ? 12 
HELX_P HELX_P38 38 GLY C 240 ? HIS C 248 ? GLY C 243 HIS C 251 1 ? 9  
HELX_P HELX_P39 39 THR C 273 ? ILE C 284 ? THR C 276 ILE C 287 1 ? 12 
HELX_P HELX_P40 40 ILE C 284 ? TYR C 290 ? ILE C 287 TYR C 293 1 ? 7  
HELX_P HELX_P41 41 THR C 294 ? GLY C 311 ? THR C 297 GLY C 314 1 ? 18 
HELX_P HELX_P42 42 CYS D 33  ? HIS D 42  ? CYS D 36  HIS D 45  1 ? 10 
HELX_P HELX_P43 43 THR D 52  ? ASN D 65  ? THR D 55  ASN D 68  1 ? 14 
HELX_P HELX_P44 44 ASP D 67  ? GLY D 83  ? ASP D 70  GLY D 86  1 ? 17 
HELX_P HELX_P45 45 THR D 96  ? GLY D 100 ? THR D 99  GLY D 103 5 ? 5  
HELX_P HELX_P46 46 ASP D 128 ? GLY D 132 ? ASP D 131 GLY D 135 5 ? 5  
HELX_P HELX_P47 47 ASN D 138 ? GLY D 153 ? ASN D 141 GLY D 156 1 ? 16 
HELX_P HELX_P48 48 ASN D 158 ? ASN D 177 ? ASN D 161 ASN D 180 1 ? 20 
HELX_P HELX_P49 49 VAL D 183 ? GLU D 193 ? VAL D 186 GLU D 196 1 ? 11 
HELX_P HELX_P50 50 THR D 195 ? PHE D 201 ? THR D 198 PHE D 204 1 ? 7  
HELX_P HELX_P51 51 ASP D 212 ? GLN D 221 ? ASP D 215 GLN D 224 1 ? 10 
HELX_P HELX_P52 52 GLY D 240 ? HIS D 248 ? GLY D 243 HIS D 251 1 ? 9  
HELX_P HELX_P53 53 THR D 273 ? ILE D 284 ? THR D 276 ILE D 287 1 ? 12 
HELX_P HELX_P54 54 ILE D 284 ? TYR D 290 ? ILE D 287 TYR D 293 1 ? 7  
HELX_P HELX_P55 55 THR D 294 ? GLY D 311 ? THR D 297 GLY D 314 1 ? 18 
# 
_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 275 SG  ? ? ? 1_555 A  CYS 316 SG  ? ? A CYS 278 A CYS 319  1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf2  disulf ? ? B  CYS 275 SG  ? ? ? 1_555 B  CYS 316 SG  ? ? B CYS 278 B CYS 319  1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf3  disulf ? ? C  CYS 275 SG  ? ? ? 1_555 C  CYS 316 SG  ? ? C CYS 278 C CYS 319  1_555 ? ? ? ? ? ? ? 2.058 ? 
disulf4  disulf ? ? D  CYS 275 SG  ? ? ? 1_555 D  CYS 316 SG  ? ? D CYS 278 D CYS 319  1_555 ? ? ? ? ? ? ? 2.042 ? 
covale1  covale ? ? A  ASN 8   ND2 ? ? ? 1_555 BA NAG .   C1  ? ? A ASN 11  A NAG 411  1_555 ? ? ? ? ? ? ? 1.438 ? 
covale2  covale ? ? A  ASN 138 ND2 ? ? ? 1_555 G  NAG .   C1  ? ? A ASN 141 A NAG 361  1_555 ? ? ? ? ? ? ? 1.449 ? 
covale3  covale ? ? A  ASN 158 ND2 ? ? ? 1_555 M  NAG .   C1  ? ? A ASN 161 A NAG 371  1_555 ? ? ? ? ? ? ? 1.442 ? 
covale4  covale ? ? A  ASN 179 ND2 ? ? ? 1_555 R  NAG .   C1  ? ? A ASN 182 A NAG 381  1_555 ? ? ? ? ? ? ? 1.435 ? 
covale5  covale ? ? A  ASN 283 ND2 ? ? ? 1_555 T  NAG .   C1  ? ? A ASN 286 A NAG 391  1_555 ? ? ? ? ? ? ? 1.440 ? 
metalc1  metalc ? ? E  HEM .   O1A ? ? ? 1_555 F  MG  .   MG  ? ? A HEM 350 A MG  353  1_555 ? ? ? ? ? ? ? 1.975 ? 
metalc2  metalc ? ? E  HEM .   FE  ? ? ? 1_555 A  CYS 33  SG  ? ? A HEM 350 A CYS 36   1_555 ? ? ? ? ? ? ? 2.317 ? 
metalc3  metalc ? ? F  MG  .   MG  ? ? ? 1_555 A  GLY 120 O   ? ? A MG  353 A GLY 123  1_555 ? ? ? ? ? ? ? 2.175 ? 
metalc4  metalc ? ? F  MG  .   MG  ? ? ? 1_555 A  SER 123 OG  ? ? A MG  353 A SER 126  1_555 ? ? ? ? ? ? ? 2.077 ? 
metalc5  metalc ? ? F  MG  .   MG  ? ? ? 1_555 MC HOH .   O   ? ? A MG  353 A HOH 2123 1_555 ? ? ? ? ? ? ? 1.969 ? 
metalc6  metalc ? ? F  MG  .   MG  ? ? ? 1_555 MC HOH .   O   ? ? A MG  353 A HOH 2124 1_555 ? ? ? ? ? ? ? 2.002 ? 
metalc7  metalc ? ? F  MG  .   MG  ? ? ? 1_555 A  GLU 119 OE2 ? ? A MG  353 A GLU 122  1_555 ? ? ? ? ? ? ? 1.963 ? 
covale6  covale ? ? G  NAG .   O4  ? ? ? 1_555 H  NAG .   C1  ? ? A NAG 361 A NAG 362  1_555 ? ? ? ? ? ? ? 1.443 ? 
covale7  covale ? ? I  BMA .   C1  ? ? ? 1_555 H  NAG .   O4  ? ? A BMA 363 A NAG 362  1_555 ? ? ? ? ? ? ? 1.441 ? 
covale8  covale ? ? J  MAN .   C1  ? ? ? 1_555 I  BMA .   O3  ? ? A MAN 364 A BMA 363  1_555 ? ? ? ? ? ? ? 1.443 ? 
covale9  covale ? ? J  MAN .   O2  ? ? ? 1_555 K  MAN .   C1  ? ? A MAN 364 A MAN 365  1_555 ? ? ? ? ? ? ? 1.439 ? 
covale10 covale ? ? L  MAN .   C1  ? ? ? 1_555 I  BMA .   O6  ? ? A MAN 366 A BMA 363  1_555 ? ? ? ? ? ? ? 1.448 ? 
covale11 covale ? ? M  NAG .   O4  ? ? ? 1_555 N  NAG .   C1  ? ? A NAG 371 A NAG 372  1_555 ? ? ? ? ? ? ? 1.431 ? 
covale12 covale ? ? O  BMA .   C1  ? ? ? 1_555 N  NAG .   O4  ? ? A BMA 373 A NAG 372  1_555 ? ? ? ? ? ? ? 1.453 ? 
covale13 covale ? ? P  MAN .   O6  ? ? ? 1_555 Q  MAN .   C1  ? ? A MAN 374 A MAN 375  1_555 ? ? ? ? ? ? ? 1.447 ? 
covale14 covale ? ? P  MAN .   C1  ? ? ? 1_555 O  BMA .   O6  ? ? A MAN 374 A BMA 373  1_555 ? ? ? ? ? ? ? 1.447 ? 
covale15 covale ? ? R  NAG .   O4  ? ? ? 1_555 S  NAG .   C1  ? ? A NAG 381 A NAG 382  1_555 ? ? ? ? ? ? ? 1.443 ? 
covale16 covale ? ? T  NAG .   O4  ? ? ? 1_555 U  NAG .   C1  ? ? A NAG 391 A NAG 392  1_555 ? ? ? ? ? ? ? 1.425 ? 
covale17 covale ? ? V  BMA .   C1  ? ? ? 1_555 U  NAG .   O4  ? ? A BMA 393 A NAG 392  1_555 ? ? ? ? ? ? ? 1.444 ? 
covale18 covale ? ? W  MAN .   C1  ? ? ? 1_555 V  BMA .   O6  ? ? A MAN 394 A BMA 393  1_555 ? ? ? ? ? ? ? 1.432 ? 
covale19 covale ? ? W  MAN .   O3  ? ? ? 1_555 Y  MAN .   C1  ? ? A MAN 394 A MAN 396  1_555 ? ? ? ? ? ? ? 1.443 ? 
covale20 covale ? ? W  MAN .   O6  ? ? ? 1_555 X  MAN .   C1  ? ? A MAN 394 A MAN 395  1_555 ? ? ? ? ? ? ? 1.443 ? 
covale21 covale ? ? Z  MAN .   O2  ? ? ? 1_555 AA MAN .   C1  ? ? A MAN 397 A MAN 398  1_555 ? ? ? ? ? ? ? 1.446 ? 
covale22 covale ? ? Z  MAN .   C1  ? ? ? 1_555 V  BMA .   O3  ? ? A MAN 397 A BMA 393  1_555 ? ? ? ? ? ? ? 1.442 ? 
covale23 covale ? ? BA NAG .   O4  ? ? ? 1_555 CA NAG .   C1  ? ? A NAG 411 A NAG 412  1_555 ? ? ? ? ? ? ? 1.436 ? 
covale24 covale ? ? B  ASN 8   ND2 ? ? ? 1_555 BB NAG .   C1  ? ? B ASN 11  B NAG 411  1_555 ? ? ? ? ? ? ? 1.434 ? 
covale25 covale ? ? B  ASN 138 ND2 ? ? ? 1_555 KA NAG .   C1  ? ? B ASN 141 B NAG 361  1_555 ? ? ? ? ? ? ? 1.448 ? 
covale26 covale ? ? B  ASN 158 ND2 ? ? ? 1_555 PA NAG .   C1  ? ? B ASN 161 B NAG 371  1_555 ? ? ? ? ? ? ? 1.442 ? 
covale27 covale ? ? B  ASN 179 ND2 ? ? ? 1_555 RA NAG .   C1  ? ? B ASN 182 B NAG 381  1_555 ? ? ? ? ? ? ? 1.434 ? 
covale28 covale ? ? B  ASN 283 ND2 ? ? ? 1_555 TA NAG .   C1  ? ? B ASN 286 B NAG 391  1_555 ? ? ? ? ? ? ? 1.445 ? 
metalc8  metalc ? ? IA HEM .   FE  ? ? ? 1_555 B  CYS 33  SG  ? ? B HEM 350 B CYS 36   1_555 ? ? ? ? ? ? ? 2.284 ? 
metalc9  metalc ? ? IA HEM .   FE  ? ? ? 1_555 DB ACT .   O   ? ? B HEM 350 B ACT 1328 1_555 ? ? ? ? ? ? ? 2.786 ? 
metalc10 metalc ? ? IA HEM .   O1A ? ? ? 1_555 JA MG  .   MG  ? ? B HEM 350 B MG  353  1_555 ? ? ? ? ? ? ? 1.972 ? 
metalc11 metalc ? ? JA MG  .   MG  ? ? ? 1_555 NC HOH .   O   ? ? B MG  353 B HOH 2157 1_555 ? ? ? ? ? ? ? 2.040 ? 
metalc12 metalc ? ? JA MG  .   MG  ? ? ? 1_555 B  GLU 119 OE2 ? ? B MG  353 B GLU 122  1_555 ? ? ? ? ? ? ? 1.967 ? 
metalc13 metalc ? ? JA MG  .   MG  ? ? ? 1_555 B  GLY 120 O   ? ? B MG  353 B GLY 123  1_555 ? ? ? ? ? ? ? 2.178 ? 
metalc14 metalc ? ? JA MG  .   MG  ? ? ? 1_555 B  SER 123 OG  ? ? B MG  353 B SER 126  1_555 ? ? ? ? ? ? ? 2.088 ? 
metalc15 metalc ? ? JA MG  .   MG  ? ? ? 1_555 NC HOH .   O   ? ? B MG  353 B HOH 2158 1_555 ? ? ? ? ? ? ? 2.051 ? 
covale29 covale ? ? KA NAG .   O4  ? ? ? 1_555 LA NAG .   C1  ? ? B NAG 361 B NAG 362  1_555 ? ? ? ? ? ? ? 1.453 ? 
covale30 covale ? ? MA BMA .   C1  ? ? ? 1_555 LA NAG .   O4  ? ? B BMA 363 B NAG 362  1_555 ? ? ? ? ? ? ? 1.452 ? 
covale31 covale ? ? NA MAN .   O2  ? ? ? 1_555 OA MAN .   C1  ? ? B MAN 364 B MAN 365  1_555 ? ? ? ? ? ? ? 1.449 ? 
covale32 covale ? ? NA MAN .   C1  ? ? ? 1_555 MA BMA .   O3  ? ? B MAN 364 B BMA 363  1_555 ? ? ? ? ? ? ? 1.448 ? 
covale33 covale ? ? PA NAG .   O4  ? ? ? 1_555 QA NAG .   C1  ? ? B NAG 371 B NAG 372  1_555 ? ? ? ? ? ? ? 1.433 ? 
covale34 covale ? ? RA NAG .   O4  ? ? ? 1_555 SA NAG .   C1  ? ? B NAG 381 B NAG 382  1_555 ? ? ? ? ? ? ? 1.433 ? 
covale35 covale ? ? TA NAG .   O4  ? ? ? 1_555 UA NAG .   C1  ? ? B NAG 391 B NAG 392  1_555 ? ? ? ? ? ? ? 1.436 ? 
covale36 covale ? ? VA BMA .   C1  ? ? ? 1_555 UA NAG .   O4  ? ? B BMA 393 B NAG 392  1_555 ? ? ? ? ? ? ? 1.442 ? 
covale37 covale ? ? WA MAN .   O2  ? ? ? 1_555 XA MAN .   C1  ? ? B MAN 394 B MAN 395  1_555 ? ? ? ? ? ? ? 1.447 ? 
covale38 covale ? ? WA MAN .   C1  ? ? ? 1_555 VA BMA .   O3  ? ? B MAN 394 B BMA 393  1_555 ? ? ? ? ? ? ? 1.435 ? 
covale39 covale ? ? YA MAN .   C1  ? ? ? 1_555 VA BMA .   O6  ? ? B MAN 396 B BMA 393  1_555 ? ? ? ? ? ? ? 1.436 ? 
covale40 covale ? ? YA MAN .   O6  ? ? ? 1_555 AB MAN .   C1  ? ? B MAN 396 B MAN 398  1_555 ? ? ? ? ? ? ? 1.454 ? 
covale41 covale ? ? YA MAN .   O3  ? ? ? 1_555 ZA MAN .   C1  ? ? B MAN 396 B MAN 397  1_555 ? ? ? ? ? ? ? 1.431 ? 
covale42 covale ? ? BB NAG .   O4  ? ? ? 1_555 CB NAG .   C1  ? ? B NAG 411 B NAG 412  1_555 ? ? ? ? ? ? ? 1.442 ? 
covale43 covale ? ? C  ASN 8   ND2 ? ? ? 1_555 RB NAG .   C1  ? ? C ASN 11  C NAG 411  1_555 ? ? ? ? ? ? ? 1.443 ? 
covale44 covale ? ? C  ASN 138 ND2 ? ? ? 1_555 JB NAG .   C1  ? ? C ASN 141 C NAG 361  1_555 ? ? ? ? ? ? ? 1.434 ? 
covale45 covale ? ? C  ASN 158 ND2 ? ? ? 1_555 MB NAG .   C1  ? ? C ASN 161 C NAG 371  1_555 ? ? ? ? ? ? ? 1.438 ? 
covale46 covale ? ? C  ASN 179 ND2 ? ? ? 1_555 OB NAG .   C1  ? ? C ASN 182 C NAG 381  1_555 ? ? ? ? ? ? ? 1.444 ? 
covale47 covale ? ? C  ASN 283 ND2 ? ? ? 1_555 PB NAG .   C1  ? ? C ASN 286 C NAG 391  1_555 ? ? ? ? ? ? ? 1.450 ? 
metalc16 metalc ? ? HB HEM .   O1A ? ? ? 1_555 IB MG  .   MG  ? ? C HEM 350 C MG  353  1_555 ? ? ? ? ? ? ? 1.957 ? 
metalc17 metalc ? ? HB HEM .   FE  ? ? ? 1_555 C  CYS 33  SG  ? ? C HEM 350 C CYS 36   1_555 ? ? ? ? ? ? ? 2.315 ? 
metalc18 metalc ? ? IB MG  .   MG  ? ? ? 1_555 OC HOH .   O   ? ? C MG  353 C HOH 2132 1_555 ? ? ? ? ? ? ? 2.010 ? 
metalc19 metalc ? ? IB MG  .   MG  ? ? ? 1_555 C  SER 123 OG  ? ? C MG  353 C SER 126  1_555 ? ? ? ? ? ? ? 2.072 ? 
metalc20 metalc ? ? IB MG  .   MG  ? ? ? 1_555 OC HOH .   O   ? ? C MG  353 C HOH 2131 1_555 ? ? ? ? ? ? ? 2.155 ? 
metalc21 metalc ? ? IB MG  .   MG  ? ? ? 1_555 C  GLY 120 O   ? ? C MG  353 C GLY 123  1_555 ? ? ? ? ? ? ? 2.174 ? 
metalc22 metalc ? ? IB MG  .   MG  ? ? ? 1_555 C  GLU 119 OE2 ? ? C MG  353 C GLU 122  1_555 ? ? ? ? ? ? ? 1.969 ? 
covale48 covale ? ? JB NAG .   O4  ? ? ? 1_555 KB NAG .   C1  ? ? C NAG 361 C NAG 362  1_555 ? ? ? ? ? ? ? 1.445 ? 
covale49 covale ? ? LB BMA .   C1  ? ? ? 1_555 KB NAG .   O4  ? ? C BMA 363 C NAG 362  1_555 ? ? ? ? ? ? ? 1.447 ? 
covale50 covale ? ? MB NAG .   O4  ? ? ? 1_555 NB NAG .   C1  ? ? C NAG 371 C NAG 372  1_555 ? ? ? ? ? ? ? 1.417 ? 
covale51 covale ? ? PB NAG .   O4  ? ? ? 1_555 QB NAG .   C1  ? ? C NAG 391 C NAG 392  1_555 ? ? ? ? ? ? ? 1.444 ? 
covale52 covale ? ? RB NAG .   O4  ? ? ? 1_555 SB NAG .   C1  ? ? C NAG 411 C NAG 412  1_555 ? ? ? ? ? ? ? 1.438 ? 
covale53 covale ? ? D  ASN 8   ND2 ? ? ? 1_555 IC NAG .   C1  ? ? D ASN 11  D NAG 411  1_555 ? ? ? ? ? ? ? 1.446 ? 
covale54 covale ? ? D  ASN 138 ND2 ? ? ? 1_555 BC NAG .   C1  ? ? D ASN 141 D NAG 361  1_555 ? ? ? ? ? ? ? 1.440 ? 
covale55 covale ? ? D  ASN 158 ND2 ? ? ? 1_555 DC NAG .   C1  ? ? D ASN 161 D NAG 371  1_555 ? ? ? ? ? ? ? 1.440 ? 
covale56 covale ? ? D  ASN 179 ND2 ? ? ? 1_555 GC NAG .   C1  ? ? D ASN 182 D NAG 381  1_555 ? ? ? ? ? ? ? 1.442 ? 
covale57 covale ? ? D  ASN 283 ND2 ? ? ? 1_555 HC NAG .   C1  ? ? D ASN 286 D NAG 391  1_555 ? ? ? ? ? ? ? 1.442 ? 
metalc23 metalc ? ? ZB HEM .   O1A ? ? ? 1_555 AC MG  .   MG  ? ? D HEM 350 D MG  353  1_555 ? ? ? ? ? ? ? 1.966 ? 
metalc24 metalc ? ? ZB HEM .   FE  ? ? ? 1_555 D  CYS 33  SG  ? ? D HEM 350 D CYS 36   1_555 ? ? ? ? ? ? ? 2.319 ? 
metalc25 metalc ? ? AC MG  .   MG  ? ? ? 1_555 D  GLU 119 OE2 ? ? D MG  353 D GLU 122  1_555 ? ? ? ? ? ? ? 1.980 ? 
metalc26 metalc ? ? AC MG  .   MG  ? ? ? 1_555 PC HOH .   O   ? ? D MG  353 D HOH 2084 1_555 ? ? ? ? ? ? ? 1.745 ? 
metalc27 metalc ? ? AC MG  .   MG  ? ? ? 1_555 PC HOH .   O   ? ? D MG  353 D HOH 2083 1_555 ? ? ? ? ? ? ? 1.968 ? 
metalc28 metalc ? ? AC MG  .   MG  ? ? ? 1_555 D  SER 123 OG  ? ? D MG  353 D SER 126  1_555 ? ? ? ? ? ? ? 2.086 ? 
metalc29 metalc ? ? AC MG  .   MG  ? ? ? 1_555 D  GLY 120 O   ? ? D MG  353 D GLY 123  1_555 ? ? ? ? ? ? ? 2.162 ? 
covale58 covale ? ? BC NAG .   O4  ? ? ? 1_555 CC NAG .   C1  ? ? D NAG 361 D NAG 362  1_555 ? ? ? ? ? ? ? 1.447 ? 
covale59 covale ? ? DC NAG .   O4  ? ? ? 1_555 EC NAG .   C1  ? ? D NAG 371 D NAG 372  1_555 ? ? ? ? ? ? ? 1.440 ? 
covale60 covale ? ? FC BMA .   C1  ? ? ? 1_555 EC NAG .   O4  ? ? D BMA 373 D NAG 372  1_555 ? ? ? ? ? ? ? 1.448 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
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 PRO 105 A . ? PRO 108 A PRO 106 A ? PRO 109 A 1 11.21 
2 PRO 105 B . ? PRO 108 B PRO 106 B ? PRO 109 B 1 16.57 
3 PRO 105 C . ? PRO 108 C PRO 106 C ? PRO 109 C 1 6.67  
4 PRO 105 D . ? PRO 108 D PRO 106 D ? PRO 109 D 1 12.31 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 2 ? 
AB ? 3 ? 
BA ? 2 ? 
BB ? 3 ? 
CA ? 2 ? 
CB ? 3 ? 
DA ? 2 ? 
DB ? 3 ? 
# 
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 
AA 1 2 ? anti-parallel 
AB 1 2 ? anti-parallel 
AB 2 3 ? anti-parallel 
BA 1 2 ? anti-parallel 
BB 1 2 ? anti-parallel 
BB 2 3 ? anti-parallel 
CA 1 2 ? anti-parallel 
CB 1 2 ? anti-parallel 
CB 2 3 ? anti-parallel 
DA 1 2 ? anti-parallel 
DB 1 2 ? anti-parallel 
DB 2 3 ? 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 
AA 1 VAL A 50  ? ALA A 51  ? VAL A 53  ALA A 54  
AA 2 LEU A 90  ? SER A 91  ? LEU A 93  SER A 94  
AB 1 SER A 181 ? PHE A 182 ? SER A 184 PHE A 185 
AB 2 GLY A 253 ? ARG A 254 ? GLY A 256 ARG A 257 
AB 3 THR A 263 ? VAL A 264 ? THR A 266 VAL A 267 
BA 1 VAL B 50  ? ALA B 51  ? VAL B 53  ALA B 54  
BA 2 LEU B 90  ? SER B 91  ? LEU B 93  SER B 94  
BB 1 SER B 181 ? PHE B 182 ? SER B 184 PHE B 185 
BB 2 GLY B 253 ? ARG B 254 ? GLY B 256 ARG B 257 
BB 3 THR B 263 ? VAL B 264 ? THR B 266 VAL B 267 
CA 1 VAL C 50  ? ALA C 51  ? VAL C 53  ALA C 54  
CA 2 LEU C 90  ? SER C 91  ? LEU C 93  SER C 94  
CB 1 SER C 181 ? PHE C 182 ? SER C 184 PHE C 185 
CB 2 GLY C 253 ? ARG C 254 ? GLY C 256 ARG C 257 
CB 3 THR C 263 ? VAL C 264 ? THR C 266 VAL C 267 
DA 1 VAL D 50  ? ALA D 51  ? VAL D 53  ALA D 54  
DA 2 LEU D 90  ? SER D 91  ? LEU D 93  SER D 94  
DB 1 SER D 181 ? PHE D 182 ? SER D 184 PHE D 185 
DB 2 GLY D 253 ? ARG D 254 ? GLY D 256 ARG D 257 
DB 3 THR D 263 ? VAL D 264 ? THR D 266 VAL D 267 
# 
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 
AA 1 2 N ALA A 51  ? N ALA A 54  O LEU A 90  ? O LEU A 93  
AB 1 2 N PHE A 182 ? N PHE A 185 O GLY A 253 ? O GLY A 256 
AB 2 3 N ARG A 254 ? N ARG A 257 O THR A 263 ? O THR A 266 
BA 1 2 N ALA B 51  ? N ALA B 54  O LEU B 90  ? O LEU B 93  
BB 1 2 N PHE B 182 ? N PHE B 185 O GLY B 253 ? O GLY B 256 
BB 2 3 N ARG B 254 ? N ARG B 257 O THR B 263 ? O THR B 266 
CA 1 2 N ALA C 51  ? N ALA C 54  O LEU C 90  ? O LEU C 93  
CB 1 2 N PHE C 182 ? N PHE C 185 O GLY C 253 ? O GLY C 256 
CB 2 3 N ARG C 254 ? N ARG C 257 O THR C 263 ? O THR C 266 
DA 1 2 N ALA D 51  ? N ALA D 54  O LEU D 90  ? O LEU D 93  
DB 1 2 N PHE D 182 ? N PHE D 185 O GLY D 253 ? O GLY D 256 
DB 2 3 N ARG D 254 ? N ARG D 257 O THR D 263 ? O THR D 266 
# 
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 ? ? ? ? 24 'BINDING SITE FOR RESIDUE HEM A 350'                                       
AC2 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE MG A 353'                                        
AC3 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ACT A 1327'                                      
AC4 Software ? ? ? ? 21 'BINDING SITE FOR RESIDUE HEM B 350'                                       
AC5 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE MG B 353'                                        
AC6 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ACT B 1328'                                      
AC7 Software ? ? ? ? 21 'BINDING SITE FOR RESIDUE HEM C 350'                                       
AC8 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE MG C 353'                                        
AC9 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE ACT C 1329'                                      
BC1 Software ? ? ? ? 23 'BINDING SITE FOR RESIDUE HEM D 350'                                       
BC2 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE MG D 353'                                        
BC3 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ACT D 1327'                                      
BC4 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE SO4 C 1330'                                      
BC5 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE SO4 A 1328'                                      
BC6 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE SO4 B 1329'                                      
BC7 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE SO4 C 1331'                                      
BC8 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE SO4 A 1329'                                      
BC9 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE SO4 A 1330'                                      
CC1 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE SO4 B 1330'                                      
CC2 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE SO4 D 1328'                                      
CC3 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 C 1332'                                      
CC4 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE SO4 D 1329'                                      
CC5 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE SO4 C 1333'                                      
CC6 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 B 1331'                                      
CC7 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE ACT C 1334'                                      
CC8 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE SO4 A 1331'                                      
CC9 Software ? ? ? ? 7  'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 11 RESIDUES 411 TO 412'  
DC1 Software ? ? ? ? 9  'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 141 RESIDUES 361 TO 366' 
DC2 Software ? ? ? ? 13 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 161 RESIDUES 371 TO 375' 
DC3 Software ? ? ? ? 6  'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 182 RESIDUES 381 TO 382' 
DC4 Software ? ? ? ? 23 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 286 RESIDUES 391 TO 398' 
DC5 Software ? ? ? ? 3  'BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B 11 RESIDUES 411 TO 412'  
DC6 Software ? ? ? ? 11 'BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B 141 RESIDUES 361 TO 365' 
DC7 Software ? ? ? ? 16 'BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B 161 RESIDUES 371 TO 372' 
DC8 Software ? ? ? ? 6  'BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B 182 RESIDUES 381 TO 382' 
DC9 Software ? ? ? ? 24 'BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B 286 RESIDUES 391 TO 398' 
EC1 Software ? ? ? ? 3  'BINDING SITE FOR CHAIN C OF SUGAR BOUND TO ASN C 11 RESIDUES 411 TO 412'  
EC2 Software ? ? ? ? 3  'BINDING SITE FOR CHAIN C OF SUGAR BOUND TO ASN C 141 RESIDUES 361 TO 363' 
EC3 Software ? ? ? ? 13 'BINDING SITE FOR CHAIN C OF SUGAR BOUND TO ASN C 161 RESIDUES 371 TO 372' 
EC4 Software ? ? ? ? 3  'BINDING SITE FOR MONO-SACCHARIDE NAG C 381 BOUND TO ASN C 182'            
EC5 Software ? ? ? ? 8  'BINDING SITE FOR CHAIN C OF SUGAR BOUND TO ASN C 286 RESIDUES 391 TO 392' 
EC6 Software ? ? ? ? 5  'BINDING SITE FOR MONO-SACCHARIDE NAG D 411 BOUND TO ASN D 11'             
EC7 Software ? ? ? ? 2  'BINDING SITE FOR CHAIN D OF SUGAR BOUND TO ASN D 141 RESIDUES 361 TO 362' 
EC8 Software ? ? ? ? 12 'BINDING SITE FOR CHAIN D OF SUGAR BOUND TO ASN D 161 RESIDUES 371 TO 373' 
EC9 Software ? ? ? ? 1  'BINDING SITE FOR MONO-SACCHARIDE NAG D 381 BOUND TO ASN D 182'            
FC1 Software ? ? ? ? 5  'BINDING SITE FOR MONO-SACCHARIDE NAG D 391 BOUND TO ASN D 286'            
# 
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 24 PRO A  32  ? PRO A 35   . ? 1_555 ? 
2   AC1 24 CYS A  33  ? CYS A 36   . ? 1_555 ? 
3   AC1 24 PRO A  34  ? PRO A 37   . ? 1_555 ? 
4   AC1 24 LEU A  36  ? LEU A 39   . ? 1_555 ? 
5   AC1 24 VAL A  60  ? VAL A 63   . ? 1_555 ? 
6   AC1 24 PHE A  66  ? PHE A 69   . ? 1_555 ? 
7   AC1 24 ALA A  74  ? ALA A 77   . ? 1_555 ? 
8   AC1 24 THR A  75  ? THR A 78   . ? 1_555 ? 
9   AC1 24 ALA A  78  ? ALA A 81   . ? 1_555 ? 
10  AC1 24 PHE A  118 ? PHE A 121  . ? 1_555 ? 
11  AC1 24 GLU A  119 ? GLU A 122  . ? 1_555 ? 
12  AC1 24 GLY A  120 ? GLY A 123  . ? 1_555 ? 
13  AC1 24 SER A  123 ? SER A 126  . ? 1_555 ? 
14  AC1 24 MET A  124 ? MET A 127  . ? 1_555 ? 
15  AC1 24 THR A  125 ? THR A 128  . ? 1_555 ? 
16  AC1 24 ARG A  186 ? ARG A 189  . ? 1_555 ? 
17  AC1 24 GLU A  193 ? GLU A 196  . ? 1_555 ? 
18  AC1 24 PHE A  196 ? PHE A 199  . ? 1_555 ? 
19  AC1 24 PHE A  201 ? PHE A 204  . ? 1_555 ? 
20  AC1 24 MG  F  .   ? MG  A 353  . ? 1_555 ? 
21  AC1 24 ACT DA .   ? ACT A 1327 . ? 1_555 ? 
22  AC1 24 HOH MC .   ? HOH A 2041 . ? 1_555 ? 
23  AC1 24 HOH MC .   ? HOH A 2123 . ? 1_555 ? 
24  AC1 24 HOH MC .   ? HOH A 2159 . ? 1_555 ? 
25  AC2 6  GLU A  119 ? GLU A 122  . ? 1_555 ? 
26  AC2 6  GLY A  120 ? GLY A 123  . ? 1_555 ? 
27  AC2 6  SER A  123 ? SER A 126  . ? 1_555 ? 
28  AC2 6  HEM E  .   ? HEM A 350  . ? 1_555 ? 
29  AC2 6  HOH MC .   ? HOH A 2123 . ? 1_555 ? 
30  AC2 6  HOH MC .   ? HOH A 2124 . ? 1_555 ? 
31  AC3 5  ALA A  74  ? ALA A 77   . ? 1_555 ? 
32  AC3 5  GLU A  193 ? GLU A 196  . ? 1_555 ? 
33  AC3 5  PHE A  196 ? PHE A 199  . ? 1_555 ? 
34  AC3 5  HEM E  .   ? HEM A 350  . ? 1_555 ? 
35  AC3 5  HOH MC .   ? HOH A 2323 . ? 1_555 ? 
36  AC4 21 CYS B  33  ? CYS B 36   . ? 1_555 ? 
37  AC4 21 PRO B  34  ? PRO B 37   . ? 1_555 ? 
38  AC4 21 GLY B  35  ? GLY B 38   . ? 1_555 ? 
39  AC4 21 VAL B  60  ? VAL B 63   . ? 1_555 ? 
40  AC4 21 PHE B  66  ? PHE B 69   . ? 1_555 ? 
41  AC4 21 ALA B  74  ? ALA B 77   . ? 1_555 ? 
42  AC4 21 THR B  75  ? THR B 78   . ? 1_555 ? 
43  AC4 21 PHE B  118 ? PHE B 121  . ? 1_555 ? 
44  AC4 21 GLU B  119 ? GLU B 122  . ? 1_555 ? 
45  AC4 21 GLY B  120 ? GLY B 123  . ? 1_555 ? 
46  AC4 21 SER B  123 ? SER B 126  . ? 1_555 ? 
47  AC4 21 MET B  124 ? MET B 127  . ? 1_555 ? 
48  AC4 21 THR B  125 ? THR B 128  . ? 1_555 ? 
49  AC4 21 ARG B  186 ? ARG B 189  . ? 1_555 ? 
50  AC4 21 GLU B  193 ? GLU B 196  . ? 1_555 ? 
51  AC4 21 PHE B  196 ? PHE B 199  . ? 1_555 ? 
52  AC4 21 LEU B  200 ? LEU B 203  . ? 1_555 ? 
53  AC4 21 MG  JA .   ? MG  B 353  . ? 1_555 ? 
54  AC4 21 ACT DB .   ? ACT B 1328 . ? 1_555 ? 
55  AC4 21 HOH NC .   ? HOH B 2157 . ? 1_555 ? 
56  AC4 21 HOH NC .   ? HOH B 2199 . ? 1_555 ? 
57  AC5 6  GLU B  119 ? GLU B 122  . ? 1_555 ? 
58  AC5 6  GLY B  120 ? GLY B 123  . ? 1_555 ? 
59  AC5 6  SER B  123 ? SER B 126  . ? 1_555 ? 
60  AC5 6  HEM IA .   ? HEM B 350  . ? 1_555 ? 
61  AC5 6  HOH NC .   ? HOH B 2157 . ? 1_555 ? 
62  AC5 6  HOH NC .   ? HOH B 2158 . ? 1_555 ? 
63  AC6 4  GLU B  193 ? GLU B 196  . ? 1_555 ? 
64  AC6 4  PHE B  196 ? PHE B 199  . ? 1_555 ? 
65  AC6 4  HEM IA .   ? HEM B 350  . ? 1_555 ? 
66  AC6 4  HOH NC .   ? HOH B 2368 . ? 1_555 ? 
67  AC7 21 PRO C  32  ? PRO C 35   . ? 1_555 ? 
68  AC7 21 CYS C  33  ? CYS C 36   . ? 1_555 ? 
69  AC7 21 PRO C  34  ? PRO C 37   . ? 1_555 ? 
70  AC7 21 GLY C  35  ? GLY C 38   . ? 1_555 ? 
71  AC7 21 PHE C  66  ? PHE C 69   . ? 1_555 ? 
72  AC7 21 ALA C  74  ? ALA C 77   . ? 1_555 ? 
73  AC7 21 THR C  75  ? THR C 78   . ? 1_555 ? 
74  AC7 21 ALA C  78  ? ALA C 81   . ? 1_555 ? 
75  AC7 21 PHE C  118 ? PHE C 121  . ? 1_555 ? 
76  AC7 21 GLU C  119 ? GLU C 122  . ? 1_555 ? 
77  AC7 21 GLY C  120 ? GLY C 123  . ? 1_555 ? 
78  AC7 21 SER C  123 ? SER C 126  . ? 1_555 ? 
79  AC7 21 MET C  124 ? MET C 127  . ? 1_555 ? 
80  AC7 21 THR C  125 ? THR C 128  . ? 1_555 ? 
81  AC7 21 ARG C  186 ? ARG C 189  . ? 1_555 ? 
82  AC7 21 GLU C  193 ? GLU C 196  . ? 1_555 ? 
83  AC7 21 PHE C  196 ? PHE C 199  . ? 1_555 ? 
84  AC7 21 LEU C  200 ? LEU C 203  . ? 1_555 ? 
85  AC7 21 MG  IB .   ? MG  C 353  . ? 1_555 ? 
86  AC7 21 ACT TB .   ? ACT C 1329 . ? 1_555 ? 
87  AC7 21 HOH OC .   ? HOH C 2131 . ? 1_555 ? 
88  AC8 6  GLU C  119 ? GLU C 122  . ? 1_555 ? 
89  AC8 6  GLY C  120 ? GLY C 123  . ? 1_555 ? 
90  AC8 6  SER C  123 ? SER C 126  . ? 1_555 ? 
91  AC8 6  HEM HB .   ? HEM C 350  . ? 1_555 ? 
92  AC8 6  HOH OC .   ? HOH C 2131 . ? 1_555 ? 
93  AC8 6  HOH OC .   ? HOH C 2132 . ? 1_555 ? 
94  AC9 6  ALA C  74  ? ALA C 77   . ? 1_555 ? 
95  AC9 6  PHE C  118 ? PHE C 121  . ? 1_555 ? 
96  AC9 6  THR C  189 ? THR C 192  . ? 1_555 ? 
97  AC9 6  GLU C  193 ? GLU C 196  . ? 1_555 ? 
98  AC9 6  PHE C  196 ? PHE C 199  . ? 1_555 ? 
99  AC9 6  HEM HB .   ? HEM C 350  . ? 1_555 ? 
100 BC1 23 CYS D  33  ? CYS D 36   . ? 1_555 ? 
101 BC1 23 PRO D  34  ? PRO D 37   . ? 1_555 ? 
102 BC1 23 GLY D  35  ? GLY D 38   . ? 1_555 ? 
103 BC1 23 LEU D  36  ? LEU D 39   . ? 1_555 ? 
104 BC1 23 PHE D  66  ? PHE D 69   . ? 1_555 ? 
105 BC1 23 ALA D  74  ? ALA D 77   . ? 1_555 ? 
106 BC1 23 THR D  75  ? THR D 78   . ? 1_555 ? 
107 BC1 23 ALA D  78  ? ALA D 81   . ? 1_555 ? 
108 BC1 23 PHE D  118 ? PHE D 121  . ? 1_555 ? 
109 BC1 23 GLU D  119 ? GLU D 122  . ? 1_555 ? 
110 BC1 23 GLY D  120 ? GLY D 123  . ? 1_555 ? 
111 BC1 23 SER D  123 ? SER D 126  . ? 1_555 ? 
112 BC1 23 MET D  124 ? MET D 127  . ? 1_555 ? 
113 BC1 23 THR D  125 ? THR D 128  . ? 1_555 ? 
114 BC1 23 ARG D  186 ? ARG D 189  . ? 1_555 ? 
115 BC1 23 GLU D  193 ? GLU D 196  . ? 1_555 ? 
116 BC1 23 PHE D  196 ? PHE D 199  . ? 1_555 ? 
117 BC1 23 LEU D  200 ? LEU D 203  . ? 1_555 ? 
118 BC1 23 MG  AC .   ? MG  D 353  . ? 1_555 ? 
119 BC1 23 ACT JC .   ? ACT D 1327 . ? 1_555 ? 
120 BC1 23 HOH PC .   ? HOH D 2029 . ? 1_555 ? 
121 BC1 23 HOH PC .   ? HOH D 2083 . ? 1_555 ? 
122 BC1 23 HOH PC .   ? HOH D 2104 . ? 1_555 ? 
123 BC2 6  GLU D  119 ? GLU D 122  . ? 1_555 ? 
124 BC2 6  GLY D  120 ? GLY D 123  . ? 1_555 ? 
125 BC2 6  SER D  123 ? SER D 126  . ? 1_555 ? 
126 BC2 6  HEM ZB .   ? HEM D 350  . ? 1_555 ? 
127 BC2 6  HOH PC .   ? HOH D 2083 . ? 1_555 ? 
128 BC2 6  HOH PC .   ? HOH D 2084 . ? 1_555 ? 
129 BC3 5  ALA D  74  ? ALA D 77   . ? 1_555 ? 
130 BC3 5  GLU D  193 ? GLU D 196  . ? 1_555 ? 
131 BC3 5  PHE D  196 ? PHE D 199  . ? 1_555 ? 
132 BC3 5  HEM ZB .   ? HEM D 350  . ? 1_555 ? 
133 BC3 5  HOH PC .   ? HOH D 2193 . ? 1_555 ? 
134 BC4 5  ARG C  94  ? ARG C 97   . ? 1_555 ? 
135 BC4 5  THR C  96  ? THR C 99   . ? 1_555 ? 
136 BC4 5  ARG C  97  ? ARG C 100  . ? 1_555 ? 
137 BC4 5  HOH OC .   ? HOH C 2092 . ? 1_555 ? 
138 BC4 5  HOH OC .   ? HOH C 2094 . ? 1_555 ? 
139 BC5 5  ARG A  94  ? ARG A 97   . ? 1_555 ? 
140 BC5 5  THR A  96  ? THR A 99   . ? 1_555 ? 
141 BC5 5  ARG A  97  ? ARG A 100  . ? 1_555 ? 
142 BC5 5  HOH MC .   ? HOH A 2034 . ? 1_555 ? 
143 BC5 5  HOH MC .   ? HOH A 2096 . ? 1_555 ? 
144 BC6 3  ARG B  94  ? ARG B 97   . ? 1_555 ? 
145 BC6 3  THR B  96  ? THR B 99   . ? 1_555 ? 
146 BC6 3  ARG B  97  ? ARG B 100  . ? 1_555 ? 
147 BC7 4  ARG C  94  ? ARG C 97   . ? 1_555 ? 
148 BC7 4  HIS C  135 ? HIS C 138  . ? 1_555 ? 
149 BC7 4  HOH OC .   ? HOH C 2039 . ? 1_555 ? 
150 BC7 4  HOH OC .   ? HOH C 2290 . ? 1_555 ? 
151 BC8 5  ARG A  94  ? ARG A 97   . ? 1_555 ? 
152 BC8 5  HOH MC .   ? HOH A 2035 . ? 1_555 ? 
153 BC8 5  HOH MC .   ? HOH A 2039 . ? 1_555 ? 
154 BC8 5  HOH MC .   ? HOH A 2324 . ? 1_555 ? 
155 BC8 5  HOH MC .   ? HOH A 2325 . ? 1_555 ? 
156 BC9 3  TYR A  148 ? TYR A 151  . ? 1_555 ? 
157 BC9 3  ARG A  151 ? ARG A 154  . ? 1_555 ? 
158 BC9 3  LYS A  168 ? LYS A 171  . ? 1_555 ? 
159 CC1 3  ARG B  94  ? ARG B 97   . ? 1_555 ? 
160 CC1 3  HIS B  135 ? HIS B 138  . ? 1_555 ? 
161 CC1 3  HOH NC .   ? HOH B 2369 . ? 1_555 ? 
162 CC2 5  THR D  96  ? THR D 99   . ? 1_555 ? 
163 CC2 5  ARG D  97  ? ARG D 100  . ? 1_555 ? 
164 CC2 5  HOH PC .   ? HOH D 2064 . ? 1_555 ? 
165 CC2 5  HOH PC .   ? HOH D 2194 . ? 1_555 ? 
166 CC2 5  HOH PC .   ? HOH D 2195 . ? 1_555 ? 
167 CC3 8  THR A  160 ? THR A 163  . ? 1_555 ? 
168 CC3 8  NAG M  .   ? NAG A 371  . ? 1_555 ? 
169 CC3 8  NAG N  .   ? NAG A 372  . ? 1_555 ? 
170 CC3 8  HOH MC .   ? HOH A 2156 . ? 1_555 ? 
171 CC3 8  THR C  273 ? THR C 276  . ? 1_555 ? 
172 CC3 8  PRO C  274 ? PRO C 277  . ? 1_555 ? 
173 CC3 8  CYS C  275 ? CYS C 278  . ? 1_555 ? 
174 CC3 8  LEU C  276 ? LEU C 279  . ? 1_555 ? 
175 CC4 9  THR B  160 ? THR B 163  . ? 1_555 ? 
176 CC4 9  NAG PA .   ? NAG B 371  . ? 1_555 ? 
177 CC4 9  NAG QA .   ? NAG B 372  . ? 1_555 ? 
178 CC4 9  HOH NC .   ? HOH B 2196 . ? 1_555 ? 
179 CC4 9  HOH NC .   ? HOH B 2351 . ? 1_555 ? 
180 CC4 9  THR D  273 ? THR D 276  . ? 1_555 ? 
181 CC4 9  PRO D  274 ? PRO D 277  . ? 1_555 ? 
182 CC4 9  CYS D  275 ? CYS D 278  . ? 1_555 ? 
183 CC4 9  LEU D  276 ? LEU D 279  . ? 1_555 ? 
184 CC5 6  ASN C  138 ? ASN C 141  . ? 1_555 ? 
185 CC5 6  GLU C  139 ? GLU C 142  . ? 1_555 ? 
186 CC5 6  THR C  140 ? THR C 143  . ? 1_555 ? 
187 CC5 6  NAG JB .   ? NAG C 361  . ? 1_555 ? 
188 CC5 6  HOH OC .   ? HOH C 2148 . ? 1_555 ? 
189 CC5 6  HOH OC .   ? HOH C 2291 . ? 1_555 ? 
190 CC6 8  THR B  273 ? THR B 276  . ? 1_555 ? 
191 CC6 8  PRO B  274 ? PRO B 277  . ? 1_555 ? 
192 CC6 8  CYS B  275 ? CYS B 278  . ? 1_555 ? 
193 CC6 8  LEU B  276 ? LEU B 279  . ? 1_555 ? 
194 CC6 8  HOH NC .   ? HOH B 2289 . ? 1_555 ? 
195 CC6 8  THR D  160 ? THR D 163  . ? 1_555 ? 
196 CC6 8  NAG DC .   ? NAG D 371  . ? 1_555 ? 
197 CC6 8  NAG EC .   ? NAG D 372  . ? 1_555 ? 
198 CC7 6  ASN B  48  ? ASN B 51   . ? 4_545 ? 
199 CC7 6  VAL B  50  ? VAL B 53   . ? 4_545 ? 
200 CC7 6  HOH NC .   ? HOH B 2125 . ? 4_545 ? 
201 CC7 6  ARG C  97  ? ARG C 100  . ? 1_555 ? 
202 CC7 6  LEU C  98  ? LEU C 101  . ? 1_555 ? 
203 CC7 6  GLY C  100 ? GLY C 103  . ? 1_555 ? 
204 CC8 9  THR A  273 ? THR A 276  . ? 1_555 ? 
205 CC8 9  PRO A  274 ? PRO A 277  . ? 1_555 ? 
206 CC8 9  CYS A  275 ? CYS A 278  . ? 1_555 ? 
207 CC8 9  LEU A  276 ? LEU A 279  . ? 1_555 ? 
208 CC8 9  HOH MC .   ? HOH A 2258 . ? 1_555 ? 
209 CC8 9  HOH MC .   ? HOH A 2326 . ? 1_555 ? 
210 CC8 9  THR C  160 ? THR C 163  . ? 1_555 ? 
211 CC8 9  NAG MB .   ? NAG C 371  . ? 1_555 ? 
212 CC8 9  NAG NB .   ? NAG C 372  . ? 1_555 ? 
213 CC9 7  ASN A  8   ? ASN A 11   . ? 1_555 ? 
214 CC9 7  SER A  10  ? SER A 13   . ? 1_555 ? 
215 CC9 7  LYS A  12  ? LYS A 15   . ? 1_555 ? 
216 CC9 7  HOH MC .   ? HOH A 2012 . ? 1_555 ? 
217 CC9 7  HOH MC .   ? HOH A 2321 . ? 1_555 ? 
218 CC9 7  HOH MC .   ? HOH A 2322 . ? 1_555 ? 
219 CC9 7  GLU C  7   ? GLU C 10   . ? 1_555 ? 
220 DC1 9  PHE A  130 ? PHE A 133  . ? 1_555 ? 
221 DC1 9  PHE A  131 ? PHE A 134  . ? 1_555 ? 
222 DC1 9  ASN A  138 ? ASN A 141  . ? 1_555 ? 
223 DC1 9  THR A  176 ? THR A 179  . ? 1_555 ? 
224 DC1 9  PRO A  178 ? PRO A 181  . ? 1_555 ? 
225 DC1 9  HOH MC .   ? HOH A 2131 . ? 1_555 ? 
226 DC1 9  HOH MC .   ? HOH A 2302 . ? 1_555 ? 
227 DC1 9  HOH MC .   ? HOH A 2304 . ? 1_555 ? 
228 DC1 9  HOH MC .   ? HOH A 2307 . ? 1_555 ? 
229 DC2 13 PHE A  152 ? PHE A 155  . ? 1_555 ? 
230 DC2 13 GLY A  153 ? GLY A 156  . ? 1_555 ? 
231 DC2 13 GLY A  154 ? GLY A 157  . ? 1_555 ? 
232 DC2 13 ASN A  158 ? ASN A 161  . ? 1_555 ? 
233 DC2 13 THR A  160 ? THR A 163  . ? 1_555 ? 
234 DC2 13 GLN A  210 ? GLN A 213  . ? 1_555 ? 
235 DC2 13 HOH MC .   ? HOH A 2308 . ? 1_555 ? 
236 DC2 13 CYS C  275 ? CYS C 278  . ? 1_555 ? 
237 DC2 13 LEU C  276 ? LEU C 279  . ? 1_555 ? 
238 DC2 13 GLU C  279 ? GLU C 282  . ? 1_555 ? 
239 DC2 13 ALA C  314 ? ALA C 317  . ? 1_555 ? 
240 DC2 13 CYS C  316 ? CYS C 319  . ? 1_555 ? 
241 DC2 13 SO4 WB .   ? SO4 C 1332 . ? 1_555 ? 
242 DC3 6  PHE A  130 ? PHE A 133  . ? 1_555 ? 
243 DC3 6  ASN A  179 ? ASN A 182  . ? 1_555 ? 
244 DC3 6  HOH MC .   ? HOH A 2311 . ? 1_555 ? 
245 DC3 6  THR D  263 ? THR D 266  . ? 2_555 ? 
246 DC3 6  VAL D  264 ? VAL D 267  . ? 2_555 ? 
247 DC3 6  HOH PC .   ? HOH D 2147 . ? 2_555 ? 
248 DC4 23 ASN A  283 ? ASN A 286  . ? 1_555 ? 
249 DC4 23 LYS A  287 ? LYS A 290  . ? 1_555 ? 
250 DC4 23 PRO A  321 ? PRO A 324  . ? 1_555 ? 
251 DC4 23 GLY A  323 ? GLY A 326  . ? 1_555 ? 
252 DC4 23 HOH MC .   ? HOH A 2262 . ? 1_555 ? 
253 DC4 23 HOH MC .   ? HOH A 2301 . ? 1_555 ? 
254 DC4 23 HOH MC .   ? HOH A 2313 . ? 1_555 ? 
255 DC4 23 HOH MC .   ? HOH A 2314 . ? 1_555 ? 
256 DC4 23 HOH MC .   ? HOH A 2315 . ? 1_555 ? 
257 DC4 23 HOH MC .   ? HOH A 2317 . ? 1_555 ? 
258 DC4 23 HOH MC .   ? HOH A 2318 . ? 1_555 ? 
259 DC4 23 HOH MC .   ? HOH A 2319 . ? 1_555 ? 
260 DC4 23 HOH MC .   ? HOH A 2320 . ? 1_555 ? 
261 DC4 23 GLU D  139 ? GLU D 142  . ? 1_655 ? 
262 DC4 23 PHE D  142 ? PHE D 145  . ? 1_655 ? 
263 DC4 23 GLU D  143 ? GLU D 146  . ? 1_655 ? 
264 DC4 23 VAL D  146 ? VAL D 149  . ? 1_655 ? 
265 DC4 23 ASP D  147 ? ASP D 150  . ? 1_655 ? 
266 DC4 23 ASN D  150 ? ASN D 153  . ? 1_655 ? 
267 DC4 23 ARG D  151 ? ARG D 154  . ? 1_655 ? 
268 DC4 23 MET D  213 ? MET D 216  . ? 1_655 ? 
269 DC4 23 ASP D  214 ? ASP D 217  . ? 1_655 ? 
270 DC4 23 ARG D  217 ? ARG D 220  . ? 1_655 ? 
271 DC5 3  ASN B  8   ? ASN B 11   . ? 1_555 ? 
272 DC5 3  ALA B  11  ? ALA B 14   . ? 1_555 ? 
273 DC5 3  HOH NC .   ? HOH B 2366 . ? 1_555 ? 
274 DC6 11 PHE B  130 ? PHE B 133  . ? 1_555 ? 
275 DC6 11 PHE B  131 ? PHE B 134  . ? 1_555 ? 
276 DC6 11 ASN B  138 ? ASN B 141  . ? 1_555 ? 
277 DC6 11 LEU B  141 ? LEU B 144  . ? 1_555 ? 
278 DC6 11 THR B  176 ? THR B 179  . ? 1_555 ? 
279 DC6 11 HOH NC .   ? HOH B 2168 . ? 1_555 ? 
280 DC6 11 HOH NC .   ? HOH B 2175 . ? 1_555 ? 
281 DC6 11 HOH NC .   ? HOH B 2346 . ? 1_555 ? 
282 DC6 11 HOH NC .   ? HOH B 2347 . ? 1_555 ? 
283 DC6 11 HOH NC .   ? HOH B 2348 . ? 1_555 ? 
284 DC6 11 HOH NC .   ? HOH B 2349 . ? 1_555 ? 
285 DC7 16 PHE B  152 ? PHE B 155  . ? 1_555 ? 
286 DC7 16 GLY B  153 ? GLY B 156  . ? 1_555 ? 
287 DC7 16 GLY B  154 ? GLY B 157  . ? 1_555 ? 
288 DC7 16 ASN B  158 ? ASN B 161  . ? 1_555 ? 
289 DC7 16 THR B  160 ? THR B 163  . ? 1_555 ? 
290 DC7 16 GLN B  210 ? GLN B 213  . ? 1_555 ? 
291 DC7 16 HOH NC .   ? HOH B 2190 . ? 1_555 ? 
292 DC7 16 HOH NC .   ? HOH B 2191 . ? 1_555 ? 
293 DC7 16 HOH NC .   ? HOH B 2236 . ? 1_555 ? 
294 DC7 16 HOH NC .   ? HOH B 2350 . ? 1_555 ? 
295 DC7 16 HOH NC .   ? HOH B 2351 . ? 1_555 ? 
296 DC7 16 CYS D  275 ? CYS D 278  . ? 1_555 ? 
297 DC7 16 GLU D  279 ? GLU D 282  . ? 1_555 ? 
298 DC7 16 ALA D  314 ? ALA D 317  . ? 1_555 ? 
299 DC7 16 CYS D  316 ? CYS D 319  . ? 1_555 ? 
300 DC7 16 SO4 LC .   ? SO4 D 1329 . ? 1_555 ? 
301 DC8 6  PHE B  130 ? PHE B 133  . ? 1_555 ? 
302 DC8 6  ASN B  179 ? ASN B 182  . ? 1_555 ? 
303 DC8 6  HOH NC .   ? HOH B 2166 . ? 1_555 ? 
304 DC8 6  HOH NC .   ? HOH B 2352 . ? 1_555 ? 
305 DC8 6  HOH NC .   ? HOH B 2355 . ? 1_555 ? 
306 DC8 6  HOH NC .   ? HOH B 2356 . ? 1_555 ? 
307 DC9 24 ASN B  283 ? ASN B 286  . ? 1_555 ? 
308 DC9 24 LYS B  287 ? LYS B 290  . ? 1_555 ? 
309 DC9 24 PRO B  321 ? PRO B 324  . ? 1_555 ? 
310 DC9 24 GLY B  323 ? GLY B 326  . ? 1_555 ? 
311 DC9 24 HOH NC .   ? HOH B 2295 . ? 1_555 ? 
312 DC9 24 HOH NC .   ? HOH B 2341 . ? 1_555 ? 
313 DC9 24 HOH NC .   ? HOH B 2342 . ? 1_555 ? 
314 DC9 24 HOH NC .   ? HOH B 2357 . ? 1_555 ? 
315 DC9 24 HOH NC .   ? HOH B 2358 . ? 1_555 ? 
316 DC9 24 HOH NC .   ? HOH B 2359 . ? 1_555 ? 
317 DC9 24 HOH NC .   ? HOH B 2360 . ? 1_555 ? 
318 DC9 24 HOH NC .   ? HOH B 2361 . ? 1_555 ? 
319 DC9 24 HOH NC .   ? HOH B 2362 . ? 1_555 ? 
320 DC9 24 HOH NC .   ? HOH B 2363 . ? 1_555 ? 
321 DC9 24 HOH NC .   ? HOH B 2364 . ? 1_555 ? 
322 DC9 24 HOH NC .   ? HOH B 2365 . ? 1_555 ? 
323 DC9 24 GLU C  139 ? GLU C 142  . ? 1_455 ? 
324 DC9 24 GLU C  143 ? GLU C 146  . ? 1_455 ? 
325 DC9 24 VAL C  146 ? VAL C 149  . ? 1_455 ? 
326 DC9 24 ASP C  147 ? ASP C 150  . ? 1_455 ? 
327 DC9 24 ASN C  150 ? ASN C 153  . ? 1_455 ? 
328 DC9 24 MET C  213 ? MET C 216  . ? 1_455 ? 
329 DC9 24 ASP C  214 ? ASP C 217  . ? 1_455 ? 
330 DC9 24 ARG C  217 ? ARG C 220  . ? 1_455 ? 
331 EC1 3  ASN C  8   ? ASN C 11   . ? 1_555 ? 
332 EC1 3  ALA C  11  ? ALA C 14   . ? 1_555 ? 
333 EC1 3  HOH OC .   ? HOH C 2288 . ? 1_555 ? 
334 EC2 3  ASN C  138 ? ASN C 141  . ? 1_555 ? 
335 EC2 3  SO4 XB .   ? SO4 C 1333 . ? 1_555 ? 
336 EC2 3  HOH OC .   ? HOH C 2284 . ? 1_555 ? 
337 EC3 13 CYS A  275 ? CYS A 278  . ? 1_555 ? 
338 EC3 13 GLU A  279 ? GLU A 282  . ? 1_555 ? 
339 EC3 13 ALA A  314 ? ALA A 317  . ? 1_555 ? 
340 EC3 13 CYS A  316 ? CYS A 319  . ? 1_555 ? 
341 EC3 13 SO4 HA .   ? SO4 A 1331 . ? 1_555 ? 
342 EC3 13 HOH MC .   ? HOH A 2294 . ? 1_555 ? 
343 EC3 13 PHE C  152 ? PHE C 155  . ? 1_555 ? 
344 EC3 13 GLY C  153 ? GLY C 156  . ? 1_555 ? 
345 EC3 13 GLY C  154 ? GLY C 157  . ? 1_555 ? 
346 EC3 13 ASN C  158 ? ASN C 161  . ? 1_555 ? 
347 EC3 13 THR C  160 ? THR C 163  . ? 1_555 ? 
348 EC3 13 GLN C  210 ? GLN C 213  . ? 1_555 ? 
349 EC3 13 HOH OC .   ? HOH C 2153 . ? 1_555 ? 
350 EC4 3  PHE C  130 ? PHE C 133  . ? 1_555 ? 
351 EC4 3  ASN C  179 ? ASN C 182  . ? 1_555 ? 
352 EC4 3  HOH OC .   ? HOH C 2286 . ? 1_555 ? 
353 EC5 8  ASN C  283 ? ASN C 286  . ? 1_555 ? 
354 EC5 8  LYS C  287 ? LYS C 290  . ? 1_555 ? 
355 EC5 8  PHE C  320 ? PHE C 323  . ? 1_555 ? 
356 EC5 8  PRO C  321 ? PRO C 324  . ? 1_555 ? 
357 EC5 8  HOH OC .   ? HOH C 2237 . ? 1_555 ? 
358 EC5 8  HOH OC .   ? HOH C 2240 . ? 1_555 ? 
359 EC5 8  HOH OC .   ? HOH C 2280 . ? 1_555 ? 
360 EC5 8  HOH OC .   ? HOH C 2287 . ? 1_555 ? 
361 EC6 5  GLU B  7   ? GLU B 10   . ? 1_555 ? 
362 EC6 5  ASN D  8   ? ASN D 11   . ? 1_555 ? 
363 EC6 5  SER D  10  ? SER D 13   . ? 1_555 ? 
364 EC6 5  ALA D  11  ? ALA D 14   . ? 1_555 ? 
365 EC6 5  LYS D  12  ? LYS D 15   . ? 1_555 ? 
366 EC7 2  ASN D  138 ? ASN D 141  . ? 1_555 ? 
367 EC7 2  HOH PC .   ? HOH D 2190 . ? 1_555 ? 
368 EC8 12 CYS B  275 ? CYS B 278  . ? 1_555 ? 
369 EC8 12 GLU B  279 ? GLU B 282  . ? 1_555 ? 
370 EC8 12 ALA B  314 ? ALA B 317  . ? 1_555 ? 
371 EC8 12 CYS B  316 ? CYS B 319  . ? 1_555 ? 
372 EC8 12 SO4 GB .   ? SO4 B 1331 . ? 1_555 ? 
373 EC8 12 HOH NC .   ? HOH B 2335 . ? 1_555 ? 
374 EC8 12 PHE D  152 ? PHE D 155  . ? 1_555 ? 
375 EC8 12 GLY D  153 ? GLY D 156  . ? 1_555 ? 
376 EC8 12 ASN D  158 ? ASN D 161  . ? 1_555 ? 
377 EC8 12 THR D  160 ? THR D 163  . ? 1_555 ? 
378 EC8 12 GLN D  210 ? GLN D 213  . ? 1_555 ? 
379 EC8 12 HOH PC .   ? HOH D 2098 . ? 1_555 ? 
380 EC9 1  ASN D  179 ? ASN D 182  . ? 1_555 ? 
381 FC1 5  ASN D  283 ? ASN D 286  . ? 1_555 ? 
382 FC1 5  LYS D  287 ? LYS D 290  . ? 1_555 ? 
383 FC1 5  PHE D  320 ? PHE D 323  . ? 1_555 ? 
384 FC1 5  PRO D  321 ? PRO D 324  . ? 1_555 ? 
385 FC1 5  HOH PC .   ? HOH D 2189 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2YP1 
_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                    2YP1 
_atom_sites.fract_transf_matrix[1][1]   0.008869 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_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]   0.006902 
_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]   0.007437 
_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  
FE 
MG 
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   . LEU A  1 1   ? 40.193  -39.873 42.417  1.00 46.54 ? 4    LEU A N   1 
ATOM   2     C  CA  . LEU A  1 1   ? 40.141  -39.227 41.072  1.00 48.07 ? 4    LEU A CA  1 
ATOM   3     C  C   . LEU A  1 1   ? 38.698  -39.070 40.583  1.00 47.91 ? 4    LEU A C   1 
ATOM   4     O  O   . LEU A  1 1   ? 37.854  -39.972 40.783  1.00 45.93 ? 4    LEU A O   1 
ATOM   5     C  CB  . LEU A  1 1   ? 40.936  -40.039 40.046  1.00 49.03 ? 4    LEU A CB  1 
ATOM   6     C  CG  . LEU A  1 1   ? 42.444  -40.182 40.250  1.00 50.56 ? 4    LEU A CG  1 
ATOM   7     C  CD1 . LEU A  1 1   ? 42.873  -41.604 39.864  1.00 50.29 ? 4    LEU A CD1 1 
ATOM   8     C  CD2 . LEU A  1 1   ? 43.220  -39.125 39.450  1.00 49.71 ? 4    LEU A CD2 1 
ATOM   9     N  N   . PRO A  1 2   ? 38.414  -37.930 39.922  1.00 45.72 ? 5    PRO A N   1 
ATOM   10    C  CA  . PRO A  1 2   ? 37.147  -37.722 39.231  1.00 42.83 ? 5    PRO A CA  1 
ATOM   11    C  C   . PRO A  1 2   ? 36.980  -38.770 38.152  1.00 38.76 ? 5    PRO A C   1 
ATOM   12    O  O   . PRO A  1 2   ? 37.932  -39.064 37.420  1.00 40.20 ? 5    PRO A O   1 
ATOM   13    C  CB  . PRO A  1 2   ? 37.313  -36.335 38.594  1.00 43.12 ? 5    PRO A CB  1 
ATOM   14    C  CG  . PRO A  1 2   ? 38.351  -35.666 39.409  1.00 44.03 ? 5    PRO A CG  1 
ATOM   15    C  CD  . PRO A  1 2   ? 39.310  -36.774 39.764  1.00 46.11 ? 5    PRO A CD  1 
ATOM   16    N  N   . PRO A  1 3   ? 35.806  -39.403 38.114  1.00 36.94 ? 6    PRO A N   1 
ATOM   17    C  CA  . PRO A  1 3   ? 35.451  -40.228 36.966  1.00 36.01 ? 6    PRO A CA  1 
ATOM   18    C  C   . PRO A  1 3   ? 35.818  -39.478 35.689  1.00 37.43 ? 6    PRO A C   1 
ATOM   19    O  O   . PRO A  1 3   ? 35.837  -38.238 35.676  1.00 33.57 ? 6    PRO A O   1 
ATOM   20    C  CB  . PRO A  1 3   ? 33.926  -40.346 37.081  1.00 36.44 ? 6    PRO A CB  1 
ATOM   21    C  CG  . PRO A  1 3   ? 33.636  -40.108 38.543  1.00 34.13 ? 6    PRO A CG  1 
ATOM   22    C  CD  . PRO A  1 3   ? 34.657  -39.130 39.001  1.00 34.27 ? 6    PRO A CD  1 
ATOM   23    N  N   . GLY A  1 4   ? 36.211  -40.218 34.660  1.00 38.20 ? 7    GLY A N   1 
ATOM   24    C  CA  . GLY A  1 4   ? 36.285  -39.649 33.320  1.00 38.81 ? 7    GLY A CA  1 
ATOM   25    C  C   . GLY A  1 4   ? 34.965  -39.833 32.591  1.00 38.27 ? 7    GLY A C   1 
ATOM   26    O  O   . GLY A  1 4   ? 33.979  -40.286 33.184  1.00 37.55 ? 7    GLY A O   1 
ATOM   27    N  N   . PRO A  1 5   ? 34.949  -39.499 31.292  1.00 36.90 ? 8    PRO A N   1 
ATOM   28    C  CA  . PRO A  1 5   ? 33.762  -39.482 30.438  1.00 35.44 ? 8    PRO A CA  1 
ATOM   29    C  C   . PRO A  1 5   ? 33.143  -40.871 30.337  1.00 36.18 ? 8    PRO A C   1 
ATOM   30    O  O   . PRO A  1 5   ? 33.843  -41.867 30.550  1.00 38.09 ? 8    PRO A O   1 
ATOM   31    C  CB  . PRO A  1 5   ? 34.324  -39.076 29.070  1.00 36.48 ? 8    PRO A CB  1 
ATOM   32    C  CG  . PRO A  1 5   ? 35.597  -38.361 29.375  1.00 37.67 ? 8    PRO A CG  1 
ATOM   33    C  CD  . PRO A  1 5   ? 36.156  -39.027 30.589  1.00 35.84 ? 8    PRO A CD  1 
ATOM   34    N  N   . LEU A  1 6   ? 31.849  -40.950 30.039  1.00 34.76 ? 9    LEU A N   1 
ATOM   35    C  CA  . LEU A  1 6   ? 31.222  -42.252 29.771  1.00 37.59 ? 9    LEU A CA  1 
ATOM   36    C  C   . LEU A  1 6   ? 31.997  -42.966 28.661  1.00 38.51 ? 9    LEU A C   1 
ATOM   37    O  O   . LEU A  1 6   ? 32.597  -42.319 27.802  1.00 37.40 ? 9    LEU A O   1 
ATOM   38    C  CB  . LEU A  1 6   ? 29.764  -42.085 29.339  1.00 38.13 ? 9    LEU A CB  1 
ATOM   39    C  CG  . LEU A  1 6   ? 28.612  -42.095 30.356  1.00 39.67 ? 9    LEU A CG  1 
ATOM   40    C  CD1 . LEU A  1 6   ? 29.054  -41.935 31.785  1.00 36.74 ? 9    LEU A CD1 1 
ATOM   41    C  CD2 . LEU A  1 6   ? 27.602  -41.022 29.984  1.00 38.93 ? 9    LEU A CD2 1 
ATOM   42    N  N   . GLU A  1 7   ? 32.019  -44.295 28.708  1.00 39.30 ? 10   GLU A N   1 
ATOM   43    C  CA  . GLU A  1 7   ? 32.600  -45.088 27.633  1.00 43.21 ? 10   GLU A CA  1 
ATOM   44    C  C   . GLU A  1 7   ? 31.637  -45.142 26.458  1.00 41.17 ? 10   GLU A C   1 
ATOM   45    O  O   . GLU A  1 7   ? 32.035  -44.980 25.307  1.00 41.74 ? 10   GLU A O   1 
ATOM   46    C  CB  . GLU A  1 7   ? 32.906  -46.513 28.109  1.00 48.70 ? 10   GLU A CB  1 
ATOM   47    C  CG  . GLU A  1 7   ? 34.012  -46.607 29.153  1.00 54.15 ? 10   GLU A CG  1 
ATOM   48    C  CD  . GLU A  1 7   ? 34.696  -47.968 29.149  1.00 57.41 ? 10   GLU A CD  1 
ATOM   49    O  OE1 . GLU A  1 7   ? 33.994  -48.990 28.976  1.00 59.12 ? 10   GLU A OE1 1 
ATOM   50    O  OE2 . GLU A  1 7   ? 35.938  -48.015 29.291  1.00 58.95 ? 10   GLU A OE2 1 
ATOM   51    N  N   . ASN A  1 8   ? 30.363  -45.359 26.759  1.00 38.76 ? 11   ASN A N   1 
ATOM   52    C  CA  . ASN A  1 8   ? 29.321  -45.324 25.741  1.00 37.31 ? 11   ASN A CA  1 
ATOM   53    C  C   . ASN A  1 8   ? 28.305  -44.222 26.037  1.00 33.82 ? 11   ASN A C   1 
ATOM   54    O  O   . ASN A  1 8   ? 27.460  -44.380 26.912  1.00 30.29 ? 11   ASN A O   1 
ATOM   55    C  CB  . ASN A  1 8   ? 28.623  -46.681 25.689  1.00 39.60 ? 11   ASN A CB  1 
ATOM   56    C  CG  . ASN A  1 8   ? 27.565  -46.750 24.617  1.00 43.12 ? 11   ASN A CG  1 
ATOM   57    O  OD1 . ASN A  1 8   ? 27.181  -45.734 24.042  1.00 39.06 ? 11   ASN A OD1 1 
ATOM   58    N  ND2 . ASN A  1 8   ? 27.093  -47.962 24.333  1.00 47.22 ? 11   ASN A ND2 1 
ATOM   59    N  N   . SER A  1 9   ? 28.369  -43.114 25.297  1.00 33.68 ? 12   SER A N   1 
ATOM   60    C  CA  . SER A  1 9   ? 27.511  -41.946 25.581  1.00 30.49 ? 12   SER A CA  1 
ATOM   61    C  C   . SER A  1 9   ? 26.211  -41.807 24.748  1.00 32.29 ? 12   SER A C   1 
ATOM   62    O  O   . SER A  1 9   ? 25.551  -40.749 24.782  1.00 27.52 ? 12   SER A O   1 
ATOM   63    C  CB  . SER A  1 9   ? 28.324  -40.649 25.524  1.00 30.79 ? 12   SER A CB  1 
ATOM   64    O  OG  . SER A  1 9   ? 28.966  -40.481 24.259  1.00 30.05 ? 12   SER A OG  1 
ATOM   65    N  N   . SER A  1 10  ? 25.800  -42.859 24.041  1.00 31.12 ? 13   SER A N   1 
ATOM   66    C  CA  . SER A  1 10  ? 24.536  -42.755 23.297  1.00 33.10 ? 13   SER A CA  1 
ATOM   67    C  C   . SER A  1 10  ? 23.300  -42.672 24.191  1.00 30.30 ? 13   SER A C   1 
ATOM   68    O  O   . SER A  1 10  ? 23.395  -42.850 25.406  1.00 27.43 ? 13   SER A O   1 
ATOM   69    C  CB  . SER A  1 10  ? 24.367  -43.819 22.200  1.00 34.49 ? 13   SER A CB  1 
ATOM   70    O  OG  . SER A  1 10  ? 24.905  -45.066 22.574  1.00 36.40 ? 13   SER A OG  1 
ATOM   71    N  N   . ALA A  1 11  ? 22.199  -42.221 23.590  1.00 28.40 ? 14   ALA A N   1 
ATOM   72    C  CA  . ALA A  1 11  ? 20.890  -42.203 24.217  1.00 29.88 ? 14   ALA A CA  1 
ATOM   73    C  C   . ALA A  1 11  ? 20.498  -43.594 24.711  1.00 30.37 ? 14   ALA A C   1 
ATOM   74    O  O   . ALA A  1 11  ? 20.743  -44.595 24.034  1.00 28.75 ? 14   ALA A O   1 
ATOM   75    C  CB  . ALA A  1 11  ? 19.846  -41.682 23.217  1.00 30.01 ? 14   ALA A CB  1 
ATOM   76    N  N   . LYS A  1 12  ? 19.891  -43.650 25.893  1.00 33.09 ? 15   LYS A N   1 
ATOM   77    C  CA  . LYS A  1 12  ? 19.292  -44.882 26.393  1.00 34.46 ? 15   LYS A CA  1 
ATOM   78    C  C   . LYS A  1 12  ? 18.200  -44.588 27.414  1.00 34.45 ? 15   LYS A C   1 
ATOM   79    O  O   . LYS A  1 12  ? 18.104  -43.471 27.914  1.00 32.97 ? 15   LYS A O   1 
ATOM   80    C  CB  . LYS A  1 12  ? 20.366  -45.792 26.996  1.00 36.90 ? 15   LYS A CB  1 
ATOM   81    C  CG  . LYS A  1 12  ? 20.973  -45.295 28.296  1.00 38.97 ? 15   LYS A CG  1 
ATOM   82    C  CD  . LYS A  1 12  ? 22.102  -46.223 28.742  1.00 41.34 ? 15   LYS A CD  1 
ATOM   83    C  CE  . LYS A  1 12  ? 22.222  -46.248 30.261  1.00 44.96 ? 15   LYS A CE  1 
ATOM   84    N  NZ  . LYS A  1 12  ? 23.275  -47.196 30.730  1.00 45.95 ? 15   LYS A NZ  1 
ATOM   85    N  N   . LEU A  1 13  ? 17.355  -45.580 27.691  1.00 35.81 ? 16   LEU A N   1 
ATOM   86    C  CA  . LEU A  1 13  ? 16.335  -45.436 28.719  1.00 33.35 ? 16   LEU A CA  1 
ATOM   87    C  C   . LEU A  1 13  ? 17.010  -45.194 30.059  1.00 32.47 ? 16   LEU A C   1 
ATOM   88    O  O   . LEU A  1 13  ? 17.877  -45.956 30.463  1.00 31.28 ? 16   LEU A O   1 
ATOM   89    C  CB  . LEU A  1 13  ? 15.450  -46.678 28.782  1.00 33.67 ? 16   LEU A CB  1 
ATOM   90    C  CG  . LEU A  1 13  ? 14.350  -46.657 29.857  1.00 35.61 ? 16   LEU A CG  1 
ATOM   91    C  CD1 . LEU A  1 13  ? 13.320  -45.571 29.586  1.00 34.80 ? 16   LEU A CD1 1 
ATOM   92    C  CD2 . LEU A  1 13  ? 13.671  -48.032 30.011  1.00 33.32 ? 16   LEU A CD2 1 
ATOM   93    N  N   . VAL A  1 14  ? 16.649  -44.113 30.740  1.00 31.71 ? 17   VAL A N   1 
ATOM   94    C  CA  . VAL A  1 14  ? 17.200  -43.899 32.071  1.00 30.02 ? 17   VAL A CA  1 
ATOM   95    C  C   . VAL A  1 14  ? 16.142  -43.932 33.157  1.00 30.51 ? 17   VAL A C   1 
ATOM   96    O  O   . VAL A  1 14  ? 16.459  -43.970 34.347  1.00 29.26 ? 17   VAL A O   1 
ATOM   97    C  CB  . VAL A  1 14  ? 18.010  -42.604 32.162  1.00 27.59 ? 17   VAL A CB  1 
ATOM   98    C  CG1 . VAL A  1 14  ? 19.293  -42.749 31.344  1.00 27.01 ? 17   VAL A CG1 1 
ATOM   99    C  CG2 . VAL A  1 14  ? 17.165  -41.419 31.690  1.00 27.02 ? 17   VAL A CG2 1 
ATOM   100   N  N   . ASN A  1 15  ? 14.883  -43.824 32.752  1.00 32.61 ? 18   ASN A N   1 
ATOM   101   C  CA  . ASN A  1 15  ? 13.812  -44.075 33.685  1.00 34.35 ? 18   ASN A CA  1 
ATOM   102   C  C   . ASN A  1 15  ? 13.500  -45.570 33.669  1.00 37.83 ? 18   ASN A C   1 
ATOM   103   O  O   . ASN A  1 15  ? 12.562  -46.006 32.999  1.00 37.21 ? 18   ASN A O   1 
ATOM   104   C  CB  . ASN A  1 15  ? 12.582  -43.252 33.339  1.00 30.47 ? 18   ASN A CB  1 
ATOM   105   C  CG  . ASN A  1 15  ? 11.493  -43.391 34.387  1.00 33.63 ? 18   ASN A CG  1 
ATOM   106   O  OD1 . ASN A  1 15  ? 11.606  -44.218 35.304  1.00 33.02 ? 18   ASN A OD1 1 
ATOM   107   N  ND2 . ASN A  1 15  ? 10.452  -42.559 34.289  1.00 29.53 ? 18   ASN A ND2 1 
ATOM   108   N  N   . ASP A  1 16  ? 14.359  -46.357 34.319  1.00 40.37 ? 19   ASP A N   1 
ATOM   109   C  CA  . ASP A  1 16  ? 14.338  -47.808 34.148  1.00 44.83 ? 19   ASP A CA  1 
ATOM   110   C  C   . ASP A  1 16  ? 14.102  -48.593 35.434  1.00 46.62 ? 19   ASP A C   1 
ATOM   111   O  O   . ASP A  1 16  ? 13.966  -48.025 36.522  1.00 45.87 ? 19   ASP A O   1 
ATOM   112   C  CB  . ASP A  1 16  ? 15.599  -48.313 33.423  1.00 44.39 ? 19   ASP A CB  1 
ATOM   113   C  CG  . ASP A  1 16  ? 16.889  -47.984 34.172  1.00 44.87 ? 19   ASP A CG  1 
ATOM   114   O  OD1 . ASP A  1 16  ? 16.838  -47.769 35.406  1.00 45.03 ? 19   ASP A OD1 1 
ATOM   115   O  OD2 . ASP A  1 16  ? 17.969  -48.005 33.537  1.00 42.98 ? 19   ASP A OD2 1 
ATOM   116   N  N   . GLU A  1 17  ? 14.020  -49.912 35.275  1.00 49.89 ? 20   GLU A N   1 
ATOM   117   C  CA  . GLU A  1 17  ? 13.685  -50.825 36.357  1.00 51.03 ? 20   GLU A CA  1 
ATOM   118   C  C   . GLU A  1 17  ? 14.674  -50.661 37.503  1.00 49.40 ? 20   GLU A C   1 
ATOM   119   O  O   . GLU A  1 17  ? 14.288  -50.694 38.675  1.00 50.23 ? 20   GLU A O   1 
ATOM   120   C  CB  . GLU A  1 17  ? 13.711  -52.267 35.841  1.00 54.59 ? 20   GLU A CB  1 
ATOM   121   C  CG  . GLU A  1 17  ? 13.225  -53.308 36.842  1.00 59.38 ? 20   GLU A CG  1 
ATOM   122   C  CD  . GLU A  1 17  ? 12.630  -54.538 36.159  1.00 62.63 ? 20   GLU A CD  1 
ATOM   123   O  OE1 . GLU A  1 17  ? 11.760  -54.360 35.275  1.00 64.02 ? 20   GLU A OE1 1 
ATOM   124   O  OE2 . GLU A  1 17  ? 13.042  -55.676 36.491  1.00 62.85 ? 20   GLU A OE2 1 
ATOM   125   N  N   . ALA A  1 18  ? 15.943  -50.461 37.149  1.00 45.59 ? 21   ALA A N   1 
ATOM   126   C  CA  . ALA A  1 18  ? 16.994  -50.187 38.120  1.00 44.24 ? 21   ALA A CA  1 
ATOM   127   C  C   . ALA A  1 18  ? 16.825  -48.842 38.838  1.00 43.32 ? 21   ALA A C   1 
ATOM   128   O  O   . ALA A  1 18  ? 17.336  -48.666 39.942  1.00 42.94 ? 21   ALA A O   1 
ATOM   129   C  CB  . ALA A  1 18  ? 18.368  -50.267 37.449  1.00 44.89 ? 21   ALA A CB  1 
ATOM   130   N  N   . HIS A  1 19  ? 16.119  -47.899 38.210  1.00 39.90 ? 22   HIS A N   1 
ATOM   131   C  CA  . HIS A  1 19  ? 16.109  -46.505 38.668  1.00 38.11 ? 22   HIS A CA  1 
ATOM   132   C  C   . HIS A  1 19  ? 14.710  -45.913 38.649  1.00 38.89 ? 22   HIS A C   1 
ATOM   133   O  O   . HIS A  1 19  ? 14.431  -45.025 37.853  1.00 35.38 ? 22   HIS A O   1 
ATOM   134   C  CB  . HIS A  1 19  ? 17.029  -45.636 37.803  1.00 36.67 ? 22   HIS A CB  1 
ATOM   135   C  CG  . HIS A  1 19  ? 18.468  -46.033 37.874  1.00 34.77 ? 22   HIS A CG  1 
ATOM   136   N  ND1 . HIS A  1 19  ? 19.085  -46.765 36.883  1.00 36.09 ? 22   HIS A ND1 1 
ATOM   137   C  CD2 . HIS A  1 19  ? 19.382  -45.891 38.862  1.00 35.10 ? 22   HIS A CD2 1 
ATOM   138   C  CE1 . HIS A  1 19  ? 20.340  -46.998 37.227  1.00 36.94 ? 22   HIS A CE1 1 
ATOM   139   N  NE2 . HIS A  1 19  ? 20.543  -46.485 38.429  1.00 36.55 ? 22   HIS A NE2 1 
ATOM   140   N  N   . PRO A  1 20  ? 13.821  -46.431 39.513  1.00 38.75 ? 23   PRO A N   1 
ATOM   141   C  CA  . PRO A  1 20  ? 12.447  -45.960 39.596  1.00 37.98 ? 23   PRO A CA  1 
ATOM   142   C  C   . PRO A  1 20  ? 12.338  -44.698 40.441  1.00 37.41 ? 23   PRO A C   1 
ATOM   143   O  O   . PRO A  1 20  ? 13.082  -44.521 41.398  1.00 38.28 ? 23   PRO A O   1 
ATOM   144   C  CB  . PRO A  1 20  ? 11.725  -47.120 40.296  1.00 38.71 ? 23   PRO A CB  1 
ATOM   145   C  CG  . PRO A  1 20  ? 12.808  -47.771 41.129  1.00 38.45 ? 23   PRO A CG  1 
ATOM   146   C  CD  . PRO A  1 20  ? 14.020  -47.697 40.242  1.00 36.02 ? 23   PRO A CD  1 
ATOM   147   N  N   . TRP A  1 21  ? 11.412  -43.826 40.081  1.00 32.63 ? 24   TRP A N   1 
ATOM   148   C  CA  . TRP A  1 21  ? 11.083  -42.706 40.931  1.00 31.80 ? 24   TRP A CA  1 
ATOM   149   C  C   . TRP A  1 21  ? 10.459  -43.212 42.240  1.00 33.93 ? 24   TRP A C   1 
ATOM   150   O  O   . TRP A  1 21  ? 9.784   -44.235 42.247  1.00 36.77 ? 24   TRP A O   1 
ATOM   151   C  CB  . TRP A  1 21  ? 10.108  -41.778 40.204  1.00 26.51 ? 24   TRP A CB  1 
ATOM   152   C  CG  . TRP A  1 21  ? 9.854   -40.528 40.944  1.00 23.67 ? 24   TRP A CG  1 
ATOM   153   C  CD1 . TRP A  1 21  ? 10.665  -39.437 41.000  1.00 22.93 ? 24   TRP A CD1 1 
ATOM   154   C  CD2 . TRP A  1 21  ? 8.772   -40.275 41.840  1.00 23.60 ? 24   TRP A CD2 1 
ATOM   155   N  NE1 . TRP A  1 21  ? 10.133  -38.500 41.847  1.00 22.27 ? 24   TRP A NE1 1 
ATOM   156   C  CE2 . TRP A  1 21  ? 8.976   -38.997 42.387  1.00 22.98 ? 24   TRP A CE2 1 
ATOM   157   C  CE3 . TRP A  1 21  ? 7.612   -40.980 42.183  1.00 26.05 ? 24   TRP A CE3 1 
ATOM   158   C  CZ2 . TRP A  1 21  ? 8.048   -38.389 43.231  1.00 24.06 ? 24   TRP A CZ2 1 
ATOM   159   C  CZ3 . TRP A  1 21  ? 6.717   -40.400 43.044  1.00 25.24 ? 24   TRP A CZ3 1 
ATOM   160   C  CH2 . TRP A  1 21  ? 6.941   -39.118 43.572  1.00 27.03 ? 24   TRP A CH2 1 
ATOM   161   N  N   . LYS A  1 22  ? 10.731  -42.529 43.350  1.00 34.34 ? 25   LYS A N   1 
ATOM   162   C  CA  . LYS A  1 22  ? 10.123  -42.869 44.637  1.00 34.38 ? 25   LYS A CA  1 
ATOM   163   C  C   . LYS A  1 22  ? 9.872   -41.595 45.428  1.00 35.75 ? 25   LYS A C   1 
ATOM   164   O  O   . LYS A  1 22  ? 10.721  -40.705 45.470  1.00 35.13 ? 25   LYS A O   1 
ATOM   165   C  CB  . LYS A  1 22  ? 11.032  -43.793 45.443  1.00 35.17 ? 25   LYS A CB  1 
ATOM   166   C  CG  . LYS A  1 22  ? 11.205  -45.166 44.834  1.00 38.66 ? 25   LYS A CG  1 
ATOM   167   C  CD  . LYS A  1 22  ? 12.122  -46.052 45.683  1.00 43.18 ? 25   LYS A CD  1 
ATOM   168   C  CE  . LYS A  1 22  ? 12.392  -47.382 44.968  1.00 44.13 ? 25   LYS A CE  1 
ATOM   169   N  NZ  . LYS A  1 22  ? 13.201  -48.319 45.788  1.00 45.47 ? 25   LYS A NZ  1 
ATOM   170   N  N   . PRO A  1 23  ? 8.687   -41.492 46.041  1.00 35.44 ? 26   PRO A N   1 
ATOM   171   C  CA  . PRO A  1 23  ? 8.374   -40.289 46.794  1.00 35.79 ? 26   PRO A CA  1 
ATOM   172   C  C   . PRO A  1 23  ? 9.371   -40.059 47.935  1.00 35.51 ? 26   PRO A C   1 
ATOM   173   O  O   . PRO A  1 23  ? 10.056  -40.986 48.360  1.00 36.72 ? 26   PRO A O   1 
ATOM   174   C  CB  . PRO A  1 23  ? 6.952   -40.560 47.323  1.00 35.91 ? 26   PRO A CB  1 
ATOM   175   C  CG  . PRO A  1 23  ? 6.829   -42.051 47.349  1.00 37.25 ? 26   PRO A CG  1 
ATOM   176   C  CD  . PRO A  1 23  ? 7.675   -42.554 46.210  1.00 36.44 ? 26   PRO A CD  1 
ATOM   177   N  N   . LEU A  1 24  ? 9.469   -38.821 48.402  1.00 34.88 ? 27   LEU A N   1 
ATOM   178   C  CA  . LEU A  1 24  ? 10.297  -38.507 49.557  1.00 37.82 ? 27   LEU A CA  1 
ATOM   179   C  C   . LEU A  1 24  ? 9.847   -39.216 50.844  1.00 39.96 ? 27   LEU A C   1 
ATOM   180   O  O   . LEU A  1 24  ? 8.670   -39.206 51.192  1.00 41.15 ? 27   LEU A O   1 
ATOM   181   C  CB  . LEU A  1 24  ? 10.341  -36.994 49.766  1.00 35.54 ? 27   LEU A CB  1 
ATOM   182   C  CG  . LEU A  1 24  ? 10.869  -36.226 48.549  1.00 35.65 ? 27   LEU A CG  1 
ATOM   183   C  CD1 . LEU A  1 24  ? 10.740  -34.720 48.764  1.00 32.92 ? 27   LEU A CD1 1 
ATOM   184   C  CD2 . LEU A  1 24  ? 12.319  -36.636 48.226  1.00 29.46 ? 27   LEU A CD2 1 
ATOM   185   N  N   . ARG A  1 25  ? 10.790  -39.873 51.515  1.00 43.77 ? 28   ARG A N   1 
ATOM   186   C  CA  . ARG A  1 25  ? 10.743  -40.047 52.968  1.00 45.43 ? 28   ARG A CA  1 
ATOM   187   C  C   . ARG A  1 25  ? 10.898  -38.689 53.671  1.00 47.21 ? 28   ARG A C   1 
ATOM   188   O  O   . ARG A  1 25  ? 11.326  -37.713 53.056  1.00 45.33 ? 28   ARG A O   1 
ATOM   189   C  CB  . ARG A  1 25  ? 11.856  -40.998 53.416  1.00 45.25 ? 28   ARG A CB  1 
ATOM   190   C  CG  . ARG A  1 25  ? 11.984  -42.255 52.564  1.00 46.72 ? 28   ARG A CG  1 
ATOM   191   C  CD  . ARG A  1 25  ? 10.614  -42.855 52.324  1.00 51.20 ? 28   ARG A CD  1 
ATOM   192   N  NE  . ARG A  1 25  ? 10.666  -44.267 51.934  1.00 56.37 ? 28   ARG A NE  1 
ATOM   193   C  CZ  . ARG A  1 25  ? 9.732   -45.168 52.246  1.00 57.13 ? 28   ARG A CZ  1 
ATOM   194   N  NH1 . ARG A  1 25  ? 8.681   -44.814 52.979  1.00 56.91 ? 28   ARG A NH1 1 
ATOM   195   N  NH2 . ARG A  1 25  ? 9.851   -46.427 51.837  1.00 55.94 ? 28   ARG A NH2 1 
ATOM   196   N  N   . PRO A  1 26  ? 10.548  -38.620 54.970  1.00 49.18 ? 29   PRO A N   1 
ATOM   197   C  CA  . PRO A  1 26  ? 10.877  -37.432 55.764  1.00 47.75 ? 29   PRO A CA  1 
ATOM   198   C  C   . PRO A  1 26  ? 12.366  -37.418 56.126  1.00 46.86 ? 29   PRO A C   1 
ATOM   199   O  O   . PRO A  1 26  ? 12.944  -38.483 56.371  1.00 45.32 ? 29   PRO A O   1 
ATOM   200   C  CB  . PRO A  1 26  ? 10.018  -37.606 57.029  1.00 49.52 ? 29   PRO A CB  1 
ATOM   201   C  CG  . PRO A  1 26  ? 9.005   -38.669 56.685  1.00 49.20 ? 29   PRO A CG  1 
ATOM   202   C  CD  . PRO A  1 26  ? 9.735   -39.577 55.737  1.00 48.67 ? 29   PRO A CD  1 
ATOM   203   N  N   . GLY A  1 27  ? 12.984  -36.234 56.109  1.00 42.31 ? 30   GLY A N   1 
ATOM   204   C  CA  . GLY A  1 27  ? 14.443  -36.120 56.168  1.00 43.61 ? 30   GLY A CA  1 
ATOM   205   C  C   . GLY A  1 27  ? 15.208  -36.487 54.892  1.00 45.70 ? 30   GLY A C   1 
ATOM   206   O  O   . GLY A  1 27  ? 16.446  -36.598 54.895  1.00 46.89 ? 30   GLY A O   1 
ATOM   207   N  N   . ASP A  1 28  ? 14.485  -36.735 53.806  1.00 42.67 ? 31   ASP A N   1 
ATOM   208   C  CA  . ASP A  1 28  ? 15.134  -36.853 52.506  1.00 41.16 ? 31   ASP A CA  1 
ATOM   209   C  C   . ASP A  1 28  ? 15.464  -35.477 51.993  1.00 36.95 ? 31   ASP A C   1 
ATOM   210   O  O   . ASP A  1 28  ? 14.636  -34.565 52.079  1.00 36.47 ? 31   ASP A O   1 
ATOM   211   C  CB  . ASP A  1 28  ? 14.229  -37.555 51.503  1.00 42.16 ? 31   ASP A CB  1 
ATOM   212   C  CG  . ASP A  1 28  ? 14.386  -39.039 51.550  1.00 42.21 ? 31   ASP A CG  1 
ATOM   213   O  OD1 . ASP A  1 28  ? 15.403  -39.496 52.100  1.00 43.64 ? 31   ASP A OD1 1 
ATOM   214   O  OD2 . ASP A  1 28  ? 13.488  -39.744 51.059  1.00 44.13 ? 31   ASP A OD2 1 
ATOM   215   N  N   . ILE A  1 29  ? 16.670  -35.321 51.459  1.00 32.20 ? 32   ILE A N   1 
ATOM   216   C  CA  . ILE A  1 29  ? 17.151  -33.984 51.127  1.00 30.45 ? 32   ILE A CA  1 
ATOM   217   C  C   . ILE A  1 29  ? 17.057  -33.645 49.633  1.00 28.82 ? 32   ILE A C   1 
ATOM   218   O  O   . ILE A  1 29  ? 17.481  -34.426 48.780  1.00 25.11 ? 32   ILE A O   1 
ATOM   219   C  CB  . ILE A  1 29  ? 18.564  -33.751 51.665  1.00 30.31 ? 32   ILE A CB  1 
ATOM   220   C  CG1 . ILE A  1 29  ? 18.503  -33.565 53.188  1.00 30.09 ? 32   ILE A CG1 1 
ATOM   221   C  CG2 . ILE A  1 29  ? 19.195  -32.553 50.986  1.00 28.77 ? 32   ILE A CG2 1 
ATOM   222   C  CD1 . ILE A  1 29  ? 19.774  -33.945 53.888  1.00 31.70 ? 32   ILE A CD1 1 
ATOM   223   N  N   . ARG A  1 30  ? 16.384  -32.535 49.333  1.00 24.54 ? 33   ARG A N   1 
ATOM   224   C  CA  . ARG A  1 30  ? 16.315  -32.019 47.969  1.00 26.79 ? 33   ARG A CA  1 
ATOM   225   C  C   . ARG A  1 30  ? 16.620  -30.508 47.982  1.00 25.88 ? 33   ARG A C   1 
ATOM   226   O  O   . ARG A  1 30  ? 16.258  -29.806 48.916  1.00 22.75 ? 33   ARG A O   1 
ATOM   227   C  CB  . ARG A  1 30  ? 14.917  -32.266 47.361  1.00 23.88 ? 33   ARG A CB  1 
ATOM   228   C  CG  . ARG A  1 30  ? 14.543  -33.723 47.141  1.00 24.79 ? 33   ARG A CG  1 
ATOM   229   C  CD  . ARG A  1 30  ? 15.585  -34.483 46.323  1.00 24.41 ? 33   ARG A CD  1 
ATOM   230   N  NE  . ARG A  1 30  ? 15.237  -35.892 46.169  1.00 22.75 ? 33   ARG A NE  1 
ATOM   231   C  CZ  . ARG A  1 30  ? 15.637  -36.865 46.985  1.00 27.57 ? 33   ARG A CZ  1 
ATOM   232   N  NH1 . ARG A  1 30  ? 16.412  -36.598 48.033  1.00 27.13 ? 33   ARG A NH1 1 
ATOM   233   N  NH2 . ARG A  1 30  ? 15.244  -38.117 46.764  1.00 26.91 ? 33   ARG A NH2 1 
ATOM   234   N  N   . GLY A  1 31  ? 17.261  -30.022 46.928  1.00 26.11 ? 34   GLY A N   1 
ATOM   235   C  CA  . GLY A  1 31  ? 17.801  -28.673 46.915  1.00 25.05 ? 34   GLY A CA  1 
ATOM   236   C  C   . GLY A  1 31  ? 17.440  -27.890 45.660  1.00 27.04 ? 34   GLY A C   1 
ATOM   237   O  O   . GLY A  1 31  ? 16.424  -28.178 45.007  1.00 24.41 ? 34   GLY A O   1 
ATOM   238   N  N   . PRO A  1 32  ? 18.270  -26.890 45.310  1.00 25.10 ? 35   PRO A N   1 
ATOM   239   C  CA  . PRO A  1 32  ? 17.784  -25.915 44.345  1.00 23.77 ? 35   PRO A CA  1 
ATOM   240   C  C   . PRO A  1 32  ? 18.059  -26.401 42.921  1.00 22.64 ? 35   PRO A C   1 
ATOM   241   O  O   . PRO A  1 32  ? 17.775  -25.681 41.968  1.00 18.99 ? 35   PRO A O   1 
ATOM   242   C  CB  . PRO A  1 32  ? 18.630  -24.683 44.652  1.00 25.23 ? 35   PRO A CB  1 
ATOM   243   C  CG  . PRO A  1 32  ? 19.934  -25.285 45.178  1.00 25.52 ? 35   PRO A CG  1 
ATOM   244   C  CD  . PRO A  1 32  ? 19.470  -26.413 46.027  1.00 23.56 ? 35   PRO A CD  1 
ATOM   245   N  N   . CYS A  1 33  ? 18.653  -27.586 42.793  1.00 20.37 ? 36   CYS A N   1 
ATOM   246   C  CA  . CYS A  1 33  ? 19.017  -28.135 41.483  1.00 21.65 ? 36   CYS A CA  1 
ATOM   247   C  C   . CYS A  1 33  ? 18.061  -29.235 41.067  1.00 22.86 ? 36   CYS A C   1 
ATOM   248   O  O   . CYS A  1 33  ? 18.047  -30.308 41.659  1.00 21.91 ? 36   CYS A O   1 
ATOM   249   C  CB  . CYS A  1 33  ? 20.434  -28.700 41.463  1.00 20.59 ? 36   CYS A CB  1 
ATOM   250   S  SG  . CYS A  1 33  ? 20.914  -29.372 39.827  1.00 23.51 ? 36   CYS A SG  1 
ATOM   251   N  N   . PRO A  1 34  ? 17.318  -29.001 39.982  1.00 23.84 ? 37   PRO A N   1 
ATOM   252   C  CA  . PRO A  1 34  ? 16.414  -30.019 39.469  1.00 20.13 ? 37   PRO A CA  1 
ATOM   253   C  C   . PRO A  1 34  ? 17.195  -31.220 38.946  1.00 20.62 ? 37   PRO A C   1 
ATOM   254   O  O   . PRO A  1 34  ? 16.691  -32.336 38.950  1.00 21.69 ? 37   PRO A O   1 
ATOM   255   C  CB  . PRO A  1 34  ? 15.677  -29.295 38.332  1.00 19.19 ? 37   PRO A CB  1 
ATOM   256   C  CG  . PRO A  1 34  ? 16.597  -28.214 37.899  1.00 23.78 ? 37   PRO A CG  1 
ATOM   257   C  CD  . PRO A  1 34  ? 17.296  -27.766 39.179  1.00 24.02 ? 37   PRO A CD  1 
ATOM   258   N  N   . GLY A  1 35  ? 18.390  -30.994 38.429  1.00 18.46 ? 38   GLY A N   1 
ATOM   259   C  CA  . GLY A  1 35  ? 19.172  -32.106 37.921  1.00 22.70 ? 38   GLY A CA  1 
ATOM   260   C  C   . GLY A  1 35  ? 19.592  -33.111 38.997  1.00 25.76 ? 38   GLY A C   1 
ATOM   261   O  O   . GLY A  1 35  ? 19.289  -34.306 38.898  1.00 26.36 ? 38   GLY A O   1 
ATOM   262   N  N   . LEU A  1 36  ? 20.296  -32.642 40.026  1.00 23.72 ? 39   LEU A N   1 
ATOM   263   C  CA  . LEU A  1 36  ? 20.611  -33.511 41.168  1.00 26.77 ? 39   LEU A CA  1 
ATOM   264   C  C   . LEU A  1 36  ? 19.352  -34.008 41.885  1.00 25.35 ? 39   LEU A C   1 
ATOM   265   O  O   . LEU A  1 36  ? 19.298  -35.135 42.348  1.00 24.77 ? 39   LEU A O   1 
ATOM   266   C  CB  . LEU A  1 36  ? 21.526  -32.783 42.158  1.00 24.93 ? 39   LEU A CB  1 
ATOM   267   C  CG  . LEU A  1 36  ? 22.753  -32.167 41.488  1.00 26.49 ? 39   LEU A CG  1 
ATOM   268   C  CD1 . LEU A  1 36  ? 23.611  -31.470 42.516  1.00 27.72 ? 39   LEU A CD1 1 
ATOM   269   C  CD2 . LEU A  1 36  ? 23.548  -33.221 40.752  1.00 25.69 ? 39   LEU A CD2 1 
ATOM   270   N  N   . ASN A  1 37  ? 18.347  -33.154 42.027  1.00 26.14 ? 40   ASN A N   1 
ATOM   271   C  CA  . ASN A  1 37  ? 17.120  -33.616 42.658  1.00 24.08 ? 40   ASN A CA  1 
ATOM   272   C  C   . ASN A  1 37  ? 16.550  -34.882 41.997  1.00 25.45 ? 40   ASN A C   1 
ATOM   273   O  O   . ASN A  1 37  ? 16.246  -35.873 42.668  1.00 24.31 ? 40   ASN A O   1 
ATOM   274   C  CB  . ASN A  1 37  ? 16.095  -32.495 42.717  1.00 22.68 ? 40   ASN A CB  1 
ATOM   275   C  CG  . ASN A  1 37  ? 16.424  -31.466 43.781  1.00 22.88 ? 40   ASN A CG  1 
ATOM   276   O  OD1 . ASN A  1 37  ? 17.381  -31.623 44.565  1.00 22.75 ? 40   ASN A OD1 1 
ATOM   277   N  ND2 . ASN A  1 37  ? 15.669  -30.387 43.788  1.00 17.17 ? 40   ASN A ND2 1 
ATOM   278   N  N   . THR A  1 38  ? 16.560  -34.898 40.667  1.00 25.12 ? 41   THR A N   1 
ATOM   279   C  CA  . THR A  1 38  ? 15.891  -35.925 39.897  1.00 20.97 ? 41   THR A CA  1 
ATOM   280   C  C   . THR A  1 38  ? 16.717  -37.199 39.943  1.00 25.07 ? 41   THR A C   1 
ATOM   281   O  O   . THR A  1 38  ? 16.182  -38.307 39.883  1.00 26.90 ? 41   THR A O   1 
ATOM   282   C  CB  . THR A  1 38  ? 15.703  -35.444 38.426  1.00 21.74 ? 41   THR A CB  1 
ATOM   283   O  OG1 . THR A  1 38  ? 14.701  -34.417 38.390  1.00 19.26 ? 41   THR A OG1 1 
ATOM   284   C  CG2 . THR A  1 38  ? 15.280  -36.589 37.508  1.00 20.56 ? 41   THR A CG2 1 
ATOM   285   N  N   . LEU A  1 39  ? 18.036  -37.051 39.984  1.00 23.93 ? 42   LEU A N   1 
ATOM   286   C  CA  . LEU A  1 39  ? 18.892  -38.214 40.051  1.00 25.93 ? 42   LEU A CA  1 
ATOM   287   C  C   . LEU A  1 39  ? 18.783  -38.891 41.415  1.00 27.75 ? 42   LEU A C   1 
ATOM   288   O  O   . LEU A  1 39  ? 18.870  -40.109 41.505  1.00 29.98 ? 42   LEU A O   1 
ATOM   289   C  CB  . LEU A  1 39  ? 20.341  -37.852 39.742  1.00 25.34 ? 42   LEU A CB  1 
ATOM   290   C  CG  . LEU A  1 39  ? 20.598  -37.245 38.364  1.00 24.76 ? 42   LEU A CG  1 
ATOM   291   C  CD1 . LEU A  1 39  ? 21.913  -36.488 38.355  1.00 24.70 ? 42   LEU A CD1 1 
ATOM   292   C  CD2 . LEU A  1 39  ? 20.568  -38.312 37.282  1.00 24.93 ? 42   LEU A CD2 1 
ATOM   293   N  N   . ALA A  1 40  ? 18.625  -38.100 42.474  1.00 27.39 ? 43   ALA A N   1 
ATOM   294   C  CA  . ALA A  1 40  ? 18.440  -38.653 43.815  1.00 27.93 ? 43   ALA A CA  1 
ATOM   295   C  C   . ALA A  1 40  ? 17.097  -39.389 43.958  1.00 31.32 ? 43   ALA A C   1 
ATOM   296   O  O   . ALA A  1 40  ? 17.043  -40.462 44.546  1.00 31.07 ? 43   ALA A O   1 
ATOM   297   C  CB  . ALA A  1 40  ? 18.559  -37.579 44.843  1.00 26.64 ? 43   ALA A CB  1 
ATOM   298   N  N   . SER A  1 41  ? 16.042  -38.840 43.352  1.00 32.80 ? 44   SER A N   1 
ATOM   299   C  CA  . SER A  1 41  ? 14.703  -39.417 43.424  1.00 29.81 ? 44   SER A CA  1 
ATOM   300   C  C   . SER A  1 41  ? 14.526  -40.616 42.490  1.00 31.65 ? 44   SER A C   1 
ATOM   301   O  O   . SER A  1 41  ? 13.479  -41.270 42.512  1.00 33.28 ? 44   SER A O   1 
ATOM   302   C  CB  . SER A  1 41  ? 13.640  -38.359 43.114  1.00 28.50 ? 44   SER A CB  1 
ATOM   303   O  OG  . SER A  1 41  ? 13.461  -37.465 44.198  1.00 26.09 ? 44   SER A OG  1 
ATOM   304   N  N   . HIS A  1 42  ? 15.550  -40.905 41.688  1.00 29.69 ? 45   HIS A N   1 
ATOM   305   C  CA  . HIS A  1 42  ? 15.577  -42.096 40.840  1.00 29.19 ? 45   HIS A CA  1 
ATOM   306   C  C   . HIS A  1 42  ? 16.654  -43.096 41.255  1.00 31.75 ? 45   HIS A C   1 
ATOM   307   O  O   . HIS A  1 42  ? 16.831  -44.139 40.615  1.00 32.94 ? 45   HIS A O   1 
ATOM   308   C  CB  . HIS A  1 42  ? 15.791  -41.718 39.367  1.00 27.84 ? 45   HIS A CB  1 
ATOM   309   C  CG  . HIS A  1 42  ? 14.539  -41.295 38.660  1.00 27.65 ? 45   HIS A CG  1 
ATOM   310   N  ND1 . HIS A  1 42  ? 13.712  -42.187 38.005  1.00 27.48 ? 45   HIS A ND1 1 
ATOM   311   C  CD2 . HIS A  1 42  ? 13.957  -40.077 38.533  1.00 26.55 ? 45   HIS A CD2 1 
ATOM   312   C  CE1 . HIS A  1 42  ? 12.667  -41.537 37.519  1.00 27.92 ? 45   HIS A CE1 1 
ATOM   313   N  NE2 . HIS A  1 42  ? 12.799  -40.252 37.812  1.00 27.04 ? 45   HIS A NE2 1 
ATOM   314   N  N   . GLY A  1 43  ? 17.378  -42.784 42.323  1.00 32.35 ? 46   GLY A N   1 
ATOM   315   C  CA  . GLY A  1 43  ? 18.387  -43.702 42.836  1.00 32.17 ? 46   GLY A CA  1 
ATOM   316   C  C   . GLY A  1 43  ? 19.656  -43.703 42.008  1.00 33.75 ? 46   GLY A C   1 
ATOM   317   O  O   . GLY A  1 43  ? 20.486  -44.600 42.140  1.00 32.71 ? 46   GLY A O   1 
ATOM   318   N  N   . TYR A  1 44  ? 19.829  -42.704 41.144  1.00 32.80 ? 47   TYR A N   1 
ATOM   319   C  CA  . TYR A  1 44  ? 21.148  -42.504 40.541  1.00 32.63 ? 47   TYR A CA  1 
ATOM   320   C  C   . TYR A  1 44  ? 22.127  -41.944 41.581  1.00 29.29 ? 47   TYR A C   1 
ATOM   321   O  O   . TYR A  1 44  ? 23.319  -42.235 41.550  1.00 25.64 ? 47   TYR A O   1 
ATOM   322   C  CB  . TYR A  1 44  ? 21.078  -41.600 39.304  1.00 32.15 ? 47   TYR A CB  1 
ATOM   323   C  CG  . TYR A  1 44  ? 20.553  -42.303 38.074  1.00 32.18 ? 47   TYR A CG  1 
ATOM   324   C  CD1 . TYR A  1 44  ? 21.392  -43.085 37.287  1.00 33.07 ? 47   TYR A CD1 1 
ATOM   325   C  CD2 . TYR A  1 44  ? 19.211  -42.203 37.711  1.00 32.02 ? 47   TYR A CD2 1 
ATOM   326   C  CE1 . TYR A  1 44  ? 20.911  -43.751 36.165  1.00 31.35 ? 47   TYR A CE1 1 
ATOM   327   C  CE2 . TYR A  1 44  ? 18.728  -42.834 36.577  1.00 33.83 ? 47   TYR A CE2 1 
ATOM   328   C  CZ  . TYR A  1 44  ? 19.580  -43.608 35.808  1.00 33.75 ? 47   TYR A CZ  1 
ATOM   329   O  OH  . TYR A  1 44  ? 19.069  -44.324 34.740  1.00 34.81 ? 47   TYR A OH  1 
ATOM   330   N  N   . LEU A  1 45  ? 21.607  -41.114 42.474  1.00 28.85 ? 48   LEU A N   1 
ATOM   331   C  CA  . LEU A  1 45  ? 22.340  -40.674 43.653  1.00 32.70 ? 48   LEU A CA  1 
ATOM   332   C  C   . LEU A  1 45  ? 21.703  -41.310 44.889  1.00 34.47 ? 48   LEU A C   1 
ATOM   333   O  O   . LEU A  1 45  ? 20.554  -41.741 44.844  1.00 34.36 ? 48   LEU A O   1 
ATOM   334   C  CB  . LEU A  1 45  ? 22.227  -39.158 43.801  1.00 30.31 ? 48   LEU A CB  1 
ATOM   335   C  CG  . LEU A  1 45  ? 23.067  -38.245 42.923  1.00 33.53 ? 48   LEU A CG  1 
ATOM   336   C  CD1 . LEU A  1 45  ? 22.606  -36.801 43.144  1.00 30.38 ? 48   LEU A CD1 1 
ATOM   337   C  CD2 . LEU A  1 45  ? 24.551  -38.401 43.252  1.00 30.43 ? 48   LEU A CD2 1 
ATOM   338   N  N   . PRO A  1 46  ? 22.381  -41.214 46.037  1.00 35.74 ? 49   PRO A N   1 
ATOM   339   C  CA  . PRO A  1 46  ? 21.693  -41.701 47.223  1.00 36.17 ? 49   PRO A CA  1 
ATOM   340   C  C   . PRO A  1 46  ? 20.388  -40.964 47.485  1.00 37.00 ? 49   PRO A C   1 
ATOM   341   O  O   . PRO A  1 46  ? 20.325  -39.734 47.380  1.00 39.75 ? 49   PRO A O   1 
ATOM   342   C  CB  . PRO A  1 46  ? 22.714  -41.446 48.327  1.00 36.48 ? 49   PRO A CB  1 
ATOM   343   C  CG  . PRO A  1 46  ? 24.039  -41.750 47.622  1.00 33.80 ? 49   PRO A CG  1 
ATOM   344   C  CD  . PRO A  1 46  ? 23.847  -41.252 46.194  1.00 34.17 ? 49   PRO A CD  1 
ATOM   345   N  N   . ARG A  1 47  ? 19.340  -41.714 47.801  1.00 35.22 ? 50   ARG A N   1 
ATOM   346   C  CA  . ARG A  1 47  ? 17.997  -41.158 47.787  1.00 35.95 ? 50   ARG A CA  1 
ATOM   347   C  C   . ARG A  1 47  ? 17.757  -40.116 48.874  1.00 35.25 ? 50   ARG A C   1 
ATOM   348   O  O   . ARG A  1 47  ? 16.833  -39.297 48.777  1.00 36.24 ? 50   ARG A O   1 
ATOM   349   C  CB  . ARG A  1 47  ? 16.952  -42.274 47.851  1.00 36.51 ? 50   ARG A CB  1 
ATOM   350   C  CG  . ARG A  1 47  ? 16.914  -43.118 46.593  1.00 35.63 ? 50   ARG A CG  1 
ATOM   351   C  CD  . ARG A  1 47  ? 15.693  -44.018 46.549  1.00 35.63 ? 50   ARG A CD  1 
ATOM   352   N  NE  . ARG A  1 47  ? 15.719  -44.867 45.358  1.00 36.73 ? 50   ARG A NE  1 
ATOM   353   C  CZ  . ARG A  1 47  ? 15.056  -44.596 44.237  1.00 37.04 ? 50   ARG A CZ  1 
ATOM   354   N  NH1 . ARG A  1 47  ? 14.318  -43.492 44.148  1.00 34.23 ? 50   ARG A NH1 1 
ATOM   355   N  NH2 . ARG A  1 47  ? 15.165  -45.409 43.192  1.00 35.84 ? 50   ARG A NH2 1 
ATOM   356   N  N   . ASN A  1 48  ? 18.602  -40.122 49.897  1.00 33.91 ? 51   ASN A N   1 
ATOM   357   C  CA  . ASN A  1 48  ? 18.454  -39.159 50.993  1.00 32.56 ? 51   ASN A CA  1 
ATOM   358   C  C   . ASN A  1 48  ? 19.126  -37.811 50.714  1.00 29.29 ? 51   ASN A C   1 
ATOM   359   O  O   . ASN A  1 48  ? 18.904  -36.837 51.442  1.00 26.95 ? 51   ASN A O   1 
ATOM   360   C  CB  . ASN A  1 48  ? 18.953  -39.746 52.313  1.00 33.98 ? 51   ASN A CB  1 
ATOM   361   C  CG  . ASN A  1 48  ? 20.468  -39.700 52.437  1.00 36.73 ? 51   ASN A CG  1 
ATOM   362   O  OD1 . ASN A  1 48  ? 21.195  -40.082 51.519  1.00 35.18 ? 51   ASN A OD1 1 
ATOM   363   N  ND2 . ASN A  1 48  ? 20.949  -39.233 53.583  1.00 38.27 ? 51   ASN A ND2 1 
ATOM   364   N  N   . GLY A  1 49  ? 19.902  -37.740 49.634  1.00 25.51 ? 52   GLY A N   1 
ATOM   365   C  CA  . GLY A  1 49  ? 20.383  -36.443 49.140  1.00 27.07 ? 52   GLY A CA  1 
ATOM   366   C  C   . GLY A  1 49  ? 21.765  -36.047 49.642  1.00 27.36 ? 52   GLY A C   1 
ATOM   367   O  O   . GLY A  1 49  ? 22.101  -34.870 49.696  1.00 27.01 ? 52   GLY A O   1 
ATOM   368   N  N   . VAL A  1 50  ? 22.595  -37.037 49.939  1.00 28.39 ? 53   VAL A N   1 
ATOM   369   C  CA  . VAL A  1 50  ? 23.942  -36.785 50.421  1.00 25.59 ? 53   VAL A CA  1 
ATOM   370   C  C   . VAL A  1 50  ? 24.858  -37.696 49.655  1.00 26.11 ? 53   VAL A C   1 
ATOM   371   O  O   . VAL A  1 50  ? 24.533  -38.865 49.450  1.00 28.26 ? 53   VAL A O   1 
ATOM   372   C  CB  . VAL A  1 50  ? 24.067  -37.105 51.916  1.00 26.25 ? 53   VAL A CB  1 
ATOM   373   C  CG1 . VAL A  1 50  ? 25.517  -36.917 52.384  1.00 24.12 ? 53   VAL A CG1 1 
ATOM   374   C  CG2 . VAL A  1 50  ? 23.093  -36.252 52.728  1.00 22.07 ? 53   VAL A CG2 1 
ATOM   375   N  N   . ALA A  1 51  ? 25.909  -37.132 49.075  1.00 27.12 ? 54   ALA A N   1 
ATOM   376   C  CA  . ALA A  1 51  ? 26.674  -37.873 48.076  1.00 29.79 ? 54   ALA A CA  1 
ATOM   377   C  C   . ALA A  1 51  ? 28.122  -37.442 48.038  1.00 27.83 ? 54   ALA A C   1 
ATOM   378   O  O   . ALA A  1 51  ? 28.455  -36.363 48.519  1.00 27.11 ? 54   ALA A O   1 
ATOM   379   C  CB  . ALA A  1 51  ? 26.033  -37.734 46.691  1.00 31.36 ? 54   ALA A CB  1 
ATOM   380   N  N   . THR A  1 52  ? 28.991  -38.321 47.543  1.00 30.56 ? 55   THR A N   1 
ATOM   381   C  CA  . THR A  1 52  ? 30.358  -37.925 47.207  1.00 32.79 ? 55   THR A CA  1 
ATOM   382   C  C   . THR A  1 52  ? 30.436  -37.212 45.857  1.00 32.82 ? 55   THR A C   1 
ATOM   383   O  O   . THR A  1 52  ? 29.564  -37.391 44.997  1.00 34.25 ? 55   THR A O   1 
ATOM   384   C  CB  . THR A  1 52  ? 31.325  -39.121 47.214  1.00 33.91 ? 55   THR A CB  1 
ATOM   385   O  OG1 . THR A  1 52  ? 31.045  -39.979 46.100  1.00 36.26 ? 55   THR A OG1 1 
ATOM   386   C  CG2 . THR A  1 52  ? 31.205  -39.906 48.528  1.00 32.28 ? 55   THR A CG2 1 
ATOM   387   N  N   . PRO A  1 53  ? 31.478  -36.385 45.671  1.00 32.75 ? 56   PRO A N   1 
ATOM   388   C  CA  . PRO A  1 53  ? 31.847  -35.902 44.350  1.00 29.96 ? 56   PRO A CA  1 
ATOM   389   C  C   . PRO A  1 53  ? 31.795  -36.993 43.293  1.00 30.91 ? 56   PRO A C   1 
ATOM   390   O  O   . PRO A  1 53  ? 31.151  -36.820 42.269  1.00 29.80 ? 56   PRO A O   1 
ATOM   391   C  CB  . PRO A  1 53  ? 33.271  -35.429 44.565  1.00 28.69 ? 56   PRO A CB  1 
ATOM   392   C  CG  . PRO A  1 53  ? 33.209  -34.824 45.933  1.00 30.41 ? 56   PRO A CG  1 
ATOM   393   C  CD  . PRO A  1 53  ? 32.230  -35.681 46.725  1.00 30.77 ? 56   PRO A CD  1 
ATOM   394   N  N   . VAL A  1 54  ? 32.411  -38.135 43.569  1.00 31.75 ? 57   VAL A N   1 
ATOM   395   C  CA  . VAL A  1 54  ? 32.522  -39.178 42.574  1.00 31.55 ? 57   VAL A CA  1 
ATOM   396   C  C   . VAL A  1 54  ? 31.145  -39.762 42.260  1.00 32.40 ? 57   VAL A C   1 
ATOM   397   O  O   . VAL A  1 54  ? 30.817  -40.012 41.093  1.00 31.85 ? 57   VAL A O   1 
ATOM   398   C  CB  . VAL A  1 54  ? 33.502  -40.266 43.029  1.00 34.58 ? 57   VAL A CB  1 
ATOM   399   C  CG1 . VAL A  1 54  ? 33.270  -41.574 42.267  1.00 33.66 ? 57   VAL A CG1 1 
ATOM   400   C  CG2 . VAL A  1 54  ? 34.939  -39.769 42.878  1.00 34.07 ? 57   VAL A CG2 1 
ATOM   401   N  N   . GLN A  1 55  ? 30.297  -39.847 43.279  1.00 30.89 ? 58   GLN A N   1 
ATOM   402   C  CA  . GLN A  1 55  ? 28.911  -40.292 43.089  1.00 33.87 ? 58   GLN A CA  1 
ATOM   403   C  C   . GLN A  1 55  ? 28.079  -39.331 42.228  1.00 33.08 ? 58   GLN A C   1 
ATOM   404   O  O   . GLN A  1 55  ? 27.288  -39.782 41.391  1.00 32.83 ? 58   GLN A O   1 
ATOM   405   C  CB  . GLN A  1 55  ? 28.204  -40.499 44.433  1.00 33.38 ? 58   GLN A CB  1 
ATOM   406   C  CG  . GLN A  1 55  ? 28.435  -41.872 45.069  1.00 35.97 ? 58   GLN A CG  1 
ATOM   407   C  CD  . GLN A  1 55  ? 27.930  -41.955 46.502  1.00 37.11 ? 58   GLN A CD  1 
ATOM   408   O  OE1 . GLN A  1 55  ? 27.727  -40.934 47.171  1.00 35.28 ? 58   GLN A OE1 1 
ATOM   409   N  NE2 . GLN A  1 55  ? 27.679  -43.181 46.966  1.00 38.94 ? 58   GLN A NE2 1 
ATOM   410   N  N   . ILE A  1 56  ? 28.137  -38.041 42.569  1.00 29.56 ? 59   ILE A N   1 
ATOM   411   C  CA  . ILE A  1 56  ? 27.481  -36.968 41.810  1.00 26.70 ? 59   ILE A CA  1 
ATOM   412   C  C   . ILE A  1 56  ? 27.910  -36.910 40.345  1.00 25.35 ? 59   ILE A C   1 
ATOM   413   O  O   . ILE A  1 56  ? 27.066  -36.875 39.460  1.00 26.17 ? 59   ILE A O   1 
ATOM   414   C  CB  . ILE A  1 56  ? 27.724  -35.593 42.448  1.00 25.85 ? 59   ILE A CB  1 
ATOM   415   C  CG1 . ILE A  1 56  ? 26.986  -35.497 43.779  1.00 26.20 ? 59   ILE A CG1 1 
ATOM   416   C  CG2 . ILE A  1 56  ? 27.223  -34.475 41.523  1.00 27.01 ? 59   ILE A CG2 1 
ATOM   417   C  CD1 . ILE A  1 56  ? 27.520  -34.412 44.695  1.00 25.76 ? 59   ILE A CD1 1 
ATOM   418   N  N   . ILE A  1 57  ? 29.214  -36.995 40.092  1.00 24.32 ? 60   ILE A N   1 
ATOM   419   C  CA  . ILE A  1 57  ? 29.730  -36.981 38.730  1.00 24.90 ? 60   ILE A CA  1 
ATOM   420   C  C   . ILE A  1 57  ? 29.313  -38.189 37.898  1.00 28.39 ? 60   ILE A C   1 
ATOM   421   O  O   . ILE A  1 57  ? 29.201  -38.094 36.671  1.00 27.48 ? 60   ILE A O   1 
ATOM   422   C  CB  . ILE A  1 57  ? 31.264  -36.812 38.689  1.00 24.88 ? 60   ILE A CB  1 
ATOM   423   C  CG1 . ILE A  1 57  ? 31.633  -35.353 38.984  1.00 26.43 ? 60   ILE A CG1 1 
ATOM   424   C  CG2 . ILE A  1 57  ? 31.815  -37.175 37.311  1.00 22.12 ? 60   ILE A CG2 1 
ATOM   425   C  CD1 . ILE A  1 57  ? 33.033  -35.165 39.489  1.00 25.14 ? 60   ILE A CD1 1 
ATOM   426   N  N   . ASN A  1 58  ? 29.173  -39.349 38.536  1.00 28.23 ? 61   ASN A N   1 
ATOM   427   C  CA  . ASN A  1 58  ? 28.782  -40.546 37.789  1.00 26.92 ? 61   ASN A CA  1 
ATOM   428   C  C   . ASN A  1 58  ? 27.307  -40.452 37.515  1.00 22.88 ? 61   ASN A C   1 
ATOM   429   O  O   . ASN A  1 58  ? 26.855  -40.804 36.431  1.00 23.68 ? 61   ASN A O   1 
ATOM   430   C  CB  . ASN A  1 58  ? 29.068  -41.845 38.560  1.00 29.48 ? 61   ASN A CB  1 
ATOM   431   C  CG  . ASN A  1 58  ? 30.513  -42.297 38.440  1.00 33.51 ? 61   ASN A CG  1 
ATOM   432   O  OD1 . ASN A  1 58  ? 31.078  -42.365 37.343  1.00 33.32 ? 61   ASN A OD1 1 
ATOM   433   N  ND2 . ASN A  1 58  ? 31.109  -42.648 39.573  1.00 34.72 ? 61   ASN A ND2 1 
ATOM   434   N  N   . ALA A  1 59  ? 26.559  -40.028 38.529  1.00 18.69 ? 62   ALA A N   1 
ATOM   435   C  CA  . ALA A  1 59  ? 25.125  -39.782 38.393  1.00 20.53 ? 62   ALA A CA  1 
ATOM   436   C  C   . ALA A  1 59  ? 24.792  -38.880 37.210  1.00 22.88 ? 62   ALA A C   1 
ATOM   437   O  O   . ALA A  1 59  ? 23.954  -39.234 36.389  1.00 24.29 ? 62   ALA A O   1 
ATOM   438   C  CB  . ALA A  1 59  ? 24.540  -39.195 39.692  1.00 18.06 ? 62   ALA A CB  1 
ATOM   439   N  N   . VAL A  1 60  ? 25.346  -37.669 37.186  1.00 23.36 ? 63   VAL A N   1 
ATOM   440   C  CA  . VAL A  1 60  ? 24.931  -36.704 36.162  1.00 27.33 ? 63   VAL A CA  1 
ATOM   441   C  C   . VAL A  1 60  ? 25.274  -37.219 34.756  1.00 25.44 ? 63   VAL A C   1 
ATOM   442   O  O   . VAL A  1 60  ? 24.489  -37.088 33.820  1.00 25.89 ? 63   VAL A O   1 
ATOM   443   C  CB  . VAL A  1 60  ? 25.549  -35.311 36.377  1.00 24.23 ? 63   VAL A CB  1 
ATOM   444   C  CG1 . VAL A  1 60  ? 24.950  -34.673 37.582  1.00 22.10 ? 63   VAL A CG1 1 
ATOM   445   C  CG2 . VAL A  1 60  ? 27.045  -35.431 36.508  1.00 23.98 ? 63   VAL A CG2 1 
ATOM   446   N  N   . GLN A  1 61  ? 26.399  -37.901 34.651  1.00 24.35 ? 64   GLN A N   1 
ATOM   447   C  CA  . GLN A  1 61  ? 26.807  -38.484 33.384  1.00 25.07 ? 64   GLN A CA  1 
ATOM   448   C  C   . GLN A  1 61  ? 25.923  -39.651 32.985  1.00 26.12 ? 64   GLN A C   1 
ATOM   449   O  O   . GLN A  1 61  ? 25.518  -39.748 31.830  1.00 24.65 ? 64   GLN A O   1 
ATOM   450   C  CB  . GLN A  1 61  ? 28.267  -38.924 33.444  1.00 24.45 ? 64   GLN A CB  1 
ATOM   451   C  CG  . GLN A  1 61  ? 29.260  -37.764 33.566  1.00 28.26 ? 64   GLN A CG  1 
ATOM   452   C  CD  . GLN A  1 61  ? 30.688  -38.240 33.347  1.00 28.78 ? 64   GLN A CD  1 
ATOM   453   O  OE1 . GLN A  1 61  ? 31.542  -37.490 32.895  1.00 30.77 ? 64   GLN A OE1 1 
ATOM   454   N  NE2 . GLN A  1 61  ? 30.922  -39.519 33.590  1.00 25.78 ? 64   GLN A NE2 1 
ATOM   455   N  N   . GLU A  1 62  ? 25.614  -40.535 33.931  1.00 28.29 ? 65   GLU A N   1 
ATOM   456   C  CA  . GLU A  1 62  ? 24.924  -41.774 33.586  1.00 33.39 ? 65   GLU A CA  1 
ATOM   457   C  C   . GLU A  1 62  ? 23.452  -41.477 33.412  1.00 31.40 ? 65   GLU A C   1 
ATOM   458   O  O   . GLU A  1 62  ? 22.784  -42.054 32.559  1.00 33.05 ? 65   GLU A O   1 
ATOM   459   C  CB  . GLU A  1 62  ? 25.095  -42.842 34.678  1.00 36.24 ? 65   GLU A CB  1 
ATOM   460   C  CG  . GLU A  1 62  ? 26.461  -43.518 34.701  1.00 42.10 ? 65   GLU A CG  1 
ATOM   461   C  CD  . GLU A  1 62  ? 26.631  -44.523 33.580  1.00 45.74 ? 65   GLU A CD  1 
ATOM   462   O  OE1 . GLU A  1 62  ? 25.604  -45.013 33.051  1.00 47.84 ? 65   GLU A OE1 1 
ATOM   463   O  OE2 . GLU A  1 62  ? 27.795  -44.814 33.220  1.00 48.18 ? 65   GLU A OE2 1 
ATOM   464   N  N   . GLY A  1 63  ? 22.937  -40.641 34.294  1.00 30.64 ? 66   GLY A N   1 
ATOM   465   C  CA  . GLY A  1 63  ? 21.517  -40.361 34.332  1.00 32.32 ? 66   GLY A CA  1 
ATOM   466   C  C   . GLY A  1 63  ? 21.061  -39.400 33.254  1.00 31.88 ? 66   GLY A C   1 
ATOM   467   O  O   . GLY A  1 63  ? 19.924  -39.497 32.782  1.00 35.45 ? 66   GLY A O   1 
ATOM   468   N  N   . LEU A  1 64  ? 21.932  -38.467 32.868  1.00 27.79 ? 67   LEU A N   1 
ATOM   469   C  CA  . LEU A  1 64  ? 21.504  -37.311 32.066  1.00 25.42 ? 67   LEU A CA  1 
ATOM   470   C  C   . LEU A  1 64  ? 22.458  -36.907 30.942  1.00 24.24 ? 67   LEU A C   1 
ATOM   471   O  O   . LEU A  1 64  ? 22.117  -36.061 30.134  1.00 26.45 ? 67   LEU A O   1 
ATOM   472   C  CB  . LEU A  1 64  ? 21.214  -36.109 32.948  1.00 22.84 ? 67   LEU A CB  1 
ATOM   473   C  CG  . LEU A  1 64  ? 20.025  -36.298 33.892  1.00 25.49 ? 67   LEU A CG  1 
ATOM   474   C  CD1 . LEU A  1 64  ? 20.074  -35.256 34.991  1.00 24.82 ? 67   LEU A CD1 1 
ATOM   475   C  CD2 . LEU A  1 64  ? 18.686  -36.279 33.148  1.00 20.77 ? 67   LEU A CD2 1 
ATOM   476   N  N   . ASN A  1 65  ? 23.620  -37.545 30.877  1.00 20.97 ? 68   ASN A N   1 
ATOM   477   C  CA  . ASN A  1 65  ? 24.656  -37.210 29.911  1.00 24.24 ? 68   ASN A CA  1 
ATOM   478   C  C   . ASN A  1 65  ? 25.192  -35.791 30.041  1.00 23.76 ? 68   ASN A C   1 
ATOM   479   O  O   . ASN A  1 65  ? 25.622  -35.194 29.062  1.00 25.34 ? 68   ASN A O   1 
ATOM   480   C  CB  . ASN A  1 65  ? 24.185  -37.477 28.483  1.00 25.90 ? 68   ASN A CB  1 
ATOM   481   C  CG  . ASN A  1 65  ? 25.169  -38.336 27.697  1.00 29.51 ? 68   ASN A CG  1 
ATOM   482   O  OD1 . ASN A  1 65  ? 26.358  -38.425 28.042  1.00 29.95 ? 68   ASN A OD1 1 
ATOM   483   N  ND2 . ASN A  1 65  ? 24.687  -38.951 26.620  1.00 26.98 ? 68   ASN A ND2 1 
ATOM   484   N  N   . PHE A  1 66  ? 25.240  -35.278 31.260  1.00 22.86 ? 69   PHE A N   1 
ATOM   485   C  CA  . PHE A  1 66  ? 26.088  -34.116 31.539  1.00 23.97 ? 69   PHE A CA  1 
ATOM   486   C  C   . PHE A  1 66  ? 27.517  -34.415 31.092  1.00 23.62 ? 69   PHE A C   1 
ATOM   487   O  O   . PHE A  1 66  ? 27.996  -35.520 31.278  1.00 26.89 ? 69   PHE A O   1 
ATOM   488   C  CB  . PHE A  1 66  ? 26.072  -33.795 33.029  1.00 20.43 ? 69   PHE A CB  1 
ATOM   489   C  CG  . PHE A  1 66  ? 26.161  -32.318 33.344  1.00 23.08 ? 69   PHE A CG  1 
ATOM   490   C  CD1 . PHE A  1 66  ? 25.247  -31.422 32.806  1.00 20.09 ? 69   PHE A CD1 1 
ATOM   491   C  CD2 . PHE A  1 66  ? 27.142  -31.834 34.206  1.00 20.53 ? 69   PHE A CD2 1 
ATOM   492   C  CE1 . PHE A  1 66  ? 25.321  -30.074 33.098  1.00 17.36 ? 69   PHE A CE1 1 
ATOM   493   C  CE2 . PHE A  1 66  ? 27.186  -30.486 34.539  1.00 21.28 ? 69   PHE A CE2 1 
ATOM   494   C  CZ  . PHE A  1 66  ? 26.252  -29.607 33.999  1.00 18.36 ? 69   PHE A CZ  1 
ATOM   495   N  N   . ASP A  1 67  ? 28.166  -33.457 30.446  1.00 23.46 ? 70   ASP A N   1 
ATOM   496   C  CA  . ASP A  1 67  ? 29.518  -33.671 29.958  1.00 26.01 ? 70   ASP A CA  1 
ATOM   497   C  C   . ASP A  1 67  ? 30.576  -33.653 31.075  1.00 26.60 ? 70   ASP A C   1 
ATOM   498   O  O   . ASP A  1 67  ? 30.357  -33.080 32.150  1.00 26.73 ? 70   ASP A O   1 
ATOM   499   C  CB  . ASP A  1 67  ? 29.867  -32.732 28.789  1.00 24.68 ? 70   ASP A CB  1 
ATOM   500   C  CG  . ASP A  1 67  ? 30.086  -31.287 29.226  1.00 30.76 ? 70   ASP A CG  1 
ATOM   501   O  OD1 . ASP A  1 67  ? 29.093  -30.531 29.291  1.00 35.86 ? 70   ASP A OD1 1 
ATOM   502   O  OD2 . ASP A  1 67  ? 31.252  -30.874 29.450  1.00 32.92 ? 70   ASP A OD2 1 
ATOM   503   N  N   . ASN A  1 68  ? 31.674  -34.377 30.859  1.00 27.66 ? 71   ASN A N   1 
ATOM   504   C  CA  . ASN A  1 68  ? 32.624  -34.673 31.946  1.00 26.59 ? 71   ASN A CA  1 
ATOM   505   C  C   . ASN A  1 68  ? 33.308  -33.431 32.541  1.00 25.17 ? 71   ASN A C   1 
ATOM   506   O  O   . ASN A  1 68  ? 33.278  -33.233 33.760  1.00 29.26 ? 71   ASN A O   1 
ATOM   507   C  CB  . ASN A  1 68  ? 33.645  -35.744 31.524  1.00 25.61 ? 71   ASN A CB  1 
ATOM   508   C  CG  . ASN A  1 68  ? 34.669  -36.046 32.622  1.00 25.52 ? 71   ASN A CG  1 
ATOM   509   O  OD1 . ASN A  1 68  ? 35.757  -35.478 32.635  1.00 25.25 ? 71   ASN A OD1 1 
ATOM   510   N  ND2 . ASN A  1 68  ? 34.287  -36.880 33.583  1.00 19.66 ? 71   ASN A ND2 1 
ATOM   511   N  N   . GLN A  1 69  ? 33.774  -32.513 31.699  1.00 25.80 ? 72   GLN A N   1 
ATOM   512   C  CA  . GLN A  1 69  ? 34.323  -31.239 32.228  1.00 24.70 ? 72   GLN A CA  1 
ATOM   513   C  C   . GLN A  1 69  ? 33.313  -30.383 33.005  1.00 25.10 ? 72   GLN A C   1 
ATOM   514   O  O   . GLN A  1 69  ? 33.631  -29.846 34.070  1.00 23.75 ? 72   GLN A O   1 
ATOM   515   C  CB  . GLN A  1 69  ? 34.988  -30.398 31.143  1.00 24.74 ? 72   GLN A CB  1 
ATOM   516   C  CG  . GLN A  1 69  ? 36.331  -30.937 30.648  1.00 28.65 ? 72   GLN A CG  1 
ATOM   517   C  CD  . GLN A  1 69  ? 37.289  -29.832 30.194  1.00 31.00 ? 72   GLN A CD  1 
ATOM   518   O  OE1 . GLN A  1 69  ? 37.205  -29.354 29.072  1.00 30.97 ? 72   GLN A OE1 1 
ATOM   519   N  NE2 . GLN A  1 69  ? 38.242  -29.473 31.053  1.00 32.71 ? 72   GLN A NE2 1 
ATOM   520   N  N   . ALA A  1 70  ? 32.093  -30.256 32.495  1.00 22.83 ? 73   ALA A N   1 
ATOM   521   C  CA  . ALA A  1 70  ? 31.109  -29.457 33.206  1.00 23.05 ? 73   ALA A CA  1 
ATOM   522   C  C   . ALA A  1 70  ? 30.750  -30.130 34.538  1.00 24.14 ? 73   ALA A C   1 
ATOM   523   O  O   . ALA A  1 70  ? 30.522  -29.449 35.536  1.00 25.54 ? 73   ALA A O   1 
ATOM   524   C  CB  . ALA A  1 70  ? 29.858  -29.228 32.362  1.00 19.90 ? 73   ALA A CB  1 
ATOM   525   N  N   . ALA A  1 71  ? 30.742  -31.461 34.558  1.00 21.46 ? 74   ALA A N   1 
ATOM   526   C  CA  . ALA A  1 71  ? 30.440  -32.203 35.782  1.00 22.09 ? 74   ALA A CA  1 
ATOM   527   C  C   . ALA A  1 71  ? 31.517  -31.996 36.854  1.00 21.34 ? 74   ALA A C   1 
ATOM   528   O  O   . ALA A  1 71  ? 31.209  -31.828 38.031  1.00 22.48 ? 74   ALA A O   1 
ATOM   529   C  CB  . ALA A  1 71  ? 30.261  -33.716 35.467  1.00 21.88 ? 74   ALA A CB  1 
ATOM   530   N  N   . VAL A  1 72  ? 32.777  -32.079 36.446  1.00 22.26 ? 75   VAL A N   1 
ATOM   531   C  CA  . VAL A  1 72  ? 33.903  -31.838 37.331  1.00 24.22 ? 75   VAL A CA  1 
ATOM   532   C  C   . VAL A  1 72  ? 33.932  -30.399 37.836  1.00 25.41 ? 75   VAL A C   1 
ATOM   533   O  O   . VAL A  1 72  ? 34.080  -30.153 39.041  1.00 24.66 ? 75   VAL A O   1 
ATOM   534   C  CB  . VAL A  1 72  ? 35.242  -32.143 36.600  1.00 27.33 ? 75   VAL A CB  1 
ATOM   535   C  CG1 . VAL A  1 72  ? 36.434  -31.684 37.433  1.00 26.50 ? 75   VAL A CG1 1 
ATOM   536   C  CG2 . VAL A  1 72  ? 35.335  -33.616 36.303  1.00 24.39 ? 75   VAL A CG2 1 
ATOM   537   N  N   . PHE A  1 73  ? 33.750  -29.448 36.928  1.00 24.48 ? 76   PHE A N   1 
ATOM   538   C  CA  . PHE A  1 73  ? 33.736  -28.017 37.305  1.00 25.42 ? 76   PHE A CA  1 
ATOM   539   C  C   . PHE A  1 73  ? 32.657  -27.702 38.353  1.00 25.22 ? 76   PHE A C   1 
ATOM   540   O  O   . PHE A  1 73  ? 32.939  -27.112 39.403  1.00 23.63 ? 76   PHE A O   1 
ATOM   541   C  CB  . PHE A  1 73  ? 33.557  -27.135 36.055  1.00 24.74 ? 76   PHE A CB  1 
ATOM   542   C  CG  . PHE A  1 73  ? 33.460  -25.661 36.349  1.00 28.92 ? 76   PHE A CG  1 
ATOM   543   C  CD1 . PHE A  1 73  ? 34.601  -24.875 36.415  1.00 31.23 ? 76   PHE A CD1 1 
ATOM   544   C  CD2 . PHE A  1 73  ? 32.231  -25.057 36.548  1.00 27.97 ? 76   PHE A CD2 1 
ATOM   545   C  CE1 . PHE A  1 73  ? 34.517  -23.507 36.689  1.00 29.28 ? 76   PHE A CE1 1 
ATOM   546   C  CE2 . PHE A  1 73  ? 32.145  -23.689 36.782  1.00 30.65 ? 76   PHE A CE2 1 
ATOM   547   C  CZ  . PHE A  1 73  ? 33.295  -22.915 36.846  1.00 27.72 ? 76   PHE A CZ  1 
ATOM   548   N  N   . ALA A  1 74  ? 31.426  -28.129 38.079  1.00 23.72 ? 77   ALA A N   1 
ATOM   549   C  CA  . ALA A  1 74  ? 30.305  -27.786 38.941  1.00 22.90 ? 77   ALA A CA  1 
ATOM   550   C  C   . ALA A  1 74  ? 30.362  -28.566 40.264  1.00 22.87 ? 77   ALA A C   1 
ATOM   551   O  O   . ALA A  1 74  ? 29.936  -28.082 41.315  1.00 19.25 ? 77   ALA A O   1 
ATOM   552   C  CB  . ALA A  1 74  ? 28.992  -28.062 38.227  1.00 15.78 ? 77   ALA A CB  1 
ATOM   553   N  N   . THR A  1 75  ? 30.787  -29.818 40.179  1.00 23.38 ? 78   THR A N   1 
ATOM   554   C  CA  . THR A  1 75  ? 30.736  -30.710 41.330  1.00 23.17 ? 78   THR A CA  1 
ATOM   555   C  C   . THR A  1 75  ? 31.796  -30.327 42.366  1.00 22.47 ? 78   THR A C   1 
ATOM   556   O  O   . THR A  1 75  ? 31.490  -30.204 43.551  1.00 25.84 ? 78   THR A O   1 
ATOM   557   C  CB  . THR A  1 75  ? 30.936  -32.165 40.886  1.00 22.97 ? 78   THR A CB  1 
ATOM   558   O  OG1 . THR A  1 75  ? 29.779  -32.574 40.153  1.00 23.27 ? 78   THR A OG1 1 
ATOM   559   C  CG2 . THR A  1 75  ? 31.088  -33.077 42.089  1.00 23.54 ? 78   THR A CG2 1 
ATOM   560   N  N   . TYR A  1 76  ? 33.012  -30.061 41.900  1.00 19.05 ? 79   TYR A N   1 
ATOM   561   C  CA  . TYR A  1 76  ? 34.091  -29.625 42.782  1.00 22.22 ? 79   TYR A CA  1 
ATOM   562   C  C   . TYR A  1 76  ? 34.030  -28.162 43.234  1.00 23.06 ? 79   TYR A C   1 
ATOM   563   O  O   . TYR A  1 76  ? 34.417  -27.847 44.369  1.00 23.18 ? 79   TYR A O   1 
ATOM   564   C  CB  . TYR A  1 76  ? 35.469  -30.025 42.231  1.00 24.42 ? 79   TYR A CB  1 
ATOM   565   C  CG  . TYR A  1 76  ? 35.691  -31.542 42.252  1.00 26.28 ? 79   TYR A CG  1 
ATOM   566   C  CD1 . TYR A  1 76  ? 35.849  -32.242 43.464  1.00 27.13 ? 79   TYR A CD1 1 
ATOM   567   C  CD2 . TYR A  1 76  ? 35.617  -32.279 41.087  1.00 24.43 ? 79   TYR A CD2 1 
ATOM   568   C  CE1 . TYR A  1 76  ? 36.006  -33.634 43.483  1.00 24.32 ? 79   TYR A CE1 1 
ATOM   569   C  CE2 . TYR A  1 76  ? 35.728  -33.652 41.090  1.00 24.96 ? 79   TYR A CE2 1 
ATOM   570   C  CZ  . TYR A  1 76  ? 35.959  -34.326 42.280  1.00 29.06 ? 79   TYR A CZ  1 
ATOM   571   O  OH  . TYR A  1 76  ? 36.052  -35.700 42.244  1.00 27.45 ? 79   TYR A OH  1 
ATOM   572   N  N   . ALA A  1 77  ? 33.392  -27.291 42.451  1.00 22.29 ? 80   ALA A N   1 
ATOM   573   C  CA  . ALA A  1 77  ? 33.064  -25.963 42.997  1.00 21.94 ? 80   ALA A CA  1 
ATOM   574   C  C   . ALA A  1 77  ? 32.121  -26.100 44.177  1.00 21.25 ? 80   ALA A C   1 
ATOM   575   O  O   . ALA A  1 77  ? 32.343  -25.509 45.227  1.00 22.38 ? 80   ALA A O   1 
ATOM   576   C  CB  . ALA A  1 77  ? 32.461  -25.040 41.946  1.00 21.68 ? 80   ALA A CB  1 
ATOM   577   N  N   . ALA A  1 78  ? 31.042  -26.851 43.992  1.00 21.41 ? 81   ALA A N   1 
ATOM   578   C  CA  . ALA A  1 78  ? 30.016  -26.968 45.036  1.00 20.84 ? 81   ALA A CA  1 
ATOM   579   C  C   . ALA A  1 78  ? 30.616  -27.574 46.313  1.00 20.86 ? 81   ALA A C   1 
ATOM   580   O  O   . ALA A  1 78  ? 30.310  -27.153 47.428  1.00 20.89 ? 81   ALA A O   1 
ATOM   581   C  CB  . ALA A  1 78  ? 28.844  -27.824 44.533  1.00 16.62 ? 81   ALA A CB  1 
ATOM   582   N  N   . HIS A  1 79  ? 31.407  -28.624 46.147  1.00 21.99 ? 82   HIS A N   1 
ATOM   583   C  CA  . HIS A  1 79  ? 31.930  -29.348 47.289  1.00 24.82 ? 82   HIS A CA  1 
ATOM   584   C  C   . HIS A  1 79  ? 32.879  -28.447 48.072  1.00 25.12 ? 82   HIS A C   1 
ATOM   585   O  O   . HIS A  1 79  ? 32.762  -28.311 49.298  1.00 24.91 ? 82   HIS A O   1 
ATOM   586   C  CB  . HIS A  1 79  ? 32.654  -30.605 46.821  1.00 26.41 ? 82   HIS A CB  1 
ATOM   587   C  CG  . HIS A  1 79  ? 33.023  -31.528 47.931  1.00 27.30 ? 82   HIS A CG  1 
ATOM   588   N  ND1 . HIS A  1 79  ? 34.266  -32.113 48.029  1.00 31.38 ? 82   HIS A ND1 1 
ATOM   589   C  CD2 . HIS A  1 79  ? 32.318  -31.955 49.002  1.00 29.24 ? 82   HIS A CD2 1 
ATOM   590   C  CE1 . HIS A  1 79  ? 34.313  -32.863 49.116  1.00 30.45 ? 82   HIS A CE1 1 
ATOM   591   N  NE2 . HIS A  1 79  ? 33.144  -32.781 49.725  1.00 32.07 ? 82   HIS A NE2 1 
ATOM   592   N  N   . LEU A  1 80  ? 33.765  -27.780 47.341  1.00 24.29 ? 83   LEU A N   1 
ATOM   593   C  CA  . LEU A  1 80  ? 34.695  -26.815 47.923  1.00 24.75 ? 83   LEU A CA  1 
ATOM   594   C  C   . LEU A  1 80  ? 33.989  -25.857 48.875  1.00 25.68 ? 83   LEU A C   1 
ATOM   595   O  O   . LEU A  1 80  ? 34.434  -25.668 50.014  1.00 28.61 ? 83   LEU A O   1 
ATOM   596   C  CB  . LEU A  1 80  ? 35.472  -26.052 46.829  1.00 21.83 ? 83   LEU A CB  1 
ATOM   597   C  CG  . LEU A  1 80  ? 36.694  -26.774 46.215  1.00 21.90 ? 83   LEU A CG  1 
ATOM   598   C  CD1 . LEU A  1 80  ? 37.234  -26.109 44.943  1.00 18.25 ? 83   LEU A CD1 1 
ATOM   599   C  CD2 . LEU A  1 80  ? 37.842  -26.982 47.235  1.00 19.09 ? 83   LEU A CD2 1 
ATOM   600   N  N   . VAL A  1 81  ? 32.875  -25.279 48.436  1.00 23.11 ? 84   VAL A N   1 
ATOM   601   C  CA  . VAL A  1 81  ? 32.212  -24.229 49.212  1.00 20.77 ? 84   VAL A CA  1 
ATOM   602   C  C   . VAL A  1 81  ? 31.052  -24.707 50.104  1.00 22.42 ? 84   VAL A C   1 
ATOM   603   O  O   . VAL A  1 81  ? 30.608  -23.960 50.976  1.00 23.55 ? 84   VAL A O   1 
ATOM   604   C  CB  . VAL A  1 81  ? 31.668  -23.119 48.298  1.00 21.59 ? 84   VAL A CB  1 
ATOM   605   C  CG1 . VAL A  1 81  ? 32.808  -22.309 47.665  1.00 16.29 ? 84   VAL A CG1 1 
ATOM   606   C  CG2 . VAL A  1 81  ? 30.725  -23.739 47.240  1.00 20.92 ? 84   VAL A CG2 1 
ATOM   607   N  N   . ASP A  1 82  ? 30.467  -25.863 49.791  1.00 22.81 ? 85   ASP A N   1 
ATOM   608   C  CA  . ASP A  1 82  ? 29.225  -26.326 50.452  1.00 23.63 ? 85   ASP A CA  1 
ATOM   609   C  C   . ASP A  1 82  ? 29.341  -27.720 51.101  1.00 24.31 ? 85   ASP A C   1 
ATOM   610   O  O   . ASP A  1 82  ? 28.428  -28.160 51.793  1.00 24.53 ? 85   ASP A O   1 
ATOM   611   C  CB  . ASP A  1 82  ? 28.061  -26.382 49.451  1.00 23.45 ? 85   ASP A CB  1 
ATOM   612   C  CG  . ASP A  1 82  ? 27.563  -24.990 49.030  1.00 25.30 ? 85   ASP A CG  1 
ATOM   613   O  OD1 . ASP A  1 82  ? 27.781  -24.029 49.790  1.00 18.40 ? 85   ASP A OD1 1 
ATOM   614   O  OD2 . ASP A  1 82  ? 26.907  -24.882 47.957  1.00 23.42 ? 85   ASP A OD2 1 
ATOM   615   N  N   . GLY A  1 83  ? 30.387  -28.461 50.763  1.00 21.18 ? 86   GLY A N   1 
ATOM   616   C  CA  . GLY A  1 83  ? 30.519  -29.836 51.240  1.00 25.95 ? 86   GLY A CA  1 
ATOM   617   C  C   . GLY A  1 83  ? 31.567  -29.982 52.343  1.00 24.54 ? 86   GLY A C   1 
ATOM   618   O  O   . GLY A  1 83  ? 32.260  -29.024 52.706  1.00 20.89 ? 86   GLY A O   1 
ATOM   619   N  N   . ASN A  1 84  ? 31.670  -31.189 52.877  1.00 25.86 ? 87   ASN A N   1 
ATOM   620   C  CA  . ASN A  1 84  ? 32.669  -31.497 53.888  1.00 26.70 ? 87   ASN A CA  1 
ATOM   621   C  C   . ASN A  1 84  ? 33.886  -32.147 53.256  1.00 25.25 ? 87   ASN A C   1 
ATOM   622   O  O   . ASN A  1 84  ? 33.806  -33.262 52.764  1.00 24.31 ? 87   ASN A O   1 
ATOM   623   C  CB  . ASN A  1 84  ? 32.071  -32.413 54.954  1.00 26.94 ? 87   ASN A CB  1 
ATOM   624   C  CG  . ASN A  1 84  ? 32.974  -32.559 56.167  1.00 29.21 ? 87   ASN A CG  1 
ATOM   625   O  OD1 . ASN A  1 84  ? 34.176  -32.789 56.030  1.00 29.21 ? 87   ASN A OD1 1 
ATOM   626   N  ND2 . ASN A  1 84  ? 32.404  -32.392 57.358  1.00 29.14 ? 87   ASN A ND2 1 
ATOM   627   N  N   . LEU A  1 85  ? 34.992  -31.410 53.197  1.00 27.13 ? 88   LEU A N   1 
ATOM   628   C  CA  . LEU A  1 85  ? 36.194  -31.878 52.510  1.00 26.16 ? 88   LEU A CA  1 
ATOM   629   C  C   . LEU A  1 85  ? 36.865  -33.069 53.244  1.00 28.51 ? 88   LEU A C   1 
ATOM   630   O  O   . LEU A  1 85  ? 37.565  -33.902 52.630  1.00 25.34 ? 88   LEU A O   1 
ATOM   631   C  CB  . LEU A  1 85  ? 37.192  -30.711 52.327  1.00 26.88 ? 88   LEU A CB  1 
ATOM   632   C  CG  . LEU A  1 85  ? 36.915  -29.537 51.361  1.00 27.42 ? 88   LEU A CG  1 
ATOM   633   C  CD1 . LEU A  1 85  ? 36.029  -29.909 50.151  1.00 28.82 ? 88   LEU A CD1 1 
ATOM   634   C  CD2 . LEU A  1 85  ? 36.302  -28.377 52.079  1.00 29.07 ? 88   LEU A CD2 1 
ATOM   635   N  N   . ILE A  1 86  ? 36.643  -33.160 54.555  1.00 29.42 ? 89   ILE A N   1 
ATOM   636   C  CA  . ILE A  1 86  ? 37.182  -34.278 55.318  1.00 31.17 ? 89   ILE A CA  1 
ATOM   637   C  C   . ILE A  1 86  ? 36.351  -35.557 55.135  1.00 31.28 ? 89   ILE A C   1 
ATOM   638   O  O   . ILE A  1 86  ? 36.896  -36.616 54.822  1.00 34.94 ? 89   ILE A O   1 
ATOM   639   C  CB  . ILE A  1 86  ? 37.395  -33.923 56.809  1.00 31.27 ? 89   ILE A CB  1 
ATOM   640   C  CG1 . ILE A  1 86  ? 38.295  -32.698 56.935  1.00 30.09 ? 89   ILE A CG1 1 
ATOM   641   C  CG2 . ILE A  1 86  ? 38.052  -35.089 57.548  1.00 32.27 ? 89   ILE A CG2 1 
ATOM   642   C  CD1 . ILE A  1 86  ? 39.692  -32.926 56.413  1.00 29.93 ? 89   ILE A CD1 1 
ATOM   643   N  N   . THR A  1 87  ? 35.032  -35.457 55.234  1.00 30.85 ? 90   THR A N   1 
ATOM   644   C  CA  . THR A  1 87  ? 34.203  -36.658 55.076  1.00 31.03 ? 90   THR A CA  1 
ATOM   645   C  C   . THR A  1 87  ? 33.927  -36.972 53.611  1.00 34.03 ? 90   THR A C   1 
ATOM   646   O  O   . THR A  1 87  ? 33.561  -38.107 53.277  1.00 32.87 ? 90   THR A O   1 
ATOM   647   C  CB  . THR A  1 87  ? 32.864  -36.559 55.818  1.00 32.23 ? 90   THR A CB  1 
ATOM   648   O  OG1 . THR A  1 87  ? 32.100  -35.465 55.296  1.00 34.72 ? 90   THR A OG1 1 
ATOM   649   C  CG2 . THR A  1 87  ? 33.082  -36.369 57.317  1.00 31.53 ? 90   THR A CG2 1 
ATOM   650   N  N   . ASP A  1 88  ? 34.090  -35.956 52.755  1.00 33.13 ? 91   ASP A N   1 
ATOM   651   C  CA  . ASP A  1 88  ? 33.914  -36.075 51.298  1.00 31.72 ? 91   ASP A CA  1 
ATOM   652   C  C   . ASP A  1 88  ? 32.447  -36.182 50.922  1.00 30.13 ? 91   ASP A C   1 
ATOM   653   O  O   . ASP A  1 88  ? 32.063  -36.984 50.065  1.00 27.48 ? 91   ASP A O   1 
ATOM   654   C  CB  . ASP A  1 88  ? 34.680  -37.271 50.737  1.00 33.98 ? 91   ASP A CB  1 
ATOM   655   C  CG  . ASP A  1 88  ? 35.007  -37.115 49.255  1.00 35.87 ? 91   ASP A CG  1 
ATOM   656   O  OD1 . ASP A  1 88  ? 35.467  -36.022 48.846  1.00 36.62 ? 91   ASP A OD1 1 
ATOM   657   O  OD2 . ASP A  1 88  ? 34.910  -38.119 48.521  1.00 37.46 ? 91   ASP A OD2 1 
ATOM   658   N  N   . LEU A  1 89  ? 31.614  -35.472 51.672  1.00 29.50 ? 92   LEU A N   1 
ATOM   659   C  CA  . LEU A  1 89  ? 30.177  -35.611 51.522  1.00 30.13 ? 92   LEU A CA  1 
ATOM   660   C  C   . LEU A  1 89  ? 29.570  -34.220 51.351  1.00 27.36 ? 92   LEU A C   1 
ATOM   661   O  O   . LEU A  1 89  ? 30.056  -33.251 51.938  1.00 22.74 ? 92   LEU A O   1 
ATOM   662   C  CB  . LEU A  1 89  ? 29.563  -36.374 52.717  1.00 29.26 ? 92   LEU A CB  1 
ATOM   663   C  CG  . LEU A  1 89  ? 29.831  -37.888 52.813  1.00 31.40 ? 92   LEU A CG  1 
ATOM   664   C  CD1 . LEU A  1 89  ? 29.388  -38.456 54.175  1.00 32.99 ? 92   LEU A CD1 1 
ATOM   665   C  CD2 . LEU A  1 89  ? 29.187  -38.687 51.691  1.00 28.35 ? 92   LEU A CD2 1 
ATOM   666   N  N   . LEU A  1 90  ? 28.599  -34.121 50.443  1.00 26.04 ? 93   LEU A N   1 
ATOM   667   C  CA  . LEU A  1 90  ? 27.889  -32.874 50.165  1.00 22.59 ? 93   LEU A CA  1 
ATOM   668   C  C   . LEU A  1 90  ? 26.386  -33.136 50.164  1.00 23.31 ? 93   LEU A C   1 
ATOM   669   O  O   . LEU A  1 90  ? 25.926  -34.181 49.709  1.00 25.27 ? 93   LEU A O   1 
ATOM   670   C  CB  . LEU A  1 90  ? 28.328  -32.323 48.799  1.00 22.74 ? 93   LEU A CB  1 
ATOM   671   C  CG  . LEU A  1 90  ? 27.448  -31.279 48.098  1.00 20.36 ? 93   LEU A CG  1 
ATOM   672   C  CD1 . LEU A  1 90  ? 27.522  -29.922 48.799  1.00 19.41 ? 93   LEU A CD1 1 
ATOM   673   C  CD2 . LEU A  1 90  ? 27.827  -31.148 46.605  1.00 22.44 ? 93   LEU A CD2 1 
ATOM   674   N  N   . SER A  1 91  ? 25.630  -32.226 50.755  1.00 25.38 ? 94   SER A N   1 
ATOM   675   C  CA  . SER A  1 91  ? 24.183  -32.310 50.748  1.00 25.93 ? 94   SER A CA  1 
ATOM   676   C  C   . SER A  1 91  ? 23.684  -31.554 49.528  1.00 26.55 ? 94   SER A C   1 
ATOM   677   O  O   . SER A  1 91  ? 24.157  -30.453 49.260  1.00 26.11 ? 94   SER A O   1 
ATOM   678   C  CB  . SER A  1 91  ? 23.640  -31.654 52.006  1.00 27.73 ? 94   SER A CB  1 
ATOM   679   O  OG  . SER A  1 91  ? 22.283  -31.265 51.847  1.00 31.77 ? 94   SER A OG  1 
ATOM   680   N  N   . ILE A  1 92  ? 22.788  -32.166 48.749  1.00 26.41 ? 95   ILE A N   1 
ATOM   681   C  CA  . ILE A  1 92  ? 22.294  -31.517 47.545  1.00 24.82 ? 95   ILE A CA  1 
ATOM   682   C  C   . ILE A  1 92  ? 21.249  -30.496 47.944  1.00 25.44 ? 95   ILE A C   1 
ATOM   683   O  O   . ILE A  1 92  ? 20.637  -29.849 47.086  1.00 26.72 ? 95   ILE A O   1 
ATOM   684   C  CB  . ILE A  1 92  ? 21.721  -32.518 46.512  1.00 25.02 ? 95   ILE A CB  1 
ATOM   685   C  CG1 . ILE A  1 92  ? 20.517  -33.259 47.096  1.00 25.25 ? 95   ILE A CG1 1 
ATOM   686   C  CG2 . ILE A  1 92  ? 22.800  -33.519 46.044  1.00 19.21 ? 95   ILE A CG2 1 
ATOM   687   C  CD1 . ILE A  1 92  ? 19.897  -34.178 46.116  1.00 25.38 ? 95   ILE A CD1 1 
ATOM   688   N  N   . GLY A  1 93  ? 21.115  -30.296 49.255  1.00 22.96 ? 96   GLY A N   1 
ATOM   689   C  CA  . GLY A  1 93  ? 20.086  -29.428 49.820  1.00 24.26 ? 96   GLY A CA  1 
ATOM   690   C  C   . GLY A  1 93  ? 20.542  -28.723 51.094  1.00 27.52 ? 96   GLY A C   1 
ATOM   691   O  O   . GLY A  1 93  ? 21.545  -28.016 51.085  1.00 26.09 ? 96   GLY A O   1 
ATOM   692   N  N   . ARG A  1 94  ? 19.786  -28.899 52.184  1.00 27.64 ? 97   ARG A N   1 
ATOM   693   C  CA  . ARG A  1 94  ? 19.999  -28.147 53.420  1.00 29.38 ? 97   ARG A CA  1 
ATOM   694   C  C   . ARG A  1 94  ? 21.286  -28.557 54.142  1.00 32.62 ? 97   ARG A C   1 
ATOM   695   O  O   . ARG A  1 94  ? 21.816  -29.657 53.921  1.00 34.13 ? 97   ARG A O   1 
ATOM   696   C  CB  . ARG A  1 94  ? 18.803  -28.327 54.352  1.00 29.04 ? 97   ARG A CB  1 
ATOM   697   C  CG  . ARG A  1 94  ? 18.560  -29.771 54.759  1.00 27.67 ? 97   ARG A CG  1 
ATOM   698   C  CD  . ARG A  1 94  ? 17.619  -29.858 55.943  1.00 28.65 ? 97   ARG A CD  1 
ATOM   699   N  NE  . ARG A  1 94  ? 17.702  -31.180 56.566  1.00 30.95 ? 97   ARG A NE  1 
ATOM   700   C  CZ  . ARG A  1 94  ? 16.984  -32.221 56.167  1.00 30.12 ? 97   ARG A CZ  1 
ATOM   701   N  NH1 . ARG A  1 94  ? 16.112  -32.079 55.177  1.00 32.31 ? 97   ARG A NH1 1 
ATOM   702   N  NH2 . ARG A  1 94  ? 17.119  -33.395 56.760  1.00 31.06 ? 97   ARG A NH2 1 
ATOM   703   N  N   . LYS A  1 95  ? 21.766  -27.701 55.040  1.00 34.25 ? 98   LYS A N   1 
ATOM   704   C  CA  . LYS A  1 95  ? 22.827  -28.118 55.959  1.00 34.96 ? 98   LYS A CA  1 
ATOM   705   C  C   . LYS A  1 95  ? 22.341  -29.335 56.731  1.00 34.29 ? 98   LYS A C   1 
ATOM   706   O  O   . LYS A  1 95  ? 21.265  -29.303 57.325  1.00 35.36 ? 98   LYS A O   1 
ATOM   707   C  CB  . LYS A  1 95  ? 23.199  -26.991 56.941  1.00 34.28 ? 98   LYS A CB  1 
ATOM   708   C  CG  . LYS A  1 95  ? 24.435  -27.318 57.812  1.00 34.14 ? 98   LYS A CG  1 
ATOM   709   C  CD  . LYS A  1 95  ? 24.789  -26.203 58.819  1.00 33.94 ? 98   LYS A CD  1 
ATOM   710   C  CE  . LYS A  1 95  ? 26.261  -26.275 59.243  1.00 36.92 ? 98   LYS A CE  1 
ATOM   711   N  NZ  . LYS A  1 95  ? 26.911  -27.603 58.907  1.00 34.73 ? 98   LYS A NZ  1 
ATOM   712   N  N   . THR A  1 96  ? 23.105  -30.419 56.696  1.00 34.19 ? 99   THR A N   1 
ATOM   713   C  CA  . THR A  1 96  ? 22.748  -31.587 57.486  1.00 35.24 ? 99   THR A CA  1 
ATOM   714   C  C   . THR A  1 96  ? 23.939  -32.136 58.266  1.00 38.84 ? 99   THR A C   1 
ATOM   715   O  O   . THR A  1 96  ? 25.058  -32.222 57.742  1.00 40.15 ? 99   THR A O   1 
ATOM   716   C  CB  . THR A  1 96  ? 22.125  -32.705 56.644  1.00 33.75 ? 99   THR A CB  1 
ATOM   717   O  OG1 . THR A  1 96  ? 21.737  -33.780 57.504  1.00 35.01 ? 99   THR A OG1 1 
ATOM   718   C  CG2 . THR A  1 96  ? 23.107  -33.228 55.617  1.00 30.51 ? 99   THR A CG2 1 
ATOM   719   N  N   . ARG A  1 97  ? 23.705  -32.457 59.535  1.00 37.42 ? 100  ARG A N   1 
ATOM   720   C  CA  . ARG A  1 97  ? 24.732  -33.070 60.359  1.00 36.40 ? 100  ARG A CA  1 
ATOM   721   C  C   . ARG A  1 97  ? 25.136  -34.405 59.733  1.00 34.82 ? 100  ARG A C   1 
ATOM   722   O  O   . ARG A  1 97  ? 26.198  -34.936 60.019  1.00 34.57 ? 100  ARG A O   1 
ATOM   723   C  CB  . ARG A  1 97  ? 24.226  -33.250 61.800  1.00 37.15 ? 100  ARG A CB  1 
ATOM   724   C  CG  . ARG A  1 97  ? 23.129  -34.310 61.940  1.00 38.79 ? 100  ARG A CG  1 
ATOM   725   C  CD  . ARG A  1 97  ? 22.038  -33.916 62.950  1.00 40.98 ? 100  ARG A CD  1 
ATOM   726   N  NE  . ARG A  1 97  ? 20.831  -34.732 62.770  1.00 43.65 ? 100  ARG A NE  1 
ATOM   727   C  CZ  . ARG A  1 97  ? 20.680  -35.975 63.225  1.00 42.61 ? 100  ARG A CZ  1 
ATOM   728   N  NH1 . ARG A  1 97  ? 21.632  -36.535 63.967  1.00 40.20 ? 100  ARG A NH1 1 
ATOM   729   N  NH2 . ARG A  1 97  ? 19.545  -36.632 62.999  1.00 41.93 ? 100  ARG A NH2 1 
ATOM   730   N  N   . LEU A  1 98  ? 24.354  -34.886 58.772  1.00 35.14 ? 101  LEU A N   1 
ATOM   731   C  CA  . LEU A  1 98  ? 24.734  -36.115 58.079  1.00 31.64 ? 101  LEU A CA  1 
ATOM   732   C  C   . LEU A  1 98  ? 25.976  -36.023 57.180  1.00 31.29 ? 101  LEU A C   1 
ATOM   733   O  O   . LEU A  1 98  ? 26.438  -37.050 56.668  1.00 29.73 ? 101  LEU A O   1 
ATOM   734   C  CB  . LEU A  1 98  ? 23.563  -36.709 57.295  1.00 33.93 ? 101  LEU A CB  1 
ATOM   735   C  CG  . LEU A  1 98  ? 22.189  -36.810 57.967  1.00 36.66 ? 101  LEU A CG  1 
ATOM   736   C  CD1 . LEU A  1 98  ? 21.131  -37.166 56.919  1.00 36.12 ? 101  LEU A CD1 1 
ATOM   737   C  CD2 . LEU A  1 98  ? 22.177  -37.816 59.121  1.00 36.57 ? 101  LEU A CD2 1 
ATOM   738   N  N   . THR A  1 99  ? 26.533  -34.828 56.981  1.00 29.88 ? 102  THR A N   1 
ATOM   739   C  CA  . THR A  1 99  ? 27.841  -34.746 56.288  1.00 29.67 ? 102  THR A CA  1 
ATOM   740   C  C   . THR A  1 99  ? 29.047  -34.918 57.206  1.00 31.74 ? 102  THR A C   1 
ATOM   741   O  O   . THR A  1 99  ? 30.192  -34.984 56.748  1.00 32.19 ? 102  THR A O   1 
ATOM   742   C  CB  . THR A  1 99  ? 28.025  -33.492 55.375  1.00 29.38 ? 102  THR A CB  1 
ATOM   743   O  OG1 . THR A  1 99  ? 27.565  -32.296 56.036  1.00 24.88 ? 102  THR A OG1 1 
ATOM   744   C  CG2 . THR A  1 99  ? 27.259  -33.678 54.057  1.00 32.08 ? 102  THR A CG2 1 
ATOM   745   N  N   . GLY A  1 100 ? 28.784  -35.019 58.504  1.00 34.18 ? 103  GLY A N   1 
ATOM   746   C  CA  . GLY A  1 100 ? 29.834  -35.344 59.458  1.00 32.64 ? 103  GLY A CA  1 
ATOM   747   C  C   . GLY A  1 100 ? 30.305  -34.145 60.250  1.00 33.08 ? 103  GLY A C   1 
ATOM   748   O  O   . GLY A  1 100 ? 29.651  -33.093 60.238  1.00 31.21 ? 103  GLY A O   1 
ATOM   749   N  N   . PRO A  1 101 ? 31.412  -34.321 61.000  1.00 33.78 ? 104  PRO A N   1 
ATOM   750   C  CA  . PRO A  1 101 ? 31.890  -33.298 61.910  1.00 36.63 ? 104  PRO A CA  1 
ATOM   751   C  C   . PRO A  1 101 ? 32.296  -32.055 61.133  1.00 35.97 ? 104  PRO A C   1 
ATOM   752   O  O   . PRO A  1 101 ? 33.041  -32.144 60.154  1.00 35.11 ? 104  PRO A O   1 
ATOM   753   C  CB  . PRO A  1 101 ? 33.126  -33.953 62.555  1.00 35.58 ? 104  PRO A CB  1 
ATOM   754   C  CG  . PRO A  1 101 ? 32.842  -35.403 62.492  1.00 35.09 ? 104  PRO A CG  1 
ATOM   755   C  CD  . PRO A  1 101 ? 32.167  -35.579 61.159  1.00 35.82 ? 104  PRO A CD  1 
ATOM   756   N  N   . ASP A  1 102 ? 31.768  -30.917 61.546  1.00 34.33 ? 105  ASP A N   1 
ATOM   757   C  CA  . ASP A  1 102 ? 31.983  -29.690 60.808  1.00 38.32 ? 105  ASP A CA  1 
ATOM   758   C  C   . ASP A  1 102 ? 33.417  -29.221 60.990  1.00 39.56 ? 105  ASP A C   1 
ATOM   759   O  O   . ASP A  1 102 ? 34.031  -29.485 62.020  1.00 42.43 ? 105  ASP A O   1 
ATOM   760   C  CB  . ASP A  1 102 ? 31.002  -28.612 61.273  1.00 39.02 ? 105  ASP A CB  1 
ATOM   761   C  CG  . ASP A  1 102 ? 29.727  -28.582 60.445  1.00 39.92 ? 105  ASP A CG  1 
ATOM   762   O  OD1 . ASP A  1 102 ? 29.706  -29.120 59.316  1.00 37.28 ? 105  ASP A OD1 1 
ATOM   763   O  OD2 . ASP A  1 102 ? 28.740  -27.987 60.923  1.00 45.54 ? 105  ASP A OD2 1 
ATOM   764   N  N   . PRO A  1 103 ? 33.982  -28.587 59.955  1.00 42.11 ? 106  PRO A N   1 
ATOM   765   C  CA  . PRO A  1 103 ? 35.233  -27.879 60.136  1.00 39.29 ? 106  PRO A CA  1 
ATOM   766   C  C   . PRO A  1 103 ? 34.878  -26.598 60.861  1.00 41.42 ? 106  PRO A C   1 
ATOM   767   O  O   . PRO A  1 103 ? 33.695  -26.372 61.134  1.00 40.33 ? 106  PRO A O   1 
ATOM   768   C  CB  . PRO A  1 103 ? 35.646  -27.573 58.703  1.00 40.99 ? 106  PRO A CB  1 
ATOM   769   C  CG  . PRO A  1 103 ? 34.344  -27.355 57.997  1.00 38.99 ? 106  PRO A CG  1 
ATOM   770   C  CD  . PRO A  1 103 ? 33.329  -28.233 58.677  1.00 40.25 ? 106  PRO A CD  1 
ATOM   771   N  N   . PRO A  1 104 ? 35.881  -25.765 61.179  1.00 41.15 ? 107  PRO A N   1 
ATOM   772   C  CA  . PRO A  1 104 ? 35.616  -24.576 61.982  1.00 42.56 ? 107  PRO A CA  1 
ATOM   773   C  C   . PRO A  1 104 ? 35.239  -23.381 61.122  1.00 45.15 ? 107  PRO A C   1 
ATOM   774   O  O   . PRO A  1 104 ? 35.509  -23.375 59.925  1.00 47.83 ? 107  PRO A O   1 
ATOM   775   C  CB  . PRO A  1 104 ? 36.953  -24.317 62.677  1.00 44.25 ? 107  PRO A CB  1 
ATOM   776   C  CG  . PRO A  1 104 ? 37.972  -24.922 61.764  1.00 44.27 ? 107  PRO A CG  1 
ATOM   777   C  CD  . PRO A  1 104 ? 37.310  -26.114 61.138  1.00 40.73 ? 107  PRO A CD  1 
ATOM   778   N  N   . PRO A  1 105 ? 34.662  -22.348 61.742  1.00 43.81 ? 108  PRO A N   1 
ATOM   779   C  CA  . PRO A  1 105 ? 34.237  -21.132 61.076  1.00 43.34 ? 108  PRO A CA  1 
ATOM   780   C  C   . PRO A  1 105 ? 35.418  -20.406 60.425  1.00 42.20 ? 108  PRO A C   1 
ATOM   781   O  O   . PRO A  1 105 ? 36.539  -20.523 60.896  1.00 44.41 ? 108  PRO A O   1 
ATOM   782   C  CB  . PRO A  1 105 ? 33.668  -20.285 62.223  1.00 43.85 ? 108  PRO A CB  1 
ATOM   783   C  CG  . PRO A  1 105 ? 33.525  -21.217 63.381  1.00 44.15 ? 108  PRO A CG  1 
ATOM   784   C  CD  . PRO A  1 105 ? 34.568  -22.240 63.205  1.00 44.39 ? 108  PRO A CD  1 
ATOM   785   N  N   . PRO A  1 106 ? 35.160  -19.632 59.361  1.00 40.11 ? 109  PRO A N   1 
ATOM   786   C  CA  . PRO A  1 106 ? 33.830  -19.256 58.935  1.00 38.92 ? 109  PRO A CA  1 
ATOM   787   C  C   . PRO A  1 106 ? 33.267  -20.162 57.843  1.00 38.74 ? 109  PRO A C   1 
ATOM   788   O  O   . PRO A  1 106 ? 32.314  -19.775 57.169  1.00 40.35 ? 109  PRO A O   1 
ATOM   789   C  CB  . PRO A  1 106 ? 34.042  -17.842 58.381  1.00 39.61 ? 109  PRO A CB  1 
ATOM   790   C  CG  . PRO A  1 106 ? 35.519  -17.809 57.944  1.00 36.99 ? 109  PRO A CG  1 
ATOM   791   C  CD  . PRO A  1 106 ? 36.192  -19.034 58.496  1.00 38.56 ? 109  PRO A CD  1 
ATOM   792   N  N   . ALA A  1 107 ? 33.858  -21.340 57.654  1.00 38.74 ? 110  ALA A N   1 
ATOM   793   C  CA  . ALA A  1 107 ? 33.286  -22.352 56.756  1.00 36.82 ? 110  ALA A CA  1 
ATOM   794   C  C   . ALA A  1 107 ? 31.941  -22.838 57.259  1.00 37.81 ? 110  ALA A C   1 
ATOM   795   O  O   . ALA A  1 107 ? 31.810  -23.184 58.432  1.00 38.72 ? 110  ALA A O   1 
ATOM   796   C  CB  . ALA A  1 107 ? 34.217  -23.514 56.623  1.00 38.30 ? 110  ALA A CB  1 
ATOM   797   N  N   . SER A  1 108 ? 30.971  -22.962 56.355  1.00 36.05 ? 111  SER A N   1 
ATOM   798   C  CA  . SER A  1 108 ? 29.605  -23.231 56.766  1.00 35.99 ? 111  SER A CA  1 
ATOM   799   C  C   . SER A  1 108 ? 29.150  -24.672 56.499  1.00 33.73 ? 111  SER A C   1 
ATOM   800   O  O   . SER A  1 108 ? 28.336  -25.221 57.248  1.00 34.05 ? 111  SER A O   1 
ATOM   801   C  CB  . SER A  1 108 ? 28.649  -22.225 56.129  1.00 36.70 ? 111  SER A CB  1 
ATOM   802   O  OG  . SER A  1 108 ? 29.101  -21.875 54.836  1.00 39.67 ? 111  SER A OG  1 
ATOM   803   N  N   . VAL A  1 109 ? 29.720  -25.302 55.478  1.00 29.66 ? 112  VAL A N   1 
ATOM   804   C  CA  . VAL A  1 109 ? 29.203  -26.576 54.980  1.00 26.05 ? 112  VAL A CA  1 
ATOM   805   C  C   . VAL A  1 109 ? 27.669  -26.615 54.994  1.00 28.11 ? 112  VAL A C   1 
ATOM   806   O  O   . VAL A  1 109 ? 27.041  -27.547 55.529  1.00 25.68 ? 112  VAL A O   1 
ATOM   807   C  CB  . VAL A  1 109 ? 29.769  -27.756 55.760  1.00 28.64 ? 112  VAL A CB  1 
ATOM   808   C  CG1 . VAL A  1 109 ? 29.242  -29.049 55.195  1.00 26.75 ? 112  VAL A CG1 1 
ATOM   809   C  CG2 . VAL A  1 109 ? 31.297  -27.727 55.726  1.00 27.24 ? 112  VAL A CG2 1 
ATOM   810   N  N   . GLY A  1 110 ? 27.073  -25.604 54.367  1.00 26.42 ? 113  GLY A N   1 
ATOM   811   C  CA  . GLY A  1 110 ? 25.626  -25.434 54.369  1.00 26.50 ? 113  GLY A CA  1 
ATOM   812   C  C   . GLY A  1 110 ? 24.903  -26.199 53.268  1.00 26.56 ? 113  GLY A C   1 
ATOM   813   O  O   . GLY A  1 110 ? 23.691  -26.051 53.108  1.00 26.83 ? 113  GLY A O   1 
ATOM   814   N  N   . GLY A  1 111 ? 25.626  -27.049 52.538  1.00 22.28 ? 114  GLY A N   1 
ATOM   815   C  CA  . GLY A  1 111 ? 25.021  -27.792 51.442  1.00 24.02 ? 114  GLY A CA  1 
ATOM   816   C  C   . GLY A  1 111 ? 24.590  -26.882 50.297  1.00 23.15 ? 114  GLY A C   1 
ATOM   817   O  O   . GLY A  1 111 ? 24.727  -25.669 50.382  1.00 22.42 ? 114  GLY A O   1 
ATOM   818   N  N   . LEU A  1 112 ? 24.004  -27.460 49.251  1.00 23.22 ? 115  LEU A N   1 
ATOM   819   C  CA  . LEU A  1 112 ? 23.617  -26.681 48.072  1.00 24.44 ? 115  LEU A CA  1 
ATOM   820   C  C   . LEU A  1 112 ? 22.695  -25.499 48.366  1.00 23.01 ? 115  LEU A C   1 
ATOM   821   O  O   . LEU A  1 112 ? 22.759  -24.487 47.670  1.00 26.75 ? 115  LEU A O   1 
ATOM   822   C  CB  . LEU A  1 112 ? 23.024  -27.570 46.981  1.00 23.67 ? 115  LEU A CB  1 
ATOM   823   C  CG  . LEU A  1 112 ? 23.996  -28.503 46.279  1.00 23.37 ? 115  LEU A CG  1 
ATOM   824   C  CD1 . LEU A  1 112 ? 23.437  -28.953 44.925  1.00 22.16 ? 115  LEU A CD1 1 
ATOM   825   C  CD2 . LEU A  1 112 ? 25.320  -27.787 46.101  1.00 22.71 ? 115  LEU A CD2 1 
ATOM   826   N  N   . ASN A  1 113 ? 21.853  -25.611 49.393  1.00 22.18 ? 116  ASN A N   1 
ATOM   827   C  CA  . ASN A  1 113 ? 20.938  -24.516 49.777  1.00 21.47 ? 116  ASN A CA  1 
ATOM   828   C  C   . ASN A  1 113 ? 21.662  -23.242 50.238  1.00 24.47 ? 116  ASN A C   1 
ATOM   829   O  O   . ASN A  1 113 ? 21.013  -22.219 50.479  1.00 24.52 ? 116  ASN A O   1 
ATOM   830   C  CB  . ASN A  1 113 ? 20.019  -24.934 50.930  1.00 23.87 ? 116  ASN A CB  1 
ATOM   831   C  CG  . ASN A  1 113 ? 18.938  -25.932 50.523  1.00 25.39 ? 116  ASN A CG  1 
ATOM   832   O  OD1 . ASN A  1 113 ? 18.032  -26.212 51.316  1.00 27.97 ? 116  ASN A OD1 1 
ATOM   833   N  ND2 . ASN A  1 113 ? 19.078  -26.543 49.360  1.00 20.71 ? 116  ASN A ND2 1 
ATOM   834   N  N   . GLU A  1 114 ? 22.962  -23.341 50.510  1.00 24.98 ? 117  GLU A N   1 
ATOM   835   C  CA  . GLU A  1 114 ? 23.709  -22.210 51.087  1.00 26.77 ? 117  GLU A CA  1 
ATOM   836   C  C   . GLU A  1 114 ? 23.748  -21.027 50.115  1.00 25.48 ? 117  GLU A C   1 
ATOM   837   O  O   . GLU A  1 114 ? 24.446  -21.062 49.094  1.00 26.42 ? 117  GLU A O   1 
ATOM   838   C  CB  . GLU A  1 114 ? 25.140  -22.639 51.463  1.00 28.71 ? 117  GLU A CB  1 
ATOM   839   C  CG  . GLU A  1 114 ? 26.001  -21.575 52.164  1.00 30.87 ? 117  GLU A CG  1 
ATOM   840   C  CD  . GLU A  1 114 ? 25.600  -21.332 53.614  1.00 32.19 ? 117  GLU A CD  1 
ATOM   841   O  OE1 . GLU A  1 114 ? 24.935  -22.196 54.213  1.00 33.33 ? 117  GLU A OE1 1 
ATOM   842   O  OE2 . GLU A  1 114 ? 25.944  -20.267 54.160  1.00 34.80 ? 117  GLU A OE2 1 
ATOM   843   N  N   . HIS A  1 115 ? 22.986  -19.989 50.426  1.00 24.40 ? 118  HIS A N   1 
ATOM   844   C  CA  . HIS A  1 115 ? 22.947  -18.797 49.586  1.00 23.76 ? 118  HIS A CA  1 
ATOM   845   C  C   . HIS A  1 115 ? 24.297  -18.105 49.428  1.00 22.59 ? 118  HIS A C   1 
ATOM   846   O  O   . HIS A  1 115 ? 24.918  -17.714 50.410  1.00 24.39 ? 118  HIS A O   1 
ATOM   847   C  CB  . HIS A  1 115 ? 21.947  -17.778 50.116  1.00 20.72 ? 118  HIS A CB  1 
ATOM   848   C  CG  . HIS A  1 115 ? 21.872  -16.543 49.269  1.00 23.89 ? 118  HIS A CG  1 
ATOM   849   N  ND1 . HIS A  1 115 ? 21.518  -16.582 47.935  1.00 20.55 ? 118  HIS A ND1 1 
ATOM   850   C  CD2 . HIS A  1 115 ? 22.172  -15.249 49.542  1.00 22.25 ? 118  HIS A CD2 1 
ATOM   851   C  CE1 . HIS A  1 115 ? 21.563  -15.359 47.437  1.00 24.60 ? 118  HIS A CE1 1 
ATOM   852   N  NE2 . HIS A  1 115 ? 21.964  -14.533 48.388  1.00 22.05 ? 118  HIS A NE2 1 
ATOM   853   N  N   . GLY A  1 116 ? 24.731  -17.915 48.189  1.00 23.42 ? 119  GLY A N   1 
ATOM   854   C  CA  . GLY A  1 116 ? 25.794  -16.959 47.907  1.00 19.26 ? 119  GLY A CA  1 
ATOM   855   C  C   . GLY A  1 116 ? 27.103  -17.652 47.635  1.00 22.87 ? 119  GLY A C   1 
ATOM   856   O  O   . GLY A  1 116 ? 28.067  -17.021 47.217  1.00 23.62 ? 119  GLY A O   1 
ATOM   857   N  N   . THR A  1 117 ? 27.151  -18.957 47.875  1.00 23.00 ? 120  THR A N   1 
ATOM   858   C  CA  . THR A  1 117 ? 28.339  -19.725 47.522  1.00 23.85 ? 120  THR A CA  1 
ATOM   859   C  C   . THR A  1 117 ? 28.252  -20.337 46.107  1.00 25.15 ? 120  THR A C   1 
ATOM   860   O  O   . THR A  1 117 ? 28.979  -19.926 45.195  1.00 25.17 ? 120  THR A O   1 
ATOM   861   C  CB  . THR A  1 117 ? 28.608  -20.813 48.564  1.00 26.04 ? 120  THR A CB  1 
ATOM   862   O  OG1 . THR A  1 117 ? 27.487  -21.704 48.618  1.00 23.16 ? 120  THR A OG1 1 
ATOM   863   C  CG2 . THR A  1 117 ? 28.844  -20.174 49.963  1.00 24.05 ? 120  THR A CG2 1 
ATOM   864   N  N   . PHE A  1 118 ? 27.356  -21.305 45.923  1.00 24.81 ? 121  PHE A N   1 
ATOM   865   C  CA  . PHE A  1 118 ? 26.945  -21.725 44.582  1.00 24.12 ? 121  PHE A CA  1 
ATOM   866   C  C   . PHE A  1 118 ? 25.546  -21.191 44.261  1.00 25.55 ? 121  PHE A C   1 
ATOM   867   O  O   . PHE A  1 118 ? 25.378  -20.475 43.281  1.00 28.81 ? 121  PHE A O   1 
ATOM   868   C  CB  . PHE A  1 118 ? 26.985  -23.250 44.461  1.00 21.73 ? 121  PHE A CB  1 
ATOM   869   C  CG  . PHE A  1 118 ? 27.086  -23.760 43.044  1.00 20.56 ? 121  PHE A CG  1 
ATOM   870   C  CD1 . PHE A  1 118 ? 26.074  -23.511 42.125  1.00 20.87 ? 121  PHE A CD1 1 
ATOM   871   C  CD2 . PHE A  1 118 ? 28.093  -24.646 42.692  1.00 20.85 ? 121  PHE A CD2 1 
ATOM   872   C  CE1 . PHE A  1 118 ? 26.129  -24.028 40.834  1.00 19.01 ? 121  PHE A CE1 1 
ATOM   873   C  CE2 . PHE A  1 118 ? 28.147  -25.192 41.424  1.00 19.48 ? 121  PHE A CE2 1 
ATOM   874   C  CZ  . PHE A  1 118 ? 27.185  -24.839 40.466  1.00 22.61 ? 121  PHE A CZ  1 
ATOM   875   N  N   . GLU A  1 119 ? 24.564  -21.494 45.115  1.00 24.95 ? 122  GLU A N   1 
ATOM   876   C  CA  . GLU A  1 119 ? 23.187  -21.001 44.961  1.00 23.45 ? 122  GLU A CA  1 
ATOM   877   C  C   . GLU A  1 119 ? 23.145  -19.484 44.858  1.00 24.00 ? 122  GLU A C   1 
ATOM   878   O  O   . GLU A  1 119 ? 23.887  -18.782 45.558  1.00 23.86 ? 122  GLU A O   1 
ATOM   879   C  CB  . GLU A  1 119 ? 22.306  -21.447 46.144  1.00 25.35 ? 122  GLU A CB  1 
ATOM   880   C  CG  . GLU A  1 119 ? 20.778  -21.327 45.933  1.00 24.90 ? 122  GLU A CG  1 
ATOM   881   C  CD  . GLU A  1 119 ? 20.270  -19.884 45.967  1.00 26.48 ? 122  GLU A CD  1 
ATOM   882   O  OE1 . GLU A  1 119 ? 20.809  -19.072 46.751  1.00 28.05 ? 122  GLU A OE1 1 
ATOM   883   O  OE2 . GLU A  1 119 ? 19.336  -19.559 45.203  1.00 22.94 ? 122  GLU A OE2 1 
ATOM   884   N  N   . GLY A  1 120 ? 22.213  -18.973 44.054  1.00 22.34 ? 123  GLY A N   1 
ATOM   885   C  CA  . GLY A  1 120 ? 22.111  -17.534 43.858  1.00 20.79 ? 123  GLY A CA  1 
ATOM   886   C  C   . GLY A  1 120 ? 20.801  -17.049 43.268  1.00 21.33 ? 123  GLY A C   1 
ATOM   887   O  O   . GLY A  1 120 ? 19.895  -17.842 42.951  1.00 18.90 ? 123  GLY A O   1 
ATOM   888   N  N   . ASP A  1 121 ? 20.733  -15.737 43.081  1.00 15.31 ? 124  ASP A N   1 
ATOM   889   C  CA  . ASP A  1 121 ? 19.489  -15.059 42.783  1.00 19.28 ? 124  ASP A CA  1 
ATOM   890   C  C   . ASP A  1 121 ? 19.070  -15.283 41.319  1.00 20.50 ? 124  ASP A C   1 
ATOM   891   O  O   . ASP A  1 121 ? 19.879  -15.729 40.473  1.00 15.80 ? 124  ASP A O   1 
ATOM   892   C  CB  . ASP A  1 121 ? 19.634  -13.547 43.057  1.00 17.41 ? 124  ASP A CB  1 
ATOM   893   C  CG  . ASP A  1 121 ? 19.829  -13.229 44.544  1.00 17.07 ? 124  ASP A CG  1 
ATOM   894   O  OD1 . ASP A  1 121 ? 19.415  -14.053 45.386  1.00 19.19 ? 124  ASP A OD1 1 
ATOM   895   O  OD2 . ASP A  1 121 ? 20.321  -12.119 44.871  1.00 14.45 ? 124  ASP A OD2 1 
ATOM   896   N  N   . ALA A  1 122 ? 17.841  -14.863 41.020  1.00 18.12 ? 125  ALA A N   1 
ATOM   897   C  CA  . ALA A  1 122 ? 17.305  -14.909 39.670  1.00 16.97 ? 125  ALA A CA  1 
ATOM   898   C  C   . ALA A  1 122 ? 17.248  -16.359 39.159  1.00 17.31 ? 125  ALA A C   1 
ATOM   899   O  O   . ALA A  1 122 ? 17.558  -16.633 38.001  1.00 19.82 ? 125  ALA A O   1 
ATOM   900   C  CB  . ALA A  1 122 ? 18.146  -14.028 38.742  1.00 13.75 ? 125  ALA A CB  1 
ATOM   901   N  N   . SER A  1 123 ? 16.920  -17.299 40.031  1.00 16.19 ? 126  SER A N   1 
ATOM   902   C  CA  . SER A  1 123 ? 16.646  -18.660 39.555  1.00 20.74 ? 126  SER A CA  1 
ATOM   903   C  C   . SER A  1 123 ? 15.334  -18.751 38.767  1.00 20.14 ? 126  SER A C   1 
ATOM   904   O  O   . SER A  1 123 ? 14.441  -17.918 38.919  1.00 22.37 ? 126  SER A O   1 
ATOM   905   C  CB  . SER A  1 123 ? 16.646  -19.646 40.717  1.00 18.34 ? 126  SER A CB  1 
ATOM   906   O  OG  . SER A  1 123 ? 17.832  -19.518 41.457  1.00 21.11 ? 126  SER A OG  1 
ATOM   907   N  N   . MET A  1 124 ? 15.198  -19.772 37.934  1.00 22.69 ? 127  MET A N   1 
ATOM   908   C  CA  . MET A  1 124 ? 14.001  -19.857 37.094  1.00 22.32 ? 127  MET A CA  1 
ATOM   909   C  C   . MET A  1 124 ? 12.749  -20.207 37.899  1.00 22.90 ? 127  MET A C   1 
ATOM   910   O  O   . MET A  1 124 ? 11.687  -19.577 37.745  1.00 21.73 ? 127  MET A O   1 
ATOM   911   C  CB  . MET A  1 124 ? 14.219  -20.818 35.932  1.00 21.33 ? 127  MET A CB  1 
ATOM   912   C  CG  . MET A  1 124 ? 15.109  -20.236 34.807  1.00 21.37 ? 127  MET A CG  1 
ATOM   913   S  SD  . MET A  1 124 ? 15.465  -21.478 33.520  1.00 26.91 ? 127  MET A SD  1 
ATOM   914   C  CE  . MET A  1 124 ? 16.352  -22.694 34.501  1.00 16.73 ? 127  MET A CE  1 
ATOM   915   N  N   . THR A  1 125 ? 12.916  -21.130 38.835  1.00 19.63 ? 128  THR A N   1 
ATOM   916   C  CA  . THR A  1 125 ? 11.795  -21.749 39.504  1.00 22.19 ? 128  THR A CA  1 
ATOM   917   C  C   . THR A  1 125 ? 11.937  -21.725 41.022  1.00 23.98 ? 128  THR A C   1 
ATOM   918   O  O   . THR A  1 125 ? 11.129  -22.324 41.717  1.00 27.90 ? 128  THR A O   1 
ATOM   919   C  CB  . THR A  1 125 ? 11.575  -23.208 39.017  1.00 22.12 ? 128  THR A CB  1 
ATOM   920   O  OG1 . THR A  1 125 ? 12.659  -24.047 39.451  1.00 19.27 ? 128  THR A OG1 1 
ATOM   921   C  CG2 . THR A  1 125 ? 11.472  -23.253 37.478  1.00 18.74 ? 128  THR A CG2 1 
ATOM   922   N  N   . ARG A  1 126 ? 12.973  -21.054 41.528  1.00 24.27 ? 129  ARG A N   1 
ATOM   923   C  CA  . ARG A  1 126 ? 13.193  -20.907 42.970  1.00 20.43 ? 129  ARG A CA  1 
ATOM   924   C  C   . ARG A  1 126 ? 13.260  -19.429 43.299  1.00 21.67 ? 129  ARG A C   1 
ATOM   925   O  O   . ARG A  1 126 ? 13.884  -18.664 42.553  1.00 19.58 ? 129  ARG A O   1 
ATOM   926   C  CB  . ARG A  1 126 ? 14.528  -21.547 43.368  1.00 23.49 ? 129  ARG A CB  1 
ATOM   927   C  CG  . ARG A  1 126 ? 14.448  -22.995 43.846  1.00 20.26 ? 129  ARG A CG  1 
ATOM   928   C  CD  . ARG A  1 126 ? 13.939  -23.951 42.744  1.00 21.89 ? 129  ARG A CD  1 
ATOM   929   N  NE  . ARG A  1 126 ? 13.788  -25.324 43.252  1.00 22.93 ? 129  ARG A NE  1 
ATOM   930   C  CZ  . ARG A  1 126 ? 13.231  -26.336 42.584  1.00 23.93 ? 129  ARG A CZ  1 
ATOM   931   N  NH1 . ARG A  1 126 ? 12.780  -26.171 41.338  1.00 22.36 ? 129  ARG A NH1 1 
ATOM   932   N  NH2 . ARG A  1 126 ? 13.088  -27.513 43.185  1.00 25.76 ? 129  ARG A NH2 1 
ATOM   933   N  N   . GLY A  1 127 ? 12.642  -19.027 44.413  1.00 16.81 ? 130  GLY A N   1 
ATOM   934   C  CA  . GLY A  1 127 ? 12.747  -17.658 44.888  1.00 18.29 ? 130  GLY A CA  1 
ATOM   935   C  C   . GLY A  1 127 ? 14.144  -17.267 45.355  1.00 19.46 ? 130  GLY A C   1 
ATOM   936   O  O   . GLY A  1 127 ? 14.931  -18.118 45.779  1.00 21.15 ? 130  GLY A O   1 
ATOM   937   N  N   . ASP A  1 128 ? 14.435  -15.971 45.343  1.00 17.23 ? 131  ASP A N   1 
ATOM   938   C  CA  . ASP A  1 128 ? 15.708  -15.491 45.864  1.00 19.35 ? 131  ASP A CA  1 
ATOM   939   C  C   . ASP A  1 128 ? 15.730  -15.726 47.385  1.00 20.38 ? 131  ASP A C   1 
ATOM   940   O  O   . ASP A  1 128 ? 14.712  -15.592 48.045  1.00 21.95 ? 131  ASP A O   1 
ATOM   941   C  CB  . ASP A  1 128 ? 15.880  -13.995 45.579  1.00 18.65 ? 131  ASP A CB  1 
ATOM   942   C  CG  . ASP A  1 128 ? 15.993  -13.667 44.096  1.00 21.22 ? 131  ASP A CG  1 
ATOM   943   O  OD1 . ASP A  1 128 ? 16.095  -14.590 43.261  1.00 22.52 ? 131  ASP A OD1 1 
ATOM   944   O  OD2 . ASP A  1 128 ? 16.073  -12.455 43.775  1.00 24.44 ? 131  ASP A OD2 1 
ATOM   945   N  N   . ALA A  1 129 ? 16.905  -15.982 47.946  1.00 23.56 ? 132  ALA A N   1 
ATOM   946   C  CA  . ALA A  1 129 ? 17.042  -16.188 49.401  1.00 26.45 ? 132  ALA A CA  1 
ATOM   947   C  C   . ALA A  1 129 ? 16.490  -15.043 50.243  1.00 27.62 ? 132  ALA A C   1 
ATOM   948   O  O   . ALA A  1 129 ? 15.880  -15.276 51.276  1.00 30.37 ? 132  ALA A O   1 
ATOM   949   C  CB  . ALA A  1 129 ? 18.488  -16.478 49.785  1.00 20.89 ? 132  ALA A CB  1 
ATOM   950   N  N   . PHE A  1 130 ? 16.643  -13.813 49.769  1.00 29.72 ? 133  PHE A N   1 
ATOM   951   C  CA  . PHE A  1 130 ? 16.100  -12.666 50.489  1.00 27.75 ? 133  PHE A CA  1 
ATOM   952   C  C   . PHE A  1 130 ? 14.639  -12.871 50.918  1.00 31.19 ? 133  PHE A C   1 
ATOM   953   O  O   . PHE A  1 130 ? 14.258  -12.554 52.054  1.00 34.14 ? 133  PHE A O   1 
ATOM   954   C  CB  . PHE A  1 130 ? 16.253  -11.393 49.663  1.00 27.44 ? 133  PHE A CB  1 
ATOM   955   C  CG  . PHE A  1 130 ? 15.726  -10.167 50.347  1.00 30.39 ? 133  PHE A CG  1 
ATOM   956   C  CD1 . PHE A  1 130 ? 16.447  -9.561  51.368  1.00 30.88 ? 133  PHE A CD1 1 
ATOM   957   C  CD2 . PHE A  1 130 ? 14.479  -9.644  50.008  1.00 31.00 ? 133  PHE A CD2 1 
ATOM   958   C  CE1 . PHE A  1 130 ? 15.921  -8.458  52.054  1.00 31.96 ? 133  PHE A CE1 1 
ATOM   959   C  CE2 . PHE A  1 130 ? 13.950  -8.550  50.687  1.00 28.66 ? 133  PHE A CE2 1 
ATOM   960   C  CZ  . PHE A  1 130 ? 14.674  -7.956  51.706  1.00 30.24 ? 133  PHE A CZ  1 
ATOM   961   N  N   . PHE A  1 131 ? 13.828  -13.431 50.027  1.00 31.04 ? 134  PHE A N   1 
ATOM   962   C  CA  . PHE A  1 131 ? 12.412  -13.633 50.317  1.00 31.53 ? 134  PHE A CA  1 
ATOM   963   C  C   . PHE A  1 131 ? 12.136  -14.812 51.260  1.00 34.14 ? 134  PHE A C   1 
ATOM   964   O  O   . PHE A  1 131 ? 11.034  -14.934 51.782  1.00 33.26 ? 134  PHE A O   1 
ATOM   965   C  CB  . PHE A  1 131 ? 11.603  -13.800 49.023  1.00 25.88 ? 134  PHE A CB  1 
ATOM   966   C  CG  . PHE A  1 131 ? 11.780  -12.674 48.054  1.00 24.92 ? 134  PHE A CG  1 
ATOM   967   C  CD1 . PHE A  1 131 ? 11.565  -11.356 48.453  1.00 23.32 ? 134  PHE A CD1 1 
ATOM   968   C  CD2 . PHE A  1 131 ? 12.222  -12.919 46.754  1.00 22.15 ? 134  PHE A CD2 1 
ATOM   969   C  CE1 . PHE A  1 131 ? 11.753  -10.299 47.569  1.00 23.93 ? 134  PHE A CE1 1 
ATOM   970   C  CE2 . PHE A  1 131 ? 12.412  -11.863 45.862  1.00 22.54 ? 134  PHE A CE2 1 
ATOM   971   C  CZ  . PHE A  1 131 ? 12.152  -10.553 46.262  1.00 24.45 ? 134  PHE A CZ  1 
ATOM   972   N  N   . GLY A  1 132 ? 13.086  -15.732 51.400  1.00 35.23 ? 135  GLY A N   1 
ATOM   973   C  CA  . GLY A  1 132 ? 13.071  -16.621 52.564  1.00 36.10 ? 135  GLY A CA  1 
ATOM   974   C  C   . GLY A  1 132 ? 13.073  -18.119 52.326  1.00 34.33 ? 135  GLY A C   1 
ATOM   975   O  O   . GLY A  1 132 ? 13.091  -18.897 53.275  1.00 38.12 ? 135  GLY A O   1 
ATOM   976   N  N   . ASN A  1 133 ? 13.070  -18.532 51.067  1.00 34.03 ? 136  ASN A N   1 
ATOM   977   C  CA  . ASN A  1 133 ? 13.170  -19.954 50.708  1.00 32.78 ? 136  ASN A CA  1 
ATOM   978   C  C   . ASN A  1 133 ? 13.774  -20.029 49.329  1.00 31.05 ? 136  ASN A C   1 
ATOM   979   O  O   . ASN A  1 133 ? 13.107  -19.701 48.338  1.00 26.52 ? 136  ASN A O   1 
ATOM   980   C  CB  . ASN A  1 133 ? 11.788  -20.623 50.675  1.00 33.19 ? 136  ASN A CB  1 
ATOM   981   C  CG  . ASN A  1 133 ? 11.858  -22.136 50.411  1.00 35.98 ? 136  ASN A CG  1 
ATOM   982   O  OD1 . ASN A  1 133 ? 12.666  -22.623 49.613  1.00 37.92 ? 136  ASN A OD1 1 
ATOM   983   N  ND2 . ASN A  1 133 ? 10.963  -22.875 51.044  1.00 34.72 ? 136  ASN A ND2 1 
ATOM   984   N  N   . ASN A  1 134 ? 15.043  -20.421 49.268  1.00 28.64 ? 137  ASN A N   1 
ATOM   985   C  CA  . ASN A  1 134 ? 15.812  -20.347 48.035  1.00 26.10 ? 137  ASN A CA  1 
ATOM   986   C  C   . ASN A  1 134 ? 15.914  -21.694 47.344  1.00 24.97 ? 137  ASN A C   1 
ATOM   987   O  O   . ASN A  1 134 ? 16.678  -21.853 46.387  1.00 22.56 ? 137  ASN A O   1 
ATOM   988   C  CB  . ASN A  1 134 ? 17.212  -19.826 48.331  1.00 27.32 ? 137  ASN A CB  1 
ATOM   989   C  CG  . ASN A  1 134 ? 18.044  -20.825 49.104  1.00 29.01 ? 137  ASN A CG  1 
ATOM   990   O  OD1 . ASN A  1 134 ? 17.510  -21.793 49.659  1.00 23.64 ? 137  ASN A OD1 1 
ATOM   991   N  ND2 . ASN A  1 134 ? 19.368  -20.631 49.100  1.00 28.04 ? 137  ASN A ND2 1 
ATOM   992   N  N   . HIS A  1 135 ? 15.123  -22.665 47.793  1.00 23.68 ? 138  HIS A N   1 
ATOM   993   C  CA  . HIS A  1 135 ? 15.352  -24.045 47.355  1.00 24.55 ? 138  HIS A CA  1 
ATOM   994   C  C   . HIS A  1 135 ? 14.110  -24.811 46.881  1.00 23.51 ? 138  HIS A C   1 
ATOM   995   O  O   . HIS A  1 135 ? 14.225  -25.711 46.052  1.00 25.86 ? 138  HIS A O   1 
ATOM   996   C  CB  . HIS A  1 135 ? 16.106  -24.845 48.429  1.00 27.64 ? 138  HIS A CB  1 
ATOM   997   C  CG  . HIS A  1 135 ? 15.503  -24.737 49.797  1.00 29.57 ? 138  HIS A CG  1 
ATOM   998   N  ND1 . HIS A  1 135 ? 14.697  -25.718 50.331  1.00 33.63 ? 138  HIS A ND1 1 
ATOM   999   C  CD2 . HIS A  1 135 ? 15.556  -23.749 50.721  1.00 32.61 ? 138  HIS A CD2 1 
ATOM   1000  C  CE1 . HIS A  1 135 ? 14.318  -25.361 51.547  1.00 34.82 ? 138  HIS A CE1 1 
ATOM   1001  N  NE2 . HIS A  1 135 ? 14.782  -24.148 51.787  1.00 34.66 ? 138  HIS A NE2 1 
ATOM   1002  N  N   . ASP A  1 136 ? 12.949  -24.520 47.461  1.00 25.72 ? 139  ASP A N   1 
ATOM   1003  C  CA  . ASP A  1 136 ? 11.718  -25.235 47.108  1.00 27.48 ? 139  ASP A CA  1 
ATOM   1004  C  C   . ASP A  1 136 ? 11.253  -24.796 45.721  1.00 26.03 ? 139  ASP A C   1 
ATOM   1005  O  O   . ASP A  1 136 ? 11.325  -23.616 45.395  1.00 24.75 ? 139  ASP A O   1 
ATOM   1006  C  CB  . ASP A  1 136 ? 10.588  -24.943 48.117  1.00 28.16 ? 139  ASP A CB  1 
ATOM   1007  C  CG  . ASP A  1 136 ? 10.754  -25.689 49.435  1.00 31.06 ? 139  ASP A CG  1 
ATOM   1008  O  OD1 . ASP A  1 136 ? 11.439  -26.726 49.480  1.00 28.47 ? 139  ASP A OD1 1 
ATOM   1009  O  OD2 . ASP A  1 136 ? 10.181  -25.225 50.438  1.00 34.69 ? 139  ASP A OD2 1 
ATOM   1010  N  N   . PHE A  1 137 ? 10.637  -25.721 44.987  1.00 25.38 ? 140  PHE A N   1 
ATOM   1011  C  CA  . PHE A  1 137 ? 9.874   -25.385 43.792  1.00 24.09 ? 140  PHE A CA  1 
ATOM   1012  C  C   . PHE A  1 137 ? 8.884   -24.313 44.122  1.00 24.10 ? 140  PHE A C   1 
ATOM   1013  O  O   . PHE A  1 137 ? 8.186   -24.364 45.147  1.00 26.13 ? 140  PHE A O   1 
ATOM   1014  C  CB  . PHE A  1 137 ? 9.130   -26.609 43.234  1.00 25.31 ? 140  PHE A CB  1 
ATOM   1015  C  CG  . PHE A  1 137 ? 8.251   -26.305 42.040  1.00 24.95 ? 140  PHE A CG  1 
ATOM   1016  C  CD1 . PHE A  1 137 ? 8.759   -26.363 40.747  1.00 21.60 ? 140  PHE A CD1 1 
ATOM   1017  C  CD2 . PHE A  1 137 ? 6.908   -25.954 42.213  1.00 25.60 ? 140  PHE A CD2 1 
ATOM   1018  C  CE1 . PHE A  1 137 ? 7.936   -26.119 39.639  1.00 21.47 ? 140  PHE A CE1 1 
ATOM   1019  C  CE2 . PHE A  1 137 ? 6.078   -25.729 41.107  1.00 23.19 ? 140  PHE A CE2 1 
ATOM   1020  C  CZ  . PHE A  1 137 ? 6.598   -25.794 39.819  1.00 18.09 ? 140  PHE A CZ  1 
ATOM   1021  N  N   . ASN A  1 138 ? 8.859   -23.302 43.272  1.00 23.69 ? 141  ASN A N   1 
ATOM   1022  C  CA  . ASN A  1 138 ? 7.956   -22.185 43.465  1.00 23.14 ? 141  ASN A CA  1 
ATOM   1023  C  C   . ASN A  1 138 ? 7.015   -22.062 42.266  1.00 22.80 ? 141  ASN A C   1 
ATOM   1024  O  O   . ASN A  1 138 ? 7.461   -21.946 41.122  1.00 19.84 ? 141  ASN A O   1 
ATOM   1025  C  CB  . ASN A  1 138 ? 8.775   -20.919 43.663  1.00 23.67 ? 141  ASN A CB  1 
ATOM   1026  C  CG  . ASN A  1 138 ? 7.946   -19.676 43.635  1.00 25.37 ? 141  ASN A CG  1 
ATOM   1027  O  OD1 . ASN A  1 138 ? 7.106   -19.500 42.761  1.00 26.57 ? 141  ASN A OD1 1 
ATOM   1028  N  ND2 . ASN A  1 138 ? 8.216   -18.769 44.566  1.00 31.29 ? 141  ASN A ND2 1 
ATOM   1029  N  N   . GLU A  1 139 ? 5.717   -22.131 42.535  1.00 23.17 ? 142  GLU A N   1 
ATOM   1030  C  CA  . GLU A  1 139 ? 4.727   -22.414 41.507  1.00 26.58 ? 142  GLU A CA  1 
ATOM   1031  C  C   . GLU A  1 139 ? 4.457   -21.190 40.624  1.00 27.21 ? 142  GLU A C   1 
ATOM   1032  O  O   . GLU A  1 139 ? 4.289   -21.315 39.407  1.00 26.96 ? 142  GLU A O   1 
ATOM   1033  C  CB  . GLU A  1 139 ? 3.415   -22.911 42.141  1.00 29.39 ? 142  GLU A CB  1 
ATOM   1034  C  CG  . GLU A  1 139 ? 2.216   -22.895 41.169  1.00 31.68 ? 142  GLU A CG  1 
ATOM   1035  C  CD  . GLU A  1 139 ? 2.377   -23.892 40.032  1.00 33.09 ? 142  GLU A CD  1 
ATOM   1036  O  OE1 . GLU A  1 139 ? 2.824   -25.037 40.288  1.00 33.00 ? 142  GLU A OE1 1 
ATOM   1037  O  OE2 . GLU A  1 139 ? 2.082   -23.527 38.875  1.00 35.66 ? 142  GLU A OE2 1 
ATOM   1038  N  N   . THR A  1 140 ? 4.417   -20.015 41.241  1.00 23.66 ? 143  THR A N   1 
ATOM   1039  C  CA  . THR A  1 140 ? 4.255   -18.749 40.520  1.00 23.91 ? 143  THR A CA  1 
ATOM   1040  C  C   . THR A  1 140 ? 5.337   -18.509 39.457  1.00 26.28 ? 143  THR A C   1 
ATOM   1041  O  O   . THR A  1 140 ? 5.042   -18.037 38.360  1.00 25.08 ? 143  THR A O   1 
ATOM   1042  C  CB  . THR A  1 140 ? 4.258   -17.590 41.520  1.00 25.19 ? 143  THR A CB  1 
ATOM   1043  O  OG1 . THR A  1 140 ? 3.091   -17.685 42.340  1.00 29.28 ? 143  THR A OG1 1 
ATOM   1044  C  CG2 . THR A  1 140 ? 4.272   -16.239 40.832  1.00 22.59 ? 143  THR A CG2 1 
ATOM   1045  N  N   . LEU A  1 141 ? 6.585   -18.849 39.790  1.00 23.32 ? 144  LEU A N   1 
ATOM   1046  C  CA  . LEU A  1 141 ? 7.704   -18.686 38.872  1.00 21.68 ? 144  LEU A CA  1 
ATOM   1047  C  C   . LEU A  1 141 ? 7.641   -19.733 37.726  1.00 21.66 ? 144  LEU A C   1 
ATOM   1048  O  O   . LEU A  1 141 ? 7.945   -19.435 36.563  1.00 18.89 ? 144  LEU A O   1 
ATOM   1049  C  CB  . LEU A  1 141 ? 9.031   -18.823 39.637  1.00 20.07 ? 144  LEU A CB  1 
ATOM   1050  C  CG  . LEU A  1 141 ? 9.388   -17.737 40.655  1.00 23.06 ? 144  LEU A CG  1 
ATOM   1051  C  CD1 . LEU A  1 141 ? 10.669  -18.101 41.375  1.00 20.49 ? 144  LEU A CD1 1 
ATOM   1052  C  CD2 . LEU A  1 141 ? 9.502   -16.356 39.957  1.00 20.27 ? 144  LEU A CD2 1 
ATOM   1053  N  N   . PHE A  1 142 ? 7.275   -20.959 38.069  1.00 16.04 ? 145  PHE A N   1 
ATOM   1054  C  CA  . PHE A  1 142 ? 7.078   -21.967 37.067  1.00 19.19 ? 145  PHE A CA  1 
ATOM   1055  C  C   . PHE A  1 142 ? 5.959   -21.593 36.083  1.00 19.52 ? 145  PHE A C   1 
ATOM   1056  O  O   . PHE A  1 142 ? 6.077   -21.826 34.882  1.00 17.63 ? 145  PHE A O   1 
ATOM   1057  C  CB  . PHE A  1 142 ? 6.782   -23.320 37.687  1.00 17.44 ? 145  PHE A CB  1 
ATOM   1058  C  CG  . PHE A  1 142 ? 6.733   -24.416 36.671  1.00 21.72 ? 145  PHE A CG  1 
ATOM   1059  C  CD1 . PHE A  1 142 ? 7.911   -24.896 36.107  1.00 19.58 ? 145  PHE A CD1 1 
ATOM   1060  C  CD2 . PHE A  1 142 ? 5.520   -24.862 36.174  1.00 17.26 ? 145  PHE A CD2 1 
ATOM   1061  C  CE1 . PHE A  1 142 ? 7.873   -25.847 35.111  1.00 20.42 ? 145  PHE A CE1 1 
ATOM   1062  C  CE2 . PHE A  1 142 ? 5.474   -25.837 35.193  1.00 20.70 ? 145  PHE A CE2 1 
ATOM   1063  C  CZ  . PHE A  1 142 ? 6.650   -26.316 34.644  1.00 19.65 ? 145  PHE A CZ  1 
ATOM   1064  N  N   . GLU A  1 143 ? 4.892   -20.998 36.604  1.00 20.09 ? 146  GLU A N   1 
ATOM   1065  C  CA  . GLU A  1 143 ? 3.844   -20.416 35.782  1.00 22.50 ? 146  GLU A CA  1 
ATOM   1066  C  C   . GLU A  1 143 ? 4.354   -19.323 34.837  1.00 24.19 ? 146  GLU A C   1 
ATOM   1067  O  O   . GLU A  1 143 ? 3.879   -19.193 33.709  1.00 22.98 ? 146  GLU A O   1 
ATOM   1068  C  CB  . GLU A  1 143 ? 2.725   -19.865 36.673  1.00 25.20 ? 146  GLU A CB  1 
ATOM   1069  C  CG  . GLU A  1 143 ? 1.550   -19.290 35.893  1.00 30.26 ? 146  GLU A CG  1 
ATOM   1070  C  CD  . GLU A  1 143 ? 0.880   -20.316 34.976  1.00 32.52 ? 146  GLU A CD  1 
ATOM   1071  O  OE1 . GLU A  1 143 ? 0.515   -21.406 35.470  1.00 33.33 ? 146  GLU A OE1 1 
ATOM   1072  O  OE2 . GLU A  1 143 ? 0.711   -20.017 33.767  1.00 33.17 ? 146  GLU A OE2 1 
ATOM   1073  N  N   . GLN A  1 144 ? 5.317   -18.528 35.291  1.00 23.87 ? 147  GLN A N   1 
ATOM   1074  C  CA  . GLN A  1 144 ? 5.968   -17.575 34.385  1.00 23.28 ? 147  GLN A CA  1 
ATOM   1075  C  C   . GLN A  1 144 ? 6.775   -18.295 33.294  1.00 21.75 ? 147  GLN A C   1 
ATOM   1076  O  O   . GLN A  1 144 ? 6.776   -17.890 32.138  1.00 21.65 ? 147  GLN A O   1 
ATOM   1077  C  CB  . GLN A  1 144 ? 6.869   -16.656 35.188  1.00 21.79 ? 147  GLN A CB  1 
ATOM   1078  C  CG  . GLN A  1 144 ? 7.749   -15.746 34.379  1.00 22.54 ? 147  GLN A CG  1 
ATOM   1079  C  CD  . GLN A  1 144 ? 8.346   -14.635 35.253  1.00 24.77 ? 147  GLN A CD  1 
ATOM   1080  O  OE1 . GLN A  1 144 ? 7.946   -13.482 35.159  1.00 22.87 ? 147  GLN A OE1 1 
ATOM   1081  N  NE2 . GLN A  1 144 ? 9.252   -15.011 36.161  1.00 22.91 ? 147  GLN A NE2 1 
ATOM   1082  N  N   . LEU A  1 145 ? 7.454   -19.369 33.675  1.00 18.74 ? 148  LEU A N   1 
ATOM   1083  C  CA  . LEU A  1 145 ? 8.166   -20.213 32.718  1.00 20.86 ? 148  LEU A CA  1 
ATOM   1084  C  C   . LEU A  1 145 ? 7.203   -20.836 31.698  1.00 19.21 ? 148  LEU A C   1 
ATOM   1085  O  O   . LEU A  1 145 ? 7.484   -20.852 30.506  1.00 20.14 ? 148  LEU A O   1 
ATOM   1086  C  CB  . LEU A  1 145 ? 8.954   -21.315 33.447  1.00 14.93 ? 148  LEU A CB  1 
ATOM   1087  C  CG  . LEU A  1 145 ? 9.884   -22.172 32.582  1.00 15.79 ? 148  LEU A CG  1 
ATOM   1088  C  CD1 . LEU A  1 145 ? 11.020  -22.772 33.442  1.00 16.07 ? 148  LEU A CD1 1 
ATOM   1089  C  CD2 . LEU A  1 145 ? 9.104   -23.301 31.933  1.00 14.40 ? 148  LEU A CD2 1 
ATOM   1090  N  N   . VAL A  1 146 ? 6.036   -21.275 32.157  1.00 17.79 ? 149  VAL A N   1 
ATOM   1091  C  CA  . VAL A  1 146 ? 5.043   -21.821 31.240  1.00 18.08 ? 149  VAL A CA  1 
ATOM   1092  C  C   . VAL A  1 146 ? 4.542   -20.726 30.279  1.00 17.09 ? 149  VAL A C   1 
ATOM   1093  O  O   . VAL A  1 146 ? 4.610   -20.889 29.057  1.00 17.33 ? 149  VAL A O   1 
ATOM   1094  C  CB  . VAL A  1 146 ? 3.887   -22.523 31.997  1.00 15.71 ? 149  VAL A CB  1 
ATOM   1095  C  CG1 . VAL A  1 146 ? 2.834   -23.014 31.004  1.00 12.81 ? 149  VAL A CG1 1 
ATOM   1096  C  CG2 . VAL A  1 146 ? 4.440   -23.682 32.820  1.00 10.44 ? 149  VAL A CG2 1 
ATOM   1097  N  N   . ASP A  1 147 ? 4.243   -19.552 30.830  1.00 13.46 ? 150  ASP A N   1 
ATOM   1098  C  CA  . ASP A  1 147 ? 3.840   -18.400 30.017  1.00 16.22 ? 150  ASP A CA  1 
ATOM   1099  C  C   . ASP A  1 147 ? 4.869   -18.001 28.977  1.00 17.85 ? 150  ASP A C   1 
ATOM   1100  O  O   . ASP A  1 147 ? 4.517   -17.678 27.845  1.00 17.26 ? 150  ASP A O   1 
ATOM   1101  C  CB  . ASP A  1 147 ? 3.534   -17.179 30.888  1.00 14.70 ? 150  ASP A CB  1 
ATOM   1102  C  CG  . ASP A  1 147 ? 3.009   -15.989 30.073  1.00 19.79 ? 150  ASP A CG  1 
ATOM   1103  O  OD1 . ASP A  1 147 ? 2.063   -16.171 29.260  1.00 14.99 ? 150  ASP A OD1 1 
ATOM   1104  O  OD2 . ASP A  1 147 ? 3.556   -14.864 30.231  1.00 21.79 ? 150  ASP A OD2 1 
ATOM   1105  N  N   . TYR A  1 148 ? 6.129   -17.893 29.392  1.00 17.29 ? 151  TYR A N   1 
ATOM   1106  C  CA  . TYR A  1 148 ? 7.184   -17.501 28.461  1.00 15.13 ? 151  TYR A CA  1 
ATOM   1107  C  C   . TYR A  1 148 ? 7.418   -18.589 27.388  1.00 14.26 ? 151  TYR A C   1 
ATOM   1108  O  O   . TYR A  1 148 ? 7.884   -18.298 26.292  1.00 12.67 ? 151  TYR A O   1 
ATOM   1109  C  CB  . TYR A  1 148 ? 8.478   -17.179 29.219  1.00 14.62 ? 151  TYR A CB  1 
ATOM   1110  C  CG  . TYR A  1 148 ? 8.579   -15.714 29.612  1.00 20.15 ? 151  TYR A CG  1 
ATOM   1111  C  CD1 . TYR A  1 148 ? 7.516   -15.066 30.255  1.00 19.52 ? 151  TYR A CD1 1 
ATOM   1112  C  CD2 . TYR A  1 148 ? 9.712   -14.963 29.303  1.00 16.71 ? 151  TYR A CD2 1 
ATOM   1113  C  CE1 . TYR A  1 148 ? 7.593   -13.704 30.601  1.00 20.19 ? 151  TYR A CE1 1 
ATOM   1114  C  CE2 . TYR A  1 148 ? 9.788   -13.593 29.627  1.00 18.68 ? 151  TYR A CE2 1 
ATOM   1115  C  CZ  . TYR A  1 148 ? 8.749   -12.984 30.299  1.00 21.26 ? 151  TYR A CZ  1 
ATOM   1116  O  OH  . TYR A  1 148 ? 8.821   -11.624 30.573  1.00 22.89 ? 151  TYR A OH  1 
ATOM   1117  N  N   . SER A  1 149 ? 7.130   -19.840 27.725  1.00 12.65 ? 152  SER A N   1 
ATOM   1118  C  CA  . SER A  1 149 ? 7.264   -20.918 26.752  1.00 15.30 ? 152  SER A CA  1 
ATOM   1119  C  C   . SER A  1 149 ? 6.159   -20.839 25.693  1.00 15.82 ? 152  SER A C   1 
ATOM   1120  O  O   . SER A  1 149 ? 6.399   -21.124 24.516  1.00 14.50 ? 152  SER A O   1 
ATOM   1121  C  CB  . SER A  1 149 ? 7.246   -22.276 27.427  1.00 12.14 ? 152  SER A CB  1 
ATOM   1122  O  OG  . SER A  1 149 ? 8.379   -22.450 28.259  1.00 17.36 ? 152  SER A OG  1 
ATOM   1123  N  N   . ASN A  1 150 ? 4.952   -20.479 26.128  1.00 14.35 ? 153  ASN A N   1 
ATOM   1124  C  CA  . ASN A  1 150 ? 3.877   -20.148 25.209  1.00 16.18 ? 153  ASN A CA  1 
ATOM   1125  C  C   . ASN A  1 150 ? 4.203   -18.930 24.353  1.00 16.22 ? 153  ASN A C   1 
ATOM   1126  O  O   . ASN A  1 150 ? 3.978   -18.941 23.155  1.00 17.69 ? 153  ASN A O   1 
ATOM   1127  C  CB  . ASN A  1 150 ? 2.561   -19.956 25.960  1.00 15.66 ? 153  ASN A CB  1 
ATOM   1128  C  CG  . ASN A  1 150 ? 1.912   -21.270 26.315  1.00 20.31 ? 153  ASN A CG  1 
ATOM   1129  O  OD1 . ASN A  1 150 ? 1.139   -21.807 25.518  1.00 21.14 ? 153  ASN A OD1 1 
ATOM   1130  N  ND2 . ASN A  1 150 ? 2.362   -21.891 27.425  1.00 16.78 ? 153  ASN A ND2 1 
ATOM   1131  N  N   . ARG A  1 151 ? 4.792   -17.902 24.944  1.00 17.84 ? 154  ARG A N   1 
ATOM   1132  C  CA  . ARG A  1 151 ? 5.015   -16.667 24.189  1.00 21.86 ? 154  ARG A CA  1 
ATOM   1133  C  C   . ARG A  1 151 ? 6.197   -16.753 23.201  1.00 20.48 ? 154  ARG A C   1 
ATOM   1134  O  O   . ARG A  1 151 ? 6.144   -16.187 22.120  1.00 21.01 ? 154  ARG A O   1 
ATOM   1135  C  CB  . ARG A  1 151 ? 5.157   -15.454 25.121  1.00 23.48 ? 154  ARG A CB  1 
ATOM   1136  C  CG  . ARG A  1 151 ? 3.886   -15.090 25.903  1.00 24.89 ? 154  ARG A CG  1 
ATOM   1137  C  CD  . ARG A  1 151 ? 4.255   -14.334 27.183  1.00 25.78 ? 154  ARG A CD  1 
ATOM   1138  N  NE  . ARG A  1 151 ? 4.922   -13.081 26.876  1.00 26.63 ? 154  ARG A NE  1 
ATOM   1139  C  CZ  . ARG A  1 151 ? 5.030   -12.070 27.734  1.00 28.82 ? 154  ARG A CZ  1 
ATOM   1140  N  NH1 . ARG A  1 151 ? 4.592   -12.205 28.978  1.00 26.39 ? 154  ARG A NH1 1 
ATOM   1141  N  NH2 . ARG A  1 151 ? 5.573   -10.921 27.349  1.00 27.38 ? 154  ARG A NH2 1 
ATOM   1142  N  N   . PHE A  1 152 ? 7.245   -17.490 23.541  1.00 19.50 ? 155  PHE A N   1 
ATOM   1143  C  CA  . PHE A  1 152 ? 8.477   -17.425 22.738  1.00 19.08 ? 155  PHE A CA  1 
ATOM   1144  C  C   . PHE A  1 152 ? 8.912   -18.770 22.191  1.00 15.79 ? 155  PHE A C   1 
ATOM   1145  O  O   . PHE A  1 152 ? 9.915   -18.863 21.495  1.00 20.58 ? 155  PHE A O   1 
ATOM   1146  C  CB  . PHE A  1 152 ? 9.622   -16.817 23.570  1.00 18.81 ? 155  PHE A CB  1 
ATOM   1147  C  CG  . PHE A  1 152 ? 9.328   -15.440 24.068  1.00 20.03 ? 155  PHE A CG  1 
ATOM   1148  C  CD1 . PHE A  1 152 ? 9.089   -14.400 23.169  1.00 23.63 ? 155  PHE A CD1 1 
ATOM   1149  C  CD2 . PHE A  1 152 ? 9.197   -15.191 25.420  1.00 17.79 ? 155  PHE A CD2 1 
ATOM   1150  C  CE1 . PHE A  1 152 ? 8.802   -13.112 23.628  1.00 21.45 ? 155  PHE A CE1 1 
ATOM   1151  C  CE2 . PHE A  1 152 ? 8.892   -13.917 25.880  1.00 19.76 ? 155  PHE A CE2 1 
ATOM   1152  C  CZ  . PHE A  1 152 ? 8.717   -12.874 24.985  1.00 20.46 ? 155  PHE A CZ  1 
ATOM   1153  N  N   . GLY A  1 153 ? 8.191   -19.821 22.552  1.00 15.71 ? 156  GLY A N   1 
ATOM   1154  C  CA  . GLY A  1 153 ? 8.668   -21.171 22.327  1.00 13.39 ? 156  GLY A CA  1 
ATOM   1155  C  C   . GLY A  1 153 ? 7.603   -22.003 21.631  1.00 15.95 ? 156  GLY A C   1 
ATOM   1156  O  O   . GLY A  1 153 ? 7.772   -23.212 21.451  1.00 16.10 ? 156  GLY A O   1 
ATOM   1157  N  N   . GLY A  1 154 ? 6.522   -21.347 21.219  1.00 13.92 ? 157  GLY A N   1 
ATOM   1158  C  CA  . GLY A  1 154 ? 5.347   -22.036 20.678  1.00 16.41 ? 157  GLY A CA  1 
ATOM   1159  C  C   . GLY A  1 154 ? 4.734   -23.067 21.625  1.00 20.74 ? 157  GLY A C   1 
ATOM   1160  O  O   . GLY A  1 154 ? 4.209   -24.090 21.193  1.00 17.65 ? 157  GLY A O   1 
ATOM   1161  N  N   . GLY A  1 155 ? 4.818   -22.821 22.927  1.00 18.27 ? 158  GLY A N   1 
ATOM   1162  C  CA  . GLY A  1 155 ? 4.317   -23.790 23.873  1.00 19.33 ? 158  GLY A CA  1 
ATOM   1163  C  C   . GLY A  1 155 ? 5.423   -24.602 24.524  1.00 22.64 ? 158  GLY A C   1 
ATOM   1164  O  O   . GLY A  1 155 ? 5.177   -25.307 25.504  1.00 25.86 ? 158  GLY A O   1 
ATOM   1165  N  N   . LYS A  1 156 ? 6.631   -24.539 23.975  1.00 19.21 ? 159  LYS A N   1 
ATOM   1166  C  CA  . LYS A  1 156 ? 7.728   -25.344 24.498  1.00 21.97 ? 159  LYS A CA  1 
ATOM   1167  C  C   . LYS A  1 156 ? 8.863   -24.464 25.060  1.00 19.77 ? 159  LYS A C   1 
ATOM   1168  O  O   . LYS A  1 156 ? 8.974   -23.302 24.720  1.00 19.41 ? 159  LYS A O   1 
ATOM   1169  C  CB  . LYS A  1 156 ? 8.250   -26.313 23.416  1.00 22.89 ? 159  LYS A CB  1 
ATOM   1170  C  CG  . LYS A  1 156 ? 7.451   -27.616 23.300  1.00 26.12 ? 159  LYS A CG  1 
ATOM   1171  C  CD  . LYS A  1 156 ? 6.210   -27.471 22.457  1.00 32.74 ? 159  LYS A CD  1 
ATOM   1172  C  CE  . LYS A  1 156 ? 5.723   -28.814 21.886  1.00 35.09 ? 159  LYS A CE  1 
ATOM   1173  N  NZ  . LYS A  1 156 ? 4.567   -29.344 22.690  1.00 37.12 ? 159  LYS A NZ  1 
ATOM   1174  N  N   . TYR A  1 157 ? 9.654   -25.006 25.971  1.00 18.83 ? 160  TYR A N   1 
ATOM   1175  C  CA  . TYR A  1 157 ? 10.822  -24.301 26.461  1.00 20.65 ? 160  TYR A CA  1 
ATOM   1176  C  C   . TYR A  1 157 ? 12.000  -24.575 25.531  1.00 21.40 ? 160  TYR A C   1 
ATOM   1177  O  O   . TYR A  1 157 ? 12.332  -25.734 25.275  1.00 22.35 ? 160  TYR A O   1 
ATOM   1178  C  CB  . TYR A  1 157 ? 11.173  -24.782 27.872  1.00 21.52 ? 160  TYR A CB  1 
ATOM   1179  C  CG  . TYR A  1 157 ? 12.306  -24.010 28.495  1.00 18.99 ? 160  TYR A CG  1 
ATOM   1180  C  CD1 . TYR A  1 157 ? 13.629  -24.366 28.259  1.00 18.87 ? 160  TYR A CD1 1 
ATOM   1181  C  CD2 . TYR A  1 157 ? 12.054  -22.928 29.330  1.00 19.81 ? 160  TYR A CD2 1 
ATOM   1182  C  CE1 . TYR A  1 157 ? 14.675  -23.631 28.801  1.00 17.23 ? 160  TYR A CE1 1 
ATOM   1183  C  CE2 . TYR A  1 157 ? 13.096  -22.158 29.843  1.00 18.45 ? 160  TYR A CE2 1 
ATOM   1184  C  CZ  . TYR A  1 157 ? 14.395  -22.543 29.610  1.00 17.47 ? 160  TYR A CZ  1 
ATOM   1185  O  OH  . TYR A  1 157 ? 15.417  -21.809 30.162  1.00 15.86 ? 160  TYR A OH  1 
ATOM   1186  N  N   . ASN A  1 158 ? 12.606  -23.518 25.000  1.00 18.09 ? 161  ASN A N   1 
ATOM   1187  C  CA  . ASN A  1 158 ? 13.776  -23.670 24.142  1.00 18.31 ? 161  ASN A CA  1 
ATOM   1188  C  C   . ASN A  1 158 ? 14.741  -22.516 24.352  1.00 17.52 ? 161  ASN A C   1 
ATOM   1189  O  O   . ASN A  1 158 ? 14.490  -21.690 25.223  1.00 15.67 ? 161  ASN A O   1 
ATOM   1190  C  CB  . ASN A  1 158 ? 13.383  -23.879 22.666  1.00 14.02 ? 161  ASN A CB  1 
ATOM   1191  C  CG  . ASN A  1 158 ? 12.772  -22.663 22.021  1.00 16.74 ? 161  ASN A CG  1 
ATOM   1192  O  OD1 . ASN A  1 158 ? 12.916  -21.527 22.498  1.00 17.80 ? 161  ASN A OD1 1 
ATOM   1193  N  ND2 . ASN A  1 158 ? 12.117  -22.887 20.866  1.00 17.70 ? 161  ASN A ND2 1 
ATOM   1194  N  N   . LEU A  1 159 ? 15.876  -22.499 23.645  1.00 18.10 ? 162  LEU A N   1 
ATOM   1195  C  CA  . LEU A  1 159 ? 16.900  -21.459 23.907  1.00 19.32 ? 162  LEU A CA  1 
ATOM   1196  C  C   . LEU A  1 159 ? 16.372  -20.036 23.759  1.00 15.86 ? 162  LEU A C   1 
ATOM   1197  O  O   . LEU A  1 159 ? 16.847  -19.116 24.424  1.00 18.30 ? 162  LEU A O   1 
ATOM   1198  C  CB  . LEU A  1 159 ? 18.163  -21.643 23.059  1.00 18.12 ? 162  LEU A CB  1 
ATOM   1199  C  CG  . LEU A  1 159 ? 18.999  -22.894 23.318  1.00 21.69 ? 162  LEU A CG  1 
ATOM   1200  C  CD1 . LEU A  1 159 ? 20.259  -22.904 22.460  1.00 20.81 ? 162  LEU A CD1 1 
ATOM   1201  C  CD2 . LEU A  1 159 ? 19.353  -23.037 24.788  1.00 22.95 ? 162  LEU A CD2 1 
ATOM   1202  N  N   . THR A  1 160 ? 15.421  -19.835 22.858  1.00 15.46 ? 163  THR A N   1 
ATOM   1203  C  CA  . THR A  1 160 ? 14.838  -18.503 22.695  1.00 11.73 ? 163  THR A CA  1 
ATOM   1204  C  C   . THR A  1 160 ? 14.040  -18.120 23.957  1.00 13.43 ? 163  THR A C   1 
ATOM   1205  O  O   . THR A  1 160 ? 14.134  -16.997 24.436  1.00 12.48 ? 163  THR A O   1 
ATOM   1206  C  CB  . THR A  1 160 ? 13.945  -18.406 21.446  1.00 11.86 ? 163  THR A CB  1 
ATOM   1207  O  OG1 . THR A  1 160 ? 14.688  -18.761 20.275  1.00 10.20 ? 163  THR A OG1 1 
ATOM   1208  C  CG2 . THR A  1 160 ? 13.391  -16.969 21.266  1.00 12.09 ? 163  THR A CG2 1 
ATOM   1209  N  N   . VAL A  1 161 ? 13.336  -19.088 24.545  1.00 13.40 ? 164  VAL A N   1 
ATOM   1210  C  CA  . VAL A  1 161 ? 12.619  -18.869 25.799  1.00 14.88 ? 164  VAL A CA  1 
ATOM   1211  C  C   . VAL A  1 161 ? 13.600  -18.616 26.974  1.00 14.54 ? 164  VAL A C   1 
ATOM   1212  O  O   . VAL A  1 161 ? 13.363  -17.783 27.870  1.00 15.48 ? 164  VAL A O   1 
ATOM   1213  C  CB  . VAL A  1 161 ? 11.715  -20.087 26.153  1.00 14.53 ? 164  VAL A CB  1 
ATOM   1214  C  CG1 . VAL A  1 161 ? 10.967  -19.835 27.480  1.00 10.79 ? 164  VAL A CG1 1 
ATOM   1215  C  CG2 . VAL A  1 161 ? 10.727  -20.381 25.010  1.00 12.22 ? 164  VAL A CG2 1 
ATOM   1216  N  N   . ALA A  1 162 ? 14.691  -19.354 26.955  1.00 10.66 ? 165  ALA A N   1 
ATOM   1217  C  CA  . ALA A  1 162 ? 15.744  -19.218 27.946  1.00 15.42 ? 165  ALA A CA  1 
ATOM   1218  C  C   . ALA A  1 162 ? 16.298  -17.800 27.947  1.00 11.42 ? 165  ALA A C   1 
ATOM   1219  O  O   . ALA A  1 162 ? 16.546  -17.242 28.995  1.00 16.76 ? 165  ALA A O   1 
ATOM   1220  C  CB  . ALA A  1 162 ? 16.858  -20.214 27.651  1.00 12.14 ? 165  ALA A CB  1 
ATOM   1221  N  N   . GLY A  1 163 ? 16.504  -17.243 26.759  1.00 13.58 ? 166  GLY A N   1 
ATOM   1222  C  CA  . GLY A  1 163 ? 16.962  -15.861 26.596  1.00 15.91 ? 166  GLY A CA  1 
ATOM   1223  C  C   . GLY A  1 163 ? 16.019  -14.815 27.187  1.00 17.77 ? 166  GLY A C   1 
ATOM   1224  O  O   . GLY A  1 163 ? 16.455  -13.901 27.875  1.00 17.73 ? 166  GLY A O   1 
ATOM   1225  N  N   . GLU A  1 164 ? 14.720  -14.970 26.968  1.00 16.78 ? 167  GLU A N   1 
ATOM   1226  C  CA  . GLU A  1 164 ? 13.766  -14.008 27.498  1.00 15.60 ? 167  GLU A CA  1 
ATOM   1227  C  C   . GLU A  1 164 ? 13.575  -14.207 28.997  1.00 16.96 ? 167  GLU A C   1 
ATOM   1228  O  O   . GLU A  1 164 ? 13.532  -13.242 29.739  1.00 14.40 ? 167  GLU A O   1 
ATOM   1229  C  CB  . GLU A  1 164 ? 12.425  -14.104 26.765  1.00 16.01 ? 167  GLU A CB  1 
ATOM   1230  C  CG  . GLU A  1 164 ? 12.548  -13.860 25.250  1.00 17.61 ? 167  GLU A CG  1 
ATOM   1231  C  CD  . GLU A  1 164 ? 13.211  -12.513 24.939  1.00 20.57 ? 167  GLU A CD  1 
ATOM   1232  O  OE1 . GLU A  1 164 ? 12.902  -11.522 25.627  1.00 20.95 ? 167  GLU A OE1 1 
ATOM   1233  O  OE2 . GLU A  1 164 ? 14.091  -12.455 24.053  1.00 26.91 ? 167  GLU A OE2 1 
ATOM   1234  N  N   . LEU A  1 165 ? 13.520  -15.457 29.444  1.00 16.47 ? 168  LEU A N   1 
ATOM   1235  C  CA  . LEU A  1 165 ? 13.258  -15.753 30.856  1.00 17.19 ? 168  LEU A CA  1 
ATOM   1236  C  C   . LEU A  1 165 ? 14.432  -15.368 31.760  1.00 16.70 ? 168  LEU A C   1 
ATOM   1237  O  O   . LEU A  1 165 ? 14.251  -14.831 32.856  1.00 16.48 ? 168  LEU A O   1 
ATOM   1238  C  CB  . LEU A  1 165 ? 12.925  -17.236 31.046  1.00 13.99 ? 168  LEU A CB  1 
ATOM   1239  C  CG  . LEU A  1 165 ? 12.415  -17.561 32.446  1.00 16.77 ? 168  LEU A CG  1 
ATOM   1240  C  CD1 . LEU A  1 165 ? 11.092  -16.840 32.774  1.00 9.86  ? 168  LEU A CD1 1 
ATOM   1241  C  CD2 . LEU A  1 165 ? 12.284  -19.090 32.601  1.00 17.52 ? 168  LEU A CD2 1 
ATOM   1242  N  N   . ARG A  1 166 ? 15.643  -15.601 31.282  1.00 18.87 ? 169  ARG A N   1 
ATOM   1243  C  CA  . ARG A  1 166 ? 16.830  -15.238 32.064  1.00 20.33 ? 169  ARG A CA  1 
ATOM   1244  C  C   . ARG A  1 166 ? 16.882  -13.735 32.354  1.00 18.71 ? 169  ARG A C   1 
ATOM   1245  O  O   . ARG A  1 166 ? 17.016  -13.336 33.508  1.00 21.13 ? 169  ARG A O   1 
ATOM   1246  C  CB  . ARG A  1 166 ? 18.104  -15.751 31.377  1.00 18.20 ? 169  ARG A CB  1 
ATOM   1247  C  CG  . ARG A  1 166 ? 19.360  -14.980 31.681  1.00 17.43 ? 169  ARG A CG  1 
ATOM   1248  C  CD  . ARG A  1 166 ? 19.867  -15.143 33.123  1.00 17.84 ? 169  ARG A CD  1 
ATOM   1249  N  NE  . ARG A  1 166 ? 19.687  -16.459 33.739  1.00 15.29 ? 169  ARG A NE  1 
ATOM   1250  C  CZ  . ARG A  1 166 ? 18.927  -16.643 34.818  1.00 17.78 ? 169  ARG A CZ  1 
ATOM   1251  N  NH1 . ARG A  1 166 ? 18.201  -15.635 35.284  1.00 19.88 ? 169  ARG A NH1 1 
ATOM   1252  N  NH2 . ARG A  1 166 ? 18.872  -17.809 35.425  1.00 16.98 ? 169  ARG A NH2 1 
ATOM   1253  N  N   . PHE A  1 167 ? 16.542  -12.929 31.351  1.00 15.79 ? 170  PHE A N   1 
ATOM   1254  C  CA  . PHE A  1 167 ? 16.525  -11.470 31.486  1.00 16.54 ? 170  PHE A CA  1 
ATOM   1255  C  C   . PHE A  1 167 ? 15.385  -11.024 32.386  1.00 18.58 ? 170  PHE A C   1 
ATOM   1256  O  O   . PHE A  1 167 ? 15.541  -10.157 33.245  1.00 16.90 ? 170  PHE A O   1 
ATOM   1257  C  CB  . PHE A  1 167 ? 16.376  -10.819 30.116  1.00 16.42 ? 170  PHE A CB  1 
ATOM   1258  C  CG  . PHE A  1 167 ? 16.275  -9.313  30.152  1.00 16.65 ? 170  PHE A CG  1 
ATOM   1259  C  CD1 . PHE A  1 167 ? 17.276  -8.545  30.724  1.00 19.59 ? 170  PHE A CD1 1 
ATOM   1260  C  CD2 . PHE A  1 167 ? 15.190  -8.666  29.576  1.00 16.82 ? 170  PHE A CD2 1 
ATOM   1261  C  CE1 . PHE A  1 167 ? 17.219  -7.146  30.700  1.00 19.84 ? 170  PHE A CE1 1 
ATOM   1262  C  CE2 . PHE A  1 167 ? 15.080  -7.277  29.631  1.00 20.24 ? 170  PHE A CE2 1 
ATOM   1263  C  CZ  . PHE A  1 167 ? 16.124  -6.510  30.163  1.00 18.13 ? 170  PHE A CZ  1 
ATOM   1264  N  N   . LYS A  1 168 ? 14.220  -11.612 32.181  1.00 16.77 ? 171  LYS A N   1 
ATOM   1265  C  CA  . LYS A  1 168 ? 13.095  -11.262 33.008  1.00 20.06 ? 171  LYS A CA  1 
ATOM   1266  C  C   . LYS A  1 168 ? 13.286  -11.572 34.518  1.00 18.48 ? 171  LYS A C   1 
ATOM   1267  O  O   . LYS A  1 168 ? 12.810  -10.830 35.367  1.00 22.29 ? 171  LYS A O   1 
ATOM   1268  C  CB  . LYS A  1 168 ? 11.817  -11.889 32.450  1.00 19.52 ? 171  LYS A CB  1 
ATOM   1269  C  CG  . LYS A  1 168 ? 10.701  -11.912 33.442  1.00 20.23 ? 171  LYS A CG  1 
ATOM   1270  C  CD  . LYS A  1 168 ? 9.877   -10.656 33.375  1.00 23.81 ? 171  LYS A CD  1 
ATOM   1271  C  CE  . LYS A  1 168 ? 8.589   -10.868 34.194  1.00 27.96 ? 171  LYS A CE  1 
ATOM   1272  N  NZ  . LYS A  1 168 ? 7.883   -9.590  34.387  1.00 35.00 ? 171  LYS A NZ  1 
ATOM   1273  N  N   . ARG A  1 169 ? 13.923  -12.695 34.846  1.00 18.36 ? 172  ARG A N   1 
ATOM   1274  C  CA  . ARG A  1 169 ? 14.198  -13.048 36.240  1.00 15.03 ? 172  ARG A CA  1 
ATOM   1275  C  C   . ARG A  1 169 ? 15.210  -12.074 36.883  1.00 16.36 ? 172  ARG A C   1 
ATOM   1276  O  O   . ARG A  1 169 ? 15.035  -11.631 38.025  1.00 15.76 ? 172  ARG A O   1 
ATOM   1277  C  CB  . ARG A  1 169 ? 14.685  -14.504 36.337  1.00 17.01 ? 172  ARG A CB  1 
ATOM   1278  C  CG  . ARG A  1 169 ? 13.598  -15.537 36.046  1.00 13.77 ? 172  ARG A CG  1 
ATOM   1279  C  CD  . ARG A  1 169 ? 12.452  -15.396 37.038  1.00 14.85 ? 172  ARG A CD  1 
ATOM   1280  N  NE  . ARG A  1 169 ? 12.886  -15.883 38.332  1.00 18.87 ? 172  ARG A NE  1 
ATOM   1281  C  CZ  . ARG A  1 169 ? 12.909  -15.166 39.448  1.00 22.23 ? 172  ARG A CZ  1 
ATOM   1282  N  NH1 . ARG A  1 169 ? 12.338  -13.967 39.488  1.00 19.12 ? 172  ARG A NH1 1 
ATOM   1283  N  NH2 . ARG A  1 169 ? 13.423  -15.703 40.554  1.00 20.69 ? 172  ARG A NH2 1 
ATOM   1284  N  N   . ILE A  1 170 ? 16.194  -11.648 36.099  1.00 18.31 ? 173  ILE A N   1 
ATOM   1285  C  CA  . ILE A  1 170 ? 17.067  -10.538 36.491  1.00 18.35 ? 173  ILE A CA  1 
ATOM   1286  C  C   . ILE A  1 170 ? 16.304  -9.242  36.799  1.00 20.94 ? 173  ILE A C   1 
ATOM   1287  O  O   . ILE A  1 170 ? 16.438  -8.672  37.893  1.00 20.56 ? 173  ILE A O   1 
ATOM   1288  C  CB  . ILE A  1 170 ? 18.168  -10.294 35.443  1.00 16.22 ? 173  ILE A CB  1 
ATOM   1289  C  CG1 . ILE A  1 170 ? 19.078  -11.530 35.362  1.00 14.36 ? 173  ILE A CG1 1 
ATOM   1290  C  CG2 . ILE A  1 170 ? 18.983  -9.040  35.790  1.00 16.31 ? 173  ILE A CG2 1 
ATOM   1291  C  CD1 . ILE A  1 170 ? 19.892  -11.587 34.069  1.00 15.22 ? 173  ILE A CD1 1 
ATOM   1292  N  N   . GLN A  1 171 ? 15.564  -8.742  35.819  1.00 19.90 ? 174  GLN A N   1 
ATOM   1293  C  CA  . GLN A  1 171 ? 14.673  -7.613  36.031  1.00 20.98 ? 174  GLN A CA  1 
ATOM   1294  C  C   . GLN A  1 171 ? 13.766  -7.797  37.259  1.00 21.17 ? 174  GLN A C   1 
ATOM   1295  O  O   . GLN A  1 171 ? 13.505  -6.842  37.983  1.00 22.74 ? 174  GLN A O   1 
ATOM   1296  C  CB  . GLN A  1 171 ? 13.788  -7.398  34.807  1.00 24.57 ? 174  GLN A CB  1 
ATOM   1297  C  CG  . GLN A  1 171 ? 14.439  -6.781  33.571  1.00 28.85 ? 174  GLN A CG  1 
ATOM   1298  C  CD  . GLN A  1 171 ? 13.368  -6.410  32.518  1.00 34.11 ? 174  GLN A CD  1 
ATOM   1299  O  OE1 . GLN A  1 171 ? 12.547  -7.255  32.125  1.00 34.83 ? 174  GLN A OE1 1 
ATOM   1300  N  NE2 . GLN A  1 171 ? 13.304  -5.128  32.153  1.00 34.07 ? 174  GLN A NE2 1 
ATOM   1301  N  N   . ASP A  1 172 ? 13.150  -8.967  37.393  1.00 21.26 ? 175  ASP A N   1 
ATOM   1302  C  CA  . ASP A  1 172 ? 12.305  -9.242  38.559  1.00 21.07 ? 175  ASP A CA  1 
ATOM   1303  C  C   . ASP A  1 172 ? 13.066  -8.973  39.861  1.00 20.13 ? 175  ASP A C   1 
ATOM   1304  O  O   . ASP A  1 172 ? 12.538  -8.365  40.792  1.00 22.91 ? 175  ASP A O   1 
ATOM   1305  C  CB  . ASP A  1 172 ? 11.838  -10.715 38.562  1.00 23.85 ? 175  ASP A CB  1 
ATOM   1306  C  CG  . ASP A  1 172 ? 10.626  -10.965 37.655  1.00 27.93 ? 175  ASP A CG  1 
ATOM   1307  O  OD1 . ASP A  1 172 ? 10.094  -9.982  37.101  1.00 28.77 ? 175  ASP A OD1 1 
ATOM   1308  O  OD2 . ASP A  1 172 ? 10.196  -12.148 37.519  1.00 26.94 ? 175  ASP A OD2 1 
ATOM   1309  N  N   . SER A  1 173 ? 14.243  -9.570  39.992  1.00 21.86 ? 176  SER A N   1 
ATOM   1310  C  CA  . SER A  1 173 ? 15.019  -9.427  41.224  1.00 23.16 ? 176  SER A CA  1 
ATOM   1311  C  C   . SER A  1 173 ? 15.495  -7.994  41.468  1.00 22.50 ? 176  SER A C   1 
ATOM   1312  O  O   . SER A  1 173 ? 15.407  -7.492  42.575  1.00 24.76 ? 176  SER A O   1 
ATOM   1313  C  CB  . SER A  1 173 ? 16.199  -10.386 41.226  1.00 22.35 ? 176  SER A CB  1 
ATOM   1314  O  OG  . SER A  1 173 ? 15.737  -11.715 41.369  1.00 23.35 ? 176  SER A OG  1 
ATOM   1315  N  N   . ILE A  1 174 ? 15.947  -7.316  40.427  1.00 22.58 ? 177  ILE A N   1 
ATOM   1316  C  CA  . ILE A  1 174 ? 16.338  -5.917  40.567  1.00 24.52 ? 177  ILE A CA  1 
ATOM   1317  C  C   . ILE A  1 174 ? 15.161  -5.112  41.115  1.00 25.62 ? 177  ILE A C   1 
ATOM   1318  O  O   . ILE A  1 174 ? 15.346  -4.189  41.912  1.00 25.09 ? 177  ILE A O   1 
ATOM   1319  C  CB  . ILE A  1 174 ? 16.739  -5.278  39.213  1.00 23.93 ? 177  ILE A CB  1 
ATOM   1320  C  CG1 . ILE A  1 174 ? 17.998  -5.930  38.620  1.00 20.00 ? 177  ILE A CG1 1 
ATOM   1321  C  CG2 . ILE A  1 174 ? 16.886  -3.780  39.371  1.00 22.88 ? 177  ILE A CG2 1 
ATOM   1322  C  CD1 . ILE A  1 174 ? 18.478  -5.258  37.241  1.00 13.99 ? 177  ILE A CD1 1 
ATOM   1323  N  N   . ALA A  1 175 ? 13.947  -5.450  40.680  1.00 23.62 ? 178  ALA A N   1 
ATOM   1324  C  CA  . ALA A  1 175 ? 12.794  -4.614  41.007  1.00 21.22 ? 178  ALA A CA  1 
ATOM   1325  C  C   . ALA A  1 175 ? 12.238  -4.927  42.387  1.00 21.66 ? 178  ALA A C   1 
ATOM   1326  O  O   . ALA A  1 175 ? 11.371  -4.213  42.862  1.00 24.85 ? 178  ALA A O   1 
ATOM   1327  C  CB  . ALA A  1 175 ? 11.692  -4.750  39.934  1.00 20.35 ? 178  ALA A CB  1 
ATOM   1328  N  N   . THR A  1 176 ? 12.638  -6.058  42.975  1.00 21.59 ? 179  THR A N   1 
ATOM   1329  C  CA  . THR A  1 176 ? 11.985  -6.531  44.191  1.00 20.29 ? 179  THR A CA  1 
ATOM   1330  C  C   . THR A  1 176 ? 12.945  -6.972  45.291  1.00 22.07 ? 179  THR A C   1 
ATOM   1331  O  O   . THR A  1 176 ? 12.530  -7.223  46.416  1.00 22.14 ? 179  THR A O   1 
ATOM   1332  C  CB  . THR A  1 176 ? 11.007  -7.694  43.935  1.00 22.85 ? 179  THR A CB  1 
ATOM   1333  O  OG1 . THR A  1 176 ? 11.732  -8.855  43.484  1.00 24.25 ? 179  THR A OG1 1 
ATOM   1334  C  CG2 . THR A  1 176 ? 9.904   -7.288  42.930  1.00 20.16 ? 179  THR A CG2 1 
ATOM   1335  N  N   . ASN A  1 177 ? 14.207  -7.176  44.959  1.00 22.91 ? 180  ASN A N   1 
ATOM   1336  C  CA  . ASN A  1 177 ? 15.122  -7.726  45.953  1.00 24.67 ? 180  ASN A CA  1 
ATOM   1337  C  C   . ASN A  1 177 ? 16.256  -6.764  46.272  1.00 23.42 ? 180  ASN A C   1 
ATOM   1338  O  O   . ASN A  1 177 ? 17.213  -6.641  45.506  1.00 24.55 ? 180  ASN A O   1 
ATOM   1339  C  CB  . ASN A  1 177 ? 15.638  -9.102  45.526  1.00 26.63 ? 180  ASN A CB  1 
ATOM   1340  C  CG  . ASN A  1 177 ? 16.634  -9.686  46.504  1.00 27.79 ? 180  ASN A CG  1 
ATOM   1341  O  OD1 . ASN A  1 177 ? 17.017  -9.046  47.493  1.00 31.66 ? 180  ASN A OD1 1 
ATOM   1342  N  ND2 . ASN A  1 177 ? 17.076  -10.895 46.226  1.00 24.79 ? 180  ASN A ND2 1 
ATOM   1343  N  N   . PRO A  1 178 ? 16.130  -6.045  47.395  1.00 23.59 ? 181  PRO A N   1 
ATOM   1344  C  CA  . PRO A  1 178 ? 17.058  -4.956  47.689  1.00 23.23 ? 181  PRO A CA  1 
ATOM   1345  C  C   . PRO A  1 178 ? 18.450  -5.502  47.924  1.00 23.41 ? 181  PRO A C   1 
ATOM   1346  O  O   . PRO A  1 178 ? 19.425  -4.756  47.873  1.00 22.88 ? 181  PRO A O   1 
ATOM   1347  C  CB  . PRO A  1 178 ? 16.479  -4.343  48.982  1.00 25.08 ? 181  PRO A CB  1 
ATOM   1348  C  CG  . PRO A  1 178 ? 15.660  -5.450  49.596  1.00 23.23 ? 181  PRO A CG  1 
ATOM   1349  C  CD  . PRO A  1 178 ? 15.056  -6.146  48.403  1.00 22.59 ? 181  PRO A CD  1 
ATOM   1350  N  N   . ASN A  1 179 ? 18.534  -6.822  48.054  1.00 23.43 ? 182  ASN A N   1 
ATOM   1351  C  CA  . ASN A  1 179 ? 19.783  -7.517  48.285  1.00 26.34 ? 182  ASN A CA  1 
ATOM   1352  C  C   . ASN A  1 179 ? 20.295  -8.266  47.059  1.00 27.37 ? 182  ASN A C   1 
ATOM   1353  O  O   . ASN A  1 179 ? 21.226  -9.078  47.165  1.00 24.61 ? 182  ASN A O   1 
ATOM   1354  C  CB  . ASN A  1 179 ? 19.603  -8.505  49.440  1.00 31.77 ? 182  ASN A CB  1 
ATOM   1355  C  CG  . ASN A  1 179 ? 19.756  -7.842  50.803  1.00 32.17 ? 182  ASN A CG  1 
ATOM   1356  O  OD1 . ASN A  1 179 ? 19.569  -6.638  50.946  1.00 30.84 ? 182  ASN A OD1 1 
ATOM   1357  N  ND2 . ASN A  1 179 ? 20.096  -8.631  51.802  1.00 36.56 ? 182  ASN A ND2 1 
ATOM   1358  N  N   . PHE A  1 180 ? 19.636  -8.054  45.918  1.00 25.23 ? 183  PHE A N   1 
ATOM   1359  C  CA  . PHE A  1 180 ? 20.008  -8.741  44.674  1.00 23.58 ? 183  PHE A CA  1 
ATOM   1360  C  C   . PHE A  1 180 ? 21.515  -8.713  44.477  1.00 21.01 ? 183  PHE A C   1 
ATOM   1361  O  O   . PHE A  1 180 ? 22.108  -7.652  44.381  1.00 24.35 ? 183  PHE A O   1 
ATOM   1362  C  CB  . PHE A  1 180 ? 19.305  -8.106  43.450  1.00 20.77 ? 183  PHE A CB  1 
ATOM   1363  C  CG  . PHE A  1 180 ? 19.499  -8.867  42.160  1.00 20.08 ? 183  PHE A CG  1 
ATOM   1364  C  CD1 . PHE A  1 180 ? 19.568  -10.262 42.153  1.00 18.60 ? 183  PHE A CD1 1 
ATOM   1365  C  CD2 . PHE A  1 180 ? 19.653  -8.186  40.957  1.00 17.94 ? 183  PHE A CD2 1 
ATOM   1366  C  CE1 . PHE A  1 180 ? 19.692  -10.951 40.962  1.00 15.45 ? 183  PHE A CE1 1 
ATOM   1367  C  CE2 . PHE A  1 180 ? 19.859  -8.857  39.776  1.00 16.90 ? 183  PHE A CE2 1 
ATOM   1368  C  CZ  . PHE A  1 180 ? 19.820  -10.250 39.764  1.00 17.35 ? 183  PHE A CZ  1 
ATOM   1369  N  N   . SER A  1 181 ? 22.101  -9.883  44.267  1.00 20.72 ? 184  SER A N   1 
ATOM   1370  C  CA  . SER A  1 181 ? 23.492  -9.962  43.874  1.00 21.66 ? 184  SER A CA  1 
ATOM   1371  C  C   . SER A  1 181 ? 23.639  -10.893 42.690  1.00 21.50 ? 184  SER A C   1 
ATOM   1372  O  O   . SER A  1 181 ? 23.110  -12.013 42.691  1.00 18.88 ? 184  SER A O   1 
ATOM   1373  C  CB  . SER A  1 181 ? 24.370  -10.476 45.026  1.00 21.76 ? 184  SER A CB  1 
ATOM   1374  O  OG  . SER A  1 181 ? 25.675  -10.771 44.550  1.00 21.42 ? 184  SER A OG  1 
ATOM   1375  N  N   . PHE A  1 182 ? 24.398  -10.432 41.706  1.00 19.42 ? 185  PHE A N   1 
ATOM   1376  C  CA  . PHE A  1 182 ? 24.474  -11.084 40.413  1.00 19.24 ? 185  PHE A CA  1 
ATOM   1377  C  C   . PHE A  1 182 ? 25.839  -10.827 39.824  1.00 19.10 ? 185  PHE A C   1 
ATOM   1378  O  O   . PHE A  1 182 ? 25.949  -10.123 38.813  1.00 20.34 ? 185  PHE A O   1 
ATOM   1379  C  CB  . PHE A  1 182 ? 23.415  -10.524 39.450  1.00 19.37 ? 185  PHE A CB  1 
ATOM   1380  C  CG  . PHE A  1 182 ? 23.000  -11.514 38.361  1.00 19.61 ? 185  PHE A CG  1 
ATOM   1381  C  CD1 . PHE A  1 182 ? 22.379  -12.715 38.691  1.00 17.48 ? 185  PHE A CD1 1 
ATOM   1382  C  CD2 . PHE A  1 182 ? 23.247  -11.243 37.025  1.00 16.54 ? 185  PHE A CD2 1 
ATOM   1383  C  CE1 . PHE A  1 182 ? 22.063  -13.649 37.697  1.00 18.56 ? 185  PHE A CE1 1 
ATOM   1384  C  CE2 . PHE A  1 182 ? 22.889  -12.150 36.022  1.00 17.97 ? 185  PHE A CE2 1 
ATOM   1385  C  CZ  . PHE A  1 182 ? 22.329  -13.365 36.363  1.00 18.02 ? 185  PHE A CZ  1 
ATOM   1386  N  N   . VAL A  1 183 ? 26.877  -11.347 40.478  1.00 16.05 ? 186  VAL A N   1 
ATOM   1387  C  CA  . VAL A  1 183 ? 28.264  -11.072 40.071  1.00 18.59 ? 186  VAL A CA  1 
ATOM   1388  C  C   . VAL A  1 183 ? 29.043  -12.371 40.053  1.00 21.28 ? 186  VAL A C   1 
ATOM   1389  O  O   . VAL A  1 183 ? 28.613  -13.375 40.639  1.00 21.23 ? 186  VAL A O   1 
ATOM   1390  C  CB  . VAL A  1 183 ? 28.985  -10.083 41.041  1.00 18.18 ? 186  VAL A CB  1 
ATOM   1391  C  CG1 . VAL A  1 183 ? 28.345  -8.702  40.976  1.00 20.07 ? 186  VAL A CG1 1 
ATOM   1392  C  CG2 . VAL A  1 183 ? 28.974  -10.617 42.500  1.00 16.85 ? 186  VAL A CG2 1 
ATOM   1393  N  N   . ASP A  1 184 ? 30.189  -12.363 39.385  1.00 21.96 ? 187  ASP A N   1 
ATOM   1394  C  CA  . ASP A  1 184 ? 31.151  -13.449 39.568  1.00 23.33 ? 187  ASP A CA  1 
ATOM   1395  C  C   . ASP A  1 184 ? 30.507  -14.826 39.318  1.00 23.25 ? 187  ASP A C   1 
ATOM   1396  O  O   . ASP A  1 184 ? 29.978  -15.081 38.232  1.00 24.71 ? 187  ASP A O   1 
ATOM   1397  C  CB  . ASP A  1 184 ? 31.765  -13.354 40.966  1.00 23.39 ? 187  ASP A CB  1 
ATOM   1398  C  CG  . ASP A  1 184 ? 32.632  -12.084 41.143  1.00 26.77 ? 187  ASP A CG  1 
ATOM   1399  O  OD1 . ASP A  1 184 ? 33.514  -11.846 40.292  1.00 25.96 ? 187  ASP A OD1 1 
ATOM   1400  O  OD2 . ASP A  1 184 ? 32.471  -11.366 42.162  1.00 25.80 ? 187  ASP A OD2 1 
ATOM   1401  N  N   . PHE A  1 185 ? 30.562  -15.720 40.300  1.00 19.83 ? 188  PHE A N   1 
ATOM   1402  C  CA  . PHE A  1 185 ? 30.230  -17.107 40.035  1.00 18.66 ? 188  PHE A CA  1 
ATOM   1403  C  C   . PHE A  1 185 ? 28.763  -17.273 39.650  1.00 17.65 ? 188  PHE A C   1 
ATOM   1404  O  O   . PHE A  1 185 ? 28.419  -18.149 38.867  1.00 18.61 ? 188  PHE A O   1 
ATOM   1405  C  CB  . PHE A  1 185 ? 30.520  -17.980 41.245  1.00 16.46 ? 188  PHE A CB  1 
ATOM   1406  C  CG  . PHE A  1 185 ? 30.442  -19.450 40.957  1.00 14.53 ? 188  PHE A CG  1 
ATOM   1407  C  CD1 . PHE A  1 185 ? 31.311  -20.034 40.058  1.00 18.56 ? 188  PHE A CD1 1 
ATOM   1408  C  CD2 . PHE A  1 185 ? 29.533  -20.253 41.621  1.00 16.78 ? 188  PHE A CD2 1 
ATOM   1409  C  CE1 . PHE A  1 185 ? 31.303  -21.436 39.860  1.00 21.39 ? 188  PHE A CE1 1 
ATOM   1410  C  CE2 . PHE A  1 185 ? 29.480  -21.634 41.404  1.00 17.68 ? 188  PHE A CE2 1 
ATOM   1411  C  CZ  . PHE A  1 185 ? 30.353  -22.221 40.509  1.00 19.69 ? 188  PHE A CZ  1 
ATOM   1412  N  N   . ARG A  1 186 ? 27.900  -16.484 40.272  1.00 18.61 ? 189  ARG A N   1 
ATOM   1413  C  CA  . ARG A  1 186 ? 26.465  -16.650 40.110  1.00 19.99 ? 189  ARG A CA  1 
ATOM   1414  C  C   . ARG A  1 186 ? 26.074  -16.062 38.775  1.00 20.24 ? 189  ARG A C   1 
ATOM   1415  O  O   . ARG A  1 186 ? 25.286  -16.643 38.046  1.00 22.49 ? 189  ARG A O   1 
ATOM   1416  C  CB  . ARG A  1 186 ? 25.704  -15.958 41.226  1.00 16.68 ? 189  ARG A CB  1 
ATOM   1417  C  CG  . ARG A  1 186 ? 24.195  -15.998 41.049  1.00 17.97 ? 189  ARG A CG  1 
ATOM   1418  C  CD  . ARG A  1 186 ? 23.715  -17.394 40.707  1.00 14.63 ? 189  ARG A CD  1 
ATOM   1419  N  NE  . ARG A  1 186 ? 22.292  -17.426 40.360  1.00 15.82 ? 189  ARG A NE  1 
ATOM   1420  C  CZ  . ARG A  1 186 ? 21.672  -18.470 39.794  1.00 16.27 ? 189  ARG A CZ  1 
ATOM   1421  N  NH1 . ARG A  1 186 ? 22.325  -19.604 39.557  1.00 10.16 ? 189  ARG A NH1 1 
ATOM   1422  N  NH2 . ARG A  1 186 ? 20.385  -18.399 39.493  1.00 13.51 ? 189  ARG A NH2 1 
ATOM   1423  N  N   . PHE A  1 187 ? 26.759  -14.991 38.401  1.00 22.00 ? 190  PHE A N   1 
ATOM   1424  C  CA  . PHE A  1 187 ? 26.606  -14.412 37.079  1.00 21.30 ? 190  PHE A CA  1 
ATOM   1425  C  C   . PHE A  1 187 ? 26.956  -15.426 35.975  1.00 21.49 ? 190  PHE A C   1 
ATOM   1426  O  O   . PHE A  1 187 ? 26.263  -15.538 34.971  1.00 16.22 ? 190  PHE A O   1 
ATOM   1427  C  CB  . PHE A  1 187 ? 27.459  -13.152 36.960  1.00 19.63 ? 190  PHE A CB  1 
ATOM   1428  C  CG  . PHE A  1 187 ? 27.276  -12.413 35.652  1.00 22.57 ? 190  PHE A CG  1 
ATOM   1429  C  CD1 . PHE A  1 187 ? 26.242  -11.505 35.492  1.00 20.39 ? 190  PHE A CD1 1 
ATOM   1430  C  CD2 . PHE A  1 187 ? 28.145  -12.624 34.597  1.00 21.51 ? 190  PHE A CD2 1 
ATOM   1431  C  CE1 . PHE A  1 187 ? 26.107  -10.800 34.324  1.00 22.46 ? 190  PHE A CE1 1 
ATOM   1432  C  CE2 . PHE A  1 187 ? 28.003  -11.936 33.401  1.00 22.58 ? 190  PHE A CE2 1 
ATOM   1433  C  CZ  . PHE A  1 187 ? 26.986  -11.013 33.265  1.00 22.16 ? 190  PHE A CZ  1 
ATOM   1434  N  N   . PHE A  1 188 ? 27.961  -16.251 36.214  1.00 21.66 ? 191  PHE A N   1 
ATOM   1435  C  CA  . PHE A  1 188 ? 28.357  -17.209 35.199  1.00 20.98 ? 191  PHE A CA  1 
ATOM   1436  C  C   . PHE A  1 188 ? 27.396  -18.390 35.117  1.00 21.67 ? 191  PHE A C   1 
ATOM   1437  O  O   . PHE A  1 188 ? 26.960  -18.772 34.022  1.00 23.63 ? 191  PHE A O   1 
ATOM   1438  C  CB  . PHE A  1 188 ? 29.798  -17.652 35.418  1.00 22.44 ? 191  PHE A CB  1 
ATOM   1439  C  CG  . PHE A  1 188 ? 30.181  -18.868 34.654  1.00 24.90 ? 191  PHE A CG  1 
ATOM   1440  C  CD1 . PHE A  1 188 ? 30.016  -20.125 35.208  1.00 25.79 ? 191  PHE A CD1 1 
ATOM   1441  C  CD2 . PHE A  1 188 ? 30.741  -18.762 33.393  1.00 25.59 ? 191  PHE A CD2 1 
ATOM   1442  C  CE1 . PHE A  1 188 ? 30.426  -21.254 34.529  1.00 27.22 ? 191  PHE A CE1 1 
ATOM   1443  C  CE2 . PHE A  1 188 ? 31.130  -19.885 32.705  1.00 26.90 ? 191  PHE A CE2 1 
ATOM   1444  C  CZ  . PHE A  1 188 ? 30.957  -21.134 33.267  1.00 27.75 ? 191  PHE A CZ  1 
ATOM   1445  N  N   . THR A  1 189 ? 27.028  -18.959 36.258  1.00 17.96 ? 192  THR A N   1 
ATOM   1446  C  CA  . THR A  1 189 ? 26.224  -20.180 36.219  1.00 17.77 ? 192  THR A CA  1 
ATOM   1447  C  C   . THR A  1 189 ? 24.745  -19.916 35.916  1.00 18.27 ? 192  THR A C   1 
ATOM   1448  O  O   . THR A  1 189 ? 24.015  -20.817 35.516  1.00 16.22 ? 192  THR A O   1 
ATOM   1449  C  CB  . THR A  1 189 ? 26.334  -20.981 37.521  1.00 18.71 ? 192  THR A CB  1 
ATOM   1450  O  OG1 . THR A  1 189 ? 25.926  -20.158 38.612  1.00 19.67 ? 192  THR A OG1 1 
ATOM   1451  C  CG2 . THR A  1 189 ? 27.766  -21.455 37.743  1.00 19.22 ? 192  THR A CG2 1 
ATOM   1452  N  N   . ALA A  1 190 ? 24.286  -18.683 36.122  1.00 17.87 ? 193  ALA A N   1 
ATOM   1453  C  CA  . ALA A  1 190 ? 22.867  -18.451 36.017  1.00 14.27 ? 193  ALA A CA  1 
ATOM   1454  C  C   . ALA A  1 190 ? 22.468  -18.504 34.545  1.00 16.56 ? 193  ALA A C   1 
ATOM   1455  O  O   . ALA A  1 190 ? 21.312  -18.757 34.226  1.00 17.88 ? 193  ALA A O   1 
ATOM   1456  C  CB  . ALA A  1 190 ? 22.490  -17.130 36.641  1.00 12.14 ? 193  ALA A CB  1 
ATOM   1457  N  N   . TYR A  1 191 ? 23.414  -18.186 33.665  1.00 12.10 ? 194  TYR A N   1 
ATOM   1458  C  CA  . TYR A  1 191 ? 23.211  -18.296 32.239  1.00 11.73 ? 194  TYR A CA  1 
ATOM   1459  C  C   . TYR A  1 191 ? 23.257  -19.743 31.752  1.00 13.61 ? 194  TYR A C   1 
ATOM   1460  O  O   . TYR A  1 191 ? 22.328  -20.207 31.096  1.00 15.29 ? 194  TYR A O   1 
ATOM   1461  C  CB  . TYR A  1 191 ? 24.242  -17.428 31.487  1.00 14.03 ? 194  TYR A CB  1 
ATOM   1462  C  CG  . TYR A  1 191 ? 23.851  -15.953 31.463  1.00 13.10 ? 194  TYR A CG  1 
ATOM   1463  C  CD1 . TYR A  1 191 ? 24.154  -15.135 32.539  1.00 11.88 ? 194  TYR A CD1 1 
ATOM   1464  C  CD2 . TYR A  1 191 ? 23.002  -15.449 30.469  1.00 12.97 ? 194  TYR A CD2 1 
ATOM   1465  C  CE1 . TYR A  1 191 ? 23.691  -13.829 32.606  1.00 16.62 ? 194  TYR A CE1 1 
ATOM   1466  C  CE2 . TYR A  1 191 ? 22.563  -14.123 30.493  1.00 14.81 ? 194  TYR A CE2 1 
ATOM   1467  C  CZ  . TYR A  1 191 ? 22.893  -13.330 31.591  1.00 16.29 ? 194  TYR A CZ  1 
ATOM   1468  O  OH  . TYR A  1 191 ? 22.516  -12.020 31.648  1.00 18.31 ? 194  TYR A OH  1 
ATOM   1469  N  N   . GLY A  1 192 ? 24.329  -20.467 32.072  1.00 12.84 ? 195  GLY A N   1 
ATOM   1470  C  CA  . GLY A  1 192 ? 24.468  -21.845 31.603  1.00 12.80 ? 195  GLY A CA  1 
ATOM   1471  C  C   . GLY A  1 192 ? 23.235  -22.643 32.017  1.00 15.74 ? 195  GLY A C   1 
ATOM   1472  O  O   . GLY A  1 192 ? 22.686  -23.416 31.237  1.00 19.32 ? 195  GLY A O   1 
ATOM   1473  N  N   . GLU A  1 193 ? 22.770  -22.411 33.236  1.00 16.56 ? 196  GLU A N   1 
ATOM   1474  C  CA  . GLU A  1 193 ? 21.653  -23.176 33.790  1.00 17.46 ? 196  GLU A CA  1 
ATOM   1475  C  C   . GLU A  1 193 ? 20.367  -23.067 32.957  1.00 17.14 ? 196  GLU A C   1 
ATOM   1476  O  O   . GLU A  1 193 ? 19.574  -23.993 32.925  1.00 17.42 ? 196  GLU A O   1 
ATOM   1477  C  CB  . GLU A  1 193 ? 21.398  -22.755 35.241  1.00 15.75 ? 196  GLU A CB  1 
ATOM   1478  C  CG  . GLU A  1 193 ? 22.441  -23.335 36.200  1.00 19.57 ? 196  GLU A CG  1 
ATOM   1479  C  CD  . GLU A  1 193 ? 22.497  -22.618 37.530  1.00 19.54 ? 196  GLU A CD  1 
ATOM   1480  O  OE1 . GLU A  1 193 ? 21.629  -21.766 37.798  1.00 20.60 ? 196  GLU A OE1 1 
ATOM   1481  O  OE2 . GLU A  1 193 ? 23.436  -22.897 38.299  1.00 22.58 ? 196  GLU A OE2 1 
ATOM   1482  N  N   . THR A  1 194 ? 20.132  -21.923 32.330  1.00 14.46 ? 197  THR A N   1 
ATOM   1483  C  CA  . THR A  1 194 ? 18.923  -21.784 31.545  1.00 16.43 ? 197  THR A CA  1 
ATOM   1484  C  C   . THR A  1 194 ? 19.004  -22.527 30.213  1.00 16.92 ? 197  THR A C   1 
ATOM   1485  O  O   . THR A  1 194 ? 18.008  -22.629 29.510  1.00 19.00 ? 197  THR A O   1 
ATOM   1486  C  CB  . THR A  1 194 ? 18.581  -20.327 31.288  1.00 16.03 ? 197  THR A CB  1 
ATOM   1487  O  OG1 . THR A  1 194 ? 19.634  -19.726 30.546  1.00 21.04 ? 197  THR A OG1 1 
ATOM   1488  C  CG2 . THR A  1 194 ? 18.442  -19.596 32.585  1.00 16.96 ? 197  THR A CG2 1 
ATOM   1489  N  N   . THR A  1 195 ? 20.183  -23.029 29.849  1.00 15.76 ? 198  THR A N   1 
ATOM   1490  C  CA  . THR A  1 195 ? 20.284  -23.886 28.681  1.00 13.55 ? 198  THR A CA  1 
ATOM   1491  C  C   . THR A  1 195 ? 20.009  -25.344 29.037  1.00 18.53 ? 198  THR A C   1 
ATOM   1492  O  O   . THR A  1 195 ? 19.645  -26.135 28.167  1.00 19.98 ? 198  THR A O   1 
ATOM   1493  C  CB  . THR A  1 195 ? 21.664  -23.813 28.000  1.00 14.27 ? 198  THR A CB  1 
ATOM   1494  O  OG1 . THR A  1 195 ? 22.615  -24.544 28.776  1.00 13.64 ? 198  THR A OG1 1 
ATOM   1495  C  CG2 . THR A  1 195 ? 22.133  -22.363 27.838  1.00 12.66 ? 198  THR A CG2 1 
ATOM   1496  N  N   . PHE A  1 196 ? 20.228  -25.711 30.297  1.00 18.07 ? 199  PHE A N   1 
ATOM   1497  C  CA  . PHE A  1 196 ? 20.174  -27.115 30.669  1.00 21.69 ? 199  PHE A CA  1 
ATOM   1498  C  C   . PHE A  1 196 ? 18.843  -27.808 30.303  1.00 18.58 ? 199  PHE A C   1 
ATOM   1499  O  O   . PHE A  1 196 ? 18.853  -28.918 29.766  1.00 23.57 ? 199  PHE A O   1 
ATOM   1500  C  CB  . PHE A  1 196 ? 20.541  -27.344 32.159  1.00 20.73 ? 199  PHE A CB  1 
ATOM   1501  C  CG  . PHE A  1 196 ? 21.967  -26.941 32.518  1.00 21.71 ? 199  PHE A CG  1 
ATOM   1502  C  CD1 . PHE A  1 196 ? 22.926  -26.752 31.538  1.00 20.67 ? 199  PHE A CD1 1 
ATOM   1503  C  CD2 . PHE A  1 196 ? 22.342  -26.768 33.845  1.00 18.78 ? 199  PHE A CD2 1 
ATOM   1504  C  CE1 . PHE A  1 196 ? 24.238  -26.348 31.875  1.00 19.99 ? 199  PHE A CE1 1 
ATOM   1505  C  CE2 . PHE A  1 196 ? 23.630  -26.344 34.176  1.00 21.44 ? 199  PHE A CE2 1 
ATOM   1506  C  CZ  . PHE A  1 196 ? 24.574  -26.128 33.186  1.00 18.28 ? 199  PHE A CZ  1 
ATOM   1507  N  N   . PRO A  1 197 ? 17.705  -27.178 30.606  1.00 14.90 ? 200  PRO A N   1 
ATOM   1508  C  CA  . PRO A  1 197 ? 16.414  -27.870 30.384  1.00 16.20 ? 200  PRO A CA  1 
ATOM   1509  C  C   . PRO A  1 197 ? 16.193  -28.247 28.917  1.00 17.51 ? 200  PRO A C   1 
ATOM   1510  O  O   . PRO A  1 197 ? 15.677  -29.328 28.616  1.00 19.43 ? 200  PRO A O   1 
ATOM   1511  C  CB  . PRO A  1 197 ? 15.365  -26.834 30.823  1.00 11.45 ? 200  PRO A CB  1 
ATOM   1512  C  CG  . PRO A  1 197 ? 16.134  -25.913 31.808  1.00 16.57 ? 200  PRO A CG  1 
ATOM   1513  C  CD  . PRO A  1 197 ? 17.520  -25.819 31.156  1.00 18.74 ? 200  PRO A CD  1 
ATOM   1514  N  N   . ALA A  1 198 ? 16.681  -27.397 28.025  1.00 17.99 ? 201  ALA A N   1 
ATOM   1515  C  CA  . ALA A  1 198 ? 16.524  -27.564 26.594  1.00 16.99 ? 201  ALA A CA  1 
ATOM   1516  C  C   . ALA A  1 198 ? 17.564  -28.557 26.076  1.00 19.98 ? 201  ALA A C   1 
ATOM   1517  O  O   . ALA A  1 198 ? 17.336  -29.232 25.054  1.00 17.28 ? 201  ALA A O   1 
ATOM   1518  C  CB  . ALA A  1 198 ? 16.699  -26.201 25.891  1.00 13.78 ? 201  ALA A CB  1 
ATOM   1519  N  N   . ASN A  1 199 ? 18.729  -28.588 26.726  1.00 16.50 ? 202  ASN A N   1 
ATOM   1520  C  CA  . ASN A  1 199 ? 19.830  -29.457 26.249  1.00 18.42 ? 202  ASN A CA  1 
ATOM   1521  C  C   . ASN A  1 199 ? 19.743  -30.868 26.839  1.00 18.37 ? 202  ASN A C   1 
ATOM   1522  O  O   . ASN A  1 199 ? 20.252  -31.814 26.256  1.00 16.42 ? 202  ASN A O   1 
ATOM   1523  C  CB  . ASN A  1 199 ? 21.202  -28.873 26.595  1.00 17.24 ? 202  ASN A CB  1 
ATOM   1524  C  CG  . ASN A  1 199 ? 21.547  -27.623 25.781  1.00 20.63 ? 202  ASN A CG  1 
ATOM   1525  O  OD1 . ASN A  1 199 ? 20.870  -27.280 24.807  1.00 22.69 ? 202  ASN A OD1 1 
ATOM   1526  N  ND2 . ASN A  1 199 ? 22.623  -26.950 26.172  1.00 19.02 ? 202  ASN A ND2 1 
ATOM   1527  N  N   . LEU A  1 200 ? 19.106  -30.995 28.004  1.00 20.23 ? 203  LEU A N   1 
ATOM   1528  C  CA  . LEU A  1 200 ? 19.280  -32.171 28.848  1.00 20.74 ? 203  LEU A CA  1 
ATOM   1529  C  C   . LEU A  1 200 ? 17.993  -32.847 29.280  1.00 20.15 ? 203  LEU A C   1 
ATOM   1530  O  O   . LEU A  1 200 ? 18.002  -34.040 29.614  1.00 19.55 ? 203  LEU A O   1 
ATOM   1531  C  CB  . LEU A  1 200 ? 20.107  -31.822 30.084  1.00 21.67 ? 203  LEU A CB  1 
ATOM   1532  C  CG  . LEU A  1 200 ? 21.545  -31.531 29.673  1.00 22.44 ? 203  LEU A CG  1 
ATOM   1533  C  CD1 . LEU A  1 200 ? 22.166  -30.565 30.635  1.00 21.36 ? 203  LEU A CD1 1 
ATOM   1534  C  CD2 . LEU A  1 200 ? 22.317  -32.838 29.590  1.00 21.27 ? 203  LEU A CD2 1 
ATOM   1535  N  N   . PHE A  1 201 ? 16.925  -32.066 29.403  1.00 19.23 ? 204  PHE A N   1 
ATOM   1536  C  CA  . PHE A  1 201 ? 15.652  -32.599 29.912  1.00 20.66 ? 204  PHE A CA  1 
ATOM   1537  C  C   . PHE A  1 201 ? 14.796  -33.066 28.743  1.00 21.41 ? 204  PHE A C   1 
ATOM   1538  O  O   . PHE A  1 201 ? 13.687  -33.588 28.920  1.00 22.80 ? 204  PHE A O   1 
ATOM   1539  C  CB  . PHE A  1 201 ? 14.892  -31.543 30.716  1.00 19.13 ? 204  PHE A CB  1 
ATOM   1540  C  CG  . PHE A  1 201 ? 15.441  -31.309 32.105  1.00 20.67 ? 204  PHE A CG  1 
ATOM   1541  C  CD1 . PHE A  1 201 ? 16.342  -32.200 32.677  1.00 21.86 ? 204  PHE A CD1 1 
ATOM   1542  C  CD2 . PHE A  1 201 ? 15.008  -30.224 32.859  1.00 19.40 ? 204  PHE A CD2 1 
ATOM   1543  C  CE1 . PHE A  1 201 ? 16.830  -31.995 33.952  1.00 22.77 ? 204  PHE A CE1 1 
ATOM   1544  C  CE2 . PHE A  1 201 ? 15.499  -30.008 34.138  1.00 21.24 ? 204  PHE A CE2 1 
ATOM   1545  C  CZ  . PHE A  1 201 ? 16.381  -30.920 34.703  1.00 21.96 ? 204  PHE A CZ  1 
ATOM   1546  N  N   . VAL A  1 202 ? 15.315  -32.859 27.542  1.00 21.78 ? 205  VAL A N   1 
ATOM   1547  C  CA  . VAL A  1 202 ? 14.602  -33.189 26.322  1.00 22.78 ? 205  VAL A CA  1 
ATOM   1548  C  C   . VAL A  1 202 ? 14.906  -34.637 25.909  1.00 25.14 ? 205  VAL A C   1 
ATOM   1549  O  O   . VAL A  1 202 ? 16.065  -35.051 25.839  1.00 25.94 ? 205  VAL A O   1 
ATOM   1550  C  CB  . VAL A  1 202 ? 14.985  -32.208 25.212  1.00 23.77 ? 205  VAL A CB  1 
ATOM   1551  C  CG1 . VAL A  1 202 ? 14.591  -32.757 23.823  1.00 25.11 ? 205  VAL A CG1 1 
ATOM   1552  C  CG2 . VAL A  1 202 ? 14.324  -30.858 25.475  1.00 19.32 ? 205  VAL A CG2 1 
ATOM   1553  N  N   . ASP A  1 203 ? 13.868  -35.451 25.785  1.00 26.25 ? 206  ASP A N   1 
ATOM   1554  C  CA  . ASP A  1 203 ? 14.092  -36.851 25.466  1.00 26.82 ? 206  ASP A CA  1 
ATOM   1555  C  C   . ASP A  1 203 ? 15.165  -37.007 24.396  1.00 24.29 ? 206  ASP A C   1 
ATOM   1556  O  O   . ASP A  1 203 ? 15.136  -36.337 23.365  1.00 25.04 ? 206  ASP A O   1 
ATOM   1557  C  CB  . ASP A  1 203 ? 12.806  -37.552 25.032  1.00 24.98 ? 206  ASP A CB  1 
ATOM   1558  C  CG  . ASP A  1 203 ? 13.008  -39.045 24.852  1.00 26.65 ? 206  ASP A CG  1 
ATOM   1559  O  OD1 . ASP A  1 203 ? 13.509  -39.465 23.772  1.00 26.72 ? 206  ASP A OD1 1 
ATOM   1560  O  OD2 . ASP A  1 203 ? 12.778  -39.783 25.836  1.00 23.84 ? 206  ASP A OD2 1 
ATOM   1561  N  N   . GLY A  1 204 ? 16.070  -37.948 24.624  1.00 25.12 ? 207  GLY A N   1 
ATOM   1562  C  CA  . GLY A  1 204 ? 17.240  -38.114 23.792  1.00 24.82 ? 207  GLY A CA  1 
ATOM   1563  C  C   . GLY A  1 204 ? 16.967  -38.633 22.393  1.00 29.72 ? 207  GLY A C   1 
ATOM   1564  O  O   . GLY A  1 204 ? 17.830  -38.508 21.511  1.00 29.03 ? 207  GLY A O   1 
ATOM   1565  N  N   . ARG A  1 205 ? 15.780  -39.206 22.178  1.00 26.34 ? 208  ARG A N   1 
ATOM   1566  C  CA  . ARG A  1 205 ? 15.436  -39.723 20.860  1.00 30.02 ? 208  ARG A CA  1 
ATOM   1567  C  C   . ARG A  1 205 ? 15.031  -38.615 19.891  1.00 31.65 ? 208  ARG A C   1 
ATOM   1568  O  O   . ARG A  1 205 ? 15.124  -38.782 18.670  1.00 32.19 ? 208  ARG A O   1 
ATOM   1569  C  CB  . ARG A  1 205 ? 14.358  -40.822 20.942  1.00 27.74 ? 208  ARG A CB  1 
ATOM   1570  C  CG  . ARG A  1 205 ? 14.823  -42.050 21.721  1.00 25.12 ? 208  ARG A CG  1 
ATOM   1571  C  CD  . ARG A  1 205 ? 13.646  -42.879 22.198  1.00 26.61 ? 208  ARG A CD  1 
ATOM   1572  N  NE  . ARG A  1 205 ? 13.073  -42.401 23.453  1.00 27.53 ? 208  ARG A NE  1 
ATOM   1573  C  CZ  . ARG A  1 205 ? 11.990  -42.927 24.030  1.00 26.23 ? 208  ARG A CZ  1 
ATOM   1574  N  NH1 . ARG A  1 205 ? 11.397  -43.988 23.499  1.00 24.99 ? 208  ARG A NH1 1 
ATOM   1575  N  NH2 . ARG A  1 205 ? 11.561  -42.463 25.188  1.00 22.19 ? 208  ARG A NH2 1 
ATOM   1576  N  N   . ARG A  1 206 ? 14.635  -37.469 20.442  1.00 31.96 ? 209  ARG A N   1 
ATOM   1577  C  CA  . ARG A  1 206 ? 14.378  -36.272 19.647  1.00 29.97 ? 209  ARG A CA  1 
ATOM   1578  C  C   . ARG A  1 206 ? 15.599  -35.343 19.631  1.00 27.44 ? 209  ARG A C   1 
ATOM   1579  O  O   . ARG A  1 206 ? 16.025  -34.860 18.581  1.00 23.79 ? 209  ARG A O   1 
ATOM   1580  C  CB  . ARG A  1 206 ? 13.161  -35.522 20.210  1.00 33.35 ? 209  ARG A CB  1 
ATOM   1581  C  CG  . ARG A  1 206 ? 11.824  -35.831 19.511  1.00 38.07 ? 209  ARG A CG  1 
ATOM   1582  C  CD  . ARG A  1 206 ? 10.659  -34.952 20.040  1.00 40.96 ? 209  ARG A CD  1 
ATOM   1583  N  NE  . ARG A  1 206 ? 10.439  -35.154 21.468  1.00 42.22 ? 209  ARG A NE  1 
ATOM   1584  C  CZ  . ARG A  1 206 ? 10.600  -34.222 22.408  1.00 43.00 ? 209  ARG A CZ  1 
ATOM   1585  N  NH1 . ARG A  1 206 ? 10.919  -32.976 22.077  1.00 40.77 ? 209  ARG A NH1 1 
ATOM   1586  N  NH2 . ARG A  1 206 ? 10.430  -34.542 23.691  1.00 43.72 ? 209  ARG A NH2 1 
ATOM   1587  N  N   . ASP A  1 207 ? 16.150  -35.090 20.812  1.00 27.33 ? 210  ASP A N   1 
ATOM   1588  C  CA  . ASP A  1 207 ? 17.167  -34.052 21.001  1.00 25.74 ? 210  ASP A CA  1 
ATOM   1589  C  C   . ASP A  1 207 ? 16.942  -32.796 20.164  1.00 23.18 ? 210  ASP A C   1 
ATOM   1590  O  O   . ASP A  1 207 ? 17.842  -32.374 19.439  1.00 19.52 ? 210  ASP A O   1 
ATOM   1591  C  CB  . ASP A  1 207 ? 18.574  -34.590 20.725  1.00 25.08 ? 210  ASP A CB  1 
ATOM   1592  C  CG  . ASP A  1 207 ? 19.656  -33.595 21.146  1.00 27.06 ? 210  ASP A CG  1 
ATOM   1593  O  OD1 . ASP A  1 207 ? 19.420  -32.837 22.113  1.00 26.73 ? 210  ASP A OD1 1 
ATOM   1594  O  OD2 . ASP A  1 207 ? 20.730  -33.556 20.516  1.00 28.91 ? 210  ASP A OD2 1 
ATOM   1595  N  N   . ASP A  1 208 ? 15.737  -32.232 20.215  1.00 21.82 ? 211  ASP A N   1 
ATOM   1596  C  CA  . ASP A  1 208 ? 15.384  -31.176 19.272  1.00 20.99 ? 211  ASP A CA  1 
ATOM   1597  C  C   . ASP A  1 208 ? 15.290  -29.808 19.930  1.00 19.60 ? 211  ASP A C   1 
ATOM   1598  O  O   . ASP A  1 208 ? 14.905  -28.835 19.281  1.00 16.18 ? 211  ASP A O   1 
ATOM   1599  C  CB  . ASP A  1 208 ? 14.116  -31.510 18.470  1.00 23.95 ? 211  ASP A CB  1 
ATOM   1600  C  CG  . ASP A  1 208 ? 12.869  -31.622 19.340  1.00 29.72 ? 211  ASP A CG  1 
ATOM   1601  O  OD1 . ASP A  1 208 ? 12.958  -31.547 20.589  1.00 25.79 ? 211  ASP A OD1 1 
ATOM   1602  O  OD2 . ASP A  1 208 ? 11.787  -31.843 18.756  1.00 33.86 ? 211  ASP A OD2 1 
ATOM   1603  N  N   . GLY A  1 209 ? 15.748  -29.722 21.184  1.00 17.36 ? 212  GLY A N   1 
ATOM   1604  C  CA  . GLY A  1 209 ? 15.849  -28.445 21.892  1.00 15.12 ? 212  GLY A CA  1 
ATOM   1605  C  C   . GLY A  1 209 ? 14.503  -27.854 22.310  1.00 19.52 ? 212  GLY A C   1 
ATOM   1606  O  O   . GLY A  1 209 ? 14.437  -26.682 22.664  1.00 20.78 ? 212  GLY A O   1 
ATOM   1607  N  N   . GLN A  1 210 ? 13.422  -28.634 22.224  1.00 15.38 ? 213  GLN A N   1 
ATOM   1608  C  CA  . GLN A  1 210 ? 12.077  -28.122 22.538  1.00 16.86 ? 213  GLN A CA  1 
ATOM   1609  C  C   . GLN A  1 210 ? 11.477  -28.938 23.681  1.00 17.56 ? 213  GLN A C   1 
ATOM   1610  O  O   . GLN A  1 210 ? 11.053  -30.075 23.485  1.00 24.86 ? 213  GLN A O   1 
ATOM   1611  C  CB  . GLN A  1 210 ? 11.123  -28.187 21.320  1.00 17.94 ? 213  GLN A CB  1 
ATOM   1612  C  CG  . GLN A  1 210 ? 11.737  -27.816 19.968  1.00 20.24 ? 213  GLN A CG  1 
ATOM   1613  C  CD  . GLN A  1 210 ? 12.274  -26.389 19.935  1.00 22.47 ? 213  GLN A CD  1 
ATOM   1614  O  OE1 . GLN A  1 210 ? 11.544  -25.431 20.205  1.00 20.05 ? 213  GLN A OE1 1 
ATOM   1615  N  NE2 . GLN A  1 210 ? 13.564  -26.246 19.621  1.00 21.89 ? 213  GLN A NE2 1 
ATOM   1616  N  N   . LEU A  1 211 ? 11.516  -28.403 24.887  1.00 16.38 ? 214  LEU A N   1 
ATOM   1617  C  CA  . LEU A  1 211 ? 11.018  -29.138 26.043  1.00 21.04 ? 214  LEU A CA  1 
ATOM   1618  C  C   . LEU A  1 211 ? 9.545   -28.836 26.346  1.00 21.48 ? 214  LEU A C   1 
ATOM   1619  O  O   . LEU A  1 211 ? 9.144   -27.669 26.404  1.00 18.08 ? 214  LEU A O   1 
ATOM   1620  C  CB  . LEU A  1 211 ? 11.889  -28.862 27.262  1.00 18.69 ? 214  LEU A CB  1 
ATOM   1621  C  CG  . LEU A  1 211 ? 11.361  -29.405 28.583  1.00 20.33 ? 214  LEU A CG  1 
ATOM   1622  C  CD1 . LEU A  1 211 ? 11.635  -30.937 28.669  1.00 18.14 ? 214  LEU A CD1 1 
ATOM   1623  C  CD2 . LEU A  1 211 ? 12.071  -28.640 29.720  1.00 16.65 ? 214  LEU A CD2 1 
ATOM   1624  N  N   . ASP A  1 212 ? 8.740   -29.894 26.482  1.00 21.80 ? 215  ASP A N   1 
ATOM   1625  C  CA  . ASP A  1 212 ? 7.301   -29.743 26.681  1.00 23.94 ? 215  ASP A CA  1 
ATOM   1626  C  C   . ASP A  1 212 ? 7.006   -29.463 28.160  1.00 23.70 ? 215  ASP A C   1 
ATOM   1627  O  O   . ASP A  1 212 ? 7.800   -29.817 29.031  1.00 26.27 ? 215  ASP A O   1 
ATOM   1628  C  CB  . ASP A  1 212 ? 6.539   -30.991 26.157  1.00 23.54 ? 215  ASP A CB  1 
ATOM   1629  C  CG  . ASP A  1 212 ? 6.624   -32.170 27.106  1.00 24.22 ? 215  ASP A CG  1 
ATOM   1630  O  OD1 . ASP A  1 212 ? 6.082   -32.081 28.234  1.00 24.53 ? 215  ASP A OD1 1 
ATOM   1631  O  OD2 . ASP A  1 212 ? 7.241   -33.196 26.734  1.00 27.25 ? 215  ASP A OD2 1 
ATOM   1632  N  N   . MET A  1 213 ? 5.872   -28.832 28.448  1.00 22.16 ? 216  MET A N   1 
ATOM   1633  C  CA  . MET A  1 213 ? 5.570   -28.394 29.814  1.00 21.09 ? 216  MET A CA  1 
ATOM   1634  C  C   . MET A  1 213 ? 5.264   -29.542 30.814  1.00 24.50 ? 216  MET A C   1 
ATOM   1635  O  O   . MET A  1 213 ? 5.505   -29.411 32.017  1.00 25.12 ? 216  MET A O   1 
ATOM   1636  C  CB  . MET A  1 213 ? 4.434   -27.370 29.799  1.00 18.78 ? 216  MET A CB  1 
ATOM   1637  C  CG  . MET A  1 213 ? 4.764   -26.060 29.078  1.00 22.05 ? 216  MET A CG  1 
ATOM   1638  S  SD  . MET A  1 213 ? 6.233   -25.191 29.728  1.00 21.03 ? 216  MET A SD  1 
ATOM   1639  C  CE  . MET A  1 213 ? 7.488   -25.734 28.576  1.00 19.23 ? 216  MET A CE  1 
ATOM   1640  N  N   . ASP A  1 214 ? 4.755   -30.665 30.320  1.00 20.91 ? 217  ASP A N   1 
ATOM   1641  C  CA  A ASP A  1 214 ? 4.583   -31.889 31.122  0.50 24.21 ? 217  ASP A CA  1 
ATOM   1642  C  CA  B ASP A  1 214 ? 4.581   -31.822 31.181  0.50 22.06 ? 217  ASP A CA  1 
ATOM   1643  C  C   . ASP A  1 214 ? 5.932   -32.341 31.686  1.00 23.02 ? 217  ASP A C   1 
ATOM   1644  O  O   . ASP A  1 214 ? 6.077   -32.651 32.870  1.00 20.81 ? 217  ASP A O   1 
ATOM   1645  C  CB  A ASP A  1 214 ? 3.983   -33.006 30.236  0.50 25.71 ? 217  ASP A CB  1 
ATOM   1646  C  CB  B ASP A  1 214 ? 3.779   -32.920 30.467  0.50 20.38 ? 217  ASP A CB  1 
ATOM   1647  C  CG  A ASP A  1 214 ? 3.584   -34.255 31.024  0.50 29.23 ? 217  ASP A CG  1 
ATOM   1648  C  CG  B ASP A  1 214 ? 2.429   -32.424 29.968  0.50 18.99 ? 217  ASP A CG  1 
ATOM   1649  O  OD1 A ASP A  1 214 ? 4.430   -34.790 31.782  0.50 29.48 ? 217  ASP A OD1 1 
ATOM   1650  O  OD1 B ASP A  1 214 ? 1.734   -31.689 30.706  0.50 19.35 ? 217  ASP A OD1 1 
ATOM   1651  O  OD2 A ASP A  1 214 ? 2.448   -34.756 30.814  0.50 29.00 ? 217  ASP A OD2 1 
ATOM   1652  O  OD2 B ASP A  1 214 ? 2.081   -32.726 28.816  0.50 21.80 ? 217  ASP A OD2 1 
ATOM   1653  N  N   . ALA A  1 215 ? 6.919   -32.425 30.801  1.00 21.72 ? 218  ALA A N   1 
ATOM   1654  C  CA  . ALA A  1 215 ? 8.234   -32.896 31.202  1.00 19.97 ? 218  ALA A CA  1 
ATOM   1655  C  C   . ALA A  1 215 ? 8.968   -31.868 32.086  1.00 20.76 ? 218  ALA A C   1 
ATOM   1656  O  O   . ALA A  1 215 ? 9.646   -32.243 33.038  1.00 21.91 ? 218  ALA A O   1 
ATOM   1657  C  CB  . ALA A  1 215 ? 9.065   -33.263 29.973  1.00 19.69 ? 218  ALA A CB  1 
ATOM   1658  N  N   . ALA A  1 216 ? 8.771   -30.579 31.804  1.00 18.78 ? 219  ALA A N   1 
ATOM   1659  C  CA  . ALA A  1 216 ? 9.386   -29.511 32.577  1.00 21.12 ? 219  ALA A CA  1 
ATOM   1660  C  C   . ALA A  1 216 ? 8.907   -29.497 34.029  1.00 19.73 ? 219  ALA A C   1 
ATOM   1661  O  O   . ALA A  1 216 ? 9.713   -29.368 34.932  1.00 18.03 ? 219  ALA A O   1 
ATOM   1662  C  CB  . ALA A  1 216 ? 9.133   -28.140 31.919  1.00 19.19 ? 219  ALA A CB  1 
ATOM   1663  N  N   . ARG A  1 217 ? 7.595   -29.612 34.239  1.00 22.68 ? 220  ARG A N   1 
ATOM   1664  C  CA  . ARG A  1 217 ? 7.025   -29.710 35.587  1.00 23.63 ? 220  ARG A CA  1 
ATOM   1665  C  C   . ARG A  1 217 ? 7.535   -30.951 36.313  1.00 27.42 ? 220  ARG A C   1 
ATOM   1666  O  O   . ARG A  1 217 ? 8.021   -30.888 37.439  1.00 30.02 ? 220  ARG A O   1 
ATOM   1667  C  CB  . ARG A  1 217 ? 5.503   -29.761 35.535  1.00 23.67 ? 220  ARG A CB  1 
ATOM   1668  C  CG  . ARG A  1 217 ? 4.879   -29.776 36.917  1.00 23.80 ? 220  ARG A CG  1 
ATOM   1669  C  CD  . ARG A  1 217 ? 3.382   -29.616 36.871  1.00 20.10 ? 220  ARG A CD  1 
ATOM   1670  N  NE  . ARG A  1 217 ? 2.971   -28.294 36.410  1.00 21.38 ? 220  ARG A NE  1 
ATOM   1671  C  CZ  . ARG A  1 217 ? 2.769   -27.242 37.193  1.00 21.14 ? 220  ARG A CZ  1 
ATOM   1672  N  NH1 . ARG A  1 217 ? 3.083   -27.283 38.483  1.00 25.07 ? 220  ARG A NH1 1 
ATOM   1673  N  NH2 . ARG A  1 217 ? 2.299   -26.125 36.673  1.00 20.28 ? 220  ARG A NH2 1 
ATOM   1674  N  N   . SER A  1 218 ? 7.476   -32.079 35.636  1.00 27.31 ? 221  SER A N   1 
ATOM   1675  C  CA  . SER A  1 218 ? 8.016   -33.299 36.193  1.00 29.12 ? 221  SER A CA  1 
ATOM   1676  C  C   . SER A  1 218 ? 9.398   -33.104 36.845  1.00 29.66 ? 221  SER A C   1 
ATOM   1677  O  O   . SER A  1 218 ? 9.601   -33.374 38.043  1.00 24.83 ? 221  SER A O   1 
ATOM   1678  C  CB  . SER A  1 218 ? 8.104   -34.337 35.091  1.00 28.28 ? 221  SER A CB  1 
ATOM   1679  O  OG  . SER A  1 218 ? 7.847   -35.592 35.639  1.00 32.34 ? 221  SER A OG  1 
ATOM   1680  N  N   . PHE A  1 219 ? 10.365  -32.725 36.016  1.00 29.04 ? 222  PHE A N   1 
ATOM   1681  C  CA  . PHE A  1 219 ? 11.717  -32.429 36.481  1.00 26.89 ? 222  PHE A CA  1 
ATOM   1682  C  C   . PHE A  1 219 ? 11.782  -31.370 37.579  1.00 27.02 ? 222  PHE A C   1 
ATOM   1683  O  O   . PHE A  1 219 ? 12.397  -31.589 38.618  1.00 28.23 ? 222  PHE A O   1 
ATOM   1684  C  CB  . PHE A  1 219 ? 12.571  -31.992 35.302  1.00 22.96 ? 222  PHE A CB  1 
ATOM   1685  C  CG  . PHE A  1 219 ? 13.009  -33.128 34.424  1.00 21.83 ? 222  PHE A CG  1 
ATOM   1686  C  CD1 . PHE A  1 219 ? 13.942  -34.040 34.876  1.00 18.79 ? 222  PHE A CD1 1 
ATOM   1687  C  CD2 . PHE A  1 219 ? 12.504  -33.265 33.130  1.00 19.92 ? 222  PHE A CD2 1 
ATOM   1688  C  CE1 . PHE A  1 219 ? 14.439  -35.022 34.028  1.00 20.72 ? 222  PHE A CE1 1 
ATOM   1689  C  CE2 . PHE A  1 219 ? 12.969  -34.248 32.292  1.00 18.60 ? 222  PHE A CE2 1 
ATOM   1690  C  CZ  . PHE A  1 219 ? 13.933  -35.144 32.749  1.00 20.33 ? 222  PHE A CZ  1 
ATOM   1691  N  N   . PHE A  1 220 ? 11.170  -30.216 37.338  1.00 24.27 ? 223  PHE A N   1 
ATOM   1692  C  CA  . PHE A  1 220 ? 11.413  -29.046 38.189  1.00 24.14 ? 223  PHE A CA  1 
ATOM   1693  C  C   . PHE A  1 220 ? 10.659  -29.158 39.521  1.00 26.19 ? 223  PHE A C   1 
ATOM   1694  O  O   . PHE A  1 220 ? 11.140  -28.673 40.556  1.00 24.53 ? 223  PHE A O   1 
ATOM   1695  C  CB  . PHE A  1 220 ? 10.983  -27.767 37.472  1.00 19.57 ? 223  PHE A CB  1 
ATOM   1696  C  CG  . PHE A  1 220 ? 12.016  -27.213 36.528  1.00 23.48 ? 223  PHE A CG  1 
ATOM   1697  C  CD1 . PHE A  1 220 ? 13.070  -26.430 37.004  1.00 20.69 ? 223  PHE A CD1 1 
ATOM   1698  C  CD2 . PHE A  1 220 ? 11.907  -27.420 35.153  1.00 21.93 ? 223  PHE A CD2 1 
ATOM   1699  C  CE1 . PHE A  1 220 ? 13.991  -25.864 36.137  1.00 19.82 ? 223  PHE A CE1 1 
ATOM   1700  C  CE2 . PHE A  1 220 ? 12.805  -26.829 34.269  1.00 21.23 ? 223  PHE A CE2 1 
ATOM   1701  C  CZ  . PHE A  1 220 ? 13.860  -26.051 34.768  1.00 23.52 ? 223  PHE A CZ  1 
ATOM   1702  N  N   . GLN A  1 221 ? 9.467   -29.757 39.486  1.00 23.00 ? 224  GLN A N   1 
ATOM   1703  C  CA  . GLN A  1 221 ? 8.635   -29.885 40.686  1.00 25.83 ? 224  GLN A CA  1 
ATOM   1704  C  C   . GLN A  1 221 ? 8.796   -31.223 41.408  1.00 27.61 ? 224  GLN A C   1 
ATOM   1705  O  O   . GLN A  1 221 ? 8.989   -31.247 42.622  1.00 25.90 ? 224  GLN A O   1 
ATOM   1706  C  CB  . GLN A  1 221 ? 7.154   -29.614 40.387  1.00 28.61 ? 224  GLN A CB  1 
ATOM   1707  C  CG  . GLN A  1 221 ? 6.244   -29.727 41.622  1.00 28.66 ? 224  GLN A CG  1 
ATOM   1708  C  CD  . GLN A  1 221 ? 4.856   -29.132 41.415  1.00 29.22 ? 224  GLN A CD  1 
ATOM   1709  O  OE1 . GLN A  1 221 ? 4.325   -29.129 40.300  1.00 29.33 ? 224  GLN A OE1 1 
ATOM   1710  N  NE2 . GLN A  1 221 ? 4.220   -28.719 42.513  1.00 28.21 ? 224  GLN A NE2 1 
ATOM   1711  N  N   . PHE A  1 222 ? 8.761   -32.331 40.667  1.00 27.86 ? 225  PHE A N   1 
ATOM   1712  C  CA  . PHE A  1 222 ? 8.643   -33.639 41.298  1.00 28.45 ? 225  PHE A CA  1 
ATOM   1713  C  C   . PHE A  1 222 ? 9.924   -34.419 41.232  1.00 28.84 ? 225  PHE A C   1 
ATOM   1714  O  O   . PHE A  1 222 ? 10.010  -35.524 41.757  1.00 28.60 ? 225  PHE A O   1 
ATOM   1715  C  CB  . PHE A  1 222 ? 7.486   -34.438 40.706  1.00 32.87 ? 225  PHE A CB  1 
ATOM   1716  C  CG  . PHE A  1 222 ? 6.142   -33.840 40.999  1.00 36.76 ? 225  PHE A CG  1 
ATOM   1717  C  CD1 . PHE A  1 222 ? 5.724   -33.661 42.310  1.00 39.88 ? 225  PHE A CD1 1 
ATOM   1718  C  CD2 . PHE A  1 222 ? 5.323   -33.397 39.973  1.00 38.60 ? 225  PHE A CD2 1 
ATOM   1719  C  CE1 . PHE A  1 222 ? 4.479   -33.080 42.600  1.00 41.19 ? 225  PHE A CE1 1 
ATOM   1720  C  CE2 . PHE A  1 222 ? 4.103   -32.788 40.251  1.00 40.95 ? 225  PHE A CE2 1 
ATOM   1721  C  CZ  . PHE A  1 222 ? 3.686   -32.621 41.569  1.00 41.07 ? 225  PHE A CZ  1 
ATOM   1722  N  N   . SER A  1 223 ? 10.949  -33.810 40.645  1.00 29.89 ? 226  SER A N   1 
ATOM   1723  C  CA  . SER A  1 223 ? 12.213  -34.491 40.467  1.00 26.82 ? 226  SER A CA  1 
ATOM   1724  C  C   . SER A  1 223 ? 11.970  -35.875 39.899  1.00 25.72 ? 226  SER A C   1 
ATOM   1725  O  O   . SER A  1 223 ? 12.578  -36.854 40.338  1.00 27.41 ? 226  SER A O   1 
ATOM   1726  C  CB  . SER A  1 223 ? 12.963  -34.569 41.799  1.00 29.91 ? 226  SER A CB  1 
ATOM   1727  O  OG  . SER A  1 223 ? 12.676  -33.420 42.592  1.00 26.70 ? 226  SER A OG  1 
ATOM   1728  N  N   . ARG A  1 224 ? 11.144  -35.925 38.854  1.00 26.95 ? 227  ARG A N   1 
ATOM   1729  C  CA  . ARG A  1 224 ? 10.789  -37.164 38.166  1.00 25.95 ? 227  ARG A CA  1 
ATOM   1730  C  C   . ARG A  1 224 ? 11.002  -37.101 36.649  1.00 25.78 ? 227  ARG A C   1 
ATOM   1731  O  O   . ARG A  1 224 ? 10.426  -36.265 35.944  1.00 25.88 ? 227  ARG A O   1 
ATOM   1732  C  CB  . ARG A  1 224 ? 9.337   -37.551 38.457  1.00 27.44 ? 227  ARG A CB  1 
ATOM   1733  C  CG  . ARG A  1 224 ? 8.979   -38.920 37.900  1.00 33.87 ? 227  ARG A CG  1 
ATOM   1734  C  CD  . ARG A  1 224 ? 7.496   -39.265 38.002  1.00 38.86 ? 227  ARG A CD  1 
ATOM   1735  N  NE  . ARG A  1 224 ? 6.807   -38.513 39.041  1.00 42.93 ? 227  ARG A NE  1 
ATOM   1736  C  CZ  . ARG A  1 224 ? 5.730   -38.949 39.687  1.00 46.07 ? 227  ARG A CZ  1 
ATOM   1737  N  NH1 . ARG A  1 224 ? 5.252   -40.169 39.443  1.00 47.11 ? 227  ARG A NH1 1 
ATOM   1738  N  NH2 . ARG A  1 224 ? 5.167   -38.188 40.619  1.00 47.86 ? 227  ARG A NH2 1 
ATOM   1739  N  N   . MET A  1 225 ? 11.719  -38.082 36.129  1.00 27.26 ? 228  MET A N   1 
ATOM   1740  C  CA  . MET A  1 225 ? 11.789  -38.271 34.694  1.00 29.62 ? 228  MET A CA  1 
ATOM   1741  C  C   . MET A  1 225 ? 10.442  -38.646 34.088  1.00 31.71 ? 228  MET A C   1 
ATOM   1742  O  O   . MET A  1 225 ? 9.654   -39.378 34.699  1.00 35.14 ? 228  MET A O   1 
ATOM   1743  C  CB  . MET A  1 225 ? 12.819  -39.342 34.370  1.00 30.44 ? 228  MET A CB  1 
ATOM   1744  C  CG  . MET A  1 225 ? 14.210  -38.998 34.864  1.00 27.89 ? 228  MET A CG  1 
ATOM   1745  S  SD  . MET A  1 225 ? 15.243  -40.441 34.625  1.00 31.47 ? 228  MET A SD  1 
ATOM   1746  C  CE  . MET A  1 225 ? 16.782  -39.950 35.418  1.00 29.91 ? 228  MET A CE  1 
ATOM   1747  N  N   . PRO A  1 226 ? 10.180  -38.173 32.866  1.00 32.09 ? 229  PRO A N   1 
ATOM   1748  C  CA  . PRO A  1 226 ? 8.974   -38.617 32.166  1.00 33.15 ? 229  PRO A CA  1 
ATOM   1749  C  C   . PRO A  1 226 ? 9.007   -40.127 32.020  1.00 31.71 ? 229  PRO A C   1 
ATOM   1750  O  O   . PRO A  1 226 ? 10.087  -40.705 32.053  1.00 32.85 ? 229  PRO A O   1 
ATOM   1751  C  CB  . PRO A  1 226 ? 9.109   -37.939 30.792  1.00 33.35 ? 229  PRO A CB  1 
ATOM   1752  C  CG  . PRO A  1 226 ? 9.868   -36.670 31.099  1.00 33.16 ? 229  PRO A CG  1 
ATOM   1753  C  CD  . PRO A  1 226 ? 10.889  -37.107 32.135  1.00 31.19 ? 229  PRO A CD  1 
ATOM   1754  N  N   . ASP A  1 227 ? 7.847   -40.766 31.911  1.00 32.57 ? 230  ASP A N   1 
ATOM   1755  C  CA  . ASP A  1 227 ? 7.796   -42.168 31.480  1.00 36.15 ? 230  ASP A CA  1 
ATOM   1756  C  C   . ASP A  1 227 ? 8.679   -42.383 30.277  1.00 33.50 ? 230  ASP A C   1 
ATOM   1757  O  O   . ASP A  1 227 ? 8.484   -41.741 29.247  1.00 34.06 ? 230  ASP A O   1 
ATOM   1758  C  CB  . ASP A  1 227 ? 6.375   -42.580 31.084  1.00 41.42 ? 230  ASP A CB  1 
ATOM   1759  C  CG  . ASP A  1 227 ? 5.408   -42.481 32.224  1.00 45.68 ? 230  ASP A CG  1 
ATOM   1760  O  OD1 . ASP A  1 227 ? 5.864   -42.583 33.384  1.00 47.88 ? 230  ASP A OD1 1 
ATOM   1761  O  OD2 . ASP A  1 227 ? 4.201   -42.263 31.965  1.00 49.67 ? 230  ASP A OD2 1 
ATOM   1762  N  N   . ASP A  1 228 ? 9.555   -43.376 30.366  1.00 31.65 ? 231  ASP A N   1 
ATOM   1763  C  CA  . ASP A  1 228 ? 10.304  -43.864 29.211  1.00 32.42 ? 231  ASP A CA  1 
ATOM   1764  C  C   . ASP A  1 228 ? 11.302  -42.841 28.690  1.00 33.43 ? 231  ASP A C   1 
ATOM   1765  O  O   . ASP A  1 228 ? 11.747  -42.914 27.528  1.00 30.09 ? 231  ASP A O   1 
ATOM   1766  C  CB  . ASP A  1 228 ? 9.365   -44.315 28.080  1.00 31.30 ? 231  ASP A CB  1 
ATOM   1767  C  CG  . ASP A  1 228 ? 10.091  -45.132 27.023  1.00 32.50 ? 231  ASP A CG  1 
ATOM   1768  O  OD1 . ASP A  1 228 ? 10.817  -46.078 27.400  1.00 32.07 ? 231  ASP A OD1 1 
ATOM   1769  O  OD2 . ASP A  1 228 ? 10.011  -44.781 25.827  1.00 33.28 ? 231  ASP A OD2 1 
ATOM   1770  N  N   . PHE A  1 229 ? 11.669  -41.904 29.565  1.00 33.40 ? 232  PHE A N   1 
ATOM   1771  C  CA  . PHE A  1 229 ? 12.688  -40.908 29.254  1.00 30.38 ? 232  PHE A CA  1 
ATOM   1772  C  C   . PHE A  1 229 ? 14.015  -41.534 28.843  1.00 27.81 ? 232  PHE A C   1 
ATOM   1773  O  O   . PHE A  1 229 ? 14.665  -42.204 29.643  1.00 30.67 ? 232  PHE A O   1 
ATOM   1774  C  CB  . PHE A  1 229 ? 12.922  -40.006 30.466  1.00 29.68 ? 232  PHE A CB  1 
ATOM   1775  C  CG  . PHE A  1 229 ? 13.859  -38.863 30.201  1.00 26.45 ? 232  PHE A CG  1 
ATOM   1776  C  CD1 . PHE A  1 229 ? 13.435  -37.754 29.462  1.00 28.54 ? 232  PHE A CD1 1 
ATOM   1777  C  CD2 . PHE A  1 229 ? 15.141  -38.866 30.720  1.00 25.39 ? 232  PHE A CD2 1 
ATOM   1778  C  CE1 . PHE A  1 229 ? 14.286  -36.667 29.248  1.00 23.97 ? 232  PHE A CE1 1 
ATOM   1779  C  CE2 . PHE A  1 229 ? 15.998  -37.788 30.512  1.00 26.24 ? 232  PHE A CE2 1 
ATOM   1780  C  CZ  . PHE A  1 229 ? 15.563  -36.686 29.769  1.00 24.69 ? 232  PHE A CZ  1 
ATOM   1781  N  N   . PHE A  1 230 ? 14.453  -41.246 27.622  1.00 25.97 ? 233  PHE A N   1 
ATOM   1782  C  CA  . PHE A  1 230 ? 15.842  -41.449 27.242  1.00 25.73 ? 233  PHE A CA  1 
ATOM   1783  C  C   . PHE A  1 230 ? 16.691  -40.204 27.548  1.00 28.65 ? 233  PHE A C   1 
ATOM   1784  O  O   . PHE A  1 230 ? 16.270  -39.060 27.297  1.00 25.56 ? 233  PHE A O   1 
ATOM   1785  C  CB  . PHE A  1 230 ? 15.941  -41.766 25.746  1.00 29.02 ? 233  PHE A CB  1 
ATOM   1786  C  CG  . PHE A  1 230 ? 15.673  -43.219 25.396  1.00 30.90 ? 233  PHE A CG  1 
ATOM   1787  C  CD1 . PHE A  1 230 ? 14.618  -43.906 25.974  1.00 29.43 ? 233  PHE A CD1 1 
ATOM   1788  C  CD2 . PHE A  1 230 ? 16.417  -43.849 24.406  1.00 30.85 ? 233  PHE A CD2 1 
ATOM   1789  C  CE1 . PHE A  1 230 ? 14.313  -45.200 25.592  1.00 33.25 ? 233  PHE A CE1 1 
ATOM   1790  C  CE2 . PHE A  1 230 ? 16.127  -45.153 24.017  1.00 34.53 ? 233  PHE A CE2 1 
ATOM   1791  C  CZ  . PHE A  1 230 ? 15.083  -45.842 24.638  1.00 35.31 ? 233  PHE A CZ  1 
ATOM   1792  N  N   . ARG A  1 231 ? 17.919  -40.430 28.004  1.00 27.71 ? 234  ARG A N   1 
ATOM   1793  C  CA  . ARG A  1 231 ? 18.891  -39.355 28.112  1.00 26.38 ? 234  ARG A CA  1 
ATOM   1794  C  C   . ARG A  1 231 ? 19.356  -38.870 26.750  1.00 26.69 ? 234  ARG A C   1 
ATOM   1795  O  O   . ARG A  1 231 ? 19.104  -39.508 25.721  1.00 27.01 ? 234  ARG A O   1 
ATOM   1796  C  CB  . ARG A  1 231 ? 20.095  -39.804 28.924  1.00 25.70 ? 234  ARG A CB  1 
ATOM   1797  C  CG  . ARG A  1 231 ? 21.006  -40.749 28.170  1.00 27.06 ? 234  ARG A CG  1 
ATOM   1798  C  CD  . ARG A  1 231 ? 22.244  -41.114 28.998  1.00 26.61 ? 234  ARG A CD  1 
ATOM   1799  N  NE  . ARG A  1 231 ? 23.180  -41.901 28.209  1.00 27.29 ? 234  ARG A NE  1 
ATOM   1800  C  CZ  . ARG A  1 231 ? 24.062  -42.755 28.718  1.00 28.54 ? 234  ARG A CZ  1 
ATOM   1801  N  NH1 . ARG A  1 231 ? 24.186  -42.897 30.039  1.00 26.76 ? 234  ARG A NH1 1 
ATOM   1802  N  NH2 . ARG A  1 231 ? 24.853  -43.433 27.899  1.00 24.54 ? 234  ARG A NH2 1 
ATOM   1803  N  N   . ALA A  1 232 ? 20.083  -37.755 26.759  1.00 25.15 ? 235  ALA A N   1 
ATOM   1804  C  CA  . ALA A  1 232 ? 20.539  -37.111 25.545  1.00 21.68 ? 235  ALA A CA  1 
ATOM   1805  C  C   . ALA A  1 232 ? 21.498  -38.051 24.832  1.00 23.24 ? 235  ALA A C   1 
ATOM   1806  O  O   . ALA A  1 232 ? 22.111  -38.897 25.478  1.00 24.17 ? 235  ALA A O   1 
ATOM   1807  C  CB  . ALA A  1 232 ? 21.246  -35.795 25.904  1.00 22.65 ? 235  ALA A CB  1 
ATOM   1808  N  N   . PRO A  1 233 ? 21.646  -37.893 23.502  1.00 23.48 ? 236  PRO A N   1 
ATOM   1809  C  CA  . PRO A  1 233 ? 22.418  -38.812 22.657  1.00 25.81 ? 236  PRO A CA  1 
ATOM   1810  C  C   . PRO A  1 233 ? 23.914  -38.547 22.646  1.00 26.61 ? 236  PRO A C   1 
ATOM   1811  O  O   . PRO A  1 233 ? 24.632  -39.189 21.875  1.00 25.05 ? 236  PRO A O   1 
ATOM   1812  C  CB  . PRO A  1 233 ? 21.867  -38.547 21.241  1.00 24.38 ? 236  PRO A CB  1 
ATOM   1813  C  CG  . PRO A  1 233 ? 21.290  -37.204 21.303  1.00 25.92 ? 236  PRO A CG  1 
ATOM   1814  C  CD  . PRO A  1 233 ? 20.716  -37.082 22.701  1.00 24.72 ? 236  PRO A CD  1 
ATOM   1815  N  N   . SER A  1 234 ? 24.363  -37.545 23.403  1.00 25.90 ? 237  SER A N   1 
ATOM   1816  C  CA  . SER A  1 234 ? 25.797  -37.289 23.562  1.00 27.18 ? 237  SER A CA  1 
ATOM   1817  C  C   . SER A  1 234 ? 26.042  -36.441 24.807  1.00 26.19 ? 237  SER A C   1 
ATOM   1818  O  O   . SER A  1 234 ? 25.097  -35.955 25.427  1.00 24.66 ? 237  SER A O   1 
ATOM   1819  C  CB  . SER A  1 234 ? 26.339  -36.564 22.332  1.00 29.30 ? 237  SER A CB  1 
ATOM   1820  O  OG  . SER A  1 234 ? 25.638  -35.342 22.155  1.00 32.00 ? 237  SER A OG  1 
ATOM   1821  N  N   . PRO A  1 235 ? 27.313  -36.264 25.194  1.00 25.37 ? 238  PRO A N   1 
ATOM   1822  C  CA  . PRO A  1 235 ? 27.490  -35.517 26.442  1.00 24.61 ? 238  PRO A CA  1 
ATOM   1823  C  C   . PRO A  1 235 ? 27.423  -34.010 26.153  1.00 24.62 ? 238  PRO A C   1 
ATOM   1824  O  O   . PRO A  1 235 ? 27.979  -33.543 25.158  1.00 23.68 ? 238  PRO A O   1 
ATOM   1825  C  CB  . PRO A  1 235 ? 28.902  -35.921 26.913  1.00 23.49 ? 238  PRO A CB  1 
ATOM   1826  C  CG  . PRO A  1 235 ? 29.360  -37.050 25.989  1.00 22.77 ? 238  PRO A CG  1 
ATOM   1827  C  CD  . PRO A  1 235 ? 28.572  -36.857 24.709  1.00 25.39 ? 238  PRO A CD  1 
ATOM   1828  N  N   . ARG A  1 236 ? 26.685  -33.267 26.965  1.00 22.01 ? 239  ARG A N   1 
ATOM   1829  C  CA  . ARG A  1 236 ? 26.627  -31.821 26.779  1.00 21.72 ? 239  ARG A CA  1 
ATOM   1830  C  C   . ARG A  1 236 ? 26.295  -31.125 28.087  1.00 22.72 ? 239  ARG A C   1 
ATOM   1831  O  O   . ARG A  1 236 ? 25.891  -31.772 29.065  1.00 22.78 ? 239  ARG A O   1 
ATOM   1832  C  CB  . ARG A  1 236 ? 25.616  -31.451 25.687  1.00 20.11 ? 239  ARG A CB  1 
ATOM   1833  C  CG  . ARG A  1 236 ? 24.158  -31.467 26.135  1.00 22.56 ? 239  ARG A CG  1 
ATOM   1834  C  CD  . ARG A  1 236 ? 23.526  -32.869 26.093  1.00 20.47 ? 239  ARG A CD  1 
ATOM   1835  N  NE  . ARG A  1 236 ? 23.614  -33.483 24.769  1.00 21.91 ? 239  ARG A NE  1 
ATOM   1836  C  CZ  . ARG A  1 236 ? 22.748  -33.295 23.775  1.00 21.47 ? 239  ARG A CZ  1 
ATOM   1837  N  NH1 . ARG A  1 236 ? 21.680  -32.516 23.926  1.00 22.62 ? 239  ARG A NH1 1 
ATOM   1838  N  NH2 . ARG A  1 236 ? 22.947  -33.894 22.620  1.00 22.11 ? 239  ARG A NH2 1 
ATOM   1839  N  N   . SER A  1 237 ? 26.525  -29.820 28.140  1.00 20.62 ? 240  SER A N   1 
ATOM   1840  C  CA  . SER A  1 237 ? 25.930  -29.033 29.214  1.00 20.80 ? 240  SER A CA  1 
ATOM   1841  C  C   . SER A  1 237 ? 25.343  -27.744 28.682  1.00 19.44 ? 240  SER A C   1 
ATOM   1842  O  O   . SER A  1 237 ? 24.165  -27.699 28.303  1.00 18.21 ? 240  SER A O   1 
ATOM   1843  C  CB  . SER A  1 237 ? 26.961  -28.749 30.314  1.00 21.06 ? 240  SER A CB  1 
ATOM   1844  O  OG  . SER A  1 237 ? 28.209  -28.402 29.744  1.00 20.89 ? 240  SER A OG  1 
ATOM   1845  N  N   . GLY A  1 238 ? 26.193  -26.724 28.566  1.00 17.88 ? 241  GLY A N   1 
ATOM   1846  C  CA  . GLY A  1 238 ? 25.716  -25.375 28.294  1.00 20.57 ? 241  GLY A CA  1 
ATOM   1847  C  C   . GLY A  1 238 ? 25.788  -24.970 26.835  1.00 21.88 ? 241  GLY A C   1 
ATOM   1848  O  O   . GLY A  1 238 ? 25.958  -23.798 26.533  1.00 24.71 ? 241  GLY A O   1 
ATOM   1849  N  N   . THR A  1 239 ? 25.686  -25.928 25.921  1.00 22.81 ? 242  THR A N   1 
ATOM   1850  C  CA  . THR A  1 239 ? 25.603  -25.583 24.496  1.00 24.47 ? 242  THR A CA  1 
ATOM   1851  C  C   . THR A  1 239 ? 24.506  -24.541 24.216  1.00 20.44 ? 242  THR A C   1 
ATOM   1852  O  O   . THR A  1 239 ? 23.354  -24.729 24.596  1.00 20.93 ? 242  THR A O   1 
ATOM   1853  C  CB  . THR A  1 239 ? 25.351  -26.811 23.617  1.00 26.28 ? 242  THR A CB  1 
ATOM   1854  O  OG1 . THR A  1 239 ? 26.323  -27.809 23.922  1.00 30.93 ? 242  THR A OG1 1 
ATOM   1855  C  CG2 . THR A  1 239 ? 25.478  -26.443 22.137  1.00 28.25 ? 242  THR A CG2 1 
ATOM   1856  N  N   . GLY A  1 240 ? 24.877  -23.459 23.536  1.00 16.15 ? 243  GLY A N   1 
ATOM   1857  C  CA  . GLY A  1 240 ? 23.953  -22.366 23.233  1.00 16.26 ? 243  GLY A CA  1 
ATOM   1858  C  C   . GLY A  1 240 ? 23.930  -21.226 24.241  1.00 16.24 ? 243  GLY A C   1 
ATOM   1859  O  O   . GLY A  1 240 ? 23.074  -20.358 24.175  1.00 15.05 ? 243  GLY A O   1 
ATOM   1860  N  N   . VAL A  1 241 ? 24.841  -21.231 25.204  1.00 14.83 ? 244  VAL A N   1 
ATOM   1861  C  CA  . VAL A  1 241 ? 24.796  -20.200 26.227  1.00 14.75 ? 244  VAL A CA  1 
ATOM   1862  C  C   . VAL A  1 241 ? 24.945  -18.799 25.601  1.00 16.07 ? 244  VAL A C   1 
ATOM   1863  O  O   . VAL A  1 241 ? 24.290  -17.843 26.031  1.00 17.30 ? 244  VAL A O   1 
ATOM   1864  C  CB  . VAL A  1 241 ? 25.849  -20.463 27.325  1.00 19.10 ? 244  VAL A CB  1 
ATOM   1865  C  CG1 . VAL A  1 241 ? 27.235  -20.067 26.833  1.00 15.86 ? 244  VAL A CG1 1 
ATOM   1866  C  CG2 . VAL A  1 241 ? 25.470  -19.740 28.637  1.00 18.17 ? 244  VAL A CG2 1 
ATOM   1867  N  N   . GLU A  1 242 ? 25.695  -18.707 24.503  1.00 14.90 ? 245  GLU A N   1 
ATOM   1868  C  CA  . GLU A  1 242 ? 25.928  -17.423 23.854  1.00 20.14 ? 245  GLU A CA  1 
ATOM   1869  C  C   . GLU A  1 242 ? 24.628  -16.804 23.370  1.00 21.18 ? 245  GLU A C   1 
ATOM   1870  O  O   . GLU A  1 242 ? 24.497  -15.582 23.352  1.00 22.68 ? 245  GLU A O   1 
ATOM   1871  C  CB  . GLU A  1 242 ? 26.908  -17.545 22.671  1.00 19.44 ? 245  GLU A CB  1 
ATOM   1872  C  CG  . GLU A  1 242 ? 26.407  -18.385 21.508  1.00 22.37 ? 245  GLU A CG  1 
ATOM   1873  C  CD  . GLU A  1 242 ? 26.712  -19.876 21.667  1.00 26.49 ? 245  GLU A CD  1 
ATOM   1874  O  OE1 . GLU A  1 242 ? 27.102  -20.323 22.774  1.00 27.27 ? 245  GLU A OE1 1 
ATOM   1875  O  OE2 . GLU A  1 242 ? 26.538  -20.613 20.675  1.00 29.50 ? 245  GLU A OE2 1 
ATOM   1876  N  N   . VAL A  1 243 ? 23.670  -17.657 22.998  1.00 20.37 ? 246  VAL A N   1 
ATOM   1877  C  CA  . VAL A  1 243 ? 22.340  -17.214 22.576  1.00 19.73 ? 246  VAL A CA  1 
ATOM   1878  C  C   . VAL A  1 243 ? 21.625  -16.511 23.725  1.00 19.21 ? 246  VAL A C   1 
ATOM   1879  O  O   . VAL A  1 243 ? 21.077  -15.418 23.563  1.00 20.04 ? 246  VAL A O   1 
ATOM   1880  C  CB  . VAL A  1 243 ? 21.491  -18.414 22.087  1.00 18.19 ? 246  VAL A CB  1 
ATOM   1881  C  CG1 . VAL A  1 243 ? 20.123  -17.976 21.682  1.00 13.07 ? 246  VAL A CG1 1 
ATOM   1882  C  CG2 . VAL A  1 243 ? 22.208  -19.100 20.915  1.00 17.73 ? 246  VAL A CG2 1 
ATOM   1883  N  N   . VAL A  1 244 ? 21.744  -17.082 24.913  1.00 16.88 ? 247  VAL A N   1 
ATOM   1884  C  CA  . VAL A  1 244 ? 21.041  -16.549 26.069  1.00 14.91 ? 247  VAL A CA  1 
ATOM   1885  C  C   . VAL A  1 244 ? 21.700  -15.252 26.503  1.00 14.72 ? 247  VAL A C   1 
ATOM   1886  O  O   . VAL A  1 244 ? 21.032  -14.268 26.799  1.00 17.23 ? 247  VAL A O   1 
ATOM   1887  C  CB  . VAL A  1 244 ? 21.033  -17.570 27.225  1.00 14.65 ? 247  VAL A CB  1 
ATOM   1888  C  CG1 . VAL A  1 244 ? 20.251  -17.037 28.399  1.00 16.34 ? 247  VAL A CG1 1 
ATOM   1889  C  CG2 . VAL A  1 244 ? 20.422  -18.860 26.758  1.00 14.44 ? 247  VAL A CG2 1 
ATOM   1890  N  N   . ILE A  1 245 ? 23.018  -15.215 26.416  1.00 16.18 ? 248  ILE A N   1 
ATOM   1891  C  CA  . ILE A  1 245 ? 23.782  -14.042 26.829  1.00 15.76 ? 248  ILE A CA  1 
ATOM   1892  C  C   . ILE A  1 245 ? 23.486  -12.825 25.943  1.00 16.50 ? 248  ILE A C   1 
ATOM   1893  O  O   . ILE A  1 245 ? 23.240  -11.732 26.441  1.00 20.16 ? 248  ILE A O   1 
ATOM   1894  C  CB  . ILE A  1 245 ? 25.295  -14.370 26.799  1.00 16.44 ? 248  ILE A CB  1 
ATOM   1895  C  CG1 . ILE A  1 245 ? 25.650  -15.375 27.904  1.00 14.53 ? 248  ILE A CG1 1 
ATOM   1896  C  CG2 . ILE A  1 245 ? 26.142  -13.111 26.867  1.00 13.83 ? 248  ILE A CG2 1 
ATOM   1897  C  CD1 . ILE A  1 245 ? 26.997  -16.126 27.643  1.00 16.47 ? 248  ILE A CD1 1 
ATOM   1898  N  N   . GLN A  1 246 ? 23.571  -13.019 24.632  1.00 16.10 ? 249  GLN A N   1 
ATOM   1899  C  CA  . GLN A  1 246 ? 23.314  -11.983 23.652  1.00 18.28 ? 249  GLN A CA  1 
ATOM   1900  C  C   . GLN A  1 246 ? 21.838  -11.560 23.536  1.00 18.65 ? 249  GLN A C   1 
ATOM   1901  O  O   . GLN A  1 246 ? 21.552  -10.487 23.028  1.00 19.07 ? 249  GLN A O   1 
ATOM   1902  C  CB  . GLN A  1 246 ? 23.810  -12.432 22.276  1.00 19.04 ? 249  GLN A CB  1 
ATOM   1903  C  CG  . GLN A  1 246 ? 25.257  -12.146 22.012  1.00 27.23 ? 249  GLN A CG  1 
ATOM   1904  C  CD  . GLN A  1 246 ? 25.631  -10.722 22.339  1.00 29.80 ? 249  GLN A CD  1 
ATOM   1905  O  OE1 . GLN A  1 246 ? 25.005  -9.775  21.862  1.00 34.66 ? 249  GLN A OE1 1 
ATOM   1906  N  NE2 . GLN A  1 246 ? 26.628  -10.560 23.192  1.00 30.94 ? 249  GLN A NE2 1 
ATOM   1907  N  N   . ALA A  1 247 ? 20.899  -12.444 23.861  1.00 17.36 ? 250  ALA A N   1 
ATOM   1908  C  CA  . ALA A  1 247 ? 19.469  -12.062 23.786  1.00 16.94 ? 250  ALA A CA  1 
ATOM   1909  C  C   . ALA A  1 247 ? 19.195  -10.763 24.548  1.00 17.96 ? 250  ALA A C   1 
ATOM   1910  O  O   . ALA A  1 247 ? 18.367  -9.952  24.131  1.00 19.68 ? 250  ALA A O   1 
ATOM   1911  C  CB  . ALA A  1 247 ? 18.584  -13.178 24.323  1.00 13.42 ? 250  ALA A CB  1 
ATOM   1912  N  N   . HIS A  1 248 ? 19.821  -10.615 25.717  1.00 16.20 ? 251  HIS A N   1 
ATOM   1913  C  CA  . HIS A  1 248 ? 19.641  -9.414  26.529  1.00 15.40 ? 251  HIS A CA  1 
ATOM   1914  C  C   . HIS A  1 248 ? 20.929  -9.086  27.297  1.00 16.91 ? 251  HIS A C   1 
ATOM   1915  O  O   . HIS A  1 248 ? 21.096  -9.475  28.466  1.00 13.68 ? 251  HIS A O   1 
ATOM   1916  C  CB  . HIS A  1 248 ? 18.466  -9.576  27.504  1.00 14.56 ? 251  HIS A CB  1 
ATOM   1917  C  CG  . HIS A  1 248 ? 17.120  -9.546  26.842  1.00 17.28 ? 251  HIS A CG  1 
ATOM   1918  N  ND1 . HIS A  1 248 ? 16.600  -8.410  26.256  1.00 15.77 ? 251  HIS A ND1 1 
ATOM   1919  C  CD2 . HIS A  1 248 ? 16.195  -10.519 26.653  1.00 16.07 ? 251  HIS A CD2 1 
ATOM   1920  C  CE1 . HIS A  1 248 ? 15.422  -8.684  25.722  1.00 14.76 ? 251  HIS A CE1 1 
ATOM   1921  N  NE2 . HIS A  1 248 ? 15.150  -9.956  25.952  1.00 17.52 ? 251  HIS A NE2 1 
ATOM   1922  N  N   . PRO A  1 249 ? 21.829  -8.333  26.664  1.00 16.38 ? 252  PRO A N   1 
ATOM   1923  C  CA  . PRO A  1 249 ? 23.135  -8.068  27.293  1.00 16.93 ? 252  PRO A CA  1 
ATOM   1924  C  C   . PRO A  1 249 ? 22.995  -7.524  28.708  1.00 19.27 ? 252  PRO A C   1 
ATOM   1925  O  O   . PRO A  1 249 ? 22.050  -6.774  28.996  1.00 19.45 ? 252  PRO A O   1 
ATOM   1926  C  CB  . PRO A  1 249 ? 23.768  -7.044  26.356  1.00 16.84 ? 252  PRO A CB  1 
ATOM   1927  C  CG  . PRO A  1 249 ? 23.158  -7.372  24.983  1.00 17.47 ? 252  PRO A CG  1 
ATOM   1928  C  CD  . PRO A  1 249 ? 21.711  -7.732  25.326  1.00 17.19 ? 252  PRO A CD  1 
ATOM   1929  N  N   . MET A  1 250 ? 23.803  -8.044  29.623  1.00 18.88 ? 253  MET A N   1 
ATOM   1930  C  CA  . MET A  1 250 ? 23.755  -7.607  31.031  1.00 22.22 ? 253  MET A CA  1 
ATOM   1931  C  C   . MET A  1 250 ? 25.192  -7.566  31.547  1.00 23.04 ? 253  MET A C   1 
ATOM   1932  O  O   . MET A  1 250 ? 25.972  -8.467  31.266  1.00 20.33 ? 253  MET A O   1 
ATOM   1933  C  CB  . MET A  1 250 ? 22.985  -8.613  31.913  1.00 24.51 ? 253  MET A CB  1 
ATOM   1934  C  CG  . MET A  1 250 ? 21.483  -8.402  32.070  1.00 28.08 ? 253  MET A CG  1 
ATOM   1935  S  SD  . MET A  1 250 ? 20.932  -6.760  32.612  1.00 32.97 ? 253  MET A SD  1 
ATOM   1936  C  CE  . MET A  1 250 ? 21.716  -6.657  34.223  1.00 30.27 ? 253  MET A CE  1 
ATOM   1937  N  N   . GLN A  1 251 ? 25.517  -6.578  32.371  1.00 23.75 ? 254  GLN A N   1 
ATOM   1938  C  CA  . GLN A  1 251 ? 26.774  -6.633  33.099  1.00 25.68 ? 254  GLN A CA  1 
ATOM   1939  C  C   . GLN A  1 251 ? 26.506  -7.137  34.488  1.00 23.19 ? 254  GLN A C   1 
ATOM   1940  O  O   . GLN A  1 251 ? 25.400  -6.991  35.008  1.00 21.45 ? 254  GLN A O   1 
ATOM   1941  C  CB  . GLN A  1 251 ? 27.433  -5.263  33.193  1.00 28.08 ? 254  GLN A CB  1 
ATOM   1942  C  CG  . GLN A  1 251 ? 27.993  -4.747  31.896  1.00 32.11 ? 254  GLN A CG  1 
ATOM   1943  C  CD  . GLN A  1 251 ? 28.802  -5.779  31.168  1.00 36.22 ? 254  GLN A CD  1 
ATOM   1944  O  OE1 . GLN A  1 251 ? 28.337  -6.343  30.194  1.00 42.59 ? 254  GLN A OE1 1 
ATOM   1945  N  NE2 . GLN A  1 251 ? 30.015  -6.053  31.644  1.00 38.01 ? 254  GLN A NE2 1 
ATOM   1946  N  N   . PRO A  1 252 ? 27.540  -7.694  35.115  1.00 22.16 ? 255  PRO A N   1 
ATOM   1947  C  CA  . PRO A  1 252 ? 27.467  -8.130  36.501  1.00 20.17 ? 255  PRO A CA  1 
ATOM   1948  C  C   . PRO A  1 252 ? 27.286  -6.941  37.462  1.00 22.04 ? 255  PRO A C   1 
ATOM   1949  O  O   . PRO A  1 252 ? 27.845  -5.856  37.244  1.00 20.50 ? 255  PRO A O   1 
ATOM   1950  C  CB  . PRO A  1 252 ? 28.811  -8.819  36.719  1.00 20.23 ? 255  PRO A CB  1 
ATOM   1951  C  CG  . PRO A  1 252 ? 29.700  -8.328  35.588  1.00 21.27 ? 255  PRO A CG  1 
ATOM   1952  C  CD  . PRO A  1 252 ? 28.772  -8.143  34.444  1.00 20.15 ? 255  PRO A CD  1 
ATOM   1953  N  N   . GLY A  1 253 ? 26.492  -7.146  38.508  1.00 20.10 ? 256  GLY A N   1 
ATOM   1954  C  CA  . GLY A  1 253 ? 26.215  -6.092  39.472  1.00 16.56 ? 256  GLY A CA  1 
ATOM   1955  C  C   . GLY A  1 253 ? 25.301  -6.536  40.591  1.00 15.00 ? 256  GLY A C   1 
ATOM   1956  O  O   . GLY A  1 253 ? 25.051  -7.727  40.788  1.00 16.06 ? 256  GLY A O   1 
ATOM   1957  N  N   . ARG A  1 254 ? 24.824  -5.581  41.368  1.00 17.41 ? 257  ARG A N   1 
ATOM   1958  C  CA  . ARG A  1 254 ? 23.956  -5.913  42.478  1.00 18.94 ? 257  ARG A CA  1 
ATOM   1959  C  C   . ARG A  1 254 ? 23.137  -4.702  42.854  1.00 17.68 ? 257  ARG A C   1 
ATOM   1960  O  O   . ARG A  1 254 ? 23.480  -3.571  42.508  1.00 17.30 ? 257  ARG A O   1 
ATOM   1961  C  CB  . ARG A  1 254 ? 24.782  -6.406  43.680  1.00 23.39 ? 257  ARG A CB  1 
ATOM   1962  C  CG  . ARG A  1 254 ? 25.507  -5.307  44.410  1.00 29.82 ? 257  ARG A CG  1 
ATOM   1963  C  CD  . ARG A  1 254 ? 26.383  -4.539  43.455  1.00 36.84 ? 257  ARG A CD  1 
ATOM   1964  N  NE  . ARG A  1 254 ? 27.212  -3.560  44.154  1.00 43.21 ? 257  ARG A NE  1 
ATOM   1965  C  CZ  . ARG A  1 254 ? 28.246  -2.923  43.610  1.00 43.39 ? 257  ARG A CZ  1 
ATOM   1966  N  NH1 . ARG A  1 254 ? 28.582  -3.163  42.344  1.00 42.12 ? 257  ARG A NH1 1 
ATOM   1967  N  NH2 . ARG A  1 254 ? 28.944  -2.051  44.340  1.00 41.91 ? 257  ARG A NH2 1 
ATOM   1968  N  N   . ASN A  1 255 ? 22.023  -4.936  43.529  1.00 18.82 ? 258  ASN A N   1 
ATOM   1969  C  CA  . ASN A  1 255 ? 21.383  -3.848  44.215  1.00 23.37 ? 258  ASN A CA  1 
ATOM   1970  C  C   . ASN A  1 255 ? 22.240  -3.469  45.421  1.00 27.38 ? 258  ASN A C   1 
ATOM   1971  O  O   . ASN A  1 255 ? 23.003  -4.292  45.950  1.00 26.56 ? 258  ASN A O   1 
ATOM   1972  C  CB  . ASN A  1 255 ? 19.962  -4.224  44.621  1.00 20.76 ? 258  ASN A CB  1 
ATOM   1973  C  CG  . ASN A  1 255 ? 18.969  -4.026  43.489  1.00 20.47 ? 258  ASN A CG  1 
ATOM   1974  O  OD1 . ASN A  1 255 ? 19.217  -3.261  42.553  1.00 18.97 ? 258  ASN A OD1 1 
ATOM   1975  N  ND2 . ASN A  1 255 ? 17.845  -4.716  43.568  1.00 19.02 ? 258  ASN A ND2 1 
ATOM   1976  N  N   . VAL A  1 256 ? 22.171  -2.198  45.791  1.00 31.44 ? 259  VAL A N   1 
ATOM   1977  C  CA  . VAL A  1 256 ? 22.951  -1.664  46.890  1.00 32.00 ? 259  VAL A CA  1 
ATOM   1978  C  C   . VAL A  1 256 ? 22.033  -1.096  47.961  1.00 32.03 ? 259  VAL A C   1 
ATOM   1979  O  O   . VAL A  1 256 ? 21.933  0.113   48.106  1.00 33.38 ? 259  VAL A O   1 
ATOM   1980  C  CB  . VAL A  1 256 ? 23.812  -0.519  46.396  1.00 33.15 ? 259  VAL A CB  1 
ATOM   1981  C  CG1 . VAL A  1 256 ? 24.685  -0.984  45.240  1.00 31.53 ? 259  VAL A CG1 1 
ATOM   1982  C  CG2 . VAL A  1 256 ? 22.907  0.633   45.956  1.00 33.44 ? 259  VAL A CG2 1 
ATOM   1983  N  N   . GLY A  1 257 ? 21.347  -1.965  48.693  1.00 31.37 ? 260  GLY A N   1 
ATOM   1984  C  CA  . GLY A  1 257 ? 20.608  -1.543  49.879  1.00 30.65 ? 260  GLY A CA  1 
ATOM   1985  C  C   . GLY A  1 257 ? 19.126  -1.301  49.657  1.00 32.10 ? 260  GLY A C   1 
ATOM   1986  O  O   . GLY A  1 257 ? 18.374  -1.031  50.608  1.00 31.75 ? 260  GLY A O   1 
ATOM   1987  N  N   . LYS A  1 258 ? 18.712  -1.344  48.395  1.00 29.73 ? 261  LYS A N   1 
ATOM   1988  C  CA  . LYS A  1 258 ? 17.341  -1.002  48.021  1.00 29.24 ? 261  LYS A CA  1 
ATOM   1989  C  C   . LYS A  1 258 ? 17.025  -1.505  46.600  1.00 27.85 ? 261  LYS A C   1 
ATOM   1990  O  O   . LYS A  1 258 ? 17.931  -1.695  45.779  1.00 24.97 ? 261  LYS A O   1 
ATOM   1991  C  CB  . LYS A  1 258 ? 17.144  0.515   48.095  1.00 30.19 ? 261  LYS A CB  1 
ATOM   1992  C  CG  . LYS A  1 258 ? 17.964  1.293   47.044  1.00 29.54 ? 261  LYS A CG  1 
ATOM   1993  C  CD  . LYS A  1 258 ? 17.961  2.799   47.289  1.00 29.20 ? 261  LYS A CD  1 
ATOM   1994  C  CE  . LYS A  1 258 ? 18.388  3.549   46.017  1.00 31.46 ? 261  LYS A CE  1 
ATOM   1995  N  NZ  . LYS A  1 258 ? 19.323  4.690   46.226  1.00 30.88 ? 261  LYS A NZ  1 
ATOM   1996  N  N   . ILE A  1 259 ? 15.739  -1.707  46.316  1.00 28.83 ? 262  ILE A N   1 
ATOM   1997  C  CA  . ILE A  1 259 ? 15.295  -2.093  44.980  1.00 28.50 ? 262  ILE A CA  1 
ATOM   1998  C  C   . ILE A  1 259 ? 15.612  -1.007  43.951  1.00 29.58 ? 262  ILE A C   1 
ATOM   1999  O  O   . ILE A  1 259 ? 15.882  0.150   44.300  1.00 28.29 ? 262  ILE A O   1 
ATOM   2000  C  CB  . ILE A  1 259 ? 13.787  -2.391  44.942  1.00 30.11 ? 262  ILE A CB  1 
ATOM   2001  C  CG1 . ILE A  1 259 ? 12.973  -1.125  45.237  1.00 31.05 ? 262  ILE A CG1 1 
ATOM   2002  C  CG2 . ILE A  1 259 ? 13.432  -3.516  45.916  1.00 30.89 ? 262  ILE A CG2 1 
ATOM   2003  C  CD1 . ILE A  1 259 ? 11.456  -1.333  45.124  1.00 29.90 ? 262  ILE A CD1 1 
ATOM   2004  N  N   . ASN A  1 260 ? 15.567  -1.391  42.679  1.00 28.13 ? 263  ASN A N   1 
ATOM   2005  C  CA  . ASN A  1 260 ? 15.892  -0.489  41.585  1.00 25.77 ? 263  ASN A CA  1 
ATOM   2006  C  C   . ASN A  1 260 ? 17.139  0.338   41.831  1.00 26.94 ? 263  ASN A C   1 
ATOM   2007  O  O   . ASN A  1 260 ? 17.206  1.525   41.475  1.00 24.68 ? 263  ASN A O   1 
ATOM   2008  C  CB  . ASN A  1 260 ? 14.687  0.376   41.204  1.00 26.15 ? 263  ASN A CB  1 
ATOM   2009  C  CG  . ASN A  1 260 ? 13.491  -0.461  40.837  1.00 30.46 ? 263  ASN A CG  1 
ATOM   2010  O  OD1 . ASN A  1 260 ? 12.467  -0.448  41.541  1.00 34.88 ? 263  ASN A OD1 1 
ATOM   2011  N  ND2 . ASN A  1 260 ? 13.674  -1.340  39.854  1.00 29.74 ? 263  ASN A ND2 1 
ATOM   2012  N  N   . SER A  1 261 ? 18.194  -0.343  42.264  1.00 27.57 ? 264  SER A N   1 
ATOM   2013  C  CA  . SER A  1 261 ? 19.485  0.313   42.393  1.00 29.21 ? 264  SER A CA  1 
ATOM   2014  C  C   . SER A  1 261 ? 20.611  -0.542  41.835  1.00 28.73 ? 264  SER A C   1 
ATOM   2015  O  O   . SER A  1 261 ? 21.698  -0.592  42.410  1.00 29.59 ? 264  SER A O   1 
ATOM   2016  C  CB  . SER A  1 261 ? 19.761  0.690   43.862  1.00 26.76 ? 264  SER A CB  1 
ATOM   2017  O  OG  . SER A  1 261 ? 19.963  -0.460  44.667  1.00 24.78 ? 264  SER A OG  1 
ATOM   2018  N  N   . TYR A  1 262 ? 20.367  -1.168  40.686  1.00 27.78 ? 265  TYR A N   1 
ATOM   2019  C  CA  . TYR A  1 262 ? 21.326  -2.114  40.128  1.00 23.67 ? 265  TYR A CA  1 
ATOM   2020  C  C   . TYR A  1 262 ? 22.599  -1.397  39.766  1.00 23.60 ? 265  TYR A C   1 
ATOM   2021  O  O   . TYR A  1 262 ? 22.628  -0.534  38.895  1.00 24.35 ? 265  TYR A O   1 
ATOM   2022  C  CB  . TYR A  1 262 ? 20.773  -2.838  38.898  1.00 21.37 ? 265  TYR A CB  1 
ATOM   2023  C  CG  . TYR A  1 262 ? 21.595  -4.049  38.484  1.00 19.27 ? 265  TYR A CG  1 
ATOM   2024  C  CD1 . TYR A  1 262 ? 21.608  -5.201  39.258  1.00 16.91 ? 265  TYR A CD1 1 
ATOM   2025  C  CD2 . TYR A  1 262 ? 22.371  -4.025  37.337  1.00 19.67 ? 265  TYR A CD2 1 
ATOM   2026  C  CE1 . TYR A  1 262 ? 22.295  -6.323  38.858  1.00 18.08 ? 265  TYR A CE1 1 
ATOM   2027  C  CE2 . TYR A  1 262 ? 23.112  -5.133  36.946  1.00 18.35 ? 265  TYR A CE2 1 
ATOM   2028  C  CZ  . TYR A  1 262 ? 23.061  -6.278  37.707  1.00 20.23 ? 265  TYR A CZ  1 
ATOM   2029  O  OH  . TYR A  1 262 ? 23.801  -7.371  37.332  1.00 20.64 ? 265  TYR A OH  1 
ATOM   2030  N  N   . THR A  1 263 ? 23.679  -1.803  40.403  1.00 24.81 ? 266  THR A N   1 
ATOM   2031  C  CA  . THR A  1 263 ? 24.927  -1.091  40.253  1.00 23.37 ? 266  THR A CA  1 
ATOM   2032  C  C   . THR A  1 263 ? 25.946  -2.048  39.688  1.00 23.29 ? 266  THR A C   1 
ATOM   2033  O  O   . THR A  1 263 ? 26.320  -3.024  40.328  1.00 21.03 ? 266  THR A O   1 
ATOM   2034  C  CB  . THR A  1 263 ? 25.394  -0.537  41.615  1.00 24.08 ? 266  THR A CB  1 
ATOM   2035  O  OG1 . THR A  1 263 ? 24.382  0.333   42.133  1.00 23.19 ? 266  THR A OG1 1 
ATOM   2036  C  CG2 . THR A  1 263 ? 26.682  0.220   41.471  1.00 26.33 ? 266  THR A CG2 1 
ATOM   2037  N  N   . VAL A  1 264 ? 26.363  -1.782  38.461  1.00 25.18 ? 267  VAL A N   1 
ATOM   2038  C  CA  . VAL A  1 264 ? 27.330  -2.615  37.809  1.00 24.99 ? 267  VAL A CA  1 
ATOM   2039  C  C   . VAL A  1 264 ? 28.599  -2.688  38.645  1.00 28.40 ? 267  VAL A C   1 
ATOM   2040  O  O   . VAL A  1 264 ? 28.962  -1.725  39.335  1.00 28.88 ? 267  VAL A O   1 
ATOM   2041  C  CB  . VAL A  1 264 ? 27.611  -2.102  36.387  1.00 24.34 ? 267  VAL A CB  1 
ATOM   2042  C  CG1 . VAL A  1 264 ? 28.788  -2.849  35.770  1.00 23.74 ? 267  VAL A CG1 1 
ATOM   2043  C  CG2 . VAL A  1 264 ? 26.372  -2.311  35.538  1.00 28.50 ? 267  VAL A CG2 1 
ATOM   2044  N  N   . ASP A  1 265 ? 29.208  -3.871  38.659  1.00 30.26 ? 268  ASP A N   1 
ATOM   2045  C  CA  . ASP A  1 265 ? 30.482  -4.080  39.328  1.00 29.85 ? 268  ASP A CA  1 
ATOM   2046  C  C   . ASP A  1 265 ? 31.612  -4.359  38.343  1.00 30.93 ? 268  ASP A C   1 
ATOM   2047  O  O   . ASP A  1 265 ? 31.755  -5.484  37.845  1.00 26.96 ? 268  ASP A O   1 
ATOM   2048  C  CB  . ASP A  1 265 ? 30.382  -5.213  40.334  1.00 31.95 ? 268  ASP A CB  1 
ATOM   2049  C  CG  . ASP A  1 265 ? 31.669  -5.413  41.115  1.00 34.64 ? 268  ASP A CG  1 
ATOM   2050  O  OD1 . ASP A  1 265 ? 32.630  -4.636  40.904  1.00 32.90 ? 268  ASP A OD1 1 
ATOM   2051  O  OD2 . ASP A  1 265 ? 31.716  -6.359  41.931  1.00 35.20 ? 268  ASP A OD2 1 
ATOM   2052  N  N   . PRO A  1 266 ? 32.454  -3.344  38.102  1.00 30.15 ? 269  PRO A N   1 
ATOM   2053  C  CA  . PRO A  1 266 ? 33.572  -3.461  37.171  1.00 30.59 ? 269  PRO A CA  1 
ATOM   2054  C  C   . PRO A  1 266 ? 34.696  -4.372  37.675  1.00 30.37 ? 269  PRO A C   1 
ATOM   2055  O  O   . PRO A  1 266 ? 35.583  -4.725  36.908  1.00 29.14 ? 269  PRO A O   1 
ATOM   2056  C  CB  . PRO A  1 266 ? 34.082  -2.014  37.028  1.00 31.06 ? 269  PRO A CB  1 
ATOM   2057  C  CG  . PRO A  1 266 ? 33.243  -1.165  37.973  1.00 31.94 ? 269  PRO A CG  1 
ATOM   2058  C  CD  . PRO A  1 266 ? 32.507  -2.098  38.887  1.00 31.85 ? 269  PRO A CD  1 
ATOM   2059  N  N   . THR A  1 267 ? 34.641  -4.804  38.931  1.00 30.05 ? 270  THR A N   1 
ATOM   2060  C  CA  . THR A  1 267 ? 35.634  -5.769  39.391  1.00 30.44 ? 270  THR A CA  1 
ATOM   2061  C  C   . THR A  1 267 ? 35.206  -7.220  39.198  1.00 29.15 ? 270  THR A C   1 
ATOM   2062  O  O   . THR A  1 267 ? 36.017  -8.121  39.388  1.00 27.33 ? 270  THR A O   1 
ATOM   2063  C  CB  . THR A  1 267 ? 36.055  -5.546  40.862  1.00 32.52 ? 270  THR A CB  1 
ATOM   2064  O  OG1 . THR A  1 267 ? 35.008  -5.966  41.749  1.00 30.62 ? 270  THR A OG1 1 
ATOM   2065  C  CG2 . THR A  1 267 ? 36.383  -4.079  41.114  1.00 32.26 ? 270  THR A CG2 1 
ATOM   2066  N  N   . SER A  1 268 ? 33.940  -7.446  38.833  1.00 25.20 ? 271  SER A N   1 
ATOM   2067  C  CA  . SER A  1 268 ? 33.424  -8.810  38.643  1.00 20.92 ? 271  SER A CA  1 
ATOM   2068  C  C   . SER A  1 268 ? 34.059  -9.410  37.403  1.00 20.71 ? 271  SER A C   1 
ATOM   2069  O  O   . SER A  1 268 ? 34.418  -8.696  36.461  1.00 22.86 ? 271  SER A O   1 
ATOM   2070  C  CB  . SER A  1 268 ? 31.896  -8.804  38.495  1.00 18.41 ? 271  SER A CB  1 
ATOM   2071  O  OG  . SER A  1 268 ? 31.372  -10.113 38.328  1.00 18.57 ? 271  SER A OG  1 
ATOM   2072  N  N   . SER A  1 269 ? 34.204  -10.721 37.385  1.00 20.33 ? 272  SER A N   1 
ATOM   2073  C  CA  . SER A  1 269 ? 34.391  -11.397 36.107  1.00 20.78 ? 272  SER A CA  1 
ATOM   2074  C  C   . SER A  1 269 ? 33.121  -11.240 35.269  1.00 19.88 ? 272  SER A C   1 
ATOM   2075  O  O   . SER A  1 269 ? 32.120  -10.703 35.737  1.00 15.60 ? 272  SER A O   1 
ATOM   2076  C  CB  . SER A  1 269 ? 34.706  -12.869 36.314  1.00 19.46 ? 272  SER A CB  1 
ATOM   2077  O  OG  . SER A  1 269 ? 33.616  -13.498 36.963  1.00 22.99 ? 272  SER A OG  1 
ATOM   2078  N  N   . ASP A  1 270 ? 33.233  -11.546 33.980  1.00 23.04 ? 273  ASP A N   1 
ATOM   2079  C  CA  . ASP A  1 270 ? 32.074  -11.808 33.142  1.00 23.37 ? 273  ASP A CA  1 
ATOM   2080  C  C   . ASP A  1 270 ? 32.461  -12.842 32.102  1.00 24.87 ? 273  ASP A C   1 
ATOM   2081  O  O   . ASP A  1 270 ? 33.463  -13.569 32.285  1.00 24.77 ? 273  ASP A O   1 
ATOM   2082  C  CB  . ASP A  1 270 ? 31.550  -10.529 32.477  1.00 23.42 ? 273  ASP A CB  1 
ATOM   2083  C  CG  . ASP A  1 270 ? 32.634  -9.749  31.712  1.00 27.70 ? 273  ASP A CG  1 
ATOM   2084  O  OD1 . ASP A  1 270 ? 33.402  -10.321 30.906  1.00 26.76 ? 273  ASP A OD1 1 
ATOM   2085  O  OD2 . ASP A  1 270 ? 32.623  -8.509  31.821  1.00 33.52 ? 273  ASP A OD2 1 
ATOM   2086  N  N   . PHE A  1 271 ? 31.682  -12.935 31.022  1.00 17.69 ? 274  PHE A N   1 
ATOM   2087  C  CA  . PHE A  1 271 ? 31.883  -14.051 30.105  1.00 18.09 ? 274  PHE A CA  1 
ATOM   2088  C  C   . PHE A  1 271 ? 33.136  -13.875 29.248  1.00 17.73 ? 274  PHE A C   1 
ATOM   2089  O  O   . PHE A  1 271 ? 33.702  -14.857 28.762  1.00 21.06 ? 274  PHE A O   1 
ATOM   2090  C  CB  . PHE A  1 271 ? 30.645  -14.314 29.249  1.00 16.54 ? 274  PHE A CB  1 
ATOM   2091  C  CG  . PHE A  1 271 ? 29.502  -14.932 30.025  1.00 16.56 ? 274  PHE A CG  1 
ATOM   2092  C  CD1 . PHE A  1 271 ? 29.464  -16.287 30.262  1.00 17.07 ? 274  PHE A CD1 1 
ATOM   2093  C  CD2 . PHE A  1 271 ? 28.484  -14.146 30.520  1.00 18.91 ? 274  PHE A CD2 1 
ATOM   2094  C  CE1 . PHE A  1 271 ? 28.414  -16.861 30.973  1.00 21.26 ? 274  PHE A CE1 1 
ATOM   2095  C  CE2 . PHE A  1 271 ? 27.470  -14.696 31.305  1.00 22.09 ? 274  PHE A CE2 1 
ATOM   2096  C  CZ  . PHE A  1 271 ? 27.440  -16.062 31.528  1.00 20.82 ? 274  PHE A CZ  1 
ATOM   2097  N  N   . SER A  1 272 ? 33.590  -12.638 29.095  1.00 14.60 ? 275  SER A N   1 
ATOM   2098  C  CA  . SER A  1 272 ? 34.882  -12.404 28.443  1.00 23.03 ? 275  SER A CA  1 
ATOM   2099  C  C   . SER A  1 272 ? 36.098  -12.813 29.291  1.00 24.89 ? 275  SER A C   1 
ATOM   2100  O  O   . SER A  1 272 ? 37.190  -12.946 28.760  1.00 29.33 ? 275  SER A O   1 
ATOM   2101  C  CB  . SER A  1 272 ? 35.033  -10.948 28.003  1.00 20.74 ? 275  SER A CB  1 
ATOM   2102  O  OG  . SER A  1 272 ? 35.148  -10.099 29.128  1.00 19.37 ? 275  SER A OG  1 
ATOM   2103  N  N   . THR A  1 273 ? 35.910  -13.027 30.592  1.00 25.99 ? 276  THR A N   1 
ATOM   2104  C  CA  . THR A  1 273 ? 37.043  -13.317 31.511  1.00 22.85 ? 276  THR A CA  1 
ATOM   2105  C  C   . THR A  1 273 ? 36.773  -14.514 32.421  1.00 22.93 ? 276  THR A C   1 
ATOM   2106  O  O   . THR A  1 273 ? 36.594  -14.358 33.632  1.00 20.08 ? 276  THR A O   1 
ATOM   2107  C  CB  . THR A  1 273 ? 37.395  -12.079 32.395  1.00 20.17 ? 276  THR A CB  1 
ATOM   2108  O  OG1 . THR A  1 273 ? 36.242  -11.666 33.150  1.00 20.80 ? 276  THR A OG1 1 
ATOM   2109  C  CG2 . THR A  1 273 ? 37.825  -10.902 31.517  1.00 18.10 ? 276  THR A CG2 1 
ATOM   2110  N  N   . PRO A  1 274 ? 36.730  -15.722 31.842  1.00 24.80 ? 277  PRO A N   1 
ATOM   2111  C  CA  . PRO A  1 274 ? 36.422  -16.897 32.638  1.00 25.76 ? 277  PRO A CA  1 
ATOM   2112  C  C   . PRO A  1 274 ? 37.583  -17.303 33.565  1.00 27.76 ? 277  PRO A C   1 
ATOM   2113  O  O   . PRO A  1 274 ? 37.372  -17.990 34.574  1.00 27.06 ? 277  PRO A O   1 
ATOM   2114  C  CB  . PRO A  1 274 ? 36.183  -17.965 31.574  1.00 23.53 ? 277  PRO A CB  1 
ATOM   2115  C  CG  . PRO A  1 274 ? 37.072  -17.559 30.482  1.00 24.98 ? 277  PRO A CG  1 
ATOM   2116  C  CD  . PRO A  1 274 ? 36.914  -16.073 30.426  1.00 25.90 ? 277  PRO A CD  1 
ATOM   2117  N  N   . CYS A  1 275 ? 38.803  -16.931 33.199  1.00 27.33 ? 278  CYS A N   1 
ATOM   2118  C  CA  . CYS A  1 275 ? 39.955  -17.266 34.033  1.00 27.70 ? 278  CYS A CA  1 
ATOM   2119  C  C   . CYS A  1 275 ? 39.965  -16.424 35.285  1.00 24.16 ? 278  CYS A C   1 
ATOM   2120  O  O   . CYS A  1 275 ? 40.195  -16.936 36.368  1.00 22.66 ? 278  CYS A O   1 
ATOM   2121  C  CB  . CYS A  1 275 ? 41.268  -17.115 33.269  1.00 27.97 ? 278  CYS A CB  1 
ATOM   2122  S  SG  . CYS A  1 275 ? 41.381  -18.265 31.895  1.00 28.19 ? 278  CYS A SG  1 
ATOM   2123  N  N   . LEU A  1 276 ? 39.558  -15.171 35.150  1.00 23.04 ? 279  LEU A N   1 
ATOM   2124  C  CA  . LEU A  1 276 ? 39.315  -14.324 36.314  1.00 23.89 ? 279  LEU A CA  1 
ATOM   2125  C  C   . LEU A  1 276 ? 38.165  -14.846 37.201  1.00 25.38 ? 279  LEU A C   1 
ATOM   2126  O  O   . LEU A  1 276 ? 38.199  -14.705 38.418  1.00 28.59 ? 279  LEU A O   1 
ATOM   2127  C  CB  . LEU A  1 276 ? 39.046  -12.877 35.876  1.00 23.00 ? 279  LEU A CB  1 
ATOM   2128  C  CG  . LEU A  1 276 ? 38.693  -11.862 36.982  1.00 25.04 ? 279  LEU A CG  1 
ATOM   2129  C  CD1 . LEU A  1 276 ? 39.931  -11.553 37.827  1.00 24.98 ? 279  LEU A CD1 1 
ATOM   2130  C  CD2 . LEU A  1 276 ? 38.090  -10.567 36.384  1.00 17.40 ? 279  LEU A CD2 1 
ATOM   2131  N  N   . MET A  1 277 ? 37.142  -15.433 36.599  1.00 23.90 ? 280  MET A N   1 
ATOM   2132  C  CA  . MET A  1 277 ? 36.068  -16.018 37.388  1.00 24.24 ? 280  MET A CA  1 
ATOM   2133  C  C   . MET A  1 277 ? 36.615  -17.199 38.206  1.00 25.02 ? 280  MET A C   1 
ATOM   2134  O  O   . MET A  1 277 ? 36.343  -17.321 39.399  1.00 24.74 ? 280  MET A O   1 
ATOM   2135  C  CB  . MET A  1 277 ? 34.913  -16.467 36.476  1.00 25.91 ? 280  MET A CB  1 
ATOM   2136  C  CG  . MET A  1 277 ? 33.705  -17.035 37.207  1.00 27.26 ? 280  MET A CG  1 
ATOM   2137  S  SD  . MET A  1 277 ? 33.822  -18.821 37.316  1.00 37.14 ? 280  MET A SD  1 
ATOM   2138  C  CE  . MET A  1 277 ? 33.545  -19.299 35.606  1.00 32.07 ? 280  MET A CE  1 
ATOM   2139  N  N   . TYR A  1 278 ? 37.357  -18.085 37.544  1.00 23.83 ? 281  TYR A N   1 
ATOM   2140  C  CA  . TYR A  1 278 ? 37.982  -19.222 38.213  1.00 24.00 ? 281  TYR A CA  1 
ATOM   2141  C  C   . TYR A  1 278 ? 38.882  -18.717 39.338  1.00 27.95 ? 281  TYR A C   1 
ATOM   2142  O  O   . TYR A  1 278 ? 38.789  -19.161 40.480  1.00 27.80 ? 281  TYR A O   1 
ATOM   2143  C  CB  . TYR A  1 278 ? 38.828  -20.018 37.211  1.00 22.14 ? 281  TYR A CB  1 
ATOM   2144  C  CG  . TYR A  1 278 ? 39.937  -20.821 37.872  1.00 23.35 ? 281  TYR A CG  1 
ATOM   2145  C  CD1 . TYR A  1 278 ? 39.649  -21.996 38.556  1.00 23.18 ? 281  TYR A CD1 1 
ATOM   2146  C  CD2 . TYR A  1 278 ? 41.262  -20.415 37.802  1.00 23.36 ? 281  TYR A CD2 1 
ATOM   2147  C  CE1 . TYR A  1 278 ? 40.641  -22.731 39.190  1.00 23.90 ? 281  TYR A CE1 1 
ATOM   2148  C  CE2 . TYR A  1 278 ? 42.272  -21.141 38.437  1.00 24.15 ? 281  TYR A CE2 1 
ATOM   2149  C  CZ  . TYR A  1 278 ? 41.943  -22.283 39.157  1.00 25.72 ? 281  TYR A CZ  1 
ATOM   2150  O  OH  . TYR A  1 278 ? 42.921  -23.034 39.771  1.00 26.28 ? 281  TYR A OH  1 
ATOM   2151  N  N   . GLU A  1 279 ? 39.733  -17.753 39.000  1.00 29.85 ? 282  GLU A N   1 
ATOM   2152  C  CA  . GLU A  1 279 ? 40.666  -17.154 39.948  1.00 30.76 ? 282  GLU A CA  1 
ATOM   2153  C  C   . GLU A  1 279 ? 39.936  -16.661 41.194  1.00 27.63 ? 282  GLU A C   1 
ATOM   2154  O  O   . GLU A  1 279 ? 40.271  -17.045 42.313  1.00 25.18 ? 282  GLU A O   1 
ATOM   2155  C  CB  . GLU A  1 279 ? 41.393  -15.995 39.261  1.00 34.11 ? 282  GLU A CB  1 
ATOM   2156  C  CG  . GLU A  1 279 ? 42.713  -15.570 39.861  1.00 39.10 ? 282  GLU A CG  1 
ATOM   2157  C  CD  . GLU A  1 279 ? 43.573  -14.797 38.845  1.00 45.14 ? 282  GLU A CD  1 
ATOM   2158  O  OE1 . GLU A  1 279 ? 44.164  -15.434 37.914  1.00 46.07 ? 282  GLU A OE1 1 
ATOM   2159  O  OE2 . GLU A  1 279 ? 43.603  -13.548 38.943  1.00 43.23 ? 282  GLU A OE2 1 
ATOM   2160  N  N   . LYS A  1 280 ? 38.992  -15.748 40.998  1.00 24.64 ? 283  LYS A N   1 
ATOM   2161  C  CA  . LYS A  1 280 ? 38.230  -15.184 42.106  1.00 25.09 ? 283  LYS A CA  1 
ATOM   2162  C  C   . LYS A  1 280 ? 37.480  -16.226 42.956  1.00 25.05 ? 283  LYS A C   1 
ATOM   2163  O  O   . LYS A  1 280 ? 37.388  -16.091 44.177  1.00 26.85 ? 283  LYS A O   1 
ATOM   2164  C  CB  . LYS A  1 280 ? 37.288  -14.078 41.597  1.00 27.65 ? 283  LYS A CB  1 
ATOM   2165  C  CG  . LYS A  1 280 ? 38.042  -12.848 41.028  1.00 27.70 ? 283  LYS A CG  1 
ATOM   2166  C  CD  . LYS A  1 280 ? 37.119  -11.644 40.713  1.00 28.38 ? 283  LYS A CD  1 
ATOM   2167  C  CE  . LYS A  1 280 ? 36.390  -11.165 41.958  1.00 29.11 ? 283  LYS A CE  1 
ATOM   2168  N  NZ  . LYS A  1 280 ? 35.640  -9.895  41.780  1.00 29.45 ? 283  LYS A NZ  1 
ATOM   2169  N  N   . PHE A  1 281 ? 37.031  -17.310 42.336  1.00 24.03 ? 284  PHE A N   1 
ATOM   2170  C  CA  . PHE A  1 281 ? 36.359  -18.392 43.069  1.00 21.20 ? 284  PHE A CA  1 
ATOM   2171  C  C   . PHE A  1 281 ? 37.291  -19.090 44.060  1.00 24.53 ? 284  PHE A C   1 
ATOM   2172  O  O   . PHE A  1 281 ? 36.955  -19.278 45.242  1.00 25.23 ? 284  PHE A O   1 
ATOM   2173  C  CB  . PHE A  1 281 ? 35.789  -19.425 42.093  1.00 19.69 ? 284  PHE A CB  1 
ATOM   2174  C  CG  . PHE A  1 281 ? 34.907  -20.440 42.752  1.00 24.16 ? 284  PHE A CG  1 
ATOM   2175  C  CD1 . PHE A  1 281 ? 33.629  -20.103 43.153  1.00 22.69 ? 284  PHE A CD1 1 
ATOM   2176  C  CD2 . PHE A  1 281 ? 35.406  -21.688 43.106  1.00 23.55 ? 284  PHE A CD2 1 
ATOM   2177  C  CE1 . PHE A  1 281 ? 32.841  -21.021 43.839  1.00 24.82 ? 284  PHE A CE1 1 
ATOM   2178  C  CE2 . PHE A  1 281 ? 34.623  -22.604 43.784  1.00 23.51 ? 284  PHE A CE2 1 
ATOM   2179  C  CZ  . PHE A  1 281 ? 33.335  -22.278 44.139  1.00 23.49 ? 284  PHE A CZ  1 
ATOM   2180  N  N   . VAL A  1 282 ? 38.402  -19.585 43.531  1.00 25.42 ? 285  VAL A N   1 
ATOM   2181  C  CA  . VAL A  1 282 ? 39.486  -20.127 44.332  1.00 29.28 ? 285  VAL A CA  1 
ATOM   2182  C  C   . VAL A  1 282 ? 40.105  -19.112 45.331  1.00 30.73 ? 285  VAL A C   1 
ATOM   2183  O  O   . VAL A  1 282 ? 40.131  -19.349 46.532  1.00 32.44 ? 285  VAL A O   1 
ATOM   2184  C  CB  . VAL A  1 282 ? 40.552  -20.751 43.415  1.00 29.49 ? 285  VAL A CB  1 
ATOM   2185  C  CG1 . VAL A  1 282 ? 41.798  -21.074 44.192  1.00 34.70 ? 285  VAL A CG1 1 
ATOM   2186  C  CG2 . VAL A  1 282 ? 40.002  -22.028 42.775  1.00 30.34 ? 285  VAL A CG2 1 
ATOM   2187  N  N   . ASN A  1 283 ? 40.494  -17.937 44.859  1.00 31.89 ? 286  ASN A N   1 
ATOM   2188  C  CA  . ASN A  1 283 ? 41.321  -17.056 45.677  1.00 30.10 ? 286  ASN A CA  1 
ATOM   2189  C  C   . ASN A  1 283 ? 40.601  -16.183 46.673  1.00 28.33 ? 286  ASN A C   1 
ATOM   2190  O  O   . ASN A  1 283 ? 41.203  -15.734 47.655  1.00 29.80 ? 286  ASN A O   1 
ATOM   2191  C  CB  . ASN A  1 283 ? 42.274  -16.221 44.835  1.00 29.28 ? 286  ASN A CB  1 
ATOM   2192  C  CG  . ASN A  1 283 ? 43.699  -16.644 45.016  1.00 31.61 ? 286  ASN A CG  1 
ATOM   2193  O  OD1 . ASN A  1 283 ? 43.972  -17.812 45.280  1.00 30.28 ? 286  ASN A OD1 1 
ATOM   2194  N  ND2 . ASN A  1 283 ? 44.623  -15.703 44.900  1.00 34.90 ? 286  ASN A ND2 1 
ATOM   2195  N  N   . ILE A  1 284 ? 39.303  -16.007 46.470  1.00 26.31 ? 287  ILE A N   1 
ATOM   2196  C  CA  . ILE A  1 284 ? 38.508  -15.158 47.333  1.00 26.87 ? 287  ILE A CA  1 
ATOM   2197  C  C   . ILE A  1 284 ? 37.382  -15.937 48.000  1.00 30.32 ? 287  ILE A C   1 
ATOM   2198  O  O   . ILE A  1 284 ? 37.235  -15.891 49.218  1.00 32.92 ? 287  ILE A O   1 
ATOM   2199  C  CB  . ILE A  1 284 ? 37.961  -13.937 46.570  1.00 28.09 ? 287  ILE A CB  1 
ATOM   2200  C  CG1 . ILE A  1 284 ? 39.126  -13.086 46.056  1.00 28.58 ? 287  ILE A CG1 1 
ATOM   2201  C  CG2 . ILE A  1 284 ? 37.035  -13.096 47.467  1.00 25.11 ? 287  ILE A CG2 1 
ATOM   2202  C  CD1 . ILE A  1 284 ? 38.722  -12.027 45.055  1.00 30.62 ? 287  ILE A CD1 1 
ATOM   2203  N  N   . THR A  1 285 ? 36.625  -16.703 47.215  1.00 31.34 ? 288  THR A N   1 
ATOM   2204  C  CA  . THR A  1 285 ? 35.471  -17.403 47.759  1.00 30.52 ? 288  THR A CA  1 
ATOM   2205  C  C   . THR A  1 285 ? 35.882  -18.571 48.657  1.00 29.09 ? 288  THR A C   1 
ATOM   2206  O  O   . THR A  1 285 ? 35.577  -18.574 49.842  1.00 29.29 ? 288  THR A O   1 
ATOM   2207  C  CB  . THR A  1 285 ? 34.506  -17.873 46.655  1.00 31.64 ? 288  THR A CB  1 
ATOM   2208  O  OG1 . THR A  1 285 ? 34.166  -16.761 45.820  1.00 32.49 ? 288  THR A OG1 1 
ATOM   2209  C  CG2 . THR A  1 285 ? 33.234  -18.454 47.265  1.00 28.67 ? 288  THR A CG2 1 
ATOM   2210  N  N   . VAL A  1 286 ? 36.548  -19.570 48.085  1.00 28.55 ? 289  VAL A N   1 
ATOM   2211  C  CA  . VAL A  1 286 ? 37.040  -20.699 48.870  1.00 30.54 ? 289  VAL A CA  1 
ATOM   2212  C  C   . VAL A  1 286 ? 37.999  -20.252 49.988  1.00 32.36 ? 289  VAL A C   1 
ATOM   2213  O  O   . VAL A  1 286 ? 37.819  -20.603 51.143  1.00 31.51 ? 289  VAL A O   1 
ATOM   2214  C  CB  . VAL A  1 286 ? 37.740  -21.750 47.989  1.00 29.70 ? 289  VAL A CB  1 
ATOM   2215  C  CG1 . VAL A  1 286 ? 38.446  -22.796 48.861  1.00 30.64 ? 289  VAL A CG1 1 
ATOM   2216  C  CG2 . VAL A  1 286 ? 36.725  -22.437 47.075  1.00 30.83 ? 289  VAL A CG2 1 
ATOM   2217  N  N   . LYS A  1 287 ? 38.968  -19.414 49.641  1.00 33.51 ? 290  LYS A N   1 
ATOM   2218  C  CA  . LYS A  1 287 ? 39.931  -18.922 50.602  1.00 35.15 ? 290  LYS A CA  1 
ATOM   2219  C  C   . LYS A  1 287 ? 39.252  -18.308 51.818  1.00 37.40 ? 290  LYS A C   1 
ATOM   2220  O  O   . LYS A  1 287 ? 39.690  -18.516 52.949  1.00 36.86 ? 290  LYS A O   1 
ATOM   2221  C  CB  . LYS A  1 287 ? 40.842  -17.898 49.942  1.00 38.08 ? 290  LYS A CB  1 
ATOM   2222  C  CG  . LYS A  1 287 ? 41.712  -17.144 50.900  1.00 40.01 ? 290  LYS A CG  1 
ATOM   2223  C  CD  . LYS A  1 287 ? 43.078  -17.789 51.044  1.00 40.34 ? 290  LYS A CD  1 
ATOM   2224  C  CE  . LYS A  1 287 ? 43.986  -16.869 51.856  1.00 41.47 ? 290  LYS A CE  1 
ATOM   2225  N  NZ  . LYS A  1 287 ? 45.353  -17.416 52.003  1.00 43.84 ? 290  LYS A NZ  1 
ATOM   2226  N  N   . SER A  1 288 ? 38.171  -17.564 51.597  1.00 35.55 ? 291  SER A N   1 
ATOM   2227  C  CA  . SER A  1 288 ? 37.552  -16.869 52.705  1.00 36.62 ? 291  SER A CA  1 
ATOM   2228  C  C   . SER A  1 288 ? 36.757  -17.820 53.610  1.00 37.39 ? 291  SER A C   1 
ATOM   2229  O  O   . SER A  1 288 ? 36.557  -17.539 54.786  1.00 36.96 ? 291  SER A O   1 
ATOM   2230  C  CB  . SER A  1 288 ? 36.696  -15.695 52.218  1.00 36.99 ? 291  SER A CB  1 
ATOM   2231  O  OG  . SER A  1 288 ? 35.353  -16.084 52.013  1.00 37.33 ? 291  SER A OG  1 
ATOM   2232  N  N   . LEU A  1 289 ? 36.348  -18.968 53.075  1.00 36.85 ? 292  LEU A N   1 
ATOM   2233  C  CA  . LEU A  1 289 ? 35.713  -20.001 53.900  1.00 36.46 ? 292  LEU A CA  1 
ATOM   2234  C  C   . LEU A  1 289 ? 36.750  -20.783 54.713  1.00 34.70 ? 292  LEU A C   1 
ATOM   2235  O  O   . LEU A  1 289 ? 36.427  -21.414 55.722  1.00 32.81 ? 292  LEU A O   1 
ATOM   2236  C  CB  . LEU A  1 289 ? 34.905  -20.969 53.031  1.00 34.35 ? 292  LEU A CB  1 
ATOM   2237  C  CG  . LEU A  1 289 ? 33.678  -20.389 52.324  1.00 34.89 ? 292  LEU A CG  1 
ATOM   2238  C  CD1 . LEU A  1 289 ? 33.314  -21.316 51.187  1.00 35.37 ? 292  LEU A CD1 1 
ATOM   2239  C  CD2 . LEU A  1 289 ? 32.496  -20.228 53.291  1.00 33.88 ? 292  LEU A CD2 1 
ATOM   2240  N  N   . TYR A  1 290 ? 37.984  -20.780 54.227  1.00 32.74 ? 293  TYR A N   1 
ATOM   2241  C  CA  . TYR A  1 290 ? 39.048  -21.576 54.821  1.00 32.74 ? 293  TYR A CA  1 
ATOM   2242  C  C   . TYR A  1 290 ? 40.335  -20.758 54.819  1.00 32.85 ? 293  TYR A C   1 
ATOM   2243  O  O   . TYR A  1 290 ? 41.239  -21.024 54.029  1.00 31.30 ? 293  TYR A O   1 
ATOM   2244  C  CB  . TYR A  1 290 ? 39.266  -22.832 53.996  1.00 33.04 ? 293  TYR A CB  1 
ATOM   2245  C  CG  . TYR A  1 290 ? 38.140  -23.822 54.075  1.00 31.40 ? 293  TYR A CG  1 
ATOM   2246  C  CD1 . TYR A  1 290 ? 38.067  -24.715 55.127  1.00 29.56 ? 293  TYR A CD1 1 
ATOM   2247  C  CD2 . TYR A  1 290 ? 37.165  -23.886 53.079  1.00 31.52 ? 293  TYR A CD2 1 
ATOM   2248  C  CE1 . TYR A  1 290 ? 37.057  -25.640 55.206  1.00 31.39 ? 293  TYR A CE1 1 
ATOM   2249  C  CE2 . TYR A  1 290 ? 36.128  -24.801 53.153  1.00 29.68 ? 293  TYR A CE2 1 
ATOM   2250  C  CZ  . TYR A  1 290 ? 36.097  -25.696 54.213  1.00 31.93 ? 293  TYR A CZ  1 
ATOM   2251  O  OH  . TYR A  1 290 ? 35.115  -26.651 54.310  1.00 28.86 ? 293  TYR A OH  1 
ATOM   2252  N  N   . PRO A  1 291 ? 40.361  -19.677 55.610  1.00 33.68 ? 294  PRO A N   1 
ATOM   2253  C  CA  . PRO A  1 291 ? 41.476  -18.724 55.564  1.00 35.57 ? 294  PRO A CA  1 
ATOM   2254  C  C   . PRO A  1 291 ? 42.785  -19.350 56.055  1.00 39.92 ? 294  PRO A C   1 
ATOM   2255  O  O   . PRO A  1 291 ? 43.859  -19.024 55.525  1.00 43.15 ? 294  PRO A O   1 
ATOM   2256  C  CB  . PRO A  1 291 ? 41.024  -17.588 56.490  1.00 33.38 ? 294  PRO A CB  1 
ATOM   2257  C  CG  . PRO A  1 291 ? 39.981  -18.202 57.396  1.00 34.15 ? 294  PRO A CG  1 
ATOM   2258  C  CD  . PRO A  1 291 ? 39.357  -19.347 56.641  1.00 33.30 ? 294  PRO A CD  1 
ATOM   2259  N  N   . ASN A  1 292 ? 42.679  -20.340 56.942  1.00 41.43 ? 295  ASN A N   1 
ATOM   2260  C  CA  . ASN A  1 292 ? 43.850  -20.897 57.621  1.00 46.41 ? 295  ASN A CA  1 
ATOM   2261  C  C   . ASN A  1 292 ? 43.768  -22.372 57.937  1.00 44.28 ? 295  ASN A C   1 
ATOM   2262  O  O   . ASN A  1 292 ? 43.980  -22.771 59.070  1.00 44.51 ? 295  ASN A O   1 
ATOM   2263  C  CB  . ASN A  1 292 ? 44.120  -20.148 58.917  1.00 49.87 ? 295  ASN A CB  1 
ATOM   2264  C  CG  . ASN A  1 292 ? 45.425  -19.404 58.881  1.00 54.54 ? 295  ASN A CG  1 
ATOM   2265  O  OD1 . ASN A  1 292 ? 45.452  -18.198 58.621  1.00 57.48 ? 295  ASN A OD1 1 
ATOM   2266  N  ND2 . ASN A  1 292 ? 46.527  -20.132 59.055  1.00 54.08 ? 295  ASN A ND2 1 
ATOM   2267  N  N   . PRO A  1 293 ? 43.524  -23.195 56.917  1.00 43.65 ? 296  PRO A N   1 
ATOM   2268  C  CA  . PRO A  1 293 ? 43.212  -24.592 57.188  1.00 42.26 ? 296  PRO A CA  1 
ATOM   2269  C  C   . PRO A  1 293 ? 44.287  -25.238 58.071  1.00 41.85 ? 296  PRO A C   1 
ATOM   2270  O  O   . PRO A  1 293 ? 45.468  -24.928 57.929  1.00 37.65 ? 296  PRO A O   1 
ATOM   2271  C  CB  . PRO A  1 293 ? 43.241  -25.221 55.797  1.00 42.07 ? 296  PRO A CB  1 
ATOM   2272  C  CG  . PRO A  1 293 ? 44.257  -24.394 55.050  1.00 40.97 ? 296  PRO A CG  1 
ATOM   2273  C  CD  . PRO A  1 293 ? 44.059  -22.992 55.560  1.00 42.49 ? 296  PRO A CD  1 
ATOM   2274  N  N   . THR A  1 294 ? 43.882  -26.167 58.933  1.00 42.34 ? 297  THR A N   1 
ATOM   2275  C  CA  . THR A  1 294 ? 44.838  -27.066 59.559  1.00 42.10 ? 297  THR A CA  1 
ATOM   2276  C  C   . THR A  1 294 ? 45.480  -27.879 58.444  1.00 44.06 ? 297  THR A C   1 
ATOM   2277  O  O   . THR A  1 294 ? 45.162  -27.664 57.272  1.00 42.83 ? 297  THR A O   1 
ATOM   2278  C  CB  . THR A  1 294 ? 44.161  -27.981 60.593  1.00 42.70 ? 297  THR A CB  1 
ATOM   2279  O  OG1 . THR A  1 294 ? 43.130  -28.765 59.965  1.00 43.58 ? 297  THR A OG1 1 
ATOM   2280  C  CG2 . THR A  1 294 ? 43.559  -27.142 61.731  1.00 40.67 ? 297  THR A CG2 1 
ATOM   2281  N  N   . VAL A  1 295 ? 46.419  -28.759 58.795  1.00 44.99 ? 298  VAL A N   1 
ATOM   2282  C  CA  . VAL A  1 295 ? 47.226  -29.466 57.798  1.00 45.24 ? 298  VAL A CA  1 
ATOM   2283  C  C   . VAL A  1 295 ? 46.367  -30.465 57.046  1.00 45.51 ? 298  VAL A C   1 
ATOM   2284  O  O   . VAL A  1 295 ? 46.539  -30.673 55.850  1.00 47.28 ? 298  VAL A O   1 
ATOM   2285  C  CB  . VAL A  1 295 ? 48.413  -30.222 58.435  1.00 47.26 ? 298  VAL A CB  1 
ATOM   2286  C  CG1 . VAL A  1 295 ? 49.128  -31.068 57.388  1.00 47.65 ? 298  VAL A CG1 1 
ATOM   2287  C  CG2 . VAL A  1 295 ? 49.387  -29.250 59.077  1.00 48.50 ? 298  VAL A CG2 1 
ATOM   2288  N  N   . GLN A  1 296 ? 45.424  -31.068 57.756  1.00 44.55 ? 299  GLN A N   1 
ATOM   2289  C  CA  . GLN A  1 296 ? 44.513  -32.034 57.164  1.00 44.69 ? 299  GLN A CA  1 
ATOM   2290  C  C   . GLN A  1 296 ? 43.524  -31.374 56.175  1.00 42.19 ? 299  GLN A C   1 
ATOM   2291  O  O   . GLN A  1 296 ? 43.399  -31.791 55.020  1.00 40.50 ? 299  GLN A O   1 
ATOM   2292  C  CB  . GLN A  1 296 ? 43.776  -32.767 58.286  1.00 49.44 ? 299  GLN A CB  1 
ATOM   2293  C  CG  . GLN A  1 296 ? 42.680  -33.710 57.833  1.00 56.88 ? 299  GLN A CG  1 
ATOM   2294  C  CD  . GLN A  1 296 ? 43.212  -34.987 57.192  1.00 60.46 ? 299  GLN A CD  1 
ATOM   2295  O  OE1 . GLN A  1 296 ? 42.462  -35.955 56.991  1.00 62.47 ? 299  GLN A OE1 1 
ATOM   2296  N  NE2 . GLN A  1 296 ? 44.499  -34.982 56.832  1.00 60.79 ? 299  GLN A NE2 1 
ATOM   2297  N  N   . LEU A  1 297 ? 42.847  -30.333 56.643  1.00 38.97 ? 300  LEU A N   1 
ATOM   2298  C  CA  . LEU A  1 297 ? 41.999  -29.497 55.815  1.00 37.61 ? 300  LEU A CA  1 
ATOM   2299  C  C   . LEU A  1 297 ? 42.727  -28.987 54.576  1.00 38.61 ? 300  LEU A C   1 
ATOM   2300  O  O   . LEU A  1 297 ? 42.195  -29.051 53.469  1.00 40.09 ? 300  LEU A O   1 
ATOM   2301  C  CB  . LEU A  1 297 ? 41.500  -28.312 56.635  1.00 37.52 ? 300  LEU A CB  1 
ATOM   2302  C  CG  . LEU A  1 297 ? 40.022  -27.919 56.586  1.00 39.18 ? 300  LEU A CG  1 
ATOM   2303  C  CD1 . LEU A  1 297 ? 39.134  -29.041 56.052  1.00 38.81 ? 300  LEU A CD1 1 
ATOM   2304  C  CD2 . LEU A  1 297 ? 39.559  -27.476 57.961  1.00 39.32 ? 300  LEU A CD2 1 
ATOM   2305  N  N   . ARG A  1 298 ? 43.944  -28.487 54.760  1.00 38.58 ? 301  ARG A N   1 
ATOM   2306  C  CA  . ARG A  1 298 ? 44.687  -27.871 53.666  1.00 38.40 ? 301  ARG A CA  1 
ATOM   2307  C  C   . ARG A  1 298 ? 44.992  -28.899 52.586  1.00 37.85 ? 301  ARG A C   1 
ATOM   2308  O  O   . ARG A  1 298 ? 44.950  -28.595 51.391  1.00 36.43 ? 301  ARG A O   1 
ATOM   2309  C  CB  . ARG A  1 298 ? 45.983  -27.234 54.176  1.00 37.48 ? 301  ARG A CB  1 
ATOM   2310  C  CG  . ARG A  1 298 ? 47.032  -26.992 53.110  1.00 36.67 ? 301  ARG A CG  1 
ATOM   2311  C  CD  . ARG A  1 298 ? 48.152  -26.075 53.629  1.00 40.06 ? 301  ARG A CD  1 
ATOM   2312  N  NE  . ARG A  1 298 ? 48.980  -25.587 52.530  1.00 39.37 ? 301  ARG A NE  1 
ATOM   2313  C  CZ  . ARG A  1 298 ? 49.695  -26.379 51.739  1.00 42.74 ? 301  ARG A CZ  1 
ATOM   2314  N  NH1 . ARG A  1 298 ? 49.735  -27.692 51.975  1.00 42.33 ? 301  ARG A NH1 1 
ATOM   2315  N  NH2 . ARG A  1 298 ? 50.342  -25.873 50.691  1.00 42.86 ? 301  ARG A NH2 1 
ATOM   2316  N  N   . LYS A  1 299 ? 45.262  -30.123 53.019  1.00 35.73 ? 302  LYS A N   1 
ATOM   2317  C  CA  . LYS A  1 299 ? 45.461  -31.240 52.110  1.00 37.53 ? 302  LYS A CA  1 
ATOM   2318  C  C   . LYS A  1 299 ? 44.222  -31.513 51.257  1.00 36.24 ? 302  LYS A C   1 
ATOM   2319  O  O   . LYS A  1 299 ? 44.319  -31.796 50.058  1.00 35.17 ? 302  LYS A O   1 
ATOM   2320  C  CB  . LYS A  1 299 ? 45.814  -32.501 52.905  1.00 39.25 ? 302  LYS A CB  1 
ATOM   2321  C  CG  . LYS A  1 299 ? 46.606  -33.507 52.104  1.00 44.23 ? 302  LYS A CG  1 
ATOM   2322  C  CD  . LYS A  1 299 ? 47.573  -32.789 51.166  1.00 47.38 ? 302  LYS A CD  1 
ATOM   2323  C  CE  . LYS A  1 299 ? 47.565  -33.405 49.758  1.00 50.62 ? 302  LYS A CE  1 
ATOM   2324  N  NZ  . LYS A  1 299 ? 48.486  -34.584 49.631  1.00 50.21 ? 302  LYS A NZ  1 
ATOM   2325  N  N   . ALA A  1 300 ? 43.064  -31.518 51.904  1.00 36.58 ? 303  ALA A N   1 
ATOM   2326  C  CA  . ALA A  1 300 ? 41.830  -31.886 51.227  1.00 35.85 ? 303  ALA A CA  1 
ATOM   2327  C  C   . ALA A  1 300 ? 41.425  -30.760 50.275  1.00 35.47 ? 303  ALA A C   1 
ATOM   2328  O  O   . ALA A  1 300 ? 41.025  -31.005 49.127  1.00 38.32 ? 303  ALA A O   1 
ATOM   2329  C  CB  . ALA A  1 300 ? 40.741  -32.167 52.235  1.00 34.14 ? 303  ALA A CB  1 
ATOM   2330  N  N   . LEU A  1 301 ? 41.631  -29.527 50.724  1.00 32.30 ? 304  LEU A N   1 
ATOM   2331  C  CA  . LEU A  1 301 ? 41.428  -28.366 49.884  1.00 30.08 ? 304  LEU A CA  1 
ATOM   2332  C  C   . LEU A  1 301 ? 42.237  -28.485 48.586  1.00 31.46 ? 304  LEU A C   1 
ATOM   2333  O  O   . LEU A  1 301 ? 41.674  -28.479 47.490  1.00 31.94 ? 304  LEU A O   1 
ATOM   2334  C  CB  . LEU A  1 301 ? 41.776  -27.088 50.651  1.00 27.92 ? 304  LEU A CB  1 
ATOM   2335  C  CG  . LEU A  1 301 ? 40.715  -26.682 51.678  1.00 26.33 ? 304  LEU A CG  1 
ATOM   2336  C  CD1 . LEU A  1 301 ? 41.281  -25.772 52.743  1.00 26.06 ? 304  LEU A CD1 1 
ATOM   2337  C  CD2 . LEU A  1 301 ? 39.527  -26.038 50.992  1.00 26.24 ? 304  LEU A CD2 1 
ATOM   2338  N  N   . ASN A  1 302 ? 43.550  -28.638 48.705  1.00 30.84 ? 305  ASN A N   1 
ATOM   2339  C  CA  . ASN A  1 302 ? 44.390  -28.684 47.521  1.00 32.81 ? 305  ASN A CA  1 
ATOM   2340  C  C   . ASN A  1 302 ? 43.970  -29.793 46.573  1.00 31.83 ? 305  ASN A C   1 
ATOM   2341  O  O   . ASN A  1 302 ? 43.891  -29.587 45.366  1.00 32.09 ? 305  ASN A O   1 
ATOM   2342  C  CB  . ASN A  1 302 ? 45.866  -28.809 47.889  1.00 33.84 ? 305  ASN A CB  1 
ATOM   2343  C  CG  . ASN A  1 302 ? 46.420  -27.536 48.492  1.00 36.85 ? 305  ASN A CG  1 
ATOM   2344  O  OD1 . ASN A  1 302 ? 45.968  -26.435 48.167  1.00 38.75 ? 305  ASN A OD1 1 
ATOM   2345  N  ND2 . ASN A  1 302 ? 47.353  -27.681 49.433  1.00 36.46 ? 305  ASN A ND2 1 
ATOM   2346  N  N   . THR A  1 303 ? 43.680  -30.963 47.126  1.00 31.78 ? 306  THR A N   1 
ATOM   2347  C  CA  . THR A  1 303 ? 43.230  -32.093 46.315  1.00 32.11 ? 306  THR A CA  1 
ATOM   2348  C  C   . THR A  1 303 ? 41.957  -31.753 45.525  1.00 29.20 ? 306  THR A C   1 
ATOM   2349  O  O   . THR A  1 303 ? 41.860  -32.026 44.329  1.00 30.07 ? 306  THR A O   1 
ATOM   2350  C  CB  . THR A  1 303 ? 42.998  -33.351 47.189  1.00 32.49 ? 306  THR A CB  1 
ATOM   2351  O  OG1 . THR A  1 303 ? 44.261  -33.849 47.627  1.00 33.07 ? 306  THR A OG1 1 
ATOM   2352  C  CG2 . THR A  1 303 ? 42.282  -34.450 46.403  1.00 32.41 ? 306  THR A CG2 1 
ATOM   2353  N  N   . ASN A  1 304 ? 40.982  -31.162 46.196  1.00 29.59 ? 307  ASN A N   1 
ATOM   2354  C  CA  . ASN A  1 304 ? 39.750  -30.741 45.523  1.00 29.37 ? 307  ASN A CA  1 
ATOM   2355  C  C   . ASN A  1 304 ? 39.929  -29.512 44.618  1.00 28.39 ? 307  ASN A C   1 
ATOM   2356  O  O   . ASN A  1 304 ? 39.247  -29.382 43.599  1.00 32.62 ? 307  ASN A O   1 
ATOM   2357  C  CB  . ASN A  1 304 ? 38.619  -30.514 46.532  1.00 28.21 ? 307  ASN A CB  1 
ATOM   2358  C  CG  . ASN A  1 304 ? 38.128  -31.806 47.161  1.00 32.02 ? 307  ASN A CG  1 
ATOM   2359  O  OD1 . ASN A  1 304 ? 37.309  -32.525 46.583  1.00 33.63 ? 307  ASN A OD1 1 
ATOM   2360  N  ND2 . ASN A  1 304 ? 38.622  -32.104 48.363  1.00 32.47 ? 307  ASN A ND2 1 
ATOM   2361  N  N   . LEU A  1 305 ? 40.845  -28.619 44.972  1.00 27.78 ? 308  LEU A N   1 
ATOM   2362  C  CA  . LEU A  1 305 ? 41.186  -27.504 44.076  1.00 28.41 ? 308  LEU A CA  1 
ATOM   2363  C  C   . LEU A  1 305 ? 41.798  -27.979 42.750  1.00 30.30 ? 308  LEU A C   1 
ATOM   2364  O  O   . LEU A  1 305 ? 41.445  -27.475 41.671  1.00 29.05 ? 308  LEU A O   1 
ATOM   2365  C  CB  . LEU A  1 305 ? 42.093  -26.492 44.771  1.00 23.74 ? 308  LEU A CB  1 
ATOM   2366  C  CG  . LEU A  1 305 ? 41.415  -25.578 45.801  1.00 26.15 ? 308  LEU A CG  1 
ATOM   2367  C  CD1 . LEU A  1 305 ? 42.437  -24.953 46.761  1.00 25.11 ? 308  LEU A CD1 1 
ATOM   2368  C  CD2 . LEU A  1 305 ? 40.580  -24.503 45.147  1.00 20.18 ? 308  LEU A CD2 1 
ATOM   2369  N  N   . ASP A  1 306 ? 42.673  -28.979 42.838  1.00 29.35 ? 309  ASP A N   1 
ATOM   2370  C  CA  . ASP A  1 306 ? 43.243  -29.609 41.666  1.00 32.83 ? 309  ASP A CA  1 
ATOM   2371  C  C   . ASP A  1 306 ? 42.131  -30.117 40.761  1.00 34.59 ? 309  ASP A C   1 
ATOM   2372  O  O   . ASP A  1 306 ? 42.150  -29.901 39.549  1.00 35.81 ? 309  ASP A O   1 
ATOM   2373  C  CB  . ASP A  1 306 ? 44.119  -30.796 42.075  1.00 36.58 ? 309  ASP A CB  1 
ATOM   2374  C  CG  . ASP A  1 306 ? 45.379  -30.381 42.815  1.00 39.76 ? 309  ASP A CG  1 
ATOM   2375  O  OD1 . ASP A  1 306 ? 45.728  -29.181 42.815  1.00 38.76 ? 309  ASP A OD1 1 
ATOM   2376  O  OD2 . ASP A  1 306 ? 46.037  -31.278 43.391  1.00 44.55 ? 309  ASP A OD2 1 
ATOM   2377  N  N   . PHE A  1 307 ? 41.203  -30.870 41.341  1.00 34.81 ? 310  PHE A N   1 
ATOM   2378  C  CA  . PHE A  1 307 ? 40.124  -31.457 40.565  1.00 33.06 ? 310  PHE A CA  1 
ATOM   2379  C  C   . PHE A  1 307 ? 39.251  -30.343 39.957  1.00 29.80 ? 310  PHE A C   1 
ATOM   2380  O  O   . PHE A  1 307 ? 38.888  -30.398 38.799  1.00 32.16 ? 310  PHE A O   1 
ATOM   2381  C  CB  . PHE A  1 307 ? 39.266  -32.401 41.424  1.00 33.19 ? 310  PHE A CB  1 
ATOM   2382  C  CG  . PHE A  1 307 ? 40.001  -33.612 41.950  1.00 32.78 ? 310  PHE A CG  1 
ATOM   2383  C  CD1 . PHE A  1 307 ? 41.079  -34.155 41.259  1.00 34.46 ? 310  PHE A CD1 1 
ATOM   2384  C  CD2 . PHE A  1 307 ? 39.542  -34.270 43.088  1.00 31.06 ? 310  PHE A CD2 1 
ATOM   2385  C  CE1 . PHE A  1 307 ? 41.790  -35.249 41.785  1.00 35.10 ? 310  PHE A CE1 1 
ATOM   2386  C  CE2 . PHE A  1 307 ? 40.211  -35.390 43.601  1.00 32.28 ? 310  PHE A CE2 1 
ATOM   2387  C  CZ  . PHE A  1 307 ? 41.333  -35.882 42.953  1.00 33.45 ? 310  PHE A CZ  1 
ATOM   2388  N  N   . PHE A  1 308 ? 38.893  -29.349 40.752  1.00 27.63 ? 311  PHE A N   1 
ATOM   2389  C  CA  . PHE A  1 308 ? 38.123  -28.222 40.236  1.00 26.74 ? 311  PHE A CA  1 
ATOM   2390  C  C   . PHE A  1 308 ? 38.801  -27.632 38.988  1.00 25.77 ? 311  PHE A C   1 
ATOM   2391  O  O   . PHE A  1 308 ? 38.188  -27.555 37.910  1.00 23.71 ? 311  PHE A O   1 
ATOM   2392  C  CB  . PHE A  1 308 ? 37.911  -27.173 41.331  1.00 24.82 ? 311  PHE A CB  1 
ATOM   2393  C  CG  . PHE A  1 308 ? 37.191  -25.935 40.865  1.00 25.34 ? 311  PHE A CG  1 
ATOM   2394  C  CD1 . PHE A  1 308 ? 35.983  -26.031 40.186  1.00 21.92 ? 311  PHE A CD1 1 
ATOM   2395  C  CD2 . PHE A  1 308 ? 37.747  -24.679 41.071  1.00 23.38 ? 311  PHE A CD2 1 
ATOM   2396  C  CE1 . PHE A  1 308 ? 35.337  -24.907 39.740  1.00 25.26 ? 311  PHE A CE1 1 
ATOM   2397  C  CE2 . PHE A  1 308 ? 37.117  -23.535 40.607  1.00 22.32 ? 311  PHE A CE2 1 
ATOM   2398  C  CZ  . PHE A  1 308 ? 35.902  -23.640 39.955  1.00 25.16 ? 311  PHE A CZ  1 
ATOM   2399  N  N   . PHE A  1 309 ? 40.099  -27.368 39.076  1.00 25.14 ? 312  PHE A N   1 
ATOM   2400  C  CA  . PHE A  1 309 ? 40.826  -26.822 37.919  1.00 24.99 ? 312  PHE A CA  1 
ATOM   2401  C  C   . PHE A  1 309 ? 40.751  -27.689 36.643  1.00 28.19 ? 312  PHE A C   1 
ATOM   2402  O  O   . PHE A  1 309 ? 40.545  -27.171 35.548  1.00 30.17 ? 312  PHE A O   1 
ATOM   2403  C  CB  . PHE A  1 309 ? 42.277  -26.482 38.275  1.00 25.58 ? 312  PHE A CB  1 
ATOM   2404  C  CG  . PHE A  1 309 ? 43.082  -25.983 37.105  1.00 26.38 ? 312  PHE A CG  1 
ATOM   2405  C  CD1 . PHE A  1 309 ? 42.980  -24.662 36.691  1.00 24.77 ? 312  PHE A CD1 1 
ATOM   2406  C  CD2 . PHE A  1 309 ? 43.915  -26.843 36.404  1.00 26.57 ? 312  PHE A CD2 1 
ATOM   2407  C  CE1 . PHE A  1 309 ? 43.707  -24.207 35.620  1.00 28.35 ? 312  PHE A CE1 1 
ATOM   2408  C  CE2 . PHE A  1 309 ? 44.624  -26.401 35.308  1.00 26.59 ? 312  PHE A CE2 1 
ATOM   2409  C  CZ  . PHE A  1 309 ? 44.508  -25.087 34.898  1.00 27.38 ? 312  PHE A CZ  1 
ATOM   2410  N  N   . GLN A  1 310 ? 40.887  -29.002 36.773  1.00 26.54 ? 313  GLN A N   1 
ATOM   2411  C  CA  . GLN A  1 310 ? 40.679  -29.888 35.629  1.00 31.36 ? 313  GLN A CA  1 
ATOM   2412  C  C   . GLN A  1 310 ? 39.398  -29.552 34.857  1.00 31.90 ? 313  GLN A C   1 
ATOM   2413  O  O   . GLN A  1 310 ? 39.281  -29.873 33.680  1.00 31.81 ? 313  GLN A O   1 
ATOM   2414  C  CB  . GLN A  1 310 ? 40.624  -31.354 36.067  1.00 35.21 ? 313  GLN A CB  1 
ATOM   2415  C  CG  . GLN A  1 310 ? 41.981  -32.000 36.347  1.00 43.05 ? 313  GLN A CG  1 
ATOM   2416  C  CD  . GLN A  1 310 ? 41.844  -33.296 37.151  1.00 47.16 ? 313  GLN A CD  1 
ATOM   2417  O  OE1 . GLN A  1 310 ? 40.825  -33.986 37.052  1.00 49.56 ? 313  GLN A OE1 1 
ATOM   2418  N  NE2 . GLN A  1 310 ? 42.836  -33.593 38.000  1.00 46.74 ? 313  GLN A NE2 1 
ATOM   2419  N  N   . GLY A  1 311 ? 38.402  -29.000 35.541  1.00 30.51 ? 314  GLY A N   1 
ATOM   2420  C  CA  . GLY A  1 311 ? 37.076  -28.864 34.947  1.00 28.11 ? 314  GLY A CA  1 
ATOM   2421  C  C   . GLY A  1 311 ? 36.905  -27.561 34.202  1.00 28.92 ? 314  GLY A C   1 
ATOM   2422  O  O   . GLY A  1 311 ? 35.895  -27.349 33.539  1.00 32.30 ? 314  GLY A O   1 
ATOM   2423  N  N   . VAL A  1 312 ? 37.897  -26.681 34.309  1.00 28.75 ? 315  VAL A N   1 
ATOM   2424  C  CA  . VAL A  1 312 ? 37.812  -25.345 33.722  1.00 27.69 ? 315  VAL A CA  1 
ATOM   2425  C  C   . VAL A  1 312 ? 38.086  -25.376 32.210  1.00 28.69 ? 315  VAL A C   1 
ATOM   2426  O  O   . VAL A  1 312 ? 39.240  -25.317 31.767  1.00 25.63 ? 315  VAL A O   1 
ATOM   2427  C  CB  . VAL A  1 312 ? 38.779  -24.368 34.416  1.00 27.00 ? 315  VAL A CB  1 
ATOM   2428  C  CG1 . VAL A  1 312 ? 38.808  -23.055 33.688  1.00 29.44 ? 315  VAL A CG1 1 
ATOM   2429  C  CG2 . VAL A  1 312 ? 38.336  -24.124 35.847  1.00 27.27 ? 315  VAL A CG2 1 
ATOM   2430  N  N   . ALA A  1 313 ? 37.002  -25.424 31.435  1.00 28.57 ? 316  ALA A N   1 
ATOM   2431  C  CA  . ALA A  1 313 ? 37.036  -25.744 30.003  1.00 27.29 ? 316  ALA A CA  1 
ATOM   2432  C  C   . ALA A  1 313 ? 37.786  -24.739 29.136  1.00 24.95 ? 316  ALA A C   1 
ATOM   2433  O  O   . ALA A  1 313 ? 38.308  -25.089 28.083  1.00 28.64 ? 316  ALA A O   1 
ATOM   2434  C  CB  . ALA A  1 313 ? 35.611  -25.929 29.471  1.00 27.79 ? 316  ALA A CB  1 
ATOM   2435  N  N   . ALA A  1 314 ? 37.838  -23.488 29.560  1.00 26.05 ? 317  ALA A N   1 
ATOM   2436  C  CA  . ALA A  1 314 ? 38.654  -22.502 28.849  1.00 27.76 ? 317  ALA A CA  1 
ATOM   2437  C  C   . ALA A  1 314 ? 40.166  -22.714 29.022  1.00 26.33 ? 317  ALA A C   1 
ATOM   2438  O  O   . ALA A  1 314 ? 40.967  -22.138 28.305  1.00 28.88 ? 317  ALA A O   1 
ATOM   2439  C  CB  . ALA A  1 314 ? 38.253  -21.092 29.253  1.00 26.17 ? 317  ALA A CB  1 
ATOM   2440  N  N   . GLY A  1 315 ? 40.561  -23.557 29.959  1.00 30.61 ? 318  GLY A N   1 
ATOM   2441  C  CA  . GLY A  1 315 ? 41.994  -23.788 30.194  1.00 32.56 ? 318  GLY A CA  1 
ATOM   2442  C  C   . GLY A  1 315 ? 42.482  -23.042 31.420  1.00 31.14 ? 318  GLY A C   1 
ATOM   2443  O  O   . GLY A  1 315 ? 42.339  -23.525 32.541  1.00 27.39 ? 318  GLY A O   1 
ATOM   2444  N  N   . CYS A  1 316 ? 43.031  -21.847 31.198  1.00 30.13 ? 319  CYS A N   1 
ATOM   2445  C  CA  . CYS A  1 316 ? 43.428  -20.957 32.282  1.00 30.91 ? 319  CYS A CA  1 
ATOM   2446  C  C   . CYS A  1 316 ? 44.708  -21.409 32.972  1.00 29.24 ? 319  CYS A C   1 
ATOM   2447  O  O   . CYS A  1 316 ? 45.161  -22.537 32.795  1.00 28.60 ? 319  CYS A O   1 
ATOM   2448  C  CB  . CYS A  1 316 ? 42.310  -20.812 33.311  1.00 32.38 ? 319  CYS A CB  1 
ATOM   2449  S  SG  . CYS A  1 316 ? 40.811  -20.073 32.668  1.00 31.00 ? 319  CYS A SG  1 
ATOM   2450  N  N   . THR A  1 317 ? 45.306  -20.503 33.731  1.00 28.57 ? 320  THR A N   1 
ATOM   2451  C  CA  . THR A  1 317 ? 46.433  -20.848 34.593  1.00 30.18 ? 320  THR A CA  1 
ATOM   2452  C  C   . THR A  1 317 ? 45.925  -21.264 35.977  1.00 30.11 ? 320  THR A C   1 
ATOM   2453  O  O   . THR A  1 317 ? 45.173  -20.521 36.611  1.00 30.40 ? 320  THR A O   1 
ATOM   2454  C  CB  . THR A  1 317 ? 47.391  -19.641 34.745  1.00 32.38 ? 320  THR A CB  1 
ATOM   2455  O  OG1 . THR A  1 317 ? 47.986  -19.340 33.479  1.00 34.02 ? 320  THR A OG1 1 
ATOM   2456  C  CG2 . THR A  1 317 ? 48.501  -19.948 35.760  1.00 32.91 ? 320  THR A CG2 1 
ATOM   2457  N  N   . GLN A  1 318 ? 46.329  -22.440 36.453  1.00 31.94 ? 321  GLN A N   1 
ATOM   2458  C  CA  . GLN A  1 318 ? 45.940  -22.859 37.802  1.00 35.11 ? 321  GLN A CA  1 
ATOM   2459  C  C   . GLN A  1 318 ? 46.440  -21.863 38.846  1.00 35.44 ? 321  GLN A C   1 
ATOM   2460  O  O   . GLN A  1 318 ? 47.472  -21.226 38.648  1.00 36.24 ? 321  GLN A O   1 
ATOM   2461  C  CB  . GLN A  1 318 ? 46.425  -24.281 38.124  1.00 35.53 ? 321  GLN A CB  1 
ATOM   2462  C  CG  . GLN A  1 318 ? 46.106  -24.727 39.544  1.00 35.23 ? 321  GLN A CG  1 
ATOM   2463  C  CD  . GLN A  1 318 ? 46.206  -26.232 39.735  1.00 38.41 ? 321  GLN A CD  1 
ATOM   2464  O  OE1 . GLN A  1 318 ? 46.765  -26.958 38.891  1.00 38.91 ? 321  GLN A OE1 1 
ATOM   2465  N  NE2 . GLN A  1 318 ? 45.624  -26.721 40.831  1.00 36.19 ? 321  GLN A NE2 1 
ATOM   2466  N  N   . VAL A  1 319 ? 45.615  -21.639 39.874  1.00 37.81 ? 322  VAL A N   1 
ATOM   2467  C  CA  . VAL A  1 319 ? 45.844  -20.653 40.928  1.00 37.16 ? 322  VAL A CA  1 
ATOM   2468  C  C   . VAL A  1 319 ? 45.922  -21.377 42.288  1.00 39.50 ? 322  VAL A C   1 
ATOM   2469  O  O   . VAL A  1 319 ? 45.313  -22.443 42.481  1.00 40.60 ? 322  VAL A O   1 
ATOM   2470  C  CB  . VAL A  1 319 ? 44.688  -19.617 40.978  1.00 39.58 ? 322  VAL A CB  1 
ATOM   2471  C  CG1 . VAL A  1 319 ? 44.716  -18.815 42.276  1.00 38.01 ? 322  VAL A CG1 1 
ATOM   2472  C  CG2 . VAL A  1 319 ? 44.741  -18.684 39.784  1.00 38.99 ? 322  VAL A CG2 1 
ATOM   2473  N  N   . PHE A  1 320 ? 46.675  -20.810 43.228  1.00 38.57 ? 323  PHE A N   1 
ATOM   2474  C  CA  . PHE A  1 320 ? 47.030  -21.538 44.452  1.00 38.22 ? 323  PHE A CA  1 
ATOM   2475  C  C   . PHE A  1 320 ? 46.845  -20.716 45.713  1.00 37.79 ? 323  PHE A C   1 
ATOM   2476  O  O   . PHE A  1 320 ? 47.766  -20.041 46.157  1.00 40.94 ? 323  PHE A O   1 
ATOM   2477  C  CB  . PHE A  1 320 ? 48.454  -22.073 44.380  1.00 35.29 ? 323  PHE A CB  1 
ATOM   2478  C  CG  . PHE A  1 320 ? 48.677  -23.028 43.245  1.00 36.47 ? 323  PHE A CG  1 
ATOM   2479  C  CD1 . PHE A  1 320 ? 48.291  -24.356 43.353  1.00 35.50 ? 323  PHE A CD1 1 
ATOM   2480  C  CD2 . PHE A  1 320 ? 49.195  -22.579 42.037  1.00 34.79 ? 323  PHE A CD2 1 
ATOM   2481  C  CE1 . PHE A  1 320 ? 48.453  -25.229 42.292  1.00 34.49 ? 323  PHE A CE1 1 
ATOM   2482  C  CE2 . PHE A  1 320 ? 49.398  -23.454 40.987  1.00 33.07 ? 323  PHE A CE2 1 
ATOM   2483  C  CZ  . PHE A  1 320 ? 49.032  -24.787 41.120  1.00 33.94 ? 323  PHE A CZ  1 
ATOM   2484  N  N   . PRO A  1 321 ? 45.652  -20.799 46.313  1.00 36.83 ? 324  PRO A N   1 
ATOM   2485  C  CA  . PRO A  1 321 ? 45.369  -20.100 47.564  1.00 36.39 ? 324  PRO A CA  1 
ATOM   2486  C  C   . PRO A  1 321 ? 46.268  -20.551 48.721  1.00 38.15 ? 324  PRO A C   1 
ATOM   2487  O  O   . PRO A  1 321 ? 46.605  -19.734 49.578  1.00 39.80 ? 324  PRO A O   1 
ATOM   2488  C  CB  . PRO A  1 321 ? 43.912  -20.455 47.847  1.00 33.33 ? 324  PRO A CB  1 
ATOM   2489  C  CG  . PRO A  1 321 ? 43.658  -21.696 47.033  1.00 34.72 ? 324  PRO A CG  1 
ATOM   2490  C  CD  . PRO A  1 321 ? 44.493  -21.558 45.819  1.00 34.24 ? 324  PRO A CD  1 
ATOM   2491  N  N   . TYR A  1 322 ? 46.657  -21.826 48.747  1.00 38.62 ? 325  TYR A N   1 
ATOM   2492  C  CA  . TYR A  1 322 ? 47.476  -22.340 49.847  1.00 41.73 ? 325  TYR A CA  1 
ATOM   2493  C  C   . TYR A  1 322 ? 48.847  -22.818 49.379  1.00 44.95 ? 325  TYR A C   1 
ATOM   2494  O  O   . TYR A  1 322 ? 49.420  -23.752 49.950  1.00 46.59 ? 325  TYR A O   1 
ATOM   2495  C  CB  . TYR A  1 322 ? 46.745  -23.440 50.619  1.00 38.38 ? 325  TYR A CB  1 
ATOM   2496  C  CG  . TYR A  1 322 ? 45.321  -23.074 50.955  1.00 38.53 ? 325  TYR A CG  1 
ATOM   2497  C  CD1 . TYR A  1 322 ? 45.041  -22.107 51.928  1.00 37.76 ? 325  TYR A CD1 1 
ATOM   2498  C  CD2 . TYR A  1 322 ? 44.257  -23.592 50.213  1.00 35.76 ? 325  TYR A CD2 1 
ATOM   2499  C  CE1 . TYR A  1 322 ? 43.732  -21.715 52.192  1.00 36.93 ? 325  TYR A CE1 1 
ATOM   2500  C  CE2 . TYR A  1 322 ? 42.952  -23.212 50.472  1.00 36.21 ? 325  TYR A CE2 1 
ATOM   2501  C  CZ  . TYR A  1 322 ? 42.693  -22.273 51.459  1.00 37.16 ? 325  TYR A CZ  1 
ATOM   2502  O  OH  . TYR A  1 322 ? 41.397  -21.898 51.715  1.00 36.43 ? 325  TYR A OH  1 
ATOM   2503  N  N   . GLY A  1 323 ? 49.376  -22.163 48.346  1.00 47.73 ? 326  GLY A N   1 
ATOM   2504  C  CA  . GLY A  1 323 ? 50.717  -22.468 47.842  1.00 48.95 ? 326  GLY A CA  1 
ATOM   2505  C  C   . GLY A  1 323 ? 50.736  -23.635 46.872  1.00 49.96 ? 326  GLY A C   1 
ATOM   2506  O  O   . GLY A  1 323 ? 49.986  -24.601 47.036  1.00 50.30 ? 326  GLY A O   1 
ATOM   2507  N  N   . LEU B  1 1   ? -36.828 -37.400 24.697  1.00 45.85 ? 4    LEU B N   1 
ATOM   2508  C  CA  . LEU B  1 1   ? -36.791 -36.621 25.970  1.00 45.19 ? 4    LEU B CA  1 
ATOM   2509  C  C   . LEU B  1 1   ? -35.359 -36.506 26.504  1.00 43.20 ? 4    LEU B C   1 
ATOM   2510  O  O   . LEU B  1 1   ? -34.537 -37.412 26.303  1.00 43.14 ? 4    LEU B O   1 
ATOM   2511  C  CB  . LEU B  1 1   ? -37.729 -37.251 27.007  1.00 45.49 ? 4    LEU B CB  1 
ATOM   2512  C  CG  . LEU B  1 1   ? -39.108 -37.661 26.457  1.00 47.15 ? 4    LEU B CG  1 
ATOM   2513  C  CD1 . LEU B  1 1   ? -39.804 -38.706 27.350  1.00 47.70 ? 4    LEU B CD1 1 
ATOM   2514  C  CD2 . LEU B  1 1   ? -40.012 -36.436 26.225  1.00 46.33 ? 4    LEU B CD2 1 
ATOM   2515  N  N   . PRO B  1 2   ? -35.045 -35.366 27.144  1.00 41.20 ? 5    PRO B N   1 
ATOM   2516  C  CA  . PRO B  1 2   ? -33.741 -35.143 27.778  1.00 38.59 ? 5    PRO B CA  1 
ATOM   2517  C  C   . PRO B  1 2   ? -33.476 -36.187 28.850  1.00 34.65 ? 5    PRO B C   1 
ATOM   2518  O  O   . PRO B  1 2   ? -34.406 -36.644 29.503  1.00 33.07 ? 5    PRO B O   1 
ATOM   2519  C  CB  . PRO B  1 2   ? -33.889 -33.763 28.426  1.00 38.96 ? 5    PRO B CB  1 
ATOM   2520  C  CG  . PRO B  1 2   ? -35.045 -33.123 27.745  1.00 40.81 ? 5    PRO B CG  1 
ATOM   2521  C  CD  . PRO B  1 2   ? -35.964 -34.234 27.348  1.00 41.83 ? 5    PRO B CD  1 
ATOM   2522  N  N   . PRO B  1 3   ? -32.212 -36.592 29.008  1.00 32.26 ? 6    PRO B N   1 
ATOM   2523  C  CA  . PRO B  1 3   ? -31.867 -37.410 30.160  1.00 28.87 ? 6    PRO B CA  1 
ATOM   2524  C  C   . PRO B  1 3   ? -32.332 -36.737 31.448  1.00 27.71 ? 6    PRO B C   1 
ATOM   2525  O  O   . PRO B  1 3   ? -32.388 -35.491 31.527  1.00 21.50 ? 6    PRO B O   1 
ATOM   2526  C  CB  . PRO B  1 3   ? -30.334 -37.466 30.098  1.00 28.12 ? 6    PRO B CB  1 
ATOM   2527  C  CG  . PRO B  1 3   ? -30.032 -37.305 28.623  1.00 28.99 ? 6    PRO B CG  1 
ATOM   2528  C  CD  . PRO B  1 3   ? -31.045 -36.295 28.158  1.00 30.47 ? 6    PRO B CD  1 
ATOM   2529  N  N   . GLY B  1 4   ? -32.738 -37.563 32.414  1.00 26.29 ? 7    GLY B N   1 
ATOM   2530  C  CA  . GLY B  1 4   ? -32.961 -37.109 33.775  1.00 25.13 ? 7    GLY B CA  1 
ATOM   2531  C  C   . GLY B  1 4   ? -31.634 -37.044 34.528  1.00 25.58 ? 7    GLY B C   1 
ATOM   2532  O  O   . GLY B  1 4   ? -30.581 -37.369 33.971  1.00 20.79 ? 7    GLY B O   1 
ATOM   2533  N  N   . PRO B  1 5   ? -31.684 -36.646 35.808  1.00 24.98 ? 8    PRO B N   1 
ATOM   2534  C  CA  . PRO B  1 5   ? -30.494 -36.584 36.655  1.00 25.93 ? 8    PRO B CA  1 
ATOM   2535  C  C   . PRO B  1 5   ? -29.746 -37.927 36.743  1.00 29.07 ? 8    PRO B C   1 
ATOM   2536  O  O   . PRO B  1 5   ? -30.356 -38.990 36.642  1.00 31.72 ? 8    PRO B O   1 
ATOM   2537  C  CB  . PRO B  1 5   ? -31.056 -36.177 38.022  1.00 25.46 ? 8    PRO B CB  1 
ATOM   2538  C  CG  . PRO B  1 5   ? -32.334 -35.422 37.701  1.00 25.85 ? 8    PRO B CG  1 
ATOM   2539  C  CD  . PRO B  1 5   ? -32.866 -36.004 36.423  1.00 23.49 ? 8    PRO B CD  1 
ATOM   2540  N  N   . LEU B  1 6   ? -28.425 -37.867 36.887  1.00 30.41 ? 9    LEU B N   1 
ATOM   2541  C  CA  . LEU B  1 6   ? -27.634 -38.997 37.392  1.00 31.10 ? 9    LEU B CA  1 
ATOM   2542  C  C   . LEU B  1 6   ? -28.344 -39.717 38.542  1.00 33.14 ? 9    LEU B C   1 
ATOM   2543  O  O   . LEU B  1 6   ? -28.900 -39.071 39.454  1.00 28.84 ? 9    LEU B O   1 
ATOM   2544  C  CB  . LEU B  1 6   ? -26.285 -38.481 37.899  1.00 30.76 ? 9    LEU B CB  1 
ATOM   2545  C  CG  . LEU B  1 6   ? -25.034 -38.657 37.032  1.00 30.28 ? 9    LEU B CG  1 
ATOM   2546  C  CD1 . LEU B  1 6   ? -25.356 -38.623 35.550  1.00 25.12 ? 9    LEU B CD1 1 
ATOM   2547  C  CD2 . LEU B  1 6   ? -24.006 -37.609 37.419  1.00 25.48 ? 9    LEU B CD2 1 
ATOM   2548  N  N   . GLU B  1 7   ? -28.292 -41.047 38.527  1.00 35.94 ? 10   GLU B N   1 
ATOM   2549  C  CA  . GLU B  1 7   ? -28.815 -41.827 39.649  1.00 37.76 ? 10   GLU B CA  1 
ATOM   2550  C  C   . GLU B  1 7   ? -27.819 -41.821 40.790  1.00 35.86 ? 10   GLU B C   1 
ATOM   2551  O  O   . GLU B  1 7   ? -28.181 -41.664 41.956  1.00 30.89 ? 10   GLU B O   1 
ATOM   2552  C  CB  . GLU B  1 7   ? -29.090 -43.264 39.225  1.00 42.79 ? 10   GLU B CB  1 
ATOM   2553  C  CG  . GLU B  1 7   ? -29.843 -43.359 37.922  1.00 51.15 ? 10   GLU B CG  1 
ATOM   2554  C  CD  . GLU B  1 7   ? -30.991 -44.344 37.983  1.00 55.99 ? 10   GLU B CD  1 
ATOM   2555  O  OE1 . GLU B  1 7   ? -32.094 -43.943 38.427  1.00 58.91 ? 10   GLU B OE1 1 
ATOM   2556  O  OE2 . GLU B  1 7   ? -30.789 -45.515 37.577  1.00 58.36 ? 10   GLU B OE2 1 
ATOM   2557  N  N   . ASN B  1 8   ? -26.551 -42.002 40.447  1.00 32.82 ? 11   ASN B N   1 
ATOM   2558  C  CA  . ASN B  1 8   ? -25.509 -41.885 41.443  1.00 31.40 ? 11   ASN B CA  1 
ATOM   2559  C  C   . ASN B  1 8   ? -24.588 -40.689 41.163  1.00 28.71 ? 11   ASN B C   1 
ATOM   2560  O  O   . ASN B  1 8   ? -23.729 -40.744 40.281  1.00 28.71 ? 11   ASN B O   1 
ATOM   2561  C  CB  . ASN B  1 8   ? -24.736 -43.198 41.506  1.00 32.67 ? 11   ASN B CB  1 
ATOM   2562  C  CG  . ASN B  1 8   ? -23.697 -43.212 42.597  1.00 37.97 ? 11   ASN B CG  1 
ATOM   2563  O  OD1 . ASN B  1 8   ? -23.352 -42.168 43.161  1.00 36.45 ? 11   ASN B OD1 1 
ATOM   2564  N  ND2 . ASN B  1 8   ? -23.168 -44.401 42.886  1.00 41.78 ? 11   ASN B ND2 1 
ATOM   2565  N  N   . SER B  1 9   ? -24.754 -39.619 41.928  1.00 27.74 ? 12   SER B N   1 
ATOM   2566  C  CA  . SER B  1 9   ? -24.092 -38.344 41.616  1.00 27.33 ? 12   SER B CA  1 
ATOM   2567  C  C   . SER B  1 9   ? -22.862 -38.083 42.482  1.00 27.96 ? 12   SER B C   1 
ATOM   2568  O  O   . SER B  1 9   ? -22.392 -36.953 42.597  1.00 28.51 ? 12   SER B O   1 
ATOM   2569  C  CB  . SER B  1 9   ? -25.081 -37.200 41.758  1.00 28.15 ? 12   SER B CB  1 
ATOM   2570  O  OG  . SER B  1 9   ? -25.506 -37.082 43.102  1.00 28.83 ? 12   SER B OG  1 
ATOM   2571  N  N   . SER B  1 10  ? -22.292 -39.156 43.019  1.00 28.44 ? 13   SER B N   1 
ATOM   2572  C  CA  . SER B  1 10  ? -21.089 -39.072 43.831  1.00 25.44 ? 13   SER B CA  1 
ATOM   2573  C  C   . SER B  1 10  ? -19.922 -38.656 42.949  1.00 24.85 ? 13   SER B C   1 
ATOM   2574  O  O   . SER B  1 10  ? -19.968 -38.826 41.730  1.00 26.23 ? 13   SER B O   1 
ATOM   2575  C  CB  . SER B  1 10  ? -20.807 -40.436 44.472  1.00 26.39 ? 13   SER B CB  1 
ATOM   2576  O  OG  . SER B  1 10  ? -21.749 -40.705 45.499  1.00 26.89 ? 13   SER B OG  1 
ATOM   2577  N  N   . ALA B  1 11  ? -18.894 -38.082 43.561  1.00 23.73 ? 14   ALA B N   1 
ATOM   2578  C  CA  . ALA B  1 11  ? -17.595 -37.932 42.905  1.00 24.85 ? 14   ALA B CA  1 
ATOM   2579  C  C   . ALA B  1 11  ? -17.004 -39.300 42.583  1.00 24.94 ? 14   ALA B C   1 
ATOM   2580  O  O   . ALA B  1 11  ? -17.139 -40.243 43.356  1.00 25.53 ? 14   ALA B O   1 
ATOM   2581  C  CB  . ALA B  1 11  ? -16.636 -37.129 43.782  1.00 22.00 ? 14   ALA B CB  1 
ATOM   2582  N  N   . LYS B  1 12  ? -16.374 -39.403 41.422  1.00 26.84 ? 15   LYS B N   1 
ATOM   2583  C  CA  . LYS B  1 12  ? -15.697 -40.630 41.013  1.00 29.52 ? 15   LYS B CA  1 
ATOM   2584  C  C   . LYS B  1 12  ? -14.604 -40.220 40.034  1.00 27.69 ? 15   LYS B C   1 
ATOM   2585  O  O   . LYS B  1 12  ? -14.624 -39.097 39.531  1.00 21.45 ? 15   LYS B O   1 
ATOM   2586  C  CB  . LYS B  1 12  ? -16.684 -41.576 40.312  1.00 32.03 ? 15   LYS B CB  1 
ATOM   2587  C  CG  . LYS B  1 12  ? -17.214 -41.023 38.990  1.00 35.75 ? 15   LYS B CG  1 
ATOM   2588  C  CD  . LYS B  1 12  ? -18.520 -41.686 38.579  1.00 40.32 ? 15   LYS B CD  1 
ATOM   2589  C  CE  . LYS B  1 12  ? -18.291 -42.795 37.553  1.00 42.37 ? 15   LYS B CE  1 
ATOM   2590  N  NZ  . LYS B  1 12  ? -19.577 -43.165 36.882  1.00 43.80 ? 15   LYS B NZ  1 
ATOM   2591  N  N   . LEU B  1 13  ? -13.672 -41.133 39.757  1.00 27.24 ? 16   LEU B N   1 
ATOM   2592  C  CA  . LEU B  1 13  ? -12.705 -40.952 38.672  1.00 28.22 ? 16   LEU B CA  1 
ATOM   2593  C  C   . LEU B  1 13  ? -13.416 -40.777 37.329  1.00 28.76 ? 16   LEU B C   1 
ATOM   2594  O  O   . LEU B  1 13  ? -14.107 -41.693 36.864  1.00 28.97 ? 16   LEU B O   1 
ATOM   2595  C  CB  . LEU B  1 13  ? -11.754 -42.157 38.608  1.00 27.22 ? 16   LEU B CB  1 
ATOM   2596  C  CG  . LEU B  1 13  ? -10.611 -42.095 37.600  1.00 28.90 ? 16   LEU B CG  1 
ATOM   2597  C  CD1 . LEU B  1 13  ? -9.626  -40.954 37.940  1.00 28.49 ? 16   LEU B CD1 1 
ATOM   2598  C  CD2 . LEU B  1 13  ? -9.895  -43.449 37.474  1.00 28.10 ? 16   LEU B CD2 1 
ATOM   2599  N  N   . VAL B  1 14  ? -13.266 -39.602 36.719  1.00 26.77 ? 17   VAL B N   1 
ATOM   2600  C  CA  . VAL B  1 14  ? -13.710 -39.406 35.337  1.00 26.84 ? 17   VAL B CA  1 
ATOM   2601  C  C   . VAL B  1 14  ? -12.606 -39.421 34.270  1.00 25.73 ? 17   VAL B C   1 
ATOM   2602  O  O   . VAL B  1 14  ? -12.876 -39.675 33.103  1.00 22.06 ? 17   VAL B O   1 
ATOM   2603  C  CB  . VAL B  1 14  ? -14.640 -38.176 35.156  1.00 25.82 ? 17   VAL B CB  1 
ATOM   2604  C  CG1 . VAL B  1 14  ? -15.999 -38.462 35.784  1.00 26.72 ? 17   VAL B CG1 1 
ATOM   2605  C  CG2 . VAL B  1 14  ? -14.026 -36.955 35.743  1.00 25.06 ? 17   VAL B CG2 1 
ATOM   2606  N  N   . ASN B  1 15  ? -11.360 -39.182 34.665  1.00 27.08 ? 18   ASN B N   1 
ATOM   2607  C  CA  . ASN B  1 15  ? -10.242 -39.415 33.745  1.00 26.50 ? 18   ASN B CA  1 
ATOM   2608  C  C   . ASN B  1 15  ? -9.777  -40.881 33.726  1.00 26.55 ? 18   ASN B C   1 
ATOM   2609  O  O   . ASN B  1 15  ? -8.660  -41.204 34.165  1.00 28.91 ? 18   ASN B O   1 
ATOM   2610  C  CB  . ASN B  1 15  ? -9.072  -38.479 34.066  1.00 23.68 ? 18   ASN B CB  1 
ATOM   2611  C  CG  . ASN B  1 15  ? -8.053  -38.417 32.947  1.00 25.73 ? 18   ASN B CG  1 
ATOM   2612  O  OD1 . ASN B  1 15  ? -8.060  -39.248 32.026  1.00 27.15 ? 18   ASN B OD1 1 
ATOM   2613  N  ND2 . ASN B  1 15  ? -7.152  -37.450 33.030  1.00 23.70 ? 18   ASN B ND2 1 
ATOM   2614  N  N   . ASP B  1 16  ? -10.631 -41.769 33.234  1.00 26.76 ? 19   ASP B N   1 
ATOM   2615  C  CA  . ASP B  1 16  ? -10.428 -43.203 33.469  1.00 29.73 ? 19   ASP B CA  1 
ATOM   2616  C  C   . ASP B  1 16  ? -10.007 -43.969 32.210  1.00 33.78 ? 19   ASP B C   1 
ATOM   2617  O  O   . ASP B  1 16  ? -9.670  -43.359 31.189  1.00 33.27 ? 19   ASP B O   1 
ATOM   2618  C  CB  . ASP B  1 16  ? -11.644 -43.838 34.155  1.00 29.50 ? 19   ASP B CB  1 
ATOM   2619  C  CG  . ASP B  1 16  ? -12.934 -43.677 33.357  1.00 31.98 ? 19   ASP B CG  1 
ATOM   2620  O  OD1 . ASP B  1 16  ? -12.880 -43.197 32.206  1.00 31.36 ? 19   ASP B OD1 1 
ATOM   2621  O  OD2 . ASP B  1 16  ? -14.001 -44.086 33.864  1.00 31.04 ? 19   ASP B OD2 1 
ATOM   2622  N  N   . GLU B  1 17  ? -9.951  -45.298 32.297  1.00 35.03 ? 20   GLU B N   1 
ATOM   2623  C  CA  A GLU B  1 17  ? -9.403  -46.068 31.192  0.60 36.23 ? 20   GLU B CA  1 
ATOM   2624  C  CA  B GLU B  1 17  ? -9.438  -46.127 31.210  0.40 35.74 ? 20   GLU B CA  1 
ATOM   2625  C  C   . GLU B  1 17  ? -10.332 -46.021 29.980  1.00 36.23 ? 20   GLU B C   1 
ATOM   2626  O  O   . GLU B  1 17  ? -9.893  -46.202 28.853  1.00 37.03 ? 20   GLU B O   1 
ATOM   2627  C  CB  A GLU B  1 17  ? -9.099  -47.514 31.607  0.60 38.64 ? 20   GLU B CB  1 
ATOM   2628  C  CB  B GLU B  1 17  ? -9.345  -47.591 31.657  0.40 36.78 ? 20   GLU B CB  1 
ATOM   2629  C  CG  A GLU B  1 17  ? -7.892  -48.125 30.888  0.60 40.29 ? 20   GLU B CG  1 
ATOM   2630  C  CG  B GLU B  1 17  ? -8.975  -48.562 30.544  0.40 37.18 ? 20   GLU B CG  1 
ATOM   2631  C  CD  A GLU B  1 17  ? -6.562  -47.646 31.455  0.60 42.04 ? 20   GLU B CD  1 
ATOM   2632  C  CD  B GLU B  1 17  ? -9.686  -49.896 30.671  0.40 37.64 ? 20   GLU B CD  1 
ATOM   2633  O  OE1 A GLU B  1 17  ? -6.328  -47.830 32.670  0.60 43.25 ? 20   GLU B OE1 1 
ATOM   2634  O  OE1 B GLU B  1 17  ? -10.873 -49.977 30.284  0.40 37.08 ? 20   GLU B OE1 1 
ATOM   2635  O  OE2 A GLU B  1 17  ? -5.748  -47.089 30.690  0.60 41.08 ? 20   GLU B OE2 1 
ATOM   2636  O  OE2 B GLU B  1 17  ? -9.050  -50.868 31.133  0.40 35.55 ? 20   GLU B OE2 1 
ATOM   2637  N  N   . ALA B  1 18  ? -11.606 -45.740 30.208  1.00 35.61 ? 21   ALA B N   1 
ATOM   2638  C  CA  . ALA B  1 18  ? -12.560 -45.705 29.110  1.00 35.16 ? 21   ALA B CA  1 
ATOM   2639  C  C   . ALA B  1 18  ? -12.709 -44.306 28.483  1.00 34.61 ? 21   ALA B C   1 
ATOM   2640  O  O   . ALA B  1 18  ? -13.340 -44.145 27.432  1.00 36.10 ? 21   ALA B O   1 
ATOM   2641  C  CB  . ALA B  1 18  ? -13.912 -46.246 29.574  1.00 33.85 ? 21   ALA B CB  1 
ATOM   2642  N  N   . HIS B  1 19  ? -12.124 -43.302 29.126  1.00 31.23 ? 22   HIS B N   1 
ATOM   2643  C  CA  . HIS B  1 19  ? -12.248 -41.930 28.661  1.00 28.34 ? 22   HIS B CA  1 
ATOM   2644  C  C   . HIS B  1 19  ? -10.900 -41.231 28.714  1.00 29.06 ? 22   HIS B C   1 
ATOM   2645  O  O   . HIS B  1 19  ? -10.733 -40.262 29.456  1.00 30.49 ? 22   HIS B O   1 
ATOM   2646  C  CB  . HIS B  1 19  ? -13.274 -41.175 29.515  1.00 27.51 ? 22   HIS B CB  1 
ATOM   2647  C  CG  . HIS B  1 19  ? -14.652 -41.758 29.456  1.00 28.34 ? 22   HIS B CG  1 
ATOM   2648  N  ND1 . HIS B  1 19  ? -15.129 -42.645 30.399  1.00 29.31 ? 22   HIS B ND1 1 
ATOM   2649  C  CD2 . HIS B  1 19  ? -15.655 -41.591 28.560  1.00 28.67 ? 22   HIS B CD2 1 
ATOM   2650  C  CE1 . HIS B  1 19  ? -16.360 -43.007 30.084  1.00 26.96 ? 22   HIS B CE1 1 
ATOM   2651  N  NE2 . HIS B  1 19  ? -16.699 -42.390 28.964  1.00 29.46 ? 22   HIS B NE2 1 
ATOM   2652  N  N   . PRO B  1 20  ? -9.921  -41.743 27.953  1.00 28.42 ? 23   PRO B N   1 
ATOM   2653  C  CA  . PRO B  1 20  ? -8.582  -41.168 27.924  1.00 29.10 ? 23   PRO B CA  1 
ATOM   2654  C  C   . PRO B  1 20  ? -8.566  -39.915 27.061  1.00 26.90 ? 23   PRO B C   1 
ATOM   2655  O  O   . PRO B  1 20  ? -9.334  -39.825 26.103  1.00 25.34 ? 23   PRO B O   1 
ATOM   2656  C  CB  . PRO B  1 20  ? -7.745  -42.268 27.250  1.00 29.53 ? 23   PRO B CB  1 
ATOM   2657  C  CG  . PRO B  1 20  ? -8.740  -42.989 26.359  1.00 28.72 ? 23   PRO B CG  1 
ATOM   2658  C  CD  . PRO B  1 20  ? -10.068 -42.890 27.033  1.00 28.24 ? 23   PRO B CD  1 
ATOM   2659  N  N   . TRP B  1 21  ? -7.706  -38.959 27.400  1.00 24.99 ? 24   TRP B N   1 
ATOM   2660  C  CA  . TRP B  1 21  ? -7.428  -37.830 26.507  1.00 23.63 ? 24   TRP B CA  1 
ATOM   2661  C  C   . TRP B  1 21  ? -6.743  -38.262 25.212  1.00 21.80 ? 24   TRP B C   1 
ATOM   2662  O  O   . TRP B  1 21  ? -5.792  -39.026 25.238  1.00 22.44 ? 24   TRP B O   1 
ATOM   2663  C  CB  . TRP B  1 21  ? -6.547  -36.795 27.208  1.00 23.22 ? 24   TRP B CB  1 
ATOM   2664  C  CG  . TRP B  1 21  ? -6.422  -35.477 26.440  1.00 23.10 ? 24   TRP B CG  1 
ATOM   2665  C  CD1 . TRP B  1 21  ? -7.279  -34.423 26.480  1.00 20.89 ? 24   TRP B CD1 1 
ATOM   2666  C  CD2 . TRP B  1 21  ? -5.383  -35.114 25.521  1.00 24.13 ? 24   TRP B CD2 1 
ATOM   2667  N  NE1 . TRP B  1 21  ? -6.837  -33.419 25.646  1.00 23.10 ? 24   TRP B NE1 1 
ATOM   2668  C  CE2 . TRP B  1 21  ? -5.664  -33.817 25.062  1.00 23.88 ? 24   TRP B CE2 1 
ATOM   2669  C  CE3 . TRP B  1 21  ? -4.228  -35.753 25.067  1.00 25.95 ? 24   TRP B CE3 1 
ATOM   2670  C  CZ2 . TRP B  1 21  ? -4.837  -33.147 24.175  1.00 26.44 ? 24   TRP B CZ2 1 
ATOM   2671  C  CZ3 . TRP B  1 21  ? -3.408  -35.090 24.188  1.00 26.09 ? 24   TRP B CZ3 1 
ATOM   2672  C  CH2 . TRP B  1 21  ? -3.712  -33.803 23.748  1.00 27.84 ? 24   TRP B CH2 1 
ATOM   2673  N  N   . LYS B  1 22  ? -7.145  -37.669 24.096  1.00 23.29 ? 25   LYS B N   1 
ATOM   2674  C  CA  . LYS B  1 22  ? -6.491  -37.927 22.815  1.00 25.50 ? 25   LYS B CA  1 
ATOM   2675  C  C   . LYS B  1 22  ? -6.312  -36.612 22.082  1.00 26.86 ? 25   LYS B C   1 
ATOM   2676  O  O   . LYS B  1 22  ? -7.061  -35.660 22.315  1.00 29.92 ? 25   LYS B O   1 
ATOM   2677  C  CB  . LYS B  1 22  ? -7.317  -38.910 21.958  1.00 24.48 ? 25   LYS B CB  1 
ATOM   2678  C  CG  . LYS B  1 22  ? -7.240  -40.364 22.422  1.00 26.58 ? 25   LYS B CG  1 
ATOM   2679  C  CD  . LYS B  1 22  ? -8.257  -41.234 21.679  1.00 31.87 ? 25   LYS B CD  1 
ATOM   2680  C  CE  . LYS B  1 22  ? -8.235  -42.678 22.145  1.00 35.42 ? 25   LYS B CE  1 
ATOM   2681  N  NZ  . LYS B  1 22  ? -8.247  -43.606 20.971  1.00 38.79 ? 25   LYS B NZ  1 
ATOM   2682  N  N   . PRO B  1 23  ? -5.322  -36.543 21.187  1.00 26.62 ? 26   PRO B N   1 
ATOM   2683  C  CA  . PRO B  1 23  ? -5.111  -35.286 20.454  1.00 26.95 ? 26   PRO B CA  1 
ATOM   2684  C  C   . PRO B  1 23  ? -6.132  -35.132 19.338  1.00 27.61 ? 26   PRO B C   1 
ATOM   2685  O  O   . PRO B  1 23  ? -6.741  -36.122 18.914  1.00 28.89 ? 26   PRO B O   1 
ATOM   2686  C  CB  . PRO B  1 23  ? -3.699  -35.430 19.855  1.00 28.25 ? 26   PRO B CB  1 
ATOM   2687  C  CG  . PRO B  1 23  ? -3.147  -36.756 20.352  1.00 29.06 ? 26   PRO B CG  1 
ATOM   2688  C  CD  . PRO B  1 23  ? -4.274  -37.549 20.944  1.00 27.72 ? 26   PRO B CD  1 
ATOM   2689  N  N   . LEU B  1 24  ? -6.331  -33.902 18.886  1.00 25.38 ? 27   LEU B N   1 
ATOM   2690  C  CA  . LEU B  1 24  ? -7.221  -33.636 17.769  1.00 32.39 ? 27   LEU B CA  1 
ATOM   2691  C  C   . LEU B  1 24  ? -6.793  -34.358 16.487  1.00 34.84 ? 27   LEU B C   1 
ATOM   2692  O  O   . LEU B  1 24  ? -5.664  -34.219 16.035  1.00 35.51 ? 27   LEU B O   1 
ATOM   2693  C  CB  . LEU B  1 24  ? -7.321  -32.125 17.518  1.00 31.23 ? 27   LEU B CB  1 
ATOM   2694  C  CG  . LEU B  1 24  ? -7.810  -31.327 18.729  1.00 33.29 ? 27   LEU B CG  1 
ATOM   2695  C  CD1 . LEU B  1 24  ? -7.863  -29.820 18.445  1.00 33.86 ? 27   LEU B CD1 1 
ATOM   2696  C  CD2 . LEU B  1 24  ? -9.145  -31.842 19.255  1.00 28.77 ? 27   LEU B CD2 1 
ATOM   2697  N  N   . ARG B  1 25  ? -7.705  -35.126 15.905  1.00 37.21 ? 28   ARG B N   1 
ATOM   2698  C  CA  . ARG B  1 25  ? -7.580  -35.518 14.509  1.00 38.50 ? 28   ARG B CA  1 
ATOM   2699  C  C   . ARG B  1 25  ? -8.085  -34.399 13.603  1.00 41.67 ? 28   ARG B C   1 
ATOM   2700  O  O   . ARG B  1 25  ? -8.846  -33.539 14.033  1.00 41.58 ? 28   ARG B O   1 
ATOM   2701  C  CB  . ARG B  1 25  ? -8.363  -36.794 14.246  1.00 36.38 ? 28   ARG B CB  1 
ATOM   2702  C  CG  . ARG B  1 25  ? -7.878  -37.988 15.038  1.00 37.14 ? 28   ARG B CG  1 
ATOM   2703  C  CD  . ARG B  1 25  ? -9.010  -38.941 15.230  1.00 40.19 ? 28   ARG B CD  1 
ATOM   2704  N  NE  . ARG B  1 25  ? -10.253 -38.195 15.414  1.00 43.87 ? 28   ARG B NE  1 
ATOM   2705  C  CZ  . ARG B  1 25  ? -11.461 -38.744 15.424  1.00 44.23 ? 28   ARG B CZ  1 
ATOM   2706  N  NH1 . ARG B  1 25  ? -11.588 -40.058 15.283  1.00 47.57 ? 28   ARG B NH1 1 
ATOM   2707  N  NH2 . ARG B  1 25  ? -12.536 -37.986 15.596  1.00 41.83 ? 28   ARG B NH2 1 
ATOM   2708  N  N   . PRO B  1 26  ? -7.705  -34.441 12.324  1.00 45.39 ? 29   PRO B N   1 
ATOM   2709  C  CA  . PRO B  1 26  ? -7.637  -33.224 11.503  1.00 45.06 ? 29   PRO B CA  1 
ATOM   2710  C  C   . PRO B  1 26  ? -8.992  -32.513 11.307  1.00 41.89 ? 29   PRO B C   1 
ATOM   2711  O  O   . PRO B  1 26  ? -9.049  -31.276 11.329  1.00 43.07 ? 29   PRO B O   1 
ATOM   2712  C  CB  . PRO B  1 26  ? -7.076  -33.737 10.169  1.00 47.79 ? 29   PRO B CB  1 
ATOM   2713  C  CG  . PRO B  1 26  ? -6.360  -35.033 10.535  1.00 47.43 ? 29   PRO B CG  1 
ATOM   2714  C  CD  . PRO B  1 26  ? -7.214  -35.632 11.604  1.00 45.47 ? 29   PRO B CD  1 
ATOM   2715  N  N   . GLY B  1 27  ? -10.074 -33.276 11.194  1.00 34.02 ? 30   GLY B N   1 
ATOM   2716  C  CA  . GLY B  1 27  ? -11.410 -32.674 11.200  1.00 30.06 ? 30   GLY B CA  1 
ATOM   2717  C  C   . GLY B  1 27  ? -12.149 -32.593 12.543  1.00 26.03 ? 30   GLY B C   1 
ATOM   2718  O  O   . GLY B  1 27  ? -13.337 -32.308 12.576  1.00 26.13 ? 30   GLY B O   1 
ATOM   2719  N  N   . ASP B  1 28  ? -11.441 -32.759 13.653  1.00 25.57 ? 31   ASP B N   1 
ATOM   2720  C  CA  . ASP B  1 28  ? -12.052 -32.673 14.981  1.00 23.60 ? 31   ASP B CA  1 
ATOM   2721  C  C   . ASP B  1 28  ? -12.393 -31.226 15.304  1.00 25.14 ? 31   ASP B C   1 
ATOM   2722  O  O   . ASP B  1 28  ? -11.601 -30.331 15.030  1.00 28.35 ? 31   ASP B O   1 
ATOM   2723  C  CB  . ASP B  1 28  ? -11.093 -33.229 16.040  1.00 24.54 ? 31   ASP B CB  1 
ATOM   2724  C  CG  . ASP B  1 28  ? -11.087 -34.761 16.083  1.00 25.21 ? 31   ASP B CG  1 
ATOM   2725  O  OD1 . ASP B  1 28  ? -12.038 -35.352 15.560  1.00 29.30 ? 31   ASP B OD1 1 
ATOM   2726  O  OD2 . ASP B  1 28  ? -10.133 -35.386 16.614  1.00 26.47 ? 31   ASP B OD2 1 
ATOM   2727  N  N   . ILE B  1 29  ? -13.577 -30.983 15.864  1.00 24.37 ? 32   ILE B N   1 
ATOM   2728  C  CA  . ILE B  1 29  ? -13.991 -29.612 16.173  1.00 20.05 ? 32   ILE B CA  1 
ATOM   2729  C  C   . ILE B  1 29  ? -13.979 -29.308 17.675  1.00 20.64 ? 32   ILE B C   1 
ATOM   2730  O  O   . ILE B  1 29  ? -14.490 -30.090 18.490  1.00 19.01 ? 32   ILE B O   1 
ATOM   2731  C  CB  . ILE B  1 29  ? -15.374 -29.308 15.582  1.00 23.55 ? 32   ILE B CB  1 
ATOM   2732  C  CG1 . ILE B  1 29  ? -15.318 -29.403 14.056  1.00 25.08 ? 32   ILE B CG1 1 
ATOM   2733  C  CG2 . ILE B  1 29  ? -15.871 -27.937 16.045  1.00 22.28 ? 32   ILE B CG2 1 
ATOM   2734  C  CD1 . ILE B  1 29  ? -16.607 -29.858 13.415  1.00 28.57 ? 32   ILE B CD1 1 
ATOM   2735  N  N   . ARG B  1 30  ? -13.305 -28.218 18.042  1.00 17.62 ? 33   ARG B N   1 
ATOM   2736  C  CA  . ARG B  1 30  ? -13.371 -27.682 19.396  1.00 19.23 ? 33   ARG B CA  1 
ATOM   2737  C  C   . ARG B  1 30  ? -13.775 -26.221 19.286  1.00 18.52 ? 33   ARG B C   1 
ATOM   2738  O  O   . ARG B  1 30  ? -13.541 -25.610 18.256  1.00 16.34 ? 33   ARG B O   1 
ATOM   2739  C  CB  . ARG B  1 30  ? -11.996 -27.801 20.087  1.00 19.17 ? 33   ARG B CB  1 
ATOM   2740  C  CG  . ARG B  1 30  ? -11.504 -29.249 20.232  1.00 18.07 ? 33   ARG B CG  1 
ATOM   2741  C  CD  . ARG B  1 30  ? -12.460 -30.081 21.106  1.00 18.10 ? 33   ARG B CD  1 
ATOM   2742  N  NE  . ARG B  1 30  ? -11.989 -31.455 21.281  1.00 17.20 ? 33   ARG B NE  1 
ATOM   2743  C  CZ  . ARG B  1 30  ? -12.388 -32.474 20.523  1.00 17.67 ? 33   ARG B CZ  1 
ATOM   2744  N  NH1 . ARG B  1 30  ? -13.274 -32.278 19.543  1.00 15.31 ? 33   ARG B NH1 1 
ATOM   2745  N  NH2 . ARG B  1 30  ? -11.888 -33.679 20.731  1.00 13.26 ? 33   ARG B NH2 1 
ATOM   2746  N  N   . GLY B  1 31  ? -14.422 -25.676 20.315  1.00 15.99 ? 34   GLY B N   1 
ATOM   2747  C  CA  . GLY B  1 31  ? -14.846 -24.286 20.265  1.00 16.63 ? 34   GLY B CA  1 
ATOM   2748  C  C   . GLY B  1 31  ? -14.576 -23.517 21.545  1.00 16.89 ? 34   GLY B C   1 
ATOM   2749  O  O   . GLY B  1 31  ? -13.608 -23.795 22.256  1.00 18.68 ? 34   GLY B O   1 
ATOM   2750  N  N   . PRO B  1 32  ? -15.529 -22.668 21.933  1.00 15.63 ? 35   PRO B N   1 
ATOM   2751  C  CA  . PRO B  1 32  ? -15.312 -21.658 22.971  1.00 14.35 ? 35   PRO B CA  1 
ATOM   2752  C  C   . PRO B  1 32  ? -15.656 -22.144 24.375  1.00 13.13 ? 35   PRO B C   1 
ATOM   2753  O  O   . PRO B  1 32  ? -15.533 -21.375 25.331  1.00 16.76 ? 35   PRO B O   1 
ATOM   2754  C  CB  . PRO B  1 32  ? -16.269 -20.535 22.560  1.00 12.16 ? 35   PRO B CB  1 
ATOM   2755  C  CG  . PRO B  1 32  ? -17.427 -21.286 21.896  1.00 14.32 ? 35   PRO B CG  1 
ATOM   2756  C  CD  . PRO B  1 32  ? -16.783 -22.460 21.190  1.00 13.48 ? 35   PRO B CD  1 
ATOM   2757  N  N   . CYS B  1 33  ? -16.151 -23.370 24.493  1.00 13.52 ? 36   CYS B N   1 
ATOM   2758  C  CA  . CYS B  1 33  ? -16.448 -23.960 25.803  1.00 14.14 ? 36   CYS B CA  1 
ATOM   2759  C  C   . CYS B  1 33  ? -15.402 -24.970 26.211  1.00 15.61 ? 36   CYS B C   1 
ATOM   2760  O  O   . CYS B  1 33  ? -15.305 -26.047 25.606  1.00 18.45 ? 36   CYS B O   1 
ATOM   2761  C  CB  . CYS B  1 33  ? -17.819 -24.650 25.822  1.00 16.02 ? 36   CYS B CB  1 
ATOM   2762  S  SG  . CYS B  1 33  ? -18.268 -25.300 27.453  1.00 18.13 ? 36   CYS B SG  1 
ATOM   2763  N  N   . PRO B  1 34  ? -14.675 -24.674 27.299  1.00 14.99 ? 37   PRO B N   1 
ATOM   2764  C  CA  . PRO B  1 34  ? -13.682 -25.602 27.843  1.00 12.01 ? 37   PRO B CA  1 
ATOM   2765  C  C   . PRO B  1 34  ? -14.325 -26.874 28.397  1.00 15.57 ? 37   PRO B C   1 
ATOM   2766  O  O   . PRO B  1 34  ? -13.701 -27.943 28.379  1.00 19.62 ? 37   PRO B O   1 
ATOM   2767  C  CB  . PRO B  1 34  ? -13.016 -24.791 28.961  1.00 12.37 ? 37   PRO B CB  1 
ATOM   2768  C  CG  . PRO B  1 34  ? -14.030 -23.777 29.374  1.00 12.73 ? 37   PRO B CG  1 
ATOM   2769  C  CD  . PRO B  1 34  ? -14.821 -23.455 28.114  1.00 12.12 ? 37   PRO B CD  1 
ATOM   2770  N  N   . GLY B  1 35  ? -15.589 -26.777 28.800  1.00 15.83 ? 38   GLY B N   1 
ATOM   2771  C  CA  . GLY B  1 35  ? -16.345 -27.924 29.310  1.00 12.81 ? 38   GLY B CA  1 
ATOM   2772  C  C   . GLY B  1 35  ? -16.647 -28.965 28.241  1.00 11.77 ? 38   GLY B C   1 
ATOM   2773  O  O   . GLY B  1 35  ? -16.130 -30.050 28.281  1.00 10.07 ? 38   GLY B O   1 
ATOM   2774  N  N   . LEU B  1 36  ? -17.462 -28.613 27.258  1.00 13.84 ? 39   LEU B N   1 
ATOM   2775  C  CA  . LEU B  1 36  ? -17.637 -29.447 26.077  1.00 12.38 ? 39   LEU B CA  1 
ATOM   2776  C  C   . LEU B  1 36  ? -16.303 -29.834 25.405  1.00 14.55 ? 39   LEU B C   1 
ATOM   2777  O  O   . LEU B  1 36  ? -16.136 -30.964 24.960  1.00 16.16 ? 39   LEU B O   1 
ATOM   2778  C  CB  . LEU B  1 36  ? -18.573 -28.752 25.081  1.00 12.29 ? 39   LEU B CB  1 
ATOM   2779  C  CG  . LEU B  1 36  ? -19.932 -28.324 25.672  1.00 14.83 ? 39   LEU B CG  1 
ATOM   2780  C  CD1 . LEU B  1 36  ? -20.903 -27.962 24.581  1.00 8.34  ? 39   LEU B CD1 1 
ATOM   2781  C  CD2 . LEU B  1 36  ? -20.537 -29.439 26.531  1.00 13.41 ? 39   LEU B CD2 1 
ATOM   2782  N  N   . ASN B  1 37  ? -15.370 -28.901 25.266  1.00 15.90 ? 40   ASN B N   1 
ATOM   2783  C  CA  . ASN B  1 37  ? -14.087 -29.267 24.624  1.00 16.73 ? 40   ASN B CA  1 
ATOM   2784  C  C   . ASN B  1 37  ? -13.421 -30.434 25.327  1.00 17.08 ? 40   ASN B C   1 
ATOM   2785  O  O   . ASN B  1 37  ? -12.929 -31.369 24.683  1.00 18.27 ? 40   ASN B O   1 
ATOM   2786  C  CB  . ASN B  1 37  ? -13.114 -28.082 24.597  1.00 13.44 ? 40   ASN B CB  1 
ATOM   2787  C  CG  . ASN B  1 37  ? -13.528 -27.031 23.600  1.00 14.46 ? 40   ASN B CG  1 
ATOM   2788  O  OD1 . ASN B  1 37  ? -14.408 -27.281 22.761  1.00 12.50 ? 40   ASN B OD1 1 
ATOM   2789  N  ND2 . ASN B  1 37  ? -12.859 -25.865 23.633  1.00 10.66 ? 40   ASN B ND2 1 
ATOM   2790  N  N   . THR B  1 38  ? -13.367 -30.341 26.657  1.00 16.81 ? 41   THR B N   1 
ATOM   2791  C  CA  . THR B  1 38  ? -12.733 -31.351 27.475  1.00 14.67 ? 41   THR B CA  1 
ATOM   2792  C  C   . THR B  1 38  ? -13.495 -32.661 27.374  1.00 17.58 ? 41   THR B C   1 
ATOM   2793  O  O   . THR B  1 38  ? -12.891 -33.713 27.210  1.00 17.35 ? 41   THR B O   1 
ATOM   2794  C  CB  . THR B  1 38  ? -12.642 -30.935 28.968  1.00 15.45 ? 41   THR B CB  1 
ATOM   2795  O  OG1 . THR B  1 38  ? -11.801 -29.784 29.092  1.00 15.00 ? 41   THR B OG1 1 
ATOM   2796  C  CG2 . THR B  1 38  ? -12.046 -32.073 29.806  1.00 15.13 ? 41   THR B CG2 1 
ATOM   2797  N  N   . LEU B  1 39  ? -14.822 -32.594 27.432  1.00 19.12 ? 42   LEU B N   1 
ATOM   2798  C  CA  . LEU B  1 39  ? -15.632 -33.808 27.353  1.00 20.05 ? 42   LEU B CA  1 
ATOM   2799  C  C   . LEU B  1 39  ? -15.451 -34.527 26.021  1.00 18.24 ? 42   LEU B C   1 
ATOM   2800  O  O   . LEU B  1 39  ? -15.414 -35.761 25.980  1.00 19.93 ? 42   LEU B O   1 
ATOM   2801  C  CB  . LEU B  1 39  ? -17.098 -33.495 27.633  1.00 19.71 ? 42   LEU B CB  1 
ATOM   2802  C  CG  . LEU B  1 39  ? -17.306 -33.052 29.087  1.00 19.79 ? 42   LEU B CG  1 
ATOM   2803  C  CD1 . LEU B  1 39  ? -18.606 -32.307 29.233  1.00 19.77 ? 42   LEU B CD1 1 
ATOM   2804  C  CD2 . LEU B  1 39  ? -17.239 -34.219 30.052  1.00 19.17 ? 42   LEU B CD2 1 
ATOM   2805  N  N   . ALA B  1 40  ? -15.211 -33.757 24.962  1.00 15.03 ? 43   ALA B N   1 
ATOM   2806  C  CA  . ALA B  1 40  ? -15.027 -34.314 23.621  1.00 19.35 ? 43   ALA B CA  1 
ATOM   2807  C  C   . ALA B  1 40  ? -13.640 -34.953 23.483  1.00 20.82 ? 43   ALA B C   1 
ATOM   2808  O  O   . ALA B  1 40  ? -13.495 -36.008 22.898  1.00 21.13 ? 43   ALA B O   1 
ATOM   2809  C  CB  . ALA B  1 40  ? -15.215 -33.226 22.548  1.00 17.42 ? 43   ALA B CB  1 
ATOM   2810  N  N   . SER B  1 41  ? -12.632 -34.294 24.036  1.00 20.00 ? 44   SER B N   1 
ATOM   2811  C  CA  . SER B  1 41  ? -11.265 -34.773 23.966  1.00 19.58 ? 44   SER B CA  1 
ATOM   2812  C  C   . SER B  1 41  ? -11.025 -35.970 24.887  1.00 21.07 ? 44   SER B C   1 
ATOM   2813  O  O   . SER B  1 41  ? -9.986  -36.598 24.819  1.00 20.86 ? 44   SER B O   1 
ATOM   2814  C  CB  . SER B  1 41  ? -10.313 -33.636 24.340  1.00 15.63 ? 44   SER B CB  1 
ATOM   2815  O  OG  . SER B  1 41  ? -10.036 -32.839 23.204  1.00 15.65 ? 44   SER B OG  1 
ATOM   2816  N  N   . HIS B  1 42  ? -11.953 -36.227 25.801  1.00 21.57 ? 45   HIS B N   1 
ATOM   2817  C  CA  . HIS B  1 42  ? -11.904 -37.445 26.608  1.00 22.01 ? 45   HIS B CA  1 
ATOM   2818  C  C   . HIS B  1 42  ? -12.900 -38.517 26.111  1.00 22.13 ? 45   HIS B C   1 
ATOM   2819  O  O   . HIS B  1 42  ? -13.099 -39.552 26.747  1.00 24.43 ? 45   HIS B O   1 
ATOM   2820  C  CB  . HIS B  1 42  ? -12.167 -37.093 28.073  1.00 18.22 ? 45   HIS B CB  1 
ATOM   2821  C  CG  . HIS B  1 42  ? -10.951 -36.586 28.786  1.00 20.37 ? 45   HIS B CG  1 
ATOM   2822  N  ND1 . HIS B  1 42  ? -10.120 -37.413 29.519  1.00 18.87 ? 45   HIS B ND1 1 
ATOM   2823  C  CD2 . HIS B  1 42  ? -10.372 -35.361 28.802  1.00 18.73 ? 45   HIS B CD2 1 
ATOM   2824  C  CE1 . HIS B  1 42  ? -9.102  -36.709 29.980  1.00 20.15 ? 45   HIS B CE1 1 
ATOM   2825  N  NE2 . HIS B  1 42  ? -9.215  -35.468 29.535  1.00 20.29 ? 45   HIS B NE2 1 
ATOM   2826  N  N   . GLY B  1 43  ? -13.563 -38.246 24.996  1.00 21.32 ? 46   GLY B N   1 
ATOM   2827  C  CA  . GLY B  1 43  ? -14.556 -39.199 24.484  1.00 23.96 ? 46   GLY B CA  1 
ATOM   2828  C  C   . GLY B  1 43  ? -15.861 -39.309 25.269  1.00 24.45 ? 46   GLY B C   1 
ATOM   2829  O  O   . GLY B  1 43  ? -16.632 -40.219 25.030  1.00 22.89 ? 46   GLY B O   1 
ATOM   2830  N  N   . TYR B  1 44  ? -16.155 -38.373 26.173  1.00 24.39 ? 47   TYR B N   1 
ATOM   2831  C  CA  . TYR B  1 44  ? -17.513 -38.334 26.729  1.00 25.86 ? 47   TYR B CA  1 
ATOM   2832  C  C   . TYR B  1 44  ? -18.504 -37.855 25.671  1.00 25.23 ? 47   TYR B C   1 
ATOM   2833  O  O   . TYR B  1 44  ? -19.632 -38.333 25.606  1.00 22.41 ? 47   TYR B O   1 
ATOM   2834  C  CB  . TYR B  1 44  ? -17.601 -37.460 27.985  1.00 25.36 ? 47   TYR B CB  1 
ATOM   2835  C  CG  . TYR B  1 44  ? -17.025 -38.136 29.208  1.00 23.34 ? 47   TYR B CG  1 
ATOM   2836  C  CD1 . TYR B  1 44  ? -17.773 -39.057 29.929  1.00 23.71 ? 47   TYR B CD1 1 
ATOM   2837  C  CD2 . TYR B  1 44  ? -15.717 -37.890 29.613  1.00 22.38 ? 47   TYR B CD2 1 
ATOM   2838  C  CE1 . TYR B  1 44  ? -17.225 -39.744 31.008  1.00 22.56 ? 47   TYR B CE1 1 
ATOM   2839  C  CE2 . TYR B  1 44  ? -15.166 -38.540 30.727  1.00 22.30 ? 47   TYR B CE2 1 
ATOM   2840  C  CZ  . TYR B  1 44  ? -15.914 -39.485 31.396  1.00 23.40 ? 47   TYR B CZ  1 
ATOM   2841  O  OH  . TYR B  1 44  ? -15.389 -40.110 32.512  1.00 24.64 ? 47   TYR B OH  1 
ATOM   2842  N  N   . LEU B  1 45  ? -18.046 -36.942 24.818  1.00 25.57 ? 48   LEU B N   1 
ATOM   2843  C  CA  . LEU B  1 45  ? -18.763 -36.554 23.596  1.00 25.47 ? 48   LEU B CA  1 
ATOM   2844  C  C   . LEU B  1 45  ? -18.062 -37.160 22.381  1.00 23.87 ? 48   LEU B C   1 
ATOM   2845  O  O   . LEU B  1 45  ? -16.851 -37.324 22.391  1.00 29.17 ? 48   LEU B O   1 
ATOM   2846  C  CB  . LEU B  1 45  ? -18.754 -35.028 23.452  1.00 21.95 ? 48   LEU B CB  1 
ATOM   2847  C  CG  . LEU B  1 45  ? -19.781 -34.307 24.315  1.00 23.96 ? 48   LEU B CG  1 
ATOM   2848  C  CD1 . LEU B  1 45  ? -19.604 -32.780 24.218  1.00 19.23 ? 48   LEU B CD1 1 
ATOM   2849  C  CD2 . LEU B  1 45  ? -21.203 -34.744 23.907  1.00 19.27 ? 48   LEU B CD2 1 
ATOM   2850  N  N   . PRO B  1 46  ? -18.793 -37.380 21.289  1.00 22.46 ? 49   PRO B N   1 
ATOM   2851  C  CA  . PRO B  1 46  ? -18.071 -37.686 20.050  1.00 24.66 ? 49   PRO B CA  1 
ATOM   2852  C  C   . PRO B  1 46  ? -16.794 -36.855 19.927  1.00 23.41 ? 49   PRO B C   1 
ATOM   2853  O  O   . PRO B  1 46  ? -16.843 -35.632 20.035  1.00 22.53 ? 49   PRO B O   1 
ATOM   2854  C  CB  . PRO B  1 46  ? -19.076 -37.288 18.956  1.00 21.57 ? 49   PRO B CB  1 
ATOM   2855  C  CG  . PRO B  1 46  ? -20.402 -37.575 19.591  1.00 21.39 ? 49   PRO B CG  1 
ATOM   2856  C  CD  . PRO B  1 46  ? -20.252 -37.326 21.087  1.00 21.46 ? 49   PRO B CD  1 
ATOM   2857  N  N   . ARG B  1 47  ? -15.682 -37.502 19.595  1.00 21.70 ? 50   ARG B N   1 
ATOM   2858  C  CA  . ARG B  1 47  ? -14.404 -36.811 19.612  1.00 24.08 ? 50   ARG B CA  1 
ATOM   2859  C  C   . ARG B  1 47  ? -14.277 -35.774 18.512  1.00 23.22 ? 50   ARG B C   1 
ATOM   2860  O  O   . ARG B  1 47  ? -13.352 -34.960 18.524  1.00 21.11 ? 50   ARG B O   1 
ATOM   2861  C  CB  . ARG B  1 47  ? -13.239 -37.798 19.561  1.00 25.95 ? 50   ARG B CB  1 
ATOM   2862  C  CG  . ARG B  1 47  ? -13.141 -38.651 20.813  1.00 25.76 ? 50   ARG B CG  1 
ATOM   2863  C  CD  . ARG B  1 47  ? -11.921 -39.544 20.814  1.00 25.31 ? 50   ARG B CD  1 
ATOM   2864  N  NE  . ARG B  1 47  ? -11.856 -40.300 22.060  1.00 24.58 ? 50   ARG B NE  1 
ATOM   2865  C  CZ  . ARG B  1 47  ? -11.203 -39.910 23.154  1.00 25.83 ? 50   ARG B CZ  1 
ATOM   2866  N  NH1 . ARG B  1 47  ? -10.544 -38.746 23.173  1.00 25.83 ? 50   ARG B NH1 1 
ATOM   2867  N  NH2 . ARG B  1 47  ? -11.226 -40.681 24.241  1.00 23.16 ? 50   ARG B NH2 1 
ATOM   2868  N  N   . ASN B  1 48  ? -15.182 -35.816 17.540  1.00 21.34 ? 51   ASN B N   1 
ATOM   2869  C  CA  . ASN B  1 48  ? -15.104 -34.847 16.466  1.00 22.29 ? 51   ASN B CA  1 
ATOM   2870  C  C   . ASN B  1 48  ? -15.905 -33.597 16.770  1.00 17.79 ? 51   ASN B C   1 
ATOM   2871  O  O   . ASN B  1 48  ? -15.869 -32.640 16.017  1.00 17.63 ? 51   ASN B O   1 
ATOM   2872  C  CB  . ASN B  1 48  ? -15.471 -35.461 15.117  1.00 26.37 ? 51   ASN B CB  1 
ATOM   2873  C  CG  . ASN B  1 48  ? -16.970 -35.675 14.952  1.00 27.86 ? 51   ASN B CG  1 
ATOM   2874  O  OD1 . ASN B  1 48  ? -17.505 -35.551 13.846  1.00 31.37 ? 51   ASN B OD1 1 
ATOM   2875  N  ND2 . ASN B  1 48  ? -17.647 -36.008 16.039  1.00 25.58 ? 51   ASN B ND2 1 
ATOM   2876  N  N   . GLY B  1 49  ? -16.570 -33.608 17.922  1.00 17.27 ? 52   GLY B N   1 
ATOM   2877  C  CA  . GLY B  1 49  ? -17.273 -32.450 18.452  1.00 15.72 ? 52   GLY B CA  1 
ATOM   2878  C  C   . GLY B  1 49  ? -18.597 -32.137 17.776  1.00 16.32 ? 52   GLY B C   1 
ATOM   2879  O  O   . GLY B  1 49  ? -19.114 -31.026 17.887  1.00 16.16 ? 52   GLY B O   1 
ATOM   2880  N  N   . VAL B  1 50  ? -19.177 -33.118 17.099  1.00 17.21 ? 53   VAL B N   1 
ATOM   2881  C  CA  . VAL B  1 50  ? -20.529 -32.958 16.578  1.00 16.49 ? 53   VAL B CA  1 
ATOM   2882  C  C   . VAL B  1 50  ? -21.439 -33.918 17.339  1.00 16.66 ? 53   VAL B C   1 
ATOM   2883  O  O   . VAL B  1 50  ? -21.180 -35.117 17.377  1.00 21.20 ? 53   VAL B O   1 
ATOM   2884  C  CB  . VAL B  1 50  ? -20.566 -33.263 15.059  1.00 19.79 ? 53   VAL B CB  1 
ATOM   2885  C  CG1 . VAL B  1 50  ? -21.993 -33.178 14.506  1.00 22.36 ? 53   VAL B CG1 1 
ATOM   2886  C  CG2 . VAL B  1 50  ? -19.645 -32.326 14.302  1.00 17.04 ? 53   VAL B CG2 1 
ATOM   2887  N  N   . ALA B  1 51  ? -22.429 -33.383 18.048  1.00 15.70 ? 54   ALA B N   1 
ATOM   2888  C  CA  . ALA B  1 51  ? -23.157 -34.151 19.066  1.00 13.68 ? 54   ALA B CA  1 
ATOM   2889  C  C   . ALA B  1 51  ? -24.634 -33.812 19.055  1.00 16.06 ? 54   ALA B C   1 
ATOM   2890  O  O   . ALA B  1 51  ? -25.020 -32.738 18.595  1.00 15.90 ? 54   ALA B O   1 
ATOM   2891  C  CB  . ALA B  1 51  ? -22.575 -33.889 20.470  1.00 12.71 ? 54   ALA B CB  1 
ATOM   2892  N  N   . THR B  1 52  ? -25.453 -34.740 19.559  1.00 17.90 ? 55   THR B N   1 
ATOM   2893  C  CA  . THR B  1 52  ? -26.882 -34.505 19.752  1.00 18.31 ? 55   THR B CA  1 
ATOM   2894  C  C   . THR B  1 52  ? -27.089 -33.894 21.130  1.00 18.20 ? 55   THR B C   1 
ATOM   2895  O  O   . THR B  1 52  ? -26.238 -34.039 22.008  1.00 16.84 ? 55   THR B O   1 
ATOM   2896  C  CB  . THR B  1 52  ? -27.681 -35.836 19.722  1.00 18.44 ? 55   THR B CB  1 
ATOM   2897  O  OG1 . THR B  1 52  ? -27.419 -36.557 20.922  1.00 14.95 ? 55   THR B OG1 1 
ATOM   2898  C  CG2 . THR B  1 52  ? -27.285 -36.702 18.521  1.00 17.08 ? 55   THR B CG2 1 
ATOM   2899  N  N   . PRO B  1 53  ? -28.246 -33.243 21.346  1.00 19.38 ? 56   PRO B N   1 
ATOM   2900  C  CA  . PRO B  1 53  ? -28.494 -32.677 22.659  1.00 16.24 ? 56   PRO B CA  1 
ATOM   2901  C  C   . PRO B  1 53  ? -28.455 -33.715 23.767  1.00 19.93 ? 56   PRO B C   1 
ATOM   2902  O  O   . PRO B  1 53  ? -27.977 -33.417 24.872  1.00 21.35 ? 56   PRO B O   1 
ATOM   2903  C  CB  . PRO B  1 53  ? -29.883 -32.102 22.510  1.00 17.44 ? 56   PRO B CB  1 
ATOM   2904  C  CG  . PRO B  1 53  ? -29.888 -31.600 21.109  1.00 19.14 ? 56   PRO B CG  1 
ATOM   2905  C  CD  . PRO B  1 53  ? -29.139 -32.655 20.330  1.00 17.52 ? 56   PRO B CD  1 
ATOM   2906  N  N   . VAL B  1 54  ? -28.902 -34.936 23.469  1.00 19.35 ? 57   VAL B N   1 
ATOM   2907  C  CA  . VAL B  1 54  ? -28.915 -35.996 24.475  1.00 20.32 ? 57   VAL B CA  1 
ATOM   2908  C  C   . VAL B  1 54  ? -27.501 -36.463 24.811  1.00 21.10 ? 57   VAL B C   1 
ATOM   2909  O  O   . VAL B  1 54  ? -27.184 -36.697 25.980  1.00 22.11 ? 57   VAL B O   1 
ATOM   2910  C  CB  . VAL B  1 54  ? -29.803 -37.213 24.058  1.00 21.69 ? 57   VAL B CB  1 
ATOM   2911  C  CG1 . VAL B  1 54  ? -29.306 -38.491 24.725  1.00 18.47 ? 57   VAL B CG1 1 
ATOM   2912  C  CG2 . VAL B  1 54  ? -31.278 -36.957 24.420  1.00 20.00 ? 57   VAL B CG2 1 
ATOM   2913  N  N   . GLN B  1 55  ? -26.645 -36.598 23.801  1.00 19.72 ? 58   GLN B N   1 
ATOM   2914  C  CA  . GLN B  1 55  ? -25.227 -36.898 24.075  1.00 21.96 ? 58   GLN B CA  1 
ATOM   2915  C  C   . GLN B  1 55  ? -24.578 -35.809 24.961  1.00 21.64 ? 58   GLN B C   1 
ATOM   2916  O  O   . GLN B  1 55  ? -23.745 -36.106 25.830  1.00 22.47 ? 58   GLN B O   1 
ATOM   2917  C  CB  . GLN B  1 55  ? -24.434 -37.068 22.771  1.00 19.91 ? 58   GLN B CB  1 
ATOM   2918  C  CG  . GLN B  1 55  ? -24.812 -38.315 21.928  1.00 21.25 ? 58   GLN B CG  1 
ATOM   2919  C  CD  . GLN B  1 55  ? -24.222 -38.252 20.507  1.00 24.62 ? 58   GLN B CD  1 
ATOM   2920  O  OE1 . GLN B  1 55  ? -24.055 -37.176 19.938  1.00 24.17 ? 58   GLN B OE1 1 
ATOM   2921  N  NE2 . GLN B  1 55  ? -23.838 -39.398 19.971  1.00 27.00 ? 58   GLN B NE2 1 
ATOM   2922  N  N   . ILE B  1 56  ? -24.960 -34.555 24.732  1.00 18.50 ? 59   ILE B N   1 
ATOM   2923  C  CA  . ILE B  1 56  ? -24.345 -33.428 25.437  1.00 19.36 ? 59   ILE B CA  1 
ATOM   2924  C  C   . ILE B  1 56  ? -24.755 -33.425 26.917  1.00 20.86 ? 59   ILE B C   1 
ATOM   2925  O  O   . ILE B  1 56  ? -23.903 -33.394 27.795  1.00 21.98 ? 59   ILE B O   1 
ATOM   2926  C  CB  . ILE B  1 56  ? -24.696 -32.094 24.747  1.00 18.62 ? 59   ILE B CB  1 
ATOM   2927  C  CG1 . ILE B  1 56  ? -24.019 -32.028 23.370  1.00 18.50 ? 59   ILE B CG1 1 
ATOM   2928  C  CG2 . ILE B  1 56  ? -24.273 -30.897 25.597  1.00 17.97 ? 59   ILE B CG2 1 
ATOM   2929  C  CD1 . ILE B  1 56  ? -24.250 -30.729 22.635  1.00 16.53 ? 59   ILE B CD1 1 
ATOM   2930  N  N   . ILE B  1 57  ? -26.045 -33.617 27.189  1.00 21.86 ? 60   ILE B N   1 
ATOM   2931  C  CA  . ILE B  1 57  ? -26.537 -33.657 28.571  1.00 22.02 ? 60   ILE B CA  1 
ATOM   2932  C  C   . ILE B  1 57  ? -25.941 -34.839 29.336  1.00 22.03 ? 60   ILE B C   1 
ATOM   2933  O  O   . ILE B  1 57  ? -25.425 -34.678 30.450  1.00 19.89 ? 60   ILE B O   1 
ATOM   2934  C  CB  . ILE B  1 57  ? -28.094 -33.684 28.626  1.00 21.87 ? 60   ILE B CB  1 
ATOM   2935  C  CG1 . ILE B  1 57  ? -28.661 -32.339 28.189  1.00 20.08 ? 60   ILE B CG1 1 
ATOM   2936  C  CG2 . ILE B  1 57  ? -28.606 -34.000 30.011  1.00 21.19 ? 60   ILE B CG2 1 
ATOM   2937  C  CD1 . ILE B  1 57  ? -29.978 -32.458 27.441  1.00 11.99 ? 60   ILE B CD1 1 
ATOM   2938  N  N   . ASN B  1 58  ? -25.932 -36.018 28.725  1.00 22.03 ? 61   ASN B N   1 
ATOM   2939  C  CA  . ASN B  1 58  ? -25.293 -37.148 29.386  1.00 22.48 ? 61   ASN B CA  1 
ATOM   2940  C  C   . ASN B  1 58  ? -23.809 -36.895 29.692  1.00 22.45 ? 61   ASN B C   1 
ATOM   2941  O  O   . ASN B  1 58  ? -23.339 -37.213 30.786  1.00 19.83 ? 61   ASN B O   1 
ATOM   2942  C  CB  . ASN B  1 58  ? -25.470 -38.426 28.584  1.00 25.03 ? 61   ASN B CB  1 
ATOM   2943  C  CG  . ASN B  1 58  ? -26.864 -39.022 28.734  1.00 27.36 ? 61   ASN B CG  1 
ATOM   2944  O  OD1 . ASN B  1 58  ? -27.458 -39.000 29.817  1.00 24.32 ? 61   ASN B OD1 1 
ATOM   2945  N  ND2 . ASN B  1 58  ? -27.364 -39.616 27.654  1.00 27.61 ? 61   ASN B ND2 1 
ATOM   2946  N  N   . ALA B  1 59  ? -23.101 -36.272 28.746  1.00 18.80 ? 62   ALA B N   1 
ATOM   2947  C  CA  . ALA B  1 59  ? -21.663 -36.034 28.890  1.00 18.93 ? 62   ALA B CA  1 
ATOM   2948  C  C   . ALA B  1 59  ? -21.368 -35.115 30.054  1.00 17.93 ? 62   ALA B C   1 
ATOM   2949  O  O   . ALA B  1 59  ? -20.498 -35.415 30.879  1.00 14.99 ? 62   ALA B O   1 
ATOM   2950  C  CB  . ALA B  1 59  ? -21.056 -35.452 27.607  1.00 14.63 ? 62   ALA B CB  1 
ATOM   2951  N  N   . VAL B  1 60  ? -22.085 -33.993 30.121  1.00 16.94 ? 63   VAL B N   1 
ATOM   2952  C  CA  . VAL B  1 60  ? -21.761 -32.999 31.130  1.00 17.32 ? 63   VAL B CA  1 
ATOM   2953  C  C   . VAL B  1 60  ? -22.149 -33.514 32.519  1.00 19.88 ? 63   VAL B C   1 
ATOM   2954  O  O   . VAL B  1 60  ? -21.581 -33.075 33.528  1.00 18.51 ? 63   VAL B O   1 
ATOM   2955  C  CB  . VAL B  1 60  ? -22.431 -31.628 30.871  1.00 16.24 ? 63   VAL B CB  1 
ATOM   2956  C  CG1 . VAL B  1 60  ? -21.856 -30.965 29.616  1.00 11.81 ? 63   VAL B CG1 1 
ATOM   2957  C  CG2 . VAL B  1 60  ? -23.936 -31.775 30.803  1.00 13.69 ? 63   VAL B CG2 1 
ATOM   2958  N  N   . GLN B  1 61  ? -23.121 -34.430 32.563  1.00 19.71 ? 64   GLN B N   1 
ATOM   2959  C  CA  . GLN B  1 61  ? -23.563 -35.024 33.827  1.00 19.21 ? 64   GLN B CA  1 
ATOM   2960  C  C   . GLN B  1 61  ? -22.546 -36.066 34.228  1.00 20.74 ? 64   GLN B C   1 
ATOM   2961  O  O   . GLN B  1 61  ? -21.955 -35.964 35.304  1.00 18.96 ? 64   GLN B O   1 
ATOM   2962  C  CB  . GLN B  1 61  ? -24.968 -35.640 33.719  1.00 19.58 ? 64   GLN B CB  1 
ATOM   2963  C  CG  . GLN B  1 61  ? -26.076 -34.614 33.414  1.00 20.27 ? 64   GLN B CG  1 
ATOM   2964  C  CD  . GLN B  1 61  ? -27.477 -35.149 33.671  1.00 22.40 ? 64   GLN B CD  1 
ATOM   2965  O  OE1 . GLN B  1 61  ? -28.335 -34.440 34.186  1.00 24.30 ? 64   GLN B OE1 1 
ATOM   2966  N  NE2 . GLN B  1 61  ? -27.701 -36.415 33.345  1.00 20.68 ? 64   GLN B NE2 1 
ATOM   2967  N  N   . GLU B  1 62  ? -22.209 -36.960 33.292  1.00 22.74 ? 65   GLU B N   1 
ATOM   2968  C  CA  . GLU B  1 62  ? -21.297 -38.055 33.599  1.00 23.45 ? 65   GLU B CA  1 
ATOM   2969  C  C   . GLU B  1 62  ? -19.897 -37.532 33.887  1.00 21.05 ? 65   GLU B C   1 
ATOM   2970  O  O   . GLU B  1 62  ? -19.249 -37.964 34.824  1.00 27.71 ? 65   GLU B O   1 
ATOM   2971  C  CB  . GLU B  1 62  ? -21.233 -39.070 32.459  1.00 26.92 ? 65   GLU B CB  1 
ATOM   2972  C  CG  . GLU B  1 62  ? -22.543 -39.765 32.156  1.00 34.50 ? 65   GLU B CG  1 
ATOM   2973  C  CD  . GLU B  1 62  ? -23.031 -40.663 33.297  1.00 38.86 ? 65   GLU B CD  1 
ATOM   2974  O  OE1 . GLU B  1 62  ? -22.218 -41.000 34.210  1.00 36.38 ? 65   GLU B OE1 1 
ATOM   2975  O  OE2 . GLU B  1 62  ? -24.240 -41.020 33.268  1.00 38.74 ? 65   GLU B OE2 1 
ATOM   2976  N  N   . GLY B  1 63  ? -19.405 -36.660 33.029  1.00 21.10 ? 66   GLY B N   1 
ATOM   2977  C  CA  . GLY B  1 63  ? -18.004 -36.255 33.078  1.00 23.09 ? 66   GLY B CA  1 
ATOM   2978  C  C   . GLY B  1 63  ? -17.703 -35.259 34.180  1.00 20.95 ? 66   GLY B C   1 
ATOM   2979  O  O   . GLY B  1 63  ? -16.668 -35.352 34.843  1.00 20.32 ? 66   GLY B O   1 
ATOM   2980  N  N   . LEU B  1 64  ? -18.649 -34.357 34.443  1.00 20.32 ? 67   LEU B N   1 
ATOM   2981  C  CA  . LEU B  1 64  ? -18.340 -33.176 35.238  1.00 19.66 ? 67   LEU B CA  1 
ATOM   2982  C  C   . LEU B  1 64  ? -19.350 -32.870 36.353  1.00 20.06 ? 67   LEU B C   1 
ATOM   2983  O  O   . LEU B  1 64  ? -19.149 -31.942 37.142  1.00 18.70 ? 67   LEU B O   1 
ATOM   2984  C  CB  . LEU B  1 64  ? -18.129 -31.975 34.307  1.00 18.34 ? 67   LEU B CB  1 
ATOM   2985  C  CG  . LEU B  1 64  ? -16.862 -32.095 33.446  1.00 19.21 ? 67   LEU B CG  1 
ATOM   2986  C  CD1 . LEU B  1 64  ? -16.763 -30.994 32.359  1.00 19.10 ? 67   LEU B CD1 1 
ATOM   2987  C  CD2 . LEU B  1 64  ? -15.643 -32.060 34.353  1.00 19.41 ? 67   LEU B CD2 1 
ATOM   2988  N  N   . ASN B  1 65  ? -20.387 -33.703 36.460  1.00 21.55 ? 68   ASN B N   1 
ATOM   2989  C  CA  . ASN B  1 65  ? -21.508 -33.474 37.385  1.00 19.27 ? 68   ASN B CA  1 
ATOM   2990  C  C   . ASN B  1 65  ? -22.164 -32.097 37.252  1.00 21.29 ? 68   ASN B C   1 
ATOM   2991  O  O   . ASN B  1 65  ? -22.554 -31.488 38.257  1.00 20.21 ? 68   ASN B O   1 
ATOM   2992  C  CB  . ASN B  1 65  ? -21.080 -33.709 38.836  1.00 19.36 ? 68   ASN B CB  1 
ATOM   2993  C  CG  . ASN B  1 65  ? -21.966 -34.734 39.557  1.00 18.62 ? 68   ASN B CG  1 
ATOM   2994  O  OD1 . ASN B  1 65  ? -23.148 -34.895 39.242  1.00 18.93 ? 68   ASN B OD1 1 
ATOM   2995  N  ND2 . ASN B  1 65  ? -21.388 -35.421 40.534  1.00 16.60 ? 68   ASN B ND2 1 
ATOM   2996  N  N   . PHE B  1 66  ? -22.339 -31.636 36.019  1.00 15.68 ? 69   PHE B N   1 
ATOM   2997  C  CA  . PHE B  1 66  ? -23.239 -30.506 35.755  1.00 15.61 ? 69   PHE B CA  1 
ATOM   2998  C  C   . PHE B  1 66  ? -24.625 -30.882 36.224  1.00 19.21 ? 69   PHE B C   1 
ATOM   2999  O  O   . PHE B  1 66  ? -25.031 -32.037 36.072  1.00 20.68 ? 69   PHE B O   1 
ATOM   3000  C  CB  . PHE B  1 66  ? -23.297 -30.202 34.260  1.00 14.81 ? 69   PHE B CB  1 
ATOM   3001  C  CG  . PHE B  1 66  ? -23.423 -28.744 33.937  1.00 14.54 ? 69   PHE B CG  1 
ATOM   3002  C  CD1 . PHE B  1 66  ? -22.580 -27.825 34.506  1.00 14.58 ? 69   PHE B CD1 1 
ATOM   3003  C  CD2 . PHE B  1 66  ? -24.396 -28.297 33.057  1.00 12.19 ? 69   PHE B CD2 1 
ATOM   3004  C  CE1 . PHE B  1 66  ? -22.673 -26.483 34.190  1.00 14.01 ? 69   PHE B CE1 1 
ATOM   3005  C  CE2 . PHE B  1 66  ? -24.456 -26.972 32.696  1.00 15.38 ? 69   PHE B CE2 1 
ATOM   3006  C  CZ  . PHE B  1 66  ? -23.597 -26.063 33.264  1.00 15.50 ? 69   PHE B CZ  1 
ATOM   3007  N  N   . ASP B  1 67  ? -25.359 -29.938 36.814  1.00 16.87 ? 70   ASP B N   1 
ATOM   3008  C  CA  . ASP B  1 67  ? -26.717 -30.271 37.207  1.00 20.48 ? 70   ASP B CA  1 
ATOM   3009  C  C   . ASP B  1 67  ? -27.683 -30.353 36.017  1.00 19.53 ? 70   ASP B C   1 
ATOM   3010  O  O   . ASP B  1 67  ? -27.457 -29.739 34.991  1.00 18.07 ? 70   ASP B O   1 
ATOM   3011  C  CB  . ASP B  1 67  ? -27.242 -29.395 38.343  1.00 20.38 ? 70   ASP B CB  1 
ATOM   3012  C  CG  . ASP B  1 67  ? -27.516 -27.991 37.912  1.00 26.69 ? 70   ASP B CG  1 
ATOM   3013  O  OD1 . ASP B  1 67  ? -26.572 -27.164 37.947  1.00 31.01 ? 70   ASP B OD1 1 
ATOM   3014  O  OD2 . ASP B  1 67  ? -28.676 -27.710 37.531  1.00 29.06 ? 70   ASP B OD2 1 
ATOM   3015  N  N   . ASN B  1 68  ? -28.731 -31.159 36.169  1.00 19.48 ? 71   ASN B N   1 
ATOM   3016  C  CA  . ASN B  1 68  ? -29.626 -31.519 35.084  1.00 20.92 ? 71   ASN B CA  1 
ATOM   3017  C  C   . ASN B  1 68  ? -30.351 -30.330 34.452  1.00 21.15 ? 71   ASN B C   1 
ATOM   3018  O  O   . ASN B  1 68  ? -30.416 -30.205 33.232  1.00 22.05 ? 71   ASN B O   1 
ATOM   3019  C  CB  . ASN B  1 68  ? -30.658 -32.550 35.575  1.00 19.70 ? 71   ASN B CB  1 
ATOM   3020  C  CG  . ASN B  1 68  ? -31.526 -33.075 34.453  1.00 20.59 ? 71   ASN B CG  1 
ATOM   3021  O  OD1 . ASN B  1 68  ? -32.658 -32.631 34.272  1.00 17.62 ? 71   ASN B OD1 1 
ATOM   3022  N  ND2 . ASN B  1 68  ? -30.982 -33.989 33.663  1.00 18.55 ? 71   ASN B ND2 1 
ATOM   3023  N  N   . GLN B  1 69  ? -30.943 -29.483 35.283  1.00 22.85 ? 72   GLN B N   1 
ATOM   3024  C  CA  . GLN B  1 69  ? -31.621 -28.302 34.779  1.00 22.83 ? 72   GLN B CA  1 
ATOM   3025  C  C   . GLN B  1 69  ? -30.698 -27.331 34.075  1.00 17.85 ? 72   GLN B C   1 
ATOM   3026  O  O   . GLN B  1 69  ? -31.072 -26.716 33.093  1.00 17.98 ? 72   GLN B O   1 
ATOM   3027  C  CB  . GLN B  1 69  ? -32.391 -27.590 35.892  1.00 26.24 ? 72   GLN B CB  1 
ATOM   3028  C  CG  . GLN B  1 69  ? -33.842 -28.013 35.964  1.00 33.77 ? 72   GLN B CG  1 
ATOM   3029  C  CD  . GLN B  1 69  ? -34.691 -27.096 36.832  1.00 37.10 ? 72   GLN B CD  1 
ATOM   3030  O  OE1 . GLN B  1 69  ? -34.384 -26.885 38.003  1.00 38.76 ? 72   GLN B OE1 1 
ATOM   3031  N  NE2 . GLN B  1 69  ? -35.796 -26.588 36.271  1.00 38.99 ? 72   GLN B NE2 1 
ATOM   3032  N  N   . ALA B  1 70  ? -29.517 -27.113 34.614  1.00 17.26 ? 73   ALA B N   1 
ATOM   3033  C  CA  . ALA B  1 70  ? -28.615 -26.207 33.942  1.00 15.42 ? 73   ALA B CA  1 
ATOM   3034  C  C   . ALA B  1 70  ? -28.196 -26.812 32.602  1.00 17.30 ? 73   ALA B C   1 
ATOM   3035  O  O   . ALA B  1 70  ? -28.031 -26.092 31.613  1.00 15.74 ? 73   ALA B O   1 
ATOM   3036  C  CB  . ALA B  1 70  ? -27.390 -25.893 34.822  1.00 18.43 ? 73   ALA B CB  1 
ATOM   3037  N  N   . ALA B  1 71  ? -28.105 -28.140 32.564  1.00 14.50 ? 74   ALA B N   1 
ATOM   3038  C  CA  . ALA B  1 71  ? -27.655 -28.854 31.377  1.00 17.40 ? 74   ALA B CA  1 
ATOM   3039  C  C   . ALA B  1 71  ? -28.687 -28.812 30.252  1.00 16.98 ? 74   ALA B C   1 
ATOM   3040  O  O   . ALA B  1 71  ? -28.348 -28.577 29.078  1.00 14.41 ? 74   ALA B O   1 
ATOM   3041  C  CB  . ALA B  1 71  ? -27.291 -30.301 31.729  1.00 12.20 ? 74   ALA B CB  1 
ATOM   3042  N  N   . VAL B  1 72  ? -29.947 -28.926 30.646  1.00 15.04 ? 75   VAL B N   1 
ATOM   3043  C  CA  . VAL B  1 72  ? -31.054 -28.893 29.721  1.00 16.30 ? 75   VAL B CA  1 
ATOM   3044  C  C   . VAL B  1 72  ? -31.180 -27.462 29.226  1.00 17.07 ? 75   VAL B C   1 
ATOM   3045  O  O   . VAL B  1 72  ? -31.302 -27.216 28.030  1.00 17.11 ? 75   VAL B O   1 
ATOM   3046  C  CB  . VAL B  1 72  ? -32.385 -29.329 30.420  1.00 17.06 ? 75   VAL B CB  1 
ATOM   3047  C  CG1 . VAL B  1 72  ? -33.538 -29.138 29.503  1.00 17.21 ? 75   VAL B CG1 1 
ATOM   3048  C  CG2 . VAL B  1 72  ? -32.323 -30.790 30.857  1.00 15.91 ? 75   VAL B CG2 1 
ATOM   3049  N  N   . PHE B  1 73  ? -31.115 -26.509 30.148  1.00 18.06 ? 76   PHE B N   1 
ATOM   3050  C  CA  . PHE B  1 73  ? -31.218 -25.096 29.780  1.00 15.91 ? 76   PHE B CA  1 
ATOM   3051  C  C   . PHE B  1 73  ? -30.166 -24.739 28.719  1.00 16.22 ? 76   PHE B C   1 
ATOM   3052  O  O   . PHE B  1 73  ? -30.493 -24.223 27.638  1.00 13.10 ? 76   PHE B O   1 
ATOM   3053  C  CB  . PHE B  1 73  ? -31.031 -24.217 31.010  1.00 18.48 ? 76   PHE B CB  1 
ATOM   3054  C  CG  . PHE B  1 73  ? -31.136 -22.746 30.725  1.00 20.54 ? 76   PHE B CG  1 
ATOM   3055  C  CD1 . PHE B  1 73  ? -32.369 -22.118 30.713  1.00 22.46 ? 76   PHE B CD1 1 
ATOM   3056  C  CD2 . PHE B  1 73  ? -30.007 -21.989 30.484  1.00 21.41 ? 76   PHE B CD2 1 
ATOM   3057  C  CE1 . PHE B  1 73  ? -32.474 -20.754 30.475  1.00 18.72 ? 76   PHE B CE1 1 
ATOM   3058  C  CE2 . PHE B  1 73  ? -30.111 -20.640 30.229  1.00 21.05 ? 76   PHE B CE2 1 
ATOM   3059  C  CZ  . PHE B  1 73  ? -31.345 -20.025 30.245  1.00 20.31 ? 76   PHE B CZ  1 
ATOM   3060  N  N   . ALA B  1 74  ? -28.900 -25.055 29.007  1.00 15.24 ? 77   ALA B N   1 
ATOM   3061  C  CA  . ALA B  1 74  ? -27.818 -24.597 28.144  1.00 16.51 ? 77   ALA B CA  1 
ATOM   3062  C  C   . ALA B  1 74  ? -27.815 -25.346 26.808  1.00 12.65 ? 77   ALA B C   1 
ATOM   3063  O  O   . ALA B  1 74  ? -27.465 -24.781 25.773  1.00 17.60 ? 77   ALA B O   1 
ATOM   3064  C  CB  . ALA B  1 74  ? -26.446 -24.719 28.847  1.00 12.20 ? 77   ALA B CB  1 
ATOM   3065  N  N   . THR B  1 75  ? -28.100 -26.639 26.854  1.00 15.90 ? 78   THR B N   1 
ATOM   3066  C  CA  . THR B  1 75  ? -27.965 -27.475 25.671  1.00 14.77 ? 78   THR B CA  1 
ATOM   3067  C  C   . THR B  1 75  ? -29.034 -27.160 24.642  1.00 17.77 ? 78   THR B C   1 
ATOM   3068  O  O   . THR B  1 75  ? -28.731 -27.050 23.450  1.00 18.50 ? 78   THR B O   1 
ATOM   3069  C  CB  . THR B  1 75  ? -28.008 -28.938 26.024  1.00 16.26 ? 78   THR B CB  1 
ATOM   3070  O  OG1 . THR B  1 75  ? -26.930 -29.207 26.926  1.00 17.11 ? 78   THR B OG1 1 
ATOM   3071  C  CG2 . THR B  1 75  ? -27.837 -29.798 24.763  1.00 15.55 ? 78   THR B CG2 1 
ATOM   3072  N  N   . TYR B  1 76  ? -30.265 -26.940 25.106  1.00 14.39 ? 79   TYR B N   1 
ATOM   3073  C  CA  . TYR B  1 76  ? -31.347 -26.626 24.188  1.00 15.13 ? 79   TYR B CA  1 
ATOM   3074  C  C   . TYR B  1 76  ? -31.280 -25.202 23.693  1.00 16.49 ? 79   TYR B C   1 
ATOM   3075  O  O   . TYR B  1 76  ? -31.490 -24.955 22.500  1.00 17.66 ? 79   TYR B O   1 
ATOM   3076  C  CB  . TYR B  1 76  ? -32.723 -27.020 24.752  1.00 12.90 ? 79   TYR B CB  1 
ATOM   3077  C  CG  . TYR B  1 76  ? -32.861 -28.529 24.795  1.00 14.82 ? 79   TYR B CG  1 
ATOM   3078  C  CD1 . TYR B  1 76  ? -32.942 -29.268 23.610  1.00 17.57 ? 79   TYR B CD1 1 
ATOM   3079  C  CD2 . TYR B  1 76  ? -32.691 -29.228 25.981  1.00 12.49 ? 79   TYR B CD2 1 
ATOM   3080  C  CE1 . TYR B  1 76  ? -32.947 -30.679 23.626  1.00 19.72 ? 79   TYR B CE1 1 
ATOM   3081  C  CE2 . TYR B  1 76  ? -32.721 -30.623 26.009  1.00 15.08 ? 79   TYR B CE2 1 
ATOM   3082  C  CZ  . TYR B  1 76  ? -32.838 -31.345 24.823  1.00 17.78 ? 79   TYR B CZ  1 
ATOM   3083  O  OH  . TYR B  1 76  ? -32.899 -32.741 24.859  1.00 20.31 ? 79   TYR B OH  1 
ATOM   3084  N  N   . ALA B  1 77  ? -30.844 -24.286 24.556  1.00 16.45 ? 80   ALA B N   1 
ATOM   3085  C  CA  . ALA B  1 77  ? -30.588 -22.910 24.123  1.00 15.89 ? 80   ALA B CA  1 
ATOM   3086  C  C   . ALA B  1 77  ? -29.619 -22.897 22.946  1.00 15.04 ? 80   ALA B C   1 
ATOM   3087  O  O   . ALA B  1 77  ? -29.904 -22.313 21.920  1.00 15.03 ? 80   ALA B O   1 
ATOM   3088  C  CB  . ALA B  1 77  ? -30.039 -22.050 25.285  1.00 16.53 ? 80   ALA B CB  1 
ATOM   3089  N  N   . ALA B  1 78  ? -28.522 -23.639 23.053  1.00 16.03 ? 81   ALA B N   1 
ATOM   3090  C  CA  . ALA B  1 78  ? -27.506 -23.613 22.002  1.00 13.60 ? 81   ALA B CA  1 
ATOM   3091  C  C   . ALA B  1 78  ? -27.997 -24.303 20.751  1.00 15.68 ? 81   ALA B C   1 
ATOM   3092  O  O   . ALA B  1 78  ? -27.674 -23.889 19.624  1.00 17.39 ? 81   ALA B O   1 
ATOM   3093  C  CB  . ALA B  1 78  ? -26.206 -24.243 22.481  1.00 10.11 ? 81   ALA B CB  1 
ATOM   3094  N  N   . HIS B  1 79  ? -28.692 -25.419 20.945  1.00 16.43 ? 82   HIS B N   1 
ATOM   3095  C  CA  . HIS B  1 79  ? -29.175 -26.203 19.832  1.00 18.67 ? 82   HIS B CA  1 
ATOM   3096  C  C   . HIS B  1 79  ? -30.201 -25.369 19.067  1.00 19.46 ? 82   HIS B C   1 
ATOM   3097  O  O   . HIS B  1 79  ? -30.087 -25.192 17.854  1.00 20.69 ? 82   HIS B O   1 
ATOM   3098  C  CB  . HIS B  1 79  ? -29.780 -27.507 20.337  1.00 19.81 ? 82   HIS B CB  1 
ATOM   3099  C  CG  . HIS B  1 79  ? -30.118 -28.475 19.252  1.00 22.38 ? 82   HIS B CG  1 
ATOM   3100  N  ND1 . HIS B  1 79  ? -29.251 -28.764 18.220  1.00 21.96 ? 82   HIS B ND1 1 
ATOM   3101  C  CD2 . HIS B  1 79  ? -31.196 -29.276 19.072  1.00 20.57 ? 82   HIS B CD2 1 
ATOM   3102  C  CE1 . HIS B  1 79  ? -29.822 -29.626 17.399  1.00 18.25 ? 82   HIS B CE1 1 
ATOM   3103  N  NE2 . HIS B  1 79  ? -30.987 -29.981 17.912  1.00 18.94 ? 82   HIS B NE2 1 
ATOM   3104  N  N   . LEU B  1 80  ? -31.098 -24.731 19.813  1.00 16.03 ? 83   LEU B N   1 
ATOM   3105  C  CA  . LEU B  1 80  ? -32.058 -23.779 19.245  1.00 17.92 ? 83   LEU B CA  1 
ATOM   3106  C  C   . LEU B  1 80  ? -31.417 -22.751 18.322  1.00 18.74 ? 83   LEU B C   1 
ATOM   3107  O  O   . LEU B  1 80  ? -31.883 -22.546 17.193  1.00 19.83 ? 83   LEU B O   1 
ATOM   3108  C  CB  . LEU B  1 80  ? -32.897 -23.083 20.354  1.00 13.90 ? 83   LEU B CB  1 
ATOM   3109  C  CG  . LEU B  1 80  ? -34.043 -23.999 20.819  1.00 15.22 ? 83   LEU B CG  1 
ATOM   3110  C  CD1 . LEU B  1 80  ? -34.632 -23.637 22.170  1.00 13.60 ? 83   LEU B CD1 1 
ATOM   3111  C  CD2 . LEU B  1 80  ? -35.135 -24.093 19.749  1.00 15.70 ? 83   LEU B CD2 1 
ATOM   3112  N  N   . VAL B  1 81  ? -30.374 -22.070 18.800  1.00 18.78 ? 84   VAL B N   1 
ATOM   3113  C  CA  . VAL B  1 81  ? -29.804 -20.983 18.015  1.00 17.46 ? 84   VAL B CA  1 
ATOM   3114  C  C   . VAL B  1 81  ? -28.639 -21.347 17.105  1.00 17.49 ? 84   VAL B C   1 
ATOM   3115  O  O   . VAL B  1 81  ? -28.369 -20.604 16.159  1.00 20.08 ? 84   VAL B O   1 
ATOM   3116  C  CB  . VAL B  1 81  ? -29.454 -19.751 18.876  1.00 18.08 ? 84   VAL B CB  1 
ATOM   3117  C  CG1 . VAL B  1 81  ? -30.702 -19.284 19.620  1.00 18.09 ? 84   VAL B CG1 1 
ATOM   3118  C  CG2 . VAL B  1 81  ? -28.317 -20.099 19.864  1.00 18.42 ? 84   VAL B CG2 1 
ATOM   3119  N  N   . ASP B  1 82  ? -27.974 -22.479 17.366  1.00 14.79 ? 85   ASP B N   1 
ATOM   3120  C  CA  . ASP B  1 82  ? -26.712 -22.852 16.677  1.00 14.64 ? 85   ASP B CA  1 
ATOM   3121  C  C   . ASP B  1 82  ? -26.777 -24.263 16.048  1.00 15.81 ? 85   ASP B C   1 
ATOM   3122  O  O   . ASP B  1 82  ? -25.883 -24.662 15.290  1.00 14.86 ? 85   ASP B O   1 
ATOM   3123  C  CB  . ASP B  1 82  ? -25.524 -22.839 17.660  1.00 13.76 ? 85   ASP B CB  1 
ATOM   3124  C  CG  . ASP B  1 82  ? -25.102 -21.427 18.088  1.00 15.38 ? 85   ASP B CG  1 
ATOM   3125  O  OD1 . ASP B  1 82  ? -25.286 -20.459 17.331  1.00 16.95 ? 85   ASP B OD1 1 
ATOM   3126  O  OD2 . ASP B  1 82  ? -24.508 -21.292 19.172  1.00 17.07 ? 85   ASP B OD2 1 
ATOM   3127  N  N   . GLY B  1 83  ? -27.766 -25.056 16.451  1.00 13.94 ? 86   GLY B N   1 
ATOM   3128  C  CA  . GLY B  1 83  ? -27.830 -26.460 16.038  1.00 14.65 ? 86   GLY B CA  1 
ATOM   3129  C  C   . GLY B  1 83  ? -28.784 -26.678 14.868  1.00 14.73 ? 86   GLY B C   1 
ATOM   3130  O  O   . GLY B  1 83  ? -29.525 -25.774 14.473  1.00 12.78 ? 86   GLY B O   1 
ATOM   3131  N  N   . ASN B  1 84  ? -28.760 -27.886 14.321  1.00 17.78 ? 87   ASN B N   1 
ATOM   3132  C  CA  . ASN B  1 84  ? -29.685 -28.288 13.275  1.00 18.23 ? 87   ASN B CA  1 
ATOM   3133  C  C   . ASN B  1 84  ? -30.832 -29.070 13.868  1.00 18.38 ? 87   ASN B C   1 
ATOM   3134  O  O   . ASN B  1 84  ? -30.673 -30.226 14.241  1.00 21.15 ? 87   ASN B O   1 
ATOM   3135  C  CB  . ASN B  1 84  ? -28.986 -29.133 12.206  1.00 13.46 ? 87   ASN B CB  1 
ATOM   3136  C  CG  . ASN B  1 84  ? -29.847 -29.307 10.948  1.00 19.03 ? 87   ASN B CG  1 
ATOM   3137  O  OD1 . ASN B  1 84  ? -30.984 -29.788 11.026  1.00 18.62 ? 87   ASN B OD1 1 
ATOM   3138  N  ND2 . ASN B  1 84  ? -29.307 -28.911 9.785   1.00 15.44 ? 87   ASN B ND2 1 
ATOM   3139  N  N   . LEU B  1 85  ? -32.004 -28.456 13.863  1.00 19.92 ? 88   LEU B N   1 
ATOM   3140  C  CA  . LEU B  1 85  ? -33.140 -28.926 14.636  1.00 21.23 ? 88   LEU B CA  1 
ATOM   3141  C  C   . LEU B  1 85  ? -33.734 -30.172 13.983  1.00 20.57 ? 88   LEU B C   1 
ATOM   3142  O  O   . LEU B  1 85  ? -34.272 -31.055 14.666  1.00 18.84 ? 88   LEU B O   1 
ATOM   3143  C  CB  . LEU B  1 85  ? -34.188 -27.811 14.708  1.00 19.06 ? 88   LEU B CB  1 
ATOM   3144  C  CG  . LEU B  1 85  ? -34.124 -26.810 15.871  1.00 23.82 ? 88   LEU B CG  1 
ATOM   3145  C  CD1 . LEU B  1 85  ? -32.759 -26.717 16.532  1.00 20.07 ? 88   LEU B CD1 1 
ATOM   3146  C  CD2 . LEU B  1 85  ? -34.637 -25.427 15.492  1.00 19.45 ? 88   LEU B CD2 1 
ATOM   3147  N  N   . ILE B  1 86  ? -33.553 -30.261 12.667  1.00 19.14 ? 89   ILE B N   1 
ATOM   3148  C  CA  . ILE B  1 86  ? -34.045 -31.373 11.870  1.00 20.03 ? 89   ILE B CA  1 
ATOM   3149  C  C   . ILE B  1 86  ? -33.209 -32.645 12.006  1.00 20.90 ? 89   ILE B C   1 
ATOM   3150  O  O   . ILE B  1 86  ? -33.748 -33.733 12.176  1.00 23.08 ? 89   ILE B O   1 
ATOM   3151  C  CB  . ILE B  1 86  ? -34.115 -30.980 10.393  1.00 24.95 ? 89   ILE B CB  1 
ATOM   3152  C  CG1 . ILE B  1 86  ? -35.309 -30.054 10.157  1.00 21.92 ? 89   ILE B CG1 1 
ATOM   3153  C  CG2 . ILE B  1 86  ? -34.208 -32.234 9.512   1.00 24.44 ? 89   ILE B CG2 1 
ATOM   3154  C  CD1 . ILE B  1 86  ? -36.636 -30.682 10.611  1.00 23.06 ? 89   ILE B CD1 1 
ATOM   3155  N  N   . THR B  1 87  ? -31.888 -32.512 11.993  1.00 18.90 ? 90   THR B N   1 
ATOM   3156  C  CA  . THR B  1 87  ? -31.034 -33.681 12.136  1.00 18.39 ? 90   THR B CA  1 
ATOM   3157  C  C   . THR B  1 87  ? -30.681 -33.945 13.594  1.00 19.69 ? 90   THR B C   1 
ATOM   3158  O  O   . THR B  1 87  ? -30.172 -35.002 13.928  1.00 20.17 ? 90   THR B O   1 
ATOM   3159  C  CB  . THR B  1 87  ? -29.720 -33.510 11.353  1.00 17.94 ? 90   THR B CB  1 
ATOM   3160  O  OG1 . THR B  1 87  ? -28.947 -32.482 11.973  1.00 20.31 ? 90   THR B OG1 1 
ATOM   3161  C  CG2 . THR B  1 87  ? -30.001 -33.109 9.928   1.00 13.14 ? 90   THR B CG2 1 
ATOM   3162  N  N   . ASP B  1 88  ? -30.896 -32.952 14.450  1.00 19.09 ? 91   ASP B N   1 
ATOM   3163  C  CA  . ASP B  1 88  ? -30.664 -33.103 15.885  1.00 19.43 ? 91   ASP B CA  1 
ATOM   3164  C  C   . ASP B  1 88  ? -29.170 -33.057 16.230  1.00 17.97 ? 91   ASP B C   1 
ATOM   3165  O  O   . ASP B  1 88  ? -28.725 -33.711 17.166  1.00 17.65 ? 91   ASP B O   1 
ATOM   3166  C  CB  . ASP B  1 88  ? -31.278 -34.398 16.390  1.00 17.27 ? 91   ASP B CB  1 
ATOM   3167  C  CG  . ASP B  1 88  ? -31.582 -34.361 17.881  1.00 21.47 ? 91   ASP B CG  1 
ATOM   3168  O  OD1 . ASP B  1 88  ? -32.046 -33.304 18.403  1.00 19.79 ? 91   ASP B OD1 1 
ATOM   3169  O  OD2 . ASP B  1 88  ? -31.420 -35.421 18.527  1.00 22.50 ? 91   ASP B OD2 1 
ATOM   3170  N  N   . LEU B  1 89  ? -28.402 -32.313 15.439  1.00 16.16 ? 92   LEU B N   1 
ATOM   3171  C  CA  . LEU B  1 89  ? -26.959 -32.283 15.601  1.00 16.11 ? 92   LEU B CA  1 
ATOM   3172  C  C   . LEU B  1 89  ? -26.507 -30.870 15.867  1.00 15.74 ? 92   LEU B C   1 
ATOM   3173  O  O   . LEU B  1 89  ? -26.955 -29.930 15.206  1.00 15.28 ? 92   LEU B O   1 
ATOM   3174  C  CB  . LEU B  1 89  ? -26.238 -32.831 14.347  1.00 15.83 ? 92   LEU B CB  1 
ATOM   3175  C  CG  . LEU B  1 89  ? -26.266 -34.362 14.174  1.00 19.34 ? 92   LEU B CG  1 
ATOM   3176  C  CD1 . LEU B  1 89  ? -25.676 -34.816 12.825  1.00 17.59 ? 92   LEU B CD1 1 
ATOM   3177  C  CD2 . LEU B  1 89  ? -25.644 -35.124 15.362  1.00 15.07 ? 92   LEU B CD2 1 
ATOM   3178  N  N   . LEU B  1 90  ? -25.538 -30.745 16.766  1.00 16.06 ? 93   LEU B N   1 
ATOM   3179  C  CA  . LEU B  1 90  ? -24.913 -29.480 17.049  1.00 16.47 ? 93   LEU B CA  1 
ATOM   3180  C  C   . LEU B  1 90  ? -23.392 -29.632 17.124  1.00 19.13 ? 93   LEU B C   1 
ATOM   3181  O  O   . LEU B  1 90  ? -22.864 -30.613 17.690  1.00 16.52 ? 93   LEU B O   1 
ATOM   3182  C  CB  . LEU B  1 90  ? -25.455 -28.927 18.358  1.00 17.84 ? 93   LEU B CB  1 
ATOM   3183  C  CG  . LEU B  1 90  ? -24.640 -27.816 19.005  1.00 20.30 ? 93   LEU B CG  1 
ATOM   3184  C  CD1 . LEU B  1 90  ? -24.991 -26.460 18.356  1.00 19.32 ? 93   LEU B CD1 1 
ATOM   3185  C  CD2 . LEU B  1 90  ? -24.961 -27.806 20.476  1.00 22.92 ? 93   LEU B CD2 1 
ATOM   3186  N  N   . SER B  1 91  ? -22.704 -28.711 16.458  1.00 15.43 ? 94   SER B N   1 
ATOM   3187  C  CA  . SER B  1 91  ? -21.264 -28.641 16.512  1.00 16.32 ? 94   SER B CA  1 
ATOM   3188  C  C   . SER B  1 91  ? -20.845 -27.768 17.701  1.00 18.58 ? 94   SER B C   1 
ATOM   3189  O  O   . SER B  1 91  ? -21.317 -26.628 17.846  1.00 13.18 ? 94   SER B O   1 
ATOM   3190  C  CB  . SER B  1 91  ? -20.714 -28.046 15.209  1.00 14.98 ? 94   SER B CB  1 
ATOM   3191  O  OG  . SER B  1 91  ? -19.439 -27.442 15.423  1.00 19.22 ? 94   SER B OG  1 
ATOM   3192  N  N   . ILE B  1 92  ? -19.934 -28.292 18.519  1.00 16.40 ? 95   ILE B N   1 
ATOM   3193  C  CA  . ILE B  1 92  ? -19.395 -27.532 19.642  1.00 18.25 ? 95   ILE B CA  1 
ATOM   3194  C  C   . ILE B  1 92  ? -18.383 -26.463 19.231  1.00 18.02 ? 95   ILE B C   1 
ATOM   3195  O  O   . ILE B  1 92  ? -17.744 -25.835 20.092  1.00 17.29 ? 95   ILE B O   1 
ATOM   3196  C  CB  . ILE B  1 92  ? -18.773 -28.452 20.703  1.00 15.00 ? 95   ILE B CB  1 
ATOM   3197  C  CG1 . ILE B  1 92  ? -17.488 -29.093 20.179  1.00 12.37 ? 95   ILE B CG1 1 
ATOM   3198  C  CG2 . ILE B  1 92  ? -19.750 -29.549 21.076  1.00 14.89 ? 95   ILE B CG2 1 
ATOM   3199  C  CD1 . ILE B  1 92  ? -16.672 -29.734 21.318  1.00 14.26 ? 95   ILE B CD1 1 
ATOM   3200  N  N   . GLY B  1 93  ? -18.266 -26.234 17.923  1.00 16.49 ? 96   GLY B N   1 
ATOM   3201  C  CA  . GLY B  1 93  ? -17.348 -25.219 17.417  1.00 16.84 ? 96   GLY B CA  1 
ATOM   3202  C  C   . GLY B  1 93  ? -17.823 -24.593 16.115  1.00 17.44 ? 96   GLY B C   1 
ATOM   3203  O  O   . GLY B  1 93  ? -18.835 -23.872 16.078  1.00 16.75 ? 96   GLY B O   1 
ATOM   3204  N  N   . ARG B  1 94  ? -17.051 -24.806 15.059  1.00 12.92 ? 97   ARG B N   1 
ATOM   3205  C  CA  . ARG B  1 94  ? -17.285 -24.095 13.820  1.00 17.90 ? 97   ARG B CA  1 
ATOM   3206  C  C   . ARG B  1 94  ? -18.468 -24.702 13.065  1.00 16.80 ? 97   ARG B C   1 
ATOM   3207  O  O   . ARG B  1 94  ? -18.831 -25.866 13.278  1.00 16.17 ? 97   ARG B O   1 
ATOM   3208  C  CB  . ARG B  1 94  ? -16.035 -24.133 12.957  1.00 18.55 ? 97   ARG B CB  1 
ATOM   3209  C  CG  . ARG B  1 94  ? -15.508 -25.517 12.739  1.00 22.70 ? 97   ARG B CG  1 
ATOM   3210  C  CD  . ARG B  1 94  ? -14.361 -25.518 11.727  1.00 27.94 ? 97   ARG B CD  1 
ATOM   3211  N  NE  . ARG B  1 94  ? -14.459 -26.702 10.885  1.00 31.66 ? 97   ARG B NE  1 
ATOM   3212  C  CZ  . ARG B  1 94  ? -13.813 -27.825 11.125  1.00 33.52 ? 97   ARG B CZ  1 
ATOM   3213  N  NH1 . ARG B  1 94  ? -12.913 -27.874 12.098  1.00 39.94 ? 97   ARG B NH1 1 
ATOM   3214  N  NH2 . ARG B  1 94  ? -14.043 -28.881 10.375  1.00 34.12 ? 97   ARG B NH2 1 
ATOM   3215  N  N   . LYS B  1 95  ? -19.088 -23.911 12.204  1.00 20.09 ? 98   LYS B N   1 
ATOM   3216  C  CA  . LYS B  1 95  ? -20.060 -24.464 11.255  1.00 20.35 ? 98   LYS B CA  1 
ATOM   3217  C  C   . LYS B  1 95  ? -19.439 -25.663 10.577  1.00 20.64 ? 98   LYS B C   1 
ATOM   3218  O  O   . LYS B  1 95  ? -18.310 -25.580 10.109  1.00 19.78 ? 98   LYS B O   1 
ATOM   3219  C  CB  . LYS B  1 95  ? -20.388 -23.419 10.183  1.00 20.72 ? 98   LYS B CB  1 
ATOM   3220  C  CG  . LYS B  1 95  ? -21.566 -23.802 9.274   1.00 20.18 ? 98   LYS B CG  1 
ATOM   3221  C  CD  . LYS B  1 95  ? -22.143 -22.575 8.577   1.00 20.89 ? 98   LYS B CD  1 
ATOM   3222  C  CE  . LYS B  1 95  ? -23.317 -22.949 7.648   1.00 20.41 ? 98   LYS B CE  1 
ATOM   3223  N  NZ  . LYS B  1 95  ? -24.126 -24.064 8.234   1.00 21.94 ? 98   LYS B NZ  1 
ATOM   3224  N  N   . THR B  1 96  ? -20.172 -26.772 10.506  1.00 24.79 ? 99   THR B N   1 
ATOM   3225  C  CA  . THR B  1 96  ? -19.749 -27.919 9.705   1.00 22.05 ? 99   THR B CA  1 
ATOM   3226  C  C   . THR B  1 96  ? -20.887 -28.461 8.822   1.00 25.79 ? 99   THR B C   1 
ATOM   3227  O  O   . THR B  1 96  ? -22.055 -28.473 9.230   1.00 26.53 ? 99   THR B O   1 
ATOM   3228  C  CB  . THR B  1 96  ? -19.185 -29.070 10.583  1.00 22.91 ? 99   THR B CB  1 
ATOM   3229  O  OG1 . THR B  1 96  ? -18.851 -30.191 9.751   1.00 19.93 ? 99   THR B OG1 1 
ATOM   3230  C  CG2 . THR B  1 96  ? -20.197 -29.520 11.645  1.00 18.05 ? 99   THR B CG2 1 
ATOM   3231  N  N   . ARG B  1 97  ? -20.535 -28.892 7.613   1.00 23.90 ? 100  ARG B N   1 
ATOM   3232  C  CA  . ARG B  1 97  ? -21.464 -29.605 6.734   1.00 26.38 ? 100  ARG B CA  1 
ATOM   3233  C  C   . ARG B  1 97  ? -21.988 -30.878 7.390   1.00 25.51 ? 100  ARG B C   1 
ATOM   3234  O  O   . ARG B  1 97  ? -23.010 -31.412 6.973   1.00 25.49 ? 100  ARG B O   1 
ATOM   3235  C  CB  . ARG B  1 97  ? -20.788 -29.965 5.401   1.00 25.53 ? 100  ARG B CB  1 
ATOM   3236  C  CG  . ARG B  1 97  ? -19.734 -31.070 5.522   1.00 25.60 ? 100  ARG B CG  1 
ATOM   3237  C  CD  . ARG B  1 97  ? -18.800 -31.107 4.282   1.00 28.05 ? 100  ARG B CD  1 
ATOM   3238  N  NE  . ARG B  1 97  ? -17.824 -32.202 4.385   1.00 29.19 ? 100  ARG B NE  1 
ATOM   3239  C  CZ  . ARG B  1 97  ? -18.039 -33.453 3.975   1.00 30.05 ? 100  ARG B CZ  1 
ATOM   3240  N  NH1 . ARG B  1 97  ? -19.167 -33.770 3.322   1.00 27.84 ? 100  ARG B NH1 1 
ATOM   3241  N  NH2 . ARG B  1 97  ? -17.116 -34.384 4.197   1.00 25.99 ? 100  ARG B NH2 1 
ATOM   3242  N  N   . LEU B  1 98  ? -21.308 -31.341 8.435   1.00 23.75 ? 101  LEU B N   1 
ATOM   3243  C  CA  . LEU B  1 98  ? -21.669 -32.596 9.083   1.00 21.97 ? 101  LEU B CA  1 
ATOM   3244  C  C   . LEU B  1 98  ? -22.995 -32.547 9.857   1.00 23.22 ? 101  LEU B C   1 
ATOM   3245  O  O   . LEU B  1 98  ? -23.524 -33.588 10.264  1.00 25.13 ? 101  LEU B O   1 
ATOM   3246  C  CB  . LEU B  1 98  ? -20.559 -33.039 10.023  1.00 21.86 ? 101  LEU B CB  1 
ATOM   3247  C  CG  . LEU B  1 98  ? -19.541 -34.099 9.598   1.00 22.88 ? 101  LEU B CG  1 
ATOM   3248  C  CD1 . LEU B  1 98  ? -19.359 -34.234 8.114   1.00 16.91 ? 101  LEU B CD1 1 
ATOM   3249  C  CD2 . LEU B  1 98  ? -18.195 -33.928 10.340  1.00 20.82 ? 101  LEU B CD2 1 
ATOM   3250  N  N   . THR B  1 99  ? -23.542 -31.353 10.067  1.00 20.45 ? 102  THR B N   1 
ATOM   3251  C  CA  . THR B  1 99  ? -24.792 -31.250 10.808  1.00 18.76 ? 102  THR B CA  1 
ATOM   3252  C  C   . THR B  1 99  ? -26.007 -31.377 9.870   1.00 21.53 ? 102  THR B C   1 
ATOM   3253  O  O   . THR B  1 99  ? -27.149 -31.351 10.329  1.00 20.88 ? 102  THR B O   1 
ATOM   3254  C  CB  . THR B  1 99  ? -24.884 -29.949 11.658  1.00 14.51 ? 102  THR B CB  1 
ATOM   3255  O  OG1 . THR B  1 99  ? -24.603 -28.796 10.840  1.00 13.66 ? 102  THR B OG1 1 
ATOM   3256  C  CG2 . THR B  1 99  ? -23.907 -29.997 12.816  1.00 16.01 ? 102  THR B CG2 1 
ATOM   3257  N  N   . GLY B  1 100 ? -25.755 -31.462 8.563   1.00 21.83 ? 103  GLY B N   1 
ATOM   3258  C  CA  . GLY B  1 100 ? -26.793 -31.843 7.586   1.00 18.75 ? 103  GLY B CA  1 
ATOM   3259  C  C   . GLY B  1 100 ? -27.315 -30.655 6.791   1.00 21.15 ? 103  GLY B C   1 
ATOM   3260  O  O   . GLY B  1 100 ? -26.671 -29.597 6.755   1.00 18.54 ? 103  GLY B O   1 
ATOM   3261  N  N   . PRO B  1 101 ? -28.465 -30.826 6.105   1.00 21.35 ? 104  PRO B N   1 
ATOM   3262  C  CA  . PRO B  1 101 ? -29.008 -29.747 5.255   1.00 21.67 ? 104  PRO B CA  1 
ATOM   3263  C  C   . PRO B  1 101 ? -29.515 -28.584 6.108   1.00 25.02 ? 104  PRO B C   1 
ATOM   3264  O  O   . PRO B  1 101 ? -30.252 -28.791 7.084   1.00 25.36 ? 104  PRO B O   1 
ATOM   3265  C  CB  . PRO B  1 101 ? -30.183 -30.419 4.509   1.00 21.05 ? 104  PRO B CB  1 
ATOM   3266  C  CG  . PRO B  1 101 ? -30.040 -31.914 4.789   1.00 21.62 ? 104  PRO B CG  1 
ATOM   3267  C  CD  . PRO B  1 101 ? -29.366 -31.984 6.152   1.00 19.65 ? 104  PRO B CD  1 
ATOM   3268  N  N   . ASP B  1 102 ? -29.109 -27.375 5.739   1.00 27.45 ? 105  ASP B N   1 
ATOM   3269  C  CA  . ASP B  1 102 ? -29.392 -26.191 6.530   1.00 28.86 ? 105  ASP B CA  1 
ATOM   3270  C  C   . ASP B  1 102 ? -30.829 -25.760 6.299   1.00 30.98 ? 105  ASP B C   1 
ATOM   3271  O  O   . ASP B  1 102 ? -31.374 -25.990 5.225   1.00 32.90 ? 105  ASP B O   1 
ATOM   3272  C  CB  . ASP B  1 102 ? -28.459 -25.051 6.130   1.00 27.03 ? 105  ASP B CB  1 
ATOM   3273  C  CG  . ASP B  1 102 ? -27.150 -25.044 6.919   1.00 27.70 ? 105  ASP B CG  1 
ATOM   3274  O  OD1 . ASP B  1 102 ? -27.011 -25.768 7.937   1.00 28.32 ? 105  ASP B OD1 1 
ATOM   3275  O  OD2 . ASP B  1 102 ? -26.265 -24.258 6.530   1.00 27.07 ? 105  ASP B OD2 1 
ATOM   3276  N  N   . PRO B  1 103 ? -31.415 -25.059 7.284   1.00 29.73 ? 106  PRO B N   1 
ATOM   3277  C  CA  . PRO B  1 103 ? -32.704 -24.399 7.161   1.00 26.13 ? 106  PRO B CA  1 
ATOM   3278  C  C   . PRO B  1 103 ? -32.518 -23.086 6.410   1.00 27.48 ? 106  PRO B C   1 
ATOM   3279  O  O   . PRO B  1 103 ? -31.391 -22.706 6.135   1.00 30.04 ? 106  PRO B O   1 
ATOM   3280  C  CB  . PRO B  1 103 ? -33.087 -24.141 8.620   1.00 26.20 ? 106  PRO B CB  1 
ATOM   3281  C  CG  . PRO B  1 103 ? -31.740 -23.930 9.321   1.00 25.61 ? 106  PRO B CG  1 
ATOM   3282  C  CD  . PRO B  1 103 ? -30.706 -24.681 8.525   1.00 26.28 ? 106  PRO B CD  1 
ATOM   3283  N  N   . PRO B  1 104 ? -33.615 -22.433 5.997   1.00 27.16 ? 107  PRO B N   1 
ATOM   3284  C  CA  . PRO B  1 104 ? -33.468 -21.105 5.377   1.00 29.79 ? 107  PRO B CA  1 
ATOM   3285  C  C   . PRO B  1 104 ? -32.844 -20.112 6.348   1.00 27.18 ? 107  PRO B C   1 
ATOM   3286  O  O   . PRO B  1 104 ? -33.046 -20.228 7.550   1.00 30.04 ? 107  PRO B O   1 
ATOM   3287  C  CB  . PRO B  1 104 ? -34.923 -20.679 5.075   1.00 28.03 ? 107  PRO B CB  1 
ATOM   3288  C  CG  . PRO B  1 104 ? -35.673 -21.964 4.996   1.00 31.09 ? 107  PRO B CG  1 
ATOM   3289  C  CD  . PRO B  1 104 ? -35.009 -22.900 5.998   1.00 27.65 ? 107  PRO B CD  1 
ATOM   3290  N  N   . PRO B  1 105 ? -32.133 -19.113 5.826   1.00 29.05 ? 108  PRO B N   1 
ATOM   3291  C  CA  . PRO B  1 105 ? -31.748 -17.943 6.618   1.00 30.42 ? 108  PRO B CA  1 
ATOM   3292  C  C   . PRO B  1 105 ? -32.980 -17.216 7.198   1.00 30.25 ? 108  PRO B C   1 
ATOM   3293  O  O   . PRO B  1 105 ? -34.076 -17.325 6.639   1.00 31.10 ? 108  PRO B O   1 
ATOM   3294  C  CB  . PRO B  1 105 ? -31.016 -17.045 5.614   1.00 31.73 ? 108  PRO B CB  1 
ATOM   3295  C  CG  . PRO B  1 105 ? -30.963 -17.786 4.307   1.00 33.85 ? 108  PRO B CG  1 
ATOM   3296  C  CD  . PRO B  1 105 ? -31.440 -19.188 4.528   1.00 32.48 ? 108  PRO B CD  1 
ATOM   3297  N  N   . PRO B  1 106 ? -32.826 -16.527 8.347   1.00 27.60 ? 109  PRO B N   1 
ATOM   3298  C  CA  . PRO B  1 106 ? -31.595 -16.071 9.001   1.00 26.67 ? 109  PRO B CA  1 
ATOM   3299  C  C   . PRO B  1 106 ? -30.902 -17.093 9.902   1.00 26.34 ? 109  PRO B C   1 
ATOM   3300  O  O   . PRO B  1 106 ? -29.762 -16.887 10.281  1.00 28.23 ? 109  PRO B O   1 
ATOM   3301  C  CB  . PRO B  1 106 ? -32.058 -14.867 9.850   1.00 25.92 ? 109  PRO B CB  1 
ATOM   3302  C  CG  . PRO B  1 106 ? -33.482 -14.593 9.450   1.00 27.21 ? 109  PRO B CG  1 
ATOM   3303  C  CD  . PRO B  1 106 ? -34.014 -15.918 8.968   1.00 27.89 ? 109  PRO B CD  1 
ATOM   3304  N  N   . ALA B  1 107 ? -31.572 -18.188 10.230  1.00 25.59 ? 110  ALA B N   1 
ATOM   3305  C  CA  . ALA B  1 107 ? -30.927 -19.291 10.927  1.00 25.19 ? 110  ALA B CA  1 
ATOM   3306  C  C   . ALA B  1 107 ? -29.602 -19.660 10.244  1.00 27.08 ? 110  ALA B C   1 
ATOM   3307  O  O   . ALA B  1 107 ? -29.555 -19.846 9.043   1.00 27.99 ? 110  ALA B O   1 
ATOM   3308  C  CB  . ALA B  1 107 ? -31.858 -20.495 10.955  1.00 22.70 ? 110  ALA B CB  1 
ATOM   3309  N  N   . SER B  1 108 ? -28.522 -19.795 11.001  1.00 27.85 ? 111  SER B N   1 
ATOM   3310  C  CA  . SER B  1 108 ? -27.244 -20.027 10.347  1.00 26.35 ? 111  SER B CA  1 
ATOM   3311  C  C   . SER B  1 108 ? -26.592 -21.358 10.703  1.00 21.77 ? 111  SER B C   1 
ATOM   3312  O  O   . SER B  1 108 ? -25.674 -21.799 10.023  1.00 21.03 ? 111  SER B O   1 
ATOM   3313  C  CB  . SER B  1 108 ? -26.305 -18.854 10.591  1.00 27.01 ? 111  SER B CB  1 
ATOM   3314  O  OG  . SER B  1 108 ? -26.200 -18.608 11.974  1.00 33.11 ? 111  SER B OG  1 
ATOM   3315  N  N   . VAL B  1 109 ? -27.135 -22.031 11.712  1.00 21.34 ? 112  VAL B N   1 
ATOM   3316  C  CA  . VAL B  1 109 ? -26.606 -23.311 12.179  1.00 18.61 ? 112  VAL B CA  1 
ATOM   3317  C  C   . VAL B  1 109 ? -25.084 -23.284 12.183  1.00 19.00 ? 112  VAL B C   1 
ATOM   3318  O  O   . VAL B  1 109 ? -24.428 -24.111 11.551  1.00 18.69 ? 112  VAL B O   1 
ATOM   3319  C  CB  . VAL B  1 109 ? -27.119 -24.488 11.348  1.00 20.28 ? 112  VAL B CB  1 
ATOM   3320  C  CG1 . VAL B  1 109 ? -26.605 -25.809 11.911  1.00 19.29 ? 112  VAL B CG1 1 
ATOM   3321  C  CG2 . VAL B  1 109 ? -28.624 -24.496 11.340  1.00 21.50 ? 112  VAL B CG2 1 
ATOM   3322  N  N   . GLY B  1 110 ? -24.535 -22.309 12.900  1.00 17.24 ? 113  GLY B N   1 
ATOM   3323  C  CA  . GLY B  1 110 ? -23.108 -22.001 12.827  1.00 19.04 ? 113  GLY B CA  1 
ATOM   3324  C  C   . GLY B  1 110 ? -22.283 -22.648 13.929  1.00 18.10 ? 113  GLY B C   1 
ATOM   3325  O  O   . GLY B  1 110 ? -21.097 -22.357 14.074  1.00 17.00 ? 113  GLY B O   1 
ATOM   3326  N  N   . GLY B  1 111 ? -22.909 -23.548 14.689  1.00 16.17 ? 114  GLY B N   1 
ATOM   3327  C  CA  . GLY B  1 111 ? -22.272 -24.121 15.861  1.00 13.99 ? 114  GLY B CA  1 
ATOM   3328  C  C   . GLY B  1 111 ? -21.997 -23.129 16.984  1.00 12.29 ? 114  GLY B C   1 
ATOM   3329  O  O   . GLY B  1 111 ? -22.241 -21.931 16.846  1.00 16.44 ? 114  GLY B O   1 
ATOM   3330  N  N   . LEU B  1 112 ? -21.373 -23.608 18.054  1.00 10.57 ? 115  LEU B N   1 
ATOM   3331  C  CA  . LEU B  1 112 ? -21.092 -22.781 19.240  1.00 12.05 ? 115  LEU B CA  1 
ATOM   3332  C  C   . LEU B  1 112 ? -20.191 -21.580 18.941  1.00 13.27 ? 115  LEU B C   1 
ATOM   3333  O  O   . LEU B  1 112 ? -20.231 -20.619 19.680  1.00 14.53 ? 115  LEU B O   1 
ATOM   3334  C  CB  . LEU B  1 112 ? -20.492 -23.622 20.373  1.00 8.69  ? 115  LEU B CB  1 
ATOM   3335  C  CG  . LEU B  1 112 ? -21.421 -24.675 20.987  1.00 9.65  ? 115  LEU B CG  1 
ATOM   3336  C  CD1 . LEU B  1 112 ? -20.811 -25.185 22.322  1.00 10.84 ? 115  LEU B CD1 1 
ATOM   3337  C  CD2 . LEU B  1 112 ? -22.793 -24.074 21.252  1.00 8.95  ? 115  LEU B CD2 1 
ATOM   3338  N  N   . ASN B  1 113 ? -19.467 -21.602 17.812  1.00 13.28 ? 116  ASN B N   1 
ATOM   3339  C  CA  . ASN B  1 113 ? -18.576 -20.498 17.408  1.00 13.90 ? 116  ASN B CA  1 
ATOM   3340  C  C   . ASN B  1 113 ? -19.348 -19.299 16.891  1.00 15.44 ? 116  ASN B C   1 
ATOM   3341  O  O   . ASN B  1 113 ? -18.789 -18.224 16.741  1.00 17.38 ? 116  ASN B O   1 
ATOM   3342  C  CB  . ASN B  1 113 ? -17.601 -20.929 16.289  1.00 16.76 ? 116  ASN B CB  1 
ATOM   3343  C  CG  . ASN B  1 113 ? -16.384 -21.676 16.807  1.00 16.94 ? 116  ASN B CG  1 
ATOM   3344  O  OD1 . ASN B  1 113 ? -16.292 -21.979 17.983  1.00 15.36 ? 116  ASN B OD1 1 
ATOM   3345  N  ND2 . ASN B  1 113 ? -15.436 -21.974 15.914  1.00 16.25 ? 116  ASN B ND2 1 
ATOM   3346  N  N   . GLU B  1 114 ? -20.597 -19.506 16.495  1.00 18.75 ? 117  GLU B N   1 
ATOM   3347  C  CA  . GLU B  1 114 ? -21.427 -18.405 15.990  1.00 15.08 ? 117  GLU B CA  1 
ATOM   3348  C  C   . GLU B  1 114 ? -21.497 -17.266 16.999  1.00 17.24 ? 117  GLU B C   1 
ATOM   3349  O  O   . GLU B  1 114 ? -22.054 -17.418 18.094  1.00 17.55 ? 117  GLU B O   1 
ATOM   3350  C  CB  . GLU B  1 114 ? -22.849 -18.902 15.697  1.00 17.51 ? 117  GLU B CB  1 
ATOM   3351  C  CG  . GLU B  1 114 ? -23.726 -17.911 14.925  1.00 19.81 ? 117  GLU B CG  1 
ATOM   3352  C  CD  . GLU B  1 114 ? -23.235 -17.683 13.517  1.00 25.74 ? 117  GLU B CD  1 
ATOM   3353  O  OE1 . GLU B  1 114 ? -22.463 -18.535 13.005  1.00 29.28 ? 117  GLU B OE1 1 
ATOM   3354  O  OE2 . GLU B  1 114 ? -23.657 -16.681 12.899  1.00 28.38 ? 117  GLU B OE2 1 
ATOM   3355  N  N   . HIS B  1 115 ? -20.933 -16.125 16.635  1.00 17.84 ? 118  HIS B N   1 
ATOM   3356  C  CA  . HIS B  1 115 ? -20.944 -14.951 17.507  1.00 18.76 ? 118  HIS B CA  1 
ATOM   3357  C  C   . HIS B  1 115 ? -22.334 -14.408 17.759  1.00 18.82 ? 118  HIS B C   1 
ATOM   3358  O  O   . HIS B  1 115 ? -23.112 -14.211 16.822  1.00 21.06 ? 118  HIS B O   1 
ATOM   3359  C  CB  . HIS B  1 115 ? -20.076 -13.828 16.919  1.00 19.22 ? 118  HIS B CB  1 
ATOM   3360  C  CG  . HIS B  1 115 ? -20.056 -12.593 17.759  1.00 20.59 ? 118  HIS B CG  1 
ATOM   3361  N  ND1 . HIS B  1 115 ? -19.613 -12.594 19.067  1.00 19.10 ? 118  HIS B ND1 1 
ATOM   3362  C  CD2 . HIS B  1 115 ? -20.500 -11.335 17.511  1.00 20.42 ? 118  HIS B CD2 1 
ATOM   3363  C  CE1 . HIS B  1 115 ? -19.730 -11.376 19.569  1.00 21.90 ? 118  HIS B CE1 1 
ATOM   3364  N  NE2 . HIS B  1 115 ? -20.265 -10.592 18.647  1.00 23.06 ? 118  HIS B NE2 1 
ATOM   3365  N  N   . GLY B  1 116 ? -22.648 -14.153 19.027  1.00 19.10 ? 119  GLY B N   1 
ATOM   3366  C  CA  . GLY B  1 116 ? -23.812 -13.331 19.386  1.00 17.59 ? 119  GLY B CA  1 
ATOM   3367  C  C   . GLY B  1 116 ? -25.131 -14.078 19.503  1.00 18.46 ? 119  GLY B C   1 
ATOM   3368  O  O   . GLY B  1 116 ? -26.170 -13.476 19.768  1.00 20.09 ? 119  GLY B O   1 
ATOM   3369  N  N   . THR B  1 117 ? -25.097 -15.393 19.337  1.00 19.24 ? 120  THR B N   1 
ATOM   3370  C  CA  . THR B  1 117 ? -26.244 -16.225 19.678  1.00 19.66 ? 120  THR B CA  1 
ATOM   3371  C  C   . THR B  1 117 ? -26.037 -16.752 21.085  1.00 22.71 ? 120  THR B C   1 
ATOM   3372  O  O   . THR B  1 117 ? -26.664 -16.289 22.043  1.00 24.71 ? 120  THR B O   1 
ATOM   3373  C  CB  . THR B  1 117 ? -26.381 -17.422 18.710  1.00 20.80 ? 120  THR B CB  1 
ATOM   3374  O  OG1 . THR B  1 117 ? -25.121 -18.107 18.592  1.00 19.86 ? 120  THR B OG1 1 
ATOM   3375  C  CG2 . THR B  1 117 ? -26.848 -16.942 17.299  1.00 18.57 ? 120  THR B CG2 1 
ATOM   3376  N  N   . PHE B  1 118 ? -25.094 -17.673 21.228  1.00 21.80 ? 121  PHE B N   1 
ATOM   3377  C  CA  . PHE B  1 118 ? -24.724 -18.138 22.545  1.00 17.78 ? 121  PHE B CA  1 
ATOM   3378  C  C   . PHE B  1 118 ? -23.363 -17.546 22.919  1.00 17.29 ? 121  PHE B C   1 
ATOM   3379  O  O   . PHE B  1 118 ? -23.262 -16.800 23.883  1.00 16.82 ? 121  PHE B O   1 
ATOM   3380  C  CB  . PHE B  1 118 ? -24.745 -19.675 22.607  1.00 15.96 ? 121  PHE B CB  1 
ATOM   3381  C  CG  . PHE B  1 118 ? -24.709 -20.233 24.019  1.00 17.52 ? 121  PHE B CG  1 
ATOM   3382  C  CD1 . PHE B  1 118 ? -23.773 -19.780 24.941  1.00 17.93 ? 121  PHE B CD1 1 
ATOM   3383  C  CD2 . PHE B  1 118 ? -25.583 -21.223 24.406  1.00 15.74 ? 121  PHE B CD2 1 
ATOM   3384  C  CE1 . PHE B  1 118 ? -23.760 -20.263 26.241  1.00 19.84 ? 121  PHE B CE1 1 
ATOM   3385  C  CE2 . PHE B  1 118 ? -25.552 -21.747 25.690  1.00 16.00 ? 121  PHE B CE2 1 
ATOM   3386  C  CZ  . PHE B  1 118 ? -24.621 -21.278 26.613  1.00 17.41 ? 121  PHE B CZ  1 
ATOM   3387  N  N   . GLU B  1 119 ? -22.347 -17.777 22.088  1.00 15.12 ? 122  GLU B N   1 
ATOM   3388  C  CA  . GLU B  1 119 ? -21.042 -17.157 22.297  1.00 14.44 ? 122  GLU B CA  1 
ATOM   3389  C  C   . GLU B  1 119 ? -21.171 -15.650 22.353  1.00 13.21 ? 122  GLU B C   1 
ATOM   3390  O  O   . GLU B  1 119 ? -21.987 -15.066 21.641  1.00 12.54 ? 122  GLU B O   1 
ATOM   3391  C  CB  . GLU B  1 119 ? -20.075 -17.498 21.169  1.00 14.88 ? 122  GLU B CB  1 
ATOM   3392  C  CG  . GLU B  1 119 ? -18.629 -17.131 21.477  1.00 14.54 ? 122  GLU B CG  1 
ATOM   3393  C  CD  . GLU B  1 119 ? -18.324 -15.651 21.292  1.00 17.29 ? 122  GLU B CD  1 
ATOM   3394  O  OE1 . GLU B  1 119 ? -18.872 -15.032 20.353  1.00 21.94 ? 122  GLU B OE1 1 
ATOM   3395  O  OE2 . GLU B  1 119 ? -17.518 -15.108 22.077  1.00 16.19 ? 122  GLU B OE2 1 
ATOM   3396  N  N   . GLY B  1 120 ? -20.306 -15.016 23.137  1.00 11.74 ? 123  GLY B N   1 
ATOM   3397  C  CA  . GLY B  1 120 ? -20.285 -13.575 23.184  1.00 13.77 ? 123  GLY B CA  1 
ATOM   3398  C  C   . GLY B  1 120 ? -19.097 -13.012 23.918  1.00 13.18 ? 123  GLY B C   1 
ATOM   3399  O  O   . GLY B  1 120 ? -18.156 -13.745 24.267  1.00 14.11 ? 123  GLY B O   1 
ATOM   3400  N  N   . ASP B  1 121 ? -19.184 -11.716 24.212  1.00 12.53 ? 124  ASP B N   1 
ATOM   3401  C  CA  . ASP B  1 121 ? -18.014 -10.886 24.515  1.00 13.91 ? 124  ASP B CA  1 
ATOM   3402  C  C   . ASP B  1 121 ? -17.592 -11.018 25.982  1.00 14.37 ? 124  ASP B C   1 
ATOM   3403  O  O   . ASP B  1 121 ? -18.335 -11.554 26.813  1.00 13.60 ? 124  ASP B O   1 
ATOM   3404  C  CB  . ASP B  1 121 ? -18.318 -9.419  24.176  1.00 16.48 ? 124  ASP B CB  1 
ATOM   3405  C  CG  . ASP B  1 121 ? -18.401 -9.172  22.674  1.00 19.50 ? 124  ASP B CG  1 
ATOM   3406  O  OD1 . ASP B  1 121 ? -17.819 -9.975  21.902  1.00 20.25 ? 124  ASP B OD1 1 
ATOM   3407  O  OD2 . ASP B  1 121 ? -19.025 -8.159  22.266  1.00 19.57 ? 124  ASP B OD2 1 
ATOM   3408  N  N   . ALA B  1 122 ? -16.394 -10.534 26.294  1.00 13.62 ? 125  ALA B N   1 
ATOM   3409  C  CA  . ALA B  1 122 ? -15.881 -10.594 27.664  1.00 14.55 ? 125  ALA B CA  1 
ATOM   3410  C  C   . ALA B  1 122 ? -15.759 -12.011 28.180  1.00 11.83 ? 125  ALA B C   1 
ATOM   3411  O  O   . ALA B  1 122 ? -15.905 -12.246 29.362  1.00 16.78 ? 125  ALA B O   1 
ATOM   3412  C  CB  . ALA B  1 122 ? -16.758 -9.755  28.639  1.00 11.42 ? 125  ALA B CB  1 
ATOM   3413  N  N   . SER B  1 123 ? -15.400 -12.943 27.317  1.00 13.12 ? 126  SER B N   1 
ATOM   3414  C  CA  . SER B  1 123 ? -15.024 -14.276 27.761  1.00 13.00 ? 126  SER B CA  1 
ATOM   3415  C  C   . SER B  1 123 ? -13.701 -14.177 28.555  1.00 17.87 ? 126  SER B C   1 
ATOM   3416  O  O   . SER B  1 123 ? -12.869 -13.283 28.279  1.00 17.15 ? 126  SER B O   1 
ATOM   3417  C  CB  . SER B  1 123 ? -14.819 -15.155 26.518  1.00 11.95 ? 126  SER B CB  1 
ATOM   3418  O  OG  . SER B  1 123 ? -16.042 -15.402 25.835  1.00 14.31 ? 126  SER B OG  1 
ATOM   3419  N  N   . MET B  1 124 ? -13.421 -15.154 29.418  1.00 15.66 ? 127  MET B N   1 
ATOM   3420  C  CA  . MET B  1 124 ? -12.247 -15.050 30.309  1.00 18.53 ? 127  MET B CA  1 
ATOM   3421  C  C   . MET B  1 124 ? -10.979 -15.385 29.562  1.00 18.11 ? 127  MET B C   1 
ATOM   3422  O  O   . MET B  1 124 ? -9.954  -14.754 29.803  1.00 15.00 ? 127  MET B O   1 
ATOM   3423  C  CB  . MET B  1 124 ? -12.346 -15.961 31.537  1.00 17.98 ? 127  MET B CB  1 
ATOM   3424  C  CG  . MET B  1 124 ? -13.546 -15.662 32.429  1.00 22.05 ? 127  MET B CG  1 
ATOM   3425  S  SD  . MET B  1 124 ? -13.632 -16.845 33.791  1.00 22.58 ? 127  MET B SD  1 
ATOM   3426  C  CE  . MET B  1 124 ? -14.515 -18.201 33.022  1.00 20.93 ? 127  MET B CE  1 
ATOM   3427  N  N   . THR B  1 125 ? -11.046 -16.398 28.684  1.00 11.88 ? 128  THR B N   1 
ATOM   3428  C  CA  . THR B  1 125 ? -9.853  -16.917 28.054  1.00 11.49 ? 128  THR B CA  1 
ATOM   3429  C  C   . THR B  1 125 ? -9.910  -16.911 26.533  1.00 13.27 ? 128  THR B C   1 
ATOM   3430  O  O   . THR B  1 125 ? -8.984  -17.409 25.898  1.00 16.58 ? 128  THR B O   1 
ATOM   3431  C  CB  . THR B  1 125 ? -9.525  -18.371 28.523  1.00 16.31 ? 128  THR B CB  1 
ATOM   3432  O  OG1 . THR B  1 125 ? -10.570 -19.261 28.121  1.00 12.27 ? 128  THR B OG1 1 
ATOM   3433  C  CG2 . THR B  1 125 ? -9.320  -18.475 30.060  1.00 12.23 ? 128  THR B CG2 1 
ATOM   3434  N  N   . ARG B  1 126 ? -11.016 -16.431 25.958  1.00 12.93 ? 129  ARG B N   1 
ATOM   3435  C  CA  . ARG B  1 126 ? -11.171 -16.232 24.500  1.00 14.71 ? 129  ARG B CA  1 
ATOM   3436  C  C   . ARG B  1 126 ? -11.353 -14.749 24.216  1.00 15.88 ? 129  ARG B C   1 
ATOM   3437  O  O   . ARG B  1 126 ? -11.974 -14.050 25.010  1.00 15.37 ? 129  ARG B O   1 
ATOM   3438  C  CB  . ARG B  1 126 ? -12.437 -16.946 23.998  1.00 12.56 ? 129  ARG B CB  1 
ATOM   3439  C  CG  . ARG B  1 126 ? -12.235 -18.403 23.610  1.00 14.92 ? 129  ARG B CG  1 
ATOM   3440  C  CD  . ARG B  1 126 ? -11.792 -19.292 24.774  1.00 13.37 ? 129  ARG B CD  1 
ATOM   3441  N  NE  . ARG B  1 126 ? -11.486 -20.616 24.257  1.00 17.32 ? 129  ARG B NE  1 
ATOM   3442  C  CZ  . ARG B  1 126 ? -10.813 -21.557 24.911  1.00 20.38 ? 129  ARG B CZ  1 
ATOM   3443  N  NH1 . ARG B  1 126 ? -10.418 -21.370 26.168  1.00 17.66 ? 129  ARG B NH1 1 
ATOM   3444  N  NH2 . ARG B  1 126 ? -10.560 -22.705 24.300  1.00 23.47 ? 129  ARG B NH2 1 
ATOM   3445  N  N   . GLY B  1 127 ? -10.865 -14.274 23.073  1.00 14.28 ? 130  GLY B N   1 
ATOM   3446  C  CA  . GLY B  1 127 ? -11.073 -12.877 22.712  1.00 11.09 ? 130  GLY B CA  1 
ATOM   3447  C  C   . GLY B  1 127 ? -12.448 -12.591 22.093  1.00 16.05 ? 130  GLY B C   1 
ATOM   3448  O  O   . GLY B  1 127 ? -13.111 -13.498 21.558  1.00 13.48 ? 130  GLY B O   1 
ATOM   3449  N  N   . ASP B  1 128 ? -12.881 -11.337 22.168  1.00 11.82 ? 131  ASP B N   1 
ATOM   3450  C  CA  . ASP B  1 128 ? -14.089 -10.898 21.470  1.00 17.33 ? 131  ASP B CA  1 
ATOM   3451  C  C   . ASP B  1 128 ? -13.984 -11.116 19.934  1.00 21.13 ? 131  ASP B C   1 
ATOM   3452  O  O   . ASP B  1 128 ? -12.939 -10.833 19.315  1.00 20.71 ? 131  ASP B O   1 
ATOM   3453  C  CB  . ASP B  1 128 ? -14.352 -9.412  21.746  1.00 17.53 ? 131  ASP B CB  1 
ATOM   3454  C  CG  . ASP B  1 128 ? -14.734 -9.113  23.207  1.00 21.23 ? 131  ASP B CG  1 
ATOM   3455  O  OD1 . ASP B  1 128 ? -14.682 -10.024 24.085  1.00 19.21 ? 131  ASP B OD1 1 
ATOM   3456  O  OD2 . ASP B  1 128 ? -15.109 -7.943  23.462  1.00 17.40 ? 131  ASP B OD2 1 
ATOM   3457  N  N   . ALA B  1 129 ? -15.089 -11.537 19.315  1.00 21.20 ? 132  ALA B N   1 
ATOM   3458  C  CA  . ALA B  1 129 ? -15.125 -11.755 17.869  1.00 22.02 ? 132  ALA B CA  1 
ATOM   3459  C  C   . ALA B  1 129 ? -14.706 -10.529 17.080  1.00 19.58 ? 132  ALA B C   1 
ATOM   3460  O  O   . ALA B  1 129 ? -14.056 -10.641 16.050  1.00 20.32 ? 132  ALA B O   1 
ATOM   3461  C  CB  . ALA B  1 129 ? -16.503 -12.243 17.413  1.00 21.66 ? 132  ALA B CB  1 
ATOM   3462  N  N   . PHE B  1 130 ? -15.055 -9.345  17.556  1.00 21.02 ? 133  PHE B N   1 
ATOM   3463  C  CA  . PHE B  1 130 ? -14.543 -8.150  16.895  1.00 21.63 ? 133  PHE B CA  1 
ATOM   3464  C  C   . PHE B  1 130 ? -13.041 -8.282  16.536  1.00 23.33 ? 133  PHE B C   1 
ATOM   3465  O  O   . PHE B  1 130 ? -12.637 -8.007  15.415  1.00 27.05 ? 133  PHE B O   1 
ATOM   3466  C  CB  . PHE B  1 130 ? -14.806 -6.902  17.733  1.00 24.73 ? 133  PHE B CB  1 
ATOM   3467  C  CG  . PHE B  1 130 ? -14.373 -5.637  17.065  1.00 25.91 ? 133  PHE B CG  1 
ATOM   3468  C  CD1 . PHE B  1 130 ? -15.199 -5.007  16.152  1.00 25.15 ? 133  PHE B CD1 1 
ATOM   3469  C  CD2 . PHE B  1 130 ? -13.098 -5.133  17.274  1.00 27.75 ? 133  PHE B CD2 1 
ATOM   3470  C  CE1 . PHE B  1 130 ? -14.769 -3.873  15.469  1.00 27.05 ? 133  PHE B CE1 1 
ATOM   3471  C  CE2 . PHE B  1 130 ? -12.661 -3.991  16.608  1.00 27.28 ? 133  PHE B CE2 1 
ATOM   3472  C  CZ  . PHE B  1 130 ? -13.490 -3.376  15.681  1.00 26.79 ? 133  PHE B CZ  1 
ATOM   3473  N  N   . PHE B  1 131 ? -12.226 -8.758  17.468  1.00 21.69 ? 134  PHE B N   1 
ATOM   3474  C  CA  . PHE B  1 131 ? -10.785 -8.852  17.246  1.00 25.00 ? 134  PHE B CA  1 
ATOM   3475  C  C   . PHE B  1 131 ? -10.354 -10.025 16.356  1.00 27.37 ? 134  PHE B C   1 
ATOM   3476  O  O   . PHE B  1 131 ? -9.183  -10.152 16.022  1.00 26.93 ? 134  PHE B O   1 
ATOM   3477  C  CB  . PHE B  1 131 ? -10.047 -8.930  18.586  1.00 22.66 ? 134  PHE B CB  1 
ATOM   3478  C  CG  . PHE B  1 131 ? -10.437 -7.847  19.548  1.00 22.85 ? 134  PHE B CG  1 
ATOM   3479  C  CD1 . PHE B  1 131 ? -10.236 -6.508  19.223  1.00 22.26 ? 134  PHE B CD1 1 
ATOM   3480  C  CD2 . PHE B  1 131 ? -11.033 -8.160  20.759  1.00 22.66 ? 134  PHE B CD2 1 
ATOM   3481  C  CE1 . PHE B  1 131 ? -10.635 -5.498  20.092  1.00 25.59 ? 134  PHE B CE1 1 
ATOM   3482  C  CE2 . PHE B  1 131 ? -11.419 -7.149  21.651  1.00 23.66 ? 134  PHE B CE2 1 
ATOM   3483  C  CZ  . PHE B  1 131 ? -11.218 -5.828  21.322  1.00 24.11 ? 134  PHE B CZ  1 
ATOM   3484  N  N   . GLY B  1 132 ? -11.302 -10.867 15.967  1.00 27.29 ? 135  GLY B N   1 
ATOM   3485  C  CA  . GLY B  1 132 ? -10.996 -12.044 15.178  1.00 30.00 ? 135  GLY B CA  1 
ATOM   3486  C  C   . GLY B  1 132 ? -11.471 -13.276 15.927  1.00 31.17 ? 135  GLY B C   1 
ATOM   3487  O  O   . GLY B  1 132 ? -12.584 -13.308 16.427  1.00 38.00 ? 135  GLY B O   1 
ATOM   3488  N  N   . ASN B  1 133 ? -10.556 -14.198 16.152  1.00 26.33 ? 136  ASN B N   1 
ATOM   3489  C  CA  . ASN B  1 133 ? -10.813 -15.493 16.760  1.00 25.64 ? 136  ASN B CA  1 
ATOM   3490  C  C   . ASN B  1 133 ? -11.598 -15.479 18.081  1.00 23.34 ? 136  ASN B C   1 
ATOM   3491  O  O   . ASN B  1 133 ? -11.098 -15.033 19.115  1.00 21.36 ? 136  ASN B O   1 
ATOM   3492  C  CB  . ASN B  1 133 ? -9.464  -16.190 16.962  1.00 23.10 ? 136  ASN B CB  1 
ATOM   3493  C  CG  . ASN B  1 133 ? -9.602  -17.677 17.185  1.00 28.12 ? 136  ASN B CG  1 
ATOM   3494  O  OD1 . ASN B  1 133 ? -10.406 -18.133 18.023  1.00 26.57 ? 136  ASN B OD1 1 
ATOM   3495  N  ND2 . ASN B  1 133 ? -8.791  -18.456 16.460  1.00 25.42 ? 136  ASN B ND2 1 
ATOM   3496  N  N   . ASN B  1 134 ? -12.802 -16.045 18.070  1.00 21.62 ? 137  ASN B N   1 
ATOM   3497  C  CA  . ASN B  1 134 ? -13.653 -16.003 19.273  1.00 17.68 ? 137  ASN B CA  1 
ATOM   3498  C  C   . ASN B  1 134 ? -13.664 -17.299 20.079  1.00 16.37 ? 137  ASN B C   1 
ATOM   3499  O  O   . ASN B  1 134 ? -14.493 -17.480 20.963  1.00 18.30 ? 137  ASN B O   1 
ATOM   3500  C  CB  . ASN B  1 134 ? -15.086 -15.580 18.910  1.00 17.21 ? 137  ASN B CB  1 
ATOM   3501  C  CG  . ASN B  1 134 ? -15.868 -16.686 18.196  1.00 17.74 ? 137  ASN B CG  1 
ATOM   3502  O  OD1 . ASN B  1 134 ? -15.283 -17.627 17.658  1.00 18.59 ? 137  ASN B OD1 1 
ATOM   3503  N  ND2 . ASN B  1 134 ? -17.197 -16.587 18.220  1.00 17.32 ? 137  ASN B ND2 1 
ATOM   3504  N  N   . HIS B  1 135 ? -12.777 -18.227 19.751  1.00 15.51 ? 138  HIS B N   1 
ATOM   3505  C  CA  . HIS B  1 135 ? -12.906 -19.584 20.275  1.00 19.08 ? 138  HIS B CA  1 
ATOM   3506  C  C   . HIS B  1 135 ? -11.602 -20.265 20.662  1.00 20.61 ? 138  HIS B C   1 
ATOM   3507  O  O   . HIS B  1 135 ? -11.616 -21.196 21.460  1.00 20.26 ? 138  HIS B O   1 
ATOM   3508  C  CB  . HIS B  1 135 ? -13.673 -20.478 19.288  1.00 21.30 ? 138  HIS B CB  1 
ATOM   3509  C  CG  . HIS B  1 135 ? -13.063 -20.535 17.923  1.00 23.34 ? 138  HIS B CG  1 
ATOM   3510  N  ND1 . HIS B  1 135 ? -13.263 -19.552 16.978  1.00 26.05 ? 138  HIS B ND1 1 
ATOM   3511  C  CD2 . HIS B  1 135 ? -12.330 -21.497 17.315  1.00 24.49 ? 138  HIS B CD2 1 
ATOM   3512  C  CE1 . HIS B  1 135 ? -12.619 -19.874 15.869  1.00 26.98 ? 138  HIS B CE1 1 
ATOM   3513  N  NE2 . HIS B  1 135 ? -12.039 -21.046 16.051  1.00 26.56 ? 138  HIS B NE2 1 
ATOM   3514  N  N   . ASP B  1 136 ? -10.481 -19.821 20.103  1.00 21.20 ? 139  ASP B N   1 
ATOM   3515  C  CA  . ASP B  1 136 ? -9.195  -20.387 20.485  1.00 22.66 ? 139  ASP B CA  1 
ATOM   3516  C  C   . ASP B  1 136 ? -8.720  -19.818 21.814  1.00 21.30 ? 139  ASP B C   1 
ATOM   3517  O  O   . ASP B  1 136 ? -9.015  -18.669 22.164  1.00 16.32 ? 139  ASP B O   1 
ATOM   3518  C  CB  . ASP B  1 136 ? -8.143  -20.183 19.383  1.00 27.56 ? 139  ASP B CB  1 
ATOM   3519  C  CG  . ASP B  1 136 ? -8.310  -21.179 18.240  1.00 31.73 ? 139  ASP B CG  1 
ATOM   3520  O  OD1 . ASP B  1 136 ? -8.696  -22.326 18.521  1.00 36.63 ? 139  ASP B OD1 1 
ATOM   3521  O  OD2 . ASP B  1 136 ? -8.164  -20.802 17.061  1.00 33.28 ? 139  ASP B OD2 1 
ATOM   3522  N  N   . PHE B  1 137 ? -8.041  -20.666 22.573  1.00 21.63 ? 140  PHE B N   1 
ATOM   3523  C  CA  . PHE B  1 137 ? -7.427  -20.279 23.841  1.00 20.91 ? 140  PHE B CA  1 
ATOM   3524  C  C   . PHE B  1 137 ? -6.430  -19.148 23.602  1.00 22.66 ? 140  PHE B C   1 
ATOM   3525  O  O   . PHE B  1 137 ? -5.719  -19.139 22.586  1.00 20.38 ? 140  PHE B O   1 
ATOM   3526  C  CB  . PHE B  1 137 ? -6.736  -21.506 24.469  1.00 20.22 ? 140  PHE B CB  1 
ATOM   3527  C  CG  . PHE B  1 137 ? -5.826  -21.177 25.613  1.00 20.46 ? 140  PHE B CG  1 
ATOM   3528  C  CD1 . PHE B  1 137 ? -4.499  -20.834 25.383  1.00 19.31 ? 140  PHE B CD1 1 
ATOM   3529  C  CD2 . PHE B  1 137 ? -6.309  -21.151 26.917  1.00 17.33 ? 140  PHE B CD2 1 
ATOM   3530  C  CE1 . PHE B  1 137 ? -3.663  -20.498 26.456  1.00 19.95 ? 140  PHE B CE1 1 
ATOM   3531  C  CE2 . PHE B  1 137 ? -5.475  -20.861 27.985  1.00 16.28 ? 140  PHE B CE2 1 
ATOM   3532  C  CZ  . PHE B  1 137 ? -4.155  -20.533 27.763  1.00 16.64 ? 140  PHE B CZ  1 
ATOM   3533  N  N   . ASN B  1 138 ? -6.496  -18.136 24.465  1.00 21.49 ? 141  ASN B N   1 
ATOM   3534  C  CA  . ASN B  1 138 ? -5.702  -16.930 24.332  1.00 21.01 ? 141  ASN B CA  1 
ATOM   3535  C  C   . ASN B  1 138 ? -4.813  -16.719 25.555  1.00 20.64 ? 141  ASN B C   1 
ATOM   3536  O  O   . ASN B  1 138 ? -5.295  -16.571 26.686  1.00 21.10 ? 141  ASN B O   1 
ATOM   3537  C  CB  . ASN B  1 138 ? -6.617  -15.725 24.138  1.00 22.19 ? 141  ASN B CB  1 
ATOM   3538  C  CG  . ASN B  1 138 ? -5.866  -14.405 24.124  1.00 24.19 ? 141  ASN B CG  1 
ATOM   3539  O  OD1 . ASN B  1 138 ? -5.077  -14.108 25.023  1.00 23.55 ? 141  ASN B OD1 1 
ATOM   3540  N  ND2 . ASN B  1 138 ? -6.177  -13.567 23.148  1.00 28.89 ? 141  ASN B ND2 1 
ATOM   3541  N  N   . GLU B  1 139 ? -3.509  -16.749 25.327  1.00 19.28 ? 142  GLU B N   1 
ATOM   3542  C  CA  . GLU B  1 139 ? -2.540  -16.880 26.405  1.00 17.80 ? 142  GLU B CA  1 
ATOM   3543  C  C   . GLU B  1 139 ? -2.504  -15.623 27.255  1.00 16.78 ? 142  GLU B C   1 
ATOM   3544  O  O   . GLU B  1 139 ? -2.504  -15.703 28.490  1.00 21.56 ? 142  GLU B O   1 
ATOM   3545  C  CB  . GLU B  1 139 ? -1.138  -17.205 25.835  1.00 16.32 ? 142  GLU B CB  1 
ATOM   3546  C  CG  . GLU B  1 139 ? 0.004   -17.080 26.858  1.00 16.95 ? 142  GLU B CG  1 
ATOM   3547  C  CD  . GLU B  1 139 ? 0.069   -18.236 27.831  1.00 16.62 ? 142  GLU B CD  1 
ATOM   3548  O  OE1 . GLU B  1 139 ? -0.597  -19.267 27.562  1.00 16.13 ? 142  GLU B OE1 1 
ATOM   3549  O  OE2 . GLU B  1 139 ? 0.804   -18.140 28.862  1.00 18.86 ? 142  GLU B OE2 1 
ATOM   3550  N  N   . THR B  1 140 ? -2.545  -14.461 26.604  1.00 15.35 ? 143  THR B N   1 
ATOM   3551  C  CA  . THR B  1 140 ? -2.568  -13.180 27.321  1.00 15.35 ? 143  THR B CA  1 
ATOM   3552  C  C   . THR B  1 140 ? -3.756  -13.117 28.281  1.00 15.29 ? 143  THR B C   1 
ATOM   3553  O  O   . THR B  1 140 ? -3.621  -12.698 29.421  1.00 15.53 ? 143  THR B O   1 
ATOM   3554  C  CB  . THR B  1 140 ? -2.627  -11.985 26.355  1.00 16.89 ? 143  THR B CB  1 
ATOM   3555  O  OG1 . THR B  1 140 ? -1.536  -12.063 25.437  1.00 19.59 ? 143  THR B OG1 1 
ATOM   3556  C  CG2 . THR B  1 140 ? -2.573  -10.643 27.103  1.00 18.82 ? 143  THR B CG2 1 
ATOM   3557  N  N   . LEU B  1 141 ? -4.909  -13.599 27.840  1.00 16.63 ? 144  LEU B N   1 
ATOM   3558  C  CA  . LEU B  1 141 ? -6.090  -13.530 28.681  1.00 16.42 ? 144  LEU B CA  1 
ATOM   3559  C  C   . LEU B  1 141 ? -5.980  -14.557 29.792  1.00 16.19 ? 144  LEU B C   1 
ATOM   3560  O  O   . LEU B  1 141 ? -6.355  -14.291 30.934  1.00 11.18 ? 144  LEU B O   1 
ATOM   3561  C  CB  . LEU B  1 141 ? -7.364  -13.756 27.856  1.00 17.00 ? 144  LEU B CB  1 
ATOM   3562  C  CG  . LEU B  1 141 ? -7.764  -12.591 26.930  1.00 15.57 ? 144  LEU B CG  1 
ATOM   3563  C  CD1 . LEU B  1 141 ? -9.044  -12.948 26.130  1.00 10.40 ? 144  LEU B CD1 1 
ATOM   3564  C  CD2 . LEU B  1 141 ? -7.974  -11.312 27.773  1.00 13.81 ? 144  LEU B CD2 1 
ATOM   3565  N  N   . PHE B  1 142 ? -5.413  -15.715 29.476  1.00 16.63 ? 145  PHE B N   1 
ATOM   3566  C  CA  . PHE B  1 142 ? -5.259  -16.722 30.514  1.00 21.15 ? 145  PHE B CA  1 
ATOM   3567  C  C   . PHE B  1 142 ? -4.312  -16.194 31.582  1.00 20.16 ? 145  PHE B C   1 
ATOM   3568  O  O   . PHE B  1 142 ? -4.539  -16.346 32.784  1.00 19.36 ? 145  PHE B O   1 
ATOM   3569  C  CB  . PHE B  1 142 ? -4.724  -18.047 29.968  1.00 18.90 ? 145  PHE B CB  1 
ATOM   3570  C  CG  . PHE B  1 142 ? -4.586  -19.099 31.031  1.00 22.77 ? 145  PHE B CG  1 
ATOM   3571  C  CD1 . PHE B  1 142 ? -5.709  -19.747 31.531  1.00 21.07 ? 145  PHE B CD1 1 
ATOM   3572  C  CD2 . PHE B  1 142 ? -3.359  -19.347 31.632  1.00 20.59 ? 145  PHE B CD2 1 
ATOM   3573  C  CE1 . PHE B  1 142 ? -5.591  -20.663 32.551  1.00 18.56 ? 145  PHE B CE1 1 
ATOM   3574  C  CE2 . PHE B  1 142 ? -3.253  -20.259 32.653  1.00 17.55 ? 145  PHE B CE2 1 
ATOM   3575  C  CZ  . PHE B  1 142 ? -4.364  -20.889 33.133  1.00 17.77 ? 145  PHE B CZ  1 
ATOM   3576  N  N   . GLU B  1 143 ? -3.236  -15.573 31.132  1.00 20.04 ? 146  GLU B N   1 
ATOM   3577  C  CA  . GLU B  1 143 ? -2.265  -15.047 32.078  1.00 24.27 ? 146  GLU B CA  1 
ATOM   3578  C  C   . GLU B  1 143 ? -2.838  -13.910 32.935  1.00 21.83 ? 146  GLU B C   1 
ATOM   3579  O  O   . GLU B  1 143 ? -2.526  -13.810 34.111  1.00 20.42 ? 146  GLU B O   1 
ATOM   3580  C  CB  . GLU B  1 143 ? -0.965  -14.660 31.368  1.00 27.13 ? 146  GLU B CB  1 
ATOM   3581  C  CG  . GLU B  1 143 ? 0.244   -14.571 32.285  1.00 34.05 ? 146  GLU B CG  1 
ATOM   3582  C  CD  . GLU B  1 143 ? 0.575   -15.863 33.051  1.00 34.26 ? 146  GLU B CD  1 
ATOM   3583  O  OE1 . GLU B  1 143 ? 0.235   -16.986 32.603  1.00 35.24 ? 146  GLU B OE1 1 
ATOM   3584  O  OE2 . GLU B  1 143 ? 1.287   -15.748 34.072  1.00 37.02 ? 146  GLU B OE2 1 
ATOM   3585  N  N   . GLN B  1 144 ? -3.777  -13.136 32.397  1.00 18.55 ? 147  GLN B N   1 
ATOM   3586  C  CA  . GLN B  1 144 ? -4.529  -12.213 33.243  1.00 16.92 ? 147  GLN B CA  1 
ATOM   3587  C  C   . GLN B  1 144 ? -5.322  -12.998 34.290  1.00 17.71 ? 147  GLN B C   1 
ATOM   3588  O  O   . GLN B  1 144 ? -5.474  -12.563 35.433  1.00 15.89 ? 147  GLN B O   1 
ATOM   3589  C  CB  . GLN B  1 144 ? -5.470  -11.359 32.383  1.00 21.47 ? 147  GLN B CB  1 
ATOM   3590  C  CG  . GLN B  1 144 ? -6.396  -10.407 33.145  1.00 21.31 ? 147  GLN B CG  1 
ATOM   3591  C  CD  . GLN B  1 144 ? -7.025  -9.343  32.236  1.00 24.67 ? 147  GLN B CD  1 
ATOM   3592  O  OE1 . GLN B  1 144 ? -7.858  -9.639  31.362  1.00 27.34 ? 147  GLN B OE1 1 
ATOM   3593  N  NE2 . GLN B  1 144 ? -6.651  -8.109  32.457  1.00 21.75 ? 147  GLN B NE2 1 
ATOM   3594  N  N   . LEU B  1 145 ? -5.821  -14.169 33.908  1.00 19.34 ? 148  LEU B N   1 
ATOM   3595  C  CA  . LEU B  1 145 ? -6.576  -14.979 34.859  1.00 19.00 ? 148  LEU B CA  1 
ATOM   3596  C  C   . LEU B  1 145 ? -5.691  -15.408 36.049  1.00 18.94 ? 148  LEU B C   1 
ATOM   3597  O  O   . LEU B  1 145 ? -6.092  -15.305 37.205  1.00 17.07 ? 148  LEU B O   1 
ATOM   3598  C  CB  . LEU B  1 145 ? -7.204  -16.183 34.163  1.00 14.52 ? 148  LEU B CB  1 
ATOM   3599  C  CG  . LEU B  1 145 ? -8.162  -17.009 35.049  1.00 20.50 ? 148  LEU B CG  1 
ATOM   3600  C  CD1 . LEU B  1 145 ? -9.315  -17.639 34.225  1.00 17.46 ? 148  LEU B CD1 1 
ATOM   3601  C  CD2 . LEU B  1 145 ? -7.386  -18.089 35.834  1.00 18.94 ? 148  LEU B CD2 1 
ATOM   3602  N  N   . VAL B  1 146 ? -4.493  -15.893 35.738  1.00 18.68 ? 149  VAL B N   1 
ATOM   3603  C  CA  . VAL B  1 146 ? -3.469  -16.219 36.725  1.00 21.58 ? 149  VAL B CA  1 
ATOM   3604  C  C   . VAL B  1 146 ? -3.124  -15.006 37.629  1.00 23.00 ? 149  VAL B C   1 
ATOM   3605  O  O   . VAL B  1 146 ? -3.105  -15.105 38.869  1.00 18.31 ? 149  VAL B O   1 
ATOM   3606  C  CB  . VAL B  1 146 ? -2.179  -16.706 35.987  1.00 23.94 ? 149  VAL B CB  1 
ATOM   3607  C  CG1 . VAL B  1 146 ? -1.051  -17.011 36.969  1.00 23.55 ? 149  VAL B CG1 1 
ATOM   3608  C  CG2 . VAL B  1 146 ? -2.474  -17.922 35.085  1.00 20.24 ? 149  VAL B CG2 1 
ATOM   3609  N  N   . ASP B  1 147 ? -2.867  -13.855 37.013  1.00 22.35 ? 150  ASP B N   1 
ATOM   3610  C  CA  A ASP B  1 147 ? -2.496  -12.684 37.780  0.50 23.28 ? 150  ASP B CA  1 
ATOM   3611  C  CA  B ASP B  1 147 ? -2.501  -12.656 37.763  0.50 23.36 ? 150  ASP B CA  1 
ATOM   3612  C  C   . ASP B  1 147 ? -3.624  -12.237 38.727  1.00 24.63 ? 150  ASP B C   1 
ATOM   3613  O  O   . ASP B  1 147 ? -3.363  -11.843 39.861  1.00 24.65 ? 150  ASP B O   1 
ATOM   3614  C  CB  A ASP B  1 147 ? -2.060  -11.557 36.847  0.50 23.96 ? 150  ASP B CB  1 
ATOM   3615  C  CB  B ASP B  1 147 ? -2.140  -11.496 36.823  0.50 24.25 ? 150  ASP B CB  1 
ATOM   3616  C  CG  A ASP B  1 147 ? -1.869  -10.250 37.568  0.50 24.64 ? 150  ASP B CG  1 
ATOM   3617  C  CG  B ASP B  1 147 ? -0.911  -11.783 35.964  0.50 24.59 ? 150  ASP B CG  1 
ATOM   3618  O  OD1 A ASP B  1 147 ? -1.150  -10.232 38.599  0.50 25.06 ? 150  ASP B OD1 1 
ATOM   3619  O  OD1 B ASP B  1 147 ? -0.272  -12.839 36.154  0.50 26.80 ? 150  ASP B OD1 1 
ATOM   3620  O  OD2 A ASP B  1 147 ? -2.448  -9.244  37.101  0.50 23.55 ? 150  ASP B OD2 1 
ATOM   3621  O  OD2 B ASP B  1 147 ? -0.616  -10.981 35.049  0.50 23.84 ? 150  ASP B OD2 1 
ATOM   3622  N  N   . TYR B  1 148 ? -4.880  -12.383 38.306  1.00 20.78 ? 151  TYR B N   1 
ATOM   3623  C  CA  . TYR B  1 148 ? -6.010  -12.128 39.210  1.00 17.96 ? 151  TYR B CA  1 
ATOM   3624  C  C   . TYR B  1 148 ? -6.169  -13.219 40.287  1.00 21.06 ? 151  TYR B C   1 
ATOM   3625  O  O   . TYR B  1 148 ? -6.623  -12.956 41.408  1.00 19.09 ? 151  TYR B O   1 
ATOM   3626  C  CB  . TYR B  1 148 ? -7.321  -11.979 38.428  1.00 17.60 ? 151  TYR B CB  1 
ATOM   3627  C  CG  . TYR B  1 148 ? -7.576  -10.574 37.976  1.00 17.16 ? 151  TYR B CG  1 
ATOM   3628  C  CD1 . TYR B  1 148 ? -6.666  -9.923  37.149  1.00 16.67 ? 151  TYR B CD1 1 
ATOM   3629  C  CD2 . TYR B  1 148 ? -8.664  -9.855  38.450  1.00 19.35 ? 151  TYR B CD2 1 
ATOM   3630  C  CE1 . TYR B  1 148 ? -6.826  -8.612  36.813  1.00 18.55 ? 151  TYR B CE1 1 
ATOM   3631  C  CE2 . TYR B  1 148 ? -8.846  -8.511  38.100  1.00 17.45 ? 151  TYR B CE2 1 
ATOM   3632  C  CZ  . TYR B  1 148 ? -7.929  -7.914  37.272  1.00 18.69 ? 151  TYR B CZ  1 
ATOM   3633  O  OH  . TYR B  1 148 ? -8.037  -6.590  36.958  1.00 20.91 ? 151  TYR B OH  1 
ATOM   3634  N  N   . SER B  1 149 ? -5.894  -14.461 39.917  1.00 18.30 ? 152  SER B N   1 
ATOM   3635  C  CA  . SER B  1 149 ? -5.836  -15.499 40.913  1.00 20.84 ? 152  SER B CA  1 
ATOM   3636  C  C   . SER B  1 149 ? -4.771  -15.169 41.966  1.00 20.75 ? 152  SER B C   1 
ATOM   3637  O  O   . SER B  1 149 ? -5.057  -15.167 43.173  1.00 23.11 ? 152  SER B O   1 
ATOM   3638  C  CB  . SER B  1 149 ? -5.584  -16.851 40.255  1.00 21.08 ? 152  SER B CB  1 
ATOM   3639  O  OG  . SER B  1 149 ? -6.685  -17.182 39.427  1.00 24.52 ? 152  SER B OG  1 
ATOM   3640  N  N   . ASN B  1 150 ? -3.558  -14.879 41.509  1.00 21.18 ? 153  ASN B N   1 
ATOM   3641  C  CA  . ASN B  1 150 ? -2.498  -14.362 42.399  1.00 25.58 ? 153  ASN B CA  1 
ATOM   3642  C  C   . ASN B  1 150 ? -2.927  -13.219 43.284  1.00 21.55 ? 153  ASN B C   1 
ATOM   3643  O  O   . ASN B  1 150 ? -2.824  -13.313 44.485  1.00 24.60 ? 153  ASN B O   1 
ATOM   3644  C  CB  . ASN B  1 150 ? -1.238  -13.996 41.616  1.00 22.74 ? 153  ASN B CB  1 
ATOM   3645  C  CG  . ASN B  1 150 ? -0.563  -15.209 41.075  1.00 27.32 ? 153  ASN B CG  1 
ATOM   3646  O  OD1 . ASN B  1 150 ? -0.975  -16.325 41.390  1.00 28.72 ? 153  ASN B OD1 1 
ATOM   3647  N  ND2 . ASN B  1 150 ? 0.406   -15.022 40.181  1.00 31.55 ? 153  ASN B ND2 1 
ATOM   3648  N  N   . ARG B  1 151 ? -3.486  -12.175 42.695  1.00 25.67 ? 154  ARG B N   1 
ATOM   3649  C  CA  . ARG B  1 151 ? -3.950  -11.018 43.464  1.00 25.49 ? 154  ARG B CA  1 
ATOM   3650  C  C   . ARG B  1 151 ? -5.046  -11.344 44.489  1.00 25.60 ? 154  ARG B C   1 
ATOM   3651  O  O   . ARG B  1 151 ? -5.004  -10.878 45.631  1.00 23.63 ? 154  ARG B O   1 
ATOM   3652  C  CB  . ARG B  1 151 ? -4.443  -9.930  42.517  1.00 30.09 ? 154  ARG B CB  1 
ATOM   3653  C  CG  . ARG B  1 151 ? -3.520  -8.732  42.398  1.00 39.63 ? 154  ARG B CG  1 
ATOM   3654  C  CD  . ARG B  1 151 ? -3.619  -8.069  41.018  1.00 44.45 ? 154  ARG B CD  1 
ATOM   3655  N  NE  . ARG B  1 151 ? -4.678  -7.060  40.956  1.00 47.30 ? 154  ARG B NE  1 
ATOM   3656  C  CZ  . ARG B  1 151 ? -5.057  -6.439  39.839  1.00 49.06 ? 154  ARG B CZ  1 
ATOM   3657  N  NH1 . ARG B  1 151 ? -4.445  -6.705  38.687  1.00 50.46 ? 154  ARG B NH1 1 
ATOM   3658  N  NH2 . ARG B  1 151 ? -6.032  -5.534  39.874  1.00 48.75 ? 154  ARG B NH2 1 
ATOM   3659  N  N   . PHE B  1 152 ? -6.093  -12.043 44.063  1.00 22.19 ? 155  PHE B N   1 
ATOM   3660  C  CA  . PHE B  1 152 ? -7.312  -12.072 44.879  1.00 19.68 ? 155  PHE B CA  1 
ATOM   3661  C  C   . PHE B  1 152 ? -7.642  -13.455 45.407  1.00 18.34 ? 155  PHE B C   1 
ATOM   3662  O  O   . PHE B  1 152 ? -8.650  -13.627 46.087  1.00 17.86 ? 155  PHE B O   1 
ATOM   3663  C  CB  . PHE B  1 152 ? -8.512  -11.579 44.076  1.00 22.04 ? 155  PHE B CB  1 
ATOM   3664  C  CG  . PHE B  1 152 ? -8.390  -10.174 43.596  1.00 22.67 ? 155  PHE B CG  1 
ATOM   3665  C  CD1 . PHE B  1 152 ? -8.598  -9.109  44.468  1.00 24.66 ? 155  PHE B CD1 1 
ATOM   3666  C  CD2 . PHE B  1 152 ? -8.179  -9.910  42.243  1.00 23.34 ? 155  PHE B CD2 1 
ATOM   3667  C  CE1 . PHE B  1 152 ? -8.554  -7.795  44.014  1.00 26.37 ? 155  PHE B CE1 1 
ATOM   3668  C  CE2 . PHE B  1 152 ? -8.082  -8.592  41.781  1.00 24.40 ? 155  PHE B CE2 1 
ATOM   3669  C  CZ  . PHE B  1 152 ? -8.263  -7.531  42.669  1.00 25.11 ? 155  PHE B CZ  1 
ATOM   3670  N  N   . GLY B  1 153 ? -6.878  -14.466 45.007  1.00 16.77 ? 156  GLY B N   1 
ATOM   3671  C  CA  . GLY B  1 153 ? -7.235  -15.833 45.403  1.00 17.16 ? 156  GLY B CA  1 
ATOM   3672  C  C   . GLY B  1 153 ? -6.054  -16.607 45.949  1.00 22.31 ? 156  GLY B C   1 
ATOM   3673  O  O   . GLY B  1 153 ? -5.997  -17.831 45.830  1.00 21.41 ? 156  GLY B O   1 
ATOM   3674  N  N   . GLY B  1 154 ? -5.059  -15.875 46.449  1.00 20.57 ? 157  GLY B N   1 
ATOM   3675  C  CA  . GLY B  1 154 ? -3.818  -16.469 46.936  1.00 20.85 ? 157  GLY B CA  1 
ATOM   3676  C  C   . GLY B  1 154 ? -3.186  -17.478 46.004  1.00 21.56 ? 157  GLY B C   1 
ATOM   3677  O  O   . GLY B  1 154 ? -2.695  -18.521 46.442  1.00 19.59 ? 157  GLY B O   1 
ATOM   3678  N  N   . GLY B  1 155 ? -3.258  -17.214 44.702  1.00 23.01 ? 158  GLY B N   1 
ATOM   3679  C  CA  . GLY B  1 155 ? -2.705  -18.149 43.732  1.00 17.65 ? 158  GLY B CA  1 
ATOM   3680  C  C   . GLY B  1 155 ? -3.746  -19.085 43.138  1.00 18.25 ? 158  GLY B C   1 
ATOM   3681  O  O   . GLY B  1 155 ? -3.460  -19.838 42.208  1.00 17.25 ? 158  GLY B O   1 
ATOM   3682  N  N   . LYS B  1 156 ? -4.959  -19.066 43.672  1.00 17.43 ? 159  LYS B N   1 
ATOM   3683  C  CA  . LYS B  1 156 ? -5.992  -19.915 43.101  1.00 20.15 ? 159  LYS B CA  1 
ATOM   3684  C  C   . LYS B  1 156 ? -7.172  -19.154 42.502  1.00 21.06 ? 159  LYS B C   1 
ATOM   3685  O  O   . LYS B  1 156 ? -7.485  -18.026 42.903  1.00 22.06 ? 159  LYS B O   1 
ATOM   3686  C  CB  . LYS B  1 156 ? -6.444  -20.945 44.133  1.00 23.84 ? 159  LYS B CB  1 
ATOM   3687  C  CG  . LYS B  1 156 ? -5.321  -21.922 44.501  1.00 26.47 ? 159  LYS B CG  1 
ATOM   3688  C  CD  . LYS B  1 156 ? -5.427  -22.342 45.937  1.00 34.02 ? 159  LYS B CD  1 
ATOM   3689  C  CE  . LYS B  1 156 ? -4.597  -23.596 46.200  1.00 37.24 ? 159  LYS B CE  1 
ATOM   3690  N  NZ  . LYS B  1 156 ? -3.419  -23.659 45.286  1.00 39.33 ? 159  LYS B NZ  1 
ATOM   3691  N  N   . TYR B  1 157 ? -7.828  -19.760 41.522  1.00 20.12 ? 160  TYR B N   1 
ATOM   3692  C  CA  . TYR B  1 157 ? -9.101  -19.236 41.069  1.00 17.76 ? 160  TYR B CA  1 
ATOM   3693  C  C   . TYR B  1 157 ? -10.237 -19.639 42.012  1.00 19.70 ? 160  TYR B C   1 
ATOM   3694  O  O   . TYR B  1 157 ? -10.538 -20.820 42.184  1.00 21.48 ? 160  TYR B O   1 
ATOM   3695  C  CB  . TYR B  1 157 ? -9.405  -19.720 39.653  1.00 18.47 ? 160  TYR B CB  1 
ATOM   3696  C  CG  . TYR B  1 157 ? -10.604 -19.033 39.019  1.00 17.80 ? 160  TYR B CG  1 
ATOM   3697  C  CD1 . TYR B  1 157 ? -10.456 -17.832 38.345  1.00 14.09 ? 160  TYR B CD1 1 
ATOM   3698  C  CD2 . TYR B  1 157 ? -11.889 -19.568 39.134  1.00 16.32 ? 160  TYR B CD2 1 
ATOM   3699  C  CE1 . TYR B  1 157 ? -11.528 -17.224 37.695  1.00 17.69 ? 160  TYR B CE1 1 
ATOM   3700  C  CE2 . TYR B  1 157 ? -12.992 -18.929 38.536  1.00 18.24 ? 160  TYR B CE2 1 
ATOM   3701  C  CZ  . TYR B  1 157 ? -12.791 -17.782 37.777  1.00 17.27 ? 160  TYR B CZ  1 
ATOM   3702  O  OH  . TYR B  1 157 ? -13.860 -17.097 37.228  1.00 14.29 ? 160  TYR B OH  1 
ATOM   3703  N  N   . ASN B  1 158 ? -10.930 -18.653 42.553  1.00 18.47 ? 161  ASN B N   1 
ATOM   3704  C  CA  . ASN B  1 158 ? -12.116 -18.925 43.342  1.00 14.61 ? 161  ASN B CA  1 
ATOM   3705  C  C   . ASN B  1 158 ? -13.139 -17.828 43.081  1.00 16.02 ? 161  ASN B C   1 
ATOM   3706  O  O   . ASN B  1 158 ? -12.925 -16.984 42.215  1.00 16.65 ? 161  ASN B O   1 
ATOM   3707  C  CB  . ASN B  1 158 ? -11.756 -19.099 44.837  1.00 15.69 ? 161  ASN B CB  1 
ATOM   3708  C  CG  . ASN B  1 158 ? -11.286 -17.803 45.514  1.00 20.20 ? 161  ASN B CG  1 
ATOM   3709  O  OD1 . ASN B  1 158 ? -11.558 -16.705 45.038  1.00 17.21 ? 161  ASN B OD1 1 
ATOM   3710  N  ND2 . ASN B  1 158 ? -10.626 -17.939 46.681  1.00 20.86 ? 161  ASN B ND2 1 
ATOM   3711  N  N   . LEU B  1 159 ? -14.279 -17.880 43.756  1.00 16.43 ? 162  LEU B N   1 
ATOM   3712  C  CA  . LEU B  1 159 ? -15.395 -17.023 43.412  1.00 16.77 ? 162  LEU B CA  1 
ATOM   3713  C  C   . LEU B  1 159 ? -15.049 -15.546 43.607  1.00 18.66 ? 162  LEU B C   1 
ATOM   3714  O  O   . LEU B  1 159 ? -15.648 -14.686 42.992  1.00 17.72 ? 162  LEU B O   1 
ATOM   3715  C  CB  . LEU B  1 159 ? -16.606 -17.381 44.272  1.00 19.05 ? 162  LEU B CB  1 
ATOM   3716  C  CG  . LEU B  1 159 ? -17.384 -18.628 43.865  1.00 18.44 ? 162  LEU B CG  1 
ATOM   3717  C  CD1 . LEU B  1 159 ? -18.565 -18.783 44.794  1.00 22.52 ? 162  LEU B CD1 1 
ATOM   3718  C  CD2 . LEU B  1 159 ? -17.882 -18.507 42.417  1.00 21.24 ? 162  LEU B CD2 1 
ATOM   3719  N  N   . THR B  1 160 ? -14.147 -15.251 44.537  1.00 16.21 ? 163  THR B N   1 
ATOM   3720  C  CA  . THR B  1 160 ? -13.735 -13.888 44.755  1.00 16.34 ? 163  THR B CA  1 
ATOM   3721  C  C   . THR B  1 160 ? -12.980 -13.388 43.523  1.00 18.98 ? 163  THR B C   1 
ATOM   3722  O  O   . THR B  1 160 ? -13.238 -12.287 43.024  1.00 18.41 ? 163  THR B O   1 
ATOM   3723  C  CB  . THR B  1 160 ? -12.839 -13.750 46.018  1.00 16.81 ? 163  THR B CB  1 
ATOM   3724  O  OG1 . THR B  1 160 ? -13.538 -14.270 47.162  1.00 14.89 ? 163  THR B OG1 1 
ATOM   3725  C  CG2 . THR B  1 160 ? -12.515 -12.291 46.281  1.00 13.55 ? 163  THR B CG2 1 
ATOM   3726  N  N   . VAL B  1 161 ? -12.078 -14.221 43.023  1.00 13.95 ? 164  VAL B N   1 
ATOM   3727  C  CA  . VAL B  1 161 ? -11.371 -13.966 41.783  1.00 15.13 ? 164  VAL B CA  1 
ATOM   3728  C  C   . VAL B  1 161 ? -12.305 -13.812 40.582  1.00 18.96 ? 164  VAL B C   1 
ATOM   3729  O  O   . VAL B  1 161 ? -12.152 -12.878 39.756  1.00 19.08 ? 164  VAL B O   1 
ATOM   3730  C  CB  . VAL B  1 161 ? -10.406 -15.105 41.472  1.00 14.07 ? 164  VAL B CB  1 
ATOM   3731  C  CG1 . VAL B  1 161 ? -9.567  -14.771 40.246  1.00 11.92 ? 164  VAL B CG1 1 
ATOM   3732  C  CG2 . VAL B  1 161 ? -9.528  -15.388 42.674  1.00 13.83 ? 164  VAL B CG2 1 
ATOM   3733  N  N   . ALA B  1 162 ? -13.255 -14.742 40.487  1.00 17.86 ? 165  ALA B N   1 
ATOM   3734  C  CA  . ALA B  1 162 ? -14.269 -14.711 39.443  1.00 16.91 ? 165  ALA B CA  1 
ATOM   3735  C  C   . ALA B  1 162 ? -15.002 -13.381 39.432  1.00 13.87 ? 165  ALA B C   1 
ATOM   3736  O  O   . ALA B  1 162 ? -15.236 -12.829 38.390  1.00 17.20 ? 165  ALA B O   1 
ATOM   3737  C  CB  . ALA B  1 162 ? -15.273 -15.882 39.621  1.00 14.11 ? 165  ALA B CB  1 
ATOM   3738  N  N   . GLY B  1 163 ? -15.384 -12.874 40.599  1.00 16.73 ? 166  GLY B N   1 
ATOM   3739  C  CA  . GLY B  1 163 ? -15.979 -11.540 40.677  1.00 16.34 ? 166  GLY B CA  1 
ATOM   3740  C  C   . GLY B  1 163 ? -15.106 -10.410 40.140  1.00 19.59 ? 166  GLY B C   1 
ATOM   3741  O  O   . GLY B  1 163 ? -15.613 -9.426  39.607  1.00 20.46 ? 166  GLY B O   1 
ATOM   3742  N  N   . GLU B  1 164 ? -13.797 -10.479 40.376  1.00 22.03 ? 167  GLU B N   1 
ATOM   3743  C  CA  . GLU B  1 164 ? -12.925 -9.389  39.964  1.00 19.34 ? 167  GLU B CA  1 
ATOM   3744  C  C   . GLU B  1 164 ? -12.604 -9.515  38.474  1.00 20.41 ? 167  GLU B C   1 
ATOM   3745  O  O   . GLU B  1 164 ? -12.641 -8.535  37.750  1.00 19.07 ? 167  GLU B O   1 
ATOM   3746  C  CB  . GLU B  1 164 ? -11.640 -9.364  40.788  1.00 21.17 ? 167  GLU B CB  1 
ATOM   3747  C  CG  . GLU B  1 164 ? -11.844 -9.060  42.257  1.00 23.61 ? 167  GLU B CG  1 
ATOM   3748  C  CD  . GLU B  1 164 ? -12.719 -7.840  42.481  1.00 27.64 ? 167  GLU B CD  1 
ATOM   3749  O  OE1 . GLU B  1 164 ? -12.397 -6.776  41.917  1.00 28.73 ? 167  GLU B OE1 1 
ATOM   3750  O  OE2 . GLU B  1 164 ? -13.725 -7.942  43.229  1.00 31.08 ? 167  GLU B OE2 1 
ATOM   3751  N  N   . LEU B  1 165 ? -12.380 -10.742 38.015  1.00 19.79 ? 168  LEU B N   1 
ATOM   3752  C  CA  . LEU B  1 165 ? -12.019 -10.981 36.628  1.00 21.58 ? 168  LEU B CA  1 
ATOM   3753  C  C   . LEU B  1 165 ? -13.207 -10.691 35.709  1.00 19.45 ? 168  LEU B C   1 
ATOM   3754  O  O   . LEU B  1 165 ? -13.047 -10.082 34.673  1.00 16.63 ? 168  LEU B O   1 
ATOM   3755  C  CB  . LEU B  1 165 ? -11.508 -12.422 36.425  1.00 17.83 ? 168  LEU B CB  1 
ATOM   3756  C  CG  . LEU B  1 165 ? -10.888 -12.701 35.046  1.00 19.63 ? 168  LEU B CG  1 
ATOM   3757  C  CD1 . LEU B  1 165 ? -9.693  -11.793 34.757  1.00 18.20 ? 168  LEU B CD1 1 
ATOM   3758  C  CD2 . LEU B  1 165 ? -10.510 -14.185 34.843  1.00 16.64 ? 168  LEU B CD2 1 
ATOM   3759  N  N   . ARG B  1 166 ? -14.409 -11.039 36.141  1.00 18.73 ? 169  ARG B N   1 
ATOM   3760  C  CA  . ARG B  1 166 ? -15.564 -10.896 35.265  1.00 19.40 ? 169  ARG B CA  1 
ATOM   3761  C  C   . ARG B  1 166 ? -15.760 -9.413  34.949  1.00 18.47 ? 169  ARG B C   1 
ATOM   3762  O  O   . ARG B  1 166 ? -16.020 -9.043  33.812  1.00 21.61 ? 169  ARG B O   1 
ATOM   3763  C  CB  . ARG B  1 166 ? -16.815 -11.514 35.908  1.00 19.36 ? 169  ARG B CB  1 
ATOM   3764  C  CG  . ARG B  1 166 ? -18.140 -10.804 35.561  1.00 18.52 ? 169  ARG B CG  1 
ATOM   3765  C  CD  . ARG B  1 166 ? -18.545 -10.943 34.076  1.00 16.60 ? 169  ARG B CD  1 
ATOM   3766  N  NE  . ARG B  1 166 ? -18.259 -12.260 33.480  1.00 17.58 ? 169  ARG B NE  1 
ATOM   3767  C  CZ  . ARG B  1 166 ? -17.494 -12.425 32.399  1.00 18.74 ? 169  ARG B CZ  1 
ATOM   3768  N  NH1 . ARG B  1 166 ? -16.875 -11.382 31.865  1.00 18.43 ? 169  ARG B NH1 1 
ATOM   3769  N  NH2 . ARG B  1 166 ? -17.324 -13.618 31.852  1.00 20.16 ? 169  ARG B NH2 1 
ATOM   3770  N  N   . PHE B  1 167 ? -15.533 -8.575  35.949  1.00 16.66 ? 170  PHE B N   1 
ATOM   3771  C  CA  . PHE B  1 167 ? -15.612 -7.120  35.820  1.00 17.89 ? 170  PHE B CA  1 
ATOM   3772  C  C   . PHE B  1 167 ? -14.469 -6.558  34.979  1.00 18.06 ? 170  PHE B C   1 
ATOM   3773  O  O   . PHE B  1 167 ? -14.682 -5.772  34.067  1.00 18.98 ? 170  PHE B O   1 
ATOM   3774  C  CB  . PHE B  1 167 ? -15.578 -6.487  37.219  1.00 17.70 ? 170  PHE B CB  1 
ATOM   3775  C  CG  . PHE B  1 167 ? -15.695 -4.988  37.212  1.00 19.54 ? 170  PHE B CG  1 
ATOM   3776  C  CD1 . PHE B  1 167 ? -16.833 -4.375  36.731  1.00 18.71 ? 170  PHE B CD1 1 
ATOM   3777  C  CD2 . PHE B  1 167 ? -14.684 -4.199  37.731  1.00 19.97 ? 170  PHE B CD2 1 
ATOM   3778  C  CE1 . PHE B  1 167 ? -16.950 -2.993  36.725  1.00 21.33 ? 170  PHE B CE1 1 
ATOM   3779  C  CE2 . PHE B  1 167 ? -14.804 -2.807  37.756  1.00 20.82 ? 170  PHE B CE2 1 
ATOM   3780  C  CZ  . PHE B  1 167 ? -15.936 -2.206  37.241  1.00 19.41 ? 170  PHE B CZ  1 
ATOM   3781  N  N   . LYS B  1 168 ? -13.250 -6.974  35.292  1.00 15.72 ? 171  LYS B N   1 
ATOM   3782  C  CA  . LYS B  1 168 ? -12.121 -6.641  34.467  1.00 19.56 ? 171  LYS B CA  1 
ATOM   3783  C  C   . LYS B  1 168 ? -12.383 -6.865  32.967  1.00 17.86 ? 171  LYS B C   1 
ATOM   3784  O  O   . LYS B  1 168 ? -12.066 -6.016  32.152  1.00 20.05 ? 171  LYS B O   1 
ATOM   3785  C  CB  . LYS B  1 168 ? -10.894 -7.432  34.913  1.00 18.90 ? 171  LYS B CB  1 
ATOM   3786  C  CG  . LYS B  1 168 ? -9.691  -7.199  34.065  1.00 19.17 ? 171  LYS B CG  1 
ATOM   3787  C  CD  . LYS B  1 168 ? -9.298  -5.748  34.076  1.00 22.15 ? 171  LYS B CD  1 
ATOM   3788  C  CE  . LYS B  1 168 ? -8.074  -5.558  33.176  1.00 27.48 ? 171  LYS B CE  1 
ATOM   3789  N  NZ  . LYS B  1 168 ? -7.456  -4.237  33.433  1.00 29.41 ? 171  LYS B NZ  1 
ATOM   3790  N  N   . ARG B  1 169 ? -12.852 -8.049  32.602  1.00 16.67 ? 172  ARG B N   1 
ATOM   3791  C  CA  . ARG B  1 169 ? -13.081 -8.374  31.190  1.00 17.04 ? 172  ARG B CA  1 
ATOM   3792  C  C   . ARG B  1 169 ? -14.147 -7.495  30.533  1.00 15.45 ? 172  ARG B C   1 
ATOM   3793  O  O   . ARG B  1 169 ? -14.047 -7.168  29.357  1.00 17.97 ? 172  ARG B O   1 
ATOM   3794  C  CB  . ARG B  1 169 ? -13.408 -9.863  31.013  1.00 15.45 ? 172  ARG B CB  1 
ATOM   3795  C  CG  . ARG B  1 169 ? -12.234 -10.775 31.382  1.00 16.44 ? 172  ARG B CG  1 
ATOM   3796  C  CD  . ARG B  1 169 ? -11.056 -10.566 30.413  1.00 17.25 ? 172  ARG B CD  1 
ATOM   3797  N  NE  . ARG B  1 169 ? -11.417 -11.039 29.091  1.00 16.99 ? 172  ARG B NE  1 
ATOM   3798  C  CZ  . ARG B  1 169 ? -11.478 -10.290 28.001  1.00 18.19 ? 172  ARG B CZ  1 
ATOM   3799  N  NH1 . ARG B  1 169 ? -11.017 -9.028  28.020  1.00 17.74 ? 172  ARG B NH1 1 
ATOM   3800  N  NH2 . ARG B  1 169 ? -11.978 -10.821 26.878  1.00 14.86 ? 172  ARG B NH2 1 
ATOM   3801  N  N   . ILE B  1 170 ? -15.139 -7.073  31.307  1.00 11.88 ? 173  ILE B N   1 
ATOM   3802  C  CA  . ILE B  1 170 ? -16.162 -6.186  30.800  1.00 14.63 ? 173  ILE B CA  1 
ATOM   3803  C  C   . ILE B  1 170 ? -15.552 -4.788  30.541  1.00 16.97 ? 173  ILE B C   1 
ATOM   3804  O  O   . ILE B  1 170 ? -15.767 -4.193  29.482  1.00 19.19 ? 173  ILE B O   1 
ATOM   3805  C  CB  . ILE B  1 170 ? -17.317 -6.084  31.823  1.00 16.02 ? 173  ILE B CB  1 
ATOM   3806  C  CG1 . ILE B  1 170 ? -18.108 -7.392  31.890  1.00 10.00 ? 173  ILE B CG1 1 
ATOM   3807  C  CG2 . ILE B  1 170 ? -18.251 -4.922  31.508  1.00 9.74  ? 173  ILE B CG2 1 
ATOM   3808  C  CD1 . ILE B  1 170 ? -18.888 -7.496  33.225  1.00 10.07 ? 173  ILE B CD1 1 
ATOM   3809  N  N   . GLN B  1 171 ? -14.725 -4.314  31.471  1.00 15.34 ? 174  GLN B N   1 
ATOM   3810  C  CA  A GLN B  1 171 ? -14.000 -3.047  31.322  0.50 17.48 ? 174  GLN B CA  1 
ATOM   3811  C  CA  B GLN B  1 171 ? -14.055 -3.037  31.286  0.50 18.09 ? 174  GLN B CA  1 
ATOM   3812  C  C   . GLN B  1 171 ? -13.084 -3.071  30.117  1.00 17.65 ? 174  GLN B C   1 
ATOM   3813  O  O   . GLN B  1 171 ? -12.985 -2.100  29.405  1.00 19.85 ? 174  GLN B O   1 
ATOM   3814  C  CB  A GLN B  1 171 ? -13.133 -2.760  32.553  0.50 17.04 ? 174  GLN B CB  1 
ATOM   3815  C  CB  B GLN B  1 171 ? -13.353 -2.575  32.571  0.50 18.91 ? 174  GLN B CB  1 
ATOM   3816  C  CG  A GLN B  1 171 ? -13.870 -2.297  33.789  0.50 18.34 ? 174  GLN B CG  1 
ATOM   3817  C  CG  B GLN B  1 171 ? -14.285 -2.443  33.773  0.50 21.49 ? 174  GLN B CG  1 
ATOM   3818  C  CD  A GLN B  1 171 ? -12.906 -1.909  34.896  0.50 19.75 ? 174  GLN B CD  1 
ATOM   3819  C  CD  B GLN B  1 171 ? -15.126 -1.181  33.733  0.50 23.97 ? 174  GLN B CD  1 
ATOM   3820  O  OE1 A GLN B  1 171 ? -12.851 -0.748  35.300  0.50 18.93 ? 174  GLN B OE1 1 
ATOM   3821  O  OE1 B GLN B  1 171 ? -16.307 -1.223  33.389  0.50 26.92 ? 174  GLN B OE1 1 
ATOM   3822  N  NE2 A GLN B  1 171 ? -12.069 -2.864  35.322  0.50 18.53 ? 174  GLN B NE2 1 
ATOM   3823  N  NE2 B GLN B  1 171 ? -14.536 -0.059  34.136  0.50 23.00 ? 174  GLN B NE2 1 
ATOM   3824  N  N   . ASP B  1 172 ? -12.342 -4.171  29.959  1.00 19.41 ? 175  ASP B N   1 
ATOM   3825  C  CA  . ASP B  1 172 ? -11.456 -4.367  28.802  1.00 19.74 ? 175  ASP B CA  1 
ATOM   3826  C  C   . ASP B  1 172 ? -12.218 -4.175  27.485  1.00 19.34 ? 175  ASP B C   1 
ATOM   3827  O  O   . ASP B  1 172 ? -11.796 -3.400  26.607  1.00 19.39 ? 175  ASP B O   1 
ATOM   3828  C  CB  . ASP B  1 172 ? -10.810 -5.769  28.804  1.00 19.43 ? 175  ASP B CB  1 
ATOM   3829  C  CG  . ASP B  1 172 ? -9.705  -5.939  29.870  1.00 26.67 ? 175  ASP B CG  1 
ATOM   3830  O  OD1 . ASP B  1 172 ? -9.219  -4.912  30.415  1.00 28.62 ? 175  ASP B OD1 1 
ATOM   3831  O  OD2 . ASP B  1 172 ? -9.220  -7.098  30.057  1.00 26.29 ? 175  ASP B OD2 1 
ATOM   3832  N  N   . SER B  1 173 ? -13.321 -4.905  27.327  1.00 17.13 ? 176  SER B N   1 
ATOM   3833  C  CA  . SER B  1 173 ? -14.117 -4.836  26.080  1.00 16.31 ? 176  SER B CA  1 
ATOM   3834  C  C   . SER B  1 173 ? -14.727 -3.444  25.840  1.00 17.20 ? 176  SER B C   1 
ATOM   3835  O  O   . SER B  1 173 ? -14.733 -2.943  24.714  1.00 17.32 ? 176  SER B O   1 
ATOM   3836  C  CB  . SER B  1 173 ? -15.225 -5.889  26.100  1.00 14.48 ? 176  SER B CB  1 
ATOM   3837  O  OG  . SER B  1 173 ? -14.651 -7.187  26.066  1.00 18.46 ? 176  SER B OG  1 
ATOM   3838  N  N   . ILE B  1 174 ? -15.227 -2.819  26.903  1.00 17.79 ? 177  ILE B N   1 
ATOM   3839  C  CA  . ILE B  1 174 ? -15.719 -1.446  26.792  1.00 19.58 ? 177  ILE B CA  1 
ATOM   3840  C  C   . ILE B  1 174 ? -14.604 -0.562  26.258  1.00 22.10 ? 177  ILE B C   1 
ATOM   3841  O  O   . ILE B  1 174 ? -14.818 0.145   25.288  1.00 23.92 ? 177  ILE B O   1 
ATOM   3842  C  CB  . ILE B  1 174 ? -16.234 -0.902  28.143  1.00 20.56 ? 177  ILE B CB  1 
ATOM   3843  C  CG1 . ILE B  1 174 ? -17.515 -1.632  28.566  1.00 20.57 ? 177  ILE B CG1 1 
ATOM   3844  C  CG2 . ILE B  1 174 ? -16.486 0.595   28.081  1.00 21.15 ? 177  ILE B CG2 1 
ATOM   3845  C  CD1 . ILE B  1 174 ? -18.063 -1.194  29.945  1.00 15.21 ? 177  ILE B CD1 1 
ATOM   3846  N  N   . ALA B  1 175 ? -13.381 -0.718  26.778  1.00 17.36 ? 178  ALA B N   1 
ATOM   3847  C  CA  . ALA B  1 175 ? -12.307 0.218   26.433  1.00 20.56 ? 178  ALA B CA  1 
ATOM   3848  C  C   . ALA B  1 175 ? -11.745 -0.031  25.033  1.00 20.69 ? 178  ALA B C   1 
ATOM   3849  O  O   . ALA B  1 175 ? -11.118 0.849   24.466  1.00 20.26 ? 178  ALA B O   1 
ATOM   3850  C  CB  . ALA B  1 175 ? -11.174 0.187   27.481  1.00 17.12 ? 178  ALA B CB  1 
ATOM   3851  N  N   . THR B  1 176 ? -11.942 -1.241  24.502  1.00 22.88 ? 179  THR B N   1 
ATOM   3852  C  CA  . THR B  1 176 ? -11.230 -1.693  23.304  1.00 21.38 ? 179  THR B CA  1 
ATOM   3853  C  C   . THR B  1 176 ? -12.117 -2.164  22.139  1.00 23.03 ? 179  THR B C   1 
ATOM   3854  O  O   . THR B  1 176 ? -11.664 -2.196  21.000  1.00 24.06 ? 179  THR B O   1 
ATOM   3855  C  CB  . THR B  1 176 ? -10.175 -2.785  23.623  1.00 25.67 ? 179  THR B CB  1 
ATOM   3856  O  OG1 . THR B  1 176 ? -10.806 -3.980  24.112  1.00 24.95 ? 179  THR B OG1 1 
ATOM   3857  C  CG2 . THR B  1 176 ? -9.172  -2.297  24.648  1.00 24.41 ? 179  THR B CG2 1 
ATOM   3858  N  N   . ASN B  1 177 ? -13.316 -2.671  22.436  1.00 23.08 ? 180  ASN B N   1 
ATOM   3859  C  CA  . ASN B  1 177 ? -14.187 -3.232  21.398  1.00 21.90 ? 180  ASN B CA  1 
ATOM   3860  C  C   . ASN B  1 177 ? -15.415 -2.349  21.092  1.00 21.39 ? 180  ASN B C   1 
ATOM   3861  O  O   . ASN B  1 177 ? -16.381 -2.317  21.875  1.00 19.37 ? 180  ASN B O   1 
ATOM   3862  C  CB  . ASN B  1 177 ? -14.632 -4.652  21.769  1.00 21.95 ? 180  ASN B CB  1 
ATOM   3863  C  CG  . ASN B  1 177 ? -15.608 -5.244  20.765  1.00 23.29 ? 180  ASN B CG  1 
ATOM   3864  O  OD1 . ASN B  1 177 ? -15.877 -4.650  19.727  1.00 25.35 ? 180  ASN B OD1 1 
ATOM   3865  N  ND2 . ASN B  1 177 ? -16.147 -6.415  21.077  1.00 21.68 ? 180  ASN B ND2 1 
ATOM   3866  N  N   . PRO B  1 178 ? -15.375 -1.619  19.960  1.00 18.07 ? 181  PRO B N   1 
ATOM   3867  C  CA  . PRO B  1 178 ? -16.411 -0.619  19.617  1.00 20.38 ? 181  PRO B CA  1 
ATOM   3868  C  C   . PRO B  1 178 ? -17.750 -1.302  19.340  1.00 22.59 ? 181  PRO B C   1 
ATOM   3869  O  O   . PRO B  1 178 ? -18.776 -0.642  19.269  1.00 24.25 ? 181  PRO B O   1 
ATOM   3870  C  CB  . PRO B  1 178 ? -15.882 0.008   18.323  1.00 17.53 ? 181  PRO B CB  1 
ATOM   3871  C  CG  . PRO B  1 178 ? -14.927 -1.019  17.762  1.00 20.98 ? 181  PRO B CG  1 
ATOM   3872  C  CD  . PRO B  1 178 ? -14.283 -1.637  18.977  1.00 19.72 ? 181  PRO B CD  1 
ATOM   3873  N  N   . ASN B  1 179 ? -17.710 -2.627  19.223  1.00 22.47 ? 182  ASN B N   1 
ATOM   3874  C  CA  . ASN B  1 179 ? -18.886 -3.445  18.978  1.00 22.01 ? 182  ASN B CA  1 
ATOM   3875  C  C   . ASN B  1 179 ? -19.324 -4.244  20.199  1.00 20.92 ? 182  ASN B C   1 
ATOM   3876  O  O   . ASN B  1 179 ? -20.062 -5.222  20.062  1.00 20.24 ? 182  ASN B O   1 
ATOM   3877  C  CB  . ASN B  1 179 ? -18.565 -4.435  17.868  1.00 24.85 ? 182  ASN B CB  1 
ATOM   3878  C  CG  . ASN B  1 179 ? -18.664 -3.820  16.491  1.00 26.16 ? 182  ASN B CG  1 
ATOM   3879  O  OD1 . ASN B  1 179 ? -18.768 -2.604  16.335  1.00 25.03 ? 182  ASN B OD1 1 
ATOM   3880  N  ND2 . ASN B  1 179 ? -18.646 -4.661  15.486  1.00 32.36 ? 182  ASN B ND2 1 
ATOM   3881  N  N   . PHE B  1 180 ? -18.773 -3.914  21.367  1.00 17.24 ? 183  PHE B N   1 
ATOM   3882  C  CA  . PHE B  1 180 ? -19.050 -4.681  22.570  1.00 18.64 ? 183  PHE B CA  1 
ATOM   3883  C  C   . PHE B  1 180 ? -20.550 -4.761  22.790  1.00 20.51 ? 183  PHE B C   1 
ATOM   3884  O  O   . PHE B  1 180 ? -21.227 -3.742  22.862  1.00 26.35 ? 183  PHE B O   1 
ATOM   3885  C  CB  . PHE B  1 180 ? -18.376 -4.068  23.792  1.00 15.77 ? 183  PHE B CB  1 
ATOM   3886  C  CG  . PHE B  1 180 ? -18.636 -4.808  25.069  1.00 16.39 ? 183  PHE B CG  1 
ATOM   3887  C  CD1 . PHE B  1 180 ? -18.498 -6.188  25.126  1.00 18.38 ? 183  PHE B CD1 1 
ATOM   3888  C  CD2 . PHE B  1 180 ? -18.897 -4.111  26.248  1.00 17.17 ? 183  PHE B CD2 1 
ATOM   3889  C  CE1 . PHE B  1 180 ? -18.679 -6.869  26.325  1.00 20.21 ? 183  PHE B CE1 1 
ATOM   3890  C  CE2 . PHE B  1 180 ? -19.070 -4.778  27.456  1.00 15.98 ? 183  PHE B CE2 1 
ATOM   3891  C  CZ  . PHE B  1 180 ? -18.959 -6.159  27.494  1.00 18.94 ? 183  PHE B CZ  1 
ATOM   3892  N  N   . SER B  1 181 ? -21.038 -5.967  23.012  1.00 16.44 ? 184  SER B N   1 
ATOM   3893  C  CA  . SER B  1 181 ? -22.450 -6.175  23.275  1.00 21.33 ? 184  SER B CA  1 
ATOM   3894  C  C   . SER B  1 181 ? -22.516 -7.046  24.492  1.00 15.95 ? 184  SER B C   1 
ATOM   3895  O  O   . SER B  1 181 ? -21.773 -8.004  24.603  1.00 18.53 ? 184  SER B O   1 
ATOM   3896  C  CB  . SER B  1 181 ? -23.134 -6.891  22.085  1.00 21.20 ? 184  SER B CB  1 
ATOM   3897  O  OG  . SER B  1 181 ? -24.452 -7.280  22.434  1.00 22.05 ? 184  SER B OG  1 
ATOM   3898  N  N   . PHE B  1 182 ? -23.353 -6.674  25.440  1.00 18.83 ? 185  PHE B N   1 
ATOM   3899  C  CA  . PHE B  1 182 ? -23.411 -7.383  26.712  1.00 17.50 ? 185  PHE B CA  1 
ATOM   3900  C  C   . PHE B  1 182 ? -24.824 -7.279  27.270  1.00 18.92 ? 185  PHE B C   1 
ATOM   3901  O  O   . PHE B  1 182 ? -25.037 -6.709  28.346  1.00 22.85 ? 185  PHE B O   1 
ATOM   3902  C  CB  . PHE B  1 182 ? -22.417 -6.761  27.696  1.00 17.35 ? 185  PHE B CB  1 
ATOM   3903  C  CG  . PHE B  1 182 ? -21.990 -7.693  28.818  1.00 17.96 ? 185  PHE B CG  1 
ATOM   3904  C  CD1 . PHE B  1 182 ? -21.263 -8.846  28.545  1.00 14.60 ? 185  PHE B CD1 1 
ATOM   3905  C  CD2 . PHE B  1 182 ? -22.248 -7.366  30.143  1.00 18.16 ? 185  PHE B CD2 1 
ATOM   3906  C  CE1 . PHE B  1 182 ? -20.807 -9.662  29.580  1.00 17.95 ? 185  PHE B CE1 1 
ATOM   3907  C  CE2 . PHE B  1 182 ? -21.756 -8.149  31.186  1.00 19.11 ? 185  PHE B CE2 1 
ATOM   3908  C  CZ  . PHE B  1 182 ? -21.064 -9.320  30.902  1.00 18.88 ? 185  PHE B CZ  1 
ATOM   3909  N  N   . VAL B  1 183 ? -25.793 -7.796  26.520  1.00 15.57 ? 186  VAL B N   1 
ATOM   3910  C  CA  . VAL B  1 183 ? -27.182 -7.750  26.927  1.00 14.79 ? 186  VAL B CA  1 
ATOM   3911  C  C   . VAL B  1 183 ? -27.821 -9.128  26.998  1.00 17.57 ? 186  VAL B C   1 
ATOM   3912  O  O   . VAL B  1 183 ? -27.247 -10.137 26.544  1.00 16.84 ? 186  VAL B O   1 
ATOM   3913  C  CB  . VAL B  1 183 ? -28.017 -6.873  25.955  1.00 18.66 ? 186  VAL B CB  1 
ATOM   3914  C  CG1 . VAL B  1 183 ? -27.565 -5.442  26.025  1.00 15.89 ? 186  VAL B CG1 1 
ATOM   3915  C  CG2 . VAL B  1 183 ? -27.922 -7.418  24.500  1.00 20.26 ? 186  VAL B CG2 1 
ATOM   3916  N  N   . ASP B  1 184 ? -29.035 -9.174  27.543  1.00 17.54 ? 187  ASP B N   1 
ATOM   3917  C  CA  . ASP B  1 184 ? -29.872 -10.364 27.393  1.00 19.54 ? 187  ASP B CA  1 
ATOM   3918  C  C   . ASP B  1 184 ? -29.095 -11.675 27.641  1.00 20.58 ? 187  ASP B C   1 
ATOM   3919  O  O   . ASP B  1 184 ? -28.535 -11.885 28.724  1.00 21.59 ? 187  ASP B O   1 
ATOM   3920  C  CB  . ASP B  1 184 ? -30.528 -10.361 26.007  1.00 22.46 ? 187  ASP B CB  1 
ATOM   3921  C  CG  . ASP B  1 184 ? -31.427 -9.131  25.782  1.00 28.29 ? 187  ASP B CG  1 
ATOM   3922  O  OD1 . ASP B  1 184 ? -32.393 -8.940  26.566  1.00 28.92 ? 187  ASP B OD1 1 
ATOM   3923  O  OD2 . ASP B  1 184 ? -31.190 -8.376  24.805  1.00 28.57 ? 187  ASP B OD2 1 
ATOM   3924  N  N   . PHE B  1 185 ? -29.143 -12.598 26.683  1.00 21.79 ? 188  PHE B N   1 
ATOM   3925  C  CA  . PHE B  1 185 ? -28.679 -13.967 26.932  1.00 20.53 ? 188  PHE B CA  1 
ATOM   3926  C  C   . PHE B  1 185 ? -27.184 -14.008 27.289  1.00 16.69 ? 188  PHE B C   1 
ATOM   3927  O  O   . PHE B  1 185 ? -26.766 -14.744 28.162  1.00 19.22 ? 188  PHE B O   1 
ATOM   3928  C  CB  . PHE B  1 185 ? -28.997 -14.893 25.737  1.00 20.94 ? 188  PHE B CB  1 
ATOM   3929  C  CG  . PHE B  1 185 ? -28.842 -16.374 26.046  1.00 21.55 ? 188  PHE B CG  1 
ATOM   3930  C  CD1 . PHE B  1 185 ? -29.637 -16.987 26.991  1.00 23.59 ? 188  PHE B CD1 1 
ATOM   3931  C  CD2 . PHE B  1 185 ? -27.844 -17.117 25.458  1.00 22.11 ? 188  PHE B CD2 1 
ATOM   3932  C  CE1 . PHE B  1 185 ? -29.488 -18.333 27.274  1.00 24.41 ? 188  PHE B CE1 1 
ATOM   3933  C  CE2 . PHE B  1 185 ? -27.636 -18.447 25.805  1.00 21.49 ? 188  PHE B CE2 1 
ATOM   3934  C  CZ  . PHE B  1 185 ? -28.465 -19.057 26.693  1.00 22.93 ? 188  PHE B CZ  1 
ATOM   3935  N  N   . ARG B  1 186 ? -26.409 -13.138 26.670  1.00 16.43 ? 189  ARG B N   1 
ATOM   3936  C  CA  . ARG B  1 186 ? -24.984 -13.060 26.931  1.00 17.04 ? 189  ARG B CA  1 
ATOM   3937  C  C   . ARG B  1 186 ? -24.695 -12.454 28.292  1.00 17.01 ? 189  ARG B C   1 
ATOM   3938  O  O   . ARG B  1 186 ? -23.933 -13.019 29.066  1.00 19.53 ? 189  ARG B O   1 
ATOM   3939  C  CB  . ARG B  1 186 ? -24.259 -12.265 25.842  1.00 12.41 ? 189  ARG B CB  1 
ATOM   3940  C  CG  . ARG B  1 186 ? -22.745 -12.218 26.078  1.00 17.33 ? 189  ARG B CG  1 
ATOM   3941  C  CD  . ARG B  1 186 ? -22.126 -13.649 26.320  1.00 14.06 ? 189  ARG B CD  1 
ATOM   3942  N  NE  . ARG B  1 186 ? -20.722 -13.569 26.755  1.00 14.78 ? 189  ARG B NE  1 
ATOM   3943  C  CZ  . ARG B  1 186 ? -20.051 -14.525 27.416  1.00 15.17 ? 189  ARG B CZ  1 
ATOM   3944  N  NH1 . ARG B  1 186 ? -20.593 -15.724 27.659  1.00 9.73  ? 189  ARG B NH1 1 
ATOM   3945  N  NH2 . ARG B  1 186 ? -18.809 -14.288 27.811  1.00 12.40 ? 189  ARG B NH2 1 
ATOM   3946  N  N   . PHE B  1 187 ? -25.303 -11.305 28.584  1.00 18.97 ? 190  PHE B N   1 
ATOM   3947  C  CA  . PHE B  1 187 ? -25.326 -10.798 29.951  1.00 19.66 ? 190  PHE B CA  1 
ATOM   3948  C  C   . PHE B  1 187 ? -25.565 -11.901 30.984  1.00 20.34 ? 190  PHE B C   1 
ATOM   3949  O  O   . PHE B  1 187 ? -24.901 -11.954 32.019  1.00 23.86 ? 190  PHE B O   1 
ATOM   3950  C  CB  . PHE B  1 187 ? -26.375 -9.706  30.129  1.00 17.04 ? 190  PHE B CB  1 
ATOM   3951  C  CG  . PHE B  1 187 ? -26.318 -9.036  31.477  1.00 17.14 ? 190  PHE B CG  1 
ATOM   3952  C  CD1 . PHE B  1 187 ? -25.324 -8.099  31.761  1.00 13.43 ? 190  PHE B CD1 1 
ATOM   3953  C  CD2 . PHE B  1 187 ? -27.238 -9.355  32.471  1.00 16.15 ? 190  PHE B CD2 1 
ATOM   3954  C  CE1 . PHE B  1 187 ? -25.288 -7.452  32.982  1.00 14.22 ? 190  PHE B CE1 1 
ATOM   3955  C  CE2 . PHE B  1 187 ? -27.158 -8.764  33.735  1.00 12.53 ? 190  PHE B CE2 1 
ATOM   3956  C  CZ  . PHE B  1 187 ? -26.192 -7.810  33.990  1.00 12.27 ? 190  PHE B CZ  1 
ATOM   3957  N  N   . PHE B  1 188 ? -26.518 -12.781 30.715  1.00 19.02 ? 191  PHE B N   1 
ATOM   3958  C  CA  . PHE B  1 188 ? -26.874 -13.778 31.716  1.00 17.50 ? 191  PHE B CA  1 
ATOM   3959  C  C   . PHE B  1 188 ? -25.837 -14.869 31.857  1.00 18.13 ? 191  PHE B C   1 
ATOM   3960  O  O   . PHE B  1 188 ? -25.420 -15.180 32.964  1.00 21.29 ? 191  PHE B O   1 
ATOM   3961  C  CB  . PHE B  1 188 ? -28.251 -14.361 31.446  1.00 20.42 ? 191  PHE B CB  1 
ATOM   3962  C  CG  . PHE B  1 188 ? -28.597 -15.523 32.319  1.00 26.66 ? 191  PHE B CG  1 
ATOM   3963  C  CD1 . PHE B  1 188 ? -29.253 -15.326 33.535  1.00 28.93 ? 191  PHE B CD1 1 
ATOM   3964  C  CD2 . PHE B  1 188 ? -28.318 -16.819 31.911  1.00 26.97 ? 191  PHE B CD2 1 
ATOM   3965  C  CE1 . PHE B  1 188 ? -29.571 -16.405 34.350  1.00 30.75 ? 191  PHE B CE1 1 
ATOM   3966  C  CE2 . PHE B  1 188 ? -28.674 -17.905 32.702  1.00 32.06 ? 191  PHE B CE2 1 
ATOM   3967  C  CZ  . PHE B  1 188 ? -29.275 -17.697 33.936  1.00 30.61 ? 191  PHE B CZ  1 
ATOM   3968  N  N   . THR B  1 189 ? -25.406 -15.454 30.743  1.00 18.42 ? 192  THR B N   1 
ATOM   3969  C  CA  . THR B  1 189 ? -24.509 -16.607 30.796  1.00 19.37 ? 192  THR B CA  1 
ATOM   3970  C  C   . THR B  1 189 ? -23.070 -16.210 31.180  1.00 19.51 ? 192  THR B C   1 
ATOM   3971  O  O   . THR B  1 189 ? -22.303 -17.028 31.687  1.00 18.67 ? 192  THR B O   1 
ATOM   3972  C  CB  . THR B  1 189 ? -24.509 -17.372 29.440  1.00 22.72 ? 192  THR B CB  1 
ATOM   3973  O  OG1 . THR B  1 189 ? -24.105 -16.483 28.395  1.00 18.72 ? 192  THR B OG1 1 
ATOM   3974  C  CG2 . THR B  1 189 ? -25.932 -17.906 29.102  1.00 22.35 ? 192  THR B CG2 1 
ATOM   3975  N  N   . ALA B  1 190 ? -22.692 -14.977 30.852  1.00 17.92 ? 193  ALA B N   1 
ATOM   3976  C  CA  . ALA B  1 190 ? -21.366 -14.445 31.183  1.00 17.64 ? 193  ALA B CA  1 
ATOM   3977  C  C   . ALA B  1 190 ? -21.012 -14.520 32.681  1.00 16.93 ? 193  ALA B C   1 
ATOM   3978  O  O   . ALA B  1 190 ? -19.881 -14.802 33.027  1.00 19.13 ? 193  ALA B O   1 
ATOM   3979  C  CB  . ALA B  1 190 ? -21.251 -13.009 30.695  1.00 15.34 ? 193  ALA B CB  1 
ATOM   3980  N  N   . TYR B  1 191 ? -21.959 -14.211 33.561  1.00 17.88 ? 194  TYR B N   1 
ATOM   3981  C  CA  . TYR B  1 191 ? -21.746 -14.348 35.007  1.00 15.43 ? 194  TYR B CA  1 
ATOM   3982  C  C   . TYR B  1 191 ? -21.664 -15.814 35.458  1.00 17.98 ? 194  TYR B C   1 
ATOM   3983  O  O   . TYR B  1 191 ? -20.717 -16.202 36.126  1.00 19.07 ? 194  TYR B O   1 
ATOM   3984  C  CB  . TYR B  1 191 ? -22.824 -13.600 35.769  1.00 12.21 ? 194  TYR B CB  1 
ATOM   3985  C  CG  . TYR B  1 191 ? -22.576 -12.122 35.784  1.00 12.09 ? 194  TYR B CG  1 
ATOM   3986  C  CD1 . TYR B  1 191 ? -22.904 -11.337 34.682  1.00 9.46  ? 194  TYR B CD1 1 
ATOM   3987  C  CD2 . TYR B  1 191 ? -21.831 -11.538 36.812  1.00 13.16 ? 194  TYR B CD2 1 
ATOM   3988  C  CE1 . TYR B  1 191 ? -22.571 -9.992  34.639  1.00 15.13 ? 194  TYR B CE1 1 
ATOM   3989  C  CE2 . TYR B  1 191 ? -21.486 -10.187 36.768  1.00 14.34 ? 194  TYR B CE2 1 
ATOM   3990  C  CZ  . TYR B  1 191 ? -21.867 -9.427  35.689  1.00 14.54 ? 194  TYR B CZ  1 
ATOM   3991  O  OH  . TYR B  1 191 ? -21.540 -8.098  35.643  1.00 20.20 ? 194  TYR B OH  1 
ATOM   3992  N  N   . GLY B  1 192 ? -22.614 -16.639 35.019  1.00 17.03 ? 195  GLY B N   1 
ATOM   3993  C  CA  . GLY B  1 192 ? -22.648 -18.057 35.406  1.00 16.08 ? 195  GLY B CA  1 
ATOM   3994  C  C   . GLY B  1 192 ? -21.359 -18.789 35.076  1.00 12.89 ? 195  GLY B C   1 
ATOM   3995  O  O   . GLY B  1 192 ? -20.769 -19.441 35.936  1.00 19.87 ? 195  GLY B O   1 
ATOM   3996  N  N   . GLU B  1 193 ? -20.846 -18.543 33.881  1.00 11.35 ? 196  GLU B N   1 
ATOM   3997  C  CA  . GLU B  1 193 ? -19.624 -19.174 33.389  1.00 12.32 ? 196  GLU B CA  1 
ATOM   3998  C  C   . GLU B  1 193 ? -18.396 -18.945 34.263  1.00 14.16 ? 196  GLU B C   1 
ATOM   3999  O  O   . GLU B  1 193 ? -17.558 -19.835 34.404  1.00 17.26 ? 196  GLU B O   1 
ATOM   4000  C  CB  . GLU B  1 193 ? -19.355 -18.742 31.945  1.00 11.74 ? 196  GLU B CB  1 
ATOM   4001  C  CG  . GLU B  1 193 ? -20.321 -19.426 30.968  1.00 14.00 ? 196  GLU B CG  1 
ATOM   4002  C  CD  . GLU B  1 193 ? -20.543 -18.679 29.673  1.00 15.85 ? 196  GLU B CD  1 
ATOM   4003  O  OE1 . GLU B  1 193 ? -19.810 -17.704 29.383  1.00 11.91 ? 196  GLU B OE1 1 
ATOM   4004  O  OE2 . GLU B  1 193 ? -21.465 -19.101 28.925  1.00 20.70 ? 196  GLU B OE2 1 
ATOM   4005  N  N   . THR B  1 194 ? -18.339 -17.815 34.949  1.00 12.28 ? 197  THR B N   1 
ATOM   4006  C  CA  . THR B  1 194 ? -17.154 -17.512 35.731  1.00 15.79 ? 197  THR B CA  1 
ATOM   4007  C  C   . THR B  1 194 ? -17.162 -18.269 37.052  1.00 14.80 ? 197  THR B C   1 
ATOM   4008  O  O   . THR B  1 194 ? -16.126 -18.476 37.653  1.00 17.50 ? 197  THR B O   1 
ATOM   4009  C  CB  . THR B  1 194 ? -16.983 -15.975 35.972  1.00 18.73 ? 197  THR B CB  1 
ATOM   4010  O  OG1 . THR B  1 194 ? -18.056 -15.482 36.793  1.00 19.85 ? 197  THR B OG1 1 
ATOM   4011  C  CG2 . THR B  1 194 ? -17.005 -15.251 34.661  1.00 15.47 ? 197  THR B CG2 1 
ATOM   4012  N  N   . THR B  1 195 ? -18.322 -18.754 37.464  1.00 16.48 ? 198  THR B N   1 
ATOM   4013  C  CA  . THR B  1 195 ? -18.385 -19.673 38.590  1.00 14.37 ? 198  THR B CA  1 
ATOM   4014  C  C   . THR B  1 195 ? -17.902 -21.083 38.251  1.00 17.88 ? 198  THR B C   1 
ATOM   4015  O  O   . THR B  1 195 ? -17.398 -21.771 39.131  1.00 19.17 ? 198  THR B O   1 
ATOM   4016  C  CB  . THR B  1 195 ? -19.798 -19.772 39.190  1.00 14.73 ? 198  THR B CB  1 
ATOM   4017  O  OG1 . THR B  1 195 ? -20.640 -20.577 38.353  1.00 16.13 ? 198  THR B OG1 1 
ATOM   4018  C  CG2 . THR B  1 195 ? -20.416 -18.395 39.352  1.00 12.04 ? 198  THR B CG2 1 
ATOM   4019  N  N   . PHE B  1 196 ? -18.091 -21.534 37.004  1.00 18.44 ? 199  PHE B N   1 
ATOM   4020  C  CA  . PHE B  1 196 ? -17.964 -22.976 36.693  1.00 12.06 ? 199  PHE B CA  1 
ATOM   4021  C  C   . PHE B  1 196 ? -16.578 -23.525 37.012  1.00 13.38 ? 199  PHE B C   1 
ATOM   4022  O  O   . PHE B  1 196 ? -16.449 -24.687 37.420  1.00 16.96 ? 199  PHE B O   1 
ATOM   4023  C  CB  . PHE B  1 196 ? -18.337 -23.337 35.234  1.00 14.51 ? 199  PHE B CB  1 
ATOM   4024  C  CG  . PHE B  1 196 ? -19.779 -23.018 34.830  1.00 14.42 ? 199  PHE B CG  1 
ATOM   4025  C  CD1 . PHE B  1 196 ? -20.769 -22.795 35.768  1.00 15.28 ? 199  PHE B CD1 1 
ATOM   4026  C  CD2 . PHE B  1 196 ? -20.138 -22.988 33.483  1.00 17.27 ? 199  PHE B CD2 1 
ATOM   4027  C  CE1 . PHE B  1 196 ? -22.091 -22.445 35.374  1.00 16.08 ? 199  PHE B CE1 1 
ATOM   4028  C  CE2 . PHE B  1 196 ? -21.446 -22.630 33.068  1.00 16.83 ? 199  PHE B CE2 1 
ATOM   4029  C  CZ  . PHE B  1 196 ? -22.429 -22.371 34.027  1.00 16.66 ? 199  PHE B CZ  1 
ATOM   4030  N  N   . PRO B  1 197 ? -15.523 -22.724 36.791  1.00 14.97 ? 200  PRO B N   1 
ATOM   4031  C  CA  . PRO B  1 197 ? -14.224 -23.323 37.034  1.00 16.05 ? 200  PRO B CA  1 
ATOM   4032  C  C   . PRO B  1 197 ? -14.012 -23.623 38.509  1.00 19.20 ? 200  PRO B C   1 
ATOM   4033  O  O   . PRO B  1 197 ? -13.350 -24.609 38.854  1.00 21.50 ? 200  PRO B O   1 
ATOM   4034  C  CB  . PRO B  1 197 ? -13.242 -22.251 36.557  1.00 17.60 ? 200  PRO B CB  1 
ATOM   4035  C  CG  . PRO B  1 197 ? -14.026 -21.442 35.537  1.00 17.14 ? 200  PRO B CG  1 
ATOM   4036  C  CD  . PRO B  1 197 ? -15.424 -21.431 36.086  1.00 14.45 ? 200  PRO B CD  1 
ATOM   4037  N  N   . ALA B  1 198 ? -14.587 -22.805 39.374  1.00 18.22 ? 201  ALA B N   1 
ATOM   4038  C  CA  . ALA B  1 198 ? -14.459 -23.016 40.803  1.00 19.93 ? 201  ALA B CA  1 
ATOM   4039  C  C   . ALA B  1 198 ? -15.386 -24.146 41.299  1.00 21.87 ? 201  ALA B C   1 
ATOM   4040  O  O   . ALA B  1 198 ? -15.083 -24.811 42.295  1.00 22.52 ? 201  ALA B O   1 
ATOM   4041  C  CB  . ALA B  1 198 ? -14.739 -21.705 41.548  1.00 17.78 ? 201  ALA B CB  1 
ATOM   4042  N  N   . ASN B  1 199 ? -16.508 -24.362 40.608  1.00 20.72 ? 202  ASN B N   1 
ATOM   4043  C  CA  . ASN B  1 199 ? -17.498 -25.350 41.053  1.00 20.38 ? 202  ASN B CA  1 
ATOM   4044  C  C   . ASN B  1 199 ? -17.202 -26.711 40.438  1.00 19.71 ? 202  ASN B C   1 
ATOM   4045  O  O   . ASN B  1 199 ? -17.550 -27.725 41.004  1.00 22.59 ? 202  ASN B O   1 
ATOM   4046  C  CB  . ASN B  1 199 ? -18.933 -24.918 40.682  1.00 19.48 ? 202  ASN B CB  1 
ATOM   4047  C  CG  . ASN B  1 199 ? -19.420 -23.687 41.464  1.00 18.61 ? 202  ASN B CG  1 
ATOM   4048  O  OD1 . ASN B  1 199 ? -18.904 -23.347 42.521  1.00 21.71 ? 202  ASN B OD1 1 
ATOM   4049  N  ND2 . ASN B  1 199 ? -20.465 -23.078 40.977  1.00 20.35 ? 202  ASN B ND2 1 
ATOM   4050  N  N   . LEU B  1 200 ? -16.612 -26.740 39.247  1.00 16.69 ? 203  LEU B N   1 
ATOM   4051  C  CA  . LEU B  1 200 ? -16.629 -27.969 38.447  1.00 14.95 ? 203  LEU B CA  1 
ATOM   4052  C  C   . LEU B  1 200 ? -15.250 -28.455 37.987  1.00 15.48 ? 203  LEU B C   1 
ATOM   4053  O  O   . LEU B  1 200 ? -15.074 -29.662 37.703  1.00 15.44 ? 203  LEU B O   1 
ATOM   4054  C  CB  . LEU B  1 200 ? -17.599 -27.850 37.251  1.00 16.34 ? 203  LEU B CB  1 
ATOM   4055  C  CG  . LEU B  1 200 ? -19.087 -27.739 37.652  1.00 17.17 ? 203  LEU B CG  1 
ATOM   4056  C  CD1 . LEU B  1 200 ? -19.867 -26.805 36.746  1.00 19.58 ? 203  LEU B CD1 1 
ATOM   4057  C  CD2 . LEU B  1 200 ? -19.751 -29.118 37.668  1.00 18.67 ? 203  LEU B CD2 1 
ATOM   4058  N  N   . PHE B  1 201 ? -14.257 -27.557 37.973  1.00 10.15 ? 204  PHE B N   1 
ATOM   4059  C  CA  . PHE B  1 201 ? -12.913 -27.944 37.506  1.00 11.40 ? 204  PHE B CA  1 
ATOM   4060  C  C   . PHE B  1 201 ? -12.043 -28.284 38.715  1.00 11.22 ? 204  PHE B C   1 
ATOM   4061  O  O   . PHE B  1 201 ? -10.905 -28.726 38.573  1.00 17.29 ? 204  PHE B O   1 
ATOM   4062  C  CB  . PHE B  1 201 ? -12.245 -26.831 36.680  1.00 14.11 ? 204  PHE B CB  1 
ATOM   4063  C  CG  . PHE B  1 201 ? -12.819 -26.650 35.280  1.00 15.56 ? 204  PHE B CG  1 
ATOM   4064  C  CD1 . PHE B  1 201 ? -13.697 -27.573 34.739  1.00 16.95 ? 204  PHE B CD1 1 
ATOM   4065  C  CD2 . PHE B  1 201 ? -12.404 -25.601 34.485  1.00 13.52 ? 204  PHE B CD2 1 
ATOM   4066  C  CE1 . PHE B  1 201 ? -14.122 -27.466 33.411  1.00 18.78 ? 204  PHE B CE1 1 
ATOM   4067  C  CE2 . PHE B  1 201 ? -12.910 -25.422 33.201  1.00 14.94 ? 204  PHE B CE2 1 
ATOM   4068  C  CZ  . PHE B  1 201 ? -13.764 -26.365 32.657  1.00 17.95 ? 204  PHE B CZ  1 
ATOM   4069  N  N   . VAL B  1 202 ? -12.588 -28.110 39.908  1.00 13.12 ? 205  VAL B N   1 
ATOM   4070  C  CA  . VAL B  1 202 ? -11.871 -28.462 41.151  1.00 14.66 ? 205  VAL B CA  1 
ATOM   4071  C  C   . VAL B  1 202 ? -12.122 -29.931 41.508  1.00 17.00 ? 205  VAL B C   1 
ATOM   4072  O  O   . VAL B  1 202 ? -13.272 -30.346 41.647  1.00 14.07 ? 205  VAL B O   1 
ATOM   4073  C  CB  . VAL B  1 202 ? -12.368 -27.577 42.318  1.00 14.70 ? 205  VAL B CB  1 
ATOM   4074  C  CG1 . VAL B  1 202 ? -11.850 -28.101 43.660  1.00 15.52 ? 205  VAL B CG1 1 
ATOM   4075  C  CG2 . VAL B  1 202 ? -11.936 -26.123 42.087  1.00 14.71 ? 205  VAL B CG2 1 
ATOM   4076  N  N   . ASP B  1 203 ? -11.058 -30.731 41.546  1.00 18.34 ? 206  ASP B N   1 
ATOM   4077  C  CA  . ASP B  1 203 ? -11.168 -32.152 41.847  1.00 17.53 ? 206  ASP B CA  1 
ATOM   4078  C  C   . ASP B  1 203 ? -12.193 -32.418 42.933  1.00 18.86 ? 206  ASP B C   1 
ATOM   4079  O  O   . ASP B  1 203 ? -12.211 -31.744 43.965  1.00 20.70 ? 206  ASP B O   1 
ATOM   4080  C  CB  . ASP B  1 203 ? -9.805  -32.721 42.247  1.00 21.50 ? 206  ASP B CB  1 
ATOM   4081  C  CG  . ASP B  1 203 ? -9.812  -34.241 42.364  1.00 22.61 ? 206  ASP B CG  1 
ATOM   4082  O  OD1 . ASP B  1 203 ? -10.217 -34.741 43.435  1.00 24.84 ? 206  ASP B OD1 1 
ATOM   4083  O  OD2 . ASP B  1 203 ? -9.367  -34.927 41.405  1.00 22.17 ? 206  ASP B OD2 1 
ATOM   4084  N  N   . GLY B  1 204 ? -13.082 -33.376 42.674  1.00 19.94 ? 207  GLY B N   1 
ATOM   4085  C  CA  . GLY B  1 204 ? -14.204 -33.639 43.570  1.00 17.52 ? 207  GLY B CA  1 
ATOM   4086  C  C   . GLY B  1 204 ? -13.859 -34.170 44.946  1.00 19.25 ? 207  GLY B C   1 
ATOM   4087  O  O   . GLY B  1 204 ? -14.667 -34.079 45.862  1.00 23.16 ? 207  GLY B O   1 
ATOM   4088  N  N   . ARG B  1 205 ? -12.660 -34.709 45.132  1.00 20.88 ? 208  ARG B N   1 
ATOM   4089  C  CA  . ARG B  1 205 ? -12.310 -35.201 46.461  1.00 23.34 ? 208  ARG B CA  1 
ATOM   4090  C  C   . ARG B  1 205 ? -12.103 -34.036 47.412  1.00 25.89 ? 208  ARG B C   1 
ATOM   4091  O  O   . ARG B  1 205 ? -12.411 -34.128 48.603  1.00 30.06 ? 208  ARG B O   1 
ATOM   4092  C  CB  . ARG B  1 205 ? -11.077 -36.099 46.398  1.00 23.63 ? 208  ARG B CB  1 
ATOM   4093  C  CG  . ARG B  1 205 ? -11.374 -37.441 45.726  1.00 22.14 ? 208  ARG B CG  1 
ATOM   4094  C  CD  . ARG B  1 205 ? -10.089 -38.114 45.251  1.00 22.95 ? 208  ARG B CD  1 
ATOM   4095  N  NE  . ARG B  1 205 ? -9.468  -37.425 44.125  1.00 16.81 ? 208  ARG B NE  1 
ATOM   4096  C  CZ  . ARG B  1 205 ? -8.482  -37.932 43.400  1.00 20.63 ? 208  ARG B CZ  1 
ATOM   4097  N  NH1 . ARG B  1 205 ? -8.022  -39.148 43.676  1.00 22.74 ? 208  ARG B NH1 1 
ATOM   4098  N  NH2 . ARG B  1 205 ? -7.955  -37.233 42.396  1.00 18.80 ? 208  ARG B NH2 1 
ATOM   4099  N  N   . ARG B  1 206 ? -11.711 -32.900 46.840  1.00 27.25 ? 209  ARG B N   1 
ATOM   4100  C  CA  . ARG B  1 206 ? -11.488 -31.652 47.572  1.00 25.72 ? 209  ARG B CA  1 
ATOM   4101  C  C   . ARG B  1 206 ? -12.738 -30.768 47.601  1.00 24.44 ? 209  ARG B C   1 
ATOM   4102  O  O   . ARG B  1 206 ? -13.172 -30.335 48.669  1.00 25.43 ? 209  ARG B O   1 
ATOM   4103  C  CB  . ARG B  1 206 ? -10.334 -30.881 46.919  1.00 24.68 ? 209  ARG B CB  1 
ATOM   4104  C  CG  . ARG B  1 206 ? -9.076  -30.850 47.743  1.00 28.32 ? 209  ARG B CG  1 
ATOM   4105  C  CD  . ARG B  1 206 ? -8.203  -29.658 47.380  1.00 29.64 ? 209  ARG B CD  1 
ATOM   4106  N  NE  . ARG B  1 206 ? -7.754  -29.754 45.995  1.00 31.99 ? 209  ARG B NE  1 
ATOM   4107  C  CZ  . ARG B  1 206 ? -8.043  -28.865 45.048  1.00 31.68 ? 209  ARG B CZ  1 
ATOM   4108  N  NH1 . ARG B  1 206 ? -8.756  -27.786 45.344  1.00 29.25 ? 209  ARG B NH1 1 
ATOM   4109  N  NH2 . ARG B  1 206 ? -7.635  -29.073 43.800  1.00 31.46 ? 209  ARG B NH2 1 
ATOM   4110  N  N   . ASP B  1 207 ? -13.339 -30.542 46.431  1.00 20.87 ? 210  ASP B N   1 
ATOM   4111  C  CA  . ASP B  1 207 ? -14.477 -29.625 46.301  1.00 22.12 ? 210  ASP B CA  1 
ATOM   4112  C  C   . ASP B  1 207 ? -14.427 -28.379 47.200  1.00 20.09 ? 210  ASP B C   1 
ATOM   4113  O  O   . ASP B  1 207 ? -15.415 -28.037 47.835  1.00 19.12 ? 210  ASP B O   1 
ATOM   4114  C  CB  . ASP B  1 207 ? -15.813 -30.362 46.487  1.00 23.22 ? 210  ASP B CB  1 
ATOM   4115  C  CG  . ASP B  1 207 ? -16.992 -29.581 45.923  1.00 27.48 ? 210  ASP B CG  1 
ATOM   4116  O  OD1 . ASP B  1 207 ? -16.801 -28.868 44.918  1.00 30.73 ? 210  ASP B OD1 1 
ATOM   4117  O  OD2 . ASP B  1 207 ? -18.102 -29.630 46.497  1.00 29.05 ? 210  ASP B OD2 1 
ATOM   4118  N  N   . ASP B  1 208 ? -13.307 -27.659 47.193  1.00 22.69 ? 211  ASP B N   1 
ATOM   4119  C  CA  . ASP B  1 208 ? -13.115 -26.548 48.132  1.00 21.53 ? 211  ASP B CA  1 
ATOM   4120  C  C   . ASP B  1 208 ? -13.172 -25.179 47.446  1.00 21.34 ? 211  ASP B C   1 
ATOM   4121  O  O   . ASP B  1 208 ? -12.852 -24.153 48.045  1.00 19.66 ? 211  ASP B O   1 
ATOM   4122  C  CB  . ASP B  1 208 ? -11.793 -26.715 48.879  1.00 25.01 ? 211  ASP B CB  1 
ATOM   4123  C  CG  . ASP B  1 208 ? -10.609 -26.731 47.944  1.00 29.63 ? 211  ASP B CG  1 
ATOM   4124  O  OD1 . ASP B  1 208 ? -10.800 -26.491 46.729  1.00 29.62 ? 211  ASP B OD1 1 
ATOM   4125  O  OD2 . ASP B  1 208 ? -9.493  -27.012 48.413  1.00 34.94 ? 211  ASP B OD2 1 
ATOM   4126  N  N   . GLY B  1 209 ? -13.594 -25.168 46.186  1.00 22.37 ? 212  GLY B N   1 
ATOM   4127  C  CA  . GLY B  1 209 ? -13.769 -23.928 45.435  1.00 18.86 ? 212  GLY B CA  1 
ATOM   4128  C  C   . GLY B  1 209 ? -12.489 -23.175 45.087  1.00 19.62 ? 212  GLY B C   1 
ATOM   4129  O  O   . GLY B  1 209 ? -12.548 -21.990 44.747  1.00 19.07 ? 212  GLY B O   1 
ATOM   4130  N  N   . GLN B  1 210 ? -11.336 -23.829 45.222  1.00 16.79 ? 213  GLN B N   1 
ATOM   4131  C  CA  . GLN B  1 210 ? -10.045 -23.230 44.833  1.00 17.08 ? 213  GLN B CA  1 
ATOM   4132  C  C   . GLN B  1 210 ? -9.388  -24.030 43.711  1.00 16.77 ? 213  GLN B C   1 
ATOM   4133  O  O   . GLN B  1 210 ? -8.908  -25.142 43.932  1.00 20.54 ? 213  GLN B O   1 
ATOM   4134  C  CB  . GLN B  1 210 ? -9.077  -23.186 46.033  1.00 16.56 ? 213  GLN B CB  1 
ATOM   4135  C  CG  . GLN B  1 210 ? -9.740  -22.894 47.374  1.00 16.90 ? 213  GLN B CG  1 
ATOM   4136  C  CD  . GLN B  1 210 ? -10.341 -21.502 47.442  1.00 20.02 ? 213  GLN B CD  1 
ATOM   4137  O  OE1 . GLN B  1 210 ? -9.683  -20.509 47.115  1.00 18.06 ? 213  GLN B OE1 1 
ATOM   4138  N  NE2 . GLN B  1 210 ? -11.596 -21.416 47.912  1.00 20.00 ? 213  GLN B NE2 1 
ATOM   4139  N  N   . LEU B  1 211 ? -9.335  -23.458 42.517  1.00 15.83 ? 214  LEU B N   1 
ATOM   4140  C  CA  . LEU B  1 211 ? -8.803  -24.161 41.347  1.00 17.00 ? 214  LEU B CA  1 
ATOM   4141  C  C   . LEU B  1 211 ? -7.364  -23.723 41.143  1.00 18.02 ? 214  LEU B C   1 
ATOM   4142  O  O   . LEU B  1 211 ? -7.101  -22.534 41.115  1.00 15.37 ? 214  LEU B O   1 
ATOM   4143  C  CB  . LEU B  1 211 ? -9.625  -23.798 40.108  1.00 15.66 ? 214  LEU B CB  1 
ATOM   4144  C  CG  . LEU B  1 211 ? -9.085  -24.229 38.745  1.00 15.63 ? 214  LEU B CG  1 
ATOM   4145  C  CD1 . LEU B  1 211 ? -9.162  -25.743 38.547  1.00 14.23 ? 214  LEU B CD1 1 
ATOM   4146  C  CD2 . LEU B  1 211 ? -9.900  -23.536 37.658  1.00 14.20 ? 214  LEU B CD2 1 
ATOM   4147  N  N   . ASP B  1 212 ? -6.431  -24.668 41.019  1.00 17.71 ? 215  ASP B N   1 
ATOM   4148  C  CA  . ASP B  1 212 ? -5.039  -24.293 40.804  1.00 19.40 ? 215  ASP B CA  1 
ATOM   4149  C  C   . ASP B  1 212 ? -4.722  -24.072 39.329  1.00 18.34 ? 215  ASP B C   1 
ATOM   4150  O  O   . ASP B  1 212 ? -5.486  -24.493 38.454  1.00 19.12 ? 215  ASP B O   1 
ATOM   4151  C  CB  . ASP B  1 212 ? -4.065  -25.278 41.471  1.00 21.16 ? 215  ASP B CB  1 
ATOM   4152  C  CG  . ASP B  1 212 ? -3.920  -26.570 40.697  1.00 24.63 ? 215  ASP B CG  1 
ATOM   4153  O  OD1 . ASP B  1 212 ? -3.463  -26.545 39.532  1.00 26.97 ? 215  ASP B OD1 1 
ATOM   4154  O  OD2 . ASP B  1 212 ? -4.286  -27.619 41.244  1.00 26.24 ? 215  ASP B OD2 1 
ATOM   4155  N  N   . MET B  1 213 ? -3.684  -23.278 39.070  1.00 18.86 ? 216  MET B N   1 
ATOM   4156  C  CA  . MET B  1 213 ? -3.388  -22.775 37.723  1.00 18.92 ? 216  MET B CA  1 
ATOM   4157  C  C   . MET B  1 213 ? -2.941  -23.872 36.748  1.00 21.10 ? 216  MET B C   1 
ATOM   4158  O  O   . MET B  1 213 ? -3.142  -23.768 35.536  1.00 22.48 ? 216  MET B O   1 
ATOM   4159  C  CB  . MET B  1 213 ? -2.356  -21.639 37.777  1.00 20.29 ? 216  MET B CB  1 
ATOM   4160  C  CG  . MET B  1 213 ? -2.900  -20.325 38.388  1.00 20.42 ? 216  MET B CG  1 
ATOM   4161  S  SD  . MET B  1 213 ? -4.456  -19.793 37.591  1.00 23.85 ? 216  MET B SD  1 
ATOM   4162  C  CE  . MET B  1 213 ? -5.628  -20.325 38.840  1.00 22.70 ? 216  MET B CE  1 
ATOM   4163  N  N   . ASP B  1 214 ? -2.388  -24.952 37.272  1.00 17.04 ? 217  ASP B N   1 
ATOM   4164  C  CA  . ASP B  1 214 ? -2.041  -26.058 36.410  1.00 19.19 ? 217  ASP B CA  1 
ATOM   4165  C  C   . ASP B  1 214 ? -3.320  -26.740 35.918  1.00 20.03 ? 217  ASP B C   1 
ATOM   4166  O  O   . ASP B  1 214 ? -3.471  -27.044 34.721  1.00 19.02 ? 217  ASP B O   1 
ATOM   4167  C  CB  . ASP B  1 214 ? -1.169  -27.053 37.168  1.00 22.55 ? 217  ASP B CB  1 
ATOM   4168  C  CG  . ASP B  1 214 ? -0.762  -28.232 36.313  1.00 26.58 ? 217  ASP B CG  1 
ATOM   4169  O  OD1 . ASP B  1 214 ? -0.524  -28.041 35.104  1.00 29.67 ? 217  ASP B OD1 1 
ATOM   4170  O  OD2 . ASP B  1 214 ? -0.589  -29.334 36.869  1.00 31.06 ? 217  ASP B OD2 1 
ATOM   4171  N  N   . ALA B  1 215 ? -4.239  -26.996 36.850  1.00 17.00 ? 218  ALA B N   1 
ATOM   4172  C  CA  . ALA B  1 215 ? -5.554  -27.511 36.483  1.00 18.45 ? 218  ALA B CA  1 
ATOM   4173  C  C   . ALA B  1 215 ? -6.297  -26.552 35.543  1.00 17.67 ? 218  ALA B C   1 
ATOM   4174  O  O   . ALA B  1 215 ? -6.834  -26.974 34.526  1.00 17.46 ? 218  ALA B O   1 
ATOM   4175  C  CB  . ALA B  1 215 ? -6.404  -27.838 37.745  1.00 19.08 ? 218  ALA B CB  1 
ATOM   4176  N  N   . ALA B  1 216 ? -6.298  -25.257 35.853  1.00 17.32 ? 219  ALA B N   1 
ATOM   4177  C  CA  . ALA B  1 216 ? -7.015  -24.308 35.005  1.00 15.40 ? 219  ALA B CA  1 
ATOM   4178  C  C   . ALA B  1 216 ? -6.495  -24.364 33.576  1.00 16.72 ? 219  ALA B C   1 
ATOM   4179  O  O   . ALA B  1 216 ? -7.272  -24.396 32.606  1.00 16.55 ? 219  ALA B O   1 
ATOM   4180  C  CB  . ALA B  1 216 ? -6.921  -22.886 35.564  1.00 15.78 ? 219  ALA B CB  1 
ATOM   4181  N  N   . ARG B  1 217 ? -5.179  -24.367 33.431  1.00 16.79 ? 220  ARG B N   1 
ATOM   4182  C  CA  . ARG B  1 217 ? -4.594  -24.387 32.079  1.00 19.18 ? 220  ARG B CA  1 
ATOM   4183  C  C   . ARG B  1 217 ? -4.912  -25.702 31.355  1.00 17.66 ? 220  ARG B C   1 
ATOM   4184  O  O   . ARG B  1 217 ? -5.153  -25.729 30.157  1.00 16.53 ? 220  ARG B O   1 
ATOM   4185  C  CB  . ARG B  1 217 ? -3.081  -24.199 32.139  1.00 13.33 ? 220  ARG B CB  1 
ATOM   4186  C  CG  . ARG B  1 217 ? -2.394  -24.145 30.772  1.00 15.62 ? 220  ARG B CG  1 
ATOM   4187  C  CD  . ARG B  1 217 ? -0.883  -23.941 30.952  1.00 18.42 ? 220  ARG B CD  1 
ATOM   4188  N  NE  . ARG B  1 217 ? -0.577  -22.567 31.373  1.00 18.12 ? 220  ARG B NE  1 
ATOM   4189  C  CZ  . ARG B  1 217 ? -0.473  -21.541 30.532  1.00 18.32 ? 220  ARG B CZ  1 
ATOM   4190  N  NH1 . ARG B  1 217 ? -0.705  -21.716 29.240  1.00 20.89 ? 220  ARG B NH1 1 
ATOM   4191  N  NH2 . ARG B  1 217 ? -0.231  -20.323 30.986  1.00 19.79 ? 220  ARG B NH2 1 
ATOM   4192  N  N   . SER B  1 218 ? -4.870  -26.802 32.079  1.00 19.30 ? 221  SER B N   1 
ATOM   4193  C  CA  . SER B  1 218 ? -5.166  -28.089 31.448  1.00 21.49 ? 221  SER B CA  1 
ATOM   4194  C  C   . SER B  1 218 ? -6.555  -28.097 30.781  1.00 17.85 ? 221  SER B C   1 
ATOM   4195  O  O   . SER B  1 218 ? -6.692  -28.451 29.611  1.00 17.74 ? 221  SER B O   1 
ATOM   4196  C  CB  . SER B  1 218 ? -5.041  -29.207 32.480  1.00 24.36 ? 221  SER B CB  1 
ATOM   4197  O  OG  . SER B  1 218 ? -4.901  -30.459 31.843  1.00 28.32 ? 221  SER B OG  1 
ATOM   4198  N  N   . PHE B  1 219 ? -7.561  -27.597 31.490  1.00 18.76 ? 222  PHE B N   1 
ATOM   4199  C  CA  . PHE B  1 219 ? -8.915  -27.508 30.934  1.00 17.42 ? 222  PHE B CA  1 
ATOM   4200  C  C   . PHE B  1 219 ? -8.978  -26.473 29.817  1.00 15.63 ? 222  PHE B C   1 
ATOM   4201  O  O   . PHE B  1 219 ? -9.382  -26.777 28.693  1.00 18.95 ? 222  PHE B O   1 
ATOM   4202  C  CB  . PHE B  1 219 ? -9.948  -27.192 32.041  1.00 16.11 ? 222  PHE B CB  1 
ATOM   4203  C  CG  . PHE B  1 219 ? -10.313 -28.390 32.916  1.00 16.17 ? 222  PHE B CG  1 
ATOM   4204  C  CD1 . PHE B  1 219 ? -11.103 -29.422 32.422  1.00 16.88 ? 222  PHE B CD1 1 
ATOM   4205  C  CD2 . PHE B  1 219 ? -9.958  -28.426 34.256  1.00 17.42 ? 222  PHE B CD2 1 
ATOM   4206  C  CE1 . PHE B  1 219 ? -11.451 -30.511 33.224  1.00 12.92 ? 222  PHE B CE1 1 
ATOM   4207  C  CE2 . PHE B  1 219 ? -10.316 -29.508 35.069  1.00 22.10 ? 222  PHE B CE2 1 
ATOM   4208  C  CZ  . PHE B  1 219 ? -11.099 -30.533 34.557  1.00 15.07 ? 222  PHE B CZ  1 
ATOM   4209  N  N   . PHE B  1 220 ? -8.599  -25.237 30.134  1.00 18.21 ? 223  PHE B N   1 
ATOM   4210  C  CA  . PHE B  1 220 ? -8.848  -24.102 29.249  1.00 16.79 ? 223  PHE B CA  1 
ATOM   4211  C  C   . PHE B  1 220 ? -8.048  -24.172 27.955  1.00 18.10 ? 223  PHE B C   1 
ATOM   4212  O  O   . PHE B  1 220 ? -8.493  -23.626 26.939  1.00 11.82 ? 223  PHE B O   1 
ATOM   4213  C  CB  . PHE B  1 220 ? -8.531  -22.783 29.934  1.00 16.88 ? 223  PHE B CB  1 
ATOM   4214  C  CG  . PHE B  1 220 ? -9.590  -22.324 30.867  1.00 17.57 ? 223  PHE B CG  1 
ATOM   4215  C  CD1 . PHE B  1 220 ? -10.765 -21.786 30.387  1.00 15.69 ? 223  PHE B CD1 1 
ATOM   4216  C  CD2 . PHE B  1 220 ? -9.371  -22.339 32.234  1.00 20.92 ? 223  PHE B CD2 1 
ATOM   4217  C  CE1 . PHE B  1 220 ? -11.714 -21.288 31.260  1.00 17.79 ? 223  PHE B CE1 1 
ATOM   4218  C  CE2 . PHE B  1 220 ? -10.352 -21.906 33.111  1.00 17.49 ? 223  PHE B CE2 1 
ATOM   4219  C  CZ  . PHE B  1 220 ? -11.521 -21.385 32.619  1.00 16.54 ? 223  PHE B CZ  1 
ATOM   4220  N  N   . GLN B  1 221 ? -6.852  -24.767 28.010  1.00 16.16 ? 224  GLN B N   1 
ATOM   4221  C  CA  . GLN B  1 221 ? -5.934  -24.741 26.846  1.00 19.12 ? 224  GLN B CA  1 
ATOM   4222  C  C   . GLN B  1 221 ? -5.937  -26.046 26.064  1.00 18.73 ? 224  GLN B C   1 
ATOM   4223  O  O   . GLN B  1 221 ? -5.985  -26.044 24.829  1.00 21.29 ? 224  GLN B O   1 
ATOM   4224  C  CB  . GLN B  1 221 ? -4.478  -24.353 27.240  1.00 17.37 ? 224  GLN B CB  1 
ATOM   4225  C  CG  . GLN B  1 221 ? -3.508  -24.333 26.038  1.00 14.46 ? 224  GLN B CG  1 
ATOM   4226  C  CD  . GLN B  1 221 ? -2.103  -23.805 26.367  1.00 17.73 ? 224  GLN B CD  1 
ATOM   4227  O  OE1 . GLN B  1 221 ? -1.619  -23.924 27.502  1.00 14.67 ? 224  GLN B OE1 1 
ATOM   4228  N  NE2 . GLN B  1 221 ? -1.399  -23.327 25.331  1.00 15.32 ? 224  GLN B NE2 1 
ATOM   4229  N  N   . PHE B  1 222 ? -5.875  -27.160 26.777  1.00 18.01 ? 225  PHE B N   1 
ATOM   4230  C  CA  . PHE B  1 222 ? -5.685  -28.463 26.137  1.00 22.55 ? 225  PHE B CA  1 
ATOM   4231  C  C   . PHE B  1 222 ? -6.944  -29.320 26.171  1.00 21.11 ? 225  PHE B C   1 
ATOM   4232  O  O   . PHE B  1 222 ? -6.925  -30.476 25.758  1.00 18.83 ? 225  PHE B O   1 
ATOM   4233  C  CB  . PHE B  1 222 ? -4.509  -29.211 26.796  1.00 23.48 ? 225  PHE B CB  1 
ATOM   4234  C  CG  . PHE B  1 222 ? -3.193  -28.526 26.600  1.00 24.48 ? 225  PHE B CG  1 
ATOM   4235  C  CD1 . PHE B  1 222 ? -2.629  -28.450 25.329  1.00 24.61 ? 225  PHE B CD1 1 
ATOM   4236  C  CD2 . PHE B  1 222 ? -2.616  -27.794 27.641  1.00 25.90 ? 225  PHE B CD2 1 
ATOM   4237  C  CE1 . PHE B  1 222 ? -1.454  -27.738 25.110  1.00 25.54 ? 225  PHE B CE1 1 
ATOM   4238  C  CE2 . PHE B  1 222 ? -1.418  -27.107 27.451  1.00 25.48 ? 225  PHE B CE2 1 
ATOM   4239  C  CZ  . PHE B  1 222 ? -0.827  -27.092 26.182  1.00 25.80 ? 225  PHE B CZ  1 
ATOM   4240  N  N   . SER B  1 223 ? -8.002  -28.789 26.771  1.00 19.44 ? 226  SER B N   1 
ATOM   4241  C  CA  . SER B  1 223 ? -9.216  -29.569 26.954  1.00 20.34 ? 226  SER B CA  1 
ATOM   4242  C  C   . SER B  1 223 ? -8.880  -30.897 27.604  1.00 19.37 ? 226  SER B C   1 
ATOM   4243  O  O   . SER B  1 223 ? -9.295  -31.949 27.127  1.00 22.90 ? 226  SER B O   1 
ATOM   4244  C  CB  . SER B  1 223 ? -9.916  -29.805 25.600  1.00 16.69 ? 226  SER B CB  1 
ATOM   4245  O  OG  . SER B  1 223 ? -9.860  -28.634 24.792  1.00 14.70 ? 226  SER B OG  1 
ATOM   4246  N  N   . ARG B  1 224 ? -8.137  -30.858 28.703  1.00 20.60 ? 227  ARG B N   1 
ATOM   4247  C  CA  . ARG B  1 224 ? -7.653  -32.097 29.312  1.00 18.00 ? 227  ARG B CA  1 
ATOM   4248  C  C   . ARG B  1 224 ? -7.902  -32.063 30.825  1.00 20.27 ? 227  ARG B C   1 
ATOM   4249  O  O   . ARG B  1 224 ? -7.535  -31.111 31.501  1.00 20.45 ? 227  ARG B O   1 
ATOM   4250  C  CB  . ARG B  1 224 ? -6.160  -32.311 28.999  1.00 18.46 ? 227  ARG B CB  1 
ATOM   4251  C  CG  . ARG B  1 224 ? -5.567  -33.629 29.556  1.00 21.86 ? 227  ARG B CG  1 
ATOM   4252  C  CD  . ARG B  1 224 ? -4.259  -34.037 28.866  1.00 23.10 ? 227  ARG B CD  1 
ATOM   4253  N  NE  . ARG B  1 224 ? -3.238  -33.017 29.078  1.00 27.39 ? 227  ARG B NE  1 
ATOM   4254  C  CZ  . ARG B  1 224 ? -2.528  -32.438 28.107  1.00 30.74 ? 227  ARG B CZ  1 
ATOM   4255  N  NH1 . ARG B  1 224 ? -2.647  -32.851 26.852  1.00 29.26 ? 227  ARG B NH1 1 
ATOM   4256  N  NH2 . ARG B  1 224 ? -1.701  -31.434 28.393  1.00 32.43 ? 227  ARG B NH2 1 
ATOM   4257  N  N   . MET B  1 225 ? -8.565  -33.097 31.330  1.00 18.13 ? 228  MET B N   1 
ATOM   4258  C  CA  . MET B  1 225 ? -8.706  -33.322 32.754  1.00 20.55 ? 228  MET B CA  1 
ATOM   4259  C  C   . MET B  1 225 ? -7.347  -33.535 33.402  1.00 21.15 ? 228  MET B C   1 
ATOM   4260  O  O   . MET B  1 225 ? -6.463  -34.131 32.810  1.00 22.37 ? 228  MET B O   1 
ATOM   4261  C  CB  . MET B  1 225 ? -9.558  -34.577 32.976  1.00 20.57 ? 228  MET B CB  1 
ATOM   4262  C  CG  . MET B  1 225 ? -10.937 -34.479 32.394  1.00 19.99 ? 228  MET B CG  1 
ATOM   4263  S  SD  . MET B  1 225 ? -11.934 -35.945 32.711  1.00 23.55 ? 228  MET B SD  1 
ATOM   4264  C  CE  . MET B  1 225 ? -13.544 -35.378 32.143  1.00 16.34 ? 228  MET B CE  1 
ATOM   4265  N  N   . PRO B  1 226 ? -7.188  -33.084 34.646  1.00 22.51 ? 229  PRO B N   1 
ATOM   4266  C  CA  . PRO B  1 226 ? -5.927  -33.432 35.293  1.00 22.87 ? 229  PRO B CA  1 
ATOM   4267  C  C   . PRO B  1 226 ? -5.833  -34.941 35.436  1.00 25.08 ? 229  PRO B C   1 
ATOM   4268  O  O   . PRO B  1 226 ? -6.858  -35.622 35.447  1.00 20.74 ? 229  PRO B O   1 
ATOM   4269  C  CB  . PRO B  1 226 ? -6.053  -32.786 36.675  1.00 22.19 ? 229  PRO B CB  1 
ATOM   4270  C  CG  . PRO B  1 226 ? -6.964  -31.584 36.442  1.00 21.30 ? 229  PRO B CG  1 
ATOM   4271  C  CD  . PRO B  1 226 ? -7.880  -31.957 35.301  1.00 22.69 ? 229  PRO B CD  1 
ATOM   4272  N  N   . ASP B  1 227 ? -4.616  -35.471 35.525  1.00 28.55 ? 230  ASP B N   1 
ATOM   4273  C  CA  . ASP B  1 227 ? -4.449  -36.894 35.840  1.00 31.86 ? 230  ASP B CA  1 
ATOM   4274  C  C   . ASP B  1 227 ? -5.218  -37.258 37.094  1.00 27.88 ? 230  ASP B C   1 
ATOM   4275  O  O   . ASP B  1 227 ? -5.167  -36.536 38.081  1.00 26.80 ? 230  ASP B O   1 
ATOM   4276  C  CB  . ASP B  1 227 ? -2.970  -37.229 36.024  1.00 38.19 ? 230  ASP B CB  1 
ATOM   4277  C  CG  . ASP B  1 227 ? -2.143  -36.813 34.835  1.00 43.25 ? 230  ASP B CG  1 
ATOM   4278  O  OD1 . ASP B  1 227 ? -2.009  -35.587 34.611  1.00 48.99 ? 230  ASP B OD1 1 
ATOM   4279  O  OD2 . ASP B  1 227 ? -1.723  -37.696 34.063  1.00 44.51 ? 230  ASP B OD2 1 
ATOM   4280  N  N   . ASP B  1 228 ? -5.958  -38.362 37.041  1.00 27.83 ? 231  ASP B N   1 
ATOM   4281  C  CA  . ASP B  1 228 ? -6.693  -38.850 38.208  1.00 26.87 ? 231  ASP B CA  1 
ATOM   4282  C  C   . ASP B  1 228 ? -7.804  -37.909 38.644  1.00 26.44 ? 231  ASP B C   1 
ATOM   4283  O  O   . ASP B  1 228 ? -8.188  -37.902 39.820  1.00 28.46 ? 231  ASP B O   1 
ATOM   4284  C  CB  . ASP B  1 228 ? -5.749  -39.089 39.398  1.00 29.19 ? 231  ASP B CB  1 
ATOM   4285  C  CG  . ASP B  1 228 ? -6.321  -40.083 40.404  1.00 32.61 ? 231  ASP B CG  1 
ATOM   4286  O  OD1 . ASP B  1 228 ? -6.895  -41.119 39.983  1.00 35.09 ? 231  ASP B OD1 1 
ATOM   4287  O  OD2 . ASP B  1 228 ? -6.233  -39.825 41.614  1.00 33.00 ? 231  ASP B OD2 1 
ATOM   4288  N  N   . PHE B  1 229 ? -8.296  -37.089 37.720  1.00 24.50 ? 232  PHE B N   1 
ATOM   4289  C  CA  . PHE B  1 229 ? -9.359  -36.142 38.042  1.00 22.24 ? 232  PHE B CA  1 
ATOM   4290  C  C   . PHE B  1 229 ? -10.593 -36.887 38.488  1.00 23.57 ? 232  PHE B C   1 
ATOM   4291  O  O   . PHE B  1 229 ? -11.138 -37.697 37.719  1.00 24.11 ? 232  PHE B O   1 
ATOM   4292  C  CB  . PHE B  1 229 ? -9.745  -35.303 36.827  1.00 19.57 ? 232  PHE B CB  1 
ATOM   4293  C  CG  . PHE B  1 229 ? -10.716 -34.199 37.145  1.00 18.09 ? 232  PHE B CG  1 
ATOM   4294  C  CD1 . PHE B  1 229 ? -10.351 -33.160 37.994  1.00 17.42 ? 232  PHE B CD1 1 
ATOM   4295  C  CD2 . PHE B  1 229 ? -11.998 -34.210 36.626  1.00 16.32 ? 232  PHE B CD2 1 
ATOM   4296  C  CE1 . PHE B  1 229 ? -11.258 -32.159 38.326  1.00 13.28 ? 232  PHE B CE1 1 
ATOM   4297  C  CE2 . PHE B  1 229 ? -12.895 -33.195 36.940  1.00 17.91 ? 232  PHE B CE2 1 
ATOM   4298  C  CZ  . PHE B  1 229 ? -12.508 -32.157 37.763  1.00 14.48 ? 232  PHE B CZ  1 
ATOM   4299  N  N   . PHE B  1 230 ? -11.090 -36.528 39.672  1.00 19.56 ? 233  PHE B N   1 
ATOM   4300  C  CA  . PHE B  1 230 ? -12.419 -36.931 40.116  1.00 19.01 ? 233  PHE B CA  1 
ATOM   4301  C  C   . PHE B  1 230 ? -13.396 -35.774 39.864  1.00 21.74 ? 233  PHE B C   1 
ATOM   4302  O  O   . PHE B  1 230 ? -13.095 -34.605 40.174  1.00 24.34 ? 233  PHE B O   1 
ATOM   4303  C  CB  . PHE B  1 230 ? -12.399 -37.230 41.628  1.00 19.72 ? 233  PHE B CB  1 
ATOM   4304  C  CG  . PHE B  1 230 ? -12.067 -38.670 41.987  1.00 20.37 ? 233  PHE B CG  1 
ATOM   4305  C  CD1 . PHE B  1 230 ? -10.893 -39.267 41.543  1.00 21.08 ? 233  PHE B CD1 1 
ATOM   4306  C  CD2 . PHE B  1 230 ? -12.886 -39.380 42.872  1.00 21.14 ? 233  PHE B CD2 1 
ATOM   4307  C  CE1 . PHE B  1 230 ? -10.580 -40.590 41.900  1.00 21.28 ? 233  PHE B CE1 1 
ATOM   4308  C  CE2 . PHE B  1 230 ? -12.580 -40.686 43.247  1.00 20.07 ? 233  PHE B CE2 1 
ATOM   4309  C  CZ  . PHE B  1 230 ? -11.416 -41.290 42.756  1.00 22.44 ? 233  PHE B CZ  1 
ATOM   4310  N  N   . ARG B  1 231 ? -14.574 -36.101 39.348  1.00 18.71 ? 234  ARG B N   1 
ATOM   4311  C  CA  . ARG B  1 231 ? -15.647 -35.131 39.188  1.00 18.46 ? 234  ARG B CA  1 
ATOM   4312  C  C   . ARG B  1 231 ? -16.182 -34.655 40.536  1.00 19.53 ? 234  ARG B C   1 
ATOM   4313  O  O   . ARG B  1 231 ? -15.848 -35.208 41.584  1.00 22.35 ? 234  ARG B O   1 
ATOM   4314  C  CB  . ARG B  1 231 ? -16.774 -35.718 38.344  1.00 18.05 ? 234  ARG B CB  1 
ATOM   4315  C  CG  . ARG B  1 231 ? -17.767 -36.548 39.131  1.00 20.52 ? 234  ARG B CG  1 
ATOM   4316  C  CD  . ARG B  1 231 ? -18.763 -37.256 38.211  1.00 21.84 ? 234  ARG B CD  1 
ATOM   4317  N  NE  . ARG B  1 231 ? -19.695 -38.075 38.978  1.00 18.55 ? 234  ARG B NE  1 
ATOM   4318  C  CZ  . ARG B  1 231 ? -20.557 -38.925 38.431  1.00 23.27 ? 234  ARG B CZ  1 
ATOM   4319  N  NH1 . ARG B  1 231 ? -20.599 -39.076 37.103  1.00 23.62 ? 234  ARG B NH1 1 
ATOM   4320  N  NH2 . ARG B  1 231 ? -21.354 -39.642 39.204  1.00 19.21 ? 234  ARG B NH2 1 
ATOM   4321  N  N   . ALA B  1 232 ? -16.910 -33.549 40.511  1.00 19.26 ? 235  ALA B N   1 
ATOM   4322  C  CA  . ALA B  1 232 ? -17.540 -33.031 41.702  1.00 21.30 ? 235  ALA B CA  1 
ATOM   4323  C  C   . ALA B  1 232 ? -18.473 -34.064 42.394  1.00 23.56 ? 235  ALA B C   1 
ATOM   4324  O  O   . ALA B  1 232 ? -18.975 -34.989 41.746  1.00 22.60 ? 235  ALA B O   1 
ATOM   4325  C  CB  . ALA B  1 232 ? -18.291 -31.789 41.349  1.00 21.22 ? 235  ALA B CB  1 
ATOM   4326  N  N   . PRO B  1 233 ? -18.692 -33.910 43.716  1.00 21.77 ? 236  PRO B N   1 
ATOM   4327  C  CA  . PRO B  1 233 ? -19.378 -34.919 44.525  1.00 21.52 ? 236  PRO B CA  1 
ATOM   4328  C  C   . PRO B  1 233 ? -20.893 -34.741 44.548  1.00 24.78 ? 236  PRO B C   1 
ATOM   4329  O  O   . PRO B  1 233 ? -21.603 -35.511 45.211  1.00 25.23 ? 236  PRO B O   1 
ATOM   4330  C  CB  . PRO B  1 233 ? -18.804 -34.687 45.931  1.00 22.90 ? 236  PRO B CB  1 
ATOM   4331  C  CG  . PRO B  1 233 ? -18.468 -33.197 45.963  1.00 20.29 ? 236  PRO B CG  1 
ATOM   4332  C  CD  . PRO B  1 233 ? -18.124 -32.815 44.532  1.00 21.63 ? 236  PRO B CD  1 
ATOM   4333  N  N   . SER B  1 234 ? -21.389 -33.760 43.795  1.00 25.76 ? 237  SER B N   1 
ATOM   4334  C  CA  . SER B  1 234 ? -22.821 -33.616 43.579  1.00 25.86 ? 237  SER B CA  1 
ATOM   4335  C  C   . SER B  1 234 ? -23.055 -32.765 42.354  1.00 25.54 ? 237  SER B C   1 
ATOM   4336  O  O   . SER B  1 234 ? -22.159 -32.050 41.926  1.00 26.58 ? 237  SER B O   1 
ATOM   4337  C  CB  . SER B  1 234 ? -23.456 -32.925 44.787  1.00 26.44 ? 237  SER B CB  1 
ATOM   4338  O  OG  . SER B  1 234 ? -22.803 -31.691 45.031  1.00 27.68 ? 237  SER B OG  1 
ATOM   4339  N  N   . PRO B  1 235 ? -24.298 -32.745 41.846  1.00 24.46 ? 238  PRO B N   1 
ATOM   4340  C  CA  . PRO B  1 235 ? -24.521 -31.922 40.664  1.00 21.92 ? 238  PRO B CA  1 
ATOM   4341  C  C   . PRO B  1 235 ? -24.517 -30.439 41.027  1.00 20.98 ? 238  PRO B C   1 
ATOM   4342  O  O   . PRO B  1 235 ? -25.172 -30.034 41.971  1.00 24.87 ? 238  PRO B O   1 
ATOM   4343  C  CB  . PRO B  1 235 ? -25.922 -32.351 40.194  1.00 23.45 ? 238  PRO B CB  1 
ATOM   4344  C  CG  . PRO B  1 235 ? -26.170 -33.717 40.868  1.00 22.11 ? 238  PRO B CG  1 
ATOM   4345  C  CD  . PRO B  1 235 ? -25.461 -33.597 42.174  1.00 24.11 ? 238  PRO B CD  1 
ATOM   4346  N  N   . ARG B  1 236 ? -23.831 -29.615 40.258  1.00 21.20 ? 239  ARG B N   1 
ATOM   4347  C  CA  . ARG B  1 236 ? -24.022 -28.174 40.414  1.00 20.63 ? 239  ARG B CA  1 
ATOM   4348  C  C   . ARG B  1 236 ? -23.651 -27.486 39.125  1.00 19.73 ? 239  ARG B C   1 
ATOM   4349  O  O   . ARG B  1 236 ? -23.134 -28.121 38.205  1.00 16.67 ? 239  ARG B O   1 
ATOM   4350  C  CB  . ARG B  1 236 ? -23.160 -27.633 41.557  1.00 15.97 ? 239  ARG B CB  1 
ATOM   4351  C  CG  . ARG B  1 236 ? -21.669 -27.474 41.150  1.00 21.16 ? 239  ARG B CG  1 
ATOM   4352  C  CD  . ARG B  1 236 ? -20.927 -28.785 41.142  1.00 19.79 ? 239  ARG B CD  1 
ATOM   4353  N  NE  . ARG B  1 236 ? -21.010 -29.449 42.444  1.00 23.05 ? 239  ARG B NE  1 
ATOM   4354  C  CZ  . ARG B  1 236 ? -20.105 -29.335 43.417  1.00 22.82 ? 239  ARG B CZ  1 
ATOM   4355  N  NH1 . ARG B  1 236 ? -19.035 -28.545 43.268  1.00 15.18 ? 239  ARG B NH1 1 
ATOM   4356  N  NH2 . ARG B  1 236 ? -20.275 -30.012 44.550  1.00 18.83 ? 239  ARG B NH2 1 
ATOM   4357  N  N   . SER B  1 237 ? -23.973 -26.202 39.039  1.00 19.52 ? 240  SER B N   1 
ATOM   4358  C  CA  . SER B  1 237 ? -23.512 -25.388 37.942  1.00 21.63 ? 240  SER B CA  1 
ATOM   4359  C  C   . SER B  1 237 ? -23.064 -24.024 38.444  1.00 20.03 ? 240  SER B C   1 
ATOM   4360  O  O   . SER B  1 237 ? -21.906 -23.859 38.841  1.00 20.01 ? 240  SER B O   1 
ATOM   4361  C  CB  . SER B  1 237 ? -24.588 -25.271 36.854  1.00 21.59 ? 240  SER B CB  1 
ATOM   4362  O  OG  . SER B  1 237 ? -25.793 -24.715 37.364  1.00 22.98 ? 240  SER B OG  1 
ATOM   4363  N  N   . GLY B  1 238 ? -24.000 -23.079 38.490  1.00 15.67 ? 241  GLY B N   1 
ATOM   4364  C  CA  . GLY B  1 238 ? -23.697 -21.713 38.897  1.00 20.31 ? 241  GLY B CA  1 
ATOM   4365  C  C   . GLY B  1 238 ? -23.846 -21.308 40.366  1.00 21.02 ? 241  GLY B C   1 
ATOM   4366  O  O   . GLY B  1 238 ? -24.037 -20.133 40.654  1.00 23.99 ? 241  GLY B O   1 
ATOM   4367  N  N   . THR B  1 239 ? -23.706 -22.240 41.302  1.00 22.43 ? 242  THR B N   1 
ATOM   4368  C  CA  . THR B  1 239 ? -23.755 -21.866 42.716  1.00 24.78 ? 242  THR B CA  1 
ATOM   4369  C  C   . THR B  1 239 ? -22.776 -20.727 43.007  1.00 22.48 ? 242  THR B C   1 
ATOM   4370  O  O   . THR B  1 239 ? -21.580 -20.861 42.759  1.00 20.59 ? 242  THR B O   1 
ATOM   4371  C  CB  . THR B  1 239 ? -23.340 -23.011 43.639  1.00 27.83 ? 242  THR B CB  1 
ATOM   4372  O  OG1 . THR B  1 239 ? -23.789 -24.263 43.111  1.00 32.17 ? 242  THR B OG1 1 
ATOM   4373  C  CG2 . THR B  1 239 ? -23.926 -22.787 45.032  1.00 28.55 ? 242  THR B CG2 1 
ATOM   4374  N  N   . GLY B  1 240 ? -23.275 -19.638 43.580  1.00 16.84 ? 243  GLY B N   1 
ATOM   4375  C  CA  . GLY B  1 240 ? -22.413 -18.532 43.986  1.00 17.40 ? 243  GLY B CA  1 
ATOM   4376  C  C   . GLY B  1 240 ? -22.321 -17.460 42.923  1.00 19.27 ? 243  GLY B C   1 
ATOM   4377  O  O   . GLY B  1 240 ? -21.538 -16.517 43.032  1.00 19.28 ? 243  GLY B O   1 
ATOM   4378  N  N   . VAL B  1 241 ? -23.197 -17.539 41.934  1.00 20.22 ? 244  VAL B N   1 
ATOM   4379  C  CA  . VAL B  1 241 ? -23.224 -16.513 40.904  1.00 17.19 ? 244  VAL B CA  1 
ATOM   4380  C  C   . VAL B  1 241 ? -23.543 -15.155 41.505  1.00 17.02 ? 244  VAL B C   1 
ATOM   4381  O  O   . VAL B  1 241 ? -23.070 -14.138 41.019  1.00 22.13 ? 244  VAL B O   1 
ATOM   4382  C  CB  . VAL B  1 241 ? -24.224 -16.851 39.778  1.00 17.94 ? 244  VAL B CB  1 
ATOM   4383  C  CG1 . VAL B  1 241 ? -25.675 -16.686 40.294  1.00 18.10 ? 244  VAL B CG1 1 
ATOM   4384  C  CG2 . VAL B  1 241 ? -23.970 -15.980 38.581  1.00 15.49 ? 244  VAL B CG2 1 
ATOM   4385  N  N   . GLU B  1 242 ? -24.330 -15.121 42.574  1.00 19.06 ? 245  GLU B N   1 
ATOM   4386  C  CA  . GLU B  1 242 ? -24.706 -13.847 43.173  1.00 19.34 ? 245  GLU B CA  1 
ATOM   4387  C  C   . GLU B  1 242 ? -23.494 -13.126 43.793  1.00 20.48 ? 245  GLU B C   1 
ATOM   4388  O  O   . GLU B  1 242 ? -23.493 -11.901 43.930  1.00 22.21 ? 245  GLU B O   1 
ATOM   4389  C  CB  . GLU B  1 242 ? -25.805 -14.031 44.215  1.00 20.73 ? 245  GLU B CB  1 
ATOM   4390  C  CG  . GLU B  1 242 ? -25.337 -14.738 45.489  1.00 25.38 ? 245  GLU B CG  1 
ATOM   4391  C  CD  . GLU B  1 242 ? -25.346 -16.257 45.342  1.00 26.65 ? 245  GLU B CD  1 
ATOM   4392  O  OE1 . GLU B  1 242 ? -25.688 -16.753 44.236  1.00 23.94 ? 245  GLU B OE1 1 
ATOM   4393  O  OE2 . GLU B  1 242 ? -24.995 -16.951 46.329  1.00 29.07 ? 245  GLU B OE2 1 
ATOM   4394  N  N   . VAL B  1 243 ? -22.475 -13.893 44.164  1.00 17.46 ? 246  VAL B N   1 
ATOM   4395  C  CA  . VAL B  1 243 ? -21.179 -13.346 44.593  1.00 16.65 ? 246  VAL B CA  1 
ATOM   4396  C  C   . VAL B  1 243 ? -20.470 -12.558 43.484  1.00 15.54 ? 246  VAL B C   1 
ATOM   4397  O  O   . VAL B  1 243 ? -19.997 -11.439 43.703  1.00 16.03 ? 246  VAL B O   1 
ATOM   4398  C  CB  . VAL B  1 243 ? -20.258 -14.494 45.094  1.00 14.81 ? 246  VAL B CB  1 
ATOM   4399  C  CG1 . VAL B  1 243 ? -18.879 -13.963 45.489  1.00 17.46 ? 246  VAL B CG1 1 
ATOM   4400  C  CG2 . VAL B  1 243 ? -20.915 -15.197 46.270  1.00 14.32 ? 246  VAL B CG2 1 
ATOM   4401  N  N   . VAL B  1 244 ? -20.495 -13.099 42.267  1.00 20.02 ? 247  VAL B N   1 
ATOM   4402  C  CA  . VAL B  1 244 ? -19.873 -12.466 41.097  1.00 19.11 ? 247  VAL B CA  1 
ATOM   4403  C  C   . VAL B  1 244 ? -20.702 -11.267 40.643  1.00 21.39 ? 247  VAL B C   1 
ATOM   4404  O  O   . VAL B  1 244 ? -20.176 -10.182 40.345  1.00 24.16 ? 247  VAL B O   1 
ATOM   4405  C  CB  . VAL B  1 244 ? -19.726 -13.490 39.943  1.00 19.73 ? 247  VAL B CB  1 
ATOM   4406  C  CG1 . VAL B  1 244 ? -19.063 -12.869 38.729  1.00 13.89 ? 247  VAL B CG1 1 
ATOM   4407  C  CG2 . VAL B  1 244 ? -18.928 -14.694 40.424  1.00 18.68 ? 247  VAL B CG2 1 
ATOM   4408  N  N   . ILE B  1 245 ? -22.010 -11.438 40.651  1.00 20.65 ? 248  ILE B N   1 
ATOM   4409  C  CA  . ILE B  1 245 ? -22.902 -10.349 40.287  1.00 21.91 ? 248  ILE B CA  1 
ATOM   4410  C  C   . ILE B  1 245 ? -22.657 -9.108  41.168  1.00 23.38 ? 248  ILE B C   1 
ATOM   4411  O  O   . ILE B  1 245 ? -22.353 -8.017  40.665  1.00 22.90 ? 248  ILE B O   1 
ATOM   4412  C  CB  . ILE B  1 245 ? -24.347 -10.809 40.394  1.00 18.77 ? 248  ILE B CB  1 
ATOM   4413  C  CG1 . ILE B  1 245 ? -24.618 -11.882 39.347  1.00 19.13 ? 248  ILE B CG1 1 
ATOM   4414  C  CG2 . ILE B  1 245 ? -25.285 -9.658  40.242  1.00 20.68 ? 248  ILE B CG2 1 
ATOM   4415  C  CD1 . ILE B  1 245 ? -25.996 -12.549 39.474  1.00 13.70 ? 248  ILE B CD1 1 
ATOM   4416  N  N   . GLN B  1 246 ? -22.702 -9.318  42.484  1.00 23.14 ? 249  GLN B N   1 
ATOM   4417  C  CA  . GLN B  1 246 ? -22.603 -8.256  43.479  1.00 20.69 ? 249  GLN B CA  1 
ATOM   4418  C  C   . GLN B  1 246 ? -21.192 -7.676  43.633  1.00 19.82 ? 249  GLN B C   1 
ATOM   4419  O  O   . GLN B  1 246 ? -21.019 -6.580  44.161  1.00 20.87 ? 249  GLN B O   1 
ATOM   4420  C  CB  . GLN B  1 246 ? -23.057 -8.802  44.834  1.00 22.71 ? 249  GLN B CB  1 
ATOM   4421  C  CG  . GLN B  1 246 ? -24.537 -8.618  45.125  1.00 26.79 ? 249  GLN B CG  1 
ATOM   4422  C  CD  . GLN B  1 246 ? -25.031 -7.209  44.824  1.00 29.03 ? 249  GLN B CD  1 
ATOM   4423  O  OE1 . GLN B  1 246 ? -24.501 -6.223  45.334  1.00 28.64 ? 249  GLN B OE1 1 
ATOM   4424  N  NE2 . GLN B  1 246 ? -26.035 -7.115  43.964  1.00 30.80 ? 249  GLN B NE2 1 
ATOM   4425  N  N   . ALA B  1 247 ? -20.172 -8.453  43.300  1.00 19.64 ? 250  ALA B N   1 
ATOM   4426  C  CA  . ALA B  1 247 ? -18.808 -7.962  43.461  1.00 19.72 ? 250  ALA B CA  1 
ATOM   4427  C  C   . ALA B  1 247 ? -18.709 -6.601  42.778  1.00 21.66 ? 250  ALA B C   1 
ATOM   4428  O  O   . ALA B  1 247 ? -17.988 -5.706  43.239  1.00 18.19 ? 250  ALA B O   1 
ATOM   4429  C  CB  . ALA B  1 247 ? -17.809 -8.932  42.865  1.00 18.26 ? 250  ALA B CB  1 
ATOM   4430  N  N   . HIS B  1 248 ? -19.404 -6.467  41.647  1.00 21.82 ? 251  HIS B N   1 
ATOM   4431  C  CA  . HIS B  1 248 ? -19.206 -5.328  40.754  1.00 20.70 ? 251  HIS B CA  1 
ATOM   4432  C  C   . HIS B  1 248 ? -20.481 -5.058  39.931  1.00 21.62 ? 251  HIS B C   1 
ATOM   4433  O  O   . HIS B  1 248 ? -20.585 -5.470  38.770  1.00 20.11 ? 251  HIS B O   1 
ATOM   4434  C  CB  . HIS B  1 248 ? -18.001 -5.581  39.836  1.00 22.96 ? 251  HIS B CB  1 
ATOM   4435  C  CG  . HIS B  1 248 ? -16.664 -5.315  40.478  1.00 22.53 ? 251  HIS B CG  1 
ATOM   4436  N  ND1 . HIS B  1 248 ? -16.241 -4.047  40.832  1.00 21.82 ? 251  HIS B ND1 1 
ATOM   4437  C  CD2 . HIS B  1 248 ? -15.622 -6.142  40.744  1.00 22.84 ? 251  HIS B CD2 1 
ATOM   4438  C  CE1 . HIS B  1 248 ? -15.047 -4.125  41.398  1.00 22.36 ? 251  HIS B CE1 1 
ATOM   4439  N  NE2 . HIS B  1 248 ? -14.632 -5.380  41.329  1.00 22.59 ? 251  HIS B NE2 1 
ATOM   4440  N  N   . PRO B  1 249 ? -21.476 -4.399  40.547  1.00 20.85 ? 252  PRO B N   1 
ATOM   4441  C  CA  . PRO B  1 249 ? -22.767 -4.195  39.880  1.00 20.71 ? 252  PRO B CA  1 
ATOM   4442  C  C   . PRO B  1 249 ? -22.595 -3.680  38.458  1.00 21.61 ? 252  PRO B C   1 
ATOM   4443  O  O   . PRO B  1 249 ? -21.806 -2.757  38.226  1.00 24.84 ? 252  PRO B O   1 
ATOM   4444  C  CB  . PRO B  1 249 ? -23.433 -3.127  40.743  1.00 20.14 ? 252  PRO B CB  1 
ATOM   4445  C  CG  . PRO B  1 249 ? -22.900 -3.418  42.154  1.00 21.98 ? 252  PRO B CG  1 
ATOM   4446  C  CD  . PRO B  1 249 ? -21.474 -3.896  41.936  1.00 20.94 ? 252  PRO B CD  1 
ATOM   4447  N  N   . MET B  1 250 ? -23.300 -4.292  37.512  1.00 19.24 ? 253  MET B N   1 
ATOM   4448  C  CA  . MET B  1 250 ? -23.317 -3.835  36.125  1.00 21.40 ? 253  MET B CA  1 
ATOM   4449  C  C   . MET B  1 250 ? -24.724 -3.965  35.575  1.00 20.78 ? 253  MET B C   1 
ATOM   4450  O  O   . MET B  1 250 ? -25.420 -4.905  35.894  1.00 21.36 ? 253  MET B O   1 
ATOM   4451  C  CB  . MET B  1 250 ? -22.416 -4.734  35.262  1.00 27.48 ? 253  MET B CB  1 
ATOM   4452  C  CG  . MET B  1 250 ? -20.941 -4.455  35.376  1.00 31.22 ? 253  MET B CG  1 
ATOM   4453  S  SD  . MET B  1 250 ? -20.490 -2.948  34.518  1.00 34.36 ? 253  MET B SD  1 
ATOM   4454  C  CE  . MET B  1 250 ? -21.211 -3.265  32.924  1.00 31.40 ? 253  MET B CE  1 
ATOM   4455  N  N   . GLN B  1 251 ? -25.110 -3.069  34.676  1.00 25.65 ? 254  GLN B N   1 
ATOM   4456  C  CA  . GLN B  1 251 ? -26.282 -3.293  33.836  1.00 25.03 ? 254  GLN B CA  1 
ATOM   4457  C  C   . GLN B  1 251 ? -25.853 -3.701  32.439  1.00 26.12 ? 254  GLN B C   1 
ATOM   4458  O  O   . GLN B  1 251 ? -24.794 -3.270  31.942  1.00 25.81 ? 254  GLN B O   1 
ATOM   4459  C  CB  . GLN B  1 251 ? -27.162 -2.040  33.735  1.00 28.32 ? 254  GLN B CB  1 
ATOM   4460  C  CG  . GLN B  1 251 ? -27.520 -1.390  35.052  1.00 32.40 ? 254  GLN B CG  1 
ATOM   4461  C  CD  . GLN B  1 251 ? -28.615 -2.128  35.804  1.00 38.03 ? 254  GLN B CD  1 
ATOM   4462  O  OE1 . GLN B  1 251 ? -28.594 -3.358  35.916  1.00 37.72 ? 254  GLN B OE1 1 
ATOM   4463  N  NE2 . GLN B  1 251 ? -29.524 -1.366  36.419  1.00 41.84 ? 254  GLN B NE2 1 
ATOM   4464  N  N   . PRO B  1 252 ? -26.723 -4.464  31.767  1.00 25.15 ? 255  PRO B N   1 
ATOM   4465  C  CA  . PRO B  1 252 ? -26.578 -4.833  30.367  1.00 23.53 ? 255  PRO B CA  1 
ATOM   4466  C  C   . PRO B  1 252 ? -26.552 -3.601  29.471  1.00 21.92 ? 255  PRO B C   1 
ATOM   4467  O  O   . PRO B  1 252 ? -27.279 -2.632  29.728  1.00 18.98 ? 255  PRO B O   1 
ATOM   4468  C  CB  . PRO B  1 252 ? -27.837 -5.657  30.101  1.00 23.75 ? 255  PRO B CB  1 
ATOM   4469  C  CG  . PRO B  1 252 ? -28.839 -5.089  31.045  1.00 23.72 ? 255  PRO B CG  1 
ATOM   4470  C  CD  . PRO B  1 252 ? -28.068 -4.780  32.286  1.00 24.36 ? 255  PRO B CD  1 
ATOM   4471  N  N   . GLY B  1 253 ? -25.641 -3.602  28.495  1.00 18.79 ? 256  GLY B N   1 
ATOM   4472  C  CA  . GLY B  1 253 ? -25.586 -2.551  27.502  1.00 13.36 ? 256  GLY B CA  1 
ATOM   4473  C  C   . GLY B  1 253 ? -24.633 -2.913  26.393  1.00 17.19 ? 256  GLY B C   1 
ATOM   4474  O  O   . GLY B  1 253 ? -24.228 -4.080  26.266  1.00 19.72 ? 256  GLY B O   1 
ATOM   4475  N  N   . ARG B  1 254 ? -24.223 -1.900  25.628  1.00 16.12 ? 257  ARG B N   1 
ATOM   4476  C  CA  A ARG B  1 254 ? -23.278 -2.104  24.555  0.50 16.03 ? 257  ARG B CA  1 
ATOM   4477  C  CA  B ARG B  1 254 ? -23.409 -2.079  24.427  0.50 16.95 ? 257  ARG B CA  1 
ATOM   4478  C  C   . ARG B  1 254 ? -22.580 -0.811  24.200  1.00 19.52 ? 257  ARG B C   1 
ATOM   4479  O  O   . ARG B  1 254 ? -23.060 0.296   24.491  1.00 23.57 ? 257  ARG B O   1 
ATOM   4480  C  CB  A ARG B  1 254 ? -23.955 -2.704  23.318  0.50 17.34 ? 257  ARG B CB  1 
ATOM   4481  C  CB  B ARG B  1 254 ? -24.331 -2.309  23.219  0.50 19.09 ? 257  ARG B CB  1 
ATOM   4482  C  CG  A ARG B  1 254 ? -25.461 -2.523  23.256  0.50 15.43 ? 257  ARG B CG  1 
ATOM   4483  C  CG  B ARG B  1 254 ? -24.999 -1.034  22.696  0.50 18.68 ? 257  ARG B CG  1 
ATOM   4484  C  CD  A ARG B  1 254 ? -25.981 -2.840  21.864  0.50 16.37 ? 257  ARG B CD  1 
ATOM   4485  C  CD  B ARG B  1 254 ? -26.445 -1.245  22.252  0.50 22.29 ? 257  ARG B CD  1 
ATOM   4486  N  NE  A ARG B  1 254 ? -26.863 -4.005  21.851  0.50 12.65 ? 257  ARG B NE  1 
ATOM   4487  N  NE  B ARG B  1 254 ? -27.176 0.022   22.062  0.50 20.91 ? 257  ARG B NE  1 
ATOM   4488  C  CZ  A ARG B  1 254 ? -28.101 -3.981  22.322  0.50 15.17 ? 257  ARG B CZ  1 
ATOM   4489  C  CZ  B ARG B  1 254 ? -27.917 0.613   22.998  0.50 19.61 ? 257  ARG B CZ  1 
ATOM   4490  N  NH1 A ARG B  1 254 ? -28.567 -2.871  22.882  0.50 14.83 ? 257  ARG B NH1 1 
ATOM   4491  N  NH1 B ARG B  1 254 ? -27.987 0.097   24.222  0.50 15.00 ? 257  ARG B NH1 1 
ATOM   4492  N  NH2 A ARG B  1 254 ? -28.864 -5.064  22.255  0.50 14.52 ? 257  ARG B NH2 1 
ATOM   4493  N  NH2 B ARG B  1 254 ? -28.569 1.738   22.716  0.50 18.52 ? 257  ARG B NH2 1 
ATOM   4494  N  N   . ASN B  1 255 ? -21.383 -0.942  23.646  1.00 18.27 ? 258  ASN B N   1 
ATOM   4495  C  CA  . ASN B  1 255 ? -20.808 0.203   22.985  1.00 22.63 ? 258  ASN B CA  1 
ATOM   4496  C  C   . ASN B  1 255 ? -21.690 0.533   21.797  1.00 24.57 ? 258  ASN B C   1 
ATOM   4497  O  O   . ASN B  1 255 ? -22.351 -0.345  21.253  1.00 26.94 ? 258  ASN B O   1 
ATOM   4498  C  CB  . ASN B  1 255 ? -19.384 -0.083  22.537  1.00 21.05 ? 258  ASN B CB  1 
ATOM   4499  C  CG  . ASN B  1 255 ? -18.369 0.169   23.651  1.00 22.45 ? 258  ASN B CG  1 
ATOM   4500  O  OD1 . ASN B  1 255 ? -18.626 0.952   24.561  1.00 17.82 ? 258  ASN B OD1 1 
ATOM   4501  N  ND2 . ASN B  1 255 ? -17.247 -0.550  23.614  1.00 18.01 ? 258  ASN B ND2 1 
ATOM   4502  N  N   . VAL B  1 256 ? -21.689 1.791   21.382  1.00 27.64 ? 259  VAL B N   1 
ATOM   4503  C  CA  . VAL B  1 256 ? -22.570 2.223   20.305  1.00 26.85 ? 259  VAL B CA  1 
ATOM   4504  C  C   . VAL B  1 256 ? -21.765 2.798   19.167  1.00 27.25 ? 259  VAL B C   1 
ATOM   4505  O  O   . VAL B  1 256 ? -21.830 3.992   18.885  1.00 33.15 ? 259  VAL B O   1 
ATOM   4506  C  CB  . VAL B  1 256 ? -23.631 3.206   20.837  1.00 28.52 ? 259  VAL B CB  1 
ATOM   4507  C  CG1 . VAL B  1 256 ? -24.306 3.960   19.715  1.00 30.35 ? 259  VAL B CG1 1 
ATOM   4508  C  CG2 . VAL B  1 256 ? -24.651 2.440   21.637  1.00 26.88 ? 259  VAL B CG2 1 
ATOM   4509  N  N   . GLY B  1 257 ? -20.921 1.957   18.580  1.00 29.99 ? 260  GLY B N   1 
ATOM   4510  C  CA  . GLY B  1 257 ? -20.161 2.321   17.389  1.00 26.77 ? 260  GLY B CA  1 
ATOM   4511  C  C   . GLY B  1 257 ? -18.734 2.761   17.680  1.00 26.98 ? 260  GLY B C   1 
ATOM   4512  O  O   . GLY B  1 257 ? -17.972 2.993   16.771  1.00 27.10 ? 260  GLY B O   1 
ATOM   4513  N  N   . LYS B  1 258 ? -18.362 2.863   18.953  1.00 28.50 ? 261  LYS B N   1 
ATOM   4514  C  CA  . LYS B  1 258 ? -17.039 3.384   19.331  1.00 26.04 ? 261  LYS B CA  1 
ATOM   4515  C  C   . LYS B  1 258 ? -16.693 2.887   20.735  1.00 26.54 ? 261  LYS B C   1 
ATOM   4516  O  O   . LYS B  1 258 ? -17.579 2.523   21.500  1.00 26.71 ? 261  LYS B O   1 
ATOM   4517  C  CB  . LYS B  1 258 ? -17.047 4.919   19.323  1.00 25.37 ? 261  LYS B CB  1 
ATOM   4518  C  CG  . LYS B  1 258 ? -17.930 5.535   20.405  1.00 29.69 ? 261  LYS B CG  1 
ATOM   4519  C  CD  . LYS B  1 258 ? -18.019 7.062   20.323  1.00 31.38 ? 261  LYS B CD  1 
ATOM   4520  C  CE  . LYS B  1 258 ? -18.967 7.614   21.396  1.00 31.69 ? 261  LYS B CE  1 
ATOM   4521  N  NZ  . LYS B  1 258 ? -19.445 9.013   21.146  1.00 32.44 ? 261  LYS B NZ  1 
ATOM   4522  N  N   . ILE B  1 259 ? -15.410 2.870   21.071  1.00 25.73 ? 262  ILE B N   1 
ATOM   4523  C  CA  . ILE B  1 259 ? -14.987 2.445   22.390  1.00 25.96 ? 262  ILE B CA  1 
ATOM   4524  C  C   . ILE B  1 259 ? -15.486 3.427   23.434  1.00 27.81 ? 262  ILE B C   1 
ATOM   4525  O  O   . ILE B  1 259 ? -15.817 4.572   23.113  1.00 29.47 ? 262  ILE B O   1 
ATOM   4526  C  CB  . ILE B  1 259 ? -13.462 2.322   22.479  1.00 25.95 ? 262  ILE B CB  1 
ATOM   4527  C  CG1 . ILE B  1 259 ? -12.801 3.634   22.045  1.00 26.11 ? 262  ILE B CG1 1 
ATOM   4528  C  CG2 . ILE B  1 259 ? -12.988 1.200   21.574  1.00 25.32 ? 262  ILE B CG2 1 
ATOM   4529  C  CD1 . ILE B  1 259 ? -11.302 3.685   22.274  1.00 24.69 ? 262  ILE B CD1 1 
ATOM   4530  N  N   . ASN B  1 260 ? -15.614 2.956   24.671  1.00 24.87 ? 263  ASN B N   1 
ATOM   4531  C  CA  . ASN B  1 260 ? -15.944 3.838   25.773  1.00 25.62 ? 263  ASN B CA  1 
ATOM   4532  C  C   . ASN B  1 260 ? -17.200 4.607   25.488  1.00 25.78 ? 263  ASN B C   1 
ATOM   4533  O  O   . ASN B  1 260 ? -17.278 5.807   25.755  1.00 24.92 ? 263  ASN B O   1 
ATOM   4534  C  CB  . ASN B  1 260 ? -14.813 4.828   26.025  1.00 26.19 ? 263  ASN B CB  1 
ATOM   4535  C  CG  . ASN B  1 260 ? -13.608 4.166   26.587  1.00 23.04 ? 263  ASN B CG  1 
ATOM   4536  O  OD1 . ASN B  1 260 ? -12.538 4.208   25.998  1.00 25.81 ? 263  ASN B OD1 1 
ATOM   4537  N  ND2 . ASN B  1 260 ? -13.803 3.427   27.666  1.00 22.54 ? 263  ASN B ND2 1 
ATOM   4538  N  N   . SER B  1 261 ? -18.197 3.909   24.964  1.00 24.04 ? 264  SER B N   1 
ATOM   4539  C  CA  . SER B  1 261 ? -19.501 4.502   24.841  1.00 25.26 ? 264  SER B CA  1 
ATOM   4540  C  C   . SER B  1 261 ? -20.556 3.571   25.378  1.00 26.06 ? 264  SER B C   1 
ATOM   4541  O  O   . SER B  1 261 ? -21.616 3.457   24.792  1.00 28.59 ? 264  SER B O   1 
ATOM   4542  C  CB  . SER B  1 261 ? -19.792 4.852   23.385  1.00 23.78 ? 264  SER B CB  1 
ATOM   4543  O  OG  . SER B  1 261 ? -19.714 3.712   22.551  1.00 25.33 ? 264  SER B OG  1 
ATOM   4544  N  N   . TYR B  1 262 ? -20.271 2.911   26.498  1.00 27.17 ? 265  TYR B N   1 
ATOM   4545  C  CA  . TYR B  1 262 ? -21.175 1.879   27.004  1.00 24.62 ? 265  TYR B CA  1 
ATOM   4546  C  C   . TYR B  1 262 ? -22.518 2.473   27.309  1.00 23.75 ? 265  TYR B C   1 
ATOM   4547  O  O   . TYR B  1 262 ? -22.655 3.267   28.234  1.00 23.63 ? 265  TYR B O   1 
ATOM   4548  C  CB  . TYR B  1 262 ? -20.626 1.177   28.250  1.00 20.78 ? 265  TYR B CB  1 
ATOM   4549  C  CG  . TYR B  1 262 ? -21.366 -0.117  28.638  1.00 21.63 ? 265  TYR B CG  1 
ATOM   4550  C  CD1 . TYR B  1 262 ? -21.147 -1.310  27.954  1.00 18.99 ? 265  TYR B CD1 1 
ATOM   4551  C  CD2 . TYR B  1 262 ? -22.157 -0.172  29.773  1.00 20.78 ? 265  TYR B CD2 1 
ATOM   4552  C  CE1 . TYR B  1 262 ? -21.739 -2.483  28.358  1.00 15.90 ? 265  TYR B CE1 1 
ATOM   4553  C  CE2 . TYR B  1 262 ? -22.733 -1.370  30.211  1.00 15.60 ? 265  TYR B CE2 1 
ATOM   4554  C  CZ  . TYR B  1 262 ? -22.520 -2.509  29.509  1.00 18.47 ? 265  TYR B CZ  1 
ATOM   4555  O  OH  . TYR B  1 262 ? -23.081 -3.688  29.973  1.00 19.13 ? 265  TYR B OH  1 
ATOM   4556  N  N   . THR B  1 263 ? -23.530 1.984   26.602  1.00 25.44 ? 266  THR B N   1 
ATOM   4557  C  CA  . THR B  1 263 ? -24.879 2.480   26.761  1.00 25.64 ? 266  THR B CA  1 
ATOM   4558  C  C   . THR B  1 263 ? -25.827 1.448   27.354  1.00 24.96 ? 266  THR B C   1 
ATOM   4559  O  O   . THR B  1 263 ? -26.080 0.403   26.762  1.00 21.62 ? 266  THR B O   1 
ATOM   4560  C  CB  . THR B  1 263 ? -25.420 2.979   25.429  1.00 27.81 ? 266  THR B CB  1 
ATOM   4561  O  OG1 . THR B  1 263 ? -24.461 3.887   24.868  1.00 28.00 ? 266  THR B OG1 1 
ATOM   4562  C  CG2 . THR B  1 263 ? -26.755 3.692   25.640  1.00 27.07 ? 266  THR B CG2 1 
ATOM   4563  N  N   . VAL B  1 264 ? -26.350 1.760   28.535  1.00 26.55 ? 267  VAL B N   1 
ATOM   4564  C  CA  . VAL B  1 264 ? -27.215 0.860   29.246  1.00 26.18 ? 267  VAL B CA  1 
ATOM   4565  C  C   . VAL B  1 264 ? -28.577 0.731   28.568  1.00 30.83 ? 267  VAL B C   1 
ATOM   4566  O  O   . VAL B  1 264 ? -29.165 1.719   28.122  1.00 31.36 ? 267  VAL B O   1 
ATOM   4567  C  CB  . VAL B  1 264 ? -27.323 1.248   30.731  1.00 28.95 ? 267  VAL B CB  1 
ATOM   4568  C  CG1 . VAL B  1 264 ? -28.534 0.569   31.403  1.00 24.66 ? 267  VAL B CG1 1 
ATOM   4569  C  CG2 . VAL B  1 264 ? -26.020 0.839   31.455  1.00 31.92 ? 267  VAL B CG2 1 
ATOM   4570  N  N   . ASP B  1 265 ? -29.033 -0.510  28.433  1.00 32.87 ? 268  ASP B N   1 
ATOM   4571  C  CA  . ASP B  1 265 ? -30.223 -0.828  27.660  1.00 36.98 ? 268  ASP B CA  1 
ATOM   4572  C  C   . ASP B  1 265 ? -31.306 -1.301  28.615  1.00 36.43 ? 268  ASP B C   1 
ATOM   4573  O  O   . ASP B  1 265 ? -31.294 -2.459  29.027  1.00 32.23 ? 268  ASP B O   1 
ATOM   4574  C  CB  . ASP B  1 265 ? -29.912 -1.952  26.662  1.00 40.40 ? 268  ASP B CB  1 
ATOM   4575  C  CG  . ASP B  1 265 ? -31.131 -2.376  25.859  1.00 43.93 ? 268  ASP B CG  1 
ATOM   4576  O  OD1 . ASP B  1 265 ? -32.225 -1.798  26.078  1.00 44.71 ? 268  ASP B OD1 1 
ATOM   4577  O  OD2 . ASP B  1 265 ? -30.978 -3.254  24.976  1.00 44.99 ? 268  ASP B OD2 1 
ATOM   4578  N  N   . PRO B  1 266 ? -32.250 -0.404  28.959  1.00 38.22 ? 269  PRO B N   1 
ATOM   4579  C  CA  . PRO B  1 266 ? -33.312 -0.698  29.925  1.00 37.60 ? 269  PRO B CA  1 
ATOM   4580  C  C   . PRO B  1 266 ? -34.341 -1.705  29.417  1.00 36.91 ? 269  PRO B C   1 
ATOM   4581  O  O   . PRO B  1 266 ? -35.124 -2.222  30.209  1.00 38.76 ? 269  PRO B O   1 
ATOM   4582  C  CB  . PRO B  1 266 ? -33.971 0.664   30.143  1.00 39.06 ? 269  PRO B CB  1 
ATOM   4583  C  CG  . PRO B  1 266 ? -33.752 1.395   28.845  1.00 40.50 ? 269  PRO B CG  1 
ATOM   4584  C  CD  . PRO B  1 266 ? -32.406 0.930   28.343  1.00 38.79 ? 269  PRO B CD  1 
ATOM   4585  N  N   . THR B  1 267 ? -34.321 -2.028  28.128  1.00 34.66 ? 270  THR B N   1 
ATOM   4586  C  CA  . THR B  1 267 ? -35.191 -3.103  27.633  1.00 36.47 ? 270  THR B CA  1 
ATOM   4587  C  C   . THR B  1 267 ? -34.579 -4.501  27.745  1.00 35.32 ? 270  THR B C   1 
ATOM   4588  O  O   . THR B  1 267 ? -35.280 -5.497  27.550  1.00 37.30 ? 270  THR B O   1 
ATOM   4589  C  CB  . THR B  1 267 ? -35.653 -2.878  26.185  1.00 37.49 ? 270  THR B CB  1 
ATOM   4590  O  OG1 . THR B  1 267 ? -34.575 -3.172  25.293  1.00 37.95 ? 270  THR B OG1 1 
ATOM   4591  C  CG2 . THR B  1 267 ? -36.097 -1.432  25.979  1.00 39.12 ? 270  THR B CG2 1 
ATOM   4592  N  N   . SER B  1 268 ? -33.295 -4.587  28.093  1.00 28.97 ? 271  SER B N   1 
ATOM   4593  C  CA  . SER B  1 268 ? -32.683 -5.892  28.344  1.00 23.69 ? 271  SER B CA  1 
ATOM   4594  C  C   . SER B  1 268 ? -33.266 -6.497  29.602  1.00 22.03 ? 271  SER B C   1 
ATOM   4595  O  O   . SER B  1 268 ? -33.602 -5.796  30.543  1.00 23.25 ? 271  SER B O   1 
ATOM   4596  C  CB  . SER B  1 268 ? -31.145 -5.801  28.454  1.00 21.74 ? 271  SER B CB  1 
ATOM   4597  O  OG  . SER B  1 268 ? -30.569 -7.071  28.792  1.00 20.12 ? 271  SER B OG  1 
ATOM   4598  N  N   . SER B  1 269 ? -33.332 -7.815  29.657  1.00 22.06 ? 272  SER B N   1 
ATOM   4599  C  CA  . SER B  1 269 ? -33.527 -8.448  30.936  1.00 21.10 ? 272  SER B CA  1 
ATOM   4600  C  C   . SER B  1 269 ? -32.268 -8.193  31.778  1.00 20.40 ? 272  SER B C   1 
ATOM   4601  O  O   . SER B  1 269 ? -31.218 -7.822  31.251  1.00 18.66 ? 272  SER B O   1 
ATOM   4602  C  CB  . SER B  1 269 ? -33.777 -9.950  30.756  1.00 22.10 ? 272  SER B CB  1 
ATOM   4603  O  OG  . SER B  1 269 ? -32.625 -10.621 30.264  1.00 24.73 ? 272  SER B OG  1 
ATOM   4604  N  N   . ASP B  1 270 ? -32.366 -8.415  33.078  1.00 22.25 ? 273  ASP B N   1 
ATOM   4605  C  CA  . ASP B  1 270 ? -31.180 -8.607  33.894  1.00 23.17 ? 273  ASP B CA  1 
ATOM   4606  C  C   . ASP B  1 270 ? -31.456 -9.691  34.906  1.00 24.55 ? 273  ASP B C   1 
ATOM   4607  O  O   . ASP B  1 270 ? -32.331 -10.555 34.689  1.00 21.70 ? 273  ASP B O   1 
ATOM   4608  C  CB  . ASP B  1 270 ? -30.785 -7.314  34.593  1.00 24.92 ? 273  ASP B CB  1 
ATOM   4609  C  CG  . ASP B  1 270 ? -31.947 -6.684  35.363  1.00 27.81 ? 273  ASP B CG  1 
ATOM   4610  O  OD1 . ASP B  1 270 ? -32.661 -7.418  36.096  1.00 28.14 ? 273  ASP B OD1 1 
ATOM   4611  O  OD2 . ASP B  1 270 ? -32.090 -5.446  35.290  1.00 27.57 ? 273  ASP B OD2 1 
ATOM   4612  N  N   . PHE B  1 271 ? -30.687 -9.692  35.992  1.00 23.14 ? 274  PHE B N   1 
ATOM   4613  C  CA  . PHE B  1 271 ? -30.761 -10.813 36.910  1.00 22.95 ? 274  PHE B CA  1 
ATOM   4614  C  C   . PHE B  1 271 ? -32.017 -10.777 37.746  1.00 22.26 ? 274  PHE B C   1 
ATOM   4615  O  O   . PHE B  1 271 ? -32.499 -11.816 38.171  1.00 19.38 ? 274  PHE B O   1 
ATOM   4616  C  CB  . PHE B  1 271 ? -29.503 -10.923 37.762  1.00 23.37 ? 274  PHE B CB  1 
ATOM   4617  C  CG  . PHE B  1 271 ? -28.380 -11.558 37.031  1.00 20.29 ? 274  PHE B CG  1 
ATOM   4618  C  CD1 . PHE B  1 271 ? -28.418 -12.910 36.754  1.00 17.01 ? 274  PHE B CD1 1 
ATOM   4619  C  CD2 . PHE B  1 271 ? -27.403 -10.776 36.439  1.00 16.72 ? 274  PHE B CD2 1 
ATOM   4620  C  CE1 . PHE B  1 271 ? -27.456 -13.476 35.961  1.00 19.97 ? 274  PHE B CE1 1 
ATOM   4621  C  CE2 . PHE B  1 271 ? -26.405 -11.349 35.708  1.00 17.59 ? 274  PHE B CE2 1 
ATOM   4622  C  CZ  . PHE B  1 271 ? -26.442 -12.691 35.440  1.00 19.12 ? 274  PHE B CZ  1 
ATOM   4623  N  N   . SER B  1 272 ? -32.623 -9.593  37.820  1.00 25.15 ? 275  SER B N   1 
ATOM   4624  C  CA  . SER B  1 272 ? -33.927 -9.429  38.460  1.00 27.76 ? 275  SER B CA  1 
ATOM   4625  C  C   . SER B  1 272 ? -35.081 -9.948  37.594  1.00 28.23 ? 275  SER B C   1 
ATOM   4626  O  O   . SER B  1 272 ? -36.174 -10.190 38.106  1.00 27.73 ? 275  SER B O   1 
ATOM   4627  C  CB  . SER B  1 272 ? -34.167 -7.960  38.824  1.00 25.28 ? 275  SER B CB  1 
ATOM   4628  O  OG  . SER B  1 272 ? -34.678 -7.249  37.714  1.00 25.75 ? 275  SER B OG  1 
ATOM   4629  N  N   . THR B  1 273 ? -34.838 -10.137 36.295  1.00 28.22 ? 276  THR B N   1 
ATOM   4630  C  CA  . THR B  1 273 ? -35.912 -10.548 35.365  1.00 26.93 ? 276  THR B CA  1 
ATOM   4631  C  C   . THR B  1 273 ? -35.578 -11.768 34.509  1.00 23.66 ? 276  THR B C   1 
ATOM   4632  O  O   . THR B  1 273 ? -35.552 -11.686 33.283  1.00 23.32 ? 276  THR B O   1 
ATOM   4633  C  CB  . THR B  1 273 ? -36.341 -9.396  34.440  1.00 28.45 ? 276  THR B CB  1 
ATOM   4634  O  OG1 . THR B  1 273 ? -35.215 -8.943  33.669  1.00 26.60 ? 276  THR B OG1 1 
ATOM   4635  C  CG2 . THR B  1 273 ? -36.912 -8.234  35.262  1.00 28.80 ? 276  THR B CG2 1 
ATOM   4636  N  N   . PRO B  1 274 ? -35.359 -12.915 35.153  1.00 24.55 ? 277  PRO B N   1 
ATOM   4637  C  CA  . PRO B  1 274 ? -35.020 -14.138 34.425  1.00 25.51 ? 277  PRO B CA  1 
ATOM   4638  C  C   . PRO B  1 274 ? -36.126 -14.611 33.470  1.00 27.06 ? 277  PRO B C   1 
ATOM   4639  O  O   . PRO B  1 274 ? -35.862 -15.348 32.503  1.00 28.49 ? 277  PRO B O   1 
ATOM   4640  C  CB  . PRO B  1 274 ? -34.804 -15.168 35.542  1.00 23.05 ? 277  PRO B CB  1 
ATOM   4641  C  CG  . PRO B  1 274 ? -35.534 -14.577 36.757  1.00 22.37 ? 277  PRO B CG  1 
ATOM   4642  C  CD  . PRO B  1 274 ? -35.367 -13.108 36.617  1.00 22.04 ? 277  PRO B CD  1 
ATOM   4643  N  N   . CYS B  1 275 ? -37.365 -14.292 33.784  1.00 25.07 ? 278  CYS B N   1 
ATOM   4644  C  CA  . CYS B  1 275 ? -38.450 -14.836 32.980  1.00 26.35 ? 278  CYS B CA  1 
ATOM   4645  C  C   . CYS B  1 275 ? -38.546 -14.035 31.713  1.00 22.69 ? 278  CYS B C   1 
ATOM   4646  O  O   . CYS B  1 275 ? -38.910 -14.562 30.680  1.00 21.39 ? 278  CYS B O   1 
ATOM   4647  C  CB  . CYS B  1 275 ? -39.781 -14.790 33.722  1.00 28.04 ? 278  CYS B CB  1 
ATOM   4648  S  SG  . CYS B  1 275 ? -39.861 -15.939 35.058  1.00 31.48 ? 278  CYS B SG  1 
ATOM   4649  N  N   . LEU B  1 276 ? -38.175 -12.766 31.800  1.00 22.64 ? 279  LEU B N   1 
ATOM   4650  C  CA  . LEU B  1 276 ? -38.131 -11.888 30.648  1.00 26.61 ? 279  LEU B CA  1 
ATOM   4651  C  C   . LEU B  1 276 ? -36.949 -12.241 29.746  1.00 28.22 ? 279  LEU B C   1 
ATOM   4652  O  O   . LEU B  1 276 ? -36.971 -12.002 28.522  1.00 27.91 ? 279  LEU B O   1 
ATOM   4653  C  CB  . LEU B  1 276 ? -37.986 -10.435 31.099  1.00 28.47 ? 279  LEU B CB  1 
ATOM   4654  C  CG  . LEU B  1 276 ? -37.851 -9.471  29.922  1.00 30.39 ? 279  LEU B CG  1 
ATOM   4655  C  CD1 . LEU B  1 276 ? -39.166 -9.436  29.112  1.00 31.39 ? 279  LEU B CD1 1 
ATOM   4656  C  CD2 . LEU B  1 276 ? -37.444 -8.064  30.368  1.00 32.32 ? 279  LEU B CD2 1 
ATOM   4657  N  N   . MET B  1 277 ? -35.892 -12.756 30.354  1.00 27.17 ? 280  MET B N   1 
ATOM   4658  C  CA  . MET B  1 277 ? -34.770 -13.222 29.559  1.00 26.55 ? 280  MET B CA  1 
ATOM   4659  C  C   . MET B  1 277 ? -35.169 -14.465 28.767  1.00 23.05 ? 280  MET B C   1 
ATOM   4660  O  O   . MET B  1 277 ? -34.863 -14.563 27.579  1.00 20.98 ? 280  MET B O   1 
ATOM   4661  C  CB  . MET B  1 277 ? -33.527 -13.455 30.419  1.00 26.39 ? 280  MET B CB  1 
ATOM   4662  C  CG  . MET B  1 277 ? -32.299 -13.917 29.632  1.00 30.12 ? 280  MET B CG  1 
ATOM   4663  S  SD  . MET B  1 277 ? -32.202 -15.732 29.618  1.00 34.03 ? 280  MET B SD  1 
ATOM   4664  C  CE  . MET B  1 277 ? -32.333 -16.078 31.370  1.00 37.93 ? 280  MET B CE  1 
ATOM   4665  N  N   . TYR B  1 278 ? -35.867 -15.395 29.418  1.00 21.99 ? 281  TYR B N   1 
ATOM   4666  C  CA  . TYR B  1 278 ? -36.441 -16.559 28.723  1.00 22.59 ? 281  TYR B CA  1 
ATOM   4667  C  C   . TYR B  1 278 ? -37.373 -16.135 27.583  1.00 25.50 ? 281  TYR B C   1 
ATOM   4668  O  O   . TYR B  1 278 ? -37.215 -16.574 26.441  1.00 24.89 ? 281  TYR B O   1 
ATOM   4669  C  CB  . TYR B  1 278 ? -37.196 -17.468 29.699  1.00 20.70 ? 281  TYR B CB  1 
ATOM   4670  C  CG  . TYR B  1 278 ? -38.222 -18.384 29.044  1.00 25.02 ? 281  TYR B CG  1 
ATOM   4671  C  CD1 . TYR B  1 278 ? -37.832 -19.553 28.388  1.00 24.59 ? 281  TYR B CD1 1 
ATOM   4672  C  CD2 . TYR B  1 278 ? -39.589 -18.121 29.149  1.00 24.77 ? 281  TYR B CD2 1 
ATOM   4673  C  CE1 . TYR B  1 278 ? -38.772 -20.402 27.792  1.00 24.44 ? 281  TYR B CE1 1 
ATOM   4674  C  CE2 . TYR B  1 278 ? -40.538 -18.945 28.533  1.00 23.25 ? 281  TYR B CE2 1 
ATOM   4675  C  CZ  . TYR B  1 278 ? -40.128 -20.079 27.842  1.00 24.89 ? 281  TYR B CZ  1 
ATOM   4676  O  OH  . TYR B  1 278 ? -41.084 -20.933 27.286  1.00 20.15 ? 281  TYR B OH  1 
ATOM   4677  N  N   . GLU B  1 279 ? -38.264 -15.190 27.873  1.00 25.52 ? 282  GLU B N   1 
ATOM   4678  C  CA  . GLU B  1 279 ? -39.295 -14.813 26.920  1.00 29.16 ? 282  GLU B CA  1 
ATOM   4679  C  C   . GLU B  1 279 ? -38.669 -14.202 25.670  1.00 27.67 ? 282  GLU B C   1 
ATOM   4680  O  O   . GLU B  1 279 ? -39.091 -14.489 24.539  1.00 24.11 ? 282  GLU B O   1 
ATOM   4681  C  CB  . GLU B  1 279 ? -40.266 -13.824 27.566  1.00 32.85 ? 282  GLU B CB  1 
ATOM   4682  C  CG  . GLU B  1 279 ? -41.664 -13.790 26.965  1.00 37.51 ? 282  GLU B CG  1 
ATOM   4683  C  CD  . GLU B  1 279 ? -42.695 -13.186 27.926  1.00 41.18 ? 282  GLU B CD  1 
ATOM   4684  O  OE1 . GLU B  1 279 ? -42.955 -13.777 29.014  1.00 42.23 ? 282  GLU B OE1 1 
ATOM   4685  O  OE2 . GLU B  1 279 ? -43.213 -12.093 27.608  1.00 42.83 ? 282  GLU B OE2 1 
ATOM   4686  N  N   . LYS B  1 280 ? -37.670 -13.346 25.878  1.00 26.42 ? 283  LYS B N   1 
ATOM   4687  C  CA  . LYS B  1 280 ? -37.006 -12.694 24.763  1.00 25.94 ? 283  LYS B CA  1 
ATOM   4688  C  C   . LYS B  1 280 ? -36.190 -13.700 23.952  1.00 25.11 ? 283  LYS B C   1 
ATOM   4689  O  O   . LYS B  1 280 ? -36.180 -13.654 22.729  1.00 27.61 ? 283  LYS B O   1 
ATOM   4690  C  CB  . LYS B  1 280 ? -36.138 -11.518 25.238  1.00 27.44 ? 283  LYS B CB  1 
ATOM   4691  C  CG  . LYS B  1 280 ? -36.947 -10.296 25.716  1.00 32.17 ? 283  LYS B CG  1 
ATOM   4692  C  CD  . LYS B  1 280 ? -36.050 -9.137  26.206  1.00 32.48 ? 283  LYS B CD  1 
ATOM   4693  C  CE  . LYS B  1 280 ? -35.169 -8.598  25.075  1.00 33.81 ? 283  LYS B CE  1 
ATOM   4694  N  NZ  . LYS B  1 280 ? -35.092 -7.100  25.020  1.00 30.88 ? 283  LYS B NZ  1 
ATOM   4695  N  N   . PHE B  1 281 ? -35.509 -14.612 24.626  1.00 21.58 ? 284  PHE B N   1 
ATOM   4696  C  CA  . PHE B  1 281 ? -34.742 -15.625 23.903  1.00 22.33 ? 284  PHE B CA  1 
ATOM   4697  C  C   . PHE B  1 281 ? -35.677 -16.379 22.963  1.00 20.63 ? 284  PHE B C   1 
ATOM   4698  O  O   . PHE B  1 281 ? -35.351 -16.610 21.818  1.00 23.35 ? 284  PHE B O   1 
ATOM   4699  C  CB  . PHE B  1 281 ? -34.072 -16.611 24.872  1.00 18.81 ? 284  PHE B CB  1 
ATOM   4700  C  CG  . PHE B  1 281 ? -33.151 -17.592 24.199  1.00 23.29 ? 284  PHE B CG  1 
ATOM   4701  C  CD1 . PHE B  1 281 ? -31.902 -17.184 23.730  1.00 20.37 ? 284  PHE B CD1 1 
ATOM   4702  C  CD2 . PHE B  1 281 ? -33.514 -18.935 24.080  1.00 22.80 ? 284  PHE B CD2 1 
ATOM   4703  C  CE1 . PHE B  1 281 ? -31.041 -18.088 23.126  1.00 24.77 ? 284  PHE B CE1 1 
ATOM   4704  C  CE2 . PHE B  1 281 ? -32.685 -19.839 23.436  1.00 24.39 ? 284  PHE B CE2 1 
ATOM   4705  C  CZ  . PHE B  1 281 ? -31.425 -19.433 22.989  1.00 25.22 ? 284  PHE B CZ  1 
ATOM   4706  N  N   . VAL B  1 282 ? -36.826 -16.803 23.468  1.00 23.49 ? 285  VAL B N   1 
ATOM   4707  C  CA  . VAL B  1 282 ? -37.671 -17.708 22.704  1.00 21.35 ? 285  VAL B CA  1 
ATOM   4708  C  C   . VAL B  1 282 ? -38.439 -16.945 21.637  1.00 20.89 ? 285  VAL B C   1 
ATOM   4709  O  O   . VAL B  1 282 ? -38.336 -17.262 20.471  1.00 20.81 ? 285  VAL B O   1 
ATOM   4710  C  CB  . VAL B  1 282 ? -38.652 -18.461 23.592  1.00 21.22 ? 285  VAL B CB  1 
ATOM   4711  C  CG1 . VAL B  1 282 ? -39.838 -18.911 22.753  1.00 23.90 ? 285  VAL B CG1 1 
ATOM   4712  C  CG2 . VAL B  1 282 ? -37.949 -19.673 24.244  1.00 20.25 ? 285  VAL B CG2 1 
ATOM   4713  N  N   . ASN B  1 283 ? -39.018 -15.813 22.028  1.00 21.60 ? 286  ASN B N   1 
ATOM   4714  C  CA  . ASN B  1 283 ? -40.022 -15.142 21.223  1.00 22.60 ? 286  ASN B CA  1 
ATOM   4715  C  C   . ASN B  1 283 ? -39.451 -13.983 20.439  1.00 20.29 ? 286  ASN B C   1 
ATOM   4716  O  O   . ASN B  1 283 ? -40.125 -13.441 19.576  1.00 23.81 ? 286  ASN B O   1 
ATOM   4717  C  CB  . ASN B  1 283 ? -41.185 -14.653 22.096  1.00 23.48 ? 286  ASN B CB  1 
ATOM   4718  C  CG  . ASN B  1 283 ? -42.468 -15.404 21.830  1.00 24.30 ? 286  ASN B CG  1 
ATOM   4719  O  OD1 . ASN B  1 283 ? -42.462 -16.623 21.635  1.00 22.58 ? 286  ASN B OD1 1 
ATOM   4720  N  ND2 . ASN B  1 283 ? -43.590 -14.683 21.872  1.00 26.16 ? 286  ASN B ND2 1 
ATOM   4721  N  N   . ILE B  1 284 ? -38.194 -13.636 20.694  1.00 20.32 ? 287  ILE B N   1 
ATOM   4722  C  CA  . ILE B  1 284 ? -37.475 -12.690 19.832  1.00 19.89 ? 287  ILE B CA  1 
ATOM   4723  C  C   . ILE B  1 284 ? -36.264 -13.298 19.117  1.00 23.72 ? 287  ILE B C   1 
ATOM   4724  O  O   . ILE B  1 284 ? -36.120 -13.156 17.894  1.00 23.32 ? 287  ILE B O   1 
ATOM   4725  C  CB  . ILE B  1 284 ? -37.069 -11.412 20.592  1.00 23.77 ? 287  ILE B CB  1 
ATOM   4726  C  CG1 . ILE B  1 284 ? -38.311 -10.719 21.178  1.00 22.49 ? 287  ILE B CG1 1 
ATOM   4727  C  CG2 . ILE B  1 284 ? -36.310 -10.424 19.669  1.00 21.09 ? 287  ILE B CG2 1 
ATOM   4728  C  CD1 . ILE B  1 284 ? -38.018 -9.289  21.637  1.00 24.35 ? 287  ILE B CD1 1 
ATOM   4729  N  N   . THR B  1 285 ? -35.427 -14.026 19.857  1.00 27.10 ? 288  THR B N   1 
ATOM   4730  C  CA  . THR B  1 285 ? -34.137 -14.472 19.321  1.00 25.81 ? 288  THR B CA  1 
ATOM   4731  C  C   . THR B  1 285 ? -34.311 -15.684 18.409  1.00 27.06 ? 288  THR B C   1 
ATOM   4732  O  O   . THR B  1 285 ? -33.946 -15.650 17.226  1.00 25.65 ? 288  THR B O   1 
ATOM   4733  C  CB  . THR B  1 285 ? -33.122 -14.762 20.456  1.00 25.25 ? 288  THR B CB  1 
ATOM   4734  O  OG1 . THR B  1 285 ? -32.788 -13.520 21.082  1.00 28.98 ? 288  THR B OG1 1 
ATOM   4735  C  CG2 . THR B  1 285 ? -31.815 -15.412 19.911  1.00 17.15 ? 288  THR B CG2 1 
ATOM   4736  N  N   . VAL B  1 286 ? -34.855 -16.760 18.968  1.00 24.51 ? 289  VAL B N   1 
ATOM   4737  C  CA  . VAL B  1 286 ? -35.222 -17.920 18.170  1.00 22.72 ? 289  VAL B CA  1 
ATOM   4738  C  C   . VAL B  1 286 ? -36.221 -17.576 17.051  1.00 21.86 ? 289  VAL B C   1 
ATOM   4739  O  O   . VAL B  1 286 ? -36.025 -17.951 15.906  1.00 24.39 ? 289  VAL B O   1 
ATOM   4740  C  CB  . VAL B  1 286 ? -35.743 -19.049 19.066  1.00 21.47 ? 289  VAL B CB  1 
ATOM   4741  C  CG1 . VAL B  1 286 ? -36.302 -20.221 18.239  1.00 19.18 ? 289  VAL B CG1 1 
ATOM   4742  C  CG2 . VAL B  1 286 ? -34.630 -19.532 19.978  1.00 20.15 ? 289  VAL B CG2 1 
ATOM   4743  N  N   . LYS B  1 287 ? -37.257 -16.814 17.377  1.00 23.72 ? 290  LYS B N   1 
ATOM   4744  C  CA  . LYS B  1 287 ? -38.283 -16.443 16.402  1.00 20.87 ? 290  LYS B CA  1 
ATOM   4745  C  C   . LYS B  1 287 ? -37.653 -15.864 15.139  1.00 22.88 ? 290  LYS B C   1 
ATOM   4746  O  O   . LYS B  1 287 ? -38.010 -16.262 14.032  1.00 23.91 ? 290  LYS B O   1 
ATOM   4747  C  CB  . LYS B  1 287 ? -39.241 -15.421 17.012  1.00 23.35 ? 290  LYS B CB  1 
ATOM   4748  C  CG  . LYS B  1 287 ? -40.357 -14.977 16.076  1.00 22.70 ? 290  LYS B CG  1 
ATOM   4749  C  CD  . LYS B  1 287 ? -41.416 -16.066 15.937  1.00 27.39 ? 290  LYS B CD  1 
ATOM   4750  C  CE  . LYS B  1 287 ? -42.484 -15.688 14.895  1.00 28.81 ? 290  LYS B CE  1 
ATOM   4751  N  NZ  . LYS B  1 287 ? -43.227 -14.446 15.311  1.00 30.89 ? 290  LYS B NZ  1 
ATOM   4752  N  N   . SER B  1 288 ? -36.746 -14.901 15.318  1.00 22.80 ? 291  SER B N   1 
ATOM   4753  C  CA  . SER B  1 288 ? -36.098 -14.198 14.218  1.00 25.61 ? 291  SER B CA  1 
ATOM   4754  C  C   . SER B  1 288 ? -35.239 -15.074 13.302  1.00 27.11 ? 291  SER B C   1 
ATOM   4755  O  O   . SER B  1 288 ? -35.111 -14.787 12.103  1.00 25.48 ? 291  SER B O   1 
ATOM   4756  C  CB  . SER B  1 288 ? -35.254 -13.037 14.746  1.00 30.47 ? 291  SER B CB  1 
ATOM   4757  O  OG  . SER B  1 288 ? -36.080 -12.021 15.296  1.00 34.75 ? 291  SER B OG  1 
ATOM   4758  N  N   . LEU B  1 289 ? -34.637 -16.120 13.866  1.00 25.39 ? 292  LEU B N   1 
ATOM   4759  C  CA  . LEU B  1 289 ? -33.899 -17.097 13.065  1.00 25.16 ? 292  LEU B CA  1 
ATOM   4760  C  C   . LEU B  1 289 ? -34.872 -17.950 12.231  1.00 25.37 ? 292  LEU B C   1 
ATOM   4761  O  O   . LEU B  1 289 ? -34.534 -18.422 11.131  1.00 23.75 ? 292  LEU B O   1 
ATOM   4762  C  CB  . LEU B  1 289 ? -33.024 -17.987 13.964  1.00 22.10 ? 292  LEU B CB  1 
ATOM   4763  C  CG  . LEU B  1 289 ? -31.933 -17.342 14.841  1.00 23.20 ? 292  LEU B CG  1 
ATOM   4764  C  CD1 . LEU B  1 289 ? -31.206 -18.401 15.688  1.00 24.56 ? 292  LEU B CD1 1 
ATOM   4765  C  CD2 . LEU B  1 289 ? -30.938 -16.552 14.021  1.00 22.81 ? 292  LEU B CD2 1 
ATOM   4766  N  N   . TYR B  1 290 ? -36.064 -18.166 12.782  1.00 22.82 ? 293  TYR B N   1 
ATOM   4767  C  CA  . TYR B  1 290 ? -37.040 -19.076 12.196  1.00 22.37 ? 293  TYR B CA  1 
ATOM   4768  C  C   . TYR B  1 290 ? -38.441 -18.450 12.163  1.00 24.19 ? 293  TYR B C   1 
ATOM   4769  O  O   . TYR B  1 290 ? -39.321 -18.872 12.908  1.00 23.92 ? 293  TYR B O   1 
ATOM   4770  C  CB  . TYR B  1 290 ? -37.112 -20.341 13.029  1.00 19.00 ? 293  TYR B CB  1 
ATOM   4771  C  CG  . TYR B  1 290 ? -35.864 -21.179 13.008  1.00 21.04 ? 293  TYR B CG  1 
ATOM   4772  C  CD1 . TYR B  1 290 ? -35.630 -22.080 11.977  1.00 18.35 ? 293  TYR B CD1 1 
ATOM   4773  C  CD2 . TYR B  1 290 ? -34.952 -21.143 14.071  1.00 20.27 ? 293  TYR B CD2 1 
ATOM   4774  C  CE1 . TYR B  1 290 ? -34.509 -22.884 11.971  1.00 18.93 ? 293  TYR B CE1 1 
ATOM   4775  C  CE2 . TYR B  1 290 ? -33.816 -21.928 14.061  1.00 17.49 ? 293  TYR B CE2 1 
ATOM   4776  C  CZ  . TYR B  1 290 ? -33.598 -22.803 13.016  1.00 18.76 ? 293  TYR B CZ  1 
ATOM   4777  O  OH  . TYR B  1 290 ? -32.464 -23.592 13.005  1.00 16.25 ? 293  TYR B OH  1 
ATOM   4778  N  N   . PRO B  1 291 ? -38.637 -17.419 11.328  1.00 25.48 ? 294  PRO B N   1 
ATOM   4779  C  CA  . PRO B  1 291 ? -39.770 -16.499 11.513  1.00 27.63 ? 294  PRO B CA  1 
ATOM   4780  C  C   . PRO B  1 291 ? -41.089 -17.091 11.059  1.00 29.11 ? 294  PRO B C   1 
ATOM   4781  O  O   . PRO B  1 291 ? -42.134 -16.776 11.618  1.00 29.49 ? 294  PRO B O   1 
ATOM   4782  C  CB  . PRO B  1 291 ? -39.419 -15.299 10.636  1.00 24.19 ? 294  PRO B CB  1 
ATOM   4783  C  CG  . PRO B  1 291 ? -38.348 -15.804 9.697   1.00 26.46 ? 294  PRO B CG  1 
ATOM   4784  C  CD  . PRO B  1 291 ? -37.608 -16.874 10.430  1.00 24.87 ? 294  PRO B CD  1 
ATOM   4785  N  N   . ASN B  1 292 ? -41.056 -17.931 10.041  1.00 31.95 ? 295  ASN B N   1 
ATOM   4786  C  CA  . ASN B  1 292 ? -42.156 -18.856 9.871   1.00 36.69 ? 295  ASN B CA  1 
ATOM   4787  C  C   . ASN B  1 292 ? -41.796 -20.129 9.153   1.00 34.67 ? 295  ASN B C   1 
ATOM   4788  O  O   . ASN B  1 292 ? -41.621 -20.153 7.932   1.00 33.79 ? 295  ASN B O   1 
ATOM   4789  C  CB  . ASN B  1 292 ? -43.403 -18.193 9.295   1.00 42.51 ? 295  ASN B CB  1 
ATOM   4790  C  CG  . ASN B  1 292 ? -43.331 -18.037 7.824   1.00 45.58 ? 295  ASN B CG  1 
ATOM   4791  O  OD1 . ASN B  1 292 ? -44.113 -18.636 7.081   1.00 46.35 ? 295  ASN B OD1 1 
ATOM   4792  N  ND2 . ASN B  1 292 ? -42.371 -17.239 7.371   1.00 49.57 ? 295  ASN B ND2 1 
ATOM   4793  N  N   . PRO B  1 293 ? -41.587 -21.178 9.948   1.00 32.86 ? 296  PRO B N   1 
ATOM   4794  C  CA  . PRO B  1 293 ? -41.025 -22.440 9.531   1.00 30.68 ? 296  PRO B CA  1 
ATOM   4795  C  C   . PRO B  1 293 ? -42.089 -23.312 8.876   1.00 31.63 ? 296  PRO B C   1 
ATOM   4796  O  O   . PRO B  1 293 ? -43.267 -23.225 9.230   1.00 28.18 ? 296  PRO B O   1 
ATOM   4797  C  CB  . PRO B  1 293 ? -40.581 -23.057 10.853  1.00 28.57 ? 296  PRO B CB  1 
ATOM   4798  C  CG  . PRO B  1 293 ? -41.589 -22.542 11.838  1.00 30.14 ? 296  PRO B CG  1 
ATOM   4799  C  CD  . PRO B  1 293 ? -41.872 -21.143 11.394  1.00 29.59 ? 296  PRO B CD  1 
ATOM   4800  N  N   . THR B  1 294 ? -41.643 -24.197 7.986   1.00 33.06 ? 297  THR B N   1 
ATOM   4801  C  CA  . THR B  1 294 ? -42.479 -25.218 7.388   1.00 32.60 ? 297  THR B CA  1 
ATOM   4802  C  C   . THR B  1 294 ? -42.970 -26.155 8.471   1.00 31.83 ? 297  THR B C   1 
ATOM   4803  O  O   . THR B  1 294 ? -42.476 -26.115 9.599   1.00 32.62 ? 297  THR B O   1 
ATOM   4804  C  CB  . THR B  1 294 ? -41.678 -26.043 6.354   1.00 35.49 ? 297  THR B CB  1 
ATOM   4805  O  OG1 . THR B  1 294 ? -40.498 -26.560 6.979   1.00 36.33 ? 297  THR B OG1 1 
ATOM   4806  C  CG2 . THR B  1 294 ? -41.280 -25.178 5.160   1.00 31.87 ? 297  THR B CG2 1 
ATOM   4807  N  N   . VAL B  1 295 ? -43.993 -26.946 8.152   1.00 29.34 ? 298  VAL B N   1 
ATOM   4808  C  CA  . VAL B  1 295 ? -44.607 -27.854 9.125   1.00 27.13 ? 298  VAL B CA  1 
ATOM   4809  C  C   . VAL B  1 295 ? -43.593 -28.662 9.940   1.00 27.87 ? 298  VAL B C   1 
ATOM   4810  O  O   . VAL B  1 295 ? -43.779 -28.875 11.147  1.00 29.00 ? 298  VAL B O   1 
ATOM   4811  C  CB  . VAL B  1 295 ? -45.581 -28.841 8.440   1.00 29.23 ? 298  VAL B CB  1 
ATOM   4812  C  CG1 . VAL B  1 295 ? -46.107 -29.877 9.454   1.00 29.12 ? 298  VAL B CG1 1 
ATOM   4813  C  CG2 . VAL B  1 295 ? -46.745 -28.079 7.780   1.00 30.36 ? 298  VAL B CG2 1 
ATOM   4814  N  N   . GLN B  1 296 ? -42.580 -29.202 9.270   1.00 25.30 ? 299  GLN B N   1 
ATOM   4815  C  CA  . GLN B  1 296 ? -41.652 -30.141 9.921   1.00 28.37 ? 299  GLN B CA  1 
ATOM   4816  C  C   . GLN B  1 296 ? -40.658 -29.446 10.838  1.00 26.29 ? 299  GLN B C   1 
ATOM   4817  O  O   . GLN B  1 296 ? -40.374 -29.910 11.929  1.00 27.30 ? 299  GLN B O   1 
ATOM   4818  C  CB  . GLN B  1 296 ? -40.905 -30.939 8.867   1.00 30.72 ? 299  GLN B CB  1 
ATOM   4819  C  CG  . GLN B  1 296 ? -39.868 -31.884 9.402   1.00 34.31 ? 299  GLN B CG  1 
ATOM   4820  C  CD  . GLN B  1 296 ? -39.164 -32.608 8.269   1.00 39.32 ? 299  GLN B CD  1 
ATOM   4821  O  OE1 . GLN B  1 296 ? -38.293 -32.037 7.603   1.00 41.58 ? 299  GLN B OE1 1 
ATOM   4822  N  NE2 . GLN B  1 296 ? -39.641 -33.811 7.949   1.00 39.87 ? 299  GLN B NE2 1 
ATOM   4823  N  N   . LEU B  1 297 ? -40.179 -28.290 10.400  1.00 29.23 ? 300  LEU B N   1 
ATOM   4824  C  CA  . LEU B  1 297 ? -39.292 -27.454 11.197  1.00 30.19 ? 300  LEU B CA  1 
ATOM   4825  C  C   . LEU B  1 297 ? -40.032 -26.879 12.418  1.00 30.88 ? 300  LEU B C   1 
ATOM   4826  O  O   . LEU B  1 297 ? -39.466 -26.810 13.519  1.00 29.85 ? 300  LEU B O   1 
ATOM   4827  C  CB  . LEU B  1 297 ? -38.728 -26.336 10.317  1.00 26.25 ? 300  LEU B CB  1 
ATOM   4828  C  CG  . LEU B  1 297 ? -37.436 -25.625 10.703  1.00 27.87 ? 300  LEU B CG  1 
ATOM   4829  C  CD1 . LEU B  1 297 ? -36.491 -26.579 11.448  1.00 27.80 ? 300  LEU B CD1 1 
ATOM   4830  C  CD2 . LEU B  1 297 ? -36.784 -25.100 9.426   1.00 24.96 ? 300  LEU B CD2 1 
ATOM   4831  N  N   . ARG B  1 298 ? -41.309 -26.537 12.240  1.00 27.40 ? 301  ARG B N   1 
ATOM   4832  C  CA  . ARG B  1 298 ? -42.116 -26.056 13.358  1.00 29.34 ? 301  ARG B CA  1 
ATOM   4833  C  C   . ARG B  1 298 ? -42.224 -27.123 14.442  1.00 28.67 ? 301  ARG B C   1 
ATOM   4834  O  O   . ARG B  1 298 ? -41.925 -26.863 15.601  1.00 28.17 ? 301  ARG B O   1 
ATOM   4835  C  CB  . ARG B  1 298 ? -43.514 -25.587 12.904  1.00 32.37 ? 301  ARG B CB  1 
ATOM   4836  C  CG  . ARG B  1 298 ? -44.183 -24.579 13.850  1.00 35.76 ? 301  ARG B CG  1 
ATOM   4837  C  CD  . ARG B  1 298 ? -45.686 -24.400 13.599  1.00 37.32 ? 301  ARG B CD  1 
ATOM   4838  N  NE  . ARG B  1 298 ? -46.395 -25.624 13.949  1.00 41.69 ? 301  ARG B NE  1 
ATOM   4839  C  CZ  . ARG B  1 298 ? -47.141 -25.794 15.034  1.00 39.85 ? 301  ARG B CZ  1 
ATOM   4840  N  NH1 . ARG B  1 298 ? -47.412 -24.778 15.842  1.00 38.69 ? 301  ARG B NH1 1 
ATOM   4841  N  NH2 . ARG B  1 298 ? -47.689 -26.977 15.256  1.00 40.59 ? 301  ARG B NH2 1 
ATOM   4842  N  N   . LYS B  1 299 ? -42.584 -28.340 14.053  1.00 26.65 ? 302  LYS B N   1 
ATOM   4843  C  CA  . LYS B  1 299 ? -42.602 -29.461 14.987  1.00 27.81 ? 302  LYS B CA  1 
ATOM   4844  C  C   . LYS B  1 299 ? -41.295 -29.597 15.792  1.00 27.36 ? 302  LYS B C   1 
ATOM   4845  O  O   . LYS B  1 299 ? -41.336 -29.741 17.012  1.00 26.42 ? 302  LYS B O   1 
ATOM   4846  C  CB  . LYS B  1 299 ? -42.910 -30.775 14.261  1.00 30.60 ? 302  LYS B CB  1 
ATOM   4847  C  CG  . LYS B  1 299 ? -43.500 -31.855 15.168  1.00 36.79 ? 302  LYS B CG  1 
ATOM   4848  C  CD  . LYS B  1 299 ? -43.675 -33.197 14.442  1.00 39.11 ? 302  LYS B CD  1 
ATOM   4849  C  CE  . LYS B  1 299 ? -42.659 -34.253 14.917  1.00 42.27 ? 302  LYS B CE  1 
ATOM   4850  N  NZ  . LYS B  1 299 ? -43.026 -34.875 16.227  1.00 42.17 ? 302  LYS B NZ  1 
ATOM   4851  N  N   . ALA B  1 300 ? -40.150 -29.553 15.102  1.00 22.05 ? 303  ALA B N   1 
ATOM   4852  C  CA  . ALA B  1 300 ? -38.843 -29.722 15.740  1.00 21.45 ? 303  ALA B CA  1 
ATOM   4853  C  C   . ALA B  1 300 ? -38.567 -28.548 16.680  1.00 20.42 ? 303  ALA B C   1 
ATOM   4854  O  O   . ALA B  1 300 ? -38.157 -28.737 17.816  1.00 21.69 ? 303  ALA B O   1 
ATOM   4855  C  CB  . ALA B  1 300 ? -37.735 -29.808 14.663  1.00 18.19 ? 303  ALA B CB  1 
ATOM   4856  N  N   . LEU B  1 301 ? -38.845 -27.334 16.208  1.00 19.83 ? 304  LEU B N   1 
ATOM   4857  C  CA  . LEU B  1 301 ? -38.719 -26.149 17.039  1.00 19.79 ? 304  LEU B CA  1 
ATOM   4858  C  C   . LEU B  1 301 ? -39.509 -26.312 18.315  1.00 23.51 ? 304  LEU B C   1 
ATOM   4859  O  O   . LEU B  1 301 ? -38.969 -26.133 19.421  1.00 25.23 ? 304  LEU B O   1 
ATOM   4860  C  CB  . LEU B  1 301 ? -39.197 -24.908 16.288  1.00 20.64 ? 304  LEU B CB  1 
ATOM   4861  C  CG  . LEU B  1 301 ? -38.107 -24.385 15.351  1.00 20.06 ? 304  LEU B CG  1 
ATOM   4862  C  CD1 . LEU B  1 301 ? -38.694 -23.654 14.122  1.00 17.14 ? 304  LEU B CD1 1 
ATOM   4863  C  CD2 . LEU B  1 301 ? -37.171 -23.480 16.159  1.00 19.97 ? 304  LEU B CD2 1 
ATOM   4864  N  N   . ASN B  1 302 ? -40.769 -26.719 18.170  1.00 21.57 ? 305  ASN B N   1 
ATOM   4865  C  CA  . ASN B  1 302 ? -41.669 -26.834 19.308  1.00 20.99 ? 305  ASN B CA  1 
ATOM   4866  C  C   . ASN B  1 302 ? -41.196 -27.831 20.336  1.00 19.82 ? 305  ASN B C   1 
ATOM   4867  O  O   . ASN B  1 302 ? -41.289 -27.577 21.524  1.00 22.53 ? 305  ASN B O   1 
ATOM   4868  C  CB  . ASN B  1 302 ? -43.109 -27.122 18.866  1.00 20.77 ? 305  ASN B CB  1 
ATOM   4869  C  CG  . ASN B  1 302 ? -43.824 -25.865 18.431  1.00 21.35 ? 305  ASN B CG  1 
ATOM   4870  O  OD1 . ASN B  1 302 ? -43.396 -24.775 18.779  1.00 21.90 ? 305  ASN B OD1 1 
ATOM   4871  N  ND2 . ASN B  1 302 ? -44.933 -26.005 17.697  1.00 21.13 ? 305  ASN B ND2 1 
ATOM   4872  N  N   . THR B  1 303 ? -40.734 -28.983 19.867  1.00 22.11 ? 306  THR B N   1 
ATOM   4873  C  CA  . THR B  1 303 ? -40.195 -30.015 20.728  1.00 20.72 ? 306  THR B CA  1 
ATOM   4874  C  C   . THR B  1 303 ? -38.971 -29.495 21.492  1.00 20.64 ? 306  THR B C   1 
ATOM   4875  O  O   . THR B  1 303 ? -38.859 -29.690 22.686  1.00 16.85 ? 306  THR B O   1 
ATOM   4876  C  CB  . THR B  1 303 ? -39.757 -31.224 19.886  1.00 23.91 ? 306  THR B CB  1 
ATOM   4877  O  OG1 . THR B  1 303 ? -40.879 -31.697 19.142  1.00 25.12 ? 306  THR B OG1 1 
ATOM   4878  C  CG2 . THR B  1 303 ? -39.242 -32.358 20.777  1.00 20.58 ? 306  THR B CG2 1 
ATOM   4879  N  N   . ASN B  1 304 ? -38.042 -28.852 20.793  1.00 21.07 ? 307  ASN B N   1 
ATOM   4880  C  CA  . ASN B  1 304 ? -36.836 -28.361 21.443  1.00 16.80 ? 307  ASN B CA  1 
ATOM   4881  C  C   . ASN B  1 304 ? -37.130 -27.148 22.339  1.00 20.81 ? 307  ASN B C   1 
ATOM   4882  O  O   . ASN B  1 304 ? -36.465 -26.953 23.357  1.00 20.61 ? 307  ASN B O   1 
ATOM   4883  C  CB  . ASN B  1 304 ? -35.743 -28.060 20.410  1.00 14.90 ? 307  ASN B CB  1 
ATOM   4884  C  CG  . ASN B  1 304 ? -35.111 -29.321 19.841  1.00 14.19 ? 307  ASN B CG  1 
ATOM   4885  O  OD1 . ASN B  1 304 ? -34.254 -29.940 20.471  1.00 15.20 ? 307  ASN B OD1 1 
ATOM   4886  N  ND2 . ASN B  1 304 ? -35.557 -29.728 18.653  1.00 13.96 ? 307  ASN B ND2 1 
ATOM   4887  N  N   . LEU B  1 305 ? -38.196 -26.405 22.019  1.00 20.46 ? 308  LEU B N   1 
ATOM   4888  C  CA  . LEU B  1 305 ? -38.660 -25.318 22.874  1.00 19.41 ? 308  LEU B CA  1 
ATOM   4889  C  C   . LEU B  1 305 ? -39.259 -25.795 24.184  1.00 22.79 ? 308  LEU B C   1 
ATOM   4890  O  O   . LEU B  1 305 ? -39.036 -25.174 25.224  1.00 22.36 ? 308  LEU B O   1 
ATOM   4891  C  CB  . LEU B  1 305 ? -39.663 -24.429 22.151  1.00 21.45 ? 308  LEU B CB  1 
ATOM   4892  C  CG  . LEU B  1 305 ? -39.025 -23.426 21.187  1.00 22.63 ? 308  LEU B CG  1 
ATOM   4893  C  CD1 . LEU B  1 305 ? -40.042 -22.833 20.188  1.00 21.55 ? 308  LEU B CD1 1 
ATOM   4894  C  CD2 . LEU B  1 305 ? -38.297 -22.352 21.959  1.00 22.89 ? 308  LEU B CD2 1 
ATOM   4895  N  N   . ASP B  1 306 ? -39.992 -26.908 24.141  1.00 22.99 ? 309  ASP B N   1 
ATOM   4896  C  CA  . ASP B  1 306 ? -40.527 -27.498 25.355  1.00 24.39 ? 309  ASP B CA  1 
ATOM   4897  C  C   . ASP B  1 306 ? -39.359 -27.917 26.242  1.00 25.75 ? 309  ASP B C   1 
ATOM   4898  O  O   . ASP B  1 306 ? -39.350 -27.666 27.442  1.00 28.45 ? 309  ASP B O   1 
ATOM   4899  C  CB  . ASP B  1 306 ? -41.376 -28.736 25.027  1.00 28.81 ? 309  ASP B CB  1 
ATOM   4900  C  CG  . ASP B  1 306 ? -42.711 -28.397 24.357  1.00 30.72 ? 309  ASP B CG  1 
ATOM   4901  O  OD1 . ASP B  1 306 ? -43.233 -27.276 24.539  1.00 32.52 ? 309  ASP B OD1 1 
ATOM   4902  O  OD2 . ASP B  1 306 ? -43.265 -29.291 23.680  1.00 32.54 ? 309  ASP B OD2 1 
ATOM   4903  N  N   . PHE B  1 307 ? -38.377 -28.580 25.642  1.00 25.09 ? 310  PHE B N   1 
ATOM   4904  C  CA  . PHE B  1 307 ? -37.207 -29.043 26.372  1.00 23.58 ? 310  PHE B CA  1 
ATOM   4905  C  C   . PHE B  1 307 ? -36.435 -27.880 26.988  1.00 20.09 ? 310  PHE B C   1 
ATOM   4906  O  O   . PHE B  1 307 ? -36.091 -27.906 28.162  1.00 19.85 ? 310  PHE B O   1 
ATOM   4907  C  CB  . PHE B  1 307 ? -36.315 -29.872 25.452  1.00 24.74 ? 310  PHE B CB  1 
ATOM   4908  C  CG  . PHE B  1 307 ? -36.941 -31.171 25.015  1.00 26.91 ? 310  PHE B CG  1 
ATOM   4909  C  CD1 . PHE B  1 307 ? -38.037 -31.683 25.685  1.00 27.29 ? 310  PHE B CD1 1 
ATOM   4910  C  CD2 . PHE B  1 307 ? -36.385 -31.917 23.979  1.00 27.80 ? 310  PHE B CD2 1 
ATOM   4911  C  CE1 . PHE B  1 307 ? -38.588 -32.924 25.323  1.00 30.84 ? 310  PHE B CE1 1 
ATOM   4912  C  CE2 . PHE B  1 307 ? -36.931 -33.161 23.602  1.00 28.57 ? 310  PHE B CE2 1 
ATOM   4913  C  CZ  . PHE B  1 307 ? -38.033 -33.659 24.266  1.00 28.89 ? 310  PHE B CZ  1 
ATOM   4914  N  N   . PHE B  1 308 ? -36.197 -26.838 26.199  1.00 21.02 ? 311  PHE B N   1 
ATOM   4915  C  CA  . PHE B  1 308 ? -35.604 -25.618 26.729  1.00 20.27 ? 311  PHE B CA  1 
ATOM   4916  C  C   . PHE B  1 308 ? -36.344 -25.197 28.002  1.00 21.36 ? 311  PHE B C   1 
ATOM   4917  O  O   . PHE B  1 308 ? -35.744 -25.141 29.080  1.00 22.43 ? 311  PHE B O   1 
ATOM   4918  C  CB  . PHE B  1 308 ? -35.632 -24.493 25.689  1.00 16.48 ? 311  PHE B CB  1 
ATOM   4919  C  CG  . PHE B  1 308 ? -34.997 -23.216 26.162  1.00 15.06 ? 311  PHE B CG  1 
ATOM   4920  C  CD1 . PHE B  1 308 ? -33.752 -23.234 26.791  1.00 16.41 ? 311  PHE B CD1 1 
ATOM   4921  C  CD2 . PHE B  1 308 ? -35.624 -21.992 25.951  1.00 15.28 ? 311  PHE B CD2 1 
ATOM   4922  C  CE1 . PHE B  1 308 ? -33.161 -22.054 27.227  1.00 18.52 ? 311  PHE B CE1 1 
ATOM   4923  C  CE2 . PHE B  1 308 ? -35.060 -20.812 26.406  1.00 17.99 ? 311  PHE B CE2 1 
ATOM   4924  C  CZ  . PHE B  1 308 ? -33.819 -20.839 27.048  1.00 19.09 ? 311  PHE B CZ  1 
ATOM   4925  N  N   . PHE B  1 309 ? -37.662 -25.029 27.902  1.00 18.74 ? 312  PHE B N   1 
ATOM   4926  C  CA  . PHE B  1 309 ? -38.412 -24.384 28.978  1.00 21.30 ? 312  PHE B CA  1 
ATOM   4927  C  C   . PHE B  1 309 ? -38.272 -25.217 30.248  1.00 23.01 ? 312  PHE B C   1 
ATOM   4928  O  O   . PHE B  1 309 ? -38.141 -24.689 31.357  1.00 23.98 ? 312  PHE B O   1 
ATOM   4929  C  CB  . PHE B  1 309 ? -39.902 -24.217 28.608  1.00 20.56 ? 312  PHE B CB  1 
ATOM   4930  C  CG  . PHE B  1 309 ? -40.772 -23.822 29.784  1.00 20.60 ? 312  PHE B CG  1 
ATOM   4931  C  CD1 . PHE B  1 309 ? -40.791 -22.505 30.240  1.00 18.21 ? 312  PHE B CD1 1 
ATOM   4932  C  CD2 . PHE B  1 309 ? -41.506 -24.779 30.468  1.00 20.44 ? 312  PHE B CD2 1 
ATOM   4933  C  CE1 . PHE B  1 309 ? -41.566 -22.136 31.327  1.00 21.21 ? 312  PHE B CE1 1 
ATOM   4934  C  CE2 . PHE B  1 309 ? -42.274 -24.439 31.574  1.00 24.22 ? 312  PHE B CE2 1 
ATOM   4935  C  CZ  . PHE B  1 309 ? -42.324 -23.108 32.000  1.00 24.28 ? 312  PHE B CZ  1 
ATOM   4936  N  N   . GLN B  1 310 ? -38.191 -26.526 30.060  1.00 22.48 ? 313  GLN B N   1 
ATOM   4937  C  CA  . GLN B  1 310 ? -38.079 -27.451 31.169  1.00 26.19 ? 313  GLN B CA  1 
ATOM   4938  C  C   . GLN B  1 310 ? -36.816 -27.148 32.007  1.00 26.05 ? 313  GLN B C   1 
ATOM   4939  O  O   . GLN B  1 310 ? -36.781 -27.397 33.207  1.00 22.64 ? 313  GLN B O   1 
ATOM   4940  C  CB  . GLN B  1 310 ? -38.072 -28.880 30.626  1.00 29.62 ? 313  GLN B CB  1 
ATOM   4941  C  CG  . GLN B  1 310 ? -38.116 -29.972 31.667  1.00 36.27 ? 313  GLN B CG  1 
ATOM   4942  C  CD  . GLN B  1 310 ? -37.548 -31.281 31.137  1.00 39.75 ? 313  GLN B CD  1 
ATOM   4943  O  OE1 . GLN B  1 310 ? -36.434 -31.686 31.510  1.00 37.38 ? 313  GLN B OE1 1 
ATOM   4944  N  NE2 . GLN B  1 310 ? -38.275 -31.911 30.196  1.00 39.26 ? 313  GLN B NE2 1 
ATOM   4945  N  N   . GLY B  1 311 ? -35.848 -26.469 31.400  1.00 24.59 ? 314  GLY B N   1 
ATOM   4946  C  CA  . GLY B  1 311 ? -34.572 -26.229 32.057  1.00 24.10 ? 314  GLY B CA  1 
ATOM   4947  C  C   . GLY B  1 311 ? -34.515 -24.886 32.742  1.00 24.37 ? 314  GLY B C   1 
ATOM   4948  O  O   . GLY B  1 311 ? -33.526 -24.559 33.387  1.00 23.85 ? 314  GLY B O   1 
ATOM   4949  N  N   . VAL B  1 312 ? -35.569 -24.095 32.589  1.00 25.11 ? 315  VAL B N   1 
ATOM   4950  C  CA  . VAL B  1 312 ? -35.640 -22.804 33.269  1.00 28.56 ? 315  VAL B CA  1 
ATOM   4951  C  C   . VAL B  1 312 ? -35.920 -22.984 34.766  1.00 32.42 ? 315  VAL B C   1 
ATOM   4952  O  O   . VAL B  1 312 ? -37.063 -23.192 35.172  1.00 34.50 ? 315  VAL B O   1 
ATOM   4953  C  CB  . VAL B  1 312 ? -36.708 -21.908 32.639  1.00 26.74 ? 315  VAL B CB  1 
ATOM   4954  C  CG1 . VAL B  1 312 ? -36.747 -20.568 33.344  1.00 28.13 ? 315  VAL B CG1 1 
ATOM   4955  C  CG2 . VAL B  1 312 ? -36.404 -21.721 31.156  1.00 22.03 ? 315  VAL B CG2 1 
ATOM   4956  N  N   . ALA B  1 313 ? -34.867 -22.925 35.579  1.00 31.88 ? 316  ALA B N   1 
ATOM   4957  C  CA  . ALA B  1 313 ? -34.989 -23.176 37.018  1.00 33.86 ? 316  ALA B CA  1 
ATOM   4958  C  C   . ALA B  1 313 ? -35.788 -22.120 37.810  1.00 31.81 ? 316  ALA B C   1 
ATOM   4959  O  O   . ALA B  1 313 ? -36.389 -22.438 38.826  1.00 32.39 ? 316  ALA B O   1 
ATOM   4960  C  CB  . ALA B  1 313 ? -33.609 -23.394 37.641  1.00 34.93 ? 316  ALA B CB  1 
ATOM   4961  N  N   . ALA B  1 314 ? -35.785 -20.867 37.368  1.00 29.24 ? 317  ALA B N   1 
ATOM   4962  C  CA  . ALA B  1 314 ? -36.705 -19.881 37.942  1.00 29.05 ? 317  ALA B CA  1 
ATOM   4963  C  C   . ALA B  1 314 ? -38.196 -20.315 37.902  1.00 29.54 ? 317  ALA B C   1 
ATOM   4964  O  O   . ALA B  1 314 ? -39.025 -19.788 38.637  1.00 30.78 ? 317  ALA B O   1 
ATOM   4965  C  CB  . ALA B  1 314 ? -36.526 -18.530 37.270  1.00 25.58 ? 317  ALA B CB  1 
ATOM   4966  N  N   . GLY B  1 315 ? -38.536 -21.253 37.028  1.00 30.47 ? 318  GLY B N   1 
ATOM   4967  C  CA  . GLY B  1 315 ? -39.942 -21.516 36.713  1.00 30.61 ? 318  GLY B CA  1 
ATOM   4968  C  C   . GLY B  1 315 ? -40.441 -20.777 35.478  1.00 28.22 ? 318  GLY B C   1 
ATOM   4969  O  O   . GLY B  1 315 ? -40.268 -21.241 34.365  1.00 26.57 ? 318  GLY B O   1 
ATOM   4970  N  N   . CYS B  1 316 ? -41.092 -19.637 35.692  1.00 28.61 ? 319  CYS B N   1 
ATOM   4971  C  CA  . CYS B  1 316 ? -41.673 -18.827 34.610  1.00 28.93 ? 319  CYS B CA  1 
ATOM   4972  C  C   . CYS B  1 316 ? -42.907 -19.438 33.943  1.00 28.15 ? 319  CYS B C   1 
ATOM   4973  O  O   . CYS B  1 316 ? -43.222 -20.604 34.137  1.00 25.05 ? 319  CYS B O   1 
ATOM   4974  C  CB  . CYS B  1 316 ? -40.620 -18.480 33.559  1.00 30.63 ? 319  CYS B CB  1 
ATOM   4975  S  SG  . CYS B  1 316 ? -39.167 -17.676 34.253  1.00 30.88 ? 319  CYS B SG  1 
ATOM   4976  N  N   . THR B  1 317 ? -43.598 -18.629 33.152  1.00 31.91 ? 320  THR B N   1 
ATOM   4977  C  CA  . THR B  1 317 ? -44.676 -19.112 32.289  1.00 33.76 ? 320  THR B CA  1 
ATOM   4978  C  C   . THR B  1 317 ? -44.087 -19.399 30.909  1.00 31.09 ? 320  THR B C   1 
ATOM   4979  O  O   . THR B  1 317 ? -43.317 -18.599 30.400  1.00 30.35 ? 320  THR B O   1 
ATOM   4980  C  CB  . THR B  1 317 ? -45.742 -18.001 32.123  1.00 36.12 ? 320  THR B CB  1 
ATOM   4981  O  OG1 . THR B  1 317 ? -46.069 -17.470 33.407  1.00 36.78 ? 320  THR B OG1 1 
ATOM   4982  C  CG2 . THR B  1 317 ? -47.012 -18.524 31.452  1.00 34.86 ? 320  THR B CG2 1 
ATOM   4983  N  N   . GLN B  1 318 ? -44.402 -20.555 30.333  1.00 28.08 ? 321  GLN B N   1 
ATOM   4984  C  CA  . GLN B  1 318 ? -43.906 -20.892 28.992  1.00 27.73 ? 321  GLN B CA  1 
ATOM   4985  C  C   . GLN B  1 318 ? -44.478 -19.973 27.901  1.00 27.26 ? 321  GLN B C   1 
ATOM   4986  O  O   . GLN B  1 318 ? -45.650 -19.594 27.947  1.00 28.56 ? 321  GLN B O   1 
ATOM   4987  C  CB  . GLN B  1 318 ? -44.213 -22.352 28.665  1.00 27.65 ? 321  GLN B CB  1 
ATOM   4988  C  CG  . GLN B  1 318 ? -43.498 -22.867 27.418  1.00 28.23 ? 321  GLN B CG  1 
ATOM   4989  C  CD  . GLN B  1 318 ? -43.702 -24.347 27.216  1.00 26.21 ? 321  GLN B CD  1 
ATOM   4990  O  OE1 . GLN B  1 318 ? -44.263 -25.036 28.076  1.00 26.20 ? 321  GLN B OE1 1 
ATOM   4991  N  NE2 . GLN B  1 318 ? -43.282 -24.844 26.061  1.00 27.42 ? 321  GLN B NE2 1 
ATOM   4992  N  N   . VAL B  1 319 ? -43.645 -19.573 26.944  1.00 25.28 ? 322  VAL B N   1 
ATOM   4993  C  CA  . VAL B  1 319 ? -44.153 -18.862 25.793  1.00 24.72 ? 322  VAL B CA  1 
ATOM   4994  C  C   . VAL B  1 319 ? -44.047 -19.689 24.502  1.00 27.66 ? 322  VAL B C   1 
ATOM   4995  O  O   . VAL B  1 319 ? -43.361 -20.725 24.458  1.00 24.24 ? 322  VAL B O   1 
ATOM   4996  C  CB  . VAL B  1 319 ? -43.544 -17.446 25.656  1.00 28.08 ? 322  VAL B CB  1 
ATOM   4997  C  CG1 . VAL B  1 319 ? -43.529 -16.745 27.020  1.00 26.04 ? 322  VAL B CG1 1 
ATOM   4998  C  CG2 . VAL B  1 319 ? -42.156 -17.498 25.041  1.00 25.62 ? 322  VAL B CG2 1 
ATOM   4999  N  N   . PHE B  1 320 ? -44.865 -19.339 23.512  1.00 26.06 ? 323  PHE B N   1 
ATOM   5000  C  CA  . PHE B  1 320 ? -45.034 -20.210 22.346  1.00 27.11 ? 323  PHE B CA  1 
ATOM   5001  C  C   . PHE B  1 320 ? -45.006 -19.374 21.090  1.00 25.93 ? 323  PHE B C   1 
ATOM   5002  O  O   . PHE B  1 320 ? -46.028 -18.797 20.723  1.00 29.40 ? 323  PHE B O   1 
ATOM   5003  C  CB  . PHE B  1 320 ? -46.373 -20.975 22.418  1.00 27.97 ? 323  PHE B CB  1 
ATOM   5004  C  CG  . PHE B  1 320 ? -46.535 -21.813 23.661  1.00 27.08 ? 323  PHE B CG  1 
ATOM   5005  C  CD1 . PHE B  1 320 ? -46.128 -23.135 23.678  1.00 25.52 ? 323  PHE B CD1 1 
ATOM   5006  C  CD2 . PHE B  1 320 ? -47.130 -21.286 24.797  1.00 27.76 ? 323  PHE B CD2 1 
ATOM   5007  C  CE1 . PHE B  1 320 ? -46.286 -23.903 24.799  1.00 25.39 ? 323  PHE B CE1 1 
ATOM   5008  C  CE2 . PHE B  1 320 ? -47.286 -22.059 25.933  1.00 27.47 ? 323  PHE B CE2 1 
ATOM   5009  C  CZ  . PHE B  1 320 ? -46.883 -23.376 25.925  1.00 25.47 ? 323  PHE B CZ  1 
ATOM   5010  N  N   . PRO B  1 321 ? -43.832 -19.265 20.451  1.00 22.87 ? 324  PRO B N   1 
ATOM   5011  C  CA  . PRO B  1 321 ? -43.710 -18.423 19.259  1.00 19.90 ? 324  PRO B CA  1 
ATOM   5012  C  C   . PRO B  1 321 ? -44.549 -18.955 18.107  1.00 21.28 ? 324  PRO B C   1 
ATOM   5013  O  O   . PRO B  1 321 ? -44.917 -18.202 17.206  1.00 24.86 ? 324  PRO B O   1 
ATOM   5014  C  CB  . PRO B  1 321 ? -42.207 -18.494 18.899  1.00 19.40 ? 324  PRO B CB  1 
ATOM   5015  C  CG  . PRO B  1 321 ? -41.650 -19.658 19.645  1.00 19.68 ? 324  PRO B CG  1 
ATOM   5016  C  CD  . PRO B  1 321 ? -42.548 -19.870 20.859  1.00 22.69 ? 324  PRO B CD  1 
ATOM   5017  N  N   . TYR B  1 322 ? -44.777 -20.259 18.084  1.00 22.02 ? 325  TYR B N   1 
ATOM   5018  C  CA  . TYR B  1 322 ? -45.531 -20.851 16.996  1.00 25.87 ? 325  TYR B CA  1 
ATOM   5019  C  C   . TYR B  1 322 ? -46.808 -21.550 17.487  1.00 27.47 ? 325  TYR B C   1 
ATOM   5020  O  O   . TYR B  1 322 ? -47.264 -22.507 16.865  1.00 28.67 ? 325  TYR B O   1 
ATOM   5021  C  CB  . TYR B  1 322 ? -44.637 -21.826 16.191  1.00 26.59 ? 325  TYR B CB  1 
ATOM   5022  C  CG  . TYR B  1 322 ? -43.238 -21.296 15.914  1.00 23.59 ? 325  TYR B CG  1 
ATOM   5023  C  CD1 . TYR B  1 322 ? -43.022 -20.320 14.962  1.00 22.52 ? 325  TYR B CD1 1 
ATOM   5024  C  CD2 . TYR B  1 322 ? -42.146 -21.735 16.663  1.00 22.89 ? 325  TYR B CD2 1 
ATOM   5025  C  CE1 . TYR B  1 322 ? -41.734 -19.823 14.721  1.00 24.79 ? 325  TYR B CE1 1 
ATOM   5026  C  CE2 . TYR B  1 322 ? -40.870 -21.218 16.468  1.00 19.49 ? 325  TYR B CE2 1 
ATOM   5027  C  CZ  . TYR B  1 322 ? -40.667 -20.274 15.503  1.00 22.96 ? 325  TYR B CZ  1 
ATOM   5028  O  OH  . TYR B  1 322 ? -39.413 -19.748 15.336  1.00 19.55 ? 325  TYR B OH  1 
ATOM   5029  N  N   . GLY B  1 323 ? -47.330 -21.135 18.639  1.00 30.27 ? 326  GLY B N   1 
ATOM   5030  C  CA  . GLY B  1 323 ? -48.470 -21.822 19.266  1.00 35.23 ? 326  GLY B CA  1 
ATOM   5031  C  C   . GLY B  1 323 ? -48.176 -23.215 19.827  1.00 40.45 ? 326  GLY B C   1 
ATOM   5032  O  O   . GLY B  1 323 ? -47.018 -23.630 19.930  1.00 40.89 ? 326  GLY B O   1 
ATOM   5033  N  N   . ARG B  1 324 ? -49.226 -23.948 20.193  1.00 45.14 ? 327  ARG B N   1 
ATOM   5034  C  CA  . ARG B  1 324 ? -49.062 -25.299 20.738  1.00 47.51 ? 327  ARG B CA  1 
ATOM   5035  C  C   . ARG B  1 324 ? -49.342 -26.396 19.713  1.00 47.09 ? 327  ARG B C   1 
ATOM   5036  O  O   . ARG B  1 324 ? -50.457 -26.522 19.207  1.00 48.06 ? 327  ARG B O   1 
ATOM   5037  C  CB  . ARG B  1 324 ? -49.943 -25.490 21.971  1.00 49.83 ? 327  ARG B CB  1 
ATOM   5038  C  CG  . ARG B  1 324 ? -49.368 -24.880 23.238  1.00 53.65 ? 327  ARG B CG  1 
ATOM   5039  C  CD  . ARG B  1 324 ? -50.441 -24.712 24.309  1.00 56.55 ? 327  ARG B CD  1 
ATOM   5040  N  NE  . ARG B  1 324 ? -50.906 -23.330 24.381  1.00 58.45 ? 327  ARG B NE  1 
ATOM   5041  C  CZ  . ARG B  1 324 ? -50.995 -22.628 25.507  1.00 59.63 ? 327  ARG B CZ  1 
ATOM   5042  N  NH1 . ARG B  1 324 ? -50.696 -23.201 26.672  1.00 59.77 ? 327  ARG B NH1 1 
ATOM   5043  N  NH2 . ARG B  1 324 ? -51.378 -21.356 25.465  1.00 59.33 ? 327  ARG B NH2 1 
ATOM   5044  N  N   . LEU C  1 1   ? 23.081  -41.613 5.174   1.00 43.19 ? 4    LEU C N   1 
ATOM   5045  C  CA  . LEU C  1 1   ? 22.950  -40.810 6.428   1.00 45.54 ? 4    LEU C CA  1 
ATOM   5046  C  C   . LEU C  1 1   ? 24.306  -40.228 6.829   1.00 42.52 ? 4    LEU C C   1 
ATOM   5047  O  O   . LEU C  1 1   ? 25.344  -40.828 6.544   1.00 44.32 ? 4    LEU C O   1 
ATOM   5048  C  CB  . LEU C  1 1   ? 22.392  -41.672 7.566   1.00 47.21 ? 4    LEU C CB  1 
ATOM   5049  C  CG  . LEU C  1 1   ? 20.902  -42.059 7.561   1.00 50.03 ? 4    LEU C CG  1 
ATOM   5050  C  CD1 . LEU C  1 1   ? 20.511  -42.683 8.906   1.00 47.62 ? 4    LEU C CD1 1 
ATOM   5051  C  CD2 . LEU C  1 1   ? 19.990  -40.873 7.238   1.00 48.45 ? 4    LEU C CD2 1 
ATOM   5052  N  N   . PRO C  1 2   ? 24.301  -39.068 7.512   1.00 39.26 ? 5    PRO C N   1 
ATOM   5053  C  CA  . PRO C  1 2   ? 25.530  -38.639 8.156   1.00 34.28 ? 5    PRO C CA  1 
ATOM   5054  C  C   . PRO C  1 2   ? 25.975  -39.667 9.192   1.00 32.54 ? 5    PRO C C   1 
ATOM   5055  O  O   . PRO C  1 2   ? 25.143  -40.382 9.774   1.00 26.86 ? 5    PRO C O   1 
ATOM   5056  C  CB  . PRO C  1 2   ? 25.139  -37.336 8.860   1.00 35.52 ? 5    PRO C CB  1 
ATOM   5057  C  CG  . PRO C  1 2   ? 23.713  -37.041 8.442   1.00 38.31 ? 5    PRO C CG  1 
ATOM   5058  C  CD  . PRO C  1 2   ? 23.128  -38.346 8.036   1.00 39.42 ? 5    PRO C CD  1 
ATOM   5059  N  N   . PRO C  1 3   ? 27.287  -39.712 9.457   1.00 29.77 ? 6    PRO C N   1 
ATOM   5060  C  CA  . PRO C  1 3   ? 27.797  -40.551 10.516  1.00 29.08 ? 6    PRO C CA  1 
ATOM   5061  C  C   . PRO C  1 3   ? 27.220  -40.193 11.882  1.00 30.58 ? 6    PRO C C   1 
ATOM   5062  O  O   . PRO C  1 3   ? 26.834  -39.047 12.121  1.00 27.14 ? 6    PRO C O   1 
ATOM   5063  C  CB  . PRO C  1 3   ? 29.294  -40.273 10.463  1.00 29.86 ? 6    PRO C CB  1 
ATOM   5064  C  CG  . PRO C  1 3   ? 29.542  -40.040 8.998   1.00 26.86 ? 6    PRO C CG  1 
ATOM   5065  C  CD  . PRO C  1 3   ? 28.365  -39.204 8.592   1.00 27.87 ? 6    PRO C CD  1 
ATOM   5066  N  N   . GLY C  1 4   ? 27.119  -41.192 12.752  1.00 30.12 ? 7    GLY C N   1 
ATOM   5067  C  CA  . GLY C  1 4   ? 26.870  -40.931 14.159  1.00 29.63 ? 7    GLY C CA  1 
ATOM   5068  C  C   . GLY C  1 4   ? 28.143  -40.507 14.869  1.00 28.94 ? 7    GLY C C   1 
ATOM   5069  O  O   . GLY C  1 4   ? 29.233  -40.612 14.317  1.00 25.73 ? 7    GLY C O   1 
ATOM   5070  N  N   . PRO C  1 5   ? 28.009  -40.053 16.121  1.00 29.79 ? 8    PRO C N   1 
ATOM   5071  C  CA  . PRO C  1 5   ? 29.176  -39.703 16.937  1.00 30.10 ? 8    PRO C CA  1 
ATOM   5072  C  C   . PRO C  1 5   ? 30.143  -40.884 17.089  1.00 34.09 ? 8    PRO C C   1 
ATOM   5073  O  O   . PRO C  1 5   ? 29.767  -42.034 16.841  1.00 36.77 ? 8    PRO C O   1 
ATOM   5074  C  CB  . PRO C  1 5   ? 28.570  -39.292 18.283  1.00 30.02 ? 8    PRO C CB  1 
ATOM   5075  C  CG  . PRO C  1 5   ? 27.167  -39.879 18.296  1.00 32.58 ? 8    PRO C CG  1 
ATOM   5076  C  CD  . PRO C  1 5   ? 26.730  -39.979 16.857  1.00 29.23 ? 8    PRO C CD  1 
ATOM   5077  N  N   . LEU C  1 6   ? 31.400  -40.597 17.403  1.00 31.39 ? 9    LEU C N   1 
ATOM   5078  C  CA  . LEU C  1 6   ? 32.375  -41.654 17.675  1.00 35.48 ? 9    LEU C CA  1 
ATOM   5079  C  C   . LEU C  1 6   ? 31.855  -42.656 18.714  1.00 36.25 ? 9    LEU C C   1 
ATOM   5080  O  O   . LEU C  1 6   ? 31.252  -42.266 19.719  1.00 34.64 ? 9    LEU C O   1 
ATOM   5081  C  CB  . LEU C  1 6   ? 33.672  -41.031 18.193  1.00 34.19 ? 9    LEU C CB  1 
ATOM   5082  C  CG  . LEU C  1 6   ? 34.885  -41.013 17.277  1.00 32.36 ? 9    LEU C CG  1 
ATOM   5083  C  CD1 . LEU C  1 6   ? 34.479  -40.946 15.818  1.00 33.77 ? 9    LEU C CD1 1 
ATOM   5084  C  CD2 . LEU C  1 6   ? 35.787  -39.871 17.675  1.00 31.03 ? 9    LEU C CD2 1 
ATOM   5085  N  N   . GLU C  1 7   ? 32.170  -43.934 18.527  1.00 39.63 ? 10   GLU C N   1 
ATOM   5086  C  CA  . GLU C  1 7   ? 31.921  -44.912 19.582  1.00 39.69 ? 10   GLU C CA  1 
ATOM   5087  C  C   . GLU C  1 7   ? 32.905  -44.748 20.749  1.00 36.79 ? 10   GLU C C   1 
ATOM   5088  O  O   . GLU C  1 7   ? 32.506  -44.666 21.904  1.00 34.85 ? 10   GLU C O   1 
ATOM   5089  C  CB  . GLU C  1 7   ? 31.928  -46.339 19.025  1.00 45.83 ? 10   GLU C CB  1 
ATOM   5090  C  CG  . GLU C  1 7   ? 30.527  -46.880 18.698  1.00 51.25 ? 10   GLU C CG  1 
ATOM   5091  C  CD  . GLU C  1 7   ? 30.538  -47.988 17.647  1.00 55.41 ? 10   GLU C CD  1 
ATOM   5092  O  OE1 . GLU C  1 7   ? 31.587  -48.190 16.989  1.00 57.80 ? 10   GLU C OE1 1 
ATOM   5093  O  OE2 . GLU C  1 7   ? 29.490  -48.651 17.465  1.00 56.06 ? 10   GLU C OE2 1 
ATOM   5094  N  N   . ASN C  1 8   ? 34.183  -44.602 20.430  1.00 35.96 ? 11   ASN C N   1 
ATOM   5095  C  CA  . ASN C  1 8   ? 35.205  -44.333 21.439  1.00 35.79 ? 11   ASN C CA  1 
ATOM   5096  C  C   . ASN C  1 8   ? 35.928  -43.001 21.168  1.00 33.95 ? 11   ASN C C   1 
ATOM   5097  O  O   . ASN C  1 8   ? 36.768  -42.901 20.262  1.00 28.65 ? 11   ASN C O   1 
ATOM   5098  C  CB  . ASN C  1 8   ? 36.203  -45.499 21.517  1.00 36.43 ? 11   ASN C CB  1 
ATOM   5099  C  CG  . ASN C  1 8   ? 37.251  -45.323 22.632  1.00 42.31 ? 11   ASN C CG  1 
ATOM   5100  O  OD1 . ASN C  1 8   ? 37.333  -44.270 23.283  1.00 37.96 ? 11   ASN C OD1 1 
ATOM   5101  N  ND2 . ASN C  1 8   ? 38.073  -46.362 22.834  1.00 46.23 ? 11   ASN C ND2 1 
ATOM   5102  N  N   . SER C  1 9   ? 35.598  -41.987 21.964  1.00 32.19 ? 12   SER C N   1 
ATOM   5103  C  CA  . SER C  1 9   ? 36.033  -40.620 21.676  1.00 34.54 ? 12   SER C CA  1 
ATOM   5104  C  C   . SER C  1 9   ? 37.183  -40.144 22.561  1.00 33.14 ? 12   SER C C   1 
ATOM   5105  O  O   . SER C  1 9   ? 37.379  -38.937 22.714  1.00 32.22 ? 12   SER C O   1 
ATOM   5106  C  CB  . SER C  1 9   ? 34.860  -39.655 21.821  1.00 35.01 ? 12   SER C CB  1 
ATOM   5107  O  OG  . SER C  1 9   ? 34.565  -39.445 23.190  1.00 36.79 ? 12   SER C OG  1 
ATOM   5108  N  N   . SER C  1 10  ? 37.912  -41.095 23.152  1.00 32.77 ? 13   SER C N   1 
ATOM   5109  C  CA  . SER C  1 10  ? 39.074  -40.816 24.011  1.00 32.26 ? 13   SER C CA  1 
ATOM   5110  C  C   . SER C  1 10  ? 40.200  -40.185 23.203  1.00 30.76 ? 13   SER C C   1 
ATOM   5111  O  O   . SER C  1 10  ? 40.186  -40.240 21.975  1.00 32.57 ? 13   SER C O   1 
ATOM   5112  C  CB  . SER C  1 10  ? 39.599  -42.115 24.633  1.00 33.42 ? 13   SER C CB  1 
ATOM   5113  O  OG  . SER C  1 10  ? 38.608  -42.769 25.411  1.00 36.05 ? 13   SER C OG  1 
ATOM   5114  N  N   . ALA C  1 11  ? 41.195  -39.634 23.890  1.00 28.78 ? 14   ALA C N   1 
ATOM   5115  C  CA  . ALA C  1 11  ? 42.370  -39.106 23.212  1.00 32.64 ? 14   ALA C CA  1 
ATOM   5116  C  C   . ALA C  1 11  ? 43.176  -40.263 22.649  1.00 34.04 ? 14   ALA C C   1 
ATOM   5117  O  O   . ALA C  1 11  ? 43.242  -41.330 23.252  1.00 34.24 ? 14   ALA C O   1 
ATOM   5118  C  CB  . ALA C  1 11  ? 43.228  -38.288 24.170  1.00 33.21 ? 14   ALA C CB  1 
ATOM   5119  N  N   . LYS C  1 12  ? 43.757  -40.065 21.473  1.00 33.30 ? 15   LYS C N   1 
ATOM   5120  C  CA  . LYS C  1 12  ? 44.727  -41.013 20.975  1.00 34.57 ? 15   LYS C CA  1 
ATOM   5121  C  C   . LYS C  1 12  ? 45.651  -40.398 19.927  1.00 34.24 ? 15   LYS C C   1 
ATOM   5122  O  O   . LYS C  1 12  ? 45.324  -39.393 19.287  1.00 33.17 ? 15   LYS C O   1 
ATOM   5123  C  CB  . LYS C  1 12  ? 44.035  -42.274 20.436  1.00 36.90 ? 15   LYS C CB  1 
ATOM   5124  C  CG  . LYS C  1 12  ? 42.852  -41.997 19.513  1.00 39.14 ? 15   LYS C CG  1 
ATOM   5125  C  CD  . LYS C  1 12  ? 42.269  -43.280 18.894  1.00 39.64 ? 15   LYS C CD  1 
ATOM   5126  C  CE  . LYS C  1 12  ? 42.879  -43.555 17.510  1.00 41.91 ? 15   LYS C CE  1 
ATOM   5127  N  NZ  . LYS C  1 12  ? 41.870  -43.994 16.489  1.00 40.68 ? 15   LYS C NZ  1 
ATOM   5128  N  N   . LEU C  1 13  ? 46.817  -41.012 19.781  1.00 32.33 ? 16   LEU C N   1 
ATOM   5129  C  CA  . LEU C  1 13  ? 47.695  -40.772 18.660  1.00 32.77 ? 16   LEU C CA  1 
ATOM   5130  C  C   . LEU C  1 13  ? 46.894  -40.741 17.366  1.00 34.13 ? 16   LEU C C   1 
ATOM   5131  O  O   . LEU C  1 13  ? 46.247  -41.731 17.001  1.00 31.43 ? 16   LEU C O   1 
ATOM   5132  C  CB  . LEU C  1 13  ? 48.732  -41.896 18.588  1.00 33.38 ? 16   LEU C CB  1 
ATOM   5133  C  CG  . LEU C  1 13  ? 49.739  -41.700 17.467  1.00 33.08 ? 16   LEU C CG  1 
ATOM   5134  C  CD1 . LEU C  1 13  ? 50.388  -40.318 17.588  1.00 29.99 ? 16   LEU C CD1 1 
ATOM   5135  C  CD2 . LEU C  1 13  ? 50.773  -42.836 17.465  1.00 32.70 ? 16   LEU C CD2 1 
ATOM   5136  N  N   . VAL C  1 14  ? 46.923  -39.603 16.678  1.00 32.33 ? 17   VAL C N   1 
ATOM   5137  C  CA  . VAL C  1 14  ? 46.328  -39.542 15.357  1.00 33.24 ? 17   VAL C CA  1 
ATOM   5138  C  C   . VAL C  1 14  ? 47.361  -39.262 14.273  1.00 32.18 ? 17   VAL C C   1 
ATOM   5139  O  O   . VAL C  1 14  ? 47.111  -39.506 13.100  1.00 33.23 ? 17   VAL C O   1 
ATOM   5140  C  CB  . VAL C  1 14  ? 45.134  -38.536 15.269  1.00 30.75 ? 17   VAL C CB  1 
ATOM   5141  C  CG1 . VAL C  1 14  ? 43.906  -39.098 16.013  1.00 29.18 ? 17   VAL C CG1 1 
ATOM   5142  C  CG2 . VAL C  1 14  ? 45.538  -37.177 15.782  1.00 26.61 ? 17   VAL C CG2 1 
ATOM   5143  N  N   . ASN C  1 15  ? 48.505  -38.719 14.662  1.00 31.10 ? 18   ASN C N   1 
ATOM   5144  C  CA  . ASN C  1 15  ? 49.663  -38.720 13.773  1.00 33.68 ? 18   ASN C CA  1 
ATOM   5145  C  C   . ASN C  1 15  ? 50.378  -40.082 13.839  1.00 35.87 ? 18   ASN C C   1 
ATOM   5146  O  O   . ASN C  1 15  ? 51.406  -40.239 14.513  1.00 35.23 ? 18   ASN C O   1 
ATOM   5147  C  CB  . ASN C  1 15  ? 50.607  -37.574 14.128  1.00 31.30 ? 18   ASN C CB  1 
ATOM   5148  C  CG  . ASN C  1 15  ? 51.642  -37.323 13.063  1.00 33.24 ? 18   ASN C CG  1 
ATOM   5149  O  OD1 . ASN C  1 15  ? 51.759  -38.078 12.098  1.00 32.28 ? 18   ASN C OD1 1 
ATOM   5150  N  ND2 . ASN C  1 15  ? 52.383  -36.236 13.215  1.00 34.91 ? 18   ASN C ND2 1 
ATOM   5151  N  N   . ASP C  1 16  ? 49.719  -41.096 13.285  1.00 37.73 ? 19   ASP C N   1 
ATOM   5152  C  CA  . ASP C  1 16  ? 50.183  -42.465 13.402  1.00 37.86 ? 19   ASP C CA  1 
ATOM   5153  C  C   . ASP C  1 16  ? 50.637  -43.037 12.073  1.00 40.14 ? 19   ASP C C   1 
ATOM   5154  O  O   . ASP C  1 16  ? 50.866  -42.315 11.093  1.00 42.17 ? 19   ASP C O   1 
ATOM   5155  C  CB  . ASP C  1 16  ? 49.107  -43.374 14.019  1.00 37.15 ? 19   ASP C CB  1 
ATOM   5156  C  CG  . ASP C  1 16  ? 47.777  -43.338 13.253  1.00 36.91 ? 19   ASP C CG  1 
ATOM   5157  O  OD1 . ASP C  1 16  ? 47.753  -42.980 12.053  1.00 35.05 ? 19   ASP C OD1 1 
ATOM   5158  O  OD2 . ASP C  1 16  ? 46.748  -43.698 13.858  1.00 35.03 ? 19   ASP C OD2 1 
ATOM   5159  N  N   . GLU C  1 17  ? 50.692  -44.360 12.054  1.00 41.97 ? 20   GLU C N   1 
ATOM   5160  C  CA  . GLU C  1 17  ? 51.374  -45.127 11.034  1.00 42.98 ? 20   GLU C CA  1 
ATOM   5161  C  C   . GLU C  1 17  ? 50.544  -45.077 9.754   1.00 40.28 ? 20   GLU C C   1 
ATOM   5162  O  O   . GLU C  1 17  ? 51.070  -44.905 8.647   1.00 38.18 ? 20   GLU C O   1 
ATOM   5163  C  CB  . GLU C  1 17  ? 51.498  -46.578 11.535  1.00 45.42 ? 20   GLU C CB  1 
ATOM   5164  C  CG  . GLU C  1 17  ? 52.108  -46.718 12.969  1.00 49.40 ? 20   GLU C CG  1 
ATOM   5165  C  CD  . GLU C  1 17  ? 51.092  -46.623 14.138  1.00 50.42 ? 20   GLU C CD  1 
ATOM   5166  O  OE1 . GLU C  1 17  ? 50.037  -47.301 14.101  1.00 52.69 ? 20   GLU C OE1 1 
ATOM   5167  O  OE2 . GLU C  1 17  ? 51.412  -45.965 15.152  1.00 46.80 ? 20   GLU C OE2 1 
ATOM   5168  N  N   . ALA C  1 18  ? 49.234  -45.186 9.926   1.00 38.22 ? 21   ALA C N   1 
ATOM   5169  C  CA  . ALA C  1 18  ? 48.313  -45.288 8.801   1.00 38.72 ? 21   ALA C CA  1 
ATOM   5170  C  C   . ALA C  1 18  ? 47.902  -43.906 8.289   1.00 38.92 ? 21   ALA C C   1 
ATOM   5171  O  O   . ALA C  1 18  ? 47.218  -43.798 7.274   1.00 40.57 ? 21   ALA C O   1 
ATOM   5172  C  CB  . ALA C  1 18  ? 47.079  -46.095 9.204   1.00 38.42 ? 21   ALA C CB  1 
ATOM   5173  N  N   . HIS C  1 19  ? 48.324  -42.856 8.993   1.00 36.56 ? 22   HIS C N   1 
ATOM   5174  C  CA  . HIS C  1 19  ? 47.994  -41.487 8.602   1.00 35.94 ? 22   HIS C CA  1 
ATOM   5175  C  C   . HIS C  1 19  ? 49.195  -40.539 8.644   1.00 36.19 ? 22   HIS C C   1 
ATOM   5176  O  O   . HIS C  1 19  ? 49.181  -39.533 9.354   1.00 34.38 ? 22   HIS C O   1 
ATOM   5177  C  CB  . HIS C  1 19  ? 46.824  -40.949 9.427   1.00 30.29 ? 22   HIS C CB  1 
ATOM   5178  C  CG  . HIS C  1 19  ? 45.572  -41.750 9.274   1.00 29.75 ? 22   HIS C CG  1 
ATOM   5179  N  ND1 . HIS C  1 19  ? 45.138  -42.641 10.229  1.00 30.54 ? 22   HIS C ND1 1 
ATOM   5180  C  CD2 . HIS C  1 19  ? 44.702  -41.855 8.242   1.00 31.73 ? 22   HIS C CD2 1 
ATOM   5181  C  CE1 . HIS C  1 19  ? 44.050  -43.254 9.799   1.00 28.48 ? 22   HIS C CE1 1 
ATOM   5182  N  NE2 . HIS C  1 19  ? 43.742  -42.765 8.613   1.00 29.33 ? 22   HIS C NE2 1 
ATOM   5183  N  N   . PRO C  1 20  ? 50.232  -40.860 7.855   1.00 37.21 ? 23   PRO C N   1 
ATOM   5184  C  CA  . PRO C  1 20  ? 51.436  -40.057 7.728   1.00 35.30 ? 23   PRO C CA  1 
ATOM   5185  C  C   . PRO C  1 20  ? 51.144  -38.785 6.969   1.00 36.07 ? 23   PRO C C   1 
ATOM   5186  O  O   . PRO C  1 20  ? 50.345  -38.804 6.030   1.00 36.26 ? 23   PRO C O   1 
ATOM   5187  C  CB  . PRO C  1 20  ? 52.345  -40.939 6.868   1.00 36.14 ? 23   PRO C CB  1 
ATOM   5188  C  CG  . PRO C  1 20  ? 51.382  -41.734 6.017   1.00 35.79 ? 23   PRO C CG  1 
ATOM   5189  C  CD  . PRO C  1 20  ? 50.270  -42.055 6.985   1.00 36.70 ? 23   PRO C CD  1 
ATOM   5190  N  N   . TRP C  1 21  ? 51.867  -37.715 7.294   1.00 32.75 ? 24   TRP C N   1 
ATOM   5191  C  CA  . TRP C  1 21  ? 51.873  -36.535 6.445   1.00 33.89 ? 24   TRP C CA  1 
ATOM   5192  C  C   . TRP C  1 21  ? 52.628  -36.791 5.154   1.00 34.89 ? 24   TRP C C   1 
ATOM   5193  O  O   . TRP C  1 21  ? 53.701  -37.393 5.165   1.00 37.11 ? 24   TRP C O   1 
ATOM   5194  C  CB  . TRP C  1 21  ? 52.504  -35.356 7.172   1.00 31.46 ? 24   TRP C CB  1 
ATOM   5195  C  CG  . TRP C  1 21  ? 52.416  -34.083 6.417   1.00 31.90 ? 24   TRP C CG  1 
ATOM   5196  C  CD1 . TRP C  1 21  ? 51.411  -33.157 6.493   1.00 32.19 ? 24   TRP C CD1 1 
ATOM   5197  C  CD2 . TRP C  1 21  ? 53.415  -33.521 5.549   1.00 34.09 ? 24   TRP C CD2 1 
ATOM   5198  N  NE1 . TRP C  1 21  ? 51.708  -32.074 5.703   1.00 32.87 ? 24   TRP C NE1 1 
ATOM   5199  C  CE2 . TRP C  1 21  ? 52.927  -32.272 5.106   1.00 32.78 ? 24   TRP C CE2 1 
ATOM   5200  C  CE3 . TRP C  1 21  ? 54.659  -33.969 5.073   1.00 35.33 ? 24   TRP C CE3 1 
ATOM   5201  C  CZ2 . TRP C  1 21  ? 53.640  -31.458 4.219   1.00 34.46 ? 24   TRP C CZ2 1 
ATOM   5202  C  CZ3 . TRP C  1 21  ? 55.364  -33.163 4.178   1.00 33.74 ? 24   TRP C CZ3 1 
ATOM   5203  C  CH2 . TRP C  1 21  ? 54.850  -31.925 3.760   1.00 36.25 ? 24   TRP C CH2 1 
ATOM   5204  N  N   . LYS C  1 22  ? 52.127  -36.234 4.058   1.00 35.65 ? 25   LYS C N   1 
ATOM   5205  C  CA  . LYS C  1 22  ? 52.839  -36.273 2.790   1.00 35.39 ? 25   LYS C CA  1 
ATOM   5206  C  C   . LYS C  1 22  ? 52.712  -34.922 2.125   1.00 37.15 ? 25   LYS C C   1 
ATOM   5207  O  O   . LYS C  1 22  ? 51.702  -34.240 2.314   1.00 37.85 ? 25   LYS C O   1 
ATOM   5208  C  CB  . LYS C  1 22  ? 52.261  -37.367 1.894   1.00 36.78 ? 25   LYS C CB  1 
ATOM   5209  C  CG  . LYS C  1 22  ? 52.138  -38.716 2.602   1.00 39.55 ? 25   LYS C CG  1 
ATOM   5210  C  CD  . LYS C  1 22  ? 51.732  -39.825 1.646   1.00 42.95 ? 25   LYS C CD  1 
ATOM   5211  C  CE  . LYS C  1 22  ? 52.220  -41.181 2.135   1.00 44.21 ? 25   LYS C CE  1 
ATOM   5212  N  NZ  . LYS C  1 22  ? 51.662  -42.300 1.328   1.00 45.16 ? 25   LYS C NZ  1 
ATOM   5213  N  N   . PRO C  1 23  ? 53.756  -34.501 1.388   1.00 36.84 ? 26   PRO C N   1 
ATOM   5214  C  CA  . PRO C  1 23  ? 53.709  -33.236 0.683   1.00 36.11 ? 26   PRO C CA  1 
ATOM   5215  C  C   . PRO C  1 23  ? 52.660  -33.319 -0.412  1.00 34.97 ? 26   PRO C C   1 
ATOM   5216  O  O   . PRO C  1 23  ? 52.204  -34.415 -0.734  1.00 29.61 ? 26   PRO C O   1 
ATOM   5217  C  CB  . PRO C  1 23  ? 55.106  -33.149 0.053   1.00 38.21 ? 26   PRO C CB  1 
ATOM   5218  C  CG  . PRO C  1 23  ? 55.488  -34.571 -0.183  1.00 36.64 ? 26   PRO C CG  1 
ATOM   5219  C  CD  . PRO C  1 23  ? 54.949  -35.290 1.023   1.00 38.11 ? 26   PRO C CD  1 
ATOM   5220  N  N   . LEU C  1 24  ? 52.335  -32.177 -1.011  1.00 35.91 ? 27   LEU C N   1 
ATOM   5221  C  CA  . LEU C  1 24  ? 51.325  -32.099 -2.070  1.00 40.21 ? 27   LEU C CA  1 
ATOM   5222  C  C   . LEU C  1 24  ? 51.858  -32.577 -3.424  1.00 41.67 ? 27   LEU C C   1 
ATOM   5223  O  O   . LEU C  1 24  ? 52.833  -32.029 -3.926  1.00 42.31 ? 27   LEU C O   1 
ATOM   5224  C  CB  . LEU C  1 24  ? 50.830  -30.649 -2.208  1.00 39.69 ? 27   LEU C CB  1 
ATOM   5225  C  CG  . LEU C  1 24  ? 50.205  -30.015 -0.956  1.00 39.77 ? 27   LEU C CG  1 
ATOM   5226  C  CD1 . LEU C  1 24  ? 50.050  -28.511 -1.108  1.00 38.70 ? 27   LEU C CD1 1 
ATOM   5227  C  CD2 . LEU C  1 24  ? 48.873  -30.654 -0.640  1.00 35.09 ? 27   LEU C CD2 1 
ATOM   5228  N  N   . ARG C  1 25  ? 51.187  -33.553 -4.037  1.00 42.90 ? 28   ARG C N   1 
ATOM   5229  C  CA  . ARG C  1 25  ? 51.343  -33.811 -5.475  1.00 43.57 ? 28   ARG C CA  1 
ATOM   5230  C  C   . ARG C  1 25  ? 50.607  -32.758 -6.308  1.00 44.63 ? 28   ARG C C   1 
ATOM   5231  O  O   . ARG C  1 25  ? 49.599  -32.215 -5.869  1.00 45.14 ? 28   ARG C O   1 
ATOM   5232  C  CB  . ARG C  1 25  ? 50.797  -35.192 -5.845  1.00 45.08 ? 28   ARG C CB  1 
ATOM   5233  C  CG  . ARG C  1 25  ? 51.051  -36.275 -4.825  1.00 45.61 ? 28   ARG C CG  1 
ATOM   5234  C  CD  . ARG C  1 25  ? 50.041  -37.406 -4.970  1.00 48.70 ? 28   ARG C CD  1 
ATOM   5235  N  NE  . ARG C  1 25  ? 48.673  -36.970 -4.691  1.00 49.85 ? 28   ARG C NE  1 
ATOM   5236  C  CZ  . ARG C  1 25  ? 47.647  -37.797 -4.500  1.00 50.19 ? 28   ARG C CZ  1 
ATOM   5237  N  NH1 . ARG C  1 25  ? 47.825  -39.108 -4.559  1.00 49.47 ? 28   ARG C NH1 1 
ATOM   5238  N  NH2 . ARG C  1 25  ? 46.441  -37.315 -4.239  1.00 48.33 ? 28   ARG C NH2 1 
ATOM   5239  N  N   . PRO C  1 26  ? 51.059  -32.527 -7.551  1.00 43.94 ? 29   PRO C N   1 
ATOM   5240  C  CA  . PRO C  1 26  ? 50.284  -31.637 -8.415  1.00 43.30 ? 29   PRO C CA  1 
ATOM   5241  C  C   . PRO C  1 26  ? 48.828  -32.093 -8.495  1.00 41.40 ? 29   PRO C C   1 
ATOM   5242  O  O   . PRO C  1 26  ? 48.540  -33.297 -8.447  1.00 36.90 ? 29   PRO C O   1 
ATOM   5243  C  CB  . PRO C  1 26  ? 50.955  -31.799 -9.784  1.00 44.83 ? 29   PRO C CB  1 
ATOM   5244  C  CG  . PRO C  1 26  ? 51.561  -33.159 -9.740  1.00 45.14 ? 29   PRO C CG  1 
ATOM   5245  C  CD  . PRO C  1 26  ? 52.005  -33.356 -8.313  1.00 43.77 ? 29   PRO C CD  1 
ATOM   5246  N  N   . GLY C  1 27  ? 47.911  -31.135 -8.541  1.00 39.73 ? 30   GLY C N   1 
ATOM   5247  C  CA  . GLY C  1 27  ? 46.495  -31.481 -8.574  1.00 40.46 ? 30   GLY C CA  1 
ATOM   5248  C  C   . GLY C  1 27  ? 45.840  -31.660 -7.208  1.00 37.88 ? 30   GLY C C   1 
ATOM   5249  O  O   . GLY C  1 27  ? 44.614  -31.660 -7.109  1.00 39.16 ? 30   GLY C O   1 
ATOM   5250  N  N   . ASP C  1 28  ? 46.647  -31.807 -6.157  1.00 34.95 ? 31   ASP C N   1 
ATOM   5251  C  CA  . ASP C  1 28  ? 46.130  -31.837 -4.793  1.00 32.59 ? 31   ASP C CA  1 
ATOM   5252  C  C   . ASP C  1 28  ? 45.589  -30.479 -4.325  1.00 30.63 ? 31   ASP C C   1 
ATOM   5253  O  O   . ASP C  1 28  ? 46.280  -29.458 -4.363  1.00 30.35 ? 31   ASP C O   1 
ATOM   5254  C  CB  . ASP C  1 28  ? 47.193  -32.348 -3.826  1.00 33.82 ? 31   ASP C CB  1 
ATOM   5255  C  CG  . ASP C  1 28  ? 47.411  -33.855 -3.937  1.00 34.23 ? 31   ASP C CG  1 
ATOM   5256  O  OD1 . ASP C  1 28  ? 46.628  -34.525 -4.641  1.00 35.33 ? 31   ASP C OD1 1 
ATOM   5257  O  OD2 . ASP C  1 28  ? 48.343  -34.374 -3.289  1.00 34.11 ? 31   ASP C OD2 1 
ATOM   5258  N  N   . ILE C  1 29  ? 44.366  -30.483 -3.817  1.00 26.88 ? 32   ILE C N   1 
ATOM   5259  C  CA  . ILE C  1 29  ? 43.655  -29.238 -3.546  1.00 23.65 ? 32   ILE C CA  1 
ATOM   5260  C  C   . ILE C  1 29  ? 43.642  -28.915 -2.050  1.00 21.20 ? 32   ILE C C   1 
ATOM   5261  O  O   . ILE C  1 29  ? 43.305  -29.763 -1.224  1.00 23.61 ? 32   ILE C O   1 
ATOM   5262  C  CB  . ILE C  1 29  ? 42.228  -29.331 -4.117  1.00 24.51 ? 32   ILE C CB  1 
ATOM   5263  C  CG1 . ILE C  1 29  ? 42.294  -29.302 -5.660  1.00 21.92 ? 32   ILE C CG1 1 
ATOM   5264  C  CG2 . ILE C  1 29  ? 41.341  -28.248 -3.540  1.00 22.62 ? 32   ILE C CG2 1 
ATOM   5265  C  CD1 . ILE C  1 29  ? 40.997  -29.690 -6.346  1.00 21.65 ? 32   ILE C CD1 1 
ATOM   5266  N  N   . ARG C  1 30  ? 44.123  -27.731 -1.684  1.00 18.69 ? 33   ARG C N   1 
ATOM   5267  C  CA  . ARG C  1 30  ? 43.978  -27.260 -0.308  1.00 18.87 ? 33   ARG C CA  1 
ATOM   5268  C  C   . ARG C  1 30  ? 43.332  -25.874 -0.299  1.00 21.97 ? 33   ARG C C   1 
ATOM   5269  O  O   . ARG C  1 30  ? 43.447  -25.107 -1.275  1.00 20.16 ? 33   ARG C O   1 
ATOM   5270  C  CB  . ARG C  1 30  ? 45.336  -27.219 0.404   1.00 22.33 ? 33   ARG C CB  1 
ATOM   5271  C  CG  . ARG C  1 30  ? 46.079  -28.567 0.464   1.00 22.30 ? 33   ARG C CG  1 
ATOM   5272  C  CD  . ARG C  1 30  ? 45.363  -29.558 1.350   1.00 23.15 ? 33   ARG C CD  1 
ATOM   5273  N  NE  . ARG C  1 30  ? 46.141  -30.781 1.516   1.00 25.08 ? 33   ARG C NE  1 
ATOM   5274  C  CZ  . ARG C  1 30  ? 45.972  -31.883 0.787   1.00 25.11 ? 33   ARG C CZ  1 
ATOM   5275  N  NH1 . ARG C  1 30  ? 44.991  -31.953 -0.105  1.00 25.46 ? 33   ARG C NH1 1 
ATOM   5276  N  NH2 . ARG C  1 30  ? 46.731  -32.943 1.007   1.00 22.27 ? 33   ARG C NH2 1 
ATOM   5277  N  N   . GLY C  1 31  ? 42.623  -25.565 0.784   1.00 20.73 ? 34   GLY C N   1 
ATOM   5278  C  CA  . GLY C  1 31  ? 41.838  -24.340 0.836   1.00 20.27 ? 34   GLY C CA  1 
ATOM   5279  C  C   . GLY C  1 31  ? 41.926  -23.577 2.145   1.00 20.90 ? 34   GLY C C   1 
ATOM   5280  O  O   . GLY C  1 31  ? 42.968  -23.531 2.769   1.00 19.84 ? 34   GLY C O   1 
ATOM   5281  N  N   . PRO C  1 32  ? 40.815  -22.953 2.559   1.00 23.70 ? 35   PRO C N   1 
ATOM   5282  C  CA  . PRO C  1 32  ? 40.943  -21.946 3.615   1.00 19.55 ? 35   PRO C CA  1 
ATOM   5283  C  C   . PRO C  1 32  ? 40.810  -22.506 5.017   1.00 18.28 ? 35   PRO C C   1 
ATOM   5284  O  O   . PRO C  1 32  ? 40.949  -21.754 5.989   1.00 19.21 ? 35   PRO C O   1 
ATOM   5285  C  CB  . PRO C  1 32  ? 39.821  -20.950 3.299   1.00 19.69 ? 35   PRO C CB  1 
ATOM   5286  C  CG  . PRO C  1 32  ? 38.825  -21.728 2.550   1.00 23.43 ? 35   PRO C CG  1 
ATOM   5287  C  CD  . PRO C  1 32  ? 39.606  -22.751 1.741   1.00 21.34 ? 35   PRO C CD  1 
ATOM   5288  N  N   . CYS C  1 33  ? 40.624  -23.822 5.125   1.00 16.58 ? 36   CYS C N   1 
ATOM   5289  C  CA  . CYS C  1 33  ? 40.448  -24.474 6.425   1.00 17.90 ? 36   CYS C CA  1 
ATOM   5290  C  C   . CYS C  1 33  ? 41.681  -25.290 6.810   1.00 19.75 ? 36   CYS C C   1 
ATOM   5291  O  O   . CYS C  1 33  ? 41.903  -26.372 6.263   1.00 17.98 ? 36   CYS C O   1 
ATOM   5292  C  CB  . CYS C  1 33  ? 39.219  -25.393 6.415   1.00 17.20 ? 36   CYS C CB  1 
ATOM   5293  S  SG  . CYS C  1 33  ? 38.914  -26.232 7.998   1.00 24.49 ? 36   CYS C SG  1 
ATOM   5294  N  N   . PRO C  1 34  ? 42.429  -24.828 7.826   1.00 20.76 ? 37   PRO C N   1 
ATOM   5295  C  CA  . PRO C  1 34  ? 43.600  -25.594 8.225   1.00 20.24 ? 37   PRO C CA  1 
ATOM   5296  C  C   . PRO C  1 34  ? 43.184  -26.941 8.792   1.00 20.02 ? 37   PRO C C   1 
ATOM   5297  O  O   . PRO C  1 34  ? 43.937  -27.906 8.695   1.00 26.29 ? 37   PRO C O   1 
ATOM   5298  C  CB  . PRO C  1 34  ? 44.226  -24.727 9.323   1.00 20.80 ? 37   PRO C CB  1 
ATOM   5299  C  CG  . PRO C  1 34  ? 43.030  -24.058 9.970   1.00 22.38 ? 37   PRO C CG  1 
ATOM   5300  C  CD  . PRO C  1 34  ? 42.017  -23.858 8.856   1.00 20.56 ? 37   PRO C CD  1 
ATOM   5301  N  N   . GLY C  1 35  ? 41.996  -27.005 9.388   1.00 19.59 ? 38   GLY C N   1 
ATOM   5302  C  CA  . GLY C  1 35  ? 41.411  -28.258 9.846   1.00 15.51 ? 38   GLY C CA  1 
ATOM   5303  C  C   . GLY C  1 35  ? 41.316  -29.320 8.770   1.00 21.15 ? 38   GLY C C   1 
ATOM   5304  O  O   . GLY C  1 35  ? 41.902  -30.388 8.897   1.00 24.50 ? 38   GLY C O   1 
ATOM   5305  N  N   . LEU C  1 36  ? 40.582  -29.032 7.698   1.00 23.41 ? 39   LEU C N   1 
ATOM   5306  C  CA  . LEU C  1 36  ? 40.381  -30.003 6.622   1.00 20.93 ? 39   LEU C CA  1 
ATOM   5307  C  C   . LEU C  1 36  ? 41.687  -30.201 5.843   1.00 21.68 ? 39   LEU C C   1 
ATOM   5308  O  O   . LEU C  1 36  ? 42.013  -31.314 5.432   1.00 18.93 ? 39   LEU C O   1 
ATOM   5309  C  CB  . LEU C  1 36  ? 39.264  -29.543 5.673   1.00 20.93 ? 39   LEU C CB  1 
ATOM   5310  C  CG  . LEU C  1 36  ? 37.837  -29.576 6.250   1.00 24.11 ? 39   LEU C CG  1 
ATOM   5311  C  CD1 . LEU C  1 36  ? 36.776  -29.356 5.195   1.00 24.89 ? 39   LEU C CD1 1 
ATOM   5312  C  CD2 . LEU C  1 36  ? 37.576  -30.850 7.016   1.00 21.72 ? 39   LEU C CD2 1 
ATOM   5313  N  N   . ASN C  1 37  ? 42.453  -29.128 5.674   1.00 20.88 ? 40   ASN C N   1 
ATOM   5314  C  CA  . ASN C  1 37  ? 43.753  -29.238 5.014   1.00 22.01 ? 40   ASN C CA  1 
ATOM   5315  C  C   . ASN C  1 37  ? 44.635  -30.326 5.659   1.00 23.52 ? 40   ASN C C   1 
ATOM   5316  O  O   . ASN C  1 37  ? 45.145  -31.207 4.978   1.00 18.86 ? 40   ASN C O   1 
ATOM   5317  C  CB  . ASN C  1 37  ? 44.466  -27.896 5.029   1.00 21.43 ? 40   ASN C CB  1 
ATOM   5318  C  CG  . ASN C  1 37  ? 43.847  -26.915 4.075   1.00 19.96 ? 40   ASN C CG  1 
ATOM   5319  O  OD1 . ASN C  1 37  ? 43.052  -27.304 3.240   1.00 21.89 ? 40   ASN C OD1 1 
ATOM   5320  N  ND2 . ASN C  1 37  ? 44.294  -25.671 4.112   1.00 17.01 ? 40   ASN C ND2 1 
ATOM   5321  N  N   . THR C  1 38  ? 44.721  -30.310 6.985   1.00 23.58 ? 41   THR C N   1 
ATOM   5322  C  CA  . THR C  1 38  ? 45.577  -31.246 7.715   1.00 23.86 ? 41   THR C CA  1 
ATOM   5323  C  C   . THR C  1 38  ? 45.064  -32.669 7.644   1.00 24.29 ? 41   THR C C   1 
ATOM   5324  O  O   . THR C  1 38  ? 45.843  -33.617 7.638   1.00 27.69 ? 41   THR C O   1 
ATOM   5325  C  CB  . THR C  1 38  ? 45.662  -30.869 9.200   1.00 21.33 ? 41   THR C CB  1 
ATOM   5326  O  OG1 . THR C  1 38  ? 46.112  -29.525 9.302   1.00 19.31 ? 41   THR C OG1 1 
ATOM   5327  C  CG2 . THR C  1 38  ? 46.622  -31.800 9.945   1.00 20.16 ? 41   THR C CG2 1 
ATOM   5328  N  N   . LEU C  1 39  ? 43.747  -32.821 7.688   1.00 22.49 ? 42   LEU C N   1 
ATOM   5329  C  CA  . LEU C  1 39  ? 43.145  -34.146 7.576   1.00 21.36 ? 42   LEU C CA  1 
ATOM   5330  C  C   . LEU C  1 39  ? 43.454  -34.769 6.218   1.00 23.69 ? 42   LEU C C   1 
ATOM   5331  O  O   . LEU C  1 39  ? 43.658  -35.993 6.099   1.00 24.37 ? 42   LEU C O   1 
ATOM   5332  C  CB  . LEU C  1 39  ? 41.641  -34.050 7.798   1.00 18.46 ? 42   LEU C CB  1 
ATOM   5333  C  CG  . LEU C  1 39  ? 41.257  -33.658 9.232   1.00 18.99 ? 42   LEU C CG  1 
ATOM   5334  C  CD1 . LEU C  1 39  ? 39.787  -33.164 9.336   1.00 14.75 ? 42   LEU C CD1 1 
ATOM   5335  C  CD2 . LEU C  1 39  ? 41.501  -34.850 10.181  1.00 16.51 ? 42   LEU C CD2 1 
ATOM   5336  N  N   . ALA C  1 40  ? 43.519  -33.919 5.197   1.00 22.67 ? 43   ALA C N   1 
ATOM   5337  C  CA  . ALA C  1 40  ? 43.744  -34.387 3.838   1.00 23.74 ? 43   ALA C CA  1 
ATOM   5338  C  C   . ALA C  1 40  ? 45.223  -34.757 3.716   1.00 24.84 ? 43   ALA C C   1 
ATOM   5339  O  O   . ALA C  1 40  ? 45.592  -35.834 3.238   1.00 26.31 ? 43   ALA C O   1 
ATOM   5340  C  CB  . ALA C  1 40  ? 43.395  -33.292 2.848   1.00 20.76 ? 43   ALA C CB  1 
ATOM   5341  N  N   . SER C  1 41  ? 46.057  -33.896 4.262   1.00 21.93 ? 44   SER C N   1 
ATOM   5342  C  CA  . SER C  1 41  ? 47.471  -34.067 4.133   1.00 23.37 ? 44   SER C CA  1 
ATOM   5343  C  C   . SER C  1 41  ? 48.021  -35.159 5.034   1.00 24.19 ? 44   SER C C   1 
ATOM   5344  O  O   . SER C  1 41  ? 49.148  -35.593 4.831   1.00 27.02 ? 44   SER C O   1 
ATOM   5345  C  CB  . SER C  1 41  ? 48.197  -32.748 4.329   1.00 19.39 ? 44   SER C CB  1 
ATOM   5346  O  OG  . SER C  1 41  ? 48.282  -32.107 3.071   1.00 22.57 ? 44   SER C OG  1 
ATOM   5347  N  N   . HIS C  1 42  ? 47.192  -35.654 5.951   1.00 21.94 ? 45   HIS C N   1 
ATOM   5348  C  CA  . HIS C  1 42  ? 47.464  -36.899 6.675   1.00 24.65 ? 45   HIS C CA  1 
ATOM   5349  C  C   . HIS C  1 42  ? 46.670  -38.113 6.167   1.00 22.31 ? 45   HIS C C   1 
ATOM   5350  O  O   . HIS C  1 42  ? 46.747  -39.180 6.757   1.00 24.49 ? 45   HIS C O   1 
ATOM   5351  C  CB  . HIS C  1 42  ? 47.199  -36.722 8.188   1.00 25.58 ? 45   HIS C CB  1 
ATOM   5352  C  CG  . HIS C  1 42  ? 48.283  -35.986 8.909   1.00 25.40 ? 45   HIS C CG  1 
ATOM   5353  N  ND1 . HIS C  1 42  ? 49.288  -36.632 9.601   1.00 25.47 ? 45   HIS C ND1 1 
ATOM   5354  C  CD2 . HIS C  1 42  ? 48.561  -34.660 8.990   1.00 27.17 ? 45   HIS C CD2 1 
ATOM   5355  C  CE1 . HIS C  1 42  ? 50.108  -35.733 10.120  1.00 26.12 ? 45   HIS C CE1 1 
ATOM   5356  N  NE2 . HIS C  1 42  ? 49.682  -34.527 9.776   1.00 27.82 ? 45   HIS C NE2 1 
ATOM   5357  N  N   . GLY C  1 43  ? 45.889  -37.948 5.103   1.00 25.72 ? 46   GLY C N   1 
ATOM   5358  C  CA  . GLY C  1 43  ? 45.109  -39.057 4.528   1.00 20.88 ? 46   GLY C CA  1 
ATOM   5359  C  C   . GLY C  1 43  ? 43.923  -39.497 5.370   1.00 22.70 ? 46   GLY C C   1 
ATOM   5360  O  O   . GLY C  1 43  ? 43.428  -40.610 5.240   1.00 23.50 ? 46   GLY C O   1 
ATOM   5361  N  N   . TYR C  1 44  ? 43.427  -38.627 6.232   1.00 23.13 ? 47   TYR C N   1 
ATOM   5362  C  CA  . TYR C  1 44  ? 42.126  -38.902 6.851   1.00 25.76 ? 47   TYR C CA  1 
ATOM   5363  C  C   . TYR C  1 44  ? 41.015  -38.585 5.863   1.00 24.45 ? 47   TYR C C   1 
ATOM   5364  O  O   . TYR C  1 44  ? 39.955  -39.200 5.885   1.00 25.81 ? 47   TYR C O   1 
ATOM   5365  C  CB  . TYR C  1 44  ? 41.939  -38.101 8.137   1.00 24.88 ? 47   TYR C CB  1 
ATOM   5366  C  CG  . TYR C  1 44  ? 42.693  -38.670 9.319   1.00 27.53 ? 47   TYR C CG  1 
ATOM   5367  C  CD1 . TYR C  1 44  ? 42.134  -39.682 10.101  1.00 28.37 ? 47   TYR C CD1 1 
ATOM   5368  C  CD2 . TYR C  1 44  ? 43.970  -38.224 9.636   1.00 24.24 ? 47   TYR C CD2 1 
ATOM   5369  C  CE1 . TYR C  1 44  ? 42.800  -40.191 11.200  1.00 27.00 ? 47   TYR C CE1 1 
ATOM   5370  C  CE2 . TYR C  1 44  ? 44.671  -38.766 10.703  1.00 24.08 ? 47   TYR C CE2 1 
ATOM   5371  C  CZ  . TYR C  1 44  ? 44.081  -39.738 11.494  1.00 28.59 ? 47   TYR C CZ  1 
ATOM   5372  O  OH  . TYR C  1 44  ? 44.778  -40.285 12.572  1.00 29.82 ? 47   TYR C OH  1 
ATOM   5373  N  N   . LEU C  1 45  ? 41.281  -37.609 5.006   1.00 25.80 ? 48   LEU C N   1 
ATOM   5374  C  CA  . LEU C  1 45  ? 40.503  -37.367 3.799   1.00 28.45 ? 48   LEU C CA  1 
ATOM   5375  C  C   . LEU C  1 45  ? 41.305  -37.867 2.602   1.00 30.52 ? 48   LEU C C   1 
ATOM   5376  O  O   . LEU C  1 45  ? 42.518  -38.051 2.704   1.00 31.41 ? 48   LEU C O   1 
ATOM   5377  C  CB  . LEU C  1 45  ? 40.257  -35.860 3.633   1.00 27.39 ? 48   LEU C CB  1 
ATOM   5378  C  CG  . LEU C  1 45  ? 39.229  -35.217 4.557   1.00 26.68 ? 48   LEU C CG  1 
ATOM   5379  C  CD1 . LEU C  1 45  ? 39.313  -33.721 4.441   1.00 27.49 ? 48   LEU C CD1 1 
ATOM   5380  C  CD2 . LEU C  1 45  ? 37.867  -35.694 4.141   1.00 28.90 ? 48   LEU C CD2 1 
ATOM   5381  N  N   . PRO C  1 46  ? 40.643  -38.033 1.447   1.00 31.57 ? 49   PRO C N   1 
ATOM   5382  C  CA  . PRO C  1 46  ? 41.376  -38.227 0.209   1.00 31.36 ? 49   PRO C CA  1 
ATOM   5383  C  C   . PRO C  1 46  ? 42.427  -37.152 0.057   1.00 31.40 ? 49   PRO C C   1 
ATOM   5384  O  O   . PRO C  1 46  ? 42.139  -35.982 0.295   1.00 35.25 ? 49   PRO C O   1 
ATOM   5385  C  CB  . PRO C  1 46  ? 40.289  -38.049 -0.850  1.00 29.87 ? 49   PRO C CB  1 
ATOM   5386  C  CG  . PRO C  1 46  ? 39.105  -38.641 -0.214  1.00 31.88 ? 49   PRO C CG  1 
ATOM   5387  C  CD  . PRO C  1 46  ? 39.199  -38.250 1.258   1.00 31.14 ? 49   PRO C CD  1 
ATOM   5388  N  N   . ARG C  1 47  ? 43.612  -37.519 -0.418  1.00 30.56 ? 50   ARG C N   1 
ATOM   5389  C  CA  . ARG C  1 47  ? 44.737  -36.588 -0.396  1.00 27.71 ? 50   ARG C CA  1 
ATOM   5390  C  C   . ARG C  1 47  ? 44.668  -35.502 -1.447  1.00 24.37 ? 50   ARG C C   1 
ATOM   5391  O  O   . ARG C  1 47  ? 45.278  -34.443 -1.283  1.00 24.15 ? 50   ARG C O   1 
ATOM   5392  C  CB  . ARG C  1 47  ? 46.088  -37.307 -0.424  1.00 28.79 ? 50   ARG C CB  1 
ATOM   5393  C  CG  . ARG C  1 47  ? 46.391  -38.033 0.870   1.00 28.02 ? 50   ARG C CG  1 
ATOM   5394  C  CD  . ARG C  1 47  ? 47.709  -38.816 0.804   1.00 29.53 ? 50   ARG C CD  1 
ATOM   5395  N  NE  . ARG C  1 47  ? 47.898  -39.622 2.009   1.00 27.22 ? 50   ARG C NE  1 
ATOM   5396  C  CZ  . ARG C  1 47  ? 48.554  -39.198 3.085   1.00 27.32 ? 50   ARG C CZ  1 
ATOM   5397  N  NH1 . ARG C  1 47  ? 49.082  -37.981 3.089   1.00 27.55 ? 50   ARG C NH1 1 
ATOM   5398  N  NH2 . ARG C  1 47  ? 48.645  -39.970 4.168   1.00 25.24 ? 50   ARG C NH2 1 
ATOM   5399  N  N   . ASN C  1 48  ? 43.885  -35.733 -2.494  1.00 23.44 ? 51   ASN C N   1 
ATOM   5400  C  CA  . ASN C  1 48  ? 43.623  -34.693 -3.487  1.00 23.95 ? 51   ASN C CA  1 
ATOM   5401  C  C   . ASN C  1 48  ? 42.646  -33.571 -3.063  1.00 23.55 ? 51   ASN C C   1 
ATOM   5402  O  O   . ASN C  1 48  ? 42.515  -32.557 -3.752  1.00 25.24 ? 51   ASN C O   1 
ATOM   5403  C  CB  . ASN C  1 48  ? 43.225  -35.298 -4.843  1.00 26.29 ? 51   ASN C CB  1 
ATOM   5404  C  CG  . ASN C  1 48  ? 41.778  -35.779 -4.890  1.00 29.46 ? 51   ASN C CG  1 
ATOM   5405  O  OD1 . ASN C  1 48  ? 41.125  -35.993 -3.860  1.00 29.64 ? 51   ASN C OD1 1 
ATOM   5406  N  ND2 . ASN C  1 48  ? 41.291  -36.010 -6.100  1.00 28.23 ? 51   ASN C ND2 1 
ATOM   5407  N  N   . GLY C  1 49  ? 42.035  -33.710 -1.895  1.00 23.00 ? 52   GLY C N   1 
ATOM   5408  C  CA  . GLY C  1 49  ? 41.221  -32.631 -1.339  1.00 22.21 ? 52   GLY C CA  1 
ATOM   5409  C  C   . GLY C  1 49  ? 39.802  -32.592 -1.899  1.00 23.27 ? 52   GLY C C   1 
ATOM   5410  O  O   . GLY C  1 49  ? 39.107  -31.579 -1.777  1.00 22.04 ? 52   GLY C O   1 
ATOM   5411  N  N   . VAL C  1 50  ? 39.360  -33.708 -2.477  1.00 20.71 ? 53   VAL C N   1 
ATOM   5412  C  CA  . VAL C  1 50  ? 38.012  -33.824 -3.003  1.00 20.39 ? 53   VAL C CA  1 
ATOM   5413  C  C   . VAL C  1 50  ? 37.314  -34.986 -2.326  1.00 21.53 ? 53   VAL C C   1 
ATOM   5414  O  O   . VAL C  1 50  ? 37.820  -36.116 -2.341  1.00 20.47 ? 53   VAL C O   1 
ATOM   5415  C  CB  . VAL C  1 50  ? 38.001  -34.010 -4.529  1.00 23.02 ? 53   VAL C CB  1 
ATOM   5416  C  CG1 . VAL C  1 50  ? 36.593  -34.307 -5.015  1.00 23.34 ? 53   VAL C CG1 1 
ATOM   5417  C  CG2 . VAL C  1 50  ? 38.541  -32.772 -5.229  1.00 21.90 ? 53   VAL C CG2 1 
ATOM   5418  N  N   . ALA C  1 51  ? 36.162  -34.711 -1.704  1.00 20.59 ? 54   ALA C N   1 
ATOM   5419  C  CA  . ALA C  1 51  ? 35.615  -35.625 -0.707  1.00 18.36 ? 54   ALA C CA  1 
ATOM   5420  C  C   . ALA C  1 51  ? 34.079  -35.670 -0.662  1.00 20.56 ? 54   ALA C C   1 
ATOM   5421  O  O   . ALA C  1 51  ? 33.420  -34.697 -1.043  1.00 17.01 ? 54   ALA C O   1 
ATOM   5422  C  CB  . ALA C  1 51  ? 36.184  -35.276 0.676   1.00 16.93 ? 54   ALA C CB  1 
ATOM   5423  N  N   . THR C  1 52  ? 33.510  -36.770 -0.139  1.00 21.82 ? 55   THR C N   1 
ATOM   5424  C  CA  . THR C  1 52  ? 32.090  -36.763 0.243   1.00 23.97 ? 55   THR C CA  1 
ATOM   5425  C  C   . THR C  1 52  ? 31.833  -36.147 1.622   1.00 25.14 ? 55   THR C C   1 
ATOM   5426  O  O   . THR C  1 52  ? 32.716  -36.157 2.473   1.00 25.18 ? 55   THR C O   1 
ATOM   5427  C  CB  . THR C  1 52  ? 31.432  -38.142 0.170   1.00 19.71 ? 55   THR C CB  1 
ATOM   5428  O  OG1 . THR C  1 52  ? 31.880  -38.961 1.254   1.00 23.30 ? 55   THR C OG1 1 
ATOM   5429  C  CG2 . THR C  1 52  ? 31.729  -38.797 -1.171  1.00 22.43 ? 55   THR C CG2 1 
ATOM   5430  N  N   . PRO C  1 53  ? 30.623  -35.597 1.838   1.00 24.94 ? 56   PRO C N   1 
ATOM   5431  C  CA  . PRO C  1 53  ? 30.308  -35.111 3.170   1.00 24.12 ? 56   PRO C CA  1 
ATOM   5432  C  C   . PRO C  1 53  ? 30.538  -36.170 4.237   1.00 22.00 ? 56   PRO C C   1 
ATOM   5433  O  O   . PRO C  1 53  ? 31.079  -35.872 5.288   1.00 21.50 ? 56   PRO C O   1 
ATOM   5434  C  CB  . PRO C  1 53  ? 28.825  -34.754 3.060   1.00 24.35 ? 56   PRO C CB  1 
ATOM   5435  C  CG  . PRO C  1 53  ? 28.719  -34.189 1.662   1.00 25.36 ? 56   PRO C CG  1 
ATOM   5436  C  CD  . PRO C  1 53  ? 29.691  -35.057 0.828   1.00 26.87 ? 56   PRO C CD  1 
ATOM   5437  N  N   . VAL C  1 54  ? 30.159  -37.404 3.955   1.00 22.11 ? 57   VAL C N   1 
ATOM   5438  C  CA  . VAL C  1 54  ? 30.409  -38.495 4.883   1.00 23.37 ? 57   VAL C CA  1 
ATOM   5439  C  C   . VAL C  1 54  ? 31.918  -38.663 5.147   1.00 24.53 ? 57   VAL C C   1 
ATOM   5440  O  O   . VAL C  1 54  ? 32.335  -38.761 6.296   1.00 23.42 ? 57   VAL C O   1 
ATOM   5441  C  CB  . VAL C  1 54  ? 29.772  -39.816 4.387   1.00 22.45 ? 57   VAL C CB  1 
ATOM   5442  C  CG1 . VAL C  1 54  ? 30.420  -41.018 5.070   1.00 22.40 ? 57   VAL C CG1 1 
ATOM   5443  C  CG2 . VAL C  1 54  ? 28.294  -39.807 4.661   1.00 19.68 ? 57   VAL C CG2 1 
ATOM   5444  N  N   . GLN C  1 55  ? 32.743  -38.583 4.105   1.00 22.35 ? 58   GLN C N   1 
ATOM   5445  C  CA  . GLN C  1 55  ? 34.175  -38.746 4.309   1.00 24.76 ? 58   GLN C CA  1 
ATOM   5446  C  C   . GLN C  1 55  ? 34.693  -37.653 5.247   1.00 25.78 ? 58   GLN C C   1 
ATOM   5447  O  O   . GLN C  1 55  ? 35.520  -37.903 6.138   1.00 23.99 ? 58   GLN C O   1 
ATOM   5448  C  CB  . GLN C  1 55  ? 34.928  -38.736 2.970   1.00 23.22 ? 58   GLN C CB  1 
ATOM   5449  C  CG  . GLN C  1 55  ? 35.025  -40.096 2.319   1.00 23.18 ? 58   GLN C CG  1 
ATOM   5450  C  CD  . GLN C  1 55  ? 35.513  -40.045 0.876   1.00 26.39 ? 58   GLN C CD  1 
ATOM   5451  O  OE1 . GLN C  1 55  ? 35.208  -39.121 0.132   1.00 29.19 ? 58   GLN C OE1 1 
ATOM   5452  N  NE2 . GLN C  1 55  ? 36.284  -41.043 0.482   1.00 26.63 ? 58   GLN C NE2 1 
ATOM   5453  N  N   . ILE C  1 56  ? 34.166  -36.446 5.047   1.00 26.59 ? 59   ILE C N   1 
ATOM   5454  C  CA  . ILE C  1 56  ? 34.603  -35.260 5.762   1.00 23.67 ? 59   ILE C CA  1 
ATOM   5455  C  C   . ILE C  1 56  ? 34.205  -35.363 7.232   1.00 22.42 ? 59   ILE C C   1 
ATOM   5456  O  O   . ILE C  1 56  ? 35.021  -35.129 8.126   1.00 23.13 ? 59   ILE C O   1 
ATOM   5457  C  CB  . ILE C  1 56  ? 33.978  -33.999 5.137   1.00 23.54 ? 59   ILE C CB  1 
ATOM   5458  C  CG1 . ILE C  1 56  ? 34.594  -33.739 3.764   1.00 18.64 ? 59   ILE C CG1 1 
ATOM   5459  C  CG2 . ILE C  1 56  ? 34.129  -32.799 6.064   1.00 20.41 ? 59   ILE C CG2 1 
ATOM   5460  C  CD1 . ILE C  1 56  ? 33.857  -32.685 2.939   1.00 14.56 ? 59   ILE C CD1 1 
ATOM   5461  N  N   . ILE C  1 57  ? 33.025  -35.912 7.486   1.00 24.65 ? 60   ILE C N   1 
ATOM   5462  C  CA  . ILE C  1 57  ? 32.548  -36.022 8.858   1.00 21.38 ? 60   ILE C CA  1 
ATOM   5463  C  C   . ILE C  1 57  ? 33.291  -37.076 9.679   1.00 23.11 ? 60   ILE C C   1 
ATOM   5464  O  O   . ILE C  1 57  ? 33.720  -36.808 10.791  1.00 24.83 ? 60   ILE C O   1 
ATOM   5465  C  CB  . ILE C  1 57  ? 31.041  -36.194 8.922   1.00 20.74 ? 60   ILE C CB  1 
ATOM   5466  C  CG1 . ILE C  1 57  ? 30.361  -34.867 8.551   1.00 19.05 ? 60   ILE C CG1 1 
ATOM   5467  C  CG2 . ILE C  1 57  ? 30.593  -36.639 10.350  1.00 19.39 ? 60   ILE C CG2 1 
ATOM   5468  C  CD1 . ILE C  1 57  ? 28.936  -35.022 8.038   1.00 19.21 ? 60   ILE C CD1 1 
ATOM   5469  N  N   . ASN C  1 58  ? 33.443  -38.271 9.127   1.00 23.44 ? 61   ASN C N   1 
ATOM   5470  C  CA  . ASN C  1 58  ? 34.339  -39.273 9.688   1.00 24.62 ? 61   ASN C CA  1 
ATOM   5471  C  C   . ASN C  1 58  ? 35.765  -38.742 9.917   1.00 22.39 ? 61   ASN C C   1 
ATOM   5472  O  O   . ASN C  1 58  ? 36.307  -38.888 11.006  1.00 20.77 ? 61   ASN C O   1 
ATOM   5473  C  CB  . ASN C  1 58  ? 34.350  -40.541 8.814   1.00 26.06 ? 61   ASN C CB  1 
ATOM   5474  C  CG  . ASN C  1 58  ? 33.069  -41.358 8.958   1.00 28.08 ? 61   ASN C CG  1 
ATOM   5475  O  OD1 . ASN C  1 58  ? 32.602  -41.614 10.071  1.00 23.75 ? 61   ASN C OD1 1 
ATOM   5476  N  ND2 . ASN C  1 58  ? 32.503  -41.780 7.831   1.00 28.80 ? 61   ASN C ND2 1 
ATOM   5477  N  N   . ALA C  1 59  ? 36.292  -37.986 8.962   1.00 19.51 ? 62   ALA C N   1 
ATOM   5478  C  CA  . ALA C  1 59  ? 37.606  -37.364 9.146   1.00 20.82 ? 62   ALA C CA  1 
ATOM   5479  C  C   . ALA C  1 59  ? 37.717  -36.445 10.352  1.00 23.99 ? 62   ALA C C   1 
ATOM   5480  O  O   . ALA C  1 59  ? 38.681  -36.541 11.112  1.00 23.13 ? 62   ALA C O   1 
ATOM   5481  C  CB  . ALA C  1 59  ? 38.040  -36.630 7.897   1.00 18.38 ? 62   ALA C CB  1 
ATOM   5482  N  N   . VAL C  1 60  ? 36.845  -35.437 10.426  1.00 22.36 ? 63   VAL C N   1 
ATOM   5483  C  CA  . VAL C  1 60  ? 36.946  -34.460 11.503  1.00 17.83 ? 63   VAL C CA  1 
ATOM   5484  C  C   . VAL C  1 60  ? 36.706  -35.132 12.864  1.00 19.29 ? 63   VAL C C   1 
ATOM   5485  O  O   . VAL C  1 60  ? 37.298  -34.750 13.883  1.00 18.17 ? 63   VAL C O   1 
ATOM   5486  C  CB  . VAL C  1 60  ? 35.943  -33.285 11.325  1.00 17.49 ? 63   VAL C CB  1 
ATOM   5487  C  CG1 . VAL C  1 60  ? 36.260  -32.493 10.081  1.00 15.22 ? 63   VAL C CG1 1 
ATOM   5488  C  CG2 . VAL C  1 60  ? 34.498  -33.785 11.300  1.00 16.87 ? 63   VAL C CG2 1 
ATOM   5489  N  N   . GLN C  1 61  ? 35.780  -36.083 12.892  1.00 19.15 ? 64   GLN C N   1 
ATOM   5490  C  CA  . GLN C  1 61  ? 35.603  -36.900 14.080  1.00 24.19 ? 64   GLN C CA  1 
ATOM   5491  C  C   . GLN C  1 61  ? 36.843  -37.773 14.386  1.00 23.33 ? 64   GLN C C   1 
ATOM   5492  O  O   . GLN C  1 61  ? 37.446  -37.634 15.456  1.00 20.30 ? 64   GLN C O   1 
ATOM   5493  C  CB  . GLN C  1 61  ? 34.280  -37.690 14.038  1.00 23.58 ? 64   GLN C CB  1 
ATOM   5494  C  CG  . GLN C  1 61  ? 33.053  -36.782 13.894  1.00 25.14 ? 64   GLN C CG  1 
ATOM   5495  C  CD  . GLN C  1 61  ? 31.705  -37.499 14.079  1.00 29.01 ? 64   GLN C CD  1 
ATOM   5496  O  OE1 . GLN C  1 61  ? 30.690  -36.852 14.361  1.00 27.18 ? 64   GLN C OE1 1 
ATOM   5497  N  NE2 . GLN C  1 61  ? 31.693  -38.833 13.941  1.00 25.63 ? 64   GLN C NE2 1 
ATOM   5498  N  N   . GLU C  1 62  ? 37.285  -38.588 13.427  1.00 26.75 ? 65   GLU C N   1 
ATOM   5499  C  CA  . GLU C  1 62  ? 38.352  -39.564 13.713  1.00 27.18 ? 65   GLU C CA  1 
ATOM   5500  C  C   . GLU C  1 62  ? 39.652  -38.827 13.975  1.00 26.62 ? 65   GLU C C   1 
ATOM   5501  O  O   . GLU C  1 62  ? 40.302  -39.053 14.982  1.00 27.36 ? 65   GLU C O   1 
ATOM   5502  C  CB  . GLU C  1 62  ? 38.566  -40.556 12.569  1.00 30.51 ? 65   GLU C CB  1 
ATOM   5503  C  CG  . GLU C  1 62  ? 37.367  -41.419 12.189  1.00 39.54 ? 65   GLU C CG  1 
ATOM   5504  C  CD  . GLU C  1 62  ? 37.166  -42.647 13.091  1.00 43.69 ? 65   GLU C CD  1 
ATOM   5505  O  OE1 . GLU C  1 62  ? 38.085  -42.981 13.891  1.00 43.32 ? 65   GLU C OE1 1 
ATOM   5506  O  OE2 . GLU C  1 62  ? 36.061  -43.251 13.002  1.00 42.73 ? 65   GLU C OE2 1 
ATOM   5507  N  N   . GLY C  1 63  ? 39.998  -37.906 13.085  1.00 24.76 ? 66   GLY C N   1 
ATOM   5508  C  CA  . GLY C  1 63  ? 41.291  -37.250 13.127  1.00 25.97 ? 66   GLY C CA  1 
ATOM   5509  C  C   . GLY C  1 63  ? 41.446  -36.250 14.263  1.00 28.24 ? 66   GLY C C   1 
ATOM   5510  O  O   . GLY C  1 63  ? 42.564  -36.017 14.738  1.00 27.87 ? 66   GLY C O   1 
ATOM   5511  N  N   . LEU C  1 64  ? 40.349  -35.601 14.665  1.00 25.80 ? 67   LEU C N   1 
ATOM   5512  C  CA  . LEU C  1 64  ? 40.467  -34.407 15.511  1.00 22.09 ? 67   LEU C CA  1 
ATOM   5513  C  C   . LEU C  1 64  ? 39.421  -34.249 16.613  1.00 19.84 ? 67   LEU C C   1 
ATOM   5514  O  O   . LEU C  1 64  ? 39.461  -33.291 17.376  1.00 23.58 ? 67   LEU C O   1 
ATOM   5515  C  CB  . LEU C  1 64  ? 40.558  -33.147 14.662  1.00 20.96 ? 67   LEU C CB  1 
ATOM   5516  C  CG  . LEU C  1 64  ? 41.868  -32.905 13.916  1.00 23.43 ? 67   LEU C CG  1 
ATOM   5517  C  CD1 . LEU C  1 64  ? 41.676  -31.793 12.914  1.00 24.29 ? 67   LEU C CD1 1 
ATOM   5518  C  CD2 . LEU C  1 64  ? 43.017  -32.581 14.893  1.00 23.74 ? 67   LEU C CD2 1 
ATOM   5519  N  N   . ASN C  1 65  ? 38.483  -35.182 16.674  1.00 20.94 ? 68   ASN C N   1 
ATOM   5520  C  CA  . ASN C  1 65  ? 37.416  -35.167 17.673  1.00 22.75 ? 68   ASN C CA  1 
ATOM   5521  C  C   . ASN C  1 65  ? 36.536  -33.923 17.623  1.00 22.08 ? 68   ASN C C   1 
ATOM   5522  O  O   . ASN C  1 65  ? 36.016  -33.484 18.655  1.00 22.29 ? 68   ASN C O   1 
ATOM   5523  C  CB  . ASN C  1 65  ? 37.997  -35.336 19.070  1.00 24.78 ? 68   ASN C CB  1 
ATOM   5524  C  CG  . ASN C  1 65  ? 37.400  -36.510 19.804  1.00 23.45 ? 68   ASN C CG  1 
ATOM   5525  O  OD1 . ASN C  1 65  ? 36.323  -36.981 19.466  1.00 24.20 ? 68   ASN C OD1 1 
ATOM   5526  N  ND2 . ASN C  1 65  ? 38.084  -36.965 20.839  1.00 24.32 ? 68   ASN C ND2 1 
ATOM   5527  N  N   . PHE C  1 66  ? 36.313  -33.405 16.420  1.00 20.70 ? 69   PHE C N   1 
ATOM   5528  C  CA  . PHE C  1 66  ? 35.240  -32.430 16.187  1.00 21.53 ? 69   PHE C CA  1 
ATOM   5529  C  C   . PHE C  1 66  ? 33.916  -33.067 16.573  1.00 24.94 ? 69   PHE C C   1 
ATOM   5530  O  O   . PHE C  1 66  ? 33.668  -34.223 16.242  1.00 24.51 ? 69   PHE C O   1 
ATOM   5531  C  CB  . PHE C  1 66  ? 35.216  -32.019 14.715  1.00 22.48 ? 69   PHE C CB  1 
ATOM   5532  C  CG  . PHE C  1 66  ? 34.733  -30.597 14.473  1.00 22.67 ? 69   PHE C CG  1 
ATOM   5533  C  CD1 . PHE C  1 66  ? 35.418  -29.516 14.994  1.00 21.79 ? 69   PHE C CD1 1 
ATOM   5534  C  CD2 . PHE C  1 66  ? 33.647  -30.353 13.644  1.00 23.08 ? 69   PHE C CD2 1 
ATOM   5535  C  CE1 . PHE C  1 66  ? 35.022  -28.212 14.714  1.00 23.48 ? 69   PHE C CE1 1 
ATOM   5536  C  CE2 . PHE C  1 66  ? 33.229  -29.051 13.357  1.00 24.11 ? 69   PHE C CE2 1 
ATOM   5537  C  CZ  . PHE C  1 66  ? 33.913  -27.977 13.894  1.00 24.62 ? 69   PHE C CZ  1 
ATOM   5538  N  N   . ASP C  1 67  ? 33.082  -32.356 17.329  1.00 23.95 ? 70   ASP C N   1 
ATOM   5539  C  CA  . ASP C  1 67  ? 31.818  -32.952 17.734  1.00 24.14 ? 70   ASP C CA  1 
ATOM   5540  C  C   . ASP C  1 67  ? 30.838  -33.222 16.577  1.00 22.63 ? 70   ASP C C   1 
ATOM   5541  O  O   . ASP C  1 67  ? 30.967  -32.656 15.494  1.00 23.50 ? 70   ASP C O   1 
ATOM   5542  C  CB  . ASP C  1 67  ? 31.185  -32.202 18.923  1.00 22.80 ? 70   ASP C CB  1 
ATOM   5543  C  CG  . ASP C  1 67  ? 30.415  -30.973 18.505  1.00 24.73 ? 70   ASP C CG  1 
ATOM   5544  O  OD1 . ASP C  1 67  ? 29.200  -31.082 18.212  1.00 26.53 ? 70   ASP C OD1 1 
ATOM   5545  O  OD2 . ASP C  1 67  ? 30.994  -29.873 18.573  1.00 27.86 ? 70   ASP C OD2 1 
ATOM   5546  N  N   . ASN C  1 68  ? 29.897  -34.136 16.791  1.00 22.44 ? 71   ASN C N   1 
ATOM   5547  C  CA  . ASN C  1 68  ? 29.049  -34.631 15.700  1.00 22.26 ? 71   ASN C CA  1 
ATOM   5548  C  C   . ASN C  1 68  ? 28.098  -33.602 15.096  1.00 23.19 ? 71   ASN C C   1 
ATOM   5549  O  O   . ASN C  1 68  ? 27.995  -33.488 13.873  1.00 27.35 ? 71   ASN C O   1 
ATOM   5550  C  CB  . ASN C  1 68  ? 28.266  -35.875 16.114  1.00 19.44 ? 71   ASN C CB  1 
ATOM   5551  C  CG  . ASN C  1 68  ? 27.449  -36.455 14.963  1.00 23.30 ? 71   ASN C CG  1 
ATOM   5552  O  OD1 . ASN C  1 68  ? 26.224  -36.367 14.963  1.00 21.18 ? 71   ASN C OD1 1 
ATOM   5553  N  ND2 . ASN C  1 68  ? 28.135  -36.989 13.940  1.00 20.42 ? 71   ASN C ND2 1 
ATOM   5554  N  N   . GLN C  1 69  ? 27.379  -32.879 15.946  1.00 23.79 ? 72   GLN C N   1 
ATOM   5555  C  CA  . GLN C  1 69  ? 26.451  -31.861 15.468  1.00 24.66 ? 72   GLN C CA  1 
ATOM   5556  C  C   . GLN C  1 69  ? 27.161  -30.748 14.699  1.00 22.90 ? 72   GLN C C   1 
ATOM   5557  O  O   . GLN C  1 69  ? 26.736  -30.398 13.603  1.00 20.81 ? 72   GLN C O   1 
ATOM   5558  C  CB  . GLN C  1 69  ? 25.594  -31.304 16.605  1.00 26.63 ? 72   GLN C CB  1 
ATOM   5559  C  CG  . GLN C  1 69  ? 24.386  -32.176 16.910  1.00 31.75 ? 72   GLN C CG  1 
ATOM   5560  C  CD  . GLN C  1 69  ? 23.276  -31.435 17.655  1.00 35.56 ? 72   GLN C CD  1 
ATOM   5561  O  OE1 . GLN C  1 69  ? 23.453  -31.049 18.814  1.00 35.39 ? 72   GLN C OE1 1 
ATOM   5562  N  NE2 . GLN C  1 69  ? 22.090  -31.323 17.025  1.00 34.88 ? 72   GLN C NE2 1 
ATOM   5563  N  N   . ALA C  1 70  ? 28.287  -30.271 15.236  1.00 20.94 ? 73   ALA C N   1 
ATOM   5564  C  CA  . ALA C  1 70  ? 29.124  -29.279 14.556  1.00 19.91 ? 73   ALA C CA  1 
ATOM   5565  C  C   . ALA C  1 70  ? 29.663  -29.790 13.212  1.00 20.27 ? 73   ALA C C   1 
ATOM   5566  O  O   . ALA C  1 70  ? 29.676  -29.059 12.227  1.00 18.51 ? 73   ALA C O   1 
ATOM   5567  C  CB  . ALA C  1 70  ? 30.281  -28.870 15.451  1.00 19.53 ? 73   ALA C CB  1 
ATOM   5568  N  N   . ALA C  1 71  ? 30.038  -31.068 13.155  1.00 19.42 ? 74   ALA C N   1 
ATOM   5569  C  CA  . ALA C  1 71  ? 30.557  -31.619 11.914  1.00 18.99 ? 74   ALA C CA  1 
ATOM   5570  C  C   . ALA C  1 71  ? 29.448  -31.739 10.866  1.00 17.12 ? 74   ALA C C   1 
ATOM   5571  O  O   . ALA C  1 71  ? 29.665  -31.483 9.697   1.00 16.38 ? 74   ALA C O   1 
ATOM   5572  C  CB  . ALA C  1 71  ? 31.220  -32.954 12.151  1.00 14.43 ? 74   ALA C CB  1 
ATOM   5573  N  N   . VAL C  1 72  ? 28.275  -32.182 11.286  1.00 16.24 ? 75   VAL C N   1 
ATOM   5574  C  CA  . VAL C  1 72  ? 27.141  -32.278 10.375  1.00 18.17 ? 75   VAL C CA  1 
ATOM   5575  C  C   . VAL C  1 72  ? 26.738  -30.864 9.897   1.00 19.78 ? 75   VAL C C   1 
ATOM   5576  O  O   . VAL C  1 72  ? 26.568  -30.611 8.699   1.00 18.71 ? 75   VAL C O   1 
ATOM   5577  C  CB  . VAL C  1 72  ? 25.947  -33.018 11.064  1.00 15.07 ? 75   VAL C CB  1 
ATOM   5578  C  CG1 . VAL C  1 72  ? 24.645  -32.845 10.286  1.00 11.16 ? 75   VAL C CG1 1 
ATOM   5579  C  CG2 . VAL C  1 72  ? 26.272  -34.478 11.222  1.00 14.09 ? 75   VAL C CG2 1 
ATOM   5580  N  N   . PHE C  1 73  ? 26.679  -29.927 10.834  1.00 19.41 ? 76   PHE C N   1 
ATOM   5581  C  CA  . PHE C  1 73  ? 26.241  -28.570 10.521  1.00 17.61 ? 76   PHE C CA  1 
ATOM   5582  C  C   . PHE C  1 73  ? 27.182  -27.967 9.464   1.00 16.05 ? 76   PHE C C   1 
ATOM   5583  O  O   . PHE C  1 73  ? 26.740  -27.450 8.434   1.00 15.24 ? 76   PHE C O   1 
ATOM   5584  C  CB  . PHE C  1 73  ? 26.208  -27.715 11.806  1.00 14.00 ? 76   PHE C CB  1 
ATOM   5585  C  CG  . PHE C  1 73  ? 25.915  -26.247 11.561  1.00 17.68 ? 76   PHE C CG  1 
ATOM   5586  C  CD1 . PHE C  1 73  ? 26.953  -25.347 11.314  1.00 17.62 ? 76   PHE C CD1 1 
ATOM   5587  C  CD2 . PHE C  1 73  ? 24.606  -25.768 11.576  1.00 18.39 ? 76   PHE C CD2 1 
ATOM   5588  C  CE1 . PHE C  1 73  ? 26.692  -24.008 11.062  1.00 17.03 ? 76   PHE C CE1 1 
ATOM   5589  C  CE2 . PHE C  1 73  ? 24.328  -24.412 11.313  1.00 18.25 ? 76   PHE C CE2 1 
ATOM   5590  C  CZ  . PHE C  1 73  ? 25.369  -23.538 11.073  1.00 17.46 ? 76   PHE C CZ  1 
ATOM   5591  N  N   . ALA C  1 74  ? 28.483  -28.042 9.708   1.00 13.34 ? 77   ALA C N   1 
ATOM   5592  C  CA  . ALA C  1 74  ? 29.426  -27.327 8.844   1.00 15.37 ? 77   ALA C CA  1 
ATOM   5593  C  C   . ALA C  1 74  ? 29.582  -28.028 7.501   1.00 12.70 ? 77   ALA C C   1 
ATOM   5594  O  O   . ALA C  1 74  ? 29.698  -27.379 6.470   1.00 14.36 ? 77   ALA C O   1 
ATOM   5595  C  CB  . ALA C  1 74  ? 30.799  -27.142 9.519   1.00 12.87 ? 77   ALA C CB  1 
ATOM   5596  N  N   . THR C  1 75  ? 29.556  -29.352 7.516   1.00 14.80 ? 78   THR C N   1 
ATOM   5597  C  CA  . THR C  1 75  ? 29.792  -30.122 6.305   1.00 16.97 ? 78   THR C CA  1 
ATOM   5598  C  C   . THR C  1 75  ? 28.689  -29.943 5.282   1.00 15.62 ? 78   THR C C   1 
ATOM   5599  O  O   . THR C  1 75  ? 28.942  -29.646 4.107   1.00 18.24 ? 78   THR C O   1 
ATOM   5600  C  CB  . THR C  1 75  ? 29.979  -31.626 6.599   1.00 17.69 ? 78   THR C CB  1 
ATOM   5601  O  OG1 . THR C  1 75  ? 31.107  -31.803 7.457   1.00 16.78 ? 78   THR C OG1 1 
ATOM   5602  C  CG2 . THR C  1 75  ? 30.260  -32.382 5.292   1.00 20.34 ? 78   THR C CG2 1 
ATOM   5603  N  N   . TYR C  1 76  ? 27.459  -30.105 5.734   1.00 15.49 ? 79   TYR C N   1 
ATOM   5604  C  CA  . TYR C  1 76  ? 26.316  -30.022 4.840   1.00 16.06 ? 79   TYR C CA  1 
ATOM   5605  C  C   . TYR C  1 76  ? 25.994  -28.576 4.453   1.00 16.02 ? 79   TYR C C   1 
ATOM   5606  O  O   . TYR C  1 76  ? 25.609  -28.321 3.320   1.00 16.90 ? 79   TYR C O   1 
ATOM   5607  C  CB  . TYR C  1 76  ? 25.131  -30.719 5.490   1.00 16.38 ? 79   TYR C CB  1 
ATOM   5608  C  CG  . TYR C  1 76  ? 25.284  -32.218 5.463   1.00 16.81 ? 79   TYR C CG  1 
ATOM   5609  C  CD1 . TYR C  1 76  ? 25.263  -32.920 4.236   1.00 15.15 ? 79   TYR C CD1 1 
ATOM   5610  C  CD2 . TYR C  1 76  ? 25.554  -32.925 6.626   1.00 14.81 ? 79   TYR C CD2 1 
ATOM   5611  C  CE1 . TYR C  1 76  ? 25.408  -34.296 4.198   1.00 14.66 ? 79   TYR C CE1 1 
ATOM   5612  C  CE2 . TYR C  1 76  ? 25.723  -34.307 6.597   1.00 18.64 ? 79   TYR C CE2 1 
ATOM   5613  C  CZ  . TYR C  1 76  ? 25.638  -34.982 5.380   1.00 17.57 ? 79   TYR C CZ  1 
ATOM   5614  O  OH  . TYR C  1 76  ? 25.800  -36.329 5.357   1.00 20.95 ? 79   TYR C OH  1 
ATOM   5615  N  N   . ALA C  1 77  ? 26.364  -27.622 5.309   1.00 14.78 ? 80   ALA C N   1 
ATOM   5616  C  CA  . ALA C  1 77  ? 26.292  -26.202 4.938   1.00 16.24 ? 80   ALA C CA  1 
ATOM   5617  C  C   . ALA C  1 77  ? 27.238  -25.921 3.784   1.00 17.32 ? 80   ALA C C   1 
ATOM   5618  O  O   . ALA C  1 77  ? 26.840  -25.336 2.776   1.00 17.59 ? 80   ALA C O   1 
ATOM   5619  C  CB  . ALA C  1 77  ? 26.622  -25.284 6.127   1.00 15.79 ? 80   ALA C CB  1 
ATOM   5620  N  N   . ALA C  1 78  ? 28.488  -26.355 3.925   1.00 15.00 ? 81   ALA C N   1 
ATOM   5621  C  CA  . ALA C  1 78  ? 29.473  -26.142 2.859   1.00 17.24 ? 81   ALA C CA  1 
ATOM   5622  C  C   . ALA C  1 78  ? 29.060  -26.843 1.562   1.00 15.48 ? 81   ALA C C   1 
ATOM   5623  O  O   . ALA C  1 78  ? 29.133  -26.276 0.483   1.00 21.37 ? 81   ALA C O   1 
ATOM   5624  C  CB  . ALA C  1 78  ? 30.884  -26.603 3.311   1.00 10.04 ? 81   ALA C CB  1 
ATOM   5625  N  N   . HIS C  1 79  ? 28.594  -28.074 1.689   1.00 15.89 ? 82   HIS C N   1 
ATOM   5626  C  CA  . HIS C  1 79  ? 28.239  -28.880 0.544   1.00 16.07 ? 82   HIS C CA  1 
ATOM   5627  C  C   . HIS C  1 79  ? 27.069  -28.245 -0.219  1.00 16.79 ? 82   HIS C C   1 
ATOM   5628  O  O   . HIS C  1 79  ? 27.110  -28.085 -1.444  1.00 19.53 ? 82   HIS C O   1 
ATOM   5629  C  CB  . HIS C  1 79  ? 27.920  -30.304 1.022   1.00 15.43 ? 82   HIS C CB  1 
ATOM   5630  C  CG  . HIS C  1 79  ? 27.664  -31.270 -0.086  1.00 20.36 ? 82   HIS C CG  1 
ATOM   5631  N  ND1 . HIS C  1 79  ? 28.468  -31.343 -1.204  1.00 20.40 ? 82   HIS C ND1 1 
ATOM   5632  C  CD2 . HIS C  1 79  ? 26.696  -32.207 -0.250  1.00 17.27 ? 82   HIS C CD2 1 
ATOM   5633  C  CE1 . HIS C  1 79  ? 27.985  -32.256 -2.028  1.00 18.86 ? 82   HIS C CE1 1 
ATOM   5634  N  NE2 . HIS C  1 79  ? 26.918  -32.802 -1.467  1.00 20.78 ? 82   HIS C NE2 1 
ATOM   5635  N  N   . LEU C  1 80  ? 26.110  -27.729 0.528   1.00 14.68 ? 83   LEU C N   1 
ATOM   5636  C  CA  . LEU C  1 80  ? 24.943  -27.084 -0.054  1.00 15.40 ? 83   LEU C CA  1 
ATOM   5637  C  C   . LEU C  1 80  ? 25.317  -25.858 -0.868  1.00 15.86 ? 83   LEU C C   1 
ATOM   5638  O  O   . LEU C  1 80  ? 24.816  -25.678 -1.991  1.00 16.07 ? 83   LEU C O   1 
ATOM   5639  C  CB  . LEU C  1 80  ? 23.944  -26.699 1.045   1.00 13.49 ? 83   LEU C CB  1 
ATOM   5640  C  CG  . LEU C  1 80  ? 23.103  -27.838 1.622   1.00 13.60 ? 83   LEU C CG  1 
ATOM   5641  C  CD1 . LEU C  1 80  ? 22.463  -27.366 2.930   1.00 7.69  ? 83   LEU C CD1 1 
ATOM   5642  C  CD2 . LEU C  1 80  ? 22.013  -28.312 0.628   1.00 12.59 ? 83   LEU C CD2 1 
ATOM   5643  N  N   . VAL C  1 81  ? 26.216  -25.026 -0.339  1.00 12.89 ? 84   VAL C N   1 
ATOM   5644  C  CA  . VAL C  1 81  ? 26.590  -23.822 -1.089  1.00 14.28 ? 84   VAL C CA  1 
ATOM   5645  C  C   . VAL C  1 81  ? 27.773  -24.017 -2.039  1.00 13.98 ? 84   VAL C C   1 
ATOM   5646  O  O   . VAL C  1 81  ? 27.889  -23.292 -3.020  1.00 15.82 ? 84   VAL C O   1 
ATOM   5647  C  CB  . VAL C  1 81  ? 26.856  -22.619 -0.170  1.00 13.83 ? 84   VAL C CB  1 
ATOM   5648  C  CG1 . VAL C  1 81  ? 25.604  -22.208 0.504   1.00 16.90 ? 84   VAL C CG1 1 
ATOM   5649  C  CG2 . VAL C  1 81  ? 27.933  -22.959 0.874   1.00 14.86 ? 84   VAL C CG2 1 
ATOM   5650  N  N   . ASP C  1 82  ? 28.682  -24.943 -1.716  1.00 15.04 ? 85   ASP C N   1 
ATOM   5651  C  CA  . ASP C  1 82  ? 29.987  -25.022 -2.401  1.00 14.88 ? 85   ASP C CA  1 
ATOM   5652  C  C   . ASP C  1 82  ? 30.185  -26.345 -3.162  1.00 17.07 ? 85   ASP C C   1 
ATOM   5653  O  O   . ASP C  1 82  ? 31.113  -26.461 -3.967  1.00 17.56 ? 85   ASP C O   1 
ATOM   5654  C  CB  . ASP C  1 82  ? 31.147  -24.888 -1.402  1.00 13.58 ? 85   ASP C CB  1 
ATOM   5655  C  CG  . ASP C  1 82  ? 31.363  -23.468 -0.910  1.00 16.94 ? 85   ASP C CG  1 
ATOM   5656  O  OD1 . ASP C  1 82  ? 30.928  -22.524 -1.592  1.00 18.26 ? 85   ASP C OD1 1 
ATOM   5657  O  OD2 . ASP C  1 82  ? 31.998  -23.297 0.169   1.00 18.34 ? 85   ASP C OD2 1 
ATOM   5658  N  N   . GLY C  1 83  ? 29.397  -27.370 -2.830  1.00 15.37 ? 86   GLY C N   1 
ATOM   5659  C  CA  . GLY C  1 83  ? 29.616  -28.711 -3.385  1.00 14.41 ? 86   GLY C CA  1 
ATOM   5660  C  C   . GLY C  1 83  ? 28.614  -29.140 -4.453  1.00 18.06 ? 86   GLY C C   1 
ATOM   5661  O  O   . GLY C  1 83  ? 27.596  -28.490 -4.648  1.00 20.02 ? 86   GLY C O   1 
ATOM   5662  N  N   . ASN C  1 84  ? 28.878  -30.272 -5.106  1.00 17.23 ? 87   ASN C N   1 
ATOM   5663  C  CA  . ASN C  1 84  ? 27.982  -30.806 -6.120  1.00 18.47 ? 87   ASN C CA  1 
ATOM   5664  C  C   . ASN C  1 84  ? 27.039  -31.855 -5.569  1.00 20.28 ? 87   ASN C C   1 
ATOM   5665  O  O   . ASN C  1 84  ? 27.470  -32.936 -5.165  1.00 16.58 ? 87   ASN C O   1 
ATOM   5666  C  CB  . ASN C  1 84  ? 28.774  -31.422 -7.266  1.00 19.13 ? 87   ASN C CB  1 
ATOM   5667  C  CG  . ASN C  1 84  ? 27.896  -31.777 -8.459  1.00 18.76 ? 87   ASN C CG  1 
ATOM   5668  O  OD1 . ASN C  1 84  ? 26.954  -32.563 -8.335  1.00 19.49 ? 87   ASN C OD1 1 
ATOM   5669  N  ND2 . ASN C  1 84  ? 28.273  -31.293 -9.641  1.00 16.31 ? 87   ASN C ND2 1 
ATOM   5670  N  N   . LEU C  1 85  ? 25.746  -31.567 -5.650  1.00 19.71 ? 88   LEU C N   1 
ATOM   5671  C  CA  . LEU C  1 85  ? 24.747  -32.301 -4.883  1.00 21.93 ? 88   LEU C CA  1 
ATOM   5672  C  C   . LEU C  1 85  ? 24.429  -33.636 -5.554  1.00 19.64 ? 88   LEU C C   1 
ATOM   5673  O  O   . LEU C  1 85  ? 23.902  -34.554 -4.924  1.00 20.94 ? 88   LEU C O   1 
ATOM   5674  C  CB  . LEU C  1 85  ? 23.469  -31.451 -4.740  1.00 18.86 ? 88   LEU C CB  1 
ATOM   5675  C  CG  . LEU C  1 85  ? 23.322  -30.550 -3.498  1.00 20.84 ? 88   LEU C CG  1 
ATOM   5676  C  CD1 . LEU C  1 85  ? 24.620  -30.293 -2.717  1.00 18.25 ? 88   LEU C CD1 1 
ATOM   5677  C  CD2 . LEU C  1 85  ? 22.590  -29.261 -3.775  1.00 18.88 ? 88   LEU C CD2 1 
ATOM   5678  N  N   . ILE C  1 86  ? 24.742  -33.740 -6.838  1.00 20.85 ? 89   ILE C N   1 
ATOM   5679  C  CA  . ILE C  1 86  ? 24.487  -34.970 -7.590  1.00 19.02 ? 89   ILE C CA  1 
ATOM   5680  C  C   . ILE C  1 86  ? 25.618  -35.998 -7.462  1.00 19.92 ? 89   ILE C C   1 
ATOM   5681  O  O   . ILE C  1 86  ? 25.373  -37.154 -7.084  1.00 18.56 ? 89   ILE C O   1 
ATOM   5682  C  CB  . ILE C  1 86  ? 24.206  -34.671 -9.071  1.00 20.95 ? 89   ILE C CB  1 
ATOM   5683  C  CG1 . ILE C  1 86  ? 23.031  -33.691 -9.206  1.00 21.49 ? 89   ILE C CG1 1 
ATOM   5684  C  CG2 . ILE C  1 86  ? 23.950  -35.979 -9.854  1.00 17.15 ? 89   ILE C CG2 1 
ATOM   5685  C  CD1 . ILE C  1 86  ? 21.711  -34.185 -8.562  1.00 21.10 ? 89   ILE C CD1 1 
ATOM   5686  N  N   . THR C  1 87  ? 26.857  -35.561 -7.691  1.00 17.54 ? 90   THR C N   1 
ATOM   5687  C  CA  . THR C  1 87  ? 28.018  -36.442 -7.491  1.00 17.42 ? 90   THR C CA  1 
ATOM   5688  C  C   . THR C  1 87  ? 28.364  -36.591 -6.016  1.00 18.59 ? 90   THR C C   1 
ATOM   5689  O  O   . THR C  1 87  ? 29.051  -37.549 -5.629  1.00 18.03 ? 90   THR C O   1 
ATOM   5690  C  CB  . THR C  1 87  ? 29.253  -35.926 -8.232  1.00 19.22 ? 90   THR C CB  1 
ATOM   5691  O  OG1 . THR C  1 87  ? 29.617  -34.635 -7.698  1.00 21.86 ? 90   THR C OG1 1 
ATOM   5692  C  CG2 . THR C  1 87  ? 28.956  -35.785 -9.749  1.00 15.19 ? 90   THR C CG2 1 
ATOM   5693  N  N   . ASP C  1 88  ? 27.804  -35.709 -5.183  1.00 16.81 ? 91   ASP C N   1 
ATOM   5694  C  CA  . ASP C  1 88  ? 27.977  -35.786 -3.733  1.00 17.17 ? 91   ASP C CA  1 
ATOM   5695  C  C   . ASP C  1 88  ? 29.419  -35.527 -3.371  1.00 18.36 ? 91   ASP C C   1 
ATOM   5696  O  O   . ASP C  1 88  ? 29.939  -36.089 -2.409  1.00 21.83 ? 91   ASP C O   1 
ATOM   5697  C  CB  . ASP C  1 88  ? 27.542  -37.149 -3.180  1.00 17.82 ? 91   ASP C CB  1 
ATOM   5698  C  CG  . ASP C  1 88  ? 27.190  -37.087 -1.700  1.00 20.44 ? 91   ASP C CG  1 
ATOM   5699  O  OD1 . ASP C  1 88  ? 26.610  -36.073 -1.284  1.00 19.67 ? 91   ASP C OD1 1 
ATOM   5700  O  OD2 . ASP C  1 88  ? 27.500  -38.031 -0.946  1.00 23.98 ? 91   ASP C OD2 1 
ATOM   5701  N  N   . LEU C  1 89  ? 30.039  -34.620 -4.116  1.00 19.70 ? 92   LEU C N   1 
ATOM   5702  C  CA  . LEU C  1 89  ? 31.451  -34.326 -3.976  1.00 20.07 ? 92   LEU C CA  1 
ATOM   5703  C  C   . LEU C  1 89  ? 31.677  -32.867 -3.648  1.00 19.32 ? 92   LEU C C   1 
ATOM   5704  O  O   . LEU C  1 89  ? 31.068  -31.980 -4.265  1.00 17.21 ? 92   LEU C O   1 
ATOM   5705  C  CB  . LEU C  1 89  ? 32.183  -34.665 -5.269  1.00 20.74 ? 92   LEU C CB  1 
ATOM   5706  C  CG  . LEU C  1 89  ? 32.282  -36.174 -5.489  1.00 18.61 ? 92   LEU C CG  1 
ATOM   5707  C  CD1 . LEU C  1 89  ? 32.966  -36.421 -6.823  1.00 17.34 ? 92   LEU C CD1 1 
ATOM   5708  C  CD2 . LEU C  1 89  ? 33.058  -36.800 -4.340  1.00 14.00 ? 92   LEU C CD2 1 
ATOM   5709  N  N   . LEU C  1 90  ? 32.610  -32.607 -2.736  1.00 16.91 ? 93   LEU C N   1 
ATOM   5710  C  CA  . LEU C  1 90  ? 32.958  -31.224 -2.416  1.00 18.19 ? 93   LEU C CA  1 
ATOM   5711  C  C   . LEU C  1 90  ? 34.464  -31.062 -2.468  1.00 18.65 ? 93   LEU C C   1 
ATOM   5712  O  O   . LEU C  1 90  ? 35.194  -31.936 -2.009  1.00 20.67 ? 93   LEU C O   1 
ATOM   5713  C  CB  . LEU C  1 90  ? 32.439  -30.867 -1.017  1.00 19.23 ? 93   LEU C CB  1 
ATOM   5714  C  CG  . LEU C  1 90  ? 32.936  -29.597 -0.338  1.00 19.47 ? 93   LEU C CG  1 
ATOM   5715  C  CD1 . LEU C  1 90  ? 32.415  -28.363 -1.066  1.00 16.26 ? 93   LEU C CD1 1 
ATOM   5716  C  CD2 . LEU C  1 90  ? 32.472  -29.602 1.119   1.00 22.18 ? 93   LEU C CD2 1 
ATOM   5717  N  N   . SER C  1 91  ? 34.933  -29.980 -3.077  1.00 19.28 ? 94   SER C N   1 
ATOM   5718  C  CA  . SER C  1 91  ? 36.348  -29.640 -2.996  1.00 18.29 ? 94   SER C CA  1 
ATOM   5719  C  C   . SER C  1 91  ? 36.609  -28.776 -1.765  1.00 18.33 ? 94   SER C C   1 
ATOM   5720  O  O   . SER C  1 91  ? 35.935  -27.767 -1.557  1.00 20.25 ? 94   SER C O   1 
ATOM   5721  C  CB  . SER C  1 91  ? 36.797  -28.894 -4.248  1.00 14.41 ? 94   SER C CB  1 
ATOM   5722  O  OG  . SER C  1 91  ? 37.924  -28.068 -3.966  1.00 19.66 ? 94   SER C OG  1 
ATOM   5723  N  N   . ILE C  1 92  ? 37.648  -29.100 -1.010  1.00 17.66 ? 95   ILE C N   1 
ATOM   5724  C  CA  . ILE C  1 92  ? 37.991  -28.305 0.163   1.00 18.41 ? 95   ILE C CA  1 
ATOM   5725  C  C   . ILE C  1 92  ? 38.777  -27.057 -0.234  1.00 19.90 ? 95   ILE C C   1 
ATOM   5726  O  O   . ILE C  1 92  ? 39.267  -26.339 0.627   1.00 21.99 ? 95   ILE C O   1 
ATOM   5727  C  CB  . ILE C  1 92  ? 38.802  -29.115 1.183   1.00 17.99 ? 95   ILE C CB  1 
ATOM   5728  C  CG1 . ILE C  1 92  ? 40.219  -29.409 0.653   1.00 18.22 ? 95   ILE C CG1 1 
ATOM   5729  C  CG2 . ILE C  1 92  ? 38.101  -30.409 1.505   1.00 19.81 ? 95   ILE C CG2 1 
ATOM   5730  C  CD1 . ILE C  1 92  ? 41.120  -30.107 1.682   1.00 14.91 ? 95   ILE C CD1 1 
ATOM   5731  N  N   . GLY C  1 93  ? 38.894  -26.803 -1.537  1.00 20.60 ? 96   GLY C N   1 
ATOM   5732  C  CA  . GLY C  1 93  ? 39.641  -25.640 -2.030  1.00 21.06 ? 96   GLY C CA  1 
ATOM   5733  C  C   . GLY C  1 93  ? 39.029  -25.032 -3.286  1.00 24.04 ? 96   GLY C C   1 
ATOM   5734  O  O   . GLY C  1 93  ? 37.870  -24.582 -3.275  1.00 24.08 ? 96   GLY C O   1 
ATOM   5735  N  N   . ARG C  1 94  ? 39.822  -24.946 -4.349  1.00 22.52 ? 97   ARG C N   1 
ATOM   5736  C  CA  . ARG C  1 94  ? 39.410  -24.226 -5.554  1.00 24.86 ? 97   ARG C CA  1 
ATOM   5737  C  C   . ARG C  1 94  ? 38.320  -24.988 -6.286  1.00 21.17 ? 97   ARG C C   1 
ATOM   5738  O  O   . ARG C  1 94  ? 38.112  -26.161 -6.018  1.00 17.90 ? 97   ARG C O   1 
ATOM   5739  C  CB  . ARG C  1 94  ? 40.596  -24.007 -6.491  1.00 28.35 ? 97   ARG C CB  1 
ATOM   5740  C  CG  . ARG C  1 94  ? 41.308  -25.304 -6.862  1.00 30.59 ? 97   ARG C CG  1 
ATOM   5741  C  CD  . ARG C  1 94  ? 42.355  -25.109 -7.975  1.00 33.58 ? 97   ARG C CD  1 
ATOM   5742  N  NE  . ARG C  1 94  ? 43.160  -26.326 -8.097  1.00 36.62 ? 97   ARG C NE  1 
ATOM   5743  C  CZ  . ARG C  1 94  ? 42.835  -27.351 -8.874  1.00 37.75 ? 97   ARG C CZ  1 
ATOM   5744  N  NH1 . ARG C  1 94  ? 41.802  -27.244 -9.712  1.00 38.29 ? 97   ARG C NH1 1 
ATOM   5745  N  NH2 . ARG C  1 94  ? 43.578  -28.452 -8.864  1.00 37.19 ? 97   ARG C NH2 1 
ATOM   5746  N  N   . LYS C  1 95  ? 37.581  -24.294 -7.159  1.00 22.60 ? 98   LYS C N   1 
ATOM   5747  C  CA  . LYS C  1 95  ? 36.638  -24.967 -8.057  1.00 21.50 ? 98   LYS C CA  1 
ATOM   5748  C  C   . LYS C  1 95  ? 37.435  -25.981 -8.870  1.00 23.57 ? 98   LYS C C   1 
ATOM   5749  O  O   . LYS C  1 95  ? 38.537  -25.672 -9.342  1.00 20.29 ? 98   LYS C O   1 
ATOM   5750  C  CB  . LYS C  1 95  ? 35.954  -23.964 -9.000  1.00 19.02 ? 98   LYS C CB  1 
ATOM   5751  C  CG  . LYS C  1 95  ? 34.795  -24.547 -9.810  1.00 19.09 ? 98   LYS C CG  1 
ATOM   5752  C  CD  . LYS C  1 95  ? 34.067  -23.473 -10.638 1.00 23.43 ? 98   LYS C CD  1 
ATOM   5753  C  CE  . LYS C  1 95  ? 33.069  -24.095 -11.645 1.00 24.93 ? 98   LYS C CE  1 
ATOM   5754  N  NZ  . LYS C  1 95  ? 32.377  -25.328 -11.088 1.00 24.23 ? 98   LYS C NZ  1 
ATOM   5755  N  N   . THR C  1 96  ? 36.903  -27.193 -9.003  1.00 23.75 ? 99   THR C N   1 
ATOM   5756  C  CA  . THR C  1 96  ? 37.572  -28.226 -9.784  1.00 24.16 ? 99   THR C CA  1 
ATOM   5757  C  C   . THR C  1 96  ? 36.572  -29.009 -10.619 1.00 28.36 ? 99   THR C C   1 
ATOM   5758  O  O   . THR C  1 96  ? 35.450  -29.237 -10.179 1.00 25.98 ? 99   THR C O   1 
ATOM   5759  C  CB  . THR C  1 96  ? 38.356  -29.210 -8.891  1.00 22.58 ? 99   THR C CB  1 
ATOM   5760  O  OG1 . THR C  1 96  ? 38.747  -30.342 -9.673  1.00 22.17 ? 99   THR C OG1 1 
ATOM   5761  C  CG2 . THR C  1 96  ? 37.493  -29.701 -7.732  1.00 21.68 ? 99   THR C CG2 1 
ATOM   5762  N  N   . ARG C  1 97  ? 37.030  -29.532 -11.757 1.00 29.24 ? 100  ARG C N   1 
ATOM   5763  C  CA  . ARG C  1 97  ? 36.207  -30.391 -12.603 1.00 26.76 ? 100  ARG C CA  1 
ATOM   5764  C  C   . ARG C  1 97  ? 35.960  -31.785 -12.022 1.00 26.12 ? 100  ARG C C   1 
ATOM   5765  O  O   . ARG C  1 97  ? 35.107  -32.533 -12.519 1.00 24.22 ? 100  ARG C O   1 
ATOM   5766  C  CB  . ARG C  1 97  ? 36.798  -30.493 -14.018 1.00 28.79 ? 100  ARG C CB  1 
ATOM   5767  C  CG  . ARG C  1 97  ? 36.274  -29.441 -14.963 1.00 34.86 ? 100  ARG C CG  1 
ATOM   5768  C  CD  . ARG C  1 97  ? 37.219  -29.227 -16.133 1.00 42.44 ? 100  ARG C CD  1 
ATOM   5769  N  NE  . ARG C  1 97  ? 38.614  -29.229 -15.701 1.00 46.95 ? 100  ARG C NE  1 
ATOM   5770  C  CZ  . ARG C  1 97  ? 39.646  -28.921 -16.486 1.00 48.80 ? 100  ARG C CZ  1 
ATOM   5771  N  NH1 . ARG C  1 97  ? 39.449  -28.609 -17.762 1.00 48.94 ? 100  ARG C NH1 1 
ATOM   5772  N  NH2 . ARG C  1 97  ? 40.879  -28.939 -15.998 1.00 48.07 ? 100  ARG C NH2 1 
ATOM   5773  N  N   . LEU C  1 98  ? 36.687  -32.131 -10.966 1.00 23.81 ? 101  LEU C N   1 
ATOM   5774  C  CA  . LEU C  1 98  ? 36.533  -33.449 -10.352 1.00 24.73 ? 101  LEU C CA  1 
ATOM   5775  C  C   . LEU C  1 98  ? 35.258  -33.572 -9.516  1.00 23.65 ? 101  LEU C C   1 
ATOM   5776  O  O   . LEU C  1 98  ? 34.935  -34.646 -9.047  1.00 19.98 ? 101  LEU C O   1 
ATOM   5777  C  CB  . LEU C  1 98  ? 37.758  -33.820 -9.494  1.00 24.79 ? 101  LEU C CB  1 
ATOM   5778  C  CG  . LEU C  1 98  ? 39.167  -33.644 -10.096 1.00 26.03 ? 101  LEU C CG  1 
ATOM   5779  C  CD1 . LEU C  1 98  ? 40.248  -34.198 -9.149  1.00 22.89 ? 101  LEU C CD1 1 
ATOM   5780  C  CD2 . LEU C  1 98  ? 39.256  -34.298 -11.454 1.00 22.75 ? 101  LEU C CD2 1 
ATOM   5781  N  N   . THR C  1 99  ? 34.522  -32.482 -9.326  1.00 24.47 ? 102  THR C N   1 
ATOM   5782  C  CA  . THR C  1 99  ? 33.226  -32.615 -8.658  1.00 22.98 ? 102  THR C CA  1 
ATOM   5783  C  C   . THR C  1 99  ? 32.062  -32.920 -9.642  1.00 24.11 ? 102  THR C C   1 
ATOM   5784  O  O   . THR C  1 99  ? 30.936  -33.237 -9.221  1.00 22.63 ? 102  THR C O   1 
ATOM   5785  C  CB  . THR C  1 99  ? 32.931  -31.431 -7.694  1.00 19.72 ? 102  THR C CB  1 
ATOM   5786  O  OG1 . THR C  1 99  ? 32.893  -30.207 -8.425  1.00 16.92 ? 102  THR C OG1 1 
ATOM   5787  C  CG2 . THR C  1 99  ? 34.031  -31.290 -6.633  1.00 19.47 ? 102  THR C CG2 1 
ATOM   5788  N  N   . GLY C  1 100 ? 32.358  -32.886 -10.944 1.00 21.80 ? 103  GLY C N   1 
ATOM   5789  C  CA  . GLY C  1 100 ? 31.451  -33.425 -11.964 1.00 19.19 ? 103  GLY C CA  1 
ATOM   5790  C  C   . GLY C  1 100 ? 30.621  -32.380 -12.708 1.00 21.71 ? 103  GLY C C   1 
ATOM   5791  O  O   . GLY C  1 100 ? 30.924  -31.183 -12.668 1.00 20.16 ? 103  GLY C O   1 
ATOM   5792  N  N   . PRO C  1 101 ? 29.596  -32.830 -13.456 1.00 21.38 ? 104  PRO C N   1 
ATOM   5793  C  CA  . PRO C  1 101 ? 28.792  -31.883 -14.229 1.00 22.82 ? 104  PRO C CA  1 
ATOM   5794  C  C   . PRO C  1 101 ? 28.128  -30.850 -13.304 1.00 23.80 ? 104  PRO C C   1 
ATOM   5795  O  O   . PRO C  1 101 ? 27.576  -31.216 -12.279 1.00 22.84 ? 104  PRO C O   1 
ATOM   5796  C  CB  . PRO C  1 101 ? 27.732  -32.775 -14.897 1.00 22.53 ? 104  PRO C CB  1 
ATOM   5797  C  CG  . PRO C  1 101 ? 28.359  -34.134 -14.941 1.00 23.86 ? 104  PRO C CG  1 
ATOM   5798  C  CD  . PRO C  1 101 ? 29.193  -34.230 -13.685 1.00 22.21 ? 104  PRO C CD  1 
ATOM   5799  N  N   . ASP C  1 102 ? 28.251  -29.571 -13.642 1.00 22.45 ? 105  ASP C N   1 
ATOM   5800  C  CA  . ASP C  1 102 ? 27.666  -28.499 -12.857 1.00 23.83 ? 105  ASP C CA  1 
ATOM   5801  C  C   . ASP C  1 102 ? 26.158  -28.368 -13.021 1.00 24.40 ? 105  ASP C C   1 
ATOM   5802  O  O   . ASP C  1 102 ? 25.608  -28.692 -14.062 1.00 26.51 ? 105  ASP C O   1 
ATOM   5803  C  CB  . ASP C  1 102 ? 28.330  -27.177 -13.198 1.00 26.49 ? 105  ASP C CB  1 
ATOM   5804  C  CG  . ASP C  1 102 ? 29.597  -26.949 -12.404 1.00 30.10 ? 105  ASP C CG  1 
ATOM   5805  O  OD1 . ASP C  1 102 ? 29.880  -27.749 -11.477 1.00 31.01 ? 105  ASP C OD1 1 
ATOM   5806  O  OD2 . ASP C  1 102 ? 30.292  -25.955 -12.691 1.00 29.08 ? 105  ASP C OD2 1 
ATOM   5807  N  N   . PRO C  1 103 ? 25.489  -27.904 -11.966 1.00 26.03 ? 106  PRO C N   1 
ATOM   5808  C  CA  . PRO C  1 103 ? 24.095  -27.470 -12.002 1.00 25.38 ? 106  PRO C CA  1 
ATOM   5809  C  C   . PRO C  1 103 ? 24.031  -26.150 -12.755 1.00 27.39 ? 106  PRO C C   1 
ATOM   5810  O  O   . PRO C  1 103 ? 25.062  -25.534 -12.975 1.00 28.05 ? 106  PRO C O   1 
ATOM   5811  C  CB  . PRO C  1 103 ? 23.786  -27.236 -10.514 1.00 23.95 ? 106  PRO C CB  1 
ATOM   5812  C  CG  . PRO C  1 103 ? 25.102  -26.751 -9.963  1.00 24.05 ? 106  PRO C CG  1 
ATOM   5813  C  CD  . PRO C  1 103 ? 26.124  -27.627 -10.658 1.00 24.95 ? 106  PRO C CD  1 
ATOM   5814  N  N   . PRO C  1 104 ? 22.824  -25.669 -13.069 1.00 27.82 ? 107  PRO C N   1 
ATOM   5815  C  CA  . PRO C  1 104 ? 22.667  -24.333 -13.648 1.00 27.35 ? 107  PRO C CA  1 
ATOM   5816  C  C   . PRO C  1 104 ? 23.111  -23.224 -12.692 1.00 28.66 ? 107  PRO C C   1 
ATOM   5817  O  O   . PRO C  1 104 ? 23.039  -23.387 -11.471 1.00 28.33 ? 107  PRO C O   1 
ATOM   5818  C  CB  . PRO C  1 104 ? 21.156  -24.226 -13.885 1.00 27.19 ? 107  PRO C CB  1 
ATOM   5819  C  CG  . PRO C  1 104 ? 20.686  -25.633 -13.972 1.00 29.38 ? 107  PRO C CG  1 
ATOM   5820  C  CD  . PRO C  1 104 ? 21.552  -26.408 -13.018 1.00 29.25 ? 107  PRO C CD  1 
ATOM   5821  N  N   . PRO C  1 105 ? 23.508  -22.074 -13.247 1.00 29.90 ? 108  PRO C N   1 
ATOM   5822  C  CA  . PRO C  1 105 ? 23.625  -20.843 -12.459 1.00 31.23 ? 108  PRO C CA  1 
ATOM   5823  C  C   . PRO C  1 105 ? 22.311  -20.526 -11.720 1.00 30.76 ? 108  PRO C C   1 
ATOM   5824  O  O   . PRO C  1 105 ? 21.240  -20.945 -12.158 1.00 29.65 ? 108  PRO C O   1 
ATOM   5825  C  CB  . PRO C  1 105 ? 23.934  -19.765 -13.513 1.00 31.46 ? 108  PRO C CB  1 
ATOM   5826  C  CG  . PRO C  1 105 ? 24.454  -20.518 -14.711 1.00 32.88 ? 108  PRO C CG  1 
ATOM   5827  C  CD  . PRO C  1 105 ? 23.771  -21.861 -14.685 1.00 31.65 ? 108  PRO C CD  1 
ATOM   5828  N  N   . PRO C  1 106 ? 22.398  -19.804 -10.590 1.00 28.74 ? 109  PRO C N   1 
ATOM   5829  C  CA  . PRO C  1 106 ? 23.623  -19.186 -10.092 1.00 28.11 ? 109  PRO C CA  1 
ATOM   5830  C  C   . PRO C  1 106 ? 24.467  -20.072 -9.166  1.00 27.34 ? 109  PRO C C   1 
ATOM   5831  O  O   . PRO C  1 106 ? 25.473  -19.616 -8.646  1.00 26.53 ? 109  PRO C O   1 
ATOM   5832  C  CB  . PRO C  1 106 ? 23.115  -17.961 -9.310  1.00 29.92 ? 109  PRO C CB  1 
ATOM   5833  C  CG  . PRO C  1 106 ? 21.651  -17.895 -9.523  1.00 31.45 ? 109  PRO C CG  1 
ATOM   5834  C  CD  . PRO C  1 106 ? 21.208  -19.270 -9.921  1.00 28.23 ? 109  PRO C CD  1 
ATOM   5835  N  N   . ALA C  1 107 ? 24.019  -21.291 -8.896  1.00 30.22 ? 110  ALA C N   1 
ATOM   5836  C  CA  . ALA C  1 107 ? 24.843  -22.251 -8.159  1.00 31.22 ? 110  ALA C CA  1 
ATOM   5837  C  C   . ALA C  1 107 ? 26.171  -22.335 -8.887  1.00 32.23 ? 110  ALA C C   1 
ATOM   5838  O  O   . ALA C  1 107 ? 26.199  -22.280 -10.115 1.00 30.14 ? 110  ALA C O   1 
ATOM   5839  C  CB  . ALA C  1 107 ? 24.177  -23.600 -8.138  1.00 27.08 ? 110  ALA C CB  1 
ATOM   5840  N  N   . SER C  1 108 ? 27.277  -22.362 -8.152  1.00 32.13 ? 111  SER C N   1 
ATOM   5841  C  CA  . SER C  1 108 ? 28.569  -22.347 -8.829  1.00 32.89 ? 111  SER C CA  1 
ATOM   5842  C  C   . SER C  1 108 ? 29.531  -23.460 -8.424  1.00 30.44 ? 111  SER C C   1 
ATOM   5843  O  O   . SER C  1 108 ? 30.578  -23.636 -9.045  1.00 31.84 ? 111  SER C O   1 
ATOM   5844  C  CB  . SER C  1 108 ? 29.229  -20.979 -8.720  1.00 34.74 ? 111  SER C CB  1 
ATOM   5845  O  OG  . SER C  1 108 ? 29.237  -20.544 -7.380  1.00 39.32 ? 111  SER C OG  1 
ATOM   5846  N  N   . VAL C  1 109 ? 29.149  -24.258 -7.433  1.00 26.72 ? 112  VAL C N   1 
ATOM   5847  C  CA  . VAL C  1 109 ? 29.988  -25.381 -7.018  1.00 21.20 ? 112  VAL C CA  1 
ATOM   5848  C  C   . VAL C  1 109 ? 31.468  -24.995 -7.019  1.00 21.63 ? 112  VAL C C   1 
ATOM   5849  O  O   . VAL C  1 109 ? 32.308  -25.702 -7.574  1.00 21.99 ? 112  VAL C O   1 
ATOM   5850  C  CB  . VAL C  1 109 ? 29.721  -26.608 -7.906  1.00 21.29 ? 112  VAL C CB  1 
ATOM   5851  C  CG1 . VAL C  1 109 ? 30.400  -27.834 -7.347  1.00 16.14 ? 112  VAL C CG1 1 
ATOM   5852  C  CG2 . VAL C  1 109 ? 28.214  -26.838 -7.980  1.00 18.64 ? 112  VAL C CG2 1 
ATOM   5853  N  N   . GLY C  1 110 ? 31.772  -23.864 -6.376  1.00 19.14 ? 113  GLY C N   1 
ATOM   5854  C  CA  . GLY C  1 110 ? 33.119  -23.303 -6.354  1.00 21.64 ? 113  GLY C CA  1 
ATOM   5855  C  C   . GLY C  1 110 ? 34.041  -23.896 -5.303  1.00 21.00 ? 113  GLY C C   1 
ATOM   5856  O  O   . GLY C  1 110 ? 35.143  -23.395 -5.081  1.00 21.81 ? 113  GLY C O   1 
ATOM   5857  N  N   . GLY C  1 111 ? 33.592  -24.935 -4.612  1.00 19.92 ? 114  GLY C N   1 
ATOM   5858  C  CA  . GLY C  1 111 ? 34.394  -25.481 -3.505  1.00 19.70 ? 114  GLY C CA  1 
ATOM   5859  C  C   . GLY C  1 111 ? 34.593  -24.483 -2.363  1.00 18.19 ? 114  GLY C C   1 
ATOM   5860  O  O   . GLY C  1 111 ? 34.063  -23.378 -2.396  1.00 13.82 ? 114  GLY C O   1 
ATOM   5861  N  N   . LEU C  1 112 ? 35.412  -24.844 -1.377  1.00 18.73 ? 115  LEU C N   1 
ATOM   5862  C  CA  . LEU C  1 112 ? 35.488  -24.057 -0.159  1.00 19.80 ? 115  LEU C CA  1 
ATOM   5863  C  C   . LEU C  1 112 ? 36.110  -22.685 -0.367  1.00 20.19 ? 115  LEU C C   1 
ATOM   5864  O  O   . LEU C  1 112 ? 35.856  -21.795 0.439   1.00 23.04 ? 115  LEU C O   1 
ATOM   5865  C  CB  . LEU C  1 112 ? 36.171  -24.820 0.987   1.00 19.44 ? 115  LEU C CB  1 
ATOM   5866  C  CG  . LEU C  1 112 ? 35.390  -26.007 1.559   1.00 19.62 ? 115  LEU C CG  1 
ATOM   5867  C  CD1 . LEU C  1 112 ? 36.099  -26.591 2.791   1.00 21.35 ? 115  LEU C CD1 1 
ATOM   5868  C  CD2 . LEU C  1 112 ? 33.993  -25.546 1.919   1.00 17.81 ? 115  LEU C CD2 1 
ATOM   5869  N  N   . ASN C  1 113 ? 36.840  -22.485 -1.475  1.00 17.36 ? 116  ASN C N   1 
ATOM   5870  C  CA  . ASN C  1 113 ? 37.398  -21.165 -1.812  1.00 18.97 ? 116  ASN C CA  1 
ATOM   5871  C  C   . ASN C  1 113 ? 36.355  -20.127 -2.244  1.00 21.27 ? 116  ASN C C   1 
ATOM   5872  O  O   . ASN C  1 113 ? 36.664  -18.938 -2.308  1.00 20.80 ? 116  ASN C O   1 
ATOM   5873  C  CB  . ASN C  1 113 ? 38.465  -21.251 -2.920  1.00 23.43 ? 116  ASN C CB  1 
ATOM   5874  C  CG  . ASN C  1 113 ? 39.781  -21.870 -2.450  1.00 25.30 ? 116  ASN C CG  1 
ATOM   5875  O  OD1 . ASN C  1 113 ? 39.863  -22.464 -1.380  1.00 27.32 ? 116  ASN C OD1 1 
ATOM   5876  N  ND2 . ASN C  1 113 ? 40.795  -21.789 -3.296  1.00 26.16 ? 116  ASN C ND2 1 
ATOM   5877  N  N   . GLU C  1 114 ? 35.204  -20.578 -2.732  1.00 19.52 ? 117  GLU C N   1 
ATOM   5878  C  CA  . GLU C  1 114 ? 34.165  -19.634 -3.131  1.00 20.85 ? 117  GLU C CA  1 
ATOM   5879  C  C   . GLU C  1 114 ? 33.919  -18.595 -2.029  1.00 22.84 ? 117  GLU C C   1 
ATOM   5880  O  O   . GLU C  1 114 ? 33.488  -18.930 -0.906  1.00 21.10 ? 117  GLU C O   1 
ATOM   5881  C  CB  . GLU C  1 114 ? 32.860  -20.367 -3.448  1.00 24.31 ? 117  GLU C CB  1 
ATOM   5882  C  CG  . GLU C  1 114 ? 31.799  -19.484 -4.077  1.00 26.87 ? 117  GLU C CG  1 
ATOM   5883  C  CD  . GLU C  1 114 ? 32.122  -19.157 -5.523  1.00 33.84 ? 117  GLU C CD  1 
ATOM   5884  O  OE1 . GLU C  1 114 ? 32.766  -20.003 -6.199  1.00 33.15 ? 117  GLU C OE1 1 
ATOM   5885  O  OE2 . GLU C  1 114 ? 31.772  -18.034 -5.968  1.00 35.34 ? 117  GLU C OE2 1 
ATOM   5886  N  N   . HIS C  1 115 ? 34.190  -17.338 -2.360  1.00 18.18 ? 118  HIS C N   1 
ATOM   5887  C  CA  . HIS C  1 115 ? 34.039  -16.236 -1.426  1.00 18.48 ? 118  HIS C CA  1 
ATOM   5888  C  C   . HIS C  1 115 ? 32.576  -15.897 -1.216  1.00 19.85 ? 118  HIS C C   1 
ATOM   5889  O  O   . HIS C  1 115 ? 31.822  -15.793 -2.184  1.00 22.09 ? 118  HIS C O   1 
ATOM   5890  C  CB  . HIS C  1 115 ? 34.727  -14.992 -1.982  1.00 18.76 ? 118  HIS C CB  1 
ATOM   5891  C  CG  . HIS C  1 115 ? 34.488  -13.767 -1.161  1.00 21.98 ? 118  HIS C CG  1 
ATOM   5892  N  ND1 . HIS C  1 115 ? 34.926  -13.653 0.141   1.00 18.98 ? 118  HIS C ND1 1 
ATOM   5893  C  CD2 . HIS C  1 115 ? 33.825  -12.620 -1.440  1.00 21.38 ? 118  HIS C CD2 1 
ATOM   5894  C  CE1 . HIS C  1 115 ? 34.536  -12.491 0.630   1.00 21.09 ? 118  HIS C CE1 1 
ATOM   5895  N  NE2 . HIS C  1 115 ? 33.856  -11.851 -0.304  1.00 22.99 ? 118  HIS C NE2 1 
ATOM   5896  N  N   . GLY C  1 116 ? 32.175  -15.691 0.039   1.00 20.04 ? 119  GLY C N   1 
ATOM   5897  C  CA  . GLY C  1 116 ? 30.878  -15.088 0.321   1.00 17.88 ? 119  GLY C CA  1 
ATOM   5898  C  C   . GLY C  1 116 ? 29.810  -16.135 0.548   1.00 19.68 ? 119  GLY C C   1 
ATOM   5899  O  O   . GLY C  1 116 ? 28.700  -15.813 0.954   1.00 20.92 ? 119  GLY C O   1 
ATOM   5900  N  N   . THR C  1 117 ? 30.175  -17.401 0.387   1.00 18.33 ? 120  THR C N   1 
ATOM   5901  C  CA  . THR C  1 117 ? 29.261  -18.477 0.720   1.00 20.56 ? 120  THR C CA  1 
ATOM   5902  C  C   . THR C  1 117 ? 29.557  -19.056 2.111   1.00 23.20 ? 120  THR C C   1 
ATOM   5903  O  O   . THR C  1 117 ? 28.805  -18.798 3.065   1.00 23.51 ? 120  THR C O   1 
ATOM   5904  C  CB  . THR C  1 117 ? 29.225  -19.595 -0.380  1.00 20.20 ? 120  THR C CB  1 
ATOM   5905  O  OG1 . THR C  1 117 ? 30.530  -20.135 -0.564  1.00 19.00 ? 120  THR C OG1 1 
ATOM   5906  C  CG2 . THR C  1 117 ? 28.762  -19.027 -1.712  1.00 17.24 ? 120  THR C CG2 1 
ATOM   5907  N  N   . PHE C  1 118 ? 30.625  -19.850 2.229   1.00 20.12 ? 121  PHE C N   1 
ATOM   5908  C  CA  . PHE C  1 118 ? 31.190  -20.201 3.539   1.00 20.29 ? 121  PHE C CA  1 
ATOM   5909  C  C   . PHE C  1 118 ? 32.368  -19.267 3.874   1.00 23.07 ? 121  PHE C C   1 
ATOM   5910  O  O   . PHE C  1 118 ? 32.276  -18.460 4.806   1.00 24.13 ? 121  PHE C O   1 
ATOM   5911  C  CB  . PHE C  1 118 ? 31.616  -21.680 3.565   1.00 17.00 ? 121  PHE C CB  1 
ATOM   5912  C  CG  . PHE C  1 118 ? 31.590  -22.318 4.951   1.00 15.23 ? 121  PHE C CG  1 
ATOM   5913  C  CD1 . PHE C  1 118 ? 32.405  -21.839 5.975   1.00 14.27 ? 121  PHE C CD1 1 
ATOM   5914  C  CD2 . PHE C  1 118 ? 30.791  -23.426 5.203   1.00 14.65 ? 121  PHE C CD2 1 
ATOM   5915  C  CE1 . PHE C  1 118 ? 32.432  -22.436 7.217   1.00 12.47 ? 121  PHE C CE1 1 
ATOM   5916  C  CE2 . PHE C  1 118 ? 30.817  -24.064 6.442   1.00 14.21 ? 121  PHE C CE2 1 
ATOM   5917  C  CZ  . PHE C  1 118 ? 31.660  -23.578 7.459   1.00 14.63 ? 121  PHE C CZ  1 
ATOM   5918  N  N   . GLU C  1 119 ? 33.429  -19.310 3.056   1.00 21.85 ? 122  GLU C N   1 
ATOM   5919  C  CA  . GLU C  1 119 ? 34.588  -18.416 3.222   1.00 19.04 ? 122  GLU C CA  1 
ATOM   5920  C  C   . GLU C  1 119 ? 34.179  -16.955 3.249   1.00 17.86 ? 122  GLU C C   1 
ATOM   5921  O  O   . GLU C  1 119 ? 33.321  -16.526 2.467   1.00 21.93 ? 122  GLU C O   1 
ATOM   5922  C  CB  . GLU C  1 119 ? 35.616  -18.624 2.102   1.00 17.71 ? 122  GLU C CB  1 
ATOM   5923  C  CG  . GLU C  1 119 ? 36.988  -17.943 2.332   1.00 17.84 ? 122  GLU C CG  1 
ATOM   5924  C  CD  . GLU C  1 119 ? 36.978  -16.413 2.163   1.00 25.59 ? 122  GLU C CD  1 
ATOM   5925  O  OE1 . GLU C  1 119 ? 36.320  -15.902 1.202   1.00 25.08 ? 122  GLU C OE1 1 
ATOM   5926  O  OE2 . GLU C  1 119 ? 37.663  -15.734 2.984   1.00 23.04 ? 122  GLU C OE2 1 
ATOM   5927  N  N   . GLY C  1 120 ? 34.892  -16.164 4.047   1.00 16.53 ? 123  GLY C N   1 
ATOM   5928  C  CA  . GLY C  1 120 ? 34.493  -14.788 4.329   1.00 17.26 ? 123  GLY C CA  1 
ATOM   5929  C  C   . GLY C  1 120 ? 35.640  -13.971 4.881   1.00 17.49 ? 123  GLY C C   1 
ATOM   5930  O  O   . GLY C  1 120 ? 36.705  -14.497 5.151   1.00 19.00 ? 123  GLY C O   1 
ATOM   5931  N  N   . ASP C  1 121 ? 35.388  -12.695 5.131   1.00 18.25 ? 124  ASP C N   1 
ATOM   5932  C  CA  . ASP C  1 121 ? 36.429  -11.757 5.501   1.00 19.86 ? 124  ASP C CA  1 
ATOM   5933  C  C   . ASP C  1 121 ? 36.917  -11.919 6.947   1.00 22.01 ? 124  ASP C C   1 
ATOM   5934  O  O   . ASP C  1 121 ? 36.304  -12.626 7.753   1.00 21.09 ? 124  ASP C O   1 
ATOM   5935  C  CB  . ASP C  1 121 ? 35.928  -10.331 5.248   1.00 18.45 ? 124  ASP C CB  1 
ATOM   5936  C  CG  . ASP C  1 121 ? 35.563  -10.100 3.794   1.00 19.76 ? 124  ASP C CG  1 
ATOM   5937  O  OD1 . ASP C  1 121 ? 36.107  -10.837 2.919   1.00 21.91 ? 124  ASP C OD1 1 
ATOM   5938  O  OD2 . ASP C  1 121 ? 34.720  -9.216  3.518   1.00 15.64 ? 124  ASP C OD2 1 
ATOM   5939  N  N   . ALA C  1 122 ? 38.046  -11.282 7.258   1.00 21.15 ? 125  ALA C N   1 
ATOM   5940  C  CA  . ALA C  1 122 ? 38.569  -11.262 8.621   1.00 21.89 ? 125  ALA C CA  1 
ATOM   5941  C  C   . ALA C  1 122 ? 38.998  -12.643 9.119   1.00 21.89 ? 125  ALA C C   1 
ATOM   5942  O  O   . ALA C  1 122 ? 38.992  -12.911 10.327  1.00 18.23 ? 125  ALA C O   1 
ATOM   5943  C  CB  . ALA C  1 122 ? 37.556  -10.618 9.594   1.00 22.62 ? 125  ALA C CB  1 
ATOM   5944  N  N   . SER C  1 123 ? 39.427  -13.500 8.193   1.00 21.54 ? 126  SER C N   1 
ATOM   5945  C  CA  . SER C  1 123 ? 40.131  -14.723 8.582   1.00 21.18 ? 126  SER C CA  1 
ATOM   5946  C  C   . SER C  1 123 ? 41.428  -14.380 9.336   1.00 21.55 ? 126  SER C C   1 
ATOM   5947  O  O   . SER C  1 123 ? 41.974  -13.278 9.172   1.00 21.85 ? 126  SER C O   1 
ATOM   5948  C  CB  . SER C  1 123 ? 40.401  -15.600 7.357   1.00 20.16 ? 126  SER C CB  1 
ATOM   5949  O  OG  . SER C  1 123 ? 39.179  -15.940 6.700   1.00 20.30 ? 126  SER C OG  1 
ATOM   5950  N  N   . MET C  1 124 ? 41.833  -15.266 10.247  1.00 20.78 ? 127  MET C N   1 
ATOM   5951  C  CA  . MET C  1 124 ? 42.980  -15.030 11.138  1.00 24.28 ? 127  MET C CA  1 
ATOM   5952  C  C   . MET C  1 124 ? 44.287  -15.100 10.355  1.00 25.56 ? 127  MET C C   1 
ATOM   5953  O  O   . MET C  1 124 ? 45.165  -14.238 10.506  1.00 26.54 ? 127  MET C O   1 
ATOM   5954  C  CB  . MET C  1 124 ? 43.025  -16.081 12.249  1.00 25.14 ? 127  MET C CB  1 
ATOM   5955  C  CG  . MET C  1 124 ? 42.005  -15.888 13.369  1.00 24.37 ? 127  MET C CG  1 
ATOM   5956  S  SD  . MET C  1 124 ? 42.111  -17.208 14.592  1.00 26.74 ? 127  MET C SD  1 
ATOM   5957  C  CE  . MET C  1 124 ? 41.414  -18.610 13.688  1.00 21.13 ? 127  MET C CE  1 
ATOM   5958  N  N   . THR C  1 125 ? 44.403  -16.125 9.516   1.00 24.22 ? 128  THR C N   1 
ATOM   5959  C  CA  . THR C  1 125 ? 45.643  -16.389 8.787   1.00 23.61 ? 128  THR C CA  1 
ATOM   5960  C  C   . THR C  1 125 ? 45.517  -16.330 7.259   1.00 23.50 ? 128  THR C C   1 
ATOM   5961  O  O   . THR C  1 125 ? 46.462  -16.656 6.536   1.00 22.63 ? 128  THR C O   1 
ATOM   5962  C  CB  . THR C  1 125 ? 46.242  -17.720 9.210   1.00 21.79 ? 128  THR C CB  1 
ATOM   5963  O  OG1 . THR C  1 125 ? 45.421  -18.798 8.737   1.00 23.38 ? 128  THR C OG1 1 
ATOM   5964  C  CG2 . THR C  1 125 ? 46.337  -17.795 10.726  1.00 19.83 ? 128  THR C CG2 1 
ATOM   5965  N  N   . ARG C  1 126 ? 44.380  -15.833 6.778   1.00 22.96 ? 129  ARG C N   1 
ATOM   5966  C  CA  . ARG C  1 126 ? 44.096  -15.734 5.338   1.00 22.05 ? 129  ARG C CA  1 
ATOM   5967  C  C   . ARG C  1 126 ? 43.668  -14.323 5.016   1.00 23.21 ? 129  ARG C C   1 
ATOM   5968  O  O   . ARG C  1 126 ? 42.982  -13.682 5.818   1.00 23.28 ? 129  ARG C O   1 
ATOM   5969  C  CB  . ARG C  1 126 ? 42.956  -16.688 4.944   1.00 23.49 ? 129  ARG C CB  1 
ATOM   5970  C  CG  . ARG C  1 126 ? 43.420  -17.995 4.323   1.00 22.79 ? 129  ARG C CG  1 
ATOM   5971  C  CD  . ARG C  1 126 ? 44.163  -18.871 5.329   1.00 22.81 ? 129  ARG C CD  1 
ATOM   5972  N  NE  . ARG C  1 126 ? 44.702  -20.081 4.688   1.00 26.15 ? 129  ARG C NE  1 
ATOM   5973  C  CZ  . ARG C  1 126 ? 45.488  -20.971 5.290   1.00 26.60 ? 129  ARG C CZ  1 
ATOM   5974  N  NH1 . ARG C  1 126 ? 45.811  -20.835 6.573   1.00 27.40 ? 129  ARG C NH1 1 
ATOM   5975  N  NH2 . ARG C  1 126 ? 45.953  -22.002 4.608   1.00 29.19 ? 129  ARG C NH2 1 
ATOM   5976  N  N   . GLY C  1 127 ? 44.037  -13.841 3.830   1.00 23.20 ? 130  GLY C N   1 
ATOM   5977  C  CA  . GLY C  1 127 ? 43.606  -12.517 3.405   1.00 19.76 ? 130  GLY C CA  1 
ATOM   5978  C  C   . GLY C  1 127 ? 42.173  -12.497 2.899   1.00 23.04 ? 130  GLY C C   1 
ATOM   5979  O  O   . GLY C  1 127 ? 41.629  -13.535 2.476   1.00 18.04 ? 130  GLY C O   1 
ATOM   5980  N  N   . ASP C  1 128 ? 41.549  -11.321 2.976   1.00 22.17 ? 131  ASP C N   1 
ATOM   5981  C  CA  . ASP C  1 128 ? 40.225  -11.113 2.420   1.00 23.36 ? 131  ASP C CA  1 
ATOM   5982  C  C   . ASP C  1 128 ? 40.262  -11.307 0.913   1.00 25.43 ? 131  ASP C C   1 
ATOM   5983  O  O   . ASP C  1 128 ? 41.203  -10.849 0.250   1.00 24.73 ? 131  ASP C O   1 
ATOM   5984  C  CB  . ASP C  1 128 ? 39.739  -9.701  2.736   1.00 23.74 ? 131  ASP C CB  1 
ATOM   5985  C  CG  . ASP C  1 128 ? 39.355  -9.527  4.187   1.00 25.63 ? 131  ASP C CG  1 
ATOM   5986  O  OD1 . ASP C  1 128 ? 39.486  -10.495 4.967   1.00 22.79 ? 131  ASP C OD1 1 
ATOM   5987  O  OD2 . ASP C  1 128 ? 38.934  -8.406  4.549   1.00 25.85 ? 131  ASP C OD2 1 
ATOM   5988  N  N   . ALA C  1 129 ? 39.189  -11.877 0.360   1.00 26.89 ? 132  ALA C N   1 
ATOM   5989  C  CA  . ALA C  1 129 ? 39.090  -12.085 -1.099  1.00 25.49 ? 132  ALA C CA  1 
ATOM   5990  C  C   . ALA C  1 129 ? 39.345  -10.810 -1.891  1.00 25.36 ? 132  ALA C C   1 
ATOM   5991  O  O   . ALA C  1 129 ? 39.887  -10.857 -2.994  1.00 26.64 ? 132  ALA C O   1 
ATOM   5992  C  CB  . ALA C  1 129 ? 37.732  -12.663 -1.473  1.00 23.67 ? 132  ALA C CB  1 
ATOM   5993  N  N   . PHE C  1 130 ? 38.904  -9.676  -1.355  1.00 24.98 ? 133  PHE C N   1 
ATOM   5994  C  CA  . PHE C  1 130 ? 39.030  -8.414  -2.069  1.00 29.12 ? 133  PHE C CA  1 
ATOM   5995  C  C   . PHE C  1 130 ? 40.481  -8.120  -2.474  1.00 32.23 ? 133  PHE C C   1 
ATOM   5996  O  O   . PHE C  1 130 ? 40.713  -7.362  -3.412  1.00 33.02 ? 133  PHE C O   1 
ATOM   5997  C  CB  . PHE C  1 130 ? 38.484  -7.243  -1.240  1.00 27.79 ? 133  PHE C CB  1 
ATOM   5998  C  CG  . PHE C  1 130 ? 38.679  -5.905  -1.899  1.00 28.92 ? 133  PHE C CG  1 
ATOM   5999  C  CD1 . PHE C  1 130 ? 39.860  -5.196  -1.721  1.00 31.03 ? 133  PHE C CD1 1 
ATOM   6000  C  CD2 . PHE C  1 130 ? 37.728  -5.409  -2.785  1.00 30.45 ? 133  PHE C CD2 1 
ATOM   6001  C  CE1 . PHE C  1 130 ? 40.090  -3.992  -2.384  1.00 31.29 ? 133  PHE C CE1 1 
ATOM   6002  C  CE2 . PHE C  1 130 ? 37.922  -4.186  -3.435  1.00 32.97 ? 133  PHE C CE2 1 
ATOM   6003  C  CZ  . PHE C  1 130 ? 39.111  -3.476  -3.234  1.00 33.46 ? 133  PHE C CZ  1 
ATOM   6004  N  N   . PHE C  1 131 ? 41.443  -8.656  -1.720  1.00 33.39 ? 134  PHE C N   1 
ATOM   6005  C  CA  . PHE C  1 131 ? 42.860  -8.366  -1.948  1.00 35.09 ? 134  PHE C CA  1 
ATOM   6006  C  C   . PHE C  1 131 ? 43.505  -9.350  -2.916  1.00 36.49 ? 134  PHE C C   1 
ATOM   6007  O  O   . PHE C  1 131 ? 44.609  -9.107  -3.390  1.00 37.60 ? 134  PHE C O   1 
ATOM   6008  C  CB  . PHE C  1 131 ? 43.665  -8.340  -0.640  1.00 34.15 ? 134  PHE C CB  1 
ATOM   6009  C  CG  . PHE C  1 131 ? 43.206  -7.298  0.337   1.00 32.97 ? 134  PHE C CG  1 
ATOM   6010  C  CD1 . PHE C  1 131 ? 43.169  -5.962  -0.021  1.00 33.32 ? 134  PHE C CD1 1 
ATOM   6011  C  CD2 . PHE C  1 131 ? 42.786  -7.659  1.604   1.00 31.15 ? 134  PHE C CD2 1 
ATOM   6012  C  CE1 . PHE C  1 131 ? 42.694  -5.000  0.858   1.00 33.09 ? 134  PHE C CE1 1 
ATOM   6013  C  CE2 . PHE C  1 131 ? 42.301  -6.704  2.493   1.00 33.17 ? 134  PHE C CE2 1 
ATOM   6014  C  CZ  . PHE C  1 131 ? 42.270  -5.368  2.124   1.00 33.17 ? 134  PHE C CZ  1 
ATOM   6015  N  N   . GLY C  1 132 ? 42.845  -10.468 -3.198  1.00 35.16 ? 135  GLY C N   1 
ATOM   6016  C  CA  . GLY C  1 132 ? 43.305  -11.301 -4.295  1.00 33.97 ? 135  GLY C CA  1 
ATOM   6017  C  C   . GLY C  1 132 ? 43.398  -12.782 -4.001  1.00 36.01 ? 135  GLY C C   1 
ATOM   6018  O  O   . GLY C  1 132 ? 43.151  -13.610 -4.877  1.00 40.88 ? 135  GLY C O   1 
ATOM   6019  N  N   . ASN C  1 133 ? 43.814  -13.142 -2.798  1.00 33.62 ? 136  ASN C N   1 
ATOM   6020  C  CA  . ASN C  1 133 ? 43.945  -14.561 -2.478  1.00 31.75 ? 136  ASN C CA  1 
ATOM   6021  C  C   . ASN C  1 133 ? 43.401  -14.887 -1.093  1.00 29.27 ? 136  ASN C C   1 
ATOM   6022  O  O   . ASN C  1 133 ? 43.879  -14.366 -0.073  1.00 25.13 ? 136  ASN C O   1 
ATOM   6023  C  CB  . ASN C  1 133 ? 45.396  -15.043 -2.634  1.00 31.58 ? 136  ASN C CB  1 
ATOM   6024  C  CG  . ASN C  1 133 ? 45.564  -16.516 -2.286  1.00 31.21 ? 136  ASN C CG  1 
ATOM   6025  O  OD1 . ASN C  1 133 ? 44.991  -16.998 -1.321  1.00 31.90 ? 136  ASN C OD1 1 
ATOM   6026  N  ND2 . ASN C  1 133 ? 46.377  -17.225 -3.057  1.00 31.52 ? 136  ASN C ND2 1 
ATOM   6027  N  N   . ASN C  1 134 ? 42.397  -15.752 -1.065  1.00 26.40 ? 137  ASN C N   1 
ATOM   6028  C  CA  . ASN C  1 134 ? 41.539  -15.867 0.105   1.00 25.19 ? 137  ASN C CA  1 
ATOM   6029  C  C   . ASN C  1 134 ? 41.762  -17.177 0.800   1.00 23.58 ? 137  ASN C C   1 
ATOM   6030  O  O   . ASN C  1 134 ? 41.002  -17.537 1.698   1.00 20.62 ? 137  ASN C O   1 
ATOM   6031  C  CB  . ASN C  1 134 ? 40.058  -15.746 -0.283  1.00 25.63 ? 137  ASN C CB  1 
ATOM   6032  C  CG  . ASN C  1 134 ? 39.526  -17.000 -0.962  1.00 26.21 ? 137  ASN C CG  1 
ATOM   6033  O  OD1 . ASN C  1 134 ? 40.294  -17.882 -1.359  1.00 23.91 ? 137  ASN C OD1 1 
ATOM   6034  N  ND2 . ASN C  1 134 ? 38.197  -17.092 -1.085  1.00 27.47 ? 137  ASN C ND2 1 
ATOM   6035  N  N   . HIS C  1 135 ? 42.721  -17.959 0.308   1.00 21.80 ? 138  HIS C N   1 
ATOM   6036  C  CA  . HIS C  1 135 ? 42.872  -19.309 0.830   1.00 21.82 ? 138  HIS C CA  1 
ATOM   6037  C  C   . HIS C  1 135 ? 44.276  -19.694 1.253   1.00 22.38 ? 138  HIS C C   1 
ATOM   6038  O  O   . HIS C  1 135 ? 44.440  -20.565 2.084   1.00 24.74 ? 138  HIS C O   1 
ATOM   6039  C  CB  . HIS C  1 135 ? 42.304  -20.339 -0.140  1.00 25.08 ? 138  HIS C CB  1 
ATOM   6040  C  CG  . HIS C  1 135 ? 42.891  -20.255 -1.511  1.00 25.58 ? 138  HIS C CG  1 
ATOM   6041  N  ND1 . HIS C  1 135 ? 42.515  -19.291 -2.422  1.00 25.74 ? 138  HIS C ND1 1 
ATOM   6042  C  CD2 . HIS C  1 135 ? 43.883  -20.964 -2.100  1.00 27.03 ? 138  HIS C CD2 1 
ATOM   6043  C  CE1 . HIS C  1 135 ? 43.196  -19.457 -3.541  1.00 27.13 ? 138  HIS C CE1 1 
ATOM   6044  N  NE2 . HIS C  1 135 ? 44.023  -20.476 -3.377  1.00 28.57 ? 138  HIS C NE2 1 
ATOM   6045  N  N   . ASP C  1 136 ? 45.295  -19.048 0.703   1.00 28.00 ? 139  ASP C N   1 
ATOM   6046  C  CA  . ASP C  1 136 ? 46.664  -19.392 1.079   1.00 29.83 ? 139  ASP C CA  1 
ATOM   6047  C  C   . ASP C  1 136 ? 47.069  -18.818 2.433   1.00 28.04 ? 139  ASP C C   1 
ATOM   6048  O  O   . ASP C  1 136 ? 46.687  -17.695 2.780   1.00 30.53 ? 139  ASP C O   1 
ATOM   6049  C  CB  . ASP C  1 136 ? 47.650  -18.959 -0.001  1.00 32.66 ? 139  ASP C CB  1 
ATOM   6050  C  CG  . ASP C  1 136 ? 47.560  -19.821 -1.248  1.00 36.82 ? 139  ASP C CG  1 
ATOM   6051  O  OD1 . ASP C  1 136 ? 47.421  -21.062 -1.124  1.00 35.30 ? 139  ASP C OD1 1 
ATOM   6052  O  OD2 . ASP C  1 136 ? 47.583  -19.244 -2.357  1.00 39.71 ? 139  ASP C OD2 1 
ATOM   6053  N  N   . PHE C  1 137 ? 47.880  -19.574 3.166   1.00 27.06 ? 140  PHE C N   1 
ATOM   6054  C  CA  . PHE C  1 137 ? 48.528  -19.084 4.383   1.00 26.42 ? 140  PHE C CA  1 
ATOM   6055  C  C   . PHE C  1 137 ? 49.258  -17.782 4.113   1.00 27.86 ? 140  PHE C C   1 
ATOM   6056  O  O   . PHE C  1 137 ? 49.984  -17.665 3.123   1.00 29.07 ? 140  PHE C O   1 
ATOM   6057  C  CB  . PHE C  1 137 ? 49.511  -20.125 4.931   1.00 27.15 ? 140  PHE C CB  1 
ATOM   6058  C  CG  . PHE C  1 137 ? 50.318  -19.641 6.116   1.00 26.52 ? 140  PHE C CG  1 
ATOM   6059  C  CD1 . PHE C  1 137 ? 49.847  -19.810 7.409   1.00 26.88 ? 140  PHE C CD1 1 
ATOM   6060  C  CD2 . PHE C  1 137 ? 51.583  -19.087 5.938   1.00 28.73 ? 140  PHE C CD2 1 
ATOM   6061  C  CE1 . PHE C  1 137 ? 50.589  -19.358 8.510   1.00 28.17 ? 140  PHE C CE1 1 
ATOM   6062  C  CE2 . PHE C  1 137 ? 52.338  -18.637 7.033   1.00 29.08 ? 140  PHE C CE2 1 
ATOM   6063  C  CZ  . PHE C  1 137 ? 51.826  -18.748 8.317   1.00 27.88 ? 140  PHE C CZ  1 
ATOM   6064  N  N   . ASN C  1 138 ? 49.050  -16.809 4.995   1.00 29.01 ? 141  ASN C N   1 
ATOM   6065  C  CA  . ASN C  1 138 ? 49.681  -15.508 4.912   1.00 29.41 ? 141  ASN C CA  1 
ATOM   6066  C  C   . ASN C  1 138 ? 50.579  -15.261 6.129   1.00 31.62 ? 141  ASN C C   1 
ATOM   6067  O  O   . ASN C  1 138 ? 50.116  -15.328 7.266   1.00 31.25 ? 141  ASN C O   1 
ATOM   6068  C  CB  . ASN C  1 138 ? 48.593  -14.436 4.820   1.00 31.67 ? 141  ASN C CB  1 
ATOM   6069  C  CG  . ASN C  1 138 ? 49.153  -13.027 4.747   1.00 34.35 ? 141  ASN C CG  1 
ATOM   6070  O  OD1 . ASN C  1 138 ? 49.945  -12.608 5.590   1.00 33.86 ? 141  ASN C OD1 1 
ATOM   6071  N  ND2 . ASN C  1 138 ? 48.709  -12.274 3.759   1.00 37.30 ? 141  ASN C ND2 1 
ATOM   6072  N  N   . GLU C  1 139 ? 51.870  -15.012 5.889   1.00 33.12 ? 142  GLU C N   1 
ATOM   6073  C  CA  . GLU C  1 139 ? 52.879  -14.964 6.966   1.00 29.97 ? 142  GLU C CA  1 
ATOM   6074  C  C   . GLU C  1 139 ? 52.743  -13.723 7.872   1.00 27.98 ? 142  GLU C C   1 
ATOM   6075  O  O   . GLU C  1 139 ? 52.943  -13.805 9.086   1.00 28.68 ? 142  GLU C O   1 
ATOM   6076  C  CB  . GLU C  1 139 ? 54.311  -15.061 6.388   1.00 31.77 ? 142  GLU C CB  1 
ATOM   6077  C  CG  . GLU C  1 139 ? 55.463  -14.924 7.429   1.00 31.33 ? 142  GLU C CG  1 
ATOM   6078  C  CD  . GLU C  1 139 ? 55.613  -16.149 8.352   1.00 30.60 ? 142  GLU C CD  1 
ATOM   6079  O  OE1 . GLU C  1 139 ? 55.307  -17.273 7.919   1.00 27.07 ? 142  GLU C OE1 1 
ATOM   6080  O  OE2 . GLU C  1 139 ? 56.077  -15.996 9.509   1.00 33.28 ? 142  GLU C OE2 1 
ATOM   6081  N  N   . THR C  1 140 ? 52.499  -12.565 7.270   1.00 24.67 ? 143  THR C N   1 
ATOM   6082  C  CA  . THR C  1 140 ? 52.225  -11.342 8.030   1.00 23.20 ? 143  THR C CA  1 
ATOM   6083  C  C   . THR C  1 140 ? 51.058  -11.515 9.032   1.00 25.65 ? 143  THR C C   1 
ATOM   6084  O  O   . THR C  1 140 ? 51.203  -11.211 10.228  1.00 25.15 ? 143  THR C O   1 
ATOM   6085  C  CB  . THR C  1 140 ? 51.941  -10.174 7.076   1.00 25.34 ? 143  THR C CB  1 
ATOM   6086  O  OG1 . THR C  1 140 ? 53.020  -10.067 6.148   1.00 28.82 ? 143  THR C OG1 1 
ATOM   6087  C  CG2 . THR C  1 140 ? 51.803  -8.839  7.824   1.00 24.62 ? 143  THR C CG2 1 
ATOM   6088  N  N   . LEU C  1 141 ? 49.949  -12.101 8.564   1.00 24.54 ? 144  LEU C N   1 
ATOM   6089  C  CA  . LEU C  1 141 ? 48.786  -12.341 9.419   1.00 21.93 ? 144  LEU C CA  1 
ATOM   6090  C  C   . LEU C  1 141 ? 49.133  -13.318 10.516  1.00 21.32 ? 144  LEU C C   1 
ATOM   6091  O  O   . LEU C  1 141 ? 48.786  -13.100 11.683  1.00 20.35 ? 144  LEU C O   1 
ATOM   6092  C  CB  . LEU C  1 141 ? 47.564  -12.818 8.606   1.00 20.61 ? 144  LEU C CB  1 
ATOM   6093  C  CG  . LEU C  1 141 ? 46.988  -11.778 7.645   1.00 19.95 ? 144  LEU C CG  1 
ATOM   6094  C  CD1 . LEU C  1 141 ? 45.809  -12.318 6.814   1.00 19.43 ? 144  LEU C CD1 1 
ATOM   6095  C  CD2 . LEU C  1 141 ? 46.598  -10.480 8.409   1.00 23.10 ? 144  LEU C CD2 1 
ATOM   6096  N  N   . PHE C  1 142 ? 49.862  -14.374 10.157  1.00 22.79 ? 145  PHE C N   1 
ATOM   6097  C  CA  . PHE C  1 142 ? 50.283  -15.339 11.161  1.00 22.37 ? 145  PHE C CA  1 
ATOM   6098  C  C   . PHE C  1 142 ? 51.178  -14.714 12.223  1.00 24.02 ? 145  PHE C C   1 
ATOM   6099  O  O   . PHE C  1 142 ? 51.051  -14.995 13.414  1.00 27.47 ? 145  PHE C O   1 
ATOM   6100  C  CB  . PHE C  1 142 ? 50.997  -16.525 10.537  1.00 20.95 ? 145  PHE C CB  1 
ATOM   6101  C  CG  . PHE C  1 142 ? 51.366  -17.579 11.540  1.00 21.24 ? 145  PHE C CG  1 
ATOM   6102  C  CD1 . PHE C  1 142 ? 50.396  -18.424 12.056  1.00 17.30 ? 145  PHE C CD1 1 
ATOM   6103  C  CD2 . PHE C  1 142 ? 52.668  -17.674 12.018  1.00 19.40 ? 145  PHE C CD2 1 
ATOM   6104  C  CE1 . PHE C  1 142 ? 50.704  -19.336 13.027  1.00 22.14 ? 145  PHE C CE1 1 
ATOM   6105  C  CE2 . PHE C  1 142 ? 52.996  -18.592 13.000  1.00 21.04 ? 145  PHE C CE2 1 
ATOM   6106  C  CZ  . PHE C  1 142 ? 52.008  -19.417 13.529  1.00 21.26 ? 145  PHE C CZ  1 
ATOM   6107  N  N   . GLU C  1 143 ? 52.082  -13.846 11.805  1.00 24.97 ? 146  GLU C N   1 
ATOM   6108  C  CA  . GLU C  1 143 ? 52.962  -13.223 12.784  1.00 25.98 ? 146  GLU C CA  1 
ATOM   6109  C  C   . GLU C  1 143 ? 52.196  -12.178 13.597  1.00 24.96 ? 146  GLU C C   1 
ATOM   6110  O  O   . GLU C  1 143 ? 52.596  -11.839 14.708  1.00 25.25 ? 146  GLU C O   1 
ATOM   6111  C  CB  . GLU C  1 143 ? 54.198  -12.618 12.112  1.00 25.21 ? 146  GLU C CB  1 
ATOM   6112  C  CG  . GLU C  1 143 ? 55.058  -13.639 11.382  1.00 27.09 ? 146  GLU C CG  1 
ATOM   6113  C  CD  . GLU C  1 143 ? 56.366  -13.039 10.876  1.00 31.23 ? 146  GLU C CD  1 
ATOM   6114  O  OE1 . GLU C  1 143 ? 56.673  -11.873 11.219  1.00 33.39 ? 146  GLU C OE1 1 
ATOM   6115  O  OE2 . GLU C  1 143 ? 57.060  -13.711 10.087  1.00 34.49 ? 146  GLU C OE2 1 
ATOM   6116  N  N   . GLN C  1 144 ? 51.068  -11.704 13.069  1.00 24.84 ? 147  GLN C N   1 
ATOM   6117  C  CA  . GLN C  1 144 ? 50.137  -10.963 13.907  1.00 25.45 ? 147  GLN C CA  1 
ATOM   6118  C  C   . GLN C  1 144 ? 49.481  -11.903 14.929  1.00 25.58 ? 147  GLN C C   1 
ATOM   6119  O  O   . GLN C  1 144 ? 49.413  -11.592 16.111  1.00 26.75 ? 147  GLN C O   1 
ATOM   6120  C  CB  . GLN C  1 144 ? 49.108  -10.182 13.073  1.00 25.42 ? 147  GLN C CB  1 
ATOM   6121  C  CG  . GLN C  1 144 ? 47.990  -9.552  13.891  1.00 24.53 ? 147  GLN C CG  1 
ATOM   6122  C  CD  . GLN C  1 144 ? 47.154  -8.551  13.104  1.00 26.47 ? 147  GLN C CD  1 
ATOM   6123  O  OE1 . GLN C  1 144 ? 47.276  -7.335  13.292  1.00 27.44 ? 147  GLN C OE1 1 
ATOM   6124  N  NE2 . GLN C  1 144 ? 46.262  -9.058  12.258  1.00 26.09 ? 147  GLN C NE2 1 
ATOM   6125  N  N   . LEU C  1 145 ? 49.145  -13.117 14.518  1.00 28.11 ? 148  LEU C N   1 
ATOM   6126  C  CA  . LEU C  1 145 ? 48.655  -14.089 15.495  1.00 25.32 ? 148  LEU C CA  1 
ATOM   6127  C  C   . LEU C  1 145 ? 49.663  -14.304 16.636  1.00 27.40 ? 148  LEU C C   1 
ATOM   6128  O  O   . LEU C  1 145 ? 49.281  -14.401 17.817  1.00 27.38 ? 148  LEU C O   1 
ATOM   6129  C  CB  . LEU C  1 145 ? 48.275  -15.401 14.827  1.00 21.68 ? 148  LEU C CB  1 
ATOM   6130  C  CG  . LEU C  1 145 ? 47.672  -16.493 15.720  1.00 24.96 ? 148  LEU C CG  1 
ATOM   6131  C  CD1 . LEU C  1 145 ? 46.760  -17.375 14.873  1.00 23.95 ? 148  LEU C CD1 1 
ATOM   6132  C  CD2 . LEU C  1 145 ? 48.792  -17.352 16.379  1.00 22.36 ? 148  LEU C CD2 1 
ATOM   6133  N  N   . VAL C  1 146 ? 50.953  -14.308 16.293  1.00 29.54 ? 149  VAL C N   1 
ATOM   6134  C  CA  . VAL C  1 146 ? 52.012  -14.532 17.293  1.00 27.33 ? 149  VAL C CA  1 
ATOM   6135  C  C   . VAL C  1 146 ? 52.117  -13.346 18.258  1.00 25.25 ? 149  VAL C C   1 
ATOM   6136  O  O   . VAL C  1 146 ? 51.979  -13.507 19.468  1.00 27.27 ? 149  VAL C O   1 
ATOM   6137  C  CB  . VAL C  1 146 ? 53.382  -14.857 16.622  1.00 28.86 ? 149  VAL C CB  1 
ATOM   6138  C  CG1 . VAL C  1 146 ? 54.479  -15.103 17.672  1.00 26.10 ? 149  VAL C CG1 1 
ATOM   6139  C  CG2 . VAL C  1 146 ? 53.252  -16.074 15.716  1.00 27.56 ? 149  VAL C CG2 1 
ATOM   6140  N  N   . ASP C  1 147 ? 52.243  -12.145 17.719  1.00 24.73 ? 150  ASP C N   1 
ATOM   6141  C  CA  . ASP C  1 147 ? 52.128  -10.943 18.545  1.00 27.82 ? 150  ASP C CA  1 
ATOM   6142  C  C   . ASP C  1 147 ? 50.998  -11.042 19.571  1.00 29.65 ? 150  ASP C C   1 
ATOM   6143  O  O   . ASP C  1 147 ? 51.165  -10.670 20.742  1.00 31.38 ? 150  ASP C O   1 
ATOM   6144  C  CB  . ASP C  1 147 ? 51.922  -9.703  17.679  1.00 27.93 ? 150  ASP C CB  1 
ATOM   6145  C  CG  . ASP C  1 147 ? 53.077  -9.463  16.726  1.00 31.21 ? 150  ASP C CG  1 
ATOM   6146  O  OD1 . ASP C  1 147 ? 54.102  -10.156 16.869  1.00 32.86 ? 150  ASP C OD1 1 
ATOM   6147  O  OD2 . ASP C  1 147 ? 52.966  -8.593  15.830  1.00 33.08 ? 150  ASP C OD2 1 
ATOM   6148  N  N   . TYR C  1 148 ? 49.825  -11.468 19.117  1.00 25.70 ? 151  TYR C N   1 
ATOM   6149  C  CA  . TYR C  1 148 ? 48.651  -11.371 19.949  1.00 24.00 ? 151  TYR C CA  1 
ATOM   6150  C  C   . TYR C  1 148 ? 48.693  -12.472 20.982  1.00 23.35 ? 151  TYR C C   1 
ATOM   6151  O  O   . TYR C  1 148 ? 48.233  -12.293 22.114  1.00 22.73 ? 151  TYR C O   1 
ATOM   6152  C  CB  . TYR C  1 148 ? 47.367  -11.407 19.124  1.00 19.53 ? 151  TYR C CB  1 
ATOM   6153  C  CG  . TYR C  1 148 ? 46.854  -10.027 18.814  1.00 21.31 ? 151  TYR C CG  1 
ATOM   6154  C  CD1 . TYR C  1 148 ? 47.560  -9.180  17.950  1.00 23.50 ? 151  TYR C CD1 1 
ATOM   6155  C  CD2 . TYR C  1 148 ? 45.700  -9.538  19.411  1.00 20.91 ? 151  TYR C CD2 1 
ATOM   6156  C  CE1 . TYR C  1 148 ? 47.115  -7.890  17.673  1.00 20.23 ? 151  TYR C CE1 1 
ATOM   6157  C  CE2 . TYR C  1 148 ? 45.254  -8.234  19.156  1.00 25.07 ? 151  TYR C CE2 1 
ATOM   6158  C  CZ  . TYR C  1 148 ? 45.964  -7.424  18.274  1.00 24.00 ? 151  TYR C CZ  1 
ATOM   6159  O  OH  . TYR C  1 148 ? 45.546  -6.138  18.029  1.00 24.36 ? 151  TYR C OH  1 
ATOM   6160  N  N   . SER C  1 149 ? 49.309  -13.585 20.604  1.00 24.57 ? 152  SER C N   1 
ATOM   6161  C  CA  . SER C  1 149 ? 49.614  -14.633 21.557  1.00 27.49 ? 152  SER C CA  1 
ATOM   6162  C  C   . SER C  1 149 ? 50.603  -14.160 22.639  1.00 26.68 ? 152  SER C C   1 
ATOM   6163  O  O   . SER C  1 149 ? 50.397  -14.410 23.825  1.00 30.34 ? 152  SER C O   1 
ATOM   6164  C  CB  . SER C  1 149 ? 50.116  -15.880 20.835  1.00 28.06 ? 152  SER C CB  1 
ATOM   6165  O  OG  . SER C  1 149 ? 49.067  -16.477 20.083  1.00 28.29 ? 152  SER C OG  1 
ATOM   6166  N  N   . ASN C  1 150 ? 51.618  -13.407 22.236  1.00 26.11 ? 153  ASN C N   1 
ATOM   6167  C  CA  . ASN C  1 150 ? 52.555  -12.790 23.182  1.00 27.57 ? 153  ASN C CA  1 
ATOM   6168  C  C   . ASN C  1 150 ? 51.888  -11.797 24.118  1.00 28.56 ? 153  ASN C C   1 
ATOM   6169  O  O   . ASN C  1 150 ? 52.129  -11.827 25.325  1.00 31.31 ? 153  ASN C O   1 
ATOM   6170  C  CB  . ASN C  1 150 ? 53.710  -12.094 22.443  1.00 24.21 ? 153  ASN C CB  1 
ATOM   6171  C  CG  . ASN C  1 150 ? 54.657  -13.081 21.781  1.00 26.84 ? 153  ASN C CG  1 
ATOM   6172  O  OD1 . ASN C  1 150 ? 54.728  -14.255 22.178  1.00 23.20 ? 153  ASN C OD1 1 
ATOM   6173  N  ND2 . ASN C  1 150 ? 55.330  -12.634 20.713  1.00 26.61 ? 153  ASN C ND2 1 
ATOM   6174  N  N   . ARG C  1 151 ? 51.081  -10.893 23.566  1.00 27.82 ? 154  ARG C N   1 
ATOM   6175  C  CA  . ARG C  1 151 ? 50.477  -9.849  24.386  1.00 28.86 ? 154  ARG C CA  1 
ATOM   6176  C  C   . ARG C  1 151 ? 49.422  -10.419 25.336  1.00 28.97 ? 154  ARG C C   1 
ATOM   6177  O  O   . ARG C  1 151 ? 49.288  -9.970  26.475  1.00 30.28 ? 154  ARG C O   1 
ATOM   6178  C  CB  . ARG C  1 151 ? 49.872  -8.746  23.515  1.00 31.14 ? 154  ARG C CB  1 
ATOM   6179  C  CG  . ARG C  1 151 ? 50.898  -7.881  22.796  1.00 33.97 ? 154  ARG C CG  1 
ATOM   6180  C  CD  . ARG C  1 151 ? 50.246  -7.048  21.703  1.00 36.05 ? 154  ARG C CD  1 
ATOM   6181  N  NE  . ARG C  1 151 ? 49.196  -6.196  22.256  1.00 38.94 ? 154  ARG C NE  1 
ATOM   6182  C  CZ  . ARG C  1 151 ? 48.290  -5.547  21.530  1.00 40.80 ? 154  ARG C CZ  1 
ATOM   6183  N  NH1 . ARG C  1 151 ? 48.307  -5.630  20.204  1.00 39.26 ? 154  ARG C NH1 1 
ATOM   6184  N  NH2 . ARG C  1 151 ? 47.362  -4.808  22.136  1.00 43.26 ? 154  ARG C NH2 1 
ATOM   6185  N  N   . PHE C  1 152 ? 48.703  -11.441 24.886  1.00 26.78 ? 155  PHE C N   1 
ATOM   6186  C  CA  . PHE C  1 152 ? 47.485  -11.825 25.558  1.00 22.40 ? 155  PHE C CA  1 
ATOM   6187  C  C   . PHE C  1 152 ? 47.480  -13.250 26.069  1.00 22.68 ? 155  PHE C C   1 
ATOM   6188  O  O   . PHE C  1 152 ? 46.669  -13.589 26.930  1.00 22.20 ? 155  PHE C O   1 
ATOM   6189  C  CB  . PHE C  1 152 ? 46.275  -11.570 24.662  1.00 20.86 ? 155  PHE C CB  1 
ATOM   6190  C  CG  . PHE C  1 152 ? 46.013  -10.108 24.398  1.00 20.09 ? 155  PHE C CG  1 
ATOM   6191  C  CD1 . PHE C  1 152 ? 45.625  -9.263  25.427  1.00 18.64 ? 155  PHE C CD1 1 
ATOM   6192  C  CD2 . PHE C  1 152 ? 46.145  -9.583  23.110  1.00 18.14 ? 155  PHE C CD2 1 
ATOM   6193  C  CE1 . PHE C  1 152 ? 45.355  -7.901  25.178  1.00 18.45 ? 155  PHE C CE1 1 
ATOM   6194  C  CE2 . PHE C  1 152 ? 45.934  -8.221  22.855  1.00 17.83 ? 155  PHE C CE2 1 
ATOM   6195  C  CZ  . PHE C  1 152 ? 45.488  -7.391  23.878  1.00 18.02 ? 155  PHE C CZ  1 
ATOM   6196  N  N   . GLY C  1 153 ? 48.384  -14.086 25.566  1.00 21.25 ? 156  GLY C N   1 
ATOM   6197  C  CA  . GLY C  1 153 ? 48.367  -15.504 25.938  1.00 22.74 ? 156  GLY C CA  1 
ATOM   6198  C  C   . GLY C  1 153 ? 49.632  -15.974 26.644  1.00 27.33 ? 156  GLY C C   1 
ATOM   6199  O  O   . GLY C  1 153 ? 49.911  -17.181 26.700  1.00 24.96 ? 156  GLY C O   1 
ATOM   6200  N  N   . GLY C  1 154 ? 50.400  -15.019 27.172  1.00 26.46 ? 157  GLY C N   1 
ATOM   6201  C  CA  . GLY C  1 154 ? 51.783  -15.270 27.565  1.00 30.61 ? 157  GLY C CA  1 
ATOM   6202  C  C   . GLY C  1 154 ? 52.551  -16.135 26.580  1.00 33.13 ? 157  GLY C C   1 
ATOM   6203  O  O   . GLY C  1 154 ? 53.322  -17.015 26.978  1.00 33.56 ? 157  GLY C O   1 
ATOM   6204  N  N   . GLY C  1 155 ? 52.310  -15.931 25.289  1.00 32.34 ? 158  GLY C N   1 
ATOM   6205  C  CA  . GLY C  1 155 ? 53.078  -16.645 24.270  1.00 30.86 ? 158  GLY C CA  1 
ATOM   6206  C  C   . GLY C  1 155 ? 52.363  -17.836 23.650  1.00 30.21 ? 158  GLY C C   1 
ATOM   6207  O  O   . GLY C  1 155 ? 52.822  -18.373 22.644  1.00 29.77 ? 158  GLY C O   1 
ATOM   6208  N  N   . LYS C  1 156 ? 51.268  -18.282 24.273  1.00 29.06 ? 159  LYS C N   1 
ATOM   6209  C  CA  . LYS C  1 156 ? 50.396  -19.309 23.691  1.00 26.51 ? 159  LYS C CA  1 
ATOM   6210  C  C   . LYS C  1 156 ? 49.186  -18.673 23.021  1.00 25.36 ? 159  LYS C C   1 
ATOM   6211  O  O   . LYS C  1 156 ? 48.882  -17.496 23.255  1.00 24.22 ? 159  LYS C O   1 
ATOM   6212  C  CB  . LYS C  1 156 ? 49.880  -20.263 24.783  1.00 30.66 ? 159  LYS C CB  1 
ATOM   6213  C  CG  . LYS C  1 156 ? 50.852  -21.346 25.244  1.00 33.70 ? 159  LYS C CG  1 
ATOM   6214  C  CD  . LYS C  1 156 ? 52.286  -20.992 24.915  1.00 36.85 ? 159  LYS C CD  1 
ATOM   6215  C  CE  . LYS C  1 156 ? 53.173  -22.217 25.023  1.00 41.71 ? 159  LYS C CE  1 
ATOM   6216  N  NZ  . LYS C  1 156 ? 53.496  -22.496 26.434  1.00 41.87 ? 159  LYS C NZ  1 
ATOM   6217  N  N   . TYR C  1 157 ? 48.464  -19.469 22.230  1.00 24.07 ? 160  TYR C N   1 
ATOM   6218  C  CA  . TYR C  1 157 ? 47.146  -19.075 21.728  1.00 20.51 ? 160  TYR C CA  1 
ATOM   6219  C  C   . TYR C  1 157 ? 46.076  -19.653 22.641  1.00 21.62 ? 160  TYR C C   1 
ATOM   6220  O  O   . TYR C  1 157 ? 46.061  -20.857 22.905  1.00 21.56 ? 160  TYR C O   1 
ATOM   6221  C  CB  . TYR C  1 157 ? 46.920  -19.583 20.305  1.00 19.46 ? 160  TYR C CB  1 
ATOM   6222  C  CG  . TYR C  1 157 ? 45.611  -19.093 19.682  1.00 20.49 ? 160  TYR C CG  1 
ATOM   6223  C  CD1 . TYR C  1 157 ? 44.435  -19.804 19.839  1.00 20.33 ? 160  TYR C CD1 1 
ATOM   6224  C  CD2 . TYR C  1 157 ? 45.577  -17.944 18.906  1.00 18.64 ? 160  TYR C CD2 1 
ATOM   6225  C  CE1 . TYR C  1 157 ? 43.264  -19.390 19.232  1.00 23.61 ? 160  TYR C CE1 1 
ATOM   6226  C  CE2 . TYR C  1 157 ? 44.410  -17.493 18.342  1.00 23.21 ? 160  TYR C CE2 1 
ATOM   6227  C  CZ  . TYR C  1 157 ? 43.254  -18.226 18.492  1.00 25.14 ? 160  TYR C CZ  1 
ATOM   6228  O  OH  . TYR C  1 157 ? 42.100  -17.799 17.877  1.00 24.11 ? 160  TYR C OH  1 
ATOM   6229  N  N   . ASN C  1 158 ? 45.225  -18.795 23.179  1.00 19.80 ? 161  ASN C N   1 
ATOM   6230  C  CA  . ASN C  1 158 ? 44.099  -19.271 23.966  1.00 23.87 ? 161  ASN C CA  1 
ATOM   6231  C  C   . ASN C  1 158 ? 42.872  -18.373 23.764  1.00 23.20 ? 161  ASN C C   1 
ATOM   6232  O  O   . ASN C  1 158 ? 42.924  -17.417 22.990  1.00 23.44 ? 161  ASN C O   1 
ATOM   6233  C  CB  . ASN C  1 158 ? 44.491  -19.434 25.453  1.00 21.84 ? 161  ASN C CB  1 
ATOM   6234  C  CG  . ASN C  1 158 ? 44.747  -18.114 26.150  1.00 26.10 ? 161  ASN C CG  1 
ATOM   6235  O  OD1 . ASN C  1 158 ? 44.350  -17.053 25.665  1.00 26.41 ? 161  ASN C OD1 1 
ATOM   6236  N  ND2 . ASN C  1 158 ? 45.399  -18.177 27.326  1.00 27.49 ? 161  ASN C ND2 1 
ATOM   6237  N  N   . LEU C  1 159 ? 41.768  -18.687 24.435  1.00 23.47 ? 162  LEU C N   1 
ATOM   6238  C  CA  . LEU C  1 159 ? 40.495  -18.044 24.113  1.00 21.30 ? 162  LEU C CA  1 
ATOM   6239  C  C   . LEU C  1 159 ? 40.566  -16.550 24.419  1.00 20.22 ? 162  LEU C C   1 
ATOM   6240  O  O   . LEU C  1 159 ? 39.899  -15.757 23.785  1.00 19.52 ? 162  LEU C O   1 
ATOM   6241  C  CB  . LEU C  1 159 ? 39.355  -18.693 24.895  1.00 23.66 ? 162  LEU C CB  1 
ATOM   6242  C  CG  . LEU C  1 159 ? 39.034  -20.142 24.529  1.00 24.00 ? 162  LEU C CG  1 
ATOM   6243  C  CD1 . LEU C  1 159 ? 37.956  -20.605 25.465  1.00 23.64 ? 162  LEU C CD1 1 
ATOM   6244  C  CD2 . LEU C  1 159 ? 38.592  -20.289 23.047  1.00 22.44 ? 162  LEU C CD2 1 
ATOM   6245  N  N   . THR C  1 160 ? 41.480  -16.147 25.291  1.00 19.52 ? 163  THR C N   1 
ATOM   6246  C  CA  . THR C  1 160 ? 41.687  -14.716 25.520  1.00 16.94 ? 163  THR C CA  1 
ATOM   6247  C  C   . THR C  1 160 ? 42.289  -14.018 24.304  1.00 18.14 ? 163  THR C C   1 
ATOM   6248  O  O   . THR C  1 160 ? 41.827  -12.943 23.889  1.00 17.58 ? 163  THR C O   1 
ATOM   6249  C  CB  . THR C  1 160 ? 42.561  -14.459 26.733  1.00 15.64 ? 163  THR C CB  1 
ATOM   6250  O  OG1 . THR C  1 160 ? 41.988  -15.120 27.871  1.00 14.93 ? 163  THR C OG1 1 
ATOM   6251  C  CG2 . THR C  1 160 ? 42.694  -12.943 26.993  1.00 12.98 ? 163  THR C CG2 1 
ATOM   6252  N  N   . VAL C  1 161 ? 43.309  -14.647 23.734  1.00 16.34 ? 164  VAL C N   1 
ATOM   6253  C  CA  . VAL C  1 161 ? 43.865  -14.255 22.430  1.00 18.36 ? 164  VAL C CA  1 
ATOM   6254  C  C   . VAL C  1 161 ? 42.842  -14.250 21.289  1.00 18.13 ? 164  VAL C C   1 
ATOM   6255  O  O   . VAL C  1 161 ? 42.781  -13.307 20.506  1.00 18.53 ? 164  VAL C O   1 
ATOM   6256  C  CB  . VAL C  1 161 ? 44.982  -15.219 22.006  1.00 16.70 ? 164  VAL C CB  1 
ATOM   6257  C  CG1 . VAL C  1 161 ? 45.690  -14.658 20.774  1.00 17.37 ? 164  VAL C CG1 1 
ATOM   6258  C  CG2 . VAL C  1 161 ? 45.979  -15.418 23.166  1.00 17.37 ? 164  VAL C CG2 1 
ATOM   6259  N  N   . ALA C  1 162 ? 42.103  -15.346 21.148  1.00 17.04 ? 165  ALA C N   1 
ATOM   6260  C  CA  . ALA C  1 162 ? 41.030  -15.408 20.173  1.00 17.42 ? 165  ALA C CA  1 
ATOM   6261  C  C   . ALA C  1 162 ? 40.180  -14.140 20.258  1.00 19.61 ? 165  ALA C C   1 
ATOM   6262  O  O   . ALA C  1 162 ? 39.942  -13.480 19.252  1.00 19.65 ? 165  ALA C O   1 
ATOM   6263  C  CB  . ALA C  1 162 ? 40.178  -16.633 20.425  1.00 16.65 ? 165  ALA C CB  1 
ATOM   6264  N  N   . GLY C  1 163 ? 39.780  -13.767 21.475  1.00 19.10 ? 166  GLY C N   1 
ATOM   6265  C  CA  . GLY C  1 163 ? 38.937  -12.600 21.670  1.00 16.52 ? 166  GLY C CA  1 
ATOM   6266  C  C   . GLY C  1 163 ? 39.560  -11.372 21.059  1.00 21.06 ? 166  GLY C C   1 
ATOM   6267  O  O   . GLY C  1 163 ? 38.871  -10.550 20.438  1.00 24.24 ? 166  GLY C O   1 
ATOM   6268  N  N   . GLU C  1 164 ? 40.855  -11.180 21.293  1.00 20.49 ? 167  GLU C N   1 
ATOM   6269  C  CA  . GLU C  1 164 ? 41.455  -9.910  20.926  1.00 19.07 ? 167  GLU C CA  1 
ATOM   6270  C  C   . GLU C  1 164 ? 41.693  -9.887  19.421  1.00 19.61 ? 167  GLU C C   1 
ATOM   6271  O  O   . GLU C  1 164 ? 41.551  -8.854  18.778  1.00 17.44 ? 167  GLU C O   1 
ATOM   6272  C  CB  . GLU C  1 164 ? 42.765  -9.699  21.672  1.00 21.35 ? 167  GLU C CB  1 
ATOM   6273  C  CG  . GLU C  1 164 ? 42.585  -9.489  23.170  1.00 25.58 ? 167  GLU C CG  1 
ATOM   6274  C  CD  . GLU C  1 164 ? 41.454  -8.529  23.484  1.00 29.73 ? 167  GLU C CD  1 
ATOM   6275  O  OE1 . GLU C  1 164 ? 41.367  -7.467  22.822  1.00 30.80 ? 167  GLU C OE1 1 
ATOM   6276  O  OE2 . GLU C  1 164 ? 40.594  -8.887  24.325  1.00 32.50 ? 167  GLU C OE2 1 
ATOM   6277  N  N   . LEU C  1 165 ? 42.106  -11.031 18.890  1.00 16.93 ? 168  LEU C N   1 
ATOM   6278  C  CA  . LEU C  1 165 ? 42.618  -11.119 17.541  1.00 21.08 ? 168  LEU C CA  1 
ATOM   6279  C  C   . LEU C  1 165 ? 41.427  -11.092 16.593  1.00 21.50 ? 168  LEU C C   1 
ATOM   6280  O  O   . LEU C  1 165 ? 41.497  -10.507 15.504  1.00 19.40 ? 168  LEU C O   1 
ATOM   6281  C  CB  . LEU C  1 165 ? 43.415  -12.422 17.356  1.00 18.20 ? 168  LEU C CB  1 
ATOM   6282  C  CG  . LEU C  1 165 ? 43.750  -12.787 15.909  1.00 21.88 ? 168  LEU C CG  1 
ATOM   6283  C  CD1 . LEU C  1 165 ? 44.613  -11.713 15.253  1.00 20.12 ? 168  LEU C CD1 1 
ATOM   6284  C  CD2 . LEU C  1 165 ? 44.440  -14.180 15.817  1.00 22.59 ? 168  LEU C CD2 1 
ATOM   6285  N  N   . ARG C  1 166 ? 40.321  -11.692 17.043  1.00 20.26 ? 169  ARG C N   1 
ATOM   6286  C  CA  . ARG C  1 166 ? 39.079  -11.694 16.275  1.00 19.57 ? 169  ARG C CA  1 
ATOM   6287  C  C   . ARG C  1 166 ? 38.612  -10.255 16.064  1.00 19.50 ? 169  ARG C C   1 
ATOM   6288  O  O   . ARG C  1 166 ? 38.331  -9.855  14.940  1.00 21.72 ? 169  ARG C O   1 
ATOM   6289  C  CB  . ARG C  1 166 ? 38.016  -12.583 16.959  1.00 16.85 ? 169  ARG C CB  1 
ATOM   6290  C  CG  . ARG C  1 166 ? 36.547  -12.274 16.637  1.00 18.38 ? 169  ARG C CG  1 
ATOM   6291  C  CD  . ARG C  1 166 ? 36.220  -12.305 15.115  1.00 17.48 ? 169  ARG C CD  1 
ATOM   6292  N  NE  . ARG C  1 166 ? 36.742  -13.486 14.438  1.00 17.37 ? 169  ARG C NE  1 
ATOM   6293  C  CZ  . ARG C  1 166 ? 37.435  -13.448 13.299  1.00 19.19 ? 169  ARG C CZ  1 
ATOM   6294  N  NH1 . ARG C  1 166 ? 37.737  -12.282 12.728  1.00 18.30 ? 169  ARG C NH1 1 
ATOM   6295  N  NH2 . ARG C  1 166 ? 37.790  -14.578 12.703  1.00 20.39 ? 169  ARG C NH2 1 
ATOM   6296  N  N   . PHE C  1 167 ? 38.707  -9.434  17.104  1.00 21.31 ? 170  PHE C N   1 
ATOM   6297  C  CA  . PHE C  1 167 ? 38.358  -8.007  16.976  1.00 22.62 ? 170  PHE C CA  1 
ATOM   6298  C  C   . PHE C  1 167 ? 39.343  -7.255  16.072  1.00 24.66 ? 170  PHE C C   1 
ATOM   6299  O  O   . PHE C  1 167 ? 38.950  -6.409  15.266  1.00 24.83 ? 170  PHE C O   1 
ATOM   6300  C  CB  . PHE C  1 167 ? 38.281  -7.334  18.355  1.00 20.28 ? 170  PHE C CB  1 
ATOM   6301  C  CG  . PHE C  1 167 ? 37.778  -5.903  18.315  1.00 21.41 ? 170  PHE C CG  1 
ATOM   6302  C  CD1 . PHE C  1 167 ? 36.508  -5.609  17.836  1.00 21.04 ? 170  PHE C CD1 1 
ATOM   6303  C  CD2 . PHE C  1 167 ? 38.565  -4.863  18.805  1.00 25.30 ? 170  PHE C CD2 1 
ATOM   6304  C  CE1 . PHE C  1 167 ? 36.019  -4.288  17.833  1.00 27.86 ? 170  PHE C CE1 1 
ATOM   6305  C  CE2 . PHE C  1 167 ? 38.103  -3.531  18.808  1.00 29.11 ? 170  PHE C CE2 1 
ATOM   6306  C  CZ  . PHE C  1 167 ? 36.827  -3.236  18.313  1.00 26.74 ? 170  PHE C CZ  1 
ATOM   6307  N  N   . LYS C  1 168 ? 40.630  -7.534  16.242  1.00 25.50 ? 171  LYS C N   1 
ATOM   6308  C  CA  . LYS C  1 168 ? 41.652  -6.872  15.455  1.00 24.33 ? 171  LYS C CA  1 
ATOM   6309  C  C   . LYS C  1 168 ? 41.495  -7.120  13.937  1.00 23.64 ? 171  LYS C C   1 
ATOM   6310  O  O   . LYS C  1 168 ? 41.613  -6.192  13.108  1.00 25.94 ? 171  LYS C O   1 
ATOM   6311  C  CB  . LYS C  1 168 ? 43.028  -7.319  15.929  1.00 25.81 ? 171  LYS C CB  1 
ATOM   6312  C  CG  . LYS C  1 168 ? 44.161  -6.641  15.187  1.00 29.03 ? 171  LYS C CG  1 
ATOM   6313  C  CD  . LYS C  1 168 ? 43.951  -5.150  15.165  1.00 29.79 ? 171  LYS C CD  1 
ATOM   6314  C  CE  . LYS C  1 168 ? 44.952  -4.463  14.257  1.00 33.31 ? 171  LYS C CE  1 
ATOM   6315  N  NZ  . LYS C  1 168 ? 46.285  -4.530  14.861  1.00 34.08 ? 171  LYS C NZ  1 
ATOM   6316  N  N   . ARG C  1 169 ? 41.217  -8.364  13.572  1.00 20.09 ? 172  ARG C N   1 
ATOM   6317  C  CA  . ARG C  1 169 ? 40.989  -8.694  12.163  1.00 23.60 ? 172  ARG C CA  1 
ATOM   6318  C  C   . ARG C  1 169 ? 39.737  -8.007  11.592  1.00 22.55 ? 172  ARG C C   1 
ATOM   6319  O  O   . ARG C  1 169 ? 39.747  -7.533  10.456  1.00 25.80 ? 172  ARG C O   1 
ATOM   6320  C  CB  . ARG C  1 169 ? 40.955  -10.198 11.964  1.00 22.77 ? 172  ARG C CB  1 
ATOM   6321  C  CG  . ARG C  1 169 ? 42.277  -10.879 12.359  1.00 22.75 ? 172  ARG C CG  1 
ATOM   6322  C  CD  . ARG C  1 169 ? 43.415  -10.569 11.364  1.00 19.90 ? 172  ARG C CD  1 
ATOM   6323  N  NE  . ARG C  1 169 ? 43.080  -10.998 10.008  1.00 21.37 ? 172  ARG C NE  1 
ATOM   6324  C  CZ  . ARG C  1 169 ? 42.906  -10.171 8.981   1.00 20.81 ? 172  ARG C CZ  1 
ATOM   6325  N  NH1 . ARG C  1 169 ? 43.104  -8.866  9.136   1.00 23.76 ? 172  ARG C NH1 1 
ATOM   6326  N  NH2 . ARG C  1 169 ? 42.468  -10.641 7.820   1.00 18.65 ? 172  ARG C NH2 1 
ATOM   6327  N  N   . ILE C  1 170 ? 38.726  -7.819  12.431  1.00 17.63 ? 173  ILE C N   1 
ATOM   6328  C  CA  . ILE C  1 170 ? 37.565  -7.042  12.036  1.00 21.47 ? 173  ILE C CA  1 
ATOM   6329  C  C   . ILE C  1 170 ? 37.921  -5.578  11.773  1.00 24.17 ? 173  ILE C C   1 
ATOM   6330  O  O   . ILE C  1 170 ? 37.527  -5.009  10.752  1.00 23.62 ? 173  ILE C O   1 
ATOM   6331  C  CB  . ILE C  1 170 ? 36.427  -7.142  13.082  1.00 20.26 ? 173  ILE C CB  1 
ATOM   6332  C  CG1 . ILE C  1 170 ? 35.855  -8.578  13.113  1.00 18.89 ? 173  ILE C CG1 1 
ATOM   6333  C  CG2 . ILE C  1 170 ? 35.369  -6.089  12.799  1.00 16.52 ? 173  ILE C CG2 1 
ATOM   6334  C  CD1 . ILE C  1 170 ? 34.987  -8.912  14.348  1.00 17.78 ? 173  ILE C CD1 1 
ATOM   6335  N  N   . GLN C  1 171 ? 38.684  -4.978  12.686  1.00 27.27 ? 174  GLN C N   1 
ATOM   6336  C  CA  . GLN C  1 171 ? 39.110  -3.593  12.535  1.00 29.44 ? 174  GLN C CA  1 
ATOM   6337  C  C   . GLN C  1 171 ? 39.987  -3.418  11.290  1.00 30.49 ? 174  GLN C C   1 
ATOM   6338  O  O   . GLN C  1 171 ? 39.804  -2.479  10.518  1.00 29.63 ? 174  GLN C O   1 
ATOM   6339  C  CB  . GLN C  1 171 ? 39.899  -3.147  13.767  1.00 33.37 ? 174  GLN C CB  1 
ATOM   6340  C  CG  . GLN C  1 171 ? 39.106  -2.943  15.048  1.00 34.65 ? 174  GLN C CG  1 
ATOM   6341  C  CD  . GLN C  1 171 ? 40.028  -2.558  16.215  1.00 41.28 ? 174  GLN C CD  1 
ATOM   6342  O  OE1 . GLN C  1 171 ? 41.034  -3.245  16.494  1.00 40.07 ? 174  GLN C OE1 1 
ATOM   6343  N  NE2 . GLN C  1 171 ? 39.760  -1.393  16.823  1.00 40.51 ? 174  GLN C NE2 1 
ATOM   6344  N  N   . ASP C  1 172 ? 40.944  -4.326  11.115  1.00 30.23 ? 175  ASP C N   1 
ATOM   6345  C  CA  . ASP C  1 172 ? 41.801  -4.352  9.930   1.00 27.45 ? 175  ASP C CA  1 
ATOM   6346  C  C   . ASP C  1 172 ? 40.952  -4.246  8.662   1.00 27.20 ? 175  ASP C C   1 
ATOM   6347  O  O   . ASP C  1 172 ? 41.299  -3.511  7.733   1.00 26.04 ? 175  ASP C O   1 
ATOM   6348  C  CB  . ASP C  1 172 ? 42.599  -5.679  9.874   1.00 28.10 ? 175  ASP C CB  1 
ATOM   6349  C  CG  . ASP C  1 172 ? 43.760  -5.744  10.892  1.00 31.43 ? 175  ASP C CG  1 
ATOM   6350  O  OD1 . ASP C  1 172 ? 44.050  -4.718  11.554  1.00 27.69 ? 175  ASP C OD1 1 
ATOM   6351  O  OD2 . ASP C  1 172 ? 44.381  -6.845  11.029  1.00 32.14 ? 175  ASP C OD2 1 
ATOM   6352  N  N   . SER C  1 173 ? 39.917  -5.088  8.565   1.00 24.94 ? 176  SER C N   1 
ATOM   6353  C  CA  . SER C  1 173 ? 39.123  -5.176  7.338   1.00 19.59 ? 176  SER C CA  1 
ATOM   6354  C  C   . SER C  1 173 ? 38.279  -3.920  7.138   1.00 19.27 ? 176  SER C C   1 
ATOM   6355  O  O   . SER C  1 173 ? 38.076  -3.473  6.019   1.00 18.10 ? 176  SER C O   1 
ATOM   6356  C  CB  . SER C  1 173 ? 38.213  -6.408  7.356   1.00 18.63 ? 176  SER C CB  1 
ATOM   6357  O  OG  . SER C  1 173 ? 38.940  -7.607  7.183   1.00 23.14 ? 176  SER C OG  1 
ATOM   6358  N  N   . ILE C  1 174 ? 37.686  -3.419  8.212   1.00 22.27 ? 177  ILE C N   1 
ATOM   6359  C  CA  . ILE C  1 174 ? 36.956  -2.159  8.124   1.00 23.54 ? 177  ILE C CA  1 
ATOM   6360  C  C   . ILE C  1 174 ? 37.885  -1.098  7.550   1.00 26.18 ? 177  ILE C C   1 
ATOM   6361  O  O   . ILE C  1 174 ? 37.471  -0.293  6.722   1.00 28.00 ? 177  ILE C O   1 
ATOM   6362  C  CB  . ILE C  1 174 ? 36.397  -1.707  9.504   1.00 21.84 ? 177  ILE C CB  1 
ATOM   6363  C  CG1 . ILE C  1 174 ? 35.378  -2.730  10.026  1.00 21.86 ? 177  ILE C CG1 1 
ATOM   6364  C  CG2 . ILE C  1 174 ? 35.751  -0.323  9.411   1.00 22.58 ? 177  ILE C CG2 1 
ATOM   6365  C  CD1 . ILE C  1 174 ? 34.815  -2.394  11.416  1.00 17.70 ? 177  ILE C CD1 1 
ATOM   6366  N  N   . ALA C  1 175 ? 39.162  -1.152  7.930   1.00 29.02 ? 178  ALA C N   1 
ATOM   6367  C  CA  . ALA C  1 175 ? 40.096  -0.057  7.630   1.00 30.78 ? 178  ALA C CA  1 
ATOM   6368  C  C   . ALA C  1 175 ? 40.668  -0.130  6.206   1.00 31.63 ? 178  ALA C C   1 
ATOM   6369  O  O   . ALA C  1 175 ? 41.069  0.884   5.650   1.00 32.97 ? 178  ALA C O   1 
ATOM   6370  C  CB  . ALA C  1 175 ? 41.228  -0.011  8.658   1.00 26.51 ? 178  ALA C CB  1 
ATOM   6371  N  N   . THR C  1 176 ? 40.654  -1.313  5.602   1.00 29.28 ? 179  THR C N   1 
ATOM   6372  C  CA  . THR C  1 176 ? 41.379  -1.529  4.353   1.00 29.45 ? 179  THR C CA  1 
ATOM   6373  C  C   . THR C  1 176 ? 40.529  -2.125  3.230   1.00 29.53 ? 179  THR C C   1 
ATOM   6374  O  O   . THR C  1 176 ? 40.935  -2.123  2.080   1.00 28.64 ? 179  THR C O   1 
ATOM   6375  C  CB  . THR C  1 176 ? 42.551  -2.479  4.567   1.00 28.85 ? 179  THR C CB  1 
ATOM   6376  O  OG1 . THR C  1 176 ? 42.050  -3.689  5.124   1.00 26.49 ? 179  THR C OG1 1 
ATOM   6377  C  CG2 . THR C  1 176 ? 43.590  -1.863  5.537   1.00 30.43 ? 179  THR C CG2 1 
ATOM   6378  N  N   . ASN C  1 177 ? 39.381  -2.703  3.563   1.00 29.77 ? 180  ASN C N   1 
ATOM   6379  C  CA  . ASN C  1 177 ? 38.637  -3.466  2.569   1.00 27.89 ? 180  ASN C CA  1 
ATOM   6380  C  C   . ASN C  1 177 ? 37.266  -2.870  2.303   1.00 27.92 ? 180  ASN C C   1 
ATOM   6381  O  O   . ASN C  1 177 ? 36.320  -3.106  3.070   1.00 32.25 ? 180  ASN C O   1 
ATOM   6382  C  CB  . ASN C  1 177 ? 38.517  -4.921  3.013   1.00 25.12 ? 180  ASN C CB  1 
ATOM   6383  C  CG  . ASN C  1 177 ? 37.651  -5.753  2.085   1.00 23.85 ? 180  ASN C CG  1 
ATOM   6384  O  OD1 . ASN C  1 177 ? 37.101  -5.253  1.096   1.00 26.91 ? 180  ASN C OD1 1 
ATOM   6385  N  ND2 . ASN C  1 177 ? 37.545  -7.043  2.389   1.00 23.68 ? 180  ASN C ND2 1 
ATOM   6386  N  N   . PRO C  1 178 ? 37.143  -2.106  1.207   1.00 27.76 ? 181  PRO C N   1 
ATOM   6387  C  CA  . PRO C  1 178 ? 35.903  -1.369  0.901   1.00 26.58 ? 181  PRO C CA  1 
ATOM   6388  C  C   . PRO C  1 178 ? 34.735  -2.312  0.627   1.00 25.90 ? 181  PRO C C   1 
ATOM   6389  O  O   . PRO C  1 178 ? 33.586  -1.872  0.526   1.00 27.27 ? 181  PRO C O   1 
ATOM   6390  C  CB  . PRO C  1 178 ? 36.260  -0.588  -0.382  1.00 24.99 ? 181  PRO C CB  1 
ATOM   6391  C  CG  . PRO C  1 178 ? 37.343  -1.375  -1.011  1.00 23.27 ? 181  PRO C CG  1 
ATOM   6392  C  CD  . PRO C  1 178 ? 38.139  -1.992  0.124   1.00 26.73 ? 181  PRO C CD  1 
ATOM   6393  N  N   . ASN C  1 179 ? 35.031  -3.591  0.453   1.00 26.13 ? 182  ASN C N   1 
ATOM   6394  C  CA  . ASN C  1 179 ? 33.972  -4.585  0.234   1.00 28.39 ? 182  ASN C CA  1 
ATOM   6395  C  C   . ASN C  1 179 ? 33.743  -5.457  1.483   1.00 26.34 ? 182  ASN C C   1 
ATOM   6396  O  O   . ASN C  1 179 ? 33.173  -6.545  1.384   1.00 26.49 ? 182  ASN C O   1 
ATOM   6397  C  CB  . ASN C  1 179 ? 34.334  -5.493  -0.946  1.00 28.56 ? 182  ASN C CB  1 
ATOM   6398  C  CG  . ASN C  1 179 ? 33.982  -4.890  -2.299  1.00 35.26 ? 182  ASN C CG  1 
ATOM   6399  O  OD1 . ASN C  1 179 ? 33.783  -3.684  -2.439  1.00 33.10 ? 182  ASN C OD1 1 
ATOM   6400  N  ND2 . ASN C  1 179 ? 33.921  -5.745  -3.317  1.00 43.00 ? 182  ASN C ND2 1 
ATOM   6401  N  N   . PHE C  1 180 ? 34.307  -5.044  2.614   1.00 22.46 ? 183  PHE C N   1 
ATOM   6402  C  CA  . PHE C  1 180 ? 34.180  -5.819  3.855   1.00 21.21 ? 183  PHE C CA  1 
ATOM   6403  C  C   . PHE C  1 180 ? 32.734  -6.199  4.106   1.00 20.42 ? 183  PHE C C   1 
ATOM   6404  O  O   . PHE C  1 180 ? 31.853  -5.327  4.180   1.00 22.69 ? 183  PHE C O   1 
ATOM   6405  C  CB  . PHE C  1 180 ? 34.721  -5.033  5.058   1.00 19.69 ? 183  PHE C CB  1 
ATOM   6406  C  CG  . PHE C  1 180 ? 34.762  -5.836  6.336   1.00 22.44 ? 183  PHE C CG  1 
ATOM   6407  C  CD1 . PHE C  1 180 ? 35.104  -7.184  6.309   1.00 20.09 ? 183  PHE C CD1 1 
ATOM   6408  C  CD2 . PHE C  1 180 ? 34.366  -5.274  7.545   1.00 19.26 ? 183  PHE C CD2 1 
ATOM   6409  C  CE1 . PHE C  1 180 ? 35.111  -7.933  7.469   1.00 18.49 ? 183  PHE C CE1 1 
ATOM   6410  C  CE2 . PHE C  1 180 ? 34.374  -6.022  8.723   1.00 19.25 ? 183  PHE C CE2 1 
ATOM   6411  C  CZ  . PHE C  1 180 ? 34.732  -7.357  8.680   1.00 19.63 ? 183  PHE C CZ  1 
ATOM   6412  N  N   . SER C  1 181 ? 32.499  -7.489  4.328   1.00 20.36 ? 184  SER C N   1 
ATOM   6413  C  CA  . SER C  1 181 ? 31.154  -7.971  4.644   1.00 19.79 ? 184  SER C CA  1 
ATOM   6414  C  C   . SER C  1 181 ? 31.208  -8.895  5.850   1.00 18.71 ? 184  SER C C   1 
ATOM   6415  O  O   . SER C  1 181 ? 32.120  -9.697  5.975   1.00 17.92 ? 184  SER C O   1 
ATOM   6416  C  CB  . SER C  1 181 ? 30.562  -8.719  3.448   1.00 21.73 ? 184  SER C CB  1 
ATOM   6417  O  OG  . SER C  1 181 ? 29.354  -9.354  3.831   1.00 23.04 ? 184  SER C OG  1 
ATOM   6418  N  N   . PHE C  1 182 ? 30.295  -8.710  6.794   1.00 17.54 ? 185  PHE C N   1 
ATOM   6419  C  CA  . PHE C  1 182 ? 30.395  -9.414  8.057   1.00 15.29 ? 185  PHE C CA  1 
ATOM   6420  C  C   . PHE C  1 182 ? 29.001  -9.583  8.631   1.00 16.68 ? 185  PHE C C   1 
ATOM   6421  O  O   . PHE C  1 182 ? 28.695  -9.083  9.714   1.00 16.24 ? 185  PHE C O   1 
ATOM   6422  C  CB  . PHE C  1 182 ? 31.283  -8.637  9.022   1.00 16.04 ? 185  PHE C CB  1 
ATOM   6423  C  CG  . PHE C  1 182 ? 31.907  -9.484  10.088  1.00 18.11 ? 185  PHE C CG  1 
ATOM   6424  C  CD1 . PHE C  1 182 ? 32.769  -10.525 9.748   1.00 16.05 ? 185  PHE C CD1 1 
ATOM   6425  C  CD2 . PHE C  1 182 ? 31.723  -9.177  11.429  1.00 16.68 ? 185  PHE C CD2 1 
ATOM   6426  C  CE1 . PHE C  1 182 ? 33.372  -11.286 10.724  1.00 17.35 ? 185  PHE C CE1 1 
ATOM   6427  C  CE2 . PHE C  1 182 ? 32.311  -9.946  12.419  1.00 16.26 ? 185  PHE C CE2 1 
ATOM   6428  C  CZ  . PHE C  1 182 ? 33.128  -11.006 12.071  1.00 16.80 ? 185  PHE C CZ  1 
ATOM   6429  N  N   . VAL C  1 183 ? 28.160  -10.302 7.896   1.00 15.39 ? 186  VAL C N   1 
ATOM   6430  C  CA  . VAL C  1 183 ? 26.778  -10.474 8.269   1.00 17.92 ? 186  VAL C CA  1 
ATOM   6431  C  C   . VAL C  1 183 ? 26.414  -11.944 8.222   1.00 20.66 ? 186  VAL C C   1 
ATOM   6432  O  O   . VAL C  1 183 ? 27.163  -12.765 7.670   1.00 23.16 ? 186  VAL C O   1 
ATOM   6433  C  CB  . VAL C  1 183 ? 25.851  -9.720  7.295   1.00 18.19 ? 186  VAL C CB  1 
ATOM   6434  C  CG1 . VAL C  1 183 ? 26.172  -8.225  7.296   1.00 13.32 ? 186  VAL C CG1 1 
ATOM   6435  C  CG2 . VAL C  1 183 ? 25.969  -10.311 5.854   1.00 15.96 ? 186  VAL C CG2 1 
ATOM   6436  N  N   . ASP C  1 184 ? 25.247  -12.276 8.770   1.00 20.27 ? 187  ASP C N   1 
ATOM   6437  C  CA  . ASP C  1 184 ? 24.626  -13.577 8.523   1.00 18.43 ? 187  ASP C CA  1 
ATOM   6438  C  C   . ASP C  1 184 ? 25.593  -14.748 8.789   1.00 18.48 ? 187  ASP C C   1 
ATOM   6439  O  O   . ASP C  1 184 ? 26.144  -14.862 9.887   1.00 22.52 ? 187  ASP C O   1 
ATOM   6440  C  CB  . ASP C  1 184 ? 24.000  -13.606 7.120   1.00 19.20 ? 187  ASP C CB  1 
ATOM   6441  C  CG  . ASP C  1 184 ? 22.894  -12.552 6.961   1.00 22.27 ? 187  ASP C CG  1 
ATOM   6442  O  OD1 . ASP C  1 184 ? 22.023  -12.480 7.850   1.00 23.13 ? 187  ASP C OD1 1 
ATOM   6443  O  OD2 . ASP C  1 184 ? 22.952  -11.722 6.022   1.00 23.11 ? 187  ASP C OD2 1 
ATOM   6444  N  N   . PHE C  1 185 ? 25.810  -15.613 7.805   1.00 19.59 ? 188  PHE C N   1 
ATOM   6445  C  CA  . PHE C  1 185 ? 26.521  -16.868 8.067   1.00 17.87 ? 188  PHE C CA  1 
ATOM   6446  C  C   . PHE C  1 185 ? 27.988  -16.640 8.416   1.00 14.78 ? 188  PHE C C   1 
ATOM   6447  O  O   . PHE C  1 185 ? 28.538  -17.279 9.291   1.00 18.78 ? 188  PHE C O   1 
ATOM   6448  C  CB  . PHE C  1 185 ? 26.396  -17.823 6.882   1.00 16.24 ? 188  PHE C CB  1 
ATOM   6449  C  CG  . PHE C  1 185 ? 26.881  -19.212 7.175   1.00 17.29 ? 188  PHE C CG  1 
ATOM   6450  C  CD1 . PHE C  1 185 ? 26.249  -19.995 8.124   1.00 21.14 ? 188  PHE C CD1 1 
ATOM   6451  C  CD2 . PHE C  1 185 ? 27.958  -19.739 6.511   1.00 14.94 ? 188  PHE C CD2 1 
ATOM   6452  C  CE1 . PHE C  1 185 ? 26.666  -21.295 8.375   1.00 19.24 ? 188  PHE C CE1 1 
ATOM   6453  C  CE2 . PHE C  1 185 ? 28.405  -21.031 6.795   1.00 18.37 ? 188  PHE C CE2 1 
ATOM   6454  C  CZ  . PHE C  1 185 ? 27.755  -21.805 7.720   1.00 15.26 ? 188  PHE C CZ  1 
ATOM   6455  N  N   . ARG C  1 186 ? 28.604  -15.670 7.774   1.00 17.29 ? 189  ARG C N   1 
ATOM   6456  C  CA  . ARG C  1 186 ? 29.982  -15.362 8.078   1.00 18.52 ? 189  ARG C CA  1 
ATOM   6457  C  C   . ARG C  1 186 ? 30.167  -14.716 9.451   1.00 17.62 ? 189  ARG C C   1 
ATOM   6458  O  O   . ARG C  1 186 ? 31.145  -14.989 10.137  1.00 19.05 ? 189  ARG C O   1 
ATOM   6459  C  CB  . ARG C  1 186 ? 30.634  -14.543 6.974   1.00 14.06 ? 189  ARG C CB  1 
ATOM   6460  C  CG  . ARG C  1 186 ? 32.031  -14.097 7.342   1.00 20.61 ? 189  ARG C CG  1 
ATOM   6461  C  CD  . ARG C  1 186 ? 32.985  -15.289 7.363   1.00 20.35 ? 189  ARG C CD  1 
ATOM   6462  N  NE  . ARG C  1 186 ? 34.309  -14.914 7.864   1.00 20.23 ? 189  ARG C NE  1 
ATOM   6463  C  CZ  . ARG C  1 186 ? 35.175  -15.768 8.410   1.00 19.93 ? 189  ARG C CZ  1 
ATOM   6464  N  NH1 . ARG C  1 186 ? 34.850  -17.047 8.561   1.00 16.02 ? 189  ARG C NH1 1 
ATOM   6465  N  NH2 . ARG C  1 186 ? 36.359  -15.334 8.834   1.00 18.68 ? 189  ARG C NH2 1 
ATOM   6466  N  N   . PHE C  1 187 ? 29.250  -13.843 9.845   1.00 18.62 ? 190  PHE C N   1 
ATOM   6467  C  CA  . PHE C  1 187 ? 29.265  -13.324 11.201  1.00 17.90 ? 190  PHE C CA  1 
ATOM   6468  C  C   . PHE C  1 187 ? 29.298  -14.472 12.199  1.00 19.44 ? 190  PHE C C   1 
ATOM   6469  O  O   . PHE C  1 187 ? 30.081  -14.460 13.148  1.00 17.70 ? 190  PHE C O   1 
ATOM   6470  C  CB  . PHE C  1 187 ? 28.051  -12.460 11.454  1.00 20.45 ? 190  PHE C CB  1 
ATOM   6471  C  CG  . PHE C  1 187 ? 28.106  -11.705 12.747  1.00 20.50 ? 190  PHE C CG  1 
ATOM   6472  C  CD1 . PHE C  1 187 ? 28.767  -10.488 12.825  1.00 23.07 ? 190  PHE C CD1 1 
ATOM   6473  C  CD2 . PHE C  1 187 ? 27.405  -12.150 13.849  1.00 21.52 ? 190  PHE C CD2 1 
ATOM   6474  C  CE1 . PHE C  1 187 ? 28.739  -9.730  14.006  1.00 23.13 ? 190  PHE C CE1 1 
ATOM   6475  C  CE2 . PHE C  1 187 ? 27.390  -11.415 15.039  1.00 22.18 ? 190  PHE C CE2 1 
ATOM   6476  C  CZ  . PHE C  1 187 ? 28.093  -10.224 15.123  1.00 22.33 ? 190  PHE C CZ  1 
ATOM   6477  N  N   . PHE C  1 188 ? 28.497  -15.496 11.937  1.00 18.98 ? 191  PHE C N   1 
ATOM   6478  C  CA  . PHE C  1 188 ? 28.451  -16.650 12.803  1.00 18.55 ? 191  PHE C CA  1 
ATOM   6479  C  C   . PHE C  1 188 ? 29.772  -17.432 12.835  1.00 22.14 ? 191  PHE C C   1 
ATOM   6480  O  O   . PHE C  1 188 ? 30.387  -17.556 13.883  1.00 22.02 ? 191  PHE C O   1 
ATOM   6481  C  CB  . PHE C  1 188 ? 27.283  -17.556 12.421  1.00 20.69 ? 191  PHE C CB  1 
ATOM   6482  C  CG  . PHE C  1 188 ? 27.177  -18.797 13.260  1.00 22.25 ? 191  PHE C CG  1 
ATOM   6483  C  CD1 . PHE C  1 188 ? 26.623  -18.744 14.523  1.00 21.10 ? 191  PHE C CD1 1 
ATOM   6484  C  CD2 . PHE C  1 188 ? 27.640  -20.018 12.785  1.00 23.56 ? 191  PHE C CD2 1 
ATOM   6485  C  CE1 . PHE C  1 188 ? 26.515  -19.894 15.308  1.00 23.51 ? 191  PHE C CE1 1 
ATOM   6486  C  CE2 . PHE C  1 188 ? 27.545  -21.174 13.564  1.00 26.34 ? 191  PHE C CE2 1 
ATOM   6487  C  CZ  . PHE C  1 188 ? 27.009  -21.103 14.845  1.00 24.45 ? 191  PHE C CZ  1 
ATOM   6488  N  N   . THR C  1 189 ? 30.223  -17.931 11.689  1.00 20.68 ? 192  THR C N   1 
ATOM   6489  C  CA  . THR C  1 189 ? 31.352  -18.862 11.668  1.00 22.23 ? 192  THR C CA  1 
ATOM   6490  C  C   . THR C  1 189 ? 32.657  -18.192 12.082  1.00 23.15 ? 192  THR C C   1 
ATOM   6491  O  O   . THR C  1 189 ? 33.616  -18.870 12.467  1.00 23.85 ? 192  THR C O   1 
ATOM   6492  C  CB  . THR C  1 189 ? 31.540  -19.537 10.252  1.00 24.00 ? 192  THR C CB  1 
ATOM   6493  O  OG1 . THR C  1 189 ? 31.878  -18.544 9.267   1.00 24.35 ? 192  THR C OG1 1 
ATOM   6494  C  CG2 . THR C  1 189 ? 30.270  -20.240 9.817   1.00 24.13 ? 192  THR C CG2 1 
ATOM   6495  N  N   . ALA C  1 190 ? 32.735  -16.870 11.927  1.00 21.06 ? 193  ALA C N   1 
ATOM   6496  C  CA  . ALA C  1 190 ? 33.997  -16.192 12.154  1.00 19.41 ? 193  ALA C CA  1 
ATOM   6497  C  C   . ALA C  1 190 ? 34.380  -16.223 13.642  1.00 23.81 ? 193  ALA C C   1 
ATOM   6498  O  O   . ALA C  1 190 ? 35.560  -16.230 13.980  1.00 23.41 ? 193  ALA C O   1 
ATOM   6499  C  CB  . ALA C  1 190 ? 33.947  -14.780 11.651  1.00 20.24 ? 193  ALA C CB  1 
ATOM   6500  N  N   . TYR C  1 191 ? 33.381  -16.242 14.526  1.00 22.65 ? 194  TYR C N   1 
ATOM   6501  C  CA  . TYR C  1 191 ? 33.650  -16.362 15.943  1.00 17.55 ? 194  TYR C CA  1 
ATOM   6502  C  C   . TYR C  1 191 ? 34.040  -17.758 16.377  1.00 18.66 ? 194  TYR C C   1 
ATOM   6503  O  O   . TYR C  1 191 ? 35.077  -17.926 17.028  1.00 18.55 ? 194  TYR C O   1 
ATOM   6504  C  CB  . TYR C  1 191 ? 32.513  -15.800 16.792  1.00 16.13 ? 194  TYR C CB  1 
ATOM   6505  C  CG  . TYR C  1 191 ? 32.493  -14.284 16.782  1.00 17.71 ? 194  TYR C CG  1 
ATOM   6506  C  CD1 . TYR C  1 191 ? 31.912  -13.588 15.718  1.00 13.71 ? 194  TYR C CD1 1 
ATOM   6507  C  CD2 . TYR C  1 191 ? 33.140  -13.547 17.778  1.00 13.82 ? 194  TYR C CD2 1 
ATOM   6508  C  CE1 . TYR C  1 191 ? 31.927  -12.194 15.674  1.00 15.48 ? 194  TYR C CE1 1 
ATOM   6509  C  CE2 . TYR C  1 191 ? 33.123  -12.131 17.757  1.00 17.49 ? 194  TYR C CE2 1 
ATOM   6510  C  CZ  . TYR C  1 191 ? 32.522  -11.470 16.690  1.00 16.51 ? 194  TYR C CZ  1 
ATOM   6511  O  OH  . TYR C  1 191 ? 32.493  -10.083 16.642  1.00 16.73 ? 194  TYR C OH  1 
ATOM   6512  N  N   . GLY C  1 192 ? 33.252  -18.770 16.009  1.00 15.79 ? 195  GLY C N   1 
ATOM   6513  C  CA  . GLY C  1 192 ? 33.574  -20.129 16.469  1.00 17.48 ? 195  GLY C CA  1 
ATOM   6514  C  C   . GLY C  1 192 ? 34.963  -20.595 16.027  1.00 19.87 ? 195  GLY C C   1 
ATOM   6515  O  O   . GLY C  1 192 ? 35.662  -21.311 16.756  1.00 23.79 ? 195  GLY C O   1 
ATOM   6516  N  N   . GLU C  1 193 ? 35.317  -20.278 14.788  1.00 17.96 ? 196  GLU C N   1 
ATOM   6517  C  CA  . GLU C  1 193 ? 36.562  -20.738 14.226  1.00 19.37 ? 196  GLU C CA  1 
ATOM   6518  C  C   . GLU C  1 193 ? 37.743  -20.286 15.071  1.00 21.36 ? 196  GLU C C   1 
ATOM   6519  O  O   . GLU C  1 193 ? 38.750  -20.988 15.131  1.00 20.47 ? 196  GLU C O   1 
ATOM   6520  C  CB  . GLU C  1 193 ? 36.724  -20.238 12.799  1.00 17.53 ? 196  GLU C CB  1 
ATOM   6521  C  CG  . GLU C  1 193 ? 35.817  -20.959 11.819  1.00 18.74 ? 196  GLU C CG  1 
ATOM   6522  C  CD  . GLU C  1 193 ? 35.650  -20.228 10.516  1.00 20.08 ? 196  GLU C CD  1 
ATOM   6523  O  OE1 . GLU C  1 193 ? 36.293  -19.166 10.321  1.00 21.71 ? 196  GLU C OE1 1 
ATOM   6524  O  OE2 . GLU C  1 193 ? 34.808  -20.685 9.705   1.00 23.77 ? 196  GLU C OE2 1 
ATOM   6525  N  N   . THR C  1 194 ? 37.622  -19.143 15.747  1.00 20.15 ? 197  THR C N   1 
ATOM   6526  C  CA  . THR C  1 194 ? 38.756  -18.644 16.526  1.00 19.97 ? 197  THR C CA  1 
ATOM   6527  C  C   . THR C  1 194 ? 38.953  -19.428 17.819  1.00 18.73 ? 197  THR C C   1 
ATOM   6528  O  O   . THR C  1 194 ? 39.968  -19.269 18.485  1.00 22.96 ? 197  THR C O   1 
ATOM   6529  C  CB  . THR C  1 194 ? 38.666  -17.133 16.849  1.00 20.38 ? 197  THR C CB  1 
ATOM   6530  O  OG1 . THR C  1 194 ? 37.448  -16.859 17.547  1.00 19.59 ? 197  THR C OG1 1 
ATOM   6531  C  CG2 . THR C  1 194 ? 38.736  -16.274 15.569  1.00 17.82 ? 197  THR C CG2 1 
ATOM   6532  N  N   . THR C  1 195 ? 37.953  -20.212 18.204  1.00 16.43 ? 198  THR C N   1 
ATOM   6533  C  CA  . THR C  1 195 ? 38.072  -21.131 19.326  1.00 17.93 ? 198  THR C CA  1 
ATOM   6534  C  C   . THR C  1 195 ? 38.727  -22.444 18.906  1.00 20.58 ? 198  THR C C   1 
ATOM   6535  O  O   . THR C  1 195 ? 39.234  -23.181 19.746  1.00 22.86 ? 198  THR C O   1 
ATOM   6536  C  CB  . THR C  1 195 ? 36.699  -21.457 19.952  1.00 17.01 ? 198  THR C CB  1 
ATOM   6537  O  OG1 . THR C  1 195 ? 35.961  -22.332 19.079  1.00 19.28 ? 198  THR C OG1 1 
ATOM   6538  C  CG2 . THR C  1 195 ? 35.903  -20.188 20.150  1.00 19.55 ? 198  THR C CG2 1 
ATOM   6539  N  N   . PHE C  1 196 ? 38.682  -22.766 17.615  1.00 19.34 ? 199  PHE C N   1 
ATOM   6540  C  CA  . PHE C  1 196 ? 39.049  -24.113 17.182  1.00 19.02 ? 199  PHE C CA  1 
ATOM   6541  C  C   . PHE C  1 196 ? 40.538  -24.419 17.465  1.00 18.83 ? 199  PHE C C   1 
ATOM   6542  O  O   . PHE C  1 196 ? 40.881  -25.527 17.871  1.00 23.00 ? 199  PHE C O   1 
ATOM   6543  C  CB  . PHE C  1 196 ? 38.696  -24.363 15.693  1.00 18.77 ? 199  PHE C CB  1 
ATOM   6544  C  CG  . PHE C  1 196 ? 37.200  -24.392 15.393  1.00 19.41 ? 199  PHE C CG  1 
ATOM   6545  C  CD1 . PHE C  1 196 ? 36.260  -24.453 16.417  1.00 20.54 ? 199  PHE C CD1 1 
ATOM   6546  C  CD2 . PHE C  1 196 ? 36.747  -24.438 14.071  1.00 21.25 ? 199  PHE C CD2 1 
ATOM   6547  C  CE1 . PHE C  1 196 ? 34.881  -24.508 16.138  1.00 20.24 ? 199  PHE C CE1 1 
ATOM   6548  C  CE2 . PHE C  1 196 ? 35.365  -24.462 13.769  1.00 20.43 ? 199  PHE C CE2 1 
ATOM   6549  C  CZ  . PHE C  1 196 ? 34.430  -24.518 14.806  1.00 20.68 ? 199  PHE C CZ  1 
ATOM   6550  N  N   . PRO C  1 197 ? 41.434  -23.455 17.224  1.00 17.09 ? 200  PRO C N   1 
ATOM   6551  C  CA  . PRO C  1 197 ? 42.836  -23.816 17.513  1.00 18.45 ? 200  PRO C CA  1 
ATOM   6552  C  C   . PRO C  1 197 ? 43.083  -24.145 19.003  1.00 22.34 ? 200  PRO C C   1 
ATOM   6553  O  O   . PRO C  1 197 ? 43.756  -25.146 19.341  1.00 23.09 ? 200  PRO C O   1 
ATOM   6554  C  CB  . PRO C  1 197 ? 43.632  -22.587 17.053  1.00 16.28 ? 200  PRO C CB  1 
ATOM   6555  C  CG  . PRO C  1 197 ? 42.598  -21.779 16.094  1.00 13.65 ? 200  PRO C CG  1 
ATOM   6556  C  CD  . PRO C  1 197 ? 41.271  -22.075 16.703  1.00 12.93 ? 200  PRO C CD  1 
ATOM   6557  N  N   . ALA C  1 198 ? 42.414  -23.415 19.881  1.00 21.05 ? 201  ALA C N   1 
ATOM   6558  C  CA  . ALA C  1 198 ? 42.562  -23.646 21.312  1.00 20.87 ? 201  ALA C CA  1 
ATOM   6559  C  C   . ALA C  1 198 ? 41.929  -24.961 21.773  1.00 22.15 ? 201  ALA C C   1 
ATOM   6560  O  O   . ALA C  1 198 ? 42.335  -25.515 22.799  1.00 17.90 ? 201  ALA C O   1 
ATOM   6561  C  CB  . ALA C  1 198 ? 41.988  -22.481 22.100  1.00 19.03 ? 201  ALA C CB  1 
ATOM   6562  N  N   . ASN C  1 199 ? 40.853  -25.377 21.102  1.00 20.54 ? 202  ASN C N   1 
ATOM   6563  C  CA  . ASN C  1 199 ? 40.058  -26.500 21.572  1.00 19.53 ? 202  ASN C CA  1 
ATOM   6564  C  C   . ASN C  1 199 ? 40.473  -27.804 20.903  1.00 20.15 ? 202  ASN C C   1 
ATOM   6565  O  O   . ASN C  1 199 ? 40.102  -28.870 21.387  1.00 21.36 ? 202  ASN C O   1 
ATOM   6566  C  CB  . ASN C  1 199 ? 38.550  -26.277 21.325  1.00 21.76 ? 202  ASN C CB  1 
ATOM   6567  C  CG  . ASN C  1 199 ? 37.951  -25.145 22.185  1.00 26.48 ? 202  ASN C CG  1 
ATOM   6568  O  OD1 . ASN C  1 199 ? 38.506  -24.748 23.213  1.00 27.50 ? 202  ASN C OD1 1 
ATOM   6569  N  ND2 . ASN C  1 199 ? 36.803  -24.637 21.759  1.00 23.48 ? 202  ASN C ND2 1 
ATOM   6570  N  N   . LEU C  1 200 ? 41.164  -27.717 19.765  1.00 19.11 ? 203  LEU C N   1 
ATOM   6571  C  CA  . LEU C  1 200 ? 41.355  -28.879 18.864  1.00 23.40 ? 203  LEU C CA  1 
ATOM   6572  C  C   . LEU C  1 200 ? 42.779  -29.119 18.331  1.00 24.51 ? 203  LEU C C   1 
ATOM   6573  O  O   . LEU C  1 200 ? 43.146  -30.273 18.015  1.00 23.35 ? 203  LEU C O   1 
ATOM   6574  C  CB  . LEU C  1 200 ? 40.370  -28.841 17.683  1.00 22.12 ? 203  LEU C CB  1 
ATOM   6575  C  CG  . LEU C  1 200 ? 38.918  -29.000 18.169  1.00 20.81 ? 203  LEU C CG  1 
ATOM   6576  C  CD1 . LEU C  1 200 ? 37.959  -28.032 17.467  1.00 22.15 ? 203  LEU C CD1 1 
ATOM   6577  C  CD2 . LEU C  1 200 ? 38.431  -30.437 18.076  1.00 19.30 ? 203  LEU C CD2 1 
ATOM   6578  N  N   . PHE C  1 201 ? 43.554  -28.041 18.198  1.00 20.25 ? 204  PHE C N   1 
ATOM   6579  C  CA  . PHE C  1 201 ? 44.954  -28.148 17.784  1.00 23.80 ? 204  PHE C CA  1 
ATOM   6580  C  C   . PHE C  1 201 ? 45.895  -28.302 19.005  1.00 24.73 ? 204  PHE C C   1 
ATOM   6581  O  O   . PHE C  1 201 ? 47.112  -28.443 18.846  1.00 27.10 ? 204  PHE C O   1 
ATOM   6582  C  CB  . PHE C  1 201 ? 45.384  -26.924 16.935  1.00 21.14 ? 204  PHE C CB  1 
ATOM   6583  C  CG  . PHE C  1 201 ? 44.773  -26.873 15.543  1.00 21.62 ? 204  PHE C CG  1 
ATOM   6584  C  CD1 . PHE C  1 201 ? 44.224  -28.010 14.955  1.00 19.81 ? 204  PHE C CD1 1 
ATOM   6585  C  CD2 . PHE C  1 201 ? 44.830  -25.688 14.787  1.00 20.48 ? 204  PHE C CD2 1 
ATOM   6586  C  CE1 . PHE C  1 201 ? 43.686  -27.958 13.656  1.00 19.41 ? 204  PHE C CE1 1 
ATOM   6587  C  CE2 . PHE C  1 201 ? 44.270  -25.612 13.510  1.00 16.83 ? 204  PHE C CE2 1 
ATOM   6588  C  CZ  . PHE C  1 201 ? 43.679  -26.760 12.949  1.00 19.83 ? 204  PHE C CZ  1 
ATOM   6589  N  N   . VAL C  1 202 ? 45.347  -28.195 20.214  1.00 25.67 ? 205  VAL C N   1 
ATOM   6590  C  CA  . VAL C  1 202 ? 46.111  -28.452 21.445  1.00 23.62 ? 205  VAL C CA  1 
ATOM   6591  C  C   . VAL C  1 202 ? 46.143  -29.959 21.720  1.00 22.81 ? 205  VAL C C   1 
ATOM   6592  O  O   . VAL C  1 202 ? 45.113  -30.607 21.685  1.00 25.38 ? 205  VAL C O   1 
ATOM   6593  C  CB  . VAL C  1 202 ? 45.508  -27.686 22.669  1.00 25.22 ? 205  VAL C CB  1 
ATOM   6594  C  CG1 . VAL C  1 202 ? 46.107  -28.188 23.991  1.00 23.64 ? 205  VAL C CG1 1 
ATOM   6595  C  CG2 . VAL C  1 202 ? 45.725  -26.169 22.539  1.00 24.22 ? 205  VAL C CG2 1 
ATOM   6596  N  N   . ASP C  1 203 ? 47.332  -30.523 21.932  1.00 24.11 ? 206  ASP C N   1 
ATOM   6597  C  CA  . ASP C  1 203 ? 47.483  -31.967 22.128  1.00 23.35 ? 206  ASP C CA  1 
ATOM   6598  C  C   . ASP C  1 203 ? 46.593  -32.475 23.257  1.00 24.02 ? 206  ASP C C   1 
ATOM   6599  O  O   . ASP C  1 203 ? 46.478  -31.841 24.314  1.00 24.17 ? 206  ASP C O   1 
ATOM   6600  C  CB  . ASP C  1 203 ? 48.968  -32.336 22.369  1.00 25.90 ? 206  ASP C CB  1 
ATOM   6601  C  CG  . ASP C  1 203 ? 49.192  -33.846 22.537  1.00 25.19 ? 206  ASP C CG  1 
ATOM   6602  O  OD1 . ASP C  1 203 ? 48.766  -34.407 23.568  1.00 26.22 ? 206  ASP C OD1 1 
ATOM   6603  O  OD2 . ASP C  1 203 ? 49.784  -34.480 21.637  1.00 23.25 ? 206  ASP C OD2 1 
ATOM   6604  N  N   . GLY C  1 204 ? 45.949  -33.614 23.027  1.00 23.01 ? 207  GLY C N   1 
ATOM   6605  C  CA  . GLY C  1 204 ? 44.809  -34.031 23.839  1.00 27.11 ? 207  GLY C CA  1 
ATOM   6606  C  C   . GLY C  1 204 ? 45.151  -34.672 25.174  1.00 32.02 ? 207  GLY C C   1 
ATOM   6607  O  O   . GLY C  1 204 ? 44.285  -34.821 26.039  1.00 32.10 ? 207  GLY C O   1 
ATOM   6608  N  N   . ARG C  1 205 ? 46.405  -35.081 25.340  1.00 34.09 ? 208  ARG C N   1 
ATOM   6609  C  CA  . ARG C  1 205 ? 46.900  -35.510 26.643  1.00 34.05 ? 208  ARG C CA  1 
ATOM   6610  C  C   . ARG C  1 205 ? 46.969  -34.324 27.599  1.00 34.78 ? 208  ARG C C   1 
ATOM   6611  O  O   . ARG C  1 205 ? 46.804  -34.485 28.805  1.00 36.81 ? 208  ARG C O   1 
ATOM   6612  C  CB  . ARG C  1 205 ? 48.282  -36.169 26.508  1.00 33.51 ? 208  ARG C CB  1 
ATOM   6613  C  CG  . ARG C  1 205 ? 48.245  -37.543 25.832  1.00 33.39 ? 208  ARG C CG  1 
ATOM   6614  C  CD  . ARG C  1 205 ? 49.606  -37.899 25.237  1.00 34.22 ? 208  ARG C CD  1 
ATOM   6615  N  NE  . ARG C  1 205 ? 50.089  -36.916 24.267  1.00 31.43 ? 208  ARG C NE  1 
ATOM   6616  C  CZ  . ARG C  1 205 ? 51.109  -37.130 23.438  1.00 30.67 ? 208  ARG C CZ  1 
ATOM   6617  N  NH1 . ARG C  1 205 ? 51.770  -38.283 23.501  1.00 30.14 ? 208  ARG C NH1 1 
ATOM   6618  N  NH2 . ARG C  1 205 ? 51.523  -36.167 22.610  1.00 26.18 ? 208  ARG C NH2 1 
ATOM   6619  N  N   . ARG C  1 206 ? 47.257  -33.143 27.059  1.00 34.62 ? 209  ARG C N   1 
ATOM   6620  C  CA  . ARG C  1 206 ? 47.197  -31.910 27.837  1.00 34.89 ? 209  ARG C CA  1 
ATOM   6621  C  C   . ARG C  1 206 ? 45.784  -31.316 27.890  1.00 33.46 ? 209  ARG C C   1 
ATOM   6622  O  O   . ARG C  1 206 ? 45.259  -31.071 28.965  1.00 32.59 ? 209  ARG C O   1 
ATOM   6623  C  CB  . ARG C  1 206 ? 48.199  -30.880 27.304  1.00 37.59 ? 209  ARG C CB  1 
ATOM   6624  C  CG  . ARG C  1 206 ? 48.672  -29.882 28.366  1.00 41.57 ? 209  ARG C CG  1 
ATOM   6625  C  CD  . ARG C  1 206 ? 49.729  -28.906 27.846  1.00 42.82 ? 209  ARG C CD  1 
ATOM   6626  N  NE  . ARG C  1 206 ? 50.297  -29.345 26.581  1.00 44.32 ? 209  ARG C NE  1 
ATOM   6627  C  CZ  . ARG C  1 206 ? 50.199  -28.674 25.438  1.00 44.33 ? 209  ARG C CZ  1 
ATOM   6628  N  NH1 . ARG C  1 206 ? 49.584  -27.499 25.396  1.00 42.45 ? 209  ARG C NH1 1 
ATOM   6629  N  NH2 . ARG C  1 206 ? 50.727  -29.186 24.333  1.00 46.72 ? 209  ARG C NH2 1 
ATOM   6630  N  N   . ASP C  1 207 ? 45.175  -31.089 26.725  1.00 34.69 ? 210  ASP C N   1 
ATOM   6631  C  CA  . ASP C  1 207 ? 43.853  -30.425 26.619  1.00 33.47 ? 210  ASP C CA  1 
ATOM   6632  C  C   . ASP C  1 207 ? 43.668  -29.207 27.530  1.00 32.28 ? 210  ASP C C   1 
ATOM   6633  O  O   . ASP C  1 207 ? 42.649  -29.093 28.213  1.00 32.59 ? 210  ASP C O   1 
ATOM   6634  C  CB  . ASP C  1 207 ? 42.709  -31.436 26.832  1.00 35.96 ? 210  ASP C CB  1 
ATOM   6635  C  CG  . ASP C  1 207 ? 41.322  -30.835 26.547  1.00 38.99 ? 210  ASP C CG  1 
ATOM   6636  O  OD1 . ASP C  1 207 ? 41.228  -29.866 25.749  1.00 38.89 ? 210  ASP C OD1 1 
ATOM   6637  O  OD2 . ASP C  1 207 ? 40.328  -31.330 27.126  1.00 36.07 ? 210  ASP C OD2 1 
ATOM   6638  N  N   . ASP C  1 208 ? 44.611  -28.267 27.486  1.00 30.60 ? 211  ASP C N   1 
ATOM   6639  C  CA  . ASP C  1 208 ? 44.645  -27.178 28.463  1.00 30.72 ? 211  ASP C CA  1 
ATOM   6640  C  C   . ASP C  1 208 ? 44.377  -25.805 27.844  1.00 28.81 ? 211  ASP C C   1 
ATOM   6641  O  O   . ASP C  1 208 ? 44.555  -24.765 28.502  1.00 24.87 ? 211  ASP C O   1 
ATOM   6642  C  CB  . ASP C  1 208 ? 45.988  -27.151 29.202  1.00 34.73 ? 211  ASP C CB  1 
ATOM   6643  C  CG  . ASP C  1 208 ? 47.162  -26.834 28.278  1.00 37.70 ? 211  ASP C CG  1 
ATOM   6644  O  OD1 . ASP C  1 208 ? 46.984  -26.798 27.040  1.00 40.31 ? 211  ASP C OD1 1 
ATOM   6645  O  OD2 . ASP C  1 208 ? 48.275  -26.620 28.790  1.00 41.39 ? 211  ASP C OD2 1 
ATOM   6646  N  N   . GLY C  1 209 ? 43.987  -25.805 26.570  1.00 26.73 ? 212  GLY C N   1 
ATOM   6647  C  CA  . GLY C  1 209 ? 43.567  -24.581 25.902  1.00 23.56 ? 212  GLY C CA  1 
ATOM   6648  C  C   . GLY C  1 209 ? 44.671  -23.574 25.631  1.00 25.18 ? 212  GLY C C   1 
ATOM   6649  O  O   . GLY C  1 209 ? 44.383  -22.410 25.341  1.00 24.51 ? 212  GLY C O   1 
ATOM   6650  N  N   . GLN C  1 210 ? 45.930  -24.009 25.744  1.00 23.40 ? 213  GLN C N   1 
ATOM   6651  C  CA  . GLN C  1 210 ? 47.090  -23.150 25.434  1.00 24.11 ? 213  GLN C CA  1 
ATOM   6652  C  C   . GLN C  1 210 ? 47.883  -23.714 24.263  1.00 25.61 ? 213  GLN C C   1 
ATOM   6653  O  O   . GLN C  1 210 ? 48.559  -24.748 24.383  1.00 26.80 ? 213  GLN C O   1 
ATOM   6654  C  CB  . GLN C  1 210 ? 48.012  -23.006 26.661  1.00 20.48 ? 213  GLN C CB  1 
ATOM   6655  C  CG  . GLN C  1 210 ? 47.261  -22.911 27.983  1.00 22.67 ? 213  GLN C CG  1 
ATOM   6656  C  CD  . GLN C  1 210 ? 46.445  -21.625 28.108  1.00 23.73 ? 213  GLN C CD  1 
ATOM   6657  O  OE1 . GLN C  1 210 ? 46.943  -20.530 27.844  1.00 17.66 ? 213  GLN C OE1 1 
ATOM   6658  N  NE2 . GLN C  1 210 ? 45.198  -21.756 28.548  1.00 25.30 ? 213  GLN C NE2 1 
ATOM   6659  N  N   . LEU C  1 211 ? 47.708  -23.116 23.096  1.00 26.68 ? 214  LEU C N   1 
ATOM   6660  C  CA  . LEU C  1 211 ? 48.298  -23.685 21.889  1.00 25.73 ? 214  LEU C CA  1 
ATOM   6661  C  C   . LEU C  1 211 ? 49.628  -23.012 21.600  1.00 24.76 ? 214  LEU C C   1 
ATOM   6662  O  O   . LEU C  1 211 ? 49.692  -21.794 21.491  1.00 22.31 ? 214  LEU C O   1 
ATOM   6663  C  CB  . LEU C  1 211 ? 47.341  -23.531 20.701  1.00 23.67 ? 214  LEU C CB  1 
ATOM   6664  C  CG  . LEU C  1 211 ? 47.875  -23.982 19.344  1.00 24.33 ? 214  LEU C CG  1 
ATOM   6665  C  CD1 . LEU C  1 211 ? 48.167  -25.469 19.328  1.00 22.80 ? 214  LEU C CD1 1 
ATOM   6666  C  CD2 . LEU C  1 211 ? 46.893  -23.607 18.242  1.00 23.78 ? 214  LEU C CD2 1 
ATOM   6667  N  N   . ASP C  1 212 ? 50.691  -23.802 21.461  1.00 26.60 ? 215  ASP C N   1 
ATOM   6668  C  CA  . ASP C  1 212 ? 52.005  -23.216 21.170  1.00 27.60 ? 215  ASP C CA  1 
ATOM   6669  C  C   . ASP C  1 212 ? 52.215  -22.811 19.713  1.00 26.02 ? 215  ASP C C   1 
ATOM   6670  O  O   . ASP C  1 212 ? 51.544  -23.303 18.801  1.00 20.53 ? 215  ASP C O   1 
ATOM   6671  C  CB  . ASP C  1 212 ? 53.162  -24.094 21.701  1.00 29.98 ? 215  ASP C CB  1 
ATOM   6672  C  CG  . ASP C  1 212 ? 53.344  -25.374 20.917  1.00 31.13 ? 215  ASP C CG  1 
ATOM   6673  O  OD1 . ASP C  1 212 ? 53.750  -25.305 19.727  1.00 31.70 ? 215  ASP C OD1 1 
ATOM   6674  O  OD2 . ASP C  1 212 ? 53.182  -26.452 21.527  1.00 32.51 ? 215  ASP C OD2 1 
ATOM   6675  N  N   . MET C  1 213 ? 53.143  -21.886 19.500  1.00 27.61 ? 216  MET C N   1 
ATOM   6676  C  CA  . MET C  1 213 ? 53.295  -21.260 18.196  1.00 26.39 ? 216  MET C CA  1 
ATOM   6677  C  C   . MET C  1 213 ? 53.928  -22.205 17.181  1.00 28.13 ? 216  MET C C   1 
ATOM   6678  O  O   . MET C  1 213 ? 53.819  -21.997 15.971  1.00 29.54 ? 216  MET C O   1 
ATOM   6679  C  CB  . MET C  1 213 ? 54.088  -19.955 18.314  1.00 25.95 ? 216  MET C CB  1 
ATOM   6680  C  CG  . MET C  1 213 ? 53.292  -18.809 18.958  1.00 29.48 ? 216  MET C CG  1 
ATOM   6681  S  SD  . MET C  1 213 ? 51.682  -18.502 18.156  1.00 31.01 ? 216  MET C SD  1 
ATOM   6682  C  CE  . MET C  1 213 ? 50.601  -19.398 19.288  1.00 33.19 ? 216  MET C CE  1 
ATOM   6683  N  N   . ASP C  1 214 ? 54.514  -23.293 17.662  1.00 26.93 ? 217  ASP C N   1 
ATOM   6684  C  CA  . ASP C  1 214 ? 54.974  -24.346 16.760  1.00 30.78 ? 217  ASP C CA  1 
ATOM   6685  C  C   . ASP C  1 214 ? 53.831  -25.193 16.192  1.00 28.17 ? 217  ASP C C   1 
ATOM   6686  O  O   . ASP C  1 214 ? 53.753  -25.420 14.986  1.00 27.24 ? 217  ASP C O   1 
ATOM   6687  C  CB  . ASP C  1 214 ? 55.970  -25.258 17.475  1.00 37.11 ? 217  ASP C CB  1 
ATOM   6688  C  CG  . ASP C  1 214 ? 57.369  -25.108 16.932  1.00 45.29 ? 217  ASP C CG  1 
ATOM   6689  O  OD1 . ASP C  1 214 ? 57.685  -25.802 15.928  1.00 51.12 ? 217  ASP C OD1 1 
ATOM   6690  O  OD2 . ASP C  1 214 ? 58.110  -24.231 17.435  1.00 44.47 ? 217  ASP C OD2 1 
ATOM   6691  N  N   . ALA C  1 215 ? 53.022  -25.749 17.086  1.00 25.76 ? 218  ALA C N   1 
ATOM   6692  C  CA  . ALA C  1 215 ? 51.797  -26.431 16.705  1.00 26.01 ? 218  ALA C CA  1 
ATOM   6693  C  C   . ALA C  1 215 ? 50.885  -25.562 15.831  1.00 25.28 ? 218  ALA C C   1 
ATOM   6694  O  O   . ALA C  1 215 ? 50.336  -26.035 14.836  1.00 25.73 ? 218  ALA C O   1 
ATOM   6695  C  CB  . ALA C  1 215 ? 51.056  -26.926 17.949  1.00 27.02 ? 218  ALA C CB  1 
ATOM   6696  N  N   . ALA C  1 216 ? 50.804  -24.273 16.145  1.00 22.84 ? 219  ALA C N   1 
ATOM   6697  C  CA  . ALA C  1 216 ? 49.990  -23.365 15.361  1.00 20.19 ? 219  ALA C CA  1 
ATOM   6698  C  C   . ALA C  1 216 ? 50.493  -23.255 13.921  1.00 24.89 ? 219  ALA C C   1 
ATOM   6699  O  O   . ALA C  1 216 ? 49.727  -23.483 12.963  1.00 22.25 ? 219  ALA C O   1 
ATOM   6700  C  CB  . ALA C  1 216 ? 49.902  -21.982 16.027  1.00 12.28 ? 219  ALA C CB  1 
ATOM   6701  N  N   . ARG C  1 217 ? 51.772  -22.918 13.758  1.00 24.76 ? 220  ARG C N   1 
ATOM   6702  C  CA  . ARG C  1 217 ? 52.309  -22.717 12.408  1.00 27.59 ? 220  ARG C CA  1 
ATOM   6703  C  C   . ARG C  1 217 ? 52.187  -24.003 11.610  1.00 29.19 ? 220  ARG C C   1 
ATOM   6704  O  O   . ARG C  1 217 ? 51.904  -23.990 10.418  1.00 30.09 ? 220  ARG C O   1 
ATOM   6705  C  CB  . ARG C  1 217 ? 53.777  -22.308 12.442  1.00 26.48 ? 220  ARG C CB  1 
ATOM   6706  C  CG  . ARG C  1 217 ? 54.425  -22.274 11.062  1.00 25.97 ? 220  ARG C CG  1 
ATOM   6707  C  CD  . ARG C  1 217 ? 55.888  -21.871 11.168  1.00 23.16 ? 220  ARG C CD  1 
ATOM   6708  N  NE  . ARG C  1 217 ? 56.040  -20.503 11.656  1.00 23.75 ? 220  ARG C NE  1 
ATOM   6709  C  CZ  . ARG C  1 217 ? 55.884  -19.416 10.911  1.00 23.16 ? 220  ARG C CZ  1 
ATOM   6710  N  NH1 . ARG C  1 217 ? 55.494  -19.517 9.649   1.00 24.81 ? 220  ARG C NH1 1 
ATOM   6711  N  NH2 . ARG C  1 217 ? 56.084  -18.222 11.438  1.00 25.55 ? 220  ARG C NH2 1 
ATOM   6712  N  N   . SER C  1 218 ? 52.457  -25.114 12.279  1.00 27.44 ? 221  SER C N   1 
ATOM   6713  C  CA  . SER C  1 218 ? 52.382  -26.409 11.660  1.00 27.36 ? 221  SER C CA  1 
ATOM   6714  C  C   . SER C  1 218 ? 50.994  -26.646 11.011  1.00 28.77 ? 221  SER C C   1 
ATOM   6715  O  O   . SER C  1 218 ? 50.898  -27.005 9.833   1.00 29.45 ? 221  SER C O   1 
ATOM   6716  C  CB  . SER C  1 218 ? 52.668  -27.463 12.730  1.00 27.41 ? 221  SER C CB  1 
ATOM   6717  O  OG  . SER C  1 218 ? 52.857  -28.731 12.156  1.00 29.47 ? 221  SER C OG  1 
ATOM   6718  N  N   . PHE C  1 219 ? 49.934  -26.500 11.804  1.00 26.56 ? 222  PHE C N   1 
ATOM   6719  C  CA  . PHE C  1 219 ? 48.555  -26.598 11.304  1.00 25.90 ? 222  PHE C CA  1 
ATOM   6720  C  C   . PHE C  1 219 ? 48.227  -25.509 10.281  1.00 24.58 ? 222  PHE C C   1 
ATOM   6721  O  O   . PHE C  1 219 ? 47.864  -25.809 9.158   1.00 26.72 ? 222  PHE C O   1 
ATOM   6722  C  CB  . PHE C  1 219 ? 47.561  -26.531 12.468  1.00 23.16 ? 222  PHE C CB  1 
ATOM   6723  C  CG  . PHE C  1 219 ? 47.467  -27.800 13.265  1.00 24.68 ? 222  PHE C CG  1 
ATOM   6724  C  CD1 . PHE C  1 219 ? 46.882  -28.939 12.721  1.00 23.86 ? 222  PHE C CD1 1 
ATOM   6725  C  CD2 . PHE C  1 219 ? 47.887  -27.837 14.581  1.00 24.34 ? 222  PHE C CD2 1 
ATOM   6726  C  CE1 . PHE C  1 219 ? 46.713  -30.095 13.492  1.00 23.75 ? 222  PHE C CE1 1 
ATOM   6727  C  CE2 . PHE C  1 219 ? 47.680  -28.975 15.359  1.00 23.18 ? 222  PHE C CE2 1 
ATOM   6728  C  CZ  . PHE C  1 219 ? 47.106  -30.106 14.805  1.00 21.79 ? 222  PHE C CZ  1 
ATOM   6729  N  N   . PHE C  1 220 ? 48.398  -24.244 10.656  1.00 24.50 ? 223  PHE C N   1 
ATOM   6730  C  CA  . PHE C  1 220 ? 47.984  -23.150 9.788   1.00 23.85 ? 223  PHE C CA  1 
ATOM   6731  C  C   . PHE C  1 220 ? 48.717  -23.091 8.450   1.00 25.47 ? 223  PHE C C   1 
ATOM   6732  O  O   . PHE C  1 220 ? 48.112  -22.754 7.439   1.00 21.00 ? 223  PHE C O   1 
ATOM   6733  C  CB  . PHE C  1 220 ? 48.051  -21.801 10.501  1.00 22.66 ? 223  PHE C CB  1 
ATOM   6734  C  CG  . PHE C  1 220 ? 46.932  -21.575 11.487  1.00 25.67 ? 223  PHE C CG  1 
ATOM   6735  C  CD1 . PHE C  1 220 ? 45.640  -21.292 11.045  1.00 26.72 ? 223  PHE C CD1 1 
ATOM   6736  C  CD2 . PHE C  1 220 ? 47.180  -21.591 12.858  1.00 25.65 ? 223  PHE C CD2 1 
ATOM   6737  C  CE1 . PHE C  1 220 ? 44.614  -21.030 11.958  1.00 25.75 ? 223  PHE C CE1 1 
ATOM   6738  C  CE2 . PHE C  1 220 ? 46.165  -21.341 13.774  1.00 27.86 ? 223  PHE C CE2 1 
ATOM   6739  C  CZ  . PHE C  1 220 ? 44.869  -21.080 13.321  1.00 26.85 ? 223  PHE C CZ  1 
ATOM   6740  N  N   . GLN C  1 221 ? 50.022  -23.368 8.457   1.00 26.94 ? 224  GLN C N   1 
ATOM   6741  C  CA  . GLN C  1 221 ? 50.856  -23.179 7.265   1.00 26.08 ? 224  GLN C CA  1 
ATOM   6742  C  C   . GLN C  1 221 ? 51.094  -24.456 6.458   1.00 24.51 ? 224  GLN C C   1 
ATOM   6743  O  O   . GLN C  1 221 ? 50.952  -24.465 5.221   1.00 25.53 ? 224  GLN C O   1 
ATOM   6744  C  CB  . GLN C  1 221 ? 52.197  -22.492 7.611   1.00 25.50 ? 224  GLN C CB  1 
ATOM   6745  C  CG  . GLN C  1 221 ? 53.187  -22.469 6.423   1.00 24.92 ? 224  GLN C CG  1 
ATOM   6746  C  CD  . GLN C  1 221 ? 54.403  -21.582 6.647   1.00 23.92 ? 224  GLN C CD  1 
ATOM   6747  O  OE1 . GLN C  1 221 ? 54.871  -21.408 7.776   1.00 24.29 ? 224  GLN C OE1 1 
ATOM   6748  N  NE2 . GLN C  1 221 ? 54.892  -20.980 5.568   1.00 23.10 ? 224  GLN C NE2 1 
ATOM   6749  N  N   . PHE C  1 222 ? 51.472  -25.529 7.138   1.00 22.52 ? 225  PHE C N   1 
ATOM   6750  C  CA  . PHE C  1 222 ? 51.873  -26.757 6.428   1.00 27.36 ? 225  PHE C CA  1 
ATOM   6751  C  C   . PHE C  1 222 ? 50.836  -27.881 6.401   1.00 26.28 ? 225  PHE C C   1 
ATOM   6752  O  O   . PHE C  1 222 ? 51.046  -28.918 5.760   1.00 26.90 ? 225  PHE C O   1 
ATOM   6753  C  CB  . PHE C  1 222 ? 53.235  -27.258 6.940   1.00 30.42 ? 225  PHE C CB  1 
ATOM   6754  C  CG  . PHE C  1 222 ? 54.375  -26.309 6.637   1.00 34.19 ? 225  PHE C CG  1 
ATOM   6755  C  CD1 . PHE C  1 222 ? 54.765  -26.077 5.324   1.00 35.08 ? 225  PHE C CD1 1 
ATOM   6756  C  CD2 . PHE C  1 222 ? 54.978  -25.572 7.656   1.00 35.38 ? 225  PHE C CD2 1 
ATOM   6757  C  CE1 . PHE C  1 222 ? 55.796  -25.167 5.024   1.00 37.44 ? 225  PHE C CE1 1 
ATOM   6758  C  CE2 . PHE C  1 222 ? 56.007  -24.654 7.373   1.00 37.33 ? 225  PHE C CE2 1 
ATOM   6759  C  CZ  . PHE C  1 222 ? 56.399  -24.440 6.046   1.00 37.70 ? 225  PHE C CZ  1 
ATOM   6760  N  N   . SER C  1 223 ? 49.699  -27.661 7.054   1.00 23.14 ? 226  SER C N   1 
ATOM   6761  C  CA  . SER C  1 223 ? 48.673  -28.705 7.185   1.00 25.47 ? 226  SER C CA  1 
ATOM   6762  C  C   . SER C  1 223 ? 49.207  -29.966 7.838   1.00 23.69 ? 226  SER C C   1 
ATOM   6763  O  O   . SER C  1 223 ? 48.827  -31.070 7.466   1.00 24.81 ? 226  SER C O   1 
ATOM   6764  C  CB  . SER C  1 223 ? 48.034  -29.053 5.836   1.00 21.49 ? 226  SER C CB  1 
ATOM   6765  O  OG  . SER C  1 223 ? 47.787  -27.873 5.069   1.00 24.57 ? 226  SER C OG  1 
ATOM   6766  N  N   . ARG C  1 224 ? 50.039  -29.802 8.859   1.00 23.97 ? 227  ARG C N   1 
ATOM   6767  C  CA  . ARG C  1 224 ? 50.747  -30.942 9.430   1.00 23.98 ? 227  ARG C CA  1 
ATOM   6768  C  C   . ARG C  1 224 ? 50.500  -31.065 10.932  1.00 22.17 ? 227  ARG C C   1 
ATOM   6769  O  O   . ARG C  1 224 ? 50.711  -30.122 11.678  1.00 23.30 ? 227  ARG C O   1 
ATOM   6770  C  CB  . ARG C  1 224 ? 52.246  -30.830 9.144   1.00 25.35 ? 227  ARG C CB  1 
ATOM   6771  C  CG  . ARG C  1 224 ? 53.067  -32.035 9.616   1.00 30.54 ? 227  ARG C CG  1 
ATOM   6772  C  CD  . ARG C  1 224 ? 54.420  -32.121 8.882   1.00 31.64 ? 227  ARG C CD  1 
ATOM   6773  N  NE  . ARG C  1 224 ? 55.234  -30.924 9.090   1.00 35.99 ? 227  ARG C NE  1 
ATOM   6774  C  CZ  . ARG C  1 224 ? 55.684  -30.127 8.118   1.00 37.76 ? 227  ARG C CZ  1 
ATOM   6775  N  NH1 . ARG C  1 224 ? 55.418  -30.391 6.848   1.00 40.28 ? 227  ARG C NH1 1 
ATOM   6776  N  NH2 . ARG C  1 224 ? 56.417  -29.067 8.412   1.00 37.60 ? 227  ARG C NH2 1 
ATOM   6777  N  N   . MET C  1 225 ? 50.092  -32.234 11.391  1.00 22.94 ? 228  MET C N   1 
ATOM   6778  C  CA  . MET C  1 225 ? 50.026  -32.418 12.832  1.00 30.30 ? 228  MET C CA  1 
ATOM   6779  C  C   . MET C  1 225 ? 51.420  -32.372 13.445  1.00 31.67 ? 228  MET C C   1 
ATOM   6780  O  O   . MET C  1 225 ? 52.408  -32.616 12.766  1.00 34.29 ? 228  MET C O   1 
ATOM   6781  C  CB  . MET C  1 225 ? 49.322  -33.715 13.197  1.00 30.03 ? 228  MET C CB  1 
ATOM   6782  C  CG  . MET C  1 225 ? 47.960  -33.849 12.557  1.00 29.47 ? 228  MET C CG  1 
ATOM   6783  S  SD  . MET C  1 225 ? 47.412  -35.525 12.762  1.00 29.10 ? 228  MET C SD  1 
ATOM   6784  C  CE  . MET C  1 225 ? 45.644  -35.365 12.487  1.00 30.93 ? 228  MET C CE  1 
ATOM   6785  N  N   . PRO C  1 226 ? 51.500  -32.020 14.728  1.00 33.21 ? 229  PRO C N   1 
ATOM   6786  C  CA  . PRO C  1 226 ? 52.770  -32.198 15.433  1.00 33.04 ? 229  PRO C CA  1 
ATOM   6787  C  C   . PRO C  1 226 ? 53.116  -33.679 15.564  1.00 33.49 ? 229  PRO C C   1 
ATOM   6788  O  O   . PRO C  1 226 ? 52.222  -34.526 15.572  1.00 28.44 ? 229  PRO C O   1 
ATOM   6789  C  CB  . PRO C  1 226 ? 52.481  -31.602 16.812  1.00 30.60 ? 229  PRO C CB  1 
ATOM   6790  C  CG  . PRO C  1 226 ? 51.468  -30.543 16.539  1.00 32.75 ? 229  PRO C CG  1 
ATOM   6791  C  CD  . PRO C  1 226 ? 50.599  -31.083 15.421  1.00 31.55 ? 229  PRO C CD  1 
ATOM   6792  N  N   . ASP C  1 227 ? 54.403  -33.977 15.736  1.00 37.39 ? 230  ASP C N   1 
ATOM   6793  C  CA  . ASP C  1 227 ? 54.859  -35.340 15.984  1.00 38.20 ? 230  ASP C CA  1 
ATOM   6794  C  C   . ASP C  1 227 ? 54.124  -35.926 17.179  1.00 35.49 ? 230  ASP C C   1 
ATOM   6795  O  O   . ASP C  1 227 ? 53.996  -35.265 18.204  1.00 34.21 ? 230  ASP C O   1 
ATOM   6796  C  CB  . ASP C  1 227 ? 56.353  -35.329 16.282  1.00 45.82 ? 230  ASP C CB  1 
ATOM   6797  C  CG  . ASP C  1 227 ? 57.189  -35.442 15.035  1.00 52.52 ? 230  ASP C CG  1 
ATOM   6798  O  OD1 . ASP C  1 227 ? 57.077  -36.484 14.350  1.00 55.24 ? 230  ASP C OD1 1 
ATOM   6799  O  OD2 . ASP C  1 227 ? 57.944  -34.484 14.729  1.00 55.94 ? 230  ASP C OD2 1 
ATOM   6800  N  N   . ASP C  1 228 ? 53.649  -37.161 17.050  1.00 31.44 ? 231  ASP C N   1 
ATOM   6801  C  CA  . ASP C  1 228 ? 53.074  -37.866 18.195  1.00 34.04 ? 231  ASP C CA  1 
ATOM   6802  C  C   . ASP C  1 228 ? 51.769  -37.197 18.665  1.00 33.36 ? 231  ASP C C   1 
ATOM   6803  O  O   . ASP C  1 228 ? 51.257  -37.514 19.746  1.00 32.07 ? 231  ASP C O   1 
ATOM   6804  C  CB  . ASP C  1 228 ? 54.107  -37.921 19.341  1.00 32.86 ? 231  ASP C CB  1 
ATOM   6805  C  CG  . ASP C  1 228 ? 53.679  -38.829 20.489  1.00 32.19 ? 231  ASP C CG  1 
ATOM   6806  O  OD1 . ASP C  1 228 ? 53.217  -39.955 20.234  1.00 35.19 ? 231  ASP C OD1 1 
ATOM   6807  O  OD2 . ASP C  1 228 ? 53.828  -38.429 21.661  1.00 31.61 ? 231  ASP C OD2 1 
ATOM   6808  N  N   . PHE C  1 229 ? 51.238  -36.277 17.855  1.00 34.93 ? 232  PHE C N   1 
ATOM   6809  C  CA  . PHE C  1 229 ? 50.022  -35.517 18.214  1.00 33.72 ? 232  PHE C CA  1 
ATOM   6810  C  C   . PHE C  1 229 ? 48.890  -36.460 18.579  1.00 33.72 ? 232  PHE C C   1 
ATOM   6811  O  O   . PHE C  1 229 ? 48.506  -37.324 17.784  1.00 36.53 ? 232  PHE C O   1 
ATOM   6812  C  CB  . PHE C  1 229 ? 49.566  -34.596 17.063  1.00 32.90 ? 232  PHE C CB  1 
ATOM   6813  C  CG  . PHE C  1 229 ? 48.381  -33.710 17.410  1.00 29.95 ? 232  PHE C CG  1 
ATOM   6814  C  CD1 . PHE C  1 229 ? 48.557  -32.551 18.146  1.00 29.51 ? 232  PHE C CD1 1 
ATOM   6815  C  CD2 . PHE C  1 229 ? 47.091  -34.067 17.038  1.00 30.43 ? 232  PHE C CD2 1 
ATOM   6816  C  CE1 . PHE C  1 229 ? 47.480  -31.756 18.502  1.00 28.20 ? 232  PHE C CE1 1 
ATOM   6817  C  CE2 . PHE C  1 229 ? 45.996  -33.251 17.357  1.00 28.30 ? 232  PHE C CE2 1 
ATOM   6818  C  CZ  . PHE C  1 229 ? 46.198  -32.088 18.080  1.00 28.03 ? 232  PHE C CZ  1 
ATOM   6819  N  N   . PHE C  1 230 ? 48.368  -36.300 19.790  1.00 32.88 ? 233  PHE C N   1 
ATOM   6820  C  CA  . PHE C  1 230 ? 47.106  -36.930 20.174  1.00 32.09 ? 233  PHE C CA  1 
ATOM   6821  C  C   . PHE C  1 230 ? 45.942  -35.960 19.933  1.00 33.51 ? 233  PHE C C   1 
ATOM   6822  O  O   . PHE C  1 230 ? 46.061  -34.753 20.188  1.00 31.09 ? 233  PHE C O   1 
ATOM   6823  C  CB  . PHE C  1 230 ? 47.140  -37.315 21.656  1.00 31.10 ? 233  PHE C CB  1 
ATOM   6824  C  CG  . PHE C  1 230 ? 47.798  -38.648 21.941  1.00 29.72 ? 233  PHE C CG  1 
ATOM   6825  C  CD1 . PHE C  1 230 ? 49.060  -38.952 21.427  1.00 30.19 ? 233  PHE C CD1 1 
ATOM   6826  C  CD2 . PHE C  1 230 ? 47.177  -39.572 22.775  1.00 29.11 ? 233  PHE C CD2 1 
ATOM   6827  C  CE1 . PHE C  1 230 ? 49.679  -40.185 21.720  1.00 29.50 ? 233  PHE C CE1 1 
ATOM   6828  C  CE2 . PHE C  1 230 ? 47.807  -40.800 23.099  1.00 30.51 ? 233  PHE C CE2 1 
ATOM   6829  C  CZ  . PHE C  1 230 ? 49.053  -41.098 22.564  1.00 28.74 ? 233  PHE C CZ  1 
ATOM   6830  N  N   . ARG C  1 231 ? 44.820  -36.495 19.460  1.00 31.60 ? 234  ARG C N   1 
ATOM   6831  C  CA  . ARG C  1 231 ? 43.599  -35.722 19.337  1.00 30.51 ? 234  ARG C CA  1 
ATOM   6832  C  C   . ARG C  1 231 ? 43.002  -35.440 20.721  1.00 29.78 ? 234  ARG C C   1 
ATOM   6833  O  O   . ARG C  1 231 ? 43.416  -36.038 21.706  1.00 30.58 ? 234  ARG C O   1 
ATOM   6834  C  CB  . ARG C  1 231 ? 42.592  -36.468 18.459  1.00 29.11 ? 234  ARG C CB  1 
ATOM   6835  C  CG  . ARG C  1 231 ? 41.905  -37.585 19.193  1.00 28.10 ? 234  ARG C CG  1 
ATOM   6836  C  CD  . ARG C  1 231 ? 41.115  -38.508 18.297  1.00 24.57 ? 234  ARG C CD  1 
ATOM   6837  N  NE  . ARG C  1 231 ? 40.396  -39.470 19.122  1.00 21.29 ? 234  ARG C NE  1 
ATOM   6838  C  CZ  . ARG C  1 231 ? 39.550  -40.382 18.658  1.00 20.78 ? 234  ARG C CZ  1 
ATOM   6839  N  NH1 . ARG C  1 231 ? 39.304  -40.479 17.357  1.00 22.39 ? 234  ARG C NH1 1 
ATOM   6840  N  NH2 . ARG C  1 231 ? 38.909  -41.161 19.504  1.00 18.61 ? 234  ARG C NH2 1 
ATOM   6841  N  N   . ALA C  1 232 ? 42.083  -34.477 20.801  1.00 29.59 ? 235  ALA C N   1 
ATOM   6842  C  CA  . ALA C  1 232 ? 41.468  -34.108 22.073  1.00 28.43 ? 235  ALA C CA  1 
ATOM   6843  C  C   . ALA C  1 232 ? 40.736  -35.294 22.712  1.00 29.49 ? 235  ALA C C   1 
ATOM   6844  O  O   . ALA C  1 232 ? 40.341  -36.229 22.024  1.00 27.90 ? 235  ALA C O   1 
ATOM   6845  C  CB  . ALA C  1 232 ? 40.527  -32.934 21.880  1.00 29.04 ? 235  ALA C CB  1 
ATOM   6846  N  N   . PRO C  1 233 ? 40.582  -35.267 24.044  1.00 30.20 ? 236  PRO C N   1 
ATOM   6847  C  CA  . PRO C  1 233 ? 40.130  -36.435 24.790  1.00 30.31 ? 236  PRO C CA  1 
ATOM   6848  C  C   . PRO C  1 233 ? 38.620  -36.566 24.805  1.00 30.37 ? 236  PRO C C   1 
ATOM   6849  O  O   . PRO C  1 233 ? 38.089  -37.458 25.479  1.00 33.63 ? 236  PRO C O   1 
ATOM   6850  C  CB  . PRO C  1 233 ? 40.620  -36.148 26.210  1.00 31.30 ? 236  PRO C CB  1 
ATOM   6851  C  CG  . PRO C  1 233 ? 40.649  -34.656 26.291  1.00 27.23 ? 236  PRO C CG  1 
ATOM   6852  C  CD  . PRO C  1 233 ? 41.104  -34.216 24.929  1.00 28.80 ? 236  PRO C CD  1 
ATOM   6853  N  N   . SER C  1 234 ? 37.938  -35.674 24.093  1.00 27.50 ? 237  SER C N   1 
ATOM   6854  C  CA  . SER C  1 234 ? 36.482  -35.743 23.936  1.00 27.42 ? 237  SER C CA  1 
ATOM   6855  C  C   . SER C  1 234 ? 36.025  -34.953 22.708  1.00 26.67 ? 237  SER C C   1 
ATOM   6856  O  O   . SER C  1 234 ? 36.735  -34.058 22.235  1.00 27.01 ? 237  SER C O   1 
ATOM   6857  C  CB  . SER C  1 234 ? 35.793  -35.176 25.171  1.00 27.29 ? 237  SER C CB  1 
ATOM   6858  O  OG  . SER C  1 234 ? 36.071  -33.785 25.263  1.00 31.90 ? 237  SER C OG  1 
ATOM   6859  N  N   . PRO C  1 235 ? 34.800  -35.216 22.234  1.00 24.20 ? 238  PRO C N   1 
ATOM   6860  C  CA  . PRO C  1 235 ? 34.346  -34.432 21.080  1.00 22.51 ? 238  PRO C CA  1 
ATOM   6861  C  C   . PRO C  1 235 ? 34.080  -32.970 21.468  1.00 22.65 ? 238  PRO C C   1 
ATOM   6862  O  O   . PRO C  1 235 ? 33.515  -32.712 22.522  1.00 21.03 ? 238  PRO C O   1 
ATOM   6863  C  CB  . PRO C  1 235 ? 33.043  -35.139 20.657  1.00 23.86 ? 238  PRO C CB  1 
ATOM   6864  C  CG  . PRO C  1 235 ? 33.018  -36.478 21.447  1.00 24.29 ? 238  PRO C CG  1 
ATOM   6865  C  CD  . PRO C  1 235 ? 33.773  -36.153 22.717  1.00 22.38 ? 238  PRO C CD  1 
ATOM   6866  N  N   . ARG C  1 236 ? 34.547  -32.016 20.662  1.00 21.36 ? 239  ARG C N   1 
ATOM   6867  C  CA  . ARG C  1 236 ? 34.160  -30.624 20.853  1.00 18.22 ? 239  ARG C CA  1 
ATOM   6868  C  C   . ARG C  1 236 ? 34.356  -29.783 19.591  1.00 20.66 ? 239  ARG C C   1 
ATOM   6869  O  O   . ARG C  1 236 ? 34.925  -30.247 18.602  1.00 21.59 ? 239  ARG C O   1 
ATOM   6870  C  CB  . ARG C  1 236 ? 34.913  -29.998 22.036  1.00 16.91 ? 239  ARG C CB  1 
ATOM   6871  C  CG  . ARG C  1 236 ? 36.299  -29.514 21.677  1.00 18.64 ? 239  ARG C CG  1 
ATOM   6872  C  CD  . ARG C  1 236 ? 37.247  -30.716 21.535  1.00 23.53 ? 239  ARG C CD  1 
ATOM   6873  N  NE  . ARG C  1 236 ? 37.331  -31.454 22.799  1.00 23.31 ? 239  ARG C NE  1 
ATOM   6874  C  CZ  . ARG C  1 236 ? 38.131  -31.117 23.812  1.00 22.72 ? 239  ARG C CZ  1 
ATOM   6875  N  NH1 . ARG C  1 236 ? 39.020  -30.140 23.663  1.00 19.74 ? 239  ARG C NH1 1 
ATOM   6876  N  NH2 . ARG C  1 236 ? 38.130  -31.840 24.925  1.00 22.01 ? 239  ARG C NH2 1 
ATOM   6877  N  N   . SER C  1 237 ? 33.897  -28.536 19.649  1.00 18.88 ? 240  SER C N   1 
ATOM   6878  C  CA  . SER C  1 237 ? 34.114  -27.578 18.581  1.00 22.38 ? 240  SER C CA  1 
ATOM   6879  C  C   . SER C  1 237 ? 34.282  -26.184 19.172  1.00 22.48 ? 240  SER C C   1 
ATOM   6880  O  O   . SER C  1 237 ? 35.373  -25.821 19.605  1.00 25.26 ? 240  SER C O   1 
ATOM   6881  C  CB  . SER C  1 237 ? 32.941  -27.598 17.584  1.00 22.80 ? 240  SER C CB  1 
ATOM   6882  O  OG  . SER C  1 237 ? 31.719  -27.322 18.249  1.00 21.93 ? 240  SER C OG  1 
ATOM   6883  N  N   . GLY C  1 238 ? 33.197  -25.416 19.247  1.00 22.44 ? 241  GLY C N   1 
ATOM   6884  C  CA  . GLY C  1 238 ? 33.311  -23.998 19.594  1.00 20.75 ? 241  GLY C CA  1 
ATOM   6885  C  C   . GLY C  1 238 ? 32.979  -23.660 21.039  1.00 25.07 ? 241  GLY C C   1 
ATOM   6886  O  O   . GLY C  1 238 ? 32.606  -22.513 21.346  1.00 27.86 ? 241  GLY C O   1 
ATOM   6887  N  N   . THR C  1 239 ? 33.117  -24.637 21.933  1.00 23.54 ? 242  THR C N   1 
ATOM   6888  C  CA  . THR C  1 239 ? 33.045  -24.383 23.377  1.00 27.13 ? 242  THR C CA  1 
ATOM   6889  C  C   . THR C  1 239 ? 33.892  -23.166 23.718  1.00 24.70 ? 242  THR C C   1 
ATOM   6890  O  O   . THR C  1 239 ? 35.043  -23.074 23.276  1.00 20.96 ? 242  THR C O   1 
ATOM   6891  C  CB  . THR C  1 239 ? 33.625  -25.568 24.184  1.00 32.68 ? 242  THR C CB  1 
ATOM   6892  O  OG1 . THR C  1 239 ? 33.109  -26.799 23.660  1.00 37.75 ? 242  THR C OG1 1 
ATOM   6893  C  CG2 . THR C  1 239 ? 33.241  -25.454 25.655  1.00 35.37 ? 242  THR C CG2 1 
ATOM   6894  N  N   . GLY C  1 240 ? 33.333  -22.246 24.508  1.00 20.81 ? 243  GLY C N   1 
ATOM   6895  C  CA  . GLY C  1 240 ? 34.034  -21.003 24.855  1.00 17.96 ? 243  GLY C CA  1 
ATOM   6896  C  C   . GLY C  1 240 ? 33.812  -19.835 23.906  1.00 18.16 ? 243  GLY C C   1 
ATOM   6897  O  O   . GLY C  1 240 ? 34.371  -18.753 24.098  1.00 18.31 ? 243  GLY C O   1 
ATOM   6898  N  N   . VAL C  1 241 ? 32.948  -20.012 22.912  1.00 19.24 ? 244  VAL C N   1 
ATOM   6899  C  CA  . VAL C  1 241 ? 32.779  -18.975 21.889  1.00 16.47 ? 244  VAL C CA  1 
ATOM   6900  C  C   . VAL C  1 241 ? 32.200  -17.684 22.459  1.00 17.86 ? 244  VAL C C   1 
ATOM   6901  O  O   . VAL C  1 241 ? 32.520  -16.583 21.979  1.00 20.66 ? 244  VAL C O   1 
ATOM   6902  C  CB  . VAL C  1 241 ? 31.984  -19.481 20.655  1.00 18.49 ? 244  VAL C CB  1 
ATOM   6903  C  CG1 . VAL C  1 241 ? 30.529  -19.764 21.021  1.00 16.64 ? 244  VAL C CG1 1 
ATOM   6904  C  CG2 . VAL C  1 241 ? 32.110  -18.493 19.481  1.00 18.67 ? 244  VAL C CG2 1 
ATOM   6905  N  N   . GLU C  1 242 ? 31.517  -17.794 23.596  1.00 16.37 ? 245  GLU C N   1 
ATOM   6906  C  CA  . GLU C  1 242 ? 31.015  -16.612 24.290  1.00 16.81 ? 245  GLU C CA  1 
ATOM   6907  C  C   . GLU C  1 242 ? 32.144  -15.721 24.802  1.00 18.58 ? 245  GLU C C   1 
ATOM   6908  O  O   . GLU C  1 242 ? 32.021  -14.496 24.806  1.00 18.13 ? 245  GLU C O   1 
ATOM   6909  C  CB  . GLU C  1 242 ? 30.083  -17.014 25.445  1.00 20.47 ? 245  GLU C CB  1 
ATOM   6910  C  CG  . GLU C  1 242 ? 30.771  -17.810 26.567  1.00 23.61 ? 245  GLU C CG  1 
ATOM   6911  C  CD  . GLU C  1 242 ? 30.799  -19.303 26.310  1.00 27.79 ? 245  GLU C CD  1 
ATOM   6912  O  OE1 . GLU C  1 242 ? 30.539  -19.738 25.161  1.00 29.30 ? 245  GLU C OE1 1 
ATOM   6913  O  OE2 . GLU C  1 242 ? 31.113  -20.056 27.262  1.00 33.11 ? 245  GLU C OE2 1 
ATOM   6914  N  N   . VAL C  1 243 ? 33.275  -16.329 25.151  1.00 20.61 ? 246  VAL C N   1 
ATOM   6915  C  CA  . VAL C  1 243 ? 34.473  -15.570 25.513  1.00 21.46 ? 246  VAL C CA  1 
ATOM   6916  C  C   . VAL C  1 243 ? 34.898  -14.682 24.363  1.00 20.94 ? 246  VAL C C   1 
ATOM   6917  O  O   . VAL C  1 243 ? 35.156  -13.484 24.543  1.00 23.05 ? 246  VAL C O   1 
ATOM   6918  C  CB  . VAL C  1 243 ? 35.645  -16.518 25.925  1.00 21.73 ? 246  VAL C CB  1 
ATOM   6919  C  CG1 . VAL C  1 243 ? 36.876  -15.721 26.306  1.00 16.41 ? 246  VAL C CG1 1 
ATOM   6920  C  CG2 . VAL C  1 243 ? 35.216  -17.409 27.087  1.00 19.95 ? 246  VAL C CG2 1 
ATOM   6921  N  N   . VAL C  1 244 ? 34.855  -15.226 23.152  1.00 20.70 ? 247  VAL C N   1 
ATOM   6922  C  CA  . VAL C  1 244 ? 35.289  -14.452 21.989  1.00 16.49 ? 247  VAL C CA  1 
ATOM   6923  C  C   . VAL C  1 244 ? 34.261  -13.393 21.599  1.00 17.91 ? 247  VAL C C   1 
ATOM   6924  O  O   . VAL C  1 244 ? 34.602  -12.280 21.189  1.00 17.79 ? 247  VAL C O   1 
ATOM   6925  C  CB  . VAL C  1 244 ? 35.534  -15.371 20.793  1.00 16.71 ? 247  VAL C CB  1 
ATOM   6926  C  CG1 . VAL C  1 244 ? 36.233  -14.610 19.685  1.00 13.03 ? 247  VAL C CG1 1 
ATOM   6927  C  CG2 . VAL C  1 244 ? 36.353  -16.579 21.236  1.00 19.23 ? 247  VAL C CG2 1 
ATOM   6928  N  N   . ILE C  1 245 ? 32.990  -13.749 21.709  1.00 20.78 ? 248  ILE C N   1 
ATOM   6929  C  CA  . ILE C  1 245 ? 31.924  -12.807 21.399  1.00 20.67 ? 248  ILE C CA  1 
ATOM   6930  C  C   . ILE C  1 245 ? 31.920  -11.627 22.362  1.00 21.34 ? 248  ILE C C   1 
ATOM   6931  O  O   . ILE C  1 245 ? 31.830  -10.472 21.941  1.00 20.49 ? 248  ILE C O   1 
ATOM   6932  C  CB  . ILE C  1 245 ? 30.551  -13.485 21.428  1.00 21.45 ? 248  ILE C CB  1 
ATOM   6933  C  CG1 . ILE C  1 245 ? 30.433  -14.473 20.265  1.00 21.77 ? 248  ILE C CG1 1 
ATOM   6934  C  CG2 . ILE C  1 245 ? 29.440  -12.430 21.368  1.00 22.76 ? 248  ILE C CG2 1 
ATOM   6935  C  CD1 . ILE C  1 245 ? 29.337  -15.519 20.453  1.00 21.35 ? 248  ILE C CD1 1 
ATOM   6936  N  N   . GLN C  1 246 ? 32.004  -11.918 23.656  1.00 21.74 ? 249  GLN C N   1 
ATOM   6937  C  CA  . GLN C  1 246 ? 31.847  -10.884 24.672  1.00 22.10 ? 249  GLN C CA  1 
ATOM   6938  C  C   . GLN C  1 246 ? 33.105  -10.017 24.845  1.00 24.40 ? 249  GLN C C   1 
ATOM   6939  O  O   . GLN C  1 246 ? 33.028  -8.906  25.385  1.00 24.35 ? 249  GLN C O   1 
ATOM   6940  C  CB  . GLN C  1 246 ? 31.447  -11.499 26.011  1.00 22.24 ? 249  GLN C CB  1 
ATOM   6941  C  CG  . GLN C  1 246 ? 30.047  -12.091 26.022  1.00 27.25 ? 249  GLN C CG  1 
ATOM   6942  C  CD  . GLN C  1 246 ? 29.003  -11.122 25.504  1.00 29.48 ? 249  GLN C CD  1 
ATOM   6943  O  OE1 . GLN C  1 246 ? 28.177  -11.480 24.663  1.00 30.71 ? 249  GLN C OE1 1 
ATOM   6944  N  NE2 . GLN C  1 246 ? 29.077  -9.865  25.952  1.00 31.11 ? 249  GLN C NE2 1 
ATOM   6945  N  N   . ALA C  1 247 ? 34.244  -10.498 24.355  1.00 22.51 ? 250  ALA C N   1 
ATOM   6946  C  CA  . ALA C  1 247 ? 35.491  -9.715  24.435  1.00 25.45 ? 250  ALA C CA  1 
ATOM   6947  C  C   . ALA C  1 247 ? 35.389  -8.357  23.765  1.00 26.52 ? 250  ALA C C   1 
ATOM   6948  O  O   . ALA C  1 247 ? 35.961  -7.380  24.257  1.00 26.74 ? 250  ALA C O   1 
ATOM   6949  C  CB  . ALA C  1 247 ? 36.656  -10.486 23.864  1.00 21.37 ? 250  ALA C CB  1 
ATOM   6950  N  N   . HIS C  1 248 ? 34.726  -8.315  22.607  1.00 23.61 ? 251  HIS C N   1 
ATOM   6951  C  CA  . HIS C  1 248 ? 34.489  -7.059  21.889  1.00 26.25 ? 251  HIS C CA  1 
ATOM   6952  C  C   . HIS C  1 248 ? 33.181  -7.166  21.090  1.00 28.70 ? 251  HIS C C   1 
ATOM   6953  O  O   . HIS C  1 248 ? 33.196  -7.512  19.896  1.00 28.26 ? 251  HIS C O   1 
ATOM   6954  C  CB  . HIS C  1 248 ? 35.642  -6.717  20.934  1.00 24.16 ? 251  HIS C CB  1 
ATOM   6955  C  CG  . HIS C  1 248 ? 36.953  -6.452  21.617  1.00 26.89 ? 251  HIS C CG  1 
ATOM   6956  N  ND1 . HIS C  1 248 ? 37.236  -5.264  22.257  1.00 29.23 ? 251  HIS C ND1 1 
ATOM   6957  C  CD2 . HIS C  1 248 ? 38.085  -7.194  21.689  1.00 26.81 ? 251  HIS C CD2 1 
ATOM   6958  C  CE1 . HIS C  1 248 ? 38.468  -5.305  22.735  1.00 28.19 ? 251  HIS C CE1 1 
ATOM   6959  N  NE2 . HIS C  1 248 ? 39.005  -6.467  22.408  1.00 26.55 ? 251  HIS C NE2 1 
ATOM   6960  N  N   . PRO C  1 249 ? 32.046  -6.951  21.772  1.00 25.86 ? 252  PRO C N   1 
ATOM   6961  C  CA  . PRO C  1 249 ? 30.740  -7.167  21.171  1.00 27.39 ? 252  PRO C CA  1 
ATOM   6962  C  C   . PRO C  1 249 ? 30.611  -6.409  19.850  1.00 26.39 ? 252  PRO C C   1 
ATOM   6963  O  O   . PRO C  1 249 ? 30.820  -5.203  19.810  1.00 23.84 ? 252  PRO C O   1 
ATOM   6964  C  CB  . PRO C  1 249 ? 29.773  -6.606  22.228  1.00 30.70 ? 252  PRO C CB  1 
ATOM   6965  C  CG  . PRO C  1 249 ? 30.551  -6.681  23.536  1.00 30.11 ? 252  PRO C CG  1 
ATOM   6966  C  CD  . PRO C  1 249 ? 31.960  -6.401  23.141  1.00 27.81 ? 252  PRO C CD  1 
ATOM   6967  N  N   . MET C  1 250 ? 30.315  -7.125  18.769  1.00 25.32 ? 253  MET C N   1 
ATOM   6968  C  CA  . MET C  1 250 ? 30.133  -6.506  17.452  1.00 27.46 ? 253  MET C CA  1 
ATOM   6969  C  C   . MET C  1 250 ? 28.709  -6.668  16.922  1.00 25.16 ? 253  MET C C   1 
ATOM   6970  O  O   . MET C  1 250 ? 28.085  -7.709  17.133  1.00 20.55 ? 253  MET C O   1 
ATOM   6971  C  CB  . MET C  1 250 ? 31.094  -7.134  16.443  1.00 29.78 ? 253  MET C CB  1 
ATOM   6972  C  CG  . MET C  1 250 ? 32.506  -6.654  16.591  1.00 31.96 ? 253  MET C CG  1 
ATOM   6973  S  SD  . MET C  1 250 ? 32.720  -5.049  15.849  1.00 34.54 ? 253  MET C SD  1 
ATOM   6974  C  CE  . MET C  1 250 ? 31.765  -5.223  14.345  1.00 31.85 ? 253  MET C CE  1 
ATOM   6975  N  N   . GLN C  1 251 ? 28.225  -5.669  16.186  1.00 22.99 ? 254  GLN C N   1 
ATOM   6976  C  CA  . GLN C  1 251 ? 27.003  -5.842  15.394  1.00 25.71 ? 254  GLN C CA  1 
ATOM   6977  C  C   . GLN C  1 251 ? 27.389  -6.232  13.983  1.00 22.29 ? 254  GLN C C   1 
ATOM   6978  O  O   . GLN C  1 251 ? 28.428  -5.813  13.488  1.00 22.72 ? 254  GLN C O   1 
ATOM   6979  C  CB  . GLN C  1 251 ? 26.166  -4.560  15.341  1.00 23.97 ? 254  GLN C CB  1 
ATOM   6980  C  CG  . GLN C  1 251 ? 25.439  -4.202  16.625  1.00 27.69 ? 254  GLN C CG  1 
ATOM   6981  C  CD  . GLN C  1 251 ? 24.666  -2.880  16.493  1.00 28.80 ? 254  GLN C CD  1 
ATOM   6982  O  OE1 . GLN C  1 251 ? 25.194  -1.823  16.818  1.00 31.11 ? 254  GLN C OE1 1 
ATOM   6983  N  NE2 . GLN C  1 251 ? 23.481  -2.930  15.883  1.00 29.63 ? 254  GLN C NE2 1 
ATOM   6984  N  N   . PRO C  1 252 ? 26.589  -7.098  13.356  1.00 21.42 ? 255  PRO C N   1 
ATOM   6985  C  CA  . PRO C  1 252 ? 26.891  -7.521  11.989  1.00 20.54 ? 255  PRO C CA  1 
ATOM   6986  C  C   . PRO C  1 252 ? 26.716  -6.347  11.043  1.00 18.97 ? 255  PRO C C   1 
ATOM   6987  O  O   . PRO C  1 252 ? 25.903  -5.475  11.297  1.00 19.44 ? 255  PRO C O   1 
ATOM   6988  C  CB  . PRO C  1 252 ? 25.822  -8.583  11.709  1.00 19.28 ? 255  PRO C CB  1 
ATOM   6989  C  CG  . PRO C  1 252 ? 24.758  -8.364  12.812  1.00 19.46 ? 255  PRO C CG  1 
ATOM   6990  C  CD  . PRO C  1 252 ? 25.557  -7.938  13.978  1.00 18.92 ? 255  PRO C CD  1 
ATOM   6991  N  N   . GLY C  1 253 ? 27.462  -6.338  9.948   1.00 19.26 ? 256  GLY C N   1 
ATOM   6992  C  CA  . GLY C  1 253 ? 27.454  -5.203  9.059   1.00 19.76 ? 256  GLY C CA  1 
ATOM   6993  C  C   . GLY C  1 253 ? 28.505  -5.293  7.982   1.00 21.72 ? 256  GLY C C   1 
ATOM   6994  O  O   . GLY C  1 253 ? 29.132  -6.354  7.773   1.00 14.11 ? 256  GLY C O   1 
ATOM   6995  N  N   . ARG C  1 254 ? 28.668  -4.185  7.264   1.00 21.20 ? 257  ARG C N   1 
ATOM   6996  C  CA  . ARG C  1 254 ? 29.555  -4.175  6.113   1.00 24.28 ? 257  ARG C CA  1 
ATOM   6997  C  C   . ARG C  1 254 ? 30.037  -2.766  5.788   1.00 22.76 ? 257  ARG C C   1 
ATOM   6998  O  O   . ARG C  1 254 ? 29.372  -1.793  6.106   1.00 26.78 ? 257  ARG C O   1 
ATOM   6999  C  CB  . ARG C  1 254 ? 28.856  -4.817  4.904   1.00 25.79 ? 257  ARG C CB  1 
ATOM   7000  C  CG  . ARG C  1 254 ? 27.912  -3.908  4.208   1.00 29.95 ? 257  ARG C CG  1 
ATOM   7001  C  CD  . ARG C  1 254 ? 26.560  -3.985  4.853   1.00 37.65 ? 257  ARG C CD  1 
ATOM   7002  N  NE  . ARG C  1 254 ? 25.587  -3.172  4.135   1.00 41.72 ? 257  ARG C NE  1 
ATOM   7003  C  CZ  . ARG C  1 254 ? 24.693  -2.387  4.729   1.00 43.87 ? 257  ARG C CZ  1 
ATOM   7004  N  NH1 . ARG C  1 254 ? 24.653  -2.310  6.058   1.00 42.11 ? 257  ARG C NH1 1 
ATOM   7005  N  NH2 . ARG C  1 254 ? 23.846  -1.677  3.991   1.00 43.09 ? 257  ARG C NH2 1 
ATOM   7006  N  N   . ASN C  1 255 ? 31.238  -2.661  5.236   1.00 23.26 ? 258  ASN C N   1 
ATOM   7007  C  CA  . ASN C  1 255 ? 31.611  -1.488  4.463   1.00 25.11 ? 258  ASN C CA  1 
ATOM   7008  C  C   . ASN C  1 255 ? 30.692  -1.285  3.257   1.00 25.69 ? 258  ASN C C   1 
ATOM   7009  O  O   . ASN C  1 255 ? 30.244  -2.249  2.616   1.00 21.48 ? 258  ASN C O   1 
ATOM   7010  C  CB  . ASN C  1 255 ? 33.088  -1.548  4.043   1.00 24.61 ? 258  ASN C CB  1 
ATOM   7011  C  CG  . ASN C  1 255 ? 34.031  -1.026  5.134   1.00 24.98 ? 258  ASN C CG  1 
ATOM   7012  O  OD1 . ASN C  1 255 ? 33.632  -0.225  5.995   1.00 25.03 ? 258  ASN C OD1 1 
ATOM   7013  N  ND2 . ASN C  1 255 ? 35.286  -1.474  5.097   1.00 22.05 ? 258  ASN C ND2 1 
ATOM   7014  N  N   . VAL C  1 256 ? 30.387  -0.023  2.975   1.00 29.96 ? 259  VAL C N   1 
ATOM   7015  C  CA  . VAL C  1 256 ? 29.468  0.313   1.902   1.00 33.92 ? 259  VAL C CA  1 
ATOM   7016  C  C   . VAL C  1 256 ? 30.209  0.993   0.733   1.00 36.52 ? 259  VAL C C   1 
ATOM   7017  O  O   . VAL C  1 256 ? 29.988  2.159   0.421   1.00 37.51 ? 259  VAL C O   1 
ATOM   7018  C  CB  . VAL C  1 256 ? 28.270  1.155   2.438   1.00 36.53 ? 259  VAL C CB  1 
ATOM   7019  C  CG1 . VAL C  1 256 ? 27.438  1.728   1.293   1.00 39.83 ? 259  VAL C CG1 1 
ATOM   7020  C  CG2 . VAL C  1 256 ? 27.385  0.293   3.331   1.00 33.92 ? 259  VAL C CG2 1 
ATOM   7021  N  N   . GLY C  1 257 ? 31.112  0.254   0.101   1.00 38.14 ? 260  GLY C N   1 
ATOM   7022  C  CA  . GLY C  1 257 ? 31.769  0.742   -1.102  1.00 39.22 ? 260  GLY C CA  1 
ATOM   7023  C  C   . GLY C  1 257 ? 33.017  1.562   -0.824  1.00 41.82 ? 260  GLY C C   1 
ATOM   7024  O  O   . GLY C  1 257 ? 33.623  2.109   -1.751  1.00 39.61 ? 260  GLY C O   1 
ATOM   7025  N  N   . LYS C  1 258 ? 33.393  1.670   0.452   1.00 43.28 ? 261  LYS C N   1 
ATOM   7026  C  CA  . LYS C  1 258 ? 34.647  2.336   0.817   1.00 43.91 ? 261  LYS C CA  1 
ATOM   7027  C  C   . LYS C  1 258 ? 35.173  1.971   2.212   1.00 41.70 ? 261  LYS C C   1 
ATOM   7028  O  O   . LYS C  1 258 ? 34.432  1.465   3.056   1.00 42.12 ? 261  LYS C O   1 
ATOM   7029  C  CB  . LYS C  1 258 ? 34.530  3.859   0.645   1.00 47.21 ? 261  LYS C CB  1 
ATOM   7030  C  CG  . LYS C  1 258 ? 33.553  4.538   1.594   1.00 51.07 ? 261  LYS C CG  1 
ATOM   7031  C  CD  . LYS C  1 258 ? 34.260  5.600   2.440   1.00 54.73 ? 261  LYS C CD  1 
ATOM   7032  C  CE  . LYS C  1 258 ? 33.267  6.487   3.192   1.00 56.98 ? 261  LYS C CE  1 
ATOM   7033  N  NZ  . LYS C  1 258 ? 32.351  7.194   2.254   1.00 57.55 ? 261  LYS C NZ  1 
ATOM   7034  N  N   . ILE C  1 259 ? 36.458  2.212   2.453   1.00 39.88 ? 262  ILE C N   1 
ATOM   7035  C  CA  . ILE C  1 259 ? 37.041  1.861   3.745   1.00 37.36 ? 262  ILE C CA  1 
ATOM   7036  C  C   . ILE C  1 259 ? 36.364  2.693   4.824   1.00 35.79 ? 262  ILE C C   1 
ATOM   7037  O  O   . ILE C  1 259 ? 35.791  3.741   4.543   1.00 32.77 ? 262  ILE C O   1 
ATOM   7038  C  CB  . ILE C  1 259 ? 38.572  2.097   3.780   1.00 37.58 ? 262  ILE C CB  1 
ATOM   7039  C  CG1 . ILE C  1 259 ? 38.911  3.510   3.306   1.00 37.25 ? 262  ILE C CG1 1 
ATOM   7040  C  CG2 . ILE C  1 259 ? 39.291  1.081   2.917   1.00 35.44 ? 262  ILE C CG2 1 
ATOM   7041  C  CD1 . ILE C  1 259 ? 40.260  4.005   3.784   1.00 36.29 ? 262  ILE C CD1 1 
ATOM   7042  N  N   . ASN C  1 260 ? 36.359  2.190   6.046   1.00 33.89 ? 263  ASN C N   1 
ATOM   7043  C  CA  . ASN C  1 260 ? 35.790  2.945   7.153   1.00 33.88 ? 263  ASN C CA  1 
ATOM   7044  C  C   . ASN C  1 260 ? 34.351  3.437   6.955   1.00 33.27 ? 263  ASN C C   1 
ATOM   7045  O  O   . ASN C  1 260 ? 34.007  4.542   7.371   1.00 36.02 ? 263  ASN C O   1 
ATOM   7046  C  CB  . ASN C  1 260 ? 36.685  4.137   7.486   1.00 36.14 ? 263  ASN C CB  1 
ATOM   7047  C  CG  . ASN C  1 260 ? 38.101  3.723   7.822   1.00 33.98 ? 263  ASN C CG  1 
ATOM   7048  O  OD1 . ASN C  1 260 ? 39.034  3.996   7.065   1.00 34.62 ? 263  ASN C OD1 1 
ATOM   7049  N  ND2 . ASN C  1 260 ? 38.269  3.058   8.959   1.00 34.84 ? 263  ASN C ND2 1 
ATOM   7050  N  N   . SER C  1 261 ? 33.485  2.588   6.423   1.00 30.12 ? 264  SER C N   1 
ATOM   7051  C  CA  . SER C  1 261 ? 32.068  2.919   6.342   1.00 28.78 ? 264  SER C CA  1 
ATOM   7052  C  C   . SER C  1 261 ? 31.220  1.739   6.818   1.00 28.14 ? 264  SER C C   1 
ATOM   7053  O  O   . SER C  1 261 ? 30.175  1.433   6.225   1.00 26.51 ? 264  SER C O   1 
ATOM   7054  C  CB  . SER C  1 261 ? 31.693  3.270   4.907   1.00 25.34 ? 264  SER C CB  1 
ATOM   7055  O  OG  . SER C  1 261 ? 32.057  2.211   4.050   1.00 25.47 ? 264  SER C OG  1 
ATOM   7056  N  N   . TYR C  1 262 ? 31.688  1.092   7.885   1.00 26.97 ? 265  TYR C N   1 
ATOM   7057  C  CA  . TYR C  1 262 ? 31.000  -0.046  8.489   1.00 28.15 ? 265  TYR C CA  1 
ATOM   7058  C  C   . TYR C  1 262 ? 29.595  0.310   8.897   1.00 25.61 ? 265  TYR C C   1 
ATOM   7059  O  O   . TYR C  1 262 ? 29.375  1.080   9.824   1.00 28.07 ? 265  TYR C O   1 
ATOM   7060  C  CB  . TYR C  1 262 ? 31.755  -0.584  9.702   1.00 27.14 ? 265  TYR C CB  1 
ATOM   7061  C  CG  . TYR C  1 262 ? 31.285  -1.959  10.148  1.00 29.72 ? 265  TYR C CG  1 
ATOM   7062  C  CD1 . TYR C  1 262 ? 31.754  -3.110  9.514   1.00 29.70 ? 265  TYR C CD1 1 
ATOM   7063  C  CD2 . TYR C  1 262 ? 30.438  -2.116  11.238  1.00 26.81 ? 265  TYR C CD2 1 
ATOM   7064  C  CE1 . TYR C  1 262 ? 31.389  -4.359  9.931   1.00 25.73 ? 265  TYR C CE1 1 
ATOM   7065  C  CE2 . TYR C  1 262 ? 30.063  -3.383  11.667  1.00 26.70 ? 265  TYR C CE2 1 
ATOM   7066  C  CZ  . TYR C  1 262 ? 30.538  -4.499  11.000  1.00 26.30 ? 265  TYR C CZ  1 
ATOM   7067  O  OH  . TYR C  1 262 ? 30.175  -5.772  11.395  1.00 23.14 ? 265  TYR C OH  1 
ATOM   7068  N  N   . THR C  1 263 ? 28.647  -0.384  8.302   1.00 25.77 ? 266  THR C N   1 
ATOM   7069  C  CA  . THR C  1 263 ? 27.265  -0.006  8.428   1.00 25.44 ? 266  THR C CA  1 
ATOM   7070  C  C   . THR C  1 263 ? 26.457  -1.203  8.895   1.00 24.79 ? 266  THR C C   1 
ATOM   7071  O  O   . THR C  1 263 ? 26.506  -2.268  8.280   1.00 24.68 ? 266  THR C O   1 
ATOM   7072  C  CB  . THR C  1 263 ? 26.742  0.468   7.081   1.00 25.82 ? 266  THR C CB  1 
ATOM   7073  O  OG1 . THR C  1 263 ? 27.531  1.586   6.656   1.00 25.47 ? 266  THR C OG1 1 
ATOM   7074  C  CG2 . THR C  1 263 ? 25.264  0.863   7.183   1.00 24.89 ? 266  THR C CG2 1 
ATOM   7075  N  N   . VAL C  1 264 ? 25.760  -1.042  10.010  1.00 23.10 ? 267  VAL C N   1 
ATOM   7076  C  CA  . VAL C  1 264 ? 25.034  -2.152  10.610  1.00 27.60 ? 267  VAL C CA  1 
ATOM   7077  C  C   . VAL C  1 264 ? 23.940  -2.677  9.671   1.00 27.23 ? 267  VAL C C   1 
ATOM   7078  O  O   . VAL C  1 264 ? 23.228  -1.906  9.038   1.00 26.09 ? 267  VAL C O   1 
ATOM   7079  C  CB  . VAL C  1 264 ? 24.455  -1.756  11.980  1.00 28.26 ? 267  VAL C CB  1 
ATOM   7080  C  CG1 . VAL C  1 264 ? 23.360  -2.725  12.412  1.00 28.20 ? 267  VAL C CG1 1 
ATOM   7081  C  CG2 . VAL C  1 264 ? 25.595  -1.644  13.032  1.00 25.02 ? 267  VAL C CG2 1 
ATOM   7082  N  N   . ASP C  1 265 ? 23.872  -3.992  9.520   1.00 26.14 ? 268  ASP C N   1 
ATOM   7083  C  CA  . ASP C  1 265 ? 22.831  -4.589  8.712   1.00 27.67 ? 268  ASP C CA  1 
ATOM   7084  C  C   . ASP C  1 265 ? 21.697  -5.099  9.576   1.00 26.53 ? 268  ASP C C   1 
ATOM   7085  O  O   . ASP C  1 265 ? 21.782  -6.185  10.122  1.00 28.67 ? 268  ASP C O   1 
ATOM   7086  C  CB  . ASP C  1 265 ? 23.395  -5.728  7.875   1.00 29.93 ? 268  ASP C CB  1 
ATOM   7087  C  CG  . ASP C  1 265 ? 22.341  -6.395  7.020   1.00 28.66 ? 268  ASP C CG  1 
ATOM   7088  O  OD1 . ASP C  1 265 ? 21.182  -5.952  7.028   1.00 31.46 ? 268  ASP C OD1 1 
ATOM   7089  O  OD2 . ASP C  1 265 ? 22.660  -7.412  6.393   1.00 32.09 ? 268  ASP C OD2 1 
ATOM   7090  N  N   . PRO C  1 266 ? 20.613  -4.322  9.681   1.00 26.54 ? 269  PRO C N   1 
ATOM   7091  C  CA  . PRO C  1 266 ? 19.565  -4.663  10.645  1.00 25.28 ? 269  PRO C CA  1 
ATOM   7092  C  C   . PRO C  1 266 ? 18.785  -5.919  10.226  1.00 24.22 ? 269  PRO C C   1 
ATOM   7093  O  O   . PRO C  1 266 ? 17.971  -6.410  10.981  1.00 25.00 ? 269  PRO C O   1 
ATOM   7094  C  CB  . PRO C  1 266 ? 18.653  -3.418  10.633  1.00 27.85 ? 269  PRO C CB  1 
ATOM   7095  C  CG  . PRO C  1 266 ? 18.800  -2.848  9.193   1.00 28.10 ? 269  PRO C CG  1 
ATOM   7096  C  CD  . PRO C  1 266 ? 20.196  -3.285  8.709   1.00 27.63 ? 269  PRO C CD  1 
ATOM   7097  N  N   . THR C  1 267 ? 19.049  -6.444  9.039   1.00 25.47 ? 270  THR C N   1 
ATOM   7098  C  CA  . THR C  1 267 ? 18.381  -7.669  8.602   1.00 27.20 ? 270  THR C CA  1 
ATOM   7099  C  C   . THR C  1 267 ? 19.247  -8.910  8.853   1.00 27.27 ? 270  THR C C   1 
ATOM   7100  O  O   . THR C  1 267 ? 18.785  -10.034 8.693   1.00 25.20 ? 270  THR C O   1 
ATOM   7101  C  CB  . THR C  1 267 ? 18.047  -7.622  7.098   1.00 30.20 ? 270  THR C CB  1 
ATOM   7102  O  OG1 . THR C  1 267 ? 19.271  -7.626  6.345   1.00 27.79 ? 270  THR C OG1 1 
ATOM   7103  C  CG2 . THR C  1 267 ? 17.236  -6.339  6.755   1.00 31.80 ? 270  THR C CG2 1 
ATOM   7104  N  N   . SER C  1 268 ? 20.516  -8.716  9.196   1.00 25.32 ? 271  SER C N   1 
ATOM   7105  C  CA  . SER C  1 268 ? 21.353  -9.868  9.568   1.00 23.13 ? 271  SER C CA  1 
ATOM   7106  C  C   . SER C  1 268 ? 20.859  -10.543 10.854  1.00 20.50 ? 271  SER C C   1 
ATOM   7107  O  O   . SER C  1 268 ? 20.360  -9.868  11.753  1.00 17.43 ? 271  SER C O   1 
ATOM   7108  C  CB  . SER C  1 268 ? 22.811  -9.451  9.735   1.00 22.60 ? 271  SER C CB  1 
ATOM   7109  O  OG  . SER C  1 268 ? 23.572  -10.547 10.182  1.00 21.48 ? 271  SER C OG  1 
ATOM   7110  N  N   . SER C  1 269 ? 20.958  -11.872 10.919  1.00 18.10 ? 272  SER C N   1 
ATOM   7111  C  CA  . SER C  1 269 ? 20.906  -12.565 12.196  1.00 17.50 ? 272  SER C CA  1 
ATOM   7112  C  C   . SER C  1 269 ? 22.115  -12.172 13.035  1.00 19.10 ? 272  SER C C   1 
ATOM   7113  O  O   . SER C  1 269 ? 22.965  -11.385 12.599  1.00 20.59 ? 272  SER C O   1 
ATOM   7114  C  CB  . SER C  1 269 ? 20.873  -14.089 11.987  1.00 21.17 ? 272  SER C CB  1 
ATOM   7115  O  OG  . SER C  1 269 ? 22.066  -14.579 11.381  1.00 18.64 ? 272  SER C OG  1 
ATOM   7116  N  N   . ASP C  1 270 ? 22.197  -12.719 14.239  1.00 19.71 ? 273  ASP C N   1 
ATOM   7117  C  CA  . ASP C  1 270 ? 23.381  -12.557 15.084  1.00 20.17 ? 273  ASP C CA  1 
ATOM   7118  C  C   . ASP C  1 270 ? 23.276  -13.632 16.141  1.00 19.15 ? 273  ASP C C   1 
ATOM   7119  O  O   . ASP C  1 270 ? 22.484  -14.553 15.995  1.00 20.01 ? 273  ASP C O   1 
ATOM   7120  C  CB  . ASP C  1 270 ? 23.407  -11.164 15.740  1.00 18.09 ? 273  ASP C CB  1 
ATOM   7121  C  CG  . ASP C  1 270 ? 22.198  -10.909 16.631  1.00 21.10 ? 273  ASP C CG  1 
ATOM   7122  O  OD1 . ASP C  1 270 ? 21.758  -11.816 17.388  1.00 24.22 ? 273  ASP C OD1 1 
ATOM   7123  O  OD2 . ASP C  1 270 ? 21.722  -9.765  16.636  1.00 24.70 ? 273  ASP C OD2 1 
ATOM   7124  N  N   . PHE C  1 271 ? 24.052  -13.520 17.211  1.00 17.62 ? 274  PHE C N   1 
ATOM   7125  C  CA  . PHE C  1 271 ? 24.177  -14.643 18.115  1.00 16.52 ? 274  PHE C CA  1 
ATOM   7126  C  C   . PHE C  1 271 ? 22.933  -14.863 18.947  1.00 17.15 ? 274  PHE C C   1 
ATOM   7127  O  O   . PHE C  1 271 ? 22.681  -15.970 19.370  1.00 17.60 ? 274  PHE C O   1 
ATOM   7128  C  CB  . PHE C  1 271 ? 25.454  -14.567 18.966  1.00 17.07 ? 274  PHE C CB  1 
ATOM   7129  C  CG  . PHE C  1 271 ? 26.687  -14.934 18.190  1.00 18.58 ? 274  PHE C CG  1 
ATOM   7130  C  CD1 . PHE C  1 271 ? 26.902  -16.244 17.821  1.00 20.13 ? 274  PHE C CD1 1 
ATOM   7131  C  CD2 . PHE C  1 271 ? 27.478  -13.949 17.629  1.00 19.66 ? 274  PHE C CD2 1 
ATOM   7132  C  CE1 . PHE C  1 271 ? 27.947  -16.573 16.980  1.00 24.70 ? 274  PHE C CE1 1 
ATOM   7133  C  CE2 . PHE C  1 271 ? 28.502  -14.273 16.764  1.00 21.76 ? 274  PHE C CE2 1 
ATOM   7134  C  CZ  . PHE C  1 271 ? 28.751  -15.583 16.460  1.00 20.94 ? 274  PHE C CZ  1 
ATOM   7135  N  N   . SER C  1 272 ? 22.086  -13.846 19.063  1.00 18.49 ? 275  SER C N   1 
ATOM   7136  C  CA  . SER C  1 272 ? 20.804  -14.031 19.756  1.00 20.16 ? 275  SER C CA  1 
ATOM   7137  C  C   . SER C  1 272 ? 19.751  -14.704 18.870  1.00 19.35 ? 275  SER C C   1 
ATOM   7138  O  O   . SER C  1 272 ? 18.721  -15.141 19.372  1.00 19.33 ? 275  SER C O   1 
ATOM   7139  C  CB  . SER C  1 272 ? 20.263  -12.703 20.279  1.00 15.92 ? 275  SER C CB  1 
ATOM   7140  O  OG  . SER C  1 272 ? 19.787  -11.938 19.187  1.00 19.57 ? 275  SER C OG  1 
ATOM   7141  N  N   . THR C  1 273 ? 20.032  -14.855 17.573  1.00 19.68 ? 276  THR C N   1 
ATOM   7142  C  CA  . THR C  1 273 ? 19.036  -15.424 16.641  1.00 17.03 ? 276  THR C CA  1 
ATOM   7143  C  C   . THR C  1 273 ? 19.578  -16.520 15.716  1.00 17.37 ? 276  THR C C   1 
ATOM   7144  O  O   . THR C  1 273 ? 19.593  -16.359 14.508  1.00 17.95 ? 276  THR C O   1 
ATOM   7145  C  CB  . THR C  1 273 ? 18.374  -14.326 15.785  1.00 18.08 ? 276  THR C CB  1 
ATOM   7146  O  OG1 . THR C  1 273 ? 19.385  -13.529 15.163  1.00 22.83 ? 276  THR C OG1 1 
ATOM   7147  C  CG2 . THR C  1 273 ? 17.474  -13.385 16.647  1.00 18.06 ? 276  THR C CG2 1 
ATOM   7148  N  N   . PRO C  1 274 ? 19.930  -17.684 16.279  1.00 17.34 ? 277  PRO C N   1 
ATOM   7149  C  CA  . PRO C  1 274 ? 20.467  -18.779 15.486  1.00 14.85 ? 277  PRO C CA  1 
ATOM   7150  C  C   . PRO C  1 274 ? 19.456  -19.414 14.527  1.00 16.17 ? 277  PRO C C   1 
ATOM   7151  O  O   . PRO C  1 274 ? 19.827  -19.851 13.424  1.00 14.47 ? 277  PRO C O   1 
ATOM   7152  C  CB  . PRO C  1 274 ? 20.904  -19.807 16.551  1.00 15.71 ? 277  PRO C CB  1 
ATOM   7153  C  CG  . PRO C  1 274 ? 20.032  -19.487 17.753  1.00 16.95 ? 277  PRO C CG  1 
ATOM   7154  C  CD  . PRO C  1 274 ? 19.954  -17.982 17.729  1.00 16.83 ? 277  PRO C CD  1 
ATOM   7155  N  N   . CYS C  1 275 ? 18.197  -19.488 14.926  1.00 15.80 ? 278  CYS C N   1 
ATOM   7156  C  CA  . CYS C  1 275 ? 17.198  -20.059 14.040  1.00 19.54 ? 278  CYS C CA  1 
ATOM   7157  C  C   . CYS C  1 275 ? 16.920  -19.151 12.865  1.00 19.46 ? 278  CYS C C   1 
ATOM   7158  O  O   . CYS C  1 275 ? 16.682  -19.629 11.756  1.00 17.66 ? 278  CYS C O   1 
ATOM   7159  C  CB  . CYS C  1 275 ? 15.901  -20.379 14.780  1.00 19.01 ? 278  CYS C CB  1 
ATOM   7160  S  SG  . CYS C  1 275 ? 16.176  -21.378 16.199  1.00 20.50 ? 278  CYS C SG  1 
ATOM   7161  N  N   . LEU C  1 276 ? 17.036  -17.846 13.086  1.00 19.10 ? 279  LEU C N   1 
ATOM   7162  C  CA  . LEU C  1 276 ? 16.949  -16.892 11.968  1.00 19.63 ? 279  LEU C CA  1 
ATOM   7163  C  C   . LEU C  1 276 ? 18.100  -17.114 10.985  1.00 19.50 ? 279  LEU C C   1 
ATOM   7164  O  O   . LEU C  1 276 ? 17.947  -17.007 9.766   1.00 16.60 ? 279  LEU C O   1 
ATOM   7165  C  CB  . LEU C  1 276 ? 16.960  -15.443 12.480  1.00 20.39 ? 279  LEU C CB  1 
ATOM   7166  C  CG  . LEU C  1 276 ? 16.901  -14.335 11.415  1.00 23.56 ? 279  LEU C CG  1 
ATOM   7167  C  CD1 . LEU C  1 276 ? 15.580  -14.396 10.630  1.00 21.18 ? 279  LEU C CD1 1 
ATOM   7168  C  CD2 . LEU C  1 276 ? 17.080  -12.938 12.025  1.00 23.00 ? 279  LEU C CD2 1 
ATOM   7169  N  N   . MET C  1 277 ? 19.272  -17.401 11.523  1.00 19.04 ? 280  MET C N   1 
ATOM   7170  C  CA  . MET C  1 277 ? 20.431  -17.645 10.681  1.00 20.75 ? 280  MET C CA  1 
ATOM   7171  C  C   . MET C  1 277 ? 20.255  -18.943 9.858   1.00 18.24 ? 280  MET C C   1 
ATOM   7172  O  O   . MET C  1 277 ? 20.500  -18.977 8.646   1.00 14.21 ? 280  MET C O   1 
ATOM   7173  C  CB  . MET C  1 277 ? 21.663  -17.716 11.573  1.00 22.05 ? 280  MET C CB  1 
ATOM   7174  C  CG  . MET C  1 277 ? 22.951  -17.646 10.827  1.00 27.33 ? 280  MET C CG  1 
ATOM   7175  S  SD  . MET C  1 277 ? 23.807  -19.192 11.058  1.00 37.25 ? 280  MET C SD  1 
ATOM   7176  C  CE  . MET C  1 277 ? 22.963  -20.268 9.939   1.00 30.25 ? 280  MET C CE  1 
ATOM   7177  N  N   . TYR C  1 278 ? 19.757  -19.988 10.515  1.00 17.34 ? 281  TYR C N   1 
ATOM   7178  C  CA  . TYR C  1 278 ? 19.471  -21.253 9.843   1.00 16.74 ? 281  TYR C CA  1 
ATOM   7179  C  C   . TYR C  1 278 ? 18.438  -20.990 8.722   1.00 17.77 ? 281  TYR C C   1 
ATOM   7180  O  O   . TYR C  1 278 ? 18.634  -21.383 7.566   1.00 19.11 ? 281  TYR C O   1 
ATOM   7181  C  CB  . TYR C  1 278 ? 18.961  -22.299 10.859  1.00 15.66 ? 281  TYR C CB  1 
ATOM   7182  C  CG  . TYR C  1 278 ? 18.108  -23.365 10.222  1.00 19.19 ? 281  TYR C CG  1 
ATOM   7183  C  CD1 . TYR C  1 278 ? 18.675  -24.311 9.378   1.00 19.88 ? 281  TYR C CD1 1 
ATOM   7184  C  CD2 . TYR C  1 278 ? 16.720  -23.355 10.356  1.00 18.10 ? 281  TYR C CD2 1 
ATOM   7185  C  CE1 . TYR C  1 278 ? 17.898  -25.238 8.715   1.00 19.56 ? 281  TYR C CE1 1 
ATOM   7186  C  CE2 . TYR C  1 278 ? 15.931  -24.235 9.644   1.00 18.21 ? 281  TYR C CE2 1 
ATOM   7187  C  CZ  . TYR C  1 278 ? 16.527  -25.192 8.833   1.00 21.22 ? 281  TYR C CZ  1 
ATOM   7188  O  OH  . TYR C  1 278 ? 15.759  -26.134 8.160   1.00 20.90 ? 281  TYR C OH  1 
ATOM   7189  N  N   . GLU C  1 279 ? 17.429  -20.186 9.029   1.00 16.18 ? 282  GLU C N   1 
ATOM   7190  C  CA  . GLU C  1 279 ? 16.299  -19.976 8.110   1.00 17.53 ? 282  GLU C CA  1 
ATOM   7191  C  C   . GLU C  1 279 ? 16.716  -19.177 6.890   1.00 17.96 ? 282  GLU C C   1 
ATOM   7192  O  O   . GLU C  1 279 ? 16.376  -19.536 5.752   1.00 11.31 ? 282  GLU C O   1 
ATOM   7193  C  CB  . GLU C  1 279 ? 15.165  -19.220 8.806   1.00 20.26 ? 282  GLU C CB  1 
ATOM   7194  C  CG  . GLU C  1 279 ? 14.344  -20.067 9.745   1.00 28.19 ? 282  GLU C CG  1 
ATOM   7195  C  CD  . GLU C  1 279 ? 12.945  -19.500 9.998   1.00 33.71 ? 282  GLU C CD  1 
ATOM   7196  O  OE1 . GLU C  1 279 ? 12.592  -18.481 9.343   1.00 35.46 ? 282  GLU C OE1 1 
ATOM   7197  O  OE2 . GLU C  1 279 ? 12.198  -20.104 10.823  1.00 31.75 ? 282  GLU C OE2 1 
ATOM   7198  N  N   . LYS C  1 280 ? 17.414  -18.067 7.141   1.00 16.36 ? 283  LYS C N   1 
ATOM   7199  C  CA  . LYS C  1 280 ? 18.090  -17.343 6.084   1.00 17.58 ? 283  LYS C CA  1 
ATOM   7200  C  C   . LYS C  1 280 ? 18.992  -18.207 5.206   1.00 17.52 ? 283  LYS C C   1 
ATOM   7201  O  O   . LYS C  1 280 ? 19.042  -18.010 3.996   1.00 20.02 ? 283  LYS C O   1 
ATOM   7202  C  CB  . LYS C  1 280 ? 18.847  -16.131 6.637   1.00 20.23 ? 283  LYS C CB  1 
ATOM   7203  C  CG  . LYS C  1 280 ? 17.920  -15.100 7.289   1.00 26.77 ? 283  LYS C CG  1 
ATOM   7204  C  CD  . LYS C  1 280 ? 18.631  -13.769 7.545   1.00 30.87 ? 283  LYS C CD  1 
ATOM   7205  C  CE  . LYS C  1 280 ? 18.595  -12.865 6.308   1.00 31.43 ? 283  LYS C CE  1 
ATOM   7206  N  NZ  . LYS C  1 280 ? 19.618  -11.774 6.375   1.00 31.91 ? 283  LYS C NZ  1 
ATOM   7207  N  N   . PHE C  1 281 ? 19.789  -19.076 5.817   1.00 18.19 ? 284  PHE C N   1 
ATOM   7208  C  CA  . PHE C  1 281 ? 20.784  -19.838 5.071   1.00 13.62 ? 284  PHE C CA  1 
ATOM   7209  C  C   . PHE C  1 281 ? 20.002  -20.736 4.116   1.00 16.73 ? 284  PHE C C   1 
ATOM   7210  O  O   . PHE C  1 281 ? 20.277  -20.774 2.914   1.00 17.38 ? 284  PHE C O   1 
ATOM   7211  C  CB  . PHE C  1 281 ? 21.639  -20.694 6.035   1.00 16.04 ? 284  PHE C CB  1 
ATOM   7212  C  CG  . PHE C  1 281 ? 22.723  -21.484 5.349   1.00 14.57 ? 284  PHE C CG  1 
ATOM   7213  C  CD1 . PHE C  1 281 ? 23.921  -20.874 4.986   1.00 17.22 ? 284  PHE C CD1 1 
ATOM   7214  C  CD2 . PHE C  1 281 ? 22.494  -22.787 4.940   1.00 17.80 ? 284  PHE C CD2 1 
ATOM   7215  C  CE1 . PHE C  1 281 ? 24.924  -21.589 4.300   1.00 17.99 ? 284  PHE C CE1 1 
ATOM   7216  C  CE2 . PHE C  1 281 ? 23.480  -23.518 4.261   1.00 17.26 ? 284  PHE C CE2 1 
ATOM   7217  C  CZ  . PHE C  1 281 ? 24.670  -22.904 3.891   1.00 18.56 ? 284  PHE C CZ  1 
ATOM   7218  N  N   . VAL C  1 282 ? 18.938  -21.349 4.633   1.00 17.16 ? 285  VAL C N   1 
ATOM   7219  C  CA  . VAL C  1 282 ? 18.110  -22.236 3.835   1.00 18.34 ? 285  VAL C CA  1 
ATOM   7220  C  C   . VAL C  1 282 ? 17.260  -21.490 2.791   1.00 21.18 ? 285  VAL C C   1 
ATOM   7221  O  O   . VAL C  1 282 ? 17.345  -21.758 1.582   1.00 22.06 ? 285  VAL C O   1 
ATOM   7222  C  CB  . VAL C  1 282 ? 17.213  -23.120 4.713   1.00 17.41 ? 285  VAL C CB  1 
ATOM   7223  C  CG1 . VAL C  1 282 ? 16.241  -23.886 3.831   1.00 20.41 ? 285  VAL C CG1 1 
ATOM   7224  C  CG2 . VAL C  1 282 ? 18.073  -24.114 5.499   1.00 16.01 ? 285  VAL C CG2 1 
ATOM   7225  N  N   . ASN C  1 283 ? 16.481  -20.522 3.249   1.00 22.22 ? 286  ASN C N   1 
ATOM   7226  C  CA  . ASN C  1 283 ? 15.377  -20.023 2.453   1.00 25.31 ? 286  ASN C CA  1 
ATOM   7227  C  C   . ASN C  1 283 ? 15.802  -18.845 1.587   1.00 26.32 ? 286  ASN C C   1 
ATOM   7228  O  O   . ASN C  1 283 ? 15.112  -18.480 0.658   1.00 30.59 ? 286  ASN C O   1 
ATOM   7229  C  CB  . ASN C  1 283 ? 14.189  -19.664 3.350   1.00 29.26 ? 286  ASN C CB  1 
ATOM   7230  C  CG  . ASN C  1 283 ? 13.029  -20.630 3.189   1.00 34.38 ? 286  ASN C CG  1 
ATOM   7231  O  OD1 . ASN C  1 283 ? 13.227  -21.832 2.965   1.00 31.46 ? 286  ASN C OD1 1 
ATOM   7232  N  ND2 . ASN C  1 283 ? 11.799  -20.106 3.283   1.00 38.72 ? 286  ASN C ND2 1 
ATOM   7233  N  N   . ILE C  1 284 ? 16.999  -18.329 1.827   1.00 25.66 ? 287  ILE C N   1 
ATOM   7234  C  CA  . ILE C  1 284 ? 17.568  -17.281 0.995   1.00 23.15 ? 287  ILE C CA  1 
ATOM   7235  C  C   . ILE C  1 284 ? 18.859  -17.742 0.293   1.00 22.51 ? 287  ILE C C   1 
ATOM   7236  O  O   . ILE C  1 284 ? 18.926  -17.781 -0.929  1.00 23.26 ? 287  ILE C O   1 
ATOM   7237  C  CB  . ILE C  1 284 ? 17.829  -16.005 1.834   1.00 25.28 ? 287  ILE C CB  1 
ATOM   7238  C  CG1 . ILE C  1 284 ? 16.519  -15.490 2.430   1.00 28.67 ? 287  ILE C CG1 1 
ATOM   7239  C  CG2 . ILE C  1 284 ? 18.463  -14.910 1.002   1.00 25.24 ? 287  ILE C CG2 1 
ATOM   7240  C  CD1 . ILE C  1 284 ? 16.662  -14.137 3.121   1.00 32.77 ? 287  ILE C CD1 1 
ATOM   7241  N  N   . THR C  1 285 ? 19.892  -18.076 1.059   1.00 20.93 ? 288  THR C N   1 
ATOM   7242  C  CA  . THR C  1 285 ? 21.185  -18.398 0.466   1.00 20.08 ? 288  THR C CA  1 
ATOM   7243  C  C   . THR C  1 285 ? 21.148  -19.635 -0.451  1.00 20.54 ? 288  THR C C   1 
ATOM   7244  O  O   . THR C  1 285 ? 21.440  -19.544 -1.655  1.00 19.95 ? 288  THR C O   1 
ATOM   7245  C  CB  . THR C  1 285 ? 22.262  -18.570 1.548   1.00 22.47 ? 288  THR C CB  1 
ATOM   7246  O  OG1 . THR C  1 285 ? 22.314  -17.388 2.357   1.00 23.91 ? 288  THR C OG1 1 
ATOM   7247  C  CG2 . THR C  1 285 ? 23.625  -18.804 0.910   1.00 19.98 ? 288  THR C CG2 1 
ATOM   7248  N  N   . VAL C  1 286 ? 20.773  -20.785 0.109   1.00 14.55 ? 289  VAL C N   1 
ATOM   7249  C  CA  . VAL C  1 286 ? 20.629  -21.984 -0.696  1.00 16.94 ? 289  VAL C CA  1 
ATOM   7250  C  C   . VAL C  1 286 ? 19.575  -21.828 -1.808  1.00 19.46 ? 289  VAL C C   1 
ATOM   7251  O  O   . VAL C  1 286 ? 19.853  -22.123 -2.978  1.00 19.70 ? 289  VAL C O   1 
ATOM   7252  C  CB  . VAL C  1 286 ? 20.329  -23.189 0.183   1.00 15.77 ? 289  VAL C CB  1 
ATOM   7253  C  CG1 . VAL C  1 286 ? 19.999  -24.383 -0.656  1.00 12.98 ? 289  VAL C CG1 1 
ATOM   7254  C  CG2 . VAL C  1 286 ? 21.506  -23.447 1.122   1.00 12.78 ? 289  VAL C CG2 1 
ATOM   7255  N  N   . LYS C  1 287 ? 18.421  -21.256 -1.467  1.00 19.58 ? 290  LYS C N   1 
ATOM   7256  C  CA  . LYS C  1 287 ? 17.338  -21.079 -2.428  1.00 20.24 ? 290  LYS C CA  1 
ATOM   7257  C  C   . LYS C  1 287 ? 17.746  -20.232 -3.619  1.00 21.19 ? 290  LYS C C   1 
ATOM   7258  O  O   . LYS C  1 287 ? 17.435  -20.570 -4.753  1.00 21.90 ? 290  LYS C O   1 
ATOM   7259  C  CB  . LYS C  1 287 ? 16.087  -20.495 -1.776  1.00 26.55 ? 290  LYS C CB  1 
ATOM   7260  C  CG  . LYS C  1 287 ? 14.921  -20.302 -2.743  1.00 27.97 ? 290  LYS C CG  1 
ATOM   7261  C  CD  . LYS C  1 287 ? 14.125  -21.572 -2.868  1.00 30.07 ? 290  LYS C CD  1 
ATOM   7262  C  CE  . LYS C  1 287 ? 12.851  -21.354 -3.664  1.00 33.60 ? 290  LYS C CE  1 
ATOM   7263  N  NZ  . LYS C  1 287 ? 11.924  -20.413 -2.964  1.00 39.24 ? 290  LYS C NZ  1 
ATOM   7264  N  N   . SER C  1 288 ? 18.521  -19.182 -3.390  1.00 23.08 ? 291  SER C N   1 
ATOM   7265  C  CA  . SER C  1 288 ? 18.931  -18.346 -4.501  1.00 25.18 ? 291  SER C CA  1 
ATOM   7266  C  C   . SER C  1 288 ? 19.927  -19.043 -5.434  1.00 25.81 ? 291  SER C C   1 
ATOM   7267  O  O   . SER C  1 288 ? 19.974  -18.763 -6.639  1.00 25.31 ? 291  SER C O   1 
ATOM   7268  C  CB  . SER C  1 288 ? 19.504  -17.033 -4.000  1.00 26.53 ? 291  SER C CB  1 
ATOM   7269  O  OG  . SER C  1 288 ? 18.551  -16.400 -3.187  1.00 32.08 ? 291  SER C OG  1 
ATOM   7270  N  N   . LEU C  1 289 ? 20.721  -19.951 -4.881  1.00 24.00 ? 292  LEU C N   1 
ATOM   7271  C  CA  . LEU C  1 289 ? 21.615  -20.749 -5.705  1.00 23.62 ? 292  LEU C CA  1 
ATOM   7272  C  C   . LEU C  1 289 ? 20.828  -21.733 -6.573  1.00 23.73 ? 292  LEU C C   1 
ATOM   7273  O  O   . LEU C  1 289 ? 21.216  -22.015 -7.710  1.00 25.07 ? 292  LEU C O   1 
ATOM   7274  C  CB  . LEU C  1 289 ? 22.613  -21.494 -4.831  1.00 20.93 ? 292  LEU C CB  1 
ATOM   7275  C  CG  . LEU C  1 289 ? 23.601  -20.579 -4.117  1.00 23.49 ? 292  LEU C CG  1 
ATOM   7276  C  CD1 . LEU C  1 289 ? 24.539  -21.418 -3.278  1.00 22.57 ? 292  LEU C CD1 1 
ATOM   7277  C  CD2 . LEU C  1 289 ? 24.385  -19.625 -5.097  1.00 20.50 ? 292  LEU C CD2 1 
ATOM   7278  N  N   . TYR C  1 290 ? 19.728  -22.252 -6.032  1.00 22.16 ? 293  TYR C N   1 
ATOM   7279  C  CA  . TYR C  1 290 ? 18.938  -23.285 -6.714  1.00 21.46 ? 293  TYR C CA  1 
ATOM   7280  C  C   . TYR C  1 290 ? 17.440  -22.909 -6.690  1.00 23.57 ? 293  TYR C C   1 
ATOM   7281  O  O   . TYR C  1 290 ? 16.655  -23.548 -5.995  1.00 21.65 ? 293  TYR C O   1 
ATOM   7282  C  CB  . TYR C  1 290 ? 19.120  -24.618 -5.997  1.00 20.31 ? 293  TYR C CB  1 
ATOM   7283  C  CG  . TYR C  1 290 ? 20.523  -25.198 -6.052  1.00 21.52 ? 293  TYR C CG  1 
ATOM   7284  C  CD1 . TYR C  1 290 ? 20.881  -26.078 -7.066  1.00 19.77 ? 293  TYR C CD1 1 
ATOM   7285  C  CD2 . TYR C  1 290 ? 21.460  -24.945 -5.043  1.00 20.50 ? 293  TYR C CD2 1 
ATOM   7286  C  CE1 . TYR C  1 290 ? 22.132  -26.654 -7.116  1.00 22.28 ? 293  TYR C CE1 1 
ATOM   7287  C  CE2 . TYR C  1 290 ? 22.745  -25.525 -5.089  1.00 21.93 ? 293  TYR C CE2 1 
ATOM   7288  C  CZ  . TYR C  1 290 ? 23.061  -26.398 -6.124  1.00 23.80 ? 293  TYR C CZ  1 
ATOM   7289  O  OH  . TYR C  1 290 ? 24.319  -26.971 -6.236  1.00 24.61 ? 293  TYR C OH  1 
ATOM   7290  N  N   . PRO C  1 291 ? 17.052  -21.844 -7.417  1.00 22.32 ? 294  PRO C N   1 
ATOM   7291  C  CA  . PRO C  1 291 ? 15.694  -21.285 -7.318  1.00 24.81 ? 294  PRO C CA  1 
ATOM   7292  C  C   . PRO C  1 291 ? 14.594  -22.221 -7.834  1.00 27.46 ? 294  PRO C C   1 
ATOM   7293  O  O   . PRO C  1 291 ? 13.550  -22.352 -7.194  1.00 30.35 ? 294  PRO C O   1 
ATOM   7294  C  CB  . PRO C  1 291 ? 15.762  -20.008 -8.158  1.00 26.80 ? 294  PRO C CB  1 
ATOM   7295  C  CG  . PRO C  1 291 ? 16.927  -20.206 -9.083  1.00 27.08 ? 294  PRO C CG  1 
ATOM   7296  C  CD  . PRO C  1 291 ? 17.903  -21.111 -8.367  1.00 24.49 ? 294  PRO C CD  1 
ATOM   7297  N  N   . ASN C  1 292 ? 14.872  -22.956 -8.907  1.00 26.99 ? 295  ASN C N   1 
ATOM   7298  C  CA  A ASN C  1 292 ? 13.858  -23.811 -9.529  0.50 26.72 ? 295  ASN C CA  1 
ATOM   7299  C  CA  B ASN C  1 292 ? 13.868  -23.800 -9.551  0.50 26.11 ? 295  ASN C CA  1 
ATOM   7300  C  C   . ASN C  1 292 ? 14.454  -25.160 -9.937  1.00 25.52 ? 295  ASN C C   1 
ATOM   7301  O  O   . ASN C  1 292 ? 14.577  -25.470 -11.106 1.00 26.22 ? 295  ASN C O   1 
ATOM   7302  C  CB  A ASN C  1 292 ? 13.218  -23.101 -10.733 0.50 25.22 ? 295  ASN C CB  1 
ATOM   7303  C  CB  B ASN C  1 292 ? 13.319  -23.112 -10.812 0.50 23.56 ? 295  ASN C CB  1 
ATOM   7304  C  CG  A ASN C  1 292 ? 11.932  -23.773 -11.204 0.50 26.02 ? 295  ASN C CG  1 
ATOM   7305  C  CG  B ASN C  1 292 ? 12.789  -21.716 -10.540 0.50 23.01 ? 295  ASN C CG  1 
ATOM   7306  O  OD1 A ASN C  1 292 ? 11.123  -24.248 -10.397 0.50 24.89 ? 295  ASN C OD1 1 
ATOM   7307  O  OD1 B ASN C  1 292 ? 11.631  -21.544 -10.163 0.50 22.74 ? 295  ASN C OD1 1 
ATOM   7308  N  ND2 A ASN C  1 292 ? 11.735  -23.807 -12.523 0.50 26.16 ? 295  ASN C ND2 1 
ATOM   7309  N  ND2 B ASN C  1 292 ? 13.616  -20.706 -10.794 0.50 22.53 ? 295  ASN C ND2 1 
ATOM   7310  N  N   . PRO C  1 293 ? 14.864  -25.960 -8.950  1.00 27.74 ? 296  PRO C N   1 
ATOM   7311  C  CA  . PRO C  1 293 ? 15.641  -27.129 -9.351  1.00 27.70 ? 296  PRO C CA  1 
ATOM   7312  C  C   . PRO C  1 293 ? 14.767  -28.089 -10.146 1.00 30.37 ? 296  PRO C C   1 
ATOM   7313  O  O   . PRO C  1 293 ? 13.555  -28.072 -9.983  1.00 33.00 ? 296  PRO C O   1 
ATOM   7314  C  CB  . PRO C  1 293 ? 16.033  -27.749 -8.015  1.00 23.64 ? 296  PRO C CB  1 
ATOM   7315  C  CG  . PRO C  1 293 ? 14.895  -27.370 -7.100  1.00 24.96 ? 296  PRO C CG  1 
ATOM   7316  C  CD  . PRO C  1 293 ? 14.441  -26.014 -7.535  1.00 21.90 ? 296  PRO C CD  1 
ATOM   7317  N  N   . THR C  1 294 ? 15.382  -28.934 -10.974 1.00 32.36 ? 297  THR C N   1 
ATOM   7318  C  CA  . THR C  1 294 ? 14.707  -30.093 -11.556 1.00 32.61 ? 297  THR C CA  1 
ATOM   7319  C  C   . THR C  1 294 ? 14.347  -31.088 -10.463 1.00 33.79 ? 297  THR C C   1 
ATOM   7320  O  O   . THR C  1 294 ? 14.882  -31.010 -9.356  1.00 35.34 ? 297  THR C O   1 
ATOM   7321  C  CB  . THR C  1 294 ? 15.627  -30.828 -12.550 1.00 32.68 ? 297  THR C CB  1 
ATOM   7322  O  OG1 . THR C  1 294 ? 16.844  -31.171 -11.881 1.00 33.63 ? 297  THR C OG1 1 
ATOM   7323  C  CG2 . THR C  1 294 ? 15.929  -29.951 -13.783 1.00 31.18 ? 297  THR C CG2 1 
ATOM   7324  N  N   . VAL C  1 295 ? 13.496  -32.061 -10.796 1.00 31.28 ? 298  VAL C N   1 
ATOM   7325  C  CA  . VAL C  1 295 ? 13.112  -33.099 -9.847  1.00 30.99 ? 298  VAL C CA  1 
ATOM   7326  C  C   . VAL C  1 295 ? 14.321  -33.745 -9.153  1.00 31.80 ? 298  VAL C C   1 
ATOM   7327  O  O   . VAL C  1 295 ? 14.269  -34.025 -7.956  1.00 33.43 ? 298  VAL C O   1 
ATOM   7328  C  CB  . VAL C  1 295 ? 12.244  -34.215 -10.509 1.00 33.98 ? 298  VAL C CB  1 
ATOM   7329  C  CG1 . VAL C  1 295 ? 12.124  -35.425 -9.575  1.00 33.11 ? 298  VAL C CG1 1 
ATOM   7330  C  CG2 . VAL C  1 295 ? 10.842  -33.694 -10.865 1.00 33.85 ? 298  VAL C CG2 1 
ATOM   7331  N  N   . GLN C  1 296 ? 15.365  -34.071 -9.913  1.00 29.81 ? 299  GLN C N   1 
ATOM   7332  C  CA  . GLN C  1 296 ? 16.511  -34.805 -9.350  1.00 29.68 ? 299  GLN C CA  1 
ATOM   7333  C  C   . GLN C  1 296 ? 17.241  -33.914 -8.335  1.00 25.30 ? 299  GLN C C   1 
ATOM   7334  O  O   . GLN C  1 296 ? 17.580  -34.347 -7.242  1.00 26.23 ? 299  GLN C O   1 
ATOM   7335  C  CB  . GLN C  1 296 ? 17.494  -35.283 -10.458 1.00 29.04 ? 299  GLN C CB  1 
ATOM   7336  C  CG  . GLN C  1 296 ? 18.511  -36.322 -9.962  1.00 30.14 ? 299  GLN C CG  1 
ATOM   7337  C  CD  . GLN C  1 296 ? 19.477  -36.860 -11.039 1.00 32.14 ? 299  GLN C CD  1 
ATOM   7338  O  OE1 . GLN C  1 296 ? 19.351  -36.563 -12.227 1.00 33.05 ? 299  GLN C OE1 1 
ATOM   7339  N  NE2 . GLN C  1 296 ? 20.473  -37.624 -10.600 1.00 27.79 ? 299  GLN C NE2 1 
ATOM   7340  N  N   . LEU C  1 297 ? 17.471  -32.668 -8.721  1.00 24.06 ? 300  LEU C N   1 
ATOM   7341  C  CA  . LEU C  1 297 ? 18.220  -31.735 -7.907  1.00 24.97 ? 300  LEU C CA  1 
ATOM   7342  C  C   . LEU C  1 297 ? 17.410  -31.427 -6.648  1.00 24.17 ? 300  LEU C C   1 
ATOM   7343  O  O   . LEU C  1 297 ? 17.952  -31.489 -5.541  1.00 24.55 ? 300  LEU C O   1 
ATOM   7344  C  CB  . LEU C  1 297 ? 18.509  -30.468 -8.710  1.00 25.36 ? 300  LEU C CB  1 
ATOM   7345  C  CG  . LEU C  1 297 ? 19.861  -29.756 -8.622  1.00 28.45 ? 300  LEU C CG  1 
ATOM   7346  C  CD1 . LEU C  1 297 ? 20.978  -30.630 -8.050  1.00 27.38 ? 300  LEU C CD1 1 
ATOM   7347  C  CD2 . LEU C  1 297 ? 20.251  -29.213 -9.989  1.00 28.43 ? 300  LEU C CD2 1 
ATOM   7348  N  N   . ARG C  1 298 ? 16.092  -31.253 -6.804  1.00 22.97 ? 301  ARG C N   1 
ATOM   7349  C  CA  . ARG C  1 298 ? 15.204  -31.039 -5.656  1.00 25.08 ? 301  ARG C CA  1 
ATOM   7350  C  C   . ARG C  1 298 ? 15.346  -32.131 -4.597  1.00 25.19 ? 301  ARG C C   1 
ATOM   7351  O  O   . ARG C  1 298 ? 15.467  -31.848 -3.398  1.00 26.93 ? 301  ARG C O   1 
ATOM   7352  C  CB  . ARG C  1 298 ? 13.729  -30.886 -6.077  1.00 27.68 ? 301  ARG C CB  1 
ATOM   7353  C  CG  . ARG C  1 298 ? 12.888  -30.092 -5.069  1.00 31.42 ? 301  ARG C CG  1 
ATOM   7354  C  CD  . ARG C  1 298 ? 11.366  -30.262 -5.244  1.00 35.03 ? 301  ARG C CD  1 
ATOM   7355  N  NE  . ARG C  1 298 ? 10.927  -31.615 -4.899  1.00 39.84 ? 301  ARG C NE  1 
ATOM   7356  C  CZ  . ARG C  1 298 ? 10.275  -31.948 -3.787  1.00 42.89 ? 301  ARG C CZ  1 
ATOM   7357  N  NH1 . ARG C  1 298 ? 9.946   -31.015 -2.888  1.00 43.85 ? 301  ARG C NH1 1 
ATOM   7358  N  NH2 . ARG C  1 298 ? 9.958   -33.225 -3.564  1.00 43.44 ? 301  ARG C NH2 1 
ATOM   7359  N  N   . LYS C  1 299 ? 15.348  -33.384 -5.020  1.00 23.02 ? 302  LYS C N   1 
ATOM   7360  C  CA  . LYS C  1 299 ? 15.437  -34.451 -4.039  1.00 28.14 ? 302  LYS C CA  1 
ATOM   7361  C  C   . LYS C  1 299 ? 16.813  -34.463 -3.336  1.00 26.79 ? 302  LYS C C   1 
ATOM   7362  O  O   . LYS C  1 299 ? 16.920  -34.838 -2.168  1.00 26.09 ? 302  LYS C O   1 
ATOM   7363  C  CB  . LYS C  1 299 ? 15.114  -35.815 -4.670  1.00 30.70 ? 302  LYS C CB  1 
ATOM   7364  C  CG  . LYS C  1 299 ? 15.625  -37.005 -3.853  1.00 34.85 ? 302  LYS C CG  1 
ATOM   7365  C  CD  . LYS C  1 299 ? 15.203  -38.339 -4.486  1.00 39.10 ? 302  LYS C CD  1 
ATOM   7366  C  CE  . LYS C  1 299 ? 15.679  -39.539 -3.677  1.00 39.44 ? 302  LYS C CE  1 
ATOM   7367  N  NZ  . LYS C  1 299 ? 14.613  -40.578 -3.586  1.00 42.51 ? 302  LYS C NZ  1 
ATOM   7368  N  N   . ALA C  1 300 ? 17.865  -34.110 -4.065  1.00 24.70 ? 303  ALA C N   1 
ATOM   7369  C  CA  . ALA C  1 300 ? 19.199  -34.030 -3.465  1.00 25.44 ? 303  ALA C CA  1 
ATOM   7370  C  C   . ALA C  1 300 ? 19.278  -32.845 -2.508  1.00 22.29 ? 303  ALA C C   1 
ATOM   7371  O  O   . ALA C  1 300 ? 19.865  -32.945 -1.431  1.00 23.72 ? 303  ALA C O   1 
ATOM   7372  C  CB  . ALA C  1 300 ? 20.275  -33.898 -4.542  1.00 21.52 ? 303  ALA C CB  1 
ATOM   7373  N  N   . LEU C  1 301 ? 18.766  -31.701 -2.940  1.00 20.88 ? 304  LEU C N   1 
ATOM   7374  C  CA  . LEU C  1 301 ? 18.695  -30.538 -2.059  1.00 19.90 ? 304  LEU C CA  1 
ATOM   7375  C  C   . LEU C  1 301 ? 17.992  -30.889 -0.750  1.00 19.87 ? 304  LEU C C   1 
ATOM   7376  O  O   . LEU C  1 301 ? 18.530  -30.619 0.345   1.00 17.63 ? 304  LEU C O   1 
ATOM   7377  C  CB  . LEU C  1 301 ? 17.997  -29.381 -2.761  1.00 19.51 ? 304  LEU C CB  1 
ATOM   7378  C  CG  . LEU C  1 301 ? 18.889  -28.743 -3.814  1.00 18.33 ? 304  LEU C CG  1 
ATOM   7379  C  CD1 . LEU C  1 301 ? 18.078  -28.044 -4.884  1.00 20.09 ? 304  LEU C CD1 1 
ATOM   7380  C  CD2 . LEU C  1 301 ? 19.841  -27.779 -3.130  1.00 21.99 ? 304  LEU C CD2 1 
ATOM   7381  N  N   . ASN C  1 302 ? 16.850  -31.576 -0.857  1.00 15.67 ? 305  ASN C N   1 
ATOM   7382  C  CA  . ASN C  1 302 ? 16.024  -31.858 0.321   1.00 18.28 ? 305  ASN C CA  1 
ATOM   7383  C  C   . ASN C  1 302 ? 16.720  -32.821 1.258   1.00 20.03 ? 305  ASN C C   1 
ATOM   7384  O  O   . ASN C  1 302 ? 16.586  -32.710 2.478   1.00 16.88 ? 305  ASN C O   1 
ATOM   7385  C  CB  . ASN C  1 302 ? 14.653  -32.432 -0.055  1.00 20.70 ? 305  ASN C CB  1 
ATOM   7386  C  CG  . ASN C  1 302 ? 13.638  -31.348 -0.404  1.00 24.59 ? 305  ASN C CG  1 
ATOM   7387  O  OD1 . ASN C  1 302 ? 13.823  -30.180 -0.077  1.00 24.87 ? 305  ASN C OD1 1 
ATOM   7388  N  ND2 . ASN C  1 302 ? 12.596  -31.728 -1.138  1.00 24.90 ? 305  ASN C ND2 1 
ATOM   7389  N  N   . THR C  1 303 ? 17.403  -33.814 0.682   1.00 19.95 ? 306  THR C N   1 
ATOM   7390  C  CA  . THR C  1 303 ? 18.173  -34.779 1.472   1.00 18.49 ? 306  THR C CA  1 
ATOM   7391  C  C   . THR C  1 303 ? 19.273  -34.057 2.262   1.00 16.16 ? 306  THR C C   1 
ATOM   7392  O  O   . THR C  1 303 ? 19.302  -34.078 3.493   1.00 19.04 ? 306  THR C O   1 
ATOM   7393  C  CB  . THR C  1 303 ? 18.781  -35.862 0.567   1.00 20.26 ? 306  THR C CB  1 
ATOM   7394  O  OG1 . THR C  1 303 ? 17.734  -36.704 0.079   1.00 23.31 ? 306  THR C OG1 1 
ATOM   7395  C  CG2 . THR C  1 303 ? 19.809  -36.705 1.317   1.00 18.79 ? 306  THR C CG2 1 
ATOM   7396  N  N   . ASN C  1 304 ? 20.120  -33.333 1.559   1.00 16.74 ? 307  ASN C N   1 
ATOM   7397  C  CA  . ASN C  1 304 ? 21.155  -32.567 2.231   1.00 17.15 ? 307  ASN C CA  1 
ATOM   7398  C  C   . ASN C  1 304 ? 20.607  -31.522 3.219   1.00 18.28 ? 307  ASN C C   1 
ATOM   7399  O  O   . ASN C  1 304 ? 21.168  -31.341 4.305   1.00 22.02 ? 307  ASN C O   1 
ATOM   7400  C  CB  . ASN C  1 304 ? 22.111  -31.950 1.207   1.00 15.96 ? 307  ASN C CB  1 
ATOM   7401  C  CG  . ASN C  1 304 ? 22.953  -33.001 0.518   1.00 22.15 ? 307  ASN C CG  1 
ATOM   7402  O  OD1 . ASN C  1 304 ? 23.880  -33.561 1.125   1.00 21.77 ? 307  ASN C OD1 1 
ATOM   7403  N  ND2 . ASN C  1 304 ? 22.529  -33.407 -0.694  1.00 19.44 ? 307  ASN C ND2 1 
ATOM   7404  N  N   . LEU C  1 305 ? 19.482  -30.899 2.879   1.00 16.02 ? 308  LEU C N   1 
ATOM   7405  C  CA  . LEU C  1 305 ? 18.864  -29.883 3.747   1.00 18.37 ? 308  LEU C CA  1 
ATOM   7406  C  C   . LEU C  1 305 ? 18.333  -30.525 5.031   1.00 20.07 ? 308  LEU C C   1 
ATOM   7407  O  O   . LEU C  1 305 ? 18.469  -29.945 6.116   1.00 18.28 ? 308  LEU C O   1 
ATOM   7408  C  CB  . LEU C  1 305 ? 17.739  -29.134 3.019   1.00 17.72 ? 308  LEU C CB  1 
ATOM   7409  C  CG  . LEU C  1 305 ? 18.147  -27.968 2.104   1.00 19.84 ? 308  LEU C CG  1 
ATOM   7410  C  CD1 . LEU C  1 305 ? 16.965  -27.513 1.234   1.00 20.28 ? 308  LEU C CD1 1 
ATOM   7411  C  CD2 . LEU C  1 305 ? 18.710  -26.781 2.885   1.00 15.45 ? 308  LEU C CD2 1 
ATOM   7412  N  N   . ASP C  1 306 ? 17.886  -31.781 4.919   1.00 19.47 ? 309  ASP C N   1 
ATOM   7413  C  CA  . ASP C  1 306 ? 17.508  -32.568 6.067   1.00 23.62 ? 309  ASP C CA  1 
ATOM   7414  C  C   . ASP C  1 306 ? 18.721  -32.756 6.963   1.00 24.23 ? 309  ASP C C   1 
ATOM   7415  O  O   . ASP C  1 306 ? 18.637  -32.587 8.177   1.00 22.78 ? 309  ASP C O   1 
ATOM   7416  C  CB  . ASP C  1 306 ? 17.001  -33.957 5.651   1.00 27.62 ? 309  ASP C CB  1 
ATOM   7417  C  CG  . ASP C  1 306 ? 15.593  -33.927 5.082   1.00 30.11 ? 309  ASP C CG  1 
ATOM   7418  O  OD1 . ASP C  1 306 ? 15.010  -32.823 5.034   1.00 29.82 ? 309  ASP C OD1 1 
ATOM   7419  O  OD2 . ASP C  1 306 ? 15.083  -35.009 4.667   1.00 28.38 ? 309  ASP C OD2 1 
ATOM   7420  N  N   . PHE C  1 307 ? 19.812  -33.229 6.374   1.00 23.85 ? 310  PHE C N   1 
ATOM   7421  C  CA  . PHE C  1 307 ? 21.006  -33.533 7.149   1.00 21.41 ? 310  PHE C CA  1 
ATOM   7422  C  C   . PHE C  1 307 ? 21.551  -32.254 7.792   1.00 19.23 ? 310  PHE C C   1 
ATOM   7423  O  O   . PHE C  1 307 ? 21.860  -32.242 8.969   1.00 22.27 ? 310  PHE C O   1 
ATOM   7424  C  CB  . PHE C  1 307 ? 22.070  -34.198 6.276   1.00 20.51 ? 310  PHE C CB  1 
ATOM   7425  C  CG  . PHE C  1 307 ? 21.645  -35.520 5.695   1.00 24.22 ? 310  PHE C CG  1 
ATOM   7426  C  CD1 . PHE C  1 307 ? 20.700  -36.304 6.336   1.00 24.14 ? 310  PHE C CD1 1 
ATOM   7427  C  CD2 . PHE C  1 307 ? 22.223  -35.996 4.514   1.00 22.28 ? 310  PHE C CD2 1 
ATOM   7428  C  CE1 . PHE C  1 307 ? 20.305  -37.515 5.790   1.00 25.55 ? 310  PHE C CE1 1 
ATOM   7429  C  CE2 . PHE C  1 307 ? 21.870  -37.218 3.992   1.00 23.88 ? 310  PHE C CE2 1 
ATOM   7430  C  CZ  . PHE C  1 307 ? 20.924  -37.993 4.640   1.00 26.12 ? 310  PHE C CZ  1 
ATOM   7431  N  N   . PHE C  1 308 ? 21.587  -31.161 7.040   1.00 17.16 ? 311  PHE C N   1 
ATOM   7432  C  CA  . PHE C  1 308 ? 21.947  -29.855 7.609   1.00 17.57 ? 311  PHE C CA  1 
ATOM   7433  C  C   . PHE C  1 308 ? 21.126  -29.464 8.844   1.00 18.59 ? 311  PHE C C   1 
ATOM   7434  O  O   . PHE C  1 308 ? 21.679  -29.101 9.895   1.00 16.66 ? 311  PHE C O   1 
ATOM   7435  C  CB  . PHE C  1 308 ? 21.831  -28.777 6.545   1.00 14.45 ? 311  PHE C CB  1 
ATOM   7436  C  CG  . PHE C  1 308 ? 22.137  -27.409 7.048   1.00 16.07 ? 311  PHE C CG  1 
ATOM   7437  C  CD1 . PHE C  1 308 ? 23.359  -27.142 7.658   1.00 16.35 ? 311  PHE C CD1 1 
ATOM   7438  C  CD2 . PHE C  1 308 ? 21.237  -26.368 6.860   1.00 14.84 ? 311  PHE C CD2 1 
ATOM   7439  C  CE1 . PHE C  1 308 ? 23.669  -25.879 8.075   1.00 13.27 ? 311  PHE C CE1 1 
ATOM   7440  C  CE2 . PHE C  1 308 ? 21.524  -25.088 7.310   1.00 16.65 ? 311  PHE C CE2 1 
ATOM   7441  C  CZ  . PHE C  1 308 ? 22.737  -24.843 7.923   1.00 19.14 ? 311  PHE C CZ  1 
ATOM   7442  N  N   . PHE C  1 309 ? 19.804  -29.542 8.723   1.00 21.42 ? 312  PHE C N   1 
ATOM   7443  C  CA  . PHE C  1 309 ? 18.918  -29.246 9.858   1.00 20.84 ? 312  PHE C CA  1 
ATOM   7444  C  C   . PHE C  1 309 ? 19.312  -30.041 11.105  1.00 22.31 ? 312  PHE C C   1 
ATOM   7445  O  O   . PHE C  1 309 ? 19.284  -29.503 12.209  1.00 18.45 ? 312  PHE C O   1 
ATOM   7446  C  CB  . PHE C  1 309 ? 17.442  -29.509 9.532   1.00 18.52 ? 312  PHE C CB  1 
ATOM   7447  C  CG  . PHE C  1 309 ? 16.529  -29.335 10.720  1.00 21.13 ? 312  PHE C CG  1 
ATOM   7448  C  CD1 . PHE C  1 309 ? 16.285  -28.074 11.245  1.00 19.70 ? 312  PHE C CD1 1 
ATOM   7449  C  CD2 . PHE C  1 309 ? 16.032  -30.441 11.399  1.00 23.49 ? 312  PHE C CD2 1 
ATOM   7450  C  CE1 . PHE C  1 309 ? 15.501  -27.915 12.359  1.00 22.15 ? 312  PHE C CE1 1 
ATOM   7451  C  CE2 . PHE C  1 309 ? 15.219  -30.283 12.503  1.00 22.81 ? 312  PHE C CE2 1 
ATOM   7452  C  CZ  . PHE C  1 309 ? 14.944  -29.023 12.982  1.00 19.32 ? 312  PHE C CZ  1 
ATOM   7453  N  N   . GLN C  1 310 ? 19.676  -31.314 10.926  1.00 23.08 ? 313  GLN C N   1 
ATOM   7454  C  CA  . GLN C  1 310 ? 20.028  -32.179 12.055  1.00 25.58 ? 313  GLN C CA  1 
ATOM   7455  C  C   . GLN C  1 310 ? 21.208  -31.627 12.855  1.00 24.22 ? 313  GLN C C   1 
ATOM   7456  O  O   . GLN C  1 310 ? 21.385  -32.005 13.993  1.00 24.92 ? 313  GLN C O   1 
ATOM   7457  C  CB  . GLN C  1 310 ? 20.378  -33.598 11.599  1.00 28.98 ? 313  GLN C CB  1 
ATOM   7458  C  CG  . GLN C  1 310 ? 19.201  -34.465 11.186  1.00 34.28 ? 313  GLN C CG  1 
ATOM   7459  C  CD  . GLN C  1 310 ? 19.643  -35.679 10.351  1.00 39.43 ? 313  GLN C CD  1 
ATOM   7460  O  OE1 . GLN C  1 310 ? 20.801  -36.143 10.445  1.00 38.36 ? 313  GLN C OE1 1 
ATOM   7461  N  NE2 . GLN C  1 310 ? 18.727  -36.185 9.513   1.00 37.57 ? 313  GLN C NE2 1 
ATOM   7462  N  N   . GLY C  1 311 ? 22.068  -30.836 12.215  1.00 22.05 ? 314  GLY C N   1 
ATOM   7463  C  CA  . GLY C  1 311 ? 23.294  -30.352 12.849  1.00 21.26 ? 314  GLY C CA  1 
ATOM   7464  C  C   . GLY C  1 311 ? 23.116  -29.039 13.584  1.00 20.93 ? 314  GLY C C   1 
ATOM   7465  O  O   . GLY C  1 311 ? 24.038  -28.566 14.257  1.00 21.55 ? 314  GLY C O   1 
ATOM   7466  N  N   . VAL C  1 312 ? 21.930  -28.450 13.454  1.00 20.57 ? 315  VAL C N   1 
ATOM   7467  C  CA  . VAL C  1 312 ? 21.571  -27.205 14.172  1.00 21.90 ? 315  VAL C CA  1 
ATOM   7468  C  C   . VAL C  1 312 ? 21.350  -27.474 15.677  1.00 21.99 ? 315  VAL C C   1 
ATOM   7469  O  O   . VAL C  1 312 ? 20.346  -28.076 16.081  1.00 20.73 ? 315  VAL C O   1 
ATOM   7470  C  CB  . VAL C  1 312 ? 20.306  -26.548 13.527  1.00 21.07 ? 315  VAL C CB  1 
ATOM   7471  C  CG1 . VAL C  1 312 ? 19.926  -25.243 14.225  1.00 21.57 ? 315  VAL C CG1 1 
ATOM   7472  C  CG2 . VAL C  1 312 ? 20.557  -26.274 12.056  1.00 22.14 ? 315  VAL C CG2 1 
ATOM   7473  N  N   . ALA C  1 313 ? 22.326  -27.091 16.491  1.00 22.95 ? 316  ALA C N   1 
ATOM   7474  C  CA  . ALA C  1 313 ? 22.373  -27.502 17.890  1.00 23.80 ? 316  ALA C CA  1 
ATOM   7475  C  C   . ALA C  1 313 ? 21.365  -26.771 18.773  1.00 22.96 ? 316  ALA C C   1 
ATOM   7476  O  O   . ALA C  1 313 ? 20.909  -27.295 19.791  1.00 27.02 ? 316  ALA C O   1 
ATOM   7477  C  CB  . ALA C  1 313 ? 23.768  -27.312 18.434  1.00 26.50 ? 316  ALA C CB  1 
ATOM   7478  N  N   . ALA C  1 314 ? 21.036  -25.552 18.397  1.00 22.65 ? 317  ALA C N   1 
ATOM   7479  C  CA  . ALA C  1 314 ? 19.999  -24.784 19.089  1.00 25.26 ? 317  ALA C CA  1 
ATOM   7480  C  C   . ALA C  1 314 ? 18.599  -25.408 18.981  1.00 26.52 ? 317  ALA C C   1 
ATOM   7481  O  O   . ALA C  1 314 ? 17.726  -25.127 19.799  1.00 30.81 ? 317  ALA C O   1 
ATOM   7482  C  CB  . ALA C  1 314 ? 19.992  -23.341 18.588  1.00 23.77 ? 317  ALA C CB  1 
ATOM   7483  N  N   . GLY C  1 315 ? 18.401  -26.293 18.010  1.00 25.57 ? 318  GLY C N   1 
ATOM   7484  C  CA  . GLY C  1 315 ? 17.083  -26.882 17.769  1.00 22.52 ? 318  GLY C CA  1 
ATOM   7485  C  C   . GLY C  1 315 ? 16.423  -26.250 16.554  1.00 21.12 ? 318  GLY C C   1 
ATOM   7486  O  O   . GLY C  1 315 ? 16.726  -26.615 15.426  1.00 17.61 ? 318  GLY C O   1 
ATOM   7487  N  N   . CYS C  1 316 ? 15.600  -25.232 16.793  1.00 19.62 ? 319  CYS C N   1 
ATOM   7488  C  CA  . CYS C  1 316 ? 14.943  -24.485 15.727  1.00 19.40 ? 319  CYS C CA  1 
ATOM   7489  C  C   . CYS C  1 316 ? 13.853  -25.302 15.049  1.00 19.82 ? 319  CYS C C   1 
ATOM   7490  O  O   . CYS C  1 316 ? 13.682  -26.472 15.325  1.00 18.72 ? 319  CYS C O   1 
ATOM   7491  C  CB  . CYS C  1 316 ? 15.974  -23.977 14.708  1.00 20.26 ? 319  CYS C CB  1 
ATOM   7492  S  SG  . CYS C  1 316 ? 17.271  -22.970 15.491  1.00 20.07 ? 319  CYS C SG  1 
ATOM   7493  N  N   . THR C  1 317 ? 13.135  -24.690 14.123  1.00 23.53 ? 320  THR C N   1 
ATOM   7494  C  CA  . THR C  1 317 ? 12.088  -25.399 13.400  1.00 24.66 ? 320  THR C CA  1 
ATOM   7495  C  C   . THR C  1 317 ? 12.544  -25.557 11.957  1.00 24.16 ? 320  THR C C   1 
ATOM   7496  O  O   . THR C  1 317 ? 13.085  -24.608 11.380  1.00 18.42 ? 320  THR C O   1 
ATOM   7497  C  CB  . THR C  1 317 ? 10.802  -24.573 13.436  1.00 29.16 ? 320  THR C CB  1 
ATOM   7498  O  OG1 . THR C  1 317 ? 10.374  -24.431 14.797  1.00 30.67 ? 320  THR C OG1 1 
ATOM   7499  C  CG2 . THR C  1 317 ? 9.678   -25.227 12.596  1.00 29.30 ? 320  THR C CG2 1 
ATOM   7500  N  N   . GLN C  1 318 ? 12.439  -26.767 11.408  1.00 22.16 ? 321  GLN C N   1 
ATOM   7501  C  CA  . GLN C  1 318 ? 12.867  -26.975 10.028  1.00 23.28 ? 321  GLN C CA  1 
ATOM   7502  C  C   . GLN C  1 318 ? 12.056  -26.101 9.084   1.00 26.13 ? 321  GLN C C   1 
ATOM   7503  O  O   . GLN C  1 318 ? 10.853  -25.928 9.269   1.00 27.38 ? 321  GLN C O   1 
ATOM   7504  C  CB  . GLN C  1 318 ? 12.732  -28.440 9.624   1.00 23.69 ? 321  GLN C CB  1 
ATOM   7505  C  CG  . GLN C  1 318 ? 13.549  -28.789 8.402   1.00 22.55 ? 321  GLN C CG  1 
ATOM   7506  C  CD  . GLN C  1 318 ? 13.698  -30.279 8.189   1.00 25.34 ? 321  GLN C CD  1 
ATOM   7507  O  OE1 . GLN C  1 318 ? 13.298  -31.087 9.031   1.00 25.14 ? 321  GLN C OE1 1 
ATOM   7508  N  NE2 . GLN C  1 318 ? 14.270  -30.655 7.043   1.00 26.07 ? 321  GLN C NE2 1 
ATOM   7509  N  N   . VAL C  1 319 ? 12.728  -25.487 8.115   1.00 28.49 ? 322  VAL C N   1 
ATOM   7510  C  CA  . VAL C  1 319 ? 12.036  -24.852 7.009   1.00 26.59 ? 322  VAL C CA  1 
ATOM   7511  C  C   . VAL C  1 319 ? 12.269  -25.624 5.718   1.00 27.39 ? 322  VAL C C   1 
ATOM   7512  O  O   . VAL C  1 319 ? 13.222  -26.409 5.620   1.00 26.00 ? 322  VAL C O   1 
ATOM   7513  C  CB  . VAL C  1 319 ? 12.397  -23.336 6.853   1.00 30.67 ? 322  VAL C CB  1 
ATOM   7514  C  CG1 . VAL C  1 319 ? 12.323  -22.620 8.212   1.00 31.16 ? 322  VAL C CG1 1 
ATOM   7515  C  CG2 . VAL C  1 319 ? 13.760  -23.151 6.218   1.00 30.23 ? 322  VAL C CG2 1 
ATOM   7516  N  N   . PHE C  1 320 ? 11.383  -25.401 4.746   1.00 24.17 ? 323  PHE C N   1 
ATOM   7517  C  CA  . PHE C  1 320 ? 11.273  -26.228 3.556   1.00 23.80 ? 323  PHE C CA  1 
ATOM   7518  C  C   . PHE C  1 320 ? 11.143  -25.364 2.290   1.00 24.69 ? 323  PHE C C   1 
ATOM   7519  O  O   . PHE C  1 320 ? 10.055  -24.924 1.920   1.00 24.99 ? 323  PHE C O   1 
ATOM   7520  C  CB  . PHE C  1 320 ? 10.079  -27.184 3.682   1.00 22.50 ? 323  PHE C CB  1 
ATOM   7521  C  CG  . PHE C  1 320 ? 10.242  -28.214 4.781   1.00 23.07 ? 323  PHE C CG  1 
ATOM   7522  C  CD1 . PHE C  1 320 ? 11.044  -29.334 4.591   1.00 21.24 ? 323  PHE C CD1 1 
ATOM   7523  C  CD2 . PHE C  1 320 ? 9.632   -28.039 6.016   1.00 20.43 ? 323  PHE C CD2 1 
ATOM   7524  C  CE1 . PHE C  1 320 ? 11.163  -30.304 5.596   1.00 20.35 ? 323  PHE C CE1 1 
ATOM   7525  C  CE2 . PHE C  1 320 ? 9.748   -28.994 7.014   1.00 20.63 ? 323  PHE C CE2 1 
ATOM   7526  C  CZ  . PHE C  1 320 ? 10.535  -30.121 6.812   1.00 19.71 ? 323  PHE C CZ  1 
ATOM   7527  N  N   . PRO C  1 321 ? 12.274  -25.096 1.640   1.00 23.53 ? 324  PRO C N   1 
ATOM   7528  C  CA  . PRO C  1 321 ? 12.252  -24.161 0.530   1.00 23.62 ? 324  PRO C CA  1 
ATOM   7529  C  C   . PRO C  1 321 ? 11.635  -24.790 -0.718  1.00 25.37 ? 324  PRO C C   1 
ATOM   7530  O  O   . PRO C  1 321 ? 11.228  -24.064 -1.632  1.00 26.99 ? 324  PRO C O   1 
ATOM   7531  C  CB  . PRO C  1 321 ? 13.743  -23.822 0.309   1.00 21.46 ? 324  PRO C CB  1 
ATOM   7532  C  CG  . PRO C  1 321 ? 14.511  -24.937 1.017   1.00 22.19 ? 324  PRO C CG  1 
ATOM   7533  C  CD  . PRO C  1 321 ? 13.638  -25.385 2.135   1.00 21.18 ? 324  PRO C CD  1 
ATOM   7534  N  N   . TYR C  1 322 ? 11.536  -26.117 -0.744  1.00 25.38 ? 325  TYR C N   1 
ATOM   7535  C  CA  . TYR C  1 322 ? 10.936  -26.824 -1.883  1.00 28.95 ? 325  TYR C CA  1 
ATOM   7536  C  C   . TYR C  1 322 ? 9.682   -27.628 -1.477  1.00 32.77 ? 325  TYR C C   1 
ATOM   7537  O  O   . TYR C  1 322 ? 9.249   -28.555 -2.171  1.00 32.09 ? 325  TYR C O   1 
ATOM   7538  C  CB  . TYR C  1 322 ? 11.990  -27.716 -2.568  1.00 26.41 ? 325  TYR C CB  1 
ATOM   7539  C  CG  . TYR C  1 322 ? 13.255  -26.951 -2.895  1.00 25.37 ? 325  TYR C CG  1 
ATOM   7540  C  CD1 . TYR C  1 322 ? 13.212  -25.857 -3.761  1.00 25.49 ? 325  TYR C CD1 1 
ATOM   7541  C  CD2 . TYR C  1 322 ? 14.427  -27.163 -2.169  1.00 23.54 ? 325  TYR C CD2 1 
ATOM   7542  C  CE1 . TYR C  1 322 ? 14.332  -25.078 -3.992  1.00 25.00 ? 325  TYR C CE1 1 
ATOM   7543  C  CE2 . TYR C  1 322 ? 15.570  -26.395 -2.402  1.00 21.84 ? 325  TYR C CE2 1 
ATOM   7544  C  CZ  . TYR C  1 322 ? 15.525  -25.367 -3.327  1.00 25.17 ? 325  TYR C CZ  1 
ATOM   7545  O  OH  . TYR C  1 322 ? 16.632  -24.554 -3.526  1.00 21.78 ? 325  TYR C OH  1 
ATOM   7546  N  N   . GLY C  1 323 ? 9.091   -27.250 -0.353  1.00 36.91 ? 326  GLY C N   1 
ATOM   7547  C  CA  . GLY C  1 323 ? 7.938   -27.956 0.175   1.00 40.88 ? 326  GLY C CA  1 
ATOM   7548  C  C   . GLY C  1 323 ? 8.385   -29.197 0.907   1.00 46.33 ? 326  GLY C C   1 
ATOM   7549  O  O   . GLY C  1 323 ? 9.504   -29.679 0.703   1.00 45.48 ? 326  GLY C O   1 
ATOM   7550  N  N   . ARG C  1 324 ? 7.528   -29.690 1.794   1.00 52.24 ? 327  ARG C N   1 
ATOM   7551  C  CA  . ARG C  1 324 ? 7.779   -30.947 2.492   1.00 57.68 ? 327  ARG C CA  1 
ATOM   7552  C  C   . ARG C  1 324 ? 7.694   -32.116 1.510   1.00 59.64 ? 327  ARG C C   1 
ATOM   7553  O  O   . ARG C  1 324 ? 7.220   -31.958 0.384   1.00 59.33 ? 327  ARG C O   1 
ATOM   7554  C  CB  . ARG C  1 324 ? 6.777   -31.126 3.641   1.00 59.35 ? 327  ARG C CB  1 
ATOM   7555  C  CG  . ARG C  1 324 ? 7.197   -30.480 4.956   1.00 60.58 ? 327  ARG C CG  1 
ATOM   7556  C  CD  . ARG C  1 324 ? 5.988   -30.191 5.842   1.00 62.83 ? 327  ARG C CD  1 
ATOM   7557  N  NE  . ARG C  1 324 ? 6.052   -28.864 6.456   1.00 65.42 ? 327  ARG C NE  1 
ATOM   7558  C  CZ  . ARG C  1 324 ? 6.238   -28.643 7.757   1.00 66.49 ? 327  ARG C CZ  1 
ATOM   7559  N  NH1 . ARG C  1 324 ? 6.361   -29.666 8.593   1.00 67.25 ? 327  ARG C NH1 1 
ATOM   7560  N  NH2 . ARG C  1 324 ? 6.309   -27.397 8.223   1.00 65.72 ? 327  ARG C NH2 1 
ATOM   7561  N  N   . ASP C  1 325 ? 8.171   -33.283 1.931   1.00 63.63 ? 328  ASP C N   1 
ATOM   7562  C  CA  . ASP C  1 325 ? 8.158   -34.464 1.071   1.00 66.74 ? 328  ASP C CA  1 
ATOM   7563  C  C   . ASP C  1 325 ? 9.262   -34.427 0.010   1.00 69.07 ? 328  ASP C C   1 
ATOM   7564  O  O   . ASP C  1 325 ? 9.056   -33.982 -1.124  1.00 70.48 ? 328  ASP C O   1 
ATOM   7565  C  CB  . ASP C  1 325 ? 6.791   -34.630 0.404   1.00 67.27 ? 328  ASP C CB  1 
ATOM   7566  C  CG  . ASP C  1 325 ? 5.962   -35.720 1.049   1.00 67.03 ? 328  ASP C CG  1 
ATOM   7567  O  OD1 . ASP C  1 325 ? 5.288   -35.431 2.055   1.00 67.67 ? 328  ASP C OD1 1 
ATOM   7568  O  OD2 . ASP C  1 325 ? 6.027   -36.876 0.586   1.00 66.42 ? 328  ASP C OD2 1 
ATOM   7569  O  OXT . ASP C  1 325 ? 10.391  -34.857 0.260   1.00 70.11 ? 328  ASP C OXT 1 
ATOM   7570  N  N   . LEU D  1 1   ? -20.042 -37.711 62.265  1.00 49.16 ? 4    LEU D N   1 
ATOM   7571  C  CA  . LEU D  1 1   ? -19.930 -37.109 60.903  1.00 48.70 ? 4    LEU D CA  1 
ATOM   7572  C  C   . LEU D  1 1   ? -21.311 -36.684 60.399  1.00 46.58 ? 4    LEU D C   1 
ATOM   7573  O  O   . LEU D  1 1   ? -22.302 -37.398 60.607  1.00 45.04 ? 4    LEU D O   1 
ATOM   7574  C  CB  . LEU D  1 1   ? -19.278 -38.100 59.932  1.00 50.70 ? 4    LEU D CB  1 
ATOM   7575  C  CG  . LEU D  1 1   ? -18.126 -37.595 59.048  1.00 53.47 ? 4    LEU D CG  1 
ATOM   7576  C  CD1 . LEU D  1 1   ? -17.059 -36.852 59.863  1.00 53.58 ? 4    LEU D CD1 1 
ATOM   7577  C  CD2 . LEU D  1 1   ? -17.497 -38.750 58.254  1.00 52.60 ? 4    LEU D CD2 1 
ATOM   7578  N  N   . PRO D  1 2   ? -21.391 -35.493 59.776  1.00 42.49 ? 5    PRO D N   1 
ATOM   7579  C  CA  . PRO D  1 2   ? -22.630 -35.100 59.124  1.00 39.34 ? 5    PRO D CA  1 
ATOM   7580  C  C   . PRO D  1 2   ? -22.986 -36.130 58.069  1.00 37.64 ? 5    PRO D C   1 
ATOM   7581  O  O   . PRO D  1 2   ? -22.085 -36.686 57.420  1.00 36.83 ? 5    PRO D O   1 
ATOM   7582  C  CB  . PRO D  1 2   ? -22.269 -33.767 58.451  1.00 38.87 ? 5    PRO D CB  1 
ATOM   7583  C  CG  . PRO D  1 2   ? -21.028 -33.296 59.145  1.00 39.67 ? 5    PRO D CG  1 
ATOM   7584  C  CD  . PRO D  1 2   ? -20.294 -34.568 59.458  1.00 42.06 ? 5    PRO D CD  1 
ATOM   7585  N  N   . PRO D  1 3   ? -24.287 -36.424 57.929  1.00 34.62 ? 6    PRO D N   1 
ATOM   7586  C  CA  . PRO D  1 3   ? -24.786 -37.305 56.868  1.00 34.12 ? 6    PRO D CA  1 
ATOM   7587  C  C   . PRO D  1 3   ? -24.416 -36.749 55.491  1.00 33.71 ? 6    PRO D C   1 
ATOM   7588  O  O   . PRO D  1 3   ? -24.469 -35.536 55.283  1.00 34.11 ? 6    PRO D O   1 
ATOM   7589  C  CB  . PRO D  1 3   ? -26.317 -37.269 57.055  1.00 33.21 ? 6    PRO D CB  1 
ATOM   7590  C  CG  . PRO D  1 3   ? -26.554 -36.603 58.368  1.00 34.45 ? 6    PRO D CG  1 
ATOM   7591  C  CD  . PRO D  1 3   ? -25.370 -35.707 58.612  1.00 33.02 ? 6    PRO D CD  1 
ATOM   7592  N  N   . GLY D  1 4   ? -24.070 -37.639 54.559  1.00 34.79 ? 7    GLY D N   1 
ATOM   7593  C  CA  . GLY D  1 4   ? -23.838 -37.275 53.160  1.00 30.86 ? 7    GLY D CA  1 
ATOM   7594  C  C   . GLY D  1 4   ? -25.111 -37.021 52.376  1.00 32.51 ? 7    GLY D C   1 
ATOM   7595  O  O   . GLY D  1 4   ? -26.219 -37.150 52.911  1.00 33.85 ? 7    GLY D O   1 
ATOM   7596  N  N   . PRO D  1 5   ? -24.964 -36.625 51.103  1.00 32.47 ? 8    PRO D N   1 
ATOM   7597  C  CA  . PRO D  1 5   ? -26.090 -36.461 50.191  1.00 32.13 ? 8    PRO D CA  1 
ATOM   7598  C  C   . PRO D  1 5   ? -26.946 -37.729 50.100  1.00 33.95 ? 8    PRO D C   1 
ATOM   7599  O  O   . PRO D  1 5   ? -26.421 -38.841 50.199  1.00 32.65 ? 8    PRO D O   1 
ATOM   7600  C  CB  . PRO D  1 5   ? -25.403 -36.200 48.841  1.00 32.56 ? 8    PRO D CB  1 
ATOM   7601  C  CG  . PRO D  1 5   ? -24.084 -35.599 49.205  1.00 32.36 ? 8    PRO D CG  1 
ATOM   7602  C  CD  . PRO D  1 5   ? -23.674 -36.342 50.441  1.00 31.99 ? 8    PRO D CD  1 
ATOM   7603  N  N   . LEU D  1 6   ? -28.251 -37.543 49.917  1.00 32.79 ? 9    LEU D N   1 
ATOM   7604  C  CA  . LEU D  1 6   ? -29.167 -38.613 49.544  1.00 35.15 ? 9    LEU D CA  1 
ATOM   7605  C  C   . LEU D  1 6   ? -28.586 -39.480 48.431  1.00 38.36 ? 9    LEU D C   1 
ATOM   7606  O  O   . LEU D  1 6   ? -27.967 -38.974 47.491  1.00 38.97 ? 9    LEU D O   1 
ATOM   7607  C  CB  . LEU D  1 6   ? -30.483 -38.002 49.059  1.00 34.47 ? 9    LEU D CB  1 
ATOM   7608  C  CG  . LEU D  1 6   ? -31.731 -38.090 49.928  1.00 34.23 ? 9    LEU D CG  1 
ATOM   7609  C  CD1 . LEU D  1 6   ? -31.416 -38.371 51.387  1.00 29.65 ? 9    LEU D CD1 1 
ATOM   7610  C  CD2 . LEU D  1 6   ? -32.610 -36.848 49.740  1.00 31.78 ? 9    LEU D CD2 1 
ATOM   7611  N  N   . GLU D  1 7   ? -28.856 -40.779 48.499  1.00 41.13 ? 10   GLU D N   1 
ATOM   7612  C  CA  . GLU D  1 7   ? -28.397 -41.712 47.478  1.00 42.76 ? 10   GLU D CA  1 
ATOM   7613  C  C   . GLU D  1 7   ? -29.324 -41.655 46.267  1.00 41.35 ? 10   GLU D C   1 
ATOM   7614  O  O   . GLU D  1 7   ? -28.882 -41.579 45.116  1.00 36.10 ? 10   GLU D O   1 
ATOM   7615  C  CB  . GLU D  1 7   ? -28.363 -43.126 48.047  1.00 47.12 ? 10   GLU D CB  1 
ATOM   7616  C  CG  . GLU D  1 7   ? -27.090 -43.440 48.823  1.00 53.40 ? 10   GLU D CG  1 
ATOM   7617  C  CD  . GLU D  1 7   ? -26.898 -44.932 49.041  1.00 56.84 ? 10   GLU D CD  1 
ATOM   7618  O  OE1 . GLU D  1 7   ? -27.854 -45.703 48.776  1.00 58.41 ? 10   GLU D OE1 1 
ATOM   7619  O  OE2 . GLU D  1 7   ? -25.785 -45.335 49.450  1.00 57.38 ? 10   GLU D OE2 1 
ATOM   7620  N  N   . ASN D  1 8   ? -30.617 -41.686 46.552  1.00 40.12 ? 11   ASN D N   1 
ATOM   7621  C  CA  . ASN D  1 8   ? -31.629 -41.522 45.539  1.00 41.78 ? 11   ASN D CA  1 
ATOM   7622  C  C   . ASN D  1 8   ? -32.431 -40.244 45.805  1.00 40.15 ? 11   ASN D C   1 
ATOM   7623  O  O   . ASN D  1 8   ? -33.231 -40.162 46.748  1.00 39.96 ? 11   ASN D O   1 
ATOM   7624  C  CB  . ASN D  1 8   ? -32.532 -42.763 45.465  1.00 43.36 ? 11   ASN D CB  1 
ATOM   7625  C  CG  . ASN D  1 8   ? -33.589 -42.651 44.383  1.00 48.01 ? 11   ASN D CG  1 
ATOM   7626  O  OD1 . ASN D  1 8   ? -33.641 -41.654 43.662  1.00 48.89 ? 11   ASN D OD1 1 
ATOM   7627  N  ND2 . ASN D  1 8   ? -34.455 -43.664 44.274  1.00 50.49 ? 11   ASN D ND2 1 
ATOM   7628  N  N   . SER D  1 9   ? -32.147 -39.214 45.022  1.00 37.48 ? 12   SER D N   1 
ATOM   7629  C  CA  . SER D  1 9   ? -32.717 -37.909 45.295  1.00 36.50 ? 12   SER D CA  1 
ATOM   7630  C  C   . SER D  1 9   ? -33.888 -37.604 44.378  1.00 36.46 ? 12   SER D C   1 
ATOM   7631  O  O   . SER D  1 9   ? -34.266 -36.448 44.224  1.00 36.25 ? 12   SER D O   1 
ATOM   7632  C  CB  . SER D  1 9   ? -31.652 -36.821 45.191  1.00 35.37 ? 12   SER D CB  1 
ATOM   7633  O  OG  . SER D  1 9   ? -31.286 -36.596 43.846  1.00 33.09 ? 12   SER D OG  1 
ATOM   7634  N  N   . SER D  1 10  ? -34.505 -38.651 43.829  1.00 36.85 ? 13   SER D N   1 
ATOM   7635  C  CA  . SER D  1 10  ? -35.714 -38.495 43.018  1.00 36.18 ? 13   SER D CA  1 
ATOM   7636  C  C   . SER D  1 10  ? -36.849 -37.862 43.812  1.00 35.51 ? 13   SER D C   1 
ATOM   7637  O  O   . SER D  1 10  ? -36.896 -37.969 45.033  1.00 33.96 ? 13   SER D O   1 
ATOM   7638  C  CB  . SER D  1 10  ? -36.172 -39.845 42.460  1.00 36.25 ? 13   SER D CB  1 
ATOM   7639  O  OG  . SER D  1 10  ? -35.155 -40.456 41.688  1.00 37.59 ? 13   SER D OG  1 
ATOM   7640  N  N   . ALA D  1 11  ? -37.784 -37.233 43.107  1.00 36.80 ? 14   ALA D N   1 
ATOM   7641  C  CA  . ALA D  1 11  ? -39.070 -36.882 43.700  1.00 36.42 ? 14   ALA D CA  1 
ATOM   7642  C  C   . ALA D  1 11  ? -39.706 -38.157 44.249  1.00 36.79 ? 14   ALA D C   1 
ATOM   7643  O  O   . ALA D  1 11  ? -39.469 -39.241 43.720  1.00 37.78 ? 14   ALA D O   1 
ATOM   7644  C  CB  . ALA D  1 11  ? -39.972 -36.231 42.656  1.00 35.70 ? 14   ALA D CB  1 
ATOM   7645  N  N   . LYS D  1 12  ? -40.433 -38.042 45.359  1.00 35.29 ? 15   LYS D N   1 
ATOM   7646  C  CA  . LYS D  1 12  ? -41.213 -39.166 45.887  1.00 35.34 ? 15   LYS D CA  1 
ATOM   7647  C  C   . LYS D  1 12  ? -42.268 -38.694 46.887  1.00 36.06 ? 15   LYS D C   1 
ATOM   7648  O  O   . LYS D  1 12  ? -42.242 -37.537 47.344  1.00 33.21 ? 15   LYS D O   1 
ATOM   7649  C  CB  . LYS D  1 12  ? -40.309 -40.214 46.536  1.00 36.44 ? 15   LYS D CB  1 
ATOM   7650  C  CG  . LYS D  1 12  ? -39.920 -39.887 47.970  1.00 39.23 ? 15   LYS D CG  1 
ATOM   7651  C  CD  . LYS D  1 12  ? -38.838 -40.820 48.482  1.00 40.67 ? 15   LYS D CD  1 
ATOM   7652  C  CE  . LYS D  1 12  ? -39.004 -41.066 49.978  1.00 41.73 ? 15   LYS D CE  1 
ATOM   7653  N  NZ  . LYS D  1 12  ? -37.995 -42.029 50.512  1.00 43.71 ? 15   LYS D NZ  1 
ATOM   7654  N  N   . LEU D  1 13  ? -43.231 -39.569 47.178  1.00 35.47 ? 16   LEU D N   1 
ATOM   7655  C  CA  . LEU D  1 13  ? -44.242 -39.270 48.198  1.00 34.70 ? 16   LEU D CA  1 
ATOM   7656  C  C   . LEU D  1 13  ? -43.543 -39.062 49.525  1.00 33.71 ? 16   LEU D C   1 
ATOM   7657  O  O   . LEU D  1 13  ? -42.878 -39.973 50.012  1.00 34.09 ? 16   LEU D O   1 
ATOM   7658  C  CB  . LEU D  1 13  ? -45.251 -40.421 48.333  1.00 31.46 ? 16   LEU D CB  1 
ATOM   7659  C  CG  . LEU D  1 13  ? -46.327 -40.217 49.405  1.00 32.70 ? 16   LEU D CG  1 
ATOM   7660  C  CD1 . LEU D  1 13  ? -47.121 -38.911 49.154  1.00 29.94 ? 16   LEU D CD1 1 
ATOM   7661  C  CD2 . LEU D  1 13  ? -47.269 -41.436 49.498  1.00 29.15 ? 16   LEU D CD2 1 
ATOM   7662  N  N   . VAL D  1 14  ? -43.699 -37.881 50.127  1.00 34.79 ? 17   VAL D N   1 
ATOM   7663  C  CA  . VAL D  1 14  ? -43.196 -37.703 51.491  1.00 33.03 ? 17   VAL D CA  1 
ATOM   7664  C  C   . VAL D  1 14  ? -44.292 -37.501 52.518  1.00 34.63 ? 17   VAL D C   1 
ATOM   7665  O  O   . VAL D  1 14  ? -44.088 -37.767 53.702  1.00 34.87 ? 17   VAL D O   1 
ATOM   7666  C  CB  . VAL D  1 14  ? -42.161 -36.574 51.612  1.00 29.78 ? 17   VAL D CB  1 
ATOM   7667  C  CG1 . VAL D  1 14  ? -40.872 -36.987 50.948  1.00 29.16 ? 17   VAL D CG1 1 
ATOM   7668  C  CG2 . VAL D  1 14  ? -42.715 -35.277 51.054  1.00 25.73 ? 17   VAL D CG2 1 
ATOM   7669  N  N   . ASN D  1 15  ? -45.450 -37.023 52.078  1.00 36.32 ? 18   ASN D N   1 
ATOM   7670  C  CA  . ASN D  1 15  ? -46.639 -37.120 52.918  1.00 40.22 ? 18   ASN D CA  1 
ATOM   7671  C  C   . ASN D  1 15  ? -47.216 -38.542 52.862  1.00 41.96 ? 18   ASN D C   1 
ATOM   7672  O  O   . ASN D  1 15  ? -48.230 -38.800 52.200  1.00 41.51 ? 18   ASN D O   1 
ATOM   7673  C  CB  . ASN D  1 15  ? -47.685 -36.066 52.541  1.00 39.15 ? 18   ASN D CB  1 
ATOM   7674  C  CG  . ASN D  1 15  ? -48.752 -35.895 53.616  1.00 38.62 ? 18   ASN D CG  1 
ATOM   7675  O  OD1 . ASN D  1 15  ? -48.746 -36.601 54.620  1.00 37.75 ? 18   ASN D OD1 1 
ATOM   7676  N  ND2 . ASN D  1 15  ? -49.661 -34.950 53.411  1.00 36.86 ? 18   ASN D ND2 1 
ATOM   7677  N  N   . ASP D  1 16  ? -46.517 -39.459 53.522  1.00 43.18 ? 19   ASP D N   1 
ATOM   7678  C  CA  . ASP D  1 16  ? -46.745 -40.879 53.367  1.00 46.46 ? 19   ASP D CA  1 
ATOM   7679  C  C   . ASP D  1 16  ? -47.016 -41.573 54.708  1.00 49.51 ? 19   ASP D C   1 
ATOM   7680  O  O   . ASP D  1 16  ? -46.988 -40.952 55.780  1.00 47.05 ? 19   ASP D O   1 
ATOM   7681  C  CB  . ASP D  1 16  ? -45.548 -41.529 52.659  1.00 48.80 ? 19   ASP D CB  1 
ATOM   7682  C  CG  . ASP D  1 16  ? -44.289 -41.557 53.524  1.00 50.12 ? 19   ASP D CG  1 
ATOM   7683  O  OD1 . ASP D  1 16  ? -44.268 -40.887 54.578  1.00 51.39 ? 19   ASP D OD1 1 
ATOM   7684  O  OD2 . ASP D  1 16  ? -43.310 -42.240 53.146  1.00 49.57 ? 19   ASP D OD2 1 
ATOM   7685  N  N   . GLU D  1 17  ? -47.274 -42.874 54.634  1.00 52.11 ? 20   GLU D N   1 
ATOM   7686  C  CA  . GLU D  1 17  ? -47.846 -43.611 55.747  1.00 54.11 ? 20   GLU D CA  1 
ATOM   7687  C  C   . GLU D  1 17  ? -46.985 -43.498 57.003  1.00 52.41 ? 20   GLU D C   1 
ATOM   7688  O  O   . GLU D  1 17  ? -47.503 -43.260 58.095  1.00 53.35 ? 20   GLU D O   1 
ATOM   7689  C  CB  . GLU D  1 17  ? -48.040 -45.080 55.359  1.00 58.20 ? 20   GLU D CB  1 
ATOM   7690  C  CG  . GLU D  1 17  ? -48.431 -45.987 56.514  1.00 63.20 ? 20   GLU D CG  1 
ATOM   7691  C  CD  . GLU D  1 17  ? -49.399 -47.080 56.090  1.00 66.20 ? 20   GLU D CD  1 
ATOM   7692  O  OE1 . GLU D  1 17  ? -50.484 -46.747 55.560  1.00 67.40 ? 20   GLU D OE1 1 
ATOM   7693  O  OE2 . GLU D  1 17  ? -49.074 -48.270 56.293  1.00 68.08 ? 20   GLU D OE2 1 
ATOM   7694  N  N   . ALA D  1 18  ? -45.675 -43.678 56.845  1.00 48.62 ? 21   ALA D N   1 
ATOM   7695  C  CA  . ALA D  1 18  ? -44.749 -43.611 57.974  1.00 46.15 ? 21   ALA D CA  1 
ATOM   7696  C  C   . ALA D  1 18  ? -44.509 -42.183 58.482  1.00 42.75 ? 21   ALA D C   1 
ATOM   7697  O  O   . ALA D  1 18  ? -43.751 -41.982 59.424  1.00 41.89 ? 21   ALA D O   1 
ATOM   7698  C  CB  . ALA D  1 18  ? -43.418 -44.295 57.629  1.00 45.46 ? 21   ALA D CB  1 
ATOM   7699  N  N   . HIS D  1 19  ? -45.181 -41.202 57.886  1.00 41.57 ? 22   HIS D N   1 
ATOM   7700  C  CA  . HIS D  1 19  ? -44.886 -39.795 58.170  1.00 39.77 ? 22   HIS D CA  1 
ATOM   7701  C  C   . HIS D  1 19  ? -46.117 -38.930 58.178  1.00 39.68 ? 22   HIS D C   1 
ATOM   7702  O  O   . HIS D  1 19  ? -46.108 -37.833 57.610  1.00 41.96 ? 22   HIS D O   1 
ATOM   7703  C  CB  . HIS D  1 19  ? -43.870 -39.231 57.175  1.00 39.33 ? 22   HIS D CB  1 
ATOM   7704  C  CG  . HIS D  1 19  ? -42.515 -39.835 57.317  1.00 38.85 ? 22   HIS D CG  1 
ATOM   7705  N  ND1 . HIS D  1 19  ? -42.012 -40.735 56.405  1.00 40.95 ? 22   HIS D ND1 1 
ATOM   7706  C  CD2 . HIS D  1 19  ? -41.658 -39.840 58.362  1.00 38.23 ? 22   HIS D CD2 1 
ATOM   7707  C  CE1 . HIS D  1 19  ? -40.850 -41.193 56.838  1.00 38.69 ? 22   HIS D CE1 1 
ATOM   7708  N  NE2 . HIS D  1 19  ? -40.624 -40.681 58.034  1.00 38.57 ? 22   HIS D NE2 1 
ATOM   7709  N  N   . PRO D  1 20  ? -47.178 -39.413 58.832  1.00 38.76 ? 23   PRO D N   1 
ATOM   7710  C  CA  . PRO D  1 20  ? -48.425 -38.671 58.934  1.00 38.88 ? 23   PRO D CA  1 
ATOM   7711  C  C   . PRO D  1 20  ? -48.243 -37.428 59.810  1.00 39.53 ? 23   PRO D C   1 
ATOM   7712  O  O   . PRO D  1 20  ? -47.494 -37.459 60.793  1.00 39.00 ? 23   PRO D O   1 
ATOM   7713  C  CB  . PRO D  1 20  ? -49.351 -39.665 59.634  1.00 40.20 ? 23   PRO D CB  1 
ATOM   7714  C  CG  . PRO D  1 20  ? -48.427 -40.442 60.532  1.00 38.89 ? 23   PRO D CG  1 
ATOM   7715  C  CD  . PRO D  1 20  ? -47.136 -40.567 59.750  1.00 38.16 ? 23   PRO D CD  1 
ATOM   7716  N  N   . TRP D  1 21  ? -48.901 -36.340 59.424  1.00 40.36 ? 24   TRP D N   1 
ATOM   7717  C  CA  . TRP D  1 21  ? -49.034 -35.163 60.265  1.00 43.11 ? 24   TRP D CA  1 
ATOM   7718  C  C   . TRP D  1 21  ? -49.861 -35.487 61.499  1.00 45.10 ? 24   TRP D C   1 
ATOM   7719  O  O   . TRP D  1 21  ? -50.964 -36.009 61.388  1.00 47.36 ? 24   TRP D O   1 
ATOM   7720  C  CB  . TRP D  1 21  ? -49.721 -34.045 59.480  1.00 43.32 ? 24   TRP D CB  1 
ATOM   7721  C  CG  . TRP D  1 21  ? -49.861 -32.758 60.240  1.00 45.74 ? 24   TRP D CG  1 
ATOM   7722  C  CD1 . TRP D  1 21  ? -49.006 -31.690 60.216  1.00 46.31 ? 24   TRP D CD1 1 
ATOM   7723  C  CD2 . TRP D  1 21  ? -50.944 -32.385 61.102  1.00 47.82 ? 24   TRP D CD2 1 
ATOM   7724  N  NE1 . TRP D  1 21  ? -49.483 -30.681 61.022  1.00 47.90 ? 24   TRP D NE1 1 
ATOM   7725  C  CE2 . TRP D  1 21  ? -50.669 -31.085 61.580  1.00 48.37 ? 24   TRP D CE2 1 
ATOM   7726  C  CE3 . TRP D  1 21  ? -52.102 -33.039 61.545  1.00 48.25 ? 24   TRP D CE3 1 
ATOM   7727  C  CZ2 . TRP D  1 21  ? -51.512 -30.427 62.472  1.00 49.67 ? 24   TRP D CZ2 1 
ATOM   7728  C  CZ3 . TRP D  1 21  ? -52.941 -32.381 62.424  1.00 49.14 ? 24   TRP D CZ3 1 
ATOM   7729  C  CH2 . TRP D  1 21  ? -52.649 -31.085 62.871  1.00 49.64 ? 24   TRP D CH2 1 
ATOM   7730  N  N   . LYS D  1 22  ? -49.340 -35.153 62.675  1.00 46.79 ? 25   LYS D N   1 
ATOM   7731  C  CA  . LYS D  1 22  ? -50.141 -35.187 63.897  1.00 47.54 ? 25   LYS D CA  1 
ATOM   7732  C  C   . LYS D  1 22  ? -50.182 -33.810 64.538  1.00 46.32 ? 25   LYS D C   1 
ATOM   7733  O  O   . LYS D  1 22  ? -49.264 -33.014 64.346  1.00 46.59 ? 25   LYS D O   1 
ATOM   7734  C  CB  . LYS D  1 22  ? -49.600 -36.235 64.872  1.00 45.89 ? 25   LYS D CB  1 
ATOM   7735  C  CG  . LYS D  1 22  ? -49.650 -37.640 64.309  1.00 47.17 ? 25   LYS D CG  1 
ATOM   7736  C  CD  . LYS D  1 22  ? -49.275 -38.701 65.333  1.00 48.06 ? 25   LYS D CD  1 
ATOM   7737  C  CE  . LYS D  1 22  ? -49.418 -40.086 64.720  1.00 48.61 ? 25   LYS D CE  1 
ATOM   7738  N  NZ  . LYS D  1 22  ? -48.678 -41.118 65.490  1.00 50.98 ? 25   LYS D NZ  1 
ATOM   7739  N  N   . PRO D  1 23  ? -51.278 -33.500 65.252  1.00 45.67 ? 26   PRO D N   1 
ATOM   7740  C  CA  . PRO D  1 23  ? -51.403 -32.204 65.928  1.00 44.74 ? 26   PRO D CA  1 
ATOM   7741  C  C   . PRO D  1 23  ? -50.420 -32.104 67.089  1.00 42.41 ? 26   PRO D C   1 
ATOM   7742  O  O   . PRO D  1 23  ? -49.825 -33.107 67.480  1.00 42.29 ? 26   PRO D O   1 
ATOM   7743  C  CB  . PRO D  1 23  ? -52.849 -32.212 66.441  1.00 45.76 ? 26   PRO D CB  1 
ATOM   7744  C  CG  . PRO D  1 23  ? -53.192 -33.656 66.586  1.00 45.29 ? 26   PRO D CG  1 
ATOM   7745  C  CD  . PRO D  1 23  ? -52.431 -34.382 65.507  1.00 45.54 ? 26   PRO D CD  1 
ATOM   7746  N  N   . LEU D  1 24  ? -50.201 -30.896 67.589  1.00 42.27 ? 27   LEU D N   1 
ATOM   7747  C  CA  . LEU D  1 24  ? -49.303 -30.698 68.724  1.00 43.99 ? 27   LEU D CA  1 
ATOM   7748  C  C   . LEU D  1 24  ? -49.868 -31.276 70.031  1.00 45.16 ? 27   LEU D C   1 
ATOM   7749  O  O   . LEU D  1 24  ? -51.011 -31.007 70.397  1.00 45.48 ? 27   LEU D O   1 
ATOM   7750  C  CB  . LEU D  1 24  ? -49.000 -29.207 68.905  1.00 44.10 ? 27   LEU D CB  1 
ATOM   7751  C  CG  . LEU D  1 24  ? -48.443 -28.440 67.699  1.00 45.30 ? 27   LEU D CG  1 
ATOM   7752  C  CD1 . LEU D  1 24  ? -48.474 -26.934 67.966  1.00 44.29 ? 27   LEU D CD1 1 
ATOM   7753  C  CD2 . LEU D  1 24  ? -47.031 -28.908 67.351  1.00 43.82 ? 27   LEU D CD2 1 
ATOM   7754  N  N   . ARG D  1 25  ? -49.047 -32.053 70.733  1.00 45.83 ? 28   ARG D N   1 
ATOM   7755  C  CA  . ARG D  1 25  ? -49.238 -32.327 72.154  1.00 46.49 ? 28   ARG D CA  1 
ATOM   7756  C  C   . ARG D  1 25  ? -48.732 -31.153 72.980  1.00 47.97 ? 28   ARG D C   1 
ATOM   7757  O  O   . ARG D  1 25  ? -47.959 -30.336 72.489  1.00 48.97 ? 28   ARG D O   1 
ATOM   7758  C  CB  . ARG D  1 25  ? -48.463 -33.580 72.556  1.00 46.67 ? 28   ARG D CB  1 
ATOM   7759  C  CG  . ARG D  1 25  ? -48.653 -34.766 71.636  1.00 46.67 ? 28   ARG D CG  1 
ATOM   7760  C  CD  . ARG D  1 25  ? -47.607 -35.839 71.926  1.00 48.84 ? 28   ARG D CD  1 
ATOM   7761  N  NE  . ARG D  1 25  ? -46.262 -35.396 71.553  1.00 49.45 ? 28   ARG D NE  1 
ATOM   7762  C  CZ  . ARG D  1 25  ? -45.222 -36.209 71.375  1.00 47.73 ? 28   ARG D CZ  1 
ATOM   7763  N  NH1 . ARG D  1 25  ? -45.354 -37.510 71.557  1.00 47.41 ? 28   ARG D NH1 1 
ATOM   7764  N  NH2 . ARG D  1 25  ? -44.043 -35.716 71.025  1.00 47.54 ? 28   ARG D NH2 1 
ATOM   7765  N  N   . PRO D  1 26  ? -49.127 -31.084 74.259  1.00 49.97 ? 29   PRO D N   1 
ATOM   7766  C  CA  . PRO D  1 26  ? -48.750 -29.898 75.026  1.00 51.03 ? 29   PRO D CA  1 
ATOM   7767  C  C   . PRO D  1 26  ? -47.229 -29.772 75.207  1.00 52.39 ? 29   PRO D C   1 
ATOM   7768  O  O   . PRO D  1 26  ? -46.726 -28.681 75.493  1.00 53.00 ? 29   PRO D O   1 
ATOM   7769  C  CB  . PRO D  1 26  ? -49.460 -30.110 76.372  1.00 51.84 ? 29   PRO D CB  1 
ATOM   7770  C  CG  . PRO D  1 26  ? -50.616 -31.013 76.046  1.00 50.87 ? 29   PRO D CG  1 
ATOM   7771  C  CD  . PRO D  1 26  ? -50.093 -31.933 74.981  1.00 50.03 ? 29   PRO D CD  1 
ATOM   7772  N  N   . GLY D  1 27  ? -46.493 -30.850 74.948  1.00 52.23 ? 30   GLY D N   1 
ATOM   7773  C  CA  . GLY D  1 27  ? -45.025 -30.771 74.941  1.00 53.09 ? 30   GLY D CA  1 
ATOM   7774  C  C   . GLY D  1 27  ? -44.386 -29.972 73.804  1.00 50.69 ? 30   GLY D C   1 
ATOM   7775  O  O   . GLY D  1 27  ? -43.403 -29.248 74.010  1.00 50.00 ? 30   GLY D O   1 
ATOM   7776  N  N   . ASP D  1 28  ? -44.951 -30.097 72.604  1.00 46.95 ? 31   ASP D N   1 
ATOM   7777  C  CA  . ASP D  1 28  ? -44.180 -30.017 71.362  1.00 42.84 ? 31   ASP D CA  1 
ATOM   7778  C  C   . ASP D  1 28  ? -43.738 -28.591 70.992  1.00 39.32 ? 31   ASP D C   1 
ATOM   7779  O  O   . ASP D  1 28  ? -44.541 -27.661 71.022  1.00 34.55 ? 31   ASP D O   1 
ATOM   7780  C  CB  . ASP D  1 28  ? -44.993 -30.613 70.212  1.00 42.79 ? 31   ASP D CB  1 
ATOM   7781  C  CG  . ASP D  1 28  ? -45.441 -32.029 70.485  1.00 44.00 ? 31   ASP D CG  1 
ATOM   7782  O  OD1 . ASP D  1 28  ? -44.669 -32.796 71.112  1.00 43.30 ? 31   ASP D OD1 1 
ATOM   7783  O  OD2 . ASP D  1 28  ? -46.530 -32.404 69.987  1.00 44.65 ? 31   ASP D OD2 1 
ATOM   7784  N  N   . ILE D  1 29  ? -42.479 -28.437 70.581  1.00 34.51 ? 32   ILE D N   1 
ATOM   7785  C  CA  . ILE D  1 29  ? -41.941 -27.108 70.315  1.00 31.27 ? 32   ILE D CA  1 
ATOM   7786  C  C   . ILE D  1 29  ? -41.873 -26.805 68.825  1.00 31.71 ? 32   ILE D C   1 
ATOM   7787  O  O   . ILE D  1 29  ? -41.381 -27.621 68.035  1.00 29.36 ? 32   ILE D O   1 
ATOM   7788  C  CB  . ILE D  1 29  ? -40.567 -26.904 70.952  1.00 31.77 ? 32   ILE D CB  1 
ATOM   7789  C  CG1 . ILE D  1 29  ? -40.708 -26.872 72.477  1.00 31.55 ? 32   ILE D CG1 1 
ATOM   7790  C  CG2 . ILE D  1 29  ? -39.948 -25.607 70.455  1.00 29.02 ? 32   ILE D CG2 1 
ATOM   7791  C  CD1 . ILE D  1 29  ? -39.442 -27.131 73.222  1.00 31.30 ? 32   ILE D CD1 1 
ATOM   7792  N  N   . ARG D  1 30  ? -42.425 -25.652 68.446  1.00 28.73 ? 33   ARG D N   1 
ATOM   7793  C  CA  . ARG D  1 30  ? -42.376 -25.188 67.072  1.00 31.33 ? 33   ARG D CA  1 
ATOM   7794  C  C   . ARG D  1 30  ? -41.866 -23.745 67.039  1.00 34.23 ? 33   ARG D C   1 
ATOM   7795  O  O   . ARG D  1 30  ? -42.201 -22.936 67.912  1.00 35.49 ? 33   ARG D O   1 
ATOM   7796  C  CB  . ARG D  1 30  ? -43.760 -25.291 66.413  1.00 29.34 ? 33   ARG D CB  1 
ATOM   7797  C  CG  . ARG D  1 30  ? -44.344 -26.723 66.379  1.00 30.08 ? 33   ARG D CG  1 
ATOM   7798  C  CD  . ARG D  1 30  ? -43.623 -27.624 65.364  1.00 29.32 ? 33   ARG D CD  1 
ATOM   7799  N  NE  . ARG D  1 30  ? -44.177 -28.981 65.278  1.00 29.70 ? 33   ARG D NE  1 
ATOM   7800  C  CZ  . ARG D  1 30  ? -43.793 -30.003 66.046  1.00 31.01 ? 33   ARG D CZ  1 
ATOM   7801  N  NH1 . ARG D  1 30  ? -42.861 -29.821 66.979  1.00 30.68 ? 33   ARG D NH1 1 
ATOM   7802  N  NH2 . ARG D  1 30  ? -44.306 -31.219 65.858  1.00 31.10 ? 33   ARG D NH2 1 
ATOM   7803  N  N   . GLY D  1 31  ? -41.048 -23.431 66.037  1.00 31.92 ? 34   GLY D N   1 
ATOM   7804  C  CA  . GLY D  1 31  ? -40.387 -22.141 65.977  1.00 29.60 ? 34   GLY D CA  1 
ATOM   7805  C  C   . GLY D  1 31  ? -40.612 -21.378 64.687  1.00 29.56 ? 34   GLY D C   1 
ATOM   7806  O  O   . GLY D  1 31  ? -41.694 -21.435 64.089  1.00 26.24 ? 34   GLY D O   1 
ATOM   7807  N  N   . PRO D  1 32  ? -39.589 -20.619 64.267  1.00 29.21 ? 35   PRO D N   1 
ATOM   7808  C  CA  . PRO D  1 32  ? -39.752 -19.619 63.228  1.00 27.12 ? 35   PRO D CA  1 
ATOM   7809  C  C   . PRO D  1 32  ? -39.472 -20.187 61.831  1.00 27.92 ? 35   PRO D C   1 
ATOM   7810  O  O   . PRO D  1 32  ? -39.651 -19.478 60.853  1.00 27.05 ? 35   PRO D O   1 
ATOM   7811  C  CB  . PRO D  1 32  ? -38.704 -18.586 63.603  1.00 26.96 ? 35   PRO D CB  1 
ATOM   7812  C  CG  . PRO D  1 32  ? -37.573 -19.427 64.136  1.00 27.84 ? 35   PRO D CG  1 
ATOM   7813  C  CD  . PRO D  1 32  ? -38.241 -20.583 64.860  1.00 27.32 ? 35   PRO D CD  1 
ATOM   7814  N  N   . CYS D  1 33  ? -39.101 -21.466 61.741  1.00 30.31 ? 36   CYS D N   1 
ATOM   7815  C  CA  . CYS D  1 33  ? -38.880 -22.134 60.436  1.00 32.13 ? 36   CYS D CA  1 
ATOM   7816  C  C   . CYS D  1 33  ? -40.038 -23.062 60.046  1.00 31.52 ? 36   CYS D C   1 
ATOM   7817  O  O   . CYS D  1 33  ? -40.240 -24.106 60.673  1.00 32.46 ? 36   CYS D O   1 
ATOM   7818  C  CB  . CYS D  1 33  ? -37.565 -22.929 60.439  1.00 30.28 ? 36   CYS D CB  1 
ATOM   7819  S  SG  . CYS D  1 33  ? -37.163 -23.817 58.870  1.00 31.43 ? 36   CYS D SG  1 
ATOM   7820  N  N   . PRO D  1 34  ? -40.761 -22.709 58.973  1.00 31.98 ? 37   PRO D N   1 
ATOM   7821  C  CA  . PRO D  1 34  ? -41.841 -23.548 58.484  1.00 32.48 ? 37   PRO D CA  1 
ATOM   7822  C  C   . PRO D  1 34  ? -41.310 -24.844 57.910  1.00 34.14 ? 37   PRO D C   1 
ATOM   7823  O  O   . PRO D  1 34  ? -42.009 -25.859 57.927  1.00 35.56 ? 37   PRO D O   1 
ATOM   7824  C  CB  . PRO D  1 34  ? -42.506 -22.699 57.385  1.00 33.30 ? 37   PRO D CB  1 
ATOM   7825  C  CG  . PRO D  1 34  ? -41.534 -21.621 57.032  1.00 32.89 ? 37   PRO D CG  1 
ATOM   7826  C  CD  . PRO D  1 34  ? -40.416 -21.620 58.036  1.00 33.99 ? 37   PRO D CD  1 
ATOM   7827  N  N   . GLY D  1 35  ? -40.059 -24.829 57.459  1.00 32.38 ? 38   GLY D N   1 
ATOM   7828  C  CA  . GLY D  1 35  ? -39.413 -26.063 57.063  1.00 30.86 ? 38   GLY D CA  1 
ATOM   7829  C  C   . GLY D  1 35  ? -39.340 -27.035 58.230  1.00 31.51 ? 38   GLY D C   1 
ATOM   7830  O  O   . GLY D  1 35  ? -39.955 -28.096 58.200  1.00 28.88 ? 38   GLY D O   1 
ATOM   7831  N  N   . LEU D  1 36  ? -38.541 -26.700 59.239  1.00 29.20 ? 39   LEU D N   1 
ATOM   7832  C  CA  . LEU D  1 36  ? -38.275 -27.635 60.332  1.00 29.09 ? 39   LEU D CA  1 
ATOM   7833  C  C   . LEU D  1 36  ? -39.556 -27.954 61.107  1.00 29.64 ? 39   LEU D C   1 
ATOM   7834  O  O   . LEU D  1 36  ? -39.738 -29.066 61.608  1.00 28.67 ? 39   LEU D O   1 
ATOM   7835  C  CB  . LEU D  1 36  ? -37.209 -27.066 61.269  1.00 27.06 ? 39   LEU D CB  1 
ATOM   7836  C  CG  . LEU D  1 36  ? -35.836 -26.908 60.625  1.00 27.53 ? 39   LEU D CG  1 
ATOM   7837  C  CD1 . LEU D  1 36  ? -34.773 -26.453 61.625  1.00 28.81 ? 39   LEU D CD1 1 
ATOM   7838  C  CD2 . LEU D  1 36  ? -35.445 -28.201 59.992  1.00 29.04 ? 39   LEU D CD2 1 
ATOM   7839  N  N   . ASN D  1 37  ? -40.473 -26.993 61.131  1.00 29.64 ? 40   ASN D N   1 
ATOM   7840  C  CA  . ASN D  1 37  ? -41.782 -27.193 61.746  1.00 30.78 ? 40   ASN D CA  1 
ATOM   7841  C  C   . ASN D  1 37  ? -42.557 -28.325 61.080  1.00 32.19 ? 40   ASN D C   1 
ATOM   7842  O  O   . ASN D  1 37  ? -43.147 -29.156 61.758  1.00 35.51 ? 40   ASN D O   1 
ATOM   7843  C  CB  . ASN D  1 37  ? -42.597 -25.893 61.693  1.00 28.60 ? 40   ASN D CB  1 
ATOM   7844  C  CG  . ASN D  1 37  ? -42.163 -24.888 62.732  1.00 24.52 ? 40   ASN D CG  1 
ATOM   7845  O  OD1 . ASN D  1 37  ? -41.342 -25.180 63.612  1.00 23.35 ? 40   ASN D OD1 1 
ATOM   7846  N  ND2 . ASN D  1 37  ? -42.723 -23.688 62.648  1.00 26.76 ? 40   ASN D ND2 1 
ATOM   7847  N  N   . THR D  1 38  ? -42.551 -28.364 59.750  1.00 33.59 ? 41   THR D N   1 
ATOM   7848  C  CA  . THR D  1 38  ? -43.309 -29.386 59.023  1.00 32.39 ? 41   THR D CA  1 
ATOM   7849  C  C   . THR D  1 38  ? -42.706 -30.779 59.163  1.00 33.37 ? 41   THR D C   1 
ATOM   7850  O  O   . THR D  1 38  ? -43.433 -31.768 59.261  1.00 33.99 ? 41   THR D O   1 
ATOM   7851  C  CB  . THR D  1 38  ? -43.500 -29.040 57.529  1.00 31.29 ? 41   THR D CB  1 
ATOM   7852  O  OG1 . THR D  1 38  ? -44.027 -27.715 57.411  1.00 28.80 ? 41   THR D OG1 1 
ATOM   7853  C  CG2 . THR D  1 38  ? -44.486 -30.005 56.886  1.00 31.72 ? 41   THR D CG2 1 
ATOM   7854  N  N   . LEU D  1 39  ? -41.382 -30.867 59.229  1.00 31.44 ? 42   LEU D N   1 
ATOM   7855  C  CA  . LEU D  1 39  ? -40.755 -32.175 59.368  1.00 32.04 ? 42   LEU D CA  1 
ATOM   7856  C  C   . LEU D  1 39  ? -40.951 -32.795 60.760  1.00 35.39 ? 42   LEU D C   1 
ATOM   7857  O  O   . LEU D  1 39  ? -40.935 -34.031 60.926  1.00 36.63 ? 42   LEU D O   1 
ATOM   7858  C  CB  . LEU D  1 39  ? -39.274 -32.090 59.025  1.00 33.01 ? 42   LEU D CB  1 
ATOM   7859  C  CG  . LEU D  1 39  ? -38.951 -31.530 57.634  1.00 32.95 ? 42   LEU D CG  1 
ATOM   7860  C  CD1 . LEU D  1 39  ? -37.483 -31.197 57.573  1.00 31.32 ? 42   LEU D CD1 1 
ATOM   7861  C  CD2 . LEU D  1 39  ? -39.321 -32.525 56.540  1.00 29.85 ? 42   LEU D CD2 1 
ATOM   7862  N  N   . ALA D  1 40  ? -41.075 -31.933 61.765  1.00 34.25 ? 43   ALA D N   1 
ATOM   7863  C  CA  . ALA D  1 40  ? -41.394 -32.376 63.121  1.00 33.91 ? 43   ALA D CA  1 
ATOM   7864  C  C   . ALA D  1 40  ? -42.845 -32.855 63.203  1.00 32.56 ? 43   ALA D C   1 
ATOM   7865  O  O   . ALA D  1 40  ? -43.130 -33.899 63.794  1.00 34.56 ? 43   ALA D O   1 
ATOM   7866  C  CB  . ALA D  1 40  ? -41.133 -31.248 64.141  1.00 31.07 ? 43   ALA D CB  1 
ATOM   7867  N  N   . SER D  1 41  ? -43.756 -32.123 62.575  1.00 30.27 ? 44   SER D N   1 
ATOM   7868  C  CA  . SER D  1 41  ? -45.154 -32.476 62.679  1.00 32.73 ? 44   SER D CA  1 
ATOM   7869  C  C   . SER D  1 41  ? -45.517 -33.693 61.844  1.00 33.81 ? 44   SER D C   1 
ATOM   7870  O  O   . SER D  1 41  ? -46.628 -34.207 61.952  1.00 38.30 ? 44   SER D O   1 
ATOM   7871  C  CB  . SER D  1 41  ? -46.052 -31.289 62.355  1.00 33.33 ? 44   SER D CB  1 
ATOM   7872  O  OG  . SER D  1 41  ? -46.055 -30.381 63.442  1.00 35.05 ? 44   SER D OG  1 
ATOM   7873  N  N   . HIS D  1 42  ? -44.558 -34.194 61.072  1.00 32.05 ? 45   HIS D N   1 
ATOM   7874  C  CA  . HIS D  1 42  ? -44.764 -35.391 60.261  1.00 30.87 ? 45   HIS D CA  1 
ATOM   7875  C  C   . HIS D  1 42  ? -43.867 -36.519 60.735  1.00 31.16 ? 45   HIS D C   1 
ATOM   7876  O  O   . HIS D  1 42  ? -43.927 -37.615 60.204  1.00 35.24 ? 45   HIS D O   1 
ATOM   7877  C  CB  . HIS D  1 42  ? -44.490 -35.115 58.773  1.00 29.88 ? 45   HIS D CB  1 
ATOM   7878  C  CG  . HIS D  1 42  ? -45.625 -34.454 58.049  1.00 28.43 ? 45   HIS D CG  1 
ATOM   7879  N  ND1 . HIS D  1 42  ? -46.484 -35.146 57.219  1.00 30.96 ? 45   HIS D ND1 1 
ATOM   7880  C  CD2 . HIS D  1 42  ? -46.009 -33.157 57.983  1.00 27.34 ? 45   HIS D CD2 1 
ATOM   7881  C  CE1 . HIS D  1 42  ? -47.386 -34.314 56.725  1.00 27.19 ? 45   HIS D CE1 1 
ATOM   7882  N  NE2 . HIS D  1 42  ? -47.121 -33.101 57.174  1.00 25.67 ? 45   HIS D NE2 1 
ATOM   7883  N  N   . GLY D  1 43  ? -43.005 -36.257 61.711  1.00 33.19 ? 46   GLY D N   1 
ATOM   7884  C  CA  . GLY D  1 43  ? -42.190 -37.336 62.284  1.00 32.66 ? 46   GLY D CA  1 
ATOM   7885  C  C   . GLY D  1 43  ? -40.925 -37.656 61.495  1.00 34.74 ? 46   GLY D C   1 
ATOM   7886  O  O   . GLY D  1 43  ? -40.291 -38.706 61.701  1.00 30.39 ? 46   GLY D O   1 
ATOM   7887  N  N   . TYR D  1 44  ? -40.499 -36.722 60.643  1.00 34.50 ? 47   TYR D N   1 
ATOM   7888  C  CA  . TYR D  1 44  ? -39.144 -36.800 60.109  1.00 34.41 ? 47   TYR D CA  1 
ATOM   7889  C  C   . TYR D  1 44  ? -38.162 -36.386 61.196  1.00 33.82 ? 47   TYR D C   1 
ATOM   7890  O  O   . TYR D  1 44  ? -37.080 -36.956 61.322  1.00 36.56 ? 47   TYR D O   1 
ATOM   7891  C  CB  . TYR D  1 44  ? -38.991 -35.942 58.851  1.00 35.55 ? 47   TYR D CB  1 
ATOM   7892  C  CG  . TYR D  1 44  ? -39.712 -36.518 57.648  1.00 35.87 ? 47   TYR D CG  1 
ATOM   7893  C  CD1 . TYR D  1 44  ? -39.248 -37.678 57.029  1.00 37.72 ? 47   TYR D CD1 1 
ATOM   7894  C  CD2 . TYR D  1 44  ? -40.889 -35.948 57.178  1.00 34.89 ? 47   TYR D CD2 1 
ATOM   7895  C  CE1 . TYR D  1 44  ? -39.895 -38.211 55.939  1.00 37.17 ? 47   TYR D CE1 1 
ATOM   7896  C  CE2 . TYR D  1 44  ? -41.553 -36.482 56.087  1.00 35.61 ? 47   TYR D CE2 1 
ATOM   7897  C  CZ  . TYR D  1 44  ? -41.044 -37.609 55.469  1.00 36.60 ? 47   TYR D CZ  1 
ATOM   7898  O  OH  . TYR D  1 44  ? -41.729 -38.190 54.431  1.00 37.16 ? 47   TYR D OH  1 
ATOM   7899  N  N   . LEU D  1 45  ? -38.584 -35.430 62.019  1.00 33.95 ? 48   LEU D N   1 
ATOM   7900  C  CA  . LEU D  1 45  ? -37.904 -35.099 63.266  1.00 33.83 ? 48   LEU D CA  1 
ATOM   7901  C  C   . LEU D  1 45  ? -38.709 -35.628 64.456  1.00 36.13 ? 48   LEU D C   1 
ATOM   7902  O  O   . LEU D  1 45  ? -39.889 -35.967 64.299  1.00 34.12 ? 48   LEU D O   1 
ATOM   7903  C  CB  . LEU D  1 45  ? -37.777 -33.587 63.386  1.00 32.50 ? 48   LEU D CB  1 
ATOM   7904  C  CG  . LEU D  1 45  ? -36.733 -32.949 62.481  1.00 31.10 ? 48   LEU D CG  1 
ATOM   7905  C  CD1 . LEU D  1 45  ? -36.741 -31.454 62.730  1.00 29.87 ? 48   LEU D CD1 1 
ATOM   7906  C  CD2 . LEU D  1 45  ? -35.389 -33.566 62.811  1.00 29.07 ? 48   LEU D CD2 1 
ATOM   7907  N  N   . PRO D  1 46  ? -38.097 -35.652 65.658  1.00 34.85 ? 49   PRO D N   1 
ATOM   7908  C  CA  . PRO D  1 46  ? -38.927 -35.875 66.847  1.00 35.47 ? 49   PRO D CA  1 
ATOM   7909  C  C   . PRO D  1 46  ? -40.034 -34.832 66.952  1.00 35.36 ? 49   PRO D C   1 
ATOM   7910  O  O   . PRO D  1 46  ? -39.801 -33.637 66.719  1.00 34.62 ? 49   PRO D O   1 
ATOM   7911  C  CB  . PRO D  1 46  ? -37.935 -35.730 68.002  1.00 34.38 ? 49   PRO D CB  1 
ATOM   7912  C  CG  . PRO D  1 46  ? -36.626 -36.178 67.417  1.00 34.81 ? 49   PRO D CG  1 
ATOM   7913  C  CD  . PRO D  1 46  ? -36.657 -35.773 65.951  1.00 34.76 ? 49   PRO D CD  1 
ATOM   7914  N  N   . ARG D  1 47  ? -41.241 -35.291 67.262  1.00 35.18 ? 50   ARG D N   1 
ATOM   7915  C  CA  . ARG D  1 47  ? -42.410 -34.429 67.228  1.00 34.50 ? 50   ARG D CA  1 
ATOM   7916  C  C   . ARG D  1 47  ? -42.445 -33.356 68.316  1.00 34.73 ? 50   ARG D C   1 
ATOM   7917  O  O   . ARG D  1 47  ? -43.237 -32.422 68.217  1.00 35.78 ? 50   ARG D O   1 
ATOM   7918  C  CB  . ARG D  1 47  ? -43.696 -35.257 67.222  1.00 36.29 ? 50   ARG D CB  1 
ATOM   7919  C  CG  . ARG D  1 47  ? -43.716 -36.291 66.108  1.00 38.08 ? 50   ARG D CG  1 
ATOM   7920  C  CD  . ARG D  1 47  ? -44.989 -37.152 66.093  1.00 36.51 ? 50   ARG D CD  1 
ATOM   7921  N  NE  . ARG D  1 47  ? -45.031 -37.972 64.887  1.00 35.18 ? 50   ARG D NE  1 
ATOM   7922  C  CZ  . ARG D  1 47  ? -45.588 -37.591 63.738  1.00 35.28 ? 50   ARG D CZ  1 
ATOM   7923  N  NH1 . ARG D  1 47  ? -46.262 -36.450 63.660  1.00 36.25 ? 50   ARG D NH1 1 
ATOM   7924  N  NH2 . ARG D  1 47  ? -45.536 -38.385 62.680  1.00 35.78 ? 50   ARG D NH2 1 
ATOM   7925  N  N   . ASN D  1 48  ? -41.547 -33.444 69.303  1.00 35.73 ? 51   ASN D N   1 
ATOM   7926  C  CA  . ASN D  1 48  ? -41.456 -32.437 70.369  1.00 34.08 ? 51   ASN D CA  1 
ATOM   7927  C  C   . ASN D  1 48  ? -40.570 -31.255 69.996  1.00 35.85 ? 51   ASN D C   1 
ATOM   7928  O  O   . ASN D  1 48  ? -40.617 -30.186 70.630  1.00 34.87 ? 51   ASN D O   1 
ATOM   7929  C  CB  . ASN D  1 48  ? -41.001 -33.059 71.698  1.00 35.24 ? 51   ASN D CB  1 
ATOM   7930  C  CG  . ASN D  1 48  ? -39.549 -33.512 71.670  1.00 38.90 ? 51   ASN D CG  1 
ATOM   7931  O  OD1 . ASN D  1 48  ? -38.898 -33.493 70.623  1.00 41.37 ? 51   ASN D OD1 1 
ATOM   7932  N  ND2 . ASN D  1 48  ? -39.022 -33.888 72.833  1.00 36.41 ? 51   ASN D ND2 1 
ATOM   7933  N  N   . GLY D  1 49  ? -39.825 -31.415 68.906  1.00 36.69 ? 52   GLY D N   1 
ATOM   7934  C  CA  . GLY D  1 49  ? -39.163 -30.281 68.266  1.00 32.30 ? 52   GLY D CA  1 
ATOM   7935  C  C   . GLY D  1 49  ? -37.763 -30.148 68.803  1.00 32.19 ? 52   GLY D C   1 
ATOM   7936  O  O   . GLY D  1 49  ? -37.191 -29.060 68.788  1.00 33.60 ? 52   GLY D O   1 
ATOM   7937  N  N   . VAL D  1 50  ? -37.230 -31.261 69.309  1.00 31.34 ? 53   VAL D N   1 
ATOM   7938  C  CA  . VAL D  1 50  ? -35.886 -31.306 69.856  1.00 30.24 ? 53   VAL D CA  1 
ATOM   7939  C  C   . VAL D  1 50  ? -35.063 -32.408 69.192  1.00 31.67 ? 53   VAL D C   1 
ATOM   7940  O  O   . VAL D  1 50  ? -35.412 -33.600 69.231  1.00 29.08 ? 53   VAL D O   1 
ATOM   7941  C  CB  . VAL D  1 50  ? -35.882 -31.515 71.384  1.00 33.62 ? 53   VAL D CB  1 
ATOM   7942  C  CG1 . VAL D  1 50  ? -34.487 -31.907 71.859  1.00 34.54 ? 53   VAL D CG1 1 
ATOM   7943  C  CG2 . VAL D  1 50  ? -36.362 -30.252 72.105  1.00 34.15 ? 53   VAL D CG2 1 
ATOM   7944  N  N   . ALA D  1 51  ? -33.969 -31.998 68.568  1.00 30.09 ? 54   ALA D N   1 
ATOM   7945  C  CA  . ALA D  1 51  ? -33.299 -32.847 67.604  1.00 31.04 ? 54   ALA D CA  1 
ATOM   7946  C  C   . ALA D  1 51  ? -31.803 -32.614 67.720  1.00 29.33 ? 54   ALA D C   1 
ATOM   7947  O  O   . ALA D  1 51  ? -31.372 -31.557 68.171  1.00 31.30 ? 54   ALA D O   1 
ATOM   7948  C  CB  . ALA D  1 51  ? -33.791 -32.506 66.184  1.00 28.59 ? 54   ALA D CB  1 
ATOM   7949  N  N   . THR D  1 52  ? -31.024 -33.613 67.337  1.00 28.53 ? 55   THR D N   1 
ATOM   7950  C  CA  . THR D  1 52  ? -29.610 -33.421 67.077  1.00 30.21 ? 55   THR D CA  1 
ATOM   7951  C  C   . THR D  1 52  ? -29.421 -32.893 65.649  1.00 30.47 ? 55   THR D C   1 
ATOM   7952  O  O   . THR D  1 52  ? -30.286 -33.069 64.780  1.00 29.92 ? 55   THR D O   1 
ATOM   7953  C  CB  . THR D  1 52  ? -28.832 -34.750 67.189  1.00 29.69 ? 55   THR D CB  1 
ATOM   7954  O  OG1 . THR D  1 52  ? -29.194 -35.575 66.088  1.00 28.40 ? 55   THR D OG1 1 
ATOM   7955  C  CG2 . THR D  1 52  ? -29.166 -35.491 68.519  1.00 27.51 ? 55   THR D CG2 1 
ATOM   7956  N  N   . PRO D  1 53  ? -28.264 -32.272 65.394  1.00 29.55 ? 56   PRO D N   1 
ATOM   7957  C  CA  . PRO D  1 53  ? -27.965 -31.776 64.059  1.00 27.86 ? 56   PRO D CA  1 
ATOM   7958  C  C   . PRO D  1 53  ? -28.141 -32.874 63.011  1.00 29.23 ? 56   PRO D C   1 
ATOM   7959  O  O   . PRO D  1 53  ? -28.769 -32.645 61.972  1.00 28.34 ? 56   PRO D O   1 
ATOM   7960  C  CB  . PRO D  1 53  ? -26.501 -31.350 64.178  1.00 29.11 ? 56   PRO D CB  1 
ATOM   7961  C  CG  . PRO D  1 53  ? -26.361 -30.929 65.615  1.00 28.49 ? 56   PRO D CG  1 
ATOM   7962  C  CD  . PRO D  1 53  ? -27.235 -31.890 66.385  1.00 27.09 ? 56   PRO D CD  1 
ATOM   7963  N  N   . VAL D  1 54  ? -27.650 -34.073 63.320  1.00 27.76 ? 57   VAL D N   1 
ATOM   7964  C  CA  . VAL D  1 54  ? -27.715 -35.194 62.399  1.00 28.99 ? 57   VAL D CA  1 
ATOM   7965  C  C   . VAL D  1 54  ? -29.151 -35.588 62.067  1.00 31.44 ? 57   VAL D C   1 
ATOM   7966  O  O   . VAL D  1 54  ? -29.489 -35.835 60.900  1.00 33.29 ? 57   VAL D O   1 
ATOM   7967  C  CB  . VAL D  1 54  ? -26.944 -36.427 62.948  1.00 29.31 ? 57   VAL D CB  1 
ATOM   7968  C  CG1 . VAL D  1 54  ? -27.461 -37.699 62.303  1.00 27.64 ? 57   VAL D CG1 1 
ATOM   7969  C  CG2 . VAL D  1 54  ? -25.437 -36.274 62.694  1.00 25.04 ? 57   VAL D CG2 1 
ATOM   7970  N  N   . GLN D  1 55  ? -30.008 -35.641 63.079  1.00 32.42 ? 58   GLN D N   1 
ATOM   7971  C  CA  . GLN D  1 55  ? -31.439 -35.878 62.833  1.00 31.76 ? 58   GLN D CA  1 
ATOM   7972  C  C   . GLN D  1 55  ? -31.978 -34.811 61.891  1.00 29.22 ? 58   GLN D C   1 
ATOM   7973  O  O   . GLN D  1 55  ? -32.803 -35.080 61.022  1.00 30.64 ? 58   GLN D O   1 
ATOM   7974  C  CB  . GLN D  1 55  ? -32.240 -35.887 64.149  1.00 30.05 ? 58   GLN D CB  1 
ATOM   7975  C  CG  . GLN D  1 55  ? -32.171 -37.210 64.885  1.00 31.18 ? 58   GLN D CG  1 
ATOM   7976  C  CD  . GLN D  1 55  ? -32.848 -37.203 66.264  1.00 33.49 ? 58   GLN D CD  1 
ATOM   7977  O  OE1 . GLN D  1 55  ? -32.820 -36.207 66.994  1.00 32.12 ? 58   GLN D OE1 1 
ATOM   7978  N  NE2 . GLN D  1 55  ? -33.385 -38.355 66.652  1.00 33.24 ? 58   GLN D NE2 1 
ATOM   7979  N  N   . ILE D  1 56  ? -31.548 -33.578 62.104  1.00 28.75 ? 59   ILE D N   1 
ATOM   7980  C  CA  . ILE D  1 56  ? -32.116 -32.458 61.374  1.00 27.48 ? 59   ILE D CA  1 
ATOM   7981  C  C   . ILE D  1 56  ? -31.693 -32.503 59.892  1.00 28.13 ? 59   ILE D C   1 
ATOM   7982  O  O   . ILE D  1 56  ? -32.478 -32.196 58.998  1.00 27.46 ? 59   ILE D O   1 
ATOM   7983  C  CB  . ILE D  1 56  ? -31.677 -31.146 62.012  1.00 28.84 ? 59   ILE D CB  1 
ATOM   7984  C  CG1 . ILE D  1 56  ? -32.385 -30.970 63.353  1.00 28.12 ? 59   ILE D CG1 1 
ATOM   7985  C  CG2 . ILE D  1 56  ? -31.919 -29.965 61.061  1.00 28.75 ? 59   ILE D CG2 1 
ATOM   7986  C  CD1 . ILE D  1 56  ? -31.903 -29.794 64.180  1.00 28.05 ? 59   ILE D CD1 1 
ATOM   7987  N  N   . ILE D  1 57  ? -30.473 -32.964 59.638  1.00 25.38 ? 60   ILE D N   1 
ATOM   7988  C  CA  . ILE D  1 57  ? -29.943 -32.975 58.293  1.00 25.07 ? 60   ILE D CA  1 
ATOM   7989  C  C   . ILE D  1 57  ? -30.548 -34.112 57.503  1.00 26.34 ? 60   ILE D C   1 
ATOM   7990  O  O   . ILE D  1 57  ? -30.902 -33.948 56.339  1.00 26.38 ? 60   ILE D O   1 
ATOM   7991  C  CB  . ILE D  1 57  ? -28.400 -33.071 58.282  1.00 23.83 ? 60   ILE D CB  1 
ATOM   7992  C  CG1 . ILE D  1 57  ? -27.783 -31.761 58.768  1.00 20.85 ? 60   ILE D CG1 1 
ATOM   7993  C  CG2 . ILE D  1 57  ? -27.890 -33.364 56.863  1.00 23.28 ? 60   ILE D CG2 1 
ATOM   7994  C  CD1 . ILE D  1 57  ? -26.311 -31.884 59.119  1.00 20.82 ? 60   ILE D CD1 1 
ATOM   7995  N  N   . ASN D  1 58  ? -30.642 -35.281 58.125  1.00 29.95 ? 61   ASN D N   1 
ATOM   7996  C  CA  . ASN D  1 58  ? -31.412 -36.362 57.539  1.00 31.17 ? 61   ASN D CA  1 
ATOM   7997  C  C   . ASN D  1 58  ? -32.838 -35.906 57.226  1.00 28.21 ? 61   ASN D C   1 
ATOM   7998  O  O   . ASN D  1 58  ? -33.339 -36.140 56.140  1.00 30.46 ? 61   ASN D O   1 
ATOM   7999  C  CB  . ASN D  1 58  ? -31.399 -37.602 58.437  1.00 32.79 ? 61   ASN D CB  1 
ATOM   8000  C  CG  . ASN D  1 58  ? -30.054 -38.317 58.430  1.00 33.54 ? 61   ASN D CG  1 
ATOM   8001  O  OD1 . ASN D  1 58  ? -29.371 -38.374 57.413  1.00 35.61 ? 61   ASN D OD1 1 
ATOM   8002  N  ND2 . ASN D  1 58  ? -29.683 -38.882 59.563  1.00 35.39 ? 61   ASN D ND2 1 
ATOM   8003  N  N   . ALA D  1 59  ? -33.423 -35.115 58.112  1.00 28.02 ? 62   ALA D N   1 
ATOM   8004  C  CA  . ALA D  1 59  ? -34.828 -34.745 57.977  1.00 26.86 ? 62   ALA D CA  1 
ATOM   8005  C  C   . ALA D  1 59  ? -35.070 -33.835 56.787  1.00 27.59 ? 62   ALA D C   1 
ATOM   8006  O  O   . ALA D  1 59  ? -35.976 -34.086 55.989  1.00 27.97 ? 62   ALA D O   1 
ATOM   8007  C  CB  . ALA D  1 59  ? -35.342 -34.104 59.249  1.00 26.91 ? 62   ALA D CB  1 
ATOM   8008  N  N   . VAL D  1 60  ? -34.255 -32.787 56.652  1.00 23.51 ? 63   VAL D N   1 
ATOM   8009  C  CA  . VAL D  1 60  ? -34.475 -31.830 55.579  1.00 23.02 ? 63   VAL D CA  1 
ATOM   8010  C  C   . VAL D  1 60  ? -34.168 -32.462 54.214  1.00 23.42 ? 63   VAL D C   1 
ATOM   8011  O  O   . VAL D  1 60  ? -34.754 -32.095 53.204  1.00 22.87 ? 63   VAL D O   1 
ATOM   8012  C  CB  . VAL D  1 60  ? -33.674 -30.496 55.805  1.00 23.58 ? 63   VAL D CB  1 
ATOM   8013  C  CG1 . VAL D  1 60  ? -34.047 -29.875 57.176  1.00 19.00 ? 63   VAL D CG1 1 
ATOM   8014  C  CG2 . VAL D  1 60  ? -32.168 -30.753 55.737  1.00 18.77 ? 63   VAL D CG2 1 
ATOM   8015  N  N   . GLN D  1 61  ? -33.268 -33.430 54.185  1.00 23.97 ? 64   GLN D N   1 
ATOM   8016  C  CA  . GLN D  1 61  ? -32.938 -34.088 52.931  1.00 29.05 ? 64   GLN D CA  1 
ATOM   8017  C  C   . GLN D  1 61  ? -34.052 -35.054 52.485  1.00 32.65 ? 64   GLN D C   1 
ATOM   8018  O  O   . GLN D  1 61  ? -34.611 -34.907 51.386  1.00 28.95 ? 64   GLN D O   1 
ATOM   8019  C  CB  . GLN D  1 61  ? -31.580 -34.796 53.029  1.00 28.66 ? 64   GLN D CB  1 
ATOM   8020  C  CG  . GLN D  1 61  ? -30.388 -33.835 53.092  1.00 31.89 ? 64   GLN D CG  1 
ATOM   8021  C  CD  . GLN D  1 61  ? -29.028 -34.552 53.028  1.00 32.10 ? 64   GLN D CD  1 
ATOM   8022  O  OE1 . GLN D  1 61  ? -28.016 -33.958 52.658  1.00 30.13 ? 64   GLN D OE1 1 
ATOM   8023  N  NE2 . GLN D  1 61  ? -29.016 -35.831 53.360  1.00 31.43 ? 64   GLN D NE2 1 
ATOM   8024  N  N   . GLU D  1 62  ? -34.378 -36.020 53.350  1.00 34.17 ? 65   GLU D N   1 
ATOM   8025  C  CA  . GLU D  1 62  ? -35.484 -36.958 53.119  1.00 37.85 ? 65   GLU D CA  1 
ATOM   8026  C  C   . GLU D  1 62  ? -36.800 -36.240 52.862  1.00 36.08 ? 65   GLU D C   1 
ATOM   8027  O  O   . GLU D  1 62  ? -37.410 -36.385 51.808  1.00 36.55 ? 65   GLU D O   1 
ATOM   8028  C  CB  . GLU D  1 62  ? -35.659 -37.886 54.324  1.00 41.18 ? 65   GLU D CB  1 
ATOM   8029  C  CG  . GLU D  1 62  ? -34.776 -39.115 54.300  1.00 47.22 ? 65   GLU D CG  1 
ATOM   8030  C  CD  . GLU D  1 62  ? -35.005 -39.975 53.062  1.00 51.63 ? 65   GLU D CD  1 
ATOM   8031  O  OE1 . GLU D  1 62  ? -36.097 -40.593 52.931  1.00 53.38 ? 65   GLU D OE1 1 
ATOM   8032  O  OE2 . GLU D  1 62  ? -34.076 -40.054 52.228  1.00 52.19 ? 65   GLU D OE2 1 
ATOM   8033  N  N   . GLY D  1 63  ? -37.246 -35.477 53.846  1.00 33.12 ? 66   GLY D N   1 
ATOM   8034  C  CA  . GLY D  1 63  ? -38.568 -34.899 53.780  1.00 34.29 ? 66   GLY D CA  1 
ATOM   8035  C  C   . GLY D  1 63  ? -38.765 -33.953 52.616  1.00 32.48 ? 66   GLY D C   1 
ATOM   8036  O  O   . GLY D  1 63  ? -39.839 -33.927 52.030  1.00 31.89 ? 66   GLY D O   1 
ATOM   8037  N  N   . LEU D  1 64  ? -37.755 -33.129 52.322  1.00 30.53 ? 67   LEU D N   1 
ATOM   8038  C  CA  . LEU D  1 64  ? -37.949 -31.972 51.441  1.00 31.82 ? 67   LEU D CA  1 
ATOM   8039  C  C   . LEU D  1 64  ? -36.872 -31.774 50.361  1.00 30.23 ? 67   LEU D C   1 
ATOM   8040  O  O   . LEU D  1 64  ? -37.009 -30.915 49.503  1.00 29.56 ? 67   LEU D O   1 
ATOM   8041  C  CB  . LEU D  1 64  ? -38.132 -30.684 52.253  1.00 33.55 ? 67   LEU D CB  1 
ATOM   8042  C  CG  . LEU D  1 64  ? -39.421 -30.540 53.068  1.00 35.16 ? 67   LEU D CG  1 
ATOM   8043  C  CD1 . LEU D  1 64  ? -39.193 -29.635 54.266  1.00 35.93 ? 67   LEU D CD1 1 
ATOM   8044  C  CD2 . LEU D  1 64  ? -40.561 -30.016 52.205  1.00 35.72 ? 67   LEU D CD2 1 
ATOM   8045  N  N   . ASN D  1 65  ? -35.833 -32.599 50.384  1.00 27.52 ? 68   ASN D N   1 
ATOM   8046  C  CA  . ASN D  1 65  ? -34.795 -32.578 49.361  1.00 28.46 ? 68   ASN D CA  1 
ATOM   8047  C  C   . ASN D  1 65  ? -33.895 -31.355 49.415  1.00 28.97 ? 68   ASN D C   1 
ATOM   8048  O  O   . ASN D  1 65  ? -33.417 -30.892 48.381  1.00 28.67 ? 68   ASN D O   1 
ATOM   8049  C  CB  . ASN D  1 65  ? -35.376 -32.732 47.950  1.00 26.46 ? 68   ASN D CB  1 
ATOM   8050  C  CG  . ASN D  1 65  ? -34.640 -33.786 47.133  1.00 28.18 ? 68   ASN D CG  1 
ATOM   8051  O  OD1 . ASN D  1 65  ? -33.504 -34.176 47.466  1.00 27.69 ? 68   ASN D OD1 1 
ATOM   8052  N  ND2 . ASN D  1 65  ? -35.281 -34.262 46.061  1.00 25.44 ? 68   ASN D ND2 1 
ATOM   8053  N  N   . PHE D  1 66  ? -33.696 -30.821 50.615  1.00 27.74 ? 69   PHE D N   1 
ATOM   8054  C  CA  . PHE D  1 66  ? -32.762 -29.710 50.834  1.00 25.92 ? 69   PHE D CA  1 
ATOM   8055  C  C   . PHE D  1 66  ? -31.361 -30.231 50.553  1.00 23.99 ? 69   PHE D C   1 
ATOM   8056  O  O   . PHE D  1 66  ? -31.043 -31.360 50.897  1.00 23.22 ? 69   PHE D O   1 
ATOM   8057  C  CB  . PHE D  1 66  ? -32.863 -29.261 52.296  1.00 25.00 ? 69   PHE D CB  1 
ATOM   8058  C  CG  . PHE D  1 66  ? -32.534 -27.805 52.529  1.00 22.61 ? 69   PHE D CG  1 
ATOM   8059  C  CD1 . PHE D  1 66  ? -33.341 -26.808 52.030  1.00 23.13 ? 69   PHE D CD1 1 
ATOM   8060  C  CD2 . PHE D  1 66  ? -31.484 -27.448 53.360  1.00 20.85 ? 69   PHE D CD2 1 
ATOM   8061  C  CE1 . PHE D  1 66  ? -33.066 -25.467 52.303  1.00 23.14 ? 69   PHE D CE1 1 
ATOM   8062  C  CE2 . PHE D  1 66  ? -31.230 -26.119 53.663  1.00 20.86 ? 69   PHE D CE2 1 
ATOM   8063  C  CZ  . PHE D  1 66  ? -32.001 -25.129 53.104  1.00 21.49 ? 69   PHE D CZ  1 
ATOM   8064  N  N   . ASP D  1 67  ? -30.526 -29.457 49.883  1.00 24.55 ? 70   ASP D N   1 
ATOM   8065  C  CA  . ASP D  1 67  ? -29.229 -30.011 49.526  1.00 26.54 ? 70   ASP D CA  1 
ATOM   8066  C  C   . ASP D  1 67  ? -28.262 -30.079 50.699  1.00 25.61 ? 70   ASP D C   1 
ATOM   8067  O  O   . ASP D  1 67  ? -28.373 -29.318 51.660  1.00 22.85 ? 70   ASP D O   1 
ATOM   8068  C  CB  . ASP D  1 67  ? -28.598 -29.324 48.314  1.00 29.73 ? 70   ASP D CB  1 
ATOM   8069  C  CG  . ASP D  1 67  ? -28.133 -27.927 48.619  1.00 31.61 ? 70   ASP D CG  1 
ATOM   8070  O  OD1 . ASP D  1 67  ? -26.977 -27.746 49.085  1.00 35.58 ? 70   ASP D OD1 1 
ATOM   8071  O  OD2 . ASP D  1 67  ? -28.934 -27.009 48.395  1.00 32.76 ? 70   ASP D OD2 1 
ATOM   8072  N  N   . ASN D  1 68  ? -27.319 -31.010 50.599  1.00 23.97 ? 71   ASN D N   1 
ATOM   8073  C  CA  . ASN D  1 68  ? -26.477 -31.395 51.717  1.00 26.05 ? 71   ASN D CA  1 
ATOM   8074  C  C   . ASN D  1 68  ? -25.728 -30.210 52.307  1.00 26.16 ? 71   ASN D C   1 
ATOM   8075  O  O   . ASN D  1 68  ? -25.917 -29.879 53.466  1.00 29.02 ? 71   ASN D O   1 
ATOM   8076  C  CB  . ASN D  1 68  ? -25.489 -32.482 51.286  1.00 24.66 ? 71   ASN D CB  1 
ATOM   8077  C  CG  . ASN D  1 68  ? -24.718 -33.058 52.448  1.00 26.94 ? 71   ASN D CG  1 
ATOM   8078  O  OD1 . ASN D  1 68  ? -23.501 -32.933 52.517  1.00 28.58 ? 71   ASN D OD1 1 
ATOM   8079  N  ND2 . ASN D  1 68  ? -25.422 -33.705 53.367  1.00 25.98 ? 71   ASN D ND2 1 
ATOM   8080  N  N   . GLN D  1 69  ? -24.924 -29.536 51.489  1.00 26.40 ? 72   GLN D N   1 
ATOM   8081  C  CA  . GLN D  1 69  ? -24.103 -28.439 51.970  1.00 24.67 ? 72   GLN D CA  1 
ATOM   8082  C  C   . GLN D  1 69  ? -24.950 -27.363 52.634  1.00 24.26 ? 72   GLN D C   1 
ATOM   8083  O  O   . GLN D  1 69  ? -24.571 -26.830 53.673  1.00 24.03 ? 72   GLN D O   1 
ATOM   8084  C  CB  . GLN D  1 69  ? -23.269 -27.831 50.834  1.00 27.64 ? 72   GLN D CB  1 
ATOM   8085  C  CG  . GLN D  1 69  ? -21.892 -28.470 50.617  1.00 30.12 ? 72   GLN D CG  1 
ATOM   8086  C  CD  . GLN D  1 69  ? -21.000 -27.632 49.690  1.00 35.70 ? 72   GLN D CD  1 
ATOM   8087  O  OE1 . GLN D  1 69  ? -21.434 -27.185 48.628  1.00 35.74 ? 72   GLN D OE1 1 
ATOM   8088  N  NE2 . GLN D  1 69  ? -19.753 -27.413 50.100  1.00 37.40 ? 72   GLN D NE2 1 
ATOM   8089  N  N   . ALA D  1 70  ? -26.088 -27.027 52.030  1.00 20.62 ? 73   ALA D N   1 
ATOM   8090  C  CA  . ALA D  1 70  ? -26.990 -26.060 52.635  1.00 22.45 ? 73   ALA D CA  1 
ATOM   8091  C  C   . ALA D  1 70  ? -27.558 -26.598 53.968  1.00 23.29 ? 73   ALA D C   1 
ATOM   8092  O  O   . ALA D  1 70  ? -27.798 -25.832 54.908  1.00 23.48 ? 73   ALA D O   1 
ATOM   8093  C  CB  . ALA D  1 70  ? -28.111 -25.694 51.678  1.00 18.54 ? 73   ALA D CB  1 
ATOM   8094  N  N   . ALA D  1 71  ? -27.695 -27.917 54.075  1.00 20.50 ? 74   ALA D N   1 
ATOM   8095  C  CA  . ALA D  1 71  ? -28.232 -28.511 55.304  1.00 19.90 ? 74   ALA D CA  1 
ATOM   8096  C  C   . ALA D  1 71  ? -27.160 -28.445 56.377  1.00 22.41 ? 74   ALA D C   1 
ATOM   8097  O  O   . ALA D  1 71  ? -27.420 -28.036 57.512  1.00 23.43 ? 74   ALA D O   1 
ATOM   8098  C  CB  . ALA D  1 71  ? -28.672 -29.957 55.074  1.00 14.28 ? 74   ALA D CB  1 
ATOM   8099  N  N   . VAL D  1 72  ? -25.946 -28.823 55.995  1.00 22.29 ? 75   VAL D N   1 
ATOM   8100  C  CA  . VAL D  1 72  ? -24.798 -28.756 56.883  1.00 23.45 ? 75   VAL D CA  1 
ATOM   8101  C  C   . VAL D  1 72  ? -24.547 -27.331 57.384  1.00 23.79 ? 75   VAL D C   1 
ATOM   8102  O  O   . VAL D  1 72  ? -24.422 -27.095 58.587  1.00 26.37 ? 75   VAL D O   1 
ATOM   8103  C  CB  . VAL D  1 72  ? -23.557 -29.339 56.182  1.00 22.79 ? 75   VAL D CB  1 
ATOM   8104  C  CG1 . VAL D  1 72  ? -22.283 -29.089 56.979  1.00 21.23 ? 75   VAL D CG1 1 
ATOM   8105  C  CG2 . VAL D  1 72  ? -23.753 -30.833 55.953  1.00 18.87 ? 75   VAL D CG2 1 
ATOM   8106  N  N   . PHE D  1 73  ? -24.554 -26.381 56.463  1.00 21.53 ? 76   PHE D N   1 
ATOM   8107  C  CA  . PHE D  1 73  ? -24.310 -24.984 56.779  1.00 22.00 ? 76   PHE D CA  1 
ATOM   8108  C  C   . PHE D  1 73  ? -25.301 -24.469 57.815  1.00 22.26 ? 76   PHE D C   1 
ATOM   8109  O  O   . PHE D  1 73  ? -24.913 -23.897 58.838  1.00 25.84 ? 76   PHE D O   1 
ATOM   8110  C  CB  . PHE D  1 73  ? -24.417 -24.127 55.496  1.00 23.64 ? 76   PHE D CB  1 
ATOM   8111  C  CG  . PHE D  1 73  ? -24.034 -22.693 55.695  1.00 20.96 ? 76   PHE D CG  1 
ATOM   8112  C  CD1 . PHE D  1 73  ? -22.709 -22.321 55.747  1.00 23.83 ? 76   PHE D CD1 1 
ATOM   8113  C  CD2 . PHE D  1 73  ? -24.992 -21.741 55.889  1.00 22.67 ? 76   PHE D CD2 1 
ATOM   8114  C  CE1 . PHE D  1 73  ? -22.336 -21.001 55.982  1.00 26.60 ? 76   PHE D CE1 1 
ATOM   8115  C  CE2 . PHE D  1 73  ? -24.637 -20.420 56.104  1.00 28.06 ? 76   PHE D CE2 1 
ATOM   8116  C  CZ  . PHE D  1 73  ? -23.297 -20.053 56.171  1.00 26.49 ? 76   PHE D CZ  1 
ATOM   8117  N  N   . ALA D  1 74  ? -26.584 -24.600 57.505  1.00 20.73 ? 77   ALA D N   1 
ATOM   8118  C  CA  . ALA D  1 74  ? -27.628 -23.977 58.303  1.00 21.37 ? 77   ALA D CA  1 
ATOM   8119  C  C   . ALA D  1 74  ? -27.749 -24.643 59.670  1.00 23.79 ? 77   ALA D C   1 
ATOM   8120  O  O   . ALA D  1 74  ? -28.079 -23.983 60.658  1.00 22.61 ? 77   ALA D O   1 
ATOM   8121  C  CB  . ALA D  1 74  ? -28.973 -24.030 57.572  1.00 18.24 ? 77   ALA D CB  1 
ATOM   8122  N  N   . THR D  1 75  ? -27.629 -25.968 59.685  1.00 22.64 ? 78   THR D N   1 
ATOM   8123  C  CA  . THR D  1 75  ? -27.836 -26.726 60.902  1.00 24.34 ? 78   THR D CA  1 
ATOM   8124  C  C   . THR D  1 75  ? -26.727 -26.454 61.919  1.00 25.16 ? 78   THR D C   1 
ATOM   8125  O  O   . THR D  1 75  ? -26.994 -26.103 63.062  1.00 25.45 ? 78   THR D O   1 
ATOM   8126  C  CB  . THR D  1 75  ? -27.926 -28.226 60.610  1.00 22.34 ? 78   THR D CB  1 
ATOM   8127  O  OG1 . THR D  1 75  ? -29.068 -28.460 59.787  1.00 26.22 ? 78   THR D OG1 1 
ATOM   8128  C  CG2 . THR D  1 75  ? -28.090 -29.002 61.886  1.00 24.54 ? 78   THR D CG2 1 
ATOM   8129  N  N   . TYR D  1 76  ? -25.479 -26.608 61.505  1.00 24.30 ? 79   TYR D N   1 
ATOM   8130  C  CA  . TYR D  1 76  ? -24.396 -26.402 62.437  1.00 25.57 ? 79   TYR D CA  1 
ATOM   8131  C  C   . TYR D  1 76  ? -24.200 -24.935 62.797  1.00 26.41 ? 79   TYR D C   1 
ATOM   8132  O  O   . TYR D  1 76  ? -23.819 -24.613 63.921  1.00 29.49 ? 79   TYR D O   1 
ATOM   8133  C  CB  . TYR D  1 76  ? -23.112 -27.047 61.944  1.00 22.32 ? 79   TYR D CB  1 
ATOM   8134  C  CG  . TYR D  1 76  ? -23.184 -28.547 61.948  1.00 25.88 ? 79   TYR D CG  1 
ATOM   8135  C  CD1 . TYR D  1 76  ? -23.034 -29.279 63.132  1.00 25.19 ? 79   TYR D CD1 1 
ATOM   8136  C  CD2 . TYR D  1 76  ? -23.388 -29.246 60.764  1.00 27.51 ? 79   TYR D CD2 1 
ATOM   8137  C  CE1 . TYR D  1 76  ? -23.067 -30.672 63.116  1.00 23.96 ? 79   TYR D CE1 1 
ATOM   8138  C  CE2 . TYR D  1 76  ? -23.458 -30.626 60.749  1.00 26.57 ? 79   TYR D CE2 1 
ATOM   8139  C  CZ  . TYR D  1 76  ? -23.309 -31.338 61.921  1.00 25.82 ? 79   TYR D CZ  1 
ATOM   8140  O  OH  . TYR D  1 76  ? -23.381 -32.725 61.862  1.00 25.72 ? 79   TYR D OH  1 
ATOM   8141  N  N   . ALA D  1 77  ? -24.534 -24.047 61.875  1.00 25.52 ? 80   ALA D N   1 
ATOM   8142  C  CA  . ALA D  1 77  ? -24.677 -22.644 62.223  1.00 25.41 ? 80   ALA D CA  1 
ATOM   8143  C  C   . ALA D  1 77  ? -25.659 -22.515 63.381  1.00 25.84 ? 80   ALA D C   1 
ATOM   8144  O  O   . ALA D  1 77  ? -25.346 -21.912 64.412  1.00 28.58 ? 80   ALA D O   1 
ATOM   8145  C  CB  . ALA D  1 77  ? -25.159 -21.836 61.021  1.00 22.93 ? 80   ALA D CB  1 
ATOM   8146  N  N   . ALA D  1 78  ? -26.864 -23.036 63.191  1.00 24.87 ? 81   ALA D N   1 
ATOM   8147  C  CA  . ALA D  1 78  ? -27.905 -22.951 64.214  1.00 26.39 ? 81   ALA D CA  1 
ATOM   8148  C  C   . ALA D  1 78  ? -27.478 -23.582 65.550  1.00 25.13 ? 81   ALA D C   1 
ATOM   8149  O  O   . ALA D  1 78  ? -27.668 -22.999 66.611  1.00 25.55 ? 81   ALA D O   1 
ATOM   8150  C  CB  . ALA D  1 78  ? -29.197 -23.572 63.710  1.00 21.84 ? 81   ALA D CB  1 
ATOM   8151  N  N   . HIS D  1 79  ? -26.870 -24.760 65.488  1.00 27.05 ? 82   HIS D N   1 
ATOM   8152  C  CA  . HIS D  1 79  ? -26.521 -25.508 66.688  1.00 25.92 ? 82   HIS D CA  1 
ATOM   8153  C  C   . HIS D  1 79  ? -25.409 -24.779 67.455  1.00 26.98 ? 82   HIS D C   1 
ATOM   8154  O  O   . HIS D  1 79  ? -25.441 -24.674 68.683  1.00 26.16 ? 82   HIS D O   1 
ATOM   8155  C  CB  . HIS D  1 79  ? -26.079 -26.918 66.289  1.00 27.89 ? 82   HIS D CB  1 
ATOM   8156  C  CG  . HIS D  1 79  ? -25.780 -27.818 67.449  1.00 30.14 ? 82   HIS D CG  1 
ATOM   8157  N  ND1 . HIS D  1 79  ? -26.723 -28.147 68.403  1.00 31.28 ? 82   HIS D ND1 1 
ATOM   8158  C  CD2 . HIS D  1 79  ? -24.656 -28.495 67.785  1.00 31.64 ? 82   HIS D CD2 1 
ATOM   8159  C  CE1 . HIS D  1 79  ? -26.187 -28.973 69.283  1.00 31.02 ? 82   HIS D CE1 1 
ATOM   8160  N  NE2 . HIS D  1 79  ? -24.929 -29.188 68.940  1.00 33.10 ? 82   HIS D NE2 1 
ATOM   8161  N  N   . LEU D  1 80  ? -24.442 -24.239 66.719  1.00 28.04 ? 83   LEU D N   1 
ATOM   8162  C  CA  . LEU D  1 80  ? -23.348 -23.485 67.326  1.00 28.27 ? 83   LEU D CA  1 
ATOM   8163  C  C   . LEU D  1 80  ? -23.870 -22.332 68.186  1.00 29.30 ? 83   LEU D C   1 
ATOM   8164  O  O   . LEU D  1 80  ? -23.389 -22.127 69.299  1.00 32.26 ? 83   LEU D O   1 
ATOM   8165  C  CB  . LEU D  1 80  ? -22.379 -22.961 66.260  1.00 24.40 ? 83   LEU D CB  1 
ATOM   8166  C  CG  . LEU D  1 80  ? -21.398 -23.974 65.661  1.00 23.67 ? 83   LEU D CG  1 
ATOM   8167  C  CD1 . LEU D  1 80  ? -20.713 -23.398 64.432  1.00 17.55 ? 83   LEU D CD1 1 
ATOM   8168  C  CD2 . LEU D  1 80  ? -20.366 -24.429 66.693  1.00 21.98 ? 83   LEU D CD2 1 
ATOM   8169  N  N   . VAL D  1 81  ? -24.835 -21.572 67.673  1.00 28.53 ? 84   VAL D N   1 
ATOM   8170  C  CA  . VAL D  1 81  ? -25.299 -20.388 68.388  1.00 28.26 ? 84   VAL D CA  1 
ATOM   8171  C  C   . VAL D  1 81  ? -26.562 -20.623 69.221  1.00 29.22 ? 84   VAL D C   1 
ATOM   8172  O  O   . VAL D  1 81  ? -26.844 -19.846 70.124  1.00 25.73 ? 84   VAL D O   1 
ATOM   8173  C  CB  . VAL D  1 81  ? -25.543 -19.182 67.446  1.00 28.39 ? 84   VAL D CB  1 
ATOM   8174  C  CG1 . VAL D  1 81  ? -24.250 -18.709 66.837  1.00 28.95 ? 84   VAL D CG1 1 
ATOM   8175  C  CG2 . VAL D  1 81  ? -26.557 -19.531 66.383  1.00 25.67 ? 84   VAL D CG2 1 
ATOM   8176  N  N   . ASP D  1 82  ? -27.349 -21.648 68.885  1.00 29.69 ? 85   ASP D N   1 
ATOM   8177  C  CA  . ASP D  1 82  ? -28.681 -21.823 69.488  1.00 26.91 ? 85   ASP D CA  1 
ATOM   8178  C  C   . ASP D  1 82  ? -28.857 -23.146 70.274  1.00 28.19 ? 85   ASP D C   1 
ATOM   8179  O  O   . ASP D  1 82  ? -29.824 -23.313 71.020  1.00 25.70 ? 85   ASP D O   1 
ATOM   8180  C  CB  . ASP D  1 82  ? -29.784 -21.686 68.431  1.00 27.18 ? 85   ASP D CB  1 
ATOM   8181  C  CG  . ASP D  1 82  ? -30.103 -20.219 68.076  1.00 27.04 ? 85   ASP D CG  1 
ATOM   8182  O  OD1 . ASP D  1 82  ? -29.578 -19.320 68.774  1.00 26.47 ? 85   ASP D OD1 1 
ATOM   8183  O  OD2 . ASP D  1 82  ? -30.845 -19.967 67.074  1.00 18.38 ? 85   ASP D OD2 1 
ATOM   8184  N  N   . GLY D  1 83  ? -27.911 -24.068 70.133  1.00 28.41 ? 86   GLY D N   1 
ATOM   8185  C  CA  . GLY D  1 83  ? -28.082 -25.419 70.660  1.00 27.55 ? 86   GLY D CA  1 
ATOM   8186  C  C   . GLY D  1 83  ? -27.050 -25.812 71.703  1.00 29.45 ? 86   GLY D C   1 
ATOM   8187  O  O   . GLY D  1 83  ? -26.055 -25.105 71.905  1.00 27.90 ? 86   GLY D O   1 
ATOM   8188  N  N   . ASN D  1 84  ? -27.239 -26.984 72.311  1.00 29.19 ? 87   ASN D N   1 
ATOM   8189  C  CA  . ASN D  1 84  ? -26.330 -27.440 73.374  1.00 31.55 ? 87   ASN D CA  1 
ATOM   8190  C  C   . ASN D  1 84  ? -25.242 -28.358 72.878  1.00 30.94 ? 87   ASN D C   1 
ATOM   8191  O  O   . ASN D  1 84  ? -25.496 -29.522 72.564  1.00 31.23 ? 87   ASN D O   1 
ATOM   8192  C  CB  . ASN D  1 84  ? -27.093 -28.143 74.507  1.00 31.93 ? 87   ASN D CB  1 
ATOM   8193  C  CG  . ASN D  1 84  ? -26.248 -28.307 75.757  1.00 34.20 ? 87   ASN D CG  1 
ATOM   8194  O  OD1 . ASN D  1 84  ? -25.229 -29.015 75.753  1.00 35.65 ? 87   ASN D OD1 1 
ATOM   8195  N  ND2 . ASN D  1 84  ? -26.681 -27.675 76.849  1.00 34.08 ? 87   ASN D ND2 1 
ATOM   8196  N  N   . LEU D  1 85  ? -24.010 -27.876 72.957  1.00 32.39 ? 88   LEU D N   1 
ATOM   8197  C  CA  . LEU D  1 85  ? -22.881 -28.546 72.337  1.00 33.20 ? 88   LEU D CA  1 
ATOM   8198  C  C   . LEU D  1 85  ? -22.510 -29.839 73.056  1.00 34.66 ? 88   LEU D C   1 
ATOM   8199  O  O   . LEU D  1 85  ? -21.880 -30.717 72.467  1.00 35.21 ? 88   LEU D O   1 
ATOM   8200  C  CB  . LEU D  1 85  ? -21.673 -27.603 72.291  1.00 34.29 ? 88   LEU D CB  1 
ATOM   8201  C  CG  . LEU D  1 85  ? -21.601 -26.635 71.110  1.00 34.89 ? 88   LEU D CG  1 
ATOM   8202  C  CD1 . LEU D  1 85  ? -22.954 -26.109 70.743  1.00 33.78 ? 88   LEU D CD1 1 
ATOM   8203  C  CD2 . LEU D  1 85  ? -20.623 -25.502 71.365  1.00 34.68 ? 88   LEU D CD2 1 
ATOM   8204  N  N   . ILE D  1 86  ? -22.845 -29.938 74.342  1.00 35.71 ? 89   ILE D N   1 
ATOM   8205  C  CA  . ILE D  1 86  ? -22.489 -31.135 75.129  1.00 35.75 ? 89   ILE D CA  1 
ATOM   8206  C  C   . ILE D  1 86  ? -23.495 -32.255 74.949  1.00 32.65 ? 89   ILE D C   1 
ATOM   8207  O  O   . ILE D  1 86  ? -23.127 -33.401 74.802  1.00 37.22 ? 89   ILE D O   1 
ATOM   8208  C  CB  . ILE D  1 86  ? -22.377 -30.824 76.642  1.00 37.23 ? 89   ILE D CB  1 
ATOM   8209  C  CG1 . ILE D  1 86  ? -21.544 -29.554 76.871  1.00 36.78 ? 89   ILE D CG1 1 
ATOM   8210  C  CG2 . ILE D  1 86  ? -21.752 -32.001 77.380  1.00 37.19 ? 89   ILE D CG2 1 
ATOM   8211  C  CD1 . ILE D  1 86  ? -20.063 -29.763 76.660  1.00 34.97 ? 89   ILE D CD1 1 
ATOM   8212  N  N   . THR D  1 87  ? -24.774 -31.921 74.978  1.00 32.77 ? 90   THR D N   1 
ATOM   8213  C  CA  . THR D  1 87  ? -25.828 -32.915 74.790  1.00 32.95 ? 90   THR D CA  1 
ATOM   8214  C  C   . THR D  1 87  ? -26.174 -33.124 73.317  1.00 32.61 ? 90   THR D C   1 
ATOM   8215  O  O   . THR D  1 87  ? -26.872 -34.079 72.964  1.00 29.14 ? 90   THR D O   1 
ATOM   8216  C  CB  . THR D  1 87  ? -27.102 -32.473 75.498  1.00 33.79 ? 90   THR D CB  1 
ATOM   8217  O  OG1 . THR D  1 87  ? -27.588 -31.285 74.858  1.00 34.56 ? 90   THR D OG1 1 
ATOM   8218  C  CG2 . THR D  1 87  ? -26.810 -32.177 76.966  1.00 30.59 ? 90   THR D CG2 1 
ATOM   8219  N  N   . ASP D  1 88  ? -25.696 -32.215 72.465  1.00 35.52 ? 91   ASP D N   1 
ATOM   8220  C  CA  . ASP D  1 88  ? -25.819 -32.359 71.016  1.00 35.12 ? 91   ASP D CA  1 
ATOM   8221  C  C   . ASP D  1 88  ? -27.264 -32.211 70.581  1.00 33.45 ? 91   ASP D C   1 
ATOM   8222  O  O   . ASP D  1 88  ? -27.741 -32.922 69.696  1.00 37.15 ? 91   ASP D O   1 
ATOM   8223  C  CB  . ASP D  1 88  ? -25.267 -33.705 70.554  1.00 36.57 ? 91   ASP D CB  1 
ATOM   8224  C  CG  . ASP D  1 88  ? -24.859 -33.686 69.106  1.00 40.77 ? 91   ASP D CG  1 
ATOM   8225  O  OD1 . ASP D  1 88  ? -24.093 -32.773 68.710  1.00 41.00 ? 91   ASP D OD1 1 
ATOM   8226  O  OD2 . ASP D  1 88  ? -25.364 -34.536 68.346  1.00 43.38 ? 91   ASP D OD2 1 
ATOM   8227  N  N   . LEU D  1 89  ? -27.960 -31.294 71.238  1.00 30.64 ? 92   LEU D N   1 
ATOM   8228  C  CA  . LEU D  1 89  ? -29.406 -31.150 71.112  1.00 29.80 ? 92   LEU D CA  1 
ATOM   8229  C  C   . LEU D  1 89  ? -29.740 -29.682 70.847  1.00 28.18 ? 92   LEU D C   1 
ATOM   8230  O  O   . LEU D  1 89  ? -29.104 -28.775 71.400  1.00 28.35 ? 92   LEU D O   1 
ATOM   8231  C  CB  . LEU D  1 89  ? -30.088 -31.597 72.414  1.00 28.60 ? 92   LEU D CB  1 
ATOM   8232  C  CG  . LEU D  1 89  ? -30.120 -33.102 72.705  1.00 29.69 ? 92   LEU D CG  1 
ATOM   8233  C  CD1 . LEU D  1 89  ? -30.598 -33.337 74.131  1.00 29.59 ? 92   LEU D CD1 1 
ATOM   8234  C  CD2 . LEU D  1 89  ? -31.004 -33.852 71.699  1.00 27.03 ? 92   LEU D CD2 1 
ATOM   8235  N  N   . LEU D  1 90  ? -30.745 -29.449 70.017  1.00 28.42 ? 93   LEU D N   1 
ATOM   8236  C  CA  . LEU D  1 90  ? -31.133 -28.089 69.663  1.00 27.57 ? 93   LEU D CA  1 
ATOM   8237  C  C   . LEU D  1 90  ? -32.637 -28.024 69.566  1.00 28.33 ? 93   LEU D C   1 
ATOM   8238  O  O   . LEU D  1 90  ? -33.276 -28.974 69.109  1.00 28.45 ? 93   LEU D O   1 
ATOM   8239  C  CB  . LEU D  1 90  ? -30.496 -27.683 68.324  1.00 28.09 ? 93   LEU D CB  1 
ATOM   8240  C  CG  . LEU D  1 90  ? -31.234 -26.663 67.449  1.00 27.35 ? 93   LEU D CG  1 
ATOM   8241  C  CD1 . LEU D  1 90  ? -30.976 -25.263 67.943  1.00 25.78 ? 93   LEU D CD1 1 
ATOM   8242  C  CD2 . LEU D  1 90  ? -30.797 -26.800 66.005  1.00 29.19 ? 93   LEU D CD2 1 
ATOM   8243  N  N   . SER D  1 91  ? -33.215 -26.903 69.990  1.00 29.45 ? 94   SER D N   1 
ATOM   8244  C  CA  . SER D  1 91  ? -34.647 -26.744 69.869  1.00 29.11 ? 94   SER D CA  1 
ATOM   8245  C  C   . SER D  1 91  ? -34.987 -25.916 68.653  1.00 26.69 ? 94   SER D C   1 
ATOM   8246  O  O   . SER D  1 91  ? -34.310 -24.931 68.357  1.00 30.15 ? 94   SER D O   1 
ATOM   8247  C  CB  . SER D  1 91  ? -35.248 -26.110 71.122  1.00 28.99 ? 94   SER D CB  1 
ATOM   8248  O  OG  . SER D  1 91  ? -36.529 -25.553 70.831  1.00 29.48 ? 94   SER D OG  1 
ATOM   8249  N  N   . ILE D  1 92  ? -36.091 -26.247 68.003  1.00 27.32 ? 95   ILE D N   1 
ATOM   8250  C  CA  . ILE D  1 92  ? -36.419 -25.606 66.729  1.00 30.28 ? 95   ILE D CA  1 
ATOM   8251  C  C   . ILE D  1 92  ? -37.310 -24.412 67.010  1.00 30.78 ? 95   ILE D C   1 
ATOM   8252  O  O   . ILE D  1 92  ? -37.826 -23.778 66.089  1.00 29.48 ? 95   ILE D O   1 
ATOM   8253  C  CB  . ILE D  1 92  ? -37.134 -26.583 65.757  1.00 29.47 ? 95   ILE D CB  1 
ATOM   8254  C  CG1 . ILE D  1 92  ? -38.503 -26.977 66.312  1.00 29.24 ? 95   ILE D CG1 1 
ATOM   8255  C  CG2 . ILE D  1 92  ? -36.294 -27.831 65.523  1.00 27.83 ? 95   ILE D CG2 1 
ATOM   8256  C  CD1 . ILE D  1 92  ? -39.335 -27.827 65.358  1.00 31.56 ? 95   ILE D CD1 1 
ATOM   8257  N  N   . GLY D  1 93  ? -37.533 -24.153 68.301  1.00 33.86 ? 96   GLY D N   1 
ATOM   8258  C  CA  . GLY D  1 93  ? -38.321 -22.999 68.761  1.00 30.64 ? 96   GLY D CA  1 
ATOM   8259  C  C   . GLY D  1 93  ? -37.761 -22.415 70.051  1.00 32.52 ? 96   GLY D C   1 
ATOM   8260  O  O   . GLY D  1 93  ? -36.627 -21.939 70.068  1.00 32.46 ? 96   GLY D O   1 
ATOM   8261  N  N   . ARG D  1 94  ? -38.544 -22.463 71.134  1.00 30.78 ? 97   ARG D N   1 
ATOM   8262  C  CA  . ARG D  1 94  ? -38.214 -21.751 72.374  1.00 30.20 ? 97   ARG D CA  1 
ATOM   8263  C  C   . ARG D  1 94  ? -37.041 -22.392 73.115  1.00 29.11 ? 97   ARG D C   1 
ATOM   8264  O  O   . ARG D  1 94  ? -36.783 -23.570 72.950  1.00 29.70 ? 97   ARG D O   1 
ATOM   8265  C  CB  . ARG D  1 94  ? -39.432 -21.700 73.298  1.00 31.85 ? 97   ARG D CB  1 
ATOM   8266  C  CG  . ARG D  1 94  ? -40.028 -23.082 73.616  1.00 33.91 ? 97   ARG D CG  1 
ATOM   8267  C  CD  . ARG D  1 94  ? -41.135 -23.022 74.685  1.00 37.47 ? 97   ARG D CD  1 
ATOM   8268  N  NE  . ARG D  1 94  ? -41.170 -24.287 75.416  1.00 42.00 ? 97   ARG D NE  1 
ATOM   8269  C  CZ  . ARG D  1 94  ? -42.041 -25.261 75.178  1.00 42.82 ? 97   ARG D CZ  1 
ATOM   8270  N  NH1 . ARG D  1 94  ? -43.065 -25.059 74.347  1.00 41.92 ? 97   ARG D NH1 1 
ATOM   8271  N  NH2 . ARG D  1 94  ? -41.903 -26.424 75.797  1.00 41.71 ? 97   ARG D NH2 1 
ATOM   8272  N  N   . LYS D  1 95  ? -36.372 -21.631 73.978  1.00 30.71 ? 98   LYS D N   1 
ATOM   8273  C  CA  . LYS D  1 95  ? -35.473 -22.228 74.965  1.00 33.80 ? 98   LYS D CA  1 
ATOM   8274  C  C   . LYS D  1 95  ? -36.223 -23.293 75.749  1.00 33.34 ? 98   LYS D C   1 
ATOM   8275  O  O   . LYS D  1 95  ? -37.394 -23.124 76.058  1.00 32.36 ? 98   LYS D O   1 
ATOM   8276  C  CB  . LYS D  1 95  ? -34.951 -21.174 75.942  1.00 34.27 ? 98   LYS D CB  1 
ATOM   8277  C  CG  . LYS D  1 95  ? -33.898 -21.718 76.915  1.00 34.77 ? 98   LYS D CG  1 
ATOM   8278  C  CD  . LYS D  1 95  ? -33.023 -20.589 77.475  1.00 34.40 ? 98   LYS D CD  1 
ATOM   8279  C  CE  . LYS D  1 95  ? -32.038 -21.106 78.508  1.00 33.50 ? 98   LYS D CE  1 
ATOM   8280  N  NZ  . LYS D  1 95  ? -31.008 -21.982 77.888  1.00 35.39 ? 98   LYS D NZ  1 
ATOM   8281  N  N   . THR D  1 96  ? -35.559 -24.412 76.014  1.00 36.49 ? 99   THR D N   1 
ATOM   8282  C  CA  . THR D  1 96  ? -36.145 -25.465 76.822  1.00 38.15 ? 99   THR D CA  1 
ATOM   8283  C  C   . THR D  1 96  ? -35.105 -26.159 77.686  1.00 39.59 ? 99   THR D C   1 
ATOM   8284  O  O   . THR D  1 96  ? -33.925 -26.216 77.334  1.00 38.79 ? 99   THR D O   1 
ATOM   8285  C  CB  . THR D  1 96  ? -36.875 -26.526 75.983  1.00 38.37 ? 99   THR D CB  1 
ATOM   8286  O  OG1 . THR D  1 96  ? -37.180 -27.641 76.822  1.00 41.76 ? 99   THR D OG1 1 
ATOM   8287  C  CG2 . THR D  1 96  ? -36.001 -27.023 74.851  1.00 39.70 ? 99   THR D CG2 1 
ATOM   8288  N  N   . ARG D  1 97  ? -35.549 -26.689 78.820  1.00 39.69 ? 100  ARG D N   1 
ATOM   8289  C  CA  . ARG D  1 97  ? -34.652 -27.388 79.717  1.00 42.21 ? 100  ARG D CA  1 
ATOM   8290  C  C   . ARG D  1 97  ? -34.348 -28.766 79.156  1.00 40.49 ? 100  ARG D C   1 
ATOM   8291  O  O   . ARG D  1 97  ? -33.344 -29.369 79.507  1.00 40.09 ? 100  ARG D O   1 
ATOM   8292  C  CB  . ARG D  1 97  ? -35.248 -27.476 81.130  1.00 45.18 ? 100  ARG D CB  1 
ATOM   8293  C  CG  . ARG D  1 97  ? -34.767 -26.355 82.053  1.00 49.56 ? 100  ARG D CG  1 
ATOM   8294  C  CD  . ARG D  1 97  ? -35.497 -26.344 83.401  1.00 52.66 ? 100  ARG D CD  1 
ATOM   8295  N  NE  . ARG D  1 97  ? -36.413 -25.211 83.525  1.00 55.28 ? 100  ARG D NE  1 
ATOM   8296  C  CZ  . ARG D  1 97  ? -36.055 -23.993 83.936  1.00 56.79 ? 100  ARG D CZ  1 
ATOM   8297  N  NH1 . ARG D  1 97  ? -34.792 -23.753 84.280  1.00 55.51 ? 100  ARG D NH1 1 
ATOM   8298  N  NH2 . ARG D  1 97  ? -36.964 -23.017 84.010  1.00 54.99 ? 100  ARG D NH2 1 
ATOM   8299  N  N   . LEU D  1 98  ? -35.174 -29.216 78.215  1.00 38.41 ? 101  LEU D N   1 
ATOM   8300  C  CA  . LEU D  1 98  ? -34.929 -30.466 77.507  1.00 39.13 ? 101  LEU D CA  1 
ATOM   8301  C  C   . LEU D  1 98  ? -33.527 -30.609 76.872  1.00 39.84 ? 101  LEU D C   1 
ATOM   8302  O  O   . LEU D  1 98  ? -33.072 -31.724 76.622  1.00 41.49 ? 101  LEU D O   1 
ATOM   8303  C  CB  . LEU D  1 98  ? -36.024 -30.720 76.464  1.00 37.56 ? 101  LEU D CB  1 
ATOM   8304  C  CG  . LEU D  1 98  ? -37.416 -30.983 77.040  1.00 38.52 ? 101  LEU D CG  1 
ATOM   8305  C  CD1 . LEU D  1 98  ? -38.259 -31.819 76.089  1.00 37.52 ? 101  LEU D CD1 1 
ATOM   8306  C  CD2 . LEU D  1 98  ? -37.321 -31.661 78.401  1.00 37.22 ? 101  LEU D CD2 1 
ATOM   8307  N  N   . THR D  1 99  ? -32.839 -29.497 76.625  1.00 38.10 ? 102  THR D N   1 
ATOM   8308  C  CA  . THR D  1 99  ? -31.503 -29.565 76.028  1.00 39.26 ? 102  THR D CA  1 
ATOM   8309  C  C   . THR D  1 99  ? -30.368 -29.606 77.067  1.00 43.67 ? 102  THR D C   1 
ATOM   8310  O  O   . THR D  1 99  ? -29.187 -29.561 76.702  1.00 44.04 ? 102  THR D O   1 
ATOM   8311  C  CB  . THR D  1 99  ? -31.251 -28.403 75.034  1.00 37.12 ? 102  THR D CB  1 
ATOM   8312  O  OG1 . THR D  1 99  ? -31.272 -27.158 75.734  1.00 34.92 ? 102  THR D OG1 1 
ATOM   8313  C  CG2 . THR D  1 99  ? -32.317 -28.375 73.946  1.00 36.11 ? 102  THR D CG2 1 
ATOM   8314  N  N   . GLY D  1 100 ? -30.714 -29.722 78.352  1.00 42.24 ? 103  GLY D N   1 
ATOM   8315  C  CA  . GLY D  1 100 ? -29.725 -30.075 79.365  1.00 43.11 ? 103  GLY D CA  1 
ATOM   8316  C  C   . GLY D  1 100 ? -29.040 -28.878 79.996  1.00 43.80 ? 103  GLY D C   1 
ATOM   8317  O  O   . GLY D  1 100 ? -29.445 -27.741 79.783  1.00 45.63 ? 103  GLY D O   1 
ATOM   8318  N  N   . PRO D  1 101 ? -27.990 -29.128 80.789  1.00 44.39 ? 104  PRO D N   1 
ATOM   8319  C  CA  . PRO D  1 101 ? -27.371 -28.055 81.574  1.00 44.47 ? 104  PRO D CA  1 
ATOM   8320  C  C   . PRO D  1 101 ? -26.655 -27.022 80.703  1.00 43.20 ? 104  PRO D C   1 
ATOM   8321  O  O   . PRO D  1 101 ? -25.758 -27.366 79.937  1.00 42.13 ? 104  PRO D O   1 
ATOM   8322  C  CB  . PRO D  1 101 ? -26.352 -28.798 82.446  1.00 43.21 ? 104  PRO D CB  1 
ATOM   8323  C  CG  . PRO D  1 101 ? -26.891 -30.195 82.527  1.00 44.51 ? 104  PRO D CG  1 
ATOM   8324  C  CD  . PRO D  1 101 ? -27.492 -30.456 81.178  1.00 43.25 ? 104  PRO D CD  1 
ATOM   8325  N  N   . ASP D  1 102 ? -26.990 -25.756 80.906  1.00 39.83 ? 105  ASP D N   1 
ATOM   8326  C  CA  . ASP D  1 102 ? -26.367 -24.678 80.173  1.00 42.22 ? 105  ASP D CA  1 
ATOM   8327  C  C   . ASP D  1 102 ? -24.871 -24.505 80.420  1.00 42.28 ? 105  ASP D C   1 
ATOM   8328  O  O   . ASP D  1 102 ? -24.368 -24.767 81.513  1.00 41.88 ? 105  ASP D O   1 
ATOM   8329  C  CB  . ASP D  1 102 ? -27.113 -23.367 80.410  1.00 43.81 ? 105  ASP D CB  1 
ATOM   8330  C  CG  . ASP D  1 102 ? -28.483 -23.366 79.762  1.00 45.68 ? 105  ASP D CG  1 
ATOM   8331  O  OD1 . ASP D  1 102 ? -28.761 -24.301 78.978  1.00 49.52 ? 105  ASP D OD1 1 
ATOM   8332  O  OD2 . ASP D  1 102 ? -29.271 -22.433 80.011  1.00 45.60 ? 105  ASP D OD2 1 
ATOM   8333  N  N   . PRO D  1 103 ? -24.150 -24.117 79.362  1.00 40.52 ? 106  PRO D N   1 
ATOM   8334  C  CA  . PRO D  1 103 ? -22.829 -23.504 79.408  1.00 40.27 ? 106  PRO D CA  1 
ATOM   8335  C  C   . PRO D  1 103 ? -22.854 -22.180 80.181  1.00 39.22 ? 106  PRO D C   1 
ATOM   8336  O  O   . PRO D  1 103 ? -23.891 -21.521 80.231  1.00 36.70 ? 106  PRO D O   1 
ATOM   8337  C  CB  . PRO D  1 103 ? -22.533 -23.230 77.926  1.00 40.63 ? 106  PRO D CB  1 
ATOM   8338  C  CG  . PRO D  1 103 ? -23.911 -23.069 77.304  1.00 39.92 ? 106  PRO D CG  1 
ATOM   8339  C  CD  . PRO D  1 103 ? -24.726 -24.106 78.003  1.00 40.07 ? 106  PRO D CD  1 
ATOM   8340  N  N   . PRO D  1 104 ? -21.693 -21.753 80.702  1.00 40.35 ? 107  PRO D N   1 
ATOM   8341  C  CA  . PRO D  1 104 ? -21.520 -20.386 81.195  1.00 42.35 ? 107  PRO D CA  1 
ATOM   8342  C  C   . PRO D  1 104 ? -22.031 -19.391 80.168  1.00 45.69 ? 107  PRO D C   1 
ATOM   8343  O  O   . PRO D  1 104 ? -22.132 -19.727 78.989  1.00 48.23 ? 107  PRO D O   1 
ATOM   8344  C  CB  . PRO D  1 104 ? -19.998 -20.238 81.317  1.00 41.86 ? 107  PRO D CB  1 
ATOM   8345  C  CG  . PRO D  1 104 ? -19.469 -21.612 81.409  1.00 41.44 ? 107  PRO D CG  1 
ATOM   8346  C  CD  . PRO D  1 104 ? -20.424 -22.501 80.662  1.00 41.78 ? 107  PRO D CD  1 
ATOM   8347  N  N   . PRO D  1 105 ? -22.322 -18.153 80.596  1.00 48.48 ? 108  PRO D N   1 
ATOM   8348  C  CA  . PRO D  1 105 ? -22.698 -17.134 79.613  1.00 47.59 ? 108  PRO D CA  1 
ATOM   8349  C  C   . PRO D  1 105 ? -21.452 -16.564 78.947  1.00 46.84 ? 108  PRO D C   1 
ATOM   8350  O  O   . PRO D  1 105 ? -20.345 -16.777 79.442  1.00 47.49 ? 108  PRO D O   1 
ATOM   8351  C  CB  . PRO D  1 105 ? -23.388 -16.067 80.467  1.00 48.49 ? 108  PRO D CB  1 
ATOM   8352  C  CG  . PRO D  1 105 ? -23.802 -16.781 81.721  1.00 48.60 ? 108  PRO D CG  1 
ATOM   8353  C  CD  . PRO D  1 105 ? -22.699 -17.760 81.965  1.00 48.70 ? 108  PRO D CD  1 
ATOM   8354  N  N   . PRO D  1 106 ? -21.622 -15.822 77.841  1.00 45.40 ? 109  PRO D N   1 
ATOM   8355  C  CA  . PRO D  1 106 ? -22.897 -15.303 77.363  1.00 44.79 ? 109  PRO D CA  1 
ATOM   8356  C  C   . PRO D  1 106 ? -23.673 -16.290 76.501  1.00 43.91 ? 109  PRO D C   1 
ATOM   8357  O  O   . PRO D  1 106 ? -24.820 -16.032 76.159  1.00 44.18 ? 109  PRO D O   1 
ATOM   8358  C  CB  . PRO D  1 106 ? -22.495 -14.082 76.523  1.00 44.91 ? 109  PRO D CB  1 
ATOM   8359  C  CG  . PRO D  1 106 ? -21.046 -13.841 76.816  1.00 44.97 ? 109  PRO D CG  1 
ATOM   8360  C  CD  . PRO D  1 106 ? -20.486 -15.171 77.176  1.00 44.37 ? 109  PRO D CD  1 
ATOM   8361  N  N   . ALA D  1 107 ? -23.076 -17.428 76.173  1.00 44.06 ? 110  ALA D N   1 
ATOM   8362  C  CA  . ALA D  1 107 ? -23.823 -18.450 75.451  1.00 43.12 ? 110  ALA D CA  1 
ATOM   8363  C  C   . ALA D  1 107 ? -25.179 -18.568 76.119  1.00 41.30 ? 110  ALA D C   1 
ATOM   8364  O  O   . ALA D  1 107 ? -25.274 -18.457 77.336  1.00 42.41 ? 110  ALA D O   1 
ATOM   8365  C  CB  . ALA D  1 107 ? -23.090 -19.783 75.499  1.00 44.23 ? 110  ALA D CB  1 
ATOM   8366  N  N   . SER D  1 108 ? -26.231 -18.787 75.340  1.00 40.12 ? 111  SER D N   1 
ATOM   8367  C  CA  . SER D  1 108 ? -27.574 -18.749 75.915  1.00 38.83 ? 111  SER D CA  1 
ATOM   8368  C  C   . SER D  1 108 ? -28.437 -19.948 75.562  1.00 35.16 ? 111  SER D C   1 
ATOM   8369  O  O   . SER D  1 108 ? -29.498 -20.142 76.141  1.00 36.44 ? 111  SER D O   1 
ATOM   8370  C  CB  . SER D  1 108 ? -28.288 -17.460 75.521  1.00 40.39 ? 111  SER D CB  1 
ATOM   8371  O  OG  . SER D  1 108 ? -28.629 -17.495 74.146  1.00 44.60 ? 111  SER D OG  1 
ATOM   8372  N  N   . VAL D  1 109 ? -27.983 -20.750 74.608  1.00 33.20 ? 112  VAL D N   1 
ATOM   8373  C  CA  . VAL D  1 109 ? -28.743 -21.909 74.142  1.00 28.76 ? 112  VAL D CA  1 
ATOM   8374  C  C   . VAL D  1 109 ? -30.252 -21.655 74.034  1.00 27.66 ? 112  VAL D C   1 
ATOM   8375  O  O   . VAL D  1 109 ? -31.065 -22.480 74.467  1.00 27.12 ? 112  VAL D O   1 
ATOM   8376  C  CB  . VAL D  1 109 ? -28.482 -23.138 75.021  1.00 26.43 ? 112  VAL D CB  1 
ATOM   8377  C  CG1 . VAL D  1 109 ? -29.043 -24.389 74.365  1.00 26.44 ? 112  VAL D CG1 1 
ATOM   8378  C  CG2 . VAL D  1 109 ? -27.014 -23.304 75.257  1.00 28.09 ? 112  VAL D CG2 1 
ATOM   8379  N  N   . GLY D  1 110 ? -30.621 -20.575 73.349  1.00 27.72 ? 113  GLY D N   1 
ATOM   8380  C  CA  . GLY D  1 110 ? -32.026 -20.142 73.284  1.00 27.71 ? 113  GLY D CA  1 
ATOM   8381  C  C   . GLY D  1 110 ? -32.993 -20.896 72.371  1.00 25.81 ? 113  GLY D C   1 
ATOM   8382  O  O   . GLY D  1 110 ? -34.155 -20.543 72.292  1.00 27.27 ? 113  GLY D O   1 
ATOM   8383  N  N   . GLY D  1 111 ? -32.527 -21.892 71.628  1.00 26.64 ? 114  GLY D N   1 
ATOM   8384  C  CA  . GLY D  1 111 ? -33.334 -22.412 70.514  1.00 26.65 ? 114  GLY D CA  1 
ATOM   8385  C  C   . GLY D  1 111 ? -33.477 -21.428 69.358  1.00 27.48 ? 114  GLY D C   1 
ATOM   8386  O  O   . GLY D  1 111 ? -33.059 -20.263 69.457  1.00 28.31 ? 114  GLY D O   1 
ATOM   8387  N  N   . LEU D  1 112 ? -34.108 -21.871 68.271  1.00 25.12 ? 115  LEU D N   1 
ATOM   8388  C  CA  . LEU D  1 112 ? -34.139 -21.083 67.045  1.00 22.02 ? 115  LEU D CA  1 
ATOM   8389  C  C   . LEU D  1 112 ? -34.870 -19.767 67.272  1.00 26.26 ? 115  LEU D C   1 
ATOM   8390  O  O   . LEU D  1 112 ? -34.693 -18.811 66.513  1.00 23.02 ? 115  LEU D O   1 
ATOM   8391  C  CB  . LEU D  1 112 ? -34.798 -21.863 65.905  1.00 24.06 ? 115  LEU D CB  1 
ATOM   8392  C  CG  . LEU D  1 112 ? -34.101 -23.146 65.429  1.00 24.84 ? 115  LEU D CG  1 
ATOM   8393  C  CD1 . LEU D  1 112 ? -34.820 -23.705 64.209  1.00 24.02 ? 115  LEU D CD1 1 
ATOM   8394  C  CD2 . LEU D  1 112 ? -32.629 -22.882 65.130  1.00 21.44 ? 115  LEU D CD2 1 
ATOM   8395  N  N   . ASN D  1 113 ? -35.633 -19.707 68.362  1.00 29.39 ? 116  ASN D N   1 
ATOM   8396  C  CA  . ASN D  1 113 ? -36.405 -18.511 68.744  1.00 32.02 ? 116  ASN D CA  1 
ATOM   8397  C  C   . ASN D  1 113 ? -35.519 -17.344 69.194  1.00 31.92 ? 116  ASN D C   1 
ATOM   8398  O  O   . ASN D  1 113 ? -35.973 -16.210 69.295  1.00 33.18 ? 116  ASN D O   1 
ATOM   8399  C  CB  . ASN D  1 113 ? -37.379 -18.858 69.882  1.00 34.06 ? 116  ASN D CB  1 
ATOM   8400  C  CG  . ASN D  1 113 ? -38.674 -19.487 69.386  1.00 34.76 ? 116  ASN D CG  1 
ATOM   8401  O  OD1 . ASN D  1 113 ? -39.714 -19.386 70.040  1.00 38.86 ? 116  ASN D OD1 1 
ATOM   8402  N  ND2 . ASN D  1 113 ? -38.609 -20.173 68.259  1.00 33.71 ? 116  ASN D ND2 1 
ATOM   8403  N  N   . GLU D  1 114 ? -34.265 -17.641 69.503  1.00 32.81 ? 117  GLU D N   1 
ATOM   8404  C  CA  . GLU D  1 114 ? -33.356 -16.646 70.043  1.00 32.55 ? 117  GLU D CA  1 
ATOM   8405  C  C   . GLU D  1 114 ? -33.088 -15.577 69.002  1.00 32.21 ? 117  GLU D C   1 
ATOM   8406  O  O   . GLU D  1 114 ? -32.619 -15.864 67.892  1.00 30.55 ? 117  GLU D O   1 
ATOM   8407  C  CB  . GLU D  1 114 ? -32.041 -17.307 70.461  1.00 35.59 ? 117  GLU D CB  1 
ATOM   8408  C  CG  . GLU D  1 114 ? -31.055 -16.373 71.128  1.00 37.05 ? 117  GLU D CG  1 
ATOM   8409  C  CD  . GLU D  1 114 ? -31.421 -16.078 72.570  1.00 41.46 ? 117  GLU D CD  1 
ATOM   8410  O  OE1 . GLU D  1 114 ? -32.258 -16.812 73.153  1.00 42.28 ? 117  GLU D OE1 1 
ATOM   8411  O  OE2 . GLU D  1 114 ? -30.889 -15.090 73.114  1.00 43.06 ? 117  GLU D OE2 1 
ATOM   8412  N  N   . HIS D  1 115 ? -33.423 -14.346 69.349  1.00 28.70 ? 118  HIS D N   1 
ATOM   8413  C  CA  . HIS D  1 115 ? -33.354 -13.267 68.410  1.00 27.68 ? 118  HIS D CA  1 
ATOM   8414  C  C   . HIS D  1 115 ? -31.904 -12.837 68.215  1.00 30.07 ? 118  HIS D C   1 
ATOM   8415  O  O   . HIS D  1 115 ? -31.137 -12.816 69.175  1.00 28.78 ? 118  HIS D O   1 
ATOM   8416  C  CB  . HIS D  1 115 ? -34.160 -12.085 68.915  1.00 30.39 ? 118  HIS D CB  1 
ATOM   8417  C  CG  . HIS D  1 115 ? -34.060 -10.886 68.029  1.00 30.23 ? 118  HIS D CG  1 
ATOM   8418  N  ND1 . HIS D  1 115 ? -34.725 -10.800 66.826  1.00 28.21 ? 118  HIS D ND1 1 
ATOM   8419  C  CD2 . HIS D  1 115 ? -33.297 -9.774  68.120  1.00 30.50 ? 118  HIS D CD2 1 
ATOM   8420  C  CE1 . HIS D  1 115 ? -34.416 -9.657  66.240  1.00 31.65 ? 118  HIS D CE1 1 
ATOM   8421  N  NE2 . HIS D  1 115 ? -33.558 -9.012  67.008  1.00 30.92 ? 118  HIS D NE2 1 
ATOM   8422  N  N   . GLY D  1 116 ? -31.518 -12.559 66.965  1.00 28.72 ? 119  GLY D N   1 
ATOM   8423  C  CA  . GLY D  1 116 ? -30.217 -11.969 66.674  1.00 24.59 ? 119  GLY D CA  1 
ATOM   8424  C  C   . GLY D  1 116 ? -29.096 -12.983 66.544  1.00 25.12 ? 119  GLY D C   1 
ATOM   8425  O  O   . GLY D  1 116 ? -27.963 -12.623 66.268  1.00 26.31 ? 119  GLY D O   1 
ATOM   8426  N  N   . THR D  1 117 ? -29.391 -14.252 66.771  1.00 24.95 ? 120  THR D N   1 
ATOM   8427  C  CA  . THR D  1 117 ? -28.424 -15.285 66.459  1.00 25.61 ? 120  THR D CA  1 
ATOM   8428  C  C   . THR D  1 117 ? -28.677 -15.831 65.054  1.00 28.55 ? 120  THR D C   1 
ATOM   8429  O  O   . THR D  1 117 ? -27.931 -15.523 64.120  1.00 32.33 ? 120  THR D O   1 
ATOM   8430  C  CB  . THR D  1 117 ? -28.470 -16.440 67.472  1.00 28.10 ? 120  THR D CB  1 
ATOM   8431  O  OG1 . THR D  1 117 ? -29.828 -16.848 67.665  1.00 26.27 ? 120  THR D OG1 1 
ATOM   8432  C  CG2 . THR D  1 117 ? -27.840 -16.021 68.822  1.00 26.61 ? 120  THR D CG2 1 
ATOM   8433  N  N   . PHE D  1 118 ? -29.723 -16.639 64.906  1.00 25.04 ? 121  PHE D N   1 
ATOM   8434  C  CA  . PHE D  1 118 ? -30.174 -17.089 63.581  1.00 25.97 ? 121  PHE D CA  1 
ATOM   8435  C  C   . PHE D  1 118 ? -31.433 -16.301 63.195  1.00 27.30 ? 121  PHE D C   1 
ATOM   8436  O  O   . PHE D  1 118 ? -31.397 -15.468 62.277  1.00 29.19 ? 121  PHE D O   1 
ATOM   8437  C  CB  . PHE D  1 118 ? -30.441 -18.607 63.592  1.00 22.45 ? 121  PHE D CB  1 
ATOM   8438  C  CG  . PHE D  1 118 ? -30.304 -19.277 62.238  1.00 22.73 ? 121  PHE D CG  1 
ATOM   8439  C  CD1 . PHE D  1 118 ? -31.118 -18.909 61.175  1.00 21.78 ? 121  PHE D CD1 1 
ATOM   8440  C  CD2 . PHE D  1 118 ? -29.355 -20.277 62.033  1.00 20.65 ? 121  PHE D CD2 1 
ATOM   8441  C  CE1 . PHE D  1 118 ? -30.976 -19.502 59.933  1.00 21.78 ? 121  PHE D CE1 1 
ATOM   8442  C  CE2 . PHE D  1 118 ? -29.220 -20.895 60.797  1.00 18.68 ? 121  PHE D CE2 1 
ATOM   8443  C  CZ  . PHE D  1 118 ? -30.048 -20.532 59.751  1.00 20.36 ? 121  PHE D CZ  1 
ATOM   8444  N  N   . GLU D  1 119 ? -32.491 -16.442 63.994  1.00 24.73 ? 122  GLU D N   1 
ATOM   8445  C  CA  . GLU D  1 119 ? -33.723 -15.658 63.800  1.00 24.27 ? 122  GLU D CA  1 
ATOM   8446  C  C   . GLU D  1 119 ? -33.465 -14.144 63.706  1.00 26.03 ? 122  GLU D C   1 
ATOM   8447  O  O   . GLU D  1 119 ? -32.542 -13.631 64.329  1.00 29.24 ? 122  GLU D O   1 
ATOM   8448  C  CB  . GLU D  1 119 ? -34.724 -15.963 64.915  1.00 24.10 ? 122  GLU D CB  1 
ATOM   8449  C  CG  . GLU D  1 119 ? -36.143 -15.483 64.646  1.00 24.75 ? 122  GLU D CG  1 
ATOM   8450  C  CD  . GLU D  1 119 ? -36.304 -14.000 64.838  1.00 26.67 ? 122  GLU D CD  1 
ATOM   8451  O  OE1 . GLU D  1 119 ? -35.648 -13.478 65.781  1.00 30.24 ? 122  GLU D OE1 1 
ATOM   8452  O  OE2 . GLU D  1 119 ? -37.050 -13.366 64.031  1.00 25.05 ? 122  GLU D OE2 1 
ATOM   8453  N  N   . GLY D  1 120 ? -34.280 -13.432 62.926  1.00 26.44 ? 123  GLY D N   1 
ATOM   8454  C  CA  . GLY D  1 120 ? -34.059 -12.013 62.690  1.00 23.03 ? 123  GLY D CA  1 
ATOM   8455  C  C   . GLY D  1 120 ? -35.254 -11.255 62.125  1.00 23.09 ? 123  GLY D C   1 
ATOM   8456  O  O   . GLY D  1 120 ? -36.282 -11.838 61.813  1.00 23.86 ? 123  GLY D O   1 
ATOM   8457  N  N   . ASP D  1 121 ? -35.079 -9.958  61.914  1.00 21.10 ? 124  ASP D N   1 
ATOM   8458  C  CA  . ASP D  1 121 ? -36.127 -9.104  61.373  1.00 25.25 ? 124  ASP D CA  1 
ATOM   8459  C  C   . ASP D  1 121 ? -36.500 -9.358  59.903  1.00 26.00 ? 124  ASP D C   1 
ATOM   8460  O  O   . ASP D  1 121 ? -35.758 -9.995  59.142  1.00 28.33 ? 124  ASP D O   1 
ATOM   8461  C  CB  . ASP D  1 121 ? -35.735 -7.637  61.547  1.00 25.60 ? 124  ASP D CB  1 
ATOM   8462  C  CG  . ASP D  1 121 ? -35.360 -7.293  62.990  1.00 27.63 ? 124  ASP D CG  1 
ATOM   8463  O  OD1 . ASP D  1 121 ? -35.801 -8.021  63.908  1.00 28.09 ? 124  ASP D OD1 1 
ATOM   8464  O  OD2 . ASP D  1 121 ? -34.641 -6.284  63.201  1.00 28.30 ? 124  ASP D OD2 1 
ATOM   8465  N  N   . ALA D  1 122 ? -37.607 -8.743  59.497  1.00 25.82 ? 125  ALA D N   1 
ATOM   8466  C  CA  . ALA D  1 122 ? -38.090 -8.765  58.116  1.00 25.81 ? 125  ALA D CA  1 
ATOM   8467  C  C   . ALA D  1 122 ? -38.479 -10.153 57.645  1.00 26.66 ? 125  ALA D C   1 
ATOM   8468  O  O   . ALA D  1 122 ? -38.426 -10.437 56.449  1.00 28.06 ? 125  ALA D O   1 
ATOM   8469  C  CB  . ALA D  1 122 ? -37.082 -8.164  57.173  1.00 22.80 ? 125  ALA D CB  1 
ATOM   8470  N  N   . SER D  1 123 ? -38.835 -11.024 58.580  1.00 26.23 ? 126  SER D N   1 
ATOM   8471  C  CA  . SER D  1 123 ? -39.345 -12.341 58.215  1.00 28.39 ? 126  SER D CA  1 
ATOM   8472  C  C   . SER D  1 123 ? -40.645 -12.175 57.422  1.00 30.00 ? 126  SER D C   1 
ATOM   8473  O  O   . SER D  1 123 ? -41.347 -11.175 57.567  1.00 29.91 ? 126  SER D O   1 
ATOM   8474  C  CB  . SER D  1 123 ? -39.566 -13.195 59.465  1.00 26.96 ? 126  SER D CB  1 
ATOM   8475  O  OG  . SER D  1 123 ? -38.350 -13.399 60.188  1.00 29.52 ? 126  SER D OG  1 
ATOM   8476  N  N   . MET D  1 124 ? -40.958 -13.126 56.552  1.00 32.11 ? 127  MET D N   1 
ATOM   8477  C  CA  . MET D  1 124 ? -42.150 -12.977 55.703  1.00 33.75 ? 127  MET D CA  1 
ATOM   8478  C  C   . MET D  1 124 ? -43.465 -13.144 56.471  1.00 31.78 ? 127  MET D C   1 
ATOM   8479  O  O   . MET D  1 124 ? -44.402 -12.362 56.293  1.00 30.01 ? 127  MET D O   1 
ATOM   8480  C  CB  . MET D  1 124 ? -42.103 -13.964 54.542  1.00 35.04 ? 127  MET D CB  1 
ATOM   8481  C  CG  . MET D  1 124 ? -41.021 -13.643 53.545  1.00 34.17 ? 127  MET D CG  1 
ATOM   8482  S  SD  . MET D  1 124 ? -40.985 -14.878 52.253  1.00 35.24 ? 127  MET D SD  1 
ATOM   8483  C  CE  . MET D  1 124 ? -40.812 -16.384 53.189  1.00 29.69 ? 127  MET D CE  1 
ATOM   8484  N  N   . THR D  1 125 ? -43.523 -14.162 57.321  1.00 28.44 ? 128  THR D N   1 
ATOM   8485  C  CA  . THR D  1 125 ? -44.767 -14.533 57.979  1.00 30.14 ? 128  THR D CA  1 
ATOM   8486  C  C   . THR D  1 125 ? -44.708 -14.509 59.517  1.00 30.58 ? 128  THR D C   1 
ATOM   8487  O  O   . THR D  1 125 ? -45.692 -14.841 60.179  1.00 29.79 ? 128  THR D O   1 
ATOM   8488  C  CB  . THR D  1 125 ? -45.228 -15.920 57.546  1.00 28.70 ? 128  THR D CB  1 
ATOM   8489  O  OG1 . THR D  1 125 ? -44.366 -16.897 58.128  1.00 27.41 ? 128  THR D OG1 1 
ATOM   8490  C  CG2 . THR D  1 125 ? -45.196 -16.055 56.018  1.00 28.83 ? 128  THR D CG2 1 
ATOM   8491  N  N   . ARG D  1 126 ? -43.568 -14.104 60.074  1.00 31.19 ? 129  ARG D N   1 
ATOM   8492  C  CA  . ARG D  1 126 ? -43.409 -13.929 61.522  1.00 28.50 ? 129  ARG D CA  1 
ATOM   8493  C  C   . ARG D  1 126 ? -43.064 -12.475 61.775  1.00 28.17 ? 129  ARG D C   1 
ATOM   8494  O  O   . ARG D  1 126 ? -42.515 -11.817 60.900  1.00 28.29 ? 129  ARG D O   1 
ATOM   8495  C  CB  . ARG D  1 126 ? -42.267 -14.797 62.038  1.00 28.22 ? 129  ARG D CB  1 
ATOM   8496  C  CG  . ARG D  1 126 ? -42.679 -16.152 62.561  1.00 29.01 ? 129  ARG D CG  1 
ATOM   8497  C  CD  . ARG D  1 126 ? -43.241 -17.058 61.473  1.00 28.39 ? 129  ARG D CD  1 
ATOM   8498  N  NE  . ARG D  1 126 ? -43.478 -18.397 62.009  1.00 29.37 ? 129  ARG D NE  1 
ATOM   8499  C  CZ  . ARG D  1 126 ? -44.245 -19.318 61.435  1.00 31.82 ? 129  ARG D CZ  1 
ATOM   8500  N  NH1 . ARG D  1 126 ? -44.817 -19.087 60.255  1.00 32.61 ? 129  ARG D NH1 1 
ATOM   8501  N  NH2 . ARG D  1 126 ? -44.454 -20.477 62.048  1.00 32.64 ? 129  ARG D NH2 1 
ATOM   8502  N  N   . GLY D  1 127 ? -43.347 -11.982 62.982  1.00 29.88 ? 130  GLY D N   1 
ATOM   8503  C  CA  . GLY D  1 127 ? -43.160 -10.560 63.301  1.00 26.01 ? 130  GLY D CA  1 
ATOM   8504  C  C   . GLY D  1 127 ? -41.763 -10.361 63.850  1.00 27.22 ? 130  GLY D C   1 
ATOM   8505  O  O   . GLY D  1 127 ? -41.103 -11.332 64.218  1.00 26.33 ? 130  GLY D O   1 
ATOM   8506  N  N   . ASP D  1 128 ? -41.268 -9.128  63.819  1.00 29.39 ? 131  ASP D N   1 
ATOM   8507  C  CA  . ASP D  1 128 ? -39.982 -8.829  64.455  1.00 31.86 ? 131  ASP D CA  1 
ATOM   8508  C  C   . ASP D  1 128 ? -40.042 -9.046  65.966  1.00 33.15 ? 131  ASP D C   1 
ATOM   8509  O  O   . ASP D  1 128 ? -41.100 -8.899  66.573  1.00 33.41 ? 131  ASP D O   1 
ATOM   8510  C  CB  . ASP D  1 128 ? -39.505 -7.417  64.110  1.00 31.76 ? 131  ASP D CB  1 
ATOM   8511  C  CG  . ASP D  1 128 ? -39.251 -7.238  62.612  1.00 33.55 ? 131  ASP D CG  1 
ATOM   8512  O  OD1 . ASP D  1 128 ? -39.347 -8.247  61.877  1.00 34.95 ? 131  ASP D OD1 1 
ATOM   8513  O  OD2 . ASP D  1 128 ? -38.951 -6.105  62.168  1.00 31.03 ? 131  ASP D OD2 1 
ATOM   8514  N  N   . ALA D  1 129 ? -38.929 -9.505  66.537  1.00 35.62 ? 132  ALA D N   1 
ATOM   8515  C  CA  . ALA D  1 129 ? -38.803 -9.730  67.979  1.00 35.80 ? 132  ALA D CA  1 
ATOM   8516  C  C   . ALA D  1 129 ? -39.199 -8.496  68.766  1.00 38.29 ? 132  ALA D C   1 
ATOM   8517  O  O   . ALA D  1 129 ? -39.824 -8.594  69.818  1.00 41.56 ? 132  ALA D O   1 
ATOM   8518  C  CB  . ALA D  1 129 ? -37.372 -10.128 68.319  1.00 33.24 ? 132  ALA D CB  1 
ATOM   8519  N  N   . PHE D  1 130 ? -38.792 -7.330  68.280  1.00 38.73 ? 133  PHE D N   1 
ATOM   8520  C  CA  . PHE D  1 130 ? -39.121 -6.099  68.965  1.00 42.39 ? 133  PHE D CA  1 
ATOM   8521  C  C   . PHE D  1 130 ? -40.581 -6.083  69.398  1.00 44.72 ? 133  PHE D C   1 
ATOM   8522  O  O   . PHE D  1 130 ? -40.898 -5.608  70.484  1.00 44.41 ? 133  PHE D O   1 
ATOM   8523  C  CB  . PHE D  1 130 ? -38.823 -4.872  68.108  1.00 41.79 ? 133  PHE D CB  1 
ATOM   8524  C  CG  . PHE D  1 130 ? -39.129 -3.573  68.803  1.00 45.19 ? 133  PHE D CG  1 
ATOM   8525  C  CD1 . PHE D  1 130 ? -38.187 -2.976  69.631  1.00 44.67 ? 133  PHE D CD1 1 
ATOM   8526  C  CD2 . PHE D  1 130 ? -40.391 -2.992  68.697  1.00 45.11 ? 133  PHE D CD2 1 
ATOM   8527  C  CE1 . PHE D  1 130 ? -38.478 -1.802  70.298  1.00 43.60 ? 133  PHE D CE1 1 
ATOM   8528  C  CE2 . PHE D  1 130 ? -40.688 -1.815  69.359  1.00 44.25 ? 133  PHE D CE2 1 
ATOM   8529  C  CZ  . PHE D  1 130 ? -39.731 -1.216  70.154  1.00 43.79 ? 133  PHE D CZ  1 
ATOM   8530  N  N   . PHE D  1 131 ? -41.468 -6.577  68.536  1.00 45.51 ? 134  PHE D N   1 
ATOM   8531  C  CA  . PHE D  1 131 ? -42.896 -6.339  68.704  1.00 47.35 ? 134  PHE D CA  1 
ATOM   8532  C  C   . PHE D  1 131 ? -43.492 -7.358  69.651  1.00 47.96 ? 134  PHE D C   1 
ATOM   8533  O  O   . PHE D  1 131 ? -44.647 -7.241  70.055  1.00 48.74 ? 134  PHE D O   1 
ATOM   8534  C  CB  . PHE D  1 131 ? -43.627 -6.346  67.356  1.00 46.73 ? 134  PHE D CB  1 
ATOM   8535  C  CG  . PHE D  1 131 ? -43.253 -5.200  66.469  1.00 46.93 ? 134  PHE D CG  1 
ATOM   8536  C  CD1 . PHE D  1 131 ? -43.459 -3.894  66.882  1.00 48.07 ? 134  PHE D CD1 1 
ATOM   8537  C  CD2 . PHE D  1 131 ? -42.627 -5.420  65.251  1.00 47.98 ? 134  PHE D CD2 1 
ATOM   8538  C  CE1 . PHE D  1 131 ? -43.086 -2.825  66.075  1.00 47.97 ? 134  PHE D CE1 1 
ATOM   8539  C  CE2 . PHE D  1 131 ? -42.281 -4.354  64.421  1.00 47.85 ? 134  PHE D CE2 1 
ATOM   8540  C  CZ  . PHE D  1 131 ? -42.500 -3.058  64.842  1.00 48.17 ? 134  PHE D CZ  1 
ATOM   8541  N  N   . GLY D  1 132 ? -42.696 -8.361  70.004  1.00 47.89 ? 135  GLY D N   1 
ATOM   8542  C  CA  . GLY D  1 132 ? -42.992 -9.179  71.170  1.00 47.04 ? 135  GLY D CA  1 
ATOM   8543  C  C   . GLY D  1 132 ? -43.111 -10.657 70.866  1.00 46.79 ? 135  GLY D C   1 
ATOM   8544  O  O   . GLY D  1 132 ? -43.042 -11.490 71.773  1.00 48.26 ? 135  GLY D O   1 
ATOM   8545  N  N   . ASN D  1 133 ? -43.303 -10.994 69.596  1.00 43.22 ? 136  ASN D N   1 
ATOM   8546  C  CA  . ASN D  1 133 ? -43.404 -12.399 69.216  1.00 41.95 ? 136  ASN D CA  1 
ATOM   8547  C  C   . ASN D  1 133 ? -42.885 -12.700 67.809  1.00 40.48 ? 136  ASN D C   1 
ATOM   8548  O  O   . ASN D  1 133 ? -43.495 -12.294 66.815  1.00 33.35 ? 136  ASN D O   1 
ATOM   8549  C  CB  . ASN D  1 133 ? -44.839 -12.913 69.370  1.00 41.55 ? 136  ASN D CB  1 
ATOM   8550  C  CG  . ASN D  1 133 ? -44.955 -14.401 69.082  1.00 43.08 ? 136  ASN D CG  1 
ATOM   8551  O  OD1 . ASN D  1 133 ? -44.340 -14.917 68.149  1.00 42.43 ? 136  ASN D OD1 1 
ATOM   8552  N  ND2 . ASN D  1 133 ? -45.755 -15.095 69.877  1.00 43.01 ? 136  ASN D ND2 1 
ATOM   8553  N  N   . ASN D  1 134 ? -41.810 -13.491 67.748  1.00 38.43 ? 137  ASN D N   1 
ATOM   8554  C  CA  . ASN D  1 134 ? -41.021 -13.656 66.531  1.00 38.26 ? 137  ASN D CA  1 
ATOM   8555  C  C   . ASN D  1 134 ? -41.053 -15.085 66.006  1.00 38.31 ? 137  ASN D C   1 
ATOM   8556  O  O   . ASN D  1 134 ? -40.135 -15.504 65.306  1.00 37.17 ? 137  ASN D O   1 
ATOM   8557  C  CB  . ASN D  1 134 ? -39.565 -13.281 66.795  1.00 37.14 ? 137  ASN D CB  1 
ATOM   8558  C  CG  . ASN D  1 134 ? -38.830 -14.343 67.617  1.00 36.08 ? 137  ASN D CG  1 
ATOM   8559  O  OD1 . ASN D  1 134 ? -39.452 -15.252 68.177  1.00 32.14 ? 137  ASN D OD1 1 
ATOM   8560  N  ND2 . ASN D  1 134 ? -37.503 -14.235 67.680  1.00 34.43 ? 137  ASN D ND2 1 
ATOM   8561  N  N   . HIS D  1 135 ? -42.036 -15.871 66.423  1.00 37.76 ? 138  HIS D N   1 
ATOM   8562  C  CA  . HIS D  1 135 ? -42.024 -17.286 66.058  1.00 40.65 ? 138  HIS D CA  1 
ATOM   8563  C  C   . HIS D  1 135 ? -43.366 -17.889 65.632  1.00 41.23 ? 138  HIS D C   1 
ATOM   8564  O  O   . HIS D  1 135 ? -43.391 -18.876 64.908  1.00 42.44 ? 138  HIS D O   1 
ATOM   8565  C  CB  . HIS D  1 135 ? -41.362 -18.139 67.144  1.00 41.81 ? 138  HIS D CB  1 
ATOM   8566  C  CG  . HIS D  1 135 ? -42.000 -18.005 68.491  1.00 44.14 ? 138  HIS D CG  1 
ATOM   8567  N  ND1 . HIS D  1 135 ? -41.726 -16.953 69.342  1.00 46.33 ? 138  HIS D ND1 1 
ATOM   8568  C  CD2 . HIS D  1 135 ? -42.857 -18.815 69.156  1.00 43.66 ? 138  HIS D CD2 1 
ATOM   8569  C  CE1 . HIS D  1 135 ? -42.409 -17.107 70.462  1.00 45.84 ? 138  HIS D CE1 1 
ATOM   8570  N  NE2 . HIS D  1 135 ? -43.109 -18.225 70.371  1.00 45.50 ? 138  HIS D NE2 1 
ATOM   8571  N  N   . ASP D  1 136 ? -44.469 -17.355 66.147  1.00 42.09 ? 139  ASP D N   1 
ATOM   8572  C  CA  . ASP D  1 136 ? -45.789 -17.843 65.765  1.00 43.49 ? 139  ASP D CA  1 
ATOM   8573  C  C   . ASP D  1 136 ? -46.162 -17.286 64.397  1.00 41.47 ? 139  ASP D C   1 
ATOM   8574  O  O   . ASP D  1 136 ? -45.828 -16.151 64.074  1.00 41.31 ? 139  ASP D O   1 
ATOM   8575  C  CB  . ASP D  1 136 ? -46.842 -17.431 66.803  1.00 44.45 ? 139  ASP D CB  1 
ATOM   8576  C  CG  . ASP D  1 136 ? -46.571 -18.024 68.181  1.00 45.65 ? 139  ASP D CG  1 
ATOM   8577  O  OD1 . ASP D  1 136 ? -46.529 -19.264 68.308  1.00 42.32 ? 139  ASP D OD1 1 
ATOM   8578  O  OD2 . ASP D  1 136 ? -46.389 -17.238 69.138  1.00 47.40 ? 139  ASP D OD2 1 
ATOM   8579  N  N   . PHE D  1 137 ? -46.831 -18.106 63.593  1.00 42.19 ? 140  PHE D N   1 
ATOM   8580  C  CA  . PHE D  1 137 ? -47.444 -17.658 62.345  1.00 39.65 ? 140  PHE D CA  1 
ATOM   8581  C  C   . PHE D  1 137 ? -48.264 -16.394 62.574  1.00 39.04 ? 140  PHE D C   1 
ATOM   8582  O  O   . PHE D  1 137 ? -48.965 -16.273 63.569  1.00 43.33 ? 140  PHE D O   1 
ATOM   8583  C  CB  . PHE D  1 137 ? -48.313 -18.778 61.767  1.00 38.39 ? 140  PHE D CB  1 
ATOM   8584  C  CG  . PHE D  1 137 ? -49.172 -18.355 60.596  1.00 41.06 ? 140  PHE D CG  1 
ATOM   8585  C  CD1 . PHE D  1 137 ? -50.464 -17.879 60.795  1.00 41.54 ? 140  PHE D CD1 1 
ATOM   8586  C  CD2 . PHE D  1 137 ? -48.719 -18.508 59.293  1.00 40.57 ? 140  PHE D CD2 1 
ATOM   8587  C  CE1 . PHE D  1 137 ? -51.270 -17.521 59.714  1.00 41.53 ? 140  PHE D CE1 1 
ATOM   8588  C  CE2 . PHE D  1 137 ? -49.517 -18.147 58.213  1.00 39.70 ? 140  PHE D CE2 1 
ATOM   8589  C  CZ  . PHE D  1 137 ? -50.796 -17.663 58.426  1.00 40.47 ? 140  PHE D CZ  1 
ATOM   8590  N  N   . ASN D  1 138 ? -48.179 -15.449 61.652  1.00 37.44 ? 141  ASN D N   1 
ATOM   8591  C  CA  . ASN D  1 138 ? -48.895 -14.189 61.802  1.00 35.95 ? 141  ASN D CA  1 
ATOM   8592  C  C   . ASN D  1 138 ? -49.804 -13.924 60.608  1.00 35.84 ? 141  ASN D C   1 
ATOM   8593  O  O   . ASN D  1 138 ? -49.317 -13.794 59.483  1.00 36.43 ? 141  ASN D O   1 
ATOM   8594  C  CB  . ASN D  1 138 ? -47.898 -13.047 61.946  1.00 37.36 ? 141  ASN D CB  1 
ATOM   8595  C  CG  . ASN D  1 138 ? -48.562 -11.696 61.934  1.00 42.42 ? 141  ASN D CG  1 
ATOM   8596  O  OD1 . ASN D  1 138 ? -49.380 -11.397 61.059  1.00 41.03 ? 141  ASN D OD1 1 
ATOM   8597  N  ND2 . ASN D  1 138 ? -48.221 -10.863 62.916  1.00 46.60 ? 141  ASN D ND2 1 
ATOM   8598  N  N   . GLU D  1 139 ? -51.114 -13.832 60.845  1.00 35.54 ? 142  GLU D N   1 
ATOM   8599  C  CA  . GLU D  1 139 ? -52.084 -13.802 59.748  1.00 35.89 ? 142  GLU D CA  1 
ATOM   8600  C  C   . GLU D  1 139 ? -52.002 -12.552 58.872  1.00 34.08 ? 142  GLU D C   1 
ATOM   8601  O  O   . GLU D  1 139 ? -51.946 -12.659 57.647  1.00 33.99 ? 142  GLU D O   1 
ATOM   8602  C  CB  . GLU D  1 139 ? -53.527 -14.081 60.223  1.00 39.38 ? 142  GLU D CB  1 
ATOM   8603  C  CG  . GLU D  1 139 ? -54.595 -14.118 59.079  1.00 39.74 ? 142  GLU D CG  1 
ATOM   8604  C  CD  . GLU D  1 139 ? -54.640 -15.454 58.324  1.00 42.81 ? 142  GLU D CD  1 
ATOM   8605  O  OE1 . GLU D  1 139 ? -54.309 -16.495 58.930  1.00 42.37 ? 142  GLU D OE1 1 
ATOM   8606  O  OE2 . GLU D  1 139 ? -55.033 -15.473 57.129  1.00 42.66 ? 142  GLU D OE2 1 
ATOM   8607  N  N   . THR D  1 140 ? -51.939 -11.374 59.482  1.00 33.47 ? 143  THR D N   1 
ATOM   8608  C  CA  . THR D  1 140 ? -51.767 -10.156 58.697  1.00 35.21 ? 143  THR D CA  1 
ATOM   8609  C  C   . THR D  1 140 ? -50.579 -10.273 57.723  1.00 36.48 ? 143  THR D C   1 
ATOM   8610  O  O   . THR D  1 140 ? -50.663 -9.826  56.571  1.00 33.81 ? 143  THR D O   1 
ATOM   8611  C  CB  . THR D  1 140 ? -51.586 -8.909  59.581  1.00 37.85 ? 143  THR D CB  1 
ATOM   8612  O  OG1 . THR D  1 140 ? -52.772 -8.694  60.359  1.00 41.39 ? 143  THR D OG1 1 
ATOM   8613  C  CG2 . THR D  1 140 ? -51.322 -7.677  58.722  1.00 37.49 ? 143  THR D CG2 1 
ATOM   8614  N  N   . LEU D  1 141 ? -49.492 -10.904 58.166  1.00 34.79 ? 144  LEU D N   1 
ATOM   8615  C  CA  . LEU D  1 141 ? -48.289 -10.953 57.335  1.00 35.33 ? 144  LEU D CA  1 
ATOM   8616  C  C   . LEU D  1 141 ? -48.503 -11.930 56.193  1.00 35.73 ? 144  LEU D C   1 
ATOM   8617  O  O   . LEU D  1 141 ? -48.252 -11.595 55.036  1.00 37.44 ? 144  LEU D O   1 
ATOM   8618  C  CB  . LEU D  1 141 ? -47.039 -11.315 58.143  1.00 32.44 ? 144  LEU D CB  1 
ATOM   8619  C  CG  . LEU D  1 141 ? -46.546 -10.247 59.130  1.00 31.55 ? 144  LEU D CG  1 
ATOM   8620  C  CD1 . LEU D  1 141 ? -45.163 -10.579 59.689  1.00 29.47 ? 144  LEU D CD1 1 
ATOM   8621  C  CD2 . LEU D  1 141 ? -46.558 -8.871  58.500  1.00 28.90 ? 144  LEU D CD2 1 
ATOM   8622  N  N   . PHE D  1 142 ? -49.088 -13.082 56.504  1.00 35.34 ? 145  PHE D N   1 
ATOM   8623  C  CA  . PHE D  1 142 ? -49.351 -14.077 55.483  1.00 36.49 ? 145  PHE D CA  1 
ATOM   8624  C  C   . PHE D  1 142 ? -50.282 -13.553 54.394  1.00 37.92 ? 145  PHE D C   1 
ATOM   8625  O  O   . PHE D  1 142 ? -50.086 -13.828 53.215  1.00 40.34 ? 145  PHE D O   1 
ATOM   8626  C  CB  . PHE D  1 142 ? -49.880 -15.382 56.067  1.00 37.12 ? 145  PHE D CB  1 
ATOM   8627  C  CG  . PHE D  1 142 ? -50.254 -16.394 55.020  1.00 38.14 ? 145  PHE D CG  1 
ATOM   8628  C  CD1 . PHE D  1 142 ? -51.488 -16.330 54.390  1.00 39.28 ? 145  PHE D CD1 1 
ATOM   8629  C  CD2 . PHE D  1 142 ? -49.324 -17.316 54.566  1.00 36.24 ? 145  PHE D CD2 1 
ATOM   8630  C  CE1 . PHE D  1 142 ? -51.821 -17.241 53.387  1.00 39.57 ? 145  PHE D CE1 1 
ATOM   8631  C  CE2 . PHE D  1 142 ? -49.635 -18.208 53.560  1.00 36.80 ? 145  PHE D CE2 1 
ATOM   8632  C  CZ  . PHE D  1 142 ? -50.891 -18.187 52.979  1.00 39.44 ? 145  PHE D CZ  1 
ATOM   8633  N  N   . GLU D  1 143 ? -51.223 -12.703 54.767  1.00 36.86 ? 146  GLU D N   1 
ATOM   8634  C  CA  . GLU D  1 143 ? -52.137 -12.165 53.777  1.00 34.98 ? 146  GLU D CA  1 
ATOM   8635  C  C   . GLU D  1 143 ? -51.519 -11.044 52.957  1.00 32.32 ? 146  GLU D C   1 
ATOM   8636  O  O   . GLU D  1 143 ? -51.969 -10.758 51.849  1.00 32.12 ? 146  GLU D O   1 
ATOM   8637  C  CB  . GLU D  1 143 ? -53.454 -11.732 54.431  1.00 36.38 ? 146  GLU D CB  1 
ATOM   8638  C  CG  . GLU D  1 143 ? -54.243 -12.910 54.974  1.00 34.73 ? 146  GLU D CG  1 
ATOM   8639  C  CD  . GLU D  1 143 ? -55.522 -12.516 55.720  1.00 37.73 ? 146  GLU D CD  1 
ATOM   8640  O  OE1 . GLU D  1 143 ? -56.044 -11.390 55.495  1.00 34.87 ? 146  GLU D OE1 1 
ATOM   8641  O  OE2 . GLU D  1 143 ? -56.012 -13.363 56.519  1.00 39.35 ? 146  GLU D OE2 1 
ATOM   8642  N  N   . GLN D  1 144 ? -50.459 -10.432 53.469  1.00 31.40 ? 147  GLN D N   1 
ATOM   8643  C  CA  . GLN D  1 144 ? -49.632 -9.571  52.626  1.00 29.42 ? 147  GLN D CA  1 
ATOM   8644  C  C   . GLN D  1 144 ? -48.895 -10.397 51.557  1.00 29.76 ? 147  GLN D C   1 
ATOM   8645  O  O   . GLN D  1 144 ? -48.693 -9.928  50.443  1.00 33.26 ? 147  GLN D O   1 
ATOM   8646  C  CB  . GLN D  1 144 ? -48.646 -8.768  53.470  1.00 29.17 ? 147  GLN D CB  1 
ATOM   8647  C  CG  . GLN D  1 144 ? -47.891 -7.719  52.699  1.00 26.98 ? 147  GLN D CG  1 
ATOM   8648  C  CD  . GLN D  1 144 ? -46.866 -6.994  53.541  1.00 31.18 ? 147  GLN D CD  1 
ATOM   8649  O  OE1 . GLN D  1 144 ? -46.764 -5.762  53.486  1.00 32.52 ? 147  GLN D OE1 1 
ATOM   8650  N  NE2 . GLN D  1 144 ? -46.071 -7.753  54.307  1.00 30.69 ? 147  GLN D NE2 1 
ATOM   8651  N  N   . LEU D  1 145 ? -48.572 -11.649 51.878  1.00 29.67 ? 148  LEU D N   1 
ATOM   8652  C  CA  . LEU D  1 145 ? -47.836 -12.536 50.969  1.00 28.92 ? 148  LEU D CA  1 
ATOM   8653  C  C   . LEU D  1 145 ? -48.768 -13.060 49.873  1.00 32.83 ? 148  LEU D C   1 
ATOM   8654  O  O   . LEU D  1 145 ? -48.451 -13.008 48.675  1.00 32.87 ? 148  LEU D O   1 
ATOM   8655  C  CB  . LEU D  1 145 ? -47.228 -13.696 51.750  1.00 26.75 ? 148  LEU D CB  1 
ATOM   8656  C  CG  . LEU D  1 145 ? -46.604 -14.909 51.040  1.00 30.58 ? 148  LEU D CG  1 
ATOM   8657  C  CD1 . LEU D  1 145 ? -45.620 -15.609 51.961  1.00 25.75 ? 148  LEU D CD1 1 
ATOM   8658  C  CD2 . LEU D  1 145 ? -47.657 -15.925 50.531  1.00 28.23 ? 148  LEU D CD2 1 
ATOM   8659  N  N   . VAL D  1 146 ? -49.955 -13.502 50.279  1.00 33.75 ? 149  VAL D N   1 
ATOM   8660  C  CA  . VAL D  1 146 ? -51.046 -13.690 49.327  1.00 31.44 ? 149  VAL D CA  1 
ATOM   8661  C  C   . VAL D  1 146 ? -51.260 -12.473 48.424  1.00 32.16 ? 149  VAL D C   1 
ATOM   8662  O  O   . VAL D  1 146 ? -51.345 -12.618 47.214  1.00 35.98 ? 149  VAL D O   1 
ATOM   8663  C  CB  . VAL D  1 146 ? -52.351 -14.107 50.030  1.00 31.37 ? 149  VAL D CB  1 
ATOM   8664  C  CG1 . VAL D  1 146 ? -53.491 -14.232 49.006  1.00 32.09 ? 149  VAL D CG1 1 
ATOM   8665  C  CG2 . VAL D  1 146 ? -52.146 -15.446 50.741  1.00 29.76 ? 149  VAL D CG2 1 
ATOM   8666  N  N   . ASP D  1 147 ? -51.285 -11.270 48.995  1.00 32.94 ? 150  ASP D N   1 
ATOM   8667  C  CA  . ASP D  1 147 ? -51.467 -10.058 48.204  1.00 33.51 ? 150  ASP D CA  1 
ATOM   8668  C  C   . ASP D  1 147 ? -50.330 -9.850  47.208  1.00 35.32 ? 150  ASP D C   1 
ATOM   8669  O  O   . ASP D  1 147 ? -50.557 -9.484  46.055  1.00 36.10 ? 150  ASP D O   1 
ATOM   8670  C  CB  . ASP D  1 147 ? -51.577 -8.827  49.104  1.00 36.14 ? 150  ASP D CB  1 
ATOM   8671  C  CG  . ASP D  1 147 ? -52.897 -8.762  49.858  1.00 40.07 ? 150  ASP D CG  1 
ATOM   8672  O  OD1 . ASP D  1 147 ? -53.714 -9.710  49.767  1.00 42.95 ? 150  ASP D OD1 1 
ATOM   8673  O  OD2 . ASP D  1 147 ? -53.120 -7.755  50.556  1.00 43.50 ? 150  ASP D OD2 1 
ATOM   8674  N  N   . TYR D  1 148 ? -49.103 -9.940  47.703  1.00 35.71 ? 151  TYR D N   1 
ATOM   8675  C  CA  . TYR D  1 148 ? -47.931 -9.838  46.854  1.00 32.97 ? 151  TYR D CA  1 
ATOM   8676  C  C   . TYR D  1 148 ? -47.933 -10.958 45.811  1.00 31.78 ? 151  TYR D C   1 
ATOM   8677  O  O   . TYR D  1 148 ? -47.632 -10.724 44.647  1.00 30.31 ? 151  TYR D O   1 
ATOM   8678  C  CB  . TYR D  1 148 ? -46.642 -9.819  47.696  1.00 31.96 ? 151  TYR D CB  1 
ATOM   8679  C  CG  . TYR D  1 148 ? -46.270 -8.416  48.095  1.00 30.61 ? 151  TYR D CG  1 
ATOM   8680  C  CD1 . TYR D  1 148 ? -47.089 -7.686  48.947  1.00 30.74 ? 151  TYR D CD1 1 
ATOM   8681  C  CD2 . TYR D  1 148 ? -45.198 -7.763  47.500  1.00 31.37 ? 151  TYR D CD2 1 
ATOM   8682  C  CE1 . TYR D  1 148 ? -46.846 -6.347  49.210  1.00 31.35 ? 151  TYR D CE1 1 
ATOM   8683  C  CE2 . TYR D  1 148 ? -44.950 -6.411  47.742  1.00 32.62 ? 151  TYR D CE2 1 
ATOM   8684  C  CZ  . TYR D  1 148 ? -45.788 -5.707  48.598  1.00 34.24 ? 151  TYR D CZ  1 
ATOM   8685  O  OH  . TYR D  1 148 ? -45.545 -4.376  48.882  1.00 33.76 ? 151  TYR D OH  1 
ATOM   8686  N  N   . SER D  1 149 ? -48.417 -12.129 46.200  1.00 31.70 ? 152  SER D N   1 
ATOM   8687  C  CA  . SER D  1 149 ? -48.559 -13.234 45.264  1.00 33.18 ? 152  SER D CA  1 
ATOM   8688  C  C   . SER D  1 149 ? -49.534 -12.915 44.124  1.00 35.90 ? 152  SER D C   1 
ATOM   8689  O  O   . SER D  1 149 ? -49.300 -13.290 42.973  1.00 37.29 ? 152  SER D O   1 
ATOM   8690  C  CB  . SER D  1 149 ? -49.013 -14.480 45.996  1.00 29.18 ? 152  SER D CB  1 
ATOM   8691  O  OG  . SER D  1 149 ? -47.929 -15.053 46.682  1.00 31.55 ? 152  SER D OG  1 
ATOM   8692  N  N   . ASN D  1 150 ? -50.616 -12.223 44.462  1.00 35.48 ? 153  ASN D N   1 
ATOM   8693  C  CA  . ASN D  1 150 ? -51.613 -11.802 43.488  1.00 39.23 ? 153  ASN D CA  1 
ATOM   8694  C  C   . ASN D  1 150 ? -51.069 -10.693 42.617  1.00 39.03 ? 153  ASN D C   1 
ATOM   8695  O  O   . ASN D  1 150 ? -51.309 -10.657 41.411  1.00 42.20 ? 153  ASN D O   1 
ATOM   8696  C  CB  . ASN D  1 150 ? -52.895 -11.320 44.195  1.00 37.41 ? 153  ASN D CB  1 
ATOM   8697  C  CG  . ASN D  1 150 ? -53.743 -12.466 44.700  1.00 35.74 ? 153  ASN D CG  1 
ATOM   8698  O  OD1 . ASN D  1 150 ? -53.730 -13.550 44.129  1.00 36.58 ? 153  ASN D OD1 1 
ATOM   8699  N  ND2 . ASN D  1 150 ? -54.475 -12.237 45.779  1.00 36.42 ? 153  ASN D ND2 1 
ATOM   8700  N  N   . ARG D  1 151 ? -50.369 -9.756  43.238  1.00 39.79 ? 154  ARG D N   1 
ATOM   8701  C  CA  . ARG D  1 151 ? -49.864 -8.608  42.505  1.00 39.07 ? 154  ARG D CA  1 
ATOM   8702  C  C   . ARG D  1 151 ? -48.774 -8.991  41.493  1.00 39.22 ? 154  ARG D C   1 
ATOM   8703  O  O   . ARG D  1 151 ? -48.678 -8.380  40.420  1.00 39.90 ? 154  ARG D O   1 
ATOM   8704  C  CB  . ARG D  1 151 ? -49.354 -7.542  43.472  1.00 41.37 ? 154  ARG D CB  1 
ATOM   8705  C  CG  . ARG D  1 151 ? -50.465 -6.801  44.223  1.00 42.91 ? 154  ARG D CG  1 
ATOM   8706  C  CD  . ARG D  1 151 ? -49.877 -5.800  45.210  1.00 42.72 ? 154  ARG D CD  1 
ATOM   8707  N  NE  . ARG D  1 151 ? -49.141 -4.734  44.535  1.00 43.02 ? 154  ARG D NE  1 
ATOM   8708  C  CZ  . ARG D  1 151 ? -48.342 -3.867  45.152  1.00 44.01 ? 154  ARG D CZ  1 
ATOM   8709  N  NH1 . ARG D  1 151 ? -48.161 -3.938  46.469  1.00 43.81 ? 154  ARG D NH1 1 
ATOM   8710  N  NH2 . ARG D  1 151 ? -47.732 -2.917  44.454  1.00 43.99 ? 154  ARG D NH2 1 
ATOM   8711  N  N   . PHE D  1 152 ? -47.966 -9.999  41.832  1.00 33.42 ? 155  PHE D N   1 
ATOM   8712  C  CA  . PHE D  1 152 ? -46.680 -10.183 41.173  1.00 31.64 ? 155  PHE D CA  1 
ATOM   8713  C  C   . PHE D  1 152 ? -46.464 -11.599 40.656  1.00 29.98 ? 155  PHE D C   1 
ATOM   8714  O  O   . PHE D  1 152 ? -45.603 -11.822 39.818  1.00 32.03 ? 155  PHE D O   1 
ATOM   8715  C  CB  . PHE D  1 152 ? -45.515 -9.771  42.083  1.00 31.60 ? 155  PHE D CB  1 
ATOM   8716  C  CG  . PHE D  1 152 ? -45.436 -8.296  42.343  1.00 31.98 ? 155  PHE D CG  1 
ATOM   8717  C  CD1 . PHE D  1 152 ? -45.018 -7.424  41.349  1.00 31.93 ? 155  PHE D CD1 1 
ATOM   8718  C  CD2 . PHE D  1 152 ? -45.727 -7.787  43.608  1.00 34.56 ? 155  PHE D CD2 1 
ATOM   8719  C  CE1 . PHE D  1 152 ? -44.917 -6.068  41.590  1.00 30.79 ? 155  PHE D CE1 1 
ATOM   8720  C  CE2 . PHE D  1 152 ? -45.653 -6.429  43.864  1.00 31.32 ? 155  PHE D CE2 1 
ATOM   8721  C  CZ  . PHE D  1 152 ? -45.268 -5.560  42.839  1.00 34.32 ? 155  PHE D CZ  1 
ATOM   8722  N  N   . GLY D  1 153 ? -47.270 -12.542 41.117  1.00 26.57 ? 156  GLY D N   1 
ATOM   8723  C  CA  . GLY D  1 153 ? -47.102 -13.935 40.722  1.00 27.76 ? 156  GLY D CA  1 
ATOM   8724  C  C   . GLY D  1 153 ? -48.392 -14.562 40.215  1.00 30.62 ? 156  GLY D C   1 
ATOM   8725  O  O   . GLY D  1 153 ? -48.582 -15.772 40.324  1.00 26.38 ? 156  GLY D O   1 
ATOM   8726  N  N   . GLY D  1 154 ? -49.267 -13.741 39.635  1.00 32.07 ? 157  GLY D N   1 
ATOM   8727  C  CA  . GLY D  1 154 ? -50.564 -14.225 39.138  1.00 34.54 ? 157  GLY D CA  1 
ATOM   8728  C  C   . GLY D  1 154 ? -51.346 -15.041 40.162  1.00 35.56 ? 157  GLY D C   1 
ATOM   8729  O  O   . GLY D  1 154 ? -52.127 -15.915 39.808  1.00 32.24 ? 157  GLY D O   1 
ATOM   8730  N  N   . GLY D  1 155 ? -51.167 -14.729 41.442  1.00 35.16 ? 158  GLY D N   1 
ATOM   8731  C  CA  . GLY D  1 155 ? -51.870 -15.449 42.489  1.00 34.07 ? 158  GLY D CA  1 
ATOM   8732  C  C   . GLY D  1 155 ? -51.030 -16.538 43.124  1.00 38.12 ? 158  GLY D C   1 
ATOM   8733  O  O   . GLY D  1 155 ? -51.431 -17.128 44.134  1.00 39.48 ? 158  GLY D O   1 
ATOM   8734  N  N   . LYS D  1 156 ? -49.897 -16.867 42.498  1.00 36.45 ? 159  LYS D N   1 
ATOM   8735  C  CA  . LYS D  1 156 ? -48.975 -17.841 43.080  1.00 36.53 ? 159  LYS D CA  1 
ATOM   8736  C  C   . LYS D  1 156 ? -47.775 -17.156 43.727  1.00 31.01 ? 159  LYS D C   1 
ATOM   8737  O  O   . LYS D  1 156 ? -47.554 -15.961 43.549  1.00 30.33 ? 159  LYS D O   1 
ATOM   8738  C  CB  . LYS D  1 156 ? -48.515 -18.852 42.032  1.00 41.89 ? 159  LYS D CB  1 
ATOM   8739  C  CG  . LYS D  1 156 ? -49.479 -20.003 41.823  1.00 45.00 ? 159  LYS D CG  1 
ATOM   8740  C  CD  . LYS D  1 156 ? -50.780 -19.503 41.243  1.00 46.85 ? 159  LYS D CD  1 
ATOM   8741  C  CE  . LYS D  1 156 ? -51.533 -20.625 40.552  1.00 47.97 ? 159  LYS D CE  1 
ATOM   8742  N  NZ  . LYS D  1 156 ? -51.957 -21.648 41.543  1.00 48.89 ? 159  LYS D NZ  1 
ATOM   8743  N  N   . TYR D  1 157 ? -47.028 -17.898 44.525  1.00 30.16 ? 160  TYR D N   1 
ATOM   8744  C  CA  . TYR D  1 157 ? -45.790 -17.357 45.059  1.00 31.99 ? 160  TYR D CA  1 
ATOM   8745  C  C   . TYR D  1 157 ? -44.644 -17.861 44.211  1.00 29.99 ? 160  TYR D C   1 
ATOM   8746  O  O   . TYR D  1 157 ? -44.442 -19.064 44.093  1.00 30.09 ? 160  TYR D O   1 
ATOM   8747  C  CB  . TYR D  1 157 ? -45.590 -17.760 46.528  1.00 32.01 ? 160  TYR D CB  1 
ATOM   8748  C  CG  . TYR D  1 157 ? -44.322 -17.198 47.160  1.00 34.38 ? 160  TYR D CG  1 
ATOM   8749  C  CD1 . TYR D  1 157 ? -43.119 -17.910 47.112  1.00 32.85 ? 160  TYR D CD1 1 
ATOM   8750  C  CD2 . TYR D  1 157 ? -44.351 -16.005 47.885  1.00 31.98 ? 160  TYR D CD2 1 
ATOM   8751  C  CE1 . TYR D  1 157 ? -41.975 -17.435 47.742  1.00 32.20 ? 160  TYR D CE1 1 
ATOM   8752  C  CE2 . TYR D  1 157 ? -43.215 -15.516 48.505  1.00 33.26 ? 160  TYR D CE2 1 
ATOM   8753  C  CZ  . TYR D  1 157 ? -42.029 -16.241 48.434  1.00 33.49 ? 160  TYR D CZ  1 
ATOM   8754  O  OH  . TYR D  1 157 ? -40.898 -15.732 49.010  1.00 29.87 ? 160  TYR D OH  1 
ATOM   8755  N  N   . ASN D  1 158 ? -43.906 -16.943 43.601  1.00 30.86 ? 161  ASN D N   1 
ATOM   8756  C  CA  . ASN D  1 158 ? -42.709 -17.337 42.873  1.00 31.02 ? 161  ASN D CA  1 
ATOM   8757  C  C   . ASN D  1 158 ? -41.559 -16.357 43.081  1.00 30.76 ? 161  ASN D C   1 
ATOM   8758  O  O   . ASN D  1 158 ? -41.687 -15.387 43.837  1.00 29.58 ? 161  ASN D O   1 
ATOM   8759  C  CB  . ASN D  1 158 ? -43.031 -17.516 41.376  1.00 31.22 ? 161  ASN D CB  1 
ATOM   8760  C  CG  . ASN D  1 158 ? -43.403 -16.213 40.694  1.00 30.63 ? 161  ASN D CG  1 
ATOM   8761  O  OD1 . ASN D  1 158 ? -43.147 -15.126 41.217  1.00 28.50 ? 161  ASN D OD1 1 
ATOM   8762  N  ND2 . ASN D  1 158 ? -44.013 -16.320 39.501  1.00 34.12 ? 161  ASN D ND2 1 
ATOM   8763  N  N   . LEU D  1 159 ? -40.447 -16.592 42.387  1.00 28.35 ? 162  LEU D N   1 
ATOM   8764  C  CA  . LEU D  1 159 ? -39.238 -15.835 42.646  1.00 28.30 ? 162  LEU D CA  1 
ATOM   8765  C  C   . LEU D  1 159 ? -39.404 -14.333 42.446  1.00 28.60 ? 162  LEU D C   1 
ATOM   8766  O  O   . LEU D  1 159 ? -38.794 -13.549 43.163  1.00 29.35 ? 162  LEU D O   1 
ATOM   8767  C  CB  . LEU D  1 159 ? -38.067 -16.378 41.827  1.00 28.16 ? 162  LEU D CB  1 
ATOM   8768  C  CG  . LEU D  1 159 ? -37.426 -17.677 42.324  1.00 26.71 ? 162  LEU D CG  1 
ATOM   8769  C  CD1 . LEU D  1 159 ? -36.099 -17.895 41.604  1.00 29.48 ? 162  LEU D CD1 1 
ATOM   8770  C  CD2 . LEU D  1 159 ? -37.220 -17.634 43.833  1.00 27.59 ? 162  LEU D CD2 1 
ATOM   8771  N  N   . THR D  1 160 ? -40.255 -13.924 41.506  1.00 27.24 ? 163  THR D N   1 
ATOM   8772  C  CA  . THR D  1 160 ? -40.587 -12.507 41.358  1.00 26.40 ? 163  THR D CA  1 
ATOM   8773  C  C   . THR D  1 160 ? -41.337 -11.960 42.577  1.00 26.74 ? 163  THR D C   1 
ATOM   8774  O  O   . THR D  1 160 ? -41.115 -10.824 42.987  1.00 26.71 ? 163  THR D O   1 
ATOM   8775  C  CB  . THR D  1 160 ? -41.448 -12.252 40.117  1.00 25.81 ? 163  THR D CB  1 
ATOM   8776  O  OG1 . THR D  1 160 ? -40.891 -12.952 38.999  1.00 27.77 ? 163  THR D OG1 1 
ATOM   8777  C  CG2 . THR D  1 160 ? -41.530 -10.756 39.807  1.00 25.42 ? 163  THR D CG2 1 
ATOM   8778  N  N   . VAL D  1 161 ? -42.241 -12.758 43.140  1.00 27.94 ? 164  VAL D N   1 
ATOM   8779  C  CA  . VAL D  1 161 ? -42.939 -12.374 44.377  1.00 30.67 ? 164  VAL D CA  1 
ATOM   8780  C  C   . VAL D  1 161 ? -41.935 -12.167 45.511  1.00 29.96 ? 164  VAL D C   1 
ATOM   8781  O  O   . VAL D  1 161 ? -41.909 -11.108 46.147  1.00 30.76 ? 164  VAL D O   1 
ATOM   8782  C  CB  . VAL D  1 161 ? -43.970 -13.443 44.811  1.00 30.52 ? 164  VAL D CB  1 
ATOM   8783  C  CG1 . VAL D  1 161 ? -44.780 -12.951 46.008  1.00 31.20 ? 164  VAL D CG1 1 
ATOM   8784  C  CG2 . VAL D  1 161 ? -44.897 -13.786 43.654  1.00 29.69 ? 164  VAL D CG2 1 
ATOM   8785  N  N   . ALA D  1 162 ? -41.061 -13.154 45.684  1.00 27.83 ? 165  ALA D N   1 
ATOM   8786  C  CA  . ALA D  1 162 ? -39.985 -13.120 46.664  1.00 27.54 ? 165  ALA D CA  1 
ATOM   8787  C  C   . ALA D  1 162 ? -39.218 -11.801 46.651  1.00 29.26 ? 165  ALA D C   1 
ATOM   8788  O  O   . ALA D  1 162 ? -39.044 -11.153 47.685  1.00 30.64 ? 165  ALA D O   1 
ATOM   8789  C  CB  . ALA D  1 162 ? -39.043 -14.295 46.435  1.00 27.37 ? 165  ALA D CB  1 
ATOM   8790  N  N   . GLY D  1 163 ? -38.828 -11.358 45.466  1.00 27.25 ? 166  GLY D N   1 
ATOM   8791  C  CA  . GLY D  1 163 ? -38.039 -10.144 45.351  1.00 27.55 ? 166  GLY D CA  1 
ATOM   8792  C  C   . GLY D  1 163 ? -38.797 -8.932  45.857  1.00 28.70 ? 166  GLY D C   1 
ATOM   8793  O  O   . GLY D  1 163 ? -38.208 -8.015  46.455  1.00 28.19 ? 166  GLY D O   1 
ATOM   8794  N  N   . GLU D  1 164 ? -40.094 -8.900  45.576  1.00 25.49 ? 167  GLU D N   1 
ATOM   8795  C  CA  . GLU D  1 164 ? -40.916 -7.745  45.917  1.00 26.85 ? 167  GLU D CA  1 
ATOM   8796  C  C   . GLU D  1 164 ? -41.215 -7.739  47.408  1.00 27.50 ? 167  GLU D C   1 
ATOM   8797  O  O   . GLU D  1 164 ? -41.210 -6.685  48.050  1.00 26.73 ? 167  GLU D O   1 
ATOM   8798  C  CB  . GLU D  1 164 ? -42.227 -7.768  45.122  1.00 30.01 ? 167  GLU D CB  1 
ATOM   8799  C  CG  . GLU D  1 164 ? -42.037 -7.491  43.635  1.00 29.65 ? 167  GLU D CG  1 
ATOM   8800  C  CD  . GLU D  1 164 ? -41.223 -6.240  43.385  1.00 34.41 ? 167  GLU D CD  1 
ATOM   8801  O  OE1 . GLU D  1 164 ? -41.633 -5.154  43.858  1.00 40.18 ? 167  GLU D OE1 1 
ATOM   8802  O  OE2 . GLU D  1 164 ? -40.171 -6.329  42.713  1.00 36.36 ? 167  GLU D OE2 1 
ATOM   8803  N  N   . LEU D  1 165 ? -41.447 -8.932  47.952  1.00 24.09 ? 168  LEU D N   1 
ATOM   8804  C  CA  . LEU D  1 165 ? -41.966 -9.076  49.290  1.00 26.18 ? 168  LEU D CA  1 
ATOM   8805  C  C   . LEU D  1 165 ? -40.825 -8.929  50.301  1.00 28.29 ? 168  LEU D C   1 
ATOM   8806  O  O   . LEU D  1 165 ? -40.980 -8.317  51.349  1.00 29.08 ? 168  LEU D O   1 
ATOM   8807  C  CB  . LEU D  1 165 ? -42.642 -10.437 49.433  1.00 25.83 ? 168  LEU D CB  1 
ATOM   8808  C  CG  . LEU D  1 165 ? -43.181 -10.793 50.807  1.00 26.87 ? 168  LEU D CG  1 
ATOM   8809  C  CD1 . LEU D  1 165 ? -44.237 -9.752  51.242  1.00 27.80 ? 168  LEU D CD1 1 
ATOM   8810  C  CD2 . LEU D  1 165 ? -43.778 -12.203 50.785  1.00 24.15 ? 168  LEU D CD2 1 
ATOM   8811  N  N   . ARG D  1 166 ? -39.669 -9.483  49.963  1.00 30.59 ? 169  ARG D N   1 
ATOM   8812  C  CA  . ARG D  1 166 ? -38.471 -9.296  50.757  1.00 29.38 ? 169  ARG D CA  1 
ATOM   8813  C  C   . ARG D  1 166 ? -38.124 -7.810  50.874  1.00 29.27 ? 169  ARG D C   1 
ATOM   8814  O  O   . ARG D  1 166 ? -37.725 -7.339  51.934  1.00 29.09 ? 169  ARG D O   1 
ATOM   8815  C  CB  . ARG D  1 166 ? -37.309 -10.073 50.141  1.00 26.52 ? 169  ARG D CB  1 
ATOM   8816  C  CG  . ARG D  1 166 ? -35.939 -9.471  50.415  1.00 28.18 ? 169  ARG D CG  1 
ATOM   8817  C  CD  . ARG D  1 166 ? -35.545 -9.565  51.890  1.00 26.23 ? 169  ARG D CD  1 
ATOM   8818  N  NE  . ARG D  1 166 ? -35.853 -10.867 52.478  1.00 29.05 ? 169  ARG D NE  1 
ATOM   8819  C  CZ  . ARG D  1 166 ? -36.639 -11.016 53.537  1.00 31.44 ? 169  ARG D CZ  1 
ATOM   8820  N  NH1 . ARG D  1 166 ? -37.210 -9.946  54.079  1.00 32.87 ? 169  ARG D NH1 1 
ATOM   8821  N  NH2 . ARG D  1 166 ? -36.871 -12.220 54.042  1.00 32.27 ? 169  ARG D NH2 1 
ATOM   8822  N  N   . PHE D  1 167 ? -38.278 -7.064  49.793  1.00 28.67 ? 170  PHE D N   1 
ATOM   8823  C  CA  . PHE D  1 167 ? -38.071 -5.624  49.901  1.00 30.71 ? 170  PHE D CA  1 
ATOM   8824  C  C   . PHE D  1 167 ? -39.168 -4.988  50.757  1.00 32.63 ? 170  PHE D C   1 
ATOM   8825  O  O   . PHE D  1 167 ? -38.906 -4.098  51.575  1.00 29.31 ? 170  PHE D O   1 
ATOM   8826  C  CB  . PHE D  1 167 ? -38.011 -4.963  48.536  1.00 25.88 ? 170  PHE D CB  1 
ATOM   8827  C  CG  . PHE D  1 167 ? -37.661 -3.510  48.590  1.00 27.78 ? 170  PHE D CG  1 
ATOM   8828  C  CD1 . PHE D  1 167 ? -36.443 -3.096  49.113  1.00 29.68 ? 170  PHE D CD1 1 
ATOM   8829  C  CD2 . PHE D  1 167 ? -38.544 -2.553  48.132  1.00 27.68 ? 170  PHE D CD2 1 
ATOM   8830  C  CE1 . PHE D  1 167 ? -36.101 -1.744  49.148  1.00 29.03 ? 170  PHE D CE1 1 
ATOM   8831  C  CE2 . PHE D  1 167 ? -38.202 -1.202  48.154  1.00 30.67 ? 170  PHE D CE2 1 
ATOM   8832  C  CZ  . PHE D  1 167 ? -36.988 -0.798  48.673  1.00 27.56 ? 170  PHE D CZ  1 
ATOM   8833  N  N   . LYS D  1 168 ? -40.401 -5.442  50.559  1.00 33.79 ? 171  LYS D N   1 
ATOM   8834  C  CA  . LYS D  1 168 ? -41.508 -4.892  51.313  1.00 34.32 ? 171  LYS D CA  1 
ATOM   8835  C  C   . LYS D  1 168 ? -41.268 -5.062  52.815  1.00 33.36 ? 171  LYS D C   1 
ATOM   8836  O  O   . LYS D  1 168 ? -41.407 -4.116  53.589  1.00 33.92 ? 171  LYS D O   1 
ATOM   8837  C  CB  . LYS D  1 168 ? -42.822 -5.555  50.904  1.00 35.32 ? 171  LYS D CB  1 
ATOM   8838  C  CG  . LYS D  1 168 ? -43.998 -5.173  51.802  1.00 36.37 ? 171  LYS D CG  1 
ATOM   8839  C  CD  . LYS D  1 168 ? -44.416 -3.711  51.631  1.00 35.38 ? 171  LYS D CD  1 
ATOM   8840  C  CE  . LYS D  1 168 ? -45.812 -3.541  52.210  1.00 38.72 ? 171  LYS D CE  1 
ATOM   8841  N  NZ  . LYS D  1 168 ? -46.157 -2.131  52.475  1.00 43.33 ? 171  LYS D NZ  1 
ATOM   8842  N  N   . ARG D  1 169 ? -40.855 -6.257  53.218  1.00 31.81 ? 172  ARG D N   1 
ATOM   8843  C  CA  . ARG D  1 169 ? -40.619 -6.521  54.622  1.00 33.90 ? 172  ARG D CA  1 
ATOM   8844  C  C   . ARG D  1 169 ? -39.512 -5.644  55.188  1.00 35.56 ? 172  ARG D C   1 
ATOM   8845  O  O   . ARG D  1 169 ? -39.668 -5.049  56.254  1.00 40.66 ? 172  ARG D O   1 
ATOM   8846  C  CB  . ARG D  1 169 ? -40.350 -7.997  54.862  1.00 34.37 ? 172  ARG D CB  1 
ATOM   8847  C  CG  . ARG D  1 169 ? -41.545 -8.865  54.473  1.00 32.57 ? 172  ARG D CG  1 
ATOM   8848  C  CD  . ARG D  1 169 ? -42.782 -8.502  55.285  1.00 31.80 ? 172  ARG D CD  1 
ATOM   8849  N  NE  . ARG D  1 169 ? -42.596 -8.898  56.675  1.00 30.53 ? 172  ARG D NE  1 
ATOM   8850  C  CZ  . ARG D  1 169 ? -42.638 -8.060  57.704  1.00 28.94 ? 172  ARG D CZ  1 
ATOM   8851  N  NH1 . ARG D  1 169 ? -43.020 -6.796  57.535  1.00 26.97 ? 172  ARG D NH1 1 
ATOM   8852  N  NH2 . ARG D  1 169 ? -42.294 -8.495  58.902  1.00 28.27 ? 172  ARG D NH2 1 
ATOM   8853  N  N   . ILE D  1 170 ? -38.452 -5.449  54.419  1.00 31.94 ? 173  ILE D N   1 
ATOM   8854  C  CA  . ILE D  1 170 ? -37.397 -4.562  54.853  1.00 30.04 ? 173  ILE D CA  1 
ATOM   8855  C  C   . ILE D  1 170 ? -37.942 -3.160  55.119  1.00 31.45 ? 173  ILE D C   1 
ATOM   8856  O  O   . ILE D  1 170 ? -37.726 -2.607  56.204  1.00 29.51 ? 173  ILE D O   1 
ATOM   8857  C  CB  . ILE D  1 170 ? -36.226 -4.531  53.861  1.00 25.93 ? 173  ILE D CB  1 
ATOM   8858  C  CG1 . ILE D  1 170 ? -35.499 -5.876  53.878  1.00 27.23 ? 173  ILE D CG1 1 
ATOM   8859  C  CG2 . ILE D  1 170 ? -35.255 -3.425  54.209  1.00 24.01 ? 173  ILE D CG2 1 
ATOM   8860  C  CD1 . ILE D  1 170 ? -34.864 -6.269  52.513  1.00 24.37 ? 173  ILE D CD1 1 
ATOM   8861  N  N   . GLN D  1 171 ? -38.678 -2.607  54.151  1.00 31.57 ? 174  GLN D N   1 
ATOM   8862  C  CA  . GLN D  1 171 ? -39.320 -1.295  54.302  1.00 32.80 ? 174  GLN D CA  1 
ATOM   8863  C  C   . GLN D  1 171 ? -40.281 -1.216  55.497  1.00 32.19 ? 174  GLN D C   1 
ATOM   8864  O  O   . GLN D  1 171 ? -40.402 -0.170  56.117  1.00 29.22 ? 174  GLN D O   1 
ATOM   8865  C  CB  . GLN D  1 171 ? -40.074 -0.918  53.031  1.00 34.38 ? 174  GLN D CB  1 
ATOM   8866  C  CG  . GLN D  1 171 ? -39.175 -0.583  51.857  1.00 38.23 ? 174  GLN D CG  1 
ATOM   8867  C  CD  . GLN D  1 171 ? -39.979 -0.062  50.681  1.00 43.02 ? 174  GLN D CD  1 
ATOM   8868  O  OE1 . GLN D  1 171 ? -41.053 -0.593  50.364  1.00 42.88 ? 174  GLN D OE1 1 
ATOM   8869  N  NE2 . GLN D  1 171 ? -39.509 1.034   50.078  1.00 43.74 ? 174  GLN D NE2 1 
ATOM   8870  N  N   . ASP D  1 172 ? -40.997 -2.304  55.772  1.00 34.02 ? 175  ASP D N   1 
ATOM   8871  C  CA  . ASP D  1 172 ? -41.926 -2.349  56.895  1.00 36.31 ? 175  ASP D CA  1 
ATOM   8872  C  C   . ASP D  1 172 ? -41.153 -2.144  58.203  1.00 37.90 ? 175  ASP D C   1 
ATOM   8873  O  O   . ASP D  1 172 ? -41.502 -1.288  59.022  1.00 38.15 ? 175  ASP D O   1 
ATOM   8874  C  CB  . ASP D  1 172 ? -42.671 -3.694  56.934  1.00 35.65 ? 175  ASP D CB  1 
ATOM   8875  C  CG  . ASP D  1 172 ? -43.845 -3.750  55.958  1.00 36.94 ? 175  ASP D CG  1 
ATOM   8876  O  OD1 . ASP D  1 172 ? -44.088 -2.726  55.276  1.00 36.20 ? 175  ASP D OD1 1 
ATOM   8877  O  OD2 . ASP D  1 172 ? -44.535 -4.807  55.898  1.00 34.49 ? 175  ASP D OD2 1 
ATOM   8878  N  N   . SER D  1 173 ? -40.094 -2.928  58.386  1.00 37.01 ? 176  SER D N   1 
ATOM   8879  C  CA  . SER D  1 173 ? -39.314 -2.886  59.621  1.00 35.88 ? 176  SER D CA  1 
ATOM   8880  C  C   . SER D  1 173 ? -38.561 -1.553  59.791  1.00 35.37 ? 176  SER D C   1 
ATOM   8881  O  O   . SER D  1 173 ? -38.426 -1.037  60.909  1.00 34.78 ? 176  SER D O   1 
ATOM   8882  C  CB  . SER D  1 173 ? -38.354 -4.082  59.682  1.00 33.93 ? 176  SER D CB  1 
ATOM   8883  O  OG  . SER D  1 173 ? -39.072 -5.313  59.761  1.00 33.85 ? 176  SER D OG  1 
ATOM   8884  N  N   . ILE D  1 174 ? -38.093 -0.980  58.684  1.00 34.45 ? 177  ILE D N   1 
ATOM   8885  C  CA  . ILE D  1 174 ? -37.413 0.312   58.748  1.00 33.93 ? 177  ILE D CA  1 
ATOM   8886  C  C   . ILE D  1 174 ? -38.370 1.373   59.287  1.00 36.90 ? 177  ILE D C   1 
ATOM   8887  O  O   . ILE D  1 174 ? -37.972 2.255   60.052  1.00 38.39 ? 177  ILE D O   1 
ATOM   8888  C  CB  . ILE D  1 174 ? -36.858 0.740   57.367  1.00 33.36 ? 177  ILE D CB  1 
ATOM   8889  C  CG1 . ILE D  1 174 ? -35.608 -0.070  57.010  1.00 29.14 ? 177  ILE D CG1 1 
ATOM   8890  C  CG2 . ILE D  1 174 ? -36.552 2.256   57.311  1.00 31.03 ? 177  ILE D CG2 1 
ATOM   8891  C  CD1 . ILE D  1 174 ? -35.237 0.035   55.549  1.00 30.27 ? 177  ILE D CD1 1 
ATOM   8892  N  N   . ALA D  1 175 ? -39.639 1.275   58.903  1.00 37.66 ? 178  ALA D N   1 
ATOM   8893  C  CA  . ALA D  1 175 ? -40.586 2.355   59.150  1.00 39.09 ? 178  ALA D CA  1 
ATOM   8894  C  C   . ALA D  1 175 ? -41.169 2.266   60.560  1.00 40.17 ? 178  ALA D C   1 
ATOM   8895  O  O   . ALA D  1 175 ? -41.537 3.281   61.144  1.00 40.85 ? 178  ALA D O   1 
ATOM   8896  C  CB  . ALA D  1 175 ? -41.702 2.336   58.119  1.00 39.68 ? 178  ALA D CB  1 
ATOM   8897  N  N   . THR D  1 176 ? -41.237 1.057   61.109  1.00 38.97 ? 179  THR D N   1 
ATOM   8898  C  CA  . THR D  1 176 ? -41.955 0.834   62.355  1.00 40.44 ? 179  THR D CA  1 
ATOM   8899  C  C   . THR D  1 176 ? -41.085 0.335   63.502  1.00 40.74 ? 179  THR D C   1 
ATOM   8900  O  O   . THR D  1 176 ? -41.459 0.476   64.660  1.00 43.40 ? 179  THR D O   1 
ATOM   8901  C  CB  . THR D  1 176 ? -43.080 -0.172  62.175  1.00 41.88 ? 179  THR D CB  1 
ATOM   8902  O  OG1 . THR D  1 176 ? -42.512 -1.470  61.958  1.00 43.12 ? 179  THR D OG1 1 
ATOM   8903  C  CG2 . THR D  1 176 ? -43.965 0.227   60.990  1.00 41.25 ? 179  THR D CG2 1 
ATOM   8904  N  N   . ASN D  1 177 ? -39.985 -0.343  63.190  1.00 38.19 ? 180  ASN D N   1 
ATOM   8905  C  CA  . ASN D  1 177 ? -39.179 -0.944  64.237  1.00 34.23 ? 180  ASN D CA  1 
ATOM   8906  C  C   . ASN D  1 177 ? -37.836 -0.266  64.473  1.00 35.50 ? 180  ASN D C   1 
ATOM   8907  O  O   . ASN D  1 177 ? -36.949 -0.308  63.616  1.00 38.68 ? 180  ASN D O   1 
ATOM   8908  C  CB  . ASN D  1 177 ? -38.993 -2.440  64.040  1.00 31.37 ? 180  ASN D CB  1 
ATOM   8909  C  CG  . ASN D  1 177 ? -37.963 -3.003  64.984  1.00 32.63 ? 180  ASN D CG  1 
ATOM   8910  O  OD1 . ASN D  1 177 ? -37.428 -2.267  65.830  1.00 35.32 ? 180  ASN D OD1 1 
ATOM   8911  N  ND2 . ASN D  1 177 ? -37.704 -4.302  64.893  1.00 29.13 ? 180  ASN D ND2 1 
ATOM   8912  N  N   . PRO D  1 178 ? -37.685 0.367   65.647  1.00 35.32 ? 181  PRO D N   1 
ATOM   8913  C  CA  . PRO D  1 178 ? -36.552 1.244   65.921  1.00 33.95 ? 181  PRO D CA  1 
ATOM   8914  C  C   . PRO D  1 178 ? -35.318 0.455   66.359  1.00 32.74 ? 181  PRO D C   1 
ATOM   8915  O  O   . PRO D  1 178 ? -34.219 1.006   66.404  1.00 30.61 ? 181  PRO D O   1 
ATOM   8916  C  CB  . PRO D  1 178 ? -37.061 2.123   67.068  1.00 36.09 ? 181  PRO D CB  1 
ATOM   8917  C  CG  . PRO D  1 178 ? -38.051 1.255   67.796  1.00 35.64 ? 181  PRO D CG  1 
ATOM   8918  C  CD  . PRO D  1 178 ? -38.692 0.385   66.728  1.00 36.49 ? 181  PRO D CD  1 
ATOM   8919  N  N   . ASN D  1 179 ? -35.498 -0.841  66.611  1.00 33.73 ? 182  ASN D N   1 
ATOM   8920  C  CA  . ASN D  1 179 ? -34.371 -1.761  66.796  1.00 35.92 ? 182  ASN D CA  1 
ATOM   8921  C  C   . ASN D  1 179 ? -34.037 -2.609  65.557  1.00 34.51 ? 182  ASN D C   1 
ATOM   8922  O  O   . ASN D  1 179 ? -33.278 -3.576  65.659  1.00 33.79 ? 182  ASN D O   1 
ATOM   8923  C  CB  . ASN D  1 179 ? -34.627 -2.690  67.987  1.00 39.81 ? 182  ASN D CB  1 
ATOM   8924  C  CG  . ASN D  1 179 ? -34.495 -1.980  69.340  1.00 44.58 ? 182  ASN D CG  1 
ATOM   8925  O  OD1 . ASN D  1 179 ? -34.568 -0.752  69.430  1.00 43.29 ? 182  ASN D OD1 1 
ATOM   8926  N  ND2 . ASN D  1 179 ? -34.338 -2.764  70.400  1.00 49.53 ? 182  ASN D ND2 1 
ATOM   8927  N  N   . PHE D  1 180 ? -34.646 -2.287  64.413  1.00 32.90 ? 183  PHE D N   1 
ATOM   8928  C  CA  . PHE D  1 180 ? -34.461 -3.078  63.183  1.00 30.59 ? 183  PHE D CA  1 
ATOM   8929  C  C   . PHE D  1 180 ? -32.996 -3.285  62.903  1.00 26.44 ? 183  PHE D C   1 
ATOM   8930  O  O   . PHE D  1 180 ? -32.253 -2.332  62.722  1.00 30.45 ? 183  PHE D O   1 
ATOM   8931  C  CB  . PHE D  1 180 ? -35.112 -2.416  61.958  1.00 26.30 ? 183  PHE D CB  1 
ATOM   8932  C  CG  . PHE D  1 180 ? -34.918 -3.191  60.663  1.00 27.92 ? 183  PHE D CG  1 
ATOM   8933  C  CD1 . PHE D  1 180 ? -35.069 -4.564  60.623  1.00 29.15 ? 183  PHE D CD1 1 
ATOM   8934  C  CD2 . PHE D  1 180 ? -34.580 -2.543  59.488  1.00 28.84 ? 183  PHE D CD2 1 
ATOM   8935  C  CE1 . PHE D  1 180 ? -34.930 -5.267  59.419  1.00 28.20 ? 183  PHE D CE1 1 
ATOM   8936  C  CE2 . PHE D  1 180 ? -34.455 -3.239  58.282  1.00 30.16 ? 183  PHE D CE2 1 
ATOM   8937  C  CZ  . PHE D  1 180 ? -34.590 -4.610  58.262  1.00 26.86 ? 183  PHE D CZ  1 
ATOM   8938  N  N   . SER D  1 181 ? -32.600 -4.540  62.814  1.00 27.35 ? 184  SER D N   1 
ATOM   8939  C  CA  . SER D  1 181 ? -31.223 -4.882  62.478  1.00 29.70 ? 184  SER D CA  1 
ATOM   8940  C  C   . SER D  1 181 ? -31.194 -5.792  61.254  1.00 26.98 ? 184  SER D C   1 
ATOM   8941  O  O   . SER D  1 181 ? -31.971 -6.727  61.165  1.00 25.85 ? 184  SER D O   1 
ATOM   8942  C  CB  . SER D  1 181 ? -30.561 -5.590  63.659  1.00 28.41 ? 184  SER D CB  1 
ATOM   8943  O  OG  . SER D  1 181 ? -29.293 -6.061  63.281  1.00 28.67 ? 184  SER D OG  1 
ATOM   8944  N  N   . PHE D  1 182 ? -30.326 -5.496  60.291  1.00 27.87 ? 185  PHE D N   1 
ATOM   8945  C  CA  . PHE D  1 182 ? -30.317 -6.258  59.037  1.00 25.87 ? 185  PHE D CA  1 
ATOM   8946  C  C   . PHE D  1 182 ? -28.890 -6.345  58.500  1.00 24.66 ? 185  PHE D C   1 
ATOM   8947  O  O   . PHE D  1 182 ? -28.576 -5.786  57.461  1.00 23.21 ? 185  PHE D O   1 
ATOM   8948  C  CB  . PHE D  1 182 ? -31.259 -5.608  58.013  1.00 26.05 ? 185  PHE D CB  1 
ATOM   8949  C  CG  . PHE D  1 182 ? -31.790 -6.565  56.962  1.00 26.71 ? 185  PHE D CG  1 
ATOM   8950  C  CD1 . PHE D  1 182 ? -32.564 -7.668  57.327  1.00 25.39 ? 185  PHE D CD1 1 
ATOM   8951  C  CD2 . PHE D  1 182 ? -31.610 -6.297  55.604  1.00 22.45 ? 185  PHE D CD2 1 
ATOM   8952  C  CE1 . PHE D  1 182 ? -33.087 -8.527  56.352  1.00 24.84 ? 185  PHE D CE1 1 
ATOM   8953  C  CE2 . PHE D  1 182 ? -32.121 -7.142  54.630  1.00 24.35 ? 185  PHE D CE2 1 
ATOM   8954  C  CZ  . PHE D  1 182 ? -32.837 -8.274  54.994  1.00 24.86 ? 185  PHE D CZ  1 
ATOM   8955  N  N   . VAL D  1 183 ? -28.006 -6.992  59.259  1.00 25.76 ? 186  VAL D N   1 
ATOM   8956  C  CA  . VAL D  1 183 ? -26.595 -7.012  58.915  1.00 22.61 ? 186  VAL D CA  1 
ATOM   8957  C  C   . VAL D  1 183 ? -26.083 -8.438  58.925  1.00 22.49 ? 186  VAL D C   1 
ATOM   8958  O  O   . VAL D  1 183 ? -26.769 -9.338  59.414  1.00 22.07 ? 186  VAL D O   1 
ATOM   8959  C  CB  . VAL D  1 183 ? -25.753 -6.102  59.856  1.00 25.49 ? 186  VAL D CB  1 
ATOM   8960  C  CG1 . VAL D  1 183 ? -26.127 -4.634  59.643  1.00 24.52 ? 186  VAL D CG1 1 
ATOM   8961  C  CG2 . VAL D  1 183 ? -25.947 -6.485  61.336  1.00 24.53 ? 186  VAL D CG2 1 
ATOM   8962  N  N   . ASP D  1 184 ? -24.913 -8.663  58.328  1.00 22.04 ? 187  ASP D N   1 
ATOM   8963  C  CA  . ASP D  1 184 ? -24.139 -9.862  58.643  1.00 23.26 ? 187  ASP D CA  1 
ATOM   8964  C  C   . ASP D  1 184 ? -24.939 -11.131 58.355  1.00 24.32 ? 187  ASP D C   1 
ATOM   8965  O  O   . ASP D  1 184 ? -25.520 -11.268 57.287  1.00 24.56 ? 187  ASP D O   1 
ATOM   8966  C  CB  . ASP D  1 184 ? -23.673 -9.824  60.111  1.00 25.03 ? 187  ASP D CB  1 
ATOM   8967  C  CG  . ASP D  1 184 ? -22.536 -8.830  60.337  1.00 27.64 ? 187  ASP D CG  1 
ATOM   8968  O  OD1 . ASP D  1 184 ? -21.532 -8.869  59.578  1.00 30.38 ? 187  ASP D OD1 1 
ATOM   8969  O  OD2 . ASP D  1 184 ? -22.660 -7.989  61.246  1.00 29.23 ? 187  ASP D OD2 1 
ATOM   8970  N  N   . PHE D  1 185 ? -24.991 -12.054 59.311  1.00 26.79 ? 188  PHE D N   1 
ATOM   8971  C  CA  . PHE D  1 185 ? -25.626 -13.351 59.058  1.00 27.16 ? 188  PHE D CA  1 
ATOM   8972  C  C   . PHE D  1 185 ? -27.103 -13.249 58.674  1.00 24.29 ? 188  PHE D C   1 
ATOM   8973  O  O   . PHE D  1 185 ? -27.606 -14.043 57.884  1.00 25.90 ? 188  PHE D O   1 
ATOM   8974  C  CB  . PHE D  1 185 ? -25.450 -14.274 60.265  1.00 28.22 ? 188  PHE D CB  1 
ATOM   8975  C  CG  . PHE D  1 185 ? -25.926 -15.680 60.035  1.00 28.98 ? 188  PHE D CG  1 
ATOM   8976  C  CD1 . PHE D  1 185 ? -25.145 -16.585 59.325  1.00 29.39 ? 188  PHE D CD1 1 
ATOM   8977  C  CD2 . PHE D  1 185 ? -27.081 -16.134 60.638  1.00 26.88 ? 188  PHE D CD2 1 
ATOM   8978  C  CE1 . PHE D  1 185 ? -25.553 -17.894 59.159  1.00 27.66 ? 188  PHE D CE1 1 
ATOM   8979  C  CE2 . PHE D  1 185 ? -27.500 -17.450 60.472  1.00 28.64 ? 188  PHE D CE2 1 
ATOM   8980  C  CZ  . PHE D  1 185 ? -26.738 -18.325 59.722  1.00 26.81 ? 188  PHE D CZ  1 
ATOM   8981  N  N   . ARG D  1 186 ? -27.802 -12.269 59.222  1.00 24.44 ? 189  ARG D N   1 
ATOM   8982  C  CA  . ARG D  1 186 ? -29.233 -12.146 58.958  1.00 24.77 ? 189  ARG D CA  1 
ATOM   8983  C  C   . ARG D  1 186 ? -29.514 -11.515 57.610  1.00 24.42 ? 189  ARG D C   1 
ATOM   8984  O  O   . ARG D  1 186 ? -30.538 -11.800 56.975  1.00 24.60 ? 189  ARG D O   1 
ATOM   8985  C  CB  . ARG D  1 186 ? -29.943 -11.346 60.051  1.00 21.71 ? 189  ARG D CB  1 
ATOM   8986  C  CG  . ARG D  1 186 ? -31.438 -11.130 59.776  1.00 24.26 ? 189  ARG D CG  1 
ATOM   8987  C  CD  . ARG D  1 186 ? -32.237 -12.456 59.697  1.00 24.79 ? 189  ARG D CD  1 
ATOM   8988  N  NE  . ARG D  1 186 ? -33.613 -12.205 59.253  1.00 23.77 ? 189  ARG D NE  1 
ATOM   8989  C  CZ  . ARG D  1 186 ? -34.375 -13.075 58.597  1.00 23.22 ? 189  ARG D CZ  1 
ATOM   8990  N  NH1 . ARG D  1 186 ? -33.940 -14.308 58.343  1.00 22.25 ? 189  ARG D NH1 1 
ATOM   8991  N  NH2 . ARG D  1 186 ? -35.592 -12.710 58.211  1.00 21.45 ? 189  ARG D NH2 1 
ATOM   8992  N  N   . PHE D  1 187 ? -28.671 -10.560 57.237  1.00 26.98 ? 190  PHE D N   1 
ATOM   8993  C  CA  . PHE D  1 187 ? -28.729 -9.992  55.901  1.00 25.48 ? 190  PHE D CA  1 
ATOM   8994  C  C   . PHE D  1 187 ? -28.687 -11.126 54.885  1.00 26.96 ? 190  PHE D C   1 
ATOM   8995  O  O   . PHE D  1 187 ? -29.498 -11.176 53.967  1.00 28.32 ? 190  PHE D O   1 
ATOM   8996  C  CB  . PHE D  1 187 ? -27.552 -9.072  55.686  1.00 23.28 ? 190  PHE D CB  1 
ATOM   8997  C  CG  . PHE D  1 187 ? -27.532 -8.435  54.334  1.00 24.23 ? 190  PHE D CG  1 
ATOM   8998  C  CD1 . PHE D  1 187 ? -28.344 -7.333  54.056  1.00 23.00 ? 190  PHE D CD1 1 
ATOM   8999  C  CD2 . PHE D  1 187 ? -26.706 -8.931  53.338  1.00 22.06 ? 190  PHE D CD2 1 
ATOM   9000  C  CE1 . PHE D  1 187 ? -28.312 -6.737  52.813  1.00 25.05 ? 190  PHE D CE1 1 
ATOM   9001  C  CE2 . PHE D  1 187 ? -26.650 -8.320  52.083  1.00 23.23 ? 190  PHE D CE2 1 
ATOM   9002  C  CZ  . PHE D  1 187 ? -27.453 -7.218  51.828  1.00 24.60 ? 190  PHE D CZ  1 
ATOM   9003  N  N   . PHE D  1 188 ? -27.808 -12.089 55.135  1.00 26.16 ? 191  PHE D N   1 
ATOM   9004  C  CA  . PHE D  1 188 ? -27.616 -13.225 54.243  1.00 30.97 ? 191  PHE D CA  1 
ATOM   9005  C  C   . PHE D  1 188 ? -28.820 -14.180 54.208  1.00 30.24 ? 191  PHE D C   1 
ATOM   9006  O  O   . PHE D  1 188 ? -29.365 -14.450 53.143  1.00 30.68 ? 191  PHE D O   1 
ATOM   9007  C  CB  . PHE D  1 188 ? -26.362 -13.992 54.658  1.00 31.13 ? 191  PHE D CB  1 
ATOM   9008  C  CG  . PHE D  1 188 ? -26.150 -15.262 53.898  1.00 34.31 ? 191  PHE D CG  1 
ATOM   9009  C  CD1 . PHE D  1 188 ? -25.532 -15.245 52.653  1.00 33.56 ? 191  PHE D CD1 1 
ATOM   9010  C  CD2 . PHE D  1 188 ? -26.487 -16.490 54.463  1.00 35.49 ? 191  PHE D CD2 1 
ATOM   9011  C  CE1 . PHE D  1 188 ? -25.289 -16.419 51.968  1.00 31.77 ? 191  PHE D CE1 1 
ATOM   9012  C  CE2 . PHE D  1 188 ? -26.237 -17.671 53.783  1.00 34.75 ? 191  PHE D CE2 1 
ATOM   9013  C  CZ  . PHE D  1 188 ? -25.639 -17.633 52.529  1.00 33.50 ? 191  PHE D CZ  1 
ATOM   9014  N  N   . THR D  1 189 ? -29.222 -14.691 55.371  1.00 27.58 ? 192  THR D N   1 
ATOM   9015  C  CA  . THR D  1 189 ? -30.235 -15.753 55.429  1.00 28.94 ? 192  THR D CA  1 
ATOM   9016  C  C   . THR D  1 189 ? -31.599 -15.257 54.985  1.00 27.83 ? 192  THR D C   1 
ATOM   9017  O  O   . THR D  1 189 ? -32.387 -16.017 54.445  1.00 31.59 ? 192  THR D O   1 
ATOM   9018  C  CB  . THR D  1 189 ? -30.374 -16.384 56.860  1.00 28.27 ? 192  THR D CB  1 
ATOM   9019  O  OG1 . THR D  1 189 ? -30.710 -15.374 57.818  1.00 27.95 ? 192  THR D OG1 1 
ATOM   9020  C  CG2 . THR D  1 189 ? -29.083 -17.068 57.280  1.00 28.54 ? 192  THR D CG2 1 
ATOM   9021  N  N   . ALA D  1 190 ? -31.884 -13.985 55.240  1.00 26.88 ? 193  ALA D N   1 
ATOM   9022  C  CA  . ALA D  1 190 ? -33.173 -13.399 54.891  1.00 27.88 ? 193  ALA D CA  1 
ATOM   9023  C  C   . ALA D  1 190 ? -33.476 -13.410 53.397  1.00 27.01 ? 193  ALA D C   1 
ATOM   9024  O  O   . ALA D  1 190 ? -34.632 -13.289 53.003  1.00 31.23 ? 193  ALA D O   1 
ATOM   9025  C  CB  . ALA D  1 190 ? -33.270 -11.973 55.434  1.00 30.16 ? 193  ALA D CB  1 
ATOM   9026  N  N   . TYR D  1 191 ? -32.441 -13.383 52.566  1.00 25.48 ? 194  TYR D N   1 
ATOM   9027  C  CA  . TYR D  1 191 ? -32.649 -13.455 51.127  1.00 22.55 ? 194  TYR D CA  1 
ATOM   9028  C  C   . TYR D  1 191 ? -32.912 -14.873 50.635  1.00 23.07 ? 194  TYR D C   1 
ATOM   9029  O  O   . TYR D  1 191 ? -33.938 -15.130 50.008  1.00 25.07 ? 194  TYR D O   1 
ATOM   9030  C  CB  . TYR D  1 191 ? -31.522 -12.783 50.356  1.00 22.89 ? 194  TYR D CB  1 
ATOM   9031  C  CG  . TYR D  1 191 ? -31.686 -11.291 50.282  1.00 22.60 ? 194  TYR D CG  1 
ATOM   9032  C  CD1 . TYR D  1 191 ? -31.211 -10.477 51.312  1.00 21.96 ? 194  TYR D CD1 1 
ATOM   9033  C  CD2 . TYR D  1 191 ? -32.395 -10.698 49.241  1.00 21.89 ? 194  TYR D CD2 1 
ATOM   9034  C  CE1 . TYR D  1 191 ? -31.415 -9.118  51.312  1.00 21.71 ? 194  TYR D CE1 1 
ATOM   9035  C  CE2 . TYR D  1 191 ? -32.604 -9.305  49.217  1.00 23.33 ? 194  TYR D CE2 1 
ATOM   9036  C  CZ  . TYR D  1 191 ? -32.094 -8.524  50.256  1.00 25.70 ? 194  TYR D CZ  1 
ATOM   9037  O  OH  . TYR D  1 191 ? -32.286 -7.156  50.276  1.00 20.28 ? 194  TYR D OH  1 
ATOM   9038  N  N   . GLY D  1 192 ? -32.016 -15.806 50.953  1.00 21.59 ? 195  GLY D N   1 
ATOM   9039  C  CA  . GLY D  1 192 ? -32.207 -17.202 50.583  1.00 19.65 ? 195  GLY D CA  1 
ATOM   9040  C  C   . GLY D  1 192 ? -33.557 -17.772 51.010  1.00 24.49 ? 195  GLY D C   1 
ATOM   9041  O  O   . GLY D  1 192 ? -34.191 -18.532 50.272  1.00 25.79 ? 195  GLY D O   1 
ATOM   9042  N  N   . GLU D  1 193 ? -33.964 -17.475 52.236  1.00 24.01 ? 196  GLU D N   1 
ATOM   9043  C  CA  . GLU D  1 193 ? -35.220 -18.000 52.770  1.00 26.74 ? 196  GLU D CA  1 
ATOM   9044  C  C   . GLU D  1 193 ? -36.436 -17.694 51.889  1.00 25.67 ? 196  GLU D C   1 
ATOM   9045  O  O   . GLU D  1 193 ? -37.366 -18.488 51.822  1.00 23.68 ? 196  GLU D O   1 
ATOM   9046  C  CB  . GLU D  1 193 ? -35.450 -17.512 54.214  1.00 26.68 ? 196  GLU D CB  1 
ATOM   9047  C  CG  . GLU D  1 193 ? -34.510 -18.192 55.209  1.00 29.18 ? 196  GLU D CG  1 
ATOM   9048  C  CD  . GLU D  1 193 ? -34.402 -17.485 56.552  1.00 30.22 ? 196  GLU D CD  1 
ATOM   9049  O  OE1 . GLU D  1 193 ? -35.070 -16.447 56.768  1.00 31.30 ? 196  GLU D OE1 1 
ATOM   9050  O  OE2 . GLU D  1 193 ? -33.662 -18.005 57.410  1.00 30.83 ? 196  GLU D OE2 1 
ATOM   9051  N  N   . THR D  1 194 ? -36.435 -16.544 51.225  1.00 24.62 ? 197  THR D N   1 
ATOM   9052  C  CA  . THR D  1 194 ? -37.588 -16.174 50.417  1.00 27.23 ? 197  THR D CA  1 
ATOM   9053  C  C   . THR D  1 194 ? -37.678 -17.015 49.153  1.00 26.05 ? 197  THR D C   1 
ATOM   9054  O  O   . THR D  1 194 ? -38.716 -17.050 48.496  1.00 27.12 ? 197  THR D O   1 
ATOM   9055  C  CB  . THR D  1 194 ? -37.588 -14.689 50.049  1.00 27.14 ? 197  THR D CB  1 
ATOM   9056  O  OG1 . THR D  1 194 ? -36.443 -14.397 49.238  1.00 30.36 ? 197  THR D OG1 1 
ATOM   9057  C  CG2 . THR D  1 194 ? -37.534 -13.841 51.299  1.00 28.51 ? 197  THR D CG2 1 
ATOM   9058  N  N   . THR D  1 195 ? -36.603 -17.709 48.809  1.00 23.89 ? 198  THR D N   1 
ATOM   9059  C  CA  . THR D  1 195 ? -36.673 -18.556 47.652  1.00 23.98 ? 198  THR D CA  1 
ATOM   9060  C  C   . THR D  1 195 ? -37.149 -19.952 48.031  1.00 26.12 ? 198  THR D C   1 
ATOM   9061  O  O   . THR D  1 195 ? -37.617 -20.697 47.159  1.00 24.84 ? 198  THR D O   1 
ATOM   9062  C  CB  . THR D  1 195 ? -35.333 -18.662 46.893  1.00 25.58 ? 198  THR D CB  1 
ATOM   9063  O  OG1 . THR D  1 195 ? -34.444 -19.547 47.587  1.00 25.20 ? 198  THR D OG1 1 
ATOM   9064  C  CG2 . THR D  1 195 ? -34.695 -17.300 46.679  1.00 25.55 ? 198  THR D CG2 1 
ATOM   9065  N  N   . PHE D  1 196 ? -36.984 -20.323 49.305  1.00 23.23 ? 199  PHE D N   1 
ATOM   9066  C  CA  . PHE D  1 196 ? -37.241 -21.706 49.728  1.00 25.87 ? 199  PHE D CA  1 
ATOM   9067  C  C   . PHE D  1 196 ? -38.673 -22.170 49.398  1.00 25.12 ? 199  PHE D C   1 
ATOM   9068  O  O   . PHE D  1 196 ? -38.865 -23.284 48.926  1.00 27.82 ? 199  PHE D O   1 
ATOM   9069  C  CB  . PHE D  1 196 ? -36.923 -21.946 51.216  1.00 24.91 ? 199  PHE D CB  1 
ATOM   9070  C  CG  . PHE D  1 196 ? -35.452 -21.824 51.577  1.00 23.46 ? 199  PHE D CG  1 
ATOM   9071  C  CD1 . PHE D  1 196 ? -34.466 -21.793 50.600  1.00 23.20 ? 199  PHE D CD1 1 
ATOM   9072  C  CD2 . PHE D  1 196 ? -35.063 -21.740 52.911  1.00 24.66 ? 199  PHE D CD2 1 
ATOM   9073  C  CE1 . PHE D  1 196 ? -33.112 -21.689 50.949  1.00 22.13 ? 199  PHE D CE1 1 
ATOM   9074  C  CE2 . PHE D  1 196 ? -33.709 -21.599 53.268  1.00 24.40 ? 199  PHE D CE2 1 
ATOM   9075  C  CZ  . PHE D  1 196 ? -32.734 -21.590 52.278  1.00 23.01 ? 199  PHE D CZ  1 
ATOM   9076  N  N   . PRO D  1 197 ? -39.676 -21.310 49.618  1.00 25.29 ? 200  PRO D N   1 
ATOM   9077  C  CA  . PRO D  1 197 ? -41.051 -21.721 49.276  1.00 28.28 ? 200  PRO D CA  1 
ATOM   9078  C  C   . PRO D  1 197 ? -41.203 -22.038 47.774  1.00 29.45 ? 200  PRO D C   1 
ATOM   9079  O  O   . PRO D  1 197 ? -41.765 -23.063 47.407  1.00 28.84 ? 200  PRO D O   1 
ATOM   9080  C  CB  . PRO D  1 197 ? -41.898 -20.484 49.641  1.00 26.22 ? 200  PRO D CB  1 
ATOM   9081  C  CG  . PRO D  1 197 ? -41.005 -19.644 50.547  1.00 23.18 ? 200  PRO D CG  1 
ATOM   9082  C  CD  . PRO D  1 197 ? -39.611 -19.918 50.099  1.00 22.58 ? 200  PRO D CD  1 
ATOM   9083  N  N   . ALA D  1 198 ? -40.694 -21.165 46.917  1.00 29.17 ? 201  ALA D N   1 
ATOM   9084  C  CA  . ALA D  1 198 ? -40.756 -21.404 45.471  1.00 29.05 ? 201  ALA D CA  1 
ATOM   9085  C  C   . ALA D  1 198 ? -39.971 -22.639 45.017  1.00 28.87 ? 201  ALA D C   1 
ATOM   9086  O  O   . ALA D  1 198 ? -40.333 -23.272 44.031  1.00 29.67 ? 201  ALA D O   1 
ATOM   9087  C  CB  . ALA D  1 198 ? -40.300 -20.169 44.715  1.00 26.92 ? 201  ALA D CB  1 
ATOM   9088  N  N   . ASN D  1 199 ? -38.917 -22.990 45.759  1.00 29.76 ? 202  ASN D N   1 
ATOM   9089  C  CA  . ASN D  1 199 ? -37.979 -24.039 45.345  1.00 28.33 ? 202  ASN D CA  1 
ATOM   9090  C  C   . ASN D  1 199 ? -38.293 -25.386 45.977  1.00 29.58 ? 202  ASN D C   1 
ATOM   9091  O  O   . ASN D  1 199 ? -37.908 -26.435 45.429  1.00 32.59 ? 202  ASN D O   1 
ATOM   9092  C  CB  . ASN D  1 199 ? -36.528 -23.655 45.700  1.00 28.76 ? 202  ASN D CB  1 
ATOM   9093  C  CG  . ASN D  1 199 ? -35.971 -22.561 44.808  1.00 29.38 ? 202  ASN D CG  1 
ATOM   9094  O  OD1 . ASN D  1 199 ? -36.581 -22.194 43.799  1.00 30.02 ? 202  ASN D OD1 1 
ATOM   9095  N  ND2 . ASN D  1 199 ? -34.815 -22.018 45.185  1.00 28.07 ? 202  ASN D ND2 1 
ATOM   9096  N  N   . LEU D  1 200 ? -38.945 -25.358 47.144  1.00 26.23 ? 203  LEU D N   1 
ATOM   9097  C  CA  . LEU D  1 200 ? -39.051 -26.535 48.012  1.00 25.81 ? 203  LEU D CA  1 
ATOM   9098  C  C   . LEU D  1 200 ? -40.484 -26.888 48.524  1.00 28.59 ? 203  LEU D C   1 
ATOM   9099  O  O   . LEU D  1 200 ? -40.774 -28.042 48.894  1.00 24.29 ? 203  LEU D O   1 
ATOM   9100  C  CB  . LEU D  1 200 ? -38.092 -26.368 49.187  1.00 28.42 ? 203  LEU D CB  1 
ATOM   9101  C  CG  . LEU D  1 200 ? -36.594 -26.514 48.863  1.00 25.33 ? 203  LEU D CG  1 
ATOM   9102  C  CD1 . LEU D  1 200 ? -35.789 -25.813 49.901  1.00 27.99 ? 203  LEU D CD1 1 
ATOM   9103  C  CD2 . LEU D  1 200 ? -36.202 -27.967 48.827  1.00 23.88 ? 203  LEU D CD2 1 
ATOM   9104  N  N   . PHE D  1 201 ? -41.392 -25.918 48.504  1.00 27.18 ? 204  PHE D N   1 
ATOM   9105  C  CA  . PHE D  1 201 ? -42.758 -26.185 48.952  1.00 29.34 ? 204  PHE D CA  1 
ATOM   9106  C  C   . PHE D  1 201 ? -43.655 -26.544 47.775  1.00 30.92 ? 204  PHE D C   1 
ATOM   9107  O  O   . PHE D  1 201 ? -44.761 -27.053 47.962  1.00 33.01 ? 204  PHE D O   1 
ATOM   9108  C  CB  . PHE D  1 201 ? -43.341 -24.990 49.723  1.00 26.61 ? 204  PHE D CB  1 
ATOM   9109  C  CG  . PHE D  1 201 ? -42.833 -24.866 51.130  1.00 22.77 ? 204  PHE D CG  1 
ATOM   9110  C  CD1 . PHE D  1 201 ? -42.102 -25.883 51.706  1.00 24.32 ? 204  PHE D CD1 1 
ATOM   9111  C  CD2 . PHE D  1 201 ? -43.084 -23.723 51.873  1.00 23.51 ? 204  PHE D CD2 1 
ATOM   9112  C  CE1 . PHE D  1 201 ? -41.625 -25.768 53.019  1.00 27.24 ? 204  PHE D CE1 1 
ATOM   9113  C  CE2 . PHE D  1 201 ? -42.610 -23.599 53.178  1.00 23.23 ? 204  PHE D CE2 1 
ATOM   9114  C  CZ  . PHE D  1 201 ? -41.872 -24.614 53.745  1.00 23.36 ? 204  PHE D CZ  1 
ATOM   9115  N  N   . VAL D  1 202 ? -43.151 -26.322 46.562  1.00 29.10 ? 205  VAL D N   1 
ATOM   9116  C  CA  . VAL D  1 202 ? -43.836 -26.745 45.341  1.00 26.22 ? 205  VAL D CA  1 
ATOM   9117  C  C   . VAL D  1 202 ? -43.682 -28.262 45.162  1.00 28.77 ? 205  VAL D C   1 
ATOM   9118  O  O   . VAL D  1 202 ? -42.609 -28.803 45.385  1.00 27.54 ? 205  VAL D O   1 
ATOM   9119  C  CB  . VAL D  1 202 ? -43.255 -26.008 44.138  1.00 26.56 ? 205  VAL D CB  1 
ATOM   9120  C  CG1 . VAL D  1 202 ? -43.854 -26.499 42.846  1.00 26.34 ? 205  VAL D CG1 1 
ATOM   9121  C  CG2 . VAL D  1 202 ? -43.437 -24.502 44.319  1.00 26.88 ? 205  VAL D CG2 1 
ATOM   9122  N  N   . ASP D  1 203 ? -44.795 -28.953 44.923  1.00 28.06 ? 206  ASP D N   1 
ATOM   9123  C  CA  . ASP D  1 203 ? -44.794 -30.392 44.657  1.00 27.45 ? 206  ASP D CA  1 
ATOM   9124  C  C   . ASP D  1 203 ? -43.812 -30.800 43.548  1.00 27.77 ? 206  ASP D C   1 
ATOM   9125  O  O   . ASP D  1 203 ? -43.847 -30.267 42.424  1.00 25.49 ? 206  ASP D O   1 
ATOM   9126  C  CB  . ASP D  1 203 ? -46.227 -30.855 44.296  1.00 29.08 ? 206  ASP D CB  1 
ATOM   9127  C  CG  . ASP D  1 203 ? -46.372 -32.368 44.296  1.00 30.25 ? 206  ASP D CG  1 
ATOM   9128  O  OD1 . ASP D  1 203 ? -46.605 -32.966 45.382  1.00 26.78 ? 206  ASP D OD1 1 
ATOM   9129  O  OD2 . ASP D  1 203 ? -46.193 -32.961 43.209  1.00 32.93 ? 206  ASP D OD2 1 
ATOM   9130  N  N   . GLY D  1 204 ? -42.996 -31.809 43.847  1.00 28.37 ? 207  GLY D N   1 
ATOM   9131  C  CA  . GLY D  1 204 ? -41.889 -32.207 42.990  1.00 29.94 ? 207  GLY D CA  1 
ATOM   9132  C  C   . GLY D  1 204 ? -42.247 -32.859 41.666  1.00 35.98 ? 207  GLY D C   1 
ATOM   9133  O  O   . GLY D  1 204 ? -41.413 -32.905 40.762  1.00 39.80 ? 207  GLY D O   1 
ATOM   9134  N  N   . ARG D  1 205 ? -43.479 -33.353 41.527  1.00 36.79 ? 208  ARG D N   1 
ATOM   9135  C  CA  . ARG D  1 205 ? -43.969 -33.798 40.219  1.00 37.17 ? 208  ARG D CA  1 
ATOM   9136  C  C   . ARG D  1 205 ? -44.169 -32.625 39.252  1.00 37.83 ? 208  ARG D C   1 
ATOM   9137  O  O   . ARG D  1 205 ? -44.250 -32.810 38.038  1.00 40.84 ? 208  ARG D O   1 
ATOM   9138  C  CB  . ARG D  1 205 ? -45.265 -34.616 40.352  1.00 36.45 ? 208  ARG D CB  1 
ATOM   9139  C  CG  . ARG D  1 205 ? -45.071 -36.040 40.874  1.00 36.01 ? 208  ARG D CG  1 
ATOM   9140  C  CD  . ARG D  1 205 ? -46.376 -36.613 41.445  1.00 38.50 ? 208  ARG D CD  1 
ATOM   9141  N  NE  . ARG D  1 205 ? -46.971 -35.719 42.440  1.00 38.77 ? 208  ARG D NE  1 
ATOM   9142  C  CZ  . ARG D  1 205 ? -47.958 -36.058 43.268  1.00 40.56 ? 208  ARG D CZ  1 
ATOM   9143  N  NH1 . ARG D  1 205 ? -48.542 -37.250 43.172  1.00 36.15 ? 208  ARG D NH1 1 
ATOM   9144  N  NH2 . ARG D  1 205 ? -48.398 -35.181 44.169  1.00 40.67 ? 208  ARG D NH2 1 
ATOM   9145  N  N   . ARG D  1 206 ? -44.168 -31.411 39.783  1.00 37.45 ? 209  ARG D N   1 
ATOM   9146  C  CA  . ARG D  1 206 ? -44.367 -30.226 38.953  1.00 35.63 ? 209  ARG D CA  1 
ATOM   9147  C  C   . ARG D  1 206 ? -43.111 -29.327 38.931  1.00 34.31 ? 209  ARG D C   1 
ATOM   9148  O  O   . ARG D  1 206 ? -42.603 -28.982 37.864  1.00 32.37 ? 209  ARG D O   1 
ATOM   9149  C  CB  . ARG D  1 206 ? -45.605 -29.467 39.436  1.00 36.40 ? 209  ARG D CB  1 
ATOM   9150  C  CG  . ARG D  1 206 ? -46.086 -28.374 38.500  1.00 38.92 ? 209  ARG D CG  1 
ATOM   9151  C  CD  . ARG D  1 206 ? -47.466 -27.874 38.939  1.00 40.95 ? 209  ARG D CD  1 
ATOM   9152  N  NE  . ARG D  1 206 ? -47.772 -28.221 40.333  1.00 39.41 ? 209  ARG D NE  1 
ATOM   9153  C  CZ  . ARG D  1 206 ? -47.780 -27.349 41.341  1.00 39.75 ? 209  ARG D CZ  1 
ATOM   9154  N  NH1 . ARG D  1 206 ? -47.417 -26.079 41.142  1.00 36.29 ? 209  ARG D NH1 1 
ATOM   9155  N  NH2 . ARG D  1 206 ? -48.120 -27.756 42.562  1.00 40.11 ? 209  ARG D NH2 1 
ATOM   9156  N  N   . ASP D  1 207 ? -42.528 -29.090 40.106  1.00 33.24 ? 210  ASP D N   1 
ATOM   9157  C  CA  . ASP D  1 207 ? -41.320 -28.292 40.228  1.00 29.84 ? 210  ASP D CA  1 
ATOM   9158  C  C   . ASP D  1 207 ? -41.278 -27.118 39.248  1.00 31.23 ? 210  ASP D C   1 
ATOM   9159  O  O   . ASP D  1 207 ? -40.261 -26.920 38.581  1.00 28.47 ? 210  ASP D O   1 
ATOM   9160  C  CB  . ASP D  1 207 ? -40.071 -29.168 40.047  1.00 33.24 ? 210  ASP D CB  1 
ATOM   9161  C  CG  . ASP D  1 207 ? -38.779 -28.457 40.476  1.00 36.57 ? 210  ASP D CG  1 
ATOM   9162  O  OD1 . ASP D  1 207 ? -38.850 -27.410 41.173  1.00 34.65 ? 210  ASP D OD1 1 
ATOM   9163  O  OD2 . ASP D  1 207 ? -37.685 -28.968 40.142  1.00 38.82 ? 210  ASP D OD2 1 
ATOM   9164  N  N   . ASP D  1 208 ? -42.346 -26.314 39.207  1.00 29.54 ? 211  ASP D N   1 
ATOM   9165  C  CA  . ASP D  1 208 ? -42.436 -25.168 38.287  1.00 28.47 ? 211  ASP D CA  1 
ATOM   9166  C  C   . ASP D  1 208 ? -42.203 -23.842 38.977  1.00 26.04 ? 211  ASP D C   1 
ATOM   9167  O  O   . ASP D  1 208 ? -42.448 -22.786 38.385  1.00 24.43 ? 211  ASP D O   1 
ATOM   9168  C  CB  . ASP D  1 208 ? -43.813 -25.108 37.619  1.00 30.34 ? 211  ASP D CB  1 
ATOM   9169  C  CG  . ASP D  1 208 ? -44.951 -25.136 38.633  1.00 33.70 ? 211  ASP D CG  1 
ATOM   9170  O  OD1 . ASP D  1 208 ? -44.715 -24.807 39.817  1.00 31.06 ? 211  ASP D OD1 1 
ATOM   9171  O  OD2 . ASP D  1 208 ? -46.074 -25.536 38.260  1.00 37.07 ? 211  ASP D OD2 1 
ATOM   9172  N  N   . GLY D  1 209 ? -41.897 -23.899 40.274  1.00 26.13 ? 212  GLY D N   1 
ATOM   9173  C  CA  . GLY D  1 209 ? -41.579 -22.704 41.054  1.00 26.15 ? 212  GLY D CA  1 
ATOM   9174  C  C   . GLY D  1 209 ? -42.749 -21.756 41.280  1.00 27.22 ? 212  GLY D C   1 
ATOM   9175  O  O   . GLY D  1 209 ? -42.546 -20.565 41.573  1.00 23.55 ? 212  GLY D O   1 
ATOM   9176  N  N   . GLN D  1 210 ? -43.973 -22.268 41.132  1.00 25.89 ? 213  GLN D N   1 
ATOM   9177  C  CA  . GLN D  1 210 ? -45.161 -21.476 41.444  1.00 28.98 ? 213  GLN D CA  1 
ATOM   9178  C  C   . GLN D  1 210 ? -45.949 -22.102 42.598  1.00 30.35 ? 213  GLN D C   1 
ATOM   9179  O  O   . GLN D  1 210 ? -46.448 -23.227 42.491  1.00 29.32 ? 213  GLN D O   1 
ATOM   9180  C  CB  . GLN D  1 210 ? -46.049 -21.283 40.212  1.00 30.78 ? 213  GLN D CB  1 
ATOM   9181  C  CG  . GLN D  1 210 ? -45.290 -21.109 38.890  1.00 28.20 ? 213  GLN D CG  1 
ATOM   9182  C  CD  . GLN D  1 210 ? -44.593 -19.775 38.784  1.00 29.08 ? 213  GLN D CD  1 
ATOM   9183  O  OE1 . GLN D  1 210 ? -45.196 -18.722 38.988  1.00 25.94 ? 213  GLN D OE1 1 
ATOM   9184  N  NE2 . GLN D  1 210 ? -43.325 -19.807 38.381  1.00 31.93 ? 213  GLN D NE2 1 
ATOM   9185  N  N   . LEU D  1 211 ? -45.969 -21.421 43.738  1.00 28.93 ? 214  LEU D N   1 
ATOM   9186  C  CA  . LEU D  1 211 ? -46.549 -22.024 44.931  1.00 31.94 ? 214  LEU D CA  1 
ATOM   9187  C  C   . LEU D  1 211 ? -47.963 -21.496 45.136  1.00 32.62 ? 214  LEU D C   1 
ATOM   9188  O  O   . LEU D  1 211 ? -48.167 -20.280 45.194  1.00 34.85 ? 214  LEU D O   1 
ATOM   9189  C  CB  . LEU D  1 211 ? -45.697 -21.722 46.163  1.00 31.28 ? 214  LEU D CB  1 
ATOM   9190  C  CG  . LEU D  1 211 ? -46.192 -22.349 47.472  1.00 31.33 ? 214  LEU D CG  1 
ATOM   9191  C  CD1 . LEU D  1 211 ? -46.019 -23.880 47.451  1.00 28.46 ? 214  LEU D CD1 1 
ATOM   9192  C  CD2 . LEU D  1 211 ? -45.466 -21.720 48.650  1.00 28.65 ? 214  LEU D CD2 1 
ATOM   9193  N  N   . ASP D  1 212 ? -48.929 -22.404 45.249  1.00 32.02 ? 215  ASP D N   1 
ATOM   9194  C  CA  . ASP D  1 212 ? -50.321 -22.010 45.461  1.00 37.61 ? 215  ASP D CA  1 
ATOM   9195  C  C   . ASP D  1 212 ? -50.567 -21.578 46.920  1.00 37.92 ? 215  ASP D C   1 
ATOM   9196  O  O   . ASP D  1 212 ? -49.804 -21.920 47.827  1.00 38.39 ? 215  ASP D O   1 
ATOM   9197  C  CB  . ASP D  1 212 ? -51.285 -23.133 45.025  1.00 38.12 ? 215  ASP D CB  1 
ATOM   9198  C  CG  . ASP D  1 212 ? -51.293 -24.295 45.983  1.00 41.24 ? 215  ASP D CG  1 
ATOM   9199  O  OD1 . ASP D  1 212 ? -51.844 -24.138 47.089  1.00 44.86 ? 215  ASP D OD1 1 
ATOM   9200  O  OD2 . ASP D  1 212 ? -50.691 -25.345 45.674  1.00 43.48 ? 215  ASP D OD2 1 
ATOM   9201  N  N   . MET D  1 213 ? -51.600 -20.775 47.139  1.00 39.54 ? 216  MET D N   1 
ATOM   9202  C  CA  . MET D  1 213 ? -51.800 -20.165 48.451  1.00 38.83 ? 216  MET D CA  1 
ATOM   9203  C  C   . MET D  1 213 ? -52.372 -21.145 49.479  1.00 41.15 ? 216  MET D C   1 
ATOM   9204  O  O   . MET D  1 213 ? -52.302 -20.909 50.689  1.00 41.06 ? 216  MET D O   1 
ATOM   9205  C  CB  . MET D  1 213 ? -52.671 -18.926 48.332  1.00 34.72 ? 216  MET D CB  1 
ATOM   9206  C  CG  . MET D  1 213 ? -51.960 -17.759 47.671  1.00 35.06 ? 216  MET D CG  1 
ATOM   9207  S  SD  . MET D  1 213 ? -50.358 -17.373 48.445  1.00 38.02 ? 216  MET D SD  1 
ATOM   9208  C  CE  . MET D  1 213 ? -49.233 -18.079 47.213  1.00 34.41 ? 216  MET D CE  1 
ATOM   9209  N  N   . ASP D  1 214 ? -52.863 -22.282 49.008  1.00 41.28 ? 217  ASP D N   1 
ATOM   9210  C  CA  . ASP D  1 214 ? -53.345 -23.305 49.920  1.00 44.58 ? 217  ASP D CA  1 
ATOM   9211  C  C   . ASP D  1 214 ? -52.166 -24.011 50.575  1.00 43.87 ? 217  ASP D C   1 
ATOM   9212  O  O   . ASP D  1 214 ? -52.111 -24.136 51.801  1.00 44.79 ? 217  ASP D O   1 
ATOM   9213  C  CB  . ASP D  1 214 ? -54.232 -24.316 49.186  1.00 49.22 ? 217  ASP D CB  1 
ATOM   9214  C  CG  . ASP D  1 214 ? -55.508 -24.654 49.957  1.00 55.23 ? 217  ASP D CG  1 
ATOM   9215  O  OD1 . ASP D  1 214 ? -55.653 -24.218 51.126  1.00 56.17 ? 217  ASP D OD1 1 
ATOM   9216  O  OD2 . ASP D  1 214 ? -56.362 -25.385 49.397  1.00 58.61 ? 217  ASP D OD2 1 
ATOM   9217  N  N   . ALA D  1 215 ? -51.234 -24.482 49.749  1.00 40.74 ? 218  ALA D N   1 
ATOM   9218  C  CA  . ALA D  1 215 ? -50.060 -25.224 50.225  1.00 38.23 ? 218  ALA D CA  1 
ATOM   9219  C  C   . ALA D  1 215 ? -49.116 -24.321 51.038  1.00 35.22 ? 218  ALA D C   1 
ATOM   9220  O  O   . ALA D  1 215 ? -48.425 -24.781 51.947  1.00 34.31 ? 218  ALA D O   1 
ATOM   9221  C  CB  . ALA D  1 215 ? -49.312 -25.846 49.035  1.00 36.71 ? 218  ALA D CB  1 
ATOM   9222  N  N   . ALA D  1 216 ? -49.110 -23.036 50.698  1.00 31.39 ? 219  ALA D N   1 
ATOM   9223  C  CA  . ALA D  1 216 ? -48.337 -22.050 51.406  1.00 30.24 ? 219  ALA D CA  1 
ATOM   9224  C  C   . ALA D  1 216 ? -48.853 -21.885 52.841  1.00 32.15 ? 219  ALA D C   1 
ATOM   9225  O  O   . ALA D  1 216 ? -48.065 -21.899 53.792  1.00 28.67 ? 219  ALA D O   1 
ATOM   9226  C  CB  . ALA D  1 216 ? -48.379 -20.726 50.658  1.00 31.04 ? 219  ALA D CB  1 
ATOM   9227  N  N   . ARG D  1 217 ? -50.171 -21.735 52.995  1.00 32.14 ? 220  ARG D N   1 
ATOM   9228  C  CA  . ARG D  1 217 ? -50.793 -21.777 54.324  1.00 33.93 ? 220  ARG D CA  1 
ATOM   9229  C  C   . ARG D  1 217 ? -50.563 -23.106 55.046  1.00 34.69 ? 220  ARG D C   1 
ATOM   9230  O  O   . ARG D  1 217 ? -50.135 -23.146 56.201  1.00 32.94 ? 220  ARG D O   1 
ATOM   9231  C  CB  . ARG D  1 217 ? -52.289 -21.460 54.258  1.00 35.43 ? 220  ARG D CB  1 
ATOM   9232  C  CG  . ARG D  1 217 ? -52.929 -21.327 55.636  1.00 35.60 ? 220  ARG D CG  1 
ATOM   9233  C  CD  . ARG D  1 217 ? -54.409 -21.008 55.549  1.00 33.97 ? 220  ARG D CD  1 
ATOM   9234  N  NE  . ARG D  1 217 ? -54.666 -19.646 55.083  1.00 33.50 ? 220  ARG D NE  1 
ATOM   9235  C  CZ  . ARG D  1 217 ? -54.517 -18.555 55.825  1.00 34.65 ? 220  ARG D CZ  1 
ATOM   9236  N  NH1 . ARG D  1 217 ? -54.103 -18.645 57.086  1.00 37.08 ? 220  ARG D NH1 1 
ATOM   9237  N  NH2 . ARG D  1 217 ? -54.812 -17.370 55.317  1.00 35.70 ? 220  ARG D NH2 1 
ATOM   9238  N  N   . SER D  1 218 ? -50.816 -24.207 54.358  1.00 34.69 ? 221  SER D N   1 
ATOM   9239  C  CA  . SER D  1 218 ? -50.587 -25.510 54.972  1.00 35.95 ? 221  SER D CA  1 
ATOM   9240  C  C   . SER D  1 218 ? -49.214 -25.520 55.658  1.00 37.00 ? 221  SER D C   1 
ATOM   9241  O  O   . SER D  1 218 ? -49.072 -25.881 56.835  1.00 33.95 ? 221  SER D O   1 
ATOM   9242  C  CB  . SER D  1 218 ? -50.641 -26.596 53.901  1.00 36.21 ? 221  SER D CB  1 
ATOM   9243  O  OG  . SER D  1 218 ? -50.725 -27.868 54.500  1.00 40.61 ? 221  SER D OG  1 
ATOM   9244  N  N   . PHE D  1 219 ? -48.216 -25.059 54.910  1.00 37.22 ? 222  PHE D N   1 
ATOM   9245  C  CA  . PHE D  1 219 ? -46.834 -25.132 55.333  1.00 36.47 ? 222  PHE D CA  1 
ATOM   9246  C  C   . PHE D  1 219 ? -46.530 -24.117 56.416  1.00 35.18 ? 222  PHE D C   1 
ATOM   9247  O  O   . PHE D  1 219 ? -45.944 -24.460 57.434  1.00 36.34 ? 222  PHE D O   1 
ATOM   9248  C  CB  . PHE D  1 219 ? -45.906 -24.904 54.139  1.00 35.66 ? 222  PHE D CB  1 
ATOM   9249  C  CG  . PHE D  1 219 ? -45.524 -26.156 53.432  1.00 32.75 ? 222  PHE D CG  1 
ATOM   9250  C  CD1 . PHE D  1 219 ? -44.889 -27.177 54.114  1.00 31.01 ? 222  PHE D CD1 1 
ATOM   9251  C  CD2 . PHE D  1 219 ? -45.834 -26.330 52.092  1.00 32.99 ? 222  PHE D CD2 1 
ATOM   9252  C  CE1 . PHE D  1 219 ? -44.521 -28.337 53.466  1.00 30.52 ? 222  PHE D CE1 1 
ATOM   9253  C  CE2 . PHE D  1 219 ? -45.455 -27.474 51.432  1.00 31.55 ? 222  PHE D CE2 1 
ATOM   9254  C  CZ  . PHE D  1 219 ? -44.766 -28.464 52.111  1.00 33.03 ? 222  PHE D CZ  1 
ATOM   9255  N  N   . PHE D  1 220 ? -46.886 -22.861 56.166  1.00 35.40 ? 223  PHE D N   1 
ATOM   9256  C  CA  . PHE D  1 220 ? -46.432 -21.756 57.002  1.00 36.23 ? 223  PHE D CA  1 
ATOM   9257  C  C   . PHE D  1 220 ? -47.132 -21.785 58.368  1.00 39.07 ? 223  PHE D C   1 
ATOM   9258  O  O   . PHE D  1 220 ? -46.479 -21.708 59.417  1.00 37.53 ? 223  PHE D O   1 
ATOM   9259  C  CB  . PHE D  1 220 ? -46.673 -20.417 56.304  1.00 35.45 ? 223  PHE D CB  1 
ATOM   9260  C  CG  . PHE D  1 220 ? -45.565 -20.008 55.357  1.00 37.10 ? 223  PHE D CG  1 
ATOM   9261  C  CD1 . PHE D  1 220 ? -44.369 -19.493 55.842  1.00 36.65 ? 223  PHE D CD1 1 
ATOM   9262  C  CD2 . PHE D  1 220 ? -45.747 -20.070 53.987  1.00 35.85 ? 223  PHE D CD2 1 
ATOM   9263  C  CE1 . PHE D  1 220 ? -43.364 -19.100 54.975  1.00 36.78 ? 223  PHE D CE1 1 
ATOM   9264  C  CE2 . PHE D  1 220 ? -44.744 -19.684 53.113  1.00 36.75 ? 223  PHE D CE2 1 
ATOM   9265  C  CZ  . PHE D  1 220 ? -43.553 -19.197 53.603  1.00 37.28 ? 223  PHE D CZ  1 
ATOM   9266  N  N   . GLN D  1 221 ? -48.456 -21.940 58.341  1.00 39.39 ? 224  GLN D N   1 
ATOM   9267  C  CA  . GLN D  1 221 ? -49.284 -21.909 59.551  1.00 41.56 ? 224  GLN D CA  1 
ATOM   9268  C  C   . GLN D  1 221 ? -49.309 -23.242 60.292  1.00 40.47 ? 224  GLN D C   1 
ATOM   9269  O  O   . GLN D  1 221 ? -48.939 -23.322 61.456  1.00 42.37 ? 224  GLN D O   1 
ATOM   9270  C  CB  . GLN D  1 221 ? -50.710 -21.475 59.205  1.00 41.78 ? 224  GLN D CB  1 
ATOM   9271  C  CG  . GLN D  1 221 ? -51.711 -21.592 60.353  1.00 43.30 ? 224  GLN D CG  1 
ATOM   9272  C  CD  . GLN D  1 221 ? -52.983 -20.812 60.071  1.00 43.90 ? 224  GLN D CD  1 
ATOM   9273  O  OE1 . GLN D  1 221 ? -53.525 -20.880 58.968  1.00 43.89 ? 224  GLN D OE1 1 
ATOM   9274  N  NE2 . GLN D  1 221 ? -53.413 -19.997 61.034  1.00 43.24 ? 224  GLN D NE2 1 
ATOM   9275  N  N   . PHE D  1 222 ? -49.691 -24.298 59.594  1.00 41.61 ? 225  PHE D N   1 
ATOM   9276  C  CA  . PHE D  1 222 ? -50.070 -25.539 60.250  1.00 42.99 ? 225  PHE D CA  1 
ATOM   9277  C  C   . PHE D  1 222 ? -48.988 -26.605 60.215  1.00 42.18 ? 225  PHE D C   1 
ATOM   9278  O  O   . PHE D  1 222 ? -49.129 -27.659 60.844  1.00 39.29 ? 225  PHE D O   1 
ATOM   9279  C  CB  . PHE D  1 222 ? -51.364 -26.073 59.647  1.00 44.87 ? 225  PHE D CB  1 
ATOM   9280  C  CG  . PHE D  1 222 ? -52.577 -25.300 60.068  1.00 48.04 ? 225  PHE D CG  1 
ATOM   9281  C  CD1 . PHE D  1 222 ? -52.854 -25.111 61.420  1.00 49.32 ? 225  PHE D CD1 1 
ATOM   9282  C  CD2 . PHE D  1 222 ? -53.408 -24.710 59.123  1.00 49.09 ? 225  PHE D CD2 1 
ATOM   9283  C  CE1 . PHE D  1 222 ? -53.970 -24.375 61.831  1.00 51.69 ? 225  PHE D CE1 1 
ATOM   9284  C  CE2 . PHE D  1 222 ? -54.518 -23.957 59.521  1.00 52.22 ? 225  PHE D CE2 1 
ATOM   9285  C  CZ  . PHE D  1 222 ? -54.803 -23.798 60.885  1.00 50.54 ? 225  PHE D CZ  1 
ATOM   9286  N  N   . SER D  1 223 ? -47.899 -26.325 59.498  1.00 40.73 ? 226  SER D N   1 
ATOM   9287  C  CA  . SER D  1 223 ? -46.769 -27.250 59.449  1.00 36.79 ? 226  SER D CA  1 
ATOM   9288  C  C   . SER D  1 223 ? -47.165 -28.582 58.834  1.00 35.80 ? 226  SER D C   1 
ATOM   9289  O  O   . SER D  1 223 ? -46.686 -29.637 59.247  1.00 39.02 ? 226  SER D O   1 
ATOM   9290  C  CB  . SER D  1 223 ? -46.197 -27.460 60.849  1.00 36.13 ? 226  SER D CB  1 
ATOM   9291  O  OG  . SER D  1 223 ? -46.004 -26.209 61.480  1.00 36.60 ? 226  SER D OG  1 
ATOM   9292  N  N   . ARG D  1 224 ? -48.048 -28.528 57.843  1.00 35.74 ? 227  ARG D N   1 
ATOM   9293  C  CA  . ARG D  1 224 ? -48.614 -29.732 57.253  1.00 36.21 ? 227  ARG D CA  1 
ATOM   9294  C  C   . ARG D  1 224 ? -48.277 -29.737 55.756  1.00 35.67 ? 227  ARG D C   1 
ATOM   9295  O  O   . ARG D  1 224 ? -48.453 -28.730 55.075  1.00 33.76 ? 227  ARG D O   1 
ATOM   9296  C  CB  . ARG D  1 224 ? -50.139 -29.745 57.470  1.00 37.50 ? 227  ARG D CB  1 
ATOM   9297  C  CG  . ARG D  1 224 ? -50.787 -31.128 57.398  1.00 42.49 ? 227  ARG D CG  1 
ATOM   9298  C  CD  . ARG D  1 224 ? -52.316 -31.103 57.631  1.00 46.74 ? 227  ARG D CD  1 
ATOM   9299  N  NE  . ARG D  1 224 ? -52.903 -29.771 57.478  1.00 50.26 ? 227  ARG D NE  1 
ATOM   9300  C  CZ  . ARG D  1 224 ? -53.573 -29.123 58.435  1.00 53.92 ? 227  ARG D CZ  1 
ATOM   9301  N  NH1 . ARG D  1 224 ? -53.784 -29.696 59.618  1.00 54.25 ? 227  ARG D NH1 1 
ATOM   9302  N  NH2 . ARG D  1 224 ? -54.049 -27.900 58.205  1.00 53.43 ? 227  ARG D NH2 1 
ATOM   9303  N  N   . MET D  1 225 ? -47.731 -30.843 55.262  1.00 36.03 ? 228  MET D N   1 
ATOM   9304  C  CA  . MET D  1 225 ? -47.518 -31.002 53.818  1.00 37.71 ? 228  MET D CA  1 
ATOM   9305  C  C   . MET D  1 225 ? -48.880 -31.198 53.165  1.00 38.73 ? 228  MET D C   1 
ATOM   9306  O  O   . MET D  1 225 ? -49.720 -31.920 53.706  1.00 39.14 ? 228  MET D O   1 
ATOM   9307  C  CB  . MET D  1 225 ? -46.673 -32.247 53.524  1.00 36.99 ? 228  MET D CB  1 
ATOM   9308  C  CG  . MET D  1 225 ? -45.301 -32.271 54.137  1.00 34.51 ? 228  MET D CG  1 
ATOM   9309  S  SD  . MET D  1 225 ? -44.637 -33.939 54.045  1.00 38.06 ? 228  MET D SD  1 
ATOM   9310  C  CE  . MET D  1 225 ? -42.985 -33.683 54.701  1.00 37.43 ? 228  MET D CE  1 
ATOM   9311  N  N   . PRO D  1 226 ? -49.085 -30.593 51.982  1.00 38.12 ? 229  PRO D N   1 
ATOM   9312  C  CA  . PRO D  1 226 ? -50.295 -30.821 51.188  1.00 37.77 ? 229  PRO D CA  1 
ATOM   9313  C  C   . PRO D  1 226 ? -50.546 -32.307 51.023  1.00 37.80 ? 229  PRO D C   1 
ATOM   9314  O  O   . PRO D  1 226 ? -49.625 -33.115 51.165  1.00 35.83 ? 229  PRO D O   1 
ATOM   9315  C  CB  . PRO D  1 226 ? -49.952 -30.191 49.833  1.00 36.26 ? 229  PRO D CB  1 
ATOM   9316  C  CG  . PRO D  1 226 ? -48.956 -29.116 50.183  1.00 35.50 ? 229  PRO D CG  1 
ATOM   9317  C  CD  . PRO D  1 226 ? -48.139 -29.692 51.303  1.00 36.15 ? 229  PRO D CD  1 
ATOM   9318  N  N   . ASP D  1 227 ? -51.807 -32.666 50.815  1.00 41.58 ? 230  ASP D N   1 
ATOM   9319  C  CA  . ASP D  1 227 ? -52.174 -34.060 50.631  1.00 43.38 ? 230  ASP D CA  1 
ATOM   9320  C  C   . ASP D  1 227 ? -51.404 -34.670 49.454  1.00 42.04 ? 230  ASP D C   1 
ATOM   9321  O  O   . ASP D  1 227 ? -51.363 -34.087 48.360  1.00 39.58 ? 230  ASP D O   1 
ATOM   9322  C  CB  . ASP D  1 227 ? -53.683 -34.163 50.398  1.00 47.29 ? 230  ASP D CB  1 
ATOM   9323  C  CG  . ASP D  1 227 ? -54.238 -35.518 50.784  1.00 50.45 ? 230  ASP D CG  1 
ATOM   9324  O  OD1 . ASP D  1 227 ? -53.472 -36.339 51.335  1.00 51.25 ? 230  ASP D OD1 1 
ATOM   9325  O  OD2 . ASP D  1 227 ? -55.433 -35.773 50.509  1.00 53.23 ? 230  ASP D OD2 1 
ATOM   9326  N  N   . ASP D  1 228 ? -50.774 -35.822 49.685  1.00 40.41 ? 231  ASP D N   1 
ATOM   9327  C  CA  . ASP D  1 228 ? -50.087 -36.549 48.608  1.00 40.79 ? 231  ASP D CA  1 
ATOM   9328  C  C   . ASP D  1 228 ? -48.877 -35.742 48.093  1.00 41.00 ? 231  ASP D C   1 
ATOM   9329  O  O   . ASP D  1 228 ? -48.631 -35.664 46.878  1.00 41.66 ? 231  ASP D O   1 
ATOM   9330  C  CB  . ASP D  1 228 ? -51.085 -36.842 47.474  1.00 40.34 ? 231  ASP D CB  1 
ATOM   9331  C  CG  . ASP D  1 228 ? -50.473 -37.635 46.315  1.00 41.00 ? 231  ASP D CG  1 
ATOM   9332  O  OD1 . ASP D  1 228 ? -49.824 -38.679 46.540  1.00 40.02 ? 231  ASP D OD1 1 
ATOM   9333  O  OD2 . ASP D  1 228 ? -50.729 -37.250 45.157  1.00 41.81 ? 231  ASP D OD2 1 
ATOM   9334  N  N   . PHE D  1 229 ? -48.169 -35.088 49.015  1.00 38.90 ? 232  PHE D N   1 
ATOM   9335  C  CA  . PHE D  1 229 ? -47.064 -34.192 48.653  1.00 36.66 ? 232  PHE D CA  1 
ATOM   9336  C  C   . PHE D  1 229 ? -45.838 -34.981 48.227  1.00 35.05 ? 232  PHE D C   1 
ATOM   9337  O  O   . PHE D  1 229 ? -45.365 -35.873 48.949  1.00 35.30 ? 232  PHE D O   1 
ATOM   9338  C  CB  . PHE D  1 229 ? -46.695 -33.258 49.812  1.00 38.13 ? 232  PHE D CB  1 
ATOM   9339  C  CG  . PHE D  1 229 ? -45.589 -32.276 49.483  1.00 37.96 ? 232  PHE D CG  1 
ATOM   9340  C  CD1 . PHE D  1 229 ? -45.854 -31.133 48.745  1.00 35.88 ? 232  PHE D CD1 1 
ATOM   9341  C  CD2 . PHE D  1 229 ? -44.290 -32.496 49.921  1.00 36.09 ? 232  PHE D CD2 1 
ATOM   9342  C  CE1 . PHE D  1 229 ? -44.850 -30.225 48.447  1.00 37.33 ? 232  PHE D CE1 1 
ATOM   9343  C  CE2 . PHE D  1 229 ? -43.278 -31.584 49.635  1.00 36.11 ? 232  PHE D CE2 1 
ATOM   9344  C  CZ  . PHE D  1 229 ? -43.562 -30.443 48.908  1.00 36.07 ? 232  PHE D CZ  1 
ATOM   9345  N  N   . PHE D  1 230 ? -45.337 -34.658 47.037  1.00 34.01 ? 233  PHE D N   1 
ATOM   9346  C  CA  . PHE D  1 230 ? -44.026 -35.124 46.600  1.00 31.41 ? 233  PHE D CA  1 
ATOM   9347  C  C   . PHE D  1 230 ? -42.929 -34.087 46.866  1.00 29.64 ? 233  PHE D C   1 
ATOM   9348  O  O   . PHE D  1 230 ? -43.103 -32.896 46.609  1.00 25.50 ? 233  PHE D O   1 
ATOM   9349  C  CB  . PHE D  1 230 ? -44.077 -35.471 45.117  1.00 35.31 ? 233  PHE D CB  1 
ATOM   9350  C  CG  . PHE D  1 230 ? -44.565 -36.863 44.841  1.00 36.66 ? 233  PHE D CG  1 
ATOM   9351  C  CD1 . PHE D  1 230 ? -45.771 -37.304 45.361  1.00 37.96 ? 233  PHE D CD1 1 
ATOM   9352  C  CD2 . PHE D  1 230 ? -43.809 -37.735 44.083  1.00 37.56 ? 233  PHE D CD2 1 
ATOM   9353  C  CE1 . PHE D  1 230 ? -46.205 -38.593 45.141  1.00 38.15 ? 233  PHE D CE1 1 
ATOM   9354  C  CE2 . PHE D  1 230 ? -44.261 -39.030 43.824  1.00 40.59 ? 233  PHE D CE2 1 
ATOM   9355  C  CZ  . PHE D  1 230 ? -45.463 -39.451 44.353  1.00 38.65 ? 233  PHE D CZ  1 
ATOM   9356  N  N   . ARG D  1 231 ? -41.791 -34.537 47.374  1.00 30.96 ? 234  ARG D N   1 
ATOM   9357  C  CA  . ARG D  1 231 ? -40.654 -33.637 47.523  1.00 30.55 ? 234  ARG D CA  1 
ATOM   9358  C  C   . ARG D  1 231 ? -40.114 -33.248 46.144  1.00 31.67 ? 234  ARG D C   1 
ATOM   9359  O  O   . ARG D  1 231 ? -40.447 -33.879 45.131  1.00 31.18 ? 234  ARG D O   1 
ATOM   9360  C  CB  . ARG D  1 231 ? -39.569 -34.282 48.373  1.00 28.74 ? 234  ARG D CB  1 
ATOM   9361  C  CG  . ARG D  1 231 ? -38.952 -35.466 47.709  1.00 28.28 ? 234  ARG D CG  1 
ATOM   9362  C  CD  . ARG D  1 231 ? -37.888 -36.084 48.574  1.00 25.28 ? 234  ARG D CD  1 
ATOM   9363  N  NE  . ARG D  1 231 ? -37.099 -37.002 47.772  1.00 25.78 ? 234  ARG D NE  1 
ATOM   9364  C  CZ  . ARG D  1 231 ? -36.252 -37.895 48.264  1.00 24.99 ? 234  ARG D CZ  1 
ATOM   9365  N  NH1 . ARG D  1 231 ? -36.090 -38.019 49.576  1.00 25.27 ? 234  ARG D NH1 1 
ATOM   9366  N  NH2 . ARG D  1 231 ? -35.553 -38.656 47.436  1.00 28.06 ? 234  ARG D NH2 1 
ATOM   9367  N  N   . ALA D  1 232 ? -39.356 -32.159 46.098  1.00 29.00 ? 235  ALA D N   1 
ATOM   9368  C  CA  . ALA D  1 232 ? -38.707 -31.733 44.861  1.00 28.63 ? 235  ALA D CA  1 
ATOM   9369  C  C   . ALA D  1 232 ? -37.896 -32.872 44.233  1.00 27.11 ? 235  ALA D C   1 
ATOM   9370  O  O   . ALA D  1 232 ? -37.370 -33.734 44.941  1.00 27.35 ? 235  ALA D O   1 
ATOM   9371  C  CB  . ALA D  1 232 ? -37.826 -30.497 45.112  1.00 25.32 ? 235  ALA D CB  1 
ATOM   9372  N  N   . PRO D  1 233 ? -37.792 -32.873 42.892  1.00 25.52 ? 236  PRO D N   1 
ATOM   9373  C  CA  . PRO D  1 233 ? -37.153 -33.934 42.103  1.00 23.93 ? 236  PRO D CA  1 
ATOM   9374  C  C   . PRO D  1 233 ? -35.626 -33.950 42.198  1.00 27.22 ? 236  PRO D C   1 
ATOM   9375  O  O   . PRO D  1 233 ? -34.975 -34.756 41.525  1.00 27.61 ? 236  PRO D O   1 
ATOM   9376  C  CB  . PRO D  1 233 ? -37.577 -33.605 40.671  1.00 21.95 ? 236  PRO D CB  1 
ATOM   9377  C  CG  . PRO D  1 233 ? -37.754 -32.110 40.656  1.00 22.36 ? 236  PRO D CG  1 
ATOM   9378  C  CD  . PRO D  1 233 ? -38.285 -31.767 42.051  1.00 25.14 ? 236  PRO D CD  1 
ATOM   9379  N  N   . SER D  1 234 ? -35.059 -33.056 43.010  1.00 27.59 ? 237  SER D N   1 
ATOM   9380  C  CA  . SER D  1 234 ? -33.604 -32.998 43.189  1.00 29.48 ? 237  SER D CA  1 
ATOM   9381  C  C   . SER D  1 234 ? -33.213 -32.065 44.339  1.00 28.80 ? 237  SER D C   1 
ATOM   9382  O  O   . SER D  1 234 ? -33.961 -31.147 44.690  1.00 27.59 ? 237  SER D O   1 
ATOM   9383  C  CB  . SER D  1 234 ? -32.925 -32.514 41.909  1.00 25.07 ? 237  SER D CB  1 
ATOM   9384  O  OG  . SER D  1 234 ? -33.237 -31.148 41.700  1.00 24.25 ? 237  SER D OG  1 
ATOM   9385  N  N   . PRO D  1 235 ? -32.016 -32.278 44.903  1.00 27.91 ? 238  PRO D N   1 
ATOM   9386  C  CA  . PRO D  1 235 ? -31.553 -31.474 46.038  1.00 26.53 ? 238  PRO D CA  1 
ATOM   9387  C  C   . PRO D  1 235 ? -31.331 -30.015 45.612  1.00 25.81 ? 238  PRO D C   1 
ATOM   9388  O  O   . PRO D  1 235 ? -30.714 -29.751 44.580  1.00 23.92 ? 238  PRO D O   1 
ATOM   9389  C  CB  . PRO D  1 235 ? -30.221 -32.135 46.427  1.00 25.15 ? 238  PRO D CB  1 
ATOM   9390  C  CG  . PRO D  1 235 ? -30.179 -33.435 45.689  1.00 26.81 ? 238  PRO D CG  1 
ATOM   9391  C  CD  . PRO D  1 235 ? -31.015 -33.266 44.471  1.00 27.38 ? 238  PRO D CD  1 
ATOM   9392  N  N   . ARG D  1 236 ? -31.935 -29.087 46.336  1.00 24.39 ? 239  ARG D N   1 
ATOM   9393  C  CA  . ARG D  1 236 ? -31.694 -27.684 46.093  1.00 26.47 ? 239  ARG D CA  1 
ATOM   9394  C  C   . ARG D  1 236 ? -31.946 -26.924 47.383  1.00 27.95 ? 239  ARG D C   1 
ATOM   9395  O  O   . ARG D  1 236 ? -32.567 -27.450 48.307  1.00 27.38 ? 239  ARG D O   1 
ATOM   9396  C  CB  . ARG D  1 236 ? -32.614 -27.170 44.984  1.00 25.07 ? 239  ARG D CB  1 
ATOM   9397  C  CG  . ARG D  1 236 ? -34.065 -26.979 45.425  1.00 25.77 ? 239  ARG D CG  1 
ATOM   9398  C  CD  . ARG D  1 236 ? -34.860 -28.292 45.387  1.00 22.54 ? 239  ARG D CD  1 
ATOM   9399  N  NE  . ARG D  1 236 ? -34.832 -28.962 44.084  1.00 21.62 ? 239  ARG D NE  1 
ATOM   9400  C  CZ  . ARG D  1 236 ? -35.648 -28.683 43.061  1.00 23.07 ? 239  ARG D CZ  1 
ATOM   9401  N  NH1 . ARG D  1 236 ? -36.486 -27.663 43.126  1.00 18.85 ? 239  ARG D NH1 1 
ATOM   9402  N  NH2 . ARG D  1 236 ? -35.549 -29.363 41.922  1.00 24.30 ? 239  ARG D NH2 1 
ATOM   9403  N  N   . SER D  1 237 ? -31.423 -25.706 47.453  1.00 25.90 ? 240  SER D N   1 
ATOM   9404  C  CA  . SER D  1 237 ? -31.776 -24.771 48.510  1.00 25.66 ? 240  SER D CA  1 
ATOM   9405  C  C   . SER D  1 237 ? -32.109 -23.383 47.929  1.00 25.14 ? 240  SER D C   1 
ATOM   9406  O  O   . SER D  1 237 ? -33.246 -23.122 47.534  1.00 22.86 ? 240  SER D O   1 
ATOM   9407  C  CB  . SER D  1 237 ? -30.621 -24.674 49.517  1.00 24.38 ? 240  SER D CB  1 
ATOM   9408  O  OG  . SER D  1 237 ? -29.380 -24.608 48.839  1.00 22.66 ? 240  SER D OG  1 
ATOM   9409  N  N   . GLY D  1 238 ? -31.105 -22.518 47.815  1.00 25.51 ? 241  GLY D N   1 
ATOM   9410  C  CA  . GLY D  1 238 ? -31.363 -21.120 47.456  1.00 26.75 ? 241  GLY D CA  1 
ATOM   9411  C  C   . GLY D  1 238 ? -31.174 -20.777 45.983  1.00 26.23 ? 241  GLY D C   1 
ATOM   9412  O  O   . GLY D  1 238 ? -30.890 -19.624 45.637  1.00 25.95 ? 241  GLY D O   1 
ATOM   9413  N  N   . THR D  1 239 ? -31.362 -21.749 45.100  1.00 26.50 ? 242  THR D N   1 
ATOM   9414  C  CA  . THR D  1 239 ? -31.238 -21.459 43.672  1.00 28.62 ? 242  THR D CA  1 
ATOM   9415  C  C   . THR D  1 239 ? -32.121 -20.260 43.311  1.00 26.83 ? 242  THR D C   1 
ATOM   9416  O  O   . THR D  1 239 ? -33.300 -20.203 43.671  1.00 25.02 ? 242  THR D O   1 
ATOM   9417  C  CB  . THR D  1 239 ? -31.657 -22.659 42.807  1.00 33.80 ? 242  THR D CB  1 
ATOM   9418  O  OG1 . THR D  1 239 ? -31.043 -23.849 43.320  1.00 39.02 ? 242  THR D OG1 1 
ATOM   9419  C  CG2 . THR D  1 239 ? -31.212 -22.450 41.348  1.00 35.84 ? 242  THR D CG2 1 
ATOM   9420  N  N   . GLY D  1 240 ? -31.560 -19.307 42.584  1.00 20.17 ? 243  GLY D N   1 
ATOM   9421  C  CA  . GLY D  1 240 ? -32.332 -18.138 42.198  1.00 16.88 ? 243  GLY D CA  1 
ATOM   9422  C  C   . GLY D  1 240 ? -32.312 -17.012 43.214  1.00 13.79 ? 243  GLY D C   1 
ATOM   9423  O  O   . GLY D  1 240 ? -33.011 -16.024 43.056  1.00 13.66 ? 243  GLY D O   1 
ATOM   9424  N  N   . VAL D  1 241 ? -31.484 -17.118 44.245  1.00 17.98 ? 244  VAL D N   1 
ATOM   9425  C  CA  . VAL D  1 241 ? -31.414 -16.031 45.217  1.00 17.54 ? 244  VAL D CA  1 
ATOM   9426  C  C   . VAL D  1 241 ? -31.012 -14.700 44.576  1.00 21.98 ? 244  VAL D C   1 
ATOM   9427  O  O   . VAL D  1 241 ? -31.431 -13.642 45.058  1.00 23.57 ? 244  VAL D O   1 
ATOM   9428  C  CB  . VAL D  1 241 ? -30.480 -16.348 46.385  1.00 19.44 ? 244  VAL D CB  1 
ATOM   9429  C  CG1 . VAL D  1 241 ? -29.014 -16.273 45.922  1.00 18.11 ? 244  VAL D CG1 1 
ATOM   9430  C  CG2 . VAL D  1 241 ? -30.737 -15.374 47.532  1.00 21.08 ? 244  VAL D CG2 1 
ATOM   9431  N  N   . GLU D  1 242 ? -30.248 -14.738 43.473  1.00 20.30 ? 245  GLU D N   1 
ATOM   9432  C  CA  . GLU D  1 242 ? -29.794 -13.498 42.832  1.00 23.80 ? 245  GLU D CA  1 
ATOM   9433  C  C   . GLU D  1 242 ? -30.928 -12.638 42.261  1.00 24.59 ? 245  GLU D C   1 
ATOM   9434  O  O   . GLU D  1 242 ? -30.805 -11.410 42.183  1.00 25.41 ? 245  GLU D O   1 
ATOM   9435  C  CB  . GLU D  1 242 ? -28.698 -13.744 41.774  1.00 24.45 ? 245  GLU D CB  1 
ATOM   9436  C  CG  . GLU D  1 242 ? -29.151 -14.508 40.551  1.00 26.25 ? 245  GLU D CG  1 
ATOM   9437  C  CD  . GLU D  1 242 ? -29.291 -15.986 40.831  1.00 31.70 ? 245  GLU D CD  1 
ATOM   9438  O  OE1 . GLU D  1 242 ? -28.942 -16.413 41.959  1.00 34.35 ? 245  GLU D OE1 1 
ATOM   9439  O  OE2 . GLU D  1 242 ? -29.719 -16.727 39.918  1.00 33.73 ? 245  GLU D OE2 1 
ATOM   9440  N  N   . VAL D  1 243 ? -32.036 -13.285 41.905  1.00 23.05 ? 246  VAL D N   1 
ATOM   9441  C  CA  . VAL D  1 243 ? -33.258 -12.594 41.470  1.00 23.30 ? 246  VAL D CA  1 
ATOM   9442  C  C   . VAL D  1 243 ? -33.842 -11.745 42.599  1.00 24.76 ? 246  VAL D C   1 
ATOM   9443  O  O   . VAL D  1 243 ? -34.164 -10.564 42.415  1.00 27.12 ? 246  VAL D O   1 
ATOM   9444  C  CB  . VAL D  1 243 ? -34.335 -13.630 41.040  1.00 25.95 ? 246  VAL D CB  1 
ATOM   9445  C  CG1 . VAL D  1 243 ? -35.618 -12.940 40.592  1.00 23.74 ? 246  VAL D CG1 1 
ATOM   9446  C  CG2 . VAL D  1 243 ? -33.791 -14.550 39.951  1.00 26.24 ? 246  VAL D CG2 1 
ATOM   9447  N  N   . VAL D  1 244 ? -33.997 -12.361 43.769  1.00 24.81 ? 247  VAL D N   1 
ATOM   9448  C  CA  . VAL D  1 244 ? -34.377 -11.644 44.979  1.00 23.58 ? 247  VAL D CA  1 
ATOM   9449  C  C   . VAL D  1 244 ? -33.424 -10.507 45.325  1.00 26.15 ? 247  VAL D C   1 
ATOM   9450  O  O   . VAL D  1 244 ? -33.854 -9.382  45.616  1.00 28.23 ? 247  VAL D O   1 
ATOM   9451  C  CB  . VAL D  1 244 ? -34.478 -12.582 46.184  1.00 24.48 ? 247  VAL D CB  1 
ATOM   9452  C  CG1 . VAL D  1 244 ? -35.284 -11.915 47.268  1.00 26.79 ? 247  VAL D CG1 1 
ATOM   9453  C  CG2 . VAL D  1 244 ? -35.153 -13.892 45.774  1.00 28.15 ? 247  VAL D CG2 1 
ATOM   9454  N  N   . ILE D  1 245 ? -32.134 -10.810 45.360  1.00 24.27 ? 248  ILE D N   1 
ATOM   9455  C  CA  . ILE D  1 245 ? -31.150 -9.797  45.685  1.00 24.39 ? 248  ILE D CA  1 
ATOM   9456  C  C   . ILE D  1 245 ? -31.194 -8.635  44.677  1.00 25.97 ? 248  ILE D C   1 
ATOM   9457  O  O   . ILE D  1 245 ? -31.010 -7.477  45.056  1.00 23.48 ? 248  ILE D O   1 
ATOM   9458  C  CB  . ILE D  1 245 ? -29.729 -10.392 45.711  1.00 24.75 ? 248  ILE D CB  1 
ATOM   9459  C  CG1 . ILE D  1 245 ? -29.607 -11.447 46.809  1.00 24.34 ? 248  ILE D CG1 1 
ATOM   9460  C  CG2 . ILE D  1 245 ? -28.675 -9.281  45.817  1.00 23.23 ? 248  ILE D CG2 1 
ATOM   9461  C  CD1 . ILE D  1 245 ? -28.307 -12.258 46.757  1.00 24.67 ? 248  ILE D CD1 1 
ATOM   9462  N  N   . GLN D  1 246 ? -31.389 -8.943  43.393  1.00 28.04 ? 249  GLN D N   1 
ATOM   9463  C  CA  . GLN D  1 246 ? -31.262 -7.907  42.360  1.00 29.32 ? 249  GLN D CA  1 
ATOM   9464  C  C   . GLN D  1 246 ? -32.529 -7.085  42.141  1.00 29.03 ? 249  GLN D C   1 
ATOM   9465  O  O   . GLN D  1 246 ? -32.473 -5.998  41.559  1.00 32.58 ? 249  GLN D O   1 
ATOM   9466  C  CB  . GLN D  1 246 ? -30.759 -8.475  41.028  1.00 28.84 ? 249  GLN D CB  1 
ATOM   9467  C  CG  . GLN D  1 246 ? -29.341 -9.035  41.067  1.00 30.40 ? 249  GLN D CG  1 
ATOM   9468  C  CD  . GLN D  1 246 ? -28.323 -8.045  41.591  1.00 33.98 ? 249  GLN D CD  1 
ATOM   9469  O  OE1 . GLN D  1 246 ? -27.566 -8.347  42.523  1.00 35.29 ? 249  GLN D OE1 1 
ATOM   9470  N  NE2 . GLN D  1 246 ? -28.311 -6.849  41.016  1.00 31.84 ? 249  GLN D NE2 1 
ATOM   9471  N  N   . ALA D  1 247 ? -33.664 -7.602  42.589  1.00 26.57 ? 250  ALA D N   1 
ATOM   9472  C  CA  . ALA D  1 247 ? -34.941 -6.898  42.398  1.00 29.36 ? 250  ALA D CA  1 
ATOM   9473  C  C   . ALA D  1 247 ? -34.935 -5.533  43.103  1.00 31.09 ? 250  ALA D C   1 
ATOM   9474  O  O   . ALA D  1 247 ? -35.413 -4.526  42.563  1.00 28.68 ? 250  ALA D O   1 
ATOM   9475  C  CB  . ALA D  1 247 ? -36.106 -7.756  42.897  1.00 25.41 ? 250  ALA D CB  1 
ATOM   9476  N  N   . HIS D  1 248 ? -34.421 -5.520  44.327  1.00 32.46 ? 251  HIS D N   1 
ATOM   9477  C  CA  . HIS D  1 248 ? -34.313 -4.290  45.097  1.00 33.46 ? 251  HIS D CA  1 
ATOM   9478  C  C   . HIS D  1 248 ? -32.997 -4.304  45.866  1.00 34.00 ? 251  HIS D C   1 
ATOM   9479  O  O   . HIS D  1 248 ? -32.927 -4.796  46.982  1.00 33.02 ? 251  HIS D O   1 
ATOM   9480  C  CB  . HIS D  1 248 ? -35.504 -4.139  46.043  1.00 30.98 ? 251  HIS D CB  1 
ATOM   9481  C  CG  . HIS D  1 248 ? -36.824 -4.032  45.338  1.00 31.31 ? 251  HIS D CG  1 
ATOM   9482  N  ND1 . HIS D  1 248 ? -37.248 -2.872  44.722  1.00 30.13 ? 251  HIS D ND1 1 
ATOM   9483  C  CD2 . HIS D  1 248 ? -37.788 -4.958  45.102  1.00 29.02 ? 251  HIS D CD2 1 
ATOM   9484  C  CE1 . HIS D  1 248 ? -38.412 -3.088  44.133  1.00 30.98 ? 251  HIS D CE1 1 
ATOM   9485  N  NE2 . HIS D  1 248 ? -38.761 -4.346  44.348  1.00 31.13 ? 251  HIS D NE2 1 
ATOM   9486  N  N   . PRO D  1 249 ? -31.928 -3.840  45.222  1.00 37.69 ? 252  PRO D N   1 
ATOM   9487  C  CA  . PRO D  1 249 ? -30.587 -3.938  45.801  1.00 38.46 ? 252  PRO D CA  1 
ATOM   9488  C  C   . PRO D  1 249 ? -30.500 -3.236  47.152  1.00 36.92 ? 252  PRO D C   1 
ATOM   9489  O  O   . PRO D  1 249 ? -30.670 -2.027  47.227  1.00 37.56 ? 252  PRO D O   1 
ATOM   9490  C  CB  . PRO D  1 249 ? -29.709 -3.220  44.764  1.00 37.54 ? 252  PRO D CB  1 
ATOM   9491  C  CG  . PRO D  1 249 ? -30.444 -3.392  43.482  1.00 37.62 ? 252  PRO D CG  1 
ATOM   9492  C  CD  . PRO D  1 249 ? -31.901 -3.360  43.827  1.00 37.28 ? 252  PRO D CD  1 
ATOM   9493  N  N   . MET D  1 250 ? -30.214 -3.994  48.202  1.00 36.89 ? 253  MET D N   1 
ATOM   9494  C  CA  . MET D  1 250 ? -30.140 -3.443  49.552  1.00 36.66 ? 253  MET D CA  1 
ATOM   9495  C  C   . MET D  1 250 ? -28.700 -3.442  50.082  1.00 34.96 ? 253  MET D C   1 
ATOM   9496  O  O   . MET D  1 250 ? -27.935 -4.374  49.833  1.00 33.56 ? 253  MET D O   1 
ATOM   9497  C  CB  . MET D  1 250 ? -31.050 -4.250  50.485  1.00 39.56 ? 253  MET D CB  1 
ATOM   9498  C  CG  . MET D  1 250 ? -31.700 -3.449  51.604  1.00 45.27 ? 253  MET D CG  1 
ATOM   9499  S  SD  . MET D  1 250 ? -32.982 -2.323  51.031  1.00 48.39 ? 253  MET D SD  1 
ATOM   9500  C  CE  . MET D  1 250 ? -32.019 -0.897  50.544  1.00 46.78 ? 253  MET D CE  1 
ATOM   9501  N  N   . GLN D  1 251 ? -28.339 -2.393  50.815  1.00 32.49 ? 254  GLN D N   1 
ATOM   9502  C  CA  . GLN D  1 251 ? -27.131 -2.408  51.633  1.00 30.84 ? 254  GLN D CA  1 
ATOM   9503  C  C   . GLN D  1 251 ? -27.455 -2.813  53.063  1.00 28.86 ? 254  GLN D C   1 
ATOM   9504  O  O   . GLN D  1 251 ? -28.447 -2.366  53.635  1.00 24.01 ? 254  GLN D O   1 
ATOM   9505  C  CB  . GLN D  1 251 ? -26.457 -1.035  51.651  1.00 31.83 ? 254  GLN D CB  1 
ATOM   9506  C  CG  . GLN D  1 251 ? -25.433 -0.804  50.566  1.00 31.70 ? 254  GLN D CG  1 
ATOM   9507  C  CD  . GLN D  1 251 ? -24.987 0.650   50.520  1.00 34.31 ? 254  GLN D CD  1 
ATOM   9508  O  OE1 . GLN D  1 251 ? -25.778 1.541   50.213  1.00 38.65 ? 254  GLN D OE1 1 
ATOM   9509  N  NE2 . GLN D  1 251 ? -23.760 0.904   50.923  1.00 31.64 ? 254  GLN D NE2 1 
ATOM   9510  N  N   . PRO D  1 252 ? -26.579 -3.623  53.667  1.00 28.05 ? 255  PRO D N   1 
ATOM   9511  C  CA  . PRO D  1 252 ? -26.798 -4.057  55.052  1.00 28.21 ? 255  PRO D CA  1 
ATOM   9512  C  C   . PRO D  1 252 ? -26.728 -2.880  56.035  1.00 27.09 ? 255  PRO D C   1 
ATOM   9513  O  O   . PRO D  1 252 ? -25.992 -1.916  55.794  1.00 24.75 ? 255  PRO D O   1 
ATOM   9514  C  CB  . PRO D  1 252 ? -25.655 -5.046  55.306  1.00 27.79 ? 255  PRO D CB  1 
ATOM   9515  C  CG  . PRO D  1 252 ? -24.590 -4.681  54.280  1.00 29.67 ? 255  PRO D CG  1 
ATOM   9516  C  CD  . PRO D  1 252 ? -25.328 -4.141  53.086  1.00 27.41 ? 255  PRO D CD  1 
ATOM   9517  N  N   . GLY D  1 253 ? -27.487 -2.976  57.125  1.00 26.47 ? 256  GLY D N   1 
ATOM   9518  C  CA  . GLY D  1 253 ? -27.581 -1.907  58.119  1.00 28.43 ? 256  GLY D CA  1 
ATOM   9519  C  C   . GLY D  1 253 ? -28.740 -2.083  59.094  1.00 29.29 ? 256  GLY D C   1 
ATOM   9520  O  O   . GLY D  1 253 ? -29.334 -3.158  59.187  1.00 27.55 ? 256  GLY D O   1 
ATOM   9521  N  N   . ARG D  1 254 ? -29.049 -1.029  59.845  1.00 30.30 ? 257  ARG D N   1 
ATOM   9522  C  CA  . ARG D  1 254 ? -29.997 -1.139  60.953  1.00 32.06 ? 257  ARG D CA  1 
ATOM   9523  C  C   . ARG D  1 254 ? -30.614 0.212   61.276  1.00 30.51 ? 257  ARG D C   1 
ATOM   9524  O  O   . ARG D  1 254 ? -30.023 1.249   60.990  1.00 31.09 ? 257  ARG D O   1 
ATOM   9525  C  CB  . ARG D  1 254 ? -29.283 -1.687  62.193  1.00 35.78 ? 257  ARG D CB  1 
ATOM   9526  C  CG  . ARG D  1 254 ? -28.417 -0.667  62.903  1.00 39.76 ? 257  ARG D CG  1 
ATOM   9527  C  CD  . ARG D  1 254 ? -27.079 -0.455  62.213  1.00 45.37 ? 257  ARG D CD  1 
ATOM   9528  N  NE  . ARG D  1 254 ? -26.221 0.426   63.005  1.00 50.02 ? 257  ARG D NE  1 
ATOM   9529  C  CZ  . ARG D  1 254 ? -25.190 1.122   62.527  1.00 52.55 ? 257  ARG D CZ  1 
ATOM   9530  N  NH1 . ARG D  1 254 ? -24.873 1.065   61.237  1.00 51.20 ? 257  ARG D NH1 1 
ATOM   9531  N  NH2 . ARG D  1 254 ? -24.495 1.910   63.342  1.00 53.33 ? 257  ARG D NH2 1 
ATOM   9532  N  N   . ASN D  1 255 ? -31.765 0.214   61.937  1.00 30.15 ? 258  ASN D N   1 
ATOM   9533  C  CA  . ASN D  1 255 ? -32.237 1.465   62.533  1.00 31.22 ? 258  ASN D CA  1 
ATOM   9534  C  C   . ASN D  1 255 ? -31.364 1.808   63.732  1.00 32.60 ? 258  ASN D C   1 
ATOM   9535  O  O   . ASN D  1 255 ? -30.730 0.927   64.322  1.00 32.02 ? 258  ASN D O   1 
ATOM   9536  C  CB  . ASN D  1 255 ? -33.722 1.396   62.923  1.00 28.15 ? 258  ASN D CB  1 
ATOM   9537  C  CG  . ASN D  1 255 ? -34.660 1.807   61.776  1.00 27.63 ? 258  ASN D CG  1 
ATOM   9538  O  OD1 . ASN D  1 255 ? -34.289 2.582   60.888  1.00 26.83 ? 258  ASN D OD1 1 
ATOM   9539  N  ND2 . ASN D  1 255 ? -35.882 1.289   61.805  1.00 26.64 ? 258  ASN D ND2 1 
ATOM   9540  N  N   . VAL D  1 256 ? -31.266 3.096   64.036  1.00 35.57 ? 259  VAL D N   1 
ATOM   9541  C  CA  . VAL D  1 256 ? -30.348 3.578   65.060  1.00 38.60 ? 259  VAL D CA  1 
ATOM   9542  C  C   . VAL D  1 256 ? -31.110 4.063   66.314  1.00 41.50 ? 259  VAL D C   1 
ATOM   9543  O  O   . VAL D  1 256 ? -30.807 5.112   66.880  1.00 43.52 ? 259  VAL D O   1 
ATOM   9544  C  CB  . VAL D  1 256 ? -29.402 4.661   64.462  1.00 41.20 ? 259  VAL D CB  1 
ATOM   9545  C  CG1 . VAL D  1 256 ? -29.418 5.954   65.266  1.00 40.81 ? 259  VAL D CG1 1 
ATOM   9546  C  CG2 . VAL D  1 256 ? -27.984 4.109   64.273  1.00 40.54 ? 259  VAL D CG2 1 
ATOM   9547  N  N   . GLY D  1 257 ? -32.088 3.274   66.757  1.00 43.84 ? 260  GLY D N   1 
ATOM   9548  C  CA  . GLY D  1 257 ? -32.865 3.607   67.956  1.00 45.66 ? 260  GLY D CA  1 
ATOM   9549  C  C   . GLY D  1 257 ? -34.220 4.246   67.683  1.00 48.02 ? 260  GLY D C   1 
ATOM   9550  O  O   . GLY D  1 257 ? -35.032 4.417   68.593  1.00 47.44 ? 260  GLY D O   1 
ATOM   9551  N  N   . LYS D  1 258 ? -34.461 4.607   66.425  1.00 48.78 ? 261  LYS D N   1 
ATOM   9552  C  CA  . LYS D  1 258 ? -35.734 5.187   66.019  1.00 47.95 ? 261  LYS D CA  1 
ATOM   9553  C  C   . LYS D  1 258 ? -36.167 4.645   64.663  1.00 47.28 ? 261  LYS D C   1 
ATOM   9554  O  O   . LYS D  1 258 ? -35.330 4.266   63.832  1.00 46.76 ? 261  LYS D O   1 
ATOM   9555  C  CB  . LYS D  1 258 ? -35.636 6.712   65.965  1.00 48.82 ? 261  LYS D CB  1 
ATOM   9556  C  CG  . LYS D  1 258 ? -34.215 7.242   65.865  1.00 52.08 ? 261  LYS D CG  1 
ATOM   9557  C  CD  . LYS D  1 258 ? -34.167 8.756   66.079  1.00 54.16 ? 261  LYS D CD  1 
ATOM   9558  C  CE  . LYS D  1 258 ? -33.460 9.461   64.915  1.00 56.04 ? 261  LYS D CE  1 
ATOM   9559  N  NZ  . LYS D  1 258 ? -33.925 10.874  64.726  1.00 55.36 ? 261  LYS D NZ  1 
ATOM   9560  N  N   . ILE D  1 259 ? -37.477 4.600   64.443  1.00 44.52 ? 262  ILE D N   1 
ATOM   9561  C  CA  . ILE D  1 259 ? -38.003 4.300   63.121  1.00 42.67 ? 262  ILE D CA  1 
ATOM   9562  C  C   . ILE D  1 259 ? -37.380 5.227   62.088  1.00 41.84 ? 262  ILE D C   1 
ATOM   9563  O  O   . ILE D  1 259 ? -36.911 6.311   62.424  1.00 42.61 ? 262  ILE D O   1 
ATOM   9564  C  CB  . ILE D  1 259 ? -39.532 4.424   63.079  1.00 41.83 ? 262  ILE D CB  1 
ATOM   9565  C  CG1 . ILE D  1 259 ? -39.965 5.875   63.334  1.00 41.24 ? 262  ILE D CG1 1 
ATOM   9566  C  CG2 . ILE D  1 259 ? -40.160 3.465   64.068  1.00 40.49 ? 262  ILE D CG2 1 
ATOM   9567  C  CD1 . ILE D  1 259 ? -41.455 6.102   63.234  1.00 38.00 ? 262  ILE D CD1 1 
ATOM   9568  N  N   . ASN D  1 260 ? -37.308 4.761   60.845  1.00 43.86 ? 263  ASN D N   1 
ATOM   9569  C  CA  . ASN D  1 260 ? -36.795 5.567   59.731  1.00 42.31 ? 263  ASN D CA  1 
ATOM   9570  C  C   . ASN D  1 260 ? -35.451 6.235   59.981  1.00 40.20 ? 263  ASN D C   1 
ATOM   9571  O  O   . ASN D  1 260 ? -35.264 7.412   59.646  1.00 39.17 ? 263  ASN D O   1 
ATOM   9572  C  CB  . ASN D  1 260 ? -37.815 6.622   59.313  1.00 43.93 ? 263  ASN D CB  1 
ATOM   9573  C  CG  . ASN D  1 260 ? -39.138 6.017   58.925  1.00 45.69 ? 263  ASN D CG  1 
ATOM   9574  O  OD1 . ASN D  1 260 ? -40.165 6.293   59.550  1.00 47.66 ? 263  ASN D OD1 1 
ATOM   9575  N  ND2 . ASN D  1 260 ? -39.121 5.159   57.910  1.00 45.60 ? 263  ASN D ND2 1 
ATOM   9576  N  N   . SER D  1 261 ? -34.502 5.463   60.506  1.00 38.26 ? 264  SER D N   1 
ATOM   9577  C  CA  . SER D  1 261 ? -33.123 5.922   60.673  1.00 37.77 ? 264  SER D CA  1 
ATOM   9578  C  C   . SER D  1 261 ? -32.130 4.874   60.136  1.00 37.48 ? 264  SER D C   1 
ATOM   9579  O  O   . SER D  1 261 ? -31.046 4.665   60.696  1.00 35.07 ? 264  SER D O   1 
ATOM   9580  C  CB  . SER D  1 261 ? -32.841 6.208   62.152  1.00 34.79 ? 264  SER D CB  1 
ATOM   9581  O  OG  . SER D  1 261 ? -32.988 5.025   62.920  1.00 31.29 ? 264  SER D OG  1 
ATOM   9582  N  N   . TYR D  1 262 ? -32.470 4.273   59.001  1.00 38.85 ? 265  TYR D N   1 
ATOM   9583  C  CA  . TYR D  1 262 ? -31.657 3.192   58.452  1.00 36.39 ? 265  TYR D CA  1 
ATOM   9584  C  C   . TYR D  1 262 ? -30.275 3.662   58.109  1.00 34.97 ? 265  TYR D C   1 
ATOM   9585  O  O   . TYR D  1 262 ? -30.083 4.414   57.163  1.00 38.84 ? 265  TYR D O   1 
ATOM   9586  C  CB  . TYR D  1 262 ? -32.290 2.602   57.216  1.00 36.33 ? 265  TYR D CB  1 
ATOM   9587  C  CG  . TYR D  1 262 ? -31.694 1.281   56.820  1.00 36.79 ? 265  TYR D CG  1 
ATOM   9588  C  CD1 . TYR D  1 262 ? -31.971 0.130   57.547  1.00 36.04 ? 265  TYR D CD1 1 
ATOM   9589  C  CD2 . TYR D  1 262 ? -30.914 1.165   55.677  1.00 36.11 ? 265  TYR D CD2 1 
ATOM   9590  C  CE1 . TYR D  1 262 ? -31.458 -1.099  57.156  1.00 35.53 ? 265  TYR D CE1 1 
ATOM   9591  C  CE2 . TYR D  1 262 ? -30.435 -0.067  55.260  1.00 36.13 ? 265  TYR D CE2 1 
ATOM   9592  C  CZ  . TYR D  1 262 ? -30.695 -1.185  56.013  1.00 34.28 ? 265  TYR D CZ  1 
ATOM   9593  O  OH  . TYR D  1 262 ? -30.180 -2.394  55.633  1.00 36.93 ? 265  TYR D OH  1 
ATOM   9594  N  N   . THR D  1 263 ? -29.302 3.133   58.831  1.00 34.05 ? 266  THR D N   1 
ATOM   9595  C  CA  . THR D  1 263 ? -27.918 3.534   58.676  1.00 33.83 ? 266  THR D CA  1 
ATOM   9596  C  C   . THR D  1 263 ? -27.126 2.319   58.207  1.00 31.89 ? 266  THR D C   1 
ATOM   9597  O  O   . THR D  1 263 ? -27.153 1.279   58.851  1.00 31.49 ? 266  THR D O   1 
ATOM   9598  C  CB  . THR D  1 263 ? -27.336 3.984   60.039  1.00 34.19 ? 266  THR D CB  1 
ATOM   9599  O  OG1 . THR D  1 263 ? -28.118 5.065   60.566  1.00 36.43 ? 266  THR D OG1 1 
ATOM   9600  C  CG2 . THR D  1 263 ? -25.897 4.405   59.897  1.00 32.30 ? 266  THR D CG2 1 
ATOM   9601  N  N   . VAL D  1 264 ? -26.428 2.460   57.086  1.00 29.88 ? 267  VAL D N   1 
ATOM   9602  C  CA  . VAL D  1 264 ? -25.574 1.411   56.575  1.00 30.66 ? 267  VAL D CA  1 
ATOM   9603  C  C   . VAL D  1 264 ? -24.480 1.061   57.578  1.00 33.16 ? 267  VAL D C   1 
ATOM   9604  O  O   . VAL D  1 264 ? -23.932 1.933   58.252  1.00 36.20 ? 267  VAL D O   1 
ATOM   9605  C  CB  . VAL D  1 264 ? -24.927 1.823   55.237  1.00 30.31 ? 267  VAL D CB  1 
ATOM   9606  C  CG1 . VAL D  1 264 ? -23.911 0.779   54.795  1.00 30.55 ? 267  VAL D CG1 1 
ATOM   9607  C  CG2 . VAL D  1 264 ? -26.009 2.044   54.146  1.00 30.18 ? 267  VAL D CG2 1 
ATOM   9608  N  N   . ASP D  1 265 ? -24.109 -0.210  57.611  1.00 32.30 ? 268  ASP D N   1 
ATOM   9609  C  CA  . ASP D  1 265 ? -23.072 -0.689  58.504  1.00 33.57 ? 268  ASP D CA  1 
ATOM   9610  C  C   . ASP D  1 265 ? -21.922 -1.212  57.652  1.00 32.61 ? 268  ASP D C   1 
ATOM   9611  O  O   . ASP D  1 265 ? -22.008 -2.293  57.075  1.00 33.08 ? 268  ASP D O   1 
ATOM   9612  C  CB  . ASP D  1 265 ? -23.642 -1.805  59.404  1.00 33.67 ? 268  ASP D CB  1 
ATOM   9613  C  CG  . ASP D  1 265 ? -22.571 -2.557  60.180  1.00 33.99 ? 268  ASP D CG  1 
ATOM   9614  O  OD1 . ASP D  1 265 ? -21.416 -2.088  60.266  1.00 32.62 ? 268  ASP D OD1 1 
ATOM   9615  O  OD2 . ASP D  1 265 ? -22.883 -3.660  60.668  1.00 37.41 ? 268  ASP D OD2 1 
ATOM   9616  N  N   . PRO D  1 266 ? -20.835 -0.439  57.566  1.00 33.07 ? 269  PRO D N   1 
ATOM   9617  C  CA  . PRO D  1 266 ? -19.842 -0.718  56.530  1.00 32.37 ? 269  PRO D CA  1 
ATOM   9618  C  C   . PRO D  1 266 ? -18.946 -1.868  56.943  1.00 30.49 ? 269  PRO D C   1 
ATOM   9619  O  O   . PRO D  1 266 ? -18.120 -2.313  56.167  1.00 31.06 ? 269  PRO D O   1 
ATOM   9620  C  CB  . PRO D  1 266 ? -19.036 0.585   56.465  1.00 32.56 ? 269  PRO D CB  1 
ATOM   9621  C  CG  . PRO D  1 266 ? -19.194 1.183   57.840  1.00 33.47 ? 269  PRO D CG  1 
ATOM   9622  C  CD  . PRO D  1 266 ? -20.586 0.842   58.254  1.00 32.22 ? 269  PRO D CD  1 
ATOM   9623  N  N   . THR D  1 267 ? -19.090 -2.327  58.177  1.00 31.93 ? 270  THR D N   1 
ATOM   9624  C  CA  . THR D  1 267 ? -18.322 -3.474  58.637  1.00 31.97 ? 270  THR D CA  1 
ATOM   9625  C  C   . THR D  1 267 ? -19.060 -4.794  58.390  1.00 28.81 ? 270  THR D C   1 
ATOM   9626  O  O   . THR D  1 267 ? -18.506 -5.868  58.611  1.00 26.45 ? 270  THR D O   1 
ATOM   9627  C  CB  . THR D  1 267 ? -17.952 -3.361  60.136  1.00 34.90 ? 270  THR D CB  1 
ATOM   9628  O  OG1 . THR D  1 267 ? -19.091 -3.690  60.940  1.00 35.39 ? 270  THR D OG1 1 
ATOM   9629  C  CG2 . THR D  1 267 ? -17.478 -1.939  60.470  1.00 36.61 ? 270  THR D CG2 1 
ATOM   9630  N  N   . SER D  1 268 ? -20.314 -4.712  57.957  1.00 24.12 ? 271  SER D N   1 
ATOM   9631  C  CA  . SER D  1 268 ? -21.068 -5.918  57.658  1.00 24.18 ? 271  SER D CA  1 
ATOM   9632  C  C   . SER D  1 268 ? -20.511 -6.582  56.398  1.00 26.01 ? 271  SER D C   1 
ATOM   9633  O  O   . SER D  1 268 ? -20.042 -5.904  55.479  1.00 25.49 ? 271  SER D O   1 
ATOM   9634  C  CB  . SER D  1 268 ? -22.552 -5.604  57.469  1.00 22.15 ? 271  SER D CB  1 
ATOM   9635  O  OG  . SER D  1 268 ? -23.288 -6.790  57.226  1.00 21.33 ? 271  SER D OG  1 
ATOM   9636  N  N   . SER D  1 269 ? -20.562 -7.909  56.362  1.00 23.52 ? 272  SER D N   1 
ATOM   9637  C  CA  . SER D  1 269 ? -20.474 -8.625  55.097  1.00 24.24 ? 272  SER D CA  1 
ATOM   9638  C  C   . SER D  1 269 ? -21.694 -8.328  54.211  1.00 24.54 ? 272  SER D C   1 
ATOM   9639  O  O   . SER D  1 269 ? -22.622 -7.640  54.632  1.00 25.08 ? 272  SER D O   1 
ATOM   9640  C  CB  . SER D  1 269 ? -20.327 -10.121 55.349  1.00 20.93 ? 272  SER D CB  1 
ATOM   9641  O  OG  . SER D  1 269 ? -21.490 -10.631 55.950  1.00 17.93 ? 272  SER D OG  1 
ATOM   9642  N  N   . ASP D  1 270 ? -21.601 -8.704  52.939  1.00 24.43 ? 273  ASP D N   1 
ATOM   9643  C  CA  . ASP D  1 270 ? -22.761 -8.760  52.047  1.00 23.08 ? 273  ASP D CA  1 
ATOM   9644  C  C   . ASP D  1 270 ? -22.542 -9.883  51.064  1.00 21.81 ? 273  ASP D C   1 
ATOM   9645  O  O   . ASP D  1 270 ? -21.677 -10.726 51.269  1.00 19.78 ? 273  ASP D O   1 
ATOM   9646  C  CB  . ASP D  1 270 ? -22.972 -7.448  51.281  1.00 21.91 ? 273  ASP D CB  1 
ATOM   9647  C  CG  . ASP D  1 270 ? -21.730 -6.992  50.536  1.00 24.51 ? 273  ASP D CG  1 
ATOM   9648  O  OD1 . ASP D  1 270 ? -21.063 -7.811  49.874  1.00 24.18 ? 273  ASP D OD1 1 
ATOM   9649  O  OD2 . ASP D  1 270 ? -21.421 -5.783  50.601  1.00 30.79 ? 273  ASP D OD2 1 
ATOM   9650  N  N   . PHE D  1 271 ? -23.310 -9.894  49.983  1.00 22.95 ? 274  PHE D N   1 
ATOM   9651  C  CA  . PHE D  1 271 ? -23.341 -11.081 49.158  1.00 22.53 ? 274  PHE D CA  1 
ATOM   9652  C  C   . PHE D  1 271 ? -22.083 -11.244 48.337  1.00 19.15 ? 274  PHE D C   1 
ATOM   9653  O  O   . PHE D  1 271 ? -21.791 -12.343 47.904  1.00 20.64 ? 274  PHE D O   1 
ATOM   9654  C  CB  . PHE D  1 271 ? -24.597 -11.118 48.287  1.00 22.04 ? 274  PHE D CB  1 
ATOM   9655  C  CG  . PHE D  1 271 ? -25.772 -11.700 48.996  1.00 19.72 ? 274  PHE D CG  1 
ATOM   9656  C  CD1 . PHE D  1 271 ? -25.845 -13.069 49.213  1.00 15.85 ? 274  PHE D CD1 1 
ATOM   9657  C  CD2 . PHE D  1 271 ? -26.717 -10.866 49.598  1.00 20.89 ? 274  PHE D CD2 1 
ATOM   9658  C  CE1 . PHE D  1 271 ? -26.850 -13.601 50.008  1.00 18.52 ? 274  PHE D CE1 1 
ATOM   9659  C  CE2 . PHE D  1 271 ? -27.723 -11.388 50.397  1.00 18.03 ? 274  PHE D CE2 1 
ATOM   9660  C  CZ  . PHE D  1 271 ? -27.834 -12.760 50.541  1.00 20.07 ? 274  PHE D CZ  1 
ATOM   9661  N  N   . SER D  1 272 ? -21.314 -10.164 48.183  1.00 19.65 ? 275  SER D N   1 
ATOM   9662  C  CA  . SER D  1 272 ? -20.001 -10.217 47.510  1.00 19.05 ? 275  SER D CA  1 
ATOM   9663  C  C   . SER D  1 272 ? -18.902 -10.682 48.450  1.00 22.88 ? 275  SER D C   1 
ATOM   9664  O  O   . SER D  1 272 ? -17.765 -10.888 48.022  1.00 25.96 ? 275  SER D O   1 
ATOM   9665  C  CB  . SER D  1 272 ? -19.609 -8.846  46.937  1.00 20.98 ? 275  SER D CB  1 
ATOM   9666  O  OG  . SER D  1 272 ? -19.096 -7.965  47.946  1.00 22.98 ? 275  SER D OG  1 
ATOM   9667  N  N   . THR D  1 273 ? -19.215 -10.827 49.734  1.00 20.49 ? 276  THR D N   1 
ATOM   9668  C  CA  . THR D  1 273 ? -18.199 -11.292 50.676  1.00 23.65 ? 276  THR D CA  1 
ATOM   9669  C  C   . THR D  1 273 ? -18.687 -12.453 51.561  1.00 24.28 ? 276  THR D C   1 
ATOM   9670  O  O   . THR D  1 273 ? -18.774 -12.325 52.782  1.00 22.27 ? 276  THR D O   1 
ATOM   9671  C  CB  . THR D  1 273 ? -17.687 -10.160 51.559  1.00 23.38 ? 276  THR D CB  1 
ATOM   9672  O  OG1 . THR D  1 273 ? -18.771 -9.627  52.315  1.00 26.41 ? 276  THR D OG1 1 
ATOM   9673  C  CG2 . THR D  1 273 ? -17.030 -9.031  50.716  1.00 24.68 ? 276  THR D CG2 1 
ATOM   9674  N  N   . PRO D  1 274 ? -18.985 -13.594 50.938  1.00 24.10 ? 277  PRO D N   1 
ATOM   9675  C  CA  . PRO D  1 274 ? -19.435 -14.754 51.706  1.00 23.47 ? 277  PRO D CA  1 
ATOM   9676  C  C   . PRO D  1 274 ? -18.369 -15.218 52.698  1.00 22.18 ? 277  PRO D C   1 
ATOM   9677  O  O   . PRO D  1 274 ? -18.700 -15.642 53.791  1.00 22.77 ? 277  PRO D O   1 
ATOM   9678  C  CB  . PRO D  1 274 ? -19.675 -15.830 50.620  1.00 21.24 ? 277  PRO D CB  1 
ATOM   9679  C  CG  . PRO D  1 274 ? -18.756 -15.450 49.503  1.00 23.49 ? 277  PRO D CG  1 
ATOM   9680  C  CD  . PRO D  1 274 ? -18.710 -13.922 49.522  1.00 22.77 ? 277  PRO D CD  1 
ATOM   9681  N  N   . CYS D  1 275 ? -17.101 -15.200 52.308  1.00 24.32 ? 278  CYS D N   1 
ATOM   9682  C  CA  . CYS D  1 275 ? -16.046 -15.652 53.219  1.00 25.54 ? 278  CYS D CA  1 
ATOM   9683  C  C   . CYS D  1 275 ? -15.899 -14.753 54.439  1.00 23.21 ? 278  CYS D C   1 
ATOM   9684  O  O   . CYS D  1 275 ? -15.603 -15.229 55.533  1.00 21.44 ? 278  CYS D O   1 
ATOM   9685  C  CB  . CYS D  1 275 ? -14.705 -15.810 52.500  1.00 27.42 ? 278  CYS D CB  1 
ATOM   9686  S  SG  . CYS D  1 275 ? -14.742 -17.031 51.164  1.00 28.44 ? 278  CYS D SG  1 
ATOM   9687  N  N   . LEU D  1 276 ? -16.110 -13.455 54.262  1.00 24.51 ? 279  LEU D N   1 
ATOM   9688  C  CA  . LEU D  1 276 ? -16.080 -12.535 55.410  1.00 25.93 ? 279  LEU D CA  1 
ATOM   9689  C  C   . LEU D  1 276 ? -17.278 -12.772 56.321  1.00 27.37 ? 279  LEU D C   1 
ATOM   9690  O  O   . LEU D  1 276 ? -17.193 -12.635 57.539  1.00 27.08 ? 279  LEU D O   1 
ATOM   9691  C  CB  . LEU D  1 276 ? -16.042 -11.080 54.956  1.00 24.89 ? 279  LEU D CB  1 
ATOM   9692  C  CG  . LEU D  1 276 ? -16.204 -9.998  56.026  1.00 26.79 ? 279  LEU D CG  1 
ATOM   9693  C  CD1 . LEU D  1 276 ? -15.012 -9.972  57.010  1.00 24.81 ? 279  LEU D CD1 1 
ATOM   9694  C  CD2 . LEU D  1 276 ? -16.388 -8.624  55.371  1.00 29.68 ? 279  LEU D CD2 1 
ATOM   9695  N  N   . MET D  1 277 ? -18.395 -13.155 55.723  1.00 27.39 ? 280  MET D N   1 
ATOM   9696  C  CA  . MET D  1 277 ? -19.554 -13.571 56.488  1.00 27.38 ? 280  MET D CA  1 
ATOM   9697  C  C   . MET D  1 277 ? -19.276 -14.822 57.315  1.00 25.71 ? 280  MET D C   1 
ATOM   9698  O  O   . MET D  1 277 ? -19.690 -14.919 58.466  1.00 25.60 ? 280  MET D O   1 
ATOM   9699  C  CB  . MET D  1 277 ? -20.731 -13.805 55.551  1.00 29.66 ? 280  MET D CB  1 
ATOM   9700  C  CG  . MET D  1 277 ? -22.054 -13.840 56.268  1.00 35.83 ? 280  MET D CG  1 
ATOM   9701  S  SD  . MET D  1 277 ? -22.816 -15.455 56.117  1.00 42.53 ? 280  MET D SD  1 
ATOM   9702  C  CE  . MET D  1 277 ? -21.519 -16.518 56.689  1.00 38.33 ? 280  MET D CE  1 
ATOM   9703  N  N   . TYR D  1 278 ? -18.608 -15.802 56.717  1.00 24.57 ? 281  TYR D N   1 
ATOM   9704  C  CA  . TYR D  1 278 ? -18.182 -16.981 57.460  1.00 23.86 ? 281  TYR D CA  1 
ATOM   9705  C  C   . TYR D  1 278 ? -17.199 -16.627 58.605  1.00 25.74 ? 281  TYR D C   1 
ATOM   9706  O  O   . TYR D  1 278 ? -17.409 -17.016 59.758  1.00 24.13 ? 281  TYR D O   1 
ATOM   9707  C  CB  . TYR D  1 278 ? -17.566 -18.018 56.512  1.00 21.75 ? 281  TYR D CB  1 
ATOM   9708  C  CG  . TYR D  1 278 ? -16.713 -19.048 57.219  1.00 21.95 ? 281  TYR D CG  1 
ATOM   9709  C  CD1 . TYR D  1 278 ? -17.296 -20.072 57.966  1.00 19.74 ? 281  TYR D CD1 1 
ATOM   9710  C  CD2 . TYR D  1 278 ? -15.323 -18.996 57.153  1.00 21.03 ? 281  TYR D CD2 1 
ATOM   9711  C  CE1 . TYR D  1 278 ? -16.511 -21.020 58.626  1.00 19.90 ? 281  TYR D CE1 1 
ATOM   9712  C  CE2 . TYR D  1 278 ? -14.539 -19.905 57.839  1.00 21.39 ? 281  TYR D CE2 1 
ATOM   9713  C  CZ  . TYR D  1 278 ? -15.141 -20.912 58.583  1.00 22.56 ? 281  TYR D CZ  1 
ATOM   9714  O  OH  . TYR D  1 278 ? -14.360 -21.849 59.228  1.00 23.69 ? 281  TYR D OH  1 
ATOM   9715  N  N   . GLU D  1 279 ? -16.180 -15.821 58.317  1.00 27.40 ? 282  GLU D N   1 
ATOM   9716  C  CA  . GLU D  1 279 ? -15.188 -15.481 59.350  1.00 30.97 ? 282  GLU D CA  1 
ATOM   9717  C  C   . GLU D  1 279 ? -15.791 -14.759 60.544  1.00 31.73 ? 282  GLU D C   1 
ATOM   9718  O  O   . GLU D  1 279 ? -15.451 -15.060 61.688  1.00 32.86 ? 282  GLU D O   1 
ATOM   9719  C  CB  . GLU D  1 279 ? -14.003 -14.695 58.796  1.00 33.18 ? 282  GLU D CB  1 
ATOM   9720  C  CG  . GLU D  1 279 ? -13.097 -15.504 57.872  1.00 39.66 ? 282  GLU D CG  1 
ATOM   9721  C  CD  . GLU D  1 279 ? -11.792 -14.773 57.528  1.00 44.23 ? 282  GLU D CD  1 
ATOM   9722  O  OE1 . GLU D  1 279 ? -11.586 -13.634 58.034  1.00 46.82 ? 282  GLU D OE1 1 
ATOM   9723  O  OE2 . GLU D  1 279 ? -10.968 -15.350 56.773  1.00 42.87 ? 282  GLU D OE2 1 
ATOM   9724  N  N   . LYS D  1 280 ? -16.687 -13.814 60.287  1.00 30.36 ? 283  LYS D N   1 
ATOM   9725  C  CA  . LYS D  1 280 ? -17.297 -13.046 61.362  1.00 29.33 ? 283  LYS D CA  1 
ATOM   9726  C  C   . LYS D  1 280 ? -18.215 -13.918 62.219  1.00 30.04 ? 283  LYS D C   1 
ATOM   9727  O  O   . LYS D  1 280 ? -18.181 -13.858 63.444  1.00 30.81 ? 283  LYS D O   1 
ATOM   9728  C  CB  . LYS D  1 280 ? -18.042 -11.830 60.803  1.00 28.85 ? 283  LYS D CB  1 
ATOM   9729  C  CG  . LYS D  1 280 ? -17.113 -10.815 60.129  1.00 32.34 ? 283  LYS D CG  1 
ATOM   9730  C  CD  . LYS D  1 280 ? -17.820 -9.491  59.801  1.00 33.40 ? 283  LYS D CD  1 
ATOM   9731  C  CE  . LYS D  1 280 ? -18.303 -8.756  61.059  1.00 34.99 ? 283  LYS D CE  1 
ATOM   9732  N  NZ  . LYS D  1 280 ? -19.186 -7.568  60.740  1.00 33.85 ? 283  LYS D NZ  1 
ATOM   9733  N  N   . PHE D  1 281 ? -19.010 -14.765 61.574  1.00 29.06 ? 284  PHE D N   1 
ATOM   9734  C  CA  . PHE D  1 281 ? -19.860 -15.682 62.302  1.00 26.15 ? 284  PHE D CA  1 
ATOM   9735  C  C   . PHE D  1 281 ? -19.015 -16.503 63.272  1.00 26.87 ? 284  PHE D C   1 
ATOM   9736  O  O   . PHE D  1 281 ? -19.409 -16.746 64.402  1.00 27.75 ? 284  PHE D O   1 
ATOM   9737  C  CB  . PHE D  1 281 ? -20.586 -16.610 61.335  1.00 24.45 ? 284  PHE D CB  1 
ATOM   9738  C  CG  . PHE D  1 281 ? -21.618 -17.477 61.992  1.00 23.72 ? 284  PHE D CG  1 
ATOM   9739  C  CD1 . PHE D  1 281 ? -22.861 -16.976 62.301  1.00 23.62 ? 284  PHE D CD1 1 
ATOM   9740  C  CD2 . PHE D  1 281 ? -21.326 -18.800 62.319  1.00 25.21 ? 284  PHE D CD2 1 
ATOM   9741  C  CE1 . PHE D  1 281 ? -23.813 -17.767 62.914  1.00 24.67 ? 284  PHE D CE1 1 
ATOM   9742  C  CE2 . PHE D  1 281 ? -22.247 -19.589 62.946  1.00 23.17 ? 284  PHE D CE2 1 
ATOM   9743  C  CZ  . PHE D  1 281 ? -23.506 -19.081 63.234  1.00 26.16 ? 284  PHE D CZ  1 
ATOM   9744  N  N   . VAL D  1 282 ? -17.903 -17.017 62.780  1.00 26.41 ? 285  VAL D N   1 
ATOM   9745  C  CA  . VAL D  1 282 ? -17.078 -17.931 63.538  1.00 27.54 ? 285  VAL D CA  1 
ATOM   9746  C  C   . VAL D  1 282 ? -16.308 -17.160 64.592  1.00 30.22 ? 285  VAL D C   1 
ATOM   9747  O  O   . VAL D  1 282 ? -16.571 -17.292 65.780  1.00 30.66 ? 285  VAL D O   1 
ATOM   9748  C  CB  . VAL D  1 282 ? -16.082 -18.642 62.618  1.00 27.89 ? 285  VAL D CB  1 
ATOM   9749  C  CG1 . VAL D  1 282 ? -14.927 -19.216 63.421  1.00 29.33 ? 285  VAL D CG1 1 
ATOM   9750  C  CG2 . VAL D  1 282 ? -16.790 -19.718 61.830  1.00 26.49 ? 285  VAL D CG2 1 
ATOM   9751  N  N   . ASN D  1 283 ? -15.475 -16.232 64.135  1.00 33.79 ? 286  ASN D N   1 
ATOM   9752  C  CA  . ASN D  1 283 ? -14.498 -15.582 64.989  1.00 34.87 ? 286  ASN D CA  1 
ATOM   9753  C  C   . ASN D  1 283 ? -15.063 -14.444 65.808  1.00 34.95 ? 286  ASN D C   1 
ATOM   9754  O  O   . ASN D  1 283 ? -14.373 -13.887 66.658  1.00 36.52 ? 286  ASN D O   1 
ATOM   9755  C  CB  . ASN D  1 283 ? -13.295 -15.108 64.181  1.00 36.35 ? 286  ASN D CB  1 
ATOM   9756  C  CG  . ASN D  1 283 ? -12.080 -15.968 64.408  1.00 41.10 ? 286  ASN D CG  1 
ATOM   9757  O  OD1 . ASN D  1 283 ? -12.195 -17.182 64.603  1.00 40.91 ? 286  ASN D OD1 1 
ATOM   9758  N  ND2 . ASN D  1 283 ? -10.899 -15.353 64.366  1.00 44.07 ? 286  ASN D ND2 1 
ATOM   9759  N  N   . ILE D  1 284 ? -16.331 -14.130 65.595  1.00 35.42 ? 287  ILE D N   1 
ATOM   9760  C  CA  . ILE D  1 284 ? -16.984 -13.077 66.374  1.00 36.50 ? 287  ILE D CA  1 
ATOM   9761  C  C   . ILE D  1 284 ? -18.258 -13.561 67.045  1.00 35.66 ? 287  ILE D C   1 
ATOM   9762  O  O   . ILE D  1 284 ? -18.409 -13.450 68.259  1.00 35.73 ? 287  ILE D O   1 
ATOM   9763  C  CB  . ILE D  1 284 ? -17.328 -11.853 65.519  1.00 37.94 ? 287  ILE D CB  1 
ATOM   9764  C  CG1 . ILE D  1 284 ? -16.058 -11.219 64.977  1.00 39.67 ? 287  ILE D CG1 1 
ATOM   9765  C  CG2 . ILE D  1 284 ? -18.115 -10.831 66.339  1.00 39.84 ? 287  ILE D CG2 1 
ATOM   9766  C  CD1 . ILE D  1 284 ? -16.280 -9.822  64.432  1.00 43.58 ? 287  ILE D CD1 1 
ATOM   9767  N  N   . THR D  1 285 ? -19.206 -14.036 66.246  1.00 34.30 ? 288  THR D N   1 
ATOM   9768  C  CA  . THR D  1 285 ? -20.501 -14.454 66.784  1.00 32.64 ? 288  THR D CA  1 
ATOM   9769  C  C   . THR D  1 285 ? -20.407 -15.678 67.705  1.00 33.13 ? 288  THR D C   1 
ATOM   9770  O  O   . THR D  1 285 ? -20.897 -15.649 68.839  1.00 34.17 ? 288  THR D O   1 
ATOM   9771  C  CB  . THR D  1 285 ? -21.533 -14.676 65.664  1.00 31.23 ? 288  THR D CB  1 
ATOM   9772  O  OG1 . THR D  1 285 ? -21.689 -13.462 64.922  1.00 26.98 ? 288  THR D OG1 1 
ATOM   9773  C  CG2 . THR D  1 285 ? -22.886 -15.092 66.237  1.00 31.89 ? 288  THR D CG2 1 
ATOM   9774  N  N   . VAL D  1 286 ? -19.750 -16.734 67.236  1.00 32.08 ? 289  VAL D N   1 
ATOM   9775  C  CA  . VAL D  1 286 ? -19.526 -17.933 68.053  1.00 30.62 ? 289  VAL D CA  1 
ATOM   9776  C  C   . VAL D  1 286 ? -18.502 -17.672 69.170  1.00 33.11 ? 289  VAL D C   1 
ATOM   9777  O  O   . VAL D  1 286 ? -18.779 -17.913 70.339  1.00 33.93 ? 289  VAL D O   1 
ATOM   9778  C  CB  . VAL D  1 286 ? -19.039 -19.140 67.189  1.00 28.27 ? 289  VAL D CB  1 
ATOM   9779  C  CG1 . VAL D  1 286 ? -18.708 -20.325 68.077  1.00 27.92 ? 289  VAL D CG1 1 
ATOM   9780  C  CG2 . VAL D  1 286 ? -20.095 -19.544 66.168  1.00 25.21 ? 289  VAL D CG2 1 
ATOM   9781  N  N   . LYS D  1 287 ? -17.295 -17.252 68.794  1.00 34.18 ? 290  LYS D N   1 
ATOM   9782  C  CA  . LYS D  1 287 ? -16.284 -16.859 69.769  1.00 38.11 ? 290  LYS D CA  1 
ATOM   9783  C  C   . LYS D  1 287 ? -16.887 -16.093 70.936  1.00 39.22 ? 290  LYS D C   1 
ATOM   9784  O  O   . LYS D  1 287 ? -16.600 -16.381 72.093  1.00 39.76 ? 290  LYS D O   1 
ATOM   9785  C  CB  . LYS D  1 287 ? -15.218 -15.999 69.118  1.00 39.14 ? 290  LYS D CB  1 
ATOM   9786  C  CG  . LYS D  1 287 ? -14.073 -15.657 70.047  1.00 41.85 ? 290  LYS D CG  1 
ATOM   9787  C  CD  . LYS D  1 287 ? -13.205 -16.876 70.295  1.00 43.23 ? 290  LYS D CD  1 
ATOM   9788  C  CE  . LYS D  1 287 ? -11.752 -16.487 70.439  1.00 46.20 ? 290  LYS D CE  1 
ATOM   9789  N  NZ  . LYS D  1 287 ? -11.453 -16.128 71.846  1.00 47.60 ? 290  LYS D NZ  1 
ATOM   9790  N  N   . SER D  1 288 ? -17.725 -15.114 70.630  1.00 39.19 ? 291  SER D N   1 
ATOM   9791  C  CA  . SER D  1 288 ? -18.244 -14.238 71.659  1.00 39.24 ? 291  SER D CA  1 
ATOM   9792  C  C   . SER D  1 288 ? -19.071 -15.012 72.667  1.00 39.63 ? 291  SER D C   1 
ATOM   9793  O  O   . SER D  1 288 ? -19.056 -14.695 73.861  1.00 41.02 ? 291  SER D O   1 
ATOM   9794  C  CB  . SER D  1 288 ? -19.087 -13.118 71.051  1.00 39.38 ? 291  SER D CB  1 
ATOM   9795  O  OG  . SER D  1 288 ? -18.262 -12.047 70.629  1.00 43.79 ? 291  SER D OG  1 
ATOM   9796  N  N   . LEU D  1 289 ? -19.844 -15.979 72.180  1.00 37.74 ? 292  LEU D N   1 
ATOM   9797  C  CA  . LEU D  1 289 ? -20.759 -16.725 73.046  1.00 37.05 ? 292  LEU D CA  1 
ATOM   9798  C  C   . LEU D  1 289 ? -19.984 -17.722 73.912  1.00 36.47 ? 292  LEU D C   1 
ATOM   9799  O  O   . LEU D  1 289 ? -20.478 -18.204 74.928  1.00 39.04 ? 292  LEU D O   1 
ATOM   9800  C  CB  . LEU D  1 289 ? -21.834 -17.456 72.228  1.00 34.62 ? 292  LEU D CB  1 
ATOM   9801  C  CG  . LEU D  1 289 ? -22.812 -16.657 71.350  1.00 34.82 ? 292  LEU D CG  1 
ATOM   9802  C  CD1 . LEU D  1 289 ? -23.492 -17.570 70.322  1.00 30.99 ? 292  LEU D CD1 1 
ATOM   9803  C  CD2 . LEU D  1 289 ? -23.862 -15.904 72.178  1.00 32.33 ? 292  LEU D CD2 1 
ATOM   9804  N  N   . TYR D  1 290 ? -18.777 -18.050 73.482  1.00 35.60 ? 293  TYR D N   1 
ATOM   9805  C  CA  . TYR D  1 290 ? -17.956 -19.030 74.168  1.00 33.63 ? 293  TYR D CA  1 
ATOM   9806  C  C   . TYR D  1 290 ? -16.530 -18.521 74.246  1.00 35.30 ? 293  TYR D C   1 
ATOM   9807  O  O   . TYR D  1 290 ? -15.636 -19.099 73.626  1.00 36.86 ? 293  TYR D O   1 
ATOM   9808  C  CB  . TYR D  1 290 ? -17.968 -20.337 73.405  1.00 29.80 ? 293  TYR D CB  1 
ATOM   9809  C  CG  . TYR D  1 290 ? -19.298 -21.040 73.446  1.00 30.19 ? 293  TYR D CG  1 
ATOM   9810  C  CD1 . TYR D  1 290 ? -19.578 -21.972 74.439  1.00 28.30 ? 293  TYR D CD1 1 
ATOM   9811  C  CD2 . TYR D  1 290 ? -20.258 -20.820 72.463  1.00 28.35 ? 293  TYR D CD2 1 
ATOM   9812  C  CE1 . TYR D  1 290 ? -20.770 -22.632 74.466  1.00 28.45 ? 293  TYR D CE1 1 
ATOM   9813  C  CE2 . TYR D  1 290 ? -21.460 -21.485 72.485  1.00 25.96 ? 293  TYR D CE2 1 
ATOM   9814  C  CZ  . TYR D  1 290 ? -21.711 -22.384 73.490  1.00 27.05 ? 293  TYR D CZ  1 
ATOM   9815  O  OH  . TYR D  1 290 ? -22.901 -23.060 73.535  1.00 26.28 ? 293  TYR D OH  1 
ATOM   9816  N  N   . PRO D  1 291 ? -16.311 -17.442 75.019  1.00 36.33 ? 294  PRO D N   1 
ATOM   9817  C  CA  . PRO D  1 291 ? -15.102 -16.630 74.817  1.00 39.09 ? 294  PRO D CA  1 
ATOM   9818  C  C   . PRO D  1 291 ? -13.841 -17.339 75.305  1.00 41.47 ? 294  PRO D C   1 
ATOM   9819  O  O   . PRO D  1 291 ? -12.743 -17.055 74.828  1.00 41.72 ? 294  PRO D O   1 
ATOM   9820  C  CB  . PRO D  1 291 ? -15.372 -15.352 75.630  1.00 38.46 ? 294  PRO D CB  1 
ATOM   9821  C  CG  . PRO D  1 291 ? -16.603 -15.630 76.463  1.00 36.43 ? 294  PRO D CG  1 
ATOM   9822  C  CD  . PRO D  1 291 ? -17.351 -16.731 75.786  1.00 36.52 ? 294  PRO D CD  1 
ATOM   9823  N  N   . ASN D  1 292 ? -14.006 -18.305 76.200  1.00 43.93 ? 295  ASN D N   1 
ATOM   9824  C  CA  . ASN D  1 292 ? -13.056 -19.399 76.269  1.00 46.77 ? 295  ASN D CA  1 
ATOM   9825  C  C   . ASN D  1 292 ? -13.542 -20.588 77.073  1.00 46.49 ? 295  ASN D C   1 
ATOM   9826  O  O   . ASN D  1 292 ? -13.549 -20.568 78.304  1.00 48.42 ? 295  ASN D O   1 
ATOM   9827  C  CB  . ASN D  1 292 ? -11.667 -18.931 76.717  1.00 49.66 ? 295  ASN D CB  1 
ATOM   9828  C  CG  . ASN D  1 292 ? -11.610 -18.603 78.183  1.00 49.90 ? 295  ASN D CG  1 
ATOM   9829  O  OD1 . ASN D  1 292 ? -12.530 -18.004 78.725  1.00 53.11 ? 295  ASN D OD1 1 
ATOM   9830  N  ND2 . ASN D  1 292 ? -10.527 -18.993 78.838  1.00 49.93 ? 295  ASN D ND2 1 
ATOM   9831  N  N   . PRO D  1 293 ? -13.947 -21.641 76.362  1.00 44.87 ? 296  PRO D N   1 
ATOM   9832  C  CA  . PRO D  1 293 ? -14.695 -22.705 76.982  1.00 42.81 ? 296  PRO D CA  1 
ATOM   9833  C  C   . PRO D  1 293 ? -13.749 -23.566 77.801  1.00 42.62 ? 296  PRO D C   1 
ATOM   9834  O  O   . PRO D  1 293 ? -12.539 -23.532 77.575  1.00 41.14 ? 296  PRO D O   1 
ATOM   9835  C  CB  . PRO D  1 293 ? -15.188 -23.496 75.778  1.00 42.03 ? 296  PRO D CB  1 
ATOM   9836  C  CG  . PRO D  1 293 ? -14.069 -23.379 74.804  1.00 40.98 ? 296  PRO D CG  1 
ATOM   9837  C  CD  . PRO D  1 293 ? -13.467 -22.014 75.018  1.00 41.14 ? 296  PRO D CD  1 
ATOM   9838  N  N   . THR D  1 294 ? -14.306 -24.404 78.666  1.00 41.79 ? 297  THR D N   1 
ATOM   9839  C  CA  . THR D  1 294 ? -13.543 -25.506 79.242  1.00 44.69 ? 297  THR D CA  1 
ATOM   9840  C  C   . THR D  1 294 ? -13.011 -26.453 78.160  1.00 45.50 ? 297  THR D C   1 
ATOM   9841  O  O   . THR D  1 294 ? -13.351 -26.325 76.979  1.00 42.92 ? 297  THR D O   1 
ATOM   9842  C  CB  . THR D  1 294 ? -14.404 -26.303 80.220  1.00 45.25 ? 297  THR D CB  1 
ATOM   9843  O  OG1 . THR D  1 294 ? -15.498 -26.911 79.509  1.00 46.41 ? 297  THR D OG1 1 
ATOM   9844  C  CG2 . THR D  1 294 ? -14.941 -25.382 81.305  1.00 43.13 ? 297  THR D CG2 1 
ATOM   9845  N  N   . VAL D  1 295 ? -12.181 -27.408 78.570  1.00 47.62 ? 298  VAL D N   1 
ATOM   9846  C  CA  . VAL D  1 295 ? -11.576 -28.349 77.629  1.00 47.61 ? 298  VAL D CA  1 
ATOM   9847  C  C   . VAL D  1 295 ? -12.627 -29.094 76.796  1.00 49.16 ? 298  VAL D C   1 
ATOM   9848  O  O   . VAL D  1 295 ? -12.533 -29.132 75.564  1.00 48.34 ? 298  VAL D O   1 
ATOM   9849  C  CB  . VAL D  1 295 ? -10.644 -29.360 78.338  1.00 46.88 ? 298  VAL D CB  1 
ATOM   9850  C  CG1 . VAL D  1 295 ? -10.207 -30.464 77.384  1.00 44.49 ? 298  VAL D CG1 1 
ATOM   9851  C  CG2 . VAL D  1 295 ? -9.429  -28.642 78.947  1.00 47.91 ? 298  VAL D CG2 1 
ATOM   9852  N  N   . GLN D  1 296 ? -13.614 -29.694 77.463  1.00 49.07 ? 299  GLN D N   1 
ATOM   9853  C  CA  . GLN D  1 296 ? -14.618 -30.502 76.761  1.00 47.81 ? 299  GLN D CA  1 
ATOM   9854  C  C   . GLN D  1 296 ? -15.488 -29.661 75.825  1.00 44.95 ? 299  GLN D C   1 
ATOM   9855  O  O   . GLN D  1 296 ? -15.769 -30.067 74.701  1.00 44.16 ? 299  GLN D O   1 
ATOM   9856  C  CB  . GLN D  1 296 ? -15.490 -31.314 77.735  1.00 48.57 ? 299  GLN D CB  1 
ATOM   9857  C  CG  . GLN D  1 296 ? -15.938 -32.668 77.167  1.00 51.30 ? 299  GLN D CG  1 
ATOM   9858  C  CD  . GLN D  1 296 ? -17.125 -33.283 77.916  1.00 55.00 ? 299  GLN D CD  1 
ATOM   9859  O  OE1 . GLN D  1 296 ? -17.206 -33.211 79.141  1.00 56.77 ? 299  GLN D OE1 1 
ATOM   9860  N  NE2 . GLN D  1 296 ? -18.031 -33.924 77.178  1.00 56.22 ? 299  GLN D NE2 1 
ATOM   9861  N  N   . LEU D  1 297 ? -15.894 -28.484 76.285  1.00 43.18 ? 300  LEU D N   1 
ATOM   9862  C  CA  . LEU D  1 297 ? -16.643 -27.558 75.451  1.00 43.38 ? 300  LEU D CA  1 
ATOM   9863  C  C   . LEU D  1 297 ? -15.832 -27.073 74.241  1.00 44.52 ? 300  LEU D C   1 
ATOM   9864  O  O   . LEU D  1 297 ? -16.375 -26.868 73.153  1.00 43.40 ? 300  LEU D O   1 
ATOM   9865  C  CB  . LEU D  1 297 ? -17.096 -26.363 76.280  1.00 44.21 ? 300  LEU D CB  1 
ATOM   9866  C  CG  . LEU D  1 297 ? -18.445 -25.773 75.874  1.00 44.64 ? 300  LEU D CG  1 
ATOM   9867  C  CD1 . LEU D  1 297 ? -19.432 -26.887 75.570  1.00 43.13 ? 300  LEU D CD1 1 
ATOM   9868  C  CD2 . LEU D  1 297 ? -18.987 -24.843 76.955  1.00 45.04 ? 300  LEU D CD2 1 
ATOM   9869  N  N   . ARG D  1 298 ? -14.536 -26.874 74.451  1.00 44.71 ? 301  ARG D N   1 
ATOM   9870  C  CA  . ARG D  1 298 ? -13.619 -26.562 73.374  1.00 44.90 ? 301  ARG D CA  1 
ATOM   9871  C  C   . ARG D  1 298 ? -13.627 -27.643 72.296  1.00 43.94 ? 301  ARG D C   1 
ATOM   9872  O  O   . ARG D  1 298 ? -13.720 -27.339 71.109  1.00 42.76 ? 301  ARG D O   1 
ATOM   9873  C  CB  . ARG D  1 298 ? -12.209 -26.359 73.926  1.00 48.40 ? 301  ARG D CB  1 
ATOM   9874  C  CG  . ARG D  1 298 ? -11.236 -25.780 72.921  1.00 52.43 ? 301  ARG D CG  1 
ATOM   9875  C  CD  . ARG D  1 298 ? -9.840  -25.613 73.505  1.00 54.87 ? 301  ARG D CD  1 
ATOM   9876  N  NE  . ARG D  1 298 ? -8.859  -25.481 72.435  1.00 57.38 ? 301  ARG D NE  1 
ATOM   9877  C  CZ  . ARG D  1 298 ? -8.550  -26.464 71.593  1.00 60.14 ? 301  ARG D CZ  1 
ATOM   9878  N  NH1 . ARG D  1 298 ? -9.109  -27.661 71.737  1.00 61.91 ? 301  ARG D NH1 1 
ATOM   9879  N  NH2 . ARG D  1 298 ? -7.689  -26.255 70.603  1.00 59.91 ? 301  ARG D NH2 1 
ATOM   9880  N  N   . LYS D  1 299 ? -13.587 -28.905 72.707  1.00 42.15 ? 302  LYS D N   1 
ATOM   9881  C  CA  . LYS D  1 299 ? -13.618 -30.013 71.747  1.00 42.35 ? 302  LYS D CA  1 
ATOM   9882  C  C   . LYS D  1 299 ? -14.938 -30.107 70.969  1.00 38.58 ? 302  LYS D C   1 
ATOM   9883  O  O   . LYS D  1 299 ? -14.943 -30.398 69.774  1.00 36.69 ? 302  LYS D O   1 
ATOM   9884  C  CB  . LYS D  1 299 ? -13.306 -31.347 72.434  1.00 46.97 ? 302  LYS D CB  1 
ATOM   9885  C  CG  . LYS D  1 299 ? -12.106 -32.095 71.848  1.00 52.40 ? 302  LYS D CG  1 
ATOM   9886  C  CD  . LYS D  1 299 ? -12.428 -32.707 70.475  1.00 55.28 ? 302  LYS D CD  1 
ATOM   9887  C  CE  . LYS D  1 299 ? -11.984 -31.784 69.322  1.00 55.87 ? 302  LYS D CE  1 
ATOM   9888  N  NZ  . LYS D  1 299 ? -13.111 -31.410 68.413  1.00 53.24 ? 302  LYS D NZ  1 
ATOM   9889  N  N   . ALA D  1 300 ? -16.053 -29.873 71.651  1.00 32.76 ? 303  ALA D N   1 
ATOM   9890  C  CA  . ALA D  1 300 ? -17.344 -29.825 70.981  1.00 31.80 ? 303  ALA D CA  1 
ATOM   9891  C  C   . ALA D  1 300 ? -17.443 -28.657 69.999  1.00 30.32 ? 303  ALA D C   1 
ATOM   9892  O  O   . ALA D  1 300 ? -18.013 -28.792 68.921  1.00 29.69 ? 303  ALA D O   1 
ATOM   9893  C  CB  . ALA D  1 300 ? -18.477 -29.764 71.981  1.00 27.56 ? 303  ALA D CB  1 
ATOM   9894  N  N   . LEU D  1 301 ? -16.888 -27.512 70.382  1.00 30.12 ? 304  LEU D N   1 
ATOM   9895  C  CA  . LEU D  1 301 ? -16.940 -26.331 69.552  1.00 26.16 ? 304  LEU D CA  1 
ATOM   9896  C  C   . LEU D  1 301 ? -16.136 -26.547 68.264  1.00 27.66 ? 304  LEU D C   1 
ATOM   9897  O  O   . LEU D  1 301 ? -16.637 -26.335 67.146  1.00 26.11 ? 304  LEU D O   1 
ATOM   9898  C  CB  . LEU D  1 301 ? -16.428 -25.129 70.332  1.00 26.47 ? 304  LEU D CB  1 
ATOM   9899  C  CG  . LEU D  1 301 ? -17.496 -24.403 71.143  1.00 25.34 ? 304  LEU D CG  1 
ATOM   9900  C  CD1 . LEU D  1 301 ? -16.880 -23.686 72.345  1.00 25.60 ? 304  LEU D CD1 1 
ATOM   9901  C  CD2 . LEU D  1 301 ? -18.231 -23.418 70.244  1.00 25.67 ? 304  LEU D CD2 1 
ATOM   9902  N  N   . ASN D  1 302 ? -14.941 -27.095 68.416  1.00 26.39 ? 305  ASN D N   1 
ATOM   9903  C  CA  . ASN D  1 302 ? -14.095 -27.378 67.274  1.00 29.67 ? 305  ASN D CA  1 
ATOM   9904  C  C   . ASN D  1 302 ? -14.690 -28.415 66.322  1.00 32.12 ? 305  ASN D C   1 
ATOM   9905  O  O   . ASN D  1 302 ? -14.545 -28.294 65.101  1.00 31.95 ? 305  ASN D O   1 
ATOM   9906  C  CB  . ASN D  1 302 ? -12.672 -27.755 67.724  1.00 30.73 ? 305  ASN D CB  1 
ATOM   9907  C  CG  . ASN D  1 302 ? -11.819 -26.515 68.099  1.00 33.34 ? 305  ASN D CG  1 
ATOM   9908  O  OD1 . ASN D  1 302 ? -11.962 -25.445 67.505  1.00 36.19 ? 305  ASN D OD1 1 
ATOM   9909  N  ND2 . ASN D  1 302 ? -10.947 -26.666 69.089  1.00 31.76 ? 305  ASN D ND2 1 
ATOM   9910  N  N   . THR D  1 303 ? -15.379 -29.414 66.872  1.00 31.83 ? 306  THR D N   1 
ATOM   9911  C  CA  . THR D  1 303 ? -15.993 -30.468 66.055  1.00 32.20 ? 306  THR D CA  1 
ATOM   9912  C  C   . THR D  1 303 ? -17.128 -29.911 65.213  1.00 31.59 ? 306  THR D C   1 
ATOM   9913  O  O   . THR D  1 303 ? -17.220 -30.172 64.023  1.00 36.15 ? 306  THR D O   1 
ATOM   9914  C  CB  . THR D  1 303 ? -16.558 -31.615 66.932  1.00 33.84 ? 306  THR D CB  1 
ATOM   9915  O  OG1 . THR D  1 303 ? -15.472 -32.375 67.466  1.00 36.19 ? 306  THR D OG1 1 
ATOM   9916  C  CG2 . THR D  1 303 ? -17.472 -32.554 66.115  1.00 33.26 ? 306  THR D CG2 1 
ATOM   9917  N  N   . ASN D  1 304 ? -18.018 -29.162 65.841  1.00 31.89 ? 307  ASN D N   1 
ATOM   9918  C  CA  . ASN D  1 304 ? -19.104 -28.535 65.112  1.00 30.98 ? 307  ASN D CA  1 
ATOM   9919  C  C   . ASN D  1 304 ? -18.651 -27.425 64.129  1.00 30.73 ? 307  ASN D C   1 
ATOM   9920  O  O   . ASN D  1 304 ? -19.166 -27.336 63.008  1.00 28.65 ? 307  ASN D O   1 
ATOM   9921  C  CB  . ASN D  1 304 ? -20.180 -28.046 66.087  1.00 31.10 ? 307  ASN D CB  1 
ATOM   9922  C  CG  . ASN D  1 304 ? -20.869 -29.191 66.811  1.00 30.89 ? 307  ASN D CG  1 
ATOM   9923  O  OD1 . ASN D  1 304 ? -21.851 -29.754 66.327  1.00 30.81 ? 307  ASN D OD1 1 
ATOM   9924  N  ND2 . ASN D  1 304 ? -20.337 -29.557 67.968  1.00 28.67 ? 307  ASN D ND2 1 
ATOM   9925  N  N   . LEU D  1 305 ? -17.627 -26.659 64.508  1.00 26.02 ? 308  LEU D N   1 
ATOM   9926  C  CA  . LEU D  1 305 ? -17.035 -25.688 63.594  1.00 25.85 ? 308  LEU D CA  1 
ATOM   9927  C  C   . LEU D  1 305 ? -16.475 -26.371 62.356  1.00 27.92 ? 308  LEU D C   1 
ATOM   9928  O  O   . LEU D  1 305 ? -16.656 -25.883 61.236  1.00 26.86 ? 308  LEU D O   1 
ATOM   9929  C  CB  . LEU D  1 305 ? -15.960 -24.833 64.280  1.00 22.76 ? 308  LEU D CB  1 
ATOM   9930  C  CG  . LEU D  1 305 ? -16.466 -23.833 65.331  1.00 23.39 ? 308  LEU D CG  1 
ATOM   9931  C  CD1 . LEU D  1 305 ? -15.327 -23.308 66.240  1.00 23.65 ? 308  LEU D CD1 1 
ATOM   9932  C  CD2 . LEU D  1 305 ? -17.226 -22.670 64.710  1.00 23.57 ? 308  LEU D CD2 1 
ATOM   9933  N  N   . ASP D  1 306 ? -15.798 -27.500 62.561  1.00 28.66 ? 309  ASP D N   1 
ATOM   9934  C  CA  . ASP D  1 306 ? -15.319 -28.302 61.455  1.00 30.59 ? 309  ASP D CA  1 
ATOM   9935  C  C   . ASP D  1 306 ? -16.448 -28.657 60.499  1.00 32.84 ? 309  ASP D C   1 
ATOM   9936  O  O   . ASP D  1 306 ? -16.304 -28.547 59.274  1.00 32.01 ? 309  ASP D O   1 
ATOM   9937  C  CB  . ASP D  1 306 ? -14.663 -29.578 61.965  1.00 34.04 ? 309  ASP D CB  1 
ATOM   9938  C  CG  . ASP D  1 306 ? -13.312 -29.319 62.600  1.00 35.97 ? 309  ASP D CG  1 
ATOM   9939  O  OD1 . ASP D  1 306 ? -12.913 -28.139 62.683  1.00 36.01 ? 309  ASP D OD1 1 
ATOM   9940  O  OD2 . ASP D  1 306 ? -12.646 -30.295 63.006  1.00 38.47 ? 309  ASP D OD2 1 
ATOM   9941  N  N   . PHE D  1 307 ? -17.556 -29.129 61.061  1.00 33.22 ? 310  PHE D N   1 
ATOM   9942  C  CA  . PHE D  1 307 ? -18.664 -29.581 60.247  1.00 30.58 ? 310  PHE D CA  1 
ATOM   9943  C  C   . PHE D  1 307 ? -19.255 -28.377 59.534  1.00 29.43 ? 310  PHE D C   1 
ATOM   9944  O  O   . PHE D  1 307 ? -19.554 -28.447 58.352  1.00 29.04 ? 310  PHE D O   1 
ATOM   9945  C  CB  . PHE D  1 307 ? -19.720 -30.257 61.109  1.00 31.42 ? 310  PHE D CB  1 
ATOM   9946  C  CG  . PHE D  1 307 ? -19.264 -31.546 61.722  1.00 34.95 ? 310  PHE D CG  1 
ATOM   9947  C  CD1 . PHE D  1 307 ? -18.370 -32.366 61.058  1.00 36.87 ? 310  PHE D CD1 1 
ATOM   9948  C  CD2 . PHE D  1 307 ? -19.765 -31.966 62.940  1.00 34.94 ? 310  PHE D CD2 1 
ATOM   9949  C  CE1 . PHE D  1 307 ? -17.947 -33.563 61.620  1.00 37.40 ? 310  PHE D CE1 1 
ATOM   9950  C  CE2 . PHE D  1 307 ? -19.366 -33.179 63.493  1.00 36.70 ? 310  PHE D CE2 1 
ATOM   9951  C  CZ  . PHE D  1 307 ? -18.466 -33.979 62.825  1.00 35.66 ? 310  PHE D CZ  1 
ATOM   9952  N  N   . PHE D  1 308 ? -19.445 -27.291 60.279  1.00 27.34 ? 311  PHE D N   1 
ATOM   9953  C  CA  . PHE D  1 308 ? -19.969 -26.039 59.748  1.00 25.43 ? 311  PHE D CA  1 
ATOM   9954  C  C   . PHE D  1 308 ? -19.198 -25.580 58.503  1.00 28.31 ? 311  PHE D C   1 
ATOM   9955  O  O   . PHE D  1 308 ? -19.794 -25.228 57.467  1.00 29.88 ? 311  PHE D O   1 
ATOM   9956  C  CB  . PHE D  1 308 ? -19.938 -24.947 60.828  1.00 21.88 ? 311  PHE D CB  1 
ATOM   9957  C  CG  . PHE D  1 308 ? -20.339 -23.574 60.328  1.00 22.35 ? 311  PHE D CG  1 
ATOM   9958  C  CD1 . PHE D  1 308 ? -21.534 -23.392 59.649  1.00 20.09 ? 311  PHE D CD1 1 
ATOM   9959  C  CD2 . PHE D  1 308 ? -19.504 -22.470 60.512  1.00 20.90 ? 311  PHE D CD2 1 
ATOM   9960  C  CE1 . PHE D  1 308 ? -21.925 -22.125 59.213  1.00 20.69 ? 311  PHE D CE1 1 
ATOM   9961  C  CE2 . PHE D  1 308 ? -19.886 -21.200 60.061  1.00 24.11 ? 311  PHE D CE2 1 
ATOM   9962  C  CZ  . PHE D  1 308 ? -21.100 -21.031 59.415  1.00 18.95 ? 311  PHE D CZ  1 
ATOM   9963  N  N   . PHE D  1 309 ? -17.875 -25.581 58.602  1.00 24.70 ? 312  PHE D N   1 
ATOM   9964  C  CA  . PHE D  1 309 ? -17.055 -25.101 57.509  1.00 24.79 ? 312  PHE D CA  1 
ATOM   9965  C  C   . PHE D  1 309 ? -17.288 -25.946 56.259  1.00 26.51 ? 312  PHE D C   1 
ATOM   9966  O  O   . PHE D  1 309 ? -17.151 -25.454 55.129  1.00 27.05 ? 312  PHE D O   1 
ATOM   9967  C  CB  . PHE D  1 309 ? -15.572 -25.120 57.891  1.00 24.07 ? 312  PHE D CB  1 
ATOM   9968  C  CG  . PHE D  1 309 ? -14.653 -24.856 56.737  1.00 22.82 ? 312  PHE D CG  1 
ATOM   9969  C  CD1 . PHE D  1 309 ? -14.586 -23.589 56.161  1.00 21.52 ? 312  PHE D CD1 1 
ATOM   9970  C  CD2 . PHE D  1 309 ? -13.927 -25.886 56.173  1.00 23.01 ? 312  PHE D CD2 1 
ATOM   9971  C  CE1 . PHE D  1 309 ? -13.760 -23.339 55.099  1.00 21.23 ? 312  PHE D CE1 1 
ATOM   9972  C  CE2 . PHE D  1 309 ? -13.126 -25.653 55.071  1.00 24.42 ? 312  PHE D CE2 1 
ATOM   9973  C  CZ  . PHE D  1 309 ? -13.001 -24.374 54.564  1.00 22.37 ? 312  PHE D CZ  1 
ATOM   9974  N  N   . GLN D  1 310 ? -17.641 -27.215 56.459  1.00 24.38 ? 313  GLN D N   1 
ATOM   9975  C  CA  A GLN D  1 310 ? -17.879 -28.182 55.381  0.50 24.84 ? 313  GLN D CA  1 
ATOM   9976  C  CA  B GLN D  1 310 ? -17.782 -28.079 55.307  0.50 25.59 ? 313  GLN D CA  1 
ATOM   9977  C  C   . GLN D  1 310 ? -19.055 -27.747 54.523  1.00 23.56 ? 313  GLN D C   1 
ATOM   9978  O  O   . GLN D  1 310 ? -19.159 -28.069 53.352  1.00 22.93 ? 313  GLN D O   1 
ATOM   9979  C  CB  A GLN D  1 310 ? -18.206 -29.558 55.968  0.50 24.76 ? 313  GLN D CB  1 
ATOM   9980  C  CB  B GLN D  1 310 ? -17.670 -29.560 55.686  0.50 25.91 ? 313  GLN D CB  1 
ATOM   9981  C  CG  A GLN D  1 310 ? -17.018 -30.427 56.318  0.50 24.64 ? 313  GLN D CG  1 
ATOM   9982  C  CG  B GLN D  1 310 ? -16.640 -30.342 54.854  0.50 28.36 ? 313  GLN D CG  1 
ATOM   9983  C  CD  A GLN D  1 310 ? -17.445 -31.733 56.971  0.50 26.63 ? 313  GLN D CD  1 
ATOM   9984  C  CD  B GLN D  1 310 ? -15.327 -29.574 54.599  0.50 28.46 ? 313  GLN D CD  1 
ATOM   9985  O  OE1 A GLN D  1 310 ? -18.517 -32.256 56.681  0.50 25.67 ? 313  GLN D OE1 1 
ATOM   9986  O  OE1 B GLN D  1 310 ? -14.404 -29.606 55.412  0.50 26.24 ? 313  GLN D OE1 1 
ATOM   9987  N  NE2 A GLN D  1 310 ? -16.629 -32.234 57.900  0.50 28.53 ? 313  GLN D NE2 1 
ATOM   9988  N  NE2 B GLN D  1 310 ? -15.224 -28.952 53.431  0.50 28.65 ? 313  GLN D NE2 1 
ATOM   9989  N  N   . GLY D  1 311 ? -19.949 -26.996 55.132  1.00 23.19 ? 314  GLY D N   1 
ATOM   9990  C  CA  . GLY D  1 311 ? -21.172 -26.611 54.472  1.00 22.86 ? 314  GLY D CA  1 
ATOM   9991  C  C   . GLY D  1 311 ? -21.077 -25.311 53.712  1.00 24.40 ? 314  GLY D C   1 
ATOM   9992  O  O   . GLY D  1 311 ? -22.019 -24.937 53.022  1.00 26.67 ? 314  GLY D O   1 
ATOM   9993  N  N   . VAL D  1 312 ? -19.946 -24.613 53.824  1.00 24.75 ? 315  VAL D N   1 
ATOM   9994  C  CA  . VAL D  1 312 ? -19.814 -23.310 53.166  1.00 22.51 ? 315  VAL D CA  1 
ATOM   9995  C  C   . VAL D  1 312 ? -19.510 -23.491 51.693  1.00 23.80 ? 315  VAL D C   1 
ATOM   9996  O  O   . VAL D  1 312 ? -18.427 -23.942 51.328  1.00 24.68 ? 315  VAL D O   1 
ATOM   9997  C  CB  . VAL D  1 312 ? -18.695 -22.452 53.771  1.00 24.61 ? 315  VAL D CB  1 
ATOM   9998  C  CG1 . VAL D  1 312 ? -18.720 -21.044 53.136  1.00 22.97 ? 315  VAL D CG1 1 
ATOM   9999  C  CG2 . VAL D  1 312 ? -18.835 -22.380 55.307  1.00 22.60 ? 315  VAL D CG2 1 
ATOM   10000 N  N   . ALA D  1 313 ? -20.492 -23.187 50.854  1.00 25.67 ? 316  ALA D N   1 
ATOM   10001 C  CA  . ALA D  1 313 ? -20.452 -23.595 49.444  1.00 30.08 ? 316  ALA D CA  1 
ATOM   10002 C  C   . ALA D  1 313 ? -19.462 -22.755 48.614  1.00 28.10 ? 316  ALA D C   1 
ATOM   10003 O  O   . ALA D  1 313 ? -18.849 -23.253 47.681  1.00 29.65 ? 316  ALA D O   1 
ATOM   10004 C  CB  . ALA D  1 313 ? -21.871 -23.538 48.834  1.00 26.98 ? 316  ALA D CB  1 
ATOM   10005 N  N   . ALA D  1 314 ? -19.247 -21.513 49.024  1.00 23.98 ? 317  ALA D N   1 
ATOM   10006 C  CA  . ALA D  1 314 ? -18.299 -20.626 48.352  1.00 26.23 ? 317  ALA D CA  1 
ATOM   10007 C  C   . ALA D  1 314 ? -16.854 -21.114 48.396  1.00 25.26 ? 317  ALA D C   1 
ATOM   10008 O  O   . ALA D  1 314 ? -16.070 -20.829 47.499  1.00 28.37 ? 317  ALA D O   1 
ATOM   10009 C  CB  . ALA D  1 314 ? -18.399 -19.218 48.924  1.00 24.34 ? 317  ALA D CB  1 
ATOM   10010 N  N   . GLY D  1 315 ? -16.523 -21.923 49.391  1.00 25.44 ? 318  GLY D N   1 
ATOM   10011 C  CA  . GLY D  1 315 ? -15.148 -22.352 49.564  1.00 25.65 ? 318  GLY D CA  1 
ATOM   10012 C  C   . GLY D  1 315 ? -14.606 -21.728 50.829  1.00 25.85 ? 318  GLY D C   1 
ATOM   10013 O  O   . GLY D  1 315 ? -14.943 -22.167 51.930  1.00 27.52 ? 318  GLY D O   1 
ATOM   10014 N  N   . CYS D  1 316 ? -13.815 -20.672 50.677  1.00 23.67 ? 319  CYS D N   1 
ATOM   10015 C  CA  . CYS D  1 316 ? -13.302 -19.925 51.826  1.00 24.16 ? 319  CYS D CA  1 
ATOM   10016 C  C   . CYS D  1 316 ? -12.188 -20.690 52.538  1.00 22.54 ? 319  CYS D C   1 
ATOM   10017 O  O   . CYS D  1 316 ? -11.884 -21.810 52.186  1.00 23.16 ? 319  CYS D O   1 
ATOM   10018 C  CB  . CYS D  1 316 ? -14.447 -19.594 52.792  1.00 23.00 ? 319  CYS D CB  1 
ATOM   10019 S  SG  . CYS D  1 316 ? -15.754 -18.595 52.001  1.00 27.66 ? 319  CYS D SG  1 
ATOM   10020 N  N   . THR D  1 317 ? -11.544 -20.054 53.503  1.00 26.76 ? 320  THR D N   1 
ATOM   10021 C  CA  . THR D  1 317 ? -10.415 -20.650 54.218  1.00 26.75 ? 320  THR D CA  1 
ATOM   10022 C  C   . THR D  1 317 ? -10.912 -20.811 55.642  1.00 26.48 ? 320  THR D C   1 
ATOM   10023 O  O   . THR D  1 317 ? -11.567 -19.914 56.157  1.00 24.28 ? 320  THR D O   1 
ATOM   10024 C  CB  . THR D  1 317 ? -9.198  -19.689 54.241  1.00 29.65 ? 320  THR D CB  1 
ATOM   10025 O  OG1 . THR D  1 317 ? -8.768  -19.421 52.904  1.00 29.56 ? 320  THR D OG1 1 
ATOM   10026 C  CG2 . THR D  1 317 ? -8.021  -20.271 55.042  1.00 28.89 ? 320  THR D CG2 1 
ATOM   10027 N  N   . GLN D  1 318 ? -10.726 -21.993 56.225  1.00 24.88 ? 321  GLN D N   1 
ATOM   10028 C  CA  . GLN D  1 318 ? -11.289 -22.246 57.536  1.00 25.83 ? 321  GLN D CA  1 
ATOM   10029 C  C   . GLN D  1 318 ? -10.587 -21.349 58.537  1.00 25.36 ? 321  GLN D C   1 
ATOM   10030 O  O   . GLN D  1 318 ? -9.379  -21.150 58.442  1.00 25.27 ? 321  GLN D O   1 
ATOM   10031 C  CB  . GLN D  1 318 ? -11.132 -23.715 57.940  1.00 26.31 ? 321  GLN D CB  1 
ATOM   10032 C  CG  . GLN D  1 318 ? -11.840 -24.044 59.247  1.00 23.72 ? 321  GLN D CG  1 
ATOM   10033 C  CD  . GLN D  1 318 ? -11.841 -25.522 59.565  1.00 25.50 ? 321  GLN D CD  1 
ATOM   10034 O  OE1 . GLN D  1 318 ? -11.398 -26.342 58.765  1.00 26.37 ? 321  GLN D OE1 1 
ATOM   10035 N  NE2 . GLN D  1 318 ? -12.387 -25.874 60.724  1.00 27.21 ? 321  GLN D NE2 1 
ATOM   10036 N  N   . VAL D  1 319 ? -11.356 -20.733 59.431  1.00 25.76 ? 322  VAL D N   1 
ATOM   10037 C  CA  . VAL D  1 319 ? -10.755 -19.995 60.530  1.00 29.11 ? 322  VAL D CA  1 
ATOM   10038 C  C   . VAL D  1 319 ? -10.970 -20.689 61.879  1.00 31.52 ? 322  VAL D C   1 
ATOM   10039 O  O   . VAL D  1 319 ? -11.904 -21.484 62.049  1.00 32.83 ? 322  VAL D O   1 
ATOM   10040 C  CB  . VAL D  1 319 ? -11.239 -18.535 60.595  1.00 29.10 ? 322  VAL D CB  1 
ATOM   10041 C  CG1 . VAL D  1 319 ? -11.330 -17.929 59.187  1.00 29.16 ? 322  VAL D CG1 1 
ATOM   10042 C  CG2 . VAL D  1 319 ? -12.551 -18.458 61.319  1.00 25.51 ? 322  VAL D CG2 1 
ATOM   10043 N  N   . PHE D  1 320 ? -10.054 -20.434 62.811  1.00 32.57 ? 323  PHE D N   1 
ATOM   10044 C  CA  . PHE D  1 320 ? -9.845  -21.316 63.964  1.00 31.74 ? 323  PHE D CA  1 
ATOM   10045 C  C   . PHE D  1 320 ? -9.822  -20.524 65.267  1.00 32.76 ? 323  PHE D C   1 
ATOM   10046 O  O   . PHE D  1 320 ? -8.751  -20.265 65.819  1.00 36.48 ? 323  PHE D O   1 
ATOM   10047 C  CB  . PHE D  1 320 ? -8.537  -22.096 63.796  1.00 26.56 ? 323  PHE D CB  1 
ATOM   10048 C  CG  . PHE D  1 320 ? -8.621  -23.191 62.772  1.00 28.44 ? 323  PHE D CG  1 
ATOM   10049 C  CD1 . PHE D  1 320 ? -9.403  -24.314 63.002  1.00 26.42 ? 323  PHE D CD1 1 
ATOM   10050 C  CD2 . PHE D  1 320 ? -8.009  -23.056 61.540  1.00 27.79 ? 323  PHE D CD2 1 
ATOM   10051 C  CE1 . PHE D  1 320 ? -9.501  -25.314 62.057  1.00 26.89 ? 323  PHE D CE1 1 
ATOM   10052 C  CE2 . PHE D  1 320 ? -8.115  -24.056 60.584  1.00 25.29 ? 323  PHE D CE2 1 
ATOM   10053 C  CZ  . PHE D  1 320 ? -8.846  -25.188 60.845  1.00 25.68 ? 323  PHE D CZ  1 
ATOM   10054 N  N   . PRO D  1 321 ? -11.005 -20.152 65.770  1.00 31.67 ? 324  PRO D N   1 
ATOM   10055 C  CA  . PRO D  1 321 ? -11.093 -19.265 66.928  1.00 33.23 ? 324  PRO D CA  1 
ATOM   10056 C  C   . PRO D  1 321 ? -10.445 -19.846 68.195  1.00 36.09 ? 324  PRO D C   1 
ATOM   10057 O  O   . PRO D  1 321 ? -10.222 -19.109 69.153  1.00 37.29 ? 324  PRO D O   1 
ATOM   10058 C  CB  . PRO D  1 321 ? -12.603 -19.120 67.135  1.00 31.45 ? 324  PRO D CB  1 
ATOM   10059 C  CG  . PRO D  1 321 ? -13.152 -20.424 66.686  1.00 31.16 ? 324  PRO D CG  1 
ATOM   10060 C  CD  . PRO D  1 321 ? -12.267 -20.881 65.540  1.00 32.33 ? 324  PRO D CD  1 
ATOM   10061 N  N   . TYR D  1 322 ? -10.161 -21.148 68.210  1.00 38.85 ? 325  TYR D N   1 
ATOM   10062 C  CA  . TYR D  1 322 ? -9.553  -21.791 69.389  1.00 40.17 ? 325  TYR D CA  1 
ATOM   10063 C  C   . TYR D  1 322 ? -8.268  -22.559 69.036  1.00 44.39 ? 325  TYR D C   1 
ATOM   10064 O  O   . TYR D  1 322 ? -7.762  -23.349 69.840  1.00 44.72 ? 325  TYR D O   1 
ATOM   10065 C  CB  . TYR D  1 322 ? -10.549 -22.736 70.079  1.00 37.45 ? 325  TYR D CB  1 
ATOM   10066 C  CG  . TYR D  1 322 ? -11.900 -22.116 70.385  1.00 35.77 ? 325  TYR D CG  1 
ATOM   10067 C  CD1 . TYR D  1 322 ? -12.023 -21.075 71.300  1.00 37.95 ? 325  TYR D CD1 1 
ATOM   10068 C  CD2 . TYR D  1 322 ? -13.042 -22.531 69.717  1.00 34.34 ? 325  TYR D CD2 1 
ATOM   10069 C  CE1 . TYR D  1 322 ? -13.263 -20.482 71.558  1.00 36.27 ? 325  TYR D CE1 1 
ATOM   10070 C  CE2 . TYR D  1 322 ? -14.275 -21.937 69.954  1.00 33.25 ? 325  TYR D CE2 1 
ATOM   10071 C  CZ  . TYR D  1 322 ? -14.382 -20.928 70.882  1.00 35.18 ? 325  TYR D CZ  1 
ATOM   10072 O  OH  . TYR D  1 322 ? -15.605 -20.343 71.113  1.00 37.84 ? 325  TYR D OH  1 
ATOM   10073 N  N   . GLY D  1 323 ? -7.763  -22.352 67.822  1.00 47.22 ? 326  GLY D N   1 
ATOM   10074 C  CA  . GLY D  1 323 ? -6.641  -23.142 67.308  1.00 48.91 ? 326  GLY D CA  1 
ATOM   10075 C  C   . GLY D  1 323 ? -7.073  -24.442 66.645  1.00 50.25 ? 326  GLY D C   1 
ATOM   10076 O  O   . GLY D  1 323 ? -6.272  -25.117 65.982  1.00 51.25 ? 326  GLY D O   1 
HETATM 10077 C  CHA . HEM E  2 .   ? 20.605  -25.022 39.447  1.00 20.57 ? 350  HEM A CHA 1 
HETATM 10078 C  CHB . HEM E  2 .   ? 24.321  -27.467 41.346  1.00 20.67 ? 350  HEM A CHB 1 
HETATM 10079 C  CHC . HEM E  2 .   ? 24.294  -30.564 37.688  1.00 21.75 ? 350  HEM A CHC 1 
HETATM 10080 C  CHD . HEM E  2 .   ? 20.193  -28.515 36.082  1.00 17.59 ? 350  HEM A CHD 1 
HETATM 10081 C  C1A . HEM E  2 .   ? 21.646  -25.424 40.245  1.00 20.67 ? 350  HEM A C1A 1 
HETATM 10082 C  C2A . HEM E  2 .   ? 21.971  -24.817 41.512  1.00 16.85 ? 350  HEM A C2A 1 
HETATM 10083 C  C3A . HEM E  2 .   ? 22.940  -25.543 42.067  1.00 18.43 ? 350  HEM A C3A 1 
HETATM 10084 C  C4A . HEM E  2 .   ? 23.285  -26.600 41.149  1.00 18.44 ? 350  HEM A C4A 1 
HETATM 10085 C  CMA . HEM E  2 .   ? 23.638  -25.261 43.431  1.00 13.88 ? 350  HEM A CMA 1 
HETATM 10086 C  CAA . HEM E  2 .   ? 21.232  -23.643 42.176  1.00 17.54 ? 350  HEM A CAA 1 
HETATM 10087 C  CBA . HEM E  2 .   ? 21.535  -22.302 41.509  1.00 19.15 ? 350  HEM A CBA 1 
HETATM 10088 C  CGA . HEM E  2 .   ? 20.313  -21.397 41.577  1.00 18.83 ? 350  HEM A CGA 1 
HETATM 10089 O  O1A . HEM E  2 .   ? 20.154  -20.609 42.548  1.00 20.71 ? 350  HEM A O1A 1 
HETATM 10090 O  O2A . HEM E  2 .   ? 19.439  -21.498 40.672  1.00 19.72 ? 350  HEM A O2A 1 
HETATM 10091 C  C1B . HEM E  2 .   ? 24.703  -28.455 40.498  1.00 19.92 ? 350  HEM A C1B 1 
HETATM 10092 C  C2B . HEM E  2 .   ? 25.820  -29.359 40.694  1.00 20.40 ? 350  HEM A C2B 1 
HETATM 10093 C  C3B . HEM E  2 .   ? 25.801  -30.221 39.685  1.00 17.22 ? 350  HEM A C3B 1 
HETATM 10094 C  C4B . HEM E  2 .   ? 24.704  -29.871 38.803  1.00 19.23 ? 350  HEM A C4B 1 
HETATM 10095 C  CMB . HEM E  2 .   ? 26.857  -29.359 41.858  1.00 18.22 ? 350  HEM A CMB 1 
HETATM 10096 C  CAB . HEM E  2 .   ? 26.833  -31.347 39.482  1.00 16.17 ? 350  HEM A CAB 1 
HETATM 10097 C  CBB . HEM E  2 .   ? 27.408  -31.514 38.287  1.00 17.52 ? 350  HEM A CBB 1 
HETATM 10098 C  C1C . HEM E  2 .   ? 23.130  -30.321 36.993  1.00 21.75 ? 350  HEM A C1C 1 
HETATM 10099 C  C2C . HEM E  2 .   ? 22.616  -31.139 35.907  1.00 19.52 ? 350  HEM A C2C 1 
HETATM 10100 C  C3C . HEM E  2 .   ? 21.503  -30.561 35.480  1.00 18.26 ? 350  HEM A C3C 1 
HETATM 10101 C  C4C . HEM E  2 .   ? 21.248  -29.381 36.274  1.00 21.05 ? 350  HEM A C4C 1 
HETATM 10102 C  CMC . HEM E  2 .   ? 23.204  -32.473 35.326  1.00 18.38 ? 350  HEM A CMC 1 
HETATM 10103 C  CAC . HEM E  2 .   ? 20.607  -31.129 34.357  1.00 20.77 ? 350  HEM A CAC 1 
HETATM 10104 C  CBC . HEM E  2 .   ? 19.795  -30.311 33.687  1.00 27.38 ? 350  HEM A CBC 1 
HETATM 10105 C  C1D . HEM E  2 .   ? 20.009  -27.313 36.732  1.00 17.21 ? 350  HEM A C1D 1 
HETATM 10106 C  C2D . HEM E  2 .   ? 19.012  -26.317 36.383  1.00 18.40 ? 350  HEM A C2D 1 
HETATM 10107 C  C3D . HEM E  2 .   ? 19.113  -25.242 37.457  1.00 18.91 ? 350  HEM A C3D 1 
HETATM 10108 C  C4D . HEM E  2 .   ? 20.142  -25.713 38.360  1.00 20.05 ? 350  HEM A C4D 1 
HETATM 10109 C  CMD . HEM E  2 .   ? 18.029  -26.296 35.193  1.00 12.59 ? 350  HEM A CMD 1 
HETATM 10110 C  CAD . HEM E  2 .   ? 18.300  -23.938 37.494  1.00 17.30 ? 350  HEM A CAD 1 
HETATM 10111 C  CBD . HEM E  2 .   ? 17.181  -24.021 38.522  1.00 20.56 ? 350  HEM A CBD 1 
HETATM 10112 C  CGD . HEM E  2 .   ? 16.293  -22.785 38.453  1.00 21.39 ? 350  HEM A CGD 1 
HETATM 10113 O  O1D . HEM E  2 .   ? 16.769  -21.693 38.040  1.00 22.10 ? 350  HEM A O1D 1 
HETATM 10114 O  O2D . HEM E  2 .   ? 15.079  -22.891 38.757  1.00 22.12 ? 350  HEM A O2D 1 
HETATM 10115 N  NA  . HEM E  2 .   ? 22.434  -26.552 40.066  1.00 19.91 ? 350  HEM A NA  1 
HETATM 10116 N  NB  . HEM E  2 .   ? 23.999  -28.839 39.375  1.00 20.76 ? 350  HEM A NB  1 
HETATM 10117 N  NC  . HEM E  2 .   ? 22.247  -29.276 37.235  1.00 19.51 ? 350  HEM A NC  1 
HETATM 10118 N  ND  . HEM E  2 .   ? 20.628  -26.939 37.920  1.00 19.16 ? 350  HEM A ND  1 
HETATM 10119 FE FE  . HEM E  2 .   ? 22.315  -27.936 38.667  1.00 21.66 3 350  HEM A FE  1 
HETATM 10120 MG MG  . MG  F  3 .   ? 18.668  -19.591 43.357  1.00 18.46 2 353  MG  A MG  1 
HETATM 10121 C  C1  . NAG G  4 .   ? 7.593   -17.463 44.638  1.00 34.49 ? 361  NAG A C1  1 
HETATM 10122 C  C2  . NAG G  4 .   ? 7.298   -16.987 46.061  1.00 37.09 ? 361  NAG A C2  1 
HETATM 10123 C  C3  . NAG G  4 .   ? 6.525   -15.680 46.020  1.00 36.91 ? 361  NAG A C3  1 
HETATM 10124 C  C4  . NAG G  4 .   ? 7.353   -14.641 45.272  1.00 38.02 ? 361  NAG A C4  1 
HETATM 10125 C  C5  . NAG G  4 .   ? 7.809   -15.196 43.921  1.00 35.85 ? 361  NAG A C5  1 
HETATM 10126 C  C6  . NAG G  4 .   ? 8.759   -14.232 43.220  1.00 34.97 ? 361  NAG A C6  1 
HETATM 10127 C  C7  . NAG G  4 .   ? 7.168   -18.390 48.029  1.00 40.59 ? 361  NAG A C7  1 
HETATM 10128 C  C8  . NAG G  4 .   ? 8.484   -17.798 48.431  1.00 41.47 ? 361  NAG A C8  1 
HETATM 10129 N  N2  . NAG G  4 .   ? 6.615   -17.980 46.874  1.00 39.74 ? 361  NAG A N2  1 
HETATM 10130 O  O3  . NAG G  4 .   ? 6.300   -15.256 47.341  1.00 36.92 ? 361  NAG A O3  1 
HETATM 10131 O  O4  . NAG G  4 .   ? 6.545   -13.501 45.072  1.00 41.65 ? 361  NAG A O4  1 
HETATM 10132 O  O5  . NAG G  4 .   ? 8.414   -16.476 44.032  1.00 33.74 ? 361  NAG A O5  1 
HETATM 10133 O  O6  . NAG G  4 .   ? 10.062  -14.323 43.770  1.00 33.79 ? 361  NAG A O6  1 
HETATM 10134 O  O7  . NAG G  4 .   ? 6.670   -19.238 48.756  1.00 41.25 ? 361  NAG A O7  1 
HETATM 10135 C  C1  . NAG H  4 .   ? 7.291   -12.280 45.260  1.00 44.36 ? 362  NAG A C1  1 
HETATM 10136 C  C2  . NAG H  4 .   ? 6.557   -11.163 44.527  1.00 46.75 ? 362  NAG A C2  1 
HETATM 10137 C  C3  . NAG H  4 .   ? 7.312   -9.850  44.635  1.00 45.63 ? 362  NAG A C3  1 
HETATM 10138 C  C4  . NAG H  4 .   ? 7.521   -9.530  46.113  1.00 46.50 ? 362  NAG A C4  1 
HETATM 10139 C  C5  . NAG H  4 .   ? 8.187   -10.724 46.786  1.00 46.10 ? 362  NAG A C5  1 
HETATM 10140 C  C6  . NAG H  4 .   ? 8.415   -10.441 48.266  1.00 47.39 ? 362  NAG A C6  1 
HETATM 10141 C  C7  . NAG H  4 .   ? 5.165   -11.914 42.673  1.00 53.54 ? 362  NAG A C7  1 
HETATM 10142 C  C8  . NAG H  4 .   ? 4.087   -12.233 43.676  1.00 52.55 ? 362  NAG A C8  1 
HETATM 10143 N  N2  . NAG H  4 .   ? 6.331   -11.454 43.127  1.00 50.83 ? 362  NAG A N2  1 
HETATM 10144 O  O3  . NAG H  4 .   ? 6.591   -8.852  43.940  1.00 40.98 ? 362  NAG A O3  1 
HETATM 10145 O  O4  . NAG H  4 .   ? 8.392   -8.433  46.275  1.00 49.38 ? 362  NAG A O4  1 
HETATM 10146 O  O5  . NAG H  4 .   ? 7.410   -11.892 46.620  1.00 45.21 ? 362  NAG A O5  1 
HETATM 10147 O  O6  . NAG H  4 .   ? 7.233   -9.926  48.838  1.00 49.36 ? 362  NAG A O6  1 
HETATM 10148 O  O7  . NAG H  4 .   ? 4.986   -12.104 41.470  1.00 56.78 ? 362  NAG A O7  1 
HETATM 10149 C  C1  . BMA I  5 .   ? 7.657   -7.201  46.410  1.00 52.14 ? 363  BMA A C1  1 
HETATM 10150 C  C2  . BMA I  5 .   ? 8.501   -6.227  47.234  1.00 53.29 ? 363  BMA A C2  1 
HETATM 10151 C  C3  . BMA I  5 .   ? 7.810   -4.871  47.345  1.00 54.02 ? 363  BMA A C3  1 
HETATM 10152 C  C4  . BMA I  5 .   ? 7.358   -4.371  45.979  1.00 55.46 ? 363  BMA A C4  1 
HETATM 10153 C  C5  . BMA I  5 .   ? 6.551   -5.438  45.225  1.00 56.10 ? 363  BMA A C5  1 
HETATM 10154 C  C6  . BMA I  5 .   ? 6.269   -5.009  43.783  1.00 59.00 ? 363  BMA A C6  1 
HETATM 10155 O  O2  . BMA I  5 .   ? 9.819   -6.094  46.723  1.00 49.61 ? 363  BMA A O2  1 
HETATM 10156 O  O3  . BMA I  5 .   ? 8.677   -3.931  47.943  1.00 55.08 ? 363  BMA A O3  1 
HETATM 10157 O  O4  . BMA I  5 .   ? 6.606   -3.195  46.184  1.00 55.82 ? 363  BMA A O4  1 
HETATM 10158 O  O5  . BMA I  5 .   ? 7.303   -6.633  45.161  1.00 53.03 ? 363  BMA A O5  1 
HETATM 10159 O  O6  . BMA I  5 .   ? 4.966   -5.364  43.353  1.00 62.72 ? 363  BMA A O6  1 
HETATM 10160 C  C1  . MAN J  6 .   ? 8.490   -3.933  49.374  1.00 56.39 ? 364  MAN A C1  1 
HETATM 10161 C  C2  . MAN J  6 .   ? 9.008   -2.609  49.922  1.00 58.15 ? 364  MAN A C2  1 
HETATM 10162 C  C3  . MAN J  6 .   ? 10.489  -2.521  49.583  1.00 55.41 ? 364  MAN A C3  1 
HETATM 10163 C  C4  . MAN J  6 .   ? 11.186  -3.705  50.263  1.00 54.46 ? 364  MAN A C4  1 
HETATM 10164 C  C5  . MAN J  6 .   ? 10.541  -5.010  49.779  1.00 54.14 ? 364  MAN A C5  1 
HETATM 10165 C  C6  . MAN J  6 .   ? 11.180  -6.272  50.349  1.00 53.87 ? 364  MAN A C6  1 
HETATM 10166 O  O2  . MAN J  6 .   ? 8.906   -2.646  51.328  1.00 63.19 ? 364  MAN A O2  1 
HETATM 10167 O  O3  . MAN J  6 .   ? 11.020  -1.271  49.974  1.00 53.05 ? 364  MAN A O3  1 
HETATM 10168 O  O4  . MAN J  6 .   ? 12.573  -3.705  49.998  1.00 51.44 ? 364  MAN A O4  1 
HETATM 10169 O  O5  . MAN J  6 .   ? 9.151   -5.003  50.038  1.00 55.06 ? 364  MAN A O5  1 
HETATM 10170 O  O6  . MAN J  6 .   ? 10.924  -6.383  51.731  1.00 52.15 ? 364  MAN A O6  1 
HETATM 10171 C  C1  . MAN K  6 .   ? 7.754   -1.929  51.807  1.00 67.16 ? 365  MAN A C1  1 
HETATM 10172 C  C2  . MAN K  6 .   ? 8.225   -0.991  52.925  1.00 68.38 ? 365  MAN A C2  1 
HETATM 10173 C  C3  . MAN K  6 .   ? 7.589   -1.336  54.270  1.00 68.51 ? 365  MAN A C3  1 
HETATM 10174 C  C4  . MAN K  6 .   ? 7.679   -2.829  54.570  1.00 68.82 ? 365  MAN A C4  1 
HETATM 10175 C  C5  . MAN K  6 .   ? 7.333   -3.668  53.334  1.00 69.64 ? 365  MAN A C5  1 
HETATM 10176 C  C6  . MAN K  6 .   ? 6.344   -4.784  53.676  1.00 70.56 ? 365  MAN A C6  1 
HETATM 10177 O  O2  . MAN K  6 .   ? 7.943   0.353   52.596  1.00 68.97 ? 365  MAN A O2  1 
HETATM 10178 O  O3  . MAN K  6 .   ? 6.229   -0.960  54.242  1.00 70.02 ? 365  MAN A O3  1 
HETATM 10179 O  O4  . MAN K  6 .   ? 8.975   -3.129  55.036  1.00 66.87 ? 365  MAN A O4  1 
HETATM 10180 O  O5  . MAN K  6 .   ? 6.791   -2.829  52.324  1.00 69.42 ? 365  MAN A O5  1 
HETATM 10181 O  O6  . MAN K  6 .   ? 6.184   -5.649  52.568  1.00 71.51 ? 365  MAN A O6  1 
HETATM 10182 C  C1  . MAN L  6 .   ? 5.029   -6.033  42.070  1.00 65.32 ? 366  MAN A C1  1 
HETATM 10183 C  C2  . MAN L  6 .   ? 5.401   -5.103  40.917  1.00 65.98 ? 366  MAN A C2  1 
HETATM 10184 C  C3  . MAN L  6 .   ? 5.800   -5.984  39.735  1.00 66.28 ? 366  MAN A C3  1 
HETATM 10185 C  C4  . MAN L  6 .   ? 5.604   -7.433  40.193  1.00 65.96 ? 366  MAN A C4  1 
HETATM 10186 C  C5  . MAN L  6 .   ? 4.154   -7.651  40.640  1.00 65.78 ? 366  MAN A C5  1 
HETATM 10187 C  C6  . MAN L  6 .   ? 3.905   -9.100  41.053  1.00 65.27 ? 366  MAN A C6  1 
HETATM 10188 O  O2  . MAN L  6 .   ? 6.468   -4.257  41.278  1.00 67.53 ? 366  MAN A O2  1 
HETATM 10189 O  O3  . MAN L  6 .   ? 7.123   -5.716  39.287  1.00 64.68 ? 366  MAN A O3  1 
HETATM 10190 O  O4  . MAN L  6 .   ? 5.958   -8.350  39.181  1.00 65.96 ? 366  MAN A O4  1 
HETATM 10191 O  O5  . MAN L  6 .   ? 3.866   -6.762  41.706  1.00 66.14 ? 366  MAN A O5  1 
HETATM 10192 O  O6  . MAN L  6 .   ? 2.549   -9.319  41.382  1.00 65.32 ? 366  MAN A O6  1 
HETATM 10193 C  C1  . NAG M  4 .   ? 11.646  -21.823 20.014  1.00 21.91 ? 371  NAG A C1  1 
HETATM 10194 C  C2  . NAG M  4 .   ? 12.592  -21.586 18.821  1.00 21.35 ? 371  NAG A C2  1 
HETATM 10195 C  C3  . NAG M  4 .   ? 12.197  -20.353 18.007  1.00 24.40 ? 371  NAG A C3  1 
HETATM 10196 C  C4  . NAG M  4 .   ? 10.709  -20.399 17.621  1.00 26.11 ? 371  NAG A C4  1 
HETATM 10197 C  C5  . NAG M  4 .   ? 9.832   -20.924 18.768  1.00 25.48 ? 371  NAG A C5  1 
HETATM 10198 C  C6  . NAG M  4 .   ? 8.445   -21.236 18.208  1.00 24.84 ? 371  NAG A C6  1 
HETATM 10199 C  C7  . NAG M  4 .   ? 14.844  -22.425 19.152  1.00 21.11 ? 371  NAG A C7  1 
HETATM 10200 C  C8  . NAG M  4 .   ? 16.253  -22.107 19.552  1.00 18.40 ? 371  NAG A C8  1 
HETATM 10201 N  N2  . NAG M  4 .   ? 13.971  -21.422 19.224  1.00 20.35 ? 371  NAG A N2  1 
HETATM 10202 O  O3  . NAG M  4 .   ? 13.052  -20.183 16.868  1.00 18.07 ? 371  NAG A O3  1 
HETATM 10203 O  O4  . NAG M  4 .   ? 10.257  -19.077 17.368  1.00 30.60 ? 371  NAG A O4  1 
HETATM 10204 O  O5  . NAG M  4 .   ? 10.347  -22.034 19.510  1.00 23.39 ? 371  NAG A O5  1 
HETATM 10205 O  O6  . NAG M  4 .   ? 8.448   -22.498 17.571  1.00 25.67 ? 371  NAG A O6  1 
HETATM 10206 O  O7  . NAG M  4 .   ? 14.521  -23.581 18.857  1.00 20.67 ? 371  NAG A O7  1 
HETATM 10207 C  C1  . NAG N  4 .   ? 10.199  -18.767 15.972  1.00 37.88 ? 372  NAG A C1  1 
HETATM 10208 C  C2  . NAG N  4 .   ? 8.955   -17.918 15.662  1.00 42.24 ? 372  NAG A C2  1 
HETATM 10209 C  C3  . NAG N  4 .   ? 8.949   -17.326 14.246  1.00 44.46 ? 372  NAG A C3  1 
HETATM 10210 C  C4  . NAG N  4 .   ? 10.331  -16.900 13.742  1.00 46.62 ? 372  NAG A C4  1 
HETATM 10211 C  C5  . NAG N  4 .   ? 11.433  -17.828 14.244  1.00 42.68 ? 372  NAG A C5  1 
HETATM 10212 C  C6  . NAG N  4 .   ? 12.802  -17.234 13.972  1.00 42.48 ? 372  NAG A C6  1 
HETATM 10213 C  C7  . NAG N  4 .   ? 7.004   -18.365 17.006  1.00 43.37 ? 372  NAG A C7  1 
HETATM 10214 C  C8  . NAG N  4 .   ? 5.681   -19.078 17.192  1.00 43.05 ? 372  NAG A C8  1 
HETATM 10215 N  N2  . NAG N  4 .   ? 7.696   -18.617 15.892  1.00 41.66 ? 372  NAG A N2  1 
HETATM 10216 O  O3  . NAG N  4 .   ? 8.064   -16.222 14.195  1.00 44.80 ? 372  NAG A O3  1 
HETATM 10217 O  O4  . NAG N  4 .   ? 10.336  -16.940 12.329  1.00 52.65 ? 372  NAG A O4  1 
HETATM 10218 O  O5  . NAG N  4 .   ? 11.327  -18.008 15.632  1.00 39.13 ? 372  NAG A O5  1 
HETATM 10219 O  O6  . NAG N  4 .   ? 13.473  -18.187 13.189  1.00 42.51 ? 372  NAG A O6  1 
HETATM 10220 O  O7  . NAG N  4 .   ? 7.456   -17.624 17.884  1.00 41.38 ? 372  NAG A O7  1 
HETATM 10221 C  C1  . BMA O  5 .   ? 10.106  -15.623 11.759  1.00 56.58 ? 373  BMA A C1  1 
HETATM 10222 C  C2  . BMA O  5 .   ? 10.820  -15.516 10.403  1.00 56.91 ? 373  BMA A C2  1 
HETATM 10223 C  C3  . BMA O  5 .   ? 10.517  -14.199 9.687   1.00 58.63 ? 373  BMA A C3  1 
HETATM 10224 C  C4  . BMA O  5 .   ? 8.998   -14.026 9.632   1.00 60.54 ? 373  BMA A C4  1 
HETATM 10225 C  C5  . BMA O  5 .   ? 8.471   -14.067 11.064  1.00 62.68 ? 373  BMA A C5  1 
HETATM 10226 C  C6  . BMA O  5 .   ? 6.986   -13.723 11.161  1.00 68.22 ? 373  BMA A C6  1 
HETATM 10227 O  O2  . BMA O  5 .   ? 10.389  -16.581 9.581   1.00 56.11 ? 373  BMA A O2  1 
HETATM 10228 O  O3  . BMA O  5 .   ? 11.092  -14.192 8.392   1.00 56.99 ? 373  BMA A O3  1 
HETATM 10229 O  O4  . BMA O  5 .   ? 8.603   -12.835 8.984   1.00 58.81 ? 373  BMA A O4  1 
HETATM 10230 O  O5  . BMA O  5 .   ? 8.722   -15.355 11.595  1.00 59.22 ? 373  BMA A O5  1 
HETATM 10231 O  O6  . BMA O  5 .   ? 6.682   -13.386 12.500  1.00 74.63 ? 373  BMA A O6  1 
HETATM 10232 C  C1  . MAN P  6 .   ? 5.251   -13.320 12.702  1.00 79.33 ? 374  MAN A C1  1 
HETATM 10233 C  C2  . MAN P  6 .   ? 4.922   -13.553 14.182  1.00 80.84 ? 374  MAN A C2  1 
HETATM 10234 C  C3  . MAN P  6 .   ? 4.826   -15.034 14.554  1.00 81.51 ? 374  MAN A C3  1 
HETATM 10235 C  C4  . MAN P  6 .   ? 4.054   -15.837 13.507  1.00 81.99 ? 374  MAN A C4  1 
HETATM 10236 C  C5  . MAN P  6 .   ? 4.572   -15.527 12.101  1.00 82.79 ? 374  MAN A C5  1 
HETATM 10237 C  C6  . MAN P  6 .   ? 3.837   -16.308 11.009  1.00 84.91 ? 374  MAN A C6  1 
HETATM 10238 O  O2  . MAN P  6 .   ? 3.717   -12.900 14.510  1.00 81.46 ? 374  MAN A O2  1 
HETATM 10239 O  O3  . MAN P  6 .   ? 4.231   -15.177 15.828  1.00 80.62 ? 374  MAN A O3  1 
HETATM 10240 O  O4  . MAN P  6 .   ? 4.216   -17.213 13.773  1.00 82.17 ? 374  MAN A O4  1 
HETATM 10241 O  O5  . MAN P  6 .   ? 4.473   -14.140 11.840  1.00 80.96 ? 374  MAN A O5  1 
HETATM 10242 O  O6  . MAN P  6 .   ? 2.809   -17.104 11.565  1.00 88.02 ? 374  MAN A O6  1 
HETATM 10243 C  C1  . MAN Q  6 .   ? 2.251   -17.979 10.556  1.00 89.96 ? 375  MAN A C1  1 
HETATM 10244 C  C2  . MAN Q  6 .   ? 1.076   -17.296 9.876   1.00 90.79 ? 375  MAN A C2  1 
HETATM 10245 C  C3  . MAN Q  6 .   ? 0.058   -16.923 10.946  1.00 90.75 ? 375  MAN A C3  1 
HETATM 10246 C  C4  . MAN Q  6 .   ? -0.327  -18.142 11.785  1.00 90.79 ? 375  MAN A C4  1 
HETATM 10247 C  C5  . MAN Q  6 .   ? 0.860   -19.040 12.147  1.00 90.31 ? 375  MAN A C5  1 
HETATM 10248 C  C6  . MAN Q  6 .   ? 0.376   -20.411 12.614  1.00 89.56 ? 375  MAN A C6  1 
HETATM 10249 O  O2  . MAN Q  6 .   ? 0.490   -18.190 8.951   1.00 91.06 ? 375  MAN A O2  1 
HETATM 10250 O  O3  . MAN Q  6 .   ? -1.087  -16.355 10.344  1.00 90.81 ? 375  MAN A O3  1 
HETATM 10251 O  O4  . MAN Q  6 .   ? -0.923  -17.691 12.982  1.00 90.85 ? 375  MAN A O4  1 
HETATM 10252 O  O5  . MAN Q  6 .   ? 1.768   -19.204 11.072  1.00 90.19 ? 375  MAN A O5  1 
HETATM 10253 O  O6  . MAN Q  6 .   ? 1.313   -21.400 12.248  1.00 88.30 ? 375  MAN A O6  1 
HETATM 10254 C  C1  . NAG R  4 .   ? 20.391  -8.102  53.103  1.00 40.16 ? 381  NAG A C1  1 
HETATM 10255 C  C2  . NAG R  4 .   ? 20.048  -9.159  54.148  1.00 43.42 ? 381  NAG A C2  1 
HETATM 10256 C  C3  . NAG R  4 .   ? 20.530  -8.674  55.514  1.00 45.37 ? 381  NAG A C3  1 
HETATM 10257 C  C4  . NAG R  4 .   ? 22.015  -8.313  55.511  1.00 47.21 ? 381  NAG A C4  1 
HETATM 10258 C  C5  . NAG R  4 .   ? 22.178  -7.266  54.411  1.00 46.09 ? 381  NAG A C5  1 
HETATM 10259 C  C6  . NAG R  4 .   ? 23.581  -6.675  54.337  1.00 45.63 ? 381  NAG A C6  1 
HETATM 10260 C  C7  . NAG R  4 .   ? 17.970  -10.462 54.347  1.00 41.21 ? 381  NAG A C7  1 
HETATM 10261 C  C8  . NAG R  4 .   ? 16.486  -10.366 54.556  1.00 41.59 ? 381  NAG A C8  1 
HETATM 10262 N  N2  . NAG R  4 .   ? 18.605  -9.299  54.254  1.00 42.22 ? 381  NAG A N2  1 
HETATM 10263 O  O3  . NAG R  4 .   ? 20.146  -9.594  56.508  1.00 44.23 ? 381  NAG A O3  1 
HETATM 10264 O  O4  . NAG R  4 .   ? 22.358  -7.662  56.719  1.00 54.46 ? 381  NAG A O4  1 
HETATM 10265 O  O5  . NAG R  4 .   ? 21.766  -7.773  53.164  1.00 41.60 ? 381  NAG A O5  1 
HETATM 10266 O  O6  . NAG R  4 .   ? 24.434  -7.498  53.577  1.00 45.51 ? 381  NAG A O6  1 
HETATM 10267 O  O7  . NAG R  4 .   ? 18.523  -11.550 54.200  1.00 39.36 ? 381  NAG A O7  1 
HETATM 10268 C  C1  . NAG S  4 .   ? 22.960  -8.562  57.673  1.00 59.29 ? 382  NAG A C1  1 
HETATM 10269 C  C2  . NAG S  4 .   ? 24.315  -8.068  58.183  1.00 60.47 ? 382  NAG A C2  1 
HETATM 10270 C  C3  . NAG S  4 .   ? 24.931  -9.124  59.099  1.00 62.91 ? 382  NAG A C3  1 
HETATM 10271 C  C4  . NAG S  4 .   ? 23.943  -9.770  60.066  1.00 64.26 ? 382  NAG A C4  1 
HETATM 10272 C  C5  . NAG S  4 .   ? 22.513  -9.891  59.532  1.00 64.21 ? 382  NAG A C5  1 
HETATM 10273 C  C6  . NAG S  4 .   ? 21.541  -10.147 60.687  1.00 64.94 ? 382  NAG A C6  1 
HETATM 10274 C  C7  . NAG S  4 .   ? 25.684  -6.514  56.870  1.00 60.59 ? 382  NAG A C7  1 
HETATM 10275 C  C8  . NAG S  4 .   ? 26.767  -6.340  55.843  1.00 57.15 ? 382  NAG A C8  1 
HETATM 10276 N  N2  . NAG S  4 .   ? 25.294  -7.763  57.150  1.00 59.67 ? 382  NAG A N2  1 
HETATM 10277 O  O3  . NAG S  4 .   ? 25.966  -8.556  59.872  1.00 63.98 ? 382  NAG A O3  1 
HETATM 10278 O  O4  . NAG S  4 .   ? 24.451  -11.048 60.394  1.00 65.84 ? 382  NAG A O4  1 
HETATM 10279 O  O5  . NAG S  4 .   ? 22.136  -8.735  58.805  1.00 61.36 ? 382  NAG A O5  1 
HETATM 10280 O  O6  . NAG S  4 .   ? 20.339  -9.429  60.504  1.00 66.66 ? 382  NAG A O6  1 
HETATM 10281 O  O7  . NAG S  4 .   ? 25.156  -5.516  57.364  1.00 61.18 ? 382  NAG A O7  1 
HETATM 10282 C  C1  . NAG T  4 .   ? 45.988  -16.053 45.194  1.00 38.13 ? 391  NAG A C1  1 
HETATM 10283 C  C2  . NAG T  4 .   ? 47.079  -15.280 44.450  1.00 39.60 ? 391  NAG A C2  1 
HETATM 10284 C  C3  . NAG T  4 .   ? 48.468  -15.509 45.029  1.00 39.97 ? 391  NAG A C3  1 
HETATM 10285 C  C4  . NAG T  4 .   ? 48.442  -15.313 46.527  1.00 40.76 ? 391  NAG A C4  1 
HETATM 10286 C  C5  . NAG T  4 .   ? 47.375  -16.194 47.171  1.00 40.57 ? 391  NAG A C5  1 
HETATM 10287 C  C6  . NAG T  4 .   ? 47.241  -15.845 48.655  1.00 40.03 ? 391  NAG A C6  1 
HETATM 10288 C  C7  . NAG T  4 .   ? 46.773  -14.714 42.164  1.00 35.42 ? 391  NAG A C7  1 
HETATM 10289 C  C8  . NAG T  4 .   ? 46.803  -15.067 40.697  1.00 34.04 ? 391  NAG A C8  1 
HETATM 10290 N  N2  . NAG T  4 .   ? 47.110  -15.636 43.046  1.00 34.84 ? 391  NAG A N2  1 
HETATM 10291 O  O3  . NAG T  4 .   ? 49.376  -14.574 44.474  1.00 42.65 ? 391  NAG A O3  1 
HETATM 10292 O  O4  . NAG T  4 .   ? 49.705  -15.704 46.989  1.00 41.88 ? 391  NAG A O4  1 
HETATM 10293 O  O5  . NAG T  4 .   ? 46.119  -15.930 46.595  1.00 38.35 ? 391  NAG A O5  1 
HETATM 10294 O  O6  . NAG T  4 .   ? 46.303  -16.725 49.242  1.00 43.65 ? 391  NAG A O6  1 
HETATM 10295 O  O7  . NAG T  4 .   ? 46.368  -13.623 42.543  1.00 37.98 ? 391  NAG A O7  1 
HETATM 10296 C  C1  . NAG U  4 .   ? 50.239  -14.689 47.834  1.00 43.30 ? 392  NAG A C1  1 
HETATM 10297 C  C2  . NAG U  4 .   ? 51.318  -15.319 48.707  1.00 45.17 ? 392  NAG A C2  1 
HETATM 10298 C  C3  . NAG U  4 .   ? 52.014  -14.259 49.564  1.00 45.84 ? 392  NAG A C3  1 
HETATM 10299 C  C4  . NAG U  4 .   ? 52.272  -12.966 48.781  1.00 44.84 ? 392  NAG A C4  1 
HETATM 10300 C  C5  . NAG U  4 .   ? 51.029  -12.573 47.988  1.00 43.94 ? 392  NAG A C5  1 
HETATM 10301 C  C6  . NAG U  4 .   ? 51.213  -11.277 47.221  1.00 42.56 ? 392  NAG A C6  1 
HETATM 10302 C  C7  . NAG U  4 .   ? 50.818  -17.681 49.220  1.00 47.78 ? 392  NAG A C7  1 
HETATM 10303 C  C8  . NAG U  4 .   ? 50.133  -18.649 50.152  1.00 47.44 ? 392  NAG A C8  1 
HETATM 10304 N  N2  . NAG U  4 .   ? 50.726  -16.374 49.516  1.00 46.35 ? 392  NAG A N2  1 
HETATM 10305 O  O3  . NAG U  4 .   ? 53.228  -14.789 50.066  1.00 47.31 ? 392  NAG A O3  1 
HETATM 10306 O  O4  . NAG U  4 .   ? 52.586  -11.892 49.645  1.00 45.96 ? 392  NAG A O4  1 
HETATM 10307 O  O5  . NAG U  4 .   ? 50.766  -13.617 47.095  1.00 42.19 ? 392  NAG A O5  1 
HETATM 10308 O  O6  . NAG U  4 .   ? 52.084  -11.543 46.153  1.00 42.52 ? 392  NAG A O6  1 
HETATM 10309 O  O7  . NAG U  4 .   ? 51.439  -18.120 48.249  1.00 47.12 ? 392  NAG A O7  1 
HETATM 10310 C  C1  . BMA V  5 .   ? 54.004  -11.617 49.645  1.00 44.28 ? 393  BMA A C1  1 
HETATM 10311 C  C2  . BMA V  5 .   ? 54.191  -10.116 49.870  1.00 42.77 ? 393  BMA A C2  1 
HETATM 10312 C  C3  . BMA V  5 .   ? 55.622  -9.745  50.251  1.00 46.09 ? 393  BMA A C3  1 
HETATM 10313 C  C4  . BMA V  5 .   ? 56.137  -10.708 51.315  1.00 44.99 ? 393  BMA A C4  1 
HETATM 10314 C  C5  . BMA V  5 .   ? 56.036  -12.119 50.783  1.00 43.75 ? 393  BMA A C5  1 
HETATM 10315 C  C6  . BMA V  5 .   ? 56.674  -13.092 51.762  1.00 44.53 ? 393  BMA A C6  1 
HETATM 10316 O  O2  . BMA V  5 .   ? 53.309  -9.693  50.882  1.00 40.16 ? 393  BMA A O2  1 
HETATM 10317 O  O3  . BMA V  5 .   ? 55.703  -8.415  50.720  1.00 48.29 ? 393  BMA A O3  1 
HETATM 10318 O  O4  . BMA V  5 .   ? 57.495  -10.467 51.573  1.00 46.37 ? 393  BMA A O4  1 
HETATM 10319 O  O5  . BMA V  5 .   ? 54.674  -12.423 50.605  1.00 43.45 ? 393  BMA A O5  1 
HETATM 10320 O  O6  . BMA V  5 .   ? 56.145  -14.361 51.482  1.00 47.74 ? 393  BMA A O6  1 
HETATM 10321 C  C1  . MAN W  6 .   ? 56.765  -15.350 52.311  1.00 49.94 ? 394  MAN A C1  1 
HETATM 10322 C  C2  . MAN W  6 .   ? 56.633  -16.703 51.614  1.00 49.49 ? 394  MAN A C2  1 
HETATM 10323 C  C3  . MAN W  6 .   ? 55.178  -17.175 51.608  1.00 50.51 ? 394  MAN A C3  1 
HETATM 10324 C  C4  . MAN W  6 .   ? 54.566  -17.055 53.003  1.00 51.76 ? 394  MAN A C4  1 
HETATM 10325 C  C5  . MAN W  6 .   ? 54.808  -15.677 53.619  1.00 53.18 ? 394  MAN A C5  1 
HETATM 10326 C  C6  . MAN W  6 .   ? 54.338  -15.703 55.069  1.00 55.42 ? 394  MAN A C6  1 
HETATM 10327 O  O2  . MAN W  6 .   ? 57.484  -17.665 52.209  1.00 46.44 ? 394  MAN A O2  1 
HETATM 10328 O  O3  . MAN W  6 .   ? 55.113  -18.520 51.185  1.00 49.88 ? 394  MAN A O3  1 
HETATM 10329 O  O4  . MAN W  6 .   ? 53.186  -17.367 52.981  1.00 49.55 ? 394  MAN A O4  1 
HETATM 10330 O  O5  . MAN W  6 .   ? 56.196  -15.380 53.602  1.00 51.70 ? 394  MAN A O5  1 
HETATM 10331 O  O6  . MAN W  6 .   ? 54.573  -17.003 55.588  1.00 59.09 ? 394  MAN A O6  1 
HETATM 10332 C  C1  . MAN X  6 .   ? 53.345  -17.517 56.146  1.00 61.85 ? 395  MAN A C1  1 
HETATM 10333 C  C2  . MAN X  6 .   ? 52.598  -16.302 56.661  1.00 61.36 ? 395  MAN A C2  1 
HETATM 10334 C  C3  . MAN X  6 .   ? 53.562  -15.630 57.625  1.00 62.11 ? 395  MAN A C3  1 
HETATM 10335 C  C4  . MAN X  6 .   ? 53.923  -16.616 58.732  1.00 61.82 ? 395  MAN A C4  1 
HETATM 10336 C  C5  . MAN X  6 .   ? 54.512  -17.889 58.135  1.00 61.69 ? 395  MAN A C5  1 
HETATM 10337 C  C6  . MAN X  6 .   ? 54.796  -18.914 59.224  1.00 62.66 ? 395  MAN A C6  1 
HETATM 10338 O  O2  . MAN X  6 .   ? 51.419  -16.716 57.309  1.00 60.84 ? 395  MAN A O2  1 
HETATM 10339 O  O3  . MAN X  6 .   ? 53.057  -14.402 58.113  1.00 63.08 ? 395  MAN A O3  1 
HETATM 10340 O  O4  . MAN X  6 .   ? 54.843  -16.037 59.620  1.00 61.94 ? 395  MAN A O4  1 
HETATM 10341 O  O5  . MAN X  6 .   ? 53.581  -18.420 57.212  1.00 62.66 ? 395  MAN A O5  1 
HETATM 10342 O  O6  . MAN X  6 .   ? 55.549  -19.994 58.704  1.00 64.47 ? 395  MAN A O6  1 
HETATM 10343 C  C1  . MAN Y  6 .   ? 54.286  -18.603 50.005  1.00 52.36 ? 396  MAN A C1  1 
HETATM 10344 C  C2  . MAN Y  6 .   ? 53.955  -20.056 49.716  1.00 53.34 ? 396  MAN A C2  1 
HETATM 10345 C  C3  . MAN Y  6 .   ? 55.245  -20.784 49.377  1.00 53.41 ? 396  MAN A C3  1 
HETATM 10346 C  C4  . MAN Y  6 .   ? 55.884  -20.119 48.169  1.00 53.61 ? 396  MAN A C4  1 
HETATM 10347 C  C5  . MAN Y  6 .   ? 56.046  -18.615 48.396  1.00 54.05 ? 396  MAN A C5  1 
HETATM 10348 C  C6  . MAN Y  6 .   ? 56.534  -17.924 47.125  1.00 54.97 ? 396  MAN A C6  1 
HETATM 10349 O  O2  . MAN Y  6 .   ? 53.108  -20.059 48.591  1.00 55.64 ? 396  MAN A O2  1 
HETATM 10350 O  O3  . MAN Y  6 .   ? 55.015  -22.151 49.113  1.00 54.24 ? 396  MAN A O3  1 
HETATM 10351 O  O4  . MAN Y  6 .   ? 57.154  -20.695 47.990  1.00 54.82 ? 396  MAN A O4  1 
HETATM 10352 O  O5  . MAN Y  6 .   ? 54.830  -18.026 48.828  1.00 52.55 ? 396  MAN A O5  1 
HETATM 10353 O  O6  . MAN Y  6 .   ? 57.270  -16.750 47.419  1.00 54.27 ? 396  MAN A O6  1 
HETATM 10354 C  C1  . MAN Z  6 .   ? 56.216  -7.561  49.678  1.00 55.26 ? 397  MAN A C1  1 
HETATM 10355 C  C2  . MAN Z  6 .   ? 56.891  -6.332  50.284  1.00 58.36 ? 397  MAN A C2  1 
HETATM 10356 C  C3  . MAN Z  6 .   ? 55.851  -5.643  51.154  1.00 59.39 ? 397  MAN A C3  1 
HETATM 10357 C  C4  . MAN Z  6 .   ? 54.713  -5.204  50.233  1.00 59.32 ? 397  MAN A C4  1 
HETATM 10358 C  C5  . MAN Z  6 .   ? 54.176  -6.429  49.489  1.00 59.34 ? 397  MAN A C5  1 
HETATM 10359 C  C6  . MAN Z  6 .   ? 53.036  -6.102  48.529  1.00 59.62 ? 397  MAN A C6  1 
HETATM 10360 O  O2  . MAN Z  6 .   ? 57.196  -5.444  49.222  1.00 62.09 ? 397  MAN A O2  1 
HETATM 10361 O  O3  . MAN Z  6 .   ? 56.401  -4.542  51.844  1.00 59.12 ? 397  MAN A O3  1 
HETATM 10362 O  O4  . MAN Z  6 .   ? 53.686  -4.636  51.004  1.00 59.48 ? 397  MAN A O4  1 
HETATM 10363 O  O5  . MAN Z  6 .   ? 55.212  -7.103  48.796  1.00 55.95 ? 397  MAN A O5  1 
HETATM 10364 O  O6  . MAN Z  6 .   ? 52.541  -7.332  48.029  1.00 60.10 ? 397  MAN A O6  1 
HETATM 10365 C  C1  . MAN AA 6 .   ? 58.548  -5.618  48.741  1.00 64.57 ? 398  MAN A C1  1 
HETATM 10366 C  C2  . MAN AA 6 .   ? 58.896  -4.457  47.810  1.00 65.42 ? 398  MAN A C2  1 
HETATM 10367 C  C3  . MAN AA 6 .   ? 58.084  -4.606  46.525  1.00 65.35 ? 398  MAN A C3  1 
HETATM 10368 C  C4  . MAN AA 6 .   ? 58.482  -5.927  45.881  1.00 64.58 ? 398  MAN A C4  1 
HETATM 10369 C  C5  . MAN AA 6 .   ? 58.176  -7.066  46.846  1.00 63.93 ? 398  MAN A C5  1 
HETATM 10370 C  C6  . MAN AA 6 .   ? 58.629  -8.389  46.244  1.00 61.72 ? 398  MAN A C6  1 
HETATM 10371 O  O2  . MAN AA 6 .   ? 60.279  -4.521  47.516  1.00 64.68 ? 398  MAN A O2  1 
HETATM 10372 O  O3  . MAN AA 6 .   ? 58.295  -3.524  45.644  1.00 65.32 ? 398  MAN A O3  1 
HETATM 10373 O  O4  . MAN AA 6 .   ? 57.800  -6.140  44.663  1.00 65.74 ? 398  MAN A O4  1 
HETATM 10374 O  O5  . MAN AA 6 .   ? 58.809  -6.867  48.103  1.00 64.59 ? 398  MAN A O5  1 
HETATM 10375 O  O6  . MAN AA 6 .   ? 58.202  -9.425  47.093  1.00 58.71 ? 398  MAN A O6  1 
HETATM 10376 C  C1  . NAG BA 4 .   ? 26.076  -48.175 23.339  1.00 56.43 ? 411  NAG A C1  1 
HETATM 10377 C  C2  . NAG BA 4 .   ? 26.428  -49.615 22.994  1.00 62.83 ? 411  NAG A C2  1 
HETATM 10378 C  C3  . NAG BA 4 .   ? 25.470  -50.058 21.901  1.00 64.32 ? 411  NAG A C3  1 
HETATM 10379 C  C4  . NAG BA 4 .   ? 24.091  -50.103 22.537  1.00 65.50 ? 411  NAG A C4  1 
HETATM 10380 C  C5  . NAG BA 4 .   ? 23.727  -48.831 23.320  1.00 62.92 ? 411  NAG A C5  1 
HETATM 10381 C  C6  . NAG BA 4 .   ? 22.752  -49.178 24.440  1.00 63.15 ? 411  NAG A C6  1 
HETATM 10382 C  C7  . NAG BA 4 .   ? 28.383  -49.674 21.494  1.00 66.03 ? 411  NAG A C7  1 
HETATM 10383 C  C8  . NAG BA 4 .   ? 29.861  -49.927 21.402  1.00 65.89 ? 411  NAG A C8  1 
HETATM 10384 N  N2  . NAG BA 4 .   ? 27.842  -49.807 22.702  1.00 64.01 ? 411  NAG A N2  1 
HETATM 10385 O  O3  . NAG BA 4 .   ? 25.767  -51.336 21.381  1.00 65.22 ? 411  NAG A O3  1 
HETATM 10386 O  O4  . NAG BA 4 .   ? 23.164  -50.326 21.498  1.00 70.69 ? 411  NAG A O4  1 
HETATM 10387 O  O5  . NAG BA 4 .   ? 24.797  -48.138 23.936  1.00 57.14 ? 411  NAG A O5  1 
HETATM 10388 O  O6  . NAG BA 4 .   ? 22.113  -48.002 24.887  1.00 62.37 ? 411  NAG A O6  1 
HETATM 10389 O  O7  . NAG BA 4 .   ? 27.737  -49.365 20.492  1.00 68.03 ? 411  NAG A O7  1 
HETATM 10390 C  C1  . NAG CA 4 .   ? 21.974  -49.562 21.750  1.00 75.44 ? 412  NAG A C1  1 
HETATM 10391 C  C2  . NAG CA 4 .   ? 21.478  -48.936 20.443  1.00 78.08 ? 412  NAG A C2  1 
HETATM 10392 C  C3  . NAG CA 4 .   ? 20.123  -49.499 20.056  1.00 77.89 ? 412  NAG A C3  1 
HETATM 10393 C  C4  . NAG CA 4 .   ? 20.153  -51.017 20.201  1.00 78.74 ? 412  NAG A C4  1 
HETATM 10394 C  C5  . NAG CA 4 .   ? 20.480  -51.427 21.639  1.00 78.45 ? 412  NAG A C5  1 
HETATM 10395 C  C6  . NAG CA 4 .   ? 21.448  -52.606 21.700  1.00 78.18 ? 412  NAG A C6  1 
HETATM 10396 C  C7  . NAG CA 4 .   ? 22.144  -46.696 19.705  1.00 81.44 ? 412  NAG A C7  1 
HETATM 10397 C  C8  . NAG CA 4 .   ? 22.988  -47.382 18.663  1.00 81.09 ? 412  NAG A C8  1 
HETATM 10398 N  N2  . NAG CA 4 .   ? 21.432  -47.481 20.525  1.00 79.96 ? 412  NAG A N2  1 
HETATM 10399 O  O3  . NAG CA 4 .   ? 19.850  -49.138 18.724  1.00 77.47 ? 412  NAG A O3  1 
HETATM 10400 O  O4  . NAG CA 4 .   ? 18.892  -51.547 19.843  1.00 80.00 ? 412  NAG A O4  1 
HETATM 10401 O  O5  . NAG CA 4 .   ? 20.970  -50.330 22.391  1.00 77.39 ? 412  NAG A O5  1 
HETATM 10402 O  O6  . NAG CA 4 .   ? 21.718  -53.052 20.389  1.00 78.07 ? 412  NAG A O6  1 
HETATM 10403 O  O7  . NAG CA 4 .   ? 22.131  -45.462 19.774  1.00 81.23 ? 412  NAG A O7  1 
HETATM 10404 C  C   . ACT DA 7 .   ? 25.173  -25.753 37.342  1.00 32.73 ? 1327 ACT A C   1 
HETATM 10405 O  O   . ACT DA 7 .   ? 24.034  -25.653 37.862  1.00 32.84 ? 1327 ACT A O   1 
HETATM 10406 O  OXT . ACT DA 7 .   ? 25.777  -24.684 37.046  1.00 32.99 ? 1327 ACT A OXT 1 
HETATM 10407 C  CH3 . ACT DA 7 .   ? 25.746  -27.103 37.048  1.00 30.96 ? 1327 ACT A CH3 1 
HETATM 10408 S  S   . SO4 EA 8 .   ? 19.722  -32.471 60.178  1.00 58.77 ? 1328 SO4 A S   1 
HETATM 10409 O  O1  . SO4 EA 8 .   ? 21.136  -32.167 60.446  1.00 57.95 ? 1328 SO4 A O1  1 
HETATM 10410 O  O2  . SO4 EA 8 .   ? 19.014  -31.236 59.824  1.00 56.60 ? 1328 SO4 A O2  1 
HETATM 10411 O  O3  . SO4 EA 8 .   ? 19.596  -33.463 59.104  1.00 56.10 ? 1328 SO4 A O3  1 
HETATM 10412 O  O4  . SO4 EA 8 .   ? 19.123  -33.008 61.398  1.00 59.23 ? 1328 SO4 A O4  1 
HETATM 10413 S  S   . SO4 FA 8 .   ? 14.224  -28.888 53.970  1.00 71.23 ? 1329 SO4 A S   1 
HETATM 10414 O  O1  . SO4 FA 8 .   ? 15.010  -29.533 52.922  1.00 71.06 ? 1329 SO4 A O1  1 
HETATM 10415 O  O2  . SO4 FA 8 .   ? 12.918  -28.514 53.429  1.00 72.17 ? 1329 SO4 A O2  1 
HETATM 10416 O  O3  . SO4 FA 8 .   ? 14.073  -29.850 55.056  1.00 71.22 ? 1329 SO4 A O3  1 
HETATM 10417 O  O4  . SO4 FA 8 .   ? 14.889  -27.675 54.450  1.00 70.53 ? 1329 SO4 A O4  1 
HETATM 10418 S  S   . SO4 GA 8 .   ? 5.957   -9.256  30.996  1.00 62.34 ? 1330 SO4 A S   1 
HETATM 10419 O  O1  . SO4 GA 8 .   ? 7.017   -8.930  30.042  1.00 63.48 ? 1330 SO4 A O1  1 
HETATM 10420 O  O2  . SO4 GA 8 .   ? 4.660   -9.028  30.351  1.00 63.26 ? 1330 SO4 A O2  1 
HETATM 10421 O  O3  . SO4 GA 8 .   ? 6.066   -10.651 31.421  1.00 59.70 ? 1330 SO4 A O3  1 
HETATM 10422 O  O4  . SO4 GA 8 .   ? 6.076   -8.362  32.147  1.00 63.18 ? 1330 SO4 A O4  1 
HETATM 10423 S  S   . SO4 HA 8 .   ? 40.807  -14.144 31.473  1.00 61.88 ? 1331 SO4 A S   1 
HETATM 10424 O  O1  . SO4 HA 8 .   ? 42.118  -14.788 31.591  1.00 63.05 ? 1331 SO4 A O1  1 
HETATM 10425 O  O2  . SO4 HA 8 .   ? 40.876  -13.219 30.336  1.00 61.04 ? 1331 SO4 A O2  1 
HETATM 10426 O  O3  . SO4 HA 8 .   ? 39.772  -15.152 31.237  1.00 60.41 ? 1331 SO4 A O3  1 
HETATM 10427 O  O4  . SO4 HA 8 .   ? 40.492  -13.432 32.719  1.00 60.18 ? 1331 SO4 A O4  1 
HETATM 10428 C  CHA . HEM IA 2 .   ? -18.333 -20.936 27.780  1.00 15.40 ? 350  HEM B CHA 1 
HETATM 10429 C  CHB . HEM IA 2 .   ? -21.833 -23.594 25.782  1.00 13.13 ? 350  HEM B CHB 1 
HETATM 10430 C  CHC . HEM IA 2 .   ? -21.525 -26.729 29.458  1.00 14.23 ? 350  HEM B CHC 1 
HETATM 10431 C  CHD . HEM IA 2 .   ? -17.753 -24.270 31.216  1.00 11.22 ? 350  HEM B CHD 1 
HETATM 10432 C  C1A . HEM IA 2 .   ? -19.266 -21.425 26.902  1.00 14.77 ? 350  HEM B C1A 1 
HETATM 10433 C  C2A . HEM IA 2 .   ? -19.596 -20.834 25.637  1.00 13.31 ? 350  HEM B C2A 1 
HETATM 10434 C  C3A . HEM IA 2 .   ? -20.557 -21.576 25.070  1.00 13.07 ? 350  HEM B C3A 1 
HETATM 10435 C  C4A . HEM IA 2 .   ? -20.910 -22.610 25.999  1.00 13.55 ? 350  HEM B C4A 1 
HETATM 10436 C  CMA . HEM IA 2 .   ? -21.213 -21.324 23.687  1.00 12.41 ? 350  HEM B CMA 1 
HETATM 10437 C  CAA . HEM IA 2 .   ? -18.914 -19.580 25.049  1.00 12.24 ? 350  HEM B CAA 1 
HETATM 10438 C  CBA . HEM IA 2 .   ? -19.492 -18.274 25.591  1.00 13.34 ? 350  HEM B CBA 1 
HETATM 10439 C  CGA . HEM IA 2 .   ? -18.406 -17.188 25.582  1.00 16.15 ? 350  HEM B CGA 1 
HETATM 10440 O  O1A . HEM IA 2 .   ? -18.192 -16.450 24.567  1.00 15.88 ? 350  HEM B O1A 1 
HETATM 10441 O  O2A . HEM IA 2 .   ? -17.687 -17.081 26.602  1.00 15.98 ? 350  HEM B O2A 1 
HETATM 10442 C  C1B . HEM IA 2 .   ? -22.111 -24.627 26.638  1.00 12.43 ? 350  HEM B C1B 1 
HETATM 10443 C  C2B . HEM IA 2 .   ? -23.171 -25.605 26.487  1.00 16.83 ? 350  HEM B C2B 1 
HETATM 10444 C  C3B . HEM IA 2 .   ? -23.104 -26.456 27.521  1.00 13.62 ? 350  HEM B C3B 1 
HETATM 10445 C  C4B . HEM IA 2 .   ? -22.025 -26.036 28.375  1.00 11.28 ? 350  HEM B C4B 1 
HETATM 10446 C  CMB . HEM IA 2 .   ? -24.209 -25.640 25.338  1.00 15.57 ? 350  HEM B CMB 1 
HETATM 10447 C  CAB . HEM IA 2 .   ? -24.046 -27.659 27.733  1.00 15.76 ? 350  HEM B CAB 1 
HETATM 10448 C  CBB . HEM IA 2 .   ? -24.290 -28.184 28.939  1.00 12.57 ? 350  HEM B CBB 1 
HETATM 10449 C  C1C . HEM IA 2 .   ? -20.398 -26.389 30.171  1.00 14.59 ? 350  HEM B C1C 1 
HETATM 10450 C  C2C . HEM IA 2 .   ? -19.795 -27.176 31.237  1.00 14.80 ? 350  HEM B C2C 1 
HETATM 10451 C  C3C . HEM IA 2 .   ? -18.762 -26.483 31.694  1.00 11.00 ? 350  HEM B C3C 1 
HETATM 10452 C  C4C . HEM IA 2 .   ? -18.693 -25.241 30.977  1.00 13.69 ? 350  HEM B C4C 1 
HETATM 10453 C  CMC . HEM IA 2 .   ? -20.270 -28.557 31.772  1.00 11.40 ? 350  HEM B CMC 1 
HETATM 10454 C  CAC . HEM IA 2 .   ? -17.802 -26.886 32.838  1.00 17.50 ? 350  HEM B CAC 1 
HETATM 10455 C  CBC . HEM IA 2 .   ? -18.329 -27.456 33.925  1.00 22.76 ? 350  HEM B CBC 1 
HETATM 10456 C  C1D . HEM IA 2 .   ? -17.646 -23.072 30.563  1.00 13.72 ? 350  HEM B C1D 1 
HETATM 10457 C  C2D . HEM IA 2 .   ? -16.727 -22.000 30.899  1.00 10.08 ? 350  HEM B C2D 1 
HETATM 10458 C  C3D . HEM IA 2 .   ? -16.941 -20.950 29.833  1.00 11.94 ? 350  HEM B C3D 1 
HETATM 10459 C  C4D . HEM IA 2 .   ? -17.872 -21.546 28.914  1.00 12.98 ? 350  HEM B C4D 1 
HETATM 10460 C  CMD . HEM IA 2 .   ? -15.800 -21.920 32.129  1.00 6.70  ? 350  HEM B CMD 1 
HETATM 10461 C  CAD . HEM IA 2 .   ? -16.276 -19.555 29.706  1.00 8.66  ? 350  HEM B CAD 1 
HETATM 10462 C  CBD . HEM IA 2 .   ? -14.927 -19.726 29.010  1.00 9.66  ? 350  HEM B CBD 1 
HETATM 10463 C  CGD . HEM IA 2 .   ? -14.188 -18.399 29.022  1.00 16.03 ? 350  HEM B CGD 1 
HETATM 10464 O  O1D . HEM IA 2 .   ? -14.855 -17.333 29.230  1.00 12.97 ? 350  HEM B O1D 1 
HETATM 10465 O  O2D . HEM IA 2 .   ? -12.936 -18.414 28.814  1.00 16.27 ? 350  HEM B O2D 1 
HETATM 10466 N  NA  . HEM IA 2 .   ? -20.027 -22.560 27.063  1.00 15.89 ? 350  HEM B NA  1 
HETATM 10467 N  NB  . HEM IA 2 .   ? -21.359 -25.015 27.717  1.00 15.41 ? 350  HEM B NB  1 
HETATM 10468 N  NC  . HEM IA 2 .   ? -19.615 -25.268 29.957  1.00 12.29 ? 350  HEM B NC  1 
HETATM 10469 N  ND  . HEM IA 2 .   ? -18.262 -22.785 29.370  1.00 14.58 ? 350  HEM B ND  1 
HETATM 10470 FE FE  . HEM IA 2 .   ? -19.766 -23.938 28.510  1.00 14.59 3 350  HEM B FE  1 
HETATM 10471 MG MG  . MG  JA 3 .   ? -16.725 -15.336 23.863  1.00 12.18 2 353  MG  B MG  1 
HETATM 10472 C  C1  . NAG KA 4 .   ? -5.604  -12.238 23.099  1.00 32.07 ? 361  NAG B C1  1 
HETATM 10473 C  C2  . NAG KA 4 .   ? -5.337  -11.739 21.686  1.00 34.04 ? 361  NAG B C2  1 
HETATM 10474 C  C3  . NAG KA 4 .   ? -4.842  -10.301 21.647  1.00 37.74 ? 361  NAG B C3  1 
HETATM 10475 C  C4  . NAG KA 4 .   ? -5.730  -9.386  22.477  1.00 39.77 ? 361  NAG B C4  1 
HETATM 10476 C  C5  . NAG KA 4 .   ? -5.935  -10.015 23.858  1.00 38.60 ? 361  NAG B C5  1 
HETATM 10477 C  C6  . NAG KA 4 .   ? -6.898  -9.172  24.684  1.00 37.93 ? 361  NAG B C6  1 
HETATM 10478 C  C7  . NAG KA 4 .   ? -4.702  -13.107 19.846  1.00 33.10 ? 361  NAG B C7  1 
HETATM 10479 C  C8  . NAG KA 4 .   ? -3.647  -13.963 19.188  1.00 31.09 ? 361  NAG B C8  1 
HETATM 10480 N  N2  . NAG KA 4 .   ? -4.373  -12.562 21.009  1.00 30.38 ? 361  NAG B N2  1 
HETATM 10481 O  O3  . NAG KA 4 .   ? -4.840  -9.893  20.298  1.00 38.09 ? 361  NAG B O3  1 
HETATM 10482 O  O4  . NAG KA 4 .   ? -5.070  -8.142  22.612  1.00 45.44 ? 361  NAG B O4  1 
HETATM 10483 O  O5  . NAG KA 4 .   ? -6.478  -11.315 23.712  1.00 33.36 ? 361  NAG B O5  1 
HETATM 10484 O  O6  . NAG KA 4 .   ? -8.161  -9.186  24.039  1.00 41.12 ? 361  NAG B O6  1 
HETATM 10485 O  O7  . NAG KA 4 .   ? -5.818  -12.954 19.337  1.00 30.39 ? 361  NAG B O7  1 
HETATM 10486 C  C1  . NAG LA 4 .   ? -5.984  -7.013  22.583  1.00 48.89 ? 362  NAG B C1  1 
HETATM 10487 C  C2  . NAG LA 4 .   ? -5.286  -5.794  23.195  1.00 49.47 ? 362  NAG B C2  1 
HETATM 10488 C  C3  . NAG LA 4 .   ? -6.189  -4.569  23.217  1.00 51.17 ? 362  NAG B C3  1 
HETATM 10489 C  C4  . NAG LA 4 .   ? -6.494  -4.245  21.755  1.00 52.35 ? 362  NAG B C4  1 
HETATM 10490 C  C5  . NAG LA 4 .   ? -7.170  -5.481  21.149  1.00 50.51 ? 362  NAG B C5  1 
HETATM 10491 C  C6  . NAG LA 4 .   ? -7.506  -5.261  19.679  1.00 51.11 ? 362  NAG B C6  1 
HETATM 10492 C  C7  . NAG LA 4 .   ? -3.320  -6.443  24.323  1.00 46.31 ? 362  NAG B C7  1 
HETATM 10493 C  C8  . NAG LA 4 .   ? -2.550  -6.743  25.573  1.00 45.43 ? 362  NAG B C8  1 
HETATM 10494 N  N2  . NAG LA 4 .   ? -4.585  -6.055  24.440  1.00 47.42 ? 362  NAG B N2  1 
HETATM 10495 O  O3  . NAG LA 4 .   ? -5.515  -3.503  23.845  1.00 50.95 ? 362  NAG B O3  1 
HETATM 10496 O  O4  . NAG LA 4 .   ? -7.355  -3.125  21.611  1.00 56.77 ? 362  NAG B O4  1 
HETATM 10497 O  O5  . NAG LA 4 .   ? -6.379  -6.657  21.261  1.00 50.11 ? 362  NAG B O5  1 
HETATM 10498 O  O6  . NAG LA 4 .   ? -6.319  -5.242  18.913  1.00 51.27 ? 362  NAG B O6  1 
HETATM 10499 O  O7  . NAG LA 4 .   ? -2.800  -6.583  23.214  1.00 47.05 ? 362  NAG B O7  1 
HETATM 10500 C  C1  . BMA MA 5 .   ? -6.688  -1.838  21.519  1.00 60.25 ? 363  BMA B C1  1 
HETATM 10501 C  C2  . BMA MA 5 .   ? -7.425  -0.972  20.487  1.00 61.59 ? 363  BMA B C2  1 
HETATM 10502 C  C3  . BMA MA 5 .   ? -6.922  0.471   20.443  1.00 63.46 ? 363  BMA B C3  1 
HETATM 10503 C  C4  . BMA MA 5 .   ? -6.814  1.037   21.851  1.00 63.61 ? 363  BMA B C4  1 
HETATM 10504 C  C5  . BMA MA 5 .   ? -6.056  0.098   22.793  1.00 63.23 ? 363  BMA B C5  1 
HETATM 10505 C  C6  . BMA MA 5 .   ? -6.056  0.642   24.230  1.00 62.84 ? 363  BMA B C6  1 
HETATM 10506 O  O2  . BMA MA 5 .   ? -8.813  -0.965  20.759  1.00 59.44 ? 363  BMA B O2  1 
HETATM 10507 O  O3  . BMA MA 5 .   ? -7.864  1.281   19.771  1.00 66.87 ? 363  BMA B O3  1 
HETATM 10508 O  O4  . BMA MA 5 .   ? -6.217  2.314   21.787  1.00 64.11 ? 363  BMA B O4  1 
HETATM 10509 O  O5  . BMA MA 5 .   ? -6.684  -1.173  22.773  1.00 62.69 ? 363  BMA B O5  1 
HETATM 10510 O  O6  . BMA MA 5 .   ? -5.156  -0.044  25.084  1.00 59.86 ? 363  BMA B O6  1 
HETATM 10511 C  C1  . MAN NA 6 .   ? -7.615  1.352   18.346  1.00 70.37 ? 364  MAN B C1  1 
HETATM 10512 C  C2  . MAN NA 6 .   ? -8.191  2.675   17.818  1.00 72.40 ? 364  MAN B C2  1 
HETATM 10513 C  C3  . MAN NA 6 .   ? -9.719  2.666   17.701  1.00 71.53 ? 364  MAN B C3  1 
HETATM 10514 C  C4  . MAN NA 6 .   ? -10.315 1.323   17.260  1.00 70.03 ? 364  MAN B C4  1 
HETATM 10515 C  C5  . MAN NA 6 .   ? -9.560  0.130   17.850  1.00 69.64 ? 364  MAN B C5  1 
HETATM 10516 C  C6  . MAN NA 6 .   ? -10.048 -1.197  17.278  1.00 68.57 ? 364  MAN B C6  1 
HETATM 10517 O  O2  . MAN NA 6 .   ? -7.547  3.148   16.637  1.00 75.71 ? 364  MAN B O2  1 
HETATM 10518 O  O3  . MAN NA 6 .   ? -10.123 3.688   16.818  1.00 72.29 ? 364  MAN B O3  1 
HETATM 10519 O  O4  . MAN NA 6 .   ? -11.674 1.267   17.649  1.00 68.15 ? 364  MAN B O4  1 
HETATM 10520 O  O5  . MAN NA 6 .   ? -8.168  0.260   17.631  1.00 69.53 ? 364  MAN B O5  1 
HETATM 10521 O  O6  . MAN NA 6 .   ? -10.965 -0.938  16.243  1.00 67.84 ? 364  MAN B O6  1 
HETATM 10522 C  C1  . MAN OA 6 .   ? -8.097  2.550   15.437  1.00 78.96 ? 365  MAN B C1  1 
HETATM 10523 C  C2  . MAN OA 6 .   ? -7.291  1.336   14.980  1.00 79.67 ? 365  MAN B C2  1 
HETATM 10524 C  C3  . MAN OA 6 .   ? -5.855  1.745   14.701  1.00 80.08 ? 365  MAN B C3  1 
HETATM 10525 C  C4  . MAN OA 6 .   ? -5.753  3.066   13.923  1.00 80.72 ? 365  MAN B C4  1 
HETATM 10526 C  C5  . MAN OA 6 .   ? -7.007  3.961   13.820  1.00 80.83 ? 365  MAN B C5  1 
HETATM 10527 C  C6  . MAN OA 6 .   ? -7.265  4.372   12.366  1.00 81.52 ? 365  MAN B C6  1 
HETATM 10528 O  O2  . MAN OA 6 .   ? -7.850  0.793   13.802  1.00 79.43 ? 365  MAN B O2  1 
HETATM 10529 O  O3  . MAN OA 6 .   ? -5.190  0.697   14.019  1.00 78.26 ? 365  MAN B O3  1 
HETATM 10530 O  O4  . MAN OA 6 .   ? -4.696  3.830   14.477  1.00 80.47 ? 365  MAN B O4  1 
HETATM 10531 O  O5  . MAN OA 6 .   ? -8.218  3.438   14.344  1.00 80.13 ? 365  MAN B O5  1 
HETATM 10532 O  O6  . MAN OA 6 .   ? -7.133  5.772   12.206  1.00 81.99 ? 365  MAN B O6  1 
HETATM 10533 C  C1  . NAG PA 4 .   ? -10.237 -16.771 47.432  1.00 22.44 ? 371  NAG B C1  1 
HETATM 10534 C  C2  . NAG PA 4 .   ? -11.224 -16.658 48.602  1.00 22.38 ? 371  NAG B C2  1 
HETATM 10535 C  C3  . NAG PA 4 .   ? -10.880 -15.538 49.576  1.00 26.49 ? 371  NAG B C3  1 
HETATM 10536 C  C4  . NAG PA 4 .   ? -9.418  -15.567 50.033  1.00 29.30 ? 371  NAG B C4  1 
HETATM 10537 C  C5  . NAG PA 4 .   ? -8.493  -15.878 48.845  1.00 27.00 ? 371  NAG B C5  1 
HETATM 10538 C  C6  . NAG PA 4 .   ? -7.118  -16.252 49.391  1.00 29.49 ? 371  NAG B C6  1 
HETATM 10539 C  C7  . NAG PA 4 .   ? -13.378 -17.607 48.207  1.00 19.95 ? 371  NAG B C7  1 
HETATM 10540 C  C8  . NAG PA 4 .   ? -14.837 -17.455 47.930  1.00 16.98 ? 371  NAG B C8  1 
HETATM 10541 N  N2  . NAG PA 4 .   ? -12.615 -16.511 48.217  1.00 20.36 ? 371  NAG B N2  1 
HETATM 10542 O  O3  . NAG PA 4 .   ? -11.782 -15.542 50.662  1.00 23.17 ? 371  NAG B O3  1 
HETATM 10543 O  O4  . NAG PA 4 .   ? -9.072  -14.257 50.434  1.00 36.41 ? 371  NAG B O4  1 
HETATM 10544 O  O5  . NAG PA 4 .   ? -8.942  -16.926 47.978  1.00 23.72 ? 371  NAG B O5  1 
HETATM 10545 O  O6  . NAG PA 4 .   ? -7.158  -17.581 49.894  1.00 29.82 ? 371  NAG B O6  1 
HETATM 10546 O  O7  . NAG PA 4 .   ? -12.902 -18.722 48.384  1.00 18.60 ? 371  NAG B O7  1 
HETATM 10547 C  C1  . NAG QA 4 .   ? -9.267  -13.966 51.824  1.00 43.34 ? 372  NAG B C1  1 
HETATM 10548 C  C2  . NAG QA 4 .   ? -8.229  -12.936 52.259  1.00 48.34 ? 372  NAG B C2  1 
HETATM 10549 C  C3  . NAG QA 4 .   ? -8.322  -12.674 53.765  1.00 49.94 ? 372  NAG B C3  1 
HETATM 10550 C  C4  . NAG QA 4 .   ? -9.770  -12.459 54.207  1.00 50.23 ? 372  NAG B C4  1 
HETATM 10551 C  C5  . NAG QA 4 .   ? -10.706 -13.438 53.514  1.00 47.77 ? 372  NAG B C5  1 
HETATM 10552 C  C6  . NAG QA 4 .   ? -12.164 -13.188 53.878  1.00 47.84 ? 372  NAG B C6  1 
HETATM 10553 C  C7  . NAG QA 4 .   ? -6.349  -12.920 50.709  1.00 51.63 ? 372  NAG B C7  1 
HETATM 10554 C  C8  . NAG QA 4 .   ? -4.917  -13.322 50.478  1.00 50.19 ? 372  NAG B C8  1 
HETATM 10555 N  N2  . NAG QA 4 .   ? -6.873  -13.299 51.877  1.00 49.84 ? 372  NAG B N2  1 
HETATM 10556 O  O3  . NAG QA 4 .   ? -7.550  -11.537 54.100  1.00 50.49 ? 372  NAG B O3  1 
HETATM 10557 O  O4  . NAG QA 4 .   ? -9.878  -12.616 55.608  1.00 53.31 ? 372  NAG B O4  1 
HETATM 10558 O  O5  . NAG QA 4 .   ? -10.501 -13.355 52.123  1.00 44.62 ? 372  NAG B O5  1 
HETATM 10559 O  O6  . NAG QA 4 .   ? -12.509 -11.875 53.494  1.00 49.03 ? 372  NAG B O6  1 
HETATM 10560 O  O7  . NAG QA 4 .   ? -6.991  -12.301 49.844  1.00 52.09 ? 372  NAG B O7  1 
HETATM 10561 C  C1  . NAG RA 4 .   ? -18.902 -4.185  14.158  1.00 39.21 ? 381  NAG B C1  1 
HETATM 10562 C  C2  . NAG RA 4 .   ? -18.457 -5.127  13.046  1.00 42.07 ? 381  NAG B C2  1 
HETATM 10563 C  C3  . NAG RA 4 .   ? -19.021 -4.775  11.677  1.00 44.07 ? 381  NAG B C3  1 
HETATM 10564 C  C4  . NAG RA 4 .   ? -20.486 -4.356  11.781  1.00 46.25 ? 381  NAG B C4  1 
HETATM 10565 C  C5  . NAG RA 4 .   ? -20.616 -3.334  12.901  1.00 44.42 ? 381  NAG B C5  1 
HETATM 10566 C  C6  . NAG RA 4 .   ? -22.009 -2.728  13.004  1.00 42.37 ? 381  NAG B C6  1 
HETATM 10567 C  C7  . NAG RA 4 .   ? -16.416 -6.359  12.954  1.00 41.93 ? 381  NAG B C7  1 
HETATM 10568 C  C8  . NAG RA 4 .   ? -14.924 -6.363  12.843  1.00 42.53 ? 381  NAG B C8  1 
HETATM 10569 N  N2  . NAG RA 4 .   ? -17.014 -5.179  12.961  1.00 41.32 ? 381  NAG B N2  1 
HETATM 10570 O  O3  . NAG RA 4 .   ? -18.869 -5.921  10.870  1.00 45.13 ? 381  NAG B O3  1 
HETATM 10571 O  O4  . NAG RA 4 .   ? -20.932 -3.694  10.623  1.00 53.00 ? 381  NAG B O4  1 
HETATM 10572 O  O5  . NAG RA 4 .   ? -20.294 -4.009  14.076  1.00 40.40 ? 381  NAG B O5  1 
HETATM 10573 O  O6  . NAG RA 4 .   ? -22.957 -3.771  13.043  1.00 43.88 ? 381  NAG B O6  1 
HETATM 10574 O  O7  . NAG RA 4 .   ? -17.051 -7.410  13.006  1.00 43.01 ? 381  NAG B O7  1 
HETATM 10575 C  C1  . NAG SA 4 .   ? -20.733 -4.477  9.439   1.00 57.33 ? 382  NAG B C1  1 
HETATM 10576 C  C2  . NAG SA 4 .   ? -22.019 -4.381  8.626   1.00 58.70 ? 382  NAG B C2  1 
HETATM 10577 C  C3  . NAG SA 4 .   ? -21.844 -4.853  7.184   1.00 60.76 ? 382  NAG B C3  1 
HETATM 10578 C  C4  . NAG SA 4 .   ? -20.573 -4.263  6.581   1.00 62.00 ? 382  NAG B C4  1 
HETATM 10579 C  C5  . NAG SA 4 .   ? -19.412 -4.622  7.497   1.00 62.13 ? 382  NAG B C5  1 
HETATM 10580 C  C6  . NAG SA 4 .   ? -18.074 -4.165  6.929   1.00 63.12 ? 382  NAG B C6  1 
HETATM 10581 C  C7  . NAG SA 4 .   ? -24.135 -4.486  9.786   1.00 58.61 ? 382  NAG B C7  1 
HETATM 10582 C  C8  . NAG SA 4 .   ? -25.216 -5.344  10.378  1.00 58.80 ? 382  NAG B C8  1 
HETATM 10583 N  N2  . NAG SA 4 .   ? -23.090 -5.119  9.264   1.00 57.84 ? 382  NAG B N2  1 
HETATM 10584 O  O3  . NAG SA 4 .   ? -22.969 -4.431  6.454   1.00 61.75 ? 382  NAG B O3  1 
HETATM 10585 O  O4  . NAG SA 4 .   ? -20.335 -4.720  5.265   1.00 63.06 ? 382  NAG B O4  1 
HETATM 10586 O  O5  . NAG SA 4 .   ? -19.644 -3.946  8.711   1.00 59.82 ? 382  NAG B O5  1 
HETATM 10587 O  O6  . NAG SA 4 .   ? -17.727 -2.943  7.538   1.00 64.14 ? 382  NAG B O6  1 
HETATM 10588 O  O7  . NAG SA 4 .   ? -24.223 -3.257  9.821   1.00 59.98 ? 382  NAG B O7  1 
HETATM 10589 C  C1  . NAG TA 4 .   ? -44.895 -15.195 21.522  1.00 30.39 ? 391  NAG B C1  1 
HETATM 10590 C  C2  . NAG TA 4 .   ? -45.993 -14.427 22.286  1.00 31.39 ? 391  NAG B C2  1 
HETATM 10591 C  C3  . NAG TA 4 .   ? -47.393 -14.749 21.757  1.00 30.69 ? 391  NAG B C3  1 
HETATM 10592 C  C4  . NAG TA 4 .   ? -47.457 -14.643 20.234  1.00 31.71 ? 391  NAG B C4  1 
HETATM 10593 C  C5  . NAG TA 4 .   ? -46.275 -15.282 19.514  1.00 32.18 ? 391  NAG B C5  1 
HETATM 10594 C  C6  . NAG TA 4 .   ? -46.240 -14.667 18.122  1.00 30.03 ? 391  NAG B C6  1 
HETATM 10595 C  C7  . NAG TA 4 .   ? -45.961 -13.708 24.625  1.00 29.49 ? 391  NAG B C7  1 
HETATM 10596 C  C8  . NAG TA 4 .   ? -46.048 -14.053 26.089  1.00 31.88 ? 391  NAG B C8  1 
HETATM 10597 N  N2  . NAG TA 4 .   ? -45.998 -14.705 23.726  1.00 29.66 ? 391  NAG B N2  1 
HETATM 10598 O  O3  . NAG TA 4 .   ? -48.315 -13.833 22.316  1.00 26.30 ? 391  NAG B O3  1 
HETATM 10599 O  O4  . NAG TA 4 .   ? -48.620 -15.275 19.736  1.00 31.38 ? 391  NAG B O4  1 
HETATM 10600 O  O5  . NAG TA 4 .   ? -45.021 -15.037 20.117  1.00 29.52 ? 391  NAG B O5  1 
HETATM 10601 O  O6  . NAG TA 4 .   ? -45.230 -15.333 17.423  1.00 37.12 ? 391  NAG B O6  1 
HETATM 10602 O  O7  . NAG TA 4 .   ? -45.859 -12.532 24.311  1.00 28.42 ? 391  NAG B O7  1 
HETATM 10603 C  C1  . NAG UA 4 .   ? -49.317 -14.384 18.851  1.00 30.28 ? 392  NAG B C1  1 
HETATM 10604 C  C2  . NAG UA 4 .   ? -50.315 -15.151 17.973  1.00 30.75 ? 392  NAG B C2  1 
HETATM 10605 C  C3  . NAG UA 4 .   ? -51.075 -14.152 17.083  1.00 32.01 ? 392  NAG B C3  1 
HETATM 10606 C  C4  . NAG UA 4 .   ? -51.609 -12.956 17.864  1.00 32.71 ? 392  NAG B C4  1 
HETATM 10607 C  C5  . NAG UA 4 .   ? -50.404 -12.380 18.618  1.00 33.69 ? 392  NAG B C5  1 
HETATM 10608 C  C6  . NAG UA 4 .   ? -50.682 -11.093 19.366  1.00 34.93 ? 392  NAG B C6  1 
HETATM 10609 C  C7  . NAG UA 4 .   ? -49.453 -17.363 17.458  1.00 26.70 ? 392  NAG B C7  1 
HETATM 10610 C  C8  . NAG UA 4 .   ? -48.637 -18.224 16.541  1.00 23.07 ? 392  NAG B C8  1 
HETATM 10611 N  N2  . NAG UA 4 .   ? -49.585 -16.083 17.126  1.00 26.17 ? 392  NAG B N2  1 
HETATM 10612 O  O3  . NAG UA 4 .   ? -52.130 -14.805 16.431  1.00 34.09 ? 392  NAG B O3  1 
HETATM 10613 O  O4  . NAG UA 4 .   ? -52.085 -12.005 16.936  1.00 33.19 ? 392  NAG B O4  1 
HETATM 10614 O  O5  . NAG UA 4 .   ? -49.973 -13.344 19.541  1.00 31.81 ? 392  NAG B O5  1 
HETATM 10615 O  O6  . NAG UA 4 .   ? -51.586 -11.435 20.382  1.00 40.04 ? 392  NAG B O6  1 
HETATM 10616 O  O7  . NAG UA 4 .   ? -49.951 -17.848 18.478  1.00 27.69 ? 392  NAG B O7  1 
HETATM 10617 C  C1  . BMA VA 5 .   ? -53.517 -11.838 16.923  1.00 33.92 ? 393  BMA B C1  1 
HETATM 10618 C  C2  . BMA VA 5 .   ? -53.847 -10.375 16.607  1.00 34.70 ? 393  BMA B C2  1 
HETATM 10619 C  C3  . BMA VA 5 .   ? -55.338 -10.182 16.299  1.00 37.09 ? 393  BMA B C3  1 
HETATM 10620 C  C4  . BMA VA 5 .   ? -55.818 -11.192 15.269  1.00 35.61 ? 393  BMA B C4  1 
HETATM 10621 C  C5  . BMA VA 5 .   ? -55.438 -12.599 15.704  1.00 33.95 ? 393  BMA B C5  1 
HETATM 10622 C  C6  . BMA VA 5 .   ? -55.764 -13.618 14.615  1.00 31.91 ? 393  BMA B C6  1 
HETATM 10623 O  O2  . BMA VA 5 .   ? -53.101 -9.959  15.484  1.00 33.99 ? 393  BMA B O2  1 
HETATM 10624 O  O3  . BMA VA 5 .   ? -55.601 -8.908  15.763  1.00 36.70 ? 393  BMA B O3  1 
HETATM 10625 O  O4  . BMA VA 5 .   ? -57.217 -11.091 15.144  1.00 34.42 ? 393  BMA B O4  1 
HETATM 10626 O  O5  . BMA VA 5 .   ? -54.050 -12.663 15.910  1.00 34.61 ? 393  BMA B O5  1 
HETATM 10627 O  O6  . BMA VA 5 .   ? -55.239 -14.850 15.044  1.00 30.22 ? 393  BMA B O6  1 
HETATM 10628 C  C1  . MAN WA 6 .   ? -55.952 -8.019  16.834  1.00 41.48 ? 394  MAN B C1  1 
HETATM 10629 C  C2  . MAN WA 6 .   ? -56.733 -6.853  16.244  1.00 45.15 ? 394  MAN B C2  1 
HETATM 10630 C  C3  . MAN WA 6 .   ? -55.851 -6.190  15.206  1.00 44.83 ? 394  MAN B C3  1 
HETATM 10631 C  C4  . MAN WA 6 .   ? -54.642 -5.654  15.960  1.00 45.14 ? 394  MAN B C4  1 
HETATM 10632 C  C5  . MAN WA 6 .   ? -53.927 -6.814  16.659  1.00 43.56 ? 394  MAN B C5  1 
HETATM 10633 C  C6  . MAN WA 6 .   ? -52.725 -6.334  17.473  1.00 43.00 ? 394  MAN B C6  1 
HETATM 10634 O  O2  . MAN WA 6 .   ? -56.967 -5.898  17.256  1.00 50.15 ? 394  MAN B O2  1 
HETATM 10635 O  O3  . MAN WA 6 .   ? -56.557 -5.125  14.623  1.00 45.70 ? 394  MAN B O3  1 
HETATM 10636 O  O4  . MAN WA 6 .   ? -53.791 -4.918  15.100  1.00 43.47 ? 394  MAN B O4  1 
HETATM 10637 O  O5  . MAN WA 6 .   ? -54.834 -7.500  17.513  1.00 42.41 ? 394  MAN B O5  1 
HETATM 10638 O  O6  . MAN WA 6 .   ? -52.564 -7.149  18.616  1.00 40.31 ? 394  MAN B O6  1 
HETATM 10639 C  C1  . MAN XA 6 .   ? -58.264 -6.076  17.873  1.00 54.09 ? 395  MAN B C1  1 
HETATM 10640 C  C2  . MAN XA 6 .   ? -58.519 -4.891  18.807  1.00 55.98 ? 395  MAN B C2  1 
HETATM 10641 C  C3  . MAN XA 6 .   ? -57.908 -5.150  20.184  1.00 56.80 ? 395  MAN B C3  1 
HETATM 10642 C  C4  . MAN XA 6 .   ? -58.451 -6.466  20.711  1.00 56.77 ? 395  MAN B C4  1 
HETATM 10643 C  C5  . MAN XA 6 .   ? -58.010 -7.586  19.778  1.00 55.68 ? 395  MAN B C5  1 
HETATM 10644 C  C6  . MAN XA 6 .   ? -58.511 -8.919  20.334  1.00 53.52 ? 395  MAN B C6  1 
HETATM 10645 O  O2  . MAN XA 6 .   ? -59.902 -4.599  18.892  1.00 56.29 ? 395  MAN B O2  1 
HETATM 10646 O  O3  . MAN XA 6 .   ? -58.194 -4.100  21.084  1.00 57.49 ? 395  MAN B O3  1 
HETATM 10647 O  O4  . MAN XA 6 .   ? -57.972 -6.719  22.014  1.00 58.17 ? 395  MAN B O4  1 
HETATM 10648 O  O5  . MAN XA 6 .   ? -58.505 -7.358  18.466  1.00 54.32 ? 395  MAN B O5  1 
HETATM 10649 O  O6  . MAN XA 6 .   ? -57.649 -9.985  19.988  1.00 52.23 ? 395  MAN B O6  1 
HETATM 10650 C  C1  . MAN YA 6 .   ? -55.768 -15.946 14.281  1.00 28.98 ? 396  MAN B C1  1 
HETATM 10651 C  C2  . MAN YA 6 .   ? -55.492 -17.243 15.038  1.00 29.82 ? 396  MAN B C2  1 
HETATM 10652 C  C3  . MAN YA 6 .   ? -53.985 -17.469 15.101  1.00 30.67 ? 396  MAN B C3  1 
HETATM 10653 C  C4  . MAN YA 6 .   ? -53.434 -17.439 13.685  1.00 29.65 ? 396  MAN B C4  1 
HETATM 10654 C  C5  . MAN YA 6 .   ? -53.906 -16.315 12.759  1.00 33.36 ? 396  MAN B C5  1 
HETATM 10655 C  C6  . MAN YA 6 .   ? -53.761 -16.898 11.348  1.00 36.56 ? 396  MAN B C6  1 
HETATM 10656 O  O2  . MAN YA 6 .   ? -56.095 -18.359 14.391  1.00 26.84 ? 396  MAN B O2  1 
HETATM 10657 O  O3  . MAN YA 6 .   ? -53.771 -18.789 15.561  1.00 32.50 ? 396  MAN B O3  1 
HETATM 10658 O  O4  . MAN YA 6 .   ? -52.035 -17.496 13.707  1.00 33.34 ? 396  MAN B O4  1 
HETATM 10659 O  O5  . MAN YA 6 .   ? -55.277 -15.970 12.953  1.00 30.70 ? 396  MAN B O5  1 
HETATM 10660 O  O6  . MAN YA 6 .   ? -53.206 -15.973 10.442  1.00 45.36 ? 396  MAN B O6  1 
HETATM 10661 C  C1  . MAN ZA 6 .   ? -52.928 -18.810 16.717  1.00 32.57 ? 397  MAN B C1  1 
HETATM 10662 C  C2  . MAN ZA 6 .   ? -52.439 -20.244 16.916  1.00 31.65 ? 397  MAN B C2  1 
HETATM 10663 C  C3  . MAN ZA 6 .   ? -53.620 -21.128 17.279  1.00 31.08 ? 397  MAN B C3  1 
HETATM 10664 C  C4  . MAN ZA 6 .   ? -54.344 -20.552 18.489  1.00 31.88 ? 397  MAN B C4  1 
HETATM 10665 C  C5  . MAN ZA 6 .   ? -54.725 -19.095 18.253  1.00 31.06 ? 397  MAN B C5  1 
HETATM 10666 C  C6  . MAN ZA 6 .   ? -55.393 -18.486 19.488  1.00 31.97 ? 397  MAN B C6  1 
HETATM 10667 O  O2  . MAN ZA 6 .   ? -51.510 -20.279 17.982  1.00 29.77 ? 397  MAN B O2  1 
HETATM 10668 O  O3  . MAN ZA 6 .   ? -53.188 -22.422 17.622  1.00 27.14 ? 397  MAN B O3  1 
HETATM 10669 O  O4  . MAN ZA 6 .   ? -55.500 -21.338 18.688  1.00 34.92 ? 397  MAN B O4  1 
HETATM 10670 O  O5  . MAN ZA 6 .   ? -53.591 -18.330 17.880  1.00 32.91 ? 397  MAN B O5  1 
HETATM 10671 O  O6  . MAN ZA 6 .   ? -56.156 -17.354 19.095  1.00 31.71 ? 397  MAN B O6  1 
HETATM 10672 C  C1  . MAN AB 6 .   ? -52.932 -16.617 9.168   1.00 49.06 ? 398  MAN B C1  1 
HETATM 10673 C  C2  . MAN AB 6 .   ? -53.560 -18.017 8.996   1.00 49.04 ? 398  MAN B C2  1 
HETATM 10674 C  C3  . MAN AB 6 .   ? -52.750 -19.156 9.595   1.00 50.87 ? 398  MAN B C3  1 
HETATM 10675 C  C4  . MAN AB 6 .   ? -51.250 -18.944 9.449   1.00 51.34 ? 398  MAN B C4  1 
HETATM 10676 C  C5  . MAN AB 6 .   ? -50.885 -17.500 9.778   1.00 51.15 ? 398  MAN B C5  1 
HETATM 10677 C  C6  . MAN AB 6 .   ? -49.387 -17.234 9.699   1.00 51.82 ? 398  MAN B C6  1 
HETATM 10678 O  O2  . MAN AB 6 .   ? -53.683 -18.355 7.630   1.00 47.85 ? 398  MAN B O2  1 
HETATM 10679 O  O3  . MAN AB 6 .   ? -53.105 -20.354 8.939   1.00 49.44 ? 398  MAN B O3  1 
HETATM 10680 O  O4  . MAN AB 6 .   ? -50.621 -19.833 10.346  1.00 52.88 ? 398  MAN B O4  1 
HETATM 10681 O  O5  . MAN AB 6 .   ? -51.552 -16.654 8.876   1.00 50.55 ? 398  MAN B O5  1 
HETATM 10682 O  O6  . MAN AB 6 .   ? -48.774 -17.903 10.777  1.00 52.85 ? 398  MAN B O6  1 
HETATM 10683 C  C1  . NAG BB 4 .   ? -22.091 -44.554 43.821  1.00 51.72 ? 411  NAG B C1  1 
HETATM 10684 C  C2  . NAG BB 4 .   ? -22.075 -45.867 44.608  1.00 57.85 ? 411  NAG B C2  1 
HETATM 10685 C  C3  . NAG BB 4 .   ? -20.837 -45.945 45.503  1.00 60.03 ? 411  NAG B C3  1 
HETATM 10686 C  C4  . NAG BB 4 .   ? -19.583 -45.607 44.709  1.00 61.56 ? 411  NAG B C4  1 
HETATM 10687 C  C5  . NAG BB 4 .   ? -19.798 -44.226 44.104  1.00 57.87 ? 411  NAG B C5  1 
HETATM 10688 C  C6  . NAG BB 4 .   ? -18.532 -43.666 43.461  1.00 56.06 ? 411  NAG B C6  1 
HETATM 10689 C  C7  . NAG BB 4 .   ? -24.280 -46.797 45.103  1.00 59.52 ? 411  NAG B C7  1 
HETATM 10690 C  C8  . NAG BB 4 .   ? -25.486 -46.771 45.997  1.00 59.28 ? 411  NAG B C8  1 
HETATM 10691 N  N2  . NAG BB 4 .   ? -23.289 -45.957 45.407  1.00 57.98 ? 411  NAG B N2  1 
HETATM 10692 O  O3  . NAG BB 4 .   ? -20.707 -47.221 46.090  1.00 62.44 ? 411  NAG B O3  1 
HETATM 10693 O  O4  . NAG BB 4 .   ? -18.462 -45.585 45.569  1.00 69.37 ? 411  NAG B O4  1 
HETATM 10694 O  O5  . NAG BB 4 .   ? -20.854 -44.325 43.178  1.00 52.31 ? 411  NAG B O5  1 
HETATM 10695 O  O6  . NAG BB 4 .   ? -18.163 -44.454 42.353  1.00 56.15 ? 411  NAG B O6  1 
HETATM 10696 O  O7  . NAG BB 4 .   ? -24.239 -47.570 44.144  1.00 60.39 ? 411  NAG B O7  1 
HETATM 10697 C  C1  . NAG CB 4 .   ? -17.326 -46.192 44.921  1.00 74.82 ? 412  NAG B C1  1 
HETATM 10698 C  C2  . NAG CB 4 .   ? -16.218 -46.430 45.939  1.00 76.85 ? 412  NAG B C2  1 
HETATM 10699 C  C3  . NAG CB 4 .   ? -14.976 -46.965 45.225  1.00 77.94 ? 412  NAG B C3  1 
HETATM 10700 C  C4  . NAG CB 4 .   ? -15.343 -48.201 44.399  1.00 78.67 ? 412  NAG B C4  1 
HETATM 10701 C  C5  . NAG CB 4 .   ? -16.584 -47.949 43.535  1.00 78.56 ? 412  NAG B C5  1 
HETATM 10702 C  C6  . NAG CB 4 .   ? -17.088 -49.227 42.865  1.00 79.58 ? 412  NAG B C6  1 
HETATM 10703 C  C7  . NAG CB 4 .   ? -16.041 -45.187 48.020  1.00 77.49 ? 412  NAG B C7  1 
HETATM 10704 C  C8  . NAG CB 4 .   ? -16.514 -46.442 48.697  1.00 77.27 ? 412  NAG B C8  1 
HETATM 10705 N  N2  . NAG CB 4 .   ? -15.929 -45.224 46.693  1.00 77.26 ? 412  NAG B N2  1 
HETATM 10706 O  O3  . NAG CB 4 .   ? -13.963 -47.281 46.162  1.00 77.46 ? 412  NAG B O3  1 
HETATM 10707 O  O4  . NAG CB 4 .   ? -14.247 -48.589 43.592  1.00 78.54 ? 412  NAG B O4  1 
HETATM 10708 O  O5  . NAG CB 4 .   ? -17.637 -47.433 44.324  1.00 77.43 ? 412  NAG B O5  1 
HETATM 10709 O  O6  . NAG CB 4 .   ? -16.141 -49.687 41.922  1.00 81.17 ? 412  NAG B O6  1 
HETATM 10710 O  O7  . NAG CB 4 .   ? -15.790 -44.177 48.677  1.00 77.38 ? 412  NAG B O7  1 
HETATM 10711 C  C   . ACT DB 7 .   ? -22.782 -22.076 29.914  1.00 30.15 ? 1328 ACT B C   1 
HETATM 10712 O  O   . ACT DB 7 .   ? -21.668 -22.072 29.323  1.00 32.68 ? 1328 ACT B O   1 
HETATM 10713 O  OXT . ACT DB 7 .   ? -23.345 -20.966 30.112  1.00 25.93 ? 1328 ACT B OXT 1 
HETATM 10714 C  CH3 . ACT DB 7 .   ? -23.360 -23.365 30.411  1.00 25.64 ? 1328 ACT B CH3 1 
HETATM 10715 S  S   . SO4 EB 8 .   ? -16.659 -29.069 6.780   1.00 61.72 ? 1329 SO4 B S   1 
HETATM 10716 O  O1  . SO4 EB 8 .   ? -15.655 -28.007 6.642   1.00 62.36 ? 1329 SO4 B O1  1 
HETATM 10717 O  O2  . SO4 EB 8 .   ? -17.966 -28.476 6.484   1.00 57.83 ? 1329 SO4 B O2  1 
HETATM 10718 O  O3  . SO4 EB 8 .   ? -16.309 -30.129 5.828   1.00 60.43 ? 1329 SO4 B O3  1 
HETATM 10719 O  O4  . SO4 EB 8 .   ? -16.645 -29.647 8.133   1.00 58.87 ? 1329 SO4 B O4  1 
HETATM 10720 S  S   . SO4 FB 8 .   ? -11.401 -24.027 13.760  1.00 65.17 ? 1330 SO4 B S   1 
HETATM 10721 O  O1  . SO4 FB 8 .   ? -10.317 -23.502 14.593  1.00 65.08 ? 1330 SO4 B O1  1 
HETATM 10722 O  O2  . SO4 FB 8 .   ? -11.562 -23.144 12.609  1.00 66.77 ? 1330 SO4 B O2  1 
HETATM 10723 O  O3  . SO4 FB 8 .   ? -11.086 -25.386 13.310  1.00 65.62 ? 1330 SO4 B O3  1 
HETATM 10724 O  O4  . SO4 FB 8 .   ? -12.666 -24.067 14.499  1.00 65.77 ? 1330 SO4 B O4  1 
HETATM 10725 S  S   . SO4 GB 8 .   ? -39.577 -11.930 35.469  1.00 69.71 ? 1331 SO4 B S   1 
HETATM 10726 O  O1  . SO4 GB 8 .   ? -38.568 -12.941 35.792  1.00 69.10 ? 1331 SO4 B O1  1 
HETATM 10727 O  O2  . SO4 GB 8 .   ? -40.788 -12.588 34.978  1.00 71.91 ? 1331 SO4 B O2  1 
HETATM 10728 O  O3  . SO4 GB 8 .   ? -39.919 -11.183 36.677  1.00 69.41 ? 1331 SO4 B O3  1 
HETATM 10729 O  O4  . SO4 GB 8 .   ? -39.072 -11.030 34.434  1.00 68.79 ? 1331 SO4 B O4  1 
HETATM 10730 C  CHA . HEM HB 2 .   ? 38.115  -21.852 8.466   1.00 20.84 ? 350  HEM C CHA 1 
HETATM 10731 C  CHB . HEM HB 2 .   ? 35.191  -25.157 6.519   1.00 17.72 ? 350  HEM C CHB 1 
HETATM 10732 C  CHC . HEM HB 2 .   ? 36.062  -28.294 10.102  1.00 18.31 ? 350  HEM C CHC 1 
HETATM 10733 C  CHD . HEM HB 2 .   ? 39.405  -25.135 11.761  1.00 18.29 ? 350  HEM C CHD 1 
HETATM 10734 C  C1A . HEM HB 2 .   ? 37.279  -22.508 7.599   1.00 19.15 ? 350  HEM C C1A 1 
HETATM 10735 C  C2A . HEM HB 2 .   ? 36.792  -21.951 6.344   1.00 16.10 ? 350  HEM C C2A 1 
HETATM 10736 C  C3A . HEM HB 2 .   ? 35.978  -22.875 5.825   1.00 14.78 ? 350  HEM C C3A 1 
HETATM 10737 C  C4A . HEM HB 2 .   ? 35.950  -24.037 6.705   1.00 17.07 ? 350  HEM C C4A 1 
HETATM 10738 C  CMA . HEM HB 2 .   ? 35.180  -22.727 4.524   1.00 14.90 ? 350  HEM C CMA 1 
HETATM 10739 C  CAA . HEM HB 2 .   ? 37.096  -20.538 5.752   1.00 15.52 ? 350  HEM C CAA 1 
HETATM 10740 C  CBA . HEM HB 2 .   ? 36.425  -19.421 6.568   1.00 15.25 ? 350  HEM C CBA 1 
HETATM 10741 C  CGA . HEM HB 2 .   ? 37.204  -18.116 6.491   1.00 18.90 ? 350  HEM C CGA 1 
HETATM 10742 O  O1A . HEM HB 2 .   ? 37.008  -17.314 5.541   1.00 19.24 ? 350  HEM C O1A 1 
HETATM 10743 O  O2A . HEM HB 2 .   ? 38.104  -17.884 7.342   1.00 16.86 ? 350  HEM C O2A 1 
HETATM 10744 C  C1B . HEM HB 2 .   ? 35.119  -26.252 7.340   1.00 16.27 ? 350  HEM C C1B 1 
HETATM 10745 C  C2B . HEM HB 2 .   ? 34.264  -27.396 7.121   1.00 14.96 ? 350  HEM C C2B 1 
HETATM 10746 C  C3B . HEM HB 2 .   ? 34.482  -28.254 8.118   1.00 14.24 ? 350  HEM C C3B 1 
HETATM 10747 C  C4B . HEM HB 2 .   ? 35.505  -27.700 8.983   1.00 17.85 ? 350  HEM C C4B 1 
HETATM 10748 C  CMB . HEM HB 2 .   ? 33.294  -27.624 5.926   1.00 13.13 ? 350  HEM C CMB 1 
HETATM 10749 C  CAB . HEM HB 2 .   ? 33.831  -29.650 8.236   1.00 15.17 ? 350  HEM C CAB 1 
HETATM 10750 C  CBB . HEM HB 2 .   ? 33.345  -30.070 9.402   1.00 16.96 ? 350  HEM C CBB 1 
HETATM 10751 C  C1C . HEM HB 2 .   ? 37.120  -27.734 10.779  1.00 19.09 ? 350  HEM C C1C 1 
HETATM 10752 C  C2C . HEM HB 2 .   ? 37.915  -28.386 11.800  1.00 17.48 ? 350  HEM C C2C 1 
HETATM 10753 C  C3C . HEM HB 2 .   ? 38.845  -27.503 12.209  1.00 17.68 ? 350  HEM C C3C 1 
HETATM 10754 C  C4C . HEM HB 2 .   ? 38.663  -26.264 11.501  1.00 18.53 ? 350  HEM C C4C 1 
HETATM 10755 C  CMC . HEM HB 2 .   ? 37.719  -29.840 12.288  1.00 17.92 ? 350  HEM C CMC 1 
HETATM 10756 C  CAC . HEM HB 2 .   ? 39.926  -27.704 13.283  1.00 19.37 ? 350  HEM C CAC 1 
HETATM 10757 C  CBC . HEM HB 2 .   ? 39.739  -28.645 14.211  1.00 23.79 ? 350  HEM C CBC 1 
HETATM 10758 C  C1D . HEM HB 2 .   ? 39.278  -23.923 11.155  1.00 16.73 ? 350  HEM C C1D 1 
HETATM 10759 C  C2D . HEM HB 2 .   ? 39.953  -22.707 11.538  1.00 18.00 ? 350  HEM C C2D 1 
HETATM 10760 C  C3D . HEM HB 2 .   ? 39.521  -21.679 10.500  1.00 18.77 ? 350  HEM C C3D 1 
HETATM 10761 C  C4D . HEM HB 2 .   ? 38.644  -22.389 9.600   1.00 18.71 ? 350  HEM C C4D 1 
HETATM 10762 C  CMD . HEM HB 2 .   ? 40.838  -22.422 12.772  1.00 17.94 ? 350  HEM C CMD 1 
HETATM 10763 C  CAD . HEM HB 2 .   ? 39.899  -20.182 10.453  1.00 19.53 ? 350  HEM C CAD 1 
HETATM 10764 C  CBD . HEM HB 2 .   ? 41.190  -20.086 9.663   1.00 19.87 ? 350  HEM C CBD 1 
HETATM 10765 C  CGD . HEM HB 2 .   ? 41.739  -18.699 9.771   1.00 22.84 ? 350  HEM C CGD 1 
HETATM 10766 O  O1D . HEM HB 2 .   ? 40.966  -17.772 10.089  1.00 22.75 ? 350  HEM C O1D 1 
HETATM 10767 O  O2D . HEM HB 2 .   ? 42.950  -18.509 9.497   1.00 26.01 ? 350  HEM C O2D 1 
HETATM 10768 N  NA  . HEM HB 2 .   ? 36.793  -23.805 7.767   1.00 17.85 ? 350  HEM C NA  1 
HETATM 10769 N  NB  . HEM HB 2 .   ? 35.890  -26.477 8.466   1.00 16.32 ? 350  HEM C NB  1 
HETATM 10770 N  NC  . HEM HB 2 .   ? 37.617  -26.439 10.599  1.00 19.29 ? 350  HEM C NC  1 
HETATM 10771 N  ND  . HEM HB 2 .   ? 38.579  -23.721 9.963   1.00 19.00 ? 350  HEM C ND  1 
HETATM 10772 FE FE  . HEM HB 2 .   ? 37.233  -25.162 9.176   1.00 18.01 3 350  HEM C FE  1 
HETATM 10773 MG MG  . MG  IB 3 .   ? 38.261  -15.983 4.843   1.00 19.87 2 353  MG  C MG  1 
HETATM 10774 C  C1  . NAG JB 4 .   ? 49.123  -10.903 3.679   1.00 41.73 ? 361  NAG C C1  1 
HETATM 10775 C  C2  . NAG JB 4 .   ? 49.240  -10.307 2.284   1.00 44.90 ? 361  NAG C C2  1 
HETATM 10776 C  C3  . NAG JB 4 .   ? 49.833  -8.901  2.353   1.00 47.14 ? 361  NAG C C3  1 
HETATM 10777 C  C4  . NAG JB 4 .   ? 49.112  -8.036  3.390   1.00 48.92 ? 361  NAG C C4  1 
HETATM 10778 C  C5  . NAG JB 4 .   ? 48.845  -8.816  4.689   1.00 47.93 ? 361  NAG C C5  1 
HETATM 10779 C  C6  . NAG JB 4 .   ? 47.934  -8.060  5.652   1.00 46.86 ? 361  NAG C C6  1 
HETATM 10780 C  C7  . NAG JB 4 .   ? 49.598  -11.574 0.260   1.00 46.47 ? 361  NAG C C7  1 
HETATM 10781 C  C8  . NAG JB 4 .   ? 48.279  -11.013 -0.179  1.00 46.04 ? 361  NAG C C8  1 
HETATM 10782 N  N2  . NAG JB 4 .   ? 50.039  -11.182 1.453   1.00 44.91 ? 361  NAG C N2  1 
HETATM 10783 O  O3  . NAG JB 4 .   ? 49.768  -8.285  1.088   1.00 44.19 ? 361  NAG C O3  1 
HETATM 10784 O  O4  . NAG JB 4 .   ? 49.955  -6.935  3.683   1.00 54.47 ? 361  NAG C O4  1 
HETATM 10785 O  O5  . NAG JB 4 .   ? 48.268  -10.080 4.438   1.00 43.30 ? 361  NAG C O5  1 
HETATM 10786 O  O6  . NAG JB 4 .   ? 47.134  -7.168  4.908   1.00 49.20 ? 361  NAG C O6  1 
HETATM 10787 O  O7  . NAG JB 4 .   ? 50.238  -12.321 -0.484  1.00 46.75 ? 361  NAG C O7  1 
HETATM 10788 C  C1  . NAG KB 4 .   ? 49.550  -5.723  3.009   1.00 59.28 ? 362  NAG C C1  1 
HETATM 10789 C  C2  . NAG KB 4 .   ? 50.086  -4.514  3.779   1.00 61.10 ? 362  NAG C C2  1 
HETATM 10790 C  C3  . NAG KB 4 .   ? 49.677  -3.207  3.102   1.00 62.85 ? 362  NAG C C3  1 
HETATM 10791 C  C4  . NAG KB 4 .   ? 49.976  -3.216  1.601   1.00 65.89 ? 362  NAG C C4  1 
HETATM 10792 C  C5  . NAG KB 4 .   ? 49.451  -4.521  0.996   1.00 64.64 ? 362  NAG C C5  1 
HETATM 10793 C  C6  . NAG KB 4 .   ? 49.707  -4.569  -0.508  1.00 64.52 ? 362  NAG C C6  1 
HETATM 10794 C  C7  . NAG KB 4 .   ? 50.422  -4.935  6.174   1.00 59.60 ? 362  NAG C C7  1 
HETATM 10795 C  C8  . NAG KB 4 .   ? 49.829  -4.877  7.555   1.00 58.19 ? 362  NAG C C8  1 
HETATM 10796 N  N2  . NAG KB 4 .   ? 49.645  -4.513  5.171   1.00 59.99 ? 362  NAG C N2  1 
HETATM 10797 O  O3  . NAG KB 4 .   ? 50.345  -2.144  3.740   1.00 62.23 ? 362  NAG C O3  1 
HETATM 10798 O  O4  . NAG KB 4 .   ? 49.284  -2.158  0.968   1.00 70.80 ? 362  NAG C O4  1 
HETATM 10799 O  O5  . NAG KB 4 .   ? 49.992  -5.647  1.664   1.00 61.45 ? 362  NAG C O5  1 
HETATM 10800 O  O6  . NAG KB 4 .   ? 50.505  -5.682  -0.840  1.00 65.78 ? 362  NAG C O6  1 
HETATM 10801 O  O7  . NAG KB 4 .   ? 51.563  -5.375  6.010   1.00 58.98 ? 362  NAG C O7  1 
HETATM 10802 C  C1  . BMA LB 5 .   ? 50.126  -1.040  0.601   1.00 75.47 ? 363  BMA C C1  1 
HETATM 10803 C  C2  . BMA LB 5 .   ? 49.509  -0.490  -0.692  1.00 77.10 ? 363  BMA C C2  1 
HETATM 10804 C  C3  . BMA LB 5 .   ? 49.813  0.973   -0.977  1.00 78.18 ? 363  BMA C C3  1 
HETATM 10805 C  C4  . BMA LB 5 .   ? 49.540  1.747   0.299   1.00 78.87 ? 363  BMA C C4  1 
HETATM 10806 C  C5  . BMA LB 5 .   ? 50.512  1.248   1.357   1.00 79.12 ? 363  BMA C C5  1 
HETATM 10807 C  C6  . BMA LB 5 .   ? 50.427  2.128   2.610   1.00 79.71 ? 363  BMA C C6  1 
HETATM 10808 O  O2  . BMA LB 5 .   ? 48.107  -0.633  -0.605  1.00 77.13 ? 363  BMA C O2  1 
HETATM 10809 O  O3  . BMA LB 5 .   ? 48.964  1.436   -2.005  1.00 78.17 ? 363  BMA C O3  1 
HETATM 10810 O  O4  . BMA LB 5 .   ? 49.683  3.134   0.096   1.00 79.82 ? 363  BMA C O4  1 
HETATM 10811 O  O5  . BMA LB 5 .   ? 50.182  -0.096  1.668   1.00 77.60 ? 363  BMA C O5  1 
HETATM 10812 O  O6  . BMA LB 5 .   ? 51.273  1.649   3.636   1.00 79.04 ? 363  BMA C O6  1 
HETATM 10813 C  C1  . NAG MB 4 .   ? 45.574  -17.019 28.160  1.00 29.94 ? 371  NAG C C1  1 
HETATM 10814 C  C2  . NAG MB 4 .   ? 44.591  -17.239 29.313  1.00 31.83 ? 371  NAG C C2  1 
HETATM 10815 C  C3  . NAG MB 4 .   ? 44.661  -16.048 30.259  1.00 33.14 ? 371  NAG C C3  1 
HETATM 10816 C  C4  . NAG MB 4 .   ? 46.079  -15.661 30.675  1.00 35.75 ? 371  NAG C C4  1 
HETATM 10817 C  C5  . NAG MB 4 .   ? 47.045  -15.766 29.504  1.00 32.27 ? 371  NAG C C5  1 
HETATM 10818 C  C6  . NAG MB 4 .   ? 48.473  -15.702 30.043  1.00 33.68 ? 371  NAG C C6  1 
HETATM 10819 C  C7  . NAG MB 4 .   ? 42.666  -18.598 28.879  1.00 27.79 ? 371  NAG C C7  1 
HETATM 10820 C  C8  . NAG MB 4 .   ? 41.208  -18.714 28.526  1.00 25.37 ? 371  NAG C C8  1 
HETATM 10821 N  N2  . NAG MB 4 .   ? 43.204  -17.391 28.908  1.00 27.57 ? 371  NAG C N2  1 
HETATM 10822 O  O3  . NAG MB 4 .   ? 43.865  -16.276 31.395  1.00 30.39 ? 371  NAG C O3  1 
HETATM 10823 O  O4  . NAG MB 4 .   ? 45.999  -14.281 30.928  1.00 42.63 ? 371  NAG C O4  1 
HETATM 10824 O  O5  . NAG MB 4 .   ? 46.844  -16.940 28.753  1.00 29.92 ? 371  NAG C O5  1 
HETATM 10825 O  O6  . NAG MB 4 .   ? 48.841  -16.967 30.547  1.00 36.15 ? 371  NAG C O6  1 
HETATM 10826 O  O7  . NAG MB 4 .   ? 43.345  -19.598 29.076  1.00 26.91 ? 371  NAG C O7  1 
HETATM 10827 C  C1  . NAG NB 4 .   ? 46.359  -13.893 32.242  1.00 47.99 ? 372  NAG C C1  1 
HETATM 10828 C  C2  . NAG NB 4 .   ? 46.896  -12.495 31.962  1.00 53.38 ? 372  NAG C C2  1 
HETATM 10829 C  C3  . NAG NB 4 .   ? 46.116  -11.371 32.650  1.00 55.25 ? 372  NAG C C3  1 
HETATM 10830 C  C4  . NAG NB 4 .   ? 45.844  -11.702 34.108  1.00 53.96 ? 372  NAG C C4  1 
HETATM 10831 C  C5  . NAG NB 4 .   ? 45.510  -13.188 34.299  1.00 52.00 ? 372  NAG C C5  1 
HETATM 10832 C  C6  . NAG NB 4 .   ? 44.302  -13.378 35.199  1.00 52.93 ? 372  NAG C C6  1 
HETATM 10833 C  C7  . NAG NB 4 .   ? 49.091  -11.949 31.150  1.00 55.01 ? 372  NAG C C7  1 
HETATM 10834 C  C8  . NAG NB 4 .   ? 50.584  -11.940 31.357  1.00 55.56 ? 372  NAG C C8  1 
HETATM 10835 N  N2  . NAG NB 4 .   ? 48.339  -12.431 32.140  1.00 54.28 ? 372  NAG C N2  1 
HETATM 10836 O  O3  . NAG NB 4 .   ? 44.892  -11.128 31.983  1.00 58.38 ? 372  NAG C O3  1 
HETATM 10837 O  O4  . NAG NB 4 .   ? 47.011  -11.333 34.816  1.00 53.44 ? 372  NAG C O4  1 
HETATM 10838 O  O5  . NAG NB 4 .   ? 45.215  -13.804 33.063  1.00 49.92 ? 372  NAG C O5  1 
HETATM 10839 O  O6  . NAG NB 4 .   ? 43.229  -13.886 34.435  1.00 49.89 ? 372  NAG C O6  1 
HETATM 10840 O  O7  . NAG NB 4 .   ? 48.595  -11.530 30.101  1.00 54.45 ? 372  NAG C O7  1 
HETATM 10841 C  C1  . NAG OB 4 .   ? 33.650  -5.330  -4.673  1.00 50.24 ? 381  NAG C C1  1 
HETATM 10842 C  C2  . NAG OB 4 .   ? 34.139  -6.035  -5.931  1.00 54.60 ? 381  NAG C C2  1 
HETATM 10843 C  C3  . NAG OB 4 .   ? 33.458  -5.605  -7.239  1.00 55.50 ? 381  NAG C C3  1 
HETATM 10844 C  C4  . NAG OB 4 .   ? 32.748  -4.246  -7.223  1.00 57.42 ? 381  NAG C C4  1 
HETATM 10845 C  C5  . NAG OB 4 .   ? 32.481  -3.692  -5.821  1.00 55.85 ? 381  NAG C C5  1 
HETATM 10846 C  C6  . NAG OB 4 .   ? 31.191  -2.886  -5.804  1.00 54.95 ? 381  NAG C C6  1 
HETATM 10847 C  C7  . NAG OB 4 .   ? 36.414  -6.835  -5.860  1.00 53.53 ? 381  NAG C C7  1 
HETATM 10848 C  C8  . NAG OB 4 .   ? 37.882  -6.539  -5.990  1.00 53.89 ? 381  NAG C C8  1 
HETATM 10849 N  N2  . NAG OB 4 .   ? 35.571  -5.823  -6.018  1.00 54.45 ? 381  NAG C N2  1 
HETATM 10850 O  O3  . NAG OB 4 .   ? 32.557  -6.591  -7.686  1.00 56.24 ? 381  NAG C O3  1 
HETATM 10851 O  O4  . NAG OB 4 .   ? 33.508  -3.308  -7.963  1.00 58.92 ? 381  NAG C O4  1 
HETATM 10852 O  O5  . NAG OB 4 .   ? 32.389  -4.749  -4.890  1.00 53.81 ? 381  NAG C O5  1 
HETATM 10853 O  O6  . NAG OB 4 .   ? 30.125  -3.781  -5.588  1.00 53.93 ? 381  NAG C O6  1 
HETATM 10854 O  O7  . NAG OB 4 .   ? 36.020  -7.970  -5.632  1.00 53.44 ? 381  NAG C O7  1 
HETATM 10855 C  C1  . NAG PB 4 .   ? 10.624  -20.903 2.991   1.00 39.69 ? 391  NAG C C1  1 
HETATM 10856 C  C2  . NAG PB 4 .   ? 9.309   -20.568 3.709   1.00 39.98 ? 391  NAG C C2  1 
HETATM 10857 C  C3  . NAG PB 4 .   ? 8.114   -21.280 3.083   1.00 42.96 ? 391  NAG C C3  1 
HETATM 10858 C  C4  . NAG PB 4 .   ? 8.044   -20.979 1.602   1.00 44.51 ? 391  NAG C C4  1 
HETATM 10859 C  C5  . NAG PB 4 .   ? 9.333   -21.534 1.020   1.00 44.88 ? 391  NAG C C5  1 
HETATM 10860 C  C6  . NAG PB 4 .   ? 9.359   -21.342 -0.487  1.00 45.33 ? 391  NAG C C6  1 
HETATM 10861 C  C7  . NAG PB 4 .   ? 9.360   -20.017 6.041   1.00 36.02 ? 391  NAG C C7  1 
HETATM 10862 C  C8  . NAG PB 4 .   ? 9.278   -20.474 7.469   1.00 31.62 ? 391  NAG C C8  1 
HETATM 10863 N  N2  . NAG PB 4 .   ? 9.320   -20.953 5.100   1.00 36.16 ? 391  NAG C N2  1 
HETATM 10864 O  O3  . NAG PB 4 .   ? 6.914   -20.930 3.738   1.00 43.33 ? 391  NAG C O3  1 
HETATM 10865 O  O4  . NAG PB 4 .   ? 6.964   -21.709 1.079   1.00 51.07 ? 391  NAG C O4  1 
HETATM 10866 O  O5  . NAG PB 4 .   ? 10.448  -20.863 1.577   1.00 42.19 ? 391  NAG C O5  1 
HETATM 10867 O  O6  . NAG PB 4 .   ? 9.532   -19.961 -0.725  1.00 48.38 ? 391  NAG C O6  1 
HETATM 10868 O  O7  . NAG PB 4 .   ? 9.496   -18.832 5.757   1.00 37.22 ? 391  NAG C O7  1 
HETATM 10869 C  C1  . NAG QB 4 .   ? 6.093   -20.886 0.273   1.00 56.84 ? 392  NAG C C1  1 
HETATM 10870 C  C2  . NAG QB 4 .   ? 5.280   -21.834 -0.618  1.00 60.19 ? 392  NAG C C2  1 
HETATM 10871 C  C3  . NAG QB 4 .   ? 4.160   -21.130 -1.379  1.00 62.38 ? 392  NAG C C3  1 
HETATM 10872 C  C4  . NAG QB 4 .   ? 3.348   -20.270 -0.421  1.00 62.45 ? 392  NAG C C4  1 
HETATM 10873 C  C5  . NAG QB 4 .   ? 4.292   -19.332 0.332   1.00 62.11 ? 392  NAG C C5  1 
HETATM 10874 C  C6  . NAG QB 4 .   ? 3.519   -18.406 1.274   1.00 62.31 ? 392  NAG C C6  1 
HETATM 10875 C  C7  . NAG QB 4 .   ? 6.415   -23.863 -1.363  1.00 59.66 ? 392  NAG C C7  1 
HETATM 10876 C  C8  . NAG QB 4 .   ? 5.862   -24.532 -0.135  1.00 58.67 ? 392  NAG C C8  1 
HETATM 10877 N  N2  . NAG QB 4 .   ? 6.120   -22.574 -1.544  1.00 60.09 ? 392  NAG C N2  1 
HETATM 10878 O  O3  . NAG QB 4 .   ? 3.326   -22.095 -1.986  1.00 63.73 ? 392  NAG C O3  1 
HETATM 10879 O  O4  . NAG QB 4 .   ? 2.362   -19.554 -1.138  1.00 65.71 ? 392  NAG C O4  1 
HETATM 10880 O  O5  . NAG QB 4 .   ? 5.224   -20.103 1.073   1.00 58.71 ? 392  NAG C O5  1 
HETATM 10881 O  O6  . NAG QB 4 .   ? 2.865   -19.178 2.264   1.00 62.64 ? 392  NAG C O6  1 
HETATM 10882 O  O7  . NAG QB 4 .   ? 7.130   -24.488 -2.147  1.00 59.02 ? 392  NAG C O7  1 
HETATM 10883 C  C1  . NAG RB 4 .   ? 39.135  -46.334 23.810  1.00 55.51 ? 411  NAG C C1  1 
HETATM 10884 C  C2  . NAG RB 4 .   ? 39.426  -47.662 24.521  1.00 60.69 ? 411  NAG C C2  1 
HETATM 10885 C  C3  . NAG RB 4 .   ? 40.616  -47.581 25.471  1.00 62.49 ? 411  NAG C C3  1 
HETATM 10886 C  C4  . NAG RB 4 .   ? 41.783  -46.857 24.814  1.00 64.64 ? 411  NAG C C4  1 
HETATM 10887 C  C5  . NAG RB 4 .   ? 41.313  -45.539 24.202  1.00 61.51 ? 411  NAG C C5  1 
HETATM 10888 C  C6  . NAG RB 4 .   ? 42.470  -44.761 23.578  1.00 60.86 ? 411  NAG C C6  1 
HETATM 10889 C  C7  . NAG RB 4 .   ? 37.568  -49.164 24.850  1.00 60.45 ? 411  NAG C C7  1 
HETATM 10890 C  C8  . NAG RB 4 .   ? 36.385  -49.571 25.678  1.00 59.86 ? 411  NAG C C8  1 
HETATM 10891 N  N2  . NAG RB 4 .   ? 38.269  -48.116 25.270  1.00 60.88 ? 411  NAG C N2  1 
HETATM 10892 O  O3  . NAG RB 4 .   ? 41.017  -48.887 25.809  1.00 63.88 ? 411  NAG C O3  1 
HETATM 10893 O  O4  . NAG RB 4 .   ? 42.785  -46.611 25.779  1.00 69.89 ? 411  NAG C O4  1 
HETATM 10894 O  O5  . NAG RB 4 .   ? 40.318  -45.809 23.241  1.00 57.70 ? 411  NAG C O5  1 
HETATM 10895 O  O6  . NAG RB 4 .   ? 42.807  -45.305 22.323  1.00 59.44 ? 411  NAG C O6  1 
HETATM 10896 O  O7  . NAG RB 4 .   ? 37.853  -49.767 23.817  1.00 60.34 ? 411  NAG C O7  1 
HETATM 10897 C  C1  . NAG SB 4 .   ? 44.042  -47.012 25.207  1.00 73.96 ? 412  NAG C C1  1 
HETATM 10898 C  C2  . NAG SB 4 .   ? 45.077  -47.229 26.305  1.00 75.69 ? 412  NAG C C2  1 
HETATM 10899 C  C3  . NAG SB 4 .   ? 46.394  -47.733 25.717  1.00 76.81 ? 412  NAG C C3  1 
HETATM 10900 C  C4  . NAG SB 4 .   ? 46.210  -48.782 24.619  1.00 77.09 ? 412  NAG C C4  1 
HETATM 10901 C  C5  . NAG SB 4 .   ? 45.077  -48.411 23.666  1.00 76.89 ? 412  NAG C C5  1 
HETATM 10902 C  C6  . NAG SB 4 .   ? 44.795  -49.523 22.661  1.00 77.71 ? 412  NAG C C6  1 
HETATM 10903 C  C7  . NAG SB 4 .   ? 45.072  -45.751 28.264  1.00 76.03 ? 412  NAG C C7  1 
HETATM 10904 C  C8  . NAG SB 4 .   ? 44.466  -46.883 29.038  1.00 75.87 ? 412  NAG C C8  1 
HETATM 10905 N  N2  . NAG SB 4 .   ? 45.331  -45.967 26.978  1.00 76.22 ? 412  NAG C N2  1 
HETATM 10906 O  O3  . NAG SB 4 .   ? 47.187  -48.268 26.754  1.00 77.38 ? 412  NAG C O3  1 
HETATM 10907 O  O4  . NAG SB 4 .   ? 47.418  -48.915 23.896  1.00 76.62 ? 412  NAG C O4  1 
HETATM 10908 O  O5  . NAG SB 4 .   ? 43.911  -48.172 24.415  1.00 76.07 ? 412  NAG C O5  1 
HETATM 10909 O  O6  . NAG SB 4 .   ? 44.999  -49.025 21.357  1.00 78.00 ? 412  NAG C O6  1 
HETATM 10910 O  O7  . NAG SB 4 .   ? 45.305  -44.671 28.806  1.00 75.61 ? 412  NAG C O7  1 
HETATM 10911 C  C   . ACT TB 7 .   ? 33.802  -23.834 10.597  1.00 37.66 ? 1329 ACT C C   1 
HETATM 10912 O  O   . ACT TB 7 .   ? 34.949  -23.662 10.134  1.00 34.28 ? 1329 ACT C O   1 
HETATM 10913 O  OXT . ACT TB 7 .   ? 33.114  -22.786 10.763  1.00 38.50 ? 1329 ACT C OXT 1 
HETATM 10914 C  CH3 . ACT TB 7 .   ? 33.297  -25.212 10.946  1.00 31.23 ? 1329 ACT C CH3 1 
HETATM 10915 S  S   . SO4 UB 8 .   ? 40.676  -28.996 -12.513 1.00 62.83 ? 1330 SO4 C S   1 
HETATM 10916 O  O1  . SO4 UB 8 .   ? 41.427  -29.715 -13.534 1.00 63.19 ? 1330 SO4 C O1  1 
HETATM 10917 O  O2  . SO4 UB 8 .   ? 39.252  -29.048 -12.827 1.00 62.52 ? 1330 SO4 C O2  1 
HETATM 10918 O  O3  . SO4 UB 8 .   ? 40.937  -29.597 -11.202 1.00 61.56 ? 1330 SO4 C O3  1 
HETATM 10919 O  O4  . SO4 UB 8 .   ? 41.081  -27.597 -12.518 1.00 63.57 ? 1330 SO4 C O4  1 
HETATM 10920 S  S   . SO4 VB 8 .   ? 45.122  -23.193 -6.165  1.00 88.97 ? 1331 SO4 C S   1 
HETATM 10921 O  O1  . SO4 VB 8 .   ? 45.689  -23.116 -7.511  1.00 88.92 ? 1331 SO4 C O1  1 
HETATM 10922 O  O2  . SO4 VB 8 .   ? 43.785  -22.601 -6.182  1.00 89.36 ? 1331 SO4 C O2  1 
HETATM 10923 O  O3  . SO4 VB 8 .   ? 45.040  -24.595 -5.757  1.00 87.94 ? 1331 SO4 C O3  1 
HETATM 10924 O  O4  . SO4 VB 8 .   ? 45.955  -22.449 -5.218  1.00 88.37 ? 1331 SO4 C O4  1 
HETATM 10925 S  S   . SO4 WB 8 .   ? 15.683  -17.307 16.838  1.00 63.73 ? 1332 SO4 C S   1 
HETATM 10926 O  O1  . SO4 WB 8 .   ? 16.006  -16.507 15.651  1.00 62.17 ? 1332 SO4 C O1  1 
HETATM 10927 O  O2  . SO4 WB 8 .   ? 14.515  -18.154 16.582  1.00 63.31 ? 1332 SO4 C O2  1 
HETATM 10928 O  O3  . SO4 WB 8 .   ? 16.829  -18.153 17.175  1.00 62.60 ? 1332 SO4 C O3  1 
HETATM 10929 O  O4  . SO4 WB 8 .   ? 15.358  -16.427 17.960  1.00 62.80 ? 1332 SO4 C O4  1 
HETATM 10930 S  S   . SO4 XB 8 .   ? 53.311  -11.892 3.134   1.00 75.39 ? 1333 SO4 C S   1 
HETATM 10931 O  O1  . SO4 XB 8 .   ? 53.070  -12.295 1.751   1.00 75.35 ? 1333 SO4 C O1  1 
HETATM 10932 O  O2  . SO4 XB 8 .   ? 52.656  -12.852 4.016   1.00 75.57 ? 1333 SO4 C O2  1 
HETATM 10933 O  O3  . SO4 XB 8 .   ? 54.752  -11.879 3.397   1.00 75.16 ? 1333 SO4 C O3  1 
HETATM 10934 O  O4  . SO4 XB 8 .   ? 52.767  -10.553 3.363   1.00 74.57 ? 1333 SO4 C O4  1 
HETATM 10935 C  C   . ACT YB 7 .   ? 35.226  -35.634 -13.454 1.00 29.02 ? 1334 ACT C C   1 
HETATM 10936 O  O   . ACT YB 7 .   ? 34.013  -35.629 -13.161 1.00 24.32 ? 1334 ACT C O   1 
HETATM 10937 O  OXT . ACT YB 7 .   ? 35.985  -36.220 -12.645 1.00 27.78 ? 1334 ACT C OXT 1 
HETATM 10938 C  CH3 . ACT YB 7 .   ? 35.742  -34.991 -14.709 1.00 30.41 ? 1334 ACT C CH3 1 
HETATM 10939 C  CHA . HEM ZB 2 .   ? -36.853 -19.250 58.409  1.00 21.15 ? 350  HEM D CHA 1 
HETATM 10940 C  CHB . HEM ZB 2 .   ? -33.708 -22.293 60.432  1.00 22.60 ? 350  HEM D CHB 1 
HETATM 10941 C  CHC . HEM ZB 2 .   ? -34.186 -25.671 56.960  1.00 26.41 ? 350  HEM D CHC 1 
HETATM 10942 C  CHD . HEM ZB 2 .   ? -37.650 -22.818 55.176  1.00 24.05 ? 350  HEM D CHD 1 
HETATM 10943 C  C1A . HEM ZB 2 .   ? -35.947 -19.787 59.285  1.00 21.75 ? 350  HEM D C1A 1 
HETATM 10944 C  C2A . HEM ZB 2 .   ? -35.493 -19.191 60.534  1.00 18.85 ? 350  HEM D C2A 1 
HETATM 10945 C  C3A . HEM ZB 2 .   ? -34.679 -20.073 61.113  1.00 21.78 ? 350  HEM D C3A 1 
HETATM 10946 C  C4A . HEM ZB 2 .   ? -34.532 -21.219 60.216  1.00 21.28 ? 350  HEM D C4A 1 
HETATM 10947 C  CMA . HEM ZB 2 .   ? -33.866 -19.846 62.415  1.00 20.01 ? 350  HEM D CMA 1 
HETATM 10948 C  CAA . HEM ZB 2 .   ? -35.913 -17.827 61.122  1.00 24.65 ? 350  HEM D CAA 1 
HETATM 10949 C  CBA . HEM ZB 2 .   ? -35.386 -16.648 60.304  1.00 28.94 ? 350  HEM D CBA 1 
HETATM 10950 C  CGA . HEM ZB 2 .   ? -36.370 -15.508 60.375  1.00 32.37 ? 350  HEM D CGA 1 
HETATM 10951 O  O1A . HEM ZB 2 .   ? -36.265 -14.656 61.314  1.00 32.05 ? 350  HEM D O1A 1 
HETATM 10952 O  O2A . HEM ZB 2 .   ? -37.300 -15.483 59.515  1.00 33.18 ? 350  HEM D O2A 1 
HETATM 10953 C  C1B . HEM ZB 2 .   ? -33.498 -23.388 59.622  1.00 24.52 ? 350  HEM D C1B 1 
HETATM 10954 C  C2B . HEM ZB 2 .   ? -32.536 -24.430 59.901  1.00 23.91 ? 350  HEM D C2B 1 
HETATM 10955 C  C3B . HEM ZB 2 .   ? -32.633 -25.354 58.950  1.00 24.49 ? 350  HEM D C3B 1 
HETATM 10956 C  C4B . HEM ZB 2 .   ? -33.730 -24.982 58.068  1.00 26.01 ? 350  HEM D C4B 1 
HETATM 10957 C  CMB . HEM ZB 2 .   ? -31.540 -24.452 61.079  1.00 28.84 ? 350  HEM D CMB 1 
HETATM 10958 C  CAB . HEM ZB 2 .   ? -31.764 -26.623 58.893  1.00 26.77 ? 350  HEM D CAB 1 
HETATM 10959 C  CBB . HEM ZB 2 .   ? -31.389 -27.149 57.728  1.00 27.74 ? 350  HEM D CBB 1 
HETATM 10960 C  C1C . HEM ZB 2 .   ? -35.236 -25.217 56.197  1.00 23.30 ? 350  HEM D C1C 1 
HETATM 10961 C  C2C . HEM ZB 2 .   ? -35.895 -25.908 55.109  1.00 22.57 ? 350  HEM D C2C 1 
HETATM 10962 C  C3C . HEM ZB 2 .   ? -36.858 -25.094 54.663  1.00 22.63 ? 350  HEM D C3C 1 
HETATM 10963 C  C4C . HEM ZB 2 .   ? -36.815 -23.867 55.404  1.00 22.40 ? 350  HEM D C4C 1 
HETATM 10964 C  CMC . HEM ZB 2 .   ? -35.601 -27.339 54.584  1.00 21.95 ? 350  HEM D CMC 1 
HETATM 10965 C  CAC . HEM ZB 2 .   ? -37.824 -25.365 53.496  1.00 25.52 ? 350  HEM D CAC 1 
HETATM 10966 C  CBC . HEM ZB 2 .   ? -37.642 -26.503 52.820  1.00 28.52 ? 350  HEM D CBC 1 
HETATM 10967 C  C1D . HEM ZB 2 .   ? -37.670 -21.597 55.793  1.00 22.85 ? 350  HEM D C1D 1 
HETATM 10968 C  C2D . HEM ZB 2 .   ? -38.463 -20.486 55.333  1.00 21.51 ? 350  HEM D C2D 1 
HETATM 10969 C  C3D . HEM ZB 2 .   ? -38.250 -19.377 56.351  1.00 19.95 ? 350  HEM D C3D 1 
HETATM 10970 C  C4D . HEM ZB 2 .   ? -37.352 -19.929 57.330  1.00 22.17 ? 350  HEM D C4D 1 
HETATM 10971 C  CMD . HEM ZB 2 .   ? -39.390 -20.446 54.109  1.00 22.62 ? 350  HEM D CMD 1 
HETATM 10972 C  CAD . HEM ZB 2 .   ? -38.841 -17.967 56.287  1.00 21.95 ? 350  HEM D CAD 1 
HETATM 10973 C  CBD . HEM ZB 2 .   ? -39.982 -17.814 57.279  1.00 22.27 ? 350  HEM D CBD 1 
HETATM 10974 C  CGD . HEM ZB 2 .   ? -40.528 -16.427 57.077  1.00 27.51 ? 350  HEM D CGD 1 
HETATM 10975 O  O1D . HEM ZB 2 .   ? -39.760 -15.523 56.613  1.00 25.51 ? 350  HEM D O1D 1 
HETATM 10976 O  O2D . HEM ZB 2 .   ? -41.742 -16.243 57.336  1.00 27.55 ? 350  HEM D O2D 1 
HETATM 10977 N  NA  . HEM ZB 2 .   ? -35.387 -21.052 59.144  1.00 21.48 ? 350  HEM D NA  1 
HETATM 10978 N  NB  . HEM ZB 2 .   ? -34.223 -23.755 58.492  1.00 24.59 ? 350  HEM D NB  1 
HETATM 10979 N  NC  . HEM ZB 2 .   ? -35.826 -23.968 56.356  1.00 23.91 ? 350  HEM D NC  1 
HETATM 10980 N  ND  . HEM ZB 2 .   ? -37.014 -21.237 56.959  1.00 23.18 ? 350  HEM D ND  1 
HETATM 10981 FE FE  . HEM ZB 2 .   ? -35.623 -22.506 57.736  1.00 25.20 3 350  HEM D FE  1 
HETATM 10982 MG MG  . MG  AC 3 .   ? -37.624 -13.501 62.141  1.00 26.68 2 353  MG  D MG  1 
HETATM 10983 C  C1  . NAG BC 4 .   ? -48.767 -9.535  63.024  1.00 50.01 ? 361  NAG D C1  1 
HETATM 10984 C  C2  . NAG BC 4 .   ? -48.990 -9.000  64.430  1.00 52.18 ? 361  NAG D C2  1 
HETATM 10985 C  C3  . NAG BC 4 .   ? -49.710 -7.665  64.367  1.00 53.67 ? 361  NAG D C3  1 
HETATM 10986 C  C4  . NAG BC 4 .   ? -49.038 -6.693  63.407  1.00 55.26 ? 361  NAG D C4  1 
HETATM 10987 C  C5  . NAG BC 4 .   ? -48.491 -7.350  62.132  1.00 54.42 ? 361  NAG D C5  1 
HETATM 10988 C  C6  . NAG BC 4 .   ? -47.349 -6.517  61.562  1.00 54.28 ? 361  NAG D C6  1 
HETATM 10989 C  C7  . NAG BC 4 .   ? -49.418 -10.273 66.447  1.00 54.11 ? 361  NAG D C7  1 
HETATM 10990 C  C8  . NAG BC 4 .   ? -50.330 -11.217 67.176  1.00 52.45 ? 361  NAG D C8  1 
HETATM 10991 N  N2  . NAG BC 4 .   ? -49.786 -9.915  65.221  1.00 53.38 ? 361  NAG D N2  1 
HETATM 10992 O  O3  . NAG BC 4 .   ? -49.691 -7.101  65.653  1.00 54.41 ? 361  NAG D O3  1 
HETATM 10993 O  O4  . NAG BC 4 .   ? -49.989 -5.702  63.072  1.00 59.13 ? 361  NAG D O4  1 
HETATM 10994 O  O5  . NAG BC 4 .   ? -47.931 -8.628  62.360  1.00 52.15 ? 361  NAG D O5  1 
HETATM 10995 O  O6  . NAG BC 4 .   ? -47.845 -5.302  61.053  1.00 56.99 ? 361  NAG D O6  1 
HETATM 10996 O  O7  . NAG BC 4 .   ? -48.378 -9.868  66.968  1.00 55.26 ? 361  NAG D O7  1 
HETATM 10997 C  C1  . NAG CC 4 .   ? -49.670 -4.442  63.708  1.00 61.83 ? 362  NAG D C1  1 
HETATM 10998 C  C2  . NAG CC 4 .   ? -50.301 -3.277  62.940  1.00 62.42 ? 362  NAG D C2  1 
HETATM 10999 C  C3  . NAG CC 4 .   ? -49.966 -1.933  63.598  1.00 63.50 ? 362  NAG D C3  1 
HETATM 11000 C  C4  . NAG CC 4 .   ? -50.272 -1.984  65.099  1.00 64.71 ? 362  NAG D C4  1 
HETATM 11001 C  C5  . NAG CC 4 .   ? -49.620 -3.219  65.729  1.00 64.78 ? 362  NAG D C5  1 
HETATM 11002 C  C6  . NAG CC 4 .   ? -49.950 -3.320  67.214  1.00 65.53 ? 362  NAG D C6  1 
HETATM 11003 C  C7  . NAG CC 4 .   ? -50.677 -3.636  60.556  1.00 62.85 ? 362  NAG D C7  1 
HETATM 11004 C  C8  . NAG CC 4 .   ? -50.097 -3.593  59.168  1.00 62.29 ? 362  NAG D C8  1 
HETATM 11005 N  N2  . NAG CC 4 .   ? -49.865 -3.279  61.552  1.00 62.71 ? 362  NAG D N2  1 
HETATM 11006 O  O3  . NAG CC 4 .   ? -50.679 -0.886  62.971  1.00 60.48 ? 362  NAG D O3  1 
HETATM 11007 O  O4  . NAG CC 4 .   ? -49.851 -0.802  65.757  1.00 65.50 ? 362  NAG D O4  1 
HETATM 11008 O  O5  . NAG CC 4 .   ? -50.065 -4.394  65.068  1.00 63.24 ? 362  NAG D O5  1 
HETATM 11009 O  O6  . NAG CC 4 .   ? -51.325 -3.604  67.369  1.00 66.19 ? 362  NAG D O6  1 
HETATM 11010 O  O7  . NAG CC 4 .   ? -51.840 -4.004  60.737  1.00 61.14 ? 362  NAG D O7  1 
HETATM 11011 C  C1  . NAG DC 4 .   ? -44.334 -15.201 38.654  1.00 33.63 ? 371  NAG D C1  1 
HETATM 11012 C  C2  . NAG DC 4 .   ? -43.323 -15.313 37.505  1.00 33.67 ? 371  NAG D C2  1 
HETATM 11013 C  C3  . NAG DC 4 .   ? -43.487 -14.123 36.577  1.00 36.25 ? 371  NAG D C3  1 
HETATM 11014 C  C4  . NAG DC 4 .   ? -44.908 -14.013 36.028  1.00 38.92 ? 371  NAG D C4  1 
HETATM 11015 C  C5  . NAG DC 4 .   ? -45.943 -14.331 37.129  1.00 38.85 ? 371  NAG D C5  1 
HETATM 11016 C  C6  . NAG DC 4 .   ? -47.326 -14.591 36.522  1.00 39.09 ? 371  NAG D C6  1 
HETATM 11017 C  C7  . NAG DC 4 .   ? -41.284 -16.483 38.094  1.00 27.99 ? 371  NAG D C7  1 
HETATM 11018 C  C8  . NAG DC 4 .   ? -39.839 -16.391 38.505  1.00 28.92 ? 371  NAG D C8  1 
HETATM 11019 N  N2  . NAG DC 4 .   ? -41.940 -15.338 37.936  1.00 29.18 ? 371  NAG D N2  1 
HETATM 11020 O  O3  . NAG DC 4 .   ? -42.533 -14.179 35.545  1.00 34.34 ? 371  NAG D O3  1 
HETATM 11021 O  O4  . NAG DC 4 .   ? -45.089 -12.644 35.697  1.00 43.57 ? 371  NAG D O4  1 
HETATM 11022 O  O5  . NAG DC 4 .   ? -45.607 -15.352 38.071  1.00 35.47 ? 371  NAG D O5  1 
HETATM 11023 O  O6  . NAG DC 4 .   ? -47.619 -15.971 36.447  1.00 39.53 ? 371  NAG D O6  1 
HETATM 11024 O  O7  . NAG DC 4 .   ? -41.810 -17.576 37.932  1.00 26.52 ? 371  NAG D O7  1 
HETATM 11025 C  C1  . NAG EC 4 .   ? -45.009 -12.297 34.302  1.00 48.65 ? 372  NAG D C1  1 
HETATM 11026 C  C2  . NAG EC 4 .   ? -45.842 -11.039 34.091  1.00 52.37 ? 372  NAG D C2  1 
HETATM 11027 C  C3  . NAG EC 4 .   ? -45.808 -10.566 32.638  1.00 53.32 ? 372  NAG D C3  1 
HETATM 11028 C  C4  . NAG EC 4 .   ? -44.389 -10.532 32.068  1.00 53.94 ? 372  NAG D C4  1 
HETATM 11029 C  C5  . NAG EC 4 .   ? -43.640 -11.809 32.469  1.00 51.95 ? 372  NAG D C5  1 
HETATM 11030 C  C6  . NAG EC 4 .   ? -42.175 -11.813 32.035  1.00 51.82 ? 372  NAG D C6  1 
HETATM 11031 C  C7  . NAG EC 4 .   ? -47.720 -10.849 35.633  1.00 57.49 ? 372  NAG D C7  1 
HETATM 11032 C  C8  . NAG EC 4 .   ? -49.161 -11.177 35.900  1.00 58.01 ? 372  NAG D C8  1 
HETATM 11033 N  N2  . NAG EC 4 .   ? -47.215 -11.295 34.481  1.00 55.74 ? 372  NAG D N2  1 
HETATM 11034 O  O3  . NAG EC 4 .   ? -46.387 -9.284  32.552  1.00 51.65 ? 372  NAG D O3  1 
HETATM 11035 O  O4  . NAG EC 4 .   ? -44.468 -10.452 30.653  1.00 56.57 ? 372  NAG D O4  1 
HETATM 11036 O  O5  . NAG EC 4 .   ? -43.705 -11.990 33.866  1.00 50.18 ? 372  NAG D O5  1 
HETATM 11037 O  O6  . NAG EC 4 .   ? -41.510 -10.655 32.508  1.00 52.48 ? 372  NAG D O6  1 
HETATM 11038 O  O7  . NAG EC 4 .   ? -47.066 -10.196 36.448  1.00 58.18 ? 372  NAG D O7  1 
HETATM 11039 C  C1  . BMA FC 5 .   ? -44.289 -9.114  30.129  1.00 58.74 ? 373  BMA D C1  1 
HETATM 11040 C  C2  . BMA FC 5 .   ? -43.494 -9.274  28.845  1.00 58.89 ? 373  BMA D C2  1 
HETATM 11041 C  C3  . BMA FC 5 .   ? -43.180 -7.931  28.202  1.00 60.38 ? 373  BMA D C3  1 
HETATM 11042 C  C4  . BMA FC 5 .   ? -44.466 -7.137  28.005  1.00 61.85 ? 373  BMA D C4  1 
HETATM 11043 C  C5  . BMA FC 5 .   ? -45.399 -7.182  29.223  1.00 62.03 ? 373  BMA D C5  1 
HETATM 11044 C  C6  . BMA FC 5 .   ? -46.768 -6.604  28.835  1.00 62.10 ? 373  BMA D C6  1 
HETATM 11045 O  O2  . BMA FC 5 .   ? -44.309 -10.005 27.965  1.00 59.39 ? 373  BMA D O2  1 
HETATM 11046 O  O3  . BMA FC 5 .   ? -42.562 -8.125  26.942  1.00 60.15 ? 373  BMA D O3  1 
HETATM 11047 O  O4  . BMA FC 5 .   ? -44.121 -5.798  27.710  1.00 62.71 ? 373  BMA D O4  1 
HETATM 11048 O  O5  . BMA FC 5 .   ? -45.517 -8.491  29.779  1.00 61.28 ? 373  BMA D O5  1 
HETATM 11049 O  O6  . BMA FC 5 .   ? -47.834 -7.211  29.539  1.00 62.00 ? 373  BMA D O6  1 
HETATM 11050 C  C1  . NAG GC 4 .   ? -34.146 -2.211  71.718  1.00 55.51 ? 381  NAG D C1  1 
HETATM 11051 C  C2  . NAG GC 4 .   ? -34.393 -3.122  72.935  1.00 57.59 ? 381  NAG D C2  1 
HETATM 11052 C  C3  . NAG GC 4 .   ? -33.949 -2.489  74.262  1.00 58.90 ? 381  NAG D C3  1 
HETATM 11053 C  C4  . NAG GC 4 .   ? -32.620 -1.743  74.136  1.00 58.89 ? 381  NAG D C4  1 
HETATM 11054 C  C5  . NAG GC 4 .   ? -32.708 -0.805  72.936  1.00 59.61 ? 381  NAG D C5  1 
HETATM 11055 C  C6  . NAG GC 4 .   ? -31.497 0.110   72.780  1.00 61.01 ? 381  NAG D C6  1 
HETATM 11056 C  C7  . NAG GC 4 .   ? -36.250 -4.716  72.722  1.00 56.56 ? 381  NAG D C7  1 
HETATM 11057 C  C8  . NAG GC 4 .   ? -37.730 -4.951  72.853  1.00 54.41 ? 381  NAG D C8  1 
HETATM 11058 N  N2  . NAG GC 4 .   ? -35.803 -3.490  73.012  1.00 56.64 ? 381  NAG D N2  1 
HETATM 11059 O  O3  . NAG GC 4 .   ? -33.840 -3.477  75.263  1.00 59.34 ? 381  NAG D O3  1 
HETATM 11060 O  O4  . NAG GC 4 .   ? -32.354 -1.024  75.322  1.00 58.27 ? 381  NAG D O4  1 
HETATM 11061 O  O5  . NAG GC 4 .   ? -32.871 -1.593  71.780  1.00 57.79 ? 381  NAG D O5  1 
HETATM 11062 O  O6  . NAG GC 4 .   ? -30.348 -0.653  72.505  1.00 62.56 ? 381  NAG D O6  1 
HETATM 11063 O  O7  . NAG GC 4 .   ? -35.512 -5.636  72.359  1.00 55.99 ? 381  NAG D O7  1 
HETATM 11064 C  C1  . NAG HC 4 .   ? -9.683  -16.056 64.692  1.00 48.66 ? 391  NAG D C1  1 
HETATM 11065 C  C2  . NAG HC 4 .   ? -8.367  -15.650 64.005  1.00 49.10 ? 391  NAG D C2  1 
HETATM 11066 C  C3  . NAG HC 4 .   ? -7.174  -16.364 64.616  1.00 48.24 ? 391  NAG D C3  1 
HETATM 11067 C  C4  . NAG HC 4 .   ? -7.180  -16.052 66.098  1.00 49.30 ? 391  NAG D C4  1 
HETATM 11068 C  C5  . NAG HC 4 .   ? -8.437  -16.693 66.669  1.00 50.44 ? 391  NAG D C5  1 
HETATM 11069 C  C6  . NAG HC 4 .   ? -8.491  -16.596 68.192  1.00 51.04 ? 391  NAG D C6  1 
HETATM 11070 C  C7  . NAG HC 4 .   ? -8.595  -14.881 61.697  1.00 48.34 ? 391  NAG D C7  1 
HETATM 11071 C  C8  . NAG HC 4 .   ? -8.450  -15.237 60.244  1.00 48.52 ? 391  NAG D C8  1 
HETATM 11072 N  N2  . NAG HC 4 .   ? -8.341  -15.856 62.569  1.00 49.19 ? 391  NAG D N2  1 
HETATM 11073 O  O3  . NAG HC 4 .   ? -5.982  -15.889 64.043  1.00 48.81 ? 391  NAG D O3  1 
HETATM 11074 O  O4  . NAG HC 4 .   ? -5.998  -16.506 66.717  1.00 47.43 ? 391  NAG D O4  1 
HETATM 11075 O  O5  . NAG HC 4 .   ? -9.561  -16.026 66.117  1.00 49.74 ? 391  NAG D O5  1 
HETATM 11076 O  O6  . NAG HC 4 .   ? -8.925  -15.307 68.569  1.00 53.15 ? 391  NAG D O6  1 
HETATM 11077 O  O7  . NAG HC 4 .   ? -8.972  -13.761 62.027  1.00 46.79 ? 391  NAG D O7  1 
HETATM 11078 C  C1  . NAG IC 4 .   ? -35.511 -43.641 43.286  1.00 53.86 ? 411  NAG D C1  1 
HETATM 11079 C  C2  . NAG IC 4 .   ? -35.474 -45.070 42.744  1.00 56.38 ? 411  NAG D C2  1 
HETATM 11080 C  C3  . NAG IC 4 .   ? -36.681 -45.405 41.870  1.00 56.61 ? 411  NAG D C3  1 
HETATM 11081 C  C4  . NAG IC 4 .   ? -37.970 -44.873 42.480  1.00 55.80 ? 411  NAG D C4  1 
HETATM 11082 C  C5  . NAG IC 4 .   ? -37.782 -43.399 42.820  1.00 55.04 ? 411  NAG D C5  1 
HETATM 11083 C  C6  . NAG IC 4 .   ? -39.071 -42.717 43.271  1.00 54.94 ? 411  NAG D C6  1 
HETATM 11084 C  C7  . NAG IC 4 .   ? -33.447 -46.258 42.116  1.00 58.76 ? 411  NAG D C7  1 
HETATM 11085 C  C8  . NAG IC 4 .   ? -32.203 -46.246 41.273  1.00 59.46 ? 411  NAG D C8  1 
HETATM 11086 N  N2  . NAG IC 4 .   ? -34.259 -45.217 41.972  1.00 57.43 ? 411  NAG D N2  1 
HETATM 11087 O  O3  . NAG IC 4 .   ? -36.786 -46.805 41.736  1.00 58.48 ? 411  NAG D O3  1 
HETATM 11088 O  O4  . NAG IC 4 .   ? -39.024 -45.052 41.559  1.00 56.59 ? 411  NAG D O4  1 
HETATM 11089 O  O5  . NAG IC 4 .   ? -36.782 -43.311 43.811  1.00 53.78 ? 411  NAG D O5  1 
HETATM 11090 O  O6  . NAG IC 4 .   ? -39.435 -43.176 44.554  1.00 54.43 ? 411  NAG D O6  1 
HETATM 11091 O  O7  . NAG IC 4 .   ? -33.690 -47.200 42.867  1.00 58.69 ? 411  NAG D O7  1 
HETATM 11092 C  C   . ACT JC 7 .   ? -32.179 -21.066 56.402  1.00 49.32 ? 1327 ACT D C   1 
HETATM 11093 O  O   . ACT JC 7 .   ? -33.233 -20.540 56.810  1.00 49.53 ? 1327 ACT D O   1 
HETATM 11094 O  OXT . ACT JC 7 .   ? -31.314 -20.287 55.929  1.00 50.33 ? 1327 ACT D OXT 1 
HETATM 11095 C  CH3 . ACT JC 7 .   ? -31.985 -22.550 56.459  1.00 48.39 ? 1327 ACT D CH3 1 
HETATM 11096 S  S   . SO4 KC 8 .   ? -38.721 -26.359 79.983  1.00 60.27 ? 1328 SO4 D S   1 
HETATM 11097 O  O1  . SO4 KC 8 .   ? -37.353 -25.953 79.674  1.00 60.64 ? 1328 SO4 D O1  1 
HETATM 11098 O  O2  . SO4 KC 8 .   ? -39.620 -26.060 78.875  1.00 60.26 ? 1328 SO4 D O2  1 
HETATM 11099 O  O3  . SO4 KC 8 .   ? -38.749 -27.805 80.232  1.00 62.36 ? 1328 SO4 D O3  1 
HETATM 11100 O  O4  . SO4 KC 8 .   ? -39.136 -25.621 81.174  1.00 61.91 ? 1328 SO4 D O4  1 
HETATM 11101 S  S   . SO4 LC 8 .   ? -14.562 -12.816 50.573  1.00 58.08 ? 1329 SO4 D S   1 
HETATM 11102 O  O1  . SO4 LC 8 .   ? -14.184 -11.917 49.481  1.00 57.59 ? 1329 SO4 D O1  1 
HETATM 11103 O  O2  . SO4 LC 8 .   ? -15.643 -13.703 50.139  1.00 56.97 ? 1329 SO4 D O2  1 
HETATM 11104 O  O3  . SO4 LC 8 .   ? -13.392 -13.616 50.918  1.00 58.59 ? 1329 SO4 D O3  1 
HETATM 11105 O  O4  . SO4 LC 8 .   ? -14.983 -12.032 51.738  1.00 55.57 ? 1329 SO4 D O4  1 
HETATM 11106 O  O   . HOH MC 9 .   ? 38.483  -38.820 44.567  1.00 37.96 ? 2001 HOH A O   1 
HETATM 11107 O  O   . HOH MC 9 .   ? 39.811  -41.705 36.056  1.00 39.23 ? 2002 HOH A O   1 
HETATM 11108 O  O   . HOH MC 9 .   ? 36.419  -43.268 35.054  1.00 44.90 ? 2003 HOH A O   1 
HETATM 11109 O  O   . HOH MC 9 .   ? 32.611  -42.714 33.802  1.00 38.13 ? 2004 HOH A O   1 
HETATM 11110 O  O   . HOH MC 9 .   ? 30.797  -38.440 29.188  1.00 17.83 ? 2005 HOH A O   1 
HETATM 11111 O  O   . HOH MC 9 .   ? 31.499  -39.852 27.086  1.00 27.83 ? 2006 HOH A O   1 
HETATM 11112 O  O   . HOH MC 9 .   ? 35.278  -41.506 26.419  1.00 40.93 ? 2007 HOH A O   1 
HETATM 11113 O  O   . HOH MC 9 .   ? 34.419  -46.975 24.083  1.00 42.81 ? 2008 HOH A O   1 
HETATM 11114 O  O   . HOH MC 9 .   ? 33.845  -42.512 24.163  1.00 38.34 ? 2009 HOH A O   1 
HETATM 11115 O  O   . HOH MC 9 .   ? 32.316  -49.656 26.644  1.00 45.52 ? 2010 HOH A O   1 
HETATM 11116 O  O   . HOH MC 9 .   ? 26.464  -45.240 30.018  1.00 39.53 ? 2011 HOH A O   1 
HETATM 11117 O  O   . HOH MC 9 .   ? 28.361  -50.959 24.880  1.00 52.12 ? 2012 HOH A O   1 
HETATM 11118 O  O   . HOH MC 9 .   ? 27.428  -39.847 22.101  1.00 24.81 ? 2013 HOH A O   1 
HETATM 11119 O  O   . HOH MC 9 .   ? 22.181  -42.112 20.422  1.00 34.79 ? 2014 HOH A O   1 
HETATM 11120 O  O   . HOH MC 9 .   ? 11.229  -48.137 34.351  1.00 40.89 ? 2015 HOH A O   1 
HETATM 11121 O  O   . HOH MC 9 .   ? 9.807   -44.205 37.738  1.00 36.23 ? 2016 HOH A O   1 
HETATM 11122 O  O   . HOH MC 9 .   ? 11.594  -46.458 36.523  1.00 44.89 ? 2017 HOH A O   1 
HETATM 11123 O  O   . HOH MC 9 .   ? 8.232   -42.360 35.957  1.00 57.38 ? 2018 HOH A O   1 
HETATM 11124 O  O   . HOH MC 9 .   ? 20.554  -46.312 33.752  1.00 45.99 ? 2019 HOH A O   1 
HETATM 11125 O  O   . HOH MC 9 .   ? 14.911  -50.715 40.952  1.00 45.77 ? 2020 HOH A O   1 
HETATM 11126 O  O   . HOH MC 9 .   ? 22.795  -46.033 39.568  1.00 46.38 ? 2021 HOH A O   1 
HETATM 11127 O  O   . HOH MC 9 .   ? 31.148  -44.306 44.086  1.00 41.13 ? 2022 HOH A O   1 
HETATM 11128 O  O   . HOH MC 9 .   ? 31.985  -43.307 48.962  1.00 46.12 ? 2023 HOH A O   1 
HETATM 11129 O  O   . HOH MC 9 .   ? 26.558  -47.864 47.109  1.00 45.48 ? 2024 HOH A O   1 
HETATM 11130 O  O   . HOH MC 9 .   ? 13.393  -41.180 45.874  1.00 32.97 ? 2025 HOH A O   1 
HETATM 11131 O  O   . HOH MC 9 .   ? 15.947  -47.984 46.898  1.00 35.30 ? 2026 HOH A O   1 
HETATM 11132 O  O   . HOH MC 9 .   ? 12.827  -41.206 49.028  1.00 33.02 ? 2027 HOH A O   1 
HETATM 11133 O  O   . HOH MC 9 .   ? 7.587   -37.801 47.573  1.00 46.48 ? 2028 HOH A O   1 
HETATM 11134 O  O   . HOH MC 9 .   ? 7.286   -41.829 51.583  1.00 37.98 ? 2029 HOH A O   1 
HETATM 11135 O  O   . HOH MC 9 .   ? 11.503  -35.023 52.719  1.00 51.28 ? 2030 HOH A O   1 
HETATM 11136 O  O   . HOH MC 9 .   ? 13.051  -46.397 52.772  1.00 43.79 ? 2031 HOH A O   1 
HETATM 11137 O  O   . HOH MC 9 .   ? 13.027  -40.850 56.565  1.00 40.71 ? 2032 HOH A O   1 
HETATM 11138 O  O   . HOH MC 9 .   ? 32.397  -35.015 26.126  1.00 42.82 ? 2033 HOH A O   1 
HETATM 11139 O  O   . HOH MC 9 .   ? 18.435  -35.736 57.391  1.00 62.25 ? 2034 HOH A O   1 
HETATM 11140 O  O   . HOH MC 9 .   ? 14.273  -31.799 51.431  1.00 27.87 ? 2035 HOH A O   1 
HETATM 11141 O  O   . HOH MC 9 .   ? 15.041  -42.447 52.061  1.00 44.10 ? 2036 HOH A O   1 
HETATM 11142 O  O   . HOH MC 9 .   ? 13.823  -28.954 46.345  1.00 36.47 ? 2037 HOH A O   1 
HETATM 11143 O  O   . HOH MC 9 .   ? 13.379  -28.301 48.783  1.00 26.43 ? 2038 HOH A O   1 
HETATM 11144 O  O   . HOH MC 9 .   ? 17.031  -29.610 51.618  1.00 35.89 ? 2039 HOH A O   1 
HETATM 11145 O  O   . HOH MC 9 .   ? 19.387  -29.746 44.597  1.00 19.53 ? 2040 HOH A O   1 
HETATM 11146 O  O   . HOH MC 9 .   ? 17.514  -23.285 41.679  1.00 20.55 ? 2041 HOH A O   1 
HETATM 11147 O  O   . HOH MC 9 .   ? 13.454  -31.110 41.052  1.00 20.09 ? 2042 HOH A O   1 
HETATM 11148 O  O   . HOH MC 9 .   ? 19.847  -46.778 43.153  1.00 41.63 ? 2043 HOH A O   1 
HETATM 11149 O  O   . HOH MC 9 .   ? 24.724  -43.759 38.913  1.00 60.69 ? 2044 HOH A O   1 
HETATM 11150 O  O   . HOH MC 9 .   ? 25.558  -42.665 43.660  1.00 68.59 ? 2045 HOH A O   1 
HETATM 11151 O  O   . HOH MC 9 .   ? 26.620  -42.453 41.386  1.00 46.46 ? 2046 HOH A O   1 
HETATM 11152 O  O   . HOH MC 9 .   ? 17.907  -47.233 45.615  1.00 35.83 ? 2047 HOH A O   1 
HETATM 11153 O  O   . HOH MC 9 .   ? 26.762  -41.165 50.135  1.00 35.83 ? 2048 HOH A O   1 
HETATM 11154 O  O   . HOH MC 9 .   ? 32.110  -42.492 46.230  1.00 40.36 ? 2049 HOH A O   1 
HETATM 11155 O  O   . HOH MC 9 .   ? 1.166   -27.883 44.934  1.00 51.88 ? 2050 HOH A O   1 
HETATM 11156 O  O   . HOH MC 9 .   ? 34.541  -38.212 45.771  1.00 23.38 ? 2051 HOH A O   1 
HETATM 11157 O  O   . HOH MC 9 .   ? 27.269  -45.460 44.561  1.00 39.32 ? 2052 HOH A O   1 
HETATM 11158 O  O   . HOH MC 9 .   ? 0.914   -26.643 29.555  1.00 15.32 ? 2053 HOH A O   1 
HETATM 11159 O  O   . HOH MC 9 .   ? 2.583   -11.052 24.587  1.00 31.91 ? 2054 HOH A O   1 
HETATM 11160 O  O   . HOH MC 9 .   ? 30.239  -42.060 34.850  1.00 40.98 ? 2055 HOH A O   1 
HETATM 11161 O  O   . HOH MC 9 .   ? 29.402  -43.554 41.872  1.00 46.94 ? 2056 HOH A O   1 
HETATM 11162 O  O   . HOH MC 9 .   ? 34.284  -43.013 39.490  1.00 41.86 ? 2057 HOH A O   1 
HETATM 11163 O  O   . HOH MC 9 .   ? 7.158   -27.183 18.755  1.00 35.38 ? 2058 HOH A O   1 
HETATM 11164 O  O   . HOH MC 9 .   ? 19.740  -36.232 29.056  1.00 25.73 ? 2059 HOH A O   1 
HETATM 11165 O  O   . HOH MC 9 .   ? 28.177  -37.921 29.902  1.00 26.96 ? 2060 HOH A O   1 
HETATM 11166 O  O   . HOH MC 9 .   ? 30.248  -30.076 26.199  1.00 44.13 ? 2061 HOH A O   1 
HETATM 11167 O  O   . HOH MC 9 .   ? 31.859  -28.022 29.222  1.00 45.54 ? 2062 HOH A O   1 
HETATM 11168 O  O   . HOH MC 9 .   ? 33.617  -32.341 28.731  1.00 25.34 ? 2063 HOH A O   1 
HETATM 11169 O  O   . HOH MC 9 .   ? 31.883  -36.064 28.613  1.00 21.11 ? 2064 HOH A O   1 
HETATM 11170 O  O   . HOH MC 9 .   ? 38.508  -35.243 34.836  1.00 42.81 ? 2065 HOH A O   1 
HETATM 11171 O  O   . HOH MC 9 .   ? 37.045  -34.705 30.482  1.00 40.15 ? 2066 HOH A O   1 
HETATM 11172 O  O   . HOH MC 9 .   ? 37.185  -33.107 33.760  1.00 27.14 ? 2067 HOH A O   1 
HETATM 11173 O  O   . HOH MC 9 .   ? 33.228  -27.047 32.148  1.00 59.61 ? 2068 HOH A O   1 
HETATM 11174 O  O   . HOH MC 9 .   ? 38.842  -28.512 26.935  1.00 36.59 ? 2069 HOH A O   1 
HETATM 11175 O  O   . HOH MC 9 .   ? 39.118  -32.782 32.262  1.00 32.34 ? 2070 HOH A O   1 
HETATM 11176 O  O   . HOH MC 9 .   ? 28.606  -21.527 30.297  1.00 42.31 ? 2071 HOH A O   1 
HETATM 11177 O  O   . HOH MC 9 .   ? 29.051  -26.714 34.943  1.00 42.25 ? 2072 HOH A O   1 
HETATM 11178 O  O   . HOH MC 9 .   ? 9.776   -36.450 27.456  1.00 25.44 ? 2073 HOH A O   1 
HETATM 11179 O  O   . HOH MC 9 .   ? 36.686  -37.048 44.632  1.00 25.22 ? 2074 HOH A O   1 
HETATM 11180 O  O   . HOH MC 9 .   ? 33.175  -26.520 52.248  1.00 26.33 ? 2075 HOH A O   1 
HETATM 11181 O  O   . HOH MC 9 .   ? -1.658  -27.894 30.695  1.00 32.08 ? 2076 HOH A O   1 
HETATM 11182 O  O   . HOH MC 9 .   ? 31.849  -24.832 53.482  1.00 27.89 ? 2077 HOH A O   1 
HETATM 11183 O  O   . HOH MC 9 .   ? 28.185  -23.630 52.920  1.00 32.56 ? 2078 HOH A O   1 
HETATM 11184 O  O   . HOH MC 9 .   ? 27.016  -30.335 52.641  1.00 22.70 ? 2079 HOH A O   1 
HETATM 11185 O  O   . HOH MC 9 .   ? 24.940  -23.316 47.610  1.00 19.16 ? 2080 HOH A O   1 
HETATM 11186 O  O   . HOH MC 9 .   ? 0.860   -30.311 43.245  1.00 50.28 ? 2081 HOH A O   1 
HETATM 11187 O  O   . HOH MC 9 .   ? 35.460  -31.049 57.130  1.00 39.39 ? 2082 HOH A O   1 
HETATM 11188 O  O   . HOH MC 9 .   ? 29.681  -31.601 57.957  1.00 32.40 ? 2083 HOH A O   1 
HETATM 11189 O  O   . HOH MC 9 .   ? 35.175  -33.369 59.508  1.00 30.07 ? 2084 HOH A O   1 
HETATM 11190 O  O   . HOH MC 9 .   ? 35.067  -29.078 55.173  1.00 19.29 ? 2085 HOH A O   1 
HETATM 11191 O  O   . HOH MC 9 .   ? 36.941  -34.154 49.821  1.00 32.22 ? 2086 HOH A O   1 
HETATM 11192 O  O   . HOH MC 9 .   ? 39.561  -35.765 52.365  1.00 34.94 ? 2087 HOH A O   1 
HETATM 11193 O  O   . HOH MC 9 .   ? 36.240  -39.822 53.553  1.00 50.35 ? 2088 HOH A O   1 
HETATM 11194 O  O   . HOH MC 9 .   ? 32.388  -40.925 53.540  1.00 46.22 ? 2089 HOH A O   1 
HETATM 11195 O  O   . HOH MC 9 .   ? 36.878  -35.096 46.614  1.00 24.33 ? 2090 HOH A O   1 
HETATM 11196 O  O   . HOH MC 9 .   ? 34.802  -40.737 49.465  1.00 39.51 ? 2091 HOH A O   1 
HETATM 11197 O  O   . HOH MC 9 .   ? 22.897  -2.103  33.425  1.00 35.39 ? 2092 HOH A O   1 
HETATM 11198 O  O   . HOH MC 9 .   ? 31.460  -2.740  33.147  1.00 44.77 ? 2093 HOH A O   1 
HETATM 11199 O  O   . HOH MC 9 .   ? 29.384  -6.864  48.328  1.00 38.42 ? 2094 HOH A O   1 
HETATM 11200 O  O   . HOH MC 9 .   ? 35.231  -3.311  31.972  1.00 52.00 ? 2095 HOH A O   1 
HETATM 11201 O  O   . HOH MC 9 .   ? 21.297  -29.515 60.866  1.00 49.70 ? 2096 HOH A O   1 
HETATM 11202 O  O   . HOH MC 9 .   ? 20.789  -3.055  53.662  1.00 35.17 ? 2097 HOH A O   1 
HETATM 11203 O  O   . HOH MC 9 .   ? 25.756  -30.061 55.396  1.00 22.57 ? 2098 HOH A O   1 
HETATM 11204 O  O   . HOH MC 9 .   ? 23.712  -35.328 64.810  1.00 43.20 ? 2099 HOH A O   1 
HETATM 11205 O  O   . HOH MC 9 .   ? 38.895  -7.618  34.358  1.00 43.05 ? 2100 HOH A O   1 
HETATM 11206 O  O   . HOH MC 9 .   ? 38.665  -4.606  34.091  1.00 48.84 ? 2101 HOH A O   1 
HETATM 11207 O  O   . HOH MC 9 .   ? 30.168  -30.683 63.893  1.00 41.40 ? 2102 HOH A O   1 
HETATM 11208 O  O   . HOH MC 9 .   ? 36.569  -30.749 59.818  1.00 64.69 ? 2103 HOH A O   1 
HETATM 11209 O  O   . HOH MC 9 .   ? 28.451  -25.661 61.701  1.00 63.74 ? 2104 HOH A O   1 
HETATM 11210 O  O   . HOH MC 9 .   ? 31.987  -24.654 60.345  1.00 51.65 ? 2105 HOH A O   1 
HETATM 11211 O  O   . HOH MC 9 .   ? 37.574  -23.022 58.190  1.00 37.46 ? 2106 HOH A O   1 
HETATM 11212 O  O   . HOH MC 9 .   ? 22.651  -23.982 53.892  1.00 31.82 ? 2107 HOH A O   1 
HETATM 11213 O  O   . HOH MC 9 .   ? 50.159  -27.270 55.842  1.00 55.72 ? 2108 HOH A O   1 
HETATM 11214 O  O   . HOH MC 9 .   ? 20.758  -22.131 53.824  1.00 29.27 ? 2109 HOH A O   1 
HETATM 11215 O  O   . HOH MC 9 .   ? 18.033  -24.328 53.999  1.00 27.98 ? 2110 HOH A O   1 
HETATM 11216 O  O   . HOH MC 9 .   ? 49.198  -38.100 45.234  1.00 55.90 ? 2111 HOH A O   1 
HETATM 11217 O  O   . HOH MC 9 .   ? 24.468  -22.980 56.877  1.00 39.11 ? 2112 HOH A O   1 
HETATM 11218 O  O   . HOH MC 9 .   ? 44.584  -30.433 35.426  1.00 36.28 ? 2113 HOH A O   1 
HETATM 11219 O  O   . HOH MC 9 .   ? 21.859  -19.490 53.111  1.00 34.75 ? 2114 HOH A O   1 
HETATM 11220 O  O   . HOH MC 9 .   ? 19.101  -16.679 46.180  1.00 22.40 ? 2115 HOH A O   1 
HETATM 11221 O  O   . HOH MC 9 .   ? 20.106  -12.316 50.148  1.00 36.36 ? 2116 HOH A O   1 
HETATM 11222 O  O   . HOH MC 9 .   ? 21.501  -11.882 47.302  1.00 26.27 ? 2117 HOH A O   1 
HETATM 11223 O  O   . HOH MC 9 .   ? 26.330  -17.478 44.334  1.00 26.78 ? 2118 HOH A O   1 
HETATM 11224 O  O   . HOH MC 9 .   ? 30.322  -17.423 44.910  1.00 31.49 ? 2119 HOH A O   1 
HETATM 11225 O  O   . HOH MC 9 .   ? 50.796  -22.557 29.445  1.00 41.14 ? 2120 HOH A O   1 
HETATM 11226 O  O   . HOH MC 9 .   ? 50.890  -25.299 38.586  1.00 60.39 ? 2121 HOH A O   1 
HETATM 11227 O  O   . HOH MC 9 .   ? 51.386  -25.359 36.965  1.00 47.83 ? 2122 HOH A O   1 
HETATM 11228 O  O   . HOH MC 9 .   ? 17.887  -21.316 43.896  1.00 18.23 ? 2123 HOH A O   1 
HETATM 11229 O  O   . HOH MC 9 .   ? 17.216  -18.422 44.087  1.00 14.58 ? 2124 HOH A O   1 
HETATM 11230 O  O   . HOH MC 9 .   ? 22.828  -14.230 44.159  1.00 29.93 ? 2125 HOH A O   1 
HETATM 11231 O  O   . HOH MC 9 .   ? 18.568  -12.806 47.920  1.00 30.97 ? 2126 HOH A O   1 
HETATM 11232 O  O   . HOH MC 9 .   ? 15.706  -16.900 42.414  1.00 16.06 ? 2127 HOH A O   1 
HETATM 11233 O  O   . HOH MC 9 .   ? 10.124  -17.913 36.135  1.00 22.28 ? 2128 HOH A O   1 
HETATM 11234 O  O   . HOH MC 9 .   ? 11.993  -21.410 46.307  1.00 27.39 ? 2129 HOH A O   1 
HETATM 11235 O  O   . HOH MC 9 .   ? 12.465  -17.157 48.246  1.00 34.27 ? 2130 HOH A O   1 
HETATM 11236 O  O   . HOH MC 9 .   ? 12.725  -14.578 43.374  1.00 21.09 ? 2131 HOH A O   1 
HETATM 11237 O  O   . HOH MC 9 .   ? 13.231  -12.431 41.884  1.00 23.38 ? 2132 HOH A O   1 
HETATM 11238 O  O   . HOH MC 9 .   ? 14.751  -13.819 54.543  1.00 38.44 ? 2133 HOH A O   1 
HETATM 11239 O  O   . HOH MC 9 .   ? 16.465  -20.372 51.982  1.00 35.95 ? 2134 HOH A O   1 
HETATM 11240 O  O   . HOH MC 9 .   ? 6.308   -24.547 14.183  1.00 46.02 ? 2135 HOH A O   1 
HETATM 11241 O  O   . HOH MC 9 .   ? 9.945   -28.331 46.019  1.00 23.81 ? 2136 HOH A O   1 
HETATM 11242 O  O   . HOH MC 9 .   ? 6.574   -26.481 46.305  1.00 30.22 ? 2137 HOH A O   1 
HETATM 11243 O  O   . HOH MC 9 .   ? 7.614   -22.325 47.092  1.00 28.02 ? 2138 HOH A O   1 
HETATM 11244 O  O   . HOH MC 9 .   ? 1.712   -26.839 42.343  1.00 34.34 ? 2139 HOH A O   1 
HETATM 11245 O  O   . HOH MC 9 .   ? -0.826  -24.119 39.825  1.00 31.54 ? 2140 HOH A O   1 
HETATM 11246 O  O   . HOH MC 9 .   ? -0.800  -23.151 34.293  1.00 23.56 ? 2141 HOH A O   1 
HETATM 11247 O  O   . HOH MC 9 .   ? 0.766   -13.968 28.384  1.00 30.96 ? 2142 HOH A O   1 
HETATM 11248 O  O   . HOH MC 9 .   ? 4.387   -14.315 32.870  1.00 37.28 ? 2143 HOH A O   1 
HETATM 11249 O  O   . HOH MC 9 .   ? 2.335   -20.554 21.554  1.00 32.97 ? 2144 HOH A O   1 
HETATM 11250 O  O   . HOH MC 9 .   ? 6.104   -18.874 20.471  1.00 17.30 ? 2145 HOH A O   1 
HETATM 11251 O  O   . HOH MC 9 .   ? 3.503   -17.911 20.090  1.00 42.69 ? 2146 HOH A O   1 
HETATM 11252 O  O   . HOH MC 9 .   ? -0.328  -20.187 23.324  1.00 38.70 ? 2147 HOH A O   1 
HETATM 11253 O  O   . HOH MC 9 .   ? 1.125   -24.692 27.837  1.00 15.94 ? 2148 HOH A O   1 
HETATM 11254 O  O   . HOH MC 9 .   ? 5.071   -11.903 24.038  1.00 34.34 ? 2149 HOH A O   1 
HETATM 11255 O  O   . HOH MC 9 .   ? 8.834   -24.894 19.528  1.00 21.50 ? 2150 HOH A O   1 
HETATM 11256 O  O   . HOH MC 9 .   ? 2.554   -25.895 25.925  1.00 18.65 ? 2151 HOH A O   1 
HETATM 11257 O  O   . HOH MC 9 .   ? 4.165   -28.505 25.935  1.00 29.29 ? 2152 HOH A O   1 
HETATM 11258 O  O   . HOH MC 9 .   ? 4.202   -32.350 23.511  1.00 41.58 ? 2153 HOH A O   1 
HETATM 11259 O  O   . HOH MC 9 .   ? 16.509  -24.976 22.147  1.00 15.14 ? 2154 HOH A O   1 
HETATM 11260 O  O   . HOH MC 9 .   ? 15.884  -14.894 23.578  1.00 22.93 ? 2155 HOH A O   1 
HETATM 11261 O  O   . HOH MC 9 .   ? 16.790  -17.744 20.029  1.00 47.88 ? 2156 HOH A O   1 
HETATM 11262 O  O   . HOH MC 9 .   ? 19.057  -13.113 28.467  1.00 12.03 ? 2157 HOH A O   1 
HETATM 11263 O  O   . HOH MC 9 .   ? 12.776  -10.899 28.670  1.00 32.35 ? 2158 HOH A O   1 
HETATM 11264 O  O   . HOH MC 9 .   ? 19.359  -20.266 37.448  1.00 17.19 ? 2159 HOH A O   1 
HETATM 11265 O  O   . HOH MC 9 .   ? 5.185   -9.601  36.242  1.00 40.89 ? 2160 HOH A O   1 
HETATM 11266 O  O   . HOH MC 9 .   ? 14.053  -4.038  36.646  1.00 33.59 ? 2161 HOH A O   1 
HETATM 11267 O  O   . HOH MC 9 .   ? 10.397  -6.694  33.170  1.00 45.92 ? 2162 HOH A O   1 
HETATM 11268 O  O   . HOH MC 9 .   ? 8.563   -12.544 39.454  1.00 35.82 ? 2163 HOH A O   1 
HETATM 11269 O  O   . HOH MC 9 .   ? 10.057  -2.106  41.432  1.00 39.55 ? 2164 HOH A O   1 
HETATM 11270 O  O   . HOH MC 9 .   ? 10.840  -11.334 42.801  1.00 37.12 ? 2165 HOH A O   1 
HETATM 11271 O  O   . HOH MC 9 .   ? 23.075  -6.698  47.203  1.00 25.28 ? 2166 HOH A O   1 
HETATM 11272 O  O   . HOH MC 9 .   ? 23.273  -9.472  49.037  1.00 37.80 ? 2167 HOH A O   1 
HETATM 11273 O  O   . HOH MC 9 .   ? 26.180  -12.880 42.983  1.00 29.72 ? 2168 HOH A O   1 
HETATM 11274 O  O   . HOH MC 9 .   ? 31.347  -14.397 35.878  1.00 28.40 ? 2169 HOH A O   1 
HETATM 11275 O  O   . HOH MC 9 .   ? 32.323  -8.453  42.420  1.00 43.07 ? 2170 HOH A O   1 
HETATM 11276 O  O   . HOH MC 9 .   ? 34.290  -13.058 44.245  1.00 40.56 ? 2171 HOH A O   1 
HETATM 11277 O  O   . HOH MC 9 .   ? 30.950  -15.597 43.326  1.00 30.82 ? 2172 HOH A O   1 
HETATM 11278 O  O   . HOH MC 9 .   ? 34.066  -16.232 40.733  1.00 22.94 ? 2173 HOH A O   1 
HETATM 11279 O  O   . HOH MC 9 .   ? 27.368  -20.465 32.117  1.00 36.03 ? 2174 HOH A O   1 
HETATM 11280 O  O   . HOH MC 9 .   ? 20.313  -11.545 30.304  1.00 10.38 ? 2175 HOH A O   1 
HETATM 11281 O  O   . HOH MC 9 .   ? 24.220  -10.975 28.863  1.00 15.27 ? 2176 HOH A O   1 
HETATM 11282 O  O   . HOH MC 9 .   ? 17.653  -31.301 22.955  1.00 19.72 ? 2177 HOH A O   1 
HETATM 11283 O  O   . HOH MC 9 .   ? 18.962  -26.825 22.607  1.00 29.30 ? 2178 HOH A O   1 
HETATM 11284 O  O   . HOH MC 9 .   ? 21.996  -26.916 22.268  1.00 39.28 ? 2179 HOH A O   1 
HETATM 11285 O  O   . HOH MC 9 .   ? 11.437  -34.508 27.362  1.00 27.06 ? 2180 HOH A O   1 
HETATM 11286 O  O   . HOH MC 9 .   ? 18.304  -34.911 23.837  1.00 31.07 ? 2181 HOH A O   1 
HETATM 11287 O  O   . HOH MC 9 .   ? 10.684  -39.427 21.757  1.00 40.68 ? 2182 HOH A O   1 
HETATM 11288 O  O   . HOH MC 9 .   ? 11.119  -39.210 27.087  1.00 46.77 ? 2183 HOH A O   1 
HETATM 11289 O  O   . HOH MC 9 .   ? 19.153  -39.037 19.054  1.00 38.93 ? 2184 HOH A O   1 
HETATM 11290 O  O   . HOH MC 9 .   ? 16.024  -41.832 17.695  1.00 54.15 ? 2185 HOH A O   1 
HETATM 11291 O  O   . HOH MC 9 .   ? 12.098  -45.679 21.452  1.00 36.90 ? 2186 HOH A O   1 
HETATM 11292 O  O   . HOH MC 9 .   ? 14.672  -34.974 16.071  1.00 35.07 ? 2187 HOH A O   1 
HETATM 11293 O  O   . HOH MC 9 .   ? 9.188   -37.873 23.268  1.00 45.64 ? 2188 HOH A O   1 
HETATM 11294 O  O   . HOH MC 9 .   ? 7.136   -33.577 24.068  1.00 37.66 ? 2189 HOH A O   1 
HETATM 11295 O  O   . HOH MC 9 .   ? 9.658   -32.859 25.897  1.00 28.73 ? 2190 HOH A O   1 
HETATM 11296 O  O   . HOH MC 9 .   ? 18.781  -29.778 18.139  1.00 26.95 ? 2191 HOH A O   1 
HETATM 11297 O  O   . HOH MC 9 .   ? 21.725  -30.947 20.590  1.00 25.92 ? 2192 HOH A O   1 
HETATM 11298 O  O   . HOH MC 9 .   ? 14.069  -28.485 16.842  1.00 19.18 ? 2193 HOH A O   1 
HETATM 11299 O  O   . HOH MC 9 .   ? 11.582  -34.104 16.744  1.00 57.26 ? 2194 HOH A O   1 
HETATM 11300 O  O   . HOH MC 9 .   ? 19.194  -28.969 20.818  1.00 32.03 ? 2195 HOH A O   1 
HETATM 11301 O  O   . HOH MC 9 .   ? 11.080  -24.580 17.147  1.00 49.01 ? 2196 HOH A O   1 
HETATM 11302 O  O   . HOH MC 9 .   ? 6.707   -34.890 28.298  1.00 44.01 ? 2197 HOH A O   1 
HETATM 11303 O  O   . HOH MC 9 .   ? 3.327   -32.773 25.933  1.00 34.78 ? 2198 HOH A O   1 
HETATM 11304 O  O   . HOH MC 9 .   ? 3.511   -30.624 27.709  1.00 34.98 ? 2199 HOH A O   1 
HETATM 11305 O  O   . HOH MC 9 .   ? 3.112   -28.693 33.611  1.00 28.33 ? 2200 HOH A O   1 
HETATM 11306 O  O   . HOH MC 9 .   ? 5.761   -36.240 32.782  0.50 19.20 ? 2201 HOH A O   1 
HETATM 11307 O  O   . HOH MC 9 .   ? 4.235   -32.971 34.846  1.00 40.35 ? 2202 HOH A O   1 
HETATM 11308 O  O   . HOH MC 9 .   ? 1.516   -34.992 32.658  0.50 22.55 ? 2203 HOH A O   1 
HETATM 11309 O  O   . HOH MC 9 .   ? 0.702   -29.046 29.152  0.50 23.12 ? 2204 HOH A O   1 
HETATM 11310 O  O   . HOH MC 9 .   ? 2.080   -31.579 34.306  1.00 47.22 ? 2205 HOH A O   1 
HETATM 11311 O  O   . HOH MC 9 .   ? 0.869   -25.535 34.395  1.00 32.20 ? 2206 HOH A O   1 
HETATM 11312 O  O   . HOH MC 9 .   ? 1.702   -30.189 40.682  1.00 38.09 ? 2207 HOH A O   1 
HETATM 11313 O  O   . HOH MC 9 .   ? 5.648   -28.361 45.020  1.00 32.98 ? 2208 HOH A O   1 
HETATM 11314 O  O   . HOH MC 9 .   ? 9.865   -35.674 44.619  1.00 30.80 ? 2209 HOH A O   1 
HETATM 11315 O  O   . HOH MC 9 .   ? 11.689  -33.483 45.069  1.00 37.81 ? 2210 HOH A O   1 
HETATM 11316 O  O   . HOH MC 9 .   ? 2.993   -42.635 41.271  1.00 53.82 ? 2211 HOH A O   1 
HETATM 11317 O  O   . HOH MC 9 .   ? 5.690   -39.227 31.738  1.00 40.23 ? 2212 HOH A O   1 
HETATM 11318 O  O   . HOH MC 9 .   ? 6.233   -39.642 28.765  1.00 62.34 ? 2213 HOH A O   1 
HETATM 11319 O  O   . HOH MC 9 .   ? 12.205  -48.389 25.961  1.00 45.30 ? 2214 HOH A O   1 
HETATM 11320 O  O   . HOH MC 9 .   ? 9.158   -47.634 24.293  1.00 41.61 ? 2215 HOH A O   1 
HETATM 11321 O  O   . HOH MC 9 .   ? 24.345  -40.719 19.952  1.00 32.99 ? 2216 HOH A O   1 
HETATM 11322 O  O   . HOH MC 9 .   ? 27.079  -32.953 22.455  1.00 32.93 ? 2217 HOH A O   1 
HETATM 11323 O  O   . HOH MC 9 .   ? 23.230  -29.935 22.524  1.00 38.11 ? 2218 HOH A O   1 
HETATM 11324 O  O   . HOH MC 9 .   ? 27.971  -28.497 26.144  1.00 21.84 ? 2219 HOH A O   1 
HETATM 11325 O  O   . HOH MC 9 .   ? 28.638  -24.871 30.543  1.00 62.91 ? 2220 HOH A O   1 
HETATM 11326 O  O   . HOH MC 9 .   ? 29.011  -23.809 27.473  1.00 47.40 ? 2221 HOH A O   1 
HETATM 11327 O  O   . HOH MC 9 .   ? 25.552  -30.473 22.346  1.00 41.03 ? 2222 HOH A O   1 
HETATM 11328 O  O   . HOH MC 9 .   ? 26.213  -23.716 20.450  1.00 47.30 ? 2223 HOH A O   1 
HETATM 11329 O  O   . HOH MC 9 .   ? 28.088  -23.437 22.154  1.00 39.23 ? 2224 HOH A O   1 
HETATM 11330 O  O   . HOH MC 9 .   ? 27.616  -14.379 23.707  1.00 36.73 ? 2225 HOH A O   1 
HETATM 11331 O  O   . HOH MC 9 .   ? 24.441  -21.016 18.866  1.00 46.19 ? 2226 HOH A O   1 
HETATM 11332 O  O   . HOH MC 9 .   ? 29.451  -20.795 17.532  1.00 44.39 ? 2227 HOH A O   1 
HETATM 11333 O  O   . HOH MC 9 .   ? 23.491  -9.937  19.729  1.00 39.23 ? 2228 HOH A O   1 
HETATM 11334 O  O   . HOH MC 9 .   ? 27.268  -7.555  24.918  1.00 32.64 ? 2229 HOH A O   1 
HETATM 11335 O  O   . HOH MC 9 .   ? 19.762  -6.205  28.073  1.00 52.49 ? 2230 HOH A O   1 
HETATM 11336 O  O   . HOH MC 9 .   ? 26.455  -5.779  28.776  1.00 26.30 ? 2231 HOH A O   1 
HETATM 11337 O  O   . HOH MC 9 .   ? 26.993  -10.396 29.373  1.00 34.08 ? 2232 HOH A O   1 
HETATM 11338 O  O   . HOH MC 9 .   ? 23.974  -4.108  32.295  1.00 20.47 ? 2233 HOH A O   1 
HETATM 11339 O  O   . HOH MC 9 .   ? 31.323  -4.207  29.934  1.00 43.94 ? 2234 HOH A O   1 
HETATM 11340 O  O   . HOH MC 9 .   ? 28.341  -3.336  46.811  1.00 55.07 ? 2235 HOH A O   1 
HETATM 11341 O  O   . HOH MC 9 .   ? 30.624  -0.838  42.332  1.00 53.17 ? 2236 HOH A O   1 
HETATM 11342 O  O   . HOH MC 9 .   ? 25.399  -4.516  47.476  1.00 54.53 ? 2237 HOH A O   1 
HETATM 11343 O  O   . HOH MC 9 .   ? 19.609  -0.528  53.150  1.00 33.46 ? 2238 HOH A O   1 
HETATM 11344 O  O   . HOH MC 9 .   ? 14.177  -1.087  48.511  1.00 32.16 ? 2239 HOH A O   1 
HETATM 11345 O  O   . HOH MC 9 .   ? 14.525  2.171   45.550  1.00 51.42 ? 2240 HOH A O   1 
HETATM 11346 O  O   . HOH MC 9 .   ? 18.336  -0.449  38.733  1.00 21.51 ? 2241 HOH A O   1 
HETATM 11347 O  O   . HOH MC 9 .   ? 12.377  2.199   43.064  1.00 35.91 ? 2242 HOH A O   1 
HETATM 11348 O  O   . HOH MC 9 .   ? 11.845  -1.683  38.104  1.00 43.10 ? 2243 HOH A O   1 
HETATM 11349 O  O   . HOH MC 9 .   ? 21.123  0.252   36.951  1.00 33.73 ? 2244 HOH A O   1 
HETATM 11350 O  O   . HOH MC 9 .   ? 25.834  2.539   44.105  1.00 38.38 ? 2245 HOH A O   1 
HETATM 11351 O  O   . HOH MC 9 .   ? 29.014  1.165   39.627  1.00 73.67 ? 2246 HOH A O   1 
HETATM 11352 O  O   . HOH MC 9 .   ? 32.555  -6.253  34.776  1.00 43.70 ? 2247 HOH A O   1 
HETATM 11353 O  O   . HOH MC 9 .   ? 33.819  -5.618  44.441  1.00 46.02 ? 2248 HOH A O   1 
HETATM 11354 O  O   . HOH MC 9 .   ? 36.917  -7.276  35.675  1.00 45.27 ? 2249 HOH A O   1 
HETATM 11355 O  O   . HOH MC 9 .   ? 34.743  -1.610  33.431  1.00 40.21 ? 2250 HOH A O   1 
HETATM 11356 O  O   . HOH MC 9 .   ? 39.048  -7.984  39.299  1.00 45.75 ? 2251 HOH A O   1 
HETATM 11357 O  O   . HOH MC 9 .   ? 35.515  -8.474  43.185  1.00 53.66 ? 2252 HOH A O   1 
HETATM 11358 O  O   . HOH MC 9 .   ? 30.715  -15.291 33.590  1.00 46.42 ? 2253 HOH A O   1 
HETATM 11359 O  O   . HOH MC 9 .   ? 33.205  -16.347 32.766  1.00 31.39 ? 2254 HOH A O   1 
HETATM 11360 O  O   . HOH MC 9 .   ? 29.700  -10.845 29.844  1.00 21.81 ? 2255 HOH A O   1 
HETATM 11361 O  O   . HOH MC 9 .   ? 33.161  -17.222 30.011  1.00 28.73 ? 2256 HOH A O   1 
HETATM 11362 O  O   . HOH MC 9 .   ? 38.955  -11.034 27.218  1.00 40.30 ? 2257 HOH A O   1 
HETATM 11363 O  O   . HOH MC 9 .   ? 39.637  -14.617 28.517  1.00 48.80 ? 2258 HOH A O   1 
HETATM 11364 O  O   . HOH MC 9 .   ? 37.718  -8.277  27.418  1.00 46.50 ? 2259 HOH A O   1 
HETATM 11365 O  O   . HOH MC 9 .   ? 43.787  -18.108 35.999  1.00 16.75 ? 2260 HOH A O   1 
HETATM 11366 O  O   . HOH MC 9 .   ? 34.096  -15.634 43.205  1.00 31.75 ? 2261 HOH A O   1 
HETATM 11367 O  O   . HOH MC 9 .   ? 43.780  -15.257 48.269  1.00 24.36 ? 2262 HOH A O   1 
HETATM 11368 O  O   . HOH MC 9 .   ? 43.767  -12.834 44.625  1.00 41.37 ? 2263 HOH A O   1 
HETATM 11369 O  O   . HOH MC 9 .   ? 33.129  -14.953 47.276  1.00 48.89 ? 2264 HOH A O   1 
HETATM 11370 O  O   . HOH MC 9 .   ? 47.345  -19.111 52.375  1.00 33.08 ? 2265 HOH A O   1 
HETATM 11371 O  O   . HOH MC 9 .   ? 47.870  -15.870 52.398  1.00 58.95 ? 2266 HOH A O   1 
HETATM 11372 O  O   . HOH MC 9 .   ? 37.418  -15.463 56.028  1.00 43.84 ? 2267 HOH A O   1 
HETATM 11373 O  O   . HOH MC 9 .   ? 33.272  -14.818 49.873  1.00 36.72 ? 2268 HOH A O   1 
HETATM 11374 O  O   . HOH MC 9 .   ? 47.468  -23.439 56.152  1.00 53.65 ? 2269 HOH A O   1 
HETATM 11375 O  O   . HOH MC 9 .   ? 48.790  -29.422 54.162  1.00 47.81 ? 2270 HOH A O   1 
HETATM 11376 O  O   . HOH MC 9 .   ? 41.004  -34.757 59.637  1.00 52.13 ? 2271 HOH A O   1 
HETATM 11377 O  O   . HOH MC 9 .   ? 45.536  -37.136 55.810  1.00 52.49 ? 2272 HOH A O   1 
HETATM 11378 O  O   . HOH MC 9 .   ? 46.527  -34.582 56.697  1.00 59.25 ? 2273 HOH A O   1 
HETATM 11379 O  O   . HOH MC 9 .   ? 48.892  -30.249 50.101  1.00 50.36 ? 2274 HOH A O   1 
HETATM 11380 O  O   . HOH MC 9 .   ? 45.708  -26.767 44.729  1.00 31.16 ? 2275 HOH A O   1 
HETATM 11381 O  O   . HOH MC 9 .   ? 44.778  -33.706 43.511  1.00 39.23 ? 2276 HOH A O   1 
HETATM 11382 O  O   . HOH MC 9 .   ? 43.476  -35.578 50.032  1.00 26.46 ? 2277 HOH A O   1 
HETATM 11383 O  O   . HOH MC 9 .   ? 45.822  -35.105 45.396  1.00 38.11 ? 2278 HOH A O   1 
HETATM 11384 O  O   . HOH MC 9 .   ? 46.962  -32.350 45.959  1.00 62.80 ? 2279 HOH A O   1 
HETATM 11385 O  O   . HOH MC 9 .   ? 44.264  -30.555 38.011  1.00 38.50 ? 2280 HOH A O   1 
HETATM 11386 O  O   . HOH MC 9 .   ? 46.128  -29.717 39.269  1.00 41.76 ? 2281 HOH A O   1 
HETATM 11387 O  O   . HOH MC 9 .   ? 48.393  -32.333 42.118  1.00 58.08 ? 2282 HOH A O   1 
HETATM 11388 O  O   . HOH MC 9 .   ? 41.917  -26.163 33.118  1.00 29.68 ? 2283 HOH A O   1 
HETATM 11389 O  O   . HOH MC 9 .   ? 41.058  -27.289 29.643  1.00 31.34 ? 2284 HOH A O   1 
HETATM 11390 O  O   . HOH MC 9 .   ? 33.912  -24.286 32.480  1.00 44.22 ? 2285 HOH A O   1 
HETATM 11391 O  O   . HOH MC 9 .   ? 35.175  -22.406 31.713  1.00 30.92 ? 2286 HOH A O   1 
HETATM 11392 O  O   . HOH MC 9 .   ? 37.052  -25.060 25.719  1.00 36.28 ? 2287 HOH A O   1 
HETATM 11393 O  O   . HOH MC 9 .   ? 40.413  -26.213 27.031  1.00 49.47 ? 2288 HOH A O   1 
HETATM 11394 O  O   . HOH MC 9 .   ? 40.012  -23.924 25.326  1.00 29.54 ? 2289 HOH A O   1 
HETATM 11395 O  O   . HOH MC 9 .   ? 34.899  -22.288 27.952  1.00 51.77 ? 2290 HOH A O   1 
HETATM 11396 O  O   . HOH MC 9 .   ? 41.829  -21.101 25.667  1.00 26.08 ? 2291 HOH A O   1 
HETATM 11397 O  O   . HOH MC 9 .   ? 47.685  -24.992 32.761  1.00 33.36 ? 2292 HOH A O   1 
HETATM 11398 O  O   . HOH MC 9 .   ? 48.060  -22.728 31.183  1.00 45.09 ? 2293 HOH A O   1 
HETATM 11399 O  O   . HOH MC 9 .   ? 44.728  -17.654 33.713  1.00 17.86 ? 2294 HOH A O   1 
HETATM 11400 O  O   . HOH MC 9 .   ? 51.335  -17.598 34.848  1.00 43.03 ? 2295 HOH A O   1 
HETATM 11401 O  O   . HOH MC 9 .   ? 48.116  -24.429 34.970  1.00 38.03 ? 2296 HOH A O   1 
HETATM 11402 O  O   . HOH MC 9 .   ? 49.952  -22.132 37.664  1.00 40.87 ? 2297 HOH A O   1 
HETATM 11403 O  O   . HOH MC 9 .   ? 48.735  -18.317 39.618  1.00 58.31 ? 2298 HOH A O   1 
HETATM 11404 O  O   . HOH MC 9 .   ? 48.216  -26.645 36.516  1.00 39.42 ? 2299 HOH A O   1 
HETATM 11405 O  O   . HOH MC 9 .   ? 44.260  -24.862 43.099  1.00 35.65 ? 2300 HOH A O   1 
HETATM 11406 O  O   . HOH MC 9 .   ? 48.233  -18.398 42.486  1.00 30.79 ? 2301 HOH A O   1 
HETATM 11407 O  O   . HOH MC 9 .   ? 4.850   -13.098 46.995  1.00 44.61 ? 2302 HOH A O   1 
HETATM 11408 O  O   . HOH MC 9 .   ? 8.642   -10.749 41.150  1.00 38.71 ? 2303 HOH A O   1 
HETATM 11409 O  O   . HOH MC 9 .   ? 4.060   -9.319  45.513  1.00 38.35 ? 2304 HOH A O   1 
HETATM 11410 O  O   . HOH MC 9 .   ? 7.713   -1.148  43.780  1.00 46.54 ? 2305 HOH A O   1 
HETATM 11411 O  O   . HOH MC 9 .   ? 10.032  0.879   47.896  1.00 43.47 ? 2306 HOH A O   1 
HETATM 11412 O  O   . HOH MC 9 .   ? 13.607  -3.727  52.482  1.00 50.61 ? 2307 HOH A O   1 
HETATM 11413 O  O   . HOH MC 9 .   ? 12.466  -21.864 14.702  1.00 16.48 ? 2308 HOH A O   1 
HETATM 11414 O  O   . HOH MC 9 .   ? 7.887   -22.368 14.472  1.00 48.55 ? 2309 HOH A O   1 
HETATM 11415 O  O   . HOH MC 9 .   ? 2.760   -23.914 10.298  1.00 57.07 ? 2310 HOH A O   1 
HETATM 11416 O  O   . HOH MC 9 .   ? 17.303  -7.194  55.080  1.00 39.07 ? 2311 HOH A O   1 
HETATM 11417 O  O   . HOH MC 9 .   ? 19.447  -14.270 52.634  1.00 37.18 ? 2312 HOH A O   1 
HETATM 11418 O  O   . HOH MC 9 .   ? 48.551  -12.363 44.817  1.00 41.80 ? 2313 HOH A O   1 
HETATM 11419 O  O   . HOH MC 9 .   ? 52.079  -15.232 44.849  1.00 51.68 ? 2314 HOH A O   1 
HETATM 11420 O  O   . HOH MC 9 .   ? 50.564  -9.453  50.583  1.00 40.83 ? 2315 HOH A O   1 
HETATM 11421 O  O   . HOH MC 9 .   ? 52.270  -9.096  44.211  1.00 41.89 ? 2316 HOH A O   1 
HETATM 11422 O  O   . HOH MC 9 .   ? 52.732  -19.487 53.166  1.00 35.87 ? 2317 HOH A O   1 
HETATM 11423 O  O   . HOH MC 9 .   ? 55.037  -21.427 56.460  1.00 41.88 ? 2318 HOH A O   1 
HETATM 11424 O  O   . HOH MC 9 .   ? 55.319  -9.856  46.884  1.00 42.83 ? 2319 HOH A O   1 
HETATM 11425 O  O   . HOH MC 9 .   ? 60.728  -2.723  45.234  1.00 60.35 ? 2320 HOH A O   1 
HETATM 11426 O  O   . HOH MC 9 .   ? 25.985  -47.401 19.426  1.00 41.60 ? 2321 HOH A O   1 
HETATM 11427 O  O   . HOH MC 9 .   ? 27.160  -50.966 18.075  1.00 53.29 ? 2322 HOH A O   1 
HETATM 11428 O  O   . HOH MC 9 .   ? 27.322  -24.182 34.698  1.00 54.05 ? 2323 HOH A O   1 
HETATM 11429 O  O   . HOH MC 9 .   ? 12.766  -25.633 54.749  1.00 43.67 ? 2324 HOH A O   1 
HETATM 11430 O  O   . HOH MC 9 .   ? 14.261  -28.656 57.183  1.00 40.55 ? 2325 HOH A O   1 
HETATM 11431 O  O   . HOH MC 9 .   ? 41.464  -10.868 33.559  1.00 50.74 ? 2326 HOH A O   1 
HETATM 11432 O  O   . HOH MC 9 .   ? 52.513  -26.538 40.061  1.00 49.85 ? 2327 HOH A O   1 
HETATM 11433 O  O   . HOH NC 9 .   ? -34.993 -36.081 22.645  1.00 31.24 ? 2001 HOH B O   1 
HETATM 11434 O  O   . HOH NC 9 .   ? -33.128 -39.233 26.708  1.00 49.48 ? 2002 HOH B O   1 
HETATM 11435 O  O   . HOH NC 9 .   ? -35.887 -34.741 30.540  1.00 79.82 ? 2003 HOH B O   1 
HETATM 11436 O  O   . HOH NC 9 .   ? -35.425 -39.000 29.653  1.00 42.05 ? 2004 HOH B O   1 
HETATM 11437 O  O   . HOH NC 9 .   ? -37.491 -35.563 20.842  1.00 29.28 ? 2005 HOH B O   1 
HETATM 11438 O  O   . HOH NC 9 .   ? -34.787 -34.270 33.226  1.00 50.25 ? 2006 HOH B O   1 
HETATM 11439 O  O   . HOH NC 9 .   ? -32.341 -40.944 31.682  1.00 30.93 ? 2007 HOH B O   1 
HETATM 11440 O  O   . HOH NC 9 .   ? -29.124 -39.440 33.504  1.00 31.50 ? 2008 HOH B O   1 
HETATM 11441 O  O   . HOH NC 9 .   ? -27.549 -45.317 42.418  1.00 47.30 ? 2009 HOH B O   1 
HETATM 11442 O  O   . HOH NC 9 .   ? -27.573 -35.055 38.015  1.00 14.99 ? 2010 HOH B O   1 
HETATM 11443 O  O   . HOH NC 9 .   ? -28.028 -36.682 40.235  1.00 33.21 ? 2011 HOH B O   1 
HETATM 11444 O  O   . HOH NC 9 .   ? -26.571 -43.468 44.406  1.00 46.34 ? 2012 HOH B O   1 
HETATM 11445 O  O   . HOH NC 9 .   ? -26.607 -39.940 44.068  1.00 37.59 ? 2013 HOH B O   1 
HETATM 11446 O  O   . HOH NC 9 .   ? -28.165 -45.370 35.452  1.00 49.86 ? 2014 HOH B O   1 
HETATM 11447 O  O   . HOH NC 9 .   ? -18.092 -41.126 47.041  1.00 42.42 ? 2015 HOH B O   1 
HETATM 11448 O  O   . HOH NC 9 .   ? -11.183 -44.717 41.026  1.00 32.22 ? 2016 HOH B O   1 
HETATM 11449 O  O   . HOH NC 9 .   ? -33.697 -47.324 35.687  1.00 55.07 ? 2017 HOH B O   1 
HETATM 11450 O  O   . HOH NC 9 .   ? -31.771 -48.421 35.095  1.00 47.38 ? 2018 HOH B O   1 
HETATM 11451 O  O   . HOH NC 9 .   ? -22.606 -41.239 37.238  1.00 25.13 ? 2019 HOH B O   1 
HETATM 11452 O  O   . HOH NC 9 .   ? -21.004 -42.510 40.593  1.00 62.42 ? 2020 HOH B O   1 
HETATM 11453 O  O   . HOH NC 9 .   ? -4.890  -42.214 29.402  1.00 32.94 ? 2021 HOH B O   1 
HETATM 11454 O  O   . HOH NC 9 .   ? -3.233  -37.300 29.453  1.00 41.15 ? 2022 HOH B O   1 
HETATM 11455 O  O   . HOH NC 9 .   ? -23.972 -36.410 45.202  1.00 31.01 ? 2023 HOH B O   1 
HETATM 11456 O  O   . HOH NC 9 .   ? -26.253 -34.883 45.549  1.00 35.71 ? 2024 HOH B O   1 
HETATM 11457 O  O   . HOH NC 9 .   ? -21.436 -39.854 28.483  1.00 41.11 ? 2025 HOH B O   1 
HETATM 11458 O  O   . HOH NC 9 .   ? -22.830 -38.998 47.401  1.00 34.19 ? 2026 HOH B O   1 
HETATM 11459 O  O   . HOH NC 9 .   ? -18.666 -38.301 46.516  1.00 29.84 ? 2027 HOH B O   1 
HETATM 11460 O  O   . HOH NC 9 .   ? -13.883 -43.916 41.093  1.00 38.17 ? 2028 HOH B O   1 
HETATM 11461 O  O   . HOH NC 9 .   ? -14.620 -44.270 36.980  1.00 40.44 ? 2029 HOH B O   1 
HETATM 11462 O  O   . HOH NC 9 .   ? -7.683  -41.765 31.128  1.00 27.74 ? 2030 HOH B O   1 
HETATM 11463 O  O   . HOH NC 9 .   ? -5.957  -40.577 35.279  1.00 31.14 ? 2031 HOH B O   1 
HETATM 11464 O  O   . HOH NC 9 .   ? -6.294  -39.378 29.720  1.00 34.20 ? 2032 HOH B O   1 
HETATM 11465 O  O   . HOH NC 9 .   ? -4.959  -36.867 31.248  1.00 41.20 ? 2033 HOH B O   1 
HETATM 11466 O  O   . HOH NC 9 .   ? -16.335 -42.266 33.635  1.00 37.30 ? 2034 HOH B O   1 
HETATM 11467 O  O   . HOH NC 9 .   ? -6.666  -45.507 28.359  1.00 45.20 ? 2035 HOH B O   1 
HETATM 11468 O  O   . HOH NC 9 .   ? -9.187  -55.283 31.963  1.00 57.48 ? 2036 HOH B O   1 
HETATM 11469 O  O   . HOH NC 9 .   ? -12.866 -42.851 24.304  1.00 38.83 ? 2037 HOH B O   1 
HETATM 11470 O  O   . HOH NC 9 .   ? -19.448 -41.910 27.969  1.00 38.73 ? 2038 HOH B O   1 
HETATM 11471 O  O   . HOH NC 9 .   ? -19.762 -41.919 30.122  1.00 58.12 ? 2039 HOH B O   1 
HETATM 11472 O  O   . HOH NC 9 .   ? -7.795  -33.166 22.197  1.00 21.92 ? 2040 HOH B O   1 
HETATM 11473 O  O   . HOH NC 9 .   ? -31.186 -38.278 20.986  1.00 25.34 ? 2041 HOH B O   1 
HETATM 11474 O  O   . HOH NC 9 .   ? -9.926  -36.295 21.282  1.00 22.92 ? 2042 HOH B O   1 
HETATM 11475 O  O   . HOH NC 9 .   ? -5.902  -42.892 18.359  1.00 52.47 ? 2043 HOH B O   1 
HETATM 11476 O  O   . HOH NC 9 .   ? -27.512 -40.912 22.688  1.00 29.98 ? 2044 HOH B O   1 
HETATM 11477 O  O   . HOH NC 9 .   ? -9.371  -36.488 18.743  1.00 30.92 ? 2045 HOH B O   1 
HETATM 11478 O  O   . HOH NC 9 .   ? -6.221  -39.433 18.355  1.00 49.43 ? 2046 HOH B O   1 
HETATM 11479 O  O   . HOH NC 9 .   ? -4.349  -31.984 19.885  1.00 36.15 ? 2047 HOH B O   1 
HETATM 11480 O  O   . HOH NC 9 .   ? -8.578  -30.535 14.358  1.00 37.81 ? 2048 HOH B O   1 
HETATM 11481 O  O   . HOH NC 9 .   ? -9.190  -39.117 18.554  1.00 44.01 ? 2049 HOH B O   1 
HETATM 11482 O  O   . HOH NC 9 .   ? -10.425 -41.662 18.130  1.00 45.86 ? 2050 HOH B O   1 
HETATM 11483 O  O   . HOH NC 9 .   ? -12.121 -35.856 13.018  1.00 34.34 ? 2051 HOH B O   1 
HETATM 11484 O  O   . HOH NC 9 .   ? -29.642 -32.108 41.034  1.00 36.95 ? 2052 HOH B O   1 
HETATM 11485 O  O   . HOH NC 9 .   ? -15.184 -34.858 11.604  1.00 30.90 ? 2053 HOH B O   1 
HETATM 11486 O  O   . HOH NC 9 .   ? -11.309 -27.303 16.186  1.00 16.54 ? 2054 HOH B O   1 
HETATM 11487 O  O   . HOH NC 9 .   ? -16.763 -25.769 22.622  1.00 9.94  ? 2055 HOH B O   1 
HETATM 11488 O  O   . HOH NC 9 .   ? -11.191 -24.179 21.062  1.00 28.10 ? 2056 HOH B O   1 
HETATM 11489 O  O   . HOH NC 9 .   ? -34.570 -27.732 7.380   1.00 34.44 ? 2057 HOH B O   1 
HETATM 11490 O  O   . HOH NC 9 .   ? -15.165 -18.678 25.383  1.00 13.01 ? 2058 HOH B O   1 
HETATM 11491 O  O   . HOH NC 9 .   ? -35.193 -35.578 15.384  1.00 33.09 ? 2059 HOH B O   1 
HETATM 11492 O  O   . HOH NC 9 .   ? -34.404 -38.963 19.387  1.00 51.50 ? 2060 HOH B O   1 
HETATM 11493 O  O   . HOH NC 9 .   ? -36.004 -33.666 19.451  1.00 29.80 ? 2061 HOH B O   1 
HETATM 11494 O  O   . HOH NC 9 .   ? -14.112 -22.308 9.874   1.00 43.12 ? 2062 HOH B O   1 
HETATM 11495 O  O   . HOH NC 9 .   ? -10.657 -26.095 26.110  1.00 18.31 ? 2063 HOH B O   1 
HETATM 11496 O  O   . HOH NC 9 .   ? -14.723 -31.243 2.186   1.00 44.31 ? 2064 HOH B O   1 
HETATM 11497 O  O   . HOH NC 9 .   ? -37.469 -21.609 9.170   1.00 24.63 ? 2065 HOH B O   1 
HETATM 11498 O  O   . HOH NC 9 .   ? -37.288 -14.755 7.104   1.00 32.16 ? 2066 HOH B O   1 
HETATM 11499 O  O   . HOH NC 9 .   ? -21.550 -14.564 10.429  1.00 51.53 ? 2067 HOH B O   1 
HETATM 11500 O  O   . HOH NC 9 .   ? -17.312 -14.031 14.731  1.00 31.33 ? 2068 HOH B O   1 
HETATM 11501 O  O   . HOH NC 9 .   ? -23.063 -38.568 25.859  1.00 32.65 ? 2069 HOH B O   1 
HETATM 11502 O  O   . HOH NC 9 .   ? -15.431 -40.382 18.928  1.00 33.23 ? 2070 HOH B O   1 
HETATM 11503 O  O   . HOH NC 9 .   ? -13.169 -42.919 20.018  1.00 46.98 ? 2071 HOH B O   1 
HETATM 11504 O  O   . HOH NC 9 .   ? -13.712 -42.650 21.818  1.00 46.74 ? 2072 HOH B O   1 
HETATM 11505 O  O   . HOH NC 9 .   ? -12.086 -17.373 13.305  1.00 35.74 ? 2073 HOH B O   1 
HETATM 11506 O  O   . HOH NC 9 .   ? -23.100 -37.473 17.409  1.00 24.44 ? 2074 HOH B O   1 
HETATM 11507 O  O   . HOH NC 9 .   ? -31.104 -35.586 21.227  1.00 28.45 ? 2075 HOH B O   1 
HETATM 11508 O  O   . HOH NC 9 .   ? -21.922 -39.875 17.357  1.00 31.59 ? 2076 HOH B O   1 
HETATM 11509 O  O   . HOH NC 9 .   ? -1.953  -13.684 48.579  1.00 43.94 ? 2077 HOH B O   1 
HETATM 11510 O  O   . HOH NC 9 .   ? -29.517 -41.075 30.750  1.00 50.90 ? 2078 HOH B O   1 
HETATM 11511 O  O   . HOH NC 9 .   ? -26.515 -38.995 32.344  1.00 33.08 ? 2079 HOH B O   1 
HETATM 11512 O  O   . HOH NC 9 .   ? -30.867 -40.487 27.679  1.00 41.93 ? 2080 HOH B O   1 
HETATM 11513 O  O   . HOH NC 9 .   ? -25.265 -40.477 25.430  1.00 39.60 ? 2081 HOH B O   1 
HETATM 11514 O  O   . HOH NC 9 .   ? -16.641 -31.924 37.989  1.00 19.19 ? 2082 HOH B O   1 
HETATM 11515 O  O   . HOH NC 9 .   ? -18.788 2.313   31.198  1.00 35.52 ? 2083 HOH B O   1 
HETATM 11516 O  O   . HOH NC 9 .   ? -7.649  -5.364  26.592  1.00 33.56 ? 2084 HOH B O   1 
HETATM 11517 O  O   . HOH NC 9 .   ? -24.986 -34.421 37.230  1.00 15.38 ? 2085 HOH B O   1 
HETATM 11518 O  O   . HOH NC 9 .   ? -29.437 -25.392 37.835  1.00 41.66 ? 2086 HOH B O   1 
HETATM 11519 O  O   . HOH NC 9 .   ? -30.881 -29.582 38.181  1.00 29.95 ? 2087 HOH B O   1 
HETATM 11520 O  O   . HOH NC 9 .   ? -28.853 -33.006 38.501  1.00 16.17 ? 2088 HOH B O   1 
HETATM 11521 O  O   . HOH NC 9 .   ? -34.199 -30.393 33.467  1.00 40.10 ? 2089 HOH B O   1 
HETATM 11522 O  O   . HOH NC 9 .   ? -29.438 -12.547 33.235  1.00 56.13 ? 2090 HOH B O   1 
HETATM 11523 O  O   . HOH NC 9 .   ? -36.554 -26.096 39.834  1.00 30.91 ? 2091 HOH B O   1 
HETATM 11524 O  O   . HOH NC 9 .   ? -27.081 -23.242 32.379  1.00 37.15 ? 2092 HOH B O   1 
HETATM 11525 O  O   . HOH NC 9 .   ? -6.683  -31.377 40.050  1.00 27.20 ? 2093 HOH B O   1 
HETATM 11526 O  O   . HOH NC 9 .   ? -8.365  -34.282 48.757  1.00 40.32 ? 2094 HOH B O   1 
HETATM 11527 O  O   . HOH NC 9 .   ? -5.059  -34.840 42.398  1.00 35.26 ? 2095 HOH B O   1 
HETATM 11528 O  O   . HOH NC 9 .   ? -33.258 -34.123 22.471  1.00 13.15 ? 2096 HOH B O   1 
HETATM 11529 O  O   . HOH NC 9 .   ? -17.965 -33.455 49.449  1.00 38.99 ? 2097 HOH B O   1 
HETATM 11530 O  O   . HOH NC 9 .   ? -11.893 -41.053 46.976  1.00 50.01 ? 2098 HOH B O   1 
HETATM 11531 O  O   . HOH NC 9 .   ? -9.600  -39.574 48.145  1.00 67.84 ? 2099 HOH B O   1 
HETATM 11532 O  O   . HOH NC 9 .   ? -17.236 -32.111 52.607  1.00 52.49 ? 2100 HOH B O   1 
HETATM 11533 O  O   . HOH NC 9 .   ? -30.645 -23.476 14.909  1.00 19.81 ? 2101 HOH B O   1 
HETATM 11534 O  O   . HOH NC 9 .   ? -33.564 -31.276 17.173  1.00 18.39 ? 2102 HOH B O   1 
HETATM 11535 O  O   . HOH NC 9 .   ? -4.151  -30.618 38.905  1.00 21.38 ? 2103 HOH B O   1 
HETATM 11536 O  O   . HOH NC 9 .   ? -29.141 -21.461 13.672  1.00 18.92 ? 2104 HOH B O   1 
HETATM 11537 O  O   . HOH NC 9 .   ? -27.781 -18.843 13.887  1.00 25.81 ? 2105 HOH B O   1 
HETATM 11538 O  O   . HOH NC 9 .   ? -25.811 -20.190 14.076  1.00 27.74 ? 2106 HOH B O   1 
HETATM 11539 O  O   . HOH NC 9 .   ? -24.130 -26.669 14.592  1.00 13.63 ? 2107 HOH B O   1 
HETATM 11540 O  O   . HOH NC 9 .   ? -22.744 -19.501 19.663  1.00 14.61 ? 2108 HOH B O   1 
HETATM 11541 O  O   . HOH NC 9 .   ? -32.684 -27.478 9.840   1.00 24.60 ? 2109 HOH B O   1 
HETATM 11542 O  O   . HOH NC 9 .   ? -26.509 -27.983 9.078   1.00 18.39 ? 2110 HOH B O   1 
HETATM 11543 O  O   . HOH NC 9 .   ? -32.616 -26.128 12.131  1.00 15.03 ? 2111 HOH B O   1 
HETATM 11544 O  O   . HOH NC 9 .   ? -35.970 -33.176 14.740  1.00 30.61 ? 2112 HOH B O   1 
HETATM 11545 O  O   . HOH NC 9 .   ? -33.804 -35.809 13.556  1.00 31.77 ? 2113 HOH B O   1 
HETATM 11546 O  O   . HOH NC 9 .   ? -31.106 -37.303 13.486  1.00 22.41 ? 2114 HOH B O   1 
HETATM 11547 O  O   . HOH NC 9 .   ? -20.392 -34.867 49.328  1.00 39.71 ? 2115 HOH B O   1 
HETATM 11548 O  O   . HOH NC 9 .   ? -34.143 -36.236 17.784  1.00 37.48 ? 2116 HOH B O   1 
HETATM 11549 O  O   . HOH NC 9 .   ? -33.787 -32.435 20.503  1.00 18.11 ? 2117 HOH B O   1 
HETATM 11550 O  O   . HOH NC 9 .   ? -16.904 -23.845 9.279   1.00 25.67 ? 2118 HOH B O   1 
HETATM 11551 O  O   . HOH NC 9 .   ? -17.804 -21.324 11.756  1.00 17.93 ? 2119 HOH B O   1 
HETATM 11552 O  O   . HOH NC 9 .   ? -23.742 -26.455 8.265   1.00 25.61 ? 2120 HOH B O   1 
HETATM 11553 O  O   . HOH NC 9 .   ? -22.990 -26.762 11.876  1.00 20.78 ? 2121 HOH B O   1 
HETATM 11554 O  O   . HOH NC 9 .   ? -23.673 -31.584 4.393   1.00 21.25 ? 2122 HOH B O   1 
HETATM 11555 O  O   . HOH NC 9 .   ? -14.620 -32.752 5.360   1.00 40.21 ? 2123 HOH B O   1 
HETATM 11556 O  O   . HOH NC 9 .   ? -21.292 -32.455 2.646   1.00 24.28 ? 2124 HOH B O   1 
HETATM 11557 O  O   . HOH NC 9 .   ? -23.186 -36.043 10.571  1.00 25.60 ? 2125 HOH B O   1 
HETATM 11558 O  O   . HOH NC 9 .   ? -27.152 -27.354 3.309   1.00 39.26 ? 2126 HOH B O   1 
HETATM 11559 O  O   . HOH NC 9 .   ? -30.292 -22.585 3.583   1.00 31.57 ? 2127 HOH B O   1 
HETATM 11560 O  O   . HOH NC 9 .   ? -35.120 -20.082 9.066   1.00 17.43 ? 2128 HOH B O   1 
HETATM 11561 O  O   . HOH NC 9 .   ? -38.141 -9.197  16.424  1.00 39.39 ? 2129 HOH B O   1 
HETATM 11562 O  O   . HOH NC 9 .   ? -34.816 -17.088 3.501   1.00 47.08 ? 2130 HOH B O   1 
HETATM 11563 O  O   . HOH NC 9 .   ? -36.908 -17.456 7.188   1.00 34.77 ? 2131 HOH B O   1 
HETATM 11564 O  O   . HOH NC 9 .   ? -31.864 -13.318 13.710  1.00 38.65 ? 2132 HOH B O   1 
HETATM 11565 O  O   . HOH NC 9 .   ? -29.547 -14.237 16.791  1.00 22.53 ? 2133 HOH B O   1 
HETATM 11566 O  O   . HOH NC 9 .   ? -27.766 -18.017 7.700   1.00 57.03 ? 2134 HOH B O   1 
HETATM 11567 O  O   . HOH NC 9 .   ? -28.268 -15.082 11.533  1.00 38.37 ? 2135 HOH B O   1 
HETATM 11568 O  O   . HOH NC 9 .   ? -36.328 -12.980 8.359   1.00 30.75 ? 2136 HOH B O   1 
HETATM 11569 O  O   . HOH NC 9 .   ? -27.251 -16.275 13.526  1.00 38.01 ? 2137 HOH B O   1 
HETATM 11570 O  O   . HOH NC 9 .   ? -42.352 -13.870 8.829   1.00 40.13 ? 2138 HOH B O   1 
HETATM 11571 O  O   . HOH NC 9 .   ? -46.742 -21.383 12.993  1.00 37.22 ? 2139 HOH B O   1 
HETATM 11572 O  O   . HOH NC 9 .   ? -48.121 -26.568 10.741  1.00 47.25 ? 2140 HOH B O   1 
HETATM 11573 O  O   . HOH NC 9 .   ? -38.304 -23.597 3.062   1.00 47.25 ? 2141 HOH B O   1 
HETATM 11574 O  O   . HOH NC 9 .   ? -19.979 -20.306 12.778  1.00 23.28 ? 2142 HOH B O   1 
HETATM 11575 O  O   . HOH NC 9 .   ? -50.007 -30.480 13.077  1.00 46.11 ? 2143 HOH B O   1 
HETATM 11576 O  O   . HOH NC 9 .   ? -41.752 -34.788 11.828  1.00 44.04 ? 2144 HOH B O   1 
HETATM 11577 O  O   . HOH NC 9 .   ? -15.962 -18.139 14.891  1.00 38.86 ? 2145 HOH B O   1 
HETATM 11578 O  O   . HOH NC 9 .   ? -15.642 -20.739 13.421  1.00 28.55 ? 2146 HOH B O   1 
HETATM 11579 O  O   . HOH NC 9 .   ? -21.735 -19.133 10.594  1.00 34.97 ? 2147 HOH B O   1 
HETATM 11580 O  O   . HOH NC 9 .   ? -24.458 -15.796 10.086  1.00 41.85 ? 2148 HOH B O   1 
HETATM 11581 O  O   . HOH NC 9 .   ? -41.152 -28.756 32.069  1.00 38.84 ? 2149 HOH B O   1 
HETATM 11582 O  O   . HOH NC 9 .   ? -19.185 -15.551 14.239  1.00 23.01 ? 2150 HOH B O   1 
HETATM 11583 O  O   . HOH NC 9 .   ? -25.243 -13.212 15.577  1.00 31.10 ? 2151 HOH B O   1 
HETATM 11584 O  O   . HOH NC 9 .   ? -17.182 -12.583 21.205  1.00 14.96 ? 2152 HOH B O   1 
HETATM 11585 O  O   . HOH NC 9 .   ? -18.403 -8.113  17.168  1.00 37.19 ? 2153 HOH B O   1 
HETATM 11586 O  O   . HOH NC 9 .   ? -20.290 -8.006  20.037  1.00 14.77 ? 2154 HOH B O   1 
HETATM 11587 O  O   . HOH NC 9 .   ? -24.158 -13.859 22.513  1.00 36.32 ? 2155 HOH B O   1 
HETATM 11588 O  O   . HOH NC 9 .   ? -48.820 -22.523 32.542  1.00 48.01 ? 2156 HOH B O   1 
HETATM 11589 O  O   . HOH NC 9 .   ? -15.781 -17.088 23.414  1.00 12.85 ? 2157 HOH B O   1 
HETATM 11590 O  O   . HOH NC 9 .   ? -15.345 -13.893 23.393  1.00 17.08 ? 2158 HOH B O   1 
HETATM 11591 O  O   . HOH NC 9 .   ? -21.297 -10.384 23.144  1.00 20.26 ? 2159 HOH B O   1 
HETATM 11592 O  O   . HOH NC 9 .   ? -17.130 -8.684  19.577  1.00 18.62 ? 2160 HOH B O   1 
HETATM 11593 O  O   . HOH NC 9 .   ? -13.990 -12.449 24.916  1.00 15.43 ? 2161 HOH B O   1 
HETATM 11594 O  O   . HOH NC 9 .   ? -8.674  -12.841 31.427  1.00 22.40 ? 2162 HOH B O   1 
HETATM 11595 O  O   . HOH NC 9 .   ? -9.790  -16.295 21.158  1.00 16.96 ? 2163 HOH B O   1 
HETATM 11596 O  O   . HOH NC 9 .   ? -10.750 -12.404 19.219  1.00 23.59 ? 2164 HOH B O   1 
HETATM 11597 O  O   . HOH NC 9 .   ? -11.253 -9.822  23.985  1.00 16.64 ? 2165 HOH B O   1 
HETATM 11598 O  O   . HOH NC 9 .   ? -16.860 -9.819  14.782  1.00 60.68 ? 2166 HOH B O   1 
HETATM 11599 O  O   . HOH NC 9 .   ? -13.273 -9.602  13.013  1.00 42.05 ? 2167 HOH B O   1 
HETATM 11600 O  O   . HOH NC 9 .   ? -6.523  -9.977  18.333  1.00 47.13 ? 2168 HOH B O   1 
HETATM 11601 O  O   . HOH NC 9 .   ? -14.702 -14.996 15.492  1.00 27.58 ? 2169 HOH B O   1 
HETATM 11602 O  O   . HOH NC 9 .   ? -11.064 -14.096 12.829  1.00 59.45 ? 2170 HOH B O   1 
HETATM 11603 O  O   . HOH NC 9 .   ? -13.482 -16.867 15.051  1.00 30.79 ? 2171 HOH B O   1 
HETATM 11604 O  O   . HOH NC 9 .   ? -7.076  -23.300 21.556  1.00 28.09 ? 2172 HOH B O   1 
HETATM 11605 O  O   . HOH NC 9 .   ? -3.561  -20.710 21.726  1.00 40.49 ? 2173 HOH B O   1 
HETATM 11606 O  O   . HOH NC 9 .   ? -5.018  -16.790 20.821  1.00 30.98 ? 2174 HOH B O   1 
HETATM 11607 O  O   . HOH NC 9 .   ? -7.474  -14.512 20.813  1.00 26.04 ? 2175 HOH B O   1 
HETATM 11608 O  O   . HOH NC 9 .   ? -2.642  -16.188 22.421  1.00 33.70 ? 2176 HOH B O   1 
HETATM 11609 O  O   . HOH NC 9 .   ? -1.825  -10.915 30.342  1.00 18.21 ? 2177 HOH B O   1 
HETATM 11610 O  O   . HOH NC 9 .   ? -1.783  -14.081 22.935  1.00 31.75 ? 2178 HOH B O   1 
HETATM 11611 O  O   . HOH NC 9 .   ? 0.894   -13.002 26.046  1.00 27.93 ? 2179 HOH B O   1 
HETATM 11612 O  O   . HOH NC 9 .   ? -1.403  -10.712 22.493  1.00 31.57 ? 2180 HOH B O   1 
HETATM 11613 O  O   . HOH NC 9 .   ? -52.944 -21.867 12.905  1.00 34.17 ? 2181 HOH B O   1 
HETATM 11614 O  O   . HOH NC 9 .   ? -4.077  -7.988  34.188  1.00 35.80 ? 2182 HOH B O   1 
HETATM 11615 O  O   . HOH NC 9 .   ? 0.708   -12.174 39.184  1.00 34.70 ? 2183 HOH B O   1 
HETATM 11616 O  O   . HOH NC 9 .   ? -0.877  -8.027  38.830  1.00 37.46 ? 2184 HOH B O   1 
HETATM 11617 O  O   . HOH NC 9 .   ? -2.359  -9.234  34.478  0.50 25.26 ? 2185 HOH B O   1 
HETATM 11618 O  O   . HOH NC 9 .   ? -10.561 -4.148  37.398  1.00 37.40 ? 2186 HOH B O   1 
HETATM 11619 O  O   . HOH NC 9 .   ? -5.752  -4.602  36.515  1.00 36.46 ? 2187 HOH B O   1 
HETATM 11620 O  O   . HOH NC 9 .   ? -4.460  -13.201 47.162  1.00 37.55 ? 2188 HOH B O   1 
HETATM 11621 O  O   . HOH NC 9 .   ? -0.652  -14.969 45.652  1.00 29.74 ? 2189 HOH B O   1 
HETATM 11622 O  O   . HOH NC 9 .   ? -8.941  -11.773 47.797  1.00 35.33 ? 2190 HOH B O   1 
HETATM 11623 O  O   . HOH NC 9 .   ? -7.298  -19.714 48.039  1.00 27.86 ? 2191 HOH B O   1 
HETATM 11624 O  O   . HOH NC 9 .   ? -1.737  -21.130 45.791  1.00 54.56 ? 2192 HOH B O   1 
HETATM 11625 O  O   . HOH NC 9 .   ? -2.294  -22.397 41.320  1.00 33.34 ? 2193 HOH B O   1 
HETATM 11626 O  O   . HOH NC 9 .   ? -14.638 -20.523 45.244  1.00 17.40 ? 2194 HOH B O   1 
HETATM 11627 O  O   . HOH NC 9 .   ? -14.939 -10.215 43.956  1.00 24.94 ? 2195 HOH B O   1 
HETATM 11628 O  O   . HOH NC 9 .   ? -15.801 -13.381 47.433  1.00 47.16 ? 2196 HOH B O   1 
HETATM 11629 O  O   . HOH NC 9 .   ? -18.212 -9.069  38.668  1.00 16.04 ? 2197 HOH B O   1 
HETATM 11630 O  O   . HOH NC 9 .   ? -15.271 -5.701  44.748  1.00 32.03 ? 2198 HOH B O   1 
HETATM 11631 O  O   . HOH NC 9 .   ? -17.563 -16.131 29.685  1.00 14.67 ? 2199 HOH B O   1 
HETATM 11632 O  O   . HOH NC 9 .   ? -11.926 -7.934  25.602  1.00 16.82 ? 2200 HOH B O   1 
HETATM 11633 O  O   . HOH NC 9 .   ? -13.481 0.451   30.668  1.00 22.81 ? 2201 HOH B O   1 
HETATM 11634 O  O   . HOH NC 9 .   ? -19.403 0.352   32.952  1.00 42.21 ? 2202 HOH B O   1 
HETATM 11635 O  O   . HOH NC 9 .   ? -7.172  -7.548  28.035  1.00 37.92 ? 2203 HOH B O   1 
HETATM 11636 O  O   . HOH NC 9 .   ? -9.878  3.022   25.770  1.00 24.53 ? 2204 HOH B O   1 
HETATM 11637 O  O   . HOH NC 9 .   ? -9.694  -6.498  24.628  1.00 30.25 ? 2205 HOH B O   1 
HETATM 11638 O  O   . HOH NC 9 .   ? -22.369 -3.136  20.176  1.00 21.44 ? 2206 HOH B O   1 
HETATM 11639 O  O   . HOH NC 9 .   ? -24.988 -9.396  24.199  1.00 26.17 ? 2207 HOH B O   1 
HETATM 11640 O  O   . HOH NC 9 .   ? -29.997 -11.316 30.708  1.00 26.02 ? 2208 HOH B O   1 
HETATM 11641 O  O   . HOH NC 9 .   ? -30.072 -9.548  22.640  1.00 37.31 ? 2209 HOH B O   1 
HETATM 11642 O  O   . HOH NC 9 .   ? -29.712 -12.549 23.425  1.00 27.00 ? 2210 HOH B O   1 
HETATM 11643 O  O   . HOH NC 9 .   ? -25.575 -17.165 34.789  1.00 35.16 ? 2211 HOH B O   1 
HETATM 11644 O  O   . HOH NC 9 .   ? -23.317 -7.345  38.180  1.00 27.62 ? 2212 HOH B O   1 
HETATM 11645 O  O   . HOH NC 9 .   ? -19.362 -7.336  37.013  1.00 14.15 ? 2213 HOH B O   1 
HETATM 11646 O  O   . HOH NC 9 .   ? -15.173 -26.692 44.449  1.00 11.75 ? 2214 HOH B O   1 
HETATM 11647 O  O   . HOH NC 9 .   ? -16.879 -22.376 44.837  1.00 27.25 ? 2215 HOH B O   1 
HETATM 11648 O  O   . HOH NC 9 .   ? -19.981 -22.378 45.230  1.00 25.92 ? 2216 HOH B O   1 
HETATM 11649 O  O   . HOH NC 9 .   ? -8.719  -29.190 40.062  1.00 21.87 ? 2217 HOH B O   1 
HETATM 11650 O  O   . HOH NC 9 .   ? -15.301 -30.720 43.220  1.00 29.63 ? 2218 HOH B O   1 
HETATM 11651 O  O   . HOH NC 9 .   ? -7.833  -34.326 45.334  1.00 44.83 ? 2219 HOH B O   1 
HETATM 11652 O  O   . HOH NC 9 .   ? -7.298  -33.848 39.900  1.00 24.06 ? 2220 HOH B O   1 
HETATM 11653 O  O   . HOH NC 9 .   ? -15.855 -34.619 48.286  1.00 28.46 ? 2221 HOH B O   1 
HETATM 11654 O  O   . HOH NC 9 .   ? -8.824  -41.109 46.048  1.00 36.25 ? 2222 HOH B O   1 
HETATM 11655 O  O   . HOH NC 9 .   ? -4.941  -37.576 42.828  1.00 41.94 ? 2223 HOH B O   1 
HETATM 11656 O  O   . HOH NC 9 .   ? -12.560 -37.863 49.409  1.00 48.53 ? 2224 HOH B O   1 
HETATM 11657 O  O   . HOH NC 9 .   ? -8.691  -37.166 49.361  1.00 45.57 ? 2225 HOH B O   1 
HETATM 11658 O  O   . HOH NC 9 .   ? -15.130 -31.846 50.440  1.00 53.07 ? 2226 HOH B O   1 
HETATM 11659 O  O   . HOH NC 9 .   ? -6.406  -32.672 44.507  1.00 35.02 ? 2227 HOH B O   1 
HETATM 11660 O  O   . HOH NC 9 .   ? -6.403  -30.743 42.853  1.00 30.04 ? 2228 HOH B O   1 
HETATM 11661 O  O   . HOH NC 9 .   ? -7.227  -27.413 41.272  1.00 29.24 ? 2229 HOH B O   1 
HETATM 11662 O  O   . HOH NC 9 .   ? -4.546  -27.700 43.761  1.00 34.14 ? 2230 HOH B O   1 
HETATM 11663 O  O   . HOH NC 9 .   ? -17.039 -25.131 46.711  1.00 40.17 ? 2231 HOH B O   1 
HETATM 11664 O  O   . HOH NC 9 .   ? -16.417 -25.697 49.105  1.00 50.97 ? 2232 HOH B O   1 
HETATM 11665 O  O   . HOH NC 9 .   ? -19.229 -26.990 46.833  1.00 28.70 ? 2233 HOH B O   1 
HETATM 11666 O  O   . HOH NC 9 .   ? -19.157 -31.162 48.804  1.00 40.96 ? 2234 HOH B O   1 
HETATM 11667 O  O   . HOH NC 9 .   ? -12.302 -24.001 50.930  1.00 25.75 ? 2235 HOH B O   1 
HETATM 11668 O  O   . HOH NC 9 .   ? -9.482  -19.495 50.187  1.00 49.31 ? 2236 HOH B O   1 
HETATM 11669 O  O   . HOH NC 9 .   ? -3.145  -30.735 36.744  1.00 38.75 ? 2237 HOH B O   1 
HETATM 11670 O  O   . HOH NC 9 .   ? 0.403   -31.763 36.743  1.00 35.26 ? 2238 HOH B O   1 
HETATM 11671 O  O   . HOH NC 9 .   ? -0.099  -28.584 40.007  1.00 35.61 ? 2239 HOH B O   1 
HETATM 11672 O  O   . HOH NC 9 .   ? -3.313  -32.245 32.522  1.00 43.10 ? 2240 HOH B O   1 
HETATM 11673 O  O   . HOH NC 9 .   ? -2.201  -30.409 30.237  1.00 42.78 ? 2241 HOH B O   1 
HETATM 11674 O  O   . HOH NC 9 .   ? -5.229  -24.630 22.822  1.00 30.72 ? 2242 HOH B O   1 
HETATM 11675 O  O   . HOH NC 9 .   ? -2.842  -22.967 22.742  1.00 28.99 ? 2243 HOH B O   1 
HETATM 11676 O  O   . HOH NC 9 .   ? -6.662  -30.538 22.710  1.00 28.61 ? 2244 HOH B O   1 
HETATM 11677 O  O   . HOH NC 9 .   ? -8.837  -29.187 22.556  1.00 27.17 ? 2245 HOH B O   1 
HETATM 11678 O  O   . HOH NC 9 .   ? -2.032  -35.575 28.166  1.00 61.68 ? 2246 HOH B O   1 
HETATM 11679 O  O   . HOH NC 9 .   ? -2.293  -33.524 36.009  1.00 26.45 ? 2247 HOH B O   1 
HETATM 11680 O  O   . HOH NC 9 .   ? -6.038  -42.071 37.833  1.00 38.21 ? 2248 HOH B O   1 
HETATM 11681 O  O   . HOH NC 9 .   ? -7.282  -43.053 42.127  1.00 37.53 ? 2249 HOH B O   1 
HETATM 11682 O  O   . HOH NC 9 .   ? -21.141 -36.686 47.468  1.00 38.08 ? 2250 HOH B O   1 
HETATM 11683 O  O   . HOH NC 9 .   ? -21.978 -31.817 48.077  1.00 40.21 ? 2251 HOH B O   1 
HETATM 11684 O  O   . HOH NC 9 .   ? -27.919 -31.081 43.341  1.00 25.25 ? 2252 HOH B O   1 
HETATM 11685 O  O   . HOH NC 9 .   ? -25.540 -24.986 40.982  1.00 22.31 ? 2253 HOH B O   1 
HETATM 11686 O  O   . HOH NC 9 .   ? -27.316 -22.947 36.640  1.00 37.84 ? 2254 HOH B O   1 
HETATM 11687 O  O   . HOH NC 9 .   ? -26.872 -23.182 39.980  1.00 28.90 ? 2255 HOH B O   1 
HETATM 11688 O  O   . HOH NC 9 .   ? -22.011 -26.391 44.881  1.00 45.00 ? 2256 HOH B O   1 
HETATM 11689 O  O   . HOH NC 9 .   ? -25.509 -19.893 44.895  1.00 50.67 ? 2257 HOH B O   1 
HETATM 11690 O  O   . HOH NC 9 .   ? -24.175 -19.759 46.968  1.00 42.41 ? 2258 HOH B O   1 
HETATM 11691 O  O   . HOH NC 9 .   ? -21.886 -21.038 46.458  1.00 46.71 ? 2259 HOH B O   1 
HETATM 11692 O  O   . HOH NC 9 .   ? -26.644 -10.911 43.164  1.00 39.48 ? 2260 HOH B O   1 
HETATM 11693 O  O   . HOH NC 9 .   ? -23.853 -4.150  45.263  1.00 48.67 ? 2261 HOH B O   1 
HETATM 11694 O  O   . HOH NC 9 .   ? -26.848 -4.150  42.432  1.00 37.91 ? 2262 HOH B O   1 
HETATM 11695 O  O   . HOH NC 9 .   ? -19.288 -2.328  39.188  1.00 44.34 ? 2263 HOH B O   1 
HETATM 11696 O  O   . HOH NC 9 .   ? -26.083 -2.174  38.045  1.00 34.05 ? 2264 HOH B O   1 
HETATM 11697 O  O   . HOH NC 9 .   ? -26.219 -6.577  37.825  1.00 25.47 ? 2265 HOH B O   1 
HETATM 11698 O  O   . HOH NC 9 .   ? -23.664 -0.543  34.617  1.00 21.94 ? 2266 HOH B O   1 
HETATM 11699 O  O   . HOH NC 9 .   ? -31.573 -0.562  36.876  1.00 40.66 ? 2267 HOH B O   1 
HETATM 11700 O  O   . HOH NC 9 .   ? -29.219 -2.190  20.144  1.00 60.61 ? 2268 HOH B O   1 
HETATM 11701 O  O   . HOH NC 9 .   ? -27.189 0.250   19.660  1.00 52.33 ? 2269 HOH B O   1 
HETATM 11702 O  O   . HOH NC 9 .   ? -30.483 3.478   24.339  1.00 39.94 ? 2270 HOH B O   1 
HETATM 11703 O  O   . HOH NC 9 .   ? -24.746 -1.058  19.109  1.00 35.50 ? 2271 HOH B O   1 
HETATM 11704 O  O   . HOH NC 9 .   ? -20.458 5.852   17.690  1.00 35.60 ? 2272 HOH B O   1 
HETATM 11705 O  O   . HOH NC 9 .   ? -13.649 3.627   18.688  1.00 30.66 ? 2273 HOH B O   1 
HETATM 11706 O  O   . HOH NC 9 .   ? -15.098 6.897   21.662  1.00 38.94 ? 2274 HOH B O   1 
HETATM 11707 O  O   . HOH NC 9 .   ? -18.212 3.866   28.485  1.00 24.33 ? 2275 HOH B O   1 
HETATM 11708 O  O   . HOH NC 9 .   ? -12.284 6.812   24.364  1.00 26.68 ? 2276 HOH B O   1 
HETATM 11709 O  O   . HOH NC 9 .   ? -14.997 3.300   29.458  1.00 31.07 ? 2277 HOH B O   1 
HETATM 11710 O  O   . HOH NC 9 .   ? -24.766 4.155   29.310  1.00 34.80 ? 2278 HOH B O   1 
HETATM 11711 O  O   . HOH NC 9 .   ? -21.286 4.324   30.224  1.00 33.27 ? 2279 HOH B O   1 
HETATM 11712 O  O   . HOH NC 9 .   ? -25.970 6.181   23.506  1.00 43.08 ? 2280 HOH B O   1 
HETATM 11713 O  O   . HOH NC 9 .   ? -38.049 -5.505  27.646  1.00 41.27 ? 2281 HOH B O   1 
HETATM 11714 O  O   . HOH NC 9 .   ? -35.976 -5.712  23.362  1.00 42.91 ? 2282 HOH B O   1 
HETATM 11715 O  O   . HOH NC 9 .   ? -35.919 -2.273  22.480  1.00 65.41 ? 2283 HOH B O   1 
HETATM 11716 O  O   . HOH NC 9 .   ? -32.433 -4.105  32.540  1.00 30.80 ? 2284 HOH B O   1 
HETATM 11717 O  O   . HOH NC 9 .   ? -31.809 -13.093 34.270  1.00 32.88 ? 2285 HOH B O   1 
HETATM 11718 O  O   . HOH NC 9 .   ? -34.631 -4.754  34.794  1.00 42.94 ? 2286 HOH B O   1 
HETATM 11719 O  O   . HOH NC 9 .   ? -28.737 -7.647  37.315  1.00 20.23 ? 2287 HOH B O   1 
HETATM 11720 O  O   . HOH NC 9 .   ? -31.934 -14.273 36.996  1.00 27.53 ? 2288 HOH B O   1 
HETATM 11721 O  O   . HOH NC 9 .   ? -38.200 -12.558 38.459  1.00 45.46 ? 2289 HOH B O   1 
HETATM 11722 O  O   . HOH NC 9 .   ? -32.770 -13.484 26.340  1.00 22.63 ? 2290 HOH B O   1 
HETATM 11723 O  O   . HOH NC 9 .   ? -40.092 -22.456 25.235  1.00 20.04 ? 2291 HOH B O   1 
HETATM 11724 O  O   . HOH NC 9 .   ? -45.857 -14.174 29.940  1.00 34.08 ? 2292 HOH B O   1 
HETATM 11725 O  O   . HOH NC 9 .   ? -42.381 -16.014 30.867  1.00 26.71 ? 2293 HOH B O   1 
HETATM 11726 O  O   . HOH NC 9 .   ? -32.292 -13.204 23.927  1.00 36.26 ? 2294 HOH B O   1 
HETATM 11727 O  O   . HOH NC 9 .   ? -42.731 -14.123 18.585  1.00 21.33 ? 2295 HOH B O   1 
HETATM 11728 O  O   . HOH NC 9 .   ? -40.068 -11.396 17.460  1.00 31.85 ? 2296 HOH B O   1 
HETATM 11729 O  O   . HOH NC 9 .   ? -43.012 -11.748 21.906  1.00 32.78 ? 2297 HOH B O   1 
HETATM 11730 O  O   . HOH NC 9 .   ? -32.249 -13.813 16.076  1.00 29.56 ? 2298 HOH B O   1 
HETATM 11731 O  O   . HOH NC 9 .   ? -33.145 -11.107 23.050  1.00 42.36 ? 2299 HOH B O   1 
HETATM 11732 O  O   . HOH NC 9 .   ? -32.127 -11.468 19.682  1.00 42.52 ? 2300 HOH B O   1 
HETATM 11733 O  O   . HOH NC 9 .   ? -36.127 -12.745 10.818  1.00 23.68 ? 2301 HOH B O   1 
HETATM 11734 O  O   . HOH NC 9 .   ? -35.500 -9.485  16.019  1.00 41.02 ? 2302 HOH B O   1 
HETATM 11735 O  O   . HOH NC 9 .   ? -38.943 -19.018 8.626   1.00 28.10 ? 2303 HOH B O   1 
HETATM 11736 O  O   . HOH NC 9 .   ? -44.460 -17.774 12.196  1.00 33.83 ? 2304 HOH B O   1 
HETATM 11737 O  O   . HOH NC 9 .   ? -42.939 -14.213 11.022  1.00 31.19 ? 2305 HOH B O   1 
HETATM 11738 O  O   . HOH NC 9 .   ? -40.140 -21.454 5.808   1.00 33.77 ? 2306 HOH B O   1 
HETATM 11739 O  O   . HOH NC 9 .   ? -41.052 -17.010 4.826   1.00 38.60 ? 2307 HOH B O   1 
HETATM 11740 O  O   . HOH NC 9 .   ? -44.977 -21.217 10.021  1.00 38.49 ? 2308 HOH B O   1 
HETATM 11741 O  O   . HOH NC 9 .   ? -45.849 -24.513 9.635   1.00 41.24 ? 2309 HOH B O   1 
HETATM 11742 O  O   . HOH NC 9 .   ? -38.805 -23.020 7.297   1.00 22.39 ? 2310 HOH B O   1 
HETATM 11743 O  O   . HOH NC 9 .   ? -37.974 -25.437 5.490   1.00 51.19 ? 2311 HOH B O   1 
HETATM 11744 O  O   . HOH NC 9 .   ? -44.542 -27.108 5.238   1.00 43.73 ? 2312 HOH B O   1 
HETATM 11745 O  O   . HOH NC 9 .   ? -46.002 -27.787 12.356  1.00 36.18 ? 2313 HOH B O   1 
HETATM 11746 O  O   . HOH NC 9 .   ? -37.256 -28.818 7.030   1.00 36.98 ? 2314 HOH B O   1 
HETATM 11747 O  O   . HOH NC 9 .   ? -49.313 -24.496 12.853  1.00 45.11 ? 2315 HOH B O   1 
HETATM 11748 O  O   . HOH NC 9 .   ? -49.771 -28.051 14.292  1.00 47.68 ? 2316 HOH B O   1 
HETATM 11749 O  O   . HOH NC 9 .   ? -45.791 -28.521 16.723  1.00 32.11 ? 2317 HOH B O   1 
HETATM 11750 O  O   . HOH NC 9 .   ? -43.610 -30.829 18.539  1.00 26.97 ? 2318 HOH B O   1 
HETATM 11751 O  O   . HOH NC 9 .   ? -40.128 -34.754 14.769  1.00 53.16 ? 2319 HOH B O   1 
HETATM 11752 O  O   . HOH NC 9 .   ? -40.022 -33.315 17.415  1.00 26.48 ? 2320 HOH B O   1 
HETATM 11753 O  O   . HOH NC 9 .   ? -44.108 -29.750 21.055  1.00 41.96 ? 2321 HOH B O   1 
HETATM 11754 O  O   . HOH NC 9 .   ? -43.046 -25.111 22.434  1.00 25.00 ? 2322 HOH B O   1 
HETATM 11755 O  O   . HOH NC 9 .   ? -44.687 -22.353 19.883  1.00 26.39 ? 2323 HOH B O   1 
HETATM 11756 O  O   . HOH NC 9 .   ? -37.254 -32.394 17.564  1.00 27.19 ? 2324 HOH B O   1 
HETATM 11757 O  O   . HOH NC 9 .   ? -41.582 -28.487 28.733  1.00 37.70 ? 2325 HOH B O   1 
HETATM 11758 O  O   . HOH NC 9 .   ? -46.195 -27.387 23.610  1.00 52.89 ? 2326 HOH B O   1 
HETATM 11759 O  O   . HOH NC 9 .   ? -43.623 -27.319 28.008  1.00 41.14 ? 2327 HOH B O   1 
HETATM 11760 O  O   . HOH NC 9 .   ? -41.913 -31.828 23.553  1.00 33.70 ? 2328 HOH B O   1 
HETATM 11761 O  O   . HOH NC 9 .   ? -39.598 -23.661 33.591  1.00 24.66 ? 2329 HOH B O   1 
HETATM 11762 O  O   . HOH NC 9 .   ? -38.674 -24.720 37.553  1.00 40.32 ? 2330 HOH B O   1 
HETATM 11763 O  O   . HOH NC 9 .   ? -38.143 -21.734 41.620  1.00 24.73 ? 2331 HOH B O   1 
HETATM 11764 O  O   . HOH NC 9 .   ? -35.288 -21.847 41.311  1.00 38.93 ? 2332 HOH B O   1 
HETATM 11765 O  O   . HOH NC 9 .   ? -40.160 -19.374 41.178  1.00 24.47 ? 2333 HOH B O   1 
HETATM 11766 O  O   . HOH NC 9 .   ? -42.944 -22.384 35.504  1.00 41.48 ? 2334 HOH B O   1 
HETATM 11767 O  O   . HOH NC 9 .   ? -43.266 -15.569 33.432  1.00 39.35 ? 2335 HOH B O   1 
HETATM 11768 O  O   . HOH NC 9 .   ? -46.846 -15.108 32.730  1.00 57.82 ? 2336 HOH B O   1 
HETATM 11769 O  O   . HOH NC 9 .   ? -45.813 -22.545 31.430  1.00 28.46 ? 2337 HOH B O   1 
HETATM 11770 O  O   . HOH NC 9 .   ? -48.339 -20.883 28.856  1.00 47.99 ? 2338 HOH B O   1 
HETATM 11771 O  O   . HOH NC 9 .   ? -45.684 -25.386 30.245  1.00 27.60 ? 2339 HOH B O   1 
HETATM 11772 O  O   . HOH NC 9 .   ? -42.368 -22.987 24.083  1.00 20.23 ? 2340 HOH B O   1 
HETATM 11773 O  O   . HOH NC 9 .   ? -47.020 -17.390 24.346  1.00 28.61 ? 2341 HOH B O   1 
HETATM 11774 O  O   . HOH NC 9 .   ? -48.801 -18.856 20.792  1.00 28.00 ? 2342 HOH B O   1 
HETATM 11775 O  O   . HOH NC 9 .   ? -45.767 -17.035 14.586  1.00 34.44 ? 2343 HOH B O   1 
HETATM 11776 O  O   . HOH NC 9 .   ? -45.528 -26.130 21.464  1.00 37.52 ? 2344 HOH B O   1 
HETATM 11777 O  O   . HOH NC 9 .   ? -51.492 -22.107 20.653  1.00 43.21 ? 2345 HOH B O   1 
HETATM 11778 O  O   . HOH NC 9 .   ? -2.439  -10.599 19.052  1.00 40.24 ? 2346 HOH B O   1 
HETATM 11779 O  O   . HOH NC 9 .   ? -3.392  -6.885  20.964  1.00 45.18 ? 2347 HOH B O   1 
HETATM 11780 O  O   . HOH NC 9 .   ? -11.764 4.219   14.994  1.00 42.16 ? 2348 HOH B O   1 
HETATM 11781 O  O   . HOH NC 9 .   ? -2.757  5.517   12.900  1.00 40.20 ? 2349 HOH B O   1 
HETATM 11782 O  O   . HOH NC 9 .   ? -11.202 -17.081 52.878  1.00 32.49 ? 2350 HOH B O   1 
HETATM 11783 O  O   . HOH NC 9 .   ? -13.533 -10.205 52.798  1.00 47.93 ? 2351 HOH B O   1 
HETATM 11784 O  O   . HOH NC 9 .   ? -22.544 -0.961  9.506   1.00 47.61 ? 2352 HOH B O   1 
HETATM 11785 O  O   . HOH NC 9 .   ? -19.795 -0.460  11.019  1.00 39.50 ? 2353 HOH B O   1 
HETATM 11786 O  O   . HOH NC 9 .   ? -25.286 -5.461  14.998  1.00 58.40 ? 2354 HOH B O   1 
HETATM 11787 O  O   . HOH NC 9 .   ? -25.032 -5.524  7.042   1.00 43.13 ? 2355 HOH B O   1 
HETATM 11788 O  O   . HOH NC 9 .   ? -25.370 -1.571  11.123  1.00 42.27 ? 2356 HOH B O   1 
HETATM 11789 O  O   . HOH NC 9 .   ? -48.371 -11.313 21.635  1.00 37.46 ? 2357 HOH B O   1 
HETATM 11790 O  O   . HOH NC 9 .   ? -51.996 -17.161 20.509  1.00 34.56 ? 2358 HOH B O   1 
HETATM 11791 O  O   . HOH NC 9 .   ? -54.285 -15.441 18.832  1.00 37.22 ? 2359 HOH B O   1 
HETATM 11792 O  O   . HOH NC 9 .   ? -54.768 -10.323 19.749  1.00 33.25 ? 2360 HOH B O   1 
HETATM 11793 O  O   . HOH NC 9 .   ? -58.404 -9.075  13.341  1.00 36.68 ? 2361 HOH B O   1 
HETATM 11794 O  O   . HOH NC 9 .   ? -54.640 -3.109  13.318  1.00 42.76 ? 2362 HOH B O   1 
HETATM 11795 O  O   . HOH NC 9 .   ? -56.489 -20.947 14.803  1.00 35.75 ? 2363 HOH B O   1 
HETATM 11796 O  O   . HOH NC 9 .   ? -51.211 -19.918 13.381  1.00 31.77 ? 2364 HOH B O   1 
HETATM 11797 O  O   . HOH NC 9 .   ? -54.970 -21.848 7.565   1.00 30.12 ? 2365 HOH B O   1 
HETATM 11798 O  O   . HOH NC 9 .   ? -23.309 -48.684 42.241  1.00 53.24 ? 2366 HOH B O   1 
HETATM 11799 O  O   . HOH NC 9 .   ? -12.368 -43.901 45.298  1.00 44.83 ? 2367 HOH B O   1 
HETATM 11800 O  O   . HOH NC 9 .   ? -25.300 -21.413 31.695  1.00 46.19 ? 2368 HOH B O   1 
HETATM 11801 O  O   . HOH NC 9 .   ? -13.163 -21.558 12.147  1.00 44.20 ? 2369 HOH B O   1 
HETATM 11802 O  O   . HOH OC 9 .   ? 23.876  -44.709 6.123   1.00 52.44 ? 2001 HOH C O   1 
HETATM 11803 O  O   . HOH OC 9 .   ? 24.563  -39.877 3.182   1.00 28.25 ? 2002 HOH C O   1 
HETATM 11804 O  O   . HOH OC 9 .   ? 27.543  -42.811 7.307   1.00 44.80 ? 2003 HOH C O   1 
HETATM 11805 O  O   . HOH OC 9 .   ? 24.933  -42.947 9.906   1.00 36.18 ? 2004 HOH C O   1 
HETATM 11806 O  O   . HOH OC 9 .   ? 23.955  -42.890 12.401  1.00 53.68 ? 2005 HOH C O   1 
HETATM 11807 O  O   . HOH OC 9 .   ? 28.094  -43.890 12.676  1.00 33.87 ? 2006 HOH C O   1 
HETATM 11808 O  O   . HOH OC 9 .   ? 30.974  -42.557 13.723  1.00 39.60 ? 2007 HOH C O   1 
HETATM 11809 O  O   . HOH OC 9 .   ? 32.143  -37.924 18.332  1.00 27.75 ? 2008 HOH C O   1 
HETATM 11810 O  O   . HOH OC 9 .   ? 31.828  -39.588 20.581  1.00 18.92 ? 2009 HOH C O   1 
HETATM 11811 O  O   . HOH OC 9 .   ? 38.810  -41.700 30.216  1.00 49.03 ? 2010 HOH C O   1 
HETATM 11812 O  O   . HOH OC 9 .   ? 43.423  -38.205 27.904  1.00 39.54 ? 2011 HOH C O   1 
HETATM 11813 O  O   . HOH OC 9 .   ? 37.881  -42.835 17.588  1.00 33.15 ? 2012 HOH C O   1 
HETATM 11814 O  O   . HOH OC 9 .   ? 35.718  -38.742 25.651  1.00 27.55 ? 2013 HOH C O   1 
HETATM 11815 O  O   . HOH OC 9 .   ? 37.705  -41.148 27.486  1.00 38.40 ? 2014 HOH C O   1 
HETATM 11816 O  O   . HOH OC 9 .   ? 41.365  -39.502 26.787  1.00 28.41 ? 2015 HOH C O   1 
HETATM 11817 O  O   . HOH OC 9 .   ? 44.169  -42.685 25.315  1.00 38.88 ? 2016 HOH C O   1 
HETATM 11818 O  O   . HOH OC 9 .   ? 56.643  -32.737 -3.329  1.00 62.11 ? 2017 HOH C O   1 
HETATM 11819 O  O   . HOH OC 9 .   ? 41.972  -44.344 12.974  1.00 47.84 ? 2018 HOH C O   1 
HETATM 11820 O  O   . HOH OC 9 .   ? 43.945  -46.119 16.521  1.00 41.94 ? 2019 HOH C O   1 
HETATM 11821 O  O   . HOH OC 9 .   ? 46.929  -26.758 -9.364  1.00 59.77 ? 2020 HOH C O   1 
HETATM 11822 O  O   . HOH OC 9 .   ? 46.841  -44.122 21.103  1.00 31.04 ? 2021 HOH C O   1 
HETATM 11823 O  O   . HOH OC 9 .   ? 53.104  -37.997 9.744   1.00 26.84 ? 2022 HOH C O   1 
HETATM 11824 O  O   . HOH OC 9 .   ? 54.495  -35.386 10.486  1.00 69.76 ? 2023 HOH C O   1 
HETATM 11825 O  O   . HOH OC 9 .   ? 43.978  -42.977 13.666  1.00 49.07 ? 2024 HOH C O   1 
HETATM 11826 O  O   . HOH OC 9 .   ? 53.696  -44.507 17.564  1.00 43.43 ? 2025 HOH C O   1 
HETATM 11827 O  O   . HOH OC 9 .   ? 47.311  -42.665 4.880   1.00 43.67 ? 2026 HOH C O   1 
HETATM 11828 O  O   . HOH OC 9 .   ? 45.407  -45.632 6.251   1.00 39.46 ? 2027 HOH C O   1 
HETATM 11829 O  O   . HOH OC 9 .   ? 28.232  -41.106 1.672   1.00 30.49 ? 2028 HOH C O   1 
HETATM 11830 O  O   . HOH OC 9 .   ? 55.502  -38.006 7.328   1.00 32.26 ? 2029 HOH C O   1 
HETATM 11831 O  O   . HOH OC 9 .   ? 56.375  -38.007 3.503   1.00 57.82 ? 2030 HOH C O   1 
HETATM 11832 O  O   . HOH OC 9 .   ? 50.677  -31.829 2.227   1.00 29.75 ? 2031 HOH C O   1 
HETATM 11833 O  O   . HOH OC 9 .   ? 49.155  -35.468 1.513   1.00 25.83 ? 2032 HOH C O   1 
HETATM 11834 O  O   . HOH OC 9 .   ? 49.562  -36.117 -1.132  1.00 30.51 ? 2033 HOH C O   1 
HETATM 11835 O  O   . HOH OC 9 .   ? 54.589  -30.652 -3.067  1.00 37.77 ? 2034 HOH C O   1 
HETATM 11836 O  O   . HOH OC 9 .   ? 53.630  -29.994 -0.342  1.00 42.09 ? 2035 HOH C O   1 
HETATM 11837 O  O   . HOH OC 9 .   ? 50.357  -38.188 -1.749  1.00 46.44 ? 2036 HOH C O   1 
HETATM 11838 O  O   . HOH OC 9 .   ? 25.382  -25.055 14.936  1.00 35.88 ? 2037 HOH C O   1 
HETATM 11839 O  O   . HOH OC 9 .   ? 46.060  -28.728 -7.315  1.00 51.05 ? 2038 HOH C O   1 
HETATM 11840 O  O   . HOH OC 9 .   ? 45.707  -26.334 -3.639  1.00 27.81 ? 2039 HOH C O   1 
HETATM 11841 O  O   . HOH OC 9 .   ? 42.752  -24.640 -3.604  1.00 22.05 ? 2040 HOH C O   1 
HETATM 11842 O  O   . HOH OC 9 .   ? 45.571  -23.156 -0.661  1.00 52.67 ? 2041 HOH C O   1 
HETATM 11843 O  O   . HOH OC 9 .   ? 40.370  -25.902 3.330   1.00 23.84 ? 2042 HOH C O   1 
HETATM 11844 O  O   . HOH OC 9 .   ? 45.606  -23.437 1.630   1.00 35.69 ? 2043 HOH C O   1 
HETATM 11845 O  O   . HOH OC 9 .   ? 23.510  -31.293 -12.108 1.00 35.30 ? 2044 HOH C O   1 
HETATM 11846 O  O   . HOH OC 9 .   ? 40.733  -19.118 6.095   1.00 22.54 ? 2045 HOH C O   1 
HETATM 11847 O  O   . HOH OC 9 .   ? 22.442  -40.882 -5.633  1.00 28.37 ? 2046 HOH C O   1 
HETATM 11848 O  O   . HOH OC 9 .   ? 23.149  -37.612 0.083   1.00 29.46 ? 2047 HOH C O   1 
HETATM 11849 O  O   . HOH OC 9 .   ? 37.415  -20.616 -9.778  1.00 41.90 ? 2048 HOH C O   1 
HETATM 11850 O  O   . HOH OC 9 .   ? 41.676  -21.258 -9.286  1.00 43.48 ? 2049 HOH C O   1 
HETATM 11851 O  O   . HOH OC 9 .   ? 46.786  -25.656 6.527   1.00 38.35 ? 2050 HOH C O   1 
HETATM 11852 O  O   . HOH OC 9 .   ? 18.711  -25.633 -10.055 1.00 22.05 ? 2051 HOH C O   1 
HETATM 11853 O  O   . HOH OC 9 .   ? 30.884  -13.153 3.350   1.00 25.69 ? 2052 HOH C O   1 
HETATM 11854 O  O   . HOH OC 9 .   ? 38.662  -41.223 8.527   1.00 32.51 ? 2053 HOH C O   1 
HETATM 11855 O  O   . HOH OC 9 .   ? 25.492  -17.421 -1.979  1.00 33.15 ? 2054 HOH C O   1 
HETATM 11856 O  O   . HOH OC 9 .   ? 43.389  -39.290 -3.455  1.00 42.14 ? 2055 HOH C O   1 
HETATM 11857 O  O   . HOH OC 9 .   ? 44.397  -40.017 -1.302  1.00 32.94 ? 2056 HOH C O   1 
HETATM 11858 O  O   . HOH OC 9 .   ? 46.579  -41.872 1.639   1.00 41.80 ? 2057 HOH C O   1 
HETATM 11859 O  O   . HOH OC 9 .   ? 31.140  -41.312 1.283   1.00 39.04 ? 2058 HOH C O   1 
HETATM 11860 O  O   . HOH OC 9 .   ? 28.266  -38.254 1.729   1.00 27.90 ? 2059 HOH C O   1 
HETATM 11861 O  O   . HOH OC 9 .   ? 37.090  -43.501 2.539   1.00 38.47 ? 2060 HOH C O   1 
HETATM 11862 O  O   . HOH OC 9 .   ? 33.235  -41.102 12.512  1.00 28.78 ? 2061 HOH C O   1 
HETATM 11863 O  O   . HOH OC 9 .   ? 29.987  -43.669 8.002   1.00 30.79 ? 2062 HOH C O   1 
HETATM 11864 O  O   . HOH OC 9 .   ? 34.111  -42.432 5.542   1.00 37.66 ? 2063 HOH C O   1 
HETATM 11865 O  O   . HOH OC 9 .   ? 41.900  -32.504 18.458  1.00 30.04 ? 2064 HOH C O   1 
HETATM 11866 O  O   . HOH OC 9 .   ? 34.111  -36.954 17.556  1.00 18.74 ? 2065 HOH C O   1 
HETATM 11867 O  O   . HOH OC 9 .   ? 27.613  -32.915 19.086  1.00 30.85 ? 2066 HOH C O   1 
HETATM 11868 O  O   . HOH OC 9 .   ? 27.658  -28.402 18.467  1.00 43.50 ? 2067 HOH C O   1 
HETATM 11869 O  O   . HOH OC 9 .   ? 30.215  -36.391 18.856  1.00 20.60 ? 2068 HOH C O   1 
HETATM 11870 O  O   . HOH OC 9 .   ? 24.010  -34.626 14.132  1.00 30.11 ? 2069 HOH C O   1 
HETATM 11871 O  O   . HOH OC 9 .   ? 26.306  -27.476 15.539  1.00 28.78 ? 2070 HOH C O   1 
HETATM 11872 O  O   . HOH OC 9 .   ? 29.889  -25.613 13.406  1.00 52.20 ? 2071 HOH C O   1 
HETATM 11873 O  O   . HOH OC 9 .   ? 25.954  -37.239 2.797   1.00 19.46 ? 2072 HOH C O   1 
HETATM 11874 O  O   . HOH OC 9 .   ? 41.210  -34.804 29.623  1.00 27.88 ? 2073 HOH C O   1 
HETATM 11875 O  O   . HOH OC 9 .   ? 43.140  -38.600 31.728  1.00 44.72 ? 2074 HOH C O   1 
HETATM 11876 O  O   . HOH OC 9 .   ? 26.107  -26.370 -4.268  1.00 15.01 ? 2075 HOH C O   1 
HETATM 11877 O  O   . HOH OC 9 .   ? 24.683  -34.742 -2.215  1.00 20.42 ? 2076 HOH C O   1 
HETATM 11878 O  O   . HOH OC 9 .   ? 27.165  -24.101 -5.440  1.00 22.92 ? 2077 HOH C O   1 
HETATM 11879 O  O   . HOH OC 9 .   ? 27.681  -21.120 -4.953  1.00 40.28 ? 2078 HOH C O   1 
HETATM 11880 O  O   . HOH OC 9 .   ? 30.153  -21.966 -5.038  1.00 25.71 ? 2079 HOH C O   1 
HETATM 11881 O  O   . HOH OC 9 .   ? 33.224  -28.238 -4.742  1.00 18.16 ? 2080 HOH C O   1 
HETATM 11882 O  O   . HOH OC 9 .   ? 33.251  -21.155 0.572   1.00 21.38 ? 2081 HOH C O   1 
HETATM 11883 O  O   . HOH OC 9 .   ? 48.643  -25.623 0.589   1.00 53.57 ? 2082 HOH C O   1 
HETATM 11884 O  O   . HOH OC 9 .   ? 24.680  -30.830 -9.580  1.00 24.69 ? 2083 HOH C O   1 
HETATM 11885 O  O   . HOH OC 9 .   ? 30.860  -29.792 -10.292 1.00 24.40 ? 2084 HOH C O   1 
HETATM 11886 O  O   . HOH OC 9 .   ? 24.829  -29.331 -7.261  1.00 21.33 ? 2085 HOH C O   1 
HETATM 11887 O  O   . HOH OC 9 .   ? 22.685  -36.807 -4.272  1.00 31.49 ? 2086 HOH C O   1 
HETATM 11888 O  O   . HOH OC 9 .   ? 22.815  -38.415 -6.499  1.00 27.16 ? 2087 HOH C O   1 
HETATM 11889 O  O   . HOH OC 9 .   ? 30.033  -39.643 -4.267  1.00 36.01 ? 2088 HOH C O   1 
HETATM 11890 O  O   . HOH OC 9 .   ? 25.074  -35.973 1.018   1.00 19.65 ? 2089 HOH C O   1 
HETATM 11891 O  O   . HOH OC 9 .   ? 28.311  -40.439 -1.811  1.00 26.80 ? 2090 HOH C O   1 
HETATM 11892 O  O   . HOH OC 9 .   ? 31.183  -22.954 16.559  1.00 45.27 ? 2091 HOH C O   1 
HETATM 11893 O  O   . HOH OC 9 .   ? 41.875  -25.337 -12.518 1.00 41.74 ? 2092 HOH C O   1 
HETATM 11894 O  O   . HOH OC 9 .   ? 38.065  -21.452 -7.463  1.00 26.76 ? 2093 HOH C O   1 
HETATM 11895 O  O   . HOH OC 9 .   ? 37.920  -26.330 -12.694 1.00 50.89 ? 2094 HOH C O   1 
HETATM 11896 O  O   . HOH OC 9 .   ? 39.676  -23.338 -10.298 1.00 32.69 ? 2095 HOH C O   1 
HETATM 11897 O  O   . HOH OC 9 .   ? 33.565  -27.826 -11.089 1.00 39.45 ? 2096 HOH C O   1 
HETATM 11898 O  O   . HOH OC 9 .   ? 34.266  -27.777 -7.458  1.00 25.84 ? 2097 HOH C O   1 
HETATM 11899 O  O   . HOH OC 9 .   ? 33.487  -31.975 -14.814 1.00 30.05 ? 2098 HOH C O   1 
HETATM 11900 O  O   . HOH OC 9 .   ? 32.387  -29.380 -13.681 1.00 49.36 ? 2099 HOH C O   1 
HETATM 11901 O  O   . HOH OC 9 .   ? 31.720  -33.620 -15.553 1.00 29.08 ? 2100 HOH C O   1 
HETATM 11902 O  O   . HOH OC 9 .   ? 25.552  -33.014 -12.016 1.00 33.39 ? 2101 HOH C O   1 
HETATM 11903 O  O   . HOH OC 9 .   ? 30.146  -28.808 -16.113 1.00 31.34 ? 2102 HOH C O   1 
HETATM 11904 O  O   . HOH OC 9 .   ? 29.423  -23.716 -13.163 1.00 39.59 ? 2103 HOH C O   1 
HETATM 11905 O  O   . HOH OC 9 .   ? 26.542  -24.400 -15.538 1.00 47.97 ? 2104 HOH C O   1 
HETATM 11906 O  O   . HOH OC 9 .   ? 26.858  -23.988 -12.219 1.00 38.86 ? 2105 HOH C O   1 
HETATM 11907 O  O   . HOH OC 9 .   ? 20.595  -23.795 -9.929  1.00 29.89 ? 2106 HOH C O   1 
HETATM 11908 O  O   . HOH OC 9 .   ? 18.703  -21.831 -11.687 1.00 45.35 ? 2107 HOH C O   1 
HETATM 11909 O  O   . HOH OC 9 .   ? 22.133  -14.959 -1.493  1.00 29.13 ? 2108 HOH C O   1 
HETATM 11910 O  O   . HOH OC 9 .   ? 25.311  -16.679 -6.847  1.00 38.50 ? 2109 HOH C O   1 
HETATM 11911 O  O   . HOH OC 9 .   ? 14.685  -17.438 -5.431  1.00 42.76 ? 2110 HOH C O   1 
HETATM 11912 O  O   . HOH OC 9 .   ? 31.084  -20.827 -10.988 1.00 52.78 ? 2111 HOH C O   1 
HETATM 11913 O  O   . HOH OC 9 .   ? 27.833  -18.841 -5.416  1.00 39.52 ? 2112 HOH C O   1 
HETATM 11914 O  O   . HOH OC 9 .   ? 35.857  -21.080 -6.139  1.00 26.40 ? 2113 HOH C O   1 
HETATM 11915 O  O   . HOH OC 9 .   ? 36.958  -18.872 -5.837  1.00 28.24 ? 2114 HOH C O   1 
HETATM 11916 O  O   . HOH OC 9 .   ? 40.299  -20.725 -6.067  1.00 30.16 ? 2115 HOH C O   1 
HETATM 11917 O  O   . HOH OC 9 .   ? 11.486  -33.802 3.897   1.00 57.09 ? 2116 HOH C O   1 
HETATM 11918 O  O   . HOH OC 9 .   ? 33.591  -19.824 -9.051  1.00 41.88 ? 2117 HOH C O   1 
HETATM 11919 O  O   . HOH OC 9 .   ? 31.276  -18.035 -9.235  1.00 63.79 ? 2118 HOH C O   1 
HETATM 11920 O  O   . HOH OC 9 .   ? 29.538  -13.551 -2.710  1.00 50.01 ? 2119 HOH C O   1 
HETATM 11921 O  O   . HOH OC 9 .   ? 37.249  -13.120 2.151   1.00 18.00 ? 2120 HOH C O   1 
HETATM 11922 O  O   . HOH OC 9 .   ? 30.873  -11.745 1.386   1.00 64.32 ? 2121 HOH C O   1 
HETATM 11923 O  O   . HOH OC 9 .   ? 33.468  -9.105  1.232   1.00 17.71 ? 2122 HOH C O   1 
HETATM 11924 O  O   . HOH OC 9 .   ? 35.570  -8.928  -1.474  1.00 40.58 ? 2123 HOH C O   1 
HETATM 11925 O  O   . HOH OC 9 .   ? 26.119  -16.238 0.392   1.00 46.13 ? 2124 HOH C O   1 
HETATM 11926 O  O   . HOH OC 9 .   ? 28.228  -12.955 1.145   1.00 30.89 ? 2125 HOH C O   1 
HETATM 11927 O  O   . HOH OC 9 .   ? 30.296  -15.972 3.920   1.00 41.77 ? 2126 HOH C O   1 
HETATM 11928 O  O   . HOH OC 9 .   ? 26.259  -17.900 3.009   1.00 35.47 ? 2127 HOH C O   1 
HETATM 11929 O  O   . HOH OC 9 .   ? 30.498  -17.943 6.807   1.00 40.58 ? 2128 HOH C O   1 
HETATM 11930 O  O   . HOH OC 9 .   ? 8.649   -28.958 12.848  1.00 48.39 ? 2129 HOH C O   1 
HETATM 11931 O  O   . HOH OC 9 .   ? 6.384   -26.613 11.804  1.00 39.13 ? 2130 HOH C O   1 
HETATM 11932 O  O   . HOH OC 9 .   ? 39.702  -17.405 4.103   1.00 17.86 ? 2131 HOH C O   1 
HETATM 11933 O  O   . HOH OC 9 .   ? 39.524  -14.502 4.343   1.00 29.38 ? 2132 HOH C O   1 
HETATM 11934 O  O   . HOH OC 9 .   ? 32.919  -11.736 4.319   1.00 19.61 ? 2133 HOH C O   1 
HETATM 11935 O  O   . HOH OC 9 .   ? 36.876  -9.436  0.851   1.00 26.13 ? 2134 HOH C O   1 
HETATM 11936 O  O   . HOH OC 9 .   ? 40.564  -12.482 5.760   1.00 25.55 ? 2135 HOH C O   1 
HETATM 11937 O  O   . HOH OC 9 .   ? 46.149  -12.179 12.178  1.00 14.28 ? 2136 HOH C O   1 
HETATM 11938 O  O   . HOH OC 9 .   ? 45.185  -15.405 1.972   1.00 29.85 ? 2137 HOH C O   1 
HETATM 11939 O  O   . HOH OC 9 .   ? 42.868  -9.539  5.057   1.00 23.53 ? 2138 HOH C O   1 
HETATM 11940 O  O   . HOH OC 9 .   ? 43.891  -11.855 0.031   1.00 18.60 ? 2139 HOH C O   1 
HETATM 11941 O  O   . HOH OC 9 .   ? 41.683  -7.990  6.714   1.00 26.74 ? 2140 HOH C O   1 
HETATM 11942 O  O   . HOH OC 9 .   ? 42.356  -5.097  -4.685  1.00 42.24 ? 2141 HOH C O   1 
HETATM 11943 O  O   . HOH OC 9 .   ? 40.896  -15.425 -3.787  1.00 31.87 ? 2142 HOH C O   1 
HETATM 11944 O  O   . HOH OC 9 .   ? 43.482  -16.814 -5.929  1.00 48.64 ? 2143 HOH C O   1 
HETATM 11945 O  O   . HOH OC 9 .   ? 45.110  -19.523 -6.586  1.00 50.78 ? 2144 HOH C O   1 
HETATM 11946 O  O   . HOH OC 9 .   ? 48.935  -22.077 2.005   1.00 24.82 ? 2145 HOH C O   1 
HETATM 11947 O  O   . HOH OC 9 .   ? 49.350  -19.760 -4.791  1.00 57.15 ? 2146 HOH C O   1 
HETATM 11948 O  O   . HOH OC 9 .   ? 50.306  -15.437 1.481   1.00 33.90 ? 2147 HOH C O   1 
HETATM 11949 O  O   . HOH OC 9 .   ? 53.105  -15.464 2.927   1.00 35.16 ? 2148 HOH C O   1 
HETATM 11950 O  O   . HOH OC 9 .   ? 56.694  -18.256 5.534   1.00 32.16 ? 2149 HOH C O   1 
HETATM 11951 O  O   . HOH OC 9 .   ? 52.524  -9.299  11.222  1.00 39.86 ? 2150 HOH C O   1 
HETATM 11952 O  O   . HOH OC 9 .   ? 50.912  -7.123  15.393  1.00 35.24 ? 2151 HOH C O   1 
HETATM 11953 O  O   . HOH OC 9 .   ? 46.372  -2.882  18.146  1.00 38.06 ? 2152 HOH C O   1 
HETATM 11954 O  O   . HOH OC 9 .   ? 50.098  -12.508 27.747  1.00 33.69 ? 2153 HOH C O   1 
HETATM 11955 O  O   . HOH OC 9 .   ? 54.444  -13.341 26.261  1.00 29.49 ? 2154 HOH C O   1 
HETATM 11956 O  O   . HOH OC 9 .   ? 55.960  -14.420 24.784  1.00 41.49 ? 2155 HOH C O   1 
HETATM 11957 O  O   . HOH OC 9 .   ? 44.524  -2.861  22.061  1.00 43.34 ? 2156 HOH C O   1 
HETATM 11958 O  O   . HOH OC 9 .   ? 47.173  -1.655  20.295  1.00 52.36 ? 2157 HOH C O   1 
HETATM 11959 O  O   . HOH OC 9 .   ? 48.030  -4.794  25.743  1.00 40.41 ? 2158 HOH C O   1 
HETATM 11960 O  O   . HOH OC 9 .   ? 45.752  -11.532 28.570  1.00 39.49 ? 2159 HOH C O   1 
HETATM 11961 O  O   . HOH OC 9 .   ? 39.720  -11.479 24.850  1.00 17.80 ? 2160 HOH C O   1 
HETATM 11962 O  O   . HOH OC 9 .   ? 36.056  -10.669 19.828  1.00 16.41 ? 2161 HOH C O   1 
HETATM 11963 O  O   . HOH OC 9 .   ? 41.900  -6.439  20.050  1.00 28.77 ? 2162 HOH C O   1 
HETATM 11964 O  O   . HOH OC 9 .   ? 37.927  -17.051 10.764  1.00 17.87 ? 2163 HOH C O   1 
HETATM 11965 O  O   . HOH OC 9 .   ? 48.537  -2.717  13.534  1.00 37.98 ? 2164 HOH C O   1 
HETATM 11966 O  O   . HOH OC 9 .   ? 39.066  -0.096  11.517  1.00 40.04 ? 2165 HOH C O   1 
HETATM 11967 O  O   . HOH OC 9 .   ? 42.906  -2.168  15.463  1.00 37.56 ? 2166 HOH C O   1 
HETATM 11968 O  O   . HOH OC 9 .   ? 41.202  -0.663  19.187  1.00 64.12 ? 2167 HOH C O   1 
HETATM 11969 O  O   . HOH OC 9 .   ? 30.689  -4.420  1.592   1.00 29.25 ? 2168 HOH C O   1 
HETATM 11970 O  O   . HOH OC 9 .   ? 29.304  -11.516 5.192   1.00 16.72 ? 2169 HOH C O   1 
HETATM 11971 O  O   . HOH OC 9 .   ? 26.164  -9.587  2.043   1.00 39.53 ? 2170 HOH C O   1 
HETATM 11972 O  O   . HOH OC 9 .   ? 24.774  -14.655 12.199  1.00 23.03 ? 2171 HOH C O   1 
HETATM 11973 O  O   . HOH OC 9 .   ? 24.393  -12.374 3.800   1.00 38.35 ? 2172 HOH C O   1 
HETATM 11974 O  O   . HOH OC 9 .   ? 21.582  -9.473  5.415   1.00 41.84 ? 2173 HOH C O   1 
HETATM 11975 O  O   . HOH OC 9 .   ? 25.111  -15.867 4.553   1.00 26.58 ? 2174 HOH C O   1 
HETATM 11976 O  O   . HOH OC 9 .   ? 30.719  -9.748  19.146  1.00 20.81 ? 2175 HOH C O   1 
HETATM 11977 O  O   . HOH OC 9 .   ? 34.492  -8.998  18.025  1.00 21.35 ? 2176 HOH C O   1 
HETATM 11978 O  O   . HOH OC 9 .   ? 42.256  -27.752 24.899  1.00 25.82 ? 2177 HOH C O   1 
HETATM 11979 O  O   . HOH OC 9 .   ? 49.294  -28.778 20.547  1.00 23.83 ? 2178 HOH C O   1 
HETATM 11980 O  O   . HOH OC 9 .   ? 42.805  -31.246 23.439  1.00 35.43 ? 2179 HOH C O   1 
HETATM 11981 O  O   . HOH OC 9 .   ? 51.416  -33.199 20.090  1.00 30.83 ? 2180 HOH C O   1 
HETATM 11982 O  O   . HOH OC 9 .   ? 43.494  -35.296 28.357  1.00 39.62 ? 2181 HOH C O   1 
HETATM 11983 O  O   . HOH OC 9 .   ? 47.437  -37.084 30.414  1.00 38.42 ? 2182 HOH C O   1 
HETATM 11984 O  O   . HOH OC 9 .   ? 54.824  -36.664 22.793  1.00 41.96 ? 2183 HOH C O   1 
HETATM 11985 O  O   . HOH OC 9 .   ? 51.570  -40.704 25.405  1.00 36.44 ? 2184 HOH C O   1 
HETATM 11986 O  O   . HOH OC 9 .   ? 46.983  -31.427 31.261  1.00 42.43 ? 2185 HOH C O   1 
HETATM 11987 O  O   . HOH OC 9 .   ? 50.516  -25.456 28.179  1.00 30.92 ? 2186 HOH C O   1 
HETATM 11988 O  O   . HOH OC 9 .   ? 50.618  -26.765 21.685  1.00 24.42 ? 2187 HOH C O   1 
HETATM 11989 O  O   . HOH OC 9 .   ? 52.188  -31.792 24.158  1.00 37.85 ? 2188 HOH C O   1 
HETATM 11990 O  O   . HOH OC 9 .   ? 48.412  -26.867 31.855  1.00 47.12 ? 2189 HOH C O   1 
HETATM 11991 O  O   . HOH OC 9 .   ? 55.933  -25.139 13.345  1.00 37.87 ? 2190 HOH C O   1 
HETATM 11992 O  O   . HOH OC 9 .   ? 57.163  -27.750 13.403  1.00 47.65 ? 2191 HOH C O   1 
HETATM 11993 O  O   . HOH OC 9 .   ? 57.927  -28.001 18.329  1.00 46.66 ? 2192 HOH C O   1 
HETATM 11994 O  O   . HOH OC 9 .   ? 57.465  -25.661 19.967  1.00 49.21 ? 2193 HOH C O   1 
HETATM 11995 O  O   . HOH OC 9 .   ? 55.896  -29.547 11.375  1.00 41.90 ? 2194 HOH C O   1 
HETATM 11996 O  O   . HOH OC 9 .   ? 51.501  -22.962 3.074   1.00 26.69 ? 2195 HOH C O   1 
HETATM 11997 O  O   . HOH OC 9 .   ? 53.295  -20.993 3.335   1.00 26.42 ? 2196 HOH C O   1 
HETATM 11998 O  O   . HOH OC 9 .   ? 51.211  -29.132 3.108   1.00 30.93 ? 2197 HOH C O   1 
HETATM 11999 O  O   . HOH OC 9 .   ? 48.901  -27.713 2.590   1.00 36.80 ? 2198 HOH C O   1 
HETATM 12000 O  O   . HOH OC 9 .   ? 56.643  -32.774 7.975   1.00 52.71 ? 2199 HOH C O   1 
HETATM 12001 O  O   . HOH OC 9 .   ? 58.117  -32.217 9.985   1.00 53.84 ? 2200 HOH C O   1 
HETATM 12002 O  O   . HOH OC 9 .   ? 56.971  -28.634 5.675   1.00 43.49 ? 2201 HOH C O   1 
HETATM 12003 O  O   . HOH OC 9 .   ? 55.811  -27.459 10.387  1.00 43.19 ? 2202 HOH C O   1 
HETATM 12004 O  O   . HOH OC 9 .   ? 56.069  -31.744 15.785  1.00 53.19 ? 2203 HOH C O   1 
HETATM 12005 O  O   . HOH OC 9 .   ? 56.486  -35.343 11.891  1.00 57.08 ? 2204 HOH C O   1 
HETATM 12006 O  O   . HOH OC 9 .   ? 60.457  -32.590 12.861  1.00 49.17 ? 2205 HOH C O   1 
HETATM 12007 O  O   . HOH OC 9 .   ? 59.713  -34.366 17.632  1.00 46.74 ? 2206 HOH C O   1 
HETATM 12008 O  O   . HOH OC 9 .   ? 52.283  -42.519 21.361  1.00 40.28 ? 2207 HOH C O   1 
HETATM 12009 O  O   . HOH OC 9 .   ? 39.033  -38.788 27.749  1.00 29.35 ? 2208 HOH C O   1 
HETATM 12010 O  O   . HOH OC 9 .   ? 37.154  -33.454 28.254  1.00 33.82 ? 2209 HOH C O   1 
HETATM 12011 O  O   . HOH OC 9 .   ? 30.862  -31.065 22.452  1.00 41.26 ? 2210 HOH C O   1 
HETATM 12012 O  O   . HOH OC 9 .   ? 36.930  -27.585 25.126  1.00 37.35 ? 2211 HOH C O   1 
HETATM 12013 O  O   . HOH OC 9 .   ? 32.005  -27.884 21.673  1.00 35.68 ? 2212 HOH C O   1 
HETATM 12014 O  O   . HOH OC 9 .   ? 30.047  -25.619 16.802  1.00 43.38 ? 2213 HOH C O   1 
HETATM 12015 O  O   . HOH OC 9 .   ? 29.905  -25.996 20.331  1.00 53.99 ? 2214 HOH C O   1 
HETATM 12016 O  O   . HOH OC 9 .   ? 30.385  -22.184 25.050  1.00 34.32 ? 2215 HOH C O   1 
HETATM 12017 O  O   . HOH OC 9 .   ? 32.020  -22.768 28.161  1.00 42.90 ? 2216 HOH C O   1 
HETATM 12018 O  O   . HOH OC 9 .   ? 33.395  -20.255 29.059  1.00 50.16 ? 2217 HOH C O   1 
HETATM 12019 O  O   . HOH OC 9 .   ? 30.565  -7.790  27.011  1.00 39.99 ? 2218 HOH C O   1 
HETATM 12020 O  O   . HOH OC 9 .   ? 27.979  -3.826  20.005  1.00 38.26 ? 2219 HOH C O   1 
HETATM 12021 O  O   . HOH OC 9 .   ? 28.026  -10.056 18.983  1.00 32.85 ? 2220 HOH C O   1 
HETATM 12022 O  O   . HOH OC 9 .   ? 29.539  -3.308  16.282  1.00 21.70 ? 2221 HOH C O   1 
HETATM 12023 O  O   . HOH OC 9 .   ? 22.613  -0.329  15.513  1.00 28.62 ? 2222 HOH C O   1 
HETATM 12024 O  O   . HOH OC 9 .   ? 22.331  -5.118  15.088  1.00 42.54 ? 2223 HOH C O   1 
HETATM 12025 O  O   . HOH OC 9 .   ? 21.734  -0.641  6.996   1.00 48.59 ? 2224 HOH C O   1 
HETATM 12026 O  O   . HOH OC 9 .   ? 24.324  0.146   1.402   1.00 50.00 ? 2225 HOH C O   1 
HETATM 12027 O  O   . HOH OC 9 .   ? 33.767  2.702   9.926   1.00 24.08 ? 2226 HOH C O   1 
HETATM 12028 O  O   . HOH OC 9 .   ? 36.102  3.360   10.484  1.00 46.00 ? 2227 HOH C O   1 
HETATM 12029 O  O   . HOH OC 9 .   ? 26.011  3.617   5.106   1.00 36.77 ? 2228 HOH C O   1 
HETATM 12030 O  O   . HOH OC 9 .   ? 21.400  -7.358  13.447  1.00 44.49 ? 2229 HOH C O   1 
HETATM 12031 O  O   . HOH OC 9 .   ? 23.541  -17.271 15.244  1.00 20.10 ? 2230 HOH C O   1 
HETATM 12032 O  O   . HOH OC 9 .   ? 25.753  -15.463 14.791  1.00 28.87 ? 2231 HOH C O   1 
HETATM 12033 O  O   . HOH OC 9 .   ? 25.589  -11.292 18.471  1.00 29.25 ? 2232 HOH C O   1 
HETATM 12034 O  O   . HOH OC 9 .   ? 23.726  -18.482 17.879  1.00 24.75 ? 2233 HOH C O   1 
HETATM 12035 O  O   . HOH OC 9 .   ? 16.776  -14.789 21.255  1.00 41.65 ? 2234 HOH C O   1 
HETATM 12036 O  O   . HOH OC 9 .   ? 22.219  -17.105 7.638   1.00 22.59 ? 2235 HOH C O   1 
HETATM 12037 O  O   . HOH OC 9 .   ? 16.975  -27.491 6.205   1.00 12.92 ? 2236 HOH C O   1 
HETATM 12038 O  O   . HOH OC 9 .   ? 12.062  -18.404 6.248   1.00 46.08 ? 2237 HOH C O   1 
HETATM 12039 O  O   . HOH OC 9 .   ? 13.633  -22.089 12.367  1.00 21.59 ? 2238 HOH C O   1 
HETATM 12040 O  O   . HOH OC 9 .   ? 9.806   -20.666 11.101  1.00 35.71 ? 2239 HOH C O   1 
HETATM 12041 O  O   . HOH OC 9 .   ? 12.652  -19.712 0.007   1.00 28.57 ? 2240 HOH C O   1 
HETATM 12042 O  O   . HOH OC 9 .   ? 22.808  -17.688 -2.552  1.00 36.44 ? 2241 HOH C O   1 
HETATM 12043 O  O   . HOH OC 9 .   ? 22.829  -15.376 0.927   1.00 36.76 ? 2242 HOH C O   1 
HETATM 12044 O  O   . HOH OC 9 .   ? 22.718  -16.750 4.887   1.00 22.31 ? 2243 HOH C O   1 
HETATM 12045 O  O   . HOH OC 9 .   ? 12.454  -17.393 -3.450  1.00 41.47 ? 2244 HOH C O   1 
HETATM 12046 O  O   . HOH OC 9 .   ? 18.604  -16.965 -7.665  1.00 31.51 ? 2245 HOH C O   1 
HETATM 12047 O  O   . HOH OC 9 .   ? 22.580  -16.793 -5.135  1.00 43.92 ? 2246 HOH C O   1 
HETATM 12048 O  O   . HOH OC 9 .   ? 20.047  -13.924 -2.673  1.00 35.69 ? 2247 HOH C O   1 
HETATM 12049 O  O   . HOH OC 9 .   ? 17.170  -23.681 -10.426 1.00 23.41 ? 2248 HOH C O   1 
HETATM 12050 O  O   . HOH OC 9 .   ? 11.218  -23.895 -6.560  1.00 26.89 ? 2249 HOH C O   1 
HETATM 12051 O  O   . HOH OC 9 .   ? 11.224  -27.069 -8.138  1.00 40.46 ? 2250 HOH C O   1 
HETATM 12052 O  O   . HOH OC 9 .   ? 17.757  -27.537 -11.722 1.00 27.07 ? 2251 HOH C O   1 
HETATM 12053 O  O   . HOH OC 9 .   ? 19.129  -31.975 -12.633 1.00 34.18 ? 2252 HOH C O   1 
HETATM 12054 O  O   . HOH OC 9 .   ? 19.401  -29.633 -12.985 1.00 45.84 ? 2253 HOH C O   1 
HETATM 12055 O  O   . HOH OC 9 .   ? 15.301  -34.935 -12.679 1.00 42.58 ? 2254 HOH C O   1 
HETATM 12056 O  O   . HOH OC 9 .   ? 18.638  -36.810 -6.446  1.00 23.61 ? 2255 HOH C O   1 
HETATM 12057 O  O   . HOH OC 9 .   ? 18.859  -39.170 -13.137 1.00 36.31 ? 2256 HOH C O   1 
HETATM 12058 O  O   . HOH OC 9 .   ? 21.010  -34.013 -12.164 1.00 39.67 ? 2257 HOH C O   1 
HETATM 12059 O  O   . HOH OC 9 .   ? 20.756  -37.655 -7.799  1.00 28.83 ? 2258 HOH C O   1 
HETATM 12060 O  O   . HOH OC 9 .   ? 7.438   -34.646 -2.988  1.00 61.97 ? 2259 HOH C O   1 
HETATM 12061 O  O   . HOH OC 9 .   ? 12.389  -34.911 -1.839  1.00 30.96 ? 2260 HOH C O   1 
HETATM 12062 O  O   . HOH OC 9 .   ? 14.804  -35.827 -0.723  1.00 34.04 ? 2261 HOH C O   1 
HETATM 12063 O  O   . HOH OC 9 .   ? 13.920  -35.131 2.056   1.00 45.43 ? 2262 HOH C O   1 
HETATM 12064 O  O   . HOH OC 9 .   ? 14.491  -30.682 3.119   1.00 22.14 ? 2263 HOH C O   1 
HETATM 12065 O  O   . HOH OC 9 .   ? 12.031  -28.222 0.921   1.00 21.21 ? 2264 HOH C O   1 
HETATM 12066 O  O   . HOH OC 9 .   ? 16.242  -38.112 1.749   1.00 51.73 ? 2265 HOH C O   1 
HETATM 12067 O  O   . HOH OC 9 .   ? 16.561  -33.776 9.503   1.00 35.42 ? 2266 HOH C O   1 
HETATM 12068 O  O   . HOH OC 9 .   ? 12.291  -32.220 2.691   1.00 51.67 ? 2267 HOH C O   1 
HETATM 12069 O  O   . HOH OC 9 .   ? 12.374  -36.617 5.437   1.00 48.54 ? 2268 HOH C O   1 
HETATM 12070 O  O   . HOH OC 9 .   ? 16.815  -37.198 4.271   1.00 60.01 ? 2269 HOH C O   1 
HETATM 12071 O  O   . HOH OC 9 .   ? 17.738  -28.818 14.627  1.00 25.82 ? 2270 HOH C O   1 
HETATM 12072 O  O   . HOH OC 9 .   ? 22.599  -36.088 12.187  1.00 26.97 ? 2271 HOH C O   1 
HETATM 12073 O  O   . HOH OC 9 .   ? 23.495  -23.495 19.834  1.00 45.21 ? 2272 HOH C O   1 
HETATM 12074 O  O   . HOH OC 9 .   ? 10.482  -26.964 16.701  1.00 41.60 ? 2273 HOH C O   1 
HETATM 12075 O  O   . HOH OC 9 .   ? 11.296  -29.190 12.655  1.00 28.83 ? 2274 HOH C O   1 
HETATM 12076 O  O   . HOH OC 9 .   ? 8.859   -24.193 8.436   1.00 35.49 ? 2275 HOH C O   1 
HETATM 12077 O  O   . HOH OC 9 .   ? 8.833   -27.510 10.441  1.00 27.98 ? 2276 HOH C O   1 
HETATM 12078 O  O   . HOH OC 9 .   ? 14.457  -33.843 8.511   1.00 51.88 ? 2277 HOH C O   1 
HETATM 12079 O  O   . HOH OC 9 .   ? 12.033  -31.187 11.497  1.00 23.89 ? 2278 HOH C O   1 
HETATM 12080 O  O   . HOH OC 9 .   ? 14.754  -28.354 5.175   1.00 22.82 ? 2279 HOH C O   1 
HETATM 12081 O  O   . HOH OC 9 .   ? 8.929   -23.921 5.638   1.00 31.15 ? 2280 HOH C O   1 
HETATM 12082 O  O   . HOH OC 9 .   ? 9.728   -27.199 -5.468  1.00 40.20 ? 2281 HOH C O   1 
HETATM 12083 O  O   . HOH OC 9 .   ? 4.774   -28.671 1.839   1.00 46.72 ? 2282 HOH C O   1 
HETATM 12084 O  O   . HOH OC 9 .   ? 11.261  -35.744 2.234   1.00 58.20 ? 2283 HOH C O   1 
HETATM 12085 O  O   . HOH OC 9 .   ? 52.621  -6.534  -2.792  1.00 47.26 ? 2284 HOH C O   1 
HETATM 12086 O  O   . HOH OC 9 .   ? 36.715  -2.921  -7.050  1.00 46.59 ? 2285 HOH C O   1 
HETATM 12087 O  O   . HOH OC 9 .   ? 36.290  -10.083 -4.117  1.00 36.30 ? 2286 HOH C O   1 
HETATM 12088 O  O   . HOH OC 9 .   ? 4.231   -21.218 3.634   1.00 45.72 ? 2287 HOH C O   1 
HETATM 12089 O  O   . HOH OC 9 .   ? 45.566  -45.460 21.421  1.00 55.31 ? 2288 HOH C O   1 
HETATM 12090 O  O   . HOH OC 9 .   ? 30.976  -23.268 13.354  1.00 51.12 ? 2289 HOH C O   1 
HETATM 12091 O  O   . HOH OC 9 .   ? 47.179  -21.028 -8.473  1.00 55.02 ? 2290 HOH C O   1 
HETATM 12092 O  O   . HOH OC 9 .   ? 54.889  -12.922 -0.287  1.00 57.38 ? 2291 HOH C O   1 
HETATM 12093 O  O   . HOH PC 9 .   ? -21.835 -36.066 64.401  1.00 35.75 ? 2001 HOH D O   1 
HETATM 12094 O  O   . HOH PC 9 .   ? -18.110 -38.742 63.202  1.00 49.33 ? 2002 HOH D O   1 
HETATM 12095 O  O   . HOH PC 9 .   ? -21.755 -38.771 57.440  1.00 45.68 ? 2003 HOH D O   1 
HETATM 12096 O  O   . HOH PC 9 .   ? -24.931 -39.304 60.246  1.00 52.38 ? 2004 HOH D O   1 
HETATM 12097 O  O   . HOH PC 9 .   ? -19.639 -35.830 66.104  1.00 31.89 ? 2005 HOH D O   1 
HETATM 12098 O  O   . HOH PC 9 .   ? -24.093 -40.390 54.822  1.00 44.21 ? 2006 HOH D O   1 
HETATM 12099 O  O   . HOH PC 9 .   ? -27.646 -39.592 53.580  1.00 38.18 ? 2007 HOH D O   1 
HETATM 12100 O  O   . HOH PC 9 .   ? -24.385 -40.212 48.913  1.00 34.50 ? 2008 HOH D O   1 
HETATM 12101 O  O   . HOH PC 9 .   ? -28.554 -36.532 46.749  1.00 28.21 ? 2009 HOH D O   1 
HETATM 12102 O  O   . HOH PC 9 .   ? -29.065 -34.953 48.811  1.00 21.32 ? 2010 HOH D O   1 
HETATM 12103 O  O   . HOH PC 9 .   ? -35.792 -41.459 46.447  1.00 58.22 ? 2011 HOH D O   1 
HETATM 12104 O  O   . HOH PC 9 .   ? -34.530 -40.255 49.677  1.00 39.42 ? 2012 HOH D O   1 
HETATM 12105 O  O   . HOH PC 9 .   ? -32.433 -36.057 41.626  1.00 17.38 ? 2013 HOH D O   1 
HETATM 12106 O  O   . HOH PC 9 .   ? -30.170 -34.730 41.268  1.00 36.43 ? 2014 HOH D O   1 
HETATM 12107 O  O   . HOH PC 9 .   ? -37.741 -37.494 40.395  1.00 28.54 ? 2015 HOH D O   1 
HETATM 12108 O  O   . HOH PC 9 .   ? -39.680 -44.156 50.523  1.00 51.01 ? 2016 HOH D O   1 
HETATM 12109 O  O   . HOH PC 9 .   ? -47.655 -43.289 61.168  1.00 51.33 ? 2017 HOH D O   1 
HETATM 12110 O  O   . HOH PC 9 .   ? -30.131 -39.821 63.685  1.00 44.72 ? 2018 HOH D O   1 
HETATM 12111 O  O   . HOH PC 9 .   ? -26.097 -38.079 65.968  1.00 43.00 ? 2019 HOH D O   1 
HETATM 12112 O  O   . HOH PC 9 .   ? -33.188 -41.135 63.687  1.00 45.26 ? 2020 HOH D O   1 
HETATM 12113 O  O   . HOH PC 9 .   ? -46.611 -33.776 65.203  1.00 36.49 ? 2021 HOH D O   1 
HETATM 12114 O  O   . HOH PC 9 .   ? -48.476 -30.366 64.583  1.00 35.63 ? 2022 HOH D O   1 
HETATM 12115 O  O   . HOH PC 9 .   ? -47.428 -33.937 68.052  1.00 47.39 ? 2023 HOH D O   1 
HETATM 12116 O  O   . HOH PC 9 .   ? -46.630 -28.581 72.377  1.00 52.50 ? 2024 HOH D O   1 
HETATM 12117 O  O   . HOH PC 9 .   ? -45.007 -40.550 72.464  1.00 53.81 ? 2025 HOH D O   1 
HETATM 12118 O  O   . HOH PC 9 .   ? -41.301 -22.466 70.655  1.00 37.23 ? 2026 HOH D O   1 
HETATM 12119 O  O   . HOH PC 9 .   ? -38.840 -23.778 63.604  1.00 30.66 ? 2027 HOH D O   1 
HETATM 12120 O  O   . HOH PC 9 .   ? -44.152 -21.384 64.735  1.00 41.24 ? 2028 HOH D O   1 
HETATM 12121 O  O   . HOH PC 9 .   ? -39.675 -16.871 60.755  1.00 36.31 ? 2029 HOH D O   1 
HETATM 12122 O  O   . HOH PC 9 .   ? -44.771 -24.040 60.211  1.00 42.50 ? 2030 HOH D O   1 
HETATM 12123 O  O   . HOH PC 9 .   ? -17.575 -21.329 77.646  1.00 42.27 ? 2031 HOH D O   1 
HETATM 12124 O  O   . HOH PC 9 .   ? -41.306 -19.233 73.613  1.00 58.94 ? 2032 HOH D O   1 
HETATM 12125 O  O   . HOH PC 9 .   ? -35.185 -6.083  68.555  1.00 37.89 ? 2033 HOH D O   1 
HETATM 12126 O  O   . HOH PC 9 .   ? -32.335 -6.055  69.057  1.00 41.05 ? 2034 HOH D O   1 
HETATM 12127 O  O   . HOH PC 9 .   ? -33.969 -37.130 61.105  1.00 41.44 ? 2035 HOH D O   1 
HETATM 12128 O  O   . HOH PC 9 .   ? -30.377 -9.685  63.567  1.00 39.60 ? 2036 HOH D O   1 
HETATM 12129 O  O   . HOH PC 9 .   ? -43.963 -41.044 65.544  1.00 49.41 ? 2037 HOH D O   1 
HETATM 12130 O  O   . HOH PC 9 .   ? -44.550 -40.731 62.793  1.00 46.18 ? 2038 HOH D O   1 
HETATM 12131 O  O   . HOH PC 9 .   ? -28.587 -38.104 65.992  1.00 33.55 ? 2039 HOH D O   1 
HETATM 12132 O  O   . HOH PC 9 .   ? -25.829 -35.132 65.529  1.00 33.95 ? 2040 HOH D O   1 
HETATM 12133 O  O   . HOH PC 9 .   ? -34.930 -38.889 63.982  1.00 40.50 ? 2041 HOH D O   1 
HETATM 12134 O  O   . HOH PC 9 .   ? -30.444 -37.977 54.703  1.00 40.14 ? 2042 HOH D O   1 
HETATM 12135 O  O   . HOH PC 9 .   ? -31.640 -39.181 61.759  1.00 36.96 ? 2043 HOH D O   1 
HETATM 12136 O  O   . HOH PC 9 .   ? -39.285 -30.196 48.567  1.00 28.61 ? 2044 HOH D O   1 
HETATM 12137 O  O   . HOH PC 9 .   ? -31.117 -33.811 49.645  1.00 30.13 ? 2045 HOH D O   1 
HETATM 12138 O  O   . HOH PC 9 .   ? -24.975 -29.363 48.228  1.00 26.41 ? 2046 HOH D O   1 
HETATM 12139 O  O   . HOH PC 9 .   ? -25.473 -25.387 48.481  1.00 48.14 ? 2047 HOH D O   1 
HETATM 12140 O  O   . HOH PC 9 .   ? -28.397 -3.297  65.510  1.00 49.13 ? 2048 HOH D O   1 
HETATM 12141 O  O   . HOH PC 9 .   ? -27.441 -32.737 48.403  1.00 33.08 ? 2049 HOH D O   1 
HETATM 12142 O  O   . HOH PC 9 .   ? -21.510 -30.534 53.511  1.00 29.43 ? 2050 HOH D O   1 
HETATM 12143 O  O   . HOH PC 9 .   ? -23.266 -33.838 64.406  1.00 30.10 ? 2051 HOH D O   1 
HETATM 12144 O  O   . HOH PC 9 .   ? -24.695 -22.752 71.643  1.00 30.14 ? 2052 HOH D O   1 
HETATM 12145 O  O   . HOH PC 9 .   ? -22.534 -30.587 69.803  1.00 37.18 ? 2053 HOH D O   1 
HETATM 12146 O  O   . HOH PC 9 .   ? -25.823 -20.438 72.686  1.00 29.06 ? 2054 HOH D O   1 
HETATM 12147 O  O   . HOH PC 9 .   ? -31.727 -25.122 71.935  1.00 21.64 ? 2055 HOH D O   1 
HETATM 12148 O  O   . HOH PC 9 .   ? -32.243 -17.849 66.482  1.00 25.19 ? 2056 HOH D O   1 
HETATM 12149 O  O   . HOH PC 9 .   ? -28.962 -26.618 77.218  1.00 37.50 ? 2057 HOH D O   1 
HETATM 12150 O  O   . HOH PC 9 .   ? -23.303 -25.518 74.540  1.00 33.51 ? 2058 HOH D O   1 
HETATM 12151 O  O   . HOH PC 9 .   ? -20.374 -35.596 73.627  1.00 36.86 ? 2059 HOH D O   1 
HETATM 12152 O  O   . HOH PC 9 .   ? -27.736 -36.592 71.925  1.00 41.49 ? 2060 HOH D O   1 
HETATM 12153 O  O   . HOH PC 9 .   ? -22.604 -32.202 66.436  1.00 21.81 ? 2061 HOH D O   1 
HETATM 12154 O  O   . HOH PC 9 .   ? -32.552 -26.837 41.747  1.00 36.00 ? 2062 HOH D O   1 
HETATM 12155 O  O   . HOH PC 9 .   ? -28.460 -22.094 54.002  1.00 43.23 ? 2063 HOH D O   1 
HETATM 12156 O  O   . HOH PC 9 .   ? -39.528 -28.089 76.934  1.00 57.52 ? 2064 HOH D O   1 
HETATM 12157 O  O   . HOH PC 9 .   ? -37.152 -19.272 74.271  1.00 32.87 ? 2065 HOH D O   1 
HETATM 12158 O  O   . HOH PC 9 .   ? -31.799 -24.456 77.750  1.00 26.19 ? 2066 HOH D O   1 
HETATM 12159 O  O   . HOH PC 9 .   ? -32.705 -24.885 74.551  1.00 33.54 ? 2067 HOH D O   1 
HETATM 12160 O  O   . HOH PC 9 .   ? -32.697 -32.110 80.423  1.00 54.45 ? 2068 HOH D O   1 
HETATM 12161 O  O   . HOH PC 9 .   ? -21.026 3.738   55.904  1.00 34.36 ? 2069 HOH D O   1 
HETATM 12162 O  O   . HOH PC 9 .   ? -28.997 -25.115 83.237  1.00 47.73 ? 2070 HOH D O   1 
HETATM 12163 O  O   . HOH PC 9 .   ? -31.747 -24.887 80.620  1.00 39.30 ? 2071 HOH D O   1 
HETATM 12164 O  O   . HOH PC 9 .   ? -19.770 -19.512 77.321  1.00 37.69 ? 2072 HOH D O   1 
HETATM 12165 O  O   . HOH PC 9 .   ? -34.659 -18.155 72.801  1.00 35.98 ? 2073 HOH D O   1 
HETATM 12166 O  O   . HOH PC 9 .   ? -39.278 -18.259 72.836  1.00 28.77 ? 2074 HOH D O   1 
HETATM 12167 O  O   . HOH PC 9 .   ? -32.790 -16.906 75.809  1.00 39.53 ? 2075 HOH D O   1 
HETATM 12168 O  O   . HOH PC 9 .   ? -32.543 -12.325 72.330  1.00 63.69 ? 2076 HOH D O   1 
HETATM 12169 O  O   . HOH PC 9 .   ? -36.735 -10.768 64.631  1.00 24.61 ? 2077 HOH D O   1 
HETATM 12170 O  O   . HOH PC 9 .   ? -33.414 -6.326  65.795  1.00 30.40 ? 2078 HOH D O   1 
HETATM 12171 O  O   . HOH PC 9 .   ? -28.675 -13.351 62.617  1.00 32.34 ? 2079 HOH D O   1 
HETATM 12172 O  O   . HOH PC 9 .   ? -5.665  -24.420 58.242  1.00 48.83 ? 2080 HOH D O   1 
HETATM 12173 O  O   . HOH PC 9 .   ? -3.268  -23.821 57.127  1.00 55.98 ? 2081 HOH D O   1 
HETATM 12174 O  O   . HOH PC 9 .   ? -4.287  -22.498 61.171  1.00 56.65 ? 2082 HOH D O   1 
HETATM 12175 O  O   . HOH PC 9 .   ? -38.832 -14.998 62.557  1.00 22.80 ? 2083 HOH D O   1 
HETATM 12176 O  O   . HOH PC 9 .   ? -38.921 -12.442 62.632  1.00 25.30 ? 2084 HOH D O   1 
HETATM 12177 O  O   . HOH PC 9 .   ? -32.962 -8.999  62.672  1.00 37.00 ? 2085 HOH D O   1 
HETATM 12178 O  O   . HOH PC 9 .   ? -36.784 -6.904  66.213  1.00 28.11 ? 2086 HOH D O   1 
HETATM 12179 O  O   . HOH PC 9 .   ? -40.279 -10.356 61.242  1.00 34.23 ? 2087 HOH D O   1 
HETATM 12180 O  O   . HOH PC 9 .   ? -45.624 -10.546 54.669  1.00 20.27 ? 2088 HOH D O   1 
HETATM 12181 O  O   . HOH PC 9 .   ? -45.045 -13.773 64.887  1.00 36.64 ? 2089 HOH D O   1 
HETATM 12182 O  O   . HOH PC 9 .   ? -42.669 -7.501  61.688  1.00 31.96 ? 2090 HOH D O   1 
HETATM 12183 O  O   . HOH PC 9 .   ? -46.622 -11.221 71.150  1.00 46.51 ? 2091 HOH D O   1 
HETATM 12184 O  O   . HOH PC 9 .   ? -42.788 -11.978 75.133  1.00 44.95 ? 2092 HOH D O   1 
HETATM 12185 O  O   . HOH PC 9 .   ? -46.579 -11.875 65.041  1.00 39.31 ? 2093 HOH D O   1 
HETATM 12186 O  O   . HOH PC 9 .   ? -52.251 -7.837  55.478  1.00 35.75 ? 2094 HOH D O   1 
HETATM 12187 O  O   . HOH PC 9 .   ? -54.937 -8.900  56.746  1.00 48.54 ? 2095 HOH D O   1 
HETATM 12188 O  O   . HOH PC 9 .   ? -47.164 -2.265  48.847  1.00 51.81 ? 2096 HOH D O   1 
HETATM 12189 O  O   . HOH PC 9 .   ? -56.944 -13.531 46.501  1.00 38.73 ? 2097 HOH D O   1 
HETATM 12190 O  O   . HOH PC 9 .   ? -45.023 -10.259 37.957  1.00 41.37 ? 2098 HOH D O   1 
HETATM 12191 O  O   . HOH PC 9 .   ? -54.248 -23.264 40.650  1.00 43.06 ? 2099 HOH D O   1 
HETATM 12192 O  O   . HOH PC 9 .   ? -39.156 -9.084  41.911  1.00 30.56 ? 2100 HOH D O   1 
HETATM 12193 O  O   . HOH PC 9 .   ? -35.852 -8.052  47.283  1.00 20.90 ? 2101 HOH D O   1 
HETATM 12194 O  O   . HOH PC 9 .   ? -41.727 -4.513  47.054  1.00 35.71 ? 2102 HOH D O   1 
HETATM 12195 O  O   . HOH PC 9 .   ? -38.612 -5.880  41.310  1.00 43.52 ? 2103 HOH D O   1 
HETATM 12196 O  O   . HOH PC 9 .   ? -37.073 -14.629 56.460  1.00 26.14 ? 2104 HOH D O   1 
HETATM 12197 O  O   . HOH PC 9 .   ? -46.924 -0.150  50.767  1.00 58.60 ? 2105 HOH D O   1 
HETATM 12198 O  O   . HOH PC 9 .   ? -48.682 -0.908  53.962  1.00 52.72 ? 2106 HOH D O   1 
HETATM 12199 O  O   . HOH PC 9 .   ? -39.691 2.141   55.262  1.00 40.11 ? 2107 HOH D O   1 
HETATM 12200 O  O   . HOH PC 9 .   ? -37.790 2.539   50.674  1.00 46.74 ? 2108 HOH D O   1 
HETATM 12201 O  O   . HOH PC 9 .   ? -30.661 -1.529  65.652  1.00 38.49 ? 2109 HOH D O   1 
HETATM 12202 O  O   . HOH PC 9 .   ? -28.763 -8.206  61.711  1.00 32.09 ? 2110 HOH D O   1 
HETATM 12203 O  O   . HOH PC 9 .   ? -27.011 -11.141 62.091  1.00 41.67 ? 2111 HOH D O   1 
HETATM 12204 O  O   . HOH PC 9 .   ? -23.896 -11.068 55.053  1.00 24.67 ? 2112 HOH D O   1 
HETATM 12205 O  O   . HOH PC 9 .   ? -24.689 -12.107 62.160  1.00 34.64 ? 2113 HOH D O   1 
HETATM 12206 O  O   . HOH PC 9 .   ? -21.749 -13.289 59.747  1.00 25.26 ? 2114 HOH D O   1 
HETATM 12207 O  O   . HOH PC 9 .   ? -34.241 -6.212  48.848  1.00 32.66 ? 2115 HOH D O   1 
HETATM 12208 O  O   . HOH PC 9 .   ? -30.057 -6.937  47.992  1.00 29.27 ? 2116 HOH D O   1 
HETATM 12209 O  O   . HOH PC 9 .   ? -40.402 -25.472 42.066  1.00 24.73 ? 2117 HOH D O   1 
HETATM 12210 O  O   . HOH PC 9 .   ? -47.031 -27.232 46.246  1.00 29.16 ? 2118 HOH D O   1 
HETATM 12211 O  O   . HOH PC 9 .   ? -48.899 -31.514 46.479  1.00 45.84 ? 2119 HOH D O   1 
HETATM 12212 O  O   . HOH PC 9 .   ? -40.620 -32.872 38.220  1.00 32.26 ? 2120 HOH D O   1 
HETATM 12213 O  O   . HOH PC 9 .   ? -46.920 -31.752 36.152  1.00 50.40 ? 2121 HOH D O   1 
HETATM 12214 O  O   . HOH PC 9 .   ? -44.441 -34.629 35.807  1.00 50.39 ? 2122 HOH D O   1 
HETATM 12215 O  O   . HOH PC 9 .   ? -51.617 -35.122 44.093  1.00 38.53 ? 2123 HOH D O   1 
HETATM 12216 O  O   . HOH PC 9 .   ? -54.512 -25.091 53.411  1.00 45.66 ? 2124 HOH D O   1 
HETATM 12217 O  O   . HOH PC 9 .   ? -54.831 -27.827 61.586  1.00 70.56 ? 2125 HOH D O   1 
HETATM 12218 O  O   . HOH PC 9 .   ? -56.382 -26.596 60.003  1.00 66.06 ? 2126 HOH D O   1 
HETATM 12219 O  O   . HOH PC 9 .   ? -54.074 -38.124 48.781  1.00 53.04 ? 2127 HOH D O   1 
HETATM 12220 O  O   . HOH PC 9 .   ? -51.265 -39.943 48.825  1.00 43.13 ? 2128 HOH D O   1 
HETATM 12221 O  O   . HOH PC 9 .   ? -49.045 -40.628 45.280  1.00 64.44 ? 2129 HOH D O   1 
HETATM 12222 O  O   . HOH PC 9 .   ? -35.556 -36.405 39.340  1.00 31.63 ? 2130 HOH D O   1 
HETATM 12223 O  O   . HOH PC 9 .   ? -34.649 -25.123 41.744  1.00 35.65 ? 2131 HOH D O   1 
HETATM 12224 O  O   . HOH PC 9 .   ? -29.881 -24.646 45.605  1.00 30.42 ? 2132 HOH D O   1 
HETATM 12225 O  O   . HOH PC 9 .   ? -28.448 -21.849 50.539  1.00 44.71 ? 2133 HOH D O   1 
HETATM 12226 O  O   . HOH PC 9 .   ? -28.038 -21.922 46.744  1.00 41.59 ? 2134 HOH D O   1 
HETATM 12227 O  O   . HOH PC 9 .   ? -28.927 -18.991 41.854  1.00 33.60 ? 2135 HOH D O   1 
HETATM 12228 O  O   . HOH PC 9 .   ? -31.478 -16.731 37.936  1.00 48.32 ? 2136 HOH D O   1 
HETATM 12229 O  O   . HOH PC 9 .   ? -30.041 -4.931  40.028  1.00 53.86 ? 2137 HOH D O   1 
HETATM 12230 O  O   . HOH PC 9 .   ? -27.488 -6.875  48.284  1.00 34.13 ? 2138 HOH D O   1 
HETATM 12231 O  O   . HOH PC 9 .   ? -25.123 -4.453  49.407  1.00 37.02 ? 2139 HOH D O   1 
HETATM 12232 O  O   . HOH PC 9 .   ? -28.411 1.495   48.901  1.00 47.56 ? 2140 HOH D O   1 
HETATM 12233 O  O   . HOH PC 9 .   ? -22.879 3.128   51.723  1.00 27.04 ? 2141 HOH D O   1 
HETATM 12234 O  O   . HOH PC 9 .   ? -28.110 0.686   66.142  1.00 35.41 ? 2142 HOH D O   1 
HETATM 12235 O  O   . HOH PC 9 .   ? -39.124 5.261   66.995  1.00 32.51 ? 2143 HOH D O   1 
HETATM 12236 O  O   . HOH PC 9 .   ? -37.784 8.561   64.355  1.00 44.86 ? 2144 HOH D O   1 
HETATM 12237 O  O   . HOH PC 9 .   ? -34.220 5.213   57.211  1.00 28.24 ? 2145 HOH D O   1 
HETATM 12238 O  O   . HOH PC 9 .   ? -41.785 4.670   56.117  1.00 53.71 ? 2146 HOH D O   1 
HETATM 12239 O  O   . HOH PC 9 .   ? -23.171 4.102   57.700  1.00 32.05 ? 2147 HOH D O   1 
HETATM 12240 O  O   . HOH PC 9 .   ? -17.466 -5.226  55.601  1.00 57.45 ? 2148 HOH D O   1 
HETATM 12241 O  O   . HOH PC 9 .   ? -19.826 -3.637  64.163  1.00 35.23 ? 2149 HOH D O   1 
HETATM 12242 O  O   . HOH PC 9 .   ? -22.583 -13.211 51.902  1.00 29.64 ? 2150 HOH D O   1 
HETATM 12243 O  O   . HOH PC 9 .   ? -24.952 -11.676 52.567  1.00 30.09 ? 2151 HOH D O   1 
HETATM 12244 O  O   . HOH PC 9 .   ? -25.140 -7.550  48.831  1.00 24.55 ? 2152 HOH D O   1 
HETATM 12245 O  O   . HOH PC 9 .   ? -22.752 -14.394 49.386  1.00 32.01 ? 2153 HOH D O   1 
HETATM 12246 O  O   . HOH PC 9 .   ? -15.600 -9.804  46.449  1.00 47.47 ? 2154 HOH D O   1 
HETATM 12247 O  O   . HOH PC 9 .   ? -15.400 -23.258 61.121  1.00 21.60 ? 2155 HOH D O   1 
HETATM 12248 O  O   . HOH PC 9 .   ? -12.331 -17.221 55.222  1.00 38.60 ? 2156 HOH D O   1 
HETATM 12249 O  O   . HOH PC 9 .   ? -8.845  -16.378 56.333  1.00 45.85 ? 2157 HOH D O   1 
HETATM 12250 O  O   . HOH PC 9 .   ? -21.478 -13.281 69.689  1.00 60.76 ? 2158 HOH D O   1 
HETATM 12251 O  O   . HOH PC 9 .   ? -21.958 -12.699 62.451  1.00 31.18 ? 2159 HOH D O   1 
HETATM 12252 O  O   . HOH PC 9 .   ? -23.150 -11.109 65.895  1.00 40.08 ? 2160 HOH D O   1 
HETATM 12253 O  O   . HOH PC 9 .   ? -17.512 -12.633 74.975  1.00 45.66 ? 2161 HOH D O   1 
HETATM 12254 O  O   . HOH PC 9 .   ? -20.000 -10.291 69.486  1.00 45.25 ? 2162 HOH D O   1 
HETATM 12255 O  O   . HOH PC 9 .   ? -16.024 -19.252 78.026  1.00 50.29 ? 2163 HOH D O   1 
HETATM 12256 O  O   . HOH PC 9 .   ? -15.752 -20.149 80.781  1.00 42.36 ? 2164 HOH D O   1 
HETATM 12257 O  O   . HOH PC 9 .   ? -8.809  -20.188 81.267  1.00 45.05 ? 2165 HOH D O   1 
HETATM 12258 O  O   . HOH PC 9 .   ? -16.710 -22.776 79.647  1.00 45.78 ? 2166 HOH D O   1 
HETATM 12259 O  O   . HOH PC 9 .   ? -14.291 -29.758 80.513  1.00 42.70 ? 2167 HOH D O   1 
HETATM 12260 O  O   . HOH PC 9 .   ? -18.298 -29.349 79.466  1.00 62.25 ? 2168 HOH D O   1 
HETATM 12261 O  O   . HOH PC 9 .   ? -18.024 -33.589 82.051  1.00 33.65 ? 2169 HOH D O   1 
HETATM 12262 O  O   . HOH PC 9 .   ? -8.119  -22.167 72.700  1.00 51.01 ? 2170 HOH D O   1 
HETATM 12263 O  O   . HOH PC 9 .   ? -8.807  -30.225 70.997  1.00 54.87 ? 2171 HOH D O   1 
HETATM 12264 O  O   . HOH PC 9 .   ? -6.803  -29.736 71.981  1.00 54.60 ? 2172 HOH D O   1 
HETATM 12265 O  O   . HOH PC 9 .   ? -12.283 -26.142 64.311  1.00 24.15 ? 2173 HOH D O   1 
HETATM 12266 O  O   . HOH PC 9 .   ? -10.320 -23.684 66.803  1.00 48.31 ? 2174 HOH D O   1 
HETATM 12267 O  O   . HOH PC 9 .   ? -9.948  -27.335 65.131  1.00 40.11 ? 2175 HOH D O   1 
HETATM 12268 O  O   . HOH PC 9 .   ? -17.135 -33.330 69.637  1.00 36.72 ? 2176 HOH D O   1 
HETATM 12269 O  O   . HOH PC 9 .   ? -14.407 -29.201 58.204  0.50 10.31 ? 2177 HOH D O   1 
HETATM 12270 O  O   . HOH PC 9 .   ? -9.909  -28.663 63.299  1.00 52.80 ? 2178 HOH D O   1 
HETATM 12271 O  O   . HOH PC 9 .   ? -14.586 -32.614 62.984  1.00 42.20 ? 2179 HOH D O   1 
HETATM 12272 O  O   . HOH PC 9 .   ? -15.856 -25.085 52.725  1.00 28.75 ? 2180 HOH D O   1 
HETATM 12273 O  O   . HOH PC 9 .   ? -14.120 -26.323 51.398  1.00 33.36 ? 2181 HOH D O   1 
HETATM 12274 O  O   . HOH PC 9 .   ? -12.666 -28.232 52.370  1.00 40.98 ? 2182 HOH D O   1 
HETATM 12275 O  O   . HOH PC 9 .   ? -9.521  -24.524 54.941  1.00 25.30 ? 2183 HOH D O   1 
HETATM 12276 O  O   . HOH PC 9 .   ? -7.081  -22.534 57.302  1.00 36.56 ? 2184 HOH D O   1 
HETATM 12277 O  O   . HOH PC 9 .   ? -7.556  -19.037 59.199  1.00 37.08 ? 2185 HOH D O   1 
HETATM 12278 O  O   . HOH PC 9 .   ? -11.191 -29.291 59.606  1.00 63.47 ? 2186 HOH D O   1 
HETATM 12279 O  O   . HOH PC 9 .   ? -9.898  -26.520 56.430  1.00 31.53 ? 2187 HOH D O   1 
HETATM 12280 O  O   . HOH PC 9 .   ? -13.156 -23.682 62.577  1.00 28.65 ? 2188 HOH D O   1 
HETATM 12281 O  O   . HOH PC 9 .   ? -7.839  -18.671 61.974  1.00 38.58 ? 2189 HOH D O   1 
HETATM 12282 O  O   . HOH PC 9 .   ? -47.489 -6.214  66.369  1.00 58.90 ? 2190 HOH D O   1 
HETATM 12283 O  O   . HOH PC 9 .   ? -27.756 -0.849  74.597  1.00 46.05 ? 2191 HOH D O   1 
HETATM 12284 O  O   . HOH PC 9 .   ? -7.916  -13.364 71.027  1.00 52.27 ? 2192 HOH D O   1 
HETATM 12285 O  O   . HOH PC 9 .   ? -30.076 -19.058 53.696  1.00 50.01 ? 2193 HOH D O   1 
HETATM 12286 O  O   . HOH PC 9 .   ? -40.773 -29.516 79.360  1.00 41.09 ? 2194 HOH D O   1 
HETATM 12287 O  O   . HOH PC 9 .   ? -38.149 -29.046 82.460  1.00 43.79 ? 2195 HOH D O   1 
HETATM 12288 O  O   . HOH PC 9 .   ? -40.872 -22.010 80.173  1.00 47.23 ? 2196 HOH D O   1 
HETATM 12289 O  O   . HOH PC 9 .   ? -3.733  -29.326 56.445  1.00 52.68 ? 2197 HOH D O   1 
HETATM 12290 O  O   . HOH PC 9 .   ? -3.742  -26.888 55.369  1.00 54.29 ? 2198 HOH D 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   LEU 1   4   4   LEU LEU A . n 
A 1 2   PRO 2   5   5   PRO PRO A . n 
A 1 3   PRO 3   6   6   PRO PRO A . n 
A 1 4   GLY 4   7   7   GLY GLY A . n 
A 1 5   PRO 5   8   8   PRO PRO A . n 
A 1 6   LEU 6   9   9   LEU LEU A . n 
A 1 7   GLU 7   10  10  GLU GLU A . n 
A 1 8   ASN 8   11  11  ASN ASN A . n 
A 1 9   SER 9   12  12  SER SER A . n 
A 1 10  SER 10  13  13  SER SER A . n 
A 1 11  ALA 11  14  14  ALA ALA A . n 
A 1 12  LYS 12  15  15  LYS LYS A . n 
A 1 13  LEU 13  16  16  LEU LEU A . n 
A 1 14  VAL 14  17  17  VAL VAL A . n 
A 1 15  ASN 15  18  18  ASN ASN A . n 
A 1 16  ASP 16  19  19  ASP ASP A . n 
A 1 17  GLU 17  20  20  GLU GLU A . n 
A 1 18  ALA 18  21  21  ALA ALA A . n 
A 1 19  HIS 19  22  22  HIS HIS A . n 
A 1 20  PRO 20  23  23  PRO PRO A . n 
A 1 21  TRP 21  24  24  TRP TRP A . n 
A 1 22  LYS 22  25  25  LYS LYS A . n 
A 1 23  PRO 23  26  26  PRO PRO A . n 
A 1 24  LEU 24  27  27  LEU LEU A . n 
A 1 25  ARG 25  28  28  ARG ARG A . n 
A 1 26  PRO 26  29  29  PRO PRO A . n 
A 1 27  GLY 27  30  30  GLY GLY A . n 
A 1 28  ASP 28  31  31  ASP ASP A . n 
A 1 29  ILE 29  32  32  ILE ILE A . n 
A 1 30  ARG 30  33  33  ARG ARG A . n 
A 1 31  GLY 31  34  34  GLY GLY A . n 
A 1 32  PRO 32  35  35  PRO PRO A . n 
A 1 33  CYS 33  36  36  CYS CYS A . n 
A 1 34  PRO 34  37  37  PRO PRO A . n 
A 1 35  GLY 35  38  38  GLY GLY A . n 
A 1 36  LEU 36  39  39  LEU LEU A . n 
A 1 37  ASN 37  40  40  ASN ASN A . n 
A 1 38  THR 38  41  41  THR THR A . n 
A 1 39  LEU 39  42  42  LEU LEU A . n 
A 1 40  ALA 40  43  43  ALA ALA A . n 
A 1 41  SER 41  44  44  SER SER A . n 
A 1 42  HIS 42  45  45  HIS HIS A . n 
A 1 43  GLY 43  46  46  GLY GLY A . n 
A 1 44  TYR 44  47  47  TYR TYR A . n 
A 1 45  LEU 45  48  48  LEU LEU A . n 
A 1 46  PRO 46  49  49  PRO PRO A . n 
A 1 47  ARG 47  50  50  ARG ARG A . n 
A 1 48  ASN 48  51  51  ASN ASN A . n 
A 1 49  GLY 49  52  52  GLY GLY A . n 
A 1 50  VAL 50  53  53  VAL VAL A . n 
A 1 51  ALA 51  54  54  ALA ALA A . n 
A 1 52  THR 52  55  55  THR THR A . n 
A 1 53  PRO 53  56  56  PRO PRO A . n 
A 1 54  VAL 54  57  57  VAL VAL A . n 
A 1 55  GLN 55  58  58  GLN GLN A . n 
A 1 56  ILE 56  59  59  ILE ILE A . n 
A 1 57  ILE 57  60  60  ILE ILE A . n 
A 1 58  ASN 58  61  61  ASN ASN A . n 
A 1 59  ALA 59  62  62  ALA ALA A . n 
A 1 60  VAL 60  63  63  VAL VAL A . n 
A 1 61  GLN 61  64  64  GLN GLN A . n 
A 1 62  GLU 62  65  65  GLU GLU A . n 
A 1 63  GLY 63  66  66  GLY GLY A . n 
A 1 64  LEU 64  67  67  LEU LEU A . n 
A 1 65  ASN 65  68  68  ASN ASN A . n 
A 1 66  PHE 66  69  69  PHE PHE A . n 
A 1 67  ASP 67  70  70  ASP ASP A . n 
A 1 68  ASN 68  71  71  ASN ASN A . n 
A 1 69  GLN 69  72  72  GLN GLN A . n 
A 1 70  ALA 70  73  73  ALA ALA A . n 
A 1 71  ALA 71  74  74  ALA ALA A . n 
A 1 72  VAL 72  75  75  VAL VAL A . n 
A 1 73  PHE 73  76  76  PHE PHE A . n 
A 1 74  ALA 74  77  77  ALA ALA A . n 
A 1 75  THR 75  78  78  THR THR A . n 
A 1 76  TYR 76  79  79  TYR TYR A . n 
A 1 77  ALA 77  80  80  ALA ALA A . n 
A 1 78  ALA 78  81  81  ALA ALA A . n 
A 1 79  HIS 79  82  82  HIS HIS A . n 
A 1 80  LEU 80  83  83  LEU LEU A . n 
A 1 81  VAL 81  84  84  VAL VAL A . n 
A 1 82  ASP 82  85  85  ASP ASP A . n 
A 1 83  GLY 83  86  86  GLY GLY A . n 
A 1 84  ASN 84  87  87  ASN ASN A . n 
A 1 85  LEU 85  88  88  LEU LEU A . n 
A 1 86  ILE 86  89  89  ILE ILE A . n 
A 1 87  THR 87  90  90  THR THR A . n 
A 1 88  ASP 88  91  91  ASP ASP A . n 
A 1 89  LEU 89  92  92  LEU LEU A . n 
A 1 90  LEU 90  93  93  LEU LEU A . n 
A 1 91  SER 91  94  94  SER SER A . n 
A 1 92  ILE 92  95  95  ILE ILE A . n 
A 1 93  GLY 93  96  96  GLY GLY A . n 
A 1 94  ARG 94  97  97  ARG ARG A . n 
A 1 95  LYS 95  98  98  LYS LYS A . n 
A 1 96  THR 96  99  99  THR THR A . n 
A 1 97  ARG 97  100 100 ARG ARG A . n 
A 1 98  LEU 98  101 101 LEU LEU A . n 
A 1 99  THR 99  102 102 THR THR A . n 
A 1 100 GLY 100 103 103 GLY GLY A . n 
A 1 101 PRO 101 104 104 PRO PRO A . n 
A 1 102 ASP 102 105 105 ASP ASP A . n 
A 1 103 PRO 103 106 106 PRO PRO A . n 
A 1 104 PRO 104 107 107 PRO PRO A . n 
A 1 105 PRO 105 108 108 PRO PRO A . n 
A 1 106 PRO 106 109 109 PRO PRO A . n 
A 1 107 ALA 107 110 110 ALA ALA A . n 
A 1 108 SER 108 111 111 SER SER A . n 
A 1 109 VAL 109 112 112 VAL VAL A . n 
A 1 110 GLY 110 113 113 GLY GLY A . n 
A 1 111 GLY 111 114 114 GLY GLY A . n 
A 1 112 LEU 112 115 115 LEU LEU A . n 
A 1 113 ASN 113 116 116 ASN ASN A . n 
A 1 114 GLU 114 117 117 GLU GLU A . n 
A 1 115 HIS 115 118 118 HIS HIS A . n 
A 1 116 GLY 116 119 119 GLY GLY A . n 
A 1 117 THR 117 120 120 THR THR A . n 
A 1 118 PHE 118 121 121 PHE PHE A . n 
A 1 119 GLU 119 122 122 GLU GLU A . n 
A 1 120 GLY 120 123 123 GLY GLY A . n 
A 1 121 ASP 121 124 124 ASP ASP A . n 
A 1 122 ALA 122 125 125 ALA ALA A . n 
A 1 123 SER 123 126 126 SER SER A . n 
A 1 124 MET 124 127 127 MET MET A . n 
A 1 125 THR 125 128 128 THR THR A . n 
A 1 126 ARG 126 129 129 ARG ARG A . n 
A 1 127 GLY 127 130 130 GLY GLY A . n 
A 1 128 ASP 128 131 131 ASP ASP A . n 
A 1 129 ALA 129 132 132 ALA ALA A . n 
A 1 130 PHE 130 133 133 PHE PHE A . n 
A 1 131 PHE 131 134 134 PHE PHE A . n 
A 1 132 GLY 132 135 135 GLY GLY A . n 
A 1 133 ASN 133 136 136 ASN ASN A . n 
A 1 134 ASN 134 137 137 ASN ASN A . n 
A 1 135 HIS 135 138 138 HIS HIS A . n 
A 1 136 ASP 136 139 139 ASP ASP A . n 
A 1 137 PHE 137 140 140 PHE PHE A . n 
A 1 138 ASN 138 141 141 ASN ASN A . n 
A 1 139 GLU 139 142 142 GLU GLU A . n 
A 1 140 THR 140 143 143 THR THR A . n 
A 1 141 LEU 141 144 144 LEU LEU A . n 
A 1 142 PHE 142 145 145 PHE PHE A . n 
A 1 143 GLU 143 146 146 GLU GLU A . n 
A 1 144 GLN 144 147 147 GLN GLN A . n 
A 1 145 LEU 145 148 148 LEU LEU A . n 
A 1 146 VAL 146 149 149 VAL VAL A . n 
A 1 147 ASP 147 150 150 ASP ASP A . n 
A 1 148 TYR 148 151 151 TYR TYR A . n 
A 1 149 SER 149 152 152 SER SER A . n 
A 1 150 ASN 150 153 153 ASN ASN A . n 
A 1 151 ARG 151 154 154 ARG ARG A . n 
A 1 152 PHE 152 155 155 PHE PHE A . n 
A 1 153 GLY 153 156 156 GLY GLY A . n 
A 1 154 GLY 154 157 157 GLY GLY A . n 
A 1 155 GLY 155 158 158 GLY GLY A . n 
A 1 156 LYS 156 159 159 LYS LYS A . n 
A 1 157 TYR 157 160 160 TYR TYR A . n 
A 1 158 ASN 158 161 161 ASN ASN A . n 
A 1 159 LEU 159 162 162 LEU LEU A . n 
A 1 160 THR 160 163 163 THR THR A . n 
A 1 161 VAL 161 164 164 VAL VAL A . n 
A 1 162 ALA 162 165 165 ALA ALA A . n 
A 1 163 GLY 163 166 166 GLY GLY A . n 
A 1 164 GLU 164 167 167 GLU GLU A . n 
A 1 165 LEU 165 168 168 LEU LEU A . n 
A 1 166 ARG 166 169 169 ARG ARG A . n 
A 1 167 PHE 167 170 170 PHE PHE A . n 
A 1 168 LYS 168 171 171 LYS LYS A . n 
A 1 169 ARG 169 172 172 ARG ARG A . n 
A 1 170 ILE 170 173 173 ILE ILE A . n 
A 1 171 GLN 171 174 174 GLN GLN A . n 
A 1 172 ASP 172 175 175 ASP ASP A . n 
A 1 173 SER 173 176 176 SER SER A . n 
A 1 174 ILE 174 177 177 ILE ILE A . n 
A 1 175 ALA 175 178 178 ALA ALA A . n 
A 1 176 THR 176 179 179 THR THR A . n 
A 1 177 ASN 177 180 180 ASN ASN A . n 
A 1 178 PRO 178 181 181 PRO PRO A . n 
A 1 179 ASN 179 182 182 ASN ASN A . n 
A 1 180 PHE 180 183 183 PHE PHE A . n 
A 1 181 SER 181 184 184 SER SER A . n 
A 1 182 PHE 182 185 185 PHE PHE A . n 
A 1 183 VAL 183 186 186 VAL VAL A . n 
A 1 184 ASP 184 187 187 ASP ASP A . n 
A 1 185 PHE 185 188 188 PHE PHE A . n 
A 1 186 ARG 186 189 189 ARG ARG A . n 
A 1 187 PHE 187 190 190 PHE PHE A . n 
A 1 188 PHE 188 191 191 PHE PHE A . n 
A 1 189 THR 189 192 192 THR THR A . n 
A 1 190 ALA 190 193 193 ALA ALA A . n 
A 1 191 TYR 191 194 194 TYR TYR A . n 
A 1 192 GLY 192 195 195 GLY GLY A . n 
A 1 193 GLU 193 196 196 GLU GLU A . n 
A 1 194 THR 194 197 197 THR THR A . n 
A 1 195 THR 195 198 198 THR THR A . n 
A 1 196 PHE 196 199 199 PHE PHE A . n 
A 1 197 PRO 197 200 200 PRO PRO A . n 
A 1 198 ALA 198 201 201 ALA ALA A . n 
A 1 199 ASN 199 202 202 ASN ASN A . n 
A 1 200 LEU 200 203 203 LEU LEU A . n 
A 1 201 PHE 201 204 204 PHE PHE A . n 
A 1 202 VAL 202 205 205 VAL VAL A . n 
A 1 203 ASP 203 206 206 ASP ASP A . n 
A 1 204 GLY 204 207 207 GLY GLY A . n 
A 1 205 ARG 205 208 208 ARG ARG A . n 
A 1 206 ARG 206 209 209 ARG ARG A . n 
A 1 207 ASP 207 210 210 ASP ASP A . n 
A 1 208 ASP 208 211 211 ASP ASP A . n 
A 1 209 GLY 209 212 212 GLY GLY A . n 
A 1 210 GLN 210 213 213 GLN GLN A . n 
A 1 211 LEU 211 214 214 LEU LEU A . n 
A 1 212 ASP 212 215 215 ASP ASP A . n 
A 1 213 MET 213 216 216 MET MET A . n 
A 1 214 ASP 214 217 217 ASP ASP A . n 
A 1 215 ALA 215 218 218 ALA ALA A . n 
A 1 216 ALA 216 219 219 ALA ALA A . n 
A 1 217 ARG 217 220 220 ARG ARG A . n 
A 1 218 SER 218 221 221 SER SER A . n 
A 1 219 PHE 219 222 222 PHE PHE A . n 
A 1 220 PHE 220 223 223 PHE PHE A . n 
A 1 221 GLN 221 224 224 GLN GLN A . n 
A 1 222 PHE 222 225 225 PHE PHE A . n 
A 1 223 SER 223 226 226 SER SER A . n 
A 1 224 ARG 224 227 227 ARG ARG A . n 
A 1 225 MET 225 228 228 MET MET A . n 
A 1 226 PRO 226 229 229 PRO PRO A . n 
A 1 227 ASP 227 230 230 ASP ASP A . n 
A 1 228 ASP 228 231 231 ASP ASP A . n 
A 1 229 PHE 229 232 232 PHE PHE A . n 
A 1 230 PHE 230 233 233 PHE PHE A . n 
A 1 231 ARG 231 234 234 ARG ARG A . n 
A 1 232 ALA 232 235 235 ALA ALA A . n 
A 1 233 PRO 233 236 236 PRO PRO A . n 
A 1 234 SER 234 237 237 SER SER A . n 
A 1 235 PRO 235 238 238 PRO PRO A . n 
A 1 236 ARG 236 239 239 ARG ARG A . n 
A 1 237 SER 237 240 240 SER SER A . n 
A 1 238 GLY 238 241 241 GLY GLY A . n 
A 1 239 THR 239 242 242 THR THR A . n 
A 1 240 GLY 240 243 243 GLY GLY A . n 
A 1 241 VAL 241 244 244 VAL VAL A . n 
A 1 242 GLU 242 245 245 GLU GLU A . n 
A 1 243 VAL 243 246 246 VAL VAL A . n 
A 1 244 VAL 244 247 247 VAL VAL A . n 
A 1 245 ILE 245 248 248 ILE ILE A . n 
A 1 246 GLN 246 249 249 GLN GLN A . n 
A 1 247 ALA 247 250 250 ALA ALA A . n 
A 1 248 HIS 248 251 251 HIS HIS A . n 
A 1 249 PRO 249 252 252 PRO PRO A . n 
A 1 250 MET 250 253 253 MET MET A . n 
A 1 251 GLN 251 254 254 GLN GLN A . n 
A 1 252 PRO 252 255 255 PRO PRO A . n 
A 1 253 GLY 253 256 256 GLY GLY A . n 
A 1 254 ARG 254 257 257 ARG ARG A . n 
A 1 255 ASN 255 258 258 ASN ASN A . n 
A 1 256 VAL 256 259 259 VAL VAL A . n 
A 1 257 GLY 257 260 260 GLY GLY A . n 
A 1 258 LYS 258 261 261 LYS LYS A . n 
A 1 259 ILE 259 262 262 ILE ILE A . n 
A 1 260 ASN 260 263 263 ASN ASN A . n 
A 1 261 SER 261 264 264 SER SER A . n 
A 1 262 TYR 262 265 265 TYR TYR A . n 
A 1 263 THR 263 266 266 THR THR A . n 
A 1 264 VAL 264 267 267 VAL VAL A . n 
A 1 265 ASP 265 268 268 ASP ASP A . n 
A 1 266 PRO 266 269 269 PRO PRO A . n 
A 1 267 THR 267 270 270 THR THR A . n 
A 1 268 SER 268 271 271 SER SER A . n 
A 1 269 SER 269 272 272 SER SER A . n 
A 1 270 ASP 270 273 273 ASP ASP A . n 
A 1 271 PHE 271 274 274 PHE PHE A . n 
A 1 272 SER 272 275 275 SER SER A . n 
A 1 273 THR 273 276 276 THR THR A . n 
A 1 274 PRO 274 277 277 PRO PRO A . n 
A 1 275 CYS 275 278 278 CYS CYS A . n 
A 1 276 LEU 276 279 279 LEU LEU A . n 
A 1 277 MET 277 280 280 MET MET A . n 
A 1 278 TYR 278 281 281 TYR TYR A . n 
A 1 279 GLU 279 282 282 GLU GLU A . n 
A 1 280 LYS 280 283 283 LYS LYS A . n 
A 1 281 PHE 281 284 284 PHE PHE A . n 
A 1 282 VAL 282 285 285 VAL VAL A . n 
A 1 283 ASN 283 286 286 ASN ASN A . n 
A 1 284 ILE 284 287 287 ILE ILE A . n 
A 1 285 THR 285 288 288 THR THR A . n 
A 1 286 VAL 286 289 289 VAL VAL A . n 
A 1 287 LYS 287 290 290 LYS LYS A . n 
A 1 288 SER 288 291 291 SER SER A . n 
A 1 289 LEU 289 292 292 LEU LEU A . n 
A 1 290 TYR 290 293 293 TYR TYR A . n 
A 1 291 PRO 291 294 294 PRO PRO A . n 
A 1 292 ASN 292 295 295 ASN ASN A . n 
A 1 293 PRO 293 296 296 PRO PRO A . n 
A 1 294 THR 294 297 297 THR THR A . n 
A 1 295 VAL 295 298 298 VAL VAL A . n 
A 1 296 GLN 296 299 299 GLN GLN A . n 
A 1 297 LEU 297 300 300 LEU LEU A . n 
A 1 298 ARG 298 301 301 ARG ARG A . n 
A 1 299 LYS 299 302 302 LYS LYS A . n 
A 1 300 ALA 300 303 303 ALA ALA A . n 
A 1 301 LEU 301 304 304 LEU LEU A . n 
A 1 302 ASN 302 305 305 ASN ASN A . n 
A 1 303 THR 303 306 306 THR THR A . n 
A 1 304 ASN 304 307 307 ASN ASN A . n 
A 1 305 LEU 305 308 308 LEU LEU A . n 
A 1 306 ASP 306 309 309 ASP ASP A . n 
A 1 307 PHE 307 310 310 PHE PHE A . n 
A 1 308 PHE 308 311 311 PHE PHE A . n 
A 1 309 PHE 309 312 312 PHE PHE A . n 
A 1 310 GLN 310 313 313 GLN GLN A . n 
A 1 311 GLY 311 314 314 GLY GLY A . n 
A 1 312 VAL 312 315 315 VAL VAL A . n 
A 1 313 ALA 313 316 316 ALA ALA A . n 
A 1 314 ALA 314 317 317 ALA ALA A . n 
A 1 315 GLY 315 318 318 GLY GLY A . n 
A 1 316 CYS 316 319 319 CYS CYS A . n 
A 1 317 THR 317 320 320 THR THR A . n 
A 1 318 GLN 318 321 321 GLN GLN A . n 
A 1 319 VAL 319 322 322 VAL VAL A . n 
A 1 320 PHE 320 323 323 PHE PHE A . n 
A 1 321 PRO 321 324 324 PRO PRO A . n 
A 1 322 TYR 322 325 325 TYR TYR A . n 
A 1 323 GLY 323 326 326 GLY GLY A . n 
A 1 324 ARG 324 327 ?   ?   ?   A . n 
A 1 325 ASP 325 328 ?   ?   ?   A . n 
B 1 1   LEU 1   4   4   LEU LEU B . n 
B 1 2   PRO 2   5   5   PRO PRO B . n 
B 1 3   PRO 3   6   6   PRO PRO B . n 
B 1 4   GLY 4   7   7   GLY GLY B . n 
B 1 5   PRO 5   8   8   PRO PRO B . n 
B 1 6   LEU 6   9   9   LEU LEU B . n 
B 1 7   GLU 7   10  10  GLU GLU B . n 
B 1 8   ASN 8   11  11  ASN ASN B . n 
B 1 9   SER 9   12  12  SER SER B . n 
B 1 10  SER 10  13  13  SER SER B . n 
B 1 11  ALA 11  14  14  ALA ALA B . n 
B 1 12  LYS 12  15  15  LYS LYS B . n 
B 1 13  LEU 13  16  16  LEU LEU B . n 
B 1 14  VAL 14  17  17  VAL VAL B . n 
B 1 15  ASN 15  18  18  ASN ASN B . n 
B 1 16  ASP 16  19  19  ASP ASP B . n 
B 1 17  GLU 17  20  20  GLU GLU B . n 
B 1 18  ALA 18  21  21  ALA ALA B . n 
B 1 19  HIS 19  22  22  HIS HIS B . n 
B 1 20  PRO 20  23  23  PRO PRO B . n 
B 1 21  TRP 21  24  24  TRP TRP B . n 
B 1 22  LYS 22  25  25  LYS LYS B . n 
B 1 23  PRO 23  26  26  PRO PRO B . n 
B 1 24  LEU 24  27  27  LEU LEU B . n 
B 1 25  ARG 25  28  28  ARG ARG B . n 
B 1 26  PRO 26  29  29  PRO PRO B . n 
B 1 27  GLY 27  30  30  GLY GLY B . n 
B 1 28  ASP 28  31  31  ASP ASP B . n 
B 1 29  ILE 29  32  32  ILE ILE B . n 
B 1 30  ARG 30  33  33  ARG ARG B . n 
B 1 31  GLY 31  34  34  GLY GLY B . n 
B 1 32  PRO 32  35  35  PRO PRO B . n 
B 1 33  CYS 33  36  36  CYS CYS B . n 
B 1 34  PRO 34  37  37  PRO PRO B . n 
B 1 35  GLY 35  38  38  GLY GLY B . n 
B 1 36  LEU 36  39  39  LEU LEU B . n 
B 1 37  ASN 37  40  40  ASN ASN B . n 
B 1 38  THR 38  41  41  THR THR B . n 
B 1 39  LEU 39  42  42  LEU LEU B . n 
B 1 40  ALA 40  43  43  ALA ALA B . n 
B 1 41  SER 41  44  44  SER SER B . n 
B 1 42  HIS 42  45  45  HIS HIS B . n 
B 1 43  GLY 43  46  46  GLY GLY B . n 
B 1 44  TYR 44  47  47  TYR TYR B . n 
B 1 45  LEU 45  48  48  LEU LEU B . n 
B 1 46  PRO 46  49  49  PRO PRO B . n 
B 1 47  ARG 47  50  50  ARG ARG B . n 
B 1 48  ASN 48  51  51  ASN ASN B . n 
B 1 49  GLY 49  52  52  GLY GLY B . n 
B 1 50  VAL 50  53  53  VAL VAL B . n 
B 1 51  ALA 51  54  54  ALA ALA B . n 
B 1 52  THR 52  55  55  THR THR B . n 
B 1 53  PRO 53  56  56  PRO PRO B . n 
B 1 54  VAL 54  57  57  VAL VAL B . n 
B 1 55  GLN 55  58  58  GLN GLN B . n 
B 1 56  ILE 56  59  59  ILE ILE B . n 
B 1 57  ILE 57  60  60  ILE ILE B . n 
B 1 58  ASN 58  61  61  ASN ASN B . n 
B 1 59  ALA 59  62  62  ALA ALA B . n 
B 1 60  VAL 60  63  63  VAL VAL B . n 
B 1 61  GLN 61  64  64  GLN GLN B . n 
B 1 62  GLU 62  65  65  GLU GLU B . n 
B 1 63  GLY 63  66  66  GLY GLY B . n 
B 1 64  LEU 64  67  67  LEU LEU B . n 
B 1 65  ASN 65  68  68  ASN ASN B . n 
B 1 66  PHE 66  69  69  PHE PHE B . n 
B 1 67  ASP 67  70  70  ASP ASP B . n 
B 1 68  ASN 68  71  71  ASN ASN B . n 
B 1 69  GLN 69  72  72  GLN GLN B . n 
B 1 70  ALA 70  73  73  ALA ALA B . n 
B 1 71  ALA 71  74  74  ALA ALA B . n 
B 1 72  VAL 72  75  75  VAL VAL B . n 
B 1 73  PHE 73  76  76  PHE PHE B . n 
B 1 74  ALA 74  77  77  ALA ALA B . n 
B 1 75  THR 75  78  78  THR THR B . n 
B 1 76  TYR 76  79  79  TYR TYR B . n 
B 1 77  ALA 77  80  80  ALA ALA B . n 
B 1 78  ALA 78  81  81  ALA ALA B . n 
B 1 79  HIS 79  82  82  HIS HIS B . n 
B 1 80  LEU 80  83  83  LEU LEU B . n 
B 1 81  VAL 81  84  84  VAL VAL B . n 
B 1 82  ASP 82  85  85  ASP ASP B . n 
B 1 83  GLY 83  86  86  GLY GLY B . n 
B 1 84  ASN 84  87  87  ASN ASN B . n 
B 1 85  LEU 85  88  88  LEU LEU B . n 
B 1 86  ILE 86  89  89  ILE ILE B . n 
B 1 87  THR 87  90  90  THR THR B . n 
B 1 88  ASP 88  91  91  ASP ASP B . n 
B 1 89  LEU 89  92  92  LEU LEU B . n 
B 1 90  LEU 90  93  93  LEU LEU B . n 
B 1 91  SER 91  94  94  SER SER B . n 
B 1 92  ILE 92  95  95  ILE ILE B . n 
B 1 93  GLY 93  96  96  GLY GLY B . n 
B 1 94  ARG 94  97  97  ARG ARG B . n 
B 1 95  LYS 95  98  98  LYS LYS B . n 
B 1 96  THR 96  99  99  THR THR B . n 
B 1 97  ARG 97  100 100 ARG ARG B . n 
B 1 98  LEU 98  101 101 LEU LEU B . n 
B 1 99  THR 99  102 102 THR THR B . n 
B 1 100 GLY 100 103 103 GLY GLY B . n 
B 1 101 PRO 101 104 104 PRO PRO B . n 
B 1 102 ASP 102 105 105 ASP ASP B . n 
B 1 103 PRO 103 106 106 PRO PRO B . n 
B 1 104 PRO 104 107 107 PRO PRO B . n 
B 1 105 PRO 105 108 108 PRO PRO B . n 
B 1 106 PRO 106 109 109 PRO PRO B . n 
B 1 107 ALA 107 110 110 ALA ALA B . n 
B 1 108 SER 108 111 111 SER SER B . n 
B 1 109 VAL 109 112 112 VAL VAL B . n 
B 1 110 GLY 110 113 113 GLY GLY B . n 
B 1 111 GLY 111 114 114 GLY GLY B . n 
B 1 112 LEU 112 115 115 LEU LEU B . n 
B 1 113 ASN 113 116 116 ASN ASN B . n 
B 1 114 GLU 114 117 117 GLU GLU B . n 
B 1 115 HIS 115 118 118 HIS HIS B . n 
B 1 116 GLY 116 119 119 GLY GLY B . n 
B 1 117 THR 117 120 120 THR THR B . n 
B 1 118 PHE 118 121 121 PHE PHE B . n 
B 1 119 GLU 119 122 122 GLU GLU B . n 
B 1 120 GLY 120 123 123 GLY GLY B . n 
B 1 121 ASP 121 124 124 ASP ASP B . n 
B 1 122 ALA 122 125 125 ALA ALA B . n 
B 1 123 SER 123 126 126 SER SER B . n 
B 1 124 MET 124 127 127 MET MET B . n 
B 1 125 THR 125 128 128 THR THR B . n 
B 1 126 ARG 126 129 129 ARG ARG B . n 
B 1 127 GLY 127 130 130 GLY GLY B . n 
B 1 128 ASP 128 131 131 ASP ASP B . n 
B 1 129 ALA 129 132 132 ALA ALA B . n 
B 1 130 PHE 130 133 133 PHE PHE B . n 
B 1 131 PHE 131 134 134 PHE PHE B . n 
B 1 132 GLY 132 135 135 GLY GLY B . n 
B 1 133 ASN 133 136 136 ASN ASN B . n 
B 1 134 ASN 134 137 137 ASN ASN B . n 
B 1 135 HIS 135 138 138 HIS HIS B . n 
B 1 136 ASP 136 139 139 ASP ASP B . n 
B 1 137 PHE 137 140 140 PHE PHE B . n 
B 1 138 ASN 138 141 141 ASN ASN B . n 
B 1 139 GLU 139 142 142 GLU GLU B . n 
B 1 140 THR 140 143 143 THR THR B . n 
B 1 141 LEU 141 144 144 LEU LEU B . n 
B 1 142 PHE 142 145 145 PHE PHE B . n 
B 1 143 GLU 143 146 146 GLU GLU B . n 
B 1 144 GLN 144 147 147 GLN GLN B . n 
B 1 145 LEU 145 148 148 LEU LEU B . n 
B 1 146 VAL 146 149 149 VAL VAL B . n 
B 1 147 ASP 147 150 150 ASP ASP B . n 
B 1 148 TYR 148 151 151 TYR TYR B . n 
B 1 149 SER 149 152 152 SER SER B . n 
B 1 150 ASN 150 153 153 ASN ASN B . n 
B 1 151 ARG 151 154 154 ARG ARG B . n 
B 1 152 PHE 152 155 155 PHE PHE B . n 
B 1 153 GLY 153 156 156 GLY GLY B . n 
B 1 154 GLY 154 157 157 GLY GLY B . n 
B 1 155 GLY 155 158 158 GLY GLY B . n 
B 1 156 LYS 156 159 159 LYS LYS B . n 
B 1 157 TYR 157 160 160 TYR TYR B . n 
B 1 158 ASN 158 161 161 ASN ASN B . n 
B 1 159 LEU 159 162 162 LEU LEU B . n 
B 1 160 THR 160 163 163 THR THR B . n 
B 1 161 VAL 161 164 164 VAL VAL B . n 
B 1 162 ALA 162 165 165 ALA ALA B . n 
B 1 163 GLY 163 166 166 GLY GLY B . n 
B 1 164 GLU 164 167 167 GLU GLU B . n 
B 1 165 LEU 165 168 168 LEU LEU B . n 
B 1 166 ARG 166 169 169 ARG ARG B . n 
B 1 167 PHE 167 170 170 PHE PHE B . n 
B 1 168 LYS 168 171 171 LYS LYS B . n 
B 1 169 ARG 169 172 172 ARG ARG B . n 
B 1 170 ILE 170 173 173 ILE ILE B . n 
B 1 171 GLN 171 174 174 GLN GLN B . n 
B 1 172 ASP 172 175 175 ASP ASP B . n 
B 1 173 SER 173 176 176 SER SER B . n 
B 1 174 ILE 174 177 177 ILE ILE B . n 
B 1 175 ALA 175 178 178 ALA ALA B . n 
B 1 176 THR 176 179 179 THR THR B . n 
B 1 177 ASN 177 180 180 ASN ASN B . n 
B 1 178 PRO 178 181 181 PRO PRO B . n 
B 1 179 ASN 179 182 182 ASN ASN B . n 
B 1 180 PHE 180 183 183 PHE PHE B . n 
B 1 181 SER 181 184 184 SER SER B . n 
B 1 182 PHE 182 185 185 PHE PHE B . n 
B 1 183 VAL 183 186 186 VAL VAL B . n 
B 1 184 ASP 184 187 187 ASP ASP B . n 
B 1 185 PHE 185 188 188 PHE PHE B . n 
B 1 186 ARG 186 189 189 ARG ARG B . n 
B 1 187 PHE 187 190 190 PHE PHE B . n 
B 1 188 PHE 188 191 191 PHE PHE B . n 
B 1 189 THR 189 192 192 THR THR B . n 
B 1 190 ALA 190 193 193 ALA ALA B . n 
B 1 191 TYR 191 194 194 TYR TYR B . n 
B 1 192 GLY 192 195 195 GLY GLY B . n 
B 1 193 GLU 193 196 196 GLU GLU B . n 
B 1 194 THR 194 197 197 THR THR B . n 
B 1 195 THR 195 198 198 THR THR B . n 
B 1 196 PHE 196 199 199 PHE PHE B . n 
B 1 197 PRO 197 200 200 PRO PRO B . n 
B 1 198 ALA 198 201 201 ALA ALA B . n 
B 1 199 ASN 199 202 202 ASN ASN B . n 
B 1 200 LEU 200 203 203 LEU LEU B . n 
B 1 201 PHE 201 204 204 PHE PHE B . n 
B 1 202 VAL 202 205 205 VAL VAL B . n 
B 1 203 ASP 203 206 206 ASP ASP B . n 
B 1 204 GLY 204 207 207 GLY GLY B . n 
B 1 205 ARG 205 208 208 ARG ARG B . n 
B 1 206 ARG 206 209 209 ARG ARG B . n 
B 1 207 ASP 207 210 210 ASP ASP B . n 
B 1 208 ASP 208 211 211 ASP ASP B . n 
B 1 209 GLY 209 212 212 GLY GLY B . n 
B 1 210 GLN 210 213 213 GLN GLN B . n 
B 1 211 LEU 211 214 214 LEU LEU B . n 
B 1 212 ASP 212 215 215 ASP ASP B . n 
B 1 213 MET 213 216 216 MET MET B . n 
B 1 214 ASP 214 217 217 ASP ASP B . n 
B 1 215 ALA 215 218 218 ALA ALA B . n 
B 1 216 ALA 216 219 219 ALA ALA B . n 
B 1 217 ARG 217 220 220 ARG ARG B . n 
B 1 218 SER 218 221 221 SER SER B . n 
B 1 219 PHE 219 222 222 PHE PHE B . n 
B 1 220 PHE 220 223 223 PHE PHE B . n 
B 1 221 GLN 221 224 224 GLN GLN B . n 
B 1 222 PHE 222 225 225 PHE PHE B . n 
B 1 223 SER 223 226 226 SER SER B . n 
B 1 224 ARG 224 227 227 ARG ARG B . n 
B 1 225 MET 225 228 228 MET MET B . n 
B 1 226 PRO 226 229 229 PRO PRO B . n 
B 1 227 ASP 227 230 230 ASP ASP B . n 
B 1 228 ASP 228 231 231 ASP ASP B . n 
B 1 229 PHE 229 232 232 PHE PHE B . n 
B 1 230 PHE 230 233 233 PHE PHE B . n 
B 1 231 ARG 231 234 234 ARG ARG B . n 
B 1 232 ALA 232 235 235 ALA ALA B . n 
B 1 233 PRO 233 236 236 PRO PRO B . n 
B 1 234 SER 234 237 237 SER SER B . n 
B 1 235 PRO 235 238 238 PRO PRO B . n 
B 1 236 ARG 236 239 239 ARG ARG B . n 
B 1 237 SER 237 240 240 SER SER B . n 
B 1 238 GLY 238 241 241 GLY GLY B . n 
B 1 239 THR 239 242 242 THR THR B . n 
B 1 240 GLY 240 243 243 GLY GLY B . n 
B 1 241 VAL 241 244 244 VAL VAL B . n 
B 1 242 GLU 242 245 245 GLU GLU B . n 
B 1 243 VAL 243 246 246 VAL VAL B . n 
B 1 244 VAL 244 247 247 VAL VAL B . n 
B 1 245 ILE 245 248 248 ILE ILE B . n 
B 1 246 GLN 246 249 249 GLN GLN B . n 
B 1 247 ALA 247 250 250 ALA ALA B . n 
B 1 248 HIS 248 251 251 HIS HIS B . n 
B 1 249 PRO 249 252 252 PRO PRO B . n 
B 1 250 MET 250 253 253 MET MET B . n 
B 1 251 GLN 251 254 254 GLN GLN B . n 
B 1 252 PRO 252 255 255 PRO PRO B . n 
B 1 253 GLY 253 256 256 GLY GLY B . n 
B 1 254 ARG 254 257 257 ARG ARG B . n 
B 1 255 ASN 255 258 258 ASN ASN B . n 
B 1 256 VAL 256 259 259 VAL VAL B . n 
B 1 257 GLY 257 260 260 GLY GLY B . n 
B 1 258 LYS 258 261 261 LYS LYS B . n 
B 1 259 ILE 259 262 262 ILE ILE B . n 
B 1 260 ASN 260 263 263 ASN ASN B . n 
B 1 261 SER 261 264 264 SER SER B . n 
B 1 262 TYR 262 265 265 TYR TYR B . n 
B 1 263 THR 263 266 266 THR THR B . n 
B 1 264 VAL 264 267 267 VAL VAL B . n 
B 1 265 ASP 265 268 268 ASP ASP B . n 
B 1 266 PRO 266 269 269 PRO PRO B . n 
B 1 267 THR 267 270 270 THR THR B . n 
B 1 268 SER 268 271 271 SER SER B . n 
B 1 269 SER 269 272 272 SER SER B . n 
B 1 270 ASP 270 273 273 ASP ASP B . n 
B 1 271 PHE 271 274 274 PHE PHE B . n 
B 1 272 SER 272 275 275 SER SER B . n 
B 1 273 THR 273 276 276 THR THR B . n 
B 1 274 PRO 274 277 277 PRO PRO B . n 
B 1 275 CYS 275 278 278 CYS CYS B . n 
B 1 276 LEU 276 279 279 LEU LEU B . n 
B 1 277 MET 277 280 280 MET MET B . n 
B 1 278 TYR 278 281 281 TYR TYR B . n 
B 1 279 GLU 279 282 282 GLU GLU B . n 
B 1 280 LYS 280 283 283 LYS LYS B . n 
B 1 281 PHE 281 284 284 PHE PHE B . n 
B 1 282 VAL 282 285 285 VAL VAL B . n 
B 1 283 ASN 283 286 286 ASN ASN B . n 
B 1 284 ILE 284 287 287 ILE ILE B . n 
B 1 285 THR 285 288 288 THR THR B . n 
B 1 286 VAL 286 289 289 VAL VAL B . n 
B 1 287 LYS 287 290 290 LYS LYS B . n 
B 1 288 SER 288 291 291 SER SER B . n 
B 1 289 LEU 289 292 292 LEU LEU B . n 
B 1 290 TYR 290 293 293 TYR TYR B . n 
B 1 291 PRO 291 294 294 PRO PRO B . n 
B 1 292 ASN 292 295 295 ASN ASN B . n 
B 1 293 PRO 293 296 296 PRO PRO B . n 
B 1 294 THR 294 297 297 THR THR B . n 
B 1 295 VAL 295 298 298 VAL VAL B . n 
B 1 296 GLN 296 299 299 GLN GLN B . n 
B 1 297 LEU 297 300 300 LEU LEU B . n 
B 1 298 ARG 298 301 301 ARG ARG B . n 
B 1 299 LYS 299 302 302 LYS LYS B . n 
B 1 300 ALA 300 303 303 ALA ALA B . n 
B 1 301 LEU 301 304 304 LEU LEU B . n 
B 1 302 ASN 302 305 305 ASN ASN B . n 
B 1 303 THR 303 306 306 THR THR B . n 
B 1 304 ASN 304 307 307 ASN ASN B . n 
B 1 305 LEU 305 308 308 LEU LEU B . n 
B 1 306 ASP 306 309 309 ASP ASP B . n 
B 1 307 PHE 307 310 310 PHE PHE B . n 
B 1 308 PHE 308 311 311 PHE PHE B . n 
B 1 309 PHE 309 312 312 PHE PHE B . n 
B 1 310 GLN 310 313 313 GLN GLN B . n 
B 1 311 GLY 311 314 314 GLY GLY B . n 
B 1 312 VAL 312 315 315 VAL VAL B . n 
B 1 313 ALA 313 316 316 ALA ALA B . n 
B 1 314 ALA 314 317 317 ALA ALA B . n 
B 1 315 GLY 315 318 318 GLY GLY B . n 
B 1 316 CYS 316 319 319 CYS CYS B . n 
B 1 317 THR 317 320 320 THR THR B . n 
B 1 318 GLN 318 321 321 GLN GLN B . n 
B 1 319 VAL 319 322 322 VAL VAL B . n 
B 1 320 PHE 320 323 323 PHE PHE B . n 
B 1 321 PRO 321 324 324 PRO PRO B . n 
B 1 322 TYR 322 325 325 TYR TYR B . n 
B 1 323 GLY 323 326 326 GLY GLY B . n 
B 1 324 ARG 324 327 327 ARG ARG B . n 
B 1 325 ASP 325 328 ?   ?   ?   B . n 
C 1 1   LEU 1   4   4   LEU LEU C . n 
C 1 2   PRO 2   5   5   PRO PRO C . n 
C 1 3   PRO 3   6   6   PRO PRO C . n 
C 1 4   GLY 4   7   7   GLY GLY C . n 
C 1 5   PRO 5   8   8   PRO PRO C . n 
C 1 6   LEU 6   9   9   LEU LEU C . n 
C 1 7   GLU 7   10  10  GLU GLU C . n 
C 1 8   ASN 8   11  11  ASN ASN C . n 
C 1 9   SER 9   12  12  SER SER C . n 
C 1 10  SER 10  13  13  SER SER C . n 
C 1 11  ALA 11  14  14  ALA ALA C . n 
C 1 12  LYS 12  15  15  LYS LYS C . n 
C 1 13  LEU 13  16  16  LEU LEU C . n 
C 1 14  VAL 14  17  17  VAL VAL C . n 
C 1 15  ASN 15  18  18  ASN ASN C . n 
C 1 16  ASP 16  19  19  ASP ASP C . n 
C 1 17  GLU 17  20  20  GLU GLU C . n 
C 1 18  ALA 18  21  21  ALA ALA C . n 
C 1 19  HIS 19  22  22  HIS HIS C . n 
C 1 20  PRO 20  23  23  PRO PRO C . n 
C 1 21  TRP 21  24  24  TRP TRP C . n 
C 1 22  LYS 22  25  25  LYS LYS C . n 
C 1 23  PRO 23  26  26  PRO PRO C . n 
C 1 24  LEU 24  27  27  LEU LEU C . n 
C 1 25  ARG 25  28  28  ARG ARG C . n 
C 1 26  PRO 26  29  29  PRO PRO C . n 
C 1 27  GLY 27  30  30  GLY GLY C . n 
C 1 28  ASP 28  31  31  ASP ASP C . n 
C 1 29  ILE 29  32  32  ILE ILE C . n 
C 1 30  ARG 30  33  33  ARG ARG C . n 
C 1 31  GLY 31  34  34  GLY GLY C . n 
C 1 32  PRO 32  35  35  PRO PRO C . n 
C 1 33  CYS 33  36  36  CYS CYS C . n 
C 1 34  PRO 34  37  37  PRO PRO C . n 
C 1 35  GLY 35  38  38  GLY GLY C . n 
C 1 36  LEU 36  39  39  LEU LEU C . n 
C 1 37  ASN 37  40  40  ASN ASN C . n 
C 1 38  THR 38  41  41  THR THR C . n 
C 1 39  LEU 39  42  42  LEU LEU C . n 
C 1 40  ALA 40  43  43  ALA ALA C . n 
C 1 41  SER 41  44  44  SER SER C . n 
C 1 42  HIS 42  45  45  HIS HIS C . n 
C 1 43  GLY 43  46  46  GLY GLY C . n 
C 1 44  TYR 44  47  47  TYR TYR C . n 
C 1 45  LEU 45  48  48  LEU LEU C . n 
C 1 46  PRO 46  49  49  PRO PRO C . n 
C 1 47  ARG 47  50  50  ARG ARG C . n 
C 1 48  ASN 48  51  51  ASN ASN C . n 
C 1 49  GLY 49  52  52  GLY GLY C . n 
C 1 50  VAL 50  53  53  VAL VAL C . n 
C 1 51  ALA 51  54  54  ALA ALA C . n 
C 1 52  THR 52  55  55  THR THR C . n 
C 1 53  PRO 53  56  56  PRO PRO C . n 
C 1 54  VAL 54  57  57  VAL VAL C . n 
C 1 55  GLN 55  58  58  GLN GLN C . n 
C 1 56  ILE 56  59  59  ILE ILE C . n 
C 1 57  ILE 57  60  60  ILE ILE C . n 
C 1 58  ASN 58  61  61  ASN ASN C . n 
C 1 59  ALA 59  62  62  ALA ALA C . n 
C 1 60  VAL 60  63  63  VAL VAL C . n 
C 1 61  GLN 61  64  64  GLN GLN C . n 
C 1 62  GLU 62  65  65  GLU GLU C . n 
C 1 63  GLY 63  66  66  GLY GLY C . n 
C 1 64  LEU 64  67  67  LEU LEU C . n 
C 1 65  ASN 65  68  68  ASN ASN C . n 
C 1 66  PHE 66  69  69  PHE PHE C . n 
C 1 67  ASP 67  70  70  ASP ASP C . n 
C 1 68  ASN 68  71  71  ASN ASN C . n 
C 1 69  GLN 69  72  72  GLN GLN C . n 
C 1 70  ALA 70  73  73  ALA ALA C . n 
C 1 71  ALA 71  74  74  ALA ALA C . n 
C 1 72  VAL 72  75  75  VAL VAL C . n 
C 1 73  PHE 73  76  76  PHE PHE C . n 
C 1 74  ALA 74  77  77  ALA ALA C . n 
C 1 75  THR 75  78  78  THR THR C . n 
C 1 76  TYR 76  79  79  TYR TYR C . n 
C 1 77  ALA 77  80  80  ALA ALA C . n 
C 1 78  ALA 78  81  81  ALA ALA C . n 
C 1 79  HIS 79  82  82  HIS HIS C . n 
C 1 80  LEU 80  83  83  LEU LEU C . n 
C 1 81  VAL 81  84  84  VAL VAL C . n 
C 1 82  ASP 82  85  85  ASP ASP C . n 
C 1 83  GLY 83  86  86  GLY GLY C . n 
C 1 84  ASN 84  87  87  ASN ASN C . n 
C 1 85  LEU 85  88  88  LEU LEU C . n 
C 1 86  ILE 86  89  89  ILE ILE C . n 
C 1 87  THR 87  90  90  THR THR C . n 
C 1 88  ASP 88  91  91  ASP ASP C . n 
C 1 89  LEU 89  92  92  LEU LEU C . n 
C 1 90  LEU 90  93  93  LEU LEU C . n 
C 1 91  SER 91  94  94  SER SER C . n 
C 1 92  ILE 92  95  95  ILE ILE C . n 
C 1 93  GLY 93  96  96  GLY GLY C . n 
C 1 94  ARG 94  97  97  ARG ARG C . n 
C 1 95  LYS 95  98  98  LYS LYS C . n 
C 1 96  THR 96  99  99  THR THR C . n 
C 1 97  ARG 97  100 100 ARG ARG C . n 
C 1 98  LEU 98  101 101 LEU LEU C . n 
C 1 99  THR 99  102 102 THR THR C . n 
C 1 100 GLY 100 103 103 GLY GLY C . n 
C 1 101 PRO 101 104 104 PRO PRO C . n 
C 1 102 ASP 102 105 105 ASP ASP C . n 
C 1 103 PRO 103 106 106 PRO PRO C . n 
C 1 104 PRO 104 107 107 PRO PRO C . n 
C 1 105 PRO 105 108 108 PRO PRO C . n 
C 1 106 PRO 106 109 109 PRO PRO C . n 
C 1 107 ALA 107 110 110 ALA ALA C . n 
C 1 108 SER 108 111 111 SER SER C . n 
C 1 109 VAL 109 112 112 VAL VAL C . n 
C 1 110 GLY 110 113 113 GLY GLY C . n 
C 1 111 GLY 111 114 114 GLY GLY C . n 
C 1 112 LEU 112 115 115 LEU LEU C . n 
C 1 113 ASN 113 116 116 ASN ASN C . n 
C 1 114 GLU 114 117 117 GLU GLU C . n 
C 1 115 HIS 115 118 118 HIS HIS C . n 
C 1 116 GLY 116 119 119 GLY GLY C . n 
C 1 117 THR 117 120 120 THR THR C . n 
C 1 118 PHE 118 121 121 PHE PHE C . n 
C 1 119 GLU 119 122 122 GLU GLU C . n 
C 1 120 GLY 120 123 123 GLY GLY C . n 
C 1 121 ASP 121 124 124 ASP ASP C . n 
C 1 122 ALA 122 125 125 ALA ALA C . n 
C 1 123 SER 123 126 126 SER SER C . n 
C 1 124 MET 124 127 127 MET MET C . n 
C 1 125 THR 125 128 128 THR THR C . n 
C 1 126 ARG 126 129 129 ARG ARG C . n 
C 1 127 GLY 127 130 130 GLY GLY C . n 
C 1 128 ASP 128 131 131 ASP ASP C . n 
C 1 129 ALA 129 132 132 ALA ALA C . n 
C 1 130 PHE 130 133 133 PHE PHE C . n 
C 1 131 PHE 131 134 134 PHE PHE C . n 
C 1 132 GLY 132 135 135 GLY GLY C . n 
C 1 133 ASN 133 136 136 ASN ASN C . n 
C 1 134 ASN 134 137 137 ASN ASN C . n 
C 1 135 HIS 135 138 138 HIS HIS C . n 
C 1 136 ASP 136 139 139 ASP ASP C . n 
C 1 137 PHE 137 140 140 PHE PHE C . n 
C 1 138 ASN 138 141 141 ASN ASN C . n 
C 1 139 GLU 139 142 142 GLU GLU C . n 
C 1 140 THR 140 143 143 THR THR C . n 
C 1 141 LEU 141 144 144 LEU LEU C . n 
C 1 142 PHE 142 145 145 PHE PHE C . n 
C 1 143 GLU 143 146 146 GLU GLU C . n 
C 1 144 GLN 144 147 147 GLN GLN C . n 
C 1 145 LEU 145 148 148 LEU LEU C . n 
C 1 146 VAL 146 149 149 VAL VAL C . n 
C 1 147 ASP 147 150 150 ASP ASP C . n 
C 1 148 TYR 148 151 151 TYR TYR C . n 
C 1 149 SER 149 152 152 SER SER C . n 
C 1 150 ASN 150 153 153 ASN ASN C . n 
C 1 151 ARG 151 154 154 ARG ARG C . n 
C 1 152 PHE 152 155 155 PHE PHE C . n 
C 1 153 GLY 153 156 156 GLY GLY C . n 
C 1 154 GLY 154 157 157 GLY GLY C . n 
C 1 155 GLY 155 158 158 GLY GLY C . n 
C 1 156 LYS 156 159 159 LYS LYS C . n 
C 1 157 TYR 157 160 160 TYR TYR C . n 
C 1 158 ASN 158 161 161 ASN ASN C . n 
C 1 159 LEU 159 162 162 LEU LEU C . n 
C 1 160 THR 160 163 163 THR THR C . n 
C 1 161 VAL 161 164 164 VAL VAL C . n 
C 1 162 ALA 162 165 165 ALA ALA C . n 
C 1 163 GLY 163 166 166 GLY GLY C . n 
C 1 164 GLU 164 167 167 GLU GLU C . n 
C 1 165 LEU 165 168 168 LEU LEU C . n 
C 1 166 ARG 166 169 169 ARG ARG C . n 
C 1 167 PHE 167 170 170 PHE PHE C . n 
C 1 168 LYS 168 171 171 LYS LYS C . n 
C 1 169 ARG 169 172 172 ARG ARG C . n 
C 1 170 ILE 170 173 173 ILE ILE C . n 
C 1 171 GLN 171 174 174 GLN GLN C . n 
C 1 172 ASP 172 175 175 ASP ASP C . n 
C 1 173 SER 173 176 176 SER SER C . n 
C 1 174 ILE 174 177 177 ILE ILE C . n 
C 1 175 ALA 175 178 178 ALA ALA C . n 
C 1 176 THR 176 179 179 THR THR C . n 
C 1 177 ASN 177 180 180 ASN ASN C . n 
C 1 178 PRO 178 181 181 PRO PRO C . n 
C 1 179 ASN 179 182 182 ASN ASN C . n 
C 1 180 PHE 180 183 183 PHE PHE C . n 
C 1 181 SER 181 184 184 SER SER C . n 
C 1 182 PHE 182 185 185 PHE PHE C . n 
C 1 183 VAL 183 186 186 VAL VAL C . n 
C 1 184 ASP 184 187 187 ASP ASP C . n 
C 1 185 PHE 185 188 188 PHE PHE C . n 
C 1 186 ARG 186 189 189 ARG ARG C . n 
C 1 187 PHE 187 190 190 PHE PHE C . n 
C 1 188 PHE 188 191 191 PHE PHE C . n 
C 1 189 THR 189 192 192 THR THR C . n 
C 1 190 ALA 190 193 193 ALA ALA C . n 
C 1 191 TYR 191 194 194 TYR TYR C . n 
C 1 192 GLY 192 195 195 GLY GLY C . n 
C 1 193 GLU 193 196 196 GLU GLU C . n 
C 1 194 THR 194 197 197 THR THR C . n 
C 1 195 THR 195 198 198 THR THR C . n 
C 1 196 PHE 196 199 199 PHE PHE C . n 
C 1 197 PRO 197 200 200 PRO PRO C . n 
C 1 198 ALA 198 201 201 ALA ALA C . n 
C 1 199 ASN 199 202 202 ASN ASN C . n 
C 1 200 LEU 200 203 203 LEU LEU C . n 
C 1 201 PHE 201 204 204 PHE PHE C . n 
C 1 202 VAL 202 205 205 VAL VAL C . n 
C 1 203 ASP 203 206 206 ASP ASP C . n 
C 1 204 GLY 204 207 207 GLY GLY C . n 
C 1 205 ARG 205 208 208 ARG ARG C . n 
C 1 206 ARG 206 209 209 ARG ARG C . n 
C 1 207 ASP 207 210 210 ASP ASP C . n 
C 1 208 ASP 208 211 211 ASP ASP C . n 
C 1 209 GLY 209 212 212 GLY GLY C . n 
C 1 210 GLN 210 213 213 GLN GLN C . n 
C 1 211 LEU 211 214 214 LEU LEU C . n 
C 1 212 ASP 212 215 215 ASP ASP C . n 
C 1 213 MET 213 216 216 MET MET C . n 
C 1 214 ASP 214 217 217 ASP ASP C . n 
C 1 215 ALA 215 218 218 ALA ALA C . n 
C 1 216 ALA 216 219 219 ALA ALA C . n 
C 1 217 ARG 217 220 220 ARG ARG C . n 
C 1 218 SER 218 221 221 SER SER C . n 
C 1 219 PHE 219 222 222 PHE PHE C . n 
C 1 220 PHE 220 223 223 PHE PHE C . n 
C 1 221 GLN 221 224 224 GLN GLN C . n 
C 1 222 PHE 222 225 225 PHE PHE C . n 
C 1 223 SER 223 226 226 SER SER C . n 
C 1 224 ARG 224 227 227 ARG ARG C . n 
C 1 225 MET 225 228 228 MET MET C . n 
C 1 226 PRO 226 229 229 PRO PRO C . n 
C 1 227 ASP 227 230 230 ASP ASP C . n 
C 1 228 ASP 228 231 231 ASP ASP C . n 
C 1 229 PHE 229 232 232 PHE PHE C . n 
C 1 230 PHE 230 233 233 PHE PHE C . n 
C 1 231 ARG 231 234 234 ARG ARG C . n 
C 1 232 ALA 232 235 235 ALA ALA C . n 
C 1 233 PRO 233 236 236 PRO PRO C . n 
C 1 234 SER 234 237 237 SER SER C . n 
C 1 235 PRO 235 238 238 PRO PRO C . n 
C 1 236 ARG 236 239 239 ARG ARG C . n 
C 1 237 SER 237 240 240 SER SER C . n 
C 1 238 GLY 238 241 241 GLY GLY C . n 
C 1 239 THR 239 242 242 THR THR C . n 
C 1 240 GLY 240 243 243 GLY GLY C . n 
C 1 241 VAL 241 244 244 VAL VAL C . n 
C 1 242 GLU 242 245 245 GLU GLU C . n 
C 1 243 VAL 243 246 246 VAL VAL C . n 
C 1 244 VAL 244 247 247 VAL VAL C . n 
C 1 245 ILE 245 248 248 ILE ILE C . n 
C 1 246 GLN 246 249 249 GLN GLN C . n 
C 1 247 ALA 247 250 250 ALA ALA C . n 
C 1 248 HIS 248 251 251 HIS HIS C . n 
C 1 249 PRO 249 252 252 PRO PRO C . n 
C 1 250 MET 250 253 253 MET MET C . n 
C 1 251 GLN 251 254 254 GLN GLN C . n 
C 1 252 PRO 252 255 255 PRO PRO C . n 
C 1 253 GLY 253 256 256 GLY GLY C . n 
C 1 254 ARG 254 257 257 ARG ARG C . n 
C 1 255 ASN 255 258 258 ASN ASN C . n 
C 1 256 VAL 256 259 259 VAL VAL C . n 
C 1 257 GLY 257 260 260 GLY GLY C . n 
C 1 258 LYS 258 261 261 LYS LYS C . n 
C 1 259 ILE 259 262 262 ILE ILE C . n 
C 1 260 ASN 260 263 263 ASN ASN C . n 
C 1 261 SER 261 264 264 SER SER C . n 
C 1 262 TYR 262 265 265 TYR TYR C . n 
C 1 263 THR 263 266 266 THR THR C . n 
C 1 264 VAL 264 267 267 VAL VAL C . n 
C 1 265 ASP 265 268 268 ASP ASP C . n 
C 1 266 PRO 266 269 269 PRO PRO C . n 
C 1 267 THR 267 270 270 THR THR C . n 
C 1 268 SER 268 271 271 SER SER C . n 
C 1 269 SER 269 272 272 SER SER C . n 
C 1 270 ASP 270 273 273 ASP ASP C . n 
C 1 271 PHE 271 274 274 PHE PHE C . n 
C 1 272 SER 272 275 275 SER SER C . n 
C 1 273 THR 273 276 276 THR THR C . n 
C 1 274 PRO 274 277 277 PRO PRO C . n 
C 1 275 CYS 275 278 278 CYS CYS C . n 
C 1 276 LEU 276 279 279 LEU LEU C . n 
C 1 277 MET 277 280 280 MET MET C . n 
C 1 278 TYR 278 281 281 TYR TYR C . n 
C 1 279 GLU 279 282 282 GLU GLU C . n 
C 1 280 LYS 280 283 283 LYS LYS C . n 
C 1 281 PHE 281 284 284 PHE PHE C . n 
C 1 282 VAL 282 285 285 VAL VAL C . n 
C 1 283 ASN 283 286 286 ASN ASN C . n 
C 1 284 ILE 284 287 287 ILE ILE C . n 
C 1 285 THR 285 288 288 THR THR C . n 
C 1 286 VAL 286 289 289 VAL VAL C . n 
C 1 287 LYS 287 290 290 LYS LYS C . n 
C 1 288 SER 288 291 291 SER SER C . n 
C 1 289 LEU 289 292 292 LEU LEU C . n 
C 1 290 TYR 290 293 293 TYR TYR C . n 
C 1 291 PRO 291 294 294 PRO PRO C . n 
C 1 292 ASN 292 295 295 ASN ASN C . n 
C 1 293 PRO 293 296 296 PRO PRO C . n 
C 1 294 THR 294 297 297 THR THR C . n 
C 1 295 VAL 295 298 298 VAL VAL C . n 
C 1 296 GLN 296 299 299 GLN GLN C . n 
C 1 297 LEU 297 300 300 LEU LEU C . n 
C 1 298 ARG 298 301 301 ARG ARG C . n 
C 1 299 LYS 299 302 302 LYS LYS C . n 
C 1 300 ALA 300 303 303 ALA ALA C . n 
C 1 301 LEU 301 304 304 LEU LEU C . n 
C 1 302 ASN 302 305 305 ASN ASN C . n 
C 1 303 THR 303 306 306 THR THR C . n 
C 1 304 ASN 304 307 307 ASN ASN C . n 
C 1 305 LEU 305 308 308 LEU LEU C . n 
C 1 306 ASP 306 309 309 ASP ASP C . n 
C 1 307 PHE 307 310 310 PHE PHE C . n 
C 1 308 PHE 308 311 311 PHE PHE C . n 
C 1 309 PHE 309 312 312 PHE PHE C . n 
C 1 310 GLN 310 313 313 GLN GLN C . n 
C 1 311 GLY 311 314 314 GLY GLY C . n 
C 1 312 VAL 312 315 315 VAL VAL C . n 
C 1 313 ALA 313 316 316 ALA ALA C . n 
C 1 314 ALA 314 317 317 ALA ALA C . n 
C 1 315 GLY 315 318 318 GLY GLY C . n 
C 1 316 CYS 316 319 319 CYS CYS C . n 
C 1 317 THR 317 320 320 THR THR C . n 
C 1 318 GLN 318 321 321 GLN GLN C . n 
C 1 319 VAL 319 322 322 VAL VAL C . n 
C 1 320 PHE 320 323 323 PHE PHE C . n 
C 1 321 PRO 321 324 324 PRO PRO C . n 
C 1 322 TYR 322 325 325 TYR TYR C . n 
C 1 323 GLY 323 326 326 GLY GLY C . n 
C 1 324 ARG 324 327 327 ARG ARG C . n 
C 1 325 ASP 325 328 328 ASP ASP C . n 
D 1 1   LEU 1   4   4   LEU LEU D . n 
D 1 2   PRO 2   5   5   PRO PRO D . n 
D 1 3   PRO 3   6   6   PRO PRO D . n 
D 1 4   GLY 4   7   7   GLY GLY D . n 
D 1 5   PRO 5   8   8   PRO PRO D . n 
D 1 6   LEU 6   9   9   LEU LEU D . n 
D 1 7   GLU 7   10  10  GLU GLU D . n 
D 1 8   ASN 8   11  11  ASN ASN D . n 
D 1 9   SER 9   12  12  SER SER D . n 
D 1 10  SER 10  13  13  SER SER D . n 
D 1 11  ALA 11  14  14  ALA ALA D . n 
D 1 12  LYS 12  15  15  LYS LYS D . n 
D 1 13  LEU 13  16  16  LEU LEU D . n 
D 1 14  VAL 14  17  17  VAL VAL D . n 
D 1 15  ASN 15  18  18  ASN ASN D . n 
D 1 16  ASP 16  19  19  ASP ASP D . n 
D 1 17  GLU 17  20  20  GLU GLU D . n 
D 1 18  ALA 18  21  21  ALA ALA D . n 
D 1 19  HIS 19  22  22  HIS HIS D . n 
D 1 20  PRO 20  23  23  PRO PRO D . n 
D 1 21  TRP 21  24  24  TRP TRP D . n 
D 1 22  LYS 22  25  25  LYS LYS D . n 
D 1 23  PRO 23  26  26  PRO PRO D . n 
D 1 24  LEU 24  27  27  LEU LEU D . n 
D 1 25  ARG 25  28  28  ARG ARG D . n 
D 1 26  PRO 26  29  29  PRO PRO D . n 
D 1 27  GLY 27  30  30  GLY GLY D . n 
D 1 28  ASP 28  31  31  ASP ASP D . n 
D 1 29  ILE 29  32  32  ILE ILE D . n 
D 1 30  ARG 30  33  33  ARG ARG D . n 
D 1 31  GLY 31  34  34  GLY GLY D . n 
D 1 32  PRO 32  35  35  PRO PRO D . n 
D 1 33  CYS 33  36  36  CYS CYS D . n 
D 1 34  PRO 34  37  37  PRO PRO D . n 
D 1 35  GLY 35  38  38  GLY GLY D . n 
D 1 36  LEU 36  39  39  LEU LEU D . n 
D 1 37  ASN 37  40  40  ASN ASN D . n 
D 1 38  THR 38  41  41  THR THR D . n 
D 1 39  LEU 39  42  42  LEU LEU D . n 
D 1 40  ALA 40  43  43  ALA ALA D . n 
D 1 41  SER 41  44  44  SER SER D . n 
D 1 42  HIS 42  45  45  HIS HIS D . n 
D 1 43  GLY 43  46  46  GLY GLY D . n 
D 1 44  TYR 44  47  47  TYR TYR D . n 
D 1 45  LEU 45  48  48  LEU LEU D . n 
D 1 46  PRO 46  49  49  PRO PRO D . n 
D 1 47  ARG 47  50  50  ARG ARG D . n 
D 1 48  ASN 48  51  51  ASN ASN D . n 
D 1 49  GLY 49  52  52  GLY GLY D . n 
D 1 50  VAL 50  53  53  VAL VAL D . n 
D 1 51  ALA 51  54  54  ALA ALA D . n 
D 1 52  THR 52  55  55  THR THR D . n 
D 1 53  PRO 53  56  56  PRO PRO D . n 
D 1 54  VAL 54  57  57  VAL VAL D . n 
D 1 55  GLN 55  58  58  GLN GLN D . n 
D 1 56  ILE 56  59  59  ILE ILE D . n 
D 1 57  ILE 57  60  60  ILE ILE D . n 
D 1 58  ASN 58  61  61  ASN ASN D . n 
D 1 59  ALA 59  62  62  ALA ALA D . n 
D 1 60  VAL 60  63  63  VAL VAL D . n 
D 1 61  GLN 61  64  64  GLN GLN D . n 
D 1 62  GLU 62  65  65  GLU GLU D . n 
D 1 63  GLY 63  66  66  GLY GLY D . n 
D 1 64  LEU 64  67  67  LEU LEU D . n 
D 1 65  ASN 65  68  68  ASN ASN D . n 
D 1 66  PHE 66  69  69  PHE PHE D . n 
D 1 67  ASP 67  70  70  ASP ASP D . n 
D 1 68  ASN 68  71  71  ASN ASN D . n 
D 1 69  GLN 69  72  72  GLN GLN D . n 
D 1 70  ALA 70  73  73  ALA ALA D . n 
D 1 71  ALA 71  74  74  ALA ALA D . n 
D 1 72  VAL 72  75  75  VAL VAL D . n 
D 1 73  PHE 73  76  76  PHE PHE D . n 
D 1 74  ALA 74  77  77  ALA ALA D . n 
D 1 75  THR 75  78  78  THR THR D . n 
D 1 76  TYR 76  79  79  TYR TYR D . n 
D 1 77  ALA 77  80  80  ALA ALA D . n 
D 1 78  ALA 78  81  81  ALA ALA D . n 
D 1 79  HIS 79  82  82  HIS HIS D . n 
D 1 80  LEU 80  83  83  LEU LEU D . n 
D 1 81  VAL 81  84  84  VAL VAL D . n 
D 1 82  ASP 82  85  85  ASP ASP D . n 
D 1 83  GLY 83  86  86  GLY GLY D . n 
D 1 84  ASN 84  87  87  ASN ASN D . n 
D 1 85  LEU 85  88  88  LEU LEU D . n 
D 1 86  ILE 86  89  89  ILE ILE D . n 
D 1 87  THR 87  90  90  THR THR D . n 
D 1 88  ASP 88  91  91  ASP ASP D . n 
D 1 89  LEU 89  92  92  LEU LEU D . n 
D 1 90  LEU 90  93  93  LEU LEU D . n 
D 1 91  SER 91  94  94  SER SER D . n 
D 1 92  ILE 92  95  95  ILE ILE D . n 
D 1 93  GLY 93  96  96  GLY GLY D . n 
D 1 94  ARG 94  97  97  ARG ARG D . n 
D 1 95  LYS 95  98  98  LYS LYS D . n 
D 1 96  THR 96  99  99  THR THR D . n 
D 1 97  ARG 97  100 100 ARG ARG D . n 
D 1 98  LEU 98  101 101 LEU LEU D . n 
D 1 99  THR 99  102 102 THR THR D . n 
D 1 100 GLY 100 103 103 GLY GLY D . n 
D 1 101 PRO 101 104 104 PRO PRO D . n 
D 1 102 ASP 102 105 105 ASP ASP D . n 
D 1 103 PRO 103 106 106 PRO PRO D . n 
D 1 104 PRO 104 107 107 PRO PRO D . n 
D 1 105 PRO 105 108 108 PRO PRO D . n 
D 1 106 PRO 106 109 109 PRO PRO D . n 
D 1 107 ALA 107 110 110 ALA ALA D . n 
D 1 108 SER 108 111 111 SER SER D . n 
D 1 109 VAL 109 112 112 VAL VAL D . n 
D 1 110 GLY 110 113 113 GLY GLY D . n 
D 1 111 GLY 111 114 114 GLY GLY D . n 
D 1 112 LEU 112 115 115 LEU LEU D . n 
D 1 113 ASN 113 116 116 ASN ASN D . n 
D 1 114 GLU 114 117 117 GLU GLU D . n 
D 1 115 HIS 115 118 118 HIS HIS D . n 
D 1 116 GLY 116 119 119 GLY GLY D . n 
D 1 117 THR 117 120 120 THR THR D . n 
D 1 118 PHE 118 121 121 PHE PHE D . n 
D 1 119 GLU 119 122 122 GLU GLU D . n 
D 1 120 GLY 120 123 123 GLY GLY D . n 
D 1 121 ASP 121 124 124 ASP ASP D . n 
D 1 122 ALA 122 125 125 ALA ALA D . n 
D 1 123 SER 123 126 126 SER SER D . n 
D 1 124 MET 124 127 127 MET MET D . n 
D 1 125 THR 125 128 128 THR THR D . n 
D 1 126 ARG 126 129 129 ARG ARG D . n 
D 1 127 GLY 127 130 130 GLY GLY D . n 
D 1 128 ASP 128 131 131 ASP ASP D . n 
D 1 129 ALA 129 132 132 ALA ALA D . n 
D 1 130 PHE 130 133 133 PHE PHE D . n 
D 1 131 PHE 131 134 134 PHE PHE D . n 
D 1 132 GLY 132 135 135 GLY GLY D . n 
D 1 133 ASN 133 136 136 ASN ASN D . n 
D 1 134 ASN 134 137 137 ASN ASN D . n 
D 1 135 HIS 135 138 138 HIS HIS D . n 
D 1 136 ASP 136 139 139 ASP ASP D . n 
D 1 137 PHE 137 140 140 PHE PHE D . n 
D 1 138 ASN 138 141 141 ASN ASN D . n 
D 1 139 GLU 139 142 142 GLU GLU D . n 
D 1 140 THR 140 143 143 THR THR D . n 
D 1 141 LEU 141 144 144 LEU LEU D . n 
D 1 142 PHE 142 145 145 PHE PHE D . n 
D 1 143 GLU 143 146 146 GLU GLU D . n 
D 1 144 GLN 144 147 147 GLN GLN D . n 
D 1 145 LEU 145 148 148 LEU LEU D . n 
D 1 146 VAL 146 149 149 VAL VAL D . n 
D 1 147 ASP 147 150 150 ASP ASP D . n 
D 1 148 TYR 148 151 151 TYR TYR D . n 
D 1 149 SER 149 152 152 SER SER D . n 
D 1 150 ASN 150 153 153 ASN ASN D . n 
D 1 151 ARG 151 154 154 ARG ARG D . n 
D 1 152 PHE 152 155 155 PHE PHE D . n 
D 1 153 GLY 153 156 156 GLY GLY D . n 
D 1 154 GLY 154 157 157 GLY GLY D . n 
D 1 155 GLY 155 158 158 GLY GLY D . n 
D 1 156 LYS 156 159 159 LYS LYS D . n 
D 1 157 TYR 157 160 160 TYR TYR D . n 
D 1 158 ASN 158 161 161 ASN ASN D . n 
D 1 159 LEU 159 162 162 LEU LEU D . n 
D 1 160 THR 160 163 163 THR THR D . n 
D 1 161 VAL 161 164 164 VAL VAL D . n 
D 1 162 ALA 162 165 165 ALA ALA D . n 
D 1 163 GLY 163 166 166 GLY GLY D . n 
D 1 164 GLU 164 167 167 GLU GLU D . n 
D 1 165 LEU 165 168 168 LEU LEU D . n 
D 1 166 ARG 166 169 169 ARG ARG D . n 
D 1 167 PHE 167 170 170 PHE PHE D . n 
D 1 168 LYS 168 171 171 LYS LYS D . n 
D 1 169 ARG 169 172 172 ARG ARG D . n 
D 1 170 ILE 170 173 173 ILE ILE D . n 
D 1 171 GLN 171 174 174 GLN GLN D . n 
D 1 172 ASP 172 175 175 ASP ASP D . n 
D 1 173 SER 173 176 176 SER SER D . n 
D 1 174 ILE 174 177 177 ILE ILE D . n 
D 1 175 ALA 175 178 178 ALA ALA D . n 
D 1 176 THR 176 179 179 THR THR D . n 
D 1 177 ASN 177 180 180 ASN ASN D . n 
D 1 178 PRO 178 181 181 PRO PRO D . n 
D 1 179 ASN 179 182 182 ASN ASN D . n 
D 1 180 PHE 180 183 183 PHE PHE D . n 
D 1 181 SER 181 184 184 SER SER D . n 
D 1 182 PHE 182 185 185 PHE PHE D . n 
D 1 183 VAL 183 186 186 VAL VAL D . n 
D 1 184 ASP 184 187 187 ASP ASP D . n 
D 1 185 PHE 185 188 188 PHE PHE D . n 
D 1 186 ARG 186 189 189 ARG ARG D . n 
D 1 187 PHE 187 190 190 PHE PHE D . n 
D 1 188 PHE 188 191 191 PHE PHE D . n 
D 1 189 THR 189 192 192 THR THR D . n 
D 1 190 ALA 190 193 193 ALA ALA D . n 
D 1 191 TYR 191 194 194 TYR TYR D . n 
D 1 192 GLY 192 195 195 GLY GLY D . n 
D 1 193 GLU 193 196 196 GLU GLU D . n 
D 1 194 THR 194 197 197 THR THR D . n 
D 1 195 THR 195 198 198 THR THR D . n 
D 1 196 PHE 196 199 199 PHE PHE D . n 
D 1 197 PRO 197 200 200 PRO PRO D . n 
D 1 198 ALA 198 201 201 ALA ALA D . n 
D 1 199 ASN 199 202 202 ASN ASN D . n 
D 1 200 LEU 200 203 203 LEU LEU D . n 
D 1 201 PHE 201 204 204 PHE PHE D . n 
D 1 202 VAL 202 205 205 VAL VAL D . n 
D 1 203 ASP 203 206 206 ASP ASP D . n 
D 1 204 GLY 204 207 207 GLY GLY D . n 
D 1 205 ARG 205 208 208 ARG ARG D . n 
D 1 206 ARG 206 209 209 ARG ARG D . n 
D 1 207 ASP 207 210 210 ASP ASP D . n 
D 1 208 ASP 208 211 211 ASP ASP D . n 
D 1 209 GLY 209 212 212 GLY GLY D . n 
D 1 210 GLN 210 213 213 GLN GLN D . n 
D 1 211 LEU 211 214 214 LEU LEU D . n 
D 1 212 ASP 212 215 215 ASP ASP D . n 
D 1 213 MET 213 216 216 MET MET D . n 
D 1 214 ASP 214 217 217 ASP ASP D . n 
D 1 215 ALA 215 218 218 ALA ALA D . n 
D 1 216 ALA 216 219 219 ALA ALA D . n 
D 1 217 ARG 217 220 220 ARG ARG D . n 
D 1 218 SER 218 221 221 SER SER D . n 
D 1 219 PHE 219 222 222 PHE PHE D . n 
D 1 220 PHE 220 223 223 PHE PHE D . n 
D 1 221 GLN 221 224 224 GLN GLN D . n 
D 1 222 PHE 222 225 225 PHE PHE D . n 
D 1 223 SER 223 226 226 SER SER D . n 
D 1 224 ARG 224 227 227 ARG ARG D . n 
D 1 225 MET 225 228 228 MET MET D . n 
D 1 226 PRO 226 229 229 PRO PRO D . n 
D 1 227 ASP 227 230 230 ASP ASP D . n 
D 1 228 ASP 228 231 231 ASP ASP D . n 
D 1 229 PHE 229 232 232 PHE PHE D . n 
D 1 230 PHE 230 233 233 PHE PHE D . n 
D 1 231 ARG 231 234 234 ARG ARG D . n 
D 1 232 ALA 232 235 235 ALA ALA D . n 
D 1 233 PRO 233 236 236 PRO PRO D . n 
D 1 234 SER 234 237 237 SER SER D . n 
D 1 235 PRO 235 238 238 PRO PRO D . n 
D 1 236 ARG 236 239 239 ARG ARG D . n 
D 1 237 SER 237 240 240 SER SER D . n 
D 1 238 GLY 238 241 241 GLY GLY D . n 
D 1 239 THR 239 242 242 THR THR D . n 
D 1 240 GLY 240 243 243 GLY GLY D . n 
D 1 241 VAL 241 244 244 VAL VAL D . n 
D 1 242 GLU 242 245 245 GLU GLU D . n 
D 1 243 VAL 243 246 246 VAL VAL D . n 
D 1 244 VAL 244 247 247 VAL VAL D . n 
D 1 245 ILE 245 248 248 ILE ILE D . n 
D 1 246 GLN 246 249 249 GLN GLN D . n 
D 1 247 ALA 247 250 250 ALA ALA D . n 
D 1 248 HIS 248 251 251 HIS HIS D . n 
D 1 249 PRO 249 252 252 PRO PRO D . n 
D 1 250 MET 250 253 253 MET MET D . n 
D 1 251 GLN 251 254 254 GLN GLN D . n 
D 1 252 PRO 252 255 255 PRO PRO D . n 
D 1 253 GLY 253 256 256 GLY GLY D . n 
D 1 254 ARG 254 257 257 ARG ARG D . n 
D 1 255 ASN 255 258 258 ASN ASN D . n 
D 1 256 VAL 256 259 259 VAL VAL D . n 
D 1 257 GLY 257 260 260 GLY GLY D . n 
D 1 258 LYS 258 261 261 LYS LYS D . n 
D 1 259 ILE 259 262 262 ILE ILE D . n 
D 1 260 ASN 260 263 263 ASN ASN D . n 
D 1 261 SER 261 264 264 SER SER D . n 
D 1 262 TYR 262 265 265 TYR TYR D . n 
D 1 263 THR 263 266 266 THR THR D . n 
D 1 264 VAL 264 267 267 VAL VAL D . n 
D 1 265 ASP 265 268 268 ASP ASP D . n 
D 1 266 PRO 266 269 269 PRO PRO D . n 
D 1 267 THR 267 270 270 THR THR D . n 
D 1 268 SER 268 271 271 SER SER D . n 
D 1 269 SER 269 272 272 SER SER D . n 
D 1 270 ASP 270 273 273 ASP ASP D . n 
D 1 271 PHE 271 274 274 PHE PHE D . n 
D 1 272 SER 272 275 275 SER SER D . n 
D 1 273 THR 273 276 276 THR THR D . n 
D 1 274 PRO 274 277 277 PRO PRO D . n 
D 1 275 CYS 275 278 278 CYS CYS D . n 
D 1 276 LEU 276 279 279 LEU LEU D . n 
D 1 277 MET 277 280 280 MET MET D . n 
D 1 278 TYR 278 281 281 TYR TYR D . n 
D 1 279 GLU 279 282 282 GLU GLU D . n 
D 1 280 LYS 280 283 283 LYS LYS D . n 
D 1 281 PHE 281 284 284 PHE PHE D . n 
D 1 282 VAL 282 285 285 VAL VAL D . n 
D 1 283 ASN 283 286 286 ASN ASN D . n 
D 1 284 ILE 284 287 287 ILE ILE D . n 
D 1 285 THR 285 288 288 THR THR D . n 
D 1 286 VAL 286 289 289 VAL VAL D . n 
D 1 287 LYS 287 290 290 LYS LYS D . n 
D 1 288 SER 288 291 291 SER SER D . n 
D 1 289 LEU 289 292 292 LEU LEU D . n 
D 1 290 TYR 290 293 293 TYR TYR D . n 
D 1 291 PRO 291 294 294 PRO PRO D . n 
D 1 292 ASN 292 295 295 ASN ASN D . n 
D 1 293 PRO 293 296 296 PRO PRO D . n 
D 1 294 THR 294 297 297 THR THR D . n 
D 1 295 VAL 295 298 298 VAL VAL D . n 
D 1 296 GLN 296 299 299 GLN GLN D . n 
D 1 297 LEU 297 300 300 LEU LEU D . n 
D 1 298 ARG 298 301 301 ARG ARG D . n 
D 1 299 LYS 299 302 302 LYS LYS D . n 
D 1 300 ALA 300 303 303 ALA ALA D . n 
D 1 301 LEU 301 304 304 LEU LEU D . n 
D 1 302 ASN 302 305 305 ASN ASN D . n 
D 1 303 THR 303 306 306 THR THR D . n 
D 1 304 ASN 304 307 307 ASN ASN D . n 
D 1 305 LEU 305 308 308 LEU LEU D . n 
D 1 306 ASP 306 309 309 ASP ASP D . n 
D 1 307 PHE 307 310 310 PHE PHE D . n 
D 1 308 PHE 308 311 311 PHE PHE D . n 
D 1 309 PHE 309 312 312 PHE PHE D . n 
D 1 310 GLN 310 313 313 GLN GLN D . n 
D 1 311 GLY 311 314 314 GLY GLY D . n 
D 1 312 VAL 312 315 315 VAL VAL D . n 
D 1 313 ALA 313 316 316 ALA ALA D . n 
D 1 314 ALA 314 317 317 ALA ALA D . n 
D 1 315 GLY 315 318 318 GLY GLY D . n 
D 1 316 CYS 316 319 319 CYS CYS D . n 
D 1 317 THR 317 320 320 THR THR D . n 
D 1 318 GLN 318 321 321 GLN GLN D . n 
D 1 319 VAL 319 322 322 VAL VAL D . n 
D 1 320 PHE 320 323 323 PHE PHE D . n 
D 1 321 PRO 321 324 324 PRO PRO D . n 
D 1 322 TYR 322 325 325 TYR TYR D . n 
D 1 323 GLY 323 326 326 GLY GLY D . n 
D 1 324 ARG 324 327 ?   ?   ?   D . n 
D 1 325 ASP 325 328 ?   ?   ?   D . 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 
E  2 HEM 1   350  350  HEM HEM A . 
F  3 MG  1   353  353  MG  MG  A . 
G  4 NAG 1   361  361  NAG NAG A . 
H  4 NAG 2   362  362  NAG NAG A . 
I  5 BMA 3   363  363  BMA BMA A . 
J  6 MAN 4   364  364  MAN MAN A . 
K  6 MAN 5   365  365  MAN MAN A . 
L  6 MAN 6   366  366  MAN MAN A . 
M  4 NAG 1   371  371  NAG NAG A . 
N  4 NAG 2   372  372  NAG NAG A . 
O  5 BMA 3   373  373  BMA BMA A . 
P  6 MAN 4   374  374  MAN MAN A . 
Q  6 MAN 5   375  375  MAN MAN A . 
R  4 NAG 1   381  381  NAG NAG A . 
S  4 NAG 2   382  382  NAG NAG A . 
T  4 NAG 1   391  391  NAG NAG A . 
U  4 NAG 2   392  392  NAG NAG A . 
V  5 BMA 3   393  393  BMA BMA A . 
W  6 MAN 4   394  394  MAN MAN A . 
X  6 MAN 5   395  395  MAN MAN A . 
Y  6 MAN 6   396  396  MAN MAN A . 
Z  6 MAN 7   397  397  MAN MAN A . 
AA 6 MAN 8   398  398  MAN MAN A . 
BA 4 NAG 1   411  411  NAG NAG A . 
CA 4 NAG 2   412  412  NAG NAG A . 
DA 7 ACT 1   1327 1327 ACT ACT A . 
EA 8 SO4 1   1328 1328 SO4 SO4 A . 
FA 8 SO4 1   1329 1329 SO4 SO4 A . 
GA 8 SO4 1   1330 1330 SO4 SO4 A . 
HA 8 SO4 1   1331 1331 SO4 SO4 A . 
IA 2 HEM 1   350  350  HEM HEM B . 
JA 3 MG  1   353  353  MG  MG  B . 
KA 4 NAG 1   361  361  NAG NAG B . 
LA 4 NAG 2   362  362  NAG NAG B . 
MA 5 BMA 3   363  363  BMA BMA B . 
NA 6 MAN 4   364  364  MAN MAN B . 
OA 6 MAN 5   365  365  MAN MAN B . 
PA 4 NAG 1   371  371  NAG NAG B . 
QA 4 NAG 2   372  372  NAG NAG B . 
RA 4 NAG 1   381  381  NAG NAG B . 
SA 4 NAG 2   382  382  NAG NAG B . 
TA 4 NAG 1   391  391  NAG NAG B . 
UA 4 NAG 2   392  392  NAG NAG B . 
VA 5 BMA 3   393  393  BMA BMA B . 
WA 6 MAN 4   394  394  MAN MAN B . 
XA 6 MAN 5   395  395  MAN MAN B . 
YA 6 MAN 6   396  396  MAN MAN B . 
ZA 6 MAN 7   397  397  MAN MAN B . 
AB 6 MAN 8   398  398  MAN MAN B . 
BB 4 NAG 1   411  411  NAG NAG B . 
CB 4 NAG 2   412  412  NAG NAG B . 
DB 7 ACT 1   1328 1328 ACT ACT B . 
EB 8 SO4 1   1329 1329 SO4 SO4 B . 
FB 8 SO4 1   1330 1330 SO4 SO4 B . 
GB 8 SO4 1   1331 1331 SO4 SO4 B . 
HB 2 HEM 1   350  350  HEM HEM C . 
IB 3 MG  1   353  353  MG  MG  C . 
JB 4 NAG 1   361  361  NAG NAG C . 
KB 4 NAG 2   362  362  NAG NAG C . 
LB 5 BMA 3   363  363  BMA BMA C . 
MB 4 NAG 1   371  371  NAG NAG C . 
NB 4 NAG 2   372  372  NAG NAG C . 
OB 4 NAG 1   381  381  NAG NAG C . 
PB 4 NAG 1   391  391  NAG NAG C . 
QB 4 NAG 2   392  392  NAG NAG C . 
RB 4 NAG 1   411  411  NAG NAG C . 
SB 4 NAG 2   412  412  NAG NAG C . 
TB 7 ACT 1   1329 1329 ACT ACT C . 
UB 8 SO4 1   1330 1330 SO4 SO4 C . 
VB 8 SO4 1   1331 1331 SO4 SO4 C . 
WB 8 SO4 1   1332 1332 SO4 SO4 C . 
XB 8 SO4 1   1333 1333 SO4 SO4 C . 
YB 7 ACT 1   1334 1334 ACT ACT C . 
ZB 2 HEM 1   350  350  HEM HEM D . 
AC 3 MG  1   353  353  MG  MG  D . 
BC 4 NAG 1   361  361  NAG NAG D . 
CC 4 NAG 2   362  362  NAG NAG D . 
DC 4 NAG 1   371  371  NAG NAG D . 
EC 4 NAG 2   372  372  NAG NAG D . 
FC 5 BMA 3   373  373  BMA BMA D . 
GC 4 NAG 1   381  381  NAG NAG D . 
HC 4 NAG 1   391  391  NAG NAG D . 
IC 4 NAG 1   411  411  NAG NAG D . 
JC 7 ACT 1   1327 1327 ACT ACT D . 
KC 8 SO4 1   1328 1328 SO4 SO4 D . 
LC 8 SO4 1   1329 1329 SO4 SO4 D . 
MC 9 HOH 1   2001 2001 HOH HOH A . 
MC 9 HOH 2   2002 2002 HOH HOH A . 
MC 9 HOH 3   2003 2003 HOH HOH A . 
MC 9 HOH 4   2004 2004 HOH HOH A . 
MC 9 HOH 5   2005 2005 HOH HOH A . 
MC 9 HOH 6   2006 2006 HOH HOH A . 
MC 9 HOH 7   2007 2007 HOH HOH A . 
MC 9 HOH 8   2008 2008 HOH HOH A . 
MC 9 HOH 9   2009 2009 HOH HOH A . 
MC 9 HOH 10  2010 2010 HOH HOH A . 
MC 9 HOH 11  2011 2011 HOH HOH A . 
MC 9 HOH 12  2012 2012 HOH HOH A . 
MC 9 HOH 13  2013 2013 HOH HOH A . 
MC 9 HOH 14  2014 2014 HOH HOH A . 
MC 9 HOH 15  2015 2015 HOH HOH A . 
MC 9 HOH 16  2016 2016 HOH HOH A . 
MC 9 HOH 17  2017 2017 HOH HOH A . 
MC 9 HOH 18  2018 2018 HOH HOH A . 
MC 9 HOH 19  2019 2019 HOH HOH A . 
MC 9 HOH 20  2020 2020 HOH HOH A . 
MC 9 HOH 21  2021 2021 HOH HOH A . 
MC 9 HOH 22  2022 2022 HOH HOH A . 
MC 9 HOH 23  2023 2023 HOH HOH A . 
MC 9 HOH 24  2024 2024 HOH HOH A . 
MC 9 HOH 25  2025 2025 HOH HOH A . 
MC 9 HOH 26  2026 2026 HOH HOH A . 
MC 9 HOH 27  2027 2027 HOH HOH A . 
MC 9 HOH 28  2028 2028 HOH HOH A . 
MC 9 HOH 29  2029 2029 HOH HOH A . 
MC 9 HOH 30  2030 2030 HOH HOH A . 
MC 9 HOH 31  2031 2031 HOH HOH A . 
MC 9 HOH 32  2032 2032 HOH HOH A . 
MC 9 HOH 33  2033 2033 HOH HOH A . 
MC 9 HOH 34  2034 2034 HOH HOH A . 
MC 9 HOH 35  2035 2035 HOH HOH A . 
MC 9 HOH 36  2036 2036 HOH HOH A . 
MC 9 HOH 37  2037 2037 HOH HOH A . 
MC 9 HOH 38  2038 2038 HOH HOH A . 
MC 9 HOH 39  2039 2039 HOH HOH A . 
MC 9 HOH 40  2040 2040 HOH HOH A . 
MC 9 HOH 41  2041 2041 HOH HOH A . 
MC 9 HOH 42  2042 2042 HOH HOH A . 
MC 9 HOH 43  2043 2043 HOH HOH A . 
MC 9 HOH 44  2044 2044 HOH HOH A . 
MC 9 HOH 45  2045 2045 HOH HOH A . 
MC 9 HOH 46  2046 2046 HOH HOH A . 
MC 9 HOH 47  2047 2047 HOH HOH A . 
MC 9 HOH 48  2048 2048 HOH HOH A . 
MC 9 HOH 49  2049 2049 HOH HOH A . 
MC 9 HOH 50  2050 2050 HOH HOH A . 
MC 9 HOH 51  2051 2051 HOH HOH A . 
MC 9 HOH 52  2052 2052 HOH HOH A . 
MC 9 HOH 53  2053 2053 HOH HOH A . 
MC 9 HOH 54  2054 2054 HOH HOH A . 
MC 9 HOH 55  2055 2055 HOH HOH A . 
MC 9 HOH 56  2056 2056 HOH HOH A . 
MC 9 HOH 57  2057 2057 HOH HOH A . 
MC 9 HOH 58  2058 2058 HOH HOH A . 
MC 9 HOH 59  2059 2059 HOH HOH A . 
MC 9 HOH 60  2060 2060 HOH HOH A . 
MC 9 HOH 61  2061 2061 HOH HOH A . 
MC 9 HOH 62  2062 2062 HOH HOH A . 
MC 9 HOH 63  2063 2063 HOH HOH A . 
MC 9 HOH 64  2064 2064 HOH HOH A . 
MC 9 HOH 65  2065 2065 HOH HOH A . 
MC 9 HOH 66  2066 2066 HOH HOH A . 
MC 9 HOH 67  2067 2067 HOH HOH A . 
MC 9 HOH 68  2068 2068 HOH HOH A . 
MC 9 HOH 69  2069 2069 HOH HOH A . 
MC 9 HOH 70  2070 2070 HOH HOH A . 
MC 9 HOH 71  2071 2071 HOH HOH A . 
MC 9 HOH 72  2072 2072 HOH HOH A . 
MC 9 HOH 73  2073 2073 HOH HOH A . 
MC 9 HOH 74  2074 2074 HOH HOH A . 
MC 9 HOH 75  2075 2075 HOH HOH A . 
MC 9 HOH 76  2076 2076 HOH HOH A . 
MC 9 HOH 77  2077 2077 HOH HOH A . 
MC 9 HOH 78  2078 2078 HOH HOH A . 
MC 9 HOH 79  2079 2079 HOH HOH A . 
MC 9 HOH 80  2080 2080 HOH HOH A . 
MC 9 HOH 81  2081 2081 HOH HOH A . 
MC 9 HOH 82  2082 2082 HOH HOH A . 
MC 9 HOH 83  2083 2083 HOH HOH A . 
MC 9 HOH 84  2084 2084 HOH HOH A . 
MC 9 HOH 85  2085 2085 HOH HOH A . 
MC 9 HOH 86  2086 2086 HOH HOH A . 
MC 9 HOH 87  2087 2087 HOH HOH A . 
MC 9 HOH 88  2088 2088 HOH HOH A . 
MC 9 HOH 89  2089 2089 HOH HOH A . 
MC 9 HOH 90  2090 2090 HOH HOH A . 
MC 9 HOH 91  2091 2091 HOH HOH A . 
MC 9 HOH 92  2092 2092 HOH HOH A . 
MC 9 HOH 93  2093 2093 HOH HOH A . 
MC 9 HOH 94  2094 2094 HOH HOH A . 
MC 9 HOH 95  2095 2095 HOH HOH A . 
MC 9 HOH 96  2096 2096 HOH HOH A . 
MC 9 HOH 97  2097 2097 HOH HOH A . 
MC 9 HOH 98  2098 2098 HOH HOH A . 
MC 9 HOH 99  2099 2099 HOH HOH A . 
MC 9 HOH 100 2100 2100 HOH HOH A . 
MC 9 HOH 101 2101 2101 HOH HOH A . 
MC 9 HOH 102 2102 2102 HOH HOH A . 
MC 9 HOH 103 2103 2103 HOH HOH A . 
MC 9 HOH 104 2104 2104 HOH HOH A . 
MC 9 HOH 105 2105 2105 HOH HOH A . 
MC 9 HOH 106 2106 2106 HOH HOH A . 
MC 9 HOH 107 2107 2107 HOH HOH A . 
MC 9 HOH 108 2108 2108 HOH HOH A . 
MC 9 HOH 109 2109 2109 HOH HOH A . 
MC 9 HOH 110 2110 2110 HOH HOH A . 
MC 9 HOH 111 2111 2111 HOH HOH A . 
MC 9 HOH 112 2112 2112 HOH HOH A . 
MC 9 HOH 113 2113 2113 HOH HOH A . 
MC 9 HOH 114 2114 2114 HOH HOH A . 
MC 9 HOH 115 2115 2115 HOH HOH A . 
MC 9 HOH 116 2116 2116 HOH HOH A . 
MC 9 HOH 117 2117 2117 HOH HOH A . 
MC 9 HOH 118 2118 2118 HOH HOH A . 
MC 9 HOH 119 2119 2119 HOH HOH A . 
MC 9 HOH 120 2120 2120 HOH HOH A . 
MC 9 HOH 121 2121 2121 HOH HOH A . 
MC 9 HOH 122 2122 2122 HOH HOH A . 
MC 9 HOH 123 2123 2123 HOH HOH A . 
MC 9 HOH 124 2124 2124 HOH HOH A . 
MC 9 HOH 125 2125 2125 HOH HOH A . 
MC 9 HOH 126 2126 2126 HOH HOH A . 
MC 9 HOH 127 2127 2127 HOH HOH A . 
MC 9 HOH 128 2128 2128 HOH HOH A . 
MC 9 HOH 129 2129 2129 HOH HOH A . 
MC 9 HOH 130 2130 2130 HOH HOH A . 
MC 9 HOH 131 2131 2131 HOH HOH A . 
MC 9 HOH 132 2132 2132 HOH HOH A . 
MC 9 HOH 133 2133 2133 HOH HOH A . 
MC 9 HOH 134 2134 2134 HOH HOH A . 
MC 9 HOH 135 2135 2135 HOH HOH A . 
MC 9 HOH 136 2136 2136 HOH HOH A . 
MC 9 HOH 137 2137 2137 HOH HOH A . 
MC 9 HOH 138 2138 2138 HOH HOH A . 
MC 9 HOH 139 2139 2139 HOH HOH A . 
MC 9 HOH 140 2140 2140 HOH HOH A . 
MC 9 HOH 141 2141 2141 HOH HOH A . 
MC 9 HOH 142 2142 2142 HOH HOH A . 
MC 9 HOH 143 2143 2143 HOH HOH A . 
MC 9 HOH 144 2144 2144 HOH HOH A . 
MC 9 HOH 145 2145 2145 HOH HOH A . 
MC 9 HOH 146 2146 2146 HOH HOH A . 
MC 9 HOH 147 2147 2147 HOH HOH A . 
MC 9 HOH 148 2148 2148 HOH HOH A . 
MC 9 HOH 149 2149 2149 HOH HOH A . 
MC 9 HOH 150 2150 2150 HOH HOH A . 
MC 9 HOH 151 2151 2151 HOH HOH A . 
MC 9 HOH 152 2152 2152 HOH HOH A . 
MC 9 HOH 153 2153 2153 HOH HOH A . 
MC 9 HOH 154 2154 2154 HOH HOH A . 
MC 9 HOH 155 2155 2155 HOH HOH A . 
MC 9 HOH 156 2156 2156 HOH HOH A . 
MC 9 HOH 157 2157 2157 HOH HOH A . 
MC 9 HOH 158 2158 2158 HOH HOH A . 
MC 9 HOH 159 2159 2159 HOH HOH A . 
MC 9 HOH 160 2160 2160 HOH HOH A . 
MC 9 HOH 161 2161 2161 HOH HOH A . 
MC 9 HOH 162 2162 2162 HOH HOH A . 
MC 9 HOH 163 2163 2163 HOH HOH A . 
MC 9 HOH 164 2164 2164 HOH HOH A . 
MC 9 HOH 165 2165 2165 HOH HOH A . 
MC 9 HOH 166 2166 2166 HOH HOH A . 
MC 9 HOH 167 2167 2167 HOH HOH A . 
MC 9 HOH 168 2168 2168 HOH HOH A . 
MC 9 HOH 169 2169 2169 HOH HOH A . 
MC 9 HOH 170 2170 2170 HOH HOH A . 
MC 9 HOH 171 2171 2171 HOH HOH A . 
MC 9 HOH 172 2172 2172 HOH HOH A . 
MC 9 HOH 173 2173 2173 HOH HOH A . 
MC 9 HOH 174 2174 2174 HOH HOH A . 
MC 9 HOH 175 2175 2175 HOH HOH A . 
MC 9 HOH 176 2176 2176 HOH HOH A . 
MC 9 HOH 177 2177 2177 HOH HOH A . 
MC 9 HOH 178 2178 2178 HOH HOH A . 
MC 9 HOH 179 2179 2179 HOH HOH A . 
MC 9 HOH 180 2180 2180 HOH HOH A . 
MC 9 HOH 181 2181 2181 HOH HOH A . 
MC 9 HOH 182 2182 2182 HOH HOH A . 
MC 9 HOH 183 2183 2183 HOH HOH A . 
MC 9 HOH 184 2184 2184 HOH HOH A . 
MC 9 HOH 185 2185 2185 HOH HOH A . 
MC 9 HOH 186 2186 2186 HOH HOH A . 
MC 9 HOH 187 2187 2187 HOH HOH A . 
MC 9 HOH 188 2188 2188 HOH HOH A . 
MC 9 HOH 189 2189 2189 HOH HOH A . 
MC 9 HOH 190 2190 2190 HOH HOH A . 
MC 9 HOH 191 2191 2191 HOH HOH A . 
MC 9 HOH 192 2192 2192 HOH HOH A . 
MC 9 HOH 193 2193 2193 HOH HOH A . 
MC 9 HOH 194 2194 2194 HOH HOH A . 
MC 9 HOH 195 2195 2195 HOH HOH A . 
MC 9 HOH 196 2196 2196 HOH HOH A . 
MC 9 HOH 197 2197 2197 HOH HOH A . 
MC 9 HOH 198 2198 2198 HOH HOH A . 
MC 9 HOH 199 2199 2199 HOH HOH A . 
MC 9 HOH 200 2200 2200 HOH HOH A . 
MC 9 HOH 201 2201 2201 HOH HOH A . 
MC 9 HOH 202 2202 2202 HOH HOH A . 
MC 9 HOH 203 2203 2203 HOH HOH A . 
MC 9 HOH 204 2204 2204 HOH HOH A . 
MC 9 HOH 205 2205 2205 HOH HOH A . 
MC 9 HOH 206 2206 2206 HOH HOH A . 
MC 9 HOH 207 2207 2207 HOH HOH A . 
MC 9 HOH 208 2208 2208 HOH HOH A . 
MC 9 HOH 209 2209 2209 HOH HOH A . 
MC 9 HOH 210 2210 2210 HOH HOH A . 
MC 9 HOH 211 2211 2211 HOH HOH A . 
MC 9 HOH 212 2212 2212 HOH HOH A . 
MC 9 HOH 213 2213 2213 HOH HOH A . 
MC 9 HOH 214 2214 2214 HOH HOH A . 
MC 9 HOH 215 2215 2215 HOH HOH A . 
MC 9 HOH 216 2216 2216 HOH HOH A . 
MC 9 HOH 217 2217 2217 HOH HOH A . 
MC 9 HOH 218 2218 2218 HOH HOH A . 
MC 9 HOH 219 2219 2219 HOH HOH A . 
MC 9 HOH 220 2220 2220 HOH HOH A . 
MC 9 HOH 221 2221 2221 HOH HOH A . 
MC 9 HOH 222 2222 2222 HOH HOH A . 
MC 9 HOH 223 2223 2223 HOH HOH A . 
MC 9 HOH 224 2224 2224 HOH HOH A . 
MC 9 HOH 225 2225 2225 HOH HOH A . 
MC 9 HOH 226 2226 2226 HOH HOH A . 
MC 9 HOH 227 2227 2227 HOH HOH A . 
MC 9 HOH 228 2228 2228 HOH HOH A . 
MC 9 HOH 229 2229 2229 HOH HOH A . 
MC 9 HOH 230 2230 2230 HOH HOH A . 
MC 9 HOH 231 2231 2231 HOH HOH A . 
MC 9 HOH 232 2232 2232 HOH HOH A . 
MC 9 HOH 233 2233 2233 HOH HOH A . 
MC 9 HOH 234 2234 2234 HOH HOH A . 
MC 9 HOH 235 2235 2235 HOH HOH A . 
MC 9 HOH 236 2236 2236 HOH HOH A . 
MC 9 HOH 237 2237 2237 HOH HOH A . 
MC 9 HOH 238 2238 2238 HOH HOH A . 
MC 9 HOH 239 2239 2239 HOH HOH A . 
MC 9 HOH 240 2240 2240 HOH HOH A . 
MC 9 HOH 241 2241 2241 HOH HOH A . 
MC 9 HOH 242 2242 2242 HOH HOH A . 
MC 9 HOH 243 2243 2243 HOH HOH A . 
MC 9 HOH 244 2244 2244 HOH HOH A . 
MC 9 HOH 245 2245 2245 HOH HOH A . 
MC 9 HOH 246 2246 2246 HOH HOH A . 
MC 9 HOH 247 2247 2247 HOH HOH A . 
MC 9 HOH 248 2248 2248 HOH HOH A . 
MC 9 HOH 249 2249 2249 HOH HOH A . 
MC 9 HOH 250 2250 2250 HOH HOH A . 
MC 9 HOH 251 2251 2251 HOH HOH A . 
MC 9 HOH 252 2252 2252 HOH HOH A . 
MC 9 HOH 253 2253 2253 HOH HOH A . 
MC 9 HOH 254 2254 2254 HOH HOH A . 
MC 9 HOH 255 2255 2255 HOH HOH A . 
MC 9 HOH 256 2256 2256 HOH HOH A . 
MC 9 HOH 257 2257 2257 HOH HOH A . 
MC 9 HOH 258 2258 2258 HOH HOH A . 
MC 9 HOH 259 2259 2259 HOH HOH A . 
MC 9 HOH 260 2260 2260 HOH HOH A . 
MC 9 HOH 261 2261 2261 HOH HOH A . 
MC 9 HOH 262 2262 2262 HOH HOH A . 
MC 9 HOH 263 2263 2263 HOH HOH A . 
MC 9 HOH 264 2264 2264 HOH HOH A . 
MC 9 HOH 265 2265 2265 HOH HOH A . 
MC 9 HOH 266 2266 2266 HOH HOH A . 
MC 9 HOH 267 2267 2267 HOH HOH A . 
MC 9 HOH 268 2268 2268 HOH HOH A . 
MC 9 HOH 269 2269 2269 HOH HOH A . 
MC 9 HOH 270 2270 2270 HOH HOH A . 
MC 9 HOH 271 2271 2271 HOH HOH A . 
MC 9 HOH 272 2272 2272 HOH HOH A . 
MC 9 HOH 273 2273 2273 HOH HOH A . 
MC 9 HOH 274 2274 2274 HOH HOH A . 
MC 9 HOH 275 2275 2275 HOH HOH A . 
MC 9 HOH 276 2276 2276 HOH HOH A . 
MC 9 HOH 277 2277 2277 HOH HOH A . 
MC 9 HOH 278 2278 2278 HOH HOH A . 
MC 9 HOH 279 2279 2279 HOH HOH A . 
MC 9 HOH 280 2280 2280 HOH HOH A . 
MC 9 HOH 281 2281 2281 HOH HOH A . 
MC 9 HOH 282 2282 2282 HOH HOH A . 
MC 9 HOH 283 2283 2283 HOH HOH A . 
MC 9 HOH 284 2284 2284 HOH HOH A . 
MC 9 HOH 285 2285 2285 HOH HOH A . 
MC 9 HOH 286 2286 2286 HOH HOH A . 
MC 9 HOH 287 2287 2287 HOH HOH A . 
MC 9 HOH 288 2288 2288 HOH HOH A . 
MC 9 HOH 289 2289 2289 HOH HOH A . 
MC 9 HOH 290 2290 2290 HOH HOH A . 
MC 9 HOH 291 2291 2291 HOH HOH A . 
MC 9 HOH 292 2292 2292 HOH HOH A . 
MC 9 HOH 293 2293 2293 HOH HOH A . 
MC 9 HOH 294 2294 2294 HOH HOH A . 
MC 9 HOH 295 2295 2295 HOH HOH A . 
MC 9 HOH 296 2296 2296 HOH HOH A . 
MC 9 HOH 297 2297 2297 HOH HOH A . 
MC 9 HOH 298 2298 2298 HOH HOH A . 
MC 9 HOH 299 2299 2299 HOH HOH A . 
MC 9 HOH 300 2300 2300 HOH HOH A . 
MC 9 HOH 301 2301 2301 HOH HOH A . 
MC 9 HOH 302 2302 2302 HOH HOH A . 
MC 9 HOH 303 2303 2303 HOH HOH A . 
MC 9 HOH 304 2304 2304 HOH HOH A . 
MC 9 HOH 305 2305 2305 HOH HOH A . 
MC 9 HOH 306 2306 2306 HOH HOH A . 
MC 9 HOH 307 2307 2307 HOH HOH A . 
MC 9 HOH 308 2308 2308 HOH HOH A . 
MC 9 HOH 309 2309 2309 HOH HOH A . 
MC 9 HOH 310 2310 2310 HOH HOH A . 
MC 9 HOH 311 2311 2311 HOH HOH A . 
MC 9 HOH 312 2312 2312 HOH HOH A . 
MC 9 HOH 313 2313 2313 HOH HOH A . 
MC 9 HOH 314 2314 2314 HOH HOH A . 
MC 9 HOH 315 2315 2315 HOH HOH A . 
MC 9 HOH 316 2316 2316 HOH HOH A . 
MC 9 HOH 317 2317 2317 HOH HOH A . 
MC 9 HOH 318 2318 2318 HOH HOH A . 
MC 9 HOH 319 2319 2319 HOH HOH A . 
MC 9 HOH 320 2320 2320 HOH HOH A . 
MC 9 HOH 321 2321 2321 HOH HOH A . 
MC 9 HOH 322 2322 2322 HOH HOH A . 
MC 9 HOH 323 2323 2323 HOH HOH A . 
MC 9 HOH 324 2324 2324 HOH HOH A . 
MC 9 HOH 325 2325 2325 HOH HOH A . 
MC 9 HOH 326 2326 2326 HOH HOH A . 
MC 9 HOH 327 2327 2327 HOH HOH A . 
NC 9 HOH 1   2001 2001 HOH HOH B . 
NC 9 HOH 2   2002 2002 HOH HOH B . 
NC 9 HOH 3   2003 2003 HOH HOH B . 
NC 9 HOH 4   2004 2004 HOH HOH B . 
NC 9 HOH 5   2005 2005 HOH HOH B . 
NC 9 HOH 6   2006 2006 HOH HOH B . 
NC 9 HOH 7   2007 2007 HOH HOH B . 
NC 9 HOH 8   2008 2008 HOH HOH B . 
NC 9 HOH 9   2009 2009 HOH HOH B . 
NC 9 HOH 10  2010 2010 HOH HOH B . 
NC 9 HOH 11  2011 2011 HOH HOH B . 
NC 9 HOH 12  2012 2012 HOH HOH B . 
NC 9 HOH 13  2013 2013 HOH HOH B . 
NC 9 HOH 14  2014 2014 HOH HOH B . 
NC 9 HOH 15  2015 2015 HOH HOH B . 
NC 9 HOH 16  2016 2016 HOH HOH B . 
NC 9 HOH 17  2017 2017 HOH HOH B . 
NC 9 HOH 18  2018 2018 HOH HOH B . 
NC 9 HOH 19  2019 2019 HOH HOH B . 
NC 9 HOH 20  2020 2020 HOH HOH B . 
NC 9 HOH 21  2021 2021 HOH HOH B . 
NC 9 HOH 22  2022 2022 HOH HOH B . 
NC 9 HOH 23  2023 2023 HOH HOH B . 
NC 9 HOH 24  2024 2024 HOH HOH B . 
NC 9 HOH 25  2025 2025 HOH HOH B . 
NC 9 HOH 26  2026 2026 HOH HOH B . 
NC 9 HOH 27  2027 2027 HOH HOH B . 
NC 9 HOH 28  2028 2028 HOH HOH B . 
NC 9 HOH 29  2029 2029 HOH HOH B . 
NC 9 HOH 30  2030 2030 HOH HOH B . 
NC 9 HOH 31  2031 2031 HOH HOH B . 
NC 9 HOH 32  2032 2032 HOH HOH B . 
NC 9 HOH 33  2033 2033 HOH HOH B . 
NC 9 HOH 34  2034 2034 HOH HOH B . 
NC 9 HOH 35  2035 2035 HOH HOH B . 
NC 9 HOH 36  2036 2036 HOH HOH B . 
NC 9 HOH 37  2037 2037 HOH HOH B . 
NC 9 HOH 38  2038 2038 HOH HOH B . 
NC 9 HOH 39  2039 2039 HOH HOH B . 
NC 9 HOH 40  2040 2040 HOH HOH B . 
NC 9 HOH 41  2041 2041 HOH HOH B . 
NC 9 HOH 42  2042 2042 HOH HOH B . 
NC 9 HOH 43  2043 2043 HOH HOH B . 
NC 9 HOH 44  2044 2044 HOH HOH B . 
NC 9 HOH 45  2045 2045 HOH HOH B . 
NC 9 HOH 46  2046 2046 HOH HOH B . 
NC 9 HOH 47  2047 2047 HOH HOH B . 
NC 9 HOH 48  2048 2048 HOH HOH B . 
NC 9 HOH 49  2049 2049 HOH HOH B . 
NC 9 HOH 50  2050 2050 HOH HOH B . 
NC 9 HOH 51  2051 2051 HOH HOH B . 
NC 9 HOH 52  2052 2052 HOH HOH B . 
NC 9 HOH 53  2053 2053 HOH HOH B . 
NC 9 HOH 54  2054 2054 HOH HOH B . 
NC 9 HOH 55  2055 2055 HOH HOH B . 
NC 9 HOH 56  2056 2056 HOH HOH B . 
NC 9 HOH 57  2057 2057 HOH HOH B . 
NC 9 HOH 58  2058 2058 HOH HOH B . 
NC 9 HOH 59  2059 2059 HOH HOH B . 
NC 9 HOH 60  2060 2060 HOH HOH B . 
NC 9 HOH 61  2061 2061 HOH HOH B . 
NC 9 HOH 62  2062 2062 HOH HOH B . 
NC 9 HOH 63  2063 2063 HOH HOH B . 
NC 9 HOH 64  2064 2064 HOH HOH B . 
NC 9 HOH 65  2065 2065 HOH HOH B . 
NC 9 HOH 66  2066 2066 HOH HOH B . 
NC 9 HOH 67  2067 2067 HOH HOH B . 
NC 9 HOH 68  2068 2068 HOH HOH B . 
NC 9 HOH 69  2069 2069 HOH HOH B . 
NC 9 HOH 70  2070 2070 HOH HOH B . 
NC 9 HOH 71  2071 2071 HOH HOH B . 
NC 9 HOH 72  2072 2072 HOH HOH B . 
NC 9 HOH 73  2073 2073 HOH HOH B . 
NC 9 HOH 74  2074 2074 HOH HOH B . 
NC 9 HOH 75  2075 2075 HOH HOH B . 
NC 9 HOH 76  2076 2076 HOH HOH B . 
NC 9 HOH 77  2077 2077 HOH HOH B . 
NC 9 HOH 78  2078 2078 HOH HOH B . 
NC 9 HOH 79  2079 2079 HOH HOH B . 
NC 9 HOH 80  2080 2080 HOH HOH B . 
NC 9 HOH 81  2081 2081 HOH HOH B . 
NC 9 HOH 82  2082 2082 HOH HOH B . 
NC 9 HOH 83  2083 2083 HOH HOH B . 
NC 9 HOH 84  2084 2084 HOH HOH B . 
NC 9 HOH 85  2085 2085 HOH HOH B . 
NC 9 HOH 86  2086 2086 HOH HOH B . 
NC 9 HOH 87  2087 2087 HOH HOH B . 
NC 9 HOH 88  2088 2088 HOH HOH B . 
NC 9 HOH 89  2089 2089 HOH HOH B . 
NC 9 HOH 90  2090 2090 HOH HOH B . 
NC 9 HOH 91  2091 2091 HOH HOH B . 
NC 9 HOH 92  2092 2092 HOH HOH B . 
NC 9 HOH 93  2093 2093 HOH HOH B . 
NC 9 HOH 94  2094 2094 HOH HOH B . 
NC 9 HOH 95  2095 2095 HOH HOH B . 
NC 9 HOH 96  2096 2096 HOH HOH B . 
NC 9 HOH 97  2097 2097 HOH HOH B . 
NC 9 HOH 98  2098 2098 HOH HOH B . 
NC 9 HOH 99  2099 2099 HOH HOH B . 
NC 9 HOH 100 2100 2100 HOH HOH B . 
NC 9 HOH 101 2101 2101 HOH HOH B . 
NC 9 HOH 102 2102 2102 HOH HOH B . 
NC 9 HOH 103 2103 2103 HOH HOH B . 
NC 9 HOH 104 2104 2104 HOH HOH B . 
NC 9 HOH 105 2105 2105 HOH HOH B . 
NC 9 HOH 106 2106 2106 HOH HOH B . 
NC 9 HOH 107 2107 2107 HOH HOH B . 
NC 9 HOH 108 2108 2108 HOH HOH B . 
NC 9 HOH 109 2109 2109 HOH HOH B . 
NC 9 HOH 110 2110 2110 HOH HOH B . 
NC 9 HOH 111 2111 2111 HOH HOH B . 
NC 9 HOH 112 2112 2112 HOH HOH B . 
NC 9 HOH 113 2113 2113 HOH HOH B . 
NC 9 HOH 114 2114 2114 HOH HOH B . 
NC 9 HOH 115 2115 2115 HOH HOH B . 
NC 9 HOH 116 2116 2116 HOH HOH B . 
NC 9 HOH 117 2117 2117 HOH HOH B . 
NC 9 HOH 118 2118 2118 HOH HOH B . 
NC 9 HOH 119 2119 2119 HOH HOH B . 
NC 9 HOH 120 2120 2120 HOH HOH B . 
NC 9 HOH 121 2121 2121 HOH HOH B . 
NC 9 HOH 122 2122 2122 HOH HOH B . 
NC 9 HOH 123 2123 2123 HOH HOH B . 
NC 9 HOH 124 2124 2124 HOH HOH B . 
NC 9 HOH 125 2125 2125 HOH HOH B . 
NC 9 HOH 126 2126 2126 HOH HOH B . 
NC 9 HOH 127 2127 2127 HOH HOH B . 
NC 9 HOH 128 2128 2128 HOH HOH B . 
NC 9 HOH 129 2129 2129 HOH HOH B . 
NC 9 HOH 130 2130 2130 HOH HOH B . 
NC 9 HOH 131 2131 2131 HOH HOH B . 
NC 9 HOH 132 2132 2132 HOH HOH B . 
NC 9 HOH 133 2133 2133 HOH HOH B . 
NC 9 HOH 134 2134 2134 HOH HOH B . 
NC 9 HOH 135 2135 2135 HOH HOH B . 
NC 9 HOH 136 2136 2136 HOH HOH B . 
NC 9 HOH 137 2137 2137 HOH HOH B . 
NC 9 HOH 138 2138 2138 HOH HOH B . 
NC 9 HOH 139 2139 2139 HOH HOH B . 
NC 9 HOH 140 2140 2140 HOH HOH B . 
NC 9 HOH 141 2141 2141 HOH HOH B . 
NC 9 HOH 142 2142 2142 HOH HOH B . 
NC 9 HOH 143 2143 2143 HOH HOH B . 
NC 9 HOH 144 2144 2144 HOH HOH B . 
NC 9 HOH 145 2145 2145 HOH HOH B . 
NC 9 HOH 146 2146 2146 HOH HOH B . 
NC 9 HOH 147 2147 2147 HOH HOH B . 
NC 9 HOH 148 2148 2148 HOH HOH B . 
NC 9 HOH 149 2149 2149 HOH HOH B . 
NC 9 HOH 150 2150 2150 HOH HOH B . 
NC 9 HOH 151 2151 2151 HOH HOH B . 
NC 9 HOH 152 2152 2152 HOH HOH B . 
NC 9 HOH 153 2153 2153 HOH HOH B . 
NC 9 HOH 154 2154 2154 HOH HOH B . 
NC 9 HOH 155 2155 2155 HOH HOH B . 
NC 9 HOH 156 2156 2156 HOH HOH B . 
NC 9 HOH 157 2157 2157 HOH HOH B . 
NC 9 HOH 158 2158 2158 HOH HOH B . 
NC 9 HOH 159 2159 2159 HOH HOH B . 
NC 9 HOH 160 2160 2160 HOH HOH B . 
NC 9 HOH 161 2161 2161 HOH HOH B . 
NC 9 HOH 162 2162 2162 HOH HOH B . 
NC 9 HOH 163 2163 2163 HOH HOH B . 
NC 9 HOH 164 2164 2164 HOH HOH B . 
NC 9 HOH 165 2165 2165 HOH HOH B . 
NC 9 HOH 166 2166 2166 HOH HOH B . 
NC 9 HOH 167 2167 2167 HOH HOH B . 
NC 9 HOH 168 2168 2168 HOH HOH B . 
NC 9 HOH 169 2169 2169 HOH HOH B . 
NC 9 HOH 170 2170 2170 HOH HOH B . 
NC 9 HOH 171 2171 2171 HOH HOH B . 
NC 9 HOH 172 2172 2172 HOH HOH B . 
NC 9 HOH 173 2173 2173 HOH HOH B . 
NC 9 HOH 174 2174 2174 HOH HOH B . 
NC 9 HOH 175 2175 2175 HOH HOH B . 
NC 9 HOH 176 2176 2176 HOH HOH B . 
NC 9 HOH 177 2177 2177 HOH HOH B . 
NC 9 HOH 178 2178 2178 HOH HOH B . 
NC 9 HOH 179 2179 2179 HOH HOH B . 
NC 9 HOH 180 2180 2180 HOH HOH B . 
NC 9 HOH 181 2181 2181 HOH HOH B . 
NC 9 HOH 182 2182 2182 HOH HOH B . 
NC 9 HOH 183 2183 2183 HOH HOH B . 
NC 9 HOH 184 2184 2184 HOH HOH B . 
NC 9 HOH 185 2185 2185 HOH HOH B . 
NC 9 HOH 186 2186 2186 HOH HOH B . 
NC 9 HOH 187 2187 2187 HOH HOH B . 
NC 9 HOH 188 2188 2188 HOH HOH B . 
NC 9 HOH 189 2189 2189 HOH HOH B . 
NC 9 HOH 190 2190 2190 HOH HOH B . 
NC 9 HOH 191 2191 2191 HOH HOH B . 
NC 9 HOH 192 2192 2192 HOH HOH B . 
NC 9 HOH 193 2193 2193 HOH HOH B . 
NC 9 HOH 194 2194 2194 HOH HOH B . 
NC 9 HOH 195 2195 2195 HOH HOH B . 
NC 9 HOH 196 2196 2196 HOH HOH B . 
NC 9 HOH 197 2197 2197 HOH HOH B . 
NC 9 HOH 198 2198 2198 HOH HOH B . 
NC 9 HOH 199 2199 2199 HOH HOH B . 
NC 9 HOH 200 2200 2200 HOH HOH B . 
NC 9 HOH 201 2201 2201 HOH HOH B . 
NC 9 HOH 202 2202 2202 HOH HOH B . 
NC 9 HOH 203 2203 2203 HOH HOH B . 
NC 9 HOH 204 2204 2204 HOH HOH B . 
NC 9 HOH 205 2205 2205 HOH HOH B . 
NC 9 HOH 206 2206 2206 HOH HOH B . 
NC 9 HOH 207 2207 2207 HOH HOH B . 
NC 9 HOH 208 2208 2208 HOH HOH B . 
NC 9 HOH 209 2209 2209 HOH HOH B . 
NC 9 HOH 210 2210 2210 HOH HOH B . 
NC 9 HOH 211 2211 2211 HOH HOH B . 
NC 9 HOH 212 2212 2212 HOH HOH B . 
NC 9 HOH 213 2213 2213 HOH HOH B . 
NC 9 HOH 214 2214 2214 HOH HOH B . 
NC 9 HOH 215 2215 2215 HOH HOH B . 
NC 9 HOH 216 2216 2216 HOH HOH B . 
NC 9 HOH 217 2217 2217 HOH HOH B . 
NC 9 HOH 218 2218 2218 HOH HOH B . 
NC 9 HOH 219 2219 2219 HOH HOH B . 
NC 9 HOH 220 2220 2220 HOH HOH B . 
NC 9 HOH 221 2221 2221 HOH HOH B . 
NC 9 HOH 222 2222 2222 HOH HOH B . 
NC 9 HOH 223 2223 2223 HOH HOH B . 
NC 9 HOH 224 2224 2224 HOH HOH B . 
NC 9 HOH 225 2225 2225 HOH HOH B . 
NC 9 HOH 226 2226 2226 HOH HOH B . 
NC 9 HOH 227 2227 2227 HOH HOH B . 
NC 9 HOH 228 2228 2228 HOH HOH B . 
NC 9 HOH 229 2229 2229 HOH HOH B . 
NC 9 HOH 230 2230 2230 HOH HOH B . 
NC 9 HOH 231 2231 2231 HOH HOH B . 
NC 9 HOH 232 2232 2232 HOH HOH B . 
NC 9 HOH 233 2233 2233 HOH HOH B . 
NC 9 HOH 234 2234 2234 HOH HOH B . 
NC 9 HOH 235 2235 2235 HOH HOH B . 
NC 9 HOH 236 2236 2236 HOH HOH B . 
NC 9 HOH 237 2237 2237 HOH HOH B . 
NC 9 HOH 238 2238 2238 HOH HOH B . 
NC 9 HOH 239 2239 2239 HOH HOH B . 
NC 9 HOH 240 2240 2240 HOH HOH B . 
NC 9 HOH 241 2241 2241 HOH HOH B . 
NC 9 HOH 242 2242 2242 HOH HOH B . 
NC 9 HOH 243 2243 2243 HOH HOH B . 
NC 9 HOH 244 2244 2244 HOH HOH B . 
NC 9 HOH 245 2245 2245 HOH HOH B . 
NC 9 HOH 246 2246 2246 HOH HOH B . 
NC 9 HOH 247 2247 2247 HOH HOH B . 
NC 9 HOH 248 2248 2248 HOH HOH B . 
NC 9 HOH 249 2249 2249 HOH HOH B . 
NC 9 HOH 250 2250 2250 HOH HOH B . 
NC 9 HOH 251 2251 2251 HOH HOH B . 
NC 9 HOH 252 2252 2252 HOH HOH B . 
NC 9 HOH 253 2253 2253 HOH HOH B . 
NC 9 HOH 254 2254 2254 HOH HOH B . 
NC 9 HOH 255 2255 2255 HOH HOH B . 
NC 9 HOH 256 2256 2256 HOH HOH B . 
NC 9 HOH 257 2257 2257 HOH HOH B . 
NC 9 HOH 258 2258 2258 HOH HOH B . 
NC 9 HOH 259 2259 2259 HOH HOH B . 
NC 9 HOH 260 2260 2260 HOH HOH B . 
NC 9 HOH 261 2261 2261 HOH HOH B . 
NC 9 HOH 262 2262 2262 HOH HOH B . 
NC 9 HOH 263 2263 2263 HOH HOH B . 
NC 9 HOH 264 2264 2264 HOH HOH B . 
NC 9 HOH 265 2265 2265 HOH HOH B . 
NC 9 HOH 266 2266 2266 HOH HOH B . 
NC 9 HOH 267 2267 2267 HOH HOH B . 
NC 9 HOH 268 2268 2268 HOH HOH B . 
NC 9 HOH 269 2269 2269 HOH HOH B . 
NC 9 HOH 270 2270 2270 HOH HOH B . 
NC 9 HOH 271 2271 2271 HOH HOH B . 
NC 9 HOH 272 2272 2272 HOH HOH B . 
NC 9 HOH 273 2273 2273 HOH HOH B . 
NC 9 HOH 274 2274 2274 HOH HOH B . 
NC 9 HOH 275 2275 2275 HOH HOH B . 
NC 9 HOH 276 2276 2276 HOH HOH B . 
NC 9 HOH 277 2277 2277 HOH HOH B . 
NC 9 HOH 278 2278 2278 HOH HOH B . 
NC 9 HOH 279 2279 2279 HOH HOH B . 
NC 9 HOH 280 2280 2280 HOH HOH B . 
NC 9 HOH 281 2281 2281 HOH HOH B . 
NC 9 HOH 282 2282 2282 HOH HOH B . 
NC 9 HOH 283 2283 2283 HOH HOH B . 
NC 9 HOH 284 2284 2284 HOH HOH B . 
NC 9 HOH 285 2285 2285 HOH HOH B . 
NC 9 HOH 286 2286 2286 HOH HOH B . 
NC 9 HOH 287 2287 2287 HOH HOH B . 
NC 9 HOH 288 2288 2288 HOH HOH B . 
NC 9 HOH 289 2289 2289 HOH HOH B . 
NC 9 HOH 290 2290 2290 HOH HOH B . 
NC 9 HOH 291 2291 2291 HOH HOH B . 
NC 9 HOH 292 2292 2292 HOH HOH B . 
NC 9 HOH 293 2293 2293 HOH HOH B . 
NC 9 HOH 294 2294 2294 HOH HOH B . 
NC 9 HOH 295 2295 2295 HOH HOH B . 
NC 9 HOH 296 2296 2296 HOH HOH B . 
NC 9 HOH 297 2297 2297 HOH HOH B . 
NC 9 HOH 298 2298 2298 HOH HOH B . 
NC 9 HOH 299 2299 2299 HOH HOH B . 
NC 9 HOH 300 2300 2300 HOH HOH B . 
NC 9 HOH 301 2301 2301 HOH HOH B . 
NC 9 HOH 302 2302 2302 HOH HOH B . 
NC 9 HOH 303 2303 2303 HOH HOH B . 
NC 9 HOH 304 2304 2304 HOH HOH B . 
NC 9 HOH 305 2305 2305 HOH HOH B . 
NC 9 HOH 306 2306 2306 HOH HOH B . 
NC 9 HOH 307 2307 2307 HOH HOH B . 
NC 9 HOH 308 2308 2308 HOH HOH B . 
NC 9 HOH 309 2309 2309 HOH HOH B . 
NC 9 HOH 310 2310 2310 HOH HOH B . 
NC 9 HOH 311 2311 2311 HOH HOH B . 
NC 9 HOH 312 2312 2312 HOH HOH B . 
NC 9 HOH 313 2313 2313 HOH HOH B . 
NC 9 HOH 314 2314 2314 HOH HOH B . 
NC 9 HOH 315 2315 2315 HOH HOH B . 
NC 9 HOH 316 2316 2316 HOH HOH B . 
NC 9 HOH 317 2317 2317 HOH HOH B . 
NC 9 HOH 318 2318 2318 HOH HOH B . 
NC 9 HOH 319 2319 2319 HOH HOH B . 
NC 9 HOH 320 2320 2320 HOH HOH B . 
NC 9 HOH 321 2321 2321 HOH HOH B . 
NC 9 HOH 322 2322 2322 HOH HOH B . 
NC 9 HOH 323 2323 2323 HOH HOH B . 
NC 9 HOH 324 2324 2324 HOH HOH B . 
NC 9 HOH 325 2325 2325 HOH HOH B . 
NC 9 HOH 326 2326 2326 HOH HOH B . 
NC 9 HOH 327 2327 2327 HOH HOH B . 
NC 9 HOH 328 2328 2328 HOH HOH B . 
NC 9 HOH 329 2329 2329 HOH HOH B . 
NC 9 HOH 330 2330 2330 HOH HOH B . 
NC 9 HOH 331 2331 2331 HOH HOH B . 
NC 9 HOH 332 2332 2332 HOH HOH B . 
NC 9 HOH 333 2333 2333 HOH HOH B . 
NC 9 HOH 334 2334 2334 HOH HOH B . 
NC 9 HOH 335 2335 2335 HOH HOH B . 
NC 9 HOH 336 2336 2336 HOH HOH B . 
NC 9 HOH 337 2337 2337 HOH HOH B . 
NC 9 HOH 338 2338 2338 HOH HOH B . 
NC 9 HOH 339 2339 2339 HOH HOH B . 
NC 9 HOH 340 2340 2340 HOH HOH B . 
NC 9 HOH 341 2341 2341 HOH HOH B . 
NC 9 HOH 342 2342 2342 HOH HOH B . 
NC 9 HOH 343 2343 2343 HOH HOH B . 
NC 9 HOH 344 2344 2344 HOH HOH B . 
NC 9 HOH 345 2345 2345 HOH HOH B . 
NC 9 HOH 346 2346 2346 HOH HOH B . 
NC 9 HOH 347 2347 2347 HOH HOH B . 
NC 9 HOH 348 2348 2348 HOH HOH B . 
NC 9 HOH 349 2349 2349 HOH HOH B . 
NC 9 HOH 350 2350 2350 HOH HOH B . 
NC 9 HOH 351 2351 2351 HOH HOH B . 
NC 9 HOH 352 2352 2352 HOH HOH B . 
NC 9 HOH 353 2353 2353 HOH HOH B . 
NC 9 HOH 354 2354 2354 HOH HOH B . 
NC 9 HOH 355 2355 2355 HOH HOH B . 
NC 9 HOH 356 2356 2356 HOH HOH B . 
NC 9 HOH 357 2357 2357 HOH HOH B . 
NC 9 HOH 358 2358 2358 HOH HOH B . 
NC 9 HOH 359 2359 2359 HOH HOH B . 
NC 9 HOH 360 2360 2360 HOH HOH B . 
NC 9 HOH 361 2361 2361 HOH HOH B . 
NC 9 HOH 362 2362 2362 HOH HOH B . 
NC 9 HOH 363 2363 2363 HOH HOH B . 
NC 9 HOH 364 2364 2364 HOH HOH B . 
NC 9 HOH 365 2365 2365 HOH HOH B . 
NC 9 HOH 366 2366 2366 HOH HOH B . 
NC 9 HOH 367 2367 2367 HOH HOH B . 
NC 9 HOH 368 2368 2368 HOH HOH B . 
NC 9 HOH 369 2369 2369 HOH HOH B . 
OC 9 HOH 1   2001 2001 HOH HOH C . 
OC 9 HOH 2   2002 2002 HOH HOH C . 
OC 9 HOH 3   2003 2003 HOH HOH C . 
OC 9 HOH 4   2004 2004 HOH HOH C . 
OC 9 HOH 5   2005 2005 HOH HOH C . 
OC 9 HOH 6   2006 2006 HOH HOH C . 
OC 9 HOH 7   2007 2007 HOH HOH C . 
OC 9 HOH 8   2008 2008 HOH HOH C . 
OC 9 HOH 9   2009 2009 HOH HOH C . 
OC 9 HOH 10  2010 2010 HOH HOH C . 
OC 9 HOH 11  2011 2011 HOH HOH C . 
OC 9 HOH 12  2012 2012 HOH HOH C . 
OC 9 HOH 13  2013 2013 HOH HOH C . 
OC 9 HOH 14  2014 2014 HOH HOH C . 
OC 9 HOH 15  2015 2015 HOH HOH C . 
OC 9 HOH 16  2016 2016 HOH HOH C . 
OC 9 HOH 17  2017 2017 HOH HOH C . 
OC 9 HOH 18  2018 2018 HOH HOH C . 
OC 9 HOH 19  2019 2019 HOH HOH C . 
OC 9 HOH 20  2020 2020 HOH HOH C . 
OC 9 HOH 21  2021 2021 HOH HOH C . 
OC 9 HOH 22  2022 2022 HOH HOH C . 
OC 9 HOH 23  2023 2023 HOH HOH C . 
OC 9 HOH 24  2024 2024 HOH HOH C . 
OC 9 HOH 25  2025 2025 HOH HOH C . 
OC 9 HOH 26  2026 2026 HOH HOH C . 
OC 9 HOH 27  2027 2027 HOH HOH C . 
OC 9 HOH 28  2028 2028 HOH HOH C . 
OC 9 HOH 29  2029 2029 HOH HOH C . 
OC 9 HOH 30  2030 2030 HOH HOH C . 
OC 9 HOH 31  2031 2031 HOH HOH C . 
OC 9 HOH 32  2032 2032 HOH HOH C . 
OC 9 HOH 33  2033 2033 HOH HOH C . 
OC 9 HOH 34  2034 2034 HOH HOH C . 
OC 9 HOH 35  2035 2035 HOH HOH C . 
OC 9 HOH 36  2036 2036 HOH HOH C . 
OC 9 HOH 37  2037 2037 HOH HOH C . 
OC 9 HOH 38  2038 2038 HOH HOH C . 
OC 9 HOH 39  2039 2039 HOH HOH C . 
OC 9 HOH 40  2040 2040 HOH HOH C . 
OC 9 HOH 41  2041 2041 HOH HOH C . 
OC 9 HOH 42  2042 2042 HOH HOH C . 
OC 9 HOH 43  2043 2043 HOH HOH C . 
OC 9 HOH 44  2044 2044 HOH HOH C . 
OC 9 HOH 45  2045 2045 HOH HOH C . 
OC 9 HOH 46  2046 2046 HOH HOH C . 
OC 9 HOH 47  2047 2047 HOH HOH C . 
OC 9 HOH 48  2048 2048 HOH HOH C . 
OC 9 HOH 49  2049 2049 HOH HOH C . 
OC 9 HOH 50  2050 2050 HOH HOH C . 
OC 9 HOH 51  2051 2051 HOH HOH C . 
OC 9 HOH 52  2052 2052 HOH HOH C . 
OC 9 HOH 53  2053 2053 HOH HOH C . 
OC 9 HOH 54  2054 2054 HOH HOH C . 
OC 9 HOH 55  2055 2055 HOH HOH C . 
OC 9 HOH 56  2056 2056 HOH HOH C . 
OC 9 HOH 57  2057 2057 HOH HOH C . 
OC 9 HOH 58  2058 2058 HOH HOH C . 
OC 9 HOH 59  2059 2059 HOH HOH C . 
OC 9 HOH 60  2060 2060 HOH HOH C . 
OC 9 HOH 61  2061 2061 HOH HOH C . 
OC 9 HOH 62  2062 2062 HOH HOH C . 
OC 9 HOH 63  2063 2063 HOH HOH C . 
OC 9 HOH 64  2064 2064 HOH HOH C . 
OC 9 HOH 65  2065 2065 HOH HOH C . 
OC 9 HOH 66  2066 2066 HOH HOH C . 
OC 9 HOH 67  2067 2067 HOH HOH C . 
OC 9 HOH 68  2068 2068 HOH HOH C . 
OC 9 HOH 69  2069 2069 HOH HOH C . 
OC 9 HOH 70  2070 2070 HOH HOH C . 
OC 9 HOH 71  2071 2071 HOH HOH C . 
OC 9 HOH 72  2072 2072 HOH HOH C . 
OC 9 HOH 73  2073 2073 HOH HOH C . 
OC 9 HOH 74  2074 2074 HOH HOH C . 
OC 9 HOH 75  2075 2075 HOH HOH C . 
OC 9 HOH 76  2076 2076 HOH HOH C . 
OC 9 HOH 77  2077 2077 HOH HOH C . 
OC 9 HOH 78  2078 2078 HOH HOH C . 
OC 9 HOH 79  2079 2079 HOH HOH C . 
OC 9 HOH 80  2080 2080 HOH HOH C . 
OC 9 HOH 81  2081 2081 HOH HOH C . 
OC 9 HOH 82  2082 2082 HOH HOH C . 
OC 9 HOH 83  2083 2083 HOH HOH C . 
OC 9 HOH 84  2084 2084 HOH HOH C . 
OC 9 HOH 85  2085 2085 HOH HOH C . 
OC 9 HOH 86  2086 2086 HOH HOH C . 
OC 9 HOH 87  2087 2087 HOH HOH C . 
OC 9 HOH 88  2088 2088 HOH HOH C . 
OC 9 HOH 89  2089 2089 HOH HOH C . 
OC 9 HOH 90  2090 2090 HOH HOH C . 
OC 9 HOH 91  2091 2091 HOH HOH C . 
OC 9 HOH 92  2092 2092 HOH HOH C . 
OC 9 HOH 93  2093 2093 HOH HOH C . 
OC 9 HOH 94  2094 2094 HOH HOH C . 
OC 9 HOH 95  2095 2095 HOH HOH C . 
OC 9 HOH 96  2096 2096 HOH HOH C . 
OC 9 HOH 97  2097 2097 HOH HOH C . 
OC 9 HOH 98  2098 2098 HOH HOH C . 
OC 9 HOH 99  2099 2099 HOH HOH C . 
OC 9 HOH 100 2100 2100 HOH HOH C . 
OC 9 HOH 101 2101 2101 HOH HOH C . 
OC 9 HOH 102 2102 2102 HOH HOH C . 
OC 9 HOH 103 2103 2103 HOH HOH C . 
OC 9 HOH 104 2104 2104 HOH HOH C . 
OC 9 HOH 105 2105 2105 HOH HOH C . 
OC 9 HOH 106 2106 2106 HOH HOH C . 
OC 9 HOH 107 2107 2107 HOH HOH C . 
OC 9 HOH 108 2108 2108 HOH HOH C . 
OC 9 HOH 109 2109 2109 HOH HOH C . 
OC 9 HOH 110 2110 2110 HOH HOH C . 
OC 9 HOH 111 2111 2111 HOH HOH C . 
OC 9 HOH 112 2112 2112 HOH HOH C . 
OC 9 HOH 113 2113 2113 HOH HOH C . 
OC 9 HOH 114 2114 2114 HOH HOH C . 
OC 9 HOH 115 2115 2115 HOH HOH C . 
OC 9 HOH 116 2116 2116 HOH HOH C . 
OC 9 HOH 117 2117 2117 HOH HOH C . 
OC 9 HOH 118 2118 2118 HOH HOH C . 
OC 9 HOH 119 2119 2119 HOH HOH C . 
OC 9 HOH 120 2120 2120 HOH HOH C . 
OC 9 HOH 121 2121 2121 HOH HOH C . 
OC 9 HOH 122 2122 2122 HOH HOH C . 
OC 9 HOH 123 2123 2123 HOH HOH C . 
OC 9 HOH 124 2124 2124 HOH HOH C . 
OC 9 HOH 125 2125 2125 HOH HOH C . 
OC 9 HOH 126 2126 2126 HOH HOH C . 
OC 9 HOH 127 2127 2127 HOH HOH C . 
OC 9 HOH 128 2128 2128 HOH HOH C . 
OC 9 HOH 129 2129 2129 HOH HOH C . 
OC 9 HOH 130 2130 2130 HOH HOH C . 
OC 9 HOH 131 2131 2131 HOH HOH C . 
OC 9 HOH 132 2132 2132 HOH HOH C . 
OC 9 HOH 133 2133 2133 HOH HOH C . 
OC 9 HOH 134 2134 2134 HOH HOH C . 
OC 9 HOH 135 2135 2135 HOH HOH C . 
OC 9 HOH 136 2136 2136 HOH HOH C . 
OC 9 HOH 137 2137 2137 HOH HOH C . 
OC 9 HOH 138 2138 2138 HOH HOH C . 
OC 9 HOH 139 2139 2139 HOH HOH C . 
OC 9 HOH 140 2140 2140 HOH HOH C . 
OC 9 HOH 141 2141 2141 HOH HOH C . 
OC 9 HOH 142 2142 2142 HOH HOH C . 
OC 9 HOH 143 2143 2143 HOH HOH C . 
OC 9 HOH 144 2144 2144 HOH HOH C . 
OC 9 HOH 145 2145 2145 HOH HOH C . 
OC 9 HOH 146 2146 2146 HOH HOH C . 
OC 9 HOH 147 2147 2147 HOH HOH C . 
OC 9 HOH 148 2148 2148 HOH HOH C . 
OC 9 HOH 149 2149 2149 HOH HOH C . 
OC 9 HOH 150 2150 2150 HOH HOH C . 
OC 9 HOH 151 2151 2151 HOH HOH C . 
OC 9 HOH 152 2152 2152 HOH HOH C . 
OC 9 HOH 153 2153 2153 HOH HOH C . 
OC 9 HOH 154 2154 2154 HOH HOH C . 
OC 9 HOH 155 2155 2155 HOH HOH C . 
OC 9 HOH 156 2156 2156 HOH HOH C . 
OC 9 HOH 157 2157 2157 HOH HOH C . 
OC 9 HOH 158 2158 2158 HOH HOH C . 
OC 9 HOH 159 2159 2159 HOH HOH C . 
OC 9 HOH 160 2160 2160 HOH HOH C . 
OC 9 HOH 161 2161 2161 HOH HOH C . 
OC 9 HOH 162 2162 2162 HOH HOH C . 
OC 9 HOH 163 2163 2163 HOH HOH C . 
OC 9 HOH 164 2164 2164 HOH HOH C . 
OC 9 HOH 165 2165 2165 HOH HOH C . 
OC 9 HOH 166 2166 2166 HOH HOH C . 
OC 9 HOH 167 2167 2167 HOH HOH C . 
OC 9 HOH 168 2168 2168 HOH HOH C . 
OC 9 HOH 169 2169 2169 HOH HOH C . 
OC 9 HOH 170 2170 2170 HOH HOH C . 
OC 9 HOH 171 2171 2171 HOH HOH C . 
OC 9 HOH 172 2172 2172 HOH HOH C . 
OC 9 HOH 173 2173 2173 HOH HOH C . 
OC 9 HOH 174 2174 2174 HOH HOH C . 
OC 9 HOH 175 2175 2175 HOH HOH C . 
OC 9 HOH 176 2176 2176 HOH HOH C . 
OC 9 HOH 177 2177 2177 HOH HOH C . 
OC 9 HOH 178 2178 2178 HOH HOH C . 
OC 9 HOH 179 2179 2179 HOH HOH C . 
OC 9 HOH 180 2180 2180 HOH HOH C . 
OC 9 HOH 181 2181 2181 HOH HOH C . 
OC 9 HOH 182 2182 2182 HOH HOH C . 
OC 9 HOH 183 2183 2183 HOH HOH C . 
OC 9 HOH 184 2184 2184 HOH HOH C . 
OC 9 HOH 185 2185 2185 HOH HOH C . 
OC 9 HOH 186 2186 2186 HOH HOH C . 
OC 9 HOH 187 2187 2187 HOH HOH C . 
OC 9 HOH 188 2188 2188 HOH HOH C . 
OC 9 HOH 189 2189 2189 HOH HOH C . 
OC 9 HOH 190 2190 2190 HOH HOH C . 
OC 9 HOH 191 2191 2191 HOH HOH C . 
OC 9 HOH 192 2192 2192 HOH HOH C . 
OC 9 HOH 193 2193 2193 HOH HOH C . 
OC 9 HOH 194 2194 2194 HOH HOH C . 
OC 9 HOH 195 2195 2195 HOH HOH C . 
OC 9 HOH 196 2196 2196 HOH HOH C . 
OC 9 HOH 197 2197 2197 HOH HOH C . 
OC 9 HOH 198 2198 2198 HOH HOH C . 
OC 9 HOH 199 2199 2199 HOH HOH C . 
OC 9 HOH 200 2200 2200 HOH HOH C . 
OC 9 HOH 201 2201 2201 HOH HOH C . 
OC 9 HOH 202 2202 2202 HOH HOH C . 
OC 9 HOH 203 2203 2203 HOH HOH C . 
OC 9 HOH 204 2204 2204 HOH HOH C . 
OC 9 HOH 205 2205 2205 HOH HOH C . 
OC 9 HOH 206 2206 2206 HOH HOH C . 
OC 9 HOH 207 2207 2207 HOH HOH C . 
OC 9 HOH 208 2208 2208 HOH HOH C . 
OC 9 HOH 209 2209 2209 HOH HOH C . 
OC 9 HOH 210 2210 2210 HOH HOH C . 
OC 9 HOH 211 2211 2211 HOH HOH C . 
OC 9 HOH 212 2212 2212 HOH HOH C . 
OC 9 HOH 213 2213 2213 HOH HOH C . 
OC 9 HOH 214 2214 2214 HOH HOH C . 
OC 9 HOH 215 2215 2215 HOH HOH C . 
OC 9 HOH 216 2216 2216 HOH HOH C . 
OC 9 HOH 217 2217 2217 HOH HOH C . 
OC 9 HOH 218 2218 2218 HOH HOH C . 
OC 9 HOH 219 2219 2219 HOH HOH C . 
OC 9 HOH 220 2220 2220 HOH HOH C . 
OC 9 HOH 221 2221 2221 HOH HOH C . 
OC 9 HOH 222 2222 2222 HOH HOH C . 
OC 9 HOH 223 2223 2223 HOH HOH C . 
OC 9 HOH 224 2224 2224 HOH HOH C . 
OC 9 HOH 225 2225 2225 HOH HOH C . 
OC 9 HOH 226 2226 2226 HOH HOH C . 
OC 9 HOH 227 2227 2227 HOH HOH C . 
OC 9 HOH 228 2228 2228 HOH HOH C . 
OC 9 HOH 229 2229 2229 HOH HOH C . 
OC 9 HOH 230 2230 2230 HOH HOH C . 
OC 9 HOH 231 2231 2231 HOH HOH C . 
OC 9 HOH 232 2232 2232 HOH HOH C . 
OC 9 HOH 233 2233 2233 HOH HOH C . 
OC 9 HOH 234 2234 2234 HOH HOH C . 
OC 9 HOH 235 2235 2235 HOH HOH C . 
OC 9 HOH 236 2236 2236 HOH HOH C . 
OC 9 HOH 237 2237 2237 HOH HOH C . 
OC 9 HOH 238 2238 2238 HOH HOH C . 
OC 9 HOH 239 2239 2239 HOH HOH C . 
OC 9 HOH 240 2240 2240 HOH HOH C . 
OC 9 HOH 241 2241 2241 HOH HOH C . 
OC 9 HOH 242 2242 2242 HOH HOH C . 
OC 9 HOH 243 2243 2243 HOH HOH C . 
OC 9 HOH 244 2244 2244 HOH HOH C . 
OC 9 HOH 245 2245 2245 HOH HOH C . 
OC 9 HOH 246 2246 2246 HOH HOH C . 
OC 9 HOH 247 2247 2247 HOH HOH C . 
OC 9 HOH 248 2248 2248 HOH HOH C . 
OC 9 HOH 249 2249 2249 HOH HOH C . 
OC 9 HOH 250 2250 2250 HOH HOH C . 
OC 9 HOH 251 2251 2251 HOH HOH C . 
OC 9 HOH 252 2252 2252 HOH HOH C . 
OC 9 HOH 253 2253 2253 HOH HOH C . 
OC 9 HOH 254 2254 2254 HOH HOH C . 
OC 9 HOH 255 2255 2255 HOH HOH C . 
OC 9 HOH 256 2256 2256 HOH HOH C . 
OC 9 HOH 257 2257 2257 HOH HOH C . 
OC 9 HOH 258 2258 2258 HOH HOH C . 
OC 9 HOH 259 2259 2259 HOH HOH C . 
OC 9 HOH 260 2260 2260 HOH HOH C . 
OC 9 HOH 261 2261 2261 HOH HOH C . 
OC 9 HOH 262 2262 2262 HOH HOH C . 
OC 9 HOH 263 2263 2263 HOH HOH C . 
OC 9 HOH 264 2264 2264 HOH HOH C . 
OC 9 HOH 265 2265 2265 HOH HOH C . 
OC 9 HOH 266 2266 2266 HOH HOH C . 
OC 9 HOH 267 2267 2267 HOH HOH C . 
OC 9 HOH 268 2268 2268 HOH HOH C . 
OC 9 HOH 269 2269 2269 HOH HOH C . 
OC 9 HOH 270 2270 2270 HOH HOH C . 
OC 9 HOH 271 2271 2271 HOH HOH C . 
OC 9 HOH 272 2272 2272 HOH HOH C . 
OC 9 HOH 273 2273 2273 HOH HOH C . 
OC 9 HOH 274 2274 2274 HOH HOH C . 
OC 9 HOH 275 2275 2275 HOH HOH C . 
OC 9 HOH 276 2276 2276 HOH HOH C . 
OC 9 HOH 277 2277 2277 HOH HOH C . 
OC 9 HOH 278 2278 2278 HOH HOH C . 
OC 9 HOH 279 2279 2279 HOH HOH C . 
OC 9 HOH 280 2280 2280 HOH HOH C . 
OC 9 HOH 281 2281 2281 HOH HOH C . 
OC 9 HOH 282 2282 2282 HOH HOH C . 
OC 9 HOH 283 2283 2283 HOH HOH C . 
OC 9 HOH 284 2284 2284 HOH HOH C . 
OC 9 HOH 285 2285 2285 HOH HOH C . 
OC 9 HOH 286 2286 2286 HOH HOH C . 
OC 9 HOH 287 2287 2287 HOH HOH C . 
OC 9 HOH 288 2288 2288 HOH HOH C . 
OC 9 HOH 289 2289 2289 HOH HOH C . 
OC 9 HOH 290 2290 2290 HOH HOH C . 
OC 9 HOH 291 2291 2291 HOH HOH C . 
PC 9 HOH 1   2001 2001 HOH HOH D . 
PC 9 HOH 2   2002 2002 HOH HOH D . 
PC 9 HOH 3   2003 2003 HOH HOH D . 
PC 9 HOH 4   2004 2004 HOH HOH D . 
PC 9 HOH 5   2005 2005 HOH HOH D . 
PC 9 HOH 6   2006 2006 HOH HOH D . 
PC 9 HOH 7   2007 2007 HOH HOH D . 
PC 9 HOH 8   2008 2008 HOH HOH D . 
PC 9 HOH 9   2009 2009 HOH HOH D . 
PC 9 HOH 10  2010 2010 HOH HOH D . 
PC 9 HOH 11  2011 2011 HOH HOH D . 
PC 9 HOH 12  2012 2012 HOH HOH D . 
PC 9 HOH 13  2013 2013 HOH HOH D . 
PC 9 HOH 14  2014 2014 HOH HOH D . 
PC 9 HOH 15  2015 2015 HOH HOH D . 
PC 9 HOH 16  2016 2016 HOH HOH D . 
PC 9 HOH 17  2017 2017 HOH HOH D . 
PC 9 HOH 18  2018 2018 HOH HOH D . 
PC 9 HOH 19  2019 2019 HOH HOH D . 
PC 9 HOH 20  2020 2020 HOH HOH D . 
PC 9 HOH 21  2021 2021 HOH HOH D . 
PC 9 HOH 22  2022 2022 HOH HOH D . 
PC 9 HOH 23  2023 2023 HOH HOH D . 
PC 9 HOH 24  2024 2024 HOH HOH D . 
PC 9 HOH 25  2025 2025 HOH HOH D . 
PC 9 HOH 26  2026 2026 HOH HOH D . 
PC 9 HOH 27  2027 2027 HOH HOH D . 
PC 9 HOH 28  2028 2028 HOH HOH D . 
PC 9 HOH 29  2029 2029 HOH HOH D . 
PC 9 HOH 30  2030 2030 HOH HOH D . 
PC 9 HOH 31  2031 2031 HOH HOH D . 
PC 9 HOH 32  2032 2032 HOH HOH D . 
PC 9 HOH 33  2033 2033 HOH HOH D . 
PC 9 HOH 34  2034 2034 HOH HOH D . 
PC 9 HOH 35  2035 2035 HOH HOH D . 
PC 9 HOH 36  2036 2036 HOH HOH D . 
PC 9 HOH 37  2037 2037 HOH HOH D . 
PC 9 HOH 38  2038 2038 HOH HOH D . 
PC 9 HOH 39  2039 2039 HOH HOH D . 
PC 9 HOH 40  2040 2040 HOH HOH D . 
PC 9 HOH 41  2041 2041 HOH HOH D . 
PC 9 HOH 42  2042 2042 HOH HOH D . 
PC 9 HOH 43  2043 2043 HOH HOH D . 
PC 9 HOH 44  2044 2044 HOH HOH D . 
PC 9 HOH 45  2045 2045 HOH HOH D . 
PC 9 HOH 46  2046 2046 HOH HOH D . 
PC 9 HOH 47  2047 2047 HOH HOH D . 
PC 9 HOH 48  2048 2048 HOH HOH D . 
PC 9 HOH 49  2049 2049 HOH HOH D . 
PC 9 HOH 50  2050 2050 HOH HOH D . 
PC 9 HOH 51  2051 2051 HOH HOH D . 
PC 9 HOH 52  2052 2052 HOH HOH D . 
PC 9 HOH 53  2053 2053 HOH HOH D . 
PC 9 HOH 54  2054 2054 HOH HOH D . 
PC 9 HOH 55  2055 2055 HOH HOH D . 
PC 9 HOH 56  2056 2056 HOH HOH D . 
PC 9 HOH 57  2057 2057 HOH HOH D . 
PC 9 HOH 58  2058 2058 HOH HOH D . 
PC 9 HOH 59  2059 2059 HOH HOH D . 
PC 9 HOH 60  2060 2060 HOH HOH D . 
PC 9 HOH 61  2061 2061 HOH HOH D . 
PC 9 HOH 62  2062 2062 HOH HOH D . 
PC 9 HOH 63  2063 2063 HOH HOH D . 
PC 9 HOH 64  2064 2064 HOH HOH D . 
PC 9 HOH 65  2065 2065 HOH HOH D . 
PC 9 HOH 66  2066 2066 HOH HOH D . 
PC 9 HOH 67  2067 2067 HOH HOH D . 
PC 9 HOH 68  2068 2068 HOH HOH D . 
PC 9 HOH 69  2069 2069 HOH HOH D . 
PC 9 HOH 70  2070 2070 HOH HOH D . 
PC 9 HOH 71  2071 2071 HOH HOH D . 
PC 9 HOH 72  2072 2072 HOH HOH D . 
PC 9 HOH 73  2073 2073 HOH HOH D . 
PC 9 HOH 74  2074 2074 HOH HOH D . 
PC 9 HOH 75  2075 2075 HOH HOH D . 
PC 9 HOH 76  2076 2076 HOH HOH D . 
PC 9 HOH 77  2077 2077 HOH HOH D . 
PC 9 HOH 78  2078 2078 HOH HOH D . 
PC 9 HOH 79  2079 2079 HOH HOH D . 
PC 9 HOH 80  2080 2080 HOH HOH D . 
PC 9 HOH 81  2081 2081 HOH HOH D . 
PC 9 HOH 82  2082 2082 HOH HOH D . 
PC 9 HOH 83  2083 2083 HOH HOH D . 
PC 9 HOH 84  2084 2084 HOH HOH D . 
PC 9 HOH 85  2085 2085 HOH HOH D . 
PC 9 HOH 86  2086 2086 HOH HOH D . 
PC 9 HOH 87  2087 2087 HOH HOH D . 
PC 9 HOH 88  2088 2088 HOH HOH D . 
PC 9 HOH 89  2089 2089 HOH HOH D . 
PC 9 HOH 90  2090 2090 HOH HOH D . 
PC 9 HOH 91  2091 2091 HOH HOH D . 
PC 9 HOH 92  2092 2092 HOH HOH D . 
PC 9 HOH 93  2093 2093 HOH HOH D . 
PC 9 HOH 94  2094 2094 HOH HOH D . 
PC 9 HOH 95  2095 2095 HOH HOH D . 
PC 9 HOH 96  2096 2096 HOH HOH D . 
PC 9 HOH 97  2097 2097 HOH HOH D . 
PC 9 HOH 98  2098 2098 HOH HOH D . 
PC 9 HOH 99  2099 2099 HOH HOH D . 
PC 9 HOH 100 2100 2100 HOH HOH D . 
PC 9 HOH 101 2101 2101 HOH HOH D . 
PC 9 HOH 102 2102 2102 HOH HOH D . 
PC 9 HOH 103 2103 2103 HOH HOH D . 
PC 9 HOH 104 2104 2104 HOH HOH D . 
PC 9 HOH 105 2105 2105 HOH HOH D . 
PC 9 HOH 106 2106 2106 HOH HOH D . 
PC 9 HOH 107 2107 2107 HOH HOH D . 
PC 9 HOH 108 2108 2108 HOH HOH D . 
PC 9 HOH 109 2109 2109 HOH HOH D . 
PC 9 HOH 110 2110 2110 HOH HOH D . 
PC 9 HOH 111 2111 2111 HOH HOH D . 
PC 9 HOH 112 2112 2112 HOH HOH D . 
PC 9 HOH 113 2113 2113 HOH HOH D . 
PC 9 HOH 114 2114 2114 HOH HOH D . 
PC 9 HOH 115 2115 2115 HOH HOH D . 
PC 9 HOH 116 2116 2116 HOH HOH D . 
PC 9 HOH 117 2117 2117 HOH HOH D . 
PC 9 HOH 118 2118 2118 HOH HOH D . 
PC 9 HOH 119 2119 2119 HOH HOH D . 
PC 9 HOH 120 2120 2120 HOH HOH D . 
PC 9 HOH 121 2121 2121 HOH HOH D . 
PC 9 HOH 122 2122 2122 HOH HOH D . 
PC 9 HOH 123 2123 2123 HOH HOH D . 
PC 9 HOH 124 2124 2124 HOH HOH D . 
PC 9 HOH 125 2125 2125 HOH HOH D . 
PC 9 HOH 126 2126 2126 HOH HOH D . 
PC 9 HOH 127 2127 2127 HOH HOH D . 
PC 9 HOH 128 2128 2128 HOH HOH D . 
PC 9 HOH 129 2129 2129 HOH HOH D . 
PC 9 HOH 130 2130 2130 HOH HOH D . 
PC 9 HOH 131 2131 2131 HOH HOH D . 
PC 9 HOH 132 2132 2132 HOH HOH D . 
PC 9 HOH 133 2133 2133 HOH HOH D . 
PC 9 HOH 134 2134 2134 HOH HOH D . 
PC 9 HOH 135 2135 2135 HOH HOH D . 
PC 9 HOH 136 2136 2136 HOH HOH D . 
PC 9 HOH 137 2137 2137 HOH HOH D . 
PC 9 HOH 138 2138 2138 HOH HOH D . 
PC 9 HOH 139 2139 2139 HOH HOH D . 
PC 9 HOH 140 2140 2140 HOH HOH D . 
PC 9 HOH 141 2141 2141 HOH HOH D . 
PC 9 HOH 142 2142 2142 HOH HOH D . 
PC 9 HOH 143 2143 2143 HOH HOH D . 
PC 9 HOH 144 2144 2144 HOH HOH D . 
PC 9 HOH 145 2145 2145 HOH HOH D . 
PC 9 HOH 146 2146 2146 HOH HOH D . 
PC 9 HOH 147 2147 2147 HOH HOH D . 
PC 9 HOH 148 2148 2148 HOH HOH D . 
PC 9 HOH 149 2149 2149 HOH HOH D . 
PC 9 HOH 150 2150 2150 HOH HOH D . 
PC 9 HOH 151 2151 2151 HOH HOH D . 
PC 9 HOH 152 2152 2152 HOH HOH D . 
PC 9 HOH 153 2153 2153 HOH HOH D . 
PC 9 HOH 154 2154 2154 HOH HOH D . 
PC 9 HOH 155 2155 2155 HOH HOH D . 
PC 9 HOH 156 2156 2156 HOH HOH D . 
PC 9 HOH 157 2157 2157 HOH HOH D . 
PC 9 HOH 158 2158 2158 HOH HOH D . 
PC 9 HOH 159 2159 2159 HOH HOH D . 
PC 9 HOH 160 2160 2160 HOH HOH D . 
PC 9 HOH 161 2161 2161 HOH HOH D . 
PC 9 HOH 162 2162 2162 HOH HOH D . 
PC 9 HOH 163 2163 2163 HOH HOH D . 
PC 9 HOH 164 2164 2164 HOH HOH D . 
PC 9 HOH 165 2165 2165 HOH HOH D . 
PC 9 HOH 166 2166 2166 HOH HOH D . 
PC 9 HOH 167 2167 2167 HOH HOH D . 
PC 9 HOH 168 2168 2168 HOH HOH D . 
PC 9 HOH 169 2169 2169 HOH HOH D . 
PC 9 HOH 170 2170 2170 HOH HOH D . 
PC 9 HOH 171 2171 2171 HOH HOH D . 
PC 9 HOH 172 2172 2172 HOH HOH D . 
PC 9 HOH 173 2173 2173 HOH HOH D . 
PC 9 HOH 174 2174 2174 HOH HOH D . 
PC 9 HOH 175 2175 2175 HOH HOH D . 
PC 9 HOH 176 2176 2176 HOH HOH D . 
PC 9 HOH 177 2177 2177 HOH HOH D . 
PC 9 HOH 178 2178 2178 HOH HOH D . 
PC 9 HOH 179 2179 2179 HOH HOH D . 
PC 9 HOH 180 2180 2180 HOH HOH D . 
PC 9 HOH 181 2181 2181 HOH HOH D . 
PC 9 HOH 182 2182 2182 HOH HOH D . 
PC 9 HOH 183 2183 2183 HOH HOH D . 
PC 9 HOH 184 2184 2184 HOH HOH D . 
PC 9 HOH 185 2185 2185 HOH HOH D . 
PC 9 HOH 186 2186 2186 HOH HOH D . 
PC 9 HOH 187 2187 2187 HOH HOH D . 
PC 9 HOH 188 2188 2188 HOH HOH D . 
PC 9 HOH 189 2189 2189 HOH HOH D . 
PC 9 HOH 190 2190 2190 HOH HOH D . 
PC 9 HOH 191 2191 2191 HOH HOH D . 
PC 9 HOH 192 2192 2192 HOH HOH D . 
PC 9 HOH 193 2193 2193 HOH HOH D . 
PC 9 HOH 194 2194 2194 HOH HOH D . 
PC 9 HOH 195 2195 2195 HOH HOH D . 
PC 9 HOH 196 2196 2196 HOH HOH D . 
PC 9 HOH 197 2197 2197 HOH HOH D . 
PC 9 HOH 198 2198 2198 HOH HOH D . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1  A ASN 8   A ASN 11  ? ASN 'GLYCOSYLATION SITE' 
2  A ASN 138 A ASN 141 ? ASN 'GLYCOSYLATION SITE' 
3  A ASN 158 A ASN 161 ? ASN 'GLYCOSYLATION SITE' 
4  A ASN 179 A ASN 182 ? ASN 'GLYCOSYLATION SITE' 
5  A ASN 283 A ASN 286 ? ASN 'GLYCOSYLATION SITE' 
6  B ASN 8   B ASN 11  ? ASN 'GLYCOSYLATION SITE' 
7  B ASN 138 B ASN 141 ? ASN 'GLYCOSYLATION SITE' 
8  B ASN 158 B ASN 161 ? ASN 'GLYCOSYLATION SITE' 
9  B ASN 179 B ASN 182 ? ASN 'GLYCOSYLATION SITE' 
10 B ASN 283 B ASN 286 ? ASN 'GLYCOSYLATION SITE' 
11 C ASN 8   C ASN 11  ? ASN 'GLYCOSYLATION SITE' 
12 C ASN 138 C ASN 141 ? ASN 'GLYCOSYLATION SITE' 
13 C ASN 158 C ASN 161 ? ASN 'GLYCOSYLATION SITE' 
14 C ASN 179 C ASN 182 ? ASN 'GLYCOSYLATION SITE' 
15 C ASN 283 C ASN 286 ? ASN 'GLYCOSYLATION SITE' 
16 D ASN 8   D ASN 11  ? ASN 'GLYCOSYLATION SITE' 
17 D ASN 138 D ASN 141 ? ASN 'GLYCOSYLATION SITE' 
18 D ASN 158 D ASN 161 ? ASN 'GLYCOSYLATION SITE' 
19 D ASN 179 D ASN 182 ? ASN 'GLYCOSYLATION SITE' 
20 D ASN 283 D ASN 286 ? ASN 'GLYCOSYLATION SITE' 
# 
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_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 
A,C,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,HB,IB,JB,KB,LB,MB,NB,OB,PB,QB,RB,SB,TB,UB,VB,WB,XB,YB,MC,OC 
2 1 B,D,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA,UA,VA,WA,XA,YA,ZA,AB,BB,CB,DB,EB,FB,GB,ZB,AC,BC,CC,DC,EC,FC,GC,HC,IC,JC,KC,LC,NC,PC 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 14780 ? 
1 MORE         -88.1 ? 
1 'SSA (A^2)'  27400 ? 
2 'ABSA (A^2)' 12750 ? 
2 MORE         -71.6 ? 
2 'SSA (A^2)'  26740 ? 
# 
_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_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   O1A ? E  HEM .   ? A HEM 350  ? 1_555 MG ? F  MG  . ? A MG  353 ? 1_555 O   ? A  GLY 120 ? A GLY 123  ? 1_555 85.0  ? 
2   O1A ? E  HEM .   ? A HEM 350  ? 1_555 MG ? F  MG  . ? A MG  353 ? 1_555 OG  ? A  SER 123 ? A SER 126  ? 1_555 86.9  ? 
3   O   ? A  GLY 120 ? A GLY 123  ? 1_555 MG ? F  MG  . ? A MG  353 ? 1_555 OG  ? A  SER 123 ? A SER 126  ? 1_555 91.6  ? 
4   O1A ? E  HEM .   ? A HEM 350  ? 1_555 MG ? F  MG  . ? A MG  353 ? 1_555 O   ? MC HOH .   ? A HOH 2123 ? 1_555 87.6  ? 
5   O   ? A  GLY 120 ? A GLY 123  ? 1_555 MG ? F  MG  . ? A MG  353 ? 1_555 O   ? MC HOH .   ? A HOH 2123 ? 1_555 168.4 ? 
6   OG  ? A  SER 123 ? A SER 126  ? 1_555 MG ? F  MG  . ? A MG  353 ? 1_555 O   ? MC HOH .   ? A HOH 2123 ? 1_555 97.0  ? 
7   O1A ? E  HEM .   ? A HEM 350  ? 1_555 MG ? F  MG  . ? A MG  353 ? 1_555 O   ? MC HOH .   ? A HOH 2124 ? 1_555 175.1 ? 
8   O   ? A  GLY 120 ? A GLY 123  ? 1_555 MG ? F  MG  . ? A MG  353 ? 1_555 O   ? MC HOH .   ? A HOH 2124 ? 1_555 90.4  ? 
9   OG  ? A  SER 123 ? A SER 126  ? 1_555 MG ? F  MG  . ? A MG  353 ? 1_555 O   ? MC HOH .   ? A HOH 2124 ? 1_555 91.2  ? 
10  O   ? MC HOH .   ? A HOH 2123 ? 1_555 MG ? F  MG  . ? A MG  353 ? 1_555 O   ? MC HOH .   ? A HOH 2124 ? 1_555 97.1  ? 
11  O1A ? E  HEM .   ? A HEM 350  ? 1_555 MG ? F  MG  . ? A MG  353 ? 1_555 OE2 ? A  GLU 119 ? A GLU 122  ? 1_555 97.9  ? 
12  O   ? A  GLY 120 ? A GLY 123  ? 1_555 MG ? F  MG  . ? A MG  353 ? 1_555 OE2 ? A  GLU 119 ? A GLU 122  ? 1_555 88.3  ? 
13  OG  ? A  SER 123 ? A SER 126  ? 1_555 MG ? F  MG  . ? A MG  353 ? 1_555 OE2 ? A  GLU 119 ? A GLU 122  ? 1_555 175.1 ? 
14  O   ? MC HOH .   ? A HOH 2123 ? 1_555 MG ? F  MG  . ? A MG  353 ? 1_555 OE2 ? A  GLU 119 ? A GLU 122  ? 1_555 83.8  ? 
15  O   ? MC HOH .   ? A HOH 2124 ? 1_555 MG ? F  MG  . ? A MG  353 ? 1_555 OE2 ? A  GLU 119 ? A GLU 122  ? 1_555 83.9  ? 
16  SG  ? A  CYS 33  ? A CYS 36   ? 1_555 FE ? E  HEM . ? A HEM 350 ? 1_555 NA  ? E  HEM .   ? A HEM 350  ? 1_555 96.7  ? 
17  SG  ? A  CYS 33  ? A CYS 36   ? 1_555 FE ? E  HEM . ? A HEM 350 ? 1_555 NB  ? E  HEM .   ? A HEM 350  ? 1_555 92.9  ? 
18  NA  ? E  HEM .   ? A HEM 350  ? 1_555 FE ? E  HEM . ? A HEM 350 ? 1_555 NB  ? E  HEM .   ? A HEM 350  ? 1_555 90.8  ? 
19  SG  ? A  CYS 33  ? A CYS 36   ? 1_555 FE ? E  HEM . ? A HEM 350 ? 1_555 NC  ? E  HEM .   ? A HEM 350  ? 1_555 85.5  ? 
20  NA  ? E  HEM .   ? A HEM 350  ? 1_555 FE ? E  HEM . ? A HEM 350 ? 1_555 NC  ? E  HEM .   ? A HEM 350  ? 1_555 177.8 ? 
21  NB  ? E  HEM .   ? A HEM 350  ? 1_555 FE ? E  HEM . ? A HEM 350 ? 1_555 NC  ? E  HEM .   ? A HEM 350  ? 1_555 88.8  ? 
22  SG  ? A  CYS 33  ? A CYS 36   ? 1_555 FE ? E  HEM . ? A HEM 350 ? 1_555 ND  ? E  HEM .   ? A HEM 350  ? 1_555 89.2  ? 
23  NA  ? E  HEM .   ? A HEM 350  ? 1_555 FE ? E  HEM . ? A HEM 350 ? 1_555 ND  ? E  HEM .   ? A HEM 350  ? 1_555 88.1  ? 
24  NB  ? E  HEM .   ? A HEM 350  ? 1_555 FE ? E  HEM . ? A HEM 350 ? 1_555 ND  ? E  HEM .   ? A HEM 350  ? 1_555 177.7 ? 
25  NC  ? E  HEM .   ? A HEM 350  ? 1_555 FE ? E  HEM . ? A HEM 350 ? 1_555 ND  ? E  HEM .   ? A HEM 350  ? 1_555 92.1  ? 
26  SG  ? B  CYS 33  ? B CYS 36   ? 1_555 FE ? IA HEM . ? B HEM 350 ? 1_555 NA  ? IA HEM .   ? B HEM 350  ? 1_555 99.2  ? 
27  SG  ? B  CYS 33  ? B CYS 36   ? 1_555 FE ? IA HEM . ? B HEM 350 ? 1_555 NB  ? IA HEM .   ? B HEM 350  ? 1_555 91.0  ? 
28  NA  ? IA HEM .   ? B HEM 350  ? 1_555 FE ? IA HEM . ? B HEM 350 ? 1_555 NB  ? IA HEM .   ? B HEM 350  ? 1_555 88.9  ? 
29  SG  ? B  CYS 33  ? B CYS 36   ? 1_555 FE ? IA HEM . ? B HEM 350 ? 1_555 NC  ? IA HEM .   ? B HEM 350  ? 1_555 83.5  ? 
30  NA  ? IA HEM .   ? B HEM 350  ? 1_555 FE ? IA HEM . ? B HEM 350 ? 1_555 NC  ? IA HEM .   ? B HEM 350  ? 1_555 176.8 ? 
31  NB  ? IA HEM .   ? B HEM 350  ? 1_555 FE ? IA HEM . ? B HEM 350 ? 1_555 NC  ? IA HEM .   ? B HEM 350  ? 1_555 89.4  ? 
32  SG  ? B  CYS 33  ? B CYS 36   ? 1_555 FE ? IA HEM . ? B HEM 350 ? 1_555 ND  ? IA HEM .   ? B HEM 350  ? 1_555 92.7  ? 
33  NA  ? IA HEM .   ? B HEM 350  ? 1_555 FE ? IA HEM . ? B HEM 350 ? 1_555 ND  ? IA HEM .   ? B HEM 350  ? 1_555 90.7  ? 
34  NB  ? IA HEM .   ? B HEM 350  ? 1_555 FE ? IA HEM . ? B HEM 350 ? 1_555 ND  ? IA HEM .   ? B HEM 350  ? 1_555 176.3 ? 
35  NC  ? IA HEM .   ? B HEM 350  ? 1_555 FE ? IA HEM . ? B HEM 350 ? 1_555 ND  ? IA HEM .   ? B HEM 350  ? 1_555 90.9  ? 
36  SG  ? B  CYS 33  ? B CYS 36   ? 1_555 FE ? IA HEM . ? B HEM 350 ? 1_555 O   ? DB ACT .   ? B ACT 1328 ? 1_555 169.2 ? 
37  NA  ? IA HEM .   ? B HEM 350  ? 1_555 FE ? IA HEM . ? B HEM 350 ? 1_555 O   ? DB ACT .   ? B ACT 1328 ? 1_555 70.3  ? 
38  NB  ? IA HEM .   ? B HEM 350  ? 1_555 FE ? IA HEM . ? B HEM 350 ? 1_555 O   ? DB ACT .   ? B ACT 1328 ? 1_555 86.3  ? 
39  NC  ? IA HEM .   ? B HEM 350  ? 1_555 FE ? IA HEM . ? B HEM 350 ? 1_555 O   ? DB ACT .   ? B ACT 1328 ? 1_555 106.9 ? 
40  ND  ? IA HEM .   ? B HEM 350  ? 1_555 FE ? IA HEM . ? B HEM 350 ? 1_555 O   ? DB ACT .   ? B ACT 1328 ? 1_555 90.1  ? 
41  O1A ? IA HEM .   ? B HEM 350  ? 1_555 MG ? JA MG  . ? B MG  353 ? 1_555 O   ? NC HOH .   ? B HOH 2157 ? 1_555 86.4  ? 
42  O1A ? IA HEM .   ? B HEM 350  ? 1_555 MG ? JA MG  . ? B MG  353 ? 1_555 OE2 ? B  GLU 119 ? B GLU 122  ? 1_555 95.1  ? 
43  O   ? NC HOH .   ? B HOH 2157 ? 1_555 MG ? JA MG  . ? B MG  353 ? 1_555 OE2 ? B  GLU 119 ? B GLU 122  ? 1_555 94.9  ? 
44  O1A ? IA HEM .   ? B HEM 350  ? 1_555 MG ? JA MG  . ? B MG  353 ? 1_555 O   ? B  GLY 120 ? B GLY 123  ? 1_555 81.8  ? 
45  O   ? NC HOH .   ? B HOH 2157 ? 1_555 MG ? JA MG  . ? B MG  353 ? 1_555 O   ? B  GLY 120 ? B GLY 123  ? 1_555 166.5 ? 
46  OE2 ? B  GLU 119 ? B GLU 122  ? 1_555 MG ? JA MG  . ? B MG  353 ? 1_555 O   ? B  GLY 120 ? B GLY 123  ? 1_555 79.6  ? 
47  O1A ? IA HEM .   ? B HEM 350  ? 1_555 MG ? JA MG  . ? B MG  353 ? 1_555 OG  ? B  SER 123 ? B SER 126  ? 1_555 83.6  ? 
48  O   ? NC HOH .   ? B HOH 2157 ? 1_555 MG ? JA MG  . ? B MG  353 ? 1_555 OG  ? B  SER 123 ? B SER 126  ? 1_555 91.7  ? 
49  OE2 ? B  GLU 119 ? B GLU 122  ? 1_555 MG ? JA MG  . ? B MG  353 ? 1_555 OG  ? B  SER 123 ? B SER 126  ? 1_555 173.2 ? 
50  O   ? B  GLY 120 ? B GLY 123  ? 1_555 MG ? JA MG  . ? B MG  353 ? 1_555 OG  ? B  SER 123 ? B SER 126  ? 1_555 93.6  ? 
51  O1A ? IA HEM .   ? B HEM 350  ? 1_555 MG ? JA MG  . ? B MG  353 ? 1_555 O   ? NC HOH .   ? B HOH 2158 ? 1_555 168.4 ? 
52  O   ? NC HOH .   ? B HOH 2157 ? 1_555 MG ? JA MG  . ? B MG  353 ? 1_555 O   ? NC HOH .   ? B HOH 2158 ? 1_555 104.0 ? 
53  OE2 ? B  GLU 119 ? B GLU 122  ? 1_555 MG ? JA MG  . ? B MG  353 ? 1_555 O   ? NC HOH .   ? B HOH 2158 ? 1_555 88.9  ? 
54  O   ? B  GLY 120 ? B GLY 123  ? 1_555 MG ? JA MG  . ? B MG  353 ? 1_555 O   ? NC HOH .   ? B HOH 2158 ? 1_555 88.3  ? 
55  OG  ? B  SER 123 ? B SER 126  ? 1_555 MG ? JA MG  . ? B MG  353 ? 1_555 O   ? NC HOH .   ? B HOH 2158 ? 1_555 91.1  ? 
56  O1A ? HB HEM .   ? C HEM 350  ? 1_555 MG ? IB MG  . ? C MG  353 ? 1_555 O   ? OC HOH .   ? C HOH 2132 ? 1_555 173.0 ? 
57  O1A ? HB HEM .   ? C HEM 350  ? 1_555 MG ? IB MG  . ? C MG  353 ? 1_555 OG  ? C  SER 123 ? C SER 126  ? 1_555 88.7  ? 
58  O   ? OC HOH .   ? C HOH 2132 ? 1_555 MG ? IB MG  . ? C MG  353 ? 1_555 OG  ? C  SER 123 ? C SER 126  ? 1_555 85.9  ? 
59  O1A ? HB HEM .   ? C HEM 350  ? 1_555 MG ? IB MG  . ? C MG  353 ? 1_555 O   ? OC HOH .   ? C HOH 2131 ? 1_555 95.8  ? 
60  O   ? OC HOH .   ? C HOH 2132 ? 1_555 MG ? IB MG  . ? C MG  353 ? 1_555 O   ? OC HOH .   ? C HOH 2131 ? 1_555 88.9  ? 
61  OG  ? C  SER 123 ? C SER 126  ? 1_555 MG ? IB MG  . ? C MG  353 ? 1_555 O   ? OC HOH .   ? C HOH 2131 ? 1_555 91.4  ? 
62  O1A ? HB HEM .   ? C HEM 350  ? 1_555 MG ? IB MG  . ? C MG  353 ? 1_555 O   ? C  GLY 120 ? C GLY 123  ? 1_555 87.5  ? 
63  O   ? OC HOH .   ? C HOH 2132 ? 1_555 MG ? IB MG  . ? C MG  353 ? 1_555 O   ? C  GLY 120 ? C GLY 123  ? 1_555 88.9  ? 
64  OG  ? C  SER 123 ? C SER 126  ? 1_555 MG ? IB MG  . ? C MG  353 ? 1_555 O   ? C  GLY 120 ? C GLY 123  ? 1_555 100.1 ? 
65  O   ? OC HOH .   ? C HOH 2131 ? 1_555 MG ? IB MG  . ? C MG  353 ? 1_555 O   ? C  GLY 120 ? C GLY 123  ? 1_555 168.0 ? 
66  O1A ? HB HEM .   ? C HEM 350  ? 1_555 MG ? IB MG  . ? C MG  353 ? 1_555 OE2 ? C  GLU 119 ? C GLU 122  ? 1_555 103.2 ? 
67  O   ? OC HOH .   ? C HOH 2132 ? 1_555 MG ? IB MG  . ? C MG  353 ? 1_555 OE2 ? C  GLU 119 ? C GLU 122  ? 1_555 82.1  ? 
68  OG  ? C  SER 123 ? C SER 126  ? 1_555 MG ? IB MG  . ? C MG  353 ? 1_555 OE2 ? C  GLU 119 ? C GLU 122  ? 1_555 168.0 ? 
69  O   ? OC HOH .   ? C HOH 2131 ? 1_555 MG ? IB MG  . ? C MG  353 ? 1_555 OE2 ? C  GLU 119 ? C GLU 122  ? 1_555 87.8  ? 
70  O   ? C  GLY 120 ? C GLY 123  ? 1_555 MG ? IB MG  . ? C MG  353 ? 1_555 OE2 ? C  GLU 119 ? C GLU 122  ? 1_555 80.2  ? 
71  SG  ? C  CYS 33  ? C CYS 36   ? 1_555 FE ? HB HEM . ? C HEM 350 ? 1_555 NA  ? HB HEM .   ? C HEM 350  ? 1_555 96.6  ? 
72  SG  ? C  CYS 33  ? C CYS 36   ? 1_555 FE ? HB HEM . ? C HEM 350 ? 1_555 NB  ? HB HEM .   ? C HEM 350  ? 1_555 90.2  ? 
73  NA  ? HB HEM .   ? C HEM 350  ? 1_555 FE ? HB HEM . ? C HEM 350 ? 1_555 NB  ? HB HEM .   ? C HEM 350  ? 1_555 92.7  ? 
74  SG  ? C  CYS 33  ? C CYS 36   ? 1_555 FE ? HB HEM . ? C HEM 350 ? 1_555 NC  ? HB HEM .   ? C HEM 350  ? 1_555 85.7  ? 
75  NA  ? HB HEM .   ? C HEM 350  ? 1_555 FE ? HB HEM . ? C HEM 350 ? 1_555 NC  ? HB HEM .   ? C HEM 350  ? 1_555 177.6 ? 
76  NB  ? HB HEM .   ? C HEM 350  ? 1_555 FE ? HB HEM . ? C HEM 350 ? 1_555 NC  ? HB HEM .   ? C HEM 350  ? 1_555 87.8  ? 
77  SG  ? C  CYS 33  ? C CYS 36   ? 1_555 FE ? HB HEM . ? C HEM 350 ? 1_555 ND  ? HB HEM .   ? C HEM 350  ? 1_555 92.4  ? 
78  NA  ? HB HEM .   ? C HEM 350  ? 1_555 FE ? HB HEM . ? C HEM 350 ? 1_555 ND  ? HB HEM .   ? C HEM 350  ? 1_555 86.6  ? 
79  NB  ? HB HEM .   ? C HEM 350  ? 1_555 FE ? HB HEM . ? C HEM 350 ? 1_555 ND  ? HB HEM .   ? C HEM 350  ? 1_555 177.4 ? 
80  NC  ? HB HEM .   ? C HEM 350  ? 1_555 FE ? HB HEM . ? C HEM 350 ? 1_555 ND  ? HB HEM .   ? C HEM 350  ? 1_555 92.8  ? 
81  O1A ? ZB HEM .   ? D HEM 350  ? 1_555 MG ? AC MG  . ? D MG  353 ? 1_555 OE2 ? D  GLU 119 ? D GLU 122  ? 1_555 104.0 ? 
82  O1A ? ZB HEM .   ? D HEM 350  ? 1_555 MG ? AC MG  . ? D MG  353 ? 1_555 O   ? PC HOH .   ? D HOH 2084 ? 1_555 171.4 ? 
83  OE2 ? D  GLU 119 ? D GLU 122  ? 1_555 MG ? AC MG  . ? D MG  353 ? 1_555 O   ? PC HOH .   ? D HOH 2084 ? 1_555 84.6  ? 
84  O1A ? ZB HEM .   ? D HEM 350  ? 1_555 MG ? AC MG  . ? D MG  353 ? 1_555 O   ? PC HOH .   ? D HOH 2083 ? 1_555 93.8  ? 
85  OE2 ? D  GLU 119 ? D GLU 122  ? 1_555 MG ? AC MG  . ? D MG  353 ? 1_555 O   ? PC HOH .   ? D HOH 2083 ? 1_555 91.6  ? 
86  O   ? PC HOH .   ? D HOH 2084 ? 1_555 MG ? AC MG  . ? D MG  353 ? 1_555 O   ? PC HOH .   ? D HOH 2083 ? 1_555 86.9  ? 
87  O1A ? ZB HEM .   ? D HEM 350  ? 1_555 MG ? AC MG  . ? D MG  353 ? 1_555 OG  ? D  SER 123 ? D SER 126  ? 1_555 82.8  ? 
88  OE2 ? D  GLU 119 ? D GLU 122  ? 1_555 MG ? AC MG  . ? D MG  353 ? 1_555 OG  ? D  SER 123 ? D SER 126  ? 1_555 172.4 ? 
89  O   ? PC HOH .   ? D HOH 2084 ? 1_555 MG ? AC MG  . ? D MG  353 ? 1_555 OG  ? D  SER 123 ? D SER 126  ? 1_555 88.6  ? 
90  O   ? PC HOH .   ? D HOH 2083 ? 1_555 MG ? AC MG  . ? D MG  353 ? 1_555 OG  ? D  SER 123 ? D SER 126  ? 1_555 91.2  ? 
91  O1A ? ZB HEM .   ? D HEM 350  ? 1_555 MG ? AC MG  . ? D MG  353 ? 1_555 O   ? D  GLY 120 ? D GLY 123  ? 1_555 87.7  ? 
92  OE2 ? D  GLU 119 ? D GLU 122  ? 1_555 MG ? AC MG  . ? D MG  353 ? 1_555 O   ? D  GLY 120 ? D GLY 123  ? 1_555 85.0  ? 
93  O   ? PC HOH .   ? D HOH 2084 ? 1_555 MG ? AC MG  . ? D MG  353 ? 1_555 O   ? D  GLY 120 ? D GLY 123  ? 1_555 92.1  ? 
94  O   ? PC HOH .   ? D HOH 2083 ? 1_555 MG ? AC MG  . ? D MG  353 ? 1_555 O   ? D  GLY 120 ? D GLY 123  ? 1_555 176.5 ? 
95  OG  ? D  SER 123 ? D SER 126  ? 1_555 MG ? AC MG  . ? D MG  353 ? 1_555 O   ? D  GLY 120 ? D GLY 123  ? 1_555 92.1  ? 
96  SG  ? D  CYS 33  ? D CYS 36   ? 1_555 FE ? ZB HEM . ? D HEM 350 ? 1_555 NA  ? ZB HEM .   ? D HEM 350  ? 1_555 98.2  ? 
97  SG  ? D  CYS 33  ? D CYS 36   ? 1_555 FE ? ZB HEM . ? D HEM 350 ? 1_555 NB  ? ZB HEM .   ? D HEM 350  ? 1_555 85.9  ? 
98  NA  ? ZB HEM .   ? D HEM 350  ? 1_555 FE ? ZB HEM . ? D HEM 350 ? 1_555 NB  ? ZB HEM .   ? D HEM 350  ? 1_555 95.9  ? 
99  SG  ? D  CYS 33  ? D CYS 36   ? 1_555 FE ? ZB HEM . ? D HEM 350 ? 1_555 NC  ? ZB HEM .   ? D HEM 350  ? 1_555 81.8  ? 
100 NA  ? ZB HEM .   ? D HEM 350  ? 1_555 FE ? ZB HEM . ? D HEM 350 ? 1_555 NC  ? ZB HEM .   ? D HEM 350  ? 1_555 178.9 ? 
101 NB  ? ZB HEM .   ? D HEM 350  ? 1_555 FE ? ZB HEM . ? D HEM 350 ? 1_555 NC  ? ZB HEM .   ? D HEM 350  ? 1_555 83.0  ? 
102 SG  ? D  CYS 33  ? D CYS 36   ? 1_555 FE ? ZB HEM . ? D HEM 350 ? 1_555 ND  ? ZB HEM .   ? D HEM 350  ? 1_555 94.9  ? 
103 NA  ? ZB HEM .   ? D HEM 350  ? 1_555 FE ? ZB HEM . ? D HEM 350 ? 1_555 ND  ? ZB HEM .   ? D HEM 350  ? 1_555 84.2  ? 
104 NB  ? ZB HEM .   ? D HEM 350  ? 1_555 FE ? ZB HEM . ? D HEM 350 ? 1_555 ND  ? ZB HEM .   ? D HEM 350  ? 1_555 179.2 ? 
105 NC  ? ZB HEM .   ? D HEM 350  ? 1_555 FE ? ZB HEM . ? D HEM 350 ? 1_555 ND  ? ZB HEM .   ? D HEM 350  ? 1_555 97.0  ? 
# 
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 2013-10-23 
2 'Structure model' 1 1 2013-12-11 
3 'Structure model' 1 2 2015-04-01 
# 
_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' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC refinement       5.5.0109 ? 1 
XDS    'data reduction' .        ? 2 
XDS    'data scaling'   .        ? 3 
PHASER phasing          .        ? 4 
# 
_pdbx_entry_details.entry_id             2YP1 
_pdbx_entry_details.compound_details     ? 
_pdbx_entry_details.source_details       ? 
_pdbx_entry_details.nonpolymer_details   ? 
_pdbx_entry_details.sequence_details     
;THE MATURE PROTEIN BEGINS AT E44 WITH RESPECT TO B9W4V6.
CRYSTALLIZED PROTEIN BEGINS AT L47, THAT IS L4 IN THE
COORDINATE FILE, DUE TO PROTEOLYTIC CLEAVAGE.
;
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 2121 ? ? O  A HOH 2122 ? ? 1.70 
2  1 O   C HOH 2021 ? ? O  C HOH 2288 ? ? 1.88 
3  1 O   B HOH 2071 ? ? O  B HOH 2072 ? ? 1.90 
4  1 NZ  A LYS 283  ? ? O  A HOH 2252 ? ? 2.00 
5  1 NE2 A GLN 299  ? ? O  A HOH 2273 ? ? 2.07 
6  1 O6  B NAG 372  ? ? O  B HOH 2351 ? ? 2.08 
7  1 O   D PRO 5    ? ? O  D HOH 2003 ? ? 2.11 
8  1 N   D ARG 100  ? ? O1 D SO4 1328 ? ? 2.13 
9  1 OE2 D GLU 167  ? ? O  D HOH 2103 ? ? 2.14 
10 1 O   C HOH 2116 ? ? O  C HOH 2267 ? ? 2.15 
11 1 OD2 A ASP 206  ? ? O  A HOH 2183 ? ? 2.16 
12 1 ND2 B ASN 263  ? ? O  B HOH 2277 ? ? 2.16 
13 1 NH2 B ARG 227  ? ? O  B HOH 2241 ? ? 2.17 
14 1 OE1 B GLN 249  ? ? O  B HOH 2261 ? ? 2.17 
15 1 O   B HOH 2038 ? ? O  B HOH 2039 ? ? 2.18 
16 1 O4  A MAN 394  ? ? O  A HOH 2317 ? ? 2.18 
# 
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 91  ? ? 73.71   35.46   
2  1 VAL A 112 ? ? 38.51   53.40   
3  1 THR A 120 ? ? -92.03  -68.18  
4  1 HIS A 138 ? ? -132.25 -32.31  
5  1 PHE A 185 ? ? -150.46 64.59   
6  1 ASP A 187 ? ? 54.31   -122.98 
7  1 ASP A 210 ? ? 37.17   50.75   
8  1 SER A 240 ? ? -135.58 -85.39  
9  1 ASN A 295 ? ? -146.89 55.35   
10 1 CYS A 319 ? ? 75.03   164.12  
11 1 PRO B 49  ? ? -38.34  132.36  
12 1 ASP B 91  ? ? 76.22   30.51   
13 1 THR B 120 ? ? -95.13  -71.38  
14 1 HIS B 138 ? ? -141.17 -22.50  
15 1 PHE B 185 ? ? -150.44 60.53   
16 1 ASP B 187 ? ? 45.19   -126.00 
17 1 ASP B 206 ? ? -39.08  131.15  
18 1 ASP B 210 ? ? 35.92   50.18   
19 1 SER B 240 ? ? -137.85 -89.70  
20 1 HIS B 251 ? ? -154.12 79.12   
21 1 ASP B 273 ? ? -140.66 -158.14 
22 1 CYS B 319 ? ? 71.04   167.55  
23 1 ASP C 19  ? ? -112.71 -161.33 
24 1 LEU C 67  ? ? -141.47 -2.03   
25 1 THR C 120 ? ? -98.41  -75.26  
26 1 PHE C 121 ? ? -96.40  -62.42  
27 1 PHE C 185 ? ? -152.40 61.95   
28 1 ASP C 187 ? ? 51.64   -124.00 
29 1 SER C 240 ? ? -145.70 -94.35  
30 1 HIS C 251 ? ? -150.46 81.64   
31 1 VAL C 259 ? ? -110.78 64.08   
32 1 ASP C 273 ? ? -163.25 -164.81 
33 1 CYS C 319 ? ? 71.40   175.83  
34 1 HIS D 22  ? ? -143.54 44.93   
35 1 ASN D 68  ? ? 70.65   30.70   
36 1 PRO D 107 ? ? -48.47  160.42  
37 1 VAL D 112 ? ? 39.39   51.27   
38 1 THR D 120 ? ? -93.62  -74.69  
39 1 PHE D 121 ? ? -103.79 -61.26  
40 1 ASP D 187 ? ? 58.52   -130.42 
41 1 ASP D 210 ? ? 36.47   50.92   
42 1 SER D 240 ? ? -132.21 -90.69  
43 1 VAL D 259 ? ? -109.35 45.29   
44 1 ILE D 287 ? ? -125.57 -58.77  
45 1 ASN D 295 ? ? -165.32 103.68  
46 1 THR D 297 ? ? -59.37  172.92  
47 1 CYS D 319 ? ? 74.68   172.77  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   D 
_pdbx_validate_peptide_omega.auth_seq_id_1    30 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   ASP 
_pdbx_validate_peptide_omega.auth_asym_id_2   D 
_pdbx_validate_peptide_omega.auth_seq_id_2    31 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -147.97 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 2327 ? 5.88 . 
2 1 O ? C HOH 2074 ? 6.24 . 
3 1 O ? D HOH 2081 ? 6.80 . 
4 1 O ? D HOH 2082 ? 5.83 . 
5 1 O ? D HOH 2197 ? 8.55 . 
6 1 O ? D HOH 2198 ? 8.39 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ARG 327 ? A ARG 324 
2 1 Y 1 A ASP 328 ? A ASP 325 
3 1 Y 1 B ASP 328 ? B ASP 325 
4 1 Y 1 D ARG 327 ? D ARG 324 
5 1 Y 1 D ASP 328 ? D ASP 325 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE' HEM 
3 'MAGNESIUM ION'                   MG  
4 N-ACETYL-D-GLUCOSAMINE            NAG 
5 BETA-D-MANNOSE                    BMA 
6 ALPHA-D-MANNOSE                   MAN 
7 'ACETATE ION'                     ACT 
8 'SULFATE ION'                     SO4 
9 water                             HOH 
# 
