data_4UM1
# 
_entry.id   4UM1 
# 
_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   4UM1         
PDBE  EBI-60625    
WWPDB D_1290060625 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          4UM3 
_pdbx_database_related.content_type   unspecified 
_pdbx_database_related.details        'ENGINEERED LS-ACHBP WITH ALPHA4-ALPHA4 INTERFACE IN COMPLEX WITH NS3920' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4UM1 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2014-05-14 
_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 
'Shahsavar, A.' 1 
'Kastrup, J.S.' 2 
'Balle, T.'     3 
'Gajhede, M.'   4 
# 
_citation.id                        primary 
_citation.title                     
;Achbp Engineered to Mimic the Alpha4-Alpha4 Binding Pocket in Alpha4Beta2 Nicotinic Acetylcholine Receptors Reveals Interface Specific Interactions Important for Binding and Activity
;
_citation.journal_abbrev            Mol.Pharmacol. 
_citation.journal_volume            88 
_citation.page_first                697 
_citation.page_last                 ? 
_citation.year                      2015 
_citation.journal_id_ASTM           MOPMA3 
_citation.country                   US 
_citation.journal_id_ISSN           0026-895X 
_citation.journal_id_CSD            0197 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   26180047 
_citation.pdbx_database_id_DOI      10.1124/MOL.115.098061 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Shahsavar, A.' 1 
primary 'Ahring, P.K.'  2 
primary 'Olsen, J.A.'   3 
primary 'Krintel, C.'   4 
primary 'Kastrup, J.S.' 5 
primary 'Balle, T.'     6 
primary 'Gajhede, M.'   7 
# 
_cell.entry_id           4UM1 
_cell.length_a           77.328 
_cell.length_b           123.104 
_cell.length_c           127.450 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              20 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         4UM1 
_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     man 'ACETYLCHOLINE-BINDING PROTEIN'          26053.143 5   ? YES ? 
'1-(5-ETHOXYPYRIDIN-3-YL)-1,4-DIAZEPANE (NS3573) BINDS AT THE INTERFACE OF EACH TWO MONOMERS' 
2 non-polymer syn '1-(5-ethoxypyridin-3-yl)-1,4-diazepane' 221.299   5   ? ?   ? ? 
3 non-polymer man N-ACETYL-D-GLUCOSAMINE                   221.208   1   ? ?   ? ? 
4 water       nat water                                    18.015    116 ? ?   ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'ACH-BINDING PROTEIN, ACHBP' 
# 
_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       
;MRRNIFCLACLWIVQACLSLDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFWQQTTWSDR
TLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQLAHVVSDGEVQYTPSIRQRFSCDVSGVDTESGATCRIKIG
SWTHHSREISVDPTTENSDDSEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEIL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MRRNIFCLACLWIVQACLSLDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFWQQTTWSDR
TLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQLAHVVSDGEVQYTPSIRQRFSCDVSGVDTESGATCRIKIG
SWTHHSREISVDPTTENSDDSEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEIL
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E 
_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   MET n 
1 2   ARG n 
1 3   ARG n 
1 4   ASN n 
1 5   ILE n 
1 6   PHE n 
1 7   CYS n 
1 8   LEU n 
1 9   ALA n 
1 10  CYS n 
1 11  LEU n 
1 12  TRP n 
1 13  ILE n 
1 14  VAL n 
1 15  GLN n 
1 16  ALA n 
1 17  CYS n 
1 18  LEU n 
1 19  SER n 
1 20  LEU n 
1 21  ASP n 
1 22  ARG n 
1 23  ALA n 
1 24  ASP n 
1 25  ILE n 
1 26  LEU n 
1 27  TYR n 
1 28  ASN n 
1 29  ILE n 
1 30  ARG n 
1 31  GLN n 
1 32  THR n 
1 33  SER n 
1 34  ARG n 
1 35  PRO n 
1 36  ASP n 
1 37  VAL n 
1 38  ILE n 
1 39  PRO n 
1 40  THR n 
1 41  GLN n 
1 42  ARG n 
1 43  ASP n 
1 44  ARG n 
1 45  PRO n 
1 46  VAL n 
1 47  ALA n 
1 48  VAL n 
1 49  SER n 
1 50  VAL n 
1 51  SER n 
1 52  LEU n 
1 53  LYS n 
1 54  PHE n 
1 55  ILE n 
1 56  ASN n 
1 57  ILE n 
1 58  LEU n 
1 59  GLU n 
1 60  VAL n 
1 61  ASN n 
1 62  GLU n 
1 63  ILE n 
1 64  THR n 
1 65  ASN n 
1 66  GLU n 
1 67  VAL n 
1 68  ASP n 
1 69  VAL n 
1 70  VAL n 
1 71  PHE n 
1 72  TRP n 
1 73  GLN n 
1 74  GLN n 
1 75  THR n 
1 76  THR n 
1 77  TRP n 
1 78  SER n 
1 79  ASP n 
1 80  ARG n 
1 81  THR n 
1 82  LEU n 
1 83  ALA n 
1 84  TRP n 
1 85  ASN n 
1 86  SER n 
1 87  SER n 
1 88  HIS n 
1 89  SER n 
1 90  PRO n 
1 91  ASP n 
1 92  GLN n 
1 93  VAL n 
1 94  SER n 
1 95  VAL n 
1 96  PRO n 
1 97  ILE n 
1 98  SER n 
1 99  SER n 
1 100 LEU n 
1 101 TRP n 
1 102 VAL n 
1 103 PRO n 
1 104 ASP n 
1 105 LEU n 
1 106 ALA n 
1 107 ALA n 
1 108 TYR n 
1 109 ASN n 
1 110 ALA n 
1 111 ILE n 
1 112 SER n 
1 113 LYS n 
1 114 PRO n 
1 115 GLU n 
1 116 VAL n 
1 117 LEU n 
1 118 THR n 
1 119 PRO n 
1 120 GLN n 
1 121 LEU n 
1 122 ALA n 
1 123 HIS n 
1 124 VAL n 
1 125 VAL n 
1 126 SER n 
1 127 ASP n 
1 128 GLY n 
1 129 GLU n 
1 130 VAL n 
1 131 GLN n 
1 132 TYR n 
1 133 THR n 
1 134 PRO n 
1 135 SER n 
1 136 ILE n 
1 137 ARG n 
1 138 GLN n 
1 139 ARG n 
1 140 PHE n 
1 141 SER n 
1 142 CYS n 
1 143 ASP n 
1 144 VAL n 
1 145 SER n 
1 146 GLY n 
1 147 VAL n 
1 148 ASP n 
1 149 THR n 
1 150 GLU n 
1 151 SER n 
1 152 GLY n 
1 153 ALA n 
1 154 THR n 
1 155 CYS n 
1 156 ARG n 
1 157 ILE n 
1 158 LYS n 
1 159 ILE n 
1 160 GLY n 
1 161 SER n 
1 162 TRP n 
1 163 THR n 
1 164 HIS n 
1 165 HIS n 
1 166 SER n 
1 167 ARG n 
1 168 GLU n 
1 169 ILE n 
1 170 SER n 
1 171 VAL n 
1 172 ASP n 
1 173 PRO n 
1 174 THR n 
1 175 THR n 
1 176 GLU n 
1 177 ASN n 
1 178 SER n 
1 179 ASP n 
1 180 ASP n 
1 181 SER n 
1 182 GLU n 
1 183 TYR n 
1 184 PHE n 
1 185 SER n 
1 186 GLN n 
1 187 TYR n 
1 188 SER n 
1 189 ARG n 
1 190 PHE n 
1 191 GLU n 
1 192 ILE n 
1 193 LEU n 
1 194 ASP n 
1 195 VAL n 
1 196 THR n 
1 197 GLN n 
1 198 LYS n 
1 199 LYS n 
1 200 ASN n 
1 201 SER n 
1 202 VAL n 
1 203 THR n 
1 204 TYR n 
1 205 SER n 
1 206 CYS n 
1 207 CYS n 
1 208 PRO n 
1 209 GLU n 
1 210 ALA n 
1 211 TYR n 
1 212 GLU n 
1 213 ASP n 
1 214 VAL n 
1 215 GLU n 
1 216 VAL n 
1 217 SER n 
1 218 LEU n 
1 219 ASN n 
1 220 PHE n 
1 221 ARG n 
1 222 LYS n 
1 223 LYS n 
1 224 GLY n 
1 225 ARG n 
1 226 SER n 
1 227 GLU n 
1 228 ILE n 
1 229 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               'GREAT POND SNAIL' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'LYMNAEA STAGNALIS' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     6523 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               'FALL ARMYWORM' 
_entity_src_gen.pdbx_host_org_scientific_name      'SPODOPTERA FRUGIPERDA' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               SF9 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          BACULOVIRUS 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       PFASTBAC 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ACHP_LYMST 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_db_accession          P58154 
_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 4UM1 A 1 ? 229 ? P58154 1 ? 229 ? -18 210 
2 1 4UM1 B 1 ? 229 ? P58154 1 ? 229 ? -18 210 
3 1 4UM1 C 1 ? 229 ? P58154 1 ? 229 ? -18 210 
4 1 4UM1 D 1 ? 229 ? P58154 1 ? 229 ? -18 210 
5 1 4UM1 E 1 ? 229 ? P58154 1 ? 229 ? -18 210 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 4UM1 HIS A 123 ? UNP P58154 ARG 123 'engineered mutation' 104 1  
1 4UM1 GLN A 131 ? UNP P58154 LEU 131 'engineered mutation' 112 2  
1 4UM1 THR A 133 ? UNP P58154 MET 133 'engineered mutation' 114 3  
2 4UM1 HIS B 123 ? UNP P58154 ARG 123 'engineered mutation' 104 4  
2 4UM1 GLN B 131 ? UNP P58154 LEU 131 'engineered mutation' 112 5  
2 4UM1 THR B 133 ? UNP P58154 MET 133 'engineered mutation' 114 6  
3 4UM1 HIS C 123 ? UNP P58154 ARG 123 'engineered mutation' 104 7  
3 4UM1 GLN C 131 ? UNP P58154 LEU 131 'engineered mutation' 112 8  
3 4UM1 THR C 133 ? UNP P58154 MET 133 'engineered mutation' 114 9  
4 4UM1 HIS D 123 ? UNP P58154 ARG 123 'engineered mutation' 104 10 
4 4UM1 GLN D 131 ? UNP P58154 LEU 131 'engineered mutation' 112 11 
4 4UM1 THR D 133 ? UNP P58154 MET 133 'engineered mutation' 114 12 
5 4UM1 HIS E 123 ? UNP P58154 ARG 123 'engineered mutation' 104 13 
5 4UM1 GLN E 131 ? UNP P58154 LEU 131 'engineered mutation' 112 14 
5 4UM1 THR E 133 ? UNP P58154 MET 133 'engineered mutation' 114 15 
# 
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 
09P non-polymer         . '1-(5-ethoxypyridin-3-yl)-1,4-diazepane' ? 'C12 H19 N3 O'   221.299 
ALA 'L-peptide linking' y ALANINE                                  ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                 ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                               ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                          ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                 ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                                ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                  ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                    ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                               ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                  ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                   ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                               ? 'C5 H11 N O2 S'  149.211 
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 
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          4UM1 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.43 
_exptl_crystal.density_percent_sol   49.34 
_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              8 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '0.1 M TRIS BASE (PH 8.0), 1-3% V/V POLYETHYLENE GLYCOL (PEG) 400 AND 1.8-2.3 M (NH4)2SO4' 
# 
_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                   'MARMOSAIC 225 mm CCD' 
_diffrn_detector.pdbx_collection_date   ? 
_diffrn_detector.details                MIRRORS 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'SI(111)' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ESRF BEAMLINE ID23-2' 
_diffrn_source.pdbx_synchrotron_site       ESRF 
_diffrn_source.pdbx_synchrotron_beamline   ID23-2 
_diffrn_source.pdbx_wavelength             1 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4UM1 
_reflns.observed_criterion_sigma_I   0.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             49.18 
_reflns.d_resolution_high            2.83 
_reflns.number_obs                   29761 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.21 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        10.50 
_reflns.B_iso_Wilson_estimate        51.25 
_reflns.pdbx_redundancy              7.8 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             2.83 
_reflns_shell.d_res_low              2.98 
_reflns_shell.percent_possible_all   100.0 
_reflns_shell.Rmerge_I_obs           1.37 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.00 
_reflns_shell.pdbx_redundancy        7.9 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4UM1 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     29726 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.16 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             49.178 
_refine.ls_d_res_high                            2.830 
_refine.ls_percent_reflns_obs                    99.99 
_refine.ls_R_factor_obs                          0.1948 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1928 
_refine.ls_R_factor_R_free                       0.2307 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  2839 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               35 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 3U8K' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.39 
_refine.pdbx_overall_phase_error                 23.85 
_refine.overall_SU_B                             ? 
_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        8020 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         94 
_refine_hist.number_atoms_solvent             116 
_refine_hist.number_atoms_total               8230 
_refine_hist.d_res_high                       2.830 
_refine_hist.d_res_low                        49.178 
# 
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 
f_bond_d           0.010  ? ? 8320  'X-RAY DIFFRACTION' ? 
f_angle_d          1.096  ? ? 11335 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 13.283 ? ? 3000  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.072  ? ? 1289  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.004  ? ? 1455  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' . 2.8300 2.8788  2689 0.3293 100.00 0.4454 . . 109 . . 
'X-RAY DIFFRACTION' . 2.8788 2.9312  2668 0.3175 100.00 0.3350 . . 124 . . 
'X-RAY DIFFRACTION' . 2.9312 2.9875  2666 0.2943 100.00 0.3683 . . 163 . . 
'X-RAY DIFFRACTION' . 2.9875 3.0485  2636 0.2865 100.00 0.3052 . . 151 . . 
'X-RAY DIFFRACTION' . 3.0485 3.1148  2661 0.2730 100.00 0.3255 . . 151 . . 
'X-RAY DIFFRACTION' . 3.1148 3.1872  2654 0.2603 100.00 0.3077 . . 129 . . 
'X-RAY DIFFRACTION' . 3.1872 3.2669  2655 0.2291 100.00 0.3294 . . 155 . . 
'X-RAY DIFFRACTION' . 3.2669 3.3552  2704 0.2099 100.00 0.2537 . . 119 . . 
'X-RAY DIFFRACTION' . 3.3552 3.4539  2650 0.2011 100.00 0.2223 . . 156 . . 
'X-RAY DIFFRACTION' . 3.4539 3.5654  2630 0.1982 100.00 0.2465 . . 142 . . 
'X-RAY DIFFRACTION' . 3.5654 3.6928  2671 0.1856 100.00 0.2534 . . 146 . . 
'X-RAY DIFFRACTION' . 3.6928 3.8406  2712 0.1784 100.00 0.1787 . . 101 . . 
'X-RAY DIFFRACTION' . 3.8406 4.0153  2634 0.1694 100.00 0.2298 . . 150 . . 
'X-RAY DIFFRACTION' . 4.0153 4.2269  2668 0.1503 100.00 0.2091 . . 143 . . 
'X-RAY DIFFRACTION' . 4.2269 4.4916  2666 0.1384 100.00 0.1725 . . 135 . . 
'X-RAY DIFFRACTION' . 4.4916 4.8381  2649 0.1403 100.00 0.1603 . . 168 . . 
'X-RAY DIFFRACTION' . 4.8381 5.3244  2645 0.1554 100.00 0.2052 . . 158 . . 
'X-RAY DIFFRACTION' . 5.3244 6.0937  2637 0.1737 100.00 0.2029 . . 157 . . 
'X-RAY DIFFRACTION' . 6.0937 7.6727  2668 0.1997 100.00 0.2322 . . 143 . . 
'X-RAY DIFFRACTION' . 7.6727 49.1852 2654 0.1927 100.00 0.1819 . . 139 . . 
# 
_struct.entry_id                  4UM1 
_struct.title                     'Engineered Ls-AChBP with alpha4-alpha4 binding pocket in complex with NS3573' 
_struct.pdbx_descriptor           'ACETYLCHOLINE-BINDING PROTEIN' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4UM1 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
_struct_keywords.text            
'SIGNALING PROTEIN, ION CHANNEL, RECEPTOR STOICHIOMETRY, CYS-LOOP RECEPTOR, ACETYLCHOLINE BINDING PROTEIN' 
# 
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 1 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 3 ? 
K N N 2 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
O N N 4 ? 
P N N 4 ? 
# 
_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  ASP A 21  ? SER A 33  ? ASP A 2   SER A 14  1 ? 13 
HELX_P HELX_P2  2  ARG A 80  ? ALA A 83  ? ARG A 61  ALA A 64  5 ? 4  
HELX_P HELX_P3  3  SER A 98  ? LEU A 100 ? SER A 79  LEU A 81  5 ? 3  
HELX_P HELX_P4  4  ASP B 21  ? SER B 33  ? ASP B 2   SER B 14  1 ? 13 
HELX_P HELX_P5  5  ARG B 80  ? ALA B 83  ? ARG B 61  ALA B 64  5 ? 4  
HELX_P HELX_P6  6  SER B 98  ? LEU B 100 ? SER B 79  LEU B 81  5 ? 3  
HELX_P HELX_P7  7  ASP C 21  ? SER C 33  ? ASP C 2   SER C 14  1 ? 13 
HELX_P HELX_P8  8  ARG C 80  ? ALA C 83  ? ARG C 61  ALA C 64  5 ? 4  
HELX_P HELX_P9  9  SER C 98  ? LEU C 100 ? SER C 79  LEU C 81  5 ? 3  
HELX_P HELX_P10 10 ASP D 21  ? SER D 33  ? ASP D 2   SER D 14  1 ? 13 
HELX_P HELX_P11 11 ARG D 80  ? ALA D 83  ? ARG D 61  ALA D 64  5 ? 4  
HELX_P HELX_P12 12 SER D 98  ? LEU D 100 ? SER D 79  LEU D 81  5 ? 3  
HELX_P HELX_P13 13 ASP D 180 ? PHE D 184 ? ASP D 161 PHE D 165 5 ? 5  
HELX_P HELX_P14 14 ASP E 21  ? SER E 33  ? ASP E 2   SER E 14  1 ? 13 
HELX_P HELX_P15 15 ARG E 80  ? ALA E 83  ? ARG E 61  ALA E 64  5 ? 4  
HELX_P HELX_P16 16 SER E 98  ? LEU E 100 ? SER E 79  LEU E 81  5 ? 3  
# 
_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 142 SG  ? ? ? 1_555 A CYS 155 SG ? ? A CYS 123 A CYS 136  1_555 ? ? ? ? ? ? ? 2.049 ? 
disulf2  disulf ? ? A CYS 206 SG  ? ? ? 1_555 A CYS 207 SG ? ? A CYS 187 A CYS 188  1_555 ? ? ? ? ? ? ? 2.054 ? 
disulf3  disulf ? ? B CYS 142 SG  ? ? ? 1_555 B CYS 155 SG ? ? B CYS 123 B CYS 136  1_555 ? ? ? ? ? ? ? 2.044 ? 
disulf4  disulf ? ? B CYS 206 SG  ? ? ? 1_555 B CYS 207 SG ? ? B CYS 187 B CYS 188  1_555 ? ? ? ? ? ? ? 2.056 ? 
disulf5  disulf ? ? C CYS 142 SG  ? ? ? 1_555 C CYS 155 SG ? ? C CYS 123 C CYS 136  1_555 ? ? ? ? ? ? ? 2.049 ? 
disulf6  disulf ? ? C CYS 206 SG  ? ? ? 1_555 C CYS 207 SG ? ? C CYS 187 C CYS 188  1_555 ? ? ? ? ? ? ? 2.055 ? 
disulf7  disulf ? ? D CYS 142 SG  ? ? ? 1_555 D CYS 155 SG ? ? D CYS 123 D CYS 136  1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf8  disulf ? ? D CYS 206 SG  ? ? ? 1_555 D CYS 207 SG ? ? D CYS 187 D CYS 188  1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf9  disulf ? ? E CYS 142 SG  ? ? ? 1_555 E CYS 155 SG ? ? E CYS 123 E CYS 136  1_555 ? ? ? ? ? ? ? 2.044 ? 
disulf10 disulf ? ? E CYS 206 SG  A ? ? 1_555 E CYS 207 SG ? ? E CYS 187 E CYS 188  1_555 ? ? ? ? ? ? ? 2.042 ? 
covale1  covale ? ? D ASN 85  ND2 ? ? ? 1_555 J NAG .   C1 ? ? D ASN 66  D NAG 1206 1_555 ? ? ? ? ? ? ? 2.017 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 6 ? 
AB ? 6 ? 
AC ? 4 ? 
BA ? 6 ? 
BB ? 6 ? 
BC ? 4 ? 
CA ? 6 ? 
CB ? 6 ? 
CC ? 4 ? 
DA ? 6 ? 
DB ? 6 ? 
DC ? 4 ? 
EA ? 6 ? 
EB ? 6 ? 
EC ? 4 ? 
# 
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 
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
AA 4 5 ? parallel      
AA 5 6 ? anti-parallel 
AB 1 2 ? anti-parallel 
AB 2 3 ? anti-parallel 
AB 3 4 ? anti-parallel 
AB 4 5 ? anti-parallel 
AB 5 6 ? parallel      
AC 1 2 ? anti-parallel 
AC 2 3 ? anti-parallel 
AC 3 4 ? anti-parallel 
BA 1 2 ? anti-parallel 
BA 2 3 ? anti-parallel 
BA 3 4 ? anti-parallel 
BA 4 5 ? parallel      
BA 5 6 ? anti-parallel 
BB 1 2 ? anti-parallel 
BB 2 3 ? anti-parallel 
BB 3 4 ? anti-parallel 
BB 4 5 ? anti-parallel 
BB 5 6 ? parallel      
BC 1 2 ? anti-parallel 
BC 2 3 ? anti-parallel 
BC 3 4 ? anti-parallel 
CA 1 2 ? anti-parallel 
CA 2 3 ? anti-parallel 
CA 3 4 ? anti-parallel 
CA 4 5 ? parallel      
CA 5 6 ? anti-parallel 
CB 1 2 ? anti-parallel 
CB 2 3 ? anti-parallel 
CB 3 4 ? anti-parallel 
CB 4 5 ? anti-parallel 
CB 5 6 ? parallel      
CC 1 2 ? anti-parallel 
CC 2 3 ? anti-parallel 
CC 3 4 ? anti-parallel 
DA 1 2 ? anti-parallel 
DA 2 3 ? anti-parallel 
DA 3 4 ? anti-parallel 
DA 4 5 ? parallel      
DA 5 6 ? anti-parallel 
DB 1 2 ? anti-parallel 
DB 2 3 ? anti-parallel 
DB 3 4 ? anti-parallel 
DB 4 5 ? anti-parallel 
DB 5 6 ? parallel      
DC 1 2 ? anti-parallel 
DC 2 3 ? anti-parallel 
DC 3 4 ? anti-parallel 
EA 1 2 ? anti-parallel 
EA 2 3 ? anti-parallel 
EA 3 4 ? anti-parallel 
EA 4 5 ? parallel      
EA 5 6 ? anti-parallel 
EB 1 2 ? anti-parallel 
EB 2 3 ? anti-parallel 
EB 3 4 ? anti-parallel 
EB 4 5 ? anti-parallel 
EB 5 6 ? parallel      
EC 1 2 ? anti-parallel 
EC 2 3 ? anti-parallel 
EC 3 4 ? 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 GLN A 92  ? PRO A 96  ? GLN A 73  PRO A 77  
AA 2 LEU A 121 ? VAL A 125 ? LEU A 102 VAL A 106 
AA 3 GLU A 129 ? TYR A 132 ? GLU A 110 TYR A 113 
AA 4 GLU A 66  ? SER A 78  ? GLU A 47  SER A 59  
AA 5 SER A 135 ? SER A 141 ? SER A 116 SER A 122 
AA 6 GLU A 115 ? VAL A 116 ? GLU A 96  VAL A 97  
AB 1 GLN A 92  ? PRO A 96  ? GLN A 73  PRO A 77  
AB 2 LEU A 121 ? VAL A 125 ? LEU A 102 VAL A 106 
AB 3 GLU A 129 ? TYR A 132 ? GLU A 110 TYR A 113 
AB 4 GLU A 66  ? SER A 78  ? GLU A 47  SER A 59  
AB 5 VAL A 46  ? ILE A 57  ? VAL A 27  ILE A 38  
AB 6 ILE A 169 ? PRO A 173 ? ILE A 150 PRO A 154 
AC 1 LEU A 105 ? ALA A 107 ? LEU A 86  ALA A 88  
AC 2 ALA A 153 ? SER A 161 ? ALA A 134 SER A 142 
AC 3 ALA A 210 ? LYS A 222 ? ALA A 191 LYS A 203 
AC 4 PHE A 190 ? THR A 203 ? PHE A 171 THR A 184 
BA 1 GLN B 92  ? PRO B 96  ? GLN B 73  PRO B 77  
BA 2 LEU B 121 ? VAL B 125 ? LEU B 102 VAL B 106 
BA 3 GLU B 129 ? TYR B 132 ? GLU B 110 TYR B 113 
BA 4 GLU B 66  ? SER B 78  ? GLU B 47  SER B 59  
BA 5 SER B 135 ? SER B 141 ? SER B 116 SER B 122 
BA 6 GLU B 115 ? VAL B 116 ? GLU B 96  VAL B 97  
BB 1 GLN B 92  ? PRO B 96  ? GLN B 73  PRO B 77  
BB 2 LEU B 121 ? VAL B 125 ? LEU B 102 VAL B 106 
BB 3 GLU B 129 ? TYR B 132 ? GLU B 110 TYR B 113 
BB 4 GLU B 66  ? SER B 78  ? GLU B 47  SER B 59  
BB 5 VAL B 46  ? ILE B 57  ? VAL B 27  ILE B 38  
BB 6 ILE B 169 ? PRO B 173 ? ILE B 150 PRO B 154 
BC 1 LEU B 105 ? ALA B 107 ? LEU B 86  ALA B 88  
BC 2 ALA B 153 ? SER B 161 ? ALA B 134 SER B 142 
BC 3 ALA B 210 ? LYS B 222 ? ALA B 191 LYS B 203 
BC 4 PHE B 190 ? THR B 203 ? PHE B 171 THR B 184 
CA 1 GLN C 92  ? PRO C 96  ? GLN C 73  PRO C 77  
CA 2 LEU C 121 ? VAL C 125 ? LEU C 102 VAL C 106 
CA 3 GLU C 129 ? TYR C 132 ? GLU C 110 TYR C 113 
CA 4 GLU C 66  ? SER C 78  ? GLU C 47  SER C 59  
CA 5 SER C 135 ? SER C 141 ? SER C 116 SER C 122 
CA 6 GLU C 115 ? VAL C 116 ? GLU C 96  VAL C 97  
CB 1 GLN C 92  ? PRO C 96  ? GLN C 73  PRO C 77  
CB 2 LEU C 121 ? VAL C 125 ? LEU C 102 VAL C 106 
CB 3 GLU C 129 ? TYR C 132 ? GLU C 110 TYR C 113 
CB 4 GLU C 66  ? SER C 78  ? GLU C 47  SER C 59  
CB 5 VAL C 46  ? ILE C 57  ? VAL C 27  ILE C 38  
CB 6 ILE C 169 ? PRO C 173 ? ILE C 150 PRO C 154 
CC 1 LEU C 105 ? ALA C 107 ? LEU C 86  ALA C 88  
CC 2 ALA C 153 ? SER C 161 ? ALA C 134 SER C 142 
CC 3 ALA C 210 ? LYS C 222 ? ALA C 191 LYS C 203 
CC 4 PHE C 190 ? THR C 203 ? PHE C 171 THR C 184 
DA 1 GLN D 92  ? PRO D 96  ? GLN D 73  PRO D 77  
DA 2 LEU D 121 ? VAL D 125 ? LEU D 102 VAL D 106 
DA 3 GLU D 129 ? TYR D 132 ? GLU D 110 TYR D 113 
DA 4 GLU D 66  ? SER D 78  ? GLU D 47  SER D 59  
DA 5 SER D 135 ? SER D 141 ? SER D 116 SER D 122 
DA 6 GLU D 115 ? VAL D 116 ? GLU D 96  VAL D 97  
DB 1 GLN D 92  ? PRO D 96  ? GLN D 73  PRO D 77  
DB 2 LEU D 121 ? VAL D 125 ? LEU D 102 VAL D 106 
DB 3 GLU D 129 ? TYR D 132 ? GLU D 110 TYR D 113 
DB 4 GLU D 66  ? SER D 78  ? GLU D 47  SER D 59  
DB 5 VAL D 46  ? ILE D 57  ? VAL D 27  ILE D 38  
DB 6 ILE D 169 ? PRO D 173 ? ILE D 150 PRO D 154 
DC 1 LEU D 105 ? ALA D 107 ? LEU D 86  ALA D 88  
DC 2 ALA D 153 ? SER D 161 ? ALA D 134 SER D 142 
DC 3 ALA D 210 ? LYS D 222 ? ALA D 191 LYS D 203 
DC 4 PHE D 190 ? THR D 203 ? PHE D 171 THR D 184 
EA 1 GLN E 92  ? PRO E 96  ? GLN E 73  PRO E 77  
EA 2 LEU E 121 ? VAL E 125 ? LEU E 102 VAL E 106 
EA 3 GLU E 129 ? TYR E 132 ? GLU E 110 TYR E 113 
EA 4 GLU E 66  ? SER E 78  ? GLU E 47  SER E 59  
EA 5 SER E 135 ? SER E 141 ? SER E 116 SER E 122 
EA 6 GLU E 115 ? VAL E 116 ? GLU E 96  VAL E 97  
EB 1 GLN E 92  ? PRO E 96  ? GLN E 73  PRO E 77  
EB 2 LEU E 121 ? VAL E 125 ? LEU E 102 VAL E 106 
EB 3 GLU E 129 ? TYR E 132 ? GLU E 110 TYR E 113 
EB 4 GLU E 66  ? SER E 78  ? GLU E 47  SER E 59  
EB 5 VAL E 46  ? ILE E 57  ? VAL E 27  ILE E 38  
EB 6 ILE E 169 ? PRO E 173 ? ILE E 150 PRO E 154 
EC 1 LEU E 105 ? ALA E 107 ? LEU E 86  ALA E 88  
EC 2 ALA E 153 ? SER E 161 ? ALA E 134 SER E 142 
EC 3 ALA E 210 ? LYS E 222 ? ALA E 191 LYS E 203 
EC 4 PHE E 190 ? THR E 203 ? PHE E 171 THR E 184 
# 
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 VAL A 95  ? N VAL A 76  O ALA A 122 ? O ALA A 103 
AA 2 3 N VAL A 125 ? N VAL A 106 O GLU A 129 ? O GLU A 110 
AA 3 4 N TYR A 132 ? N TYR A 113 O THR A 75  ? O THR A 56  
AA 4 5 N PHE A 71  ? N PHE A 52  O ILE A 136 ? O ILE A 117 
AA 5 6 N ARG A 137 ? N ARG A 118 O GLU A 115 ? O GLU A 96  
AB 1 2 N VAL A 95  ? N VAL A 76  O ALA A 122 ? O ALA A 103 
AB 2 3 N VAL A 125 ? N VAL A 106 O GLU A 129 ? O GLU A 110 
AB 3 4 N TYR A 132 ? N TYR A 113 O THR A 75  ? O THR A 56  
AB 4 5 N THR A 76  ? N THR A 57  O SER A 49  ? O SER A 30  
AB 5 6 N VAL A 48  ? N VAL A 29  O SER A 170 ? O SER A 151 
AC 1 2 N ALA A 106 ? N ALA A 87  O GLY A 160 ? O GLY A 141 
AC 2 3 N SER A 161 ? N SER A 142 O GLU A 212 ? O GLU A 193 
AC 3 4 N ARG A 221 ? N ARG A 202 O GLU A 191 ? O GLU A 172 
BA 1 2 N VAL B 95  ? N VAL B 76  O ALA B 122 ? O ALA B 103 
BA 2 3 N VAL B 125 ? N VAL B 106 O GLU B 129 ? O GLU B 110 
BA 3 4 N TYR B 132 ? N TYR B 113 O THR B 75  ? O THR B 56  
BA 4 5 N PHE B 71  ? N PHE B 52  O ILE B 136 ? O ILE B 117 
BA 5 6 N ARG B 137 ? N ARG B 118 O GLU B 115 ? O GLU B 96  
BB 1 2 N VAL B 95  ? N VAL B 76  O ALA B 122 ? O ALA B 103 
BB 2 3 N VAL B 125 ? N VAL B 106 O GLU B 129 ? O GLU B 110 
BB 3 4 N TYR B 132 ? N TYR B 113 O THR B 75  ? O THR B 56  
BB 4 5 N THR B 76  ? N THR B 57  O SER B 49  ? O SER B 30  
BB 5 6 N VAL B 48  ? N VAL B 29  O SER B 170 ? O SER B 151 
BC 1 2 N ALA B 106 ? N ALA B 87  O GLY B 160 ? O GLY B 141 
BC 2 3 N SER B 161 ? N SER B 142 O GLU B 212 ? O GLU B 193 
BC 3 4 N ARG B 221 ? N ARG B 202 O GLU B 191 ? O GLU B 172 
CA 1 2 N VAL C 95  ? N VAL C 76  O ALA C 122 ? O ALA C 103 
CA 2 3 N VAL C 125 ? N VAL C 106 O GLU C 129 ? O GLU C 110 
CA 3 4 N TYR C 132 ? N TYR C 113 O THR C 75  ? O THR C 56  
CA 4 5 N PHE C 71  ? N PHE C 52  O ILE C 136 ? O ILE C 117 
CA 5 6 N ARG C 137 ? N ARG C 118 O GLU C 115 ? O GLU C 96  
CB 1 2 N VAL C 95  ? N VAL C 76  O ALA C 122 ? O ALA C 103 
CB 2 3 N VAL C 125 ? N VAL C 106 O GLU C 129 ? O GLU C 110 
CB 3 4 N TYR C 132 ? N TYR C 113 O THR C 75  ? O THR C 56  
CB 4 5 N THR C 76  ? N THR C 57  O SER C 49  ? O SER C 30  
CB 5 6 N VAL C 48  ? N VAL C 29  O SER C 170 ? O SER C 151 
CC 1 2 N ALA C 106 ? N ALA C 87  O GLY C 160 ? O GLY C 141 
CC 2 3 N SER C 161 ? N SER C 142 O GLU C 212 ? O GLU C 193 
CC 3 4 N ARG C 221 ? N ARG C 202 O GLU C 191 ? O GLU C 172 
DA 1 2 N VAL D 95  ? N VAL D 76  O ALA D 122 ? O ALA D 103 
DA 2 3 N VAL D 125 ? N VAL D 106 O GLU D 129 ? O GLU D 110 
DA 3 4 N TYR D 132 ? N TYR D 113 O THR D 75  ? O THR D 56  
DA 4 5 N PHE D 71  ? N PHE D 52  O ILE D 136 ? O ILE D 117 
DA 5 6 N ARG D 137 ? N ARG D 118 O GLU D 115 ? O GLU D 96  
DB 1 2 N VAL D 95  ? N VAL D 76  O ALA D 122 ? O ALA D 103 
DB 2 3 N VAL D 125 ? N VAL D 106 O GLU D 129 ? O GLU D 110 
DB 3 4 N TYR D 132 ? N TYR D 113 O THR D 75  ? O THR D 56  
DB 4 5 N THR D 76  ? N THR D 57  O SER D 49  ? O SER D 30  
DB 5 6 N VAL D 48  ? N VAL D 29  O SER D 170 ? O SER D 151 
DC 1 2 N ALA D 106 ? N ALA D 87  O GLY D 160 ? O GLY D 141 
DC 2 3 N SER D 161 ? N SER D 142 O GLU D 212 ? O GLU D 193 
DC 3 4 N ARG D 221 ? N ARG D 202 O GLU D 191 ? O GLU D 172 
EA 1 2 N VAL E 95  ? N VAL E 76  O ALA E 122 ? O ALA E 103 
EA 2 3 N VAL E 125 ? N VAL E 106 O GLU E 129 ? O GLU E 110 
EA 3 4 N TYR E 132 ? N TYR E 113 O THR E 75  ? O THR E 56  
EA 4 5 N PHE E 71  ? N PHE E 52  O ILE E 136 ? O ILE E 117 
EA 5 6 N ARG E 137 ? N ARG E 118 O GLU E 115 ? O GLU E 96  
EB 1 2 N VAL E 95  ? N VAL E 76  O ALA E 122 ? O ALA E 103 
EB 2 3 N VAL E 125 ? N VAL E 106 O GLU E 129 ? O GLU E 110 
EB 3 4 N TYR E 132 ? N TYR E 113 O THR E 75  ? O THR E 56  
EB 4 5 N THR E 76  ? N THR E 57  O SER E 49  ? O SER E 30  
EB 5 6 N VAL E 48  ? N VAL E 29  O SER E 170 ? O SER E 151 
EC 1 2 N ALA E 106 ? N ALA E 87  O GLY E 160 ? O GLY E 141 
EC 2 3 N SER E 161 ? N SER E 142 O GLU E 212 ? O GLU E 193 
EC 3 4 N ARG E 221 ? N ARG E 202 O GLU E 191 ? O GLU E 172 
# 
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 ? ? ? ? 7 'BINDING SITE FOR RESIDUE 09P A 211'                           
AC2 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE 09P B 211'                           
AC3 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE 09P C 211'                           
AC4 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE 09P D 211'                           
AC5 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE 09P E 211'                           
AC6 Software ? ? ? ? 3 'Binding site for Mono-Saccharide NAG D1206 bound to ASN D 66' 
# 
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 7 TYR A 108 ? TYR A 89   . ? 1_555 ? 
2  AC1 7 TRP A 162 ? TRP A 143  . ? 1_555 ? 
3  AC1 7 CYS A 207 ? CYS A 188  . ? 1_555 ? 
4  AC1 7 TYR A 211 ? TYR A 192  . ? 1_555 ? 
5  AC1 7 HIS B 123 ? HIS B 104  . ? 1_555 ? 
6  AC1 7 GLN B 131 ? GLN B 112  . ? 1_555 ? 
7  AC1 7 THR B 133 ? THR B 114  . ? 1_555 ? 
8  AC2 8 TYR B 108 ? TYR B 89   . ? 1_555 ? 
9  AC2 8 TRP B 162 ? TRP B 143  . ? 1_555 ? 
10 AC2 8 TYR B 204 ? TYR B 185  . ? 1_555 ? 
11 AC2 8 CYS B 207 ? CYS B 188  . ? 1_555 ? 
12 AC2 8 TRP C 72  ? TRP C 53   . ? 1_555 ? 
13 AC2 8 HIS C 123 ? HIS C 104  . ? 1_555 ? 
14 AC2 8 GLN C 131 ? GLN C 112  . ? 1_555 ? 
15 AC2 8 THR C 133 ? THR C 114  . ? 1_555 ? 
16 AC3 8 TYR C 108 ? TYR C 89   . ? 1_555 ? 
17 AC3 8 TRP C 162 ? TRP C 143  . ? 1_555 ? 
18 AC3 8 TYR C 204 ? TYR C 185  . ? 1_555 ? 
19 AC3 8 CYS C 207 ? CYS C 188  . ? 1_555 ? 
20 AC3 8 TYR C 211 ? TYR C 192  . ? 1_555 ? 
21 AC3 8 HOH N .   ? HOH C 2017 . ? 1_555 ? 
22 AC3 8 HIS D 123 ? HIS D 104  . ? 1_555 ? 
23 AC3 8 THR D 133 ? THR D 114  . ? 1_555 ? 
24 AC4 8 TYR D 108 ? TYR D 89   . ? 1_555 ? 
25 AC4 8 TRP D 162 ? TRP D 143  . ? 1_555 ? 
26 AC4 8 TYR D 204 ? TYR D 185  . ? 1_555 ? 
27 AC4 8 CYS D 207 ? CYS D 188  . ? 1_555 ? 
28 AC4 8 HOH O .   ? HOH D 2026 . ? 1_555 ? 
29 AC4 8 HIS E 123 ? HIS E 104  . ? 1_555 ? 
30 AC4 8 GLN E 131 ? GLN E 112  . ? 1_555 ? 
31 AC4 8 THR E 133 ? THR E 114  . ? 1_555 ? 
32 AC5 9 TRP A 72  ? TRP A 53   . ? 1_555 ? 
33 AC5 9 HIS A 123 ? HIS A 104  . ? 1_555 ? 
34 AC5 9 GLN A 131 ? GLN A 112  . ? 1_555 ? 
35 AC5 9 THR A 133 ? THR A 114  . ? 1_555 ? 
36 AC5 9 HOH L .   ? HOH A 2017 . ? 1_555 ? 
37 AC5 9 TYR E 108 ? TYR E 89   . ? 1_555 ? 
38 AC5 9 TRP E 162 ? TRP E 143  . ? 1_555 ? 
39 AC5 9 TYR E 204 ? TYR E 185  . ? 1_555 ? 
40 AC5 9 TYR E 211 ? TYR E 192  . ? 1_555 ? 
41 AC6 3 ARG C 42  ? ARG C 23   . ? 2_565 ? 
42 AC6 3 ASN D 85  ? ASN D 66   . ? 1_555 ? 
43 AC6 3 SER D 87  ? SER D 68   . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4UM1 
_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                    4UM1 
_atom_sites.fract_transf_matrix[1][1]   0.012932 
_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]   0.008123 
_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]   0.007846 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LEU A 1 20  ? -11.161 63.784 -4.333  1.00 45.45  ? 1    LEU A N   1 
ATOM   2    C CA  . LEU A 1 20  ? -10.887 62.752 -5.333  1.00 39.77  ? 1    LEU A CA  1 
ATOM   3    C C   . LEU A 1 20  ? -12.056 61.794 -5.504  1.00 41.63  ? 1    LEU A C   1 
ATOM   4    O O   . LEU A 1 20  ? -12.591 61.269 -4.526  1.00 46.41  ? 1    LEU A O   1 
ATOM   5    C CB  . LEU A 1 20  ? -9.663  61.931 -4.943  1.00 42.64  ? 1    LEU A CB  1 
ATOM   6    C CG  . LEU A 1 20  ? -8.292  62.574 -5.103  1.00 42.18  ? 1    LEU A CG  1 
ATOM   7    C CD1 . LEU A 1 20  ? -7.210  61.538 -4.832  1.00 36.99  ? 1    LEU A CD1 1 
ATOM   8    C CD2 . LEU A 1 20  ? -8.147  63.154 -6.489  1.00 31.25  ? 1    LEU A CD2 1 
ATOM   9    N N   . ASP A 1 21  ? -12.454 61.564 -6.747  1.00 40.38  ? 2    ASP A N   1 
ATOM   10   C CA  . ASP A 1 21  ? -13.413 60.505 -7.041  1.00 38.89  ? 2    ASP A CA  1 
ATOM   11   C C   . ASP A 1 21  ? -12.700 59.383 -7.813  1.00 40.04  ? 2    ASP A C   1 
ATOM   12   O O   . ASP A 1 21  ? -11.514 59.511 -8.146  1.00 37.12  ? 2    ASP A O   1 
ATOM   13   C CB  . ASP A 1 21  ? -14.630 61.049 -7.810  1.00 39.45  ? 2    ASP A CB  1 
ATOM   14   C CG  . ASP A 1 21  ? -14.243 62.012 -8.932  1.00 56.31  ? 2    ASP A CG  1 
ATOM   15   O OD1 . ASP A 1 21  ? -13.211 61.775 -9.604  1.00 57.52  ? 2    ASP A OD1 1 
ATOM   16   O OD2 . ASP A 1 21  ? -14.973 63.010 -9.146  1.00 67.19  ? 2    ASP A OD2 1 
ATOM   17   N N   . ARG A 1 22  ? -13.405 58.288 -8.089  1.00 33.82  ? 3    ARG A N   1 
ATOM   18   C CA  . ARG A 1 22  ? -12.800 57.188 -8.818  1.00 27.89  ? 3    ARG A CA  1 
ATOM   19   C C   . ARG A 1 22  ? -12.213 57.626 -10.151 1.00 29.03  ? 3    ARG A C   1 
ATOM   20   O O   . ARG A 1 22  ? -11.134 57.160 -10.534 1.00 35.36  ? 3    ARG A O   1 
ATOM   21   C CB  . ARG A 1 22  ? -13.798 56.065 -9.045  1.00 29.31  ? 3    ARG A CB  1 
ATOM   22   C CG  . ARG A 1 22  ? -14.027 55.198 -7.855  1.00 26.28  ? 3    ARG A CG  1 
ATOM   23   C CD  . ARG A 1 22  ? -15.027 54.106 -8.188  1.00 33.18  ? 3    ARG A CD  1 
ATOM   24   N NE  . ARG A 1 22  ? -15.232 53.242 -7.035  1.00 45.67  ? 3    ARG A NE  1 
ATOM   25   C CZ  . ARG A 1 22  ? -16.056 53.535 -6.033  1.00 58.72  ? 3    ARG A CZ  1 
ATOM   26   N NH1 . ARG A 1 22  ? -16.766 54.663 -6.057  1.00 50.45  ? 3    ARG A NH1 1 
ATOM   27   N NH2 . ARG A 1 22  ? -16.169 52.696 -5.009  1.00 65.32  ? 3    ARG A NH2 1 
ATOM   28   N N   . ALA A 1 23  ? -12.916 58.514 -10.849 1.00 26.31  ? 4    ALA A N   1 
ATOM   29   C CA  . ALA A 1 23  ? -12.479 58.945 -12.169 1.00 27.99  ? 4    ALA A CA  1 
ATOM   30   C C   . ALA A 1 23  ? -11.098 59.589 -12.098 1.00 31.11  ? 4    ALA A C   1 
ATOM   31   O O   . ALA A 1 23  ? -10.217 59.295 -12.918 1.00 27.77  ? 4    ALA A O   1 
ATOM   32   C CB  . ALA A 1 23  ? -13.483 59.888 -12.767 1.00 36.90  ? 4    ALA A CB  1 
ATOM   33   N N   . ASP A 1 24  ? -10.914 60.447 -11.093 1.00 34.29  ? 5    ASP A N   1 
ATOM   34   C CA  . ASP A 1 24  ? -9.649  61.146 -10.855 1.00 26.61  ? 5    ASP A CA  1 
ATOM   35   C C   . ASP A 1 24  ? -8.487  60.198 -10.515 1.00 26.01  ? 5    ASP A C   1 
ATOM   36   O O   . ASP A 1 24  ? -7.392  60.324 -11.075 1.00 24.86  ? 5    ASP A O   1 
ATOM   37   C CB  . ASP A 1 24  ? -9.841  62.188 -9.753  1.00 34.51  ? 5    ASP A CB  1 
ATOM   38   C CG  . ASP A 1 24  ? -10.684 63.384 -10.209 1.00 54.21  ? 5    ASP A CG  1 
ATOM   39   O OD1 . ASP A 1 24  ? -10.604 63.733 -11.418 1.00 58.36  ? 5    ASP A OD1 1 
ATOM   40   O OD2 . ASP A 1 24  ? -11.412 63.971 -9.352  1.00 52.38  ? 5    ASP A OD2 1 
ATOM   41   N N   . ILE A 1 25  ? -8.742  59.241 -9.618  1.00 27.52  ? 6    ILE A N   1 
ATOM   42   C CA  . ILE A 1 25  ? -7.751  58.228 -9.225  1.00 24.10  ? 6    ILE A CA  1 
ATOM   43   C C   . ILE A 1 25  ? -7.265  57.370 -10.390 1.00 21.30  ? 6    ILE A C   1 
ATOM   44   O O   . ILE A 1 25  ? -6.060  57.200 -10.607 1.00 19.28  ? 6    ILE A O   1 
ATOM   45   C CB  . ILE A 1 25  ? -8.292  57.297 -8.106  1.00 24.42  ? 6    ILE A CB  1 
ATOM   46   C CG1 . ILE A 1 25  ? -8.568  58.102 -6.835  1.00 27.93  ? 6    ILE A CG1 1 
ATOM   47   C CG2 . ILE A 1 25  ? -7.293  56.178 -7.789  1.00 20.62  ? 6    ILE A CG2 1 
ATOM   48   C CD1 . ILE A 1 25  ? -9.345  57.339 -5.780  1.00 28.12  ? 6    ILE A CD1 1 
ATOM   49   N N   . LEU A 1 26  ? -8.215  56.827 -11.138 1.00 21.87  ? 7    LEU A N   1 
ATOM   50   C CA  . LEU A 1 26  ? -7.883  55.985 -12.274 1.00 20.57  ? 7    LEU A CA  1 
ATOM   51   C C   . LEU A 1 26  ? -7.142  56.781 -13.335 1.00 22.02  ? 7    LEU A C   1 
ATOM   52   O O   . LEU A 1 26  ? -6.256  56.254 -14.018 1.00 24.72  ? 7    LEU A O   1 
ATOM   53   C CB  . LEU A 1 26  ? -9.136  55.326 -12.837 1.00 18.93  ? 7    LEU A CB  1 
ATOM   54   C CG  . LEU A 1 26  ? -9.746  54.323 -11.853 1.00 20.01  ? 7    LEU A CG  1 
ATOM   55   C CD1 . LEU A 1 26  ? -11.195 54.026 -12.201 1.00 21.42  ? 7    LEU A CD1 1 
ATOM   56   C CD2 . LEU A 1 26  ? -8.931  53.024 -11.777 1.00 15.60  ? 7    LEU A CD2 1 
ATOM   57   N N   . TYR A 1 27  ? -7.487  58.059 -13.453 1.00 20.50  ? 8    TYR A N   1 
ATOM   58   C CA  . TYR A 1 27  ? -6.786  58.940 -14.376 1.00 20.36  ? 8    TYR A CA  1 
ATOM   59   C C   . TYR A 1 27  ? -5.332  59.089 -13.963 1.00 20.54  ? 8    TYR A C   1 
ATOM   60   O O   . TYR A 1 27  ? -4.441  58.843 -14.765 1.00 21.76  ? 8    TYR A O   1 
ATOM   61   C CB  . TYR A 1 27  ? -7.460  60.306 -14.442 1.00 23.98  ? 8    TYR A CB  1 
ATOM   62   C CG  . TYR A 1 27  ? -6.761  61.277 -15.359 1.00 26.92  ? 8    TYR A CG  1 
ATOM   63   C CD1 . TYR A 1 27  ? -6.918  61.191 -16.736 1.00 31.90  ? 8    TYR A CD1 1 
ATOM   64   C CD2 . TYR A 1 27  ? -5.950  62.293 -14.848 1.00 27.35  ? 8    TYR A CD2 1 
ATOM   65   C CE1 . TYR A 1 27  ? -6.281  62.088 -17.589 1.00 35.06  ? 8    TYR A CE1 1 
ATOM   66   C CE2 . TYR A 1 27  ? -5.319  63.203 -15.687 1.00 31.88  ? 8    TYR A CE2 1 
ATOM   67   C CZ  . TYR A 1 27  ? -5.486  63.089 -17.058 1.00 40.74  ? 8    TYR A CZ  1 
ATOM   68   O OH  . TYR A 1 27  ? -4.859  63.979 -17.901 1.00 58.29  ? 8    TYR A OH  1 
ATOM   69   N N   . ASN A 1 28  ? -5.096  59.487 -12.715 1.00 18.02  ? 9    ASN A N   1 
ATOM   70   C CA  . ASN A 1 28  ? -3.733  59.600 -12.211 1.00 21.20  ? 9    ASN A CA  1 
ATOM   71   C C   . ASN A 1 28  ? -2.926  58.320 -12.371 1.00 21.47  ? 9    ASN A C   1 
ATOM   72   O O   . ASN A 1 28  ? -1.755  58.370 -12.750 1.00 25.36  ? 9    ASN A O   1 
ATOM   73   C CB  . ASN A 1 28  ? -3.717  60.048 -10.749 1.00 24.36  ? 9    ASN A CB  1 
ATOM   74   C CG  . ASN A 1 28  ? -4.327  61.423 -10.559 1.00 22.42  ? 9    ASN A CG  1 
ATOM   75   O OD1 . ASN A 1 28  ? -4.349  62.239 -11.480 1.00 22.43  ? 9    ASN A OD1 1 
ATOM   76   N ND2 . ASN A 1 28  ? -4.840  61.681 -9.356  1.00 20.69  ? 9    ASN A ND2 1 
ATOM   77   N N   . ILE A 1 29  ? -3.559  57.180 -12.095 1.00 23.18  ? 10   ILE A N   1 
ATOM   78   C CA  . ILE A 1 29  ? -2.895  55.889 -12.233 1.00 18.26  ? 10   ILE A CA  1 
ATOM   79   C C   . ILE A 1 29  ? -2.497  55.609 -13.670 1.00 22.02  ? 10   ILE A C   1 
ATOM   80   O O   . ILE A 1 29  ? -1.375  55.200 -13.936 1.00 26.76  ? 10   ILE A O   1 
ATOM   81   C CB  . ILE A 1 29  ? -3.720  54.735 -11.658 1.00 16.84  ? 10   ILE A CB  1 
ATOM   82   C CG1 . ILE A 1 29  ? -3.790  54.883 -10.130 1.00 16.31  ? 10   ILE A CG1 1 
ATOM   83   C CG2 . ILE A 1 29  ? -3.096  53.389 -12.056 1.00 15.57  ? 10   ILE A CG2 1 
ATOM   84   C CD1 . ILE A 1 29  ? -4.514  53.764 -9.394  1.00 14.37  ? 10   ILE A CD1 1 
ATOM   85   N N   . ARG A 1 30  ? -3.398  55.869 -14.606 1.00 19.03  ? 11   ARG A N   1 
ATOM   86   C CA  . ARG A 1 30  ? -3.070  55.661 -16.003 1.00 19.30  ? 11   ARG A CA  1 
ATOM   87   C C   . ARG A 1 30  ? -1.904  56.523 -16.499 1.00 24.94  ? 11   ARG A C   1 
ATOM   88   O O   . ARG A 1 30  ? -1.148  56.097 -17.362 1.00 30.90  ? 11   ARG A O   1 
ATOM   89   C CB  . ARG A 1 30  ? -4.293  55.892 -16.871 1.00 28.96  ? 11   ARG A CB  1 
ATOM   90   C CG  . ARG A 1 30  ? -4.393  54.912 -17.992 1.00 50.83  ? 11   ARG A CG  1 
ATOM   91   C CD  . ARG A 1 30  ? -4.946  55.535 -19.259 1.00 60.55  ? 11   ARG A CD  1 
ATOM   92   N NE  . ARG A 1 30  ? -4.608  54.693 -20.410 1.00 89.27  ? 11   ARG A NE  1 
ATOM   93   C CZ  . ARG A 1 30  ? -4.935  54.956 -21.673 1.00 77.76  ? 11   ARG A CZ  1 
ATOM   94   N NH1 . ARG A 1 30  ? -5.626  56.049 -21.976 1.00 66.58  ? 11   ARG A NH1 1 
ATOM   95   N NH2 . ARG A 1 30  ? -4.567  54.118 -22.635 1.00 76.10  ? 11   ARG A NH2 1 
ATOM   96   N N   . GLN A 1 31  ? -1.752  57.726 -15.947 1.00 30.73  ? 12   GLN A N   1 
ATOM   97   C CA  . GLN A 1 31  ? -0.702  58.663 -16.374 1.00 24.91  ? 12   GLN A CA  1 
ATOM   98   C C   . GLN A 1 31  ? 0.679   58.469 -15.730 1.00 26.55  ? 12   GLN A C   1 
ATOM   99   O O   . GLN A 1 31  ? 1.671   58.915 -16.286 1.00 35.65  ? 12   GLN A O   1 
ATOM   100  C CB  . GLN A 1 31  ? -1.142  60.099 -16.129 1.00 24.06  ? 12   GLN A CB  1 
ATOM   101  C CG  . GLN A 1 31  ? -2.453  60.504 -16.797 1.00 31.66  ? 12   GLN A CG  1 
ATOM   102  C CD  . GLN A 1 31  ? -2.347  60.564 -18.304 1.00 41.90  ? 12   GLN A CD  1 
ATOM   103  O OE1 . GLN A 1 31  ? -1.244  60.525 -18.865 1.00 46.70  ? 12   GLN A OE1 1 
ATOM   104  N NE2 . GLN A 1 31  ? -3.497  60.647 -18.975 1.00 37.59  ? 12   GLN A NE2 1 
ATOM   105  N N   . THR A 1 32  ? 0.754   57.816 -14.574 1.00 20.36  ? 13   THR A N   1 
ATOM   106  C CA  . THR A 1 32  ? 1.976   57.876 -13.787 1.00 25.19  ? 13   THR A CA  1 
ATOM   107  C C   . THR A 1 32  ? 2.476   56.532 -13.296 1.00 36.98  ? 13   THR A C   1 
ATOM   108  O O   . THR A 1 32  ? 3.414   56.465 -12.481 1.00 41.39  ? 13   THR A O   1 
ATOM   109  C CB  . THR A 1 32  ? 1.775   58.772 -12.528 1.00 32.39  ? 13   THR A CB  1 
ATOM   110  O OG1 . THR A 1 32  ? 0.745   58.224 -11.699 1.00 26.18  ? 13   THR A OG1 1 
ATOM   111  C CG2 . THR A 1 32  ? 1.388   60.202 -12.907 1.00 31.93  ? 13   THR A CG2 1 
ATOM   112  N N   . SER A 1 33  ? 1.786   55.498 -13.723 1.00 44.86  ? 14   SER A N   1 
ATOM   113  C CA  . SER A 1 33  ? 1.945   54.163 -13.186 1.00 40.28  ? 14   SER A CA  1 
ATOM   114  C C   . SER A 1 33  ? 3.265   53.483 -13.427 1.00 44.77  ? 14   SER A C   1 
ATOM   115  O O   . SER A 1 33  ? 3.761   52.835 -12.527 1.00 37.78  ? 14   SER A O   1 
ATOM   116  C CB  . SER A 1 33  ? 0.798   53.283 -13.617 1.00 31.49  ? 14   SER A CB  1 
ATOM   117  O OG  . SER A 1 33  ? 1.001   51.986 -13.198 1.00 33.90  ? 14   SER A OG  1 
ATOM   118  N N   . ARG A 1 34  ? 3.853   53.631 -14.610 1.00 35.32  ? 15   ARG A N   1 
ATOM   119  C CA  . ARG A 1 34  ? 5.093   52.920 -14.876 1.00 30.81  ? 15   ARG A CA  1 
ATOM   120  C C   . ARG A 1 34  ? 5.048   51.407 -14.750 1.00 24.52  ? 15   ARG A C   1 
ATOM   121  O O   . ARG A 1 34  ? 5.605   50.853 -13.890 1.00 25.00  ? 15   ARG A O   1 
ATOM   122  C CB  . ARG A 1 34  ? 6.207   53.477 -14.002 1.00 37.47  ? 15   ARG A CB  1 
ATOM   123  C CG  . ARG A 1 34  ? 6.588   54.891 -14.318 1.00 39.26  ? 15   ARG A CG  1 
ATOM   124  C CD  . ARG A 1 34  ? 6.719   55.102 -15.807 1.00 45.42  ? 15   ARG A CD  1 
ATOM   125  N NE  . ARG A 1 34  ? 7.969   54.593 -16.354 1.00 49.21  ? 15   ARG A NE  1 
ATOM   126  C CZ  . ARG A 1 34  ? 9.156   55.157 -16.219 1.00 39.80  ? 15   ARG A CZ  1 
ATOM   127  N NH1 . ARG A 1 34  ? 9.300   56.279 -15.556 1.00 31.65  ? 15   ARG A NH1 1 
ATOM   128  N NH2 . ARG A 1 34  ? 10.193  54.599 -16.766 1.00 26.05  ? 15   ARG A NH2 1 
ATOM   129  N N   . PRO A 1 35  ? 4.316   50.748 -15.709 1.00 25.13  ? 16   PRO A N   1 
ATOM   130  C CA  . PRO A 1 35  ? 4.248   49.285 -15.607 1.00 24.79  ? 16   PRO A CA  1 
ATOM   131  C C   . PRO A 1 35  ? 5.523   48.478 -15.861 1.00 24.40  ? 16   PRO A C   1 
ATOM   132  O O   . PRO A 1 35  ? 5.549   47.307 -15.663 1.00 18.88  ? 16   PRO A O   1 
ATOM   133  C CB  . PRO A 1 35  ? 3.263   48.924 -16.693 1.00 22.53  ? 16   PRO A CB  1 
ATOM   134  C CG  . PRO A 1 35  ? 2.480   50.102 -16.900 1.00 21.34  ? 16   PRO A CG  1 
ATOM   135  C CD  . PRO A 1 35  ? 3.507   51.107 -16.944 1.00 26.04  ? 16   PRO A CD  1 
ATOM   136  N N   . ASP A 1 36  ? 6.533   49.100 -16.420 1.00 30.71  ? 17   ASP A N   1 
ATOM   137  C CA  . ASP A 1 36  ? 7.800   48.466 -16.681 1.00 28.04  ? 17   ASP A CA  1 
ATOM   138  C C   . ASP A 1 36  ? 8.766   48.523 -15.522 1.00 19.69  ? 17   ASP A C   1 
ATOM   139  O O   . ASP A 1 36  ? 9.765   47.908 -15.541 1.00 23.91  ? 17   ASP A O   1 
ATOM   140  C CB  . ASP A 1 36  ? 8.395   49.065 -17.953 1.00 22.32  ? 17   ASP A CB  1 
ATOM   141  C CG  . ASP A 1 36  ? 8.250   50.551 -18.020 1.00 44.24  ? 17   ASP A CG  1 
ATOM   142  O OD1 . ASP A 1 36  ? 7.259   51.084 -17.533 1.00 39.25  ? 17   ASP A OD1 1 
ATOM   143  O OD2 . ASP A 1 36  ? 9.133   51.207 -18.591 1.00 50.27  ? 17   ASP A OD2 1 
ATOM   144  N N   . VAL A 1 37  ? 8.413   49.254 -14.495 1.00 21.65  ? 18   VAL A N   1 
ATOM   145  C CA  . VAL A 1 37  ? 9.322   49.534 -13.376 1.00 22.34  ? 18   VAL A CA  1 
ATOM   146  C C   . VAL A 1 37  ? 8.935   48.834 -12.072 1.00 20.93  ? 18   VAL A C   1 
ATOM   147  O O   . VAL A 1 37  ? 7.909   49.151 -11.457 1.00 17.83  ? 18   VAL A O   1 
ATOM   148  C CB  . VAL A 1 37  ? 9.381   51.038 -13.052 1.00 18.53  ? 18   VAL A CB  1 
ATOM   149  C CG1 . VAL A 1 37  ? 10.279  51.266 -11.848 1.00 10.96  ? 18   VAL A CG1 1 
ATOM   150  C CG2 . VAL A 1 37  ? 9.848   51.826 -14.252 1.00 21.77  ? 18   VAL A CG2 1 
ATOM   151  N N   . ILE A 1 38  ? 9.778   47.902 -11.646 1.00 21.10  ? 19   ILE A N   1 
ATOM   152  C CA  . ILE A 1 38  ? 9.583   47.192 -10.381 1.00 24.13  ? 19   ILE A CA  1 
ATOM   153  C C   . ILE A 1 38  ? 9.617   48.162 -9.172  1.00 22.58  ? 19   ILE A C   1 
ATOM   154  O O   . ILE A 1 38  ? 10.558  48.943 -9.022  1.00 28.21  ? 19   ILE A O   1 
ATOM   155  C CB  . ILE A 1 38  ? 10.621  46.032 -10.252 1.00 20.38  ? 19   ILE A CB  1 
ATOM   156  C CG1 . ILE A 1 38  ? 10.371  45.193 -9.002  1.00 22.57  ? 19   ILE A CG1 1 
ATOM   157  C CG2 . ILE A 1 38  ? 12.051  46.566 -10.288 1.00 16.79  ? 19   ILE A CG2 1 
ATOM   158  C CD1 . ILE A 1 38  ? 11.231  43.934 -8.949  1.00 26.34  ? 19   ILE A CD1 1 
ATOM   159  N N   . PRO A 1 39  ? 8.571   48.123 -8.316  1.00 23.71  ? 20   PRO A N   1 
ATOM   160  C CA  . PRO A 1 39  ? 8.429   49.090 -7.215  1.00 22.12  ? 20   PRO A CA  1 
ATOM   161  C C   . PRO A 1 39  ? 9.265   48.729 -5.984  1.00 27.06  ? 20   PRO A C   1 
ATOM   162  O O   . PRO A 1 39  ? 8.708   48.520 -4.892  1.00 25.99  ? 20   PRO A O   1 
ATOM   163  C CB  . PRO A 1 39  ? 6.924   49.034 -6.890  1.00 19.48  ? 20   PRO A CB  1 
ATOM   164  C CG  . PRO A 1 39  ? 6.526   47.615 -7.214  1.00 20.55  ? 20   PRO A CG  1 
ATOM   165  C CD  . PRO A 1 39  ? 7.426   47.183 -8.380  1.00 25.06  ? 20   PRO A CD  1 
ATOM   166  N N   . THR A 1 40  ? 10.584  48.665 -6.163  1.00 29.37  ? 21   THR A N   1 
ATOM   167  C CA  . THR A 1 40  ? 11.495  48.400 -5.050  1.00 37.64  ? 21   THR A CA  1 
ATOM   168  C C   . THR A 1 40  ? 11.544  49.602 -4.123  1.00 46.16  ? 21   THR A C   1 
ATOM   169  O O   . THR A 1 40  ? 11.327  50.735 -4.556  1.00 47.60  ? 21   THR A O   1 
ATOM   170  C CB  . THR A 1 40  ? 12.922  48.083 -5.532  1.00 36.95  ? 21   THR A CB  1 
ATOM   171  O OG1 . THR A 1 40  ? 13.355  49.121 -6.414  1.00 44.23  ? 21   THR A OG1 1 
ATOM   172  C CG2 . THR A 1 40  ? 12.971  46.749 -6.271  1.00 34.04  ? 21   THR A CG2 1 
ATOM   173  N N   . GLN A 1 41  ? 11.821  49.342 -2.848  1.00 53.99  ? 22   GLN A N   1 
ATOM   174  C CA  . GLN A 1 41  ? 11.925  50.397 -1.847  1.00 63.28  ? 22   GLN A CA  1 
ATOM   175  C C   . GLN A 1 41  ? 13.279  50.339 -1.153  1.00 67.64  ? 22   GLN A C   1 
ATOM   176  O O   . GLN A 1 41  ? 13.423  49.665 -0.135  1.00 67.67  ? 22   GLN A O   1 
ATOM   177  C CB  . GLN A 1 41  ? 10.820  50.261 -0.795  1.00 62.88  ? 22   GLN A CB  1 
ATOM   178  C CG  . GLN A 1 41  ? 9.506   50.962 -1.118  1.00 67.58  ? 22   GLN A CG  1 
ATOM   179  C CD  . GLN A 1 41  ? 8.495   50.859 0.029   1.00 80.43  ? 22   GLN A CD  1 
ATOM   180  O OE1 . GLN A 1 41  ? 8.139   49.753 0.472   1.00 60.61  ? 22   GLN A OE1 1 
ATOM   181  N NE2 . GLN A 1 41  ? 8.037   52.018 0.525   1.00 79.48  ? 22   GLN A NE2 1 
ATOM   182  N N   . ARG A 1 42  ? 14.199  51.143 -1.642  1.00 74.48  ? 23   ARG A N   1 
ATOM   183  C CA  . ARG A 1 42  ? 15.489  51.277 -1.033  1.00 75.51  ? 23   ARG A CA  1 
ATOM   184  C C   . ARG A 1 42  ? 16.187  49.969 -1.102  1.00 74.10  ? 23   ARG A C   1 
ATOM   185  O O   . ARG A 1 42  ? 16.874  49.589 -0.190  1.00 80.85  ? 23   ARG A O   1 
ATOM   186  C CB  . ARG A 1 42  ? 15.349  51.738 0.410   1.00 82.26  ? 23   ARG A CB  1 
ATOM   187  C CG  . ARG A 1 42  ? 14.526  53.009 0.590   1.00 81.59  ? 23   ARG A CG  1 
ATOM   188  C CD  . ARG A 1 42  ? 14.705  53.594 1.981   1.00 89.03  ? 23   ARG A CD  1 
ATOM   189  N NE  . ARG A 1 42  ? 13.437  53.974 2.589   1.00 91.17  ? 23   ARG A NE  1 
ATOM   190  C CZ  . ARG A 1 42  ? 13.209  53.984 3.895   1.00 89.64  ? 23   ARG A CZ  1 
ATOM   191  N NH1 . ARG A 1 42  ? 14.159  53.640 4.748   1.00 90.11  ? 23   ARG A NH1 1 
ATOM   192  N NH2 . ARG A 1 42  ? 12.026  54.326 4.350   1.00 92.39  ? 23   ARG A NH2 1 
ATOM   193  N N   . ASP A 1 43  ? 15.987  49.274 -2.205  1.00 70.38  ? 24   ASP A N   1 
ATOM   194  C CA  . ASP A 1 43  ? 16.831  48.155 -2.583  1.00 75.36  ? 24   ASP A CA  1 
ATOM   195  C C   . ASP A 1 43  ? 16.565  46.897 -1.781  1.00 65.76  ? 24   ASP A C   1 
ATOM   196  O O   . ASP A 1 43  ? 17.364  45.973 -1.757  1.00 61.39  ? 24   ASP A O   1 
ATOM   197  C CB  . ASP A 1 43  ? 18.306  48.552 -2.506  1.00 93.72  ? 24   ASP A CB  1 
ATOM   198  C CG  . ASP A 1 43  ? 18.755  49.425 -3.686  1.00 104.83 ? 24   ASP A CG  1 
ATOM   199  O OD1 . ASP A 1 43  ? 18.336  49.159 -4.829  1.00 98.44  ? 24   ASP A OD1 1 
ATOM   200  O OD2 . ASP A 1 43  ? 19.546  50.373 -3.478  1.00 107.05 ? 24   ASP A OD2 1 
ATOM   201  N N   . ARG A 1 44  ? 15.439  46.904 -1.100  1.00 56.98  ? 25   ARG A N   1 
ATOM   202  C CA  . ARG A 1 44  ? 14.819  45.737 -0.561  1.00 52.02  ? 25   ARG A CA  1 
ATOM   203  C C   . ARG A 1 44  ? 14.016  45.101 -1.667  1.00 52.37  ? 25   ARG A C   1 
ATOM   204  O O   . ARG A 1 44  ? 13.655  45.758 -2.610  1.00 50.47  ? 25   ARG A O   1 
ATOM   205  C CB  . ARG A 1 44  ? 13.912  46.165 0.563   1.00 55.81  ? 25   ARG A CB  1 
ATOM   206  C CG  . ARG A 1 44  ? 14.631  47.033 1.569   1.00 74.32  ? 25   ARG A CG  1 
ATOM   207  C CD  . ARG A 1 44  ? 13.774  47.275 2.800   1.00 88.38  ? 25   ARG A CD  1 
ATOM   208  N NE  . ARG A 1 44  ? 14.527  47.877 3.885   1.00 98.29  ? 25   ARG A NE  1 
ATOM   209  C CZ  . ARG A 1 44  ? 14.452  49.152 4.223   1.00 95.07  ? 25   ARG A CZ  1 
ATOM   210  N NH1 . ARG A 1 44  ? 13.645  49.956 3.552   1.00 94.60  ? 25   ARG A NH1 1 
ATOM   211  N NH2 . ARG A 1 44  ? 15.181  49.618 5.226   1.00 86.79  ? 25   ARG A NH2 1 
ATOM   212  N N   . PRO A 1 45  ? 13.749  43.815 -1.554  1.00 39.23  ? 26   PRO A N   1 
ATOM   213  C CA  . PRO A 1 45  ? 12.916  43.103 -2.527  1.00 26.99  ? 26   PRO A CA  1 
ATOM   214  C C   . PRO A 1 45  ? 11.467  43.556 -2.410  1.00 29.06  ? 26   PRO A C   1 
ATOM   215  O O   . PRO A 1 45  ? 11.061  44.060 -1.364  1.00 34.26  ? 26   PRO A O   1 
ATOM   216  C CB  . PRO A 1 45  ? 13.029  41.644 -2.084  1.00 27.82  ? 26   PRO A CB  1 
ATOM   217  C CG  . PRO A 1 45  ? 14.237  41.592 -1.214  1.00 36.58  ? 26   PRO A CG  1 
ATOM   218  C CD  . PRO A 1 45  ? 14.339  42.918 -0.548  1.00 36.24  ? 26   PRO A CD  1 
ATOM   219  N N   . VAL A 1 46  ? 10.698  43.407 -3.478  1.00 28.87  ? 27   VAL A N   1 
ATOM   220  C CA  . VAL A 1 46  ? 9.251   43.525 -3.374  1.00 25.42  ? 27   VAL A CA  1 
ATOM   221  C C   . VAL A 1 46  ? 8.763   42.215 -2.766  1.00 20.25  ? 27   VAL A C   1 
ATOM   222  O O   . VAL A 1 46  ? 9.095   41.136 -3.262  1.00 19.97  ? 27   VAL A O   1 
ATOM   223  C CB  . VAL A 1 46  ? 8.631   43.703 -4.758  1.00 20.91  ? 27   VAL A CB  1 
ATOM   224  C CG1 . VAL A 1 46  ? 7.110   43.776 -4.661  1.00 18.39  ? 27   VAL A CG1 1 
ATOM   225  C CG2 . VAL A 1 46  ? 9.217   44.925 -5.437  1.00 17.59  ? 27   VAL A CG2 1 
ATOM   226  N N   . ALA A 1 47  ? 8.012   42.285 -1.677  1.00 20.46  ? 28   ALA A N   1 
ATOM   227  C CA  . ALA A 1 47  ? 7.498   41.045 -1.087  1.00 22.70  ? 28   ALA A CA  1 
ATOM   228  C C   . ALA A 1 47  ? 6.189   40.638 -1.757  1.00 24.85  ? 28   ALA A C   1 
ATOM   229  O O   . ALA A 1 47  ? 5.149   41.264 -1.535  1.00 22.97  ? 28   ALA A O   1 
ATOM   230  C CB  . ALA A 1 47  ? 7.297   41.192 0.384   1.00 15.01  ? 28   ALA A CB  1 
ATOM   231  N N   . VAL A 1 48  ? 6.240   39.586 -2.567  1.00 22.40  ? 29   VAL A N   1 
ATOM   232  C CA  . VAL A 1 48  ? 5.042   39.043 -3.214  1.00 21.84  ? 29   VAL A CA  1 
ATOM   233  C C   . VAL A 1 48  ? 4.532   37.803 -2.458  1.00 22.21  ? 29   VAL A C   1 
ATOM   234  O O   . VAL A 1 48  ? 5.290   36.866 -2.196  1.00 23.07  ? 29   VAL A O   1 
ATOM   235  C CB  . VAL A 1 48  ? 5.362   38.645 -4.666  1.00 22.02  ? 29   VAL A CB  1 
ATOM   236  C CG1 . VAL A 1 48  ? 4.126   38.111 -5.382  1.00 14.09  ? 29   VAL A CG1 1 
ATOM   237  C CG2 . VAL A 1 48  ? 6.004   39.816 -5.409  1.00 13.63  ? 29   VAL A CG2 1 
ATOM   238  N N   . SER A 1 49  ? 3.253   37.799 -2.110  1.00 19.25  ? 30   SER A N   1 
ATOM   239  C CA  . SER A 1 49  ? 2.635   36.618 -1.518  1.00 18.93  ? 30   SER A CA  1 
ATOM   240  C C   . SER A 1 49  ? 1.850   35.874 -2.582  1.00 26.99  ? 30   SER A C   1 
ATOM   241  O O   . SER A 1 49  ? 1.120   36.495 -3.390  1.00 23.90  ? 30   SER A O   1 
ATOM   242  C CB  . SER A 1 49  ? 1.676   37.004 -0.408  1.00 20.20  ? 30   SER A CB  1 
ATOM   243  O OG  . SER A 1 49  ? 2.241   38.022 0.368   1.00 42.57  ? 30   SER A OG  1 
ATOM   244  N N   . VAL A 1 50  ? 1.981   34.547 -2.568  1.00 24.50  ? 31   VAL A N   1 
ATOM   245  C CA  . VAL A 1 50  ? 1.286   33.699 -3.525  1.00 23.76  ? 31   VAL A CA  1 
ATOM   246  C C   . VAL A 1 50  ? 0.471   32.627 -2.827  1.00 30.27  ? 31   VAL A C   1 
ATOM   247  O O   . VAL A 1 50  ? 0.961   31.971 -1.912  1.00 38.06  ? 31   VAL A O   1 
ATOM   248  C CB  . VAL A 1 50  ? 2.258   33.025 -4.464  1.00 17.81  ? 31   VAL A CB  1 
ATOM   249  C CG1 . VAL A 1 50  ? 1.501   32.204 -5.481  1.00 19.24  ? 31   VAL A CG1 1 
ATOM   250  C CG2 . VAL A 1 50  ? 3.109   34.065 -5.146  1.00 17.74  ? 31   VAL A CG2 1 
ATOM   251  N N   . SER A 1 51  ? -0.773  32.450 -3.262  1.00 28.75  ? 32   SER A N   1 
ATOM   252  C CA  . SER A 1 51  ? -1.638  31.438 -2.681  1.00 26.59  ? 32   SER A CA  1 
ATOM   253  C C   . SER A 1 51  ? -2.496  30.778 -3.761  1.00 23.87  ? 32   SER A C   1 
ATOM   254  O O   . SER A 1 51  ? -3.175  31.480 -4.504  1.00 28.26  ? 32   SER A O   1 
ATOM   255  C CB  . SER A 1 51  ? -2.522  32.079 -1.614  1.00 24.62  ? 32   SER A CB  1 
ATOM   256  O OG  . SER A 1 51  ? -3.329  31.097 -0.991  1.00 43.64  ? 32   SER A OG  1 
ATOM   257  N N   . LEU A 1 52  ? -2.465  29.445 -3.871  1.00 21.85  ? 33   LEU A N   1 
ATOM   258  C CA  . LEU A 1 52  ? -3.345  28.759 -4.836  1.00 18.20  ? 33   LEU A CA  1 
ATOM   259  C C   . LEU A 1 52  ? -4.615  28.230 -4.169  1.00 23.45  ? 33   LEU A C   1 
ATOM   260  O O   . LEU A 1 52  ? -4.547  27.544 -3.158  1.00 34.33  ? 33   LEU A O   1 
ATOM   261  C CB  . LEU A 1 52  ? -2.629  27.611 -5.541  1.00 13.57  ? 33   LEU A CB  1 
ATOM   262  C CG  . LEU A 1 52  ? -1.260  27.956 -6.128  1.00 19.46  ? 33   LEU A CG  1 
ATOM   263  C CD1 . LEU A 1 52  ? -0.720  26.850 -7.013  1.00 15.96  ? 33   LEU A CD1 1 
ATOM   264  C CD2 . LEU A 1 52  ? -1.309  29.277 -6.896  1.00 19.96  ? 33   LEU A CD2 1 
ATOM   265  N N   . LYS A 1 53  ? -5.776  28.557 -4.725  1.00 26.85  ? 34   LYS A N   1 
ATOM   266  C CA  . LYS A 1 53  ? -7.036  27.965 -4.280  1.00 24.47  ? 34   LYS A CA  1 
ATOM   267  C C   . LYS A 1 53  ? -7.482  27.010 -5.367  1.00 23.41  ? 34   LYS A C   1 
ATOM   268  O O   . LYS A 1 53  ? -7.778  27.449 -6.483  1.00 21.05  ? 34   LYS A O   1 
ATOM   269  C CB  . LYS A 1 53  ? -8.105  29.040 -4.083  1.00 21.51  ? 34   LYS A CB  1 
ATOM   270  C CG  . LYS A 1 53  ? -7.600  30.306 -3.406  1.00 30.21  ? 34   LYS A CG  1 
ATOM   271  C CD  . LYS A 1 53  ? -7.289  30.113 -1.927  1.00 39.79  ? 34   LYS A CD  1 
ATOM   272  C CE  . LYS A 1 53  ? -6.772  31.420 -1.290  1.00 31.16  ? 34   LYS A CE  1 
ATOM   273  N NZ  . LYS A 1 53  ? -6.450  31.192 0.163   1.00 61.59  ? 34   LYS A NZ  1 
ATOM   274  N N   . PHE A 1 54  ? -7.519  25.713 -5.064  1.00 21.41  ? 35   PHE A N   1 
ATOM   275  C CA  . PHE A 1 54  ? -7.891  24.747 -6.094  1.00 22.33  ? 35   PHE A CA  1 
ATOM   276  C C   . PHE A 1 54  ? -9.386  24.709 -6.341  1.00 20.96  ? 35   PHE A C   1 
ATOM   277  O O   . PHE A 1 54  ? -10.182 24.687 -5.408  1.00 27.71  ? 35   PHE A O   1 
ATOM   278  C CB  . PHE A 1 54  ? -7.324  23.368 -5.783  1.00 21.83  ? 35   PHE A CB  1 
ATOM   279  C CG  . PHE A 1 54  ? -5.836  23.346 -5.791  1.00 21.11  ? 35   PHE A CG  1 
ATOM   280  C CD1 . PHE A 1 54  ? -5.147  23.210 -6.983  1.00 23.22  ? 35   PHE A CD1 1 
ATOM   281  C CD2 . PHE A 1 54  ? -5.118  23.533 -4.617  1.00 21.25  ? 35   PHE A CD2 1 
ATOM   282  C CE1 . PHE A 1 54  ? -3.758  23.225 -7.005  1.00 20.23  ? 35   PHE A CE1 1 
ATOM   283  C CE2 . PHE A 1 54  ? -3.735  23.550 -4.626  1.00 15.20  ? 35   PHE A CE2 1 
ATOM   284  C CZ  . PHE A 1 54  ? -3.059  23.396 -5.820  1.00 18.91  ? 35   PHE A CZ  1 
ATOM   285  N N   . ILE A 1 55  ? -9.757  24.729 -7.612  1.00 20.18  ? 36   ILE A N   1 
ATOM   286  C CA  . ILE A 1 55  ? -11.166 24.737 -7.977  1.00 28.61  ? 36   ILE A CA  1 
ATOM   287  C C   . ILE A 1 55  ? -11.588 23.398 -8.596  1.00 25.43  ? 36   ILE A C   1 
ATOM   288  O O   . ILE A 1 55  ? -12.692 22.910 -8.345  1.00 25.20  ? 36   ILE A O   1 
ATOM   289  C CB  . ILE A 1 55  ? -11.513 25.931 -8.932  1.00 23.66  ? 36   ILE A CB  1 
ATOM   290  C CG1 . ILE A 1 55  ? -10.929 27.252 -8.396  1.00 19.45  ? 36   ILE A CG1 1 
ATOM   291  C CG2 . ILE A 1 55  ? -13.025 26.025 -9.152  1.00 13.11  ? 36   ILE A CG2 1 
ATOM   292  C CD1 . ILE A 1 55  ? -11.436 27.654 -7.009  1.00 18.21  ? 36   ILE A CD1 1 
ATOM   293  N N   . ASN A 1 56  ? -10.707 22.807 -9.402  1.00 22.02  ? 37   ASN A N   1 
ATOM   294  C CA  . ASN A 1 56  ? -11.048 21.579 -10.097 1.00 20.64  ? 37   ASN A CA  1 
ATOM   295  C C   . ASN A 1 56  ? -9.830  20.783 -10.514 1.00 24.52  ? 37   ASN A C   1 
ATOM   296  O O   . ASN A 1 56  ? -8.756  21.342 -10.691 1.00 25.67  ? 37   ASN A O   1 
ATOM   297  C CB  . ASN A 1 56  ? -11.905 21.894 -11.333 1.00 23.39  ? 37   ASN A CB  1 
ATOM   298  C CG  . ASN A 1 56  ? -13.044 20.901 -11.525 1.00 28.99  ? 37   ASN A CG  1 
ATOM   299  O OD1 . ASN A 1 56  ? -12.862 19.673 -11.441 1.00 22.99  ? 37   ASN A OD1 1 
ATOM   300  N ND2 . ASN A 1 56  ? -14.235 21.435 -11.776 1.00 33.51  ? 37   ASN A ND2 1 
ATOM   301  N N   . ILE A 1 57  ? -10.005 19.471 -10.670 1.00 31.30  ? 38   ILE A N   1 
ATOM   302  C CA  . ILE A 1 57  ? -8.973  18.618 -11.268 1.00 27.40  ? 38   ILE A CA  1 
ATOM   303  C C   . ILE A 1 57  ? -9.624  17.862 -12.416 1.00 27.63  ? 38   ILE A C   1 
ATOM   304  O O   . ILE A 1 57  ? -10.672 17.248 -12.231 1.00 33.65  ? 38   ILE A O   1 
ATOM   305  C CB  . ILE A 1 57  ? -8.344  17.673 -10.234 1.00 20.62  ? 38   ILE A CB  1 
ATOM   306  C CG1 . ILE A 1 57  ? -7.618  18.511 -9.178  1.00 18.27  ? 38   ILE A CG1 1 
ATOM   307  C CG2 . ILE A 1 57  ? -7.388  16.724 -10.912 1.00 17.92  ? 38   ILE A CG2 1 
ATOM   308  C CD1 . ILE A 1 57  ? -7.098  17.760 -8.023  1.00 18.02  ? 38   ILE A CD1 1 
ATOM   309  N N   . LEU A 1 58  ? -9.038  17.939 -13.610 1.00 31.11  ? 39   LEU A N   1 
ATOM   310  C CA  . LEU A 1 58  ? -9.817  17.670 -14.816 1.00 33.65  ? 39   LEU A CA  1 
ATOM   311  C C   . LEU A 1 58  ? -9.392  16.470 -15.607 1.00 42.58  ? 39   LEU A C   1 
ATOM   312  O O   . LEU A 1 58  ? -10.226 15.629 -15.966 1.00 60.81  ? 39   LEU A O   1 
ATOM   313  C CB  . LEU A 1 58  ? -9.853  18.882 -15.743 1.00 34.04  ? 39   LEU A CB  1 
ATOM   314  C CG  . LEU A 1 58  ? -10.690 20.062 -15.256 1.00 33.70  ? 39   LEU A CG  1 
ATOM   315  C CD1 . LEU A 1 58  ? -10.621 21.159 -16.276 1.00 39.59  ? 39   LEU A CD1 1 
ATOM   316  C CD2 . LEU A 1 58  ? -12.132 19.654 -15.024 1.00 38.95  ? 39   LEU A CD2 1 
ATOM   317  N N   . GLU A 1 59  ? -8.113  16.389 -15.926 1.00 31.76  ? 40   GLU A N   1 
ATOM   318  C CA  . GLU A 1 59  ? -7.684  15.285 -16.774 1.00 34.82  ? 40   GLU A CA  1 
ATOM   319  C C   . GLU A 1 59  ? -6.407  14.704 -16.266 1.00 39.04  ? 40   GLU A C   1 
ATOM   320  O O   . GLU A 1 59  ? -5.325  15.270 -16.439 1.00 44.35  ? 40   GLU A O   1 
ATOM   321  C CB  . GLU A 1 59  ? -7.528  15.725 -18.218 1.00 38.04  ? 40   GLU A CB  1 
ATOM   322  C CG  . GLU A 1 59  ? -8.594  15.147 -19.112 1.00 54.22  ? 40   GLU A CG  1 
ATOM   323  C CD  . GLU A 1 59  ? -8.977  16.088 -20.237 1.00 65.72  ? 40   GLU A CD  1 
ATOM   324  O OE1 . GLU A 1 59  ? -8.441  17.222 -20.262 1.00 70.71  ? 40   GLU A OE1 1 
ATOM   325  O OE2 . GLU A 1 59  ? -9.812  15.694 -21.087 1.00 72.26  ? 40   GLU A OE2 1 
ATOM   326  N N   . VAL A 1 60  ? -6.531  13.562 -15.621 1.00 36.00  ? 41   VAL A N   1 
ATOM   327  C CA  . VAL A 1 60  ? -5.366  12.948 -15.041 1.00 32.64  ? 41   VAL A CA  1 
ATOM   328  C C   . VAL A 1 60  ? -4.920  11.804 -15.937 1.00 27.30  ? 41   VAL A C   1 
ATOM   329  O O   . VAL A 1 60  ? -5.738  11.077 -16.488 1.00 30.24  ? 41   VAL A O   1 
ATOM   330  C CB  . VAL A 1 60  ? -5.663  12.498 -13.613 1.00 34.37  ? 41   VAL A CB  1 
ATOM   331  C CG1 . VAL A 1 60  ? -4.516  11.728 -13.067 1.00 34.65  ? 41   VAL A CG1 1 
ATOM   332  C CG2 . VAL A 1 60  ? -5.934  13.712 -12.734 1.00 32.18  ? 41   VAL A CG2 1 
ATOM   333  N N   . ASN A 1 61  ? -3.616  11.692 -16.129 1.00 27.48  ? 42   ASN A N   1 
ATOM   334  C CA  . ASN A 1 61  ? -3.048  10.574 -16.857 1.00 26.36  ? 42   ASN A CA  1 
ATOM   335  C C   . ASN A 1 61  ? -1.880  9.985  -16.073 1.00 30.31  ? 42   ASN A C   1 
ATOM   336  O O   . ASN A 1 61  ? -0.796  10.587 -16.005 1.00 27.39  ? 42   ASN A O   1 
ATOM   337  C CB  . ASN A 1 61  ? -2.608  11.014 -18.255 1.00 26.55  ? 42   ASN A CB  1 
ATOM   338  C CG  . ASN A 1 61  ? -2.197  9.841  -19.147 1.00 34.52  ? 42   ASN A CG  1 
ATOM   339  O OD1 . ASN A 1 61  ? -1.564  8.867  -18.691 1.00 33.09  ? 42   ASN A OD1 1 
ATOM   340  N ND2 . ASN A 1 61  ? -2.566  9.926  -20.430 1.00 31.98  ? 42   ASN A ND2 1 
ATOM   341  N N   . GLU A 1 62  ? -2.115  8.808  -15.480 1.00 35.88  ? 43   GLU A N   1 
ATOM   342  C CA  . GLU A 1 62  ? -1.118  8.150  -14.627 1.00 31.63  ? 43   GLU A CA  1 
ATOM   343  C C   . GLU A 1 62  ? 0.009   7.615  -15.490 1.00 30.69  ? 43   GLU A C   1 
ATOM   344  O O   . GLU A 1 62  ? 1.154   7.538  -15.035 1.00 41.78  ? 43   GLU A O   1 
ATOM   345  C CB  . GLU A 1 62  ? -1.735  7.044  -13.750 1.00 31.91  ? 43   GLU A CB  1 
ATOM   346  C CG  . GLU A 1 62  ? -0.908  6.689  -12.477 1.00 44.14  ? 43   GLU A CG  1 
ATOM   347  C CD  . GLU A 1 62  ? -1.596  5.653  -11.546 1.00 52.25  ? 43   GLU A CD  1 
ATOM   348  O OE1 . GLU A 1 62  ? -2.811  5.370  -11.728 1.00 48.61  ? 43   GLU A OE1 1 
ATOM   349  O OE2 . GLU A 1 62  ? -0.913  5.127  -10.625 1.00 44.38  ? 43   GLU A OE2 1 
ATOM   350  N N   . ILE A 1 63  ? -0.305  7.286  -16.743 1.00 28.00  ? 44   ILE A N   1 
ATOM   351  C CA  . ILE A 1 63  ? 0.708   6.762  -17.662 1.00 32.50  ? 44   ILE A CA  1 
ATOM   352  C C   . ILE A 1 63  ? 1.767   7.803  -18.001 1.00 30.09  ? 44   ILE A C   1 
ATOM   353  O O   . ILE A 1 63  ? 2.965   7.503  -17.979 1.00 38.68  ? 44   ILE A O   1 
ATOM   354  C CB  . ILE A 1 63  ? 0.124   6.235  -19.012 1.00 36.89  ? 44   ILE A CB  1 
ATOM   355  C CG1 . ILE A 1 63  ? -0.973  5.185  -18.798 1.00 28.25  ? 44   ILE A CG1 1 
ATOM   356  C CG2 . ILE A 1 63  ? 1.254   5.695  -19.902 1.00 28.72  ? 44   ILE A CG2 1 
ATOM   357  C CD1 . ILE A 1 63  ? -0.509  3.946  -18.114 1.00 26.81  ? 44   ILE A CD1 1 
ATOM   358  N N   . THR A 1 64  ? 1.325   9.016  -18.327 1.00 33.70  ? 45   THR A N   1 
ATOM   359  C CA  . THR A 1 64  ? 2.237   10.058 -18.815 1.00 31.01  ? 45   THR A CA  1 
ATOM   360  C C   . THR A 1 64  ? 2.612   11.041 -17.725 1.00 30.99  ? 45   THR A C   1 
ATOM   361  O O   . THR A 1 64  ? 3.417   11.938 -17.963 1.00 36.27  ? 45   THR A O   1 
ATOM   362  C CB  . THR A 1 64  ? 1.628   10.872 -19.963 1.00 22.74  ? 45   THR A CB  1 
ATOM   363  O OG1 . THR A 1 64  ? 0.500   11.591 -19.468 1.00 28.02  ? 45   THR A OG1 1 
ATOM   364  C CG2 . THR A 1 64  ? 1.179   9.983  -21.083 1.00 22.74  ? 45   THR A CG2 1 
ATOM   365  N N   . ASN A 1 65  ? 2.013   10.889 -16.546 1.00 28.69  ? 46   ASN A N   1 
ATOM   366  C CA  . ASN A 1 65  ? 2.277   11.797 -15.429 1.00 35.78  ? 46   ASN A CA  1 
ATOM   367  C C   . ASN A 1 65  ? 1.933   13.277 -15.709 1.00 32.37  ? 46   ASN A C   1 
ATOM   368  O O   . ASN A 1 65  ? 2.766   14.172 -15.549 1.00 29.36  ? 46   ASN A O   1 
ATOM   369  C CB  . ASN A 1 65  ? 3.728   11.654 -14.936 1.00 35.01  ? 46   ASN A CB  1 
ATOM   370  C CG  . ASN A 1 65  ? 3.876   10.622 -13.827 1.00 38.40  ? 46   ASN A CG  1 
ATOM   371  O OD1 . ASN A 1 65  ? 2.909   10.280 -13.136 1.00 37.25  ? 46   ASN A OD1 1 
ATOM   372  N ND2 . ASN A 1 65  ? 5.101   10.131 -13.640 1.00 35.44  ? 46   ASN A ND2 1 
ATOM   373  N N   . GLU A 1 66  ? 0.692   13.512 -16.117 1.00 29.97  ? 47   GLU A N   1 
ATOM   374  C CA  . GLU A 1 66  ? 0.213   14.848 -16.436 1.00 31.91  ? 47   GLU A CA  1 
ATOM   375  C C   . GLU A 1 66  ? -1.162  15.130 -15.813 1.00 32.15  ? 47   GLU A C   1 
ATOM   376  O O   . GLU A 1 66  ? -2.046  14.272 -15.821 1.00 28.52  ? 47   GLU A O   1 
ATOM   377  C CB  . GLU A 1 66  ? 0.138   15.019 -17.954 1.00 30.19  ? 47   GLU A CB  1 
ATOM   378  C CG  . GLU A 1 66  ? 1.473   14.859 -18.641 1.00 34.48  ? 47   GLU A CG  1 
ATOM   379  C CD  . GLU A 1 66  ? 1.395   15.028 -20.156 1.00 49.55  ? 47   GLU A CD  1 
ATOM   380  O OE1 . GLU A 1 66  ? 0.343   15.504 -20.658 1.00 51.17  ? 47   GLU A OE1 1 
ATOM   381  O OE2 . GLU A 1 66  ? 2.399   14.681 -20.835 1.00 49.13  ? 47   GLU A OE2 1 
ATOM   382  N N   . VAL A 1 67  ? -1.346  16.338 -15.285 1.00 32.49  ? 48   VAL A N   1 
ATOM   383  C CA  . VAL A 1 67  ? -2.647  16.714 -14.722 1.00 36.08  ? 48   VAL A CA  1 
ATOM   384  C C   . VAL A 1 67  ? -3.128  18.037 -15.283 1.00 26.35  ? 48   VAL A C   1 
ATOM   385  O O   . VAL A 1 67  ? -2.349  18.847 -15.744 1.00 25.83  ? 48   VAL A O   1 
ATOM   386  C CB  . VAL A 1 67  ? -2.633  16.816 -13.167 1.00 31.22  ? 48   VAL A CB  1 
ATOM   387  C CG1 . VAL A 1 67  ? -2.207  15.509 -12.549 1.00 32.56  ? 48   VAL A CG1 1 
ATOM   388  C CG2 . VAL A 1 67  ? -1.694  17.924 -12.723 1.00 28.57  ? 48   VAL A CG2 1 
ATOM   389  N N   . ASP A 1 68  ? -4.429  18.251 -15.212 1.00 32.95  ? 49   ASP A N   1 
ATOM   390  C CA  . ASP A 1 68  ? -5.044  19.482 -15.672 1.00 23.98  ? 49   ASP A CA  1 
ATOM   391  C C   . ASP A 1 68  ? -5.716  20.131 -14.492 1.00 24.99  ? 49   ASP A C   1 
ATOM   392  O O   . ASP A 1 68  ? -6.710  19.623 -13.974 1.00 32.55  ? 49   ASP A O   1 
ATOM   393  C CB  . ASP A 1 68  ? -6.121  19.157 -16.694 1.00 38.26  ? 49   ASP A CB  1 
ATOM   394  C CG  . ASP A 1 68  ? -5.969  19.949 -17.946 1.00 48.22  ? 49   ASP A CG  1 
ATOM   395  O OD1 . ASP A 1 68  ? -4.818  20.386 -18.184 1.00 56.08  ? 49   ASP A OD1 1 
ATOM   396  O OD2 . ASP A 1 68  ? -6.973  20.138 -18.681 1.00 62.81  ? 49   ASP A OD2 1 
ATOM   397  N N   . VAL A 1 69  ? -5.197  21.261 -14.052 1.00 26.02  ? 50   VAL A N   1 
ATOM   398  C CA  . VAL A 1 69  ? -5.756  21.896 -12.868 1.00 21.80  ? 50   VAL A CA  1 
ATOM   399  C C   . VAL A 1 69  ? -6.398  23.250 -13.159 1.00 21.28  ? 50   VAL A C   1 
ATOM   400  O O   . VAL A 1 69  ? -5.925  23.996 -14.014 1.00 25.02  ? 50   VAL A O   1 
ATOM   401  C CB  . VAL A 1 69  ? -4.671  22.051 -11.833 1.00 21.52  ? 50   VAL A CB  1 
ATOM   402  C CG1 . VAL A 1 69  ? -5.239  22.620 -10.538 1.00 17.07  ? 50   VAL A CG1 1 
ATOM   403  C CG2 . VAL A 1 69  ? -4.016  20.707 -11.604 1.00 19.59  ? 50   VAL A CG2 1 
ATOM   404  N N   . VAL A 1 70  ? -7.500  23.539 -12.468 1.00 21.64  ? 51   VAL A N   1 
ATOM   405  C CA  . VAL A 1 70  ? -8.074  24.883 -12.431 1.00 20.00  ? 51   VAL A CA  1 
ATOM   406  C C   . VAL A 1 70  ? -7.954  25.424 -11.010 1.00 20.95  ? 51   VAL A C   1 
ATOM   407  O O   . VAL A 1 70  ? -8.414  24.805 -10.044 1.00 18.47  ? 51   VAL A O   1 
ATOM   408  C CB  . VAL A 1 70  ? -9.545  24.902 -12.836 1.00 20.44  ? 51   VAL A CB  1 
ATOM   409  C CG1 . VAL A 1 70  ? -10.134 26.272 -12.550 1.00 16.49  ? 51   VAL A CG1 1 
ATOM   410  C CG2 . VAL A 1 70  ? -9.707  24.516 -14.305 1.00 21.42  ? 51   VAL A CG2 1 
ATOM   411  N N   . PHE A 1 71  ? -7.325  26.587 -10.891 1.00 22.65  ? 52   PHE A N   1 
ATOM   412  C CA  . PHE A 1 71  ? -7.064  27.191 -9.587  1.00 24.15  ? 52   PHE A CA  1 
ATOM   413  C C   . PHE A 1 71  ? -7.073  28.724 -9.652  1.00 21.69  ? 52   PHE A C   1 
ATOM   414  O O   . PHE A 1 71  ? -6.840  29.306 -10.715 1.00 17.96  ? 52   PHE A O   1 
ATOM   415  C CB  . PHE A 1 71  ? -5.708  26.722 -9.077  1.00 20.14  ? 52   PHE A CB  1 
ATOM   416  C CG  . PHE A 1 71  ? -4.581  27.039 -10.016 1.00 18.91  ? 52   PHE A CG  1 
ATOM   417  C CD1 . PHE A 1 71  ? -4.309  26.219 -11.101 1.00 21.06  ? 52   PHE A CD1 1 
ATOM   418  C CD2 . PHE A 1 71  ? -3.797  28.168 -9.820  1.00 21.46  ? 52   PHE A CD2 1 
ATOM   419  C CE1 . PHE A 1 71  ? -3.256  26.517 -11.978 1.00 26.73  ? 52   PHE A CE1 1 
ATOM   420  C CE2 . PHE A 1 71  ? -2.752  28.477 -10.686 1.00 21.03  ? 52   PHE A CE2 1 
ATOM   421  C CZ  . PHE A 1 71  ? -2.478  27.650 -11.768 1.00 22.79  ? 52   PHE A CZ  1 
ATOM   422  N N   . TRP A 1 72  ? -7.341  29.365 -8.509  1.00 19.22  ? 53   TRP A N   1 
ATOM   423  C CA  . TRP A 1 72  ? -7.173  30.809 -8.382  1.00 20.42  ? 53   TRP A CA  1 
ATOM   424  C C   . TRP A 1 72  ? -5.755  31.043 -7.931  1.00 20.31  ? 53   TRP A C   1 
ATOM   425  O O   . TRP A 1 72  ? -5.291  30.395 -6.994  1.00 20.48  ? 53   TRP A O   1 
ATOM   426  C CB  . TRP A 1 72  ? -8.104  31.421 -7.335  1.00 18.77  ? 53   TRP A CB  1 
ATOM   427  C CG  . TRP A 1 72  ? -9.562  31.279 -7.630  1.00 19.69  ? 53   TRP A CG  1 
ATOM   428  C CD1 . TRP A 1 72  ? -10.135 30.682 -8.728  1.00 21.11  ? 53   TRP A CD1 1 
ATOM   429  C CD2 . TRP A 1 72  ? -10.645 31.754 -6.819  1.00 20.17  ? 53   TRP A CD2 1 
ATOM   430  N NE1 . TRP A 1 72  ? -11.509 30.747 -8.636  1.00 24.70  ? 53   TRP A NE1 1 
ATOM   431  C CE2 . TRP A 1 72  ? -11.850 31.404 -7.477  1.00 20.56  ? 53   TRP A CE2 1 
ATOM   432  C CE3 . TRP A 1 72  ? -10.715 32.449 -5.599  1.00 21.80  ? 53   TRP A CE3 1 
ATOM   433  C CZ2 . TRP A 1 72  ? -13.113 31.714 -6.954  1.00 19.47  ? 53   TRP A CZ2 1 
ATOM   434  C CZ3 . TRP A 1 72  ? -11.978 32.757 -5.071  1.00 27.08  ? 53   TRP A CZ3 1 
ATOM   435  C CH2 . TRP A 1 72  ? -13.161 32.385 -5.752  1.00 22.92  ? 53   TRP A CH2 1 
ATOM   436  N N   . GLN A 1 73  ? -5.062  31.963 -8.594  1.00 19.54  ? 54   GLN A N   1 
ATOM   437  C CA  . GLN A 1 73  ? -3.689  32.283 -8.224  1.00 18.52  ? 54   GLN A CA  1 
ATOM   438  C C   . GLN A 1 73  ? -3.628  33.625 -7.508  1.00 18.06  ? 54   GLN A C   1 
ATOM   439  O O   . GLN A 1 73  ? -3.320  34.652 -8.102  1.00 19.61  ? 54   GLN A O   1 
ATOM   440  C CB  . GLN A 1 73  ? -2.791  32.293 -9.458  1.00 17.31  ? 54   GLN A CB  1 
ATOM   441  C CG  . GLN A 1 73  ? -1.337  32.587 -9.137  1.00 20.61  ? 54   GLN A CG  1 
ATOM   442  C CD  . GLN A 1 73  ? -0.427  32.417 -10.333 1.00 23.32  ? 54   GLN A CD  1 
ATOM   443  O OE1 . GLN A 1 73  ? -0.380  31.357 -10.957 1.00 23.64  ? 54   GLN A OE1 1 
ATOM   444  N NE2 . GLN A 1 73  ? 0.305   33.473 -10.662 1.00 39.20  ? 54   GLN A NE2 1 
ATOM   445  N N   . GLN A 1 74  ? -3.934  33.620 -6.222  1.00 20.45  ? 55   GLN A N   1 
ATOM   446  C CA  . GLN A 1 74  ? -4.034  34.869 -5.475  1.00 22.01  ? 55   GLN A CA  1 
ATOM   447  C C   . GLN A 1 74  ? -2.655  35.474 -5.222  1.00 25.01  ? 55   GLN A C   1 
ATOM   448  O O   . GLN A 1 74  ? -1.832  34.877 -4.530  1.00 26.47  ? 55   GLN A O   1 
ATOM   449  C CB  . GLN A 1 74  ? -4.751  34.637 -4.149  1.00 22.46  ? 55   GLN A CB  1 
ATOM   450  C CG  . GLN A 1 74  ? -4.815  35.872 -3.294  1.00 26.43  ? 55   GLN A CG  1 
ATOM   451  C CD  . GLN A 1 74  ? -5.629  35.665 -2.042  1.00 33.12  ? 55   GLN A CD  1 
ATOM   452  O OE1 . GLN A 1 74  ? -6.615  34.927 -2.047  1.00 56.58  ? 55   GLN A OE1 1 
ATOM   453  N NE2 . GLN A 1 74  ? -5.216  36.305 -0.952  1.00 36.04  ? 55   GLN A NE2 1 
ATOM   454  N N   . THR A 1 75  ? -2.412  36.661 -5.781  1.00 21.42  ? 56   THR A N   1 
ATOM   455  C CA  . THR A 1 75  ? -1.090  37.278 -5.751  1.00 16.55  ? 56   THR A CA  1 
ATOM   456  C C   . THR A 1 75  ? -1.185  38.657 -5.127  1.00 20.00  ? 56   THR A C   1 
ATOM   457  O O   . THR A 1 75  ? -2.033  39.456 -5.526  1.00 22.67  ? 56   THR A O   1 
ATOM   458  C CB  . THR A 1 75  ? -0.533  37.425 -7.164  1.00 18.59  ? 56   THR A CB  1 
ATOM   459  O OG1 . THR A 1 75  ? -0.725  36.197 -7.895  1.00 25.99  ? 56   THR A OG1 1 
ATOM   460  C CG2 . THR A 1 75  ? 0.947   37.763 -7.103  1.00 23.04  ? 56   THR A CG2 1 
ATOM   461  N N   . THR A 1 76  ? -0.317  38.950 -4.158  1.00 18.88  ? 57   THR A N   1 
ATOM   462  C CA  . THR A 1 76  ? -0.423  40.206 -3.394  1.00 20.61  ? 57   THR A CA  1 
ATOM   463  C C   . THR A 1 76  ? 0.926   40.892 -3.161  1.00 19.54  ? 57   THR A C   1 
ATOM   464  O O   . THR A 1 76  ? 1.901   40.244 -2.794  1.00 22.83  ? 57   THR A O   1 
ATOM   465  C CB  . THR A 1 76  ? -1.124  39.968 -2.026  1.00 29.43  ? 57   THR A CB  1 
ATOM   466  O OG1 . THR A 1 76  ? -2.503  39.617 -2.237  1.00 30.29  ? 57   THR A OG1 1 
ATOM   467  C CG2 . THR A 1 76  ? -1.059  41.225 -1.127  1.00 23.55  ? 57   THR A CG2 1 
ATOM   468  N N   . TRP A 1 77  ? 0.981   42.201 -3.383  1.00 16.71  ? 58   TRP A N   1 
ATOM   469  C CA  . TRP A 1 77  ? 2.219   42.950 -3.183  1.00 18.25  ? 58   TRP A CA  1 
ATOM   470  C C   . TRP A 1 77  ? 1.937   44.413 -2.926  1.00 20.73  ? 58   TRP A C   1 
ATOM   471  O O   . TRP A 1 77  ? 0.786   44.864 -2.976  1.00 20.31  ? 58   TRP A O   1 
ATOM   472  C CB  . TRP A 1 77  ? 3.160   42.810 -4.383  1.00 14.88  ? 58   TRP A CB  1 
ATOM   473  C CG  . TRP A 1 77  ? 2.657   43.495 -5.589  1.00 13.51  ? 58   TRP A CG  1 
ATOM   474  C CD1 . TRP A 1 77  ? 2.957   44.757 -5.993  1.00 17.47  ? 58   TRP A CD1 1 
ATOM   475  C CD2 . TRP A 1 77  ? 1.743   42.965 -6.559  1.00 17.20  ? 58   TRP A CD2 1 
ATOM   476  N NE1 . TRP A 1 77  ? 2.288   45.057 -7.157  1.00 17.49  ? 58   TRP A NE1 1 
ATOM   477  C CE2 . TRP A 1 77  ? 1.541   43.980 -7.530  1.00 18.34  ? 58   TRP A CE2 1 
ATOM   478  C CE3 . TRP A 1 77  ? 1.084   41.741 -6.701  1.00 15.76  ? 58   TRP A CE3 1 
ATOM   479  C CZ2 . TRP A 1 77  ? 0.701   43.799 -8.638  1.00 14.12  ? 58   TRP A CZ2 1 
ATOM   480  C CZ3 . TRP A 1 77  ? 0.241   41.569 -7.798  1.00 17.95  ? 58   TRP A CZ3 1 
ATOM   481  C CH2 . TRP A 1 77  ? 0.065   42.598 -8.758  1.00 14.79  ? 58   TRP A CH2 1 
ATOM   482  N N   . SER A 1 78  ? 3.000   45.162 -2.670  1.00 19.00  ? 59   SER A N   1 
ATOM   483  C CA  . SER A 1 78  ? 2.846   46.577 -2.376  1.00 21.01  ? 59   SER A CA  1 
ATOM   484  C C   . SER A 1 78  ? 3.518   47.483 -3.409  1.00 18.51  ? 59   SER A C   1 
ATOM   485  O O   . SER A 1 78  ? 4.654   47.238 -3.799  1.00 22.35  ? 59   SER A O   1 
ATOM   486  C CB  . SER A 1 78  ? 3.369   46.874 -0.978  1.00 22.89  ? 59   SER A CB  1 
ATOM   487  O OG  . SER A 1 78  ? 3.230   48.245 -0.706  1.00 26.92  ? 59   SER A OG  1 
ATOM   488  N N   . ASP A 1 79  ? 2.797   48.513 -3.856  1.00 18.84  ? 60   ASP A N   1 
ATOM   489  C CA  . ASP A 1 79  ? 3.327   49.513 -4.788  1.00 21.44  ? 60   ASP A CA  1 
ATOM   490  C C   . ASP A 1 79  ? 2.927   50.942 -4.379  1.00 29.81  ? 60   ASP A C   1 
ATOM   491  O O   . ASP A 1 79  ? 1.839   51.413 -4.741  1.00 25.53  ? 60   ASP A O   1 
ATOM   492  C CB  . ASP A 1 79  ? 2.831   49.223 -6.205  1.00 23.37  ? 60   ASP A CB  1 
ATOM   493  C CG  . ASP A 1 79  ? 3.621   49.980 -7.288  1.00 31.68  ? 60   ASP A CG  1 
ATOM   494  O OD1 . ASP A 1 79  ? 4.222   51.049 -6.990  1.00 30.05  ? 60   ASP A OD1 1 
ATOM   495  O OD2 . ASP A 1 79  ? 3.644   49.488 -8.449  1.00 26.31  ? 60   ASP A OD2 1 
ATOM   496  N N   . ARG A 1 80  ? 3.814   51.628 -3.647  1.00 31.34  ? 61   ARG A N   1 
ATOM   497  C CA  . ARG A 1 80  ? 3.506   52.951 -3.071  1.00 33.33  ? 61   ARG A CA  1 
ATOM   498  C C   . ARG A 1 80  ? 3.273   54.030 -4.131  1.00 23.63  ? 61   ARG A C   1 
ATOM   499  O O   . ARG A 1 80  ? 2.662   55.053 -3.857  1.00 25.84  ? 61   ARG A O   1 
ATOM   500  C CB  . ARG A 1 80  ? 4.602   53.414 -2.097  1.00 42.85  ? 61   ARG A CB  1 
ATOM   501  C CG  . ARG A 1 80  ? 5.022   52.375 -1.066  1.00 49.21  ? 61   ARG A CG  1 
ATOM   502  C CD  . ARG A 1 80  ? 4.080   52.286 0.137   1.00 59.91  ? 61   ARG A CD  1 
ATOM   503  N NE  . ARG A 1 80  ? 4.662   51.442 1.194   1.00 78.46  ? 61   ARG A NE  1 
ATOM   504  C CZ  . ARG A 1 80  ? 4.076   50.372 1.738   1.00 79.93  ? 61   ARG A CZ  1 
ATOM   505  N NH1 . ARG A 1 80  ? 2.854   49.999 1.352   1.00 74.32  ? 61   ARG A NH1 1 
ATOM   506  N NH2 . ARG A 1 80  ? 4.712   49.674 2.679   1.00 69.43  ? 61   ARG A NH2 1 
ATOM   507  N N   . THR A 1 81  ? 3.779   53.800 -5.334  1.00 24.69  ? 62   THR A N   1 
ATOM   508  C CA  . THR A 1 81  ? 3.518   54.664 -6.492  1.00 25.71  ? 62   THR A CA  1 
ATOM   509  C C   . THR A 1 81  ? 2.013   54.849 -6.764  1.00 21.85  ? 62   THR A C   1 
ATOM   510  O O   . THR A 1 81  ? 1.591   55.844 -7.327  1.00 19.94  ? 62   THR A O   1 
ATOM   511  C CB  . THR A 1 81  ? 4.178   54.041 -7.766  1.00 34.06  ? 62   THR A CB  1 
ATOM   512  O OG1 . THR A 1 81  ? 5.584   53.843 -7.543  1.00 35.49  ? 62   THR A OG1 1 
ATOM   513  C CG2 . THR A 1 81  ? 3.968   54.903 -9.018  1.00 38.10  ? 62   THR A CG2 1 
ATOM   514  N N   . LEU A 1 82  ? 1.204   53.874 -6.368  1.00 24.65  ? 63   LEU A N   1 
ATOM   515  C CA  . LEU A 1 82  ? -0.219  53.926 -6.647  1.00 18.37  ? 63   LEU A CA  1 
ATOM   516  C C   . LEU A 1 82  ? -1.028  54.602 -5.543  1.00 20.45  ? 63   LEU A C   1 
ATOM   517  O O   . LEU A 1 82  ? -2.230  54.813 -5.701  1.00 28.60  ? 63   LEU A O   1 
ATOM   518  C CB  . LEU A 1 82  ? -0.751  52.515 -6.869  1.00 17.62  ? 63   LEU A CB  1 
ATOM   519  C CG  . LEU A 1 82  ? -0.016  51.687 -7.915  1.00 21.33  ? 63   LEU A CG  1 
ATOM   520  C CD1 . LEU A 1 82  ? -0.377  50.212 -7.776  1.00 19.39  ? 63   LEU A CD1 1 
ATOM   521  C CD2 . LEU A 1 82  ? -0.372  52.199 -9.301  1.00 17.27  ? 63   LEU A CD2 1 
ATOM   522  N N   . ALA A 1 83  ? -0.391  54.932 -4.426  1.00 15.68  ? 64   ALA A N   1 
ATOM   523  C CA  . ALA A 1 83  ? -1.139  55.366 -3.250  1.00 18.65  ? 64   ALA A CA  1 
ATOM   524  C C   . ALA A 1 83  ? -1.788  56.742 -3.428  1.00 24.45  ? 64   ALA A C   1 
ATOM   525  O O   . ALA A 1 83  ? -1.321  57.547 -4.229  1.00 25.98  ? 64   ALA A O   1 
ATOM   526  C CB  . ALA A 1 83  ? -0.267  55.348 -2.028  1.00 20.53  ? 64   ALA A CB  1 
ATOM   527  N N   . TRP A 1 84  ? -2.874  56.989 -2.688  1.00 24.38  ? 65   TRP A N   1 
ATOM   528  C CA  . TRP A 1 84  ? -3.545  58.290 -2.663  1.00 21.82  ? 65   TRP A CA  1 
ATOM   529  C C   . TRP A 1 84  ? -4.120  58.599 -1.274  1.00 25.67  ? 65   TRP A C   1 
ATOM   530  O O   . TRP A 1 84  ? -4.247  57.709 -0.439  1.00 23.46  ? 65   TRP A O   1 
ATOM   531  C CB  . TRP A 1 84  ? -4.638  58.363 -3.735  1.00 23.11  ? 65   TRP A CB  1 
ATOM   532  C CG  . TRP A 1 84  ? -5.850  57.477 -3.499  1.00 26.56  ? 65   TRP A CG  1 
ATOM   533  C CD1 . TRP A 1 84  ? -7.006  57.820 -2.844  1.00 28.15  ? 65   TRP A CD1 1 
ATOM   534  C CD2 . TRP A 1 84  ? -6.033  56.113 -3.942  1.00 27.77  ? 65   TRP A CD2 1 
ATOM   535  N NE1 . TRP A 1 84  ? -7.884  56.758 -2.843  1.00 25.04  ? 65   TRP A NE1 1 
ATOM   536  C CE2 . TRP A 1 84  ? -7.314  55.702 -3.506  1.00 22.17  ? 65   TRP A CE2 1 
ATOM   537  C CE3 . TRP A 1 84  ? -5.227  55.195 -4.641  1.00 21.94  ? 65   TRP A CE3 1 
ATOM   538  C CZ2 . TRP A 1 84  ? -7.805  54.418 -3.747  1.00 20.76  ? 65   TRP A CZ2 1 
ATOM   539  C CZ3 . TRP A 1 84  ? -5.717  53.925 -4.880  1.00 16.26  ? 65   TRP A CZ3 1 
ATOM   540  C CH2 . TRP A 1 84  ? -6.998  53.548 -4.441  1.00 19.32  ? 65   TRP A CH2 1 
ATOM   541  N N   . ASN A 1 85  ? -4.468  59.836 -1.026  1.00 35.56  ? 66   ASN A N   1 
ATOM   542  C CA  . ASN A 1 85  ? -5.066  60.200 0.221   1.00 36.34  ? 66   ASN A CA  1 
ATOM   543  C C   . ASN A 1 85  ? -6.545  60.095 0.067   1.00 47.70  ? 66   ASN A C   1 
ATOM   544  O O   . ASN A 1 85  ? -7.113  60.669 -0.827  1.00 51.33  ? 66   ASN A O   1 
ATOM   545  C CB  . ASN A 1 85  ? -4.689  61.615 0.566   1.00 41.89  ? 66   ASN A CB  1 
ATOM   546  C CG  . ASN A 1 85  ? -5.475  62.162 1.721   1.00 63.20  ? 66   ASN A CG  1 
ATOM   547  O OD1 . ASN A 1 85  ? -6.219  61.459 2.378   1.00 52.97  ? 66   ASN A OD1 1 
ATOM   548  N ND2 . ASN A 1 85  ? -5.310  63.442 1.972   1.00 68.09  ? 66   ASN A ND2 1 
ATOM   549  N N   . SER A 1 86  ? -7.167  59.349 0.959   1.00 48.82  ? 67   SER A N   1 
ATOM   550  C CA  . SER A 1 86  ? -8.546  58.960 0.832   1.00 46.41  ? 67   SER A CA  1 
ATOM   551  C C   . SER A 1 86  ? -9.428  59.522 1.927   1.00 54.24  ? 67   SER A C   1 
ATOM   552  O O   . SER A 1 86  ? -10.300 58.854 2.423   1.00 55.92  ? 67   SER A O   1 
ATOM   553  C CB  . SER A 1 86  ? -8.652  57.470 0.801   1.00 44.74  ? 67   SER A CB  1 
ATOM   554  O OG  . SER A 1 86  ? -8.452  56.976 2.074   1.00 61.94  ? 67   SER A OG  1 
ATOM   555  N N   . SER A 1 87  ? -9.177  60.754 2.330   1.00 66.76  ? 68   SER A N   1 
ATOM   556  C CA  . SER A 1 87  ? -9.925  61.341 3.416   1.00 69.96  ? 68   SER A CA  1 
ATOM   557  C C   . SER A 1 87  ? -11.393 61.430 3.094   1.00 66.78  ? 68   SER A C   1 
ATOM   558  O O   . SER A 1 87  ? -12.210 61.024 3.897   1.00 70.38  ? 68   SER A O   1 
ATOM   559  C CB  . SER A 1 87  ? -9.380  62.735 3.719   1.00 66.45  ? 68   SER A CB  1 
ATOM   560  O OG  . SER A 1 87  ? -9.924  63.257 4.905   1.00 55.88  ? 68   SER A OG  1 
ATOM   561  N N   . HIS A 1 88  ? -11.736 61.888 1.912   1.00 57.24  ? 69   HIS A N   1 
ATOM   562  C CA  . HIS A 1 88  ? -13.117 61.876 1.525   1.00 62.93  ? 69   HIS A CA  1 
ATOM   563  C C   . HIS A 1 88  ? -13.128 61.276 0.181   1.00 67.47  ? 69   HIS A C   1 
ATOM   564  O O   . HIS A 1 88  ? -13.449 61.907 -0.801  1.00 69.19  ? 69   HIS A O   1 
ATOM   565  C CB  . HIS A 1 88  ? -13.667 63.282 1.511   1.00 77.83  ? 69   HIS A CB  1 
ATOM   566  C CG  . HIS A 1 88  ? -13.802 63.884 2.870   1.00 86.73  ? 69   HIS A CG  1 
ATOM   567  N ND1 . HIS A 1 88  ? -14.611 63.344 3.840   1.00 76.68  ? 69   HIS A ND1 1 
ATOM   568  C CD2 . HIS A 1 88  ? -13.231 64.976 3.419   1.00 87.79  ? 69   HIS A CD2 1 
ATOM   569  C CE1 . HIS A 1 88  ? -14.531 64.075 4.930   1.00 84.14  ? 69   HIS A CE1 1 
ATOM   570  N NE2 . HIS A 1 88  ? -13.698 65.070 4.702   1.00 89.80  ? 69   HIS A NE2 1 
ATOM   571  N N   . SER A 1 89  ? -12.770 60.013 0.152   1.00 59.32  ? 70   SER A N   1 
ATOM   572  C CA  . SER A 1 89  ? -12.444 59.390 -1.071  1.00 51.48  ? 70   SER A CA  1 
ATOM   573  C C   . SER A 1 89  ? -12.635 57.938 -1.004  1.00 45.99  ? 70   SER A C   1 
ATOM   574  O O   . SER A 1 89  ? -12.659 57.363 0.042   1.00 40.49  ? 70   SER A O   1 
ATOM   575  C CB  . SER A 1 89  ? -11.007 59.685 -1.384  1.00 56.44  ? 70   SER A CB  1 
ATOM   576  O OG  . SER A 1 89  ? -10.804 61.071 -1.381  1.00 60.90  ? 70   SER A OG  1 
ATOM   577  N N   . PRO A 1 90  ? -12.772 57.346 -2.241  1.00 48.47  ? 71   PRO A N   1 
ATOM   578  C CA  . PRO A 1 90  ? -12.816 55.892 -2.220  1.00 37.25  ? 71   PRO A CA  1 
ATOM   579  C C   . PRO A 1 90  ? -11.521 55.354 -1.748  1.00 32.36  ? 71   PRO A C   1 
ATOM   580  O O   . PRO A 1 90  ? -10.530 55.959 -1.970  1.00 36.37  ? 71   PRO A O   1 
ATOM   581  C CB  . PRO A 1 90  ? -12.972 55.540 -3.673  1.00 38.96  ? 71   PRO A CB  1 
ATOM   582  C CG  . PRO A 1 90  ? -13.746 56.645 -4.225  1.00 43.82  ? 71   PRO A CG  1 
ATOM   583  C CD  . PRO A 1 90  ? -12.995 57.777 -3.686  1.00 40.38  ? 71   PRO A CD  1 
ATOM   584  N N   . ASP A 1 91  ? -11.548 54.235 -1.067  1.00 33.70  ? 72   ASP A N   1 
ATOM   585  C CA  . ASP A 1 91  ? -10.332 53.611 -0.545  1.00 36.82  ? 72   ASP A CA  1 
ATOM   586  C C   . ASP A 1 91  ? -9.856  52.428 -1.416  1.00 30.76  ? 72   ASP A C   1 
ATOM   587  O O   . ASP A 1 91  ? -8.862  51.773 -1.101  1.00 30.90  ? 72   ASP A O   1 
ATOM   588  C CB  . ASP A 1 91  ? -10.556 53.162 0.902   1.00 39.48  ? 72   ASP A CB  1 
ATOM   589  C CG  . ASP A 1 91  ? -11.891 52.443 1.086   1.00 52.85  ? 72   ASP A CG  1 
ATOM   590  O OD1 . ASP A 1 91  ? -12.687 52.427 0.109   1.00 52.30  ? 72   ASP A OD1 1 
ATOM   591  O OD2 . ASP A 1 91  ? -12.155 51.912 2.203   1.00 54.50  ? 72   ASP A OD2 1 
ATOM   592  N N   . GLN A 1 92  ? -10.556 52.183 -2.522  1.00 25.06  ? 73   GLN A N   1 
ATOM   593  C CA  . GLN A 1 92  ? -10.204 51.109 -3.442  1.00 23.08  ? 73   GLN A CA  1 
ATOM   594  C C   . GLN A 1 92  ? -10.741 51.346 -4.869  1.00 22.76  ? 73   GLN A C   1 
ATOM   595  O O   . GLN A 1 92  ? -11.748 52.025 -5.061  1.00 25.25  ? 73   GLN A O   1 
ATOM   596  C CB  . GLN A 1 92  ? -10.778 49.812 -2.912  1.00 30.62  ? 73   GLN A CB  1 
ATOM   597  C CG  . GLN A 1 92  ? -12.278 49.909 -2.756  1.00 36.46  ? 73   GLN A CG  1 
ATOM   598  C CD  . GLN A 1 92  ? -12.911 48.577 -2.537  1.00 46.96  ? 73   GLN A CD  1 
ATOM   599  O OE1 . GLN A 1 92  ? -12.362 47.724 -1.839  1.00 50.60  ? 73   GLN A OE1 1 
ATOM   600  N NE2 . GLN A 1 92  ? -14.074 48.373 -3.142  1.00 55.59  ? 73   GLN A NE2 1 
ATOM   601  N N   . VAL A 1 93  ? -10.067 50.771 -5.861  1.00 18.68  ? 74   VAL A N   1 
ATOM   602  C CA  . VAL A 1 93  ? -10.497 50.830 -7.257  1.00 15.07  ? 74   VAL A CA  1 
ATOM   603  C C   . VAL A 1 93  ? -10.035 49.564 -7.957  1.00 15.84  ? 74   VAL A C   1 
ATOM   604  O O   . VAL A 1 93  ? -9.148  48.862 -7.461  1.00 16.50  ? 74   VAL A O   1 
ATOM   605  C CB  . VAL A 1 93  ? -9.916  52.055 -8.031  1.00 15.69  ? 74   VAL A CB  1 
ATOM   606  C CG1 . VAL A 1 93  ? -10.481 53.365 -7.504  1.00 18.54  ? 74   VAL A CG1 1 
ATOM   607  C CG2 . VAL A 1 93  ? -8.413  52.073 -7.941  1.00 15.41  ? 74   VAL A CG2 1 
ATOM   608  N N   . SER A 1 94  ? -10.634 49.269 -9.109  1.00 16.21  ? 75   SER A N   1 
ATOM   609  C CA  . SER A 1 94  ? -10.209 48.131 -9.918  1.00 13.68  ? 75   SER A CA  1 
ATOM   610  C C   . SER A 1 94  ? -9.470  48.655 -11.134 1.00 14.33  ? 75   SER A C   1 
ATOM   611  O O   . SER A 1 94  ? -9.943  49.562 -11.820 1.00 16.64  ? 75   SER A O   1 
ATOM   612  C CB  . SER A 1 94  ? -11.398 47.268 -10.339 1.00 17.49  ? 75   SER A CB  1 
ATOM   613  O OG  . SER A 1 94  ? -11.799 46.419 -9.277  1.00 22.27  ? 75   SER A OG  1 
ATOM   614  N N   . VAL A 1 95  ? -8.300  48.089 -11.395 1.00 11.11  ? 76   VAL A N   1 
ATOM   615  C CA  . VAL A 1 95  ? -7.419  48.612 -12.428 1.00 15.03  ? 76   VAL A CA  1 
ATOM   616  C C   . VAL A 1 95  ? -7.045  47.513 -13.421 1.00 17.93  ? 76   VAL A C   1 
ATOM   617  O O   . VAL A 1 95  ? -6.652  46.417 -13.009 1.00 18.77  ? 76   VAL A O   1 
ATOM   618  C CB  . VAL A 1 95  ? -6.118  49.150 -11.787 1.00 16.43  ? 76   VAL A CB  1 
ATOM   619  C CG1 . VAL A 1 95  ? -5.170  49.686 -12.848 1.00 18.27  ? 76   VAL A CG1 1 
ATOM   620  C CG2 . VAL A 1 95  ? -6.424  50.204 -10.763 1.00 16.53  ? 76   VAL A CG2 1 
ATOM   621  N N   . PRO A 1 96  ? -7.136  47.799 -14.733 1.00 16.36  ? 77   PRO A N   1 
ATOM   622  C CA  . PRO A 1 96  ? -6.675  46.805 -15.721 1.00 13.18  ? 77   PRO A CA  1 
ATOM   623  C C   . PRO A 1 96  ? -5.192  46.552 -15.526 1.00 18.27  ? 77   PRO A C   1 
ATOM   624  O O   . PRO A 1 96  ? -4.446  47.530 -15.386 1.00 23.62  ? 77   PRO A O   1 
ATOM   625  C CB  . PRO A 1 96  ? -6.893  47.503 -17.056 1.00 14.46  ? 77   PRO A CB  1 
ATOM   626  C CG  . PRO A 1 96  ? -7.934  48.587 -16.763 1.00 18.93  ? 77   PRO A CG  1 
ATOM   627  C CD  . PRO A 1 96  ? -7.620  49.040 -15.365 1.00 17.63  ? 77   PRO A CD  1 
ATOM   628  N N   . ILE A 1 97  ? -4.766  45.288 -15.482 1.00 20.35  ? 78   ILE A N   1 
ATOM   629  C CA  . ILE A 1 97  ? -3.374  44.967 -15.146 1.00 15.81  ? 78   ILE A CA  1 
ATOM   630  C C   . ILE A 1 97  ? -2.398  45.539 -16.166 1.00 19.59  ? 78   ILE A C   1 
ATOM   631  O O   . ILE A 1 97  ? -1.216  45.708 -15.879 1.00 25.44  ? 78   ILE A O   1 
ATOM   632  C CB  . ILE A 1 97  ? -3.112  43.452 -14.984 1.00 13.86  ? 78   ILE A CB  1 
ATOM   633  C CG1 . ILE A 1 97  ? -3.443  42.692 -16.268 1.00 14.43  ? 78   ILE A CG1 1 
ATOM   634  C CG2 . ILE A 1 97  ? -3.874  42.897 -13.803 1.00 15.00  ? 78   ILE A CG2 1 
ATOM   635  C CD1 . ILE A 1 97  ? -3.014  41.266 -16.239 1.00 11.45  ? 78   ILE A CD1 1 
ATOM   636  N N   . SER A 1 98  ? -2.881  45.836 -17.364 1.00 16.43  ? 79   SER A N   1 
ATOM   637  C CA  . SER A 1 98  ? -2.013  46.471 -18.348 1.00 20.55  ? 79   SER A CA  1 
ATOM   638  C C   . SER A 1 98  ? -1.476  47.856 -17.869 1.00 21.29  ? 79   SER A C   1 
ATOM   639  O O   . SER A 1 98  ? -0.474  48.351 -18.379 1.00 22.11  ? 79   SER A O   1 
ATOM   640  C CB  . SER A 1 98  ? -2.721  46.549 -19.701 1.00 19.79  ? 79   SER A CB  1 
ATOM   641  O OG  . SER A 1 98  ? -3.796  47.469 -19.655 1.00 31.98  ? 79   SER A OG  1 
ATOM   642  N N   . SER A 1 99  ? -2.124  48.455 -16.873 1.00 18.87  ? 80   SER A N   1 
ATOM   643  C CA  . SER A 1 99  ? -1.691  49.742 -16.344 1.00 20.26  ? 80   SER A CA  1 
ATOM   644  C C   . SER A 1 99  ? -0.884  49.663 -15.046 1.00 26.85  ? 80   SER A C   1 
ATOM   645  O O   . SER A 1 99  ? -0.720  50.674 -14.376 1.00 29.45  ? 80   SER A O   1 
ATOM   646  C CB  . SER A 1 99  ? -2.904  50.641 -16.086 1.00 21.40  ? 80   SER A CB  1 
ATOM   647  O OG  . SER A 1 99  ? -3.787  50.643 -17.194 1.00 31.61  ? 80   SER A OG  1 
ATOM   648  N N   . LEU A 1 100 ? -0.397  48.479 -14.681 1.00 24.14  ? 81   LEU A N   1 
ATOM   649  C CA  . LEU A 1 100 ? 0.294   48.280 -13.401 1.00 21.27  ? 81   LEU A CA  1 
ATOM   650  C C   . LEU A 1 100 ? 1.533   47.454 -13.599 1.00 23.01  ? 81   LEU A C   1 
ATOM   651  O O   . LEU A 1 100 ? 1.570   46.595 -14.490 1.00 24.62  ? 81   LEU A O   1 
ATOM   652  C CB  . LEU A 1 100 ? -0.583  47.456 -12.454 1.00 23.36  ? 81   LEU A CB  1 
ATOM   653  C CG  . LEU A 1 100 ? -1.863  48.072 -11.944 1.00 24.35  ? 81   LEU A CG  1 
ATOM   654  C CD1 . LEU A 1 100 ? -2.494  47.132 -10.980 1.00 18.46  ? 81   LEU A CD1 1 
ATOM   655  C CD2 . LEU A 1 100 ? -1.483  49.347 -11.249 1.00 30.69  ? 81   LEU A CD2 1 
ATOM   656  N N   . TRP A 1 101 ? 2.528   47.641 -12.739 1.00 18.17  ? 82   TRP A N   1 
ATOM   657  C CA  . TRP A 1 101 ? 3.573   46.631 -12.667 1.00 17.96  ? 82   TRP A CA  1 
ATOM   658  C C   . TRP A 1 101 ? 2.989   45.356 -12.051 1.00 18.68  ? 82   TRP A C   1 
ATOM   659  O O   . TRP A 1 101 ? 2.193   45.414 -11.120 1.00 22.37  ? 82   TRP A O   1 
ATOM   660  C CB  . TRP A 1 101 ? 4.778   47.103 -11.865 1.00 17.74  ? 82   TRP A CB  1 
ATOM   661  C CG  . TRP A 1 101 ? 5.812   46.037 -11.734 1.00 19.24  ? 82   TRP A CG  1 
ATOM   662  C CD1 . TRP A 1 101 ? 6.838   45.772 -12.601 1.00 20.13  ? 82   TRP A CD1 1 
ATOM   663  C CD2 . TRP A 1 101 ? 5.909   45.066 -10.685 1.00 20.41  ? 82   TRP A CD2 1 
ATOM   664  N NE1 . TRP A 1 101 ? 7.575   44.704 -12.147 1.00 20.25  ? 82   TRP A NE1 1 
ATOM   665  C CE2 . TRP A 1 101 ? 7.025   44.249 -10.977 1.00 20.50  ? 82   TRP A CE2 1 
ATOM   666  C CE3 . TRP A 1 101 ? 5.152   44.802 -9.532  1.00 17.91  ? 82   TRP A CE3 1 
ATOM   667  C CZ2 . TRP A 1 101 ? 7.410   43.185 -10.152 1.00 19.21  ? 82   TRP A CZ2 1 
ATOM   668  C CZ3 . TRP A 1 101 ? 5.535   43.748 -8.704  1.00 15.69  ? 82   TRP A CZ3 1 
ATOM   669  C CH2 . TRP A 1 101 ? 6.660   42.953 -9.021  1.00 17.95  ? 82   TRP A CH2 1 
ATOM   670  N N   . VAL A 1 102 ? 3.398   44.210 -12.574 1.00 19.37  ? 83   VAL A N   1 
ATOM   671  C CA  . VAL A 1 102 ? 2.920   42.914 -12.119 1.00 19.16  ? 83   VAL A CA  1 
ATOM   672  C C   . VAL A 1 102 ? 4.118   41.970 -12.051 1.00 19.18  ? 83   VAL A C   1 
ATOM   673  O O   . VAL A 1 102 ? 4.961   41.979 -12.945 1.00 20.97  ? 83   VAL A O   1 
ATOM   674  C CB  . VAL A 1 102 ? 1.860   42.350 -13.101 1.00 21.45  ? 83   VAL A CB  1 
ATOM   675  C CG1 . VAL A 1 102 ? 1.803   40.841 -13.038 1.00 26.35  ? 83   VAL A CG1 1 
ATOM   676  C CG2 . VAL A 1 102 ? 0.484   42.947 -12.819 1.00 20.30  ? 83   VAL A CG2 1 
ATOM   677  N N   . PRO A 1 103 ? 4.197   41.146 -10.989 1.00 18.65  ? 84   PRO A N   1 
ATOM   678  C CA  . PRO A 1 103 ? 5.344   40.230 -10.873 1.00 15.11  ? 84   PRO A CA  1 
ATOM   679  C C   . PRO A 1 103 ? 5.343   39.179 -11.980 1.00 13.93  ? 84   PRO A C   1 
ATOM   680  O O   . PRO A 1 103 ? 4.267   38.709 -12.339 1.00 11.66  ? 84   PRO A O   1 
ATOM   681  C CB  . PRO A 1 103 ? 5.141   39.585 -9.491  1.00 14.58  ? 84   PRO A CB  1 
ATOM   682  C CG  . PRO A 1 103 ? 3.685   39.777 -9.174  1.00 14.87  ? 84   PRO A CG  1 
ATOM   683  C CD  . PRO A 1 103 ? 3.258   41.047 -9.848  1.00 14.44  ? 84   PRO A CD  1 
ATOM   684  N N   . ASP A 1 104 ? 6.524   38.840 -12.506 1.00 18.63  ? 85   ASP A N   1 
ATOM   685  C CA  . ASP A 1 104 ? 6.682   37.862 -13.605 1.00 14.13  ? 85   ASP A CA  1 
ATOM   686  C C   . ASP A 1 104 ? 6.749   36.410 -13.137 1.00 16.70  ? 85   ASP A C   1 
ATOM   687  O O   . ASP A 1 104 ? 7.714   35.694 -13.423 1.00 20.19  ? 85   ASP A O   1 
ATOM   688  C CB  . ASP A 1 104 ? 7.928   38.177 -14.463 1.00 16.31  ? 85   ASP A CB  1 
ATOM   689  C CG  . ASP A 1 104 ? 9.257   38.130 -13.665 1.00 21.71  ? 85   ASP A CG  1 
ATOM   690  O OD1 . ASP A 1 104 ? 9.260   38.410 -12.438 1.00 23.56  ? 85   ASP A OD1 1 
ATOM   691  O OD2 . ASP A 1 104 ? 10.309  37.822 -14.277 1.00 19.36  ? 85   ASP A OD2 1 
ATOM   692  N N   . LEU A 1 105 ? 5.716   35.966 -12.431 1.00 17.23  ? 86   LEU A N   1 
ATOM   693  C CA  . LEU A 1 105 ? 5.664   34.597 -11.932 1.00 16.34  ? 86   LEU A CA  1 
ATOM   694  C C   . LEU A 1 105 ? 5.402   33.593 -13.070 1.00 21.21  ? 86   LEU A C   1 
ATOM   695  O O   . LEU A 1 105 ? 4.705   33.907 -14.041 1.00 21.70  ? 86   LEU A O   1 
ATOM   696  C CB  . LEU A 1 105 ? 4.590   34.482 -10.850 1.00 16.88  ? 86   LEU A CB  1 
ATOM   697  C CG  . LEU A 1 105 ? 4.775   35.501 -9.714  1.00 14.95  ? 86   LEU A CG  1 
ATOM   698  C CD1 . LEU A 1 105 ? 3.605   35.452 -8.746  1.00 12.56  ? 86   LEU A CD1 1 
ATOM   699  C CD2 . LEU A 1 105 ? 6.102   35.272 -8.983  1.00 15.67  ? 86   LEU A CD2 1 
ATOM   700  N N   . ALA A 1 106 ? 5.987   32.398 -12.954 1.00 24.29  ? 87   ALA A N   1 
ATOM   701  C CA  . ALA A 1 106 ? 5.779   31.306 -13.910 1.00 15.09  ? 87   ALA A CA  1 
ATOM   702  C C   . ALA A 1 106 ? 5.819   30.004 -13.154 1.00 19.47  ? 87   ALA A C   1 
ATOM   703  O O   . ALA A 1 106 ? 6.500   29.904 -12.124 1.00 23.29  ? 87   ALA A O   1 
ATOM   704  C CB  . ALA A 1 106 ? 6.850   31.310 -14.967 1.00 14.95  ? 87   ALA A CB  1 
ATOM   705  N N   . ALA A 1 107 ? 5.091   29.010 -13.663 1.00 19.59  ? 88   ALA A N   1 
ATOM   706  C CA  . ALA A 1 107 ? 5.099   27.655 -13.098 1.00 18.44  ? 88   ALA A CA  1 
ATOM   707  C C   . ALA A 1 107 ? 6.167   26.831 -13.817 1.00 18.39  ? 88   ALA A C   1 
ATOM   708  O O   . ALA A 1 107 ? 6.057   26.566 -15.021 1.00 17.77  ? 88   ALA A O   1 
ATOM   709  C CB  . ALA A 1 107 ? 3.716   27.003 -13.217 1.00 15.45  ? 88   ALA A CB  1 
ATOM   710  N N   . TYR A 1 108 ? 7.204   26.447 -13.075 1.00 18.70  ? 89   TYR A N   1 
ATOM   711  C CA  . TYR A 1 108 ? 8.373   25.772 -13.651 1.00 18.52  ? 89   TYR A CA  1 
ATOM   712  C C   . TYR A 1 108 ? 8.064   24.423 -14.302 1.00 20.35  ? 89   TYR A C   1 
ATOM   713  O O   . TYR A 1 108 ? 8.735   24.023 -15.251 1.00 26.88  ? 89   TYR A O   1 
ATOM   714  C CB  . TYR A 1 108 ? 9.465   25.597 -12.592 1.00 23.59  ? 89   TYR A CB  1 
ATOM   715  C CG  . TYR A 1 108 ? 10.290  26.839 -12.354 1.00 26.97  ? 89   TYR A CG  1 
ATOM   716  C CD1 . TYR A 1 108 ? 9.756   27.939 -11.703 1.00 29.97  ? 89   TYR A CD1 1 
ATOM   717  C CD2 . TYR A 1 108 ? 11.603  26.909 -12.786 1.00 27.65  ? 89   TYR A CD2 1 
ATOM   718  C CE1 . TYR A 1 108 ? 10.518  29.087 -11.492 1.00 36.65  ? 89   TYR A CE1 1 
ATOM   719  C CE2 . TYR A 1 108 ? 12.374  28.038 -12.580 1.00 34.57  ? 89   TYR A CE2 1 
ATOM   720  C CZ  . TYR A 1 108 ? 11.831  29.128 -11.933 1.00 37.03  ? 89   TYR A CZ  1 
ATOM   721  O OH  . TYR A 1 108 ? 12.603  30.254 -11.729 1.00 33.02  ? 89   TYR A OH  1 
ATOM   722  N N   . ASN A 1 109 ? 7.059   23.716 -13.797 1.00 17.58  ? 90   ASN A N   1 
ATOM   723  C CA  . ASN A 1 109 ? 6.715   22.407 -14.347 1.00 14.40  ? 90   ASN A CA  1 
ATOM   724  C C   . ASN A 1 109 ? 5.390   22.417 -15.134 1.00 20.41  ? 90   ASN A C   1 
ATOM   725  O O   . ASN A 1 109 ? 4.718   21.390 -15.294 1.00 20.47  ? 90   ASN A O   1 
ATOM   726  C CB  . ASN A 1 109 ? 6.730   21.319 -13.257 1.00 13.42  ? 90   ASN A CB  1 
ATOM   727  C CG  . ASN A 1 109 ? 5.760   21.599 -12.116 1.00 20.33  ? 90   ASN A CG  1 
ATOM   728  O OD1 . ASN A 1 109 ? 5.722   22.696 -11.550 1.00 23.09  ? 90   ASN A OD1 1 
ATOM   729  N ND2 . ASN A 1 109 ? 4.953   20.603 -11.785 1.00 26.63  ? 90   ASN A ND2 1 
ATOM   730  N N   . ALA A 1 110 ? 5.013   23.596 -15.616 1.00 22.16  ? 91   ALA A N   1 
ATOM   731  C CA  . ALA A 1 110 ? 3.856   23.728 -16.493 1.00 22.22  ? 91   ALA A CA  1 
ATOM   732  C C   . ALA A 1 110 ? 4.248   23.233 -17.896 1.00 20.76  ? 91   ALA A C   1 
ATOM   733  O O   . ALA A 1 110 ? 5.386   23.412 -18.340 1.00 17.03  ? 91   ALA A O   1 
ATOM   734  C CB  . ALA A 1 110 ? 3.377   25.182 -16.523 1.00 17.84  ? 91   ALA A CB  1 
ATOM   735  N N   . ILE A 1 111 ? 3.322   22.579 -18.583 1.00 22.43  ? 92   ILE A N   1 
ATOM   736  C CA  . ILE A 1 111 ? 3.608   22.126 -19.942 1.00 28.12  ? 92   ILE A CA  1 
ATOM   737  C C   . ILE A 1 111 ? 2.660   22.753 -20.973 1.00 25.57  ? 92   ILE A C   1 
ATOM   738  O O   . ILE A 1 111 ? 2.599   22.316 -22.121 1.00 24.43  ? 92   ILE A O   1 
ATOM   739  C CB  . ILE A 1 111 ? 3.599   20.589 -20.049 1.00 26.67  ? 92   ILE A CB  1 
ATOM   740  C CG1 . ILE A 1 111 ? 2.291   20.019 -19.488 1.00 25.52  ? 92   ILE A CG1 1 
ATOM   741  C CG2 . ILE A 1 111 ? 4.800   19.994 -19.335 1.00 20.93  ? 92   ILE A CG2 1 
ATOM   742  C CD1 . ILE A 1 111 ? 2.180   18.516 -19.655 1.00 33.32  ? 92   ILE A CD1 1 
ATOM   743  N N   . SER A 1 112 ? 1.926   23.774 -20.538 1.00 20.82  ? 93   SER A N   1 
ATOM   744  C CA  . SER A 1 112 ? 1.059   24.555 -21.414 1.00 25.19  ? 93   SER A CA  1 
ATOM   745  C C   . SER A 1 112 ? 1.047   25.966 -20.849 1.00 25.51  ? 93   SER A C   1 
ATOM   746  O O   . SER A 1 112 ? 1.335   26.159 -19.666 1.00 24.10  ? 93   SER A O   1 
ATOM   747  C CB  . SER A 1 112 ? -0.350  23.974 -21.423 1.00 22.27  ? 93   SER A CB  1 
ATOM   748  O OG  . SER A 1 112 ? -0.976  24.159 -20.164 1.00 23.09  ? 93   SER A OG  1 
ATOM   749  N N   . LYS A 1 113 ? 0.714   26.960 -21.660 1.00 24.55  ? 94   LYS A N   1 
ATOM   750  C CA  . LYS A 1 113 ? 0.674   28.318 -21.106 1.00 26.41  ? 94   LYS A CA  1 
ATOM   751  C C   . LYS A 1 113 ? -0.590  28.538 -20.294 1.00 23.67  ? 94   LYS A C   1 
ATOM   752  O O   . LYS A 1 113 ? -1.606  27.882 -20.536 1.00 26.06  ? 94   LYS A O   1 
ATOM   753  C CB  . LYS A 1 113 ? 0.845   29.396 -22.190 1.00 32.40  ? 94   LYS A CB  1 
ATOM   754  C CG  . LYS A 1 113 ? -0.225  29.438 -23.255 1.00 39.38  ? 94   LYS A CG  1 
ATOM   755  C CD  . LYS A 1 113 ? 0.233   30.345 -24.411 1.00 47.18  ? 94   LYS A CD  1 
ATOM   756  C CE  . LYS A 1 113 ? 0.701   31.713 -23.896 1.00 50.27  ? 94   LYS A CE  1 
ATOM   757  N NZ  . LYS A 1 113 ? 0.818   32.748 -24.973 1.00 44.43  ? 94   LYS A NZ  1 
ATOM   758  N N   . PRO A 1 114 ? -0.536  29.456 -19.316 1.00 24.85  ? 95   PRO A N   1 
ATOM   759  C CA  . PRO A 1 114 ? -1.729  29.646 -18.479 1.00 20.13  ? 95   PRO A CA  1 
ATOM   760  C C   . PRO A 1 114 ? -2.894  30.119 -19.333 1.00 23.48  ? 95   PRO A C   1 
ATOM   761  O O   . PRO A 1 114 ? -2.697  31.015 -20.154 1.00 32.43  ? 95   PRO A O   1 
ATOM   762  C CB  . PRO A 1 114 ? -1.319  30.777 -17.538 1.00 18.71  ? 95   PRO A CB  1 
ATOM   763  C CG  . PRO A 1 114 ? 0.173   30.855 -17.632 1.00 20.92  ? 95   PRO A CG  1 
ATOM   764  C CD  . PRO A 1 114 ? 0.538   30.415 -18.993 1.00 17.13  ? 95   PRO A CD  1 
ATOM   765  N N   . GLU A 1 115 ? -4.070  29.524 -19.158 1.00 21.40  ? 96   GLU A N   1 
ATOM   766  C CA  . GLU A 1 115 ? -5.288  30.002 -19.808 1.00 21.00  ? 96   GLU A CA  1 
ATOM   767  C C   . GLU A 1 115 ? -6.079  30.788 -18.777 1.00 24.56  ? 96   GLU A C   1 
ATOM   768  O O   . GLU A 1 115 ? -6.626  30.192 -17.832 1.00 21.23  ? 96   GLU A O   1 
ATOM   769  C CB  . GLU A 1 115 ? -6.125  28.831 -20.288 1.00 22.82  ? 96   GLU A CB  1 
ATOM   770  C CG  . GLU A 1 115 ? -7.351  29.181 -21.098 1.00 21.79  ? 96   GLU A CG  1 
ATOM   771  C CD  . GLU A 1 115 ? -8.077  27.916 -21.574 1.00 58.35  ? 96   GLU A CD  1 
ATOM   772  O OE1 . GLU A 1 115 ? -7.444  26.821 -21.537 1.00 63.14  ? 96   GLU A OE1 1 
ATOM   773  O OE2 . GLU A 1 115 ? -9.278  28.010 -21.967 1.00 66.51  ? 96   GLU A OE2 1 
ATOM   774  N N   . VAL A 1 116 ? -6.132  32.117 -18.942 1.00 22.65  ? 97   VAL A N   1 
ATOM   775  C CA  . VAL A 1 116 ? -6.791  32.989 -17.959 1.00 18.33  ? 97   VAL A CA  1 
ATOM   776  C C   . VAL A 1 116 ? -8.303  33.074 -18.170 1.00 16.97  ? 97   VAL A C   1 
ATOM   777  O O   . VAL A 1 116 ? -8.772  33.569 -19.183 1.00 25.71  ? 97   VAL A O   1 
ATOM   778  C CB  . VAL A 1 116 ? -6.173  34.394 -17.949 1.00 17.01  ? 97   VAL A CB  1 
ATOM   779  C CG1 . VAL A 1 116 ? -6.800  35.242 -16.858 1.00 14.31  ? 97   VAL A CG1 1 
ATOM   780  C CG2 . VAL A 1 116 ? -4.690  34.289 -17.752 1.00 18.26  ? 97   VAL A CG2 1 
ATOM   781  N N   . LEU A 1 117 ? -9.061  32.591 -17.198 1.00 17.12  ? 98   LEU A N   1 
ATOM   782  C CA  . LEU A 1 117 ? -10.502 32.435 -17.355 1.00 19.06  ? 98   LEU A CA  1 
ATOM   783  C C   . LEU A 1 117 ? -11.302 33.697 -17.010 1.00 21.90  ? 98   LEU A C   1 
ATOM   784  O O   . LEU A 1 117 ? -12.434 33.877 -17.467 1.00 29.07  ? 98   LEU A O   1 
ATOM   785  C CB  . LEU A 1 117 ? -10.995 31.238 -16.522 1.00 20.56  ? 98   LEU A CB  1 
ATOM   786  C CG  . LEU A 1 117 ? -10.408 29.852 -16.863 1.00 22.74  ? 98   LEU A CG  1 
ATOM   787  C CD1 . LEU A 1 117 ? -10.984 28.774 -15.961 1.00 21.54  ? 98   LEU A CD1 1 
ATOM   788  C CD2 . LEU A 1 117 ? -10.590 29.444 -18.322 1.00 15.76  ? 98   LEU A CD2 1 
ATOM   789  N N   . THR A 1 118 ? -10.700 34.584 -16.233 1.00 18.04  ? 99   THR A N   1 
ATOM   790  C CA  . THR A 1 118 ? -11.431 35.707 -15.675 1.00 19.71  ? 99   THR A CA  1 
ATOM   791  C C   . THR A 1 118 ? -10.975 37.019 -16.264 1.00 17.01  ? 99   THR A C   1 
ATOM   792  O O   . THR A 1 118 ? -9.930  37.052 -16.910 1.00 19.00  ? 99   THR A O   1 
ATOM   793  C CB  . THR A 1 118 ? -11.243 35.730 -14.161 1.00 22.21  ? 99   THR A CB  1 
ATOM   794  O OG1 . THR A 1 118 ? -9.846  35.601 -13.865 1.00 16.05  ? 99   THR A OG1 1 
ATOM   795  C CG2 . THR A 1 118 ? -12.034 34.565 -13.515 1.00 21.62  ? 99   THR A CG2 1 
ATOM   796  N N   . PRO A 1 119 ? -11.760 38.101 -16.054 1.00 18.53  ? 100  PRO A N   1 
ATOM   797  C CA  . PRO A 1 119 ? -11.359 39.473 -16.421 1.00 18.07  ? 100  PRO A CA  1 
ATOM   798  C C   . PRO A 1 119 ? -10.007 39.839 -15.802 1.00 24.69  ? 100  PRO A C   1 
ATOM   799  O O   . PRO A 1 119 ? -9.761  39.513 -14.629 1.00 26.68  ? 100  PRO A O   1 
ATOM   800  C CB  . PRO A 1 119 ? -12.441 40.336 -15.777 1.00 17.12  ? 100  PRO A CB  1 
ATOM   801  C CG  . PRO A 1 119 ? -13.652 39.475 -15.775 1.00 19.79  ? 100  PRO A CG  1 
ATOM   802  C CD  . PRO A 1 119 ? -13.163 38.046 -15.597 1.00 19.48  ? 100  PRO A CD  1 
ATOM   803  N N   . GLN A 1 120 ? -9.148  40.515 -16.561 1.00 21.34  ? 101  GLN A N   1 
ATOM   804  C CA  . GLN A 1 120 ? -7.808  40.801 -16.070 1.00 16.60  ? 101  GLN A CA  1 
ATOM   805  C C   . GLN A 1 120 ? -7.694  42.128 -15.316 1.00 15.93  ? 101  GLN A C   1 
ATOM   806  O O   . GLN A 1 120 ? -7.023  43.060 -15.765 1.00 19.31  ? 101  GLN A O   1 
ATOM   807  C CB  . GLN A 1 120 ? -6.795  40.657 -17.203 1.00 15.12  ? 101  GLN A CB  1 
ATOM   808  C CG  . GLN A 1 120 ? -6.653  39.201 -17.630 1.00 17.65  ? 101  GLN A CG  1 
ATOM   809  C CD  . GLN A 1 120 ? -5.723  38.975 -18.821 1.00 22.15  ? 101  GLN A CD  1 
ATOM   810  O OE1 . GLN A 1 120 ? -4.693  39.633 -18.961 1.00 42.37  ? 101  GLN A OE1 1 
ATOM   811  N NE2 . GLN A 1 120 ? -6.080  38.019 -19.677 1.00 23.44  ? 101  GLN A NE2 1 
ATOM   812  N N   . LEU A 1 121 ? -8.358  42.196 -14.161 1.00 14.93  ? 102  LEU A N   1 
ATOM   813  C CA  . LEU A 1 121 ? -8.335  43.391 -13.314 1.00 13.01  ? 102  LEU A CA  1 
ATOM   814  C C   . LEU A 1 121 ? -7.662  43.106 -11.984 1.00 13.72  ? 102  LEU A C   1 
ATOM   815  O O   . LEU A 1 121 ? -7.804  42.019 -11.429 1.00 20.31  ? 102  LEU A O   1 
ATOM   816  C CB  . LEU A 1 121 ? -9.757  43.876 -13.037 1.00 17.24  ? 102  LEU A CB  1 
ATOM   817  C CG  . LEU A 1 121 ? -10.573 44.252 -14.269 1.00 16.33  ? 102  LEU A CG  1 
ATOM   818  C CD1 . LEU A 1 121 ? -11.978 44.675 -13.888 1.00 11.44  ? 102  LEU A CD1 1 
ATOM   819  C CD2 . LEU A 1 121 ? -9.853  45.341 -15.021 1.00 12.99  ? 102  LEU A CD2 1 
ATOM   820  N N   . ALA A 1 122 ? -6.937  44.091 -11.469 1.00 12.59  ? 103  ALA A N   1 
ATOM   821  C CA  . ALA A 1 122 ? -6.378  44.017 -10.127 1.00 14.57  ? 103  ALA A CA  1 
ATOM   822  C C   . ALA A 1 122 ? -7.109  44.946 -9.146  1.00 14.83  ? 103  ALA A C   1 
ATOM   823  O O   . ALA A 1 122 ? -7.623  46.001 -9.517  1.00 18.79  ? 103  ALA A O   1 
ATOM   824  C CB  . ALA A 1 122 ? -4.890  44.345 -10.161 1.00 13.88  ? 103  ALA A CB  1 
ATOM   825  N N   . HIS A 1 123 ? -7.127  44.560 -7.884  1.00 15.35  ? 104  HIS A N   1 
ATOM   826  C CA  . HIS A 1 123 ? -7.732  45.366 -6.835  1.00 17.53  ? 104  HIS A CA  1 
ATOM   827  C C   . HIS A 1 123 ? -6.641  46.230 -6.213  1.00 15.89  ? 104  HIS A C   1 
ATOM   828  O O   . HIS A 1 123 ? -5.571  45.721 -5.874  1.00 18.02  ? 104  HIS A O   1 
ATOM   829  C CB  . HIS A 1 123 ? -8.324  44.421 -5.797  1.00 26.03  ? 104  HIS A CB  1 
ATOM   830  C CG  . HIS A 1 123 ? -9.257  45.078 -4.839  1.00 29.37  ? 104  HIS A CG  1 
ATOM   831  N ND1 . HIS A 1 123 ? -8.905  45.350 -3.536  1.00 31.30  ? 104  HIS A ND1 1 
ATOM   832  C CD2 . HIS A 1 123 ? -10.537 45.495 -4.985  1.00 33.73  ? 104  HIS A CD2 1 
ATOM   833  C CE1 . HIS A 1 123 ? -9.929  45.917 -2.919  1.00 37.75  ? 104  HIS A CE1 1 
ATOM   834  N NE2 . HIS A 1 123 ? -10.929 46.023 -3.775  1.00 35.83  ? 104  HIS A NE2 1 
ATOM   835  N N   . VAL A 1 124 ? -6.885  47.535 -6.094  1.00 18.02  ? 105  VAL A N   1 
ATOM   836  C CA  . VAL A 1 124 ? -5.883  48.462 -5.543  1.00 16.74  ? 105  VAL A CA  1 
ATOM   837  C C   . VAL A 1 124 ? -6.488  49.244 -4.392  1.00 19.34  ? 105  VAL A C   1 
ATOM   838  O O   . VAL A 1 124 ? -7.550  49.839 -4.536  1.00 20.64  ? 105  VAL A O   1 
ATOM   839  C CB  . VAL A 1 124 ? -5.386  49.481 -6.581  1.00 12.66  ? 105  VAL A CB  1 
ATOM   840  C CG1 . VAL A 1 124 ? -4.251  50.293 -6.004  1.00 12.95  ? 105  VAL A CG1 1 
ATOM   841  C CG2 . VAL A 1 124 ? -4.936  48.802 -7.854  1.00 12.05  ? 105  VAL A CG2 1 
ATOM   842  N N   . VAL A 1 125 ? -5.811  49.233 -3.250  1.00 15.98  ? 106  VAL A N   1 
ATOM   843  C CA  . VAL A 1 125 ? -6.283  49.928 -2.057  1.00 18.21  ? 106  VAL A CA  1 
ATOM   844  C C   . VAL A 1 125 ? -5.468  51.224 -1.920  1.00 21.70  ? 106  VAL A C   1 
ATOM   845  O O   . VAL A 1 125 ? -4.325  51.265 -2.363  1.00 24.79  ? 106  VAL A O   1 
ATOM   846  C CB  . VAL A 1 125 ? -6.124  49.016 -0.808  1.00 18.87  ? 106  VAL A CB  1 
ATOM   847  C CG1 . VAL A 1 125 ? -6.397  49.786 0.456   1.00 24.79  ? 106  VAL A CG1 1 
ATOM   848  C CG2 . VAL A 1 125 ? -7.042  47.807 -0.908  1.00 13.57  ? 106  VAL A CG2 1 
ATOM   849  N N   . SER A 1 126 ? -6.040  52.273 -1.326  1.00 22.03  ? 107  SER A N   1 
ATOM   850  C CA  . SER A 1 126 ? -5.381  53.580 -1.259  1.00 19.33  ? 107  SER A CA  1 
ATOM   851  C C   . SER A 1 126 ? -3.969  53.594 -0.653  1.00 22.57  ? 107  SER A C   1 
ATOM   852  O O   . SER A 1 126 ? -3.192  54.507 -0.931  1.00 23.41  ? 107  SER A O   1 
ATOM   853  C CB  . SER A 1 126 ? -6.261  54.578 -0.529  1.00 21.34  ? 107  SER A CB  1 
ATOM   854  O OG  . SER A 1 126 ? -6.573  54.084 0.747   1.00 27.90  ? 107  SER A OG  1 
ATOM   855  N N   . ASP A 1 127 ? -3.626  52.603 0.168   1.00 20.89  ? 108  ASP A N   1 
ATOM   856  C CA  . ASP A 1 127 ? -2.265  52.549 0.713   1.00 21.23  ? 108  ASP A CA  1 
ATOM   857  C C   . ASP A 1 127 ? -1.211  52.072 -0.287  1.00 23.07  ? 108  ASP A C   1 
ATOM   858  O O   . ASP A 1 127 ? -0.015  52.231 -0.057  1.00 34.34  ? 108  ASP A O   1 
ATOM   859  C CB  . ASP A 1 127 ? -2.179  51.728 2.014   1.00 22.37  ? 108  ASP A CB  1 
ATOM   860  C CG  . ASP A 1 127 ? -2.643  50.271 1.847   1.00 42.88  ? 108  ASP A CG  1 
ATOM   861  O OD1 . ASP A 1 127 ? -2.807  49.792 0.688   1.00 40.18  ? 108  ASP A OD1 1 
ATOM   862  O OD2 . ASP A 1 127 ? -2.830  49.594 2.896   1.00 44.51  ? 108  ASP A OD2 1 
ATOM   863  N N   . GLY A 1 128 ? -1.656  51.485 -1.391  1.00 22.49  ? 109  GLY A N   1 
ATOM   864  C CA  . GLY A 1 128 ? -0.746  50.968 -2.390  1.00 24.13  ? 109  GLY A CA  1 
ATOM   865  C C   . GLY A 1 128 ? -0.692  49.453 -2.428  1.00 24.42  ? 109  GLY A C   1 
ATOM   866  O O   . GLY A 1 128 ? 0.175   48.886 -3.098  1.00 23.17  ? 109  GLY A O   1 
ATOM   867  N N   . GLU A 1 129 ? -1.609  48.797 -1.716  1.00 23.29  ? 110  GLU A N   1 
ATOM   868  C CA  . GLU A 1 129 ? -1.697  47.325 -1.726  1.00 23.01  ? 110  GLU A CA  1 
ATOM   869  C C   . GLU A 1 129 ? -2.437  46.805 -2.950  1.00 19.82  ? 110  GLU A C   1 
ATOM   870  O O   . GLU A 1 129 ? -3.555  47.228 -3.263  1.00 19.68  ? 110  GLU A O   1 
ATOM   871  C CB  . GLU A 1 129 ? -2.373  46.807 -0.458  1.00 25.14  ? 110  GLU A CB  1 
ATOM   872  C CG  . GLU A 1 129 ? -1.435  46.651 0.713   1.00 37.61  ? 110  GLU A CG  1 
ATOM   873  C CD  . GLU A 1 129 ? -0.513  45.449 0.549   1.00 54.87  ? 110  GLU A CD  1 
ATOM   874  O OE1 . GLU A 1 129 ? -1.024  44.353 0.195   1.00 58.40  ? 110  GLU A OE1 1 
ATOM   875  O OE2 . GLU A 1 129 ? 0.718   45.605 0.763   1.00 61.07  ? 110  GLU A OE2 1 
ATOM   876  N N   . VAL A 1 130 ? -1.811  45.887 -3.656  1.00 17.23  ? 111  VAL A N   1 
ATOM   877  C CA  . VAL A 1 130 ? -2.421  45.366 -4.861  1.00 18.38  ? 111  VAL A CA  1 
ATOM   878  C C   . VAL A 1 130 ? -2.719  43.883 -4.684  1.00 19.77  ? 111  VAL A C   1 
ATOM   879  O O   . VAL A 1 130 ? -1.902  43.134 -4.131  1.00 22.03  ? 111  VAL A O   1 
ATOM   880  C CB  . VAL A 1 130 ? -1.493  45.578 -6.073  1.00 19.21  ? 111  VAL A CB  1 
ATOM   881  C CG1 . VAL A 1 130 ? -2.182  45.144 -7.393  1.00 16.14  ? 111  VAL A CG1 1 
ATOM   882  C CG2 . VAL A 1 130 ? -1.052  47.010 -6.140  1.00 11.11  ? 111  VAL A CG2 1 
ATOM   883  N N   . GLN A 1 131 ? -3.886  43.453 -5.152  1.00 21.20  ? 112  GLN A N   1 
ATOM   884  C CA  . GLN A 1 131 ? -4.184  42.021 -5.216  1.00 20.38  ? 112  GLN A CA  1 
ATOM   885  C C   . GLN A 1 131 ? -4.691  41.618 -6.602  1.00 19.05  ? 112  GLN A C   1 
ATOM   886  O O   . GLN A 1 131 ? -5.626  42.214 -7.129  1.00 19.01  ? 112  GLN A O   1 
ATOM   887  C CB  . GLN A 1 131 ? -5.197  41.622 -4.152  1.00 19.74  ? 112  GLN A CB  1 
ATOM   888  C CG  . GLN A 1 131 ? -5.503  40.143 -4.158  1.00 28.43  ? 112  GLN A CG  1 
ATOM   889  C CD  . GLN A 1 131 ? -6.463  39.748 -3.062  1.00 35.99  ? 112  GLN A CD  1 
ATOM   890  O OE1 . GLN A 1 131 ? -6.364  40.237 -1.935  1.00 40.70  ? 112  GLN A OE1 1 
ATOM   891  N NE2 . GLN A 1 131 ? -7.410  38.858 -3.386  1.00 46.75  ? 112  GLN A NE2 1 
ATOM   892  N N   . TYR A 1 132 ? -4.068  40.609 -7.193  1.00 15.96  ? 113  TYR A N   1 
ATOM   893  C CA  . TYR A 1 132 ? -4.493  40.125 -8.494  1.00 15.53  ? 113  TYR A CA  1 
ATOM   894  C C   . TYR A 1 132 ? -4.740  38.623 -8.383  1.00 21.33  ? 113  TYR A C   1 
ATOM   895  O O   . TYR A 1 132 ? -3.819  37.852 -8.096  1.00 21.28  ? 113  TYR A O   1 
ATOM   896  C CB  . TYR A 1 132 ? -3.430  40.453 -9.552  1.00 12.75  ? 113  TYR A CB  1 
ATOM   897  C CG  . TYR A 1 132 ? -3.727  39.912 -10.923 1.00 13.20  ? 113  TYR A CG  1 
ATOM   898  C CD1 . TYR A 1 132 ? -5.001  40.013 -11.472 1.00 17.49  ? 113  TYR A CD1 1 
ATOM   899  C CD2 . TYR A 1 132 ? -2.741  39.301 -11.676 1.00 10.08  ? 113  TYR A CD2 1 
ATOM   900  C CE1 . TYR A 1 132 ? -5.283  39.505 -12.747 1.00 17.59  ? 113  TYR A CE1 1 
ATOM   901  C CE2 . TYR A 1 132 ? -3.014  38.788 -12.940 1.00 12.35  ? 113  TYR A CE2 1 
ATOM   902  C CZ  . TYR A 1 132 ? -4.283  38.887 -13.474 1.00 13.01  ? 113  TYR A CZ  1 
ATOM   903  O OH  . TYR A 1 132 ? -4.539  38.383 -14.743 1.00 15.03  ? 113  TYR A OH  1 
ATOM   904  N N   . THR A 1 133 ? -5.987  38.214 -8.612  1.00 20.12  ? 114  THR A N   1 
ATOM   905  C CA  . THR A 1 133 ? -6.391  36.838 -8.400  1.00 15.49  ? 114  THR A CA  1 
ATOM   906  C C   . THR A 1 133 ? -7.121  36.295 -9.622  1.00 18.44  ? 114  THR A C   1 
ATOM   907  O O   . THR A 1 133 ? -8.351  36.208 -9.650  1.00 21.66  ? 114  THR A O   1 
ATOM   908  C CB  . THR A 1 133 ? -7.300  36.719 -7.164  1.00 21.73  ? 114  THR A CB  1 
ATOM   909  O OG1 . THR A 1 133 ? -6.744  37.474 -6.075  1.00 22.92  ? 114  THR A OG1 1 
ATOM   910  C CG2 . THR A 1 133 ? -7.485  35.252 -6.754  1.00 20.54  ? 114  THR A CG2 1 
ATOM   911  N N   . PRO A 1 134 ? -6.362  35.920 -10.657 1.00 18.91  ? 115  PRO A N   1 
ATOM   912  C CA  . PRO A 1 134 ? -7.040  35.338 -11.834 1.00 17.86  ? 115  PRO A CA  1 
ATOM   913  C C   . PRO A 1 134 ? -7.383  33.867 -11.616 1.00 23.63  ? 115  PRO A C   1 
ATOM   914  O O   . PRO A 1 134 ? -6.696  33.173 -10.845 1.00 21.54  ? 115  PRO A O   1 
ATOM   915  C CB  . PRO A 1 134 ? -5.981  35.452 -12.937 1.00 13.39  ? 115  PRO A CB  1 
ATOM   916  C CG  . PRO A 1 134 ? -4.656  35.442 -12.172 1.00 11.99  ? 115  PRO A CG  1 
ATOM   917  C CD  . PRO A 1 134 ? -4.911  36.117 -10.857 1.00 12.66  ? 115  PRO A CD  1 
ATOM   918  N N   . SER A 1 135 ? -8.427  33.387 -12.290 1.00 26.68  ? 116  SER A N   1 
ATOM   919  C CA  . SER A 1 135 ? -8.688  31.950 -12.330 1.00 18.57  ? 116  SER A CA  1 
ATOM   920  C C   . SER A 1 135 ? -7.965  31.377 -13.544 1.00 21.38  ? 116  SER A C   1 
ATOM   921  O O   . SER A 1 135 ? -8.116  31.879 -14.661 1.00 21.16  ? 116  SER A O   1 
ATOM   922  C CB  . SER A 1 135 ? -10.175 31.670 -12.438 1.00 17.19  ? 116  SER A CB  1 
ATOM   923  O OG  . SER A 1 135 ? -10.412 30.277 -12.403 1.00 24.62  ? 116  SER A OG  1 
ATOM   924  N N   . ILE A 1 136 ? -7.172  30.330 -13.316 1.00 20.86  ? 117  ILE A N   1 
ATOM   925  C CA  . ILE A 1 136 ? -6.307  29.762 -14.352 1.00 18.42  ? 117  ILE A CA  1 
ATOM   926  C C   . ILE A 1 136 ? -6.497  28.247 -14.574 1.00 23.33  ? 117  ILE A C   1 
ATOM   927  O O   . ILE A 1 136 ? -6.501  27.451 -13.626 1.00 23.57  ? 117  ILE A O   1 
ATOM   928  C CB  . ILE A 1 136 ? -4.828  30.045 -14.022 1.00 14.09  ? 117  ILE A CB  1 
ATOM   929  C CG1 . ILE A 1 136 ? -4.558  31.552 -14.063 1.00 19.72  ? 117  ILE A CG1 1 
ATOM   930  C CG2 . ILE A 1 136 ? -3.906  29.326 -14.983 1.00 17.35  ? 117  ILE A CG2 1 
ATOM   931  C CD1 . ILE A 1 136 ? -3.168  31.942 -13.597 1.00 18.37  ? 117  ILE A CD1 1 
ATOM   932  N N   . ARG A 1 137 ? -6.655  27.848 -15.833 1.00 22.53  ? 118  ARG A N   1 
ATOM   933  C CA  . ARG A 1 137 ? -6.580  26.436 -16.182 1.00 16.54  ? 118  ARG A CA  1 
ATOM   934  C C   . ARG A 1 137 ? -5.212  26.167 -16.800 1.00 15.94  ? 118  ARG A C   1 
ATOM   935  O O   . ARG A 1 137 ? -4.845  26.796 -17.780 1.00 16.21  ? 118  ARG A O   1 
ATOM   936  C CB  . ARG A 1 137 ? -7.691  26.051 -17.164 1.00 19.12  ? 118  ARG A CB  1 
ATOM   937  C CG  . ARG A 1 137 ? -7.487  24.696 -17.786 1.00 26.05  ? 118  ARG A CG  1 
ATOM   938  C CD  . ARG A 1 137 ? -8.770  24.109 -18.326 1.00 31.16  ? 118  ARG A CD  1 
ATOM   939  N NE  . ARG A 1 137 ? -8.583  22.729 -18.777 1.00 32.47  ? 118  ARG A NE  1 
ATOM   940  C CZ  . ARG A 1 137 ? -9.567  21.950 -19.212 1.00 31.73  ? 118  ARG A CZ  1 
ATOM   941  N NH1 . ARG A 1 137 ? -10.809 22.410 -19.239 1.00 32.32  ? 118  ARG A NH1 1 
ATOM   942  N NH2 . ARG A 1 137 ? -9.313  20.708 -19.600 1.00 39.85  ? 118  ARG A NH2 1 
ATOM   943  N N   . GLN A 1 138 ? -4.460  25.236 -16.224 1.00 17.27  ? 119  GLN A N   1 
ATOM   944  C CA  . GLN A 1 138 ? -3.128  24.902 -16.733 1.00 21.74  ? 119  GLN A CA  1 
ATOM   945  C C   . GLN A 1 138 ? -2.802  23.397 -16.637 1.00 22.06  ? 119  GLN A C   1 
ATOM   946  O O   . GLN A 1 138 ? -3.270  22.714 -15.728 1.00 22.40  ? 119  GLN A O   1 
ATOM   947  C CB  . GLN A 1 138 ? -2.068  25.729 -15.996 1.00 19.76  ? 119  GLN A CB  1 
ATOM   948  C CG  . GLN A 1 138 ? -0.739  25.831 -16.730 1.00 23.34  ? 119  GLN A CG  1 
ATOM   949  C CD  . GLN A 1 138 ? 0.096   27.020 -16.245 1.00 28.83  ? 119  GLN A CD  1 
ATOM   950  O OE1 . GLN A 1 138 ? -0.120  27.541 -15.147 1.00 34.15  ? 119  GLN A OE1 1 
ATOM   951  N NE2 . GLN A 1 138 ? 1.043   27.462 -17.070 1.00 27.65  ? 119  GLN A NE2 1 
ATOM   952  N N   . ARG A 1 139 ? -1.995  22.895 -17.571 1.00 21.78  ? 120  ARG A N   1 
ATOM   953  C CA  . ARG A 1 139 ? -1.538  21.505 -17.547 1.00 21.36  ? 120  ARG A CA  1 
ATOM   954  C C   . ARG A 1 139 ? -0.123  21.387 -16.923 1.00 20.29  ? 120  ARG A C   1 
ATOM   955  O O   . ARG A 1 139 ? 0.776   22.170 -17.236 1.00 22.03  ? 120  ARG A O   1 
ATOM   956  C CB  . ARG A 1 139 ? -1.592  20.906 -18.963 1.00 18.81  ? 120  ARG A CB  1 
ATOM   957  C CG  . ARG A 1 139 ? -1.557  19.393 -18.978 1.00 29.09  ? 120  ARG A CG  1 
ATOM   958  C CD  . ARG A 1 139 ? -2.151  18.736 -20.235 1.00 35.17  ? 120  ARG A CD  1 
ATOM   959  N NE  . ARG A 1 139 ? -2.154  17.271 -20.098 1.00 35.54  ? 120  ARG A NE  1 
ATOM   960  C CZ  . ARG A 1 139 ? -3.149  16.558 -19.558 1.00 40.69  ? 120  ARG A CZ  1 
ATOM   961  N NH1 . ARG A 1 139 ? -4.250  17.150 -19.113 1.00 40.89  ? 120  ARG A NH1 1 
ATOM   962  N NH2 . ARG A 1 139 ? -3.051  15.242 -19.460 1.00 43.17  ? 120  ARG A NH2 1 
ATOM   963  N N   . PHE A 1 140 ? 0.065   20.429 -16.021 1.00 20.38  ? 121  PHE A N   1 
ATOM   964  C CA  . PHE A 1 140 ? 1.370   20.228 -15.368 1.00 27.39  ? 121  PHE A CA  1 
ATOM   965  C C   . PHE A 1 140 ? 1.973   18.829 -15.518 1.00 25.17  ? 121  PHE A C   1 
ATOM   966  O O   . PHE A 1 140 ? 1.286   17.853 -15.814 1.00 26.85  ? 121  PHE A O   1 
ATOM   967  C CB  . PHE A 1 140 ? 1.297   20.529 -13.872 1.00 21.58  ? 121  PHE A CB  1 
ATOM   968  C CG  . PHE A 1 140 ? 0.885   21.922 -13.562 1.00 24.62  ? 121  PHE A CG  1 
ATOM   969  C CD1 . PHE A 1 140 ? -0.464  22.252 -13.485 1.00 25.12  ? 121  PHE A CD1 1 
ATOM   970  C CD2 . PHE A 1 140 ? 1.837   22.910 -13.339 1.00 20.79  ? 121  PHE A CD2 1 
ATOM   971  C CE1 . PHE A 1 140 ? -0.866  23.545 -13.194 1.00 24.55  ? 121  PHE A CE1 1 
ATOM   972  C CE2 . PHE A 1 140 ? 1.444   24.213 -13.050 1.00 23.83  ? 121  PHE A CE2 1 
ATOM   973  C CZ  . PHE A 1 140 ? 0.087   24.531 -12.979 1.00 25.21  ? 121  PHE A CZ  1 
ATOM   974  N N   . SER A 1 141 ? 3.272   18.748 -15.279 1.00 25.11  ? 122  SER A N   1 
ATOM   975  C CA  . SER A 1 141 ? 3.979   17.482 -15.265 1.00 27.41  ? 122  SER A CA  1 
ATOM   976  C C   . SER A 1 141 ? 4.368   17.215 -13.817 1.00 28.13  ? 122  SER A C   1 
ATOM   977  O O   . SER A 1 141 ? 5.147   17.963 -13.226 1.00 34.98  ? 122  SER A O   1 
ATOM   978  C CB  . SER A 1 141 ? 5.223   17.570 -16.157 1.00 21.73  ? 122  SER A CB  1 
ATOM   979  O OG  . SER A 1 141 ? 6.194   16.613 -15.785 1.00 19.38  ? 122  SER A OG  1 
ATOM   980  N N   . CYS A 1 142 ? 3.813   16.159 -13.241 1.00 30.38  ? 123  CYS A N   1 
ATOM   981  C CA  . CYS A 1 142 ? 4.088   15.819 -11.846 1.00 40.50  ? 123  CYS A CA  1 
ATOM   982  C C   . CYS A 1 142 ? 3.807   14.338 -11.520 1.00 35.40  ? 123  CYS A C   1 
ATOM   983  O O   . CYS A 1 142 ? 3.381   13.563 -12.382 1.00 25.69  ? 123  CYS A O   1 
ATOM   984  C CB  . CYS A 1 142 ? 3.284   16.736 -10.924 1.00 39.42  ? 123  CYS A CB  1 
ATOM   985  S SG  . CYS A 1 142 ? 1.506   16.711 -11.282 1.00 65.60  ? 123  CYS A SG  1 
ATOM   986  N N   . ASP A 1 143 ? 4.043   13.960 -10.266 1.00 37.41  ? 124  ASP A N   1 
ATOM   987  C CA  . ASP A 1 143 ? 3.884   12.568 -9.842  1.00 34.35  ? 124  ASP A CA  1 
ATOM   988  C C   . ASP A 1 143 ? 2.426   12.213 -9.590  1.00 30.72  ? 124  ASP A C   1 
ATOM   989  O O   . ASP A 1 143 ? 1.800   12.713 -8.656  1.00 38.94  ? 124  ASP A O   1 
ATOM   990  C CB  . ASP A 1 143 ? 4.720   12.282 -8.596  1.00 35.50  ? 124  ASP A CB  1 
ATOM   991  C CG  . ASP A 1 143 ? 4.923   10.805 -8.364  1.00 37.49  ? 124  ASP A CG  1 
ATOM   992  O OD1 . ASP A 1 143 ? 4.575   10.002 -9.263  1.00 34.11  ? 124  ASP A OD1 1 
ATOM   993  O OD2 . ASP A 1 143 ? 5.450   10.452 -7.288  1.00 48.14  ? 124  ASP A OD2 1 
ATOM   994  N N   . VAL A 1 144 ? 1.896   11.335 -10.429 1.00 32.68  ? 125  VAL A N   1 
ATOM   995  C CA  . VAL A 1 144 ? 0.469   11.017 -10.436 1.00 30.40  ? 125  VAL A CA  1 
ATOM   996  C C   . VAL A 1 144 ? 0.206   9.619  -9.858  1.00 33.98  ? 125  VAL A C   1 
ATOM   997  O O   . VAL A 1 144 ? -0.933  9.267  -9.551  1.00 33.61  ? 125  VAL A O   1 
ATOM   998  C CB  . VAL A 1 144 ? -0.080  11.123 -11.883 1.00 36.23  ? 125  VAL A CB  1 
ATOM   999  C CG1 . VAL A 1 144 ? -1.554  10.851 -11.938 1.00 31.87  ? 125  VAL A CG1 1 
ATOM   1000 C CG2 . VAL A 1 144 ? 0.208   12.498 -12.474 1.00 36.05  ? 125  VAL A CG2 1 
ATOM   1001 N N   . SER A 1 145 ? 1.276   8.839  -9.698  1.00 34.56  ? 126  SER A N   1 
ATOM   1002 C CA  . SER A 1 145 ? 1.191   7.478  -9.176  1.00 32.33  ? 126  SER A CA  1 
ATOM   1003 C C   . SER A 1 145 ? 0.423   7.396  -7.847  1.00 35.68  ? 126  SER A C   1 
ATOM   1004 O O   . SER A 1 145 ? 0.680   8.164  -6.910  1.00 35.79  ? 126  SER A O   1 
ATOM   1005 C CB  . SER A 1 145 ? 2.591   6.900  -8.996  1.00 30.52  ? 126  SER A CB  1 
ATOM   1006 O OG  . SER A 1 145 ? 3.323   7.678  -8.069  1.00 39.96  ? 126  SER A OG  1 
ATOM   1007 N N   . GLY A 1 146 ? -0.529  6.469  -7.782  1.00 34.19  ? 127  GLY A N   1 
ATOM   1008 C CA  . GLY A 1 146 ? -1.276  6.227  -6.561  1.00 30.87  ? 127  GLY A CA  1 
ATOM   1009 C C   . GLY A 1 146 ? -2.531  7.061  -6.509  1.00 38.58  ? 127  GLY A C   1 
ATOM   1010 O O   . GLY A 1 146 ? -3.135  7.234  -5.447  1.00 41.32  ? 127  GLY A O   1 
ATOM   1011 N N   . VAL A 1 147 ? -2.924  7.591  -7.663  1.00 38.61  ? 128  VAL A N   1 
ATOM   1012 C CA  . VAL A 1 147 ? -4.096  8.460  -7.728  1.00 37.71  ? 128  VAL A CA  1 
ATOM   1013 C C   . VAL A 1 147 ? -5.359  7.641  -7.462  1.00 32.22  ? 128  VAL A C   1 
ATOM   1014 O O   . VAL A 1 147 ? -6.362  8.161  -6.966  1.00 33.53  ? 128  VAL A O   1 
ATOM   1015 C CB  . VAL A 1 147 ? -4.169  9.221  -9.081  1.00 31.46  ? 128  VAL A CB  1 
ATOM   1016 C CG1 . VAL A 1 147 ? -4.229  8.245  -10.230 1.00 31.25  ? 128  VAL A CG1 1 
ATOM   1017 C CG2 . VAL A 1 147 ? -5.350  10.192 -9.107  1.00 27.77  ? 128  VAL A CG2 1 
ATOM   1018 N N   . ASP A 1 148 ? -5.286  6.348  -7.764  1.00 37.63  ? 129  ASP A N   1 
ATOM   1019 C CA  . ASP A 1 148 ? -6.425  5.449  -7.567  1.00 44.79  ? 129  ASP A CA  1 
ATOM   1020 C C   . ASP A 1 148 ? -6.283  4.590  -6.299  1.00 34.58  ? 129  ASP A C   1 
ATOM   1021 O O   . ASP A 1 148 ? -6.699  3.449  -6.271  1.00 41.63  ? 129  ASP A O   1 
ATOM   1022 C CB  . ASP A 1 148 ? -6.625  4.577  -8.810  1.00 39.60  ? 129  ASP A CB  1 
ATOM   1023 C CG  . ASP A 1 148 ? -8.092  4.316  -9.101  1.00 48.69  ? 129  ASP A CG  1 
ATOM   1024 O OD1 . ASP A 1 148 ? -8.845  4.067  -8.127  1.00 48.24  ? 129  ASP A OD1 1 
ATOM   1025 O OD2 . ASP A 1 148 ? -8.489  4.373  -10.290 1.00 56.54  ? 129  ASP A OD2 1 
ATOM   1026 N N   . THR A 1 149 ? -5.717  5.187  -5.255  1.00 31.35  ? 130  THR A N   1 
ATOM   1027 C CA  . THR A 1 149 ? -5.324  4.524  -4.021  1.00 27.02  ? 130  THR A CA  1 
ATOM   1028 C C   . THR A 1 149 ? -5.903  5.316  -2.843  1.00 39.98  ? 130  THR A C   1 
ATOM   1029 O O   . THR A 1 149 ? -6.216  6.499  -2.973  1.00 46.23  ? 130  THR A O   1 
ATOM   1030 C CB  . THR A 1 149 ? -3.779  4.496  -3.942  1.00 34.10  ? 130  THR A CB  1 
ATOM   1031 O OG1 . THR A 1 149 ? -3.279  3.576  -4.914  1.00 27.71  ? 130  THR A OG1 1 
ATOM   1032 C CG2 . THR A 1 149 ? -3.248  4.102  -2.552  1.00 42.09  ? 130  THR A CG2 1 
ATOM   1033 N N   . GLU A 1 150 ? -6.058  4.683  -1.692  1.00 39.22  ? 131  GLU A N   1 
ATOM   1034 C CA  . GLU A 1 150 ? -6.623  5.371  -0.549  1.00 43.89  ? 131  GLU A CA  1 
ATOM   1035 C C   . GLU A 1 150 ? -5.730  6.521  -0.048  1.00 43.91  ? 131  GLU A C   1 
ATOM   1036 O O   . GLU A 1 150 ? -6.228  7.493  0.524   1.00 46.01  ? 131  GLU A O   1 
ATOM   1037 C CB  . GLU A 1 150 ? -6.901  4.362  0.562   1.00 48.12  ? 131  GLU A CB  1 
ATOM   1038 C CG  . GLU A 1 150 ? -7.834  4.852  1.640   1.00 60.29  ? 131  GLU A CG  1 
ATOM   1039 C CD  . GLU A 1 150 ? -7.703  4.044  2.917   1.00 74.65  ? 131  GLU A CD  1 
ATOM   1040 O OE1 . GLU A 1 150 ? -6.562  3.688  3.284   1.00 79.93  ? 131  GLU A OE1 1 
ATOM   1041 O OE2 . GLU A 1 150 ? -8.740  3.755  3.549   1.00 86.92  ? 131  GLU A OE2 1 
ATOM   1042 N N   . SER A 1 151 ? -4.420  6.420  -0.276  1.00 43.17  ? 132  SER A N   1 
ATOM   1043 C CA  . SER A 1 151 ? -3.466  7.454  0.177   1.00 49.47  ? 132  SER A CA  1 
ATOM   1044 C C   . SER A 1 151 ? -3.202  8.574  -0.854  1.00 43.62  ? 132  SER A C   1 
ATOM   1045 O O   . SER A 1 151 ? -2.627  9.622  -0.534  1.00 38.04  ? 132  SER A O   1 
ATOM   1046 C CB  . SER A 1 151 ? -2.143  6.810  0.616   1.00 52.39  ? 132  SER A CB  1 
ATOM   1047 O OG  . SER A 1 151 ? -1.624  5.964  -0.399  1.00 59.08  ? 132  SER A OG  1 
ATOM   1048 N N   . GLY A 1 152 ? -3.607  8.332  -2.095  1.00 39.66  ? 133  GLY A N   1 
ATOM   1049 C CA  . GLY A 1 152 ? -3.602  9.363  -3.116  1.00 40.70  ? 133  GLY A CA  1 
ATOM   1050 C C   . GLY A 1 152 ? -2.250  9.668  -3.740  1.00 41.96  ? 133  GLY A C   1 
ATOM   1051 O O   . GLY A 1 152 ? -1.218  9.144  -3.296  1.00 40.22  ? 133  GLY A O   1 
ATOM   1052 N N   . ALA A 1 153 ? -2.265  10.508 -4.782  1.00 35.09  ? 134  ALA A N   1 
ATOM   1053 C CA  . ALA A 1 153 ? -1.037  11.033 -5.384  1.00 35.03  ? 134  ALA A CA  1 
ATOM   1054 C C   . ALA A 1 153 ? -0.662  12.378 -4.754  1.00 33.70  ? 134  ALA A C   1 
ATOM   1055 O O   . ALA A 1 153 ? -1.525  13.105 -4.246  1.00 31.67  ? 134  ALA A O   1 
ATOM   1056 C CB  . ALA A 1 153 ? -1.198  11.177 -6.884  1.00 28.83  ? 134  ALA A CB  1 
ATOM   1057 N N   . THR A 1 154 ? 0.625   12.704 -4.784  1.00 33.98  ? 135  THR A N   1 
ATOM   1058 C CA  . THR A 1 154 ? 1.058   14.039 -4.389  1.00 31.97  ? 135  THR A CA  1 
ATOM   1059 C C   . THR A 1 154 ? 1.788   14.745 -5.528  1.00 34.10  ? 135  THR A C   1 
ATOM   1060 O O   . THR A 1 154 ? 2.931   14.419 -5.855  1.00 31.74  ? 135  THR A O   1 
ATOM   1061 C CB  . THR A 1 154 ? 1.932   14.034 -3.127  1.00 38.09  ? 135  THR A CB  1 
ATOM   1062 O OG1 . THR A 1 154 ? 1.300   13.239 -2.117  1.00 48.81  ? 135  THR A OG1 1 
ATOM   1063 C CG2 . THR A 1 154 ? 2.109   15.467 -2.594  1.00 40.11  ? 135  THR A CG2 1 
ATOM   1064 N N   . CYS A 1 155 ? 1.100   15.714 -6.120  1.00 31.45  ? 136  CYS A N   1 
ATOM   1065 C CA  . CYS A 1 155 ? 1.629   16.541 -7.191  1.00 33.07  ? 136  CYS A CA  1 
ATOM   1066 C C   . CYS A 1 155 ? 2.161   17.888 -6.643  1.00 35.92  ? 136  CYS A C   1 
ATOM   1067 O O   . CYS A 1 155 ? 1.453   18.582 -5.906  1.00 34.88  ? 136  CYS A O   1 
ATOM   1068 C CB  . CYS A 1 155 ? 0.507   16.795 -8.197  1.00 40.86  ? 136  CYS A CB  1 
ATOM   1069 S SG  . CYS A 1 155 ? 0.967   17.799 -9.632  1.00 82.15  ? 136  CYS A SG  1 
ATOM   1070 N N   . ARG A 1 156 ? 3.399   18.249 -6.992  1.00 35.43  ? 137  ARG A N   1 
ATOM   1071 C CA  . ARG A 1 156 ? 3.994   19.519 -6.560  1.00 28.03  ? 137  ARG A CA  1 
ATOM   1072 C C   . ARG A 1 156 ? 4.022   20.536 -7.714  1.00 30.18  ? 137  ARG A C   1 
ATOM   1073 O O   . ARG A 1 156 ? 4.370   20.202 -8.842  1.00 33.66  ? 137  ARG A O   1 
ATOM   1074 C CB  . ARG A 1 156 ? 5.417   19.325 -6.005  1.00 29.88  ? 137  ARG A CB  1 
ATOM   1075 C CG  . ARG A 1 156 ? 5.619   18.117 -5.069  1.00 29.73  ? 137  ARG A CG  1 
ATOM   1076 C CD  . ARG A 1 156 ? 7.066   18.027 -4.544  1.00 42.59  ? 137  ARG A CD  1 
ATOM   1077 N NE  . ARG A 1 156 ? 8.100   18.504 -5.486  1.00 55.11  ? 137  ARG A NE  1 
ATOM   1078 C CZ  . ARG A 1 156 ? 8.776   17.730 -6.342  1.00 51.89  ? 137  ARG A CZ  1 
ATOM   1079 N NH1 . ARG A 1 156 ? 8.520   16.433 -6.405  1.00 43.03  ? 137  ARG A NH1 1 
ATOM   1080 N NH2 . ARG A 1 156 ? 9.702   18.248 -7.149  1.00 50.69  ? 137  ARG A NH2 1 
ATOM   1081 N N   . ILE A 1 157 ? 3.654   21.779 -7.420  1.00 29.00  ? 138  ILE A N   1 
ATOM   1082 C CA  . ILE A 1 157 ? 3.724   22.858 -8.389  1.00 22.77  ? 138  ILE A CA  1 
ATOM   1083 C C   . ILE A 1 157 ? 4.680   23.939 -7.914  1.00 22.48  ? 138  ILE A C   1 
ATOM   1084 O O   . ILE A 1 157 ? 4.522   24.490 -6.819  1.00 25.13  ? 138  ILE A O   1 
ATOM   1085 C CB  . ILE A 1 157 ? 2.358   23.487 -8.588  1.00 25.18  ? 138  ILE A CB  1 
ATOM   1086 C CG1 . ILE A 1 157 ? 1.381   22.435 -9.107  1.00 25.82  ? 138  ILE A CG1 1 
ATOM   1087 C CG2 . ILE A 1 157 ? 2.452   24.679 -9.544  1.00 18.67  ? 138  ILE A CG2 1 
ATOM   1088 C CD1 . ILE A 1 157 ? 0.098   23.018 -9.637  1.00 25.85  ? 138  ILE A CD1 1 
ATOM   1089 N N   . LYS A 1 158 ? 5.672   24.248 -8.736  1.00 22.85  ? 139  LYS A N   1 
ATOM   1090 C CA  . LYS A 1 158 ? 6.720   25.181 -8.339  1.00 23.46  ? 139  LYS A CA  1 
ATOM   1091 C C   . LYS A 1 158 ? 6.523   26.529 -9.050  1.00 26.41  ? 139  LYS A C   1 
ATOM   1092 O O   . LYS A 1 158 ? 6.575   26.615 -10.289 1.00 26.90  ? 139  LYS A O   1 
ATOM   1093 C CB  . LYS A 1 158 ? 8.096   24.565 -8.635  1.00 23.18  ? 139  LYS A CB  1 
ATOM   1094 C CG  . LYS A 1 158 ? 9.265   25.503 -8.417  1.00 42.03  ? 139  LYS A CG  1 
ATOM   1095 C CD  . LYS A 1 158 ? 10.537  24.984 -9.109  1.00 53.71  ? 139  LYS A CD  1 
ATOM   1096 C CE  . LYS A 1 158 ? 11.612  26.085 -9.293  1.00 43.11  ? 139  LYS A CE  1 
ATOM   1097 N NZ  . LYS A 1 158 ? 12.920  25.513 -9.766  1.00 52.78  ? 139  LYS A NZ  1 
ATOM   1098 N N   . ILE A 1 159 ? 6.288   27.581 -8.270  1.00 23.06  ? 140  ILE A N   1 
ATOM   1099 C CA  . ILE A 1 159 ? 6.035   28.905 -8.841  1.00 19.33  ? 140  ILE A CA  1 
ATOM   1100 C C   . ILE A 1 159 ? 6.997   29.963 -8.316  1.00 15.75  ? 140  ILE A C   1 
ATOM   1101 O O   . ILE A 1 159 ? 7.161   30.112 -7.113  1.00 18.74  ? 140  ILE A O   1 
ATOM   1102 C CB  . ILE A 1 159 ? 4.614   29.347 -8.525  1.00 22.88  ? 140  ILE A CB  1 
ATOM   1103 C CG1 . ILE A 1 159 ? 3.611   28.368 -9.146  1.00 22.38  ? 140  ILE A CG1 1 
ATOM   1104 C CG2 . ILE A 1 159 ? 4.373   30.773 -9.017  1.00 19.99  ? 140  ILE A CG2 1 
ATOM   1105 C CD1 . ILE A 1 159 ? 2.139   28.762 -8.922  1.00 26.86  ? 140  ILE A CD1 1 
ATOM   1106 N N   . GLY A 1 160 ? 7.624   30.708 -9.213  1.00 18.54  ? 141  GLY A N   1 
ATOM   1107 C CA  . GLY A 1 160 ? 8.538   31.773 -8.811  1.00 19.70  ? 141  GLY A CA  1 
ATOM   1108 C C   . GLY A 1 160 ? 8.748   32.859 -9.866  1.00 20.76  ? 141  GLY A C   1 
ATOM   1109 O O   . GLY A 1 160 ? 8.250   32.766 -10.993 1.00 19.11  ? 141  GLY A O   1 
ATOM   1110 N N   . SER A 1 161 ? 9.484   33.905 -9.508  1.00 22.06  ? 142  SER A N   1 
ATOM   1111 C CA  . SER A 1 161 ? 9.864   34.915 -10.504 1.00 20.54  ? 142  SER A CA  1 
ATOM   1112 C C   . SER A 1 161 ? 10.815  34.365 -11.574 1.00 18.05  ? 142  SER A C   1 
ATOM   1113 O O   . SER A 1 161 ? 11.771  33.649 -11.271 1.00 24.20  ? 142  SER A O   1 
ATOM   1114 C CB  . SER A 1 161 ? 10.531  36.109 -9.841  1.00 23.82  ? 142  SER A CB  1 
ATOM   1115 O OG  . SER A 1 161 ? 10.957  37.019 -10.843 1.00 24.00  ? 142  SER A OG  1 
ATOM   1116 N N   . TRP A 1 162 ? 10.572  34.728 -12.824 1.00 16.98  ? 143  TRP A N   1 
ATOM   1117 C CA  . TRP A 1 162 ? 11.338  34.170 -13.927 1.00 16.69  ? 143  TRP A CA  1 
ATOM   1118 C C   . TRP A 1 162 ? 12.641  34.899 -14.173 1.00 19.37  ? 143  TRP A C   1 
ATOM   1119 O O   . TRP A 1 162 ? 13.624  34.278 -14.576 1.00 24.02  ? 143  TRP A O   1 
ATOM   1120 C CB  . TRP A 1 162 ? 10.506  34.152 -15.218 1.00 20.38  ? 143  TRP A CB  1 
ATOM   1121 C CG  . TRP A 1 162 ? 11.097  33.264 -16.286 1.00 19.45  ? 143  TRP A CG  1 
ATOM   1122 C CD1 . TRP A 1 162 ? 11.717  33.659 -17.435 1.00 17.01  ? 143  TRP A CD1 1 
ATOM   1123 C CD2 . TRP A 1 162 ? 11.127  31.829 -16.291 1.00 22.98  ? 143  TRP A CD2 1 
ATOM   1124 N NE1 . TRP A 1 162 ? 12.128  32.563 -18.154 1.00 17.59  ? 143  TRP A NE1 1 
ATOM   1125 C CE2 . TRP A 1 162 ? 11.772  31.421 -17.480 1.00 20.37  ? 143  TRP A CE2 1 
ATOM   1126 C CE3 . TRP A 1 162 ? 10.674  30.841 -15.400 1.00 24.22  ? 143  TRP A CE3 1 
ATOM   1127 C CZ2 . TRP A 1 162 ? 11.981  30.076 -17.808 1.00 20.37  ? 143  TRP A CZ2 1 
ATOM   1128 C CZ3 . TRP A 1 162 ? 10.876  29.495 -15.723 1.00 19.55  ? 143  TRP A CZ3 1 
ATOM   1129 C CH2 . TRP A 1 162 ? 11.528  29.128 -16.913 1.00 19.26  ? 143  TRP A CH2 1 
ATOM   1130 N N   . THR A 1 163 ? 12.651  36.215 -13.949 1.00 22.40  ? 144  THR A N   1 
ATOM   1131 C CA  . THR A 1 163 ? 13.838  37.042 -14.245 1.00 23.50  ? 144  THR A CA  1 
ATOM   1132 C C   . THR A 1 163 ? 14.405  37.839 -13.069 1.00 23.97  ? 144  THR A C   1 
ATOM   1133 O O   . THR A 1 163 ? 15.466  38.442 -13.195 1.00 34.72  ? 144  THR A O   1 
ATOM   1134 C CB  . THR A 1 163 ? 13.593  38.045 -15.401 1.00 21.06  ? 144  THR A CB  1 
ATOM   1135 O OG1 . THR A 1 163 ? 12.634  39.028 -14.985 1.00 19.63  ? 144  THR A OG1 1 
ATOM   1136 C CG2 . THR A 1 163 ? 13.098  37.336 -16.640 1.00 19.85  ? 144  THR A CG2 1 
ATOM   1137 N N   . HIS A 1 164 ? 13.697  37.883 -11.950 1.00 19.59  ? 145  HIS A N   1 
ATOM   1138 C CA  . HIS A 1 164 ? 14.169  38.666 -10.814 1.00 19.52  ? 145  HIS A CA  1 
ATOM   1139 C C   . HIS A 1 164 ? 14.696  37.788 -9.682  1.00 22.92  ? 145  HIS A C   1 
ATOM   1140 O O   . HIS A 1 164 ? 13.986  36.907 -9.194  1.00 24.38  ? 145  HIS A O   1 
ATOM   1141 C CB  . HIS A 1 164 ? 13.052  39.570 -10.294 1.00 24.77  ? 145  HIS A CB  1 
ATOM   1142 C CG  . HIS A 1 164 ? 12.658  40.659 -11.248 1.00 30.06  ? 145  HIS A CG  1 
ATOM   1143 N ND1 . HIS A 1 164 ? 13.462  41.752 -11.498 1.00 29.09  ? 145  HIS A ND1 1 
ATOM   1144 C CD2 . HIS A 1 164 ? 11.545  40.824 -12.001 1.00 27.93  ? 145  HIS A CD2 1 
ATOM   1145 C CE1 . HIS A 1 164 ? 12.859  42.541 -12.372 1.00 28.53  ? 145  HIS A CE1 1 
ATOM   1146 N NE2 . HIS A 1 164 ? 11.694  42.008 -12.690 1.00 25.74  ? 145  HIS A NE2 1 
ATOM   1147 N N   . HIS A 1 165 ? 15.934  38.029 -9.252  1.00 25.53  ? 146  HIS A N   1 
ATOM   1148 C CA  . HIS A 1 165 ? 16.523  37.252 -8.149  1.00 28.12  ? 146  HIS A CA  1 
ATOM   1149 C C   . HIS A 1 165 ? 16.011  37.669 -6.755  1.00 25.89  ? 146  HIS A C   1 
ATOM   1150 O O   . HIS A 1 165 ? 15.167  38.543 -6.634  1.00 24.54  ? 146  HIS A O   1 
ATOM   1151 C CB  . HIS A 1 165 ? 18.056  37.245 -8.222  1.00 30.25  ? 146  HIS A CB  1 
ATOM   1152 C CG  . HIS A 1 165 ? 18.671  38.597 -8.117  1.00 34.75  ? 146  HIS A CG  1 
ATOM   1153 N ND1 . HIS A 1 165 ? 18.567  39.395 -6.997  1.00 34.48  ? 146  HIS A ND1 1 
ATOM   1154 C CD2 . HIS A 1 165 ? 19.422  39.313 -9.006  1.00 37.60  ? 146  HIS A CD2 1 
ATOM   1155 C CE1 . HIS A 1 165 ? 19.206  40.529 -7.191  1.00 31.59  ? 146  HIS A CE1 1 
ATOM   1156 N NE2 . HIS A 1 165 ? 19.741  40.496 -8.405  1.00 34.56  ? 146  HIS A NE2 1 
ATOM   1157 N N   . SER A 1 166 ? 16.537  37.038 -5.711  1.00 31.39  ? 147  SER A N   1 
ATOM   1158 C CA  . SER A 1 166 ? 15.976  37.139 -4.356  1.00 28.44  ? 147  SER A CA  1 
ATOM   1159 C C   . SER A 1 166 ? 16.084  38.519 -3.700  1.00 29.04  ? 147  SER A C   1 
ATOM   1160 O O   . SER A 1 166 ? 15.404  38.780 -2.705  1.00 31.32  ? 147  SER A O   1 
ATOM   1161 C CB  . SER A 1 166 ? 16.657  36.121 -3.456  1.00 28.93  ? 147  SER A CB  1 
ATOM   1162 O OG  . SER A 1 166 ? 18.027  36.467 -3.334  1.00 41.37  ? 147  SER A OG  1 
ATOM   1163 N N   . ARG A 1 167 ? 16.938  39.391 -4.231  1.00 29.12  ? 148  ARG A N   1 
ATOM   1164 C CA  . ARG A 1 167 ? 17.079  40.734 -3.668  1.00 29.53  ? 148  ARG A CA  1 
ATOM   1165 C C   . ARG A 1 167 ? 16.159  41.721 -4.367  1.00 26.81  ? 148  ARG A C   1 
ATOM   1166 O O   . ARG A 1 167 ? 16.054  42.872 -3.962  1.00 36.04  ? 148  ARG A O   1 
ATOM   1167 C CB  . ARG A 1 167 ? 18.522  41.237 -3.756  1.00 39.31  ? 148  ARG A CB  1 
ATOM   1168 C CG  . ARG A 1 167 ? 19.524  40.514 -2.858  1.00 43.53  ? 148  ARG A CG  1 
ATOM   1169 C CD  . ARG A 1 167 ? 20.938  41.137 -2.979  1.00 71.81  ? 148  ARG A CD  1 
ATOM   1170 N NE  . ARG A 1 167 ? 21.094  42.044 -4.131  1.00 78.63  ? 148  ARG A NE  1 
ATOM   1171 C CZ  . ARG A 1 167 ? 22.147  42.063 -4.959  1.00 81.74  ? 148  ARG A CZ  1 
ATOM   1172 N NH1 . ARG A 1 167 ? 23.165  41.219 -4.783  1.00 71.29  ? 148  ARG A NH1 1 
ATOM   1173 N NH2 . ARG A 1 167 ? 22.179  42.925 -5.974  1.00 68.72  ? 148  ARG A NH2 1 
ATOM   1174 N N   . GLU A 1 168 ? 15.501  41.265 -5.425  1.00 30.76  ? 149  GLU A N   1 
ATOM   1175 C CA  . GLU A 1 168 ? 14.547  42.089 -6.171  1.00 29.25  ? 149  GLU A CA  1 
ATOM   1176 C C   . GLU A 1 168 ? 13.085  41.681 -5.907  1.00 23.83  ? 149  GLU A C   1 
ATOM   1177 O O   . GLU A 1 168 ? 12.222  42.529 -5.648  1.00 24.35  ? 149  GLU A O   1 
ATOM   1178 C CB  . GLU A 1 168 ? 14.885  42.063 -7.676  1.00 26.21  ? 149  GLU A CB  1 
ATOM   1179 C CG  . GLU A 1 168 ? 16.213  42.741 -8.024  1.00 32.54  ? 149  GLU A CG  1 
ATOM   1180 C CD  . GLU A 1 168 ? 16.604  42.598 -9.490  1.00 39.05  ? 149  GLU A CD  1 
ATOM   1181 O OE1 . GLU A 1 168 ? 16.273  41.554 -10.088 1.00 41.74  ? 149  GLU A OE1 1 
ATOM   1182 O OE2 . GLU A 1 168 ? 17.243  43.529 -10.042 1.00 46.76  ? 149  GLU A OE2 1 
ATOM   1183 N N   . ILE A 1 169 ? 12.817  40.381 -5.994  1.00 20.60  ? 150  ILE A N   1 
ATOM   1184 C CA  . ILE A 1 169 ? 11.519  39.820 -5.639  1.00 18.57  ? 150  ILE A CA  1 
ATOM   1185 C C   . ILE A 1 169 ? 11.691  38.648 -4.675  1.00 20.72  ? 150  ILE A C   1 
ATOM   1186 O O   . ILE A 1 169 ? 12.475  37.729 -4.930  1.00 26.54  ? 150  ILE A O   1 
ATOM   1187 C CB  . ILE A 1 169 ? 10.764  39.343 -6.886  1.00 21.17  ? 150  ILE A CB  1 
ATOM   1188 C CG1 . ILE A 1 169 ? 10.313  40.554 -7.711  1.00 24.76  ? 150  ILE A CG1 1 
ATOM   1189 C CG2 . ILE A 1 169 ? 9.572   38.466 -6.498  1.00 20.94  ? 150  ILE A CG2 1 
ATOM   1190 C CD1 . ILE A 1 169 ? 9.481   40.226 -8.957  1.00 21.29  ? 150  ILE A CD1 1 
ATOM   1191 N N   . SER A 1 170 ? 10.982  38.688 -3.554  1.00 20.23  ? 151  SER A N   1 
ATOM   1192 C CA  . SER A 1 170 ? 10.873  37.511 -2.702  1.00 25.44  ? 151  SER A CA  1 
ATOM   1193 C C   . SER A 1 170 ? 9.434   36.975 -2.745  1.00 25.95  ? 151  SER A C   1 
ATOM   1194 O O   . SER A 1 170 ? 8.475   37.739 -2.629  1.00 30.67  ? 151  SER A O   1 
ATOM   1195 C CB  . SER A 1 170 ? 11.308  37.816 -1.273  1.00 23.70  ? 151  SER A CB  1 
ATOM   1196 O OG  . SER A 1 170 ? 10.408  38.726 -0.676  1.00 33.11  ? 151  SER A OG  1 
ATOM   1197 N N   . VAL A 1 171 ? 9.279   35.669 -2.931  1.00 25.72  ? 152  VAL A N   1 
ATOM   1198 C CA  . VAL A 1 171 ? 7.955   35.047 -2.874  1.00 33.11  ? 152  VAL A CA  1 
ATOM   1199 C C   . VAL A 1 171 ? 7.782   34.285 -1.573  1.00 29.16  ? 152  VAL A C   1 
ATOM   1200 O O   . VAL A 1 171 ? 8.702   33.620 -1.120  1.00 33.73  ? 152  VAL A O   1 
ATOM   1201 C CB  . VAL A 1 171 ? 7.717   34.072 -4.045  1.00 27.66  ? 152  VAL A CB  1 
ATOM   1202 C CG1 . VAL A 1 171 ? 7.360   34.829 -5.297  1.00 20.10  ? 152  VAL A CG1 1 
ATOM   1203 C CG2 . VAL A 1 171 ? 8.946   33.222 -4.271  1.00 26.17  ? 152  VAL A CG2 1 
ATOM   1204 N N   . ASP A 1 172 ? 6.599   34.381 -0.980  1.00 30.30  ? 153  ASP A N   1 
ATOM   1205 C CA  . ASP A 1 172 ? 6.317   33.736 0.296   1.00 36.70  ? 153  ASP A CA  1 
ATOM   1206 C C   . ASP A 1 172 ? 4.900   33.164 0.263   1.00 37.15  ? 153  ASP A C   1 
ATOM   1207 O O   . ASP A 1 172 ? 4.013   33.722 -0.374  1.00 33.27  ? 153  ASP A O   1 
ATOM   1208 C CB  . ASP A 1 172 ? 6.464   34.743 1.456   1.00 44.12  ? 153  ASP A CB  1 
ATOM   1209 C CG  . ASP A 1 172 ? 7.653   35.718 1.265   1.00 60.29  ? 153  ASP A CG  1 
ATOM   1210 O OD1 . ASP A 1 172 ? 8.804   35.314 1.584   1.00 62.12  ? 153  ASP A OD1 1 
ATOM   1211 O OD2 . ASP A 1 172 ? 7.431   36.881 0.802   1.00 44.17  ? 153  ASP A OD2 1 
ATOM   1212 N N   . PRO A 1 173 ? 4.684   32.025 0.929   1.00 43.72  ? 154  PRO A N   1 
ATOM   1213 C CA  . PRO A 1 173 ? 3.330   31.470 1.074   1.00 33.06  ? 154  PRO A CA  1 
ATOM   1214 C C   . PRO A 1 173 ? 2.523   32.325 2.028   1.00 38.16  ? 154  PRO A C   1 
ATOM   1215 O O   . PRO A 1 173 ? 3.119   33.035 2.849   1.00 42.97  ? 154  PRO A O   1 
ATOM   1216 C CB  . PRO A 1 173 ? 3.584   30.110 1.721   1.00 34.36  ? 154  PRO A CB  1 
ATOM   1217 C CG  . PRO A 1 173 ? 5.030   29.813 1.438   1.00 33.55  ? 154  PRO A CG  1 
ATOM   1218 C CD  . PRO A 1 173 ? 5.714   31.133 1.484   1.00 38.28  ? 154  PRO A CD  1 
ATOM   1219 N N   . THR A 1 174 ? 1.199   32.253 1.940   1.00 41.93  ? 155  THR A N   1 
ATOM   1220 C CA  . THR A 1 174 ? 0.317   33.079 2.777   1.00 48.78  ? 155  THR A CA  1 
ATOM   1221 C C   . THR A 1 174 ? 0.066   32.477 4.163   1.00 60.30  ? 155  THR A C   1 
ATOM   1222 O O   . THR A 1 174 ? -0.084  31.264 4.294   1.00 62.86  ? 155  THR A O   1 
ATOM   1223 C CB  . THR A 1 174 ? -1.039  33.304 2.082   1.00 50.90  ? 155  THR A CB  1 
ATOM   1224 O OG1 . THR A 1 174 ? -0.847  34.139 0.930   1.00 48.93  ? 155  THR A OG1 1 
ATOM   1225 C CG2 . THR A 1 174 ? -2.043  33.968 3.021   1.00 56.42  ? 155  THR A CG2 1 
ATOM   1226 N N   . THR A 1 175 ? -0.005  33.317 5.194   1.00 60.85  ? 156  THR A N   1 
ATOM   1227 C CA  . THR A 1 175 ? -0.352  32.835 6.535   1.00 70.87  ? 156  THR A CA  1 
ATOM   1228 C C   . THR A 1 175 ? -1.767  32.217 6.607   1.00 74.15  ? 156  THR A C   1 
ATOM   1229 O O   . THR A 1 175 ? -2.777  32.911 6.772   1.00 67.36  ? 156  THR A O   1 
ATOM   1230 C CB  . THR A 1 175 ? -0.196  33.949 7.588   1.00 68.22  ? 156  THR A CB  1 
ATOM   1231 O OG1 . THR A 1 175 ? 1.022   34.670 7.354   1.00 65.98  ? 156  THR A OG1 1 
ATOM   1232 C CG2 . THR A 1 175 ? -0.179  33.358 8.992   1.00 61.76  ? 156  THR A CG2 1 
ATOM   1233 N N   . ASP A 1 180 ? -9.192  24.220 2.213   1.00 49.18  ? 161  ASP A N   1 
ATOM   1234 C CA  . ASP A 1 180 ? -8.423  23.596 1.142   1.00 63.40  ? 161  ASP A CA  1 
ATOM   1235 C C   . ASP A 1 180 ? -9.280  23.338 -0.054  1.00 50.36  ? 161  ASP A C   1 
ATOM   1236 O O   . ASP A 1 180 ? -8.985  23.718 -1.153  1.00 45.94  ? 161  ASP A O   1 
ATOM   1237 C CB  . ASP A 1 180 ? -7.815  22.286 1.608   1.00 57.32  ? 161  ASP A CB  1 
ATOM   1238 C CG  . ASP A 1 180 ? -6.741  22.480 2.634   1.00 67.11  ? 161  ASP A CG  1 
ATOM   1239 O OD1 . ASP A 1 180 ? -6.338  23.622 2.858   1.00 63.50  ? 161  ASP A OD1 1 
ATOM   1240 O OD2 . ASP A 1 180 ? -6.304  21.486 3.227   1.00 61.93  ? 161  ASP A OD2 1 
ATOM   1241 N N   . SER A 1 181 ? -10.369 22.679 0.203   1.00 55.99  ? 162  SER A N   1 
ATOM   1242 C CA  . SER A 1 181 ? -11.355 22.355 -0.792  1.00 56.46  ? 162  SER A CA  1 
ATOM   1243 C C   . SER A 1 181 ? -12.529 23.298 -0.597  1.00 50.05  ? 162  SER A C   1 
ATOM   1244 O O   . SER A 1 181 ? -13.647 22.970 -0.907  1.00 47.23  ? 162  SER A O   1 
ATOM   1245 C CB  . SER A 1 181 ? -11.727 20.869 -0.690  1.00 60.64  ? 162  SER A CB  1 
ATOM   1246 O OG  . SER A 1 181 ? -13.119 20.675 -0.686  1.00 50.79  ? 162  SER A OG  1 
ATOM   1247 N N   . GLU A 1 182 ? -12.234 24.457 -0.036  1.00 44.90  ? 163  GLU A N   1 
ATOM   1248 C CA  . GLU A 1 182 ? -13.202 25.447 0.327   1.00 45.88  ? 163  GLU A CA  1 
ATOM   1249 C C   . GLU A 1 182 ? -13.919 25.851 -0.915  1.00 47.50  ? 163  GLU A C   1 
ATOM   1250 O O   . GLU A 1 182 ? -15.092 26.102 -0.876  1.00 47.31  ? 163  GLU A O   1 
ATOM   1251 C CB  . GLU A 1 182 ? -12.470 26.638 0.899   1.00 52.03  ? 163  GLU A CB  1 
ATOM   1252 C CG  . GLU A 1 182 ? -13.286 27.606 1.723   1.00 65.85  ? 163  GLU A CG  1 
ATOM   1253 C CD  . GLU A 1 182 ? -12.575 28.942 1.956   1.00 82.02  ? 163  GLU A CD  1 
ATOM   1254 O OE1 . GLU A 1 182 ? -11.458 28.972 2.490   1.00 77.95  ? 163  GLU A OE1 1 
ATOM   1255 O OE2 . GLU A 1 182 ? -13.138 29.994 1.631   1.00 83.13  ? 163  GLU A OE2 1 
ATOM   1256 N N   . TYR A 1 183 ? -13.207 25.959 -2.021  1.00 44.13  ? 164  TYR A N   1 
ATOM   1257 C CA  . TYR A 1 183 ? -13.851 26.201 -3.271  1.00 38.97  ? 164  TYR A CA  1 
ATOM   1258 C C   . TYR A 1 183 ? -13.725 25.095 -4.267  1.00 32.42  ? 164  TYR A C   1 
ATOM   1259 O O   . TYR A 1 183 ? -13.989 25.295 -5.408  1.00 24.64  ? 164  TYR A O   1 
ATOM   1260 C CB  . TYR A 1 183 ? -13.312 27.447 -3.906  1.00 48.59  ? 164  TYR A CB  1 
ATOM   1261 C CG  . TYR A 1 183 ? -12.999 28.590 -3.014  1.00 44.83  ? 164  TYR A CG  1 
ATOM   1262 C CD1 . TYR A 1 183 ? -13.965 29.234 -2.301  1.00 49.35  ? 164  TYR A CD1 1 
ATOM   1263 C CD2 . TYR A 1 183 ? -11.746 29.058 -2.960  1.00 48.29  ? 164  TYR A CD2 1 
ATOM   1264 C CE1 . TYR A 1 183 ? -13.652 30.296 -1.506  1.00 59.59  ? 164  TYR A CE1 1 
ATOM   1265 C CE2 . TYR A 1 183 ? -11.420 30.120 -2.188  1.00 54.28  ? 164  TYR A CE2 1 
ATOM   1266 C CZ  . TYR A 1 183 ? -12.367 30.734 -1.470  1.00 69.47  ? 164  TYR A CZ  1 
ATOM   1267 O OH  . TYR A 1 183 ? -11.969 31.788 -0.716  1.00 77.87  ? 164  TYR A OH  1 
ATOM   1268 N N   . PHE A 1 184 ? -13.271 23.941 -3.843  1.00 33.68  ? 165  PHE A N   1 
ATOM   1269 C CA  . PHE A 1 184 ? -13.107 22.835 -4.748  1.00 35.47  ? 165  PHE A CA  1 
ATOM   1270 C C   . PHE A 1 184 ? -14.469 22.353 -5.162  1.00 35.58  ? 165  PHE A C   1 
ATOM   1271 O O   . PHE A 1 184 ? -15.386 22.388 -4.397  1.00 37.06  ? 165  PHE A O   1 
ATOM   1272 C CB  . PHE A 1 184 ? -12.270 21.747 -4.120  1.00 34.42  ? 165  PHE A CB  1 
ATOM   1273 C CG  . PHE A 1 184 ? -11.824 20.707 -5.060  1.00 30.51  ? 165  PHE A CG  1 
ATOM   1274 C CD1 . PHE A 1 184 ? -10.833 20.950 -5.943  1.00 30.27  ? 165  PHE A CD1 1 
ATOM   1275 C CD2 . PHE A 1 184 ? -12.358 19.477 -5.017  1.00 29.17  ? 165  PHE A CD2 1 
ATOM   1276 C CE1 . PHE A 1 184 ? -10.412 19.990 -6.801  1.00 30.04  ? 165  PHE A CE1 1 
ATOM   1277 C CE2 . PHE A 1 184 ? -11.951 18.514 -5.876  1.00 28.06  ? 165  PHE A CE2 1 
ATOM   1278 C CZ  . PHE A 1 184 ? -10.978 18.766 -6.771  1.00 26.61  ? 165  PHE A CZ  1 
ATOM   1279 N N   . SER A 1 185 ? -14.581 21.935 -6.403  1.00 31.75  ? 166  SER A N   1 
ATOM   1280 C CA  . SER A 1 185 ? -15.833 21.489 -6.989  1.00 31.00  ? 166  SER A CA  1 
ATOM   1281 C C   . SER A 1 185 ? -16.260 20.133 -6.432  1.00 33.79  ? 166  SER A C   1 
ATOM   1282 O O   . SER A 1 185 ? -15.486 19.166 -6.447  1.00 37.46  ? 166  SER A O   1 
ATOM   1283 C CB  . SER A 1 185 ? -15.692 21.406 -8.510  1.00 29.60  ? 166  SER A CB  1 
ATOM   1284 O OG  . SER A 1 185 ? -16.932 21.106 -9.120  1.00 31.93  ? 166  SER A OG  1 
ATOM   1285 N N   . GLN A 1 186 ? -17.498 20.064 -5.950  1.00 35.23  ? 167  GLN A N   1 
ATOM   1286 C CA  . GLN A 1 186 ? -18.083 18.796 -5.523  1.00 36.85  ? 167  GLN A CA  1 
ATOM   1287 C C   . GLN A 1 186 ? -18.331 17.857 -6.703  1.00 35.45  ? 167  GLN A C   1 
ATOM   1288 O O   . GLN A 1 186 ? -18.492 16.661 -6.500  1.00 42.89  ? 167  GLN A O   1 
ATOM   1289 C CB  . GLN A 1 186 ? -19.397 19.044 -4.786  1.00 32.86  ? 167  GLN A CB  1 
ATOM   1290 C CG  . GLN A 1 186 ? -20.204 20.176 -5.406  1.00 44.27  ? 167  GLN A CG  1 
ATOM   1291 C CD  . GLN A 1 186 ? -21.614 20.316 -4.840  1.00 64.01  ? 167  GLN A CD  1 
ATOM   1292 O OE1 . GLN A 1 186 ? -22.229 19.336 -4.379  1.00 75.84  ? 167  GLN A OE1 1 
ATOM   1293 N NE2 . GLN A 1 186 ? -22.141 21.547 -4.878  1.00 53.59  ? 167  GLN A NE2 1 
ATOM   1294 N N   . TYR A 1 187 ? -18.361 18.390 -7.925  1.00 25.14  ? 168  TYR A N   1 
ATOM   1295 C CA  . TYR A 1 187 ? -18.631 17.562 -9.097  1.00 27.45  ? 168  TYR A CA  1 
ATOM   1296 C C   . TYR A 1 187 ? -17.386 16.997 -9.795  1.00 24.55  ? 168  TYR A C   1 
ATOM   1297 O O   . TYR A 1 187 ? -17.505 16.225 -10.738 1.00 31.82  ? 168  TYR A O   1 
ATOM   1298 C CB  . TYR A 1 187 ? -19.542 18.306 -10.078 1.00 33.99  ? 168  TYR A CB  1 
ATOM   1299 C CG  . TYR A 1 187 ? -20.791 18.816 -9.406  1.00 36.80  ? 168  TYR A CG  1 
ATOM   1300 C CD1 . TYR A 1 187 ? -21.723 17.929 -8.897  1.00 36.19  ? 168  TYR A CD1 1 
ATOM   1301 C CD2 . TYR A 1 187 ? -21.039 20.181 -9.268  1.00 39.07  ? 168  TYR A CD2 1 
ATOM   1302 C CE1 . TYR A 1 187 ? -22.869 18.371 -8.260  1.00 37.93  ? 168  TYR A CE1 1 
ATOM   1303 C CE2 . TYR A 1 187 ? -22.195 20.642 -8.631  1.00 42.44  ? 168  TYR A CE2 1 
ATOM   1304 C CZ  . TYR A 1 187 ? -23.106 19.723 -8.133  1.00 44.95  ? 168  TYR A CZ  1 
ATOM   1305 O OH  . TYR A 1 187 ? -24.258 20.143 -7.504  1.00 47.57  ? 168  TYR A OH  1 
ATOM   1306 N N   . SER A 1 188 ? -16.197 17.367 -9.334  1.00 22.14  ? 169  SER A N   1 
ATOM   1307 C CA  . SER A 1 188 ? -14.971 16.745 -9.836  1.00 24.71  ? 169  SER A CA  1 
ATOM   1308 C C   . SER A 1 188 ? -14.968 15.224 -9.617  1.00 25.68  ? 169  SER A C   1 
ATOM   1309 O O   . SER A 1 188 ? -15.616 14.719 -8.693  1.00 27.66  ? 169  SER A O   1 
ATOM   1310 C CB  . SER A 1 188 ? -13.752 17.358 -9.142  1.00 28.82  ? 169  SER A CB  1 
ATOM   1311 O OG  . SER A 1 188 ? -12.543 16.859 -9.695  1.00 29.93  ? 169  SER A OG  1 
ATOM   1312 N N   . ARG A 1 189 ? -14.234 14.491 -10.451 1.00 25.73  ? 170  ARG A N   1 
ATOM   1313 C CA  . ARG A 1 189 ? -14.050 13.050 -10.216 1.00 24.16  ? 170  ARG A CA  1 
ATOM   1314 C C   . ARG A 1 189 ? -13.047 12.801 -9.105  1.00 28.43  ? 170  ARG A C   1 
ATOM   1315 O O   . ARG A 1 189 ? -12.769 11.652 -8.757  1.00 31.86  ? 170  ARG A O   1 
ATOM   1316 C CB  . ARG A 1 189 ? -13.586 12.306 -11.481 1.00 22.07  ? 170  ARG A CB  1 
ATOM   1317 C CG  . ARG A 1 189 ? -14.591 12.332 -12.623 1.00 37.30  ? 170  ARG A CG  1 
ATOM   1318 C CD  . ARG A 1 189 ? -14.658 11.011 -13.358 1.00 36.48  ? 170  ARG A CD  1 
ATOM   1319 N NE  . ARG A 1 189 ? -13.381 10.669 -13.978 1.00 45.43  ? 170  ARG A NE  1 
ATOM   1320 C CZ  . ARG A 1 189 ? -13.008 9.428  -14.271 1.00 52.32  ? 170  ARG A CZ  1 
ATOM   1321 N NH1 . ARG A 1 189 ? -13.811 8.408  -13.991 1.00 52.80  ? 170  ARG A NH1 1 
ATOM   1322 N NH2 . ARG A 1 189 ? -11.826 9.208  -14.833 1.00 56.70  ? 170  ARG A NH2 1 
ATOM   1323 N N   . PHE A 1 190 ? -12.477 13.874 -8.565  1.00 32.43  ? 171  PHE A N   1 
ATOM   1324 C CA  . PHE A 1 190 ? -11.396 13.729 -7.599  1.00 26.92  ? 171  PHE A CA  1 
ATOM   1325 C C   . PHE A 1 190 ? -11.705 14.517 -6.355  1.00 24.53  ? 171  PHE A C   1 
ATOM   1326 O O   . PHE A 1 190 ? -12.605 15.347 -6.356  1.00 30.17  ? 171  PHE A O   1 
ATOM   1327 C CB  . PHE A 1 190 ? -10.063 14.195 -8.186  1.00 27.45  ? 171  PHE A CB  1 
ATOM   1328 C CG  . PHE A 1 190 ? -9.702  13.530 -9.481  1.00 22.80  ? 171  PHE A CG  1 
ATOM   1329 C CD1 . PHE A 1 190 ? -10.218 13.996 -10.680 1.00 24.93  ? 171  PHE A CD1 1 
ATOM   1330 C CD2 . PHE A 1 190 ? -8.846  12.447 -9.501  1.00 26.05  ? 171  PHE A CD2 1 
ATOM   1331 C CE1 . PHE A 1 190 ? -9.891  13.388 -11.892 1.00 26.68  ? 171  PHE A CE1 1 
ATOM   1332 C CE2 . PHE A 1 190 ? -8.517  11.830 -10.701 1.00 26.61  ? 171  PHE A CE2 1 
ATOM   1333 C CZ  . PHE A 1 190 ? -9.040  12.311 -11.900 1.00 27.40  ? 171  PHE A CZ  1 
ATOM   1334 N N   . GLU A 1 191 ? -10.958 14.235 -5.291  1.00 35.69  ? 172  GLU A N   1 
ATOM   1335 C CA  . GLU A 1 191 ? -11.095 14.960 -4.029  1.00 38.57  ? 172  GLU A CA  1 
ATOM   1336 C C   . GLU A 1 191 ? -9.730  15.307 -3.421  1.00 35.30  ? 172  GLU A C   1 
ATOM   1337 O O   . GLU A 1 191 ? -8.734  14.589 -3.629  1.00 34.16  ? 172  GLU A O   1 
ATOM   1338 C CB  . GLU A 1 191 ? -11.961 14.171 -3.044  1.00 35.19  ? 172  GLU A CB  1 
ATOM   1339 C CG  . GLU A 1 191 ? -11.428 12.801 -2.672  1.00 35.13  ? 172  GLU A CG  1 
ATOM   1340 C CD  . GLU A 1 191 ? -12.422 12.036 -1.804  1.00 54.71  ? 172  GLU A CD  1 
ATOM   1341 O OE1 . GLU A 1 191 ? -13.406 12.677 -1.354  1.00 61.40  ? 172  GLU A OE1 1 
ATOM   1342 O OE2 . GLU A 1 191 ? -12.236 10.806 -1.583  1.00 57.22  ? 172  GLU A OE2 1 
ATOM   1343 N N   . ILE A 1 192 ? -9.681  16.415 -2.686  1.00 30.86  ? 173  ILE A N   1 
ATOM   1344 C CA  . ILE A 1 192 ? -8.417  16.866 -2.113  1.00 34.49  ? 173  ILE A CA  1 
ATOM   1345 C C   . ILE A 1 192 ? -8.280  16.312 -0.697  1.00 32.96  ? 173  ILE A C   1 
ATOM   1346 O O   . ILE A 1 192 ? -9.204  16.413 0.099   1.00 33.93  ? 173  ILE A O   1 
ATOM   1347 C CB  . ILE A 1 192 ? -8.282  18.414 -2.149  1.00 31.37  ? 173  ILE A CB  1 
ATOM   1348 C CG1 . ILE A 1 192 ? -8.327  18.915 -3.591  1.00 30.44  ? 173  ILE A CG1 1 
ATOM   1349 C CG2 . ILE A 1 192 ? -6.995  18.874 -1.487  1.00 32.10  ? 173  ILE A CG2 1 
ATOM   1350 C CD1 . ILE A 1 192 ? -8.306  20.424 -3.714  1.00 30.77  ? 173  ILE A CD1 1 
ATOM   1351 N N   . LEU A 1 193 ? -7.126  15.715 -0.408  1.00 37.21  ? 174  LEU A N   1 
ATOM   1352 C CA  . LEU A 1 193 ? -6.823  15.163 0.913   1.00 34.96  ? 174  LEU A CA  1 
ATOM   1353 C C   . LEU A 1 193 ? -6.060  16.168 1.750   1.00 35.69  ? 174  LEU A C   1 
ATOM   1354 O O   . LEU A 1 193 ? -6.331  16.308 2.945   1.00 44.29  ? 174  LEU A O   1 
ATOM   1355 C CB  . LEU A 1 193 ? -6.016  13.869 0.789   1.00 33.81  ? 174  LEU A CB  1 
ATOM   1356 C CG  . LEU A 1 193 ? -6.701  12.845 -0.119  1.00 31.97  ? 174  LEU A CG  1 
ATOM   1357 C CD1 . LEU A 1 193 ? -5.882  11.574 -0.280  1.00 30.83  ? 174  LEU A CD1 1 
ATOM   1358 C CD2 . LEU A 1 193 ? -8.112  12.537 0.388   1.00 35.00  ? 174  LEU A CD2 1 
ATOM   1359 N N   . ASP A 1 194 ? -5.114  16.867 1.120   1.00 34.15  ? 175  ASP A N   1 
ATOM   1360 C CA  . ASP A 1 194 ? -4.339  17.909 1.803   1.00 37.94  ? 175  ASP A CA  1 
ATOM   1361 C C   . ASP A 1 194 ? -3.563  18.848 0.861   1.00 32.72  ? 175  ASP A C   1 
ATOM   1362 O O   . ASP A 1 194 ? -3.160  18.458 -0.241  1.00 34.00  ? 175  ASP A O   1 
ATOM   1363 C CB  . ASP A 1 194 ? -3.368  17.263 2.796   1.00 41.92  ? 175  ASP A CB  1 
ATOM   1364 C CG  . ASP A 1 194 ? -2.912  18.225 3.870   1.00 57.24  ? 175  ASP A CG  1 
ATOM   1365 O OD1 . ASP A 1 194 ? -3.749  19.060 4.297   1.00 64.69  ? 175  ASP A OD1 1 
ATOM   1366 O OD2 . ASP A 1 194 ? -1.725  18.150 4.276   1.00 53.10  ? 175  ASP A OD2 1 
ATOM   1367 N N   . VAL A 1 195 ? -3.346  20.080 1.309   1.00 28.35  ? 176  VAL A N   1 
ATOM   1368 C CA  . VAL A 1 195 ? -2.514  21.021 0.571   1.00 30.62  ? 176  VAL A CA  1 
ATOM   1369 C C   . VAL A 1 195 ? -1.458  21.644 1.476   1.00 30.65  ? 176  VAL A C   1 
ATOM   1370 O O   . VAL A 1 195 ? -1.801  22.293 2.450   1.00 35.65  ? 176  VAL A O   1 
ATOM   1371 C CB  . VAL A 1 195 ? -3.340  22.163 -0.039  1.00 23.65  ? 176  VAL A CB  1 
ATOM   1372 C CG1 . VAL A 1 195 ? -2.415  23.147 -0.719  1.00 21.49  ? 176  VAL A CG1 1 
ATOM   1373 C CG2 . VAL A 1 195 ? -4.369  21.624 -1.020  1.00 29.52  ? 176  VAL A CG2 1 
ATOM   1374 N N   . THR A 1 196 ? -0.182  21.457 1.144   1.00 26.39  ? 177  THR A N   1 
ATOM   1375 C CA  . THR A 1 196 ? 0.914   22.074 1.896   1.00 26.35  ? 177  THR A CA  1 
ATOM   1376 C C   . THR A 1 196 ? 1.757   23.012 1.035   1.00 26.17  ? 177  THR A C   1 
ATOM   1377 O O   . THR A 1 196 ? 1.853   22.832 -0.175  1.00 28.89  ? 177  THR A O   1 
ATOM   1378 C CB  . THR A 1 196 ? 1.842   21.014 2.562   1.00 44.20  ? 177  THR A CB  1 
ATOM   1379 O OG1 . THR A 1 196 ? 2.449   20.173 1.563   1.00 34.37  ? 177  THR A OG1 1 
ATOM   1380 C CG2 . THR A 1 196 ? 1.065   20.151 3.555   1.00 44.91  ? 177  THR A CG2 1 
ATOM   1381 N N   . GLN A 1 197 ? 2.387   23.992 1.675   1.00 27.35  ? 178  GLN A N   1 
ATOM   1382 C CA  . GLN A 1 197 ? 3.170   25.008 0.978   1.00 25.12  ? 178  GLN A CA  1 
ATOM   1383 C C   . GLN A 1 197 ? 4.562   25.066 1.599   1.00 24.79  ? 178  GLN A C   1 
ATOM   1384 O O   . GLN A 1 197 ? 4.693   24.995 2.806   1.00 29.63  ? 178  GLN A O   1 
ATOM   1385 C CB  . GLN A 1 197 ? 2.479   26.391 1.092   1.00 23.69  ? 178  GLN A CB  1 
ATOM   1386 C CG  . GLN A 1 197 ? 1.017   26.416 0.596   1.00 38.97  ? 178  GLN A CG  1 
ATOM   1387 C CD  . GLN A 1 197 ? 0.544   27.799 0.105   1.00 56.60  ? 178  GLN A CD  1 
ATOM   1388 O OE1 . GLN A 1 197 ? 0.986   28.822 0.625   1.00 56.69  ? 178  GLN A OE1 1 
ATOM   1389 N NE2 . GLN A 1 197 ? -0.361  27.825 -0.910  1.00 52.82  ? 178  GLN A NE2 1 
ATOM   1390 N N   . LYS A 1 198 ? 5.613   25.187 0.799   1.00 25.06  ? 179  LYS A N   1 
ATOM   1391 C CA  . LYS A 1 198 ? 6.903   25.544 1.380   1.00 21.39  ? 179  LYS A CA  1 
ATOM   1392 C C   . LYS A 1 198 ? 7.705   26.429 0.435   1.00 24.85  ? 179  LYS A C   1 
ATOM   1393 O O   . LYS A 1 198 ? 7.480   26.412 -0.775  1.00 25.08  ? 179  LYS A O   1 
ATOM   1394 C CB  . LYS A 1 198 ? 7.697   24.306 1.773   1.00 23.43  ? 179  LYS A CB  1 
ATOM   1395 C CG  . LYS A 1 198 ? 8.594   23.781 0.675   1.00 31.57  ? 179  LYS A CG  1 
ATOM   1396 C CD  . LYS A 1 198 ? 9.448   22.618 1.164   1.00 35.21  ? 179  LYS A CD  1 
ATOM   1397 C CE  . LYS A 1 198 ? 10.175  21.929 0.002   1.00 40.58  ? 179  LYS A CE  1 
ATOM   1398 N NZ  . LYS A 1 198 ? 11.085  20.822 0.465   1.00 51.26  ? 179  LYS A NZ  1 
ATOM   1399 N N   . LYS A 1 199 ? 8.635   27.205 0.991   1.00 24.33  ? 180  LYS A N   1 
ATOM   1400 C CA  . LYS A 1 199 ? 9.436   28.131 0.194   1.00 23.20  ? 180  LYS A CA  1 
ATOM   1401 C C   . LYS A 1 199 ? 10.847  27.612 -0.130  1.00 27.25  ? 180  LYS A C   1 
ATOM   1402 O O   . LYS A 1 199 ? 11.530  27.108 0.744   1.00 29.54  ? 180  LYS A O   1 
ATOM   1403 C CB  . LYS A 1 199 ? 9.526   29.461 0.911   1.00 24.35  ? 180  LYS A CB  1 
ATOM   1404 C CG  . LYS A 1 199 ? 10.594  30.373 0.367   1.00 28.56  ? 180  LYS A CG  1 
ATOM   1405 C CD  . LYS A 1 199 ? 10.620  31.665 1.143   1.00 29.80  ? 180  LYS A CD  1 
ATOM   1406 C CE  . LYS A 1 199 ? 11.801  32.498 0.719   1.00 38.28  ? 180  LYS A CE  1 
ATOM   1407 N NZ  . LYS A 1 199 ? 11.755  33.864 1.327   1.00 56.74  ? 180  LYS A NZ  1 
ATOM   1408 N N   . ASN A 1 200 ? 11.272  27.729 -1.390  1.00 28.61  ? 181  ASN A N   1 
ATOM   1409 C CA  . ASN A 1 200 ? 12.632  27.350 -1.780  1.00 30.29  ? 181  ASN A CA  1 
ATOM   1410 C C   . ASN A 1 200 ? 13.488  28.508 -2.262  1.00 31.12  ? 181  ASN A C   1 
ATOM   1411 O O   . ASN A 1 200 ? 12.973  29.494 -2.777  1.00 31.21  ? 181  ASN A O   1 
ATOM   1412 C CB  . ASN A 1 200 ? 12.634  26.266 -2.854  1.00 32.34  ? 181  ASN A CB  1 
ATOM   1413 C CG  . ASN A 1 200 ? 11.766  25.091 -2.495  1.00 40.61  ? 181  ASN A CG  1 
ATOM   1414 O OD1 . ASN A 1 200 ? 12.123  24.269 -1.645  1.00 41.80  ? 181  ASN A OD1 1 
ATOM   1415 N ND2 . ASN A 1 200 ? 10.612  24.991 -3.161  1.00 42.79  ? 181  ASN A ND2 1 
ATOM   1416 N N   . SER A 1 201 ? 14.800  28.380 -2.080  1.00 35.05  ? 182  SER A N   1 
ATOM   1417 C CA  . SER A 1 201 ? 15.751  29.362 -2.583  1.00 35.34  ? 182  SER A CA  1 
ATOM   1418 C C   . SER A 1 201 ? 16.820  28.601 -3.353  1.00 33.02  ? 182  SER A C   1 
ATOM   1419 O O   . SER A 1 201 ? 17.582  27.844 -2.767  1.00 33.13  ? 182  SER A O   1 
ATOM   1420 C CB  . SER A 1 201 ? 16.369  30.143 -1.426  1.00 31.01  ? 182  SER A CB  1 
ATOM   1421 O OG  . SER A 1 201 ? 17.008  31.308 -1.901  1.00 35.49  ? 182  SER A OG  1 
ATOM   1422 N N   . VAL A 1 202 ? 16.847  28.788 -4.668  1.00 35.80  ? 183  VAL A N   1 
ATOM   1423 C CA  . VAL A 1 202 ? 17.633  27.960 -5.580  1.00 30.53  ? 183  VAL A CA  1 
ATOM   1424 C C   . VAL A 1 202 ? 18.672  28.804 -6.312  1.00 37.97  ? 183  VAL A C   1 
ATOM   1425 O O   . VAL A 1 202 ? 18.392  29.941 -6.736  1.00 38.99  ? 183  VAL A O   1 
ATOM   1426 C CB  . VAL A 1 202 ? 16.700  27.301 -6.628  1.00 34.61  ? 183  VAL A CB  1 
ATOM   1427 C CG1 . VAL A 1 202 ? 17.486  26.479 -7.633  1.00 38.87  ? 183  VAL A CG1 1 
ATOM   1428 C CG2 . VAL A 1 202 ? 15.653  26.461 -5.943  1.00 36.26  ? 183  VAL A CG2 1 
ATOM   1429 N N   . THR A 1 203 ? 19.876  28.254 -6.460  1.00 45.75  ? 184  THR A N   1 
ATOM   1430 C CA  . THR A 1 203 ? 20.881  28.865 -7.338  1.00 52.36  ? 184  THR A CA  1 
ATOM   1431 C C   . THR A 1 203 ? 21.035  28.096 -8.665  1.00 54.09  ? 184  THR A C   1 
ATOM   1432 O O   . THR A 1 203 ? 21.369  26.912 -8.668  1.00 60.39  ? 184  THR A O   1 
ATOM   1433 C CB  . THR A 1 203 ? 22.246  29.010 -6.637  1.00 44.54  ? 184  THR A CB  1 
ATOM   1434 O OG1 . THR A 1 203 ? 22.141  29.962 -5.559  1.00 39.82  ? 184  THR A OG1 1 
ATOM   1435 C CG2 . THR A 1 203 ? 23.297  29.470 -7.635  1.00 45.84  ? 184  THR A CG2 1 
ATOM   1436 N N   . TYR A 1 204 ? 20.780  28.768 -9.785  1.00 53.77  ? 185  TYR A N   1 
ATOM   1437 C CA  . TYR A 1 204 ? 20.905  28.130 -11.093 1.00 67.26  ? 185  TYR A CA  1 
ATOM   1438 C C   . TYR A 1 204 ? 22.316  28.277 -11.685 1.00 80.70  ? 185  TYR A C   1 
ATOM   1439 O O   . TYR A 1 204 ? 23.101  29.135 -11.259 1.00 74.04  ? 185  TYR A O   1 
ATOM   1440 C CB  . TYR A 1 204 ? 19.843  28.660 -12.063 1.00 64.43  ? 185  TYR A CB  1 
ATOM   1441 C CG  . TYR A 1 204 ? 18.436  28.358 -11.618 1.00 54.89  ? 185  TYR A CG  1 
ATOM   1442 C CD1 . TYR A 1 204 ? 17.761  29.218 -10.761 1.00 48.53  ? 185  TYR A CD1 1 
ATOM   1443 C CD2 . TYR A 1 204 ? 17.780  27.213 -12.050 1.00 53.67  ? 185  TYR A CD2 1 
ATOM   1444 C CE1 . TYR A 1 204 ? 16.470  28.950 -10.341 1.00 45.80  ? 185  TYR A CE1 1 
ATOM   1445 C CE2 . TYR A 1 204 ? 16.477  26.932 -11.640 1.00 53.78  ? 185  TYR A CE2 1 
ATOM   1446 C CZ  . TYR A 1 204 ? 15.824  27.805 -10.785 1.00 52.82  ? 185  TYR A CZ  1 
ATOM   1447 O OH  . TYR A 1 204 ? 14.531  27.533 -10.362 1.00 45.69  ? 185  TYR A OH  1 
ATOM   1448 N N   . SER A 1 205 ? 22.619  27.429 -12.670 1.00 89.27  ? 186  SER A N   1 
ATOM   1449 C CA  . SER A 1 205 ? 23.941  27.367 -13.295 1.00 88.05  ? 186  SER A CA  1 
ATOM   1450 C C   . SER A 1 205 ? 24.328  28.651 -14.039 1.00 79.71  ? 186  SER A C   1 
ATOM   1451 O O   . SER A 1 205 ? 25.500  28.890 -14.310 1.00 84.18  ? 186  SER A O   1 
ATOM   1452 C CB  . SER A 1 205 ? 24.015  26.160 -14.239 1.00 78.73  ? 186  SER A CB  1 
ATOM   1453 O OG  . SER A 1 205 ? 23.842  24.957 -13.517 1.00 72.09  ? 186  SER A OG  1 
ATOM   1454 N N   . CYS A 1 206 ? 23.342  29.478 -14.354 1.00 74.73  ? 187  CYS A N   1 
ATOM   1455 C CA  . CYS A 1 206 ? 23.588  30.674 -15.141 1.00 80.68  ? 187  CYS A CA  1 
ATOM   1456 C C   . CYS A 1 206 ? 24.182  31.826 -14.311 1.00 85.64  ? 187  CYS A C   1 
ATOM   1457 O O   . CYS A 1 206 ? 25.112  32.492 -14.764 1.00 79.28  ? 187  CYS A O   1 
ATOM   1458 C CB  . CYS A 1 206 ? 22.298  31.121 -15.852 1.00 88.00  ? 187  CYS A CB  1 
ATOM   1459 S SG  . CYS A 1 206 ? 21.117  32.081 -14.805 1.00 107.43 ? 187  CYS A SG  1 
ATOM   1460 N N   . CYS A 1 207 ? 23.657  32.045 -13.102 1.00 88.94  ? 188  CYS A N   1 
ATOM   1461 C CA  . CYS A 1 207 ? 23.939  33.261 -12.314 1.00 82.41  ? 188  CYS A CA  1 
ATOM   1462 C C   . CYS A 1 207 ? 24.322  32.941 -10.852 1.00 78.57  ? 188  CYS A C   1 
ATOM   1463 O O   . CYS A 1 207 ? 23.925  31.902 -10.316 1.00 80.82  ? 188  CYS A O   1 
ATOM   1464 C CB  . CYS A 1 207 ? 22.718  34.206 -12.361 1.00 68.89  ? 188  CYS A CB  1 
ATOM   1465 S SG  . CYS A 1 207 ? 21.439  33.703 -13.587 1.00 95.82  ? 188  CYS A SG  1 
ATOM   1466 N N   . PRO A 1 208 ? 25.093  33.835 -10.201 1.00 73.19  ? 189  PRO A N   1 
ATOM   1467 C CA  . PRO A 1 208 ? 25.514  33.660 -8.799  1.00 60.15  ? 189  PRO A CA  1 
ATOM   1468 C C   . PRO A 1 208 ? 24.443  34.079 -7.776  1.00 60.90  ? 189  PRO A C   1 
ATOM   1469 O O   . PRO A 1 208 ? 24.650  33.936 -6.578  1.00 66.31  ? 189  PRO A O   1 
ATOM   1470 C CB  . PRO A 1 208 ? 26.703  34.614 -8.685  1.00 65.35  ? 189  PRO A CB  1 
ATOM   1471 C CG  . PRO A 1 208 ? 26.338  35.738 -9.609  1.00 75.29  ? 189  PRO A CG  1 
ATOM   1472 C CD  . PRO A 1 208 ? 25.641  35.076 -10.785 1.00 77.50  ? 189  PRO A CD  1 
ATOM   1473 N N   . GLU A 1 209 ? 23.321  34.601 -8.254  1.00 58.25  ? 190  GLU A N   1 
ATOM   1474 C CA  . GLU A 1 209 ? 22.235  35.059 -7.400  1.00 47.60  ? 190  GLU A CA  1 
ATOM   1475 C C   . GLU A 1 209 ? 21.222  33.944 -7.137  1.00 41.56  ? 190  GLU A C   1 
ATOM   1476 O O   . GLU A 1 209 ? 21.114  32.996 -7.917  1.00 47.43  ? 190  GLU A O   1 
ATOM   1477 C CB  . GLU A 1 209 ? 21.524  36.212 -8.101  1.00 61.41  ? 190  GLU A CB  1 
ATOM   1478 C CG  . GLU A 1 209 ? 22.469  37.226 -8.742  1.00 62.63  ? 190  GLU A CG  1 
ATOM   1479 C CD  . GLU A 1 209 ? 23.054  38.185 -7.720  1.00 73.10  ? 190  GLU A CD  1 
ATOM   1480 O OE1 . GLU A 1 209 ? 22.746  38.018 -6.511  1.00 72.31  ? 190  GLU A OE1 1 
ATOM   1481 O OE2 . GLU A 1 209 ? 23.810  39.103 -8.122  1.00 73.99  ? 190  GLU A OE2 1 
ATOM   1482 N N   . ALA A 1 210 ? 20.473  34.059 -6.046  1.00 35.74  ? 191  ALA A N   1 
ATOM   1483 C CA  . ALA A 1 210 ? 19.483  33.045 -5.694  1.00 32.52  ? 191  ALA A CA  1 
ATOM   1484 C C   . ALA A 1 210 ? 18.116  33.462 -6.194  1.00 31.01  ? 191  ALA A C   1 
ATOM   1485 O O   . ALA A 1 210 ? 17.791  34.654 -6.180  1.00 27.43  ? 191  ALA A O   1 
ATOM   1486 C CB  . ALA A 1 210 ? 19.447  32.851 -4.203  1.00 24.47  ? 191  ALA A CB  1 
ATOM   1487 N N   . TYR A 1 211 ? 17.314  32.484 -6.620  1.00 24.20  ? 192  TYR A N   1 
ATOM   1488 C CA  . TYR A 1 211 ? 15.943  32.759 -7.060  1.00 26.29  ? 192  TYR A CA  1 
ATOM   1489 C C   . TYR A 1 211 ? 14.941  32.072 -6.157  1.00 24.86  ? 192  TYR A C   1 
ATOM   1490 O O   . TYR A 1 211 ? 14.955  30.858 -6.044  1.00 28.54  ? 192  TYR A O   1 
ATOM   1491 C CB  . TYR A 1 211 ? 15.730  32.332 -8.521  1.00 27.11  ? 192  TYR A CB  1 
ATOM   1492 C CG  . TYR A 1 211 ? 16.460  33.212 -9.502  1.00 25.60  ? 192  TYR A CG  1 
ATOM   1493 C CD1 . TYR A 1 211 ? 17.828  33.077 -9.689  1.00 29.63  ? 192  TYR A CD1 1 
ATOM   1494 C CD2 . TYR A 1 211 ? 15.788  34.194 -10.231 1.00 29.19  ? 192  TYR A CD2 1 
ATOM   1495 C CE1 . TYR A 1 211 ? 18.519  33.894 -10.577 1.00 40.58  ? 192  TYR A CE1 1 
ATOM   1496 C CE2 . TYR A 1 211 ? 16.471  35.025 -11.130 1.00 32.04  ? 192  TYR A CE2 1 
ATOM   1497 C CZ  . TYR A 1 211 ? 17.838  34.863 -11.299 1.00 39.41  ? 192  TYR A CZ  1 
ATOM   1498 O OH  . TYR A 1 211 ? 18.538  35.660 -12.178 1.00 45.92  ? 192  TYR A OH  1 
ATOM   1499 N N   . GLU A 1 212 ? 14.061  32.841 -5.522  1.00 24.68  ? 193  GLU A N   1 
ATOM   1500 C CA  . GLU A 1 212 ? 13.031  32.245 -4.672  1.00 23.94  ? 193  GLU A CA  1 
ATOM   1501 C C   . GLU A 1 212 ? 11.833  31.678 -5.460  1.00 20.64  ? 193  GLU A C   1 
ATOM   1502 O O   . GLU A 1 212 ? 11.416  32.237 -6.477  1.00 25.00  ? 193  GLU A O   1 
ATOM   1503 C CB  . GLU A 1 212 ? 12.553  33.253 -3.622  1.00 21.49  ? 193  GLU A CB  1 
ATOM   1504 C CG  . GLU A 1 212 ? 13.655  33.786 -2.739  1.00 27.48  ? 193  GLU A CG  1 
ATOM   1505 C CD  . GLU A 1 212 ? 13.133  34.644 -1.589  1.00 36.68  ? 193  GLU A CD  1 
ATOM   1506 O OE1 . GLU A 1 212 ? 11.905  34.795 -1.477  1.00 41.62  ? 193  GLU A OE1 1 
ATOM   1507 O OE2 . GLU A 1 212 ? 13.946  35.172 -0.793  1.00 48.40  ? 193  GLU A OE2 1 
ATOM   1508 N N   . ASP A 1 213 ? 11.287  30.572 -4.971  1.00 18.79  ? 194  ASP A N   1 
ATOM   1509 C CA  . ASP A 1 213 ? 10.006  30.051 -5.445  1.00 19.60  ? 194  ASP A CA  1 
ATOM   1510 C C   . ASP A 1 213 ? 9.164   29.442 -4.319  1.00 24.25  ? 194  ASP A C   1 
ATOM   1511 O O   . ASP A 1 213 ? 9.658   29.162 -3.220  1.00 26.33  ? 194  ASP A O   1 
ATOM   1512 C CB  . ASP A 1 213 ? 10.205  29.007 -6.529  1.00 22.81  ? 194  ASP A CB  1 
ATOM   1513 C CG  . ASP A 1 213 ? 11.125  27.869 -6.083  1.00 50.37  ? 194  ASP A CG  1 
ATOM   1514 O OD1 . ASP A 1 213 ? 10.634  26.906 -5.418  1.00 48.39  ? 194  ASP A OD1 1 
ATOM   1515 O OD2 . ASP A 1 213 ? 12.345  27.940 -6.406  1.00 57.80  ? 194  ASP A OD2 1 
ATOM   1516 N N   . VAL A 1 214 ? 7.881   29.247 -4.609  1.00 24.88  ? 195  VAL A N   1 
ATOM   1517 C CA  . VAL A 1 214 ? 6.980   28.542 -3.707  1.00 27.38  ? 195  VAL A CA  1 
ATOM   1518 C C   . VAL A 1 214 ? 6.561   27.203 -4.305  1.00 24.01  ? 195  VAL A C   1 
ATOM   1519 O O   . VAL A 1 214 ? 6.187   27.132 -5.479  1.00 23.18  ? 195  VAL A O   1 
ATOM   1520 C CB  . VAL A 1 214 ? 5.749   29.388 -3.370  1.00 18.70  ? 195  VAL A CB  1 
ATOM   1521 C CG1 . VAL A 1 214 ? 4.755   28.577 -2.565  1.00 20.97  ? 195  VAL A CG1 1 
ATOM   1522 C CG2 . VAL A 1 214 ? 6.184   30.600 -2.583  1.00 25.54  ? 195  VAL A CG2 1 
ATOM   1523 N N   . GLU A 1 215 ? 6.665   26.145 -3.500  1.00 24.49  ? 196  GLU A N   1 
ATOM   1524 C CA  . GLU A 1 215 ? 6.306   24.798 -3.930  1.00 29.30  ? 196  GLU A CA  1 
ATOM   1525 C C   . GLU A 1 215 ? 5.005   24.438 -3.243  1.00 28.71  ? 196  GLU A C   1 
ATOM   1526 O O   . GLU A 1 215 ? 4.917   24.459 -2.007  1.00 28.52  ? 196  GLU A O   1 
ATOM   1527 C CB  . GLU A 1 215 ? 7.393   23.792 -3.534  1.00 37.47  ? 196  GLU A CB  1 
ATOM   1528 C CG  . GLU A 1 215 ? 7.843   22.860 -4.649  1.00 45.44  ? 196  GLU A CG  1 
ATOM   1529 C CD  . GLU A 1 215 ? 9.004   21.933 -4.232  1.00 70.92  ? 196  GLU A CD  1 
ATOM   1530 O OE1 . GLU A 1 215 ? 8.907   21.287 -3.154  1.00 61.52  ? 196  GLU A OE1 1 
ATOM   1531 O OE2 . GLU A 1 215 ? 10.010  21.853 -4.991  1.00 78.47  ? 196  GLU A OE2 1 
ATOM   1532 N N   . VAL A 1 216 ? 3.985   24.125 -4.035  1.00 26.71  ? 197  VAL A N   1 
ATOM   1533 C CA  . VAL A 1 216 ? 2.682   23.781 -3.473  1.00 27.09  ? 197  VAL A CA  1 
ATOM   1534 C C   . VAL A 1 216 ? 2.379   22.311 -3.691  1.00 24.39  ? 197  VAL A C   1 
ATOM   1535 O O   . VAL A 1 216 ? 2.264   21.874 -4.827  1.00 27.05  ? 197  VAL A O   1 
ATOM   1536 C CB  . VAL A 1 216 ? 1.556   24.642 -4.061  1.00 24.62  ? 197  VAL A CB  1 
ATOM   1537 C CG1 . VAL A 1 216 ? 0.224   24.160 -3.538  1.00 20.89  ? 197  VAL A CG1 1 
ATOM   1538 C CG2 . VAL A 1 216 ? 1.768   26.118 -3.695  1.00 20.98  ? 197  VAL A CG2 1 
ATOM   1539 N N   . SER A 1 217 ? 2.272   21.553 -2.599  1.00 28.36  ? 198  SER A N   1 
ATOM   1540 C CA  . SER A 1 217 ? 2.032   20.103 -2.670  1.00 30.17  ? 198  SER A CA  1 
ATOM   1541 C C   . SER A 1 217 ? 0.547   19.763 -2.557  1.00 27.31  ? 198  SER A C   1 
ATOM   1542 O O   . SER A 1 217 ? -0.107  20.052 -1.548  1.00 25.18  ? 198  SER A O   1 
ATOM   1543 C CB  . SER A 1 217 ? 2.820   19.361 -1.593  1.00 25.58  ? 198  SER A CB  1 
ATOM   1544 O OG  . SER A 1 217 ? 4.194   19.694 -1.669  1.00 30.96  ? 198  SER A OG  1 
ATOM   1545 N N   . LEU A 1 218 ? 0.019   19.147 -3.603  1.00 21.78  ? 199  LEU A N   1 
ATOM   1546 C CA  . LEU A 1 218 ? -1.400  18.869 -3.663  1.00 23.88  ? 199  LEU A CA  1 
ATOM   1547 C C   . LEU A 1 218 ? -1.632  17.379 -3.533  1.00 28.20  ? 199  LEU A C   1 
ATOM   1548 O O   . LEU A 1 218 ? -1.302  16.601 -4.438  1.00 33.18  ? 199  LEU A O   1 
ATOM   1549 C CB  . LEU A 1 218 ? -1.978  19.389 -4.978  1.00 24.93  ? 199  LEU A CB  1 
ATOM   1550 C CG  . LEU A 1 218 ? -3.384  18.888 -5.281  1.00 21.63  ? 199  LEU A CG  1 
ATOM   1551 C CD1 . LEU A 1 218 ? -4.346  19.388 -4.222  1.00 24.82  ? 199  LEU A CD1 1 
ATOM   1552 C CD2 . LEU A 1 218 ? -3.816  19.314 -6.673  1.00 23.75  ? 199  LEU A CD2 1 
ATOM   1553 N N   . ASN A 1 219 ? -2.192  16.968 -2.404  1.00 25.96  ? 200  ASN A N   1 
ATOM   1554 C CA  . ASN A 1 219 ? -2.471  15.548 -2.202  1.00 32.84  ? 200  ASN A CA  1 
ATOM   1555 C C   . ASN A 1 219 ? -3.933  15.220 -2.532  1.00 25.77  ? 200  ASN A C   1 
ATOM   1556 O O   . ASN A 1 219 ? -4.847  15.727 -1.885  1.00 31.75  ? 200  ASN A O   1 
ATOM   1557 C CB  . ASN A 1 219 ? -2.088  15.139 -0.777  1.00 34.77  ? 200  ASN A CB  1 
ATOM   1558 C CG  . ASN A 1 219 ? -2.256  13.651 -0.532  1.00 38.45  ? 200  ASN A CG  1 
ATOM   1559 O OD1 . ASN A 1 219 ? -2.759  13.240 0.522   1.00 48.50  ? 200  ASN A OD1 1 
ATOM   1560 N ND2 . ASN A 1 219 ? -1.845  12.831 -1.508  1.00 32.19  ? 200  ASN A ND2 1 
ATOM   1561 N N   . PHE A 1 220 ? -4.156  14.406 -3.558  1.00 19.59  ? 201  PHE A N   1 
ATOM   1562 C CA  . PHE A 1 220 ? -5.522  14.153 -4.045  1.00 23.54  ? 201  PHE A CA  1 
ATOM   1563 C C   . PHE A 1 220 ? -5.684  12.733 -4.553  1.00 25.01  ? 201  PHE A C   1 
ATOM   1564 O O   . PHE A 1 220 ? -4.704  12.072 -4.892  1.00 28.31  ? 201  PHE A O   1 
ATOM   1565 C CB  . PHE A 1 220 ? -5.865  15.103 -5.185  1.00 22.63  ? 201  PHE A CB  1 
ATOM   1566 C CG  . PHE A 1 220 ? -5.137  14.797 -6.464  1.00 21.02  ? 201  PHE A CG  1 
ATOM   1567 C CD1 . PHE A 1 220 ? -3.756  14.972 -6.558  1.00 26.96  ? 201  PHE A CD1 1 
ATOM   1568 C CD2 . PHE A 1 220 ? -5.828  14.338 -7.581  1.00 23.09  ? 201  PHE A CD2 1 
ATOM   1569 C CE1 . PHE A 1 220 ? -3.072  14.681 -7.749  1.00 30.38  ? 201  PHE A CE1 1 
ATOM   1570 C CE2 . PHE A 1 220 ? -5.154  14.049 -8.786  1.00 23.17  ? 201  PHE A CE2 1 
ATOM   1571 C CZ  . PHE A 1 220 ? -3.779  14.213 -8.867  1.00 24.41  ? 201  PHE A CZ  1 
ATOM   1572 N N   . ARG A 1 221 ? -6.922  12.261 -4.620  1.00 27.09  ? 202  ARG A N   1 
ATOM   1573 C CA  . ARG A 1 221 ? -7.197  10.933 -5.198  1.00 32.07  ? 202  ARG A CA  1 
ATOM   1574 C C   . ARG A 1 221 ? -8.528  10.891 -5.933  1.00 34.66  ? 202  ARG A C   1 
ATOM   1575 O O   . ARG A 1 221 ? -9.346  11.811 -5.817  1.00 34.85  ? 202  ARG A O   1 
ATOM   1576 C CB  . ARG A 1 221 ? -7.202  9.843  -4.124  1.00 37.15  ? 202  ARG A CB  1 
ATOM   1577 C CG  . ARG A 1 221 ? -8.262  10.068 -3.062  1.00 37.86  ? 202  ARG A CG  1 
ATOM   1578 C CD  . ARG A 1 221 ? -8.808  8.769  -2.499  1.00 38.65  ? 202  ARG A CD  1 
ATOM   1579 N NE  . ARG A 1 221 ? -9.809  9.054  -1.474  1.00 47.47  ? 202  ARG A NE  1 
ATOM   1580 C CZ  . ARG A 1 221 ? -9.594  8.951  -0.168  1.00 42.63  ? 202  ARG A CZ  1 
ATOM   1581 N NH1 . ARG A 1 221 ? -8.415  8.528  0.273   1.00 35.85  ? 202  ARG A NH1 1 
ATOM   1582 N NH2 . ARG A 1 221 ? -10.562 9.258  0.691   1.00 38.29  ? 202  ARG A NH2 1 
ATOM   1583 N N   . LYS A 1 222 ? -8.741  9.807  -6.678  1.00 37.25  ? 203  LYS A N   1 
ATOM   1584 C CA  . LYS A 1 222 ? -10.022 9.545  -7.334  1.00 33.23  ? 203  LYS A CA  1 
ATOM   1585 C C   . LYS A 1 222 ? -11.085 9.137  -6.309  1.00 36.72  ? 203  LYS A C   1 
ATOM   1586 O O   . LYS A 1 222 ? -10.791 8.428  -5.347  1.00 41.59  ? 203  LYS A O   1 
ATOM   1587 C CB  . LYS A 1 222 ? -9.857  8.440  -8.362  1.00 32.91  ? 203  LYS A CB  1 
ATOM   1588 C CG  . LYS A 1 222 ? -11.090 8.194  -9.206  1.00 40.40  ? 203  LYS A CG  1 
ATOM   1589 C CD  . LYS A 1 222 ? -10.777 7.160  -10.277 1.00 49.08  ? 203  LYS A CD  1 
ATOM   1590 C CE  . LYS A 1 222 ? -11.963 6.903  -11.184 1.00 60.76  ? 203  LYS A CE  1 
ATOM   1591 N NZ  . LYS A 1 222 ? -11.618 5.862  -12.195 1.00 67.17  ? 203  LYS A NZ  1 
ATOM   1592 N N   . LYS A 1 223 ? -12.312 9.602  -6.506  1.00 33.63  ? 204  LYS A N   1 
ATOM   1593 C CA  . LYS A 1 223 ? -13.409 9.281  -5.599  1.00 40.89  ? 204  LYS A CA  1 
ATOM   1594 C C   . LYS A 1 223 ? -13.887 7.822  -5.733  1.00 50.14  ? 204  LYS A C   1 
ATOM   1595 O O   . LYS A 1 223 ? -13.782 7.207  -6.800  1.00 51.92  ? 204  LYS A O   1 
ATOM   1596 C CB  . LYS A 1 223 ? -14.584 10.213 -5.864  1.00 41.27  ? 204  LYS A CB  1 
ATOM   1597 C CG  . LYS A 1 223 ? -14.443 11.623 -5.326  1.00 35.66  ? 204  LYS A CG  1 
ATOM   1598 C CD  . LYS A 1 223 ? -15.579 12.482 -5.895  1.00 41.10  ? 204  LYS A CD  1 
ATOM   1599 C CE  . LYS A 1 223 ? -15.862 13.719 -5.061  1.00 41.56  ? 204  LYS A CE  1 
ATOM   1600 N NZ  . LYS A 1 223 ? -17.120 14.390 -5.500  1.00 41.47  ? 204  LYS A NZ  1 
ATOM   1601 N N   . LEU B 1 20  ? 21.330  57.600 -11.500 1.00 52.19  ? 1    LEU B N   1 
ATOM   1602 C CA  . LEU B 1 20  ? 20.339  56.830 -12.249 1.00 37.32  ? 1    LEU B CA  1 
ATOM   1603 C C   . LEU B 1 20  ? 19.658  55.772 -11.396 1.00 38.59  ? 1    LEU B C   1 
ATOM   1604 O O   . LEU B 1 20  ? 20.327  55.010 -10.696 1.00 45.73  ? 1    LEU B O   1 
ATOM   1605 C CB  . LEU B 1 20  ? 21.003  56.125 -13.418 1.00 37.76  ? 1    LEU B CB  1 
ATOM   1606 C CG  . LEU B 1 20  ? 21.365  56.970 -14.630 1.00 33.92  ? 1    LEU B CG  1 
ATOM   1607 C CD1 . LEU B 1 20  ? 21.828  56.036 -15.732 1.00 33.53  ? 1    LEU B CD1 1 
ATOM   1608 C CD2 . LEU B 1 20  ? 20.184  57.812 -15.078 1.00 29.38  ? 1    LEU B CD2 1 
ATOM   1609 N N   . ASP B 1 21  ? 18.331  55.719 -11.453 1.00 33.91  ? 2    ASP B N   1 
ATOM   1610 C CA  . ASP B 1 21  ? 17.604  54.621 -10.824 1.00 35.10  ? 2    ASP B CA  1 
ATOM   1611 C C   . ASP B 1 21  ? 16.964  53.789 -11.917 1.00 34.24  ? 2    ASP B C   1 
ATOM   1612 O O   . ASP B 1 21  ? 17.048  54.156 -13.099 1.00 28.55  ? 2    ASP B O   1 
ATOM   1613 C CB  . ASP B 1 21  ? 16.559  55.125 -9.819  1.00 43.16  ? 2    ASP B CB  1 
ATOM   1614 C CG  . ASP B 1 21  ? 15.737  56.300 -10.351 1.00 52.12  ? 2    ASP B CG  1 
ATOM   1615 O OD1 . ASP B 1 21  ? 15.399  56.291 -11.557 1.00 51.14  ? 2    ASP B OD1 1 
ATOM   1616 O OD2 . ASP B 1 21  ? 15.428  57.234 -9.563  1.00 65.32  ? 2    ASP B OD2 1 
ATOM   1617 N N   . ARG B 1 22  ? 16.343  52.673 -11.530 1.00 32.20  ? 3    ARG B N   1 
ATOM   1618 C CA  . ARG B 1 22  ? 15.705  51.792 -12.508 1.00 31.82  ? 3    ARG B CA  1 
ATOM   1619 C C   . ARG B 1 22  ? 14.706  52.530 -13.381 1.00 26.42  ? 3    ARG B C   1 
ATOM   1620 O O   . ARG B 1 22  ? 14.662  52.302 -14.593 1.00 23.20  ? 3    ARG B O   1 
ATOM   1621 C CB  . ARG B 1 22  ? 15.027  50.593 -11.846 1.00 30.55  ? 3    ARG B CB  1 
ATOM   1622 C CG  . ARG B 1 22  ? 15.973  49.496 -11.440 1.00 29.14  ? 3    ARG B CG  1 
ATOM   1623 C CD  . ARG B 1 22  ? 15.217  48.376 -10.778 1.00 32.99  ? 3    ARG B CD  1 
ATOM   1624 N NE  . ARG B 1 22  ? 16.131  47.311 -10.407 1.00 41.44  ? 3    ARG B NE  1 
ATOM   1625 C CZ  . ARG B 1 22  ? 16.813  47.297 -9.272  1.00 50.53  ? 3    ARG B CZ  1 
ATOM   1626 N NH1 . ARG B 1 22  ? 16.669  48.291 -8.397  1.00 49.20  ? 3    ARG B NH1 1 
ATOM   1627 N NH2 . ARG B 1 22  ? 17.636  46.291 -9.013  1.00 60.07  ? 3    ARG B NH2 1 
ATOM   1628 N N   . ALA B 1 23  ? 13.920  53.414 -12.767 1.00 26.31  ? 4    ALA B N   1 
ATOM   1629 C CA  . ALA B 1 23  ? 12.895  54.152 -13.501 1.00 23.11  ? 4    ALA B CA  1 
ATOM   1630 C C   . ALA B 1 23  ? 13.511  54.956 -14.655 1.00 28.93  ? 4    ALA B C   1 
ATOM   1631 O O   . ALA B 1 23  ? 13.008  54.946 -15.788 1.00 22.90  ? 4    ALA B O   1 
ATOM   1632 C CB  . ALA B 1 23  ? 12.125  55.046 -12.570 1.00 20.48  ? 4    ALA B CB  1 
ATOM   1633 N N   . ASP B 1 24  ? 14.618  55.630 -14.356 1.00 31.73  ? 5    ASP B N   1 
ATOM   1634 C CA  . ASP B 1 24  ? 15.359  56.407 -15.346 1.00 32.57  ? 5    ASP B CA  1 
ATOM   1635 C C   . ASP B 1 24  ? 15.935  55.558 -16.517 1.00 30.57  ? 5    ASP B C   1 
ATOM   1636 O O   . ASP B 1 24  ? 15.792  55.915 -17.699 1.00 25.49  ? 5    ASP B O   1 
ATOM   1637 C CB  . ASP B 1 24  ? 16.467  57.213 -14.641 1.00 36.39  ? 5    ASP B CB  1 
ATOM   1638 C CG  . ASP B 1 24  ? 15.914  58.389 -13.811 1.00 51.15  ? 5    ASP B CG  1 
ATOM   1639 O OD1 . ASP B 1 24  ? 14.862  58.954 -14.199 1.00 55.21  ? 5    ASP B OD1 1 
ATOM   1640 O OD2 . ASP B 1 24  ? 16.534  58.754 -12.777 1.00 49.32  ? 5    ASP B OD2 1 
ATOM   1641 N N   . ILE B 1 25  ? 16.569  54.436 -16.180 1.00 26.83  ? 6    ILE B N   1 
ATOM   1642 C CA  . ILE B 1 25  ? 17.155  53.548 -17.183 1.00 23.00  ? 6    ILE B CA  1 
ATOM   1643 C C   . ILE B 1 25  ? 16.114  52.963 -18.144 1.00 26.30  ? 6    ILE B C   1 
ATOM   1644 O O   . ILE B 1 25  ? 16.317  52.963 -19.365 1.00 24.46  ? 6    ILE B O   1 
ATOM   1645 C CB  . ILE B 1 25  ? 17.925  52.394 -16.528 1.00 22.68  ? 6    ILE B CB  1 
ATOM   1646 C CG1 . ILE B 1 25  ? 19.096  52.933 -15.700 1.00 26.56  ? 6    ILE B CG1 1 
ATOM   1647 C CG2 . ILE B 1 25  ? 18.376  51.375 -17.570 1.00 17.53  ? 6    ILE B CG2 1 
ATOM   1648 C CD1 . ILE B 1 25  ? 19.706  51.887 -14.747 1.00 31.36  ? 6    ILE B CD1 1 
ATOM   1649 N N   . LEU B 1 26  ? 15.005  52.466 -17.591 1.00 24.33  ? 7    LEU B N   1 
ATOM   1650 C CA  . LEU B 1 26  ? 13.951  51.855 -18.395 1.00 15.63  ? 7    LEU B CA  1 
ATOM   1651 C C   . LEU B 1 26  ? 13.298  52.910 -19.265 1.00 20.02  ? 7    LEU B C   1 
ATOM   1652 O O   . LEU B 1 26  ? 12.884  52.632 -20.390 1.00 20.43  ? 7    LEU B O   1 
ATOM   1653 C CB  . LEU B 1 26  ? 12.938  51.137 -17.506 1.00 18.65  ? 7    LEU B CB  1 
ATOM   1654 C CG  . LEU B 1 26  ? 13.545  49.909 -16.796 1.00 22.51  ? 7    LEU B CG  1 
ATOM   1655 C CD1 . LEU B 1 26  ? 12.779  49.483 -15.563 1.00 19.36  ? 7    LEU B CD1 1 
ATOM   1656 C CD2 . LEU B 1 26  ? 13.659  48.735 -17.753 1.00 22.09  ? 7    LEU B CD2 1 
ATOM   1657 N N   . TYR B 1 27  ? 13.240  54.137 -18.753 1.00 24.20  ? 8    TYR B N   1 
ATOM   1658 C CA  . TYR B 1 27  ? 12.723  55.262 -19.526 1.00 19.99  ? 8    TYR B CA  1 
ATOM   1659 C C   . TYR B 1 27  ? 13.590  55.530 -20.732 1.00 21.45  ? 8    TYR B C   1 
ATOM   1660 O O   . TYR B 1 27  ? 13.094  55.540 -21.854 1.00 22.59  ? 8    TYR B O   1 
ATOM   1661 C CB  . TYR B 1 27  ? 12.634  56.513 -18.673 1.00 22.21  ? 8    TYR B CB  1 
ATOM   1662 C CG  . TYR B 1 27  ? 12.116  57.714 -19.425 1.00 33.26  ? 8    TYR B CG  1 
ATOM   1663 C CD1 . TYR B 1 27  ? 10.760  57.861 -19.692 1.00 37.59  ? 8    TYR B CD1 1 
ATOM   1664 C CD2 . TYR B 1 27  ? 12.980  58.713 -19.861 1.00 36.66  ? 8    TYR B CD2 1 
ATOM   1665 C CE1 . TYR B 1 27  ? 10.278  58.969 -20.378 1.00 33.84  ? 8    TYR B CE1 1 
ATOM   1666 C CE2 . TYR B 1 27  ? 12.511  59.818 -20.543 1.00 35.10  ? 8    TYR B CE2 1 
ATOM   1667 C CZ  . TYR B 1 27  ? 11.160  59.942 -20.799 1.00 39.96  ? 8    TYR B CZ  1 
ATOM   1668 O OH  . TYR B 1 27  ? 10.695  61.053 -21.481 1.00 48.61  ? 8    TYR B OH  1 
ATOM   1669 N N   . ASN B 1 28  ? 14.883  55.749 -20.501 1.00 21.31  ? 9    ASN B N   1 
ATOM   1670 C CA  . ASN B 1 28  ? 15.827  55.923 -21.607 1.00 21.46  ? 9    ASN B CA  1 
ATOM   1671 C C   . ASN B 1 28  ? 15.776  54.785 -22.628 1.00 25.01  ? 9    ASN B C   1 
ATOM   1672 O O   . ASN B 1 28  ? 15.788  55.033 -23.824 1.00 30.66  ? 9    ASN B O   1 
ATOM   1673 C CB  . ASN B 1 28  ? 17.261  56.127 -21.103 1.00 19.76  ? 9    ASN B CB  1 
ATOM   1674 C CG  . ASN B 1 28  ? 17.401  57.350 -20.212 1.00 22.59  ? 9    ASN B CG  1 
ATOM   1675 O OD1 . ASN B 1 28  ? 16.634  58.303 -20.325 1.00 27.93  ? 9    ASN B OD1 1 
ATOM   1676 N ND2 . ASN B 1 28  ? 18.383  57.325 -19.315 1.00 22.92  ? 9    ASN B ND2 1 
ATOM   1677 N N   . ILE B 1 29  ? 15.714  53.542 -22.158 1.00 23.43  ? 10   ILE B N   1 
ATOM   1678 C CA  . ILE B 1 29  ? 15.639  52.400 -23.062 1.00 22.84  ? 10   ILE B CA  1 
ATOM   1679 C C   . ILE B 1 29  ? 14.377  52.417 -23.922 1.00 27.55  ? 10   ILE B C   1 
ATOM   1680 O O   . ILE B 1 29  ? 14.448  52.196 -25.122 1.00 27.53  ? 10   ILE B O   1 
ATOM   1681 C CB  . ILE B 1 29  ? 15.754  51.057 -22.316 1.00 25.28  ? 10   ILE B CB  1 
ATOM   1682 C CG1 . ILE B 1 29  ? 17.166  50.914 -21.738 1.00 21.93  ? 10   ILE B CG1 1 
ATOM   1683 C CG2 . ILE B 1 29  ? 15.409  49.889 -23.251 1.00 23.31  ? 10   ILE B CG2 1 
ATOM   1684 C CD1 . ILE B 1 29  ? 17.427  49.624 -20.990 1.00 16.17  ? 10   ILE B CD1 1 
ATOM   1685 N N   . ARG B 1 30  ? 13.230  52.712 -23.314 1.00 30.61  ? 11   ARG B N   1 
ATOM   1686 C CA  . ARG B 1 30  ? 11.981  52.830 -24.069 1.00 27.58  ? 11   ARG B CA  1 
ATOM   1687 C C   . ARG B 1 30  ? 12.010  53.924 -25.149 1.00 32.65  ? 11   ARG B C   1 
ATOM   1688 O O   . ARG B 1 30  ? 11.397  53.774 -26.197 1.00 37.79  ? 11   ARG B O   1 
ATOM   1689 C CB  . ARG B 1 30  ? 10.795  53.051 -23.141 1.00 23.76  ? 11   ARG B CB  1 
ATOM   1690 C CG  . ARG B 1 30  ? 9.608   52.239 -23.544 1.00 35.63  ? 11   ARG B CG  1 
ATOM   1691 C CD  . ARG B 1 30  ? 8.315   52.972 -23.286 1.00 57.87  ? 11   ARG B CD  1 
ATOM   1692 N NE  . ARG B 1 30  ? 7.249   52.418 -24.121 1.00 82.75  ? 11   ARG B NE  1 
ATOM   1693 C CZ  . ARG B 1 30  ? 5.999   52.872 -24.159 1.00 87.79  ? 11   ARG B CZ  1 
ATOM   1694 N NH1 . ARG B 1 30  ? 5.632   53.901 -23.400 1.00 82.92  ? 11   ARG B NH1 1 
ATOM   1695 N NH2 . ARG B 1 30  ? 5.116   52.290 -24.963 1.00 75.26  ? 11   ARG B NH2 1 
ATOM   1696 N N   . GLN B 1 31  ? 12.733  55.010 -24.903 1.00 33.29  ? 12   GLN B N   1 
ATOM   1697 C CA  . GLN B 1 31  ? 12.786  56.125 -25.850 1.00 30.16  ? 12   GLN B CA  1 
ATOM   1698 C C   . GLN B 1 31  ? 13.803  56.011 -27.000 1.00 32.48  ? 12   GLN B C   1 
ATOM   1699 O O   . GLN B 1 31  ? 13.624  56.658 -28.029 1.00 35.95  ? 12   GLN B O   1 
ATOM   1700 C CB  . GLN B 1 31  ? 13.066  57.428 -25.101 1.00 35.99  ? 12   GLN B CB  1 
ATOM   1701 C CG  . GLN B 1 31  ? 12.065  57.781 -24.012 1.00 41.91  ? 12   GLN B CG  1 
ATOM   1702 C CD  . GLN B 1 31  ? 10.696  58.118 -24.573 1.00 49.09  ? 12   GLN B CD  1 
ATOM   1703 O OE1 . GLN B 1 31  ? 10.553  58.403 -25.764 1.00 53.17  ? 12   GLN B OE1 1 
ATOM   1704 N NE2 . GLN B 1 31  ? 9.676   58.083 -23.713 1.00 49.71  ? 12   GLN B NE2 1 
ATOM   1705 N N   . THR B 1 32  ? 14.904  55.326 -26.792 1.00 30.18  ? 13   THR B N   1 
ATOM   1706 C CA  . THR B 1 32  ? 15.951  55.309 -27.771 1.00 32.78  ? 13   THR B CA  1 
ATOM   1707 C C   . THR B 1 32  ? 16.367  53.975 -28.347 1.00 37.81  ? 13   THR B C   1 
ATOM   1708 O O   . THR B 1 32  ? 17.245  53.919 -29.170 1.00 41.02  ? 13   THR B O   1 
ATOM   1709 C CB  . THR B 1 32  ? 17.202  55.981 -27.220 1.00 27.92  ? 13   THR B CB  1 
ATOM   1710 O OG1 . THR B 1 32  ? 17.823  55.105 -26.305 1.00 40.29  ? 13   THR B OG1 1 
ATOM   1711 C CG2 . THR B 1 32  ? 16.863  57.206 -26.519 1.00 21.53  ? 13   THR B CG2 1 
ATOM   1712 N N   . SER B 1 33  ? 15.734  52.904 -27.924 1.00 41.20  ? 14   SER B N   1 
ATOM   1713 C CA  . SER B 1 33  ? 16.192  51.536 -28.179 1.00 41.75  ? 14   SER B CA  1 
ATOM   1714 C C   . SER B 1 33  ? 16.266  51.029 -29.625 1.00 44.93  ? 14   SER B C   1 
ATOM   1715 O O   . SER B 1 33  ? 17.185  50.299 -29.959 1.00 31.52  ? 14   SER B O   1 
ATOM   1716 C CB  . SER B 1 33  ? 15.469  50.576 -27.236 1.00 35.35  ? 14   SER B CB  1 
ATOM   1717 O OG  . SER B 1 33  ? 14.940  49.433 -27.844 1.00 40.68  ? 14   SER B OG  1 
ATOM   1718 N N   . ARG B 1 34  ? 15.322  51.419 -30.477 1.00 36.44  ? 15   ARG B N   1 
ATOM   1719 C CA  . ARG B 1 34  ? 15.311  50.958 -31.863 1.00 34.35  ? 15   ARG B CA  1 
ATOM   1720 C C   . ARG B 1 34  ? 15.208  49.464 -32.060 1.00 31.35  ? 15   ARG B C   1 
ATOM   1721 O O   . ARG B 1 34  ? 16.121  48.827 -32.465 1.00 32.52  ? 15   ARG B O   1 
ATOM   1722 C CB  . ARG B 1 34  ? 16.495  51.492 -32.671 1.00 38.13  ? 15   ARG B CB  1 
ATOM   1723 C CG  . ARG B 1 34  ? 16.650  52.994 -32.818 1.00 41.60  ? 15   ARG B CG  1 
ATOM   1724 C CD  . ARG B 1 34  ? 15.485  53.760 -33.418 1.00 41.98  ? 15   ARG B CD  1 
ATOM   1725 N NE  . ARG B 1 34  ? 14.889  53.239 -34.651 1.00 58.01  ? 15   ARG B NE  1 
ATOM   1726 C CZ  . ARG B 1 34  ? 15.267  53.507 -35.898 1.00 46.56  ? 15   ARG B CZ  1 
ATOM   1727 N NH1 . ARG B 1 34  ? 16.296  54.260 -36.158 1.00 44.14  ? 15   ARG B NH1 1 
ATOM   1728 N NH2 . ARG B 1 34  ? 14.597  52.975 -36.883 1.00 34.06  ? 15   ARG B NH2 1 
ATOM   1729 N N   . PRO B 1 35  ? 13.980  48.920 -31.757 1.00 27.48  ? 16   PRO B N   1 
ATOM   1730 C CA  . PRO B 1 35  ? 13.875  47.468 -31.865 1.00 27.74  ? 16   PRO B CA  1 
ATOM   1731 C C   . PRO B 1 35  ? 14.006  46.843 -33.245 1.00 22.91  ? 16   PRO B C   1 
ATOM   1732 O O   . PRO B 1 35  ? 14.044  45.654 -33.356 1.00 22.86  ? 16   PRO B O   1 
ATOM   1733 C CB  . PRO B 1 35  ? 12.490  47.177 -31.331 1.00 23.42  ? 16   PRO B CB  1 
ATOM   1734 C CG  . PRO B 1 35  ? 12.123  48.302 -30.540 1.00 20.87  ? 16   PRO B CG  1 
ATOM   1735 C CD  . PRO B 1 35  ? 12.617  49.420 -31.296 1.00 28.35  ? 16   PRO B CD  1 
ATOM   1736 N N   . ASP B 1 36  ? 13.937  47.634 -34.281 1.00 22.68  ? 17   ASP B N   1 
ATOM   1737 C CA  . ASP B 1 36  ? 14.056  47.110 -35.613 1.00 23.70  ? 17   ASP B CA  1 
ATOM   1738 C C   . ASP B 1 36  ? 15.428  47.183 -36.198 1.00 24.82  ? 17   ASP B C   1 
ATOM   1739 O O   . ASP B 1 36  ? 15.668  46.691 -37.250 1.00 28.17  ? 17   ASP B O   1 
ATOM   1740 C CB  . ASP B 1 36  ? 13.025  47.741 -36.501 1.00 26.84  ? 17   ASP B CB  1 
ATOM   1741 C CG  . ASP B 1 36  ? 12.976  49.207 -36.370 1.00 54.47  ? 17   ASP B CG  1 
ATOM   1742 O OD1 . ASP B 1 36  ? 13.140  49.745 -35.260 1.00 48.98  ? 17   ASP B OD1 1 
ATOM   1743 O OD2 . ASP B 1 36  ? 12.765  49.848 -37.404 1.00 56.25  ? 17   ASP B OD2 1 
ATOM   1744 N N   . VAL B 1 37  ? 16.338  47.761 -35.460 1.00 23.08  ? 18   VAL B N   1 
ATOM   1745 C CA  . VAL B 1 37  ? 17.712  47.952 -35.931 1.00 25.83  ? 18   VAL B CA  1 
ATOM   1746 C C   . VAL B 1 37  ? 18.714  46.997 -35.298 1.00 23.87  ? 18   VAL B C   1 
ATOM   1747 O O   . VAL B 1 37  ? 19.003  47.098 -34.103 1.00 23.85  ? 18   VAL B O   1 
ATOM   1748 C CB  . VAL B 1 37  ? 18.236  49.373 -35.637 1.00 27.94  ? 18   VAL B CB  1 
ATOM   1749 C CG1 . VAL B 1 37  ? 19.700  49.499 -36.090 1.00 23.05  ? 18   VAL B CG1 1 
ATOM   1750 C CG2 . VAL B 1 37  ? 17.355  50.415 -36.292 1.00 28.16  ? 18   VAL B CG2 1 
ATOM   1751 N N   . ILE B 1 38  ? 19.257  46.096 -36.113 1.00 25.97  ? 19   ILE B N   1 
ATOM   1752 C CA  . ILE B 1 38  ? 20.318  45.182 -35.688 1.00 25.05  ? 19   ILE B CA  1 
ATOM   1753 C C   . ILE B 1 38  ? 21.561  45.935 -35.183 1.00 26.76  ? 19   ILE B C   1 
ATOM   1754 O O   . ILE B 1 38  ? 22.085  46.829 -35.859 1.00 30.03  ? 19   ILE B O   1 
ATOM   1755 C CB  . ILE B 1 38  ? 20.656  44.179 -36.840 1.00 25.14  ? 19   ILE B CB  1 
ATOM   1756 C CG1 . ILE B 1 38  ? 21.702  43.140 -36.430 1.00 21.56  ? 19   ILE B CG1 1 
ATOM   1757 C CG2 . ILE B 1 38  ? 21.070  44.907 -38.107 1.00 25.40  ? 19   ILE B CG2 1 
ATOM   1758 C CD1 . ILE B 1 38  ? 21.771  41.960 -37.407 1.00 21.95  ? 19   ILE B CD1 1 
ATOM   1759 N N   . PRO B 1 39  ? 22.022  45.586 -33.973 1.00 26.12  ? 20   PRO B N   1 
ATOM   1760 C CA  . PRO B 1 39  ? 23.134  46.313 -33.344 1.00 26.61  ? 20   PRO B CA  1 
ATOM   1761 C C   . PRO B 1 39  ? 24.515  45.824 -33.828 1.00 34.34  ? 20   PRO B C   1 
ATOM   1762 O O   . PRO B 1 39  ? 25.316  45.307 -33.031 1.00 39.16  ? 20   PRO B O   1 
ATOM   1763 C CB  . PRO B 1 39  ? 22.922  46.036 -31.849 1.00 25.22  ? 20   PRO B CB  1 
ATOM   1764 C CG  . PRO B 1 39  ? 22.278  44.654 -31.823 1.00 24.61  ? 20   PRO B CG  1 
ATOM   1765 C CD  . PRO B 1 39  ? 21.446  44.554 -33.086 1.00 20.91  ? 20   PRO B CD  1 
ATOM   1766 N N   . THR B 1 40  ? 24.783  45.986 -35.127 1.00 33.97  ? 21   THR B N   1 
ATOM   1767 C CA  . THR B 1 40  ? 26.100  45.666 -35.683 1.00 34.57  ? 21   THR B CA  1 
ATOM   1768 C C   . THR B 1 40  ? 27.123  46.694 -35.221 1.00 44.41  ? 21   THR B C   1 
ATOM   1769 O O   . THR B 1 40  ? 26.771  47.842 -34.921 1.00 41.25  ? 21   THR B O   1 
ATOM   1770 C CB  . THR B 1 40  ? 26.077  45.608 -37.219 1.00 39.11  ? 21   THR B CB  1 
ATOM   1771 O OG1 . THR B 1 40  ? 25.530  46.828 -37.732 1.00 44.79  ? 21   THR B OG1 1 
ATOM   1772 C CG2 . THR B 1 40  ? 25.218  44.433 -37.701 1.00 39.39  ? 21   THR B CG2 1 
ATOM   1773 N N   . GLN B 1 41  ? 28.383  46.267 -35.148 1.00 56.69  ? 22   GLN B N   1 
ATOM   1774 C CA  . GLN B 1 41  ? 29.492  47.140 -34.746 1.00 58.90  ? 22   GLN B CA  1 
ATOM   1775 C C   . GLN B 1 41  ? 30.579  47.140 -35.811 1.00 60.61  ? 22   GLN B C   1 
ATOM   1776 O O   . GLN B 1 41  ? 31.476  46.302 -35.777 1.00 72.38  ? 22   GLN B O   1 
ATOM   1777 C CB  . GLN B 1 41  ? 30.106  46.675 -33.421 1.00 58.86  ? 22   GLN B CB  1 
ATOM   1778 C CG  . GLN B 1 41  ? 29.468  47.234 -32.163 1.00 68.32  ? 22   GLN B CG  1 
ATOM   1779 C CD  . GLN B 1 41  ? 30.198  46.792 -30.893 1.00 82.76  ? 22   GLN B CD  1 
ATOM   1780 O OE1 . GLN B 1 41  ? 30.331  45.589 -30.616 1.00 80.05  ? 22   GLN B OE1 1 
ATOM   1781 N NE2 . GLN B 1 41  ? 30.682  47.766 -30.120 1.00 71.89  ? 22   GLN B NE2 1 
ATOM   1782 N N   . ARG B 1 42  ? 30.669  48.200 -36.564 1.00 63.38  ? 23   ARG B N   1 
ATOM   1783 C CA  . ARG B 1 42  ? 31.791  48.293 -37.445 1.00 70.56  ? 23   ARG B CA  1 
ATOM   1784 C C   . ARG B 1 42  ? 31.785  47.111 -38.388 1.00 69.77  ? 23   ARG B C   1 
ATOM   1785 O O   . ARG B 1 42  ? 32.809  46.547 -38.690 1.00 70.76  ? 23   ARG B O   1 
ATOM   1786 C CB  . ARG B 1 42  ? 33.089  48.278 -36.644 1.00 72.78  ? 23   ARG B CB  1 
ATOM   1787 C CG  . ARG B 1 42  ? 33.274  49.334 -35.579 1.00 78.11  ? 23   ARG B CG  1 
ATOM   1788 C CD  . ARG B 1 42  ? 34.741  49.348 -35.168 1.00 91.82  ? 23   ARG B CD  1 
ATOM   1789 N NE  . ARG B 1 42  ? 35.002  49.481 -33.732 1.00 108.73 ? 23   ARG B NE  1 
ATOM   1790 C CZ  . ARG B 1 42  ? 35.523  50.561 -33.151 1.00 101.78 ? 23   ARG B CZ  1 
ATOM   1791 N NH1 . ARG B 1 42  ? 35.834  51.621 -33.875 1.00 104.58 ? 23   ARG B NH1 1 
ATOM   1792 N NH2 . ARG B 1 42  ? 35.736  50.583 -31.849 1.00 78.95  ? 23   ARG B NH2 1 
ATOM   1793 N N   . ASP B 1 43  ? 30.617  46.741 -38.872 1.00 71.02  ? 24   ASP B N   1 
ATOM   1794 C CA  . ASP B 1 43  ? 30.541  45.739 -39.917 1.00 77.87  ? 24   ASP B CA  1 
ATOM   1795 C C   . ASP B 1 43  ? 30.868  44.344 -39.485 1.00 66.70  ? 24   ASP B C   1 
ATOM   1796 O O   . ASP B 1 43  ? 31.307  43.528 -40.272 1.00 65.81  ? 24   ASP B O   1 
ATOM   1797 C CB  . ASP B 1 43  ? 31.471  46.116 -41.057 1.00 75.11  ? 24   ASP B CB  1 
ATOM   1798 C CG  . ASP B 1 43  ? 30.773  46.880 -42.134 1.00 84.94  ? 24   ASP B CG  1 
ATOM   1799 O OD1 . ASP B 1 43  ? 29.877  47.666 -41.804 1.00 87.28  ? 24   ASP B OD1 1 
ATOM   1800 O OD2 . ASP B 1 43  ? 31.120  46.688 -43.312 1.00 86.08  ? 24   ASP B OD2 1 
ATOM   1801 N N   . ARG B 1 44  ? 30.631  44.068 -38.228 1.00 56.07  ? 25   ARG B N   1 
ATOM   1802 C CA  . ARG B 1 44  ? 30.901  42.771 -37.711 1.00 50.56  ? 25   ARG B CA  1 
ATOM   1803 C C   . ARG B 1 44  ? 29.612  42.169 -37.340 1.00 40.64  ? 25   ARG B C   1 
ATOM   1804 O O   . ARG B 1 44  ? 28.681  42.860 -37.054 1.00 42.38  ? 25   ARG B O   1 
ATOM   1805 C CB  . ARG B 1 44  ? 31.776  42.880 -36.509 1.00 52.23  ? 25   ARG B CB  1 
ATOM   1806 C CG  . ARG B 1 44  ? 32.900  43.830 -36.747 1.00 64.51  ? 25   ARG B CG  1 
ATOM   1807 C CD  . ARG B 1 44  ? 33.970  43.653 -35.719 1.00 68.39  ? 25   ARG B CD  1 
ATOM   1808 N NE  . ARG B 1 44  ? 35.129  44.352 -36.189 1.00 86.11  ? 25   ARG B NE  1 
ATOM   1809 C CZ  . ARG B 1 44  ? 35.483  45.552 -35.780 1.00 85.03  ? 25   ARG B CZ  1 
ATOM   1810 N NH1 . ARG B 1 44  ? 34.781  46.151 -34.828 1.00 74.70  ? 25   ARG B NH1 1 
ATOM   1811 N NH2 . ARG B 1 44  ? 36.574  46.121 -36.291 1.00 84.85  ? 25   ARG B NH2 1 
ATOM   1812 N N   . PRO B 1 45  ? 29.581  40.798 -37.424 1.00 35.33  ? 26   PRO B N   1 
ATOM   1813 C CA  . PRO B 1 45  ? 28.305  40.201 -37.083 1.00 35.23  ? 26   PRO B CA  1 
ATOM   1814 C C   . PRO B 1 45  ? 27.949  40.366 -35.644 1.00 33.85  ? 26   PRO B C   1 
ATOM   1815 O O   . PRO B 1 45  ? 28.808  40.459 -34.828 1.00 33.97  ? 26   PRO B O   1 
ATOM   1816 C CB  . PRO B 1 45  ? 28.538  38.743 -37.316 1.00 39.46  ? 26   PRO B CB  1 
ATOM   1817 C CG  . PRO B 1 45  ? 29.556  38.681 -38.327 1.00 38.25  ? 26   PRO B CG  1 
ATOM   1818 C CD  . PRO B 1 45  ? 30.504  39.662 -37.846 1.00 35.73  ? 26   PRO B CD  1 
ATOM   1819 N N   . VAL B 1 46  ? 26.677  40.411 -35.331 1.00 28.94  ? 27   VAL B N   1 
ATOM   1820 C CA  . VAL B 1 46  ? 26.306  40.335 -33.934 1.00 26.84  ? 27   VAL B CA  1 
ATOM   1821 C C   . VAL B 1 46  ? 26.545  38.889 -33.521 1.00 28.23  ? 27   VAL B C   1 
ATOM   1822 O O   . VAL B 1 46  ? 26.050  37.966 -34.183 1.00 30.83  ? 27   VAL B O   1 
ATOM   1823 C CB  . VAL B 1 46  ? 24.827  40.672 -33.756 1.00 25.17  ? 27   VAL B CB  1 
ATOM   1824 C CG1 . VAL B 1 46  ? 24.422  40.557 -32.285 1.00 24.95  ? 27   VAL B CG1 1 
ATOM   1825 C CG2 . VAL B 1 46  ? 24.546  42.051 -34.278 1.00 20.93  ? 27   VAL B CG2 1 
ATOM   1826 N N   . ALA B 1 47  ? 27.310  38.664 -32.456 1.00 22.46  ? 28   ALA B N   1 
ATOM   1827 C CA  . ALA B 1 47  ? 27.552  37.281 -32.031 1.00 27.20  ? 28   ALA B CA  1 
ATOM   1828 C C   . ALA B 1 47  ? 26.448  36.796 -31.082 1.00 30.93  ? 28   ALA B C   1 
ATOM   1829 O O   . ALA B 1 47  ? 26.345  37.243 -29.940 1.00 33.04  ? 28   ALA B O   1 
ATOM   1830 C CB  . ALA B 1 47  ? 28.906  37.132 -31.394 1.00 22.94  ? 28   ALA B CB  1 
ATOM   1831 N N   . VAL B 1 48  ? 25.625  35.877 -31.558 1.00 25.42  ? 29   VAL B N   1 
ATOM   1832 C CA  . VAL B 1 48  ? 24.537  35.355 -30.753 1.00 26.73  ? 29   VAL B CA  1 
ATOM   1833 C C   . VAL B 1 48  ? 24.928  33.960 -30.254 1.00 29.59  ? 29   VAL B C   1 
ATOM   1834 O O   . VAL B 1 48  ? 25.335  33.105 -31.034 1.00 33.16  ? 29   VAL B O   1 
ATOM   1835 C CB  . VAL B 1 48  ? 23.216  35.265 -31.587 1.00 25.35  ? 29   VAL B CB  1 
ATOM   1836 C CG1 . VAL B 1 48  ? 22.061  34.749 -30.752 1.00 16.97  ? 29   VAL B CG1 1 
ATOM   1837 C CG2 . VAL B 1 48  ? 22.864  36.613 -32.201 1.00 22.10  ? 29   VAL B CG2 1 
ATOM   1838 N N   . SER B 1 49  ? 24.803  33.727 -28.955 1.00 29.13  ? 30   SER B N   1 
ATOM   1839 C CA  . SER B 1 49  ? 25.008  32.396 -28.399 1.00 25.31  ? 30   SER B CA  1 
ATOM   1840 C C   . SER B 1 49  ? 23.666  31.762 -28.123 1.00 24.05  ? 30   SER B C   1 
ATOM   1841 O O   . SER B 1 49  ? 22.769  32.411 -27.606 1.00 25.42  ? 30   SER B O   1 
ATOM   1842 C CB  . SER B 1 49  ? 25.770  32.485 -27.093 1.00 26.51  ? 30   SER B CB  1 
ATOM   1843 O OG  . SER B 1 49  ? 26.804  33.440 -27.204 1.00 36.69  ? 30   SER B OG  1 
ATOM   1844 N N   . VAL B 1 50  ? 23.539  30.484 -28.453 1.00 29.51  ? 31   VAL B N   1 
ATOM   1845 C CA  . VAL B 1 50  ? 22.301  29.758 -28.249 1.00 23.94  ? 31   VAL B CA  1 
ATOM   1846 C C   . VAL B 1 50  ? 22.569  28.483 -27.462 1.00 29.64  ? 31   VAL B C   1 
ATOM   1847 O O   . VAL B 1 50  ? 23.504  27.737 -27.746 1.00 36.84  ? 31   VAL B O   1 
ATOM   1848 C CB  . VAL B 1 50  ? 21.670  29.381 -29.577 1.00 25.24  ? 31   VAL B CB  1 
ATOM   1849 C CG1 . VAL B 1 50  ? 20.362  28.665 -29.336 1.00 24.15  ? 31   VAL B CG1 1 
ATOM   1850 C CG2 . VAL B 1 50  ? 21.458  30.618 -30.423 1.00 27.19  ? 31   VAL B CG2 1 
ATOM   1851 N N   . SER B 1 51  ? 21.741  28.225 -26.467 1.00 28.46  ? 32   SER B N   1 
ATOM   1852 C CA  . SER B 1 51  ? 21.865  27.001 -25.693 1.00 27.71  ? 32   SER B CA  1 
ATOM   1853 C C   . SER B 1 51  ? 20.480  26.444 -25.310 1.00 25.03  ? 32   SER B C   1 
ATOM   1854 O O   . SER B 1 51  ? 19.648  27.173 -24.764 1.00 29.09  ? 32   SER B O   1 
ATOM   1855 C CB  . SER B 1 51  ? 22.691  27.285 -24.449 1.00 33.10  ? 32   SER B CB  1 
ATOM   1856 O OG  . SER B 1 51  ? 22.862  26.101 -23.697 1.00 61.67  ? 32   SER B OG  1 
ATOM   1857 N N   . LEU B 1 52  ? 20.224  25.168 -25.598 1.00 24.94  ? 33   LEU B N   1 
ATOM   1858 C CA  . LEU B 1 52  ? 18.948  24.549 -25.206 1.00 26.20  ? 33   LEU B CA  1 
ATOM   1859 C C   . LEU B 1 52  ? 19.079  23.732 -23.915 1.00 27.06  ? 33   LEU B C   1 
ATOM   1860 O O   . LEU B 1 52  ? 19.965  22.901 -23.783 1.00 31.09  ? 33   LEU B O   1 
ATOM   1861 C CB  . LEU B 1 52  ? 18.383  23.667 -26.315 1.00 19.92  ? 33   LEU B CB  1 
ATOM   1862 C CG  . LEU B 1 52  ? 18.337  24.293 -27.712 1.00 20.07  ? 33   LEU B CG  1 
ATOM   1863 C CD1 . LEU B 1 52  ? 17.506  23.453 -28.650 1.00 24.68  ? 33   LEU B CD1 1 
ATOM   1864 C CD2 . LEU B 1 52  ? 17.794  25.696 -27.665 1.00 24.78  ? 33   LEU B CD2 1 
ATOM   1865 N N   . LYS B 1 53  ? 18.208  23.990 -22.950 1.00 28.51  ? 34   LYS B N   1 
ATOM   1866 C CA  . LYS B 1 53  ? 18.158  23.183 -21.742 1.00 25.65  ? 34   LYS B CA  1 
ATOM   1867 C C   . LYS B 1 53  ? 16.856  22.414 -21.792 1.00 25.62  ? 34   LYS B C   1 
ATOM   1868 O O   . LYS B 1 53  ? 15.771  23.008 -21.696 1.00 21.98  ? 34   LYS B O   1 
ATOM   1869 C CB  . LYS B 1 53  ? 18.167  24.056 -20.486 1.00 32.60  ? 34   LYS B CB  1 
ATOM   1870 C CG  . LYS B 1 53  ? 19.121  25.238 -20.524 1.00 39.35  ? 34   LYS B CG  1 
ATOM   1871 C CD  . LYS B 1 53  ? 20.568  24.811 -20.376 1.00 47.88  ? 34   LYS B CD  1 
ATOM   1872 C CE  . LYS B 1 53  ? 21.510  26.018 -20.439 1.00 52.72  ? 34   LYS B CE  1 
ATOM   1873 N NZ  . LYS B 1 53  ? 22.956  25.598 -20.347 1.00 62.21  ? 34   LYS B NZ  1 
ATOM   1874 N N   . PHE B 1 54  ? 16.952  21.094 -21.952 1.00 35.03  ? 35   PHE B N   1 
ATOM   1875 C CA  . PHE B 1 54  ? 15.741  20.271 -22.066 1.00 28.69  ? 35   PHE B CA  1 
ATOM   1876 C C   . PHE B 1 54  ? 15.026  20.074 -20.739 1.00 26.69  ? 35   PHE B C   1 
ATOM   1877 O O   . PHE B 1 54  ? 15.644  19.810 -19.700 1.00 22.44  ? 35   PHE B O   1 
ATOM   1878 C CB  . PHE B 1 54  ? 16.035  18.957 -22.754 1.00 18.59  ? 35   PHE B CB  1 
ATOM   1879 C CG  . PHE B 1 54  ? 16.511  19.139 -24.146 1.00 22.55  ? 35   PHE B CG  1 
ATOM   1880 C CD1 . PHE B 1 54  ? 15.604  19.287 -25.181 1.00 23.56  ? 35   PHE B CD1 1 
ATOM   1881 C CD2 . PHE B 1 54  ? 17.865  19.218 -24.422 1.00 25.85  ? 35   PHE B CD2 1 
ATOM   1882 C CE1 . PHE B 1 54  ? 16.033  19.469 -26.481 1.00 21.88  ? 35   PHE B CE1 1 
ATOM   1883 C CE2 . PHE B 1 54  ? 18.310  19.409 -25.716 1.00 25.91  ? 35   PHE B CE2 1 
ATOM   1884 C CZ  . PHE B 1 54  ? 17.390  19.537 -26.746 1.00 26.47  ? 35   PHE B CZ  1 
ATOM   1885 N N   . ILE B 1 55  ? 13.712  20.261 -20.780 1.00 25.42  ? 36   ILE B N   1 
ATOM   1886 C CA  . ILE B 1 55  ? 12.917  20.181 -19.566 1.00 27.22  ? 36   ILE B CA  1 
ATOM   1887 C C   . ILE B 1 55  ? 12.012  18.949 -19.587 1.00 24.21  ? 36   ILE B C   1 
ATOM   1888 O O   . ILE B 1 55  ? 11.834  18.278 -18.561 1.00 22.13  ? 36   ILE B O   1 
ATOM   1889 C CB  . ILE B 1 55  ? 12.097  21.478 -19.324 1.00 25.27  ? 36   ILE B CB  1 
ATOM   1890 C CG1 . ILE B 1 55  ? 12.975  22.724 -19.512 1.00 19.64  ? 36   ILE B CG1 1 
ATOM   1891 C CG2 . ILE B 1 55  ? 11.461  21.453 -17.944 1.00 15.88  ? 36   ILE B CG2 1 
ATOM   1892 C CD1 . ILE B 1 55  ? 14.138  22.806 -18.551 1.00 19.23  ? 36   ILE B CD1 1 
ATOM   1893 N N   . ASN B 1 56  ? 11.455  18.646 -20.759 1.00 23.81  ? 37   ASN B N   1 
ATOM   1894 C CA  . ASN B 1 56  ? 10.534  17.513 -20.888 1.00 20.98  ? 37   ASN B CA  1 
ATOM   1895 C C   . ASN B 1 56  ? 10.445  16.962 -22.298 1.00 21.22  ? 37   ASN B C   1 
ATOM   1896 O O   . ASN B 1 56  ? 10.704  17.677 -23.264 1.00 33.29  ? 37   ASN B O   1 
ATOM   1897 C CB  . ASN B 1 56  ? 9.141   17.923 -20.403 1.00 20.09  ? 37   ASN B CB  1 
ATOM   1898 C CG  . ASN B 1 56  ? 8.448   16.834 -19.581 1.00 23.20  ? 37   ASN B CG  1 
ATOM   1899 O OD1 . ASN B 1 56  ? 8.426   15.667 -19.962 1.00 30.66  ? 37   ASN B OD1 1 
ATOM   1900 N ND2 . ASN B 1 56  ? 7.870   17.221 -18.453 1.00 21.14  ? 37   ASN B ND2 1 
ATOM   1901 N N   . ILE B 1 57  ? 10.094  15.689 -22.411 1.00 20.42  ? 38   ILE B N   1 
ATOM   1902 C CA  . ILE B 1 57  ? 9.780   15.081 -23.700 1.00 25.26  ? 38   ILE B CA  1 
ATOM   1903 C C   . ILE B 1 57  ? 8.392   14.466 -23.573 1.00 28.42  ? 38   ILE B C   1 
ATOM   1904 O O   . ILE B 1 57  ? 8.139   13.688 -22.660 1.00 28.51  ? 38   ILE B O   1 
ATOM   1905 C CB  . ILE B 1 57  ? 10.856  14.050 -24.131 1.00 25.45  ? 38   ILE B CB  1 
ATOM   1906 C CG1 . ILE B 1 57  ? 12.197  14.777 -24.304 1.00 23.95  ? 38   ILE B CG1 1 
ATOM   1907 C CG2 . ILE B 1 57  ? 10.446  13.342 -25.423 1.00 21.68  ? 38   ILE B CG2 1 
ATOM   1908 C CD1 . ILE B 1 57  ? 13.356  13.922 -24.597 1.00 24.35  ? 38   ILE B CD1 1 
ATOM   1909 N N   . LEU B 1 58  ? 7.479   14.833 -24.465 1.00 30.73  ? 39   LEU B N   1 
ATOM   1910 C CA  . LEU B 1 58  ? 6.070   14.670 -24.146 1.00 28.47  ? 39   LEU B CA  1 
ATOM   1911 C C   . LEU B 1 58  ? 5.324   13.679 -24.982 1.00 33.30  ? 39   LEU B C   1 
ATOM   1912 O O   . LEU B 1 58  ? 4.592   12.854 -24.443 1.00 34.04  ? 39   LEU B O   1 
ATOM   1913 C CB  . LEU B 1 58  ? 5.347   16.015 -24.212 1.00 33.01  ? 39   LEU B CB  1 
ATOM   1914 C CG  . LEU B 1 58  ? 5.680   16.976 -23.081 1.00 30.29  ? 39   LEU B CG  1 
ATOM   1915 C CD1 . LEU B 1 58  ? 4.899   18.251 -23.248 1.00 39.18  ? 39   LEU B CD1 1 
ATOM   1916 C CD2 . LEU B 1 58  ? 5.378   16.343 -21.735 1.00 32.81  ? 39   LEU B CD2 1 
ATOM   1917 N N   . GLU B 1 59  ? 5.451   13.788 -26.296 1.00 32.54  ? 40   GLU B N   1 
ATOM   1918 C CA  . GLU B 1 59  ? 4.639   12.944 -27.160 1.00 38.59  ? 40   GLU B CA  1 
ATOM   1919 C C   . GLU B 1 59  ? 5.458   12.448 -28.308 1.00 43.38  ? 40   GLU B C   1 
ATOM   1920 O O   . GLU B 1 59  ? 5.714   13.168 -29.275 1.00 49.36  ? 40   GLU B O   1 
ATOM   1921 C CB  . GLU B 1 59  ? 3.395   13.673 -27.667 1.00 39.49  ? 40   GLU B CB  1 
ATOM   1922 C CG  . GLU B 1 59  ? 2.113   13.121 -27.086 1.00 55.58  ? 40   GLU B CG  1 
ATOM   1923 C CD  . GLU B 1 59  ? 1.057   14.194 -26.895 1.00 78.48  ? 40   GLU B CD  1 
ATOM   1924 O OE1 . GLU B 1 59  ? 1.353   15.376 -27.212 1.00 78.27  ? 40   GLU B OE1 1 
ATOM   1925 O OE2 . GLU B 1 59  ? -0.057  13.854 -26.426 1.00 78.78  ? 40   GLU B OE2 1 
ATOM   1926 N N   . VAL B 1 60  ? 5.882   11.205 -28.199 1.00 38.03  ? 41   VAL B N   1 
ATOM   1927 C CA  . VAL B 1 60  ? 6.724   10.659 -29.232 1.00 35.39  ? 41   VAL B CA  1 
ATOM   1928 C C   . VAL B 1 60  ? 5.885   9.770  -30.124 1.00 32.19  ? 41   VAL B C   1 
ATOM   1929 O O   . VAL B 1 60  ? 4.987   9.080  -29.650 1.00 39.21  ? 41   VAL B O   1 
ATOM   1930 C CB  . VAL B 1 60  ? 7.897   9.927  -28.609 1.00 32.87  ? 41   VAL B CB  1 
ATOM   1931 C CG1 . VAL B 1 60  ? 8.656   9.205  -29.646 1.00 30.90  ? 41   VAL B CG1 1 
ATOM   1932 C CG2 . VAL B 1 60  ? 8.796   10.937 -27.907 1.00 36.31  ? 41   VAL B CG2 1 
ATOM   1933 N N   . ASN B 1 61  ? 6.135   9.845  -31.424 1.00 29.30  ? 42   ASN B N   1 
ATOM   1934 C CA  . ASN B 1 61  ? 5.482   8.972  -32.385 1.00 29.00  ? 42   ASN B CA  1 
ATOM   1935 C C   . ASN B 1 61  ? 6.542   8.418  -33.343 1.00 37.76  ? 42   ASN B C   1 
ATOM   1936 O O   . ASN B 1 61  ? 7.051   9.132  -34.215 1.00 33.86  ? 42   ASN B O   1 
ATOM   1937 C CB  . ASN B 1 61  ? 4.364   9.713  -33.119 1.00 30.56  ? 42   ASN B CB  1 
ATOM   1938 C CG  . ASN B 1 61  ? 3.520   8.797  -33.998 1.00 37.87  ? 42   ASN B CG  1 
ATOM   1939 O OD1 . ASN B 1 61  ? 4.031   7.868  -34.633 1.00 39.67  ? 42   ASN B OD1 1 
ATOM   1940 N ND2 . ASN B 1 61  ? 2.208   9.063  -34.041 1.00 40.13  ? 42   ASN B ND2 1 
ATOM   1941 N N   . GLU B 1 62  ? 6.879   7.141  -33.159 1.00 38.59  ? 43   GLU B N   1 
ATOM   1942 C CA  . GLU B 1 62  ? 7.923   6.503  -33.954 1.00 37.01  ? 43   GLU B CA  1 
ATOM   1943 C C   . GLU B 1 62  ? 7.428   6.266  -35.383 1.00 38.92  ? 43   GLU B C   1 
ATOM   1944 O O   . GLU B 1 62  ? 8.228   6.250  -36.331 1.00 40.62  ? 43   GLU B O   1 
ATOM   1945 C CB  . GLU B 1 62  ? 8.405   5.197  -33.299 1.00 41.78  ? 43   GLU B CB  1 
ATOM   1946 C CG  . GLU B 1 62  ? 9.777   4.681  -33.799 1.00 48.62  ? 43   GLU B CG  1 
ATOM   1947 C CD  . GLU B 1 62  ? 10.254  3.398  -33.078 1.00 55.82  ? 43   GLU B CD  1 
ATOM   1948 O OE1 . GLU B 1 62  ? 9.643   3.017  -32.041 1.00 54.37  ? 43   GLU B OE1 1 
ATOM   1949 O OE2 . GLU B 1 62  ? 11.241  2.776  -33.555 1.00 45.19  ? 43   GLU B OE2 1 
ATOM   1950 N N   . ILE B 1 63  ? 6.109   6.113  -35.535 1.00 39.65  ? 44   ILE B N   1 
ATOM   1951 C CA  . ILE B 1 63  ? 5.506   5.884  -36.854 1.00 41.69  ? 44   ILE B CA  1 
ATOM   1952 C C   . ILE B 1 63  ? 5.651   7.112  -37.751 1.00 41.20  ? 44   ILE B C   1 
ATOM   1953 O O   . ILE B 1 63  ? 6.029   6.987  -38.915 1.00 42.33  ? 44   ILE B O   1 
ATOM   1954 C CB  . ILE B 1 63  ? 3.984   5.520  -36.798 1.00 43.65  ? 44   ILE B CB  1 
ATOM   1955 C CG1 . ILE B 1 63  ? 3.704   4.324  -35.880 1.00 33.80  ? 44   ILE B CG1 1 
ATOM   1956 C CG2 . ILE B 1 63  ? 3.443   5.282  -38.213 1.00 38.10  ? 44   ILE B CG2 1 
ATOM   1957 C CD1 . ILE B 1 63  ? 4.305   3.036  -36.358 1.00 36.60  ? 44   ILE B CD1 1 
ATOM   1958 N N   . THR B 1 64  ? 5.336   8.289  -37.207 1.00 38.10  ? 45   THR B N   1 
ATOM   1959 C CA  . THR B 1 64  ? 5.311   9.516  -38.004 1.00 41.03  ? 45   THR B CA  1 
ATOM   1960 C C   . THR B 1 64  ? 6.578   10.346 -37.853 1.00 39.11  ? 45   THR B C   1 
ATOM   1961 O O   . THR B 1 64  ? 6.717   11.386 -38.499 1.00 36.39  ? 45   THR B O   1 
ATOM   1962 C CB  . THR B 1 64  ? 4.131   10.430 -37.625 1.00 44.08  ? 45   THR B CB  1 
ATOM   1963 O OG1 . THR B 1 64  ? 4.338   10.962 -36.307 1.00 43.29  ? 45   THR B OG1 1 
ATOM   1964 C CG2 . THR B 1 64  ? 2.815   9.679  -37.681 1.00 33.78  ? 45   THR B CG2 1 
ATOM   1965 N N   . ASN B 1 65  ? 7.480   9.902  -36.983 1.00 37.50  ? 46   ASN B N   1 
ATOM   1966 C CA  . ASN B 1 65  ? 8.728   10.628 -36.723 1.00 40.42  ? 46   ASN B CA  1 
ATOM   1967 C C   . ASN B 1 65  ? 8.535   12.077 -36.225 1.00 34.11  ? 46   ASN B C   1 
ATOM   1968 O O   . ASN B 1 65  ? 9.091   13.021 -36.779 1.00 26.75  ? 46   ASN B O   1 
ATOM   1969 C CB  . ASN B 1 65  ? 9.654   10.595 -37.945 1.00 35.81  ? 46   ASN B CB  1 
ATOM   1970 C CG  . ASN B 1 65  ? 10.598  9.409  -37.946 1.00 37.47  ? 46   ASN B CG  1 
ATOM   1971 O OD1 . ASN B 1 65  ? 10.882  8.803  -36.908 1.00 40.50  ? 46   ASN B OD1 1 
ATOM   1972 N ND2 . ASN B 1 65  ? 11.107  9.082  -39.128 1.00 41.83  ? 46   ASN B ND2 1 
ATOM   1973 N N   . GLU B 1 66  ? 7.750   12.222 -35.163 1.00 35.90  ? 47   GLU B N   1 
ATOM   1974 C CA  . GLU B 1 66  ? 7.471   13.512 -34.558 1.00 35.38  ? 47   GLU B CA  1 
ATOM   1975 C C   . GLU B 1 66  ? 7.637   13.484 -33.041 1.00 34.07  ? 47   GLU B C   1 
ATOM   1976 O O   . GLU B 1 66  ? 7.218   12.539 -32.392 1.00 37.30  ? 47   GLU B O   1 
ATOM   1977 C CB  . GLU B 1 66  ? 6.050   13.933 -34.902 1.00 41.33  ? 47   GLU B CB  1 
ATOM   1978 C CG  . GLU B 1 66  ? 5.828   14.106 -36.392 1.00 48.16  ? 47   GLU B CG  1 
ATOM   1979 C CD  . GLU B 1 66  ? 4.402   14.514 -36.750 1.00 59.05  ? 47   GLU B CD  1 
ATOM   1980 O OE1 . GLU B 1 66  ? 3.631   14.905 -35.835 1.00 68.82  ? 47   GLU B OE1 1 
ATOM   1981 O OE2 . GLU B 1 66  ? 4.062   14.440 -37.956 1.00 50.98  ? 47   GLU B OE2 1 
ATOM   1982 N N   . VAL B 1 67  ? 8.242   14.526 -32.477 1.00 39.89  ? 48   VAL B N   1 
ATOM   1983 C CA  . VAL B 1 67  ? 8.387   14.625 -31.027 1.00 36.55  ? 48   VAL B CA  1 
ATOM   1984 C C   . VAL B 1 67  ? 7.869   15.958 -30.518 1.00 34.28  ? 48   VAL B C   1 
ATOM   1985 O O   . VAL B 1 67  ? 7.825   16.938 -31.252 1.00 32.32  ? 48   VAL B O   1 
ATOM   1986 C CB  . VAL B 1 67  ? 9.850   14.455 -30.562 1.00 29.05  ? 48   VAL B CB  1 
ATOM   1987 C CG1 . VAL B 1 67  ? 10.404  13.160 -31.047 1.00 38.80  ? 48   VAL B CG1 1 
ATOM   1988 C CG2 . VAL B 1 67  ? 10.689  15.573 -31.092 1.00 34.27  ? 48   VAL B CG2 1 
ATOM   1989 N N   . ASP B 1 68  ? 7.493   15.974 -29.244 1.00 40.22  ? 49   ASP B N   1 
ATOM   1990 C CA  . ASP B 1 68  ? 7.035   17.176 -28.564 1.00 30.67  ? 49   ASP B CA  1 
ATOM   1991 C C   . ASP B 1 68  ? 8.009   17.517 -27.451 1.00 33.48  ? 49   ASP B C   1 
ATOM   1992 O O   . ASP B 1 68  ? 8.124   16.784 -26.465 1.00 35.01  ? 49   ASP B O   1 
ATOM   1993 C CB  . ASP B 1 68  ? 5.680   16.915 -27.942 1.00 37.94  ? 49   ASP B CB  1 
ATOM   1994 C CG  . ASP B 1 68  ? 4.676   17.962 -28.307 1.00 46.31  ? 49   ASP B CG  1 
ATOM   1995 O OD1 . ASP B 1 68  ? 4.875   18.583 -29.369 1.00 52.63  ? 49   ASP B OD1 1 
ATOM   1996 O OD2 . ASP B 1 68  ? 3.698   18.164 -27.546 1.00 57.64  ? 49   ASP B OD2 1 
ATOM   1997 N N   . VAL B 1 69  ? 8.718   18.626 -27.594 1.00 26.97  ? 50   VAL B N   1 
ATOM   1998 C CA  . VAL B 1 69  ? 9.726   18.963 -26.610 1.00 24.60  ? 50   VAL B CA  1 
ATOM   1999 C C   . VAL B 1 69  ? 9.413   20.254 -25.838 1.00 29.76  ? 50   VAL B C   1 
ATOM   2000 O O   . VAL B 1 69  ? 8.837   21.200 -26.386 1.00 24.74  ? 50   VAL B O   1 
ATOM   2001 C CB  . VAL B 1 69  ? 11.079  19.054 -27.278 1.00 28.32  ? 50   VAL B CB  1 
ATOM   2002 C CG1 . VAL B 1 69  ? 12.173  19.262 -26.234 1.00 30.68  ? 50   VAL B CG1 1 
ATOM   2003 C CG2 . VAL B 1 69  ? 11.331  17.779 -28.056 1.00 33.31  ? 50   VAL B CG2 1 
ATOM   2004 N N   . VAL B 1 70  ? 9.765   20.269 -24.552 1.00 23.94  ? 51   VAL B N   1 
ATOM   2005 C CA  . VAL B 1 70  ? 9.782   21.498 -23.775 1.00 17.74  ? 51   VAL B CA  1 
ATOM   2006 C C   . VAL B 1 70  ? 11.225  21.774 -23.397 1.00 22.77  ? 51   VAL B C   1 
ATOM   2007 O O   . VAL B 1 70  ? 11.904  20.905 -22.826 1.00 24.80  ? 51   VAL B O   1 
ATOM   2008 C CB  . VAL B 1 70  ? 8.934   21.387 -22.507 1.00 18.23  ? 51   VAL B CB  1 
ATOM   2009 C CG1 . VAL B 1 70  ? 9.180   22.583 -21.598 1.00 14.01  ? 51   VAL B CG1 1 
ATOM   2010 C CG2 . VAL B 1 70  ? 7.468   21.274 -22.880 1.00 22.19  ? 51   VAL B CG2 1 
ATOM   2011 N N   . PHE B 1 71  ? 11.696  22.979 -23.723 1.00 22.23  ? 52   PHE B N   1 
ATOM   2012 C CA  . PHE B 1 71  ? 13.078  23.371 -23.454 1.00 21.64  ? 52   PHE B CA  1 
ATOM   2013 C C   . PHE B 1 71  ? 13.203  24.870 -23.173 1.00 23.96  ? 52   PHE B C   1 
ATOM   2014 O O   . PHE B 1 71  ? 12.361  25.661 -23.617 1.00 23.27  ? 52   PHE B O   1 
ATOM   2015 C CB  . PHE B 1 71  ? 13.949  22.999 -24.655 1.00 20.67  ? 52   PHE B CB  1 
ATOM   2016 C CG  . PHE B 1 71  ? 13.499  23.626 -25.938 1.00 22.29  ? 52   PHE B CG  1 
ATOM   2017 C CD1 . PHE B 1 71  ? 12.472  23.059 -26.676 1.00 23.40  ? 52   PHE B CD1 1 
ATOM   2018 C CD2 . PHE B 1 71  ? 14.102  24.789 -26.409 1.00 21.80  ? 52   PHE B CD2 1 
ATOM   2019 C CE1 . PHE B 1 71  ? 12.038  23.647 -27.865 1.00 23.62  ? 52   PHE B CE1 1 
ATOM   2020 C CE2 . PHE B 1 71  ? 13.674  25.379 -27.592 1.00 22.00  ? 52   PHE B CE2 1 
ATOM   2021 C CZ  . PHE B 1 71  ? 12.633  24.806 -28.319 1.00 18.83  ? 52   PHE B CZ  1 
ATOM   2022 N N   . TRP B 1 72  ? 14.252  25.258 -22.442 1.00 22.67  ? 53   TRP B N   1 
ATOM   2023 C CA  . TRP B 1 72  ? 14.627  26.668 -22.321 1.00 19.04  ? 53   TRP B CA  1 
ATOM   2024 C C   . TRP B 1 72  ? 15.554  26.991 -23.475 1.00 21.94  ? 53   TRP B C   1 
ATOM   2025 O O   . TRP B 1 72  ? 16.513  26.256 -23.709 1.00 17.57  ? 53   TRP B O   1 
ATOM   2026 C CB  . TRP B 1 72  ? 15.382  26.953 -21.024 1.00 15.24  ? 53   TRP B CB  1 
ATOM   2027 C CG  . TRP B 1 72  ? 14.607  26.704 -19.795 1.00 16.05  ? 53   TRP B CG  1 
ATOM   2028 C CD1 . TRP B 1 72  ? 13.315  26.262 -19.706 1.00 19.66  ? 53   TRP B CD1 1 
ATOM   2029 C CD2 . TRP B 1 72  ? 15.074  26.862 -18.453 1.00 20.26  ? 53   TRP B CD2 1 
ATOM   2030 N NE1 . TRP B 1 72  ? 12.948  26.140 -18.385 1.00 18.05  ? 53   TRP B NE1 1 
ATOM   2031 C CE2 . TRP B 1 72  ? 14.004  26.498 -17.596 1.00 20.63  ? 53   TRP B CE2 1 
ATOM   2032 C CE3 . TRP B 1 72  ? 16.281  27.288 -17.890 1.00 26.83  ? 53   TRP B CE3 1 
ATOM   2033 C CZ2 . TRP B 1 72  ? 14.117  26.546 -16.202 1.00 19.76  ? 53   TRP B CZ2 1 
ATOM   2034 C CZ3 . TRP B 1 72  ? 16.395  27.338 -16.503 1.00 28.45  ? 53   TRP B CZ3 1 
ATOM   2035 C CH2 . TRP B 1 72  ? 15.315  26.965 -15.674 1.00 26.01  ? 53   TRP B CH2 1 
ATOM   2036 N N   . GLN B 1 73  ? 15.273  28.087 -24.188 1.00 24.96  ? 54   GLN B N   1 
ATOM   2037 C CA  . GLN B 1 73  ? 16.120  28.529 -25.295 1.00 21.33  ? 54   GLN B CA  1 
ATOM   2038 C C   . GLN B 1 73  ? 16.964  29.724 -24.877 1.00 20.54  ? 54   GLN B C   1 
ATOM   2039 O O   . GLN B 1 73  ? 16.627  30.869 -25.144 1.00 24.15  ? 54   GLN B O   1 
ATOM   2040 C CB  . GLN B 1 73  ? 15.277  28.866 -26.514 1.00 15.68  ? 54   GLN B CB  1 
ATOM   2041 C CG  . GLN B 1 73  ? 16.096  29.269 -27.711 1.00 18.00  ? 54   GLN B CG  1 
ATOM   2042 C CD  . GLN B 1 73  ? 15.252  29.446 -28.963 1.00 34.32  ? 54   GLN B CD  1 
ATOM   2043 O OE1 . GLN B 1 73  ? 14.511  28.534 -29.386 1.00 27.25  ? 54   GLN B OE1 1 
ATOM   2044 N NE2 . GLN B 1 73  ? 15.341  30.638 -29.558 1.00 45.44  ? 54   GLN B NE2 1 
ATOM   2045 N N   . GLN B 1 74  ? 18.073  29.455 -24.210 1.00 21.66  ? 55   GLN B N   1 
ATOM   2046 C CA  . GLN B 1 74  ? 18.896  30.537 -23.685 1.00 25.12  ? 55   GLN B CA  1 
ATOM   2047 C C   . GLN B 1 74  ? 19.684  31.257 -24.783 1.00 27.11  ? 55   GLN B C   1 
ATOM   2048 O O   . GLN B 1 74  ? 20.586  30.678 -25.398 1.00 26.13  ? 55   GLN B O   1 
ATOM   2049 C CB  . GLN B 1 74  ? 19.849  30.008 -22.627 1.00 27.95  ? 55   GLN B CB  1 
ATOM   2050 C CG  . GLN B 1 74  ? 20.777  31.062 -22.072 1.00 30.87  ? 55   GLN B CG  1 
ATOM   2051 C CD  . GLN B 1 74  ? 21.689  30.501 -21.005 1.00 46.06  ? 55   GLN B CD  1 
ATOM   2052 O OE1 . GLN B 1 74  ? 21.280  29.647 -20.205 1.00 51.27  ? 55   GLN B OE1 1 
ATOM   2053 N NE2 . GLN B 1 74  ? 22.940  30.966 -20.991 1.00 48.44  ? 55   GLN B NE2 1 
ATOM   2054 N N   . THR B 1 75  ? 19.347  32.527 -25.006 1.00 25.34  ? 56   THR B N   1 
ATOM   2055 C CA  . THR B 1 75  ? 19.904  33.316 -26.104 1.00 18.07  ? 56   THR B CA  1 
ATOM   2056 C C   . THR B 1 75  ? 20.629  34.553 -25.571 1.00 24.94  ? 56   THR B C   1 
ATOM   2057 O O   . THR B 1 75  ? 20.096  35.293 -24.734 1.00 23.42  ? 56   THR B O   1 
ATOM   2058 C CB  . THR B 1 75  ? 18.797  33.747 -27.062 1.00 21.72  ? 56   THR B CB  1 
ATOM   2059 O OG1 . THR B 1 75  ? 17.944  32.620 -27.363 1.00 23.85  ? 56   THR B OG1 1 
ATOM   2060 C CG2 . THR B 1 75  ? 19.389  34.297 -28.333 1.00 21.67  ? 56   THR B CG2 1 
ATOM   2061 N N   . THR B 1 76  ? 21.848  34.779 -26.056 1.00 24.84  ? 57   THR B N   1 
ATOM   2062 C CA  . THR B 1 76  ? 22.704  35.833 -25.503 1.00 25.95  ? 57   THR B CA  1 
ATOM   2063 C C   . THR B 1 76  ? 23.446  36.661 -26.573 1.00 25.33  ? 57   THR B C   1 
ATOM   2064 O O   . THR B 1 76  ? 24.045  36.115 -27.492 1.00 27.81  ? 57   THR B O   1 
ATOM   2065 C CB  . THR B 1 76  ? 23.706  35.234 -24.482 1.00 22.21  ? 57   THR B CB  1 
ATOM   2066 O OG1 . THR B 1 76  ? 22.979  34.783 -23.326 1.00 24.23  ? 57   THR B OG1 1 
ATOM   2067 C CG2 . THR B 1 76  ? 24.740  36.285 -24.046 1.00 30.52  ? 57   THR B CG2 1 
ATOM   2068 N N   . TRP B 1 77  ? 23.416  37.981 -26.453 1.00 24.65  ? 58   TRP B N   1 
ATOM   2069 C CA  . TRP B 1 77  ? 24.126  38.811 -27.416 1.00 25.96  ? 58   TRP B CA  1 
ATOM   2070 C C   . TRP B 1 77  ? 24.442  40.165 -26.814 1.00 30.34  ? 58   TRP B C   1 
ATOM   2071 O O   . TRP B 1 77  ? 24.039  40.465 -25.689 1.00 32.96  ? 58   TRP B O   1 
ATOM   2072 C CB  . TRP B 1 77  ? 23.299  39.001 -28.689 1.00 24.49  ? 58   TRP B CB  1 
ATOM   2073 C CG  . TRP B 1 77  ? 22.079  39.853 -28.460 1.00 30.76  ? 58   TRP B CG  1 
ATOM   2074 C CD1 . TRP B 1 77  ? 21.965  41.227 -28.626 1.00 25.82  ? 58   TRP B CD1 1 
ATOM   2075 C CD2 . TRP B 1 77  ? 20.804  39.397 -27.997 1.00 25.66  ? 58   TRP B CD2 1 
ATOM   2076 N NE1 . TRP B 1 77  ? 20.693  41.632 -28.290 1.00 20.90  ? 58   TRP B NE1 1 
ATOM   2077 C CE2 . TRP B 1 77  ? 19.962  40.533 -27.909 1.00 24.16  ? 58   TRP B CE2 1 
ATOM   2078 C CE3 . TRP B 1 77  ? 20.298  38.143 -27.646 1.00 21.27  ? 58   TRP B CE3 1 
ATOM   2079 C CZ2 . TRP B 1 77  ? 18.637  40.436 -27.495 1.00 20.70  ? 58   TRP B CZ2 1 
ATOM   2080 C CZ3 . TRP B 1 77  ? 18.992  38.053 -27.227 1.00 22.43  ? 58   TRP B CZ3 1 
ATOM   2081 C CH2 . TRP B 1 77  ? 18.170  39.197 -27.154 1.00 20.89  ? 58   TRP B CH2 1 
ATOM   2082 N N   . SER B 1 78  ? 25.140  40.997 -27.576 1.00 27.53  ? 59   SER B N   1 
ATOM   2083 C CA  . SER B 1 78  ? 25.540  42.301 -27.071 1.00 26.45  ? 59   SER B CA  1 
ATOM   2084 C C   . SER B 1 78  ? 24.936  43.461 -27.858 1.00 26.01  ? 59   SER B C   1 
ATOM   2085 O O   . SER B 1 78  ? 24.942  43.452 -29.092 1.00 29.55  ? 59   SER B O   1 
ATOM   2086 C CB  . SER B 1 78  ? 27.060  42.401 -27.061 1.00 38.43  ? 59   SER B CB  1 
ATOM   2087 O OG  . SER B 1 78  ? 27.474  43.675 -26.605 1.00 51.78  ? 59   SER B OG  1 
ATOM   2088 N N   . ASP B 1 79  ? 24.422  44.458 -27.132 1.00 29.28  ? 60   ASP B N   1 
ATOM   2089 C CA  . ASP B 1 79  ? 23.822  45.662 -27.733 1.00 33.20  ? 60   ASP B CA  1 
ATOM   2090 C C   . ASP B 1 79  ? 24.271  46.926 -26.990 1.00 30.17  ? 60   ASP B C   1 
ATOM   2091 O O   . ASP B 1 79  ? 23.659  47.305 -25.991 1.00 32.59  ? 60   ASP B O   1 
ATOM   2092 C CB  . ASP B 1 79  ? 22.283  45.554 -27.727 1.00 33.41  ? 60   ASP B CB  1 
ATOM   2093 C CG  . ASP B 1 79  ? 21.601  46.581 -28.648 1.00 41.24  ? 60   ASP B CG  1 
ATOM   2094 O OD1 . ASP B 1 79  ? 22.213  47.643 -28.941 1.00 44.57  ? 60   ASP B OD1 1 
ATOM   2095 O OD2 . ASP B 1 79  ? 20.446  46.320 -29.070 1.00 33.12  ? 60   ASP B OD2 1 
ATOM   2096 N N   . ARG B 1 80  ? 25.315  47.586 -27.492 1.00 27.13  ? 61   ARG B N   1 
ATOM   2097 C CA  . ARG B 1 80  ? 25.915  48.734 -26.790 1.00 33.07  ? 61   ARG B CA  1 
ATOM   2098 C C   . ARG B 1 80  ? 24.982  49.944 -26.673 1.00 29.39  ? 61   ARG B C   1 
ATOM   2099 O O   . ARG B 1 80  ? 25.154  50.777 -25.800 1.00 26.75  ? 61   ARG B O   1 
ATOM   2100 C CB  . ARG B 1 80  ? 27.232  49.156 -27.446 1.00 40.99  ? 61   ARG B CB  1 
ATOM   2101 C CG  . ARG B 1 80  ? 28.212  48.008 -27.714 1.00 62.41  ? 61   ARG B CG  1 
ATOM   2102 C CD  . ARG B 1 80  ? 29.002  47.565 -26.471 1.00 65.52  ? 61   ARG B CD  1 
ATOM   2103 N NE  . ARG B 1 80  ? 30.082  46.632 -26.825 1.00 80.94  ? 61   ARG B NE  1 
ATOM   2104 C CZ  . ARG B 1 80  ? 30.263  45.419 -26.293 1.00 83.09  ? 61   ARG B CZ  1 
ATOM   2105 N NH1 . ARG B 1 80  ? 29.437  44.963 -25.348 1.00 64.80  ? 61   ARG B NH1 1 
ATOM   2106 N NH2 . ARG B 1 80  ? 31.283  44.664 -26.705 1.00 73.87  ? 61   ARG B NH2 1 
ATOM   2107 N N   . THR B 1 81  ? 24.009  50.032 -27.572 1.00 30.71  ? 62   THR B N   1 
ATOM   2108 C CA  . THR B 1 81  ? 22.942  51.025 -27.513 1.00 26.23  ? 62   THR B CA  1 
ATOM   2109 C C   . THR B 1 81  ? 22.229  51.057 -26.151 1.00 27.48  ? 62   THR B C   1 
ATOM   2110 O O   . THR B 1 81  ? 21.704  52.083 -25.743 1.00 26.30  ? 62   THR B O   1 
ATOM   2111 C CB  . THR B 1 81  ? 21.889  50.704 -28.613 1.00 32.24  ? 62   THR B CB  1 
ATOM   2112 O OG1 . THR B 1 81  ? 22.531  50.674 -29.892 1.00 34.14  ? 62   THR B OG1 1 
ATOM   2113 C CG2 . THR B 1 81  ? 20.733  51.704 -28.643 1.00 38.68  ? 62   THR B CG2 1 
ATOM   2114 N N   . LEU B 1 82  ? 22.192  49.927 -25.457 1.00 28.07  ? 63   LEU B N   1 
ATOM   2115 C CA  . LEU B 1 82  ? 21.460  49.842 -24.195 1.00 25.11  ? 63   LEU B CA  1 
ATOM   2116 C C   . LEU B 1 82  ? 22.307  50.170 -22.960 1.00 26.42  ? 63   LEU B C   1 
ATOM   2117 O O   . LEU B 1 82  ? 21.783  50.211 -21.843 1.00 24.25  ? 63   LEU B O   1 
ATOM   2118 C CB  . LEU B 1 82  ? 20.876  48.443 -24.020 1.00 21.19  ? 63   LEU B CB  1 
ATOM   2119 C CG  . LEU B 1 82  ? 20.057  47.908 -25.179 1.00 21.98  ? 63   LEU B CG  1 
ATOM   2120 C CD1 . LEU B 1 82  ? 19.860  46.406 -25.036 1.00 25.34  ? 63   LEU B CD1 1 
ATOM   2121 C CD2 . LEU B 1 82  ? 18.735  48.620 -25.189 1.00 22.63  ? 63   LEU B CD2 1 
ATOM   2122 N N   . ALA B 1 83  ? 23.607  50.389 -23.150 1.00 28.87  ? 64   ALA B N   1 
ATOM   2123 C CA  . ALA B 1 83  ? 24.533  50.524 -22.018 1.00 22.82  ? 64   ALA B CA  1 
ATOM   2124 C C   . ALA B 1 83  ? 24.321  51.820 -21.226 1.00 26.51  ? 64   ALA B C   1 
ATOM   2125 O O   . ALA B 1 83  ? 23.832  52.823 -21.753 1.00 24.26  ? 64   ALA B O   1 
ATOM   2126 C CB  . ALA B 1 83  ? 25.979  50.413 -22.483 1.00 18.83  ? 64   ALA B CB  1 
ATOM   2127 N N   . TRP B 1 84  ? 24.694  51.792 -19.953 1.00 26.22  ? 65   TRP B N   1 
ATOM   2128 C CA  . TRP B 1 84  ? 24.645  52.982 -19.119 1.00 23.48  ? 65   TRP B CA  1 
ATOM   2129 C C   . TRP B 1 84  ? 25.799  52.954 -18.109 1.00 28.13  ? 65   TRP B C   1 
ATOM   2130 O O   . TRP B 1 84  ? 26.423  51.911 -17.915 1.00 25.25  ? 65   TRP B O   1 
ATOM   2131 C CB  . TRP B 1 84  ? 23.288  53.093 -18.414 1.00 20.17  ? 65   TRP B CB  1 
ATOM   2132 C CG  . TRP B 1 84  ? 23.010  52.036 -17.358 1.00 24.73  ? 65   TRP B CG  1 
ATOM   2133 C CD1 . TRP B 1 84  ? 23.288  52.117 -16.020 1.00 26.82  ? 65   TRP B CD1 1 
ATOM   2134 C CD2 . TRP B 1 84  ? 22.379  50.751 -17.557 1.00 25.92  ? 65   TRP B CD2 1 
ATOM   2135 N NE1 . TRP B 1 84  ? 22.881  50.963 -15.381 1.00 25.77  ? 65   TRP B NE1 1 
ATOM   2136 C CE2 . TRP B 1 84  ? 22.309  50.117 -16.299 1.00 25.92  ? 65   TRP B CE2 1 
ATOM   2137 C CE3 . TRP B 1 84  ? 21.877  50.074 -18.680 1.00 24.31  ? 65   TRP B CE3 1 
ATOM   2138 C CZ2 . TRP B 1 84  ? 21.746  48.835 -16.133 1.00 26.61  ? 65   TRP B CZ2 1 
ATOM   2139 C CZ3 . TRP B 1 84  ? 21.322  48.808 -18.514 1.00 21.21  ? 65   TRP B CZ3 1 
ATOM   2140 C CH2 . TRP B 1 84  ? 21.261  48.202 -17.250 1.00 22.79  ? 65   TRP B CH2 1 
ATOM   2141 N N   . ASN B 1 85  ? 26.090  54.100 -17.487 1.00 34.72  ? 66   ASN B N   1 
ATOM   2142 C CA  . ASN B 1 85  ? 27.113  54.190 -16.431 1.00 36.26  ? 66   ASN B CA  1 
ATOM   2143 C C   . ASN B 1 85  ? 26.550  53.619 -15.122 1.00 38.01  ? 66   ASN B C   1 
ATOM   2144 O O   . ASN B 1 85  ? 25.629  54.205 -14.537 1.00 39.30  ? 66   ASN B O   1 
ATOM   2145 C CB  . ASN B 1 85  ? 27.552  55.663 -16.246 1.00 39.42  ? 66   ASN B CB  1 
ATOM   2146 C CG  . ASN B 1 85  ? 28.786  55.828 -15.334 1.00 50.10  ? 66   ASN B CG  1 
ATOM   2147 O OD1 . ASN B 1 85  ? 29.120  54.939 -14.540 1.00 55.96  ? 66   ASN B OD1 1 
ATOM   2148 N ND2 . ASN B 1 85  ? 29.455  56.988 -15.440 1.00 43.68  ? 66   ASN B ND2 1 
ATOM   2149 N N   . SER B 1 86  ? 27.085  52.486 -14.658 1.00 29.37  ? 67   SER B N   1 
ATOM   2150 C CA  . SER B 1 86  ? 26.511  51.843 -13.468 1.00 40.61  ? 67   SER B CA  1 
ATOM   2151 C C   . SER B 1 86  ? 27.213  52.226 -12.171 1.00 48.60  ? 67   SER B C   1 
ATOM   2152 O O   . SER B 1 86  ? 27.194  51.456 -11.207 1.00 47.10  ? 67   SER B O   1 
ATOM   2153 C CB  . SER B 1 86  ? 26.485  50.319 -13.611 1.00 39.61  ? 67   SER B CB  1 
ATOM   2154 O OG  . SER B 1 86  ? 27.776  49.761 -13.453 1.00 31.43  ? 67   SER B OG  1 
ATOM   2155 N N   . SER B 1 87  ? 27.811  53.419 -12.156 1.00 57.14  ? 68   SER B N   1 
ATOM   2156 C CA  . SER B 1 87  ? 28.620  53.887 -11.030 1.00 56.55  ? 68   SER B CA  1 
ATOM   2157 C C   . SER B 1 87  ? 27.874  53.828 -9.685  1.00 61.10  ? 68   SER B C   1 
ATOM   2158 O O   . SER B 1 87  ? 28.254  53.064 -8.783  1.00 70.68  ? 68   SER B O   1 
ATOM   2159 C CB  . SER B 1 87  ? 29.154  55.298 -11.306 1.00 58.70  ? 68   SER B CB  1 
ATOM   2160 O OG  . SER B 1 87  ? 30.119  55.677 -10.336 1.00 57.22  ? 68   SER B OG  1 
ATOM   2161 N N   . HIS B 1 88  ? 26.817  54.621 -9.549  1.00 48.65  ? 69   HIS B N   1 
ATOM   2162 C CA  . HIS B 1 88  ? 26.000  54.559 -8.341  1.00 48.70  ? 69   HIS B CA  1 
ATOM   2163 C C   . HIS B 1 88  ? 24.588  54.176 -8.732  1.00 46.56  ? 69   HIS B C   1 
ATOM   2164 O O   . HIS B 1 88  ? 23.618  54.808 -8.326  1.00 51.70  ? 69   HIS B O   1 
ATOM   2165 C CB  . HIS B 1 88  ? 26.020  55.892 -7.590  1.00 56.15  ? 69   HIS B CB  1 
ATOM   2166 C CG  . HIS B 1 88  ? 27.377  56.275 -7.098  1.00 71.68  ? 69   HIS B CG  1 
ATOM   2167 N ND1 . HIS B 1 88  ? 27.978  55.661 -6.021  1.00 91.77  ? 69   HIS B ND1 1 
ATOM   2168 C CD2 . HIS B 1 88  ? 28.266  57.194 -7.553  1.00 71.66  ? 69   HIS B CD2 1 
ATOM   2169 C CE1 . HIS B 1 88  ? 29.174  56.190 -5.826  1.00 92.07  ? 69   HIS B CE1 1 
ATOM   2170 N NE2 . HIS B 1 88  ? 29.370  57.124 -6.742  1.00 79.82  ? 69   HIS B NE2 1 
ATOM   2171 N N   . SER B 1 89  ? 24.488  53.119 -9.525  1.00 44.67  ? 70   SER B N   1 
ATOM   2172 C CA  . SER B 1 89  ? 23.252  52.780 -10.196 1.00 38.71  ? 70   SER B CA  1 
ATOM   2173 C C   . SER B 1 89  ? 23.098  51.281 -10.222 1.00 32.18  ? 70   SER B C   1 
ATOM   2174 O O   . SER B 1 89  ? 24.069  50.561 -9.995  1.00 26.73  ? 70   SER B O   1 
ATOM   2175 C CB  . SER B 1 89  ? 23.301  53.309 -11.629 1.00 41.05  ? 70   SER B CB  1 
ATOM   2176 O OG  . SER B 1 89  ? 23.629  54.685 -11.640 1.00 48.34  ? 70   SER B OG  1 
ATOM   2177 N N   . PRO B 1 90  ? 21.871  50.805 -10.505 1.00 37.32  ? 71   PRO B N   1 
ATOM   2178 C CA  . PRO B 1 90  ? 21.680  49.367 -10.735 1.00 33.00  ? 71   PRO B CA  1 
ATOM   2179 C C   . PRO B 1 90  ? 22.535  48.910 -11.914 1.00 31.85  ? 71   PRO B C   1 
ATOM   2180 O O   . PRO B 1 90  ? 22.735  49.682 -12.858 1.00 34.74  ? 71   PRO B O   1 
ATOM   2181 C CB  . PRO B 1 90  ? 20.194  49.264 -11.102 1.00 34.61  ? 71   PRO B CB  1 
ATOM   2182 C CG  . PRO B 1 90  ? 19.546  50.496 -10.525 1.00 36.64  ? 71   PRO B CG  1 
ATOM   2183 C CD  . PRO B 1 90  ? 20.602  51.565 -10.575 1.00 34.72  ? 71   PRO B CD  1 
ATOM   2184 N N   . ASP B 1 91  ? 23.033  47.680 -11.859 1.00 27.22  ? 72   ASP B N   1 
ATOM   2185 C CA  . ASP B 1 91  ? 23.837  47.133 -12.944 1.00 32.52  ? 72   ASP B CA  1 
ATOM   2186 C C   . ASP B 1 91  ? 23.033  46.167 -13.833 1.00 33.66  ? 72   ASP B C   1 
ATOM   2187 O O   . ASP B 1 91  ? 23.585  45.559 -14.762 1.00 29.90  ? 72   ASP B O   1 
ATOM   2188 C CB  . ASP B 1 91  ? 25.056  46.421 -12.366 1.00 40.20  ? 72   ASP B CB  1 
ATOM   2189 C CG  . ASP B 1 91  ? 24.692  45.536 -11.180 1.00 53.94  ? 72   ASP B CG  1 
ATOM   2190 O OD1 . ASP B 1 91  ? 23.499  45.570 -10.768 1.00 46.04  ? 72   ASP B OD1 1 
ATOM   2191 O OD2 . ASP B 1 91  ? 25.589  44.820 -10.657 1.00 60.54  ? 72   ASP B OD2 1 
ATOM   2192 N N   . GLN B 1 92  ? 21.734  46.040 -13.553 1.00 30.28  ? 73   GLN B N   1 
ATOM   2193 C CA  . GLN B 1 92  ? 20.848  45.219 -14.366 1.00 28.53  ? 73   GLN B CA  1 
ATOM   2194 C C   . GLN B 1 92  ? 19.374  45.630 -14.260 1.00 26.50  ? 73   GLN B C   1 
ATOM   2195 O O   . GLN B 1 92  ? 18.938  46.118 -13.220 1.00 31.74  ? 73   GLN B O   1 
ATOM   2196 C CB  . GLN B 1 92  ? 20.969  43.785 -13.910 1.00 35.28  ? 73   GLN B CB  1 
ATOM   2197 C CG  . GLN B 1 92  ? 20.674  43.669 -12.444 1.00 44.22  ? 73   GLN B CG  1 
ATOM   2198 C CD  . GLN B 1 92  ? 20.514  42.242 -12.016 1.00 50.81  ? 73   GLN B CD  1 
ATOM   2199 O OE1 . GLN B 1 92  ? 21.262  41.367 -12.457 1.00 50.60  ? 73   GLN B OE1 1 
ATOM   2200 N NE2 . GLN B 1 92  ? 19.526  41.986 -11.157 1.00 55.42  ? 73   GLN B NE2 1 
ATOM   2201 N N   . VAL B 1 93  ? 18.615  45.415 -15.338 1.00 24.63  ? 74   VAL B N   1 
ATOM   2202 C CA  . VAL B 1 93  ? 17.163  45.622 -15.350 1.00 23.31  ? 74   VAL B CA  1 
ATOM   2203 C C   . VAL B 1 93  ? 16.464  44.542 -16.206 1.00 24.27  ? 74   VAL B C   1 
ATOM   2204 O O   . VAL B 1 93  ? 17.109  43.869 -17.012 1.00 23.92  ? 74   VAL B O   1 
ATOM   2205 C CB  . VAL B 1 93  ? 16.785  47.017 -15.882 1.00 21.58  ? 74   VAL B CB  1 
ATOM   2206 C CG1 . VAL B 1 93  ? 17.220  48.118 -14.920 1.00 22.78  ? 74   VAL B CG1 1 
ATOM   2207 C CG2 . VAL B 1 93  ? 17.395  47.231 -17.257 1.00 25.67  ? 74   VAL B CG2 1 
ATOM   2208 N N   . SER B 1 94  ? 15.159  44.362 -16.017 1.00 19.73  ? 75   SER B N   1 
ATOM   2209 C CA  . SER B 1 94  ? 14.398  43.453 -16.863 1.00 19.80  ? 75   SER B CA  1 
ATOM   2210 C C   . SER B 1 94  ? 13.584  44.283 -17.834 1.00 22.55  ? 75   SER B C   1 
ATOM   2211 O O   . SER B 1 94  ? 12.932  45.263 -17.434 1.00 17.65  ? 75   SER B O   1 
ATOM   2212 C CB  . SER B 1 94  ? 13.466  42.567 -16.034 1.00 21.89  ? 75   SER B CB  1 
ATOM   2213 O OG  . SER B 1 94  ? 14.181  41.491 -15.463 1.00 33.17  ? 75   SER B OG  1 
ATOM   2214 N N   . VAL B 1 95  ? 13.623  43.901 -19.111 1.00 19.50  ? 76   VAL B N   1 
ATOM   2215 C CA  . VAL B 1 95  ? 13.022  44.731 -20.156 1.00 17.37  ? 76   VAL B CA  1 
ATOM   2216 C C   . VAL B 1 95  ? 12.094  43.900 -20.998 1.00 16.98  ? 76   VAL B C   1 
ATOM   2217 O O   . VAL B 1 95  ? 12.468  42.810 -21.423 1.00 21.34  ? 76   VAL B O   1 
ATOM   2218 C CB  . VAL B 1 95  ? 14.105  45.333 -21.074 1.00 18.09  ? 76   VAL B CB  1 
ATOM   2219 C CG1 . VAL B 1 95  ? 13.467  46.177 -22.144 1.00 19.29  ? 76   VAL B CG1 1 
ATOM   2220 C CG2 . VAL B 1 95  ? 15.102  46.157 -20.280 1.00 17.78  ? 76   VAL B CG2 1 
ATOM   2221 N N   . PRO B 1 96  ? 10.877  44.401 -21.245 1.00 16.86  ? 77   PRO B N   1 
ATOM   2222 C CA  . PRO B 1 96  ? 9.984   43.665 -22.157 1.00 17.31  ? 77   PRO B CA  1 
ATOM   2223 C C   . PRO B 1 96  ? 10.644  43.547 -23.542 1.00 16.56  ? 77   PRO B C   1 
ATOM   2224 O O   . PRO B 1 96  ? 11.203  44.547 -24.021 1.00 17.49  ? 77   PRO B O   1 
ATOM   2225 C CB  . PRO B 1 96  ? 8.743   44.572 -22.229 1.00 16.15  ? 77   PRO B CB  1 
ATOM   2226 C CG  . PRO B 1 96  ? 8.809   45.427 -20.988 1.00 15.04  ? 77   PRO B CG  1 
ATOM   2227 C CD  . PRO B 1 96  ? 10.272  45.646 -20.734 1.00 14.12  ? 77   PRO B CD  1 
ATOM   2228 N N   . ILE B 1 97  ? 10.592  42.372 -24.170 1.00 11.86  ? 78   ILE B N   1 
ATOM   2229 C CA  . ILE B 1 97  ? 11.313  42.179 -25.430 1.00 12.56  ? 78   ILE B CA  1 
ATOM   2230 C C   . ILE B 1 97  ? 10.763  43.033 -26.561 1.00 12.90  ? 78   ILE B C   1 
ATOM   2231 O O   . ILE B 1 97  ? 11.440  43.259 -27.547 1.00 16.96  ? 78   ILE B O   1 
ATOM   2232 C CB  . ILE B 1 97  ? 11.382  40.708 -25.899 1.00 13.94  ? 78   ILE B CB  1 
ATOM   2233 C CG1 . ILE B 1 97  ? 9.986   40.157 -26.166 1.00 14.07  ? 78   ILE B CG1 1 
ATOM   2234 C CG2 . ILE B 1 97  ? 12.155  39.855 -24.883 1.00 11.94  ? 78   ILE B CG2 1 
ATOM   2235 C CD1 . ILE B 1 97  ? 9.995   38.819 -26.842 1.00 11.78  ? 78   ILE B CD1 1 
ATOM   2236 N N   . SER B 1 98  ? 9.534   43.507 -26.422 1.00 14.11  ? 79   SER B N   1 
ATOM   2237 C CA  . SER B 1 98  ? 8.969   44.430 -27.402 1.00 13.89  ? 79   SER B CA  1 
ATOM   2238 C C   . SER B 1 98  ? 9.771   45.756 -27.493 1.00 18.36  ? 79   SER B C   1 
ATOM   2239 O O   . SER B 1 98  ? 9.677   46.479 -28.485 1.00 18.42  ? 79   SER B O   1 
ATOM   2240 C CB  . SER B 1 98  ? 7.488   44.697 -27.099 1.00 14.73  ? 79   SER B CB  1 
ATOM   2241 O OG  . SER B 1 98  ? 7.331   45.488 -25.924 1.00 20.07  ? 79   SER B OG  1 
ATOM   2242 N N   . SER B 1 99  ? 10.560  46.071 -26.470 1.00 12.92  ? 80   SER B N   1 
ATOM   2243 C CA  . SER B 1 99  ? 11.369  47.281 -26.495 1.00 13.91  ? 80   SER B CA  1 
ATOM   2244 C C   . SER B 1 99  ? 12.829  47.089 -26.895 1.00 23.00  ? 80   SER B C   1 
ATOM   2245 O O   . SER B 1 99  ? 13.624  47.998 -26.692 1.00 26.44  ? 80   SER B O   1 
ATOM   2246 C CB  . SER B 1 99  ? 11.354  47.949 -25.123 1.00 14.08  ? 80   SER B CB  1 
ATOM   2247 O OG  . SER B 1 99  ? 10.030  48.062 -24.654 1.00 28.96  ? 80   SER B OG  1 
ATOM   2248 N N   . LEU B 1 100 ? 13.191  45.923 -27.434 1.00 22.19  ? 81   LEU B N   1 
ATOM   2249 C CA  . LEU B 1 100 ? 14.590  45.602 -27.739 1.00 16.51  ? 81   LEU B CA  1 
ATOM   2250 C C   . LEU B 1 100 ? 14.697  44.988 -29.116 1.00 20.41  ? 81   LEU B C   1 
ATOM   2251 O O   . LEU B 1 100 ? 13.760  44.329 -29.570 1.00 23.39  ? 81   LEU B O   1 
ATOM   2252 C CB  . LEU B 1 100 ? 15.082  44.535 -26.791 1.00 15.10  ? 81   LEU B CB  1 
ATOM   2253 C CG  . LEU B 1 100 ? 15.221  44.871 -25.333 1.00 18.02  ? 81   LEU B CG  1 
ATOM   2254 C CD1 . LEU B 1 100 ? 15.813  43.663 -24.639 1.00 16.84  ? 81   LEU B CD1 1 
ATOM   2255 C CD2 . LEU B 1 100 ? 16.129  46.060 -25.227 1.00 24.86  ? 81   LEU B CD2 1 
ATOM   2256 N N   . TRP B 1 101 ? 15.837  45.145 -29.776 1.00 17.36  ? 82   TRP B N   1 
ATOM   2257 C CA  . TRP B 1 101 ? 16.101  44.281 -30.909 1.00 14.13  ? 82   TRP B CA  1 
ATOM   2258 C C   . TRP B 1 101 ? 16.352  42.875 -30.373 1.00 19.60  ? 82   TRP B C   1 
ATOM   2259 O O   . TRP B 1 101 ? 16.980  42.691 -29.322 1.00 18.20  ? 82   TRP B O   1 
ATOM   2260 C CB  . TRP B 1 101 ? 17.304  44.746 -31.696 1.00 14.79  ? 82   TRP B CB  1 
ATOM   2261 C CG  . TRP B 1 101 ? 17.650  43.819 -32.815 1.00 17.89  ? 82   TRP B CG  1 
ATOM   2262 C CD1 . TRP B 1 101 ? 17.160  43.854 -34.084 1.00 17.78  ? 82   TRP B CD1 1 
ATOM   2263 C CD2 . TRP B 1 101 ? 18.556  42.706 -32.764 1.00 20.38  ? 82   TRP B CD2 1 
ATOM   2264 N NE1 . TRP B 1 101 ? 17.705  42.841 -34.830 1.00 14.62  ? 82   TRP B NE1 1 
ATOM   2265 C CE2 . TRP B 1 101 ? 18.570  42.122 -34.046 1.00 17.29  ? 82   TRP B CE2 1 
ATOM   2266 C CE3 . TRP B 1 101 ? 19.354  42.143 -31.755 1.00 22.17  ? 82   TRP B CE3 1 
ATOM   2267 C CZ2 . TRP B 1 101 ? 19.353  40.998 -34.356 1.00 16.40  ? 82   TRP B CZ2 1 
ATOM   2268 C CZ3 . TRP B 1 101 ? 20.135  41.022 -32.061 1.00 19.66  ? 82   TRP B CZ3 1 
ATOM   2269 C CH2 . TRP B 1 101 ? 20.124  40.463 -33.356 1.00 16.23  ? 82   TRP B CH2 1 
ATOM   2270 N N   . VAL B 1 102 ? 15.865  41.888 -31.113 1.00 19.41  ? 83   VAL B N   1 
ATOM   2271 C CA  . VAL B 1 102 ? 15.999  40.480 -30.758 1.00 20.97  ? 83   VAL B CA  1 
ATOM   2272 C C   . VAL B 1 102 ? 16.348  39.709 -32.039 1.00 22.62  ? 83   VAL B C   1 
ATOM   2273 O O   . VAL B 1 102 ? 15.817  40.017 -33.109 1.00 26.27  ? 83   VAL B O   1 
ATOM   2274 C CB  . VAL B 1 102 ? 14.674  39.950 -30.149 1.00 22.54  ? 83   VAL B CB  1 
ATOM   2275 C CG1 . VAL B 1 102 ? 14.512  38.445 -30.382 1.00 23.19  ? 83   VAL B CG1 1 
ATOM   2276 C CG2 . VAL B 1 102 ? 14.576  40.309 -28.671 1.00 15.97  ? 83   VAL B CG2 1 
ATOM   2277 N N   . PRO B 1 103 ? 17.244  38.712 -31.945 1.00 21.64  ? 84   PRO B N   1 
ATOM   2278 C CA  . PRO B 1 103 ? 17.610  37.952 -33.149 1.00 18.37  ? 84   PRO B CA  1 
ATOM   2279 C C   . PRO B 1 103 ? 16.439  37.122 -33.664 1.00 19.28  ? 84   PRO B C   1 
ATOM   2280 O O   . PRO B 1 103 ? 15.672  36.618 -32.838 1.00 18.50  ? 84   PRO B O   1 
ATOM   2281 C CB  . PRO B 1 103 ? 18.747  37.039 -32.659 1.00 18.60  ? 84   PRO B CB  1 
ATOM   2282 C CG  . PRO B 1 103 ? 18.582  36.966 -31.173 1.00 18.12  ? 84   PRO B CG  1 
ATOM   2283 C CD  . PRO B 1 103 ? 17.987  38.276 -30.746 1.00 22.25  ? 84   PRO B CD  1 
ATOM   2284 N N   . ASP B 1 104 ? 16.314  36.998 -34.992 1.00 20.90  ? 85   ASP B N   1 
ATOM   2285 C CA  . ASP B 1 104 ? 15.195  36.287 -35.654 1.00 20.70  ? 85   ASP B CA  1 
ATOM   2286 C C   . ASP B 1 104 ? 15.443  34.774 -35.858 1.00 24.56  ? 85   ASP B C   1 
ATOM   2287 O O   . ASP B 1 104 ? 15.401  34.245 -36.982 1.00 19.99  ? 85   ASP B O   1 
ATOM   2288 C CB  . ASP B 1 104 ? 14.834  36.947 -36.997 1.00 23.28  ? 85   ASP B CB  1 
ATOM   2289 C CG  . ASP B 1 104 ? 15.997  36.931 -38.006 1.00 26.59  ? 85   ASP B CG  1 
ATOM   2290 O OD1 . ASP B 1 104 ? 17.179  36.955 -37.582 1.00 29.47  ? 85   ASP B OD1 1 
ATOM   2291 O OD2 . ASP B 1 104 ? 15.720  36.892 -39.227 1.00 24.68  ? 85   ASP B OD2 1 
ATOM   2292 N N   . LEU B 1 105 ? 15.684  34.080 -34.750 1.00 28.13  ? 86   LEU B N   1 
ATOM   2293 C CA  . LEU B 1 105 ? 15.989  32.661 -34.783 1.00 18.56  ? 86   LEU B CA  1 
ATOM   2294 C C   . LEU B 1 105 ? 14.724  31.849 -35.073 1.00 20.58  ? 86   LEU B C   1 
ATOM   2295 O O   . LEU B 1 105 ? 13.617  32.251 -34.693 1.00 22.51  ? 86   LEU B O   1 
ATOM   2296 C CB  . LEU B 1 105 ? 16.641  32.240 -33.465 1.00 15.40  ? 86   LEU B CB  1 
ATOM   2297 C CG  . LEU B 1 105 ? 17.916  33.025 -33.110 1.00 15.20  ? 86   LEU B CG  1 
ATOM   2298 C CD1 . LEU B 1 105 ? 18.438  32.644 -31.713 1.00 16.97  ? 86   LEU B CD1 1 
ATOM   2299 C CD2 . LEU B 1 105 ? 19.015  32.825 -34.153 1.00 11.81  ? 86   LEU B CD2 1 
ATOM   2300 N N   . ALA B 1 106 ? 14.892  30.731 -35.785 1.00 18.21  ? 87   ALA B N   1 
ATOM   2301 C CA  . ALA B 1 106 ? 13.795  29.812 -36.063 1.00 16.56  ? 87   ALA B CA  1 
ATOM   2302 C C   . ALA B 1 106 ? 14.320  28.396 -36.081 1.00 21.06  ? 87   ALA B C   1 
ATOM   2303 O O   . ALA B 1 106 ? 15.487  28.171 -36.389 1.00 23.99  ? 87   ALA B O   1 
ATOM   2304 C CB  . ALA B 1 106 ? 13.147  30.134 -37.374 1.00 17.70  ? 87   ALA B CB  1 
ATOM   2305 N N   . ALA B 1 107 ? 13.460  27.439 -35.743 1.00 23.99  ? 88   ALA B N   1 
ATOM   2306 C CA  . ALA B 1 107 ? 13.815  26.017 -35.831 1.00 26.21  ? 88   ALA B CA  1 
ATOM   2307 C C   . ALA B 1 107 ? 13.400  25.480 -37.196 1.00 25.19  ? 88   ALA B C   1 
ATOM   2308 O O   . ALA B 1 107 ? 12.202  25.395 -37.502 1.00 27.90  ? 88   ALA B O   1 
ATOM   2309 C CB  . ALA B 1 107 ? 13.142  25.229 -34.727 1.00 21.62  ? 88   ALA B CB  1 
ATOM   2310 N N   . TYR B 1 108 ? 14.386  25.119 -38.011 1.00 20.93  ? 89   TYR B N   1 
ATOM   2311 C CA  . TYR B 1 108 ? 14.138  24.727 -39.397 1.00 20.73  ? 89   TYR B CA  1 
ATOM   2312 C C   . TYR B 1 108 ? 13.240  23.496 -39.535 1.00 21.91  ? 89   TYR B C   1 
ATOM   2313 O O   . TYR B 1 108 ? 12.499  23.359 -40.515 1.00 23.29  ? 89   TYR B O   1 
ATOM   2314 C CB  . TYR B 1 108 ? 15.464  24.510 -40.131 1.00 22.33  ? 89   TYR B CB  1 
ATOM   2315 C CG  . TYR B 1 108 ? 16.108  25.795 -40.613 1.00 24.62  ? 89   TYR B CG  1 
ATOM   2316 C CD1 . TYR B 1 108 ? 16.673  26.698 -39.716 1.00 28.01  ? 89   TYR B CD1 1 
ATOM   2317 C CD2 . TYR B 1 108 ? 16.150  26.106 -41.967 1.00 23.21  ? 89   TYR B CD2 1 
ATOM   2318 C CE1 . TYR B 1 108 ? 17.262  27.869 -40.154 1.00 21.69  ? 89   TYR B CE1 1 
ATOM   2319 C CE2 . TYR B 1 108 ? 16.736  27.265 -42.417 1.00 20.98  ? 89   TYR B CE2 1 
ATOM   2320 C CZ  . TYR B 1 108 ? 17.286  28.144 -41.512 1.00 24.95  ? 89   TYR B CZ  1 
ATOM   2321 O OH  . TYR B 1 108 ? 17.873  29.298 -41.982 1.00 24.48  ? 89   TYR B OH  1 
ATOM   2322 N N   . ASN B 1 109 ? 13.302  22.597 -38.561 1.00 24.87  ? 90   ASN B N   1 
ATOM   2323 C CA  . ASN B 1 109 ? 12.510  21.362 -38.628 1.00 28.84  ? 90   ASN B CA  1 
ATOM   2324 C C   . ASN B 1 109 ? 11.339  21.335 -37.639 1.00 26.73  ? 90   ASN B C   1 
ATOM   2325 O O   . ASN B 1 109 ? 10.851  20.270 -37.239 1.00 28.25  ? 90   ASN B O   1 
ATOM   2326 C CB  . ASN B 1 109 ? 13.395  20.108 -38.493 1.00 20.35  ? 90   ASN B CB  1 
ATOM   2327 C CG  . ASN B 1 109 ? 14.169  20.057 -37.178 1.00 23.29  ? 90   ASN B CG  1 
ATOM   2328 O OD1 . ASN B 1 109 ? 14.861  21.004 -36.794 1.00 22.69  ? 90   ASN B OD1 1 
ATOM   2329 N ND2 . ASN B 1 109 ? 14.064  18.923 -36.487 1.00 34.14  ? 90   ASN B ND2 1 
ATOM   2330 N N   . ALA B 1 110 ? 10.896  22.522 -37.243 1.00 23.45  ? 91   ALA B N   1 
ATOM   2331 C CA  . ALA B 1 110 ? 9.719   22.637 -36.392 1.00 24.74  ? 91   ALA B CA  1 
ATOM   2332 C C   . ALA B 1 110 ? 8.485   22.436 -37.266 1.00 25.75  ? 91   ALA B C   1 
ATOM   2333 O O   . ALA B 1 110 ? 8.493   22.780 -38.453 1.00 24.69  ? 91   ALA B O   1 
ATOM   2334 C CB  . ALA B 1 110 ? 9.684   23.990 -35.717 1.00 27.09  ? 91   ALA B CB  1 
ATOM   2335 N N   . ILE B 1 111 ? 7.435   21.849 -36.706 1.00 21.45  ? 92   ILE B N   1 
ATOM   2336 C CA  . ILE B 1 111 ? 6.222   21.664 -37.487 1.00 22.43  ? 92   ILE B CA  1 
ATOM   2337 C C   . ILE B 1 111 ? 5.034   22.336 -36.813 1.00 24.03  ? 92   ILE B C   1 
ATOM   2338 O O   . ILE B 1 111 ? 3.884   22.135 -37.194 1.00 23.23  ? 92   ILE B O   1 
ATOM   2339 C CB  . ILE B 1 111 ? 5.925   20.181 -37.792 1.00 24.11  ? 92   ILE B CB  1 
ATOM   2340 C CG1 . ILE B 1 111 ? 5.919   19.359 -36.509 1.00 28.25  ? 92   ILE B CG1 1 
ATOM   2341 C CG2 . ILE B 1 111 ? 6.933   19.622 -38.782 1.00 24.26  ? 92   ILE B CG2 1 
ATOM   2342 C CD1 . ILE B 1 111 ? 5.537   17.899 -36.727 1.00 36.10  ? 92   ILE B CD1 1 
ATOM   2343 N N   . SER B 1 112 ? 5.327   23.140 -35.801 1.00 26.01  ? 93   SER B N   1 
ATOM   2344 C CA  . SER B 1 112 ? 4.317   23.960 -35.136 1.00 21.67  ? 93   SER B CA  1 
ATOM   2345 C C   . SER B 1 112 ? 5.024   25.245 -34.728 1.00 22.47  ? 93   SER B C   1 
ATOM   2346 O O   . SER B 1 112 ? 6.250   25.259 -34.656 1.00 22.53  ? 93   SER B O   1 
ATOM   2347 C CB  . SER B 1 112 ? 3.780   23.228 -33.914 1.00 17.17  ? 93   SER B CB  1 
ATOM   2348 O OG  . SER B 1 112 ? 4.774   23.134 -32.909 1.00 25.49  ? 93   SER B OG  1 
ATOM   2349 N N   . LYS B 1 113 ? 4.288   26.325 -34.464 1.00 27.32  ? 94   LYS B N   1 
ATOM   2350 C CA  . LYS B 1 113 ? 4.962   27.556 -34.008 1.00 24.66  ? 94   LYS B CA  1 
ATOM   2351 C C   . LYS B 1 113 ? 5.322   27.467 -32.532 1.00 20.60  ? 94   LYS B C   1 
ATOM   2352 O O   . LYS B 1 113 ? 4.676   26.734 -31.786 1.00 24.11  ? 94   LYS B O   1 
ATOM   2353 C CB  . LYS B 1 113 ? 4.146   28.810 -34.312 1.00 25.61  ? 94   LYS B CB  1 
ATOM   2354 C CG  . LYS B 1 113 ? 2.834   28.905 -33.577 1.00 37.16  ? 94   LYS B CG  1 
ATOM   2355 C CD  . LYS B 1 113 ? 1.988   30.038 -34.169 1.00 44.65  ? 94   LYS B CD  1 
ATOM   2356 C CE  . LYS B 1 113 ? 2.787   31.341 -34.250 1.00 45.61  ? 94   LYS B CE  1 
ATOM   2357 N NZ  . LYS B 1 113 ? 1.936   32.549 -34.567 1.00 50.44  ? 94   LYS B NZ  1 
ATOM   2358 N N   . PRO B 1 114 ? 6.386   28.173 -32.113 1.00 22.24  ? 95   PRO B N   1 
ATOM   2359 C CA  . PRO B 1 114 ? 6.808   28.078 -30.704 1.00 22.49  ? 95   PRO B CA  1 
ATOM   2360 C C   . PRO B 1 114 ? 5.699   28.541 -29.778 1.00 26.37  ? 95   PRO B C   1 
ATOM   2361 O O   . PRO B 1 114 ? 5.124   29.592 -30.036 1.00 35.53  ? 95   PRO B O   1 
ATOM   2362 C CB  . PRO B 1 114 ? 7.966   29.068 -30.609 1.00 18.91  ? 95   PRO B CB  1 
ATOM   2363 C CG  . PRO B 1 114 ? 8.426   29.270 -32.032 1.00 22.15  ? 95   PRO B CG  1 
ATOM   2364 C CD  . PRO B 1 114 ? 7.233   29.097 -32.892 1.00 20.82  ? 95   PRO B CD  1 
ATOM   2365 N N   . GLU B 1 115 ? 5.376   27.757 -28.751 1.00 26.38  ? 96   GLU B N   1 
ATOM   2366 C CA  . GLU B 1 115 ? 4.421   28.175 -27.721 1.00 22.79  ? 96   GLU B CA  1 
ATOM   2367 C C   . GLU B 1 115 ? 5.205   28.699 -26.505 1.00 26.72  ? 96   GLU B C   1 
ATOM   2368 O O   . GLU B 1 115 ? 5.823   27.902 -25.755 1.00 24.56  ? 96   GLU B O   1 
ATOM   2369 C CB  . GLU B 1 115 ? 3.563   26.982 -27.312 1.00 19.49  ? 96   GLU B CB  1 
ATOM   2370 C CG  . GLU B 1 115 ? 2.411   27.299 -26.370 1.00 33.22  ? 96   GLU B CG  1 
ATOM   2371 C CD  . GLU B 1 115 ? 1.590   26.050 -26.030 1.00 45.96  ? 96   GLU B CD  1 
ATOM   2372 O OE1 . GLU B 1 115 ? 1.741   25.037 -26.766 1.00 46.16  ? 96   GLU B OE1 1 
ATOM   2373 O OE2 . GLU B 1 115 ? 0.811   26.070 -25.030 1.00 54.73  ? 96   GLU B OE2 1 
ATOM   2374 N N   . VAL B 1 116 ? 5.201   30.018 -26.298 1.00 18.06  ? 97   VAL B N   1 
ATOM   2375 C CA  . VAL B 1 116 ? 6.032   30.576 -25.220 1.00 21.68  ? 97   VAL B CA  1 
ATOM   2376 C C   . VAL B 1 116 ? 5.351   30.499 -23.853 1.00 21.69  ? 97   VAL B C   1 
ATOM   2377 O O   . VAL B 1 116 ? 4.324   31.124 -23.635 1.00 26.72  ? 97   VAL B O   1 
ATOM   2378 C CB  . VAL B 1 116 ? 6.493   32.011 -25.493 1.00 15.55  ? 97   VAL B CB  1 
ATOM   2379 C CG1 . VAL B 1 116 ? 7.400   32.457 -24.377 1.00 14.01  ? 97   VAL B CG1 1 
ATOM   2380 C CG2 . VAL B 1 116 ? 7.217   32.091 -26.823 1.00 13.60  ? 97   VAL B CG2 1 
ATOM   2381 N N   . LEU B 1 117 ? 5.941   29.737 -22.935 1.00 18.65  ? 98   LEU B N   1 
ATOM   2382 C CA  . LEU B 1 117 ? 5.311   29.435 -21.652 1.00 15.05  ? 98   LEU B CA  1 
ATOM   2383 C C   . LEU B 1 117 ? 5.542   30.505 -20.578 1.00 18.09  ? 98   LEU B C   1 
ATOM   2384 O O   . LEU B 1 117 ? 4.777   30.624 -19.625 1.00 17.90  ? 98   LEU B O   1 
ATOM   2385 C CB  . LEU B 1 117 ? 5.795   28.077 -21.142 1.00 17.32  ? 98   LEU B CB  1 
ATOM   2386 C CG  . LEU B 1 117 ? 5.497   26.864 -22.036 1.00 21.79  ? 98   LEU B CG  1 
ATOM   2387 C CD1 . LEU B 1 117 ? 6.015   25.575 -21.418 1.00 16.40  ? 98   LEU B CD1 1 
ATOM   2388 C CD2 . LEU B 1 117 ? 4.012   26.738 -22.378 1.00 19.41  ? 98   LEU B CD2 1 
ATOM   2389 N N   . THR B 1 118 ? 6.590   31.300 -20.742 1.00 20.52  ? 99   THR B N   1 
ATOM   2390 C CA  . THR B 1 118 ? 7.008   32.206 -19.682 1.00 19.23  ? 99   THR B CA  1 
ATOM   2391 C C   . THR B 1 118 ? 6.757   33.671 -20.070 1.00 20.66  ? 99   THR B C   1 
ATOM   2392 O O   . THR B 1 118 ? 6.485   33.949 -21.248 1.00 16.89  ? 99   THR B O   1 
ATOM   2393 C CB  . THR B 1 118 ? 8.492   31.993 -19.385 1.00 17.16  ? 99   THR B CB  1 
ATOM   2394 O OG1 . THR B 1 118 ? 9.212   31.986 -20.631 1.00 23.47  ? 99   THR B OG1 1 
ATOM   2395 C CG2 . THR B 1 118 ? 8.697   30.692 -18.669 1.00 16.73  ? 99   THR B CG2 1 
ATOM   2396 N N   . PRO B 1 119 ? 6.836   34.598 -19.079 1.00 17.08  ? 100  PRO B N   1 
ATOM   2397 C CA  . PRO B 1 119 ? 6.830   36.044 -19.310 1.00 15.35  ? 100  PRO B CA  1 
ATOM   2398 C C   . PRO B 1 119 ? 7.899   36.444 -20.310 1.00 16.78  ? 100  PRO B C   1 
ATOM   2399 O O   . PRO B 1 119 ? 9.014   35.895 -20.272 1.00 18.76  ? 100  PRO B O   1 
ATOM   2400 C CB  . PRO B 1 119 ? 7.215   36.599 -17.946 1.00 17.60  ? 100  PRO B CB  1 
ATOM   2401 C CG  . PRO B 1 119 ? 6.694   35.614 -16.972 1.00 13.65  ? 100  PRO B CG  1 
ATOM   2402 C CD  . PRO B 1 119 ? 6.788   34.285 -17.635 1.00 18.65  ? 100  PRO B CD  1 
ATOM   2403 N N   . GLN B 1 120 ? 7.575   37.383 -21.191 1.00 16.44  ? 101  GLN B N   1 
ATOM   2404 C CA  . GLN B 1 120 ? 8.492   37.713 -22.273 1.00 21.67  ? 101  GLN B CA  1 
ATOM   2405 C C   . GLN B 1 120 ? 9.435   38.880 -21.963 1.00 17.26  ? 101  GLN B C   1 
ATOM   2406 O O   . GLN B 1 120 ? 9.393   39.924 -22.616 1.00 20.06  ? 101  GLN B O   1 
ATOM   2407 C CB  . GLN B 1 120 ? 7.732   37.879 -23.594 1.00 17.45  ? 101  GLN B CB  1 
ATOM   2408 C CG  . GLN B 1 120 ? 7.251   36.547 -24.152 1.00 15.12  ? 101  GLN B CG  1 
ATOM   2409 C CD  . GLN B 1 120 ? 6.397   36.689 -25.410 1.00 24.36  ? 101  GLN B CD  1 
ATOM   2410 O OE1 . GLN B 1 120 ? 6.675   37.525 -26.281 1.00 37.50  ? 101  GLN B OE1 1 
ATOM   2411 N NE2 . GLN B 1 120 ? 5.342   35.877 -25.505 1.00 15.59  ? 101  GLN B NE2 1 
ATOM   2412 N N   . LEU B 1 121 ? 10.294  38.666 -20.967 1.00 15.68  ? 102  LEU B N   1 
ATOM   2413 C CA  . LEU B 1 121 ? 11.239  39.690 -20.504 1.00 17.10  ? 102  LEU B CA  1 
ATOM   2414 C C   . LEU B 1 121 ? 12.665  39.265 -20.782 1.00 16.87  ? 102  LEU B C   1 
ATOM   2415 O O   . LEU B 1 121 ? 13.000  38.083 -20.672 1.00 28.14  ? 102  LEU B O   1 
ATOM   2416 C CB  . LEU B 1 121 ? 11.090  39.920 -18.992 1.00 17.89  ? 102  LEU B CB  1 
ATOM   2417 C CG  . LEU B 1 121 ? 9.701   40.380 -18.551 1.00 20.00  ? 102  LEU B CG  1 
ATOM   2418 C CD1 . LEU B 1 121 ? 9.607   40.554 -17.029 1.00 21.10  ? 102  LEU B CD1 1 
ATOM   2419 C CD2 . LEU B 1 121 ? 9.359   41.665 -19.277 1.00 14.59  ? 102  LEU B CD2 1 
ATOM   2420 N N   . ALA B 1 122 ? 13.509  40.224 -21.130 1.00 14.79  ? 103  ALA B N   1 
ATOM   2421 C CA  . ALA B 1 122 ? 14.938  39.975 -21.248 1.00 13.12  ? 103  ALA B CA  1 
ATOM   2422 C C   . ALA B 1 122 ? 15.710  40.615 -20.081 1.00 17.93  ? 103  ALA B C   1 
ATOM   2423 O O   . ALA B 1 122 ? 15.282  41.627 -19.477 1.00 15.11  ? 103  ALA B O   1 
ATOM   2424 C CB  . ALA B 1 122 ? 15.446  40.490 -22.563 1.00 11.21  ? 103  ALA B CB  1 
ATOM   2425 N N   . HIS B 1 123 ? 16.864  40.031 -19.786 1.00 14.92  ? 104  HIS B N   1 
ATOM   2426 C CA  . HIS B 1 123 ? 17.756  40.549 -18.764 1.00 17.76  ? 104  HIS B CA  1 
ATOM   2427 C C   . HIS B 1 123 ? 18.802  41.423 -19.450 1.00 22.66  ? 104  HIS B C   1 
ATOM   2428 O O   . HIS B 1 123 ? 19.398  41.008 -20.445 1.00 22.41  ? 104  HIS B O   1 
ATOM   2429 C CB  . HIS B 1 123 ? 18.417  39.384 -18.061 1.00 24.77  ? 104  HIS B CB  1 
ATOM   2430 C CG  . HIS B 1 123 ? 19.086  39.749 -16.775 1.00 29.36  ? 104  HIS B CG  1 
ATOM   2431 N ND1 . HIS B 1 123 ? 20.460  39.841 -16.660 1.00 40.52  ? 104  HIS B ND1 1 
ATOM   2432 C CD2 . HIS B 1 123 ? 18.582  39.988 -15.551 1.00 34.67  ? 104  HIS B CD2 1 
ATOM   2433 C CE1 . HIS B 1 123 ? 20.769  40.154 -15.414 1.00 34.78  ? 104  HIS B CE1 1 
ATOM   2434 N NE2 . HIS B 1 123 ? 19.656  40.249 -14.717 1.00 43.71  ? 104  HIS B NE2 1 
ATOM   2435 N N   . VAL B 1 124 ? 19.000  42.642 -18.948 1.00 19.53  ? 105  VAL B N   1 
ATOM   2436 C CA  . VAL B 1 124 ? 19.967  43.560 -19.531 1.00 18.43  ? 105  VAL B CA  1 
ATOM   2437 C C   . VAL B 1 124 ? 20.934  44.046 -18.468 1.00 22.16  ? 105  VAL B C   1 
ATOM   2438 O O   . VAL B 1 124 ? 20.525  44.527 -17.419 1.00 23.23  ? 105  VAL B O   1 
ATOM   2439 C CB  . VAL B 1 124 ? 19.301  44.799 -20.139 1.00 21.82  ? 105  VAL B CB  1 
ATOM   2440 C CG1 . VAL B 1 124 ? 20.350  45.651 -20.888 1.00 18.06  ? 105  VAL B CG1 1 
ATOM   2441 C CG2 . VAL B 1 124 ? 18.166  44.404 -21.052 1.00 18.72  ? 105  VAL B CG2 1 
ATOM   2442 N N   . VAL B 1 125 ? 22.223  43.935 -18.760 1.00 23.70  ? 106  VAL B N   1 
ATOM   2443 C CA  . VAL B 1 125 ? 23.278  44.353 -17.841 1.00 27.34  ? 106  VAL B CA  1 
ATOM   2444 C C   . VAL B 1 125 ? 23.838  45.685 -18.345 1.00 26.34  ? 106  VAL B C   1 
ATOM   2445 O O   . VAL B 1 125 ? 23.806  45.929 -19.546 1.00 28.17  ? 106  VAL B O   1 
ATOM   2446 C CB  . VAL B 1 125 ? 24.389  43.273 -17.778 1.00 25.85  ? 106  VAL B CB  1 
ATOM   2447 C CG1 . VAL B 1 125 ? 25.588  43.759 -16.972 1.00 23.87  ? 106  VAL B CG1 1 
ATOM   2448 C CG2 . VAL B 1 125 ? 23.833  41.996 -17.188 1.00 28.59  ? 106  VAL B CG2 1 
ATOM   2449 N N   . SER B 1 126 ? 24.339  46.534 -17.444 1.00 21.71  ? 107  SER B N   1 
ATOM   2450 C CA  . SER B 1 126 ? 24.806  47.880 -17.802 1.00 25.01  ? 107  SER B CA  1 
ATOM   2451 C C   . SER B 1 126 ? 25.842  47.972 -18.932 1.00 26.32  ? 107  SER B C   1 
ATOM   2452 O O   . SER B 1 126 ? 25.977  49.029 -19.572 1.00 26.46  ? 107  SER B O   1 
ATOM   2453 C CB  . SER B 1 126 ? 25.347  48.615 -16.577 1.00 26.23  ? 107  SER B CB  1 
ATOM   2454 O OG  . SER B 1 126 ? 26.367  47.870 -15.957 1.00 25.74  ? 107  SER B OG  1 
ATOM   2455 N N   . ASP B 1 127 ? 26.577  46.892 -19.180 1.00 23.43  ? 108  ASP B N   1 
ATOM   2456 C CA  . ASP B 1 127 ? 27.531  46.907 -20.294 1.00 28.83  ? 108  ASP B CA  1 
ATOM   2457 C C   . ASP B 1 127 ? 26.888  46.713 -21.685 1.00 34.25  ? 108  ASP B C   1 
ATOM   2458 O O   . ASP B 1 127 ? 27.539  46.934 -22.706 1.00 37.79  ? 108  ASP B O   1 
ATOM   2459 C CB  . ASP B 1 127 ? 28.670  45.897 -20.090 1.00 30.77  ? 108  ASP B CB  1 
ATOM   2460 C CG  . ASP B 1 127 ? 28.178  44.446 -19.985 1.00 41.35  ? 108  ASP B CG  1 
ATOM   2461 O OD1 . ASP B 1 127 ? 26.984  44.190 -20.297 1.00 44.75  ? 108  ASP B OD1 1 
ATOM   2462 O OD2 . ASP B 1 127 ? 28.992  43.559 -19.596 1.00 34.12  ? 108  ASP B OD2 1 
ATOM   2463 N N   . GLY B 1 128 ? 25.627  46.289 -21.725 1.00 25.14  ? 109  GLY B N   1 
ATOM   2464 C CA  . GLY B 1 128 ? 24.949  46.097 -22.989 1.00 21.21  ? 109  GLY B CA  1 
ATOM   2465 C C   . GLY B 1 128 ? 24.677  44.637 -23.287 1.00 28.73  ? 109  GLY B C   1 
ATOM   2466 O O   . GLY B 1 128 ? 24.199  44.294 -24.370 1.00 30.09  ? 109  GLY B O   1 
ATOM   2467 N N   . GLU B 1 129 ? 24.972  43.769 -22.327 1.00 26.96  ? 110  GLU B N   1 
ATOM   2468 C CA  . GLU B 1 129 ? 24.751  42.339 -22.511 1.00 25.65  ? 110  GLU B CA  1 
ATOM   2469 C C   . GLU B 1 129 ? 23.295  41.950 -22.260 1.00 25.79  ? 110  GLU B C   1 
ATOM   2470 O O   . GLU B 1 129 ? 22.726  42.244 -21.209 1.00 26.26  ? 110  GLU B O   1 
ATOM   2471 C CB  . GLU B 1 129 ? 25.659  41.530 -21.580 1.00 36.48  ? 110  GLU B CB  1 
ATOM   2472 C CG  . GLU B 1 129 ? 27.045  41.266 -22.141 1.00 47.81  ? 110  GLU B CG  1 
ATOM   2473 C CD  . GLU B 1 129 ? 27.034  40.232 -23.275 1.00 63.00  ? 110  GLU B CD  1 
ATOM   2474 O OE1 . GLU B 1 129 ? 26.415  39.143 -23.086 1.00 54.98  ? 110  GLU B OE1 1 
ATOM   2475 O OE2 . GLU B 1 129 ? 27.638  40.519 -24.351 1.00 58.90  ? 110  GLU B OE2 1 
ATOM   2476 N N   . VAL B 1 130 ? 22.699  41.264 -23.223 1.00 28.05  ? 111  VAL B N   1 
ATOM   2477 C CA  . VAL B 1 130 ? 21.304  40.880 -23.130 1.00 20.06  ? 111  VAL B CA  1 
ATOM   2478 C C   . VAL B 1 130 ? 21.201  39.365 -23.061 1.00 20.83  ? 111  VAL B C   1 
ATOM   2479 O O   . VAL B 1 130 ? 21.909  38.658 -23.780 1.00 23.17  ? 111  VAL B O   1 
ATOM   2480 C CB  . VAL B 1 130 ? 20.522  41.394 -24.354 1.00 16.99  ? 111  VAL B CB  1 
ATOM   2481 C CG1 . VAL B 1 130 ? 19.038  41.111 -24.200 1.00 14.25  ? 111  VAL B CG1 1 
ATOM   2482 C CG2 . VAL B 1 130 ? 20.760  42.864 -24.530 1.00 18.09  ? 111  VAL B CG2 1 
ATOM   2483 N N   . GLN B 1 131 ? 20.326  38.868 -22.193 1.00 19.44  ? 112  GLN B N   1 
ATOM   2484 C CA  . GLN B 1 131 ? 20.001  37.452 -22.193 1.00 21.11  ? 112  GLN B CA  1 
ATOM   2485 C C   . GLN B 1 131 ? 18.491  37.246 -22.177 1.00 21.11  ? 112  GLN B C   1 
ATOM   2486 O O   . GLN B 1 131 ? 17.794  37.790 -21.332 1.00 24.24  ? 112  GLN B O   1 
ATOM   2487 C CB  . GLN B 1 131 ? 20.635  36.741 -21.007 1.00 22.08  ? 112  GLN B CB  1 
ATOM   2488 C CG  . GLN B 1 131 ? 20.335  35.260 -20.997 1.00 33.81  ? 112  GLN B CG  1 
ATOM   2489 C CD  . GLN B 1 131 ? 20.997  34.537 -19.844 1.00 46.92  ? 112  GLN B CD  1 
ATOM   2490 O OE1 . GLN B 1 131 ? 22.138  34.846 -19.476 1.00 41.56  ? 112  GLN B OE1 1 
ATOM   2491 N NE2 . GLN B 1 131 ? 20.279  33.565 -19.255 1.00 51.06  ? 112  GLN B NE2 1 
ATOM   2492 N N   . TYR B 1 132 ? 17.988  36.466 -23.124 1.00 22.41  ? 113  TYR B N   1 
ATOM   2493 C CA  . TYR B 1 132 ? 16.567  36.152 -23.194 1.00 19.10  ? 113  TYR B CA  1 
ATOM   2494 C C   . TYR B 1 132 ? 16.406  34.630 -23.202 1.00 23.39  ? 113  TYR B C   1 
ATOM   2495 O O   . TYR B 1 132 ? 16.862  33.948 -24.124 1.00 25.95  ? 113  TYR B O   1 
ATOM   2496 C CB  . TYR B 1 132 ? 15.956  36.783 -24.451 1.00 18.07  ? 113  TYR B CB  1 
ATOM   2497 C CG  . TYR B 1 132 ? 14.494  36.454 -24.684 1.00 13.79  ? 113  TYR B CG  1 
ATOM   2498 C CD1 . TYR B 1 132 ? 13.582  36.492 -23.636 1.00 11.43  ? 113  TYR B CD1 1 
ATOM   2499 C CD2 . TYR B 1 132 ? 14.024  36.144 -25.956 1.00 10.55  ? 113  TYR B CD2 1 
ATOM   2500 C CE1 . TYR B 1 132 ? 12.247  36.207 -23.839 1.00 11.18  ? 113  TYR B CE1 1 
ATOM   2501 C CE2 . TYR B 1 132 ? 12.698  35.847 -26.178 1.00 11.00  ? 113  TYR B CE2 1 
ATOM   2502 C CZ  . TYR B 1 132 ? 11.806  35.870 -25.105 1.00 15.36  ? 113  TYR B CZ  1 
ATOM   2503 O OH  . TYR B 1 132 ? 10.453  35.582 -25.279 1.00 18.76  ? 113  TYR B OH  1 
ATOM   2504 N N   . THR B 1 133 ? 15.757  34.102 -22.167 1.00 24.93  ? 114  THR B N   1 
ATOM   2505 C CA  . THR B 1 133 ? 15.634  32.650 -21.973 1.00 22.08  ? 114  THR B CA  1 
ATOM   2506 C C   . THR B 1 133 ? 14.166  32.225 -21.772 1.00 17.72  ? 114  THR B C   1 
ATOM   2507 O O   . THR B 1 133 ? 13.723  31.960 -20.652 1.00 16.86  ? 114  THR B O   1 
ATOM   2508 C CB  . THR B 1 133 ? 16.480  32.179 -20.748 1.00 24.85  ? 114  THR B CB  1 
ATOM   2509 O OG1 . THR B 1 133 ? 17.783  32.802 -20.759 1.00 27.81  ? 114  THR B OG1 1 
ATOM   2510 C CG2 . THR B 1 133 ? 16.617  30.656 -20.717 1.00 18.67  ? 114  THR B CG2 1 
ATOM   2511 N N   . PRO B 1 134 ? 13.395  32.163 -22.863 1.00 16.36  ? 115  PRO B N   1 
ATOM   2512 C CA  . PRO B 1 134 ? 11.999  31.738 -22.704 1.00 15.76  ? 115  PRO B CA  1 
ATOM   2513 C C   . PRO B 1 134 ? 11.880  30.222 -22.608 1.00 17.49  ? 115  PRO B C   1 
ATOM   2514 O O   . PRO B 1 134 ? 12.683  29.490 -23.205 1.00 18.65  ? 115  PRO B O   1 
ATOM   2515 C CB  . PRO B 1 134 ? 11.350  32.213 -24.004 1.00 13.43  ? 115  PRO B CB  1 
ATOM   2516 C CG  . PRO B 1 134 ? 12.472  32.203 -24.995 1.00 12.22  ? 115  PRO B CG  1 
ATOM   2517 C CD  . PRO B 1 134 ? 13.711  32.561 -24.247 1.00 14.00  ? 115  PRO B CD  1 
ATOM   2518 N N   . SER B 1 135 ? 10.887  29.741 -21.872 1.00 15.97  ? 116  SER B N   1 
ATOM   2519 C CA  . SER B 1 135 ? 10.573  28.315 -21.930 1.00 16.54  ? 116  SER B CA  1 
ATOM   2520 C C   . SER B 1 135 ? 9.603   28.055 -23.079 1.00 16.76  ? 116  SER B C   1 
ATOM   2521 O O   . SER B 1 135 ? 8.573   28.711 -23.191 1.00 18.45  ? 116  SER B O   1 
ATOM   2522 C CB  . SER B 1 135 ? 9.971   27.835 -20.619 1.00 18.44  ? 116  SER B CB  1 
ATOM   2523 O OG  . SER B 1 135 ? 9.781   26.426 -20.639 1.00 23.73  ? 116  SER B OG  1 
ATOM   2524 N N   . ILE B 1 136 ? 9.927   27.089 -23.928 1.00 17.98  ? 117  ILE B N   1 
ATOM   2525 C CA  . ILE B 1 136 ? 9.160   26.859 -25.151 1.00 17.68  ? 117  ILE B CA  1 
ATOM   2526 C C   . ILE B 1 136 ? 8.708   25.413 -25.314 1.00 19.47  ? 117  ILE B C   1 
ATOM   2527 O O   . ILE B 1 136 ? 9.504   24.482 -25.178 1.00 25.19  ? 117  ILE B O   1 
ATOM   2528 C CB  . ILE B 1 136 ? 9.991   27.252 -26.391 1.00 18.26  ? 117  ILE B CB  1 
ATOM   2529 C CG1 . ILE B 1 136 ? 10.303  28.754 -26.364 1.00 16.91  ? 117  ILE B CG1 1 
ATOM   2530 C CG2 . ILE B 1 136 ? 9.288   26.839 -27.673 1.00 15.41  ? 117  ILE B CG2 1 
ATOM   2531 C CD1 . ILE B 1 136 ? 11.234  29.211 -27.459 1.00 14.36  ? 117  ILE B CD1 1 
ATOM   2532 N N   . ARG B 1 137 ? 7.426   25.220 -25.604 1.00 21.47  ? 118  ARG B N   1 
ATOM   2533 C CA  . ARG B 1 137 ? 6.946   23.919 -26.051 1.00 21.57  ? 118  ARG B CA  1 
ATOM   2534 C C   . ARG B 1 137 ? 6.802   23.947 -27.578 1.00 19.72  ? 118  ARG B C   1 
ATOM   2535 O O   . ARG B 1 137 ? 6.128   24.822 -28.121 1.00 19.32  ? 118  ARG B O   1 
ATOM   2536 C CB  . ARG B 1 137 ? 5.605   23.576 -25.391 1.00 21.72  ? 118  ARG B CB  1 
ATOM   2537 C CG  . ARG B 1 137 ? 4.916   22.375 -26.019 1.00 24.90  ? 118  ARG B CG  1 
ATOM   2538 C CD  . ARG B 1 137 ? 3.905   21.738 -25.095 1.00 33.17  ? 118  ARG B CD  1 
ATOM   2539 N NE  . ARG B 1 137 ? 3.385   20.488 -25.650 1.00 38.29  ? 118  ARG B NE  1 
ATOM   2540 C CZ  . ARG B 1 137 ? 2.567   19.665 -25.006 1.00 39.24  ? 118  ARG B CZ  1 
ATOM   2541 N NH1 . ARG B 1 137 ? 2.180   19.940 -23.763 1.00 40.90  ? 118  ARG B NH1 1 
ATOM   2542 N NH2 . ARG B 1 137 ? 2.157   18.550 -25.595 1.00 50.94  ? 118  ARG B NH2 1 
ATOM   2543 N N   . GLN B 1 138 ? 7.430   22.997 -28.265 1.00 18.28  ? 119  GLN B N   1 
ATOM   2544 C CA  . GLN B 1 138 ? 7.360   22.922 -29.724 1.00 20.56  ? 119  GLN B CA  1 
ATOM   2545 C C   . GLN B 1 138 ? 7.378   21.475 -30.268 1.00 26.77  ? 119  GLN B C   1 
ATOM   2546 O O   . GLN B 1 138 ? 8.015   20.588 -29.695 1.00 27.41  ? 119  GLN B O   1 
ATOM   2547 C CB  . GLN B 1 138 ? 8.504   23.741 -30.345 1.00 20.67  ? 119  GLN B CB  1 
ATOM   2548 C CG  . GLN B 1 138 ? 8.279   24.154 -31.802 1.00 20.54  ? 119  GLN B CG  1 
ATOM   2549 C CD  . GLN B 1 138 ? 9.151   25.336 -32.206 1.00 22.15  ? 119  GLN B CD  1 
ATOM   2550 O OE1 . GLN B 1 138 ? 10.172  25.619 -31.572 1.00 26.18  ? 119  GLN B OE1 1 
ATOM   2551 N NE2 . GLN B 1 138 ? 8.745   26.044 -33.253 1.00 24.62  ? 119  GLN B NE2 1 
ATOM   2552 N N   . ARG B 1 139 ? 6.689   21.248 -31.386 1.00 26.70  ? 120  ARG B N   1 
ATOM   2553 C CA  . ARG B 1 139 ? 6.689   19.945 -32.044 1.00 21.85  ? 120  ARG B CA  1 
ATOM   2554 C C   . ARG B 1 139 ? 7.687   19.914 -33.224 1.00 26.68  ? 120  ARG B C   1 
ATOM   2555 O O   . ARG B 1 139 ? 7.725   20.848 -34.033 1.00 30.74  ? 120  ARG B O   1 
ATOM   2556 C CB  . ARG B 1 139 ? 5.269   19.608 -32.497 1.00 24.32  ? 120  ARG B CB  1 
ATOM   2557 C CG  . ARG B 1 139 ? 5.082   18.150 -32.869 1.00 40.34  ? 120  ARG B CG  1 
ATOM   2558 C CD  . ARG B 1 139 ? 3.632   17.657 -32.808 1.00 40.52  ? 120  ARG B CD  1 
ATOM   2559 N NE  . ARG B 1 139 ? 3.570   16.206 -33.037 1.00 46.04  ? 120  ARG B NE  1 
ATOM   2560 C CZ  . ARG B 1 139 ? 3.669   15.285 -32.070 1.00 58.55  ? 120  ARG B CZ  1 
ATOM   2561 N NH1 . ARG B 1 139 ? 3.811   15.665 -30.803 1.00 56.21  ? 120  ARG B NH1 1 
ATOM   2562 N NH2 . ARG B 1 139 ? 3.618   13.984 -32.360 1.00 51.98  ? 120  ARG B NH2 1 
ATOM   2563 N N   . PHE B 1 140 ? 8.508   18.864 -33.308 1.00 26.19  ? 121  PHE B N   1 
ATOM   2564 C CA  . PHE B 1 140 ? 9.523   18.747 -34.374 1.00 26.90  ? 121  PHE B CA  1 
ATOM   2565 C C   . PHE B 1 140 ? 9.405   17.493 -35.229 1.00 31.01  ? 121  PHE B C   1 
ATOM   2566 O O   . PHE B 1 140 ? 8.732   16.526 -34.871 1.00 29.78  ? 121  PHE B O   1 
ATOM   2567 C CB  . PHE B 1 140 ? 10.937  18.766 -33.801 1.00 27.00  ? 121  PHE B CB  1 
ATOM   2568 C CG  . PHE B 1 140 ? 11.258  20.003 -33.056 1.00 25.27  ? 121  PHE B CG  1 
ATOM   2569 C CD1 . PHE B 1 140 ? 10.928  20.121 -31.712 1.00 23.65  ? 121  PHE B CD1 1 
ATOM   2570 C CD2 . PHE B 1 140 ? 11.886  21.058 -33.701 1.00 26.73  ? 121  PHE B CD2 1 
ATOM   2571 C CE1 . PHE B 1 140 ? 11.213  21.271 -31.014 1.00 26.85  ? 121  PHE B CE1 1 
ATOM   2572 C CE2 . PHE B 1 140 ? 12.184  22.226 -33.018 1.00 29.32  ? 121  PHE B CE2 1 
ATOM   2573 C CZ  . PHE B 1 140 ? 11.846  22.337 -31.665 1.00 31.80  ? 121  PHE B CZ  1 
ATOM   2574 N N   . SER B 1 141 ? 10.095  17.523 -36.360 1.00 29.81  ? 122  SER B N   1 
ATOM   2575 C CA  . SER B 1 141 ? 10.172  16.379 -37.250 1.00 30.11  ? 122  SER B CA  1 
ATOM   2576 C C   . SER B 1 141 ? 11.605  15.895 -37.243 1.00 31.45  ? 122  SER B C   1 
ATOM   2577 O O   . SER B 1 141 ? 12.506  16.622 -37.665 1.00 35.08  ? 122  SER B O   1 
ATOM   2578 C CB  . SER B 1 141 ? 9.782   16.779 -38.666 1.00 28.77  ? 122  SER B CB  1 
ATOM   2579 O OG  . SER B 1 141 ? 10.392  15.913 -39.603 1.00 27.13  ? 122  SER B OG  1 
ATOM   2580 N N   . CYS B 1 142 ? 11.821  14.677 -36.752 1.00 34.01  ? 123  CYS B N   1 
ATOM   2581 C CA  . CYS B 1 142 ? 13.177  14.136 -36.622 1.00 41.10  ? 123  CYS B CA  1 
ATOM   2582 C C   . CYS B 1 142 ? 13.216  12.613 -36.552 1.00 37.28  ? 123  CYS B C   1 
ATOM   2583 O O   . CYS B 1 142 ? 12.174  11.950 -36.588 1.00 39.65  ? 123  CYS B O   1 
ATOM   2584 C CB  . CYS B 1 142 ? 13.871  14.737 -35.398 1.00 41.37  ? 123  CYS B CB  1 
ATOM   2585 S SG  . CYS B 1 142 ? 12.956  14.467 -33.860 1.00 52.15  ? 123  CYS B SG  1 
ATOM   2586 N N   . ASP B 1 143 ? 14.422  12.064 -36.448 1.00 30.51  ? 124  ASP B N   1 
ATOM   2587 C CA  . ASP B 1 143 ? 14.580  10.617 -36.412 1.00 39.64  ? 124  ASP B CA  1 
ATOM   2588 C C   . ASP B 1 143 ? 14.278  10.045 -35.017 1.00 41.61  ? 124  ASP B C   1 
ATOM   2589 O O   . ASP B 1 143 ? 15.004  10.314 -34.052 1.00 38.34  ? 124  ASP B O   1 
ATOM   2590 C CB  . ASP B 1 143 ? 15.983  10.218 -36.878 1.00 38.82  ? 124  ASP B CB  1 
ATOM   2591 C CG  . ASP B 1 143 ? 16.076  8.755  -37.278 1.00 46.54  ? 124  ASP B CG  1 
ATOM   2592 O OD1 . ASP B 1 143 ? 15.025  8.059  -37.319 1.00 49.91  ? 124  ASP B OD1 1 
ATOM   2593 O OD2 . ASP B 1 143 ? 17.207  8.310  -37.571 1.00 51.94  ? 124  ASP B OD2 1 
ATOM   2594 N N   . VAL B 1 144 ? 13.210  9.250  -34.938 1.00 36.86  ? 125  VAL B N   1 
ATOM   2595 C CA  . VAL B 1 144 ? 12.689  8.733  -33.681 1.00 35.65  ? 125  VAL B CA  1 
ATOM   2596 C C   . VAL B 1 144 ? 12.976  7.225  -33.516 1.00 42.94  ? 125  VAL B C   1 
ATOM   2597 O O   . VAL B 1 144 ? 12.857  6.667  -32.421 1.00 45.03  ? 125  VAL B O   1 
ATOM   2598 C CB  . VAL B 1 144 ? 11.171  9.023  -33.598 1.00 38.19  ? 125  VAL B CB  1 
ATOM   2599 C CG1 . VAL B 1 144 ? 10.578  8.559  -32.288 1.00 42.22  ? 125  VAL B CG1 1 
ATOM   2600 C CG2 . VAL B 1 144 ? 10.921  10.490 -33.768 1.00 38.70  ? 125  VAL B CG2 1 
ATOM   2601 N N   . SER B 1 145 ? 13.373  6.577  -34.607 1.00 43.17  ? 126  SER B N   1 
ATOM   2602 C CA  . SER B 1 145 ? 13.670  5.144  -34.598 1.00 42.80  ? 126  SER B CA  1 
ATOM   2603 C C   . SER B 1 145 ? 14.653  4.719  -33.490 1.00 39.10  ? 126  SER B C   1 
ATOM   2604 O O   . SER B 1 145 ? 15.720  5.329  -33.308 1.00 35.92  ? 126  SER B O   1 
ATOM   2605 C CB  . SER B 1 145 ? 14.236  4.724  -35.953 1.00 50.00  ? 126  SER B CB  1 
ATOM   2606 O OG  . SER B 1 145 ? 15.459  5.401  -36.205 1.00 54.02  ? 126  SER B OG  1 
ATOM   2607 N N   . GLY B 1 146 ? 14.282  3.667  -32.760 1.00 35.00  ? 127  GLY B N   1 
ATOM   2608 C CA  . GLY B 1 146 ? 15.116  3.123  -31.708 1.00 38.83  ? 127  GLY B CA  1 
ATOM   2609 C C   . GLY B 1 146 ? 14.889  3.803  -30.377 1.00 42.39  ? 127  GLY B C   1 
ATOM   2610 O O   . GLY B 1 146 ? 15.715  3.726  -29.466 1.00 40.25  ? 127  GLY B O   1 
ATOM   2611 N N   . VAL B 1 147 ? 13.755  4.481  -30.264 1.00 46.89  ? 128  VAL B N   1 
ATOM   2612 C CA  . VAL B 1 147 ? 13.422  5.177  -29.027 1.00 48.81  ? 128  VAL B CA  1 
ATOM   2613 C C   . VAL B 1 147 ? 13.164  4.154  -27.900 1.00 48.12  ? 128  VAL B C   1 
ATOM   2614 O O   . VAL B 1 147 ? 13.399  4.441  -26.718 1.00 42.22  ? 128  VAL B O   1 
ATOM   2615 C CB  . VAL B 1 147 ? 12.225  6.159  -29.228 1.00 40.05  ? 128  VAL B CB  1 
ATOM   2616 C CG1 . VAL B 1 147 ? 10.968  5.412  -29.703 1.00 38.35  ? 128  VAL B CG1 1 
ATOM   2617 C CG2 . VAL B 1 147 ? 11.951  6.936  -27.957 1.00 37.10  ? 128  VAL B CG2 1 
ATOM   2618 N N   . ASP B 1 148 ? 12.720  2.955  -28.285 1.00 45.27  ? 129  ASP B N   1 
ATOM   2619 C CA  . ASP B 1 148 ? 12.422  1.892  -27.325 1.00 47.69  ? 129  ASP B CA  1 
ATOM   2620 C C   . ASP B 1 148 ? 13.565  0.852  -27.227 1.00 39.71  ? 129  ASP B C   1 
ATOM   2621 O O   . ASP B 1 148 ? 13.346  -0.325 -27.019 1.00 36.96  ? 129  ASP B O   1 
ATOM   2622 C CB  . ASP B 1 148 ? 11.081  1.234  -27.681 1.00 52.21  ? 129  ASP B CB  1 
ATOM   2623 C CG  . ASP B 1 148 ? 10.273  0.841  -26.446 1.00 74.38  ? 129  ASP B CG  1 
ATOM   2624 O OD1 . ASP B 1 148 ? 10.875  0.317  -25.472 1.00 77.01  ? 129  ASP B OD1 1 
ATOM   2625 O OD2 . ASP B 1 148 ? 9.036   1.064  -26.447 1.00 76.62  ? 129  ASP B OD2 1 
ATOM   2626 N N   . THR B 1 149 ? 14.791  1.334  -27.355 1.00 43.87  ? 130  THR B N   1 
ATOM   2627 C CA  . THR B 1 149 ? 15.990  0.517  -27.465 1.00 44.34  ? 130  THR B CA  1 
ATOM   2628 C C   . THR B 1 149 ? 17.005  0.990  -26.422 1.00 46.92  ? 130  THR B C   1 
ATOM   2629 O O   . THR B 1 149 ? 16.926  2.120  -25.951 1.00 52.54  ? 130  THR B O   1 
ATOM   2630 C CB  . THR B 1 149 ? 16.561  0.674  -28.890 1.00 41.40  ? 130  THR B CB  1 
ATOM   2631 O OG1 . THR B 1 149 ? 15.691  -0.008 -29.796 1.00 45.45  ? 130  THR B OG1 1 
ATOM   2632 C CG2 . THR B 1 149 ? 17.988  0.121  -29.035 1.00 48.61  ? 130  THR B CG2 1 
ATOM   2633 N N   . GLU B 1 150 ? 17.958  0.146  -26.052 1.00 46.73  ? 131  GLU B N   1 
ATOM   2634 C CA  . GLU B 1 150 ? 18.933  0.542  -25.052 1.00 52.92  ? 131  GLU B CA  1 
ATOM   2635 C C   . GLU B 1 150 ? 19.847  1.689  -25.509 1.00 49.99  ? 131  GLU B C   1 
ATOM   2636 O O   . GLU B 1 150 ? 20.345  2.465  -24.680 1.00 46.32  ? 131  GLU B O   1 
ATOM   2637 C CB  . GLU B 1 150 ? 19.760  -0.667 -24.634 1.00 57.04  ? 131  GLU B CB  1 
ATOM   2638 C CG  . GLU B 1 150 ? 20.508  -0.479 -23.339 1.00 64.19  ? 131  GLU B CG  1 
ATOM   2639 C CD  . GLU B 1 150 ? 21.639  -1.464 -23.201 1.00 80.41  ? 131  GLU B CD  1 
ATOM   2640 O OE1 . GLU B 1 150 ? 22.314  -1.719 -24.221 1.00 82.97  ? 131  GLU B OE1 1 
ATOM   2641 O OE2 . GLU B 1 150 ? 21.844  -1.989 -22.085 1.00 93.70  ? 131  GLU B OE2 1 
ATOM   2642 N N   . SER B 1 151 ? 20.051  1.803  -26.821 1.00 46.83  ? 132  SER B N   1 
ATOM   2643 C CA  . SER B 1 151 ? 20.912  2.859  -27.389 1.00 52.14  ? 132  SER B CA  1 
ATOM   2644 C C   . SER B 1 151 ? 20.176  4.181  -27.753 1.00 48.93  ? 132  SER B C   1 
ATOM   2645 O O   . SER B 1 151 ? 20.807  5.222  -27.993 1.00 47.67  ? 132  SER B O   1 
ATOM   2646 C CB  . SER B 1 151 ? 21.670  2.316  -28.601 1.00 46.26  ? 132  SER B CB  1 
ATOM   2647 O OG  . SER B 1 151 ? 20.771  1.688  -29.500 1.00 60.44  ? 132  SER B OG  1 
ATOM   2648 N N   . GLY B 1 152 ? 18.849  4.123  -27.810 1.00 42.96  ? 133  GLY B N   1 
ATOM   2649 C CA  . GLY B 1 152 ? 18.032  5.315  -27.928 1.00 38.69  ? 133  GLY B CA  1 
ATOM   2650 C C   . GLY B 1 152 ? 17.924  5.887  -29.327 1.00 47.12  ? 133  GLY B C   1 
ATOM   2651 O O   . GLY B 1 152 ? 18.616  5.434  -30.250 1.00 44.49  ? 133  GLY B O   1 
ATOM   2652 N N   . ALA B 1 153 ? 17.041  6.881  -29.482 1.00 52.08  ? 134  ALA B N   1 
ATOM   2653 C CA  . ALA B 1 153 ? 16.926  7.655  -30.727 1.00 41.73  ? 134  ALA B CA  1 
ATOM   2654 C C   . ALA B 1 153 ? 17.806  8.900  -30.656 1.00 37.75  ? 134  ALA B C   1 
ATOM   2655 O O   . ALA B 1 153 ? 18.071  9.418  -29.566 1.00 40.94  ? 134  ALA B O   1 
ATOM   2656 C CB  . ALA B 1 153 ? 15.485  8.044  -30.984 1.00 32.40  ? 134  ALA B CB  1 
ATOM   2657 N N   . THR B 1 154 ? 18.276  9.371  -31.808 1.00 36.32  ? 135  THR B N   1 
ATOM   2658 C CA  . THR B 1 154 ? 18.951  10.667 -31.856 1.00 41.18  ? 135  THR B CA  1 
ATOM   2659 C C   . THR B 1 154 ? 18.200  11.654 -32.739 1.00 39.55  ? 135  THR B C   1 
ATOM   2660 O O   . THR B 1 154 ? 18.188  11.519 -33.958 1.00 44.86  ? 135  THR B O   1 
ATOM   2661 C CB  . THR B 1 154 ? 20.413  10.564 -32.311 1.00 37.39  ? 135  THR B CB  1 
ATOM   2662 O OG1 . THR B 1 154 ? 21.064  9.533  -31.569 1.00 45.35  ? 135  THR B OG1 1 
ATOM   2663 C CG2 . THR B 1 154 ? 21.140  11.874 -32.039 1.00 39.94  ? 135  THR B CG2 1 
ATOM   2664 N N   . CYS B 1 155 ? 17.568  12.632 -32.098 1.00 39.62  ? 136  CYS B N   1 
ATOM   2665 C CA  . CYS B 1 155 ? 16.827  13.682 -32.778 1.00 40.79  ? 136  CYS B CA  1 
ATOM   2666 C C   . CYS B 1 155 ? 17.687  14.957 -32.884 1.00 37.30  ? 136  CYS B C   1 
ATOM   2667 O O   . CYS B 1 155 ? 18.229  15.412 -31.873 1.00 38.49  ? 136  CYS B O   1 
ATOM   2668 C CB  . CYS B 1 155 ? 15.551  13.969 -31.983 1.00 41.12  ? 136  CYS B CB  1 
ATOM   2669 S SG  . CYS B 1 155 ? 14.476  15.236 -32.730 1.00 87.55  ? 136  CYS B SG  1 
ATOM   2670 N N   . ARG B 1 156 ? 17.831  15.519 -34.092 1.00 34.25  ? 137  ARG B N   1 
ATOM   2671 C CA  . ARG B 1 156 ? 18.569  16.785 -34.282 1.00 32.13  ? 137  ARG B CA  1 
ATOM   2672 C C   . ARG B 1 156 ? 17.635  17.993 -34.471 1.00 37.67  ? 137  ARG B C   1 
ATOM   2673 O O   . ARG B 1 156 ? 16.638  17.919 -35.195 1.00 40.21  ? 137  ARG B O   1 
ATOM   2674 C CB  . ARG B 1 156 ? 19.540  16.710 -35.467 1.00 34.85  ? 137  ARG B CB  1 
ATOM   2675 C CG  . ARG B 1 156 ? 20.311  15.392 -35.619 1.00 46.02  ? 137  ARG B CG  1 
ATOM   2676 C CD  . ARG B 1 156 ? 21.305  15.423 -36.817 1.00 54.01  ? 137  ARG B CD  1 
ATOM   2677 N NE  . ARG B 1 156 ? 20.827  16.172 -37.997 1.00 58.65  ? 137  ARG B NE  1 
ATOM   2678 C CZ  . ARG B 1 156 ? 20.140  15.647 -39.019 1.00 61.57  ? 137  ARG B CZ  1 
ATOM   2679 N NH1 . ARG B 1 156 ? 19.819  14.358 -39.033 1.00 57.69  ? 137  ARG B NH1 1 
ATOM   2680 N NH2 . ARG B 1 156 ? 19.763  16.417 -40.034 1.00 54.60  ? 137  ARG B NH2 1 
ATOM   2681 N N   . ILE B 1 157 ? 17.962  19.107 -33.821 1.00 38.71  ? 138  ILE B N   1 
ATOM   2682 C CA  . ILE B 1 157 ? 17.190  20.339 -33.985 1.00 32.44  ? 138  ILE B CA  1 
ATOM   2683 C C   . ILE B 1 157 ? 18.083  21.419 -34.552 1.00 29.64  ? 138  ILE B C   1 
ATOM   2684 O O   . ILE B 1 157 ? 19.138  21.714 -33.989 1.00 33.11  ? 138  ILE B O   1 
ATOM   2685 C CB  . ILE B 1 157 ? 16.625  20.829 -32.652 1.00 31.94  ? 138  ILE B CB  1 
ATOM   2686 C CG1 . ILE B 1 157 ? 15.681  19.780 -32.065 1.00 30.61  ? 138  ILE B CG1 1 
ATOM   2687 C CG2 . ILE B 1 157 ? 15.930  22.173 -32.824 1.00 26.96  ? 138  ILE B CG2 1 
ATOM   2688 C CD1 . ILE B 1 157 ? 14.838  20.303 -30.936 1.00 28.02  ? 138  ILE B CD1 1 
ATOM   2689 N N   . LYS B 1 158 ? 17.670  22.003 -35.670 1.00 30.53  ? 139  LYS B N   1 
ATOM   2690 C CA  . LYS B 1 158 ? 18.497  22.992 -36.360 1.00 28.61  ? 139  LYS B CA  1 
ATOM   2691 C C   . LYS B 1 158 ? 17.937  24.406 -36.165 1.00 27.79  ? 139  LYS B C   1 
ATOM   2692 O O   . LYS B 1 158 ? 16.802  24.705 -36.556 1.00 30.54  ? 139  LYS B O   1 
ATOM   2693 C CB  . LYS B 1 158 ? 18.602  22.636 -37.845 1.00 28.89  ? 139  LYS B CB  1 
ATOM   2694 C CG  . LYS B 1 158 ? 19.297  23.679 -38.705 1.00 26.57  ? 139  LYS B CG  1 
ATOM   2695 C CD  . LYS B 1 158 ? 19.019  23.420 -40.187 1.00 32.20  ? 139  LYS B CD  1 
ATOM   2696 C CE  . LYS B 1 158 ? 19.363  24.628 -41.063 1.00 33.05  ? 139  LYS B CE  1 
ATOM   2697 N NZ  . LYS B 1 158 ? 19.282  24.342 -42.524 1.00 30.06  ? 139  LYS B NZ  1 
ATOM   2698 N N   . ILE B 1 159 ? 18.731  25.272 -35.543 1.00 26.19  ? 140  ILE B N   1 
ATOM   2699 C CA  . ILE B 1 159 ? 18.281  26.614 -35.193 1.00 20.89  ? 140  ILE B CA  1 
ATOM   2700 C C   . ILE B 1 159 ? 19.218  27.679 -35.754 1.00 26.32  ? 140  ILE B C   1 
ATOM   2701 O O   . ILE B 1 159 ? 20.435  27.600 -35.557 1.00 27.37  ? 140  ILE B O   1 
ATOM   2702 C CB  . ILE B 1 159 ? 18.229  26.779 -33.669 1.00 23.15  ? 140  ILE B CB  1 
ATOM   2703 C CG1 . ILE B 1 159 ? 17.171  25.846 -33.073 1.00 24.44  ? 140  ILE B CG1 1 
ATOM   2704 C CG2 . ILE B 1 159 ? 17.944  28.231 -33.293 1.00 23.69  ? 140  ILE B CG2 1 
ATOM   2705 C CD1 . ILE B 1 159 ? 16.994  26.001 -31.570 1.00 26.63  ? 140  ILE B CD1 1 
ATOM   2706 N N   . GLY B 1 160 ? 18.664  28.679 -36.443 1.00 27.51  ? 141  GLY B N   1 
ATOM   2707 C CA  . GLY B 1 160 ? 19.480  29.750 -36.992 1.00 23.17  ? 141  GLY B CA  1 
ATOM   2708 C C   . GLY B 1 160 ? 18.708  31.007 -37.335 1.00 23.76  ? 141  GLY B C   1 
ATOM   2709 O O   . GLY B 1 160 ? 17.480  31.045 -37.207 1.00 22.62  ? 141  GLY B O   1 
ATOM   2710 N N   . SER B 1 161 ? 19.422  32.045 -37.772 1.00 26.38  ? 142  SER B N   1 
ATOM   2711 C CA  . SER B 1 161 ? 18.765  33.274 -38.225 1.00 21.56  ? 142  SER B CA  1 
ATOM   2712 C C   . SER B 1 161 ? 17.990  33.042 -39.509 1.00 18.83  ? 142  SER B C   1 
ATOM   2713 O O   . SER B 1 161 ? 18.489  32.411 -40.429 1.00 19.11  ? 142  SER B O   1 
ATOM   2714 C CB  . SER B 1 161 ? 19.784  34.369 -38.479 1.00 21.99  ? 142  SER B CB  1 
ATOM   2715 O OG  . SER B 1 161 ? 19.131  35.509 -39.016 1.00 24.96  ? 142  SER B OG  1 
ATOM   2716 N N   . TRP B 1 162 ? 16.774  33.567 -39.576 1.00 22.05  ? 143  TRP B N   1 
ATOM   2717 C CA  . TRP B 1 162 ? 15.927  33.332 -40.734 1.00 18.70  ? 143  TRP B CA  1 
ATOM   2718 C C   . TRP B 1 162 ? 16.255  34.254 -41.912 1.00 21.26  ? 143  TRP B C   1 
ATOM   2719 O O   . TRP B 1 162 ? 16.160  33.835 -43.067 1.00 23.28  ? 143  TRP B O   1 
ATOM   2720 C CB  . TRP B 1 162 ? 14.446  33.438 -40.356 1.00 18.04  ? 143  TRP B CB  1 
ATOM   2721 C CG  . TRP B 1 162 ? 13.529  32.838 -41.397 1.00 19.08  ? 143  TRP B CG  1 
ATOM   2722 C CD1 . TRP B 1 162 ? 12.715  33.515 -42.274 1.00 22.84  ? 143  TRP B CD1 1 
ATOM   2723 C CD2 . TRP B 1 162 ? 13.358  31.446 -41.680 1.00 20.27  ? 143  TRP B CD2 1 
ATOM   2724 N NE1 . TRP B 1 162 ? 12.039  32.624 -43.079 1.00 24.19  ? 143  TRP B NE1 1 
ATOM   2725 C CE2 . TRP B 1 162 ? 12.413  31.350 -42.738 1.00 26.58  ? 143  TRP B CE2 1 
ATOM   2726 C CE3 . TRP B 1 162 ? 13.903  30.268 -41.149 1.00 22.86  ? 143  TRP B CE3 1 
ATOM   2727 C CZ2 . TRP B 1 162 ? 12.006  30.106 -43.267 1.00 23.16  ? 143  TRP B CZ2 1 
ATOM   2728 C CZ3 . TRP B 1 162 ? 13.495  29.042 -41.667 1.00 22.57  ? 143  TRP B CZ3 1 
ATOM   2729 C CH2 . TRP B 1 162 ? 12.556  28.973 -42.723 1.00 21.26  ? 143  TRP B CH2 1 
ATOM   2730 N N   . THR B 1 163 ? 16.637  35.499 -41.627 1.00 21.71  ? 144  THR B N   1 
ATOM   2731 C CA  . THR B 1 163 ? 16.812  36.501 -42.687 1.00 23.01  ? 144  THR B CA  1 
ATOM   2732 C C   . THR B 1 163 ? 18.179  37.151 -42.714 1.00 25.23  ? 144  THR B C   1 
ATOM   2733 O O   . THR B 1 163 ? 18.476  37.882 -43.648 1.00 34.22  ? 144  THR B O   1 
ATOM   2734 C CB  . THR B 1 163 ? 15.765  37.658 -42.617 1.00 26.51  ? 144  THR B CB  1 
ATOM   2735 O OG1 . THR B 1 163 ? 15.961  38.425 -41.416 1.00 27.88  ? 144  THR B OG1 1 
ATOM   2736 C CG2 . THR B 1 163 ? 14.334  37.143 -42.680 1.00 20.09  ? 144  THR B CG2 1 
ATOM   2737 N N   . HIS B 1 164 ? 18.994  36.925 -41.690 1.00 26.28  ? 145  HIS B N   1 
ATOM   2738 C CA  . HIS B 1 164 ? 20.326  37.538 -41.649 1.00 30.33  ? 145  HIS B CA  1 
ATOM   2739 C C   . HIS B 1 164 ? 21.455  36.550 -41.972 1.00 28.82  ? 145  HIS B C   1 
ATOM   2740 O O   . HIS B 1 164 ? 21.550  35.487 -41.359 1.00 28.53  ? 145  HIS B O   1 
ATOM   2741 C CB  . HIS B 1 164 ? 20.566  38.181 -40.281 1.00 28.47  ? 145  HIS B CB  1 
ATOM   2742 C CG  . HIS B 1 164 ? 19.688  39.359 -40.008 1.00 28.98  ? 145  HIS B CG  1 
ATOM   2743 N ND1 . HIS B 1 164 ? 19.841  40.564 -40.655 1.00 31.77  ? 145  HIS B ND1 1 
ATOM   2744 C CD2 . HIS B 1 164 ? 18.653  39.517 -39.150 1.00 28.32  ? 145  HIS B CD2 1 
ATOM   2745 C CE1 . HIS B 1 164 ? 18.939  41.421 -40.207 1.00 29.86  ? 145  HIS B CE1 1 
ATOM   2746 N NE2 . HIS B 1 164 ? 18.204  40.806 -39.297 1.00 35.89  ? 145  HIS B NE2 1 
ATOM   2747 N N   . HIS B 1 165 ? 22.321  36.901 -42.919 1.00 29.49  ? 146  HIS B N   1 
ATOM   2748 C CA  . HIS B 1 165 ? 23.427  36.003 -43.276 1.00 33.12  ? 146  HIS B CA  1 
ATOM   2749 C C   . HIS B 1 165 ? 24.622  36.078 -42.307 1.00 31.39  ? 146  HIS B C   1 
ATOM   2750 O O   . HIS B 1 165 ? 24.577  36.790 -41.308 1.00 34.53  ? 146  HIS B O   1 
ATOM   2751 C CB  . HIS B 1 165 ? 23.851  36.194 -44.742 1.00 38.14  ? 146  HIS B CB  1 
ATOM   2752 C CG  . HIS B 1 165 ? 24.325  37.579 -45.066 1.00 38.07  ? 146  HIS B CG  1 
ATOM   2753 N ND1 . HIS B 1 165 ? 25.452  38.127 -44.497 1.00 40.85  ? 146  HIS B ND1 1 
ATOM   2754 C CD2 . HIS B 1 165 ? 23.822  38.509 -45.909 1.00 40.93  ? 146  HIS B CD2 1 
ATOM   2755 C CE1 . HIS B 1 165 ? 25.620  39.355 -44.971 1.00 48.82  ? 146  HIS B CE1 1 
ATOM   2756 N NE2 . HIS B 1 165 ? 24.651  39.609 -45.827 1.00 49.18  ? 146  HIS B NE2 1 
ATOM   2757 N N   . SER B 1 166 ? 25.688  35.349 -42.619 1.00 32.82  ? 147  SER B N   1 
ATOM   2758 C CA  . SER B 1 166 ? 26.807  35.146 -41.688 1.00 35.83  ? 147  SER B CA  1 
ATOM   2759 C C   . SER B 1 166 ? 27.612  36.390 -41.322 1.00 37.89  ? 147  SER B C   1 
ATOM   2760 O O   . SER B 1 166 ? 28.344  36.375 -40.330 1.00 38.04  ? 147  SER B O   1 
ATOM   2761 C CB  . SER B 1 166 ? 27.765  34.094 -42.240 1.00 33.44  ? 147  SER B CB  1 
ATOM   2762 O OG  . SER B 1 166 ? 28.352  34.559 -43.442 1.00 39.84  ? 147  SER B OG  1 
ATOM   2763 N N   . ARG B 1 167 ? 27.505  37.447 -42.128 1.00 41.19  ? 148  ARG B N   1 
ATOM   2764 C CA  . ARG B 1 167 ? 28.243  38.682 -41.855 1.00 44.38  ? 148  ARG B CA  1 
ATOM   2765 C C   . ARG B 1 167 ? 27.426  39.663 -41.014 1.00 40.52  ? 148  ARG B C   1 
ATOM   2766 O O   . ARG B 1 167 ? 27.940  40.697 -40.564 1.00 36.06  ? 148  ARG B O   1 
ATOM   2767 C CB  . ARG B 1 167 ? 28.693  39.358 -43.152 1.00 55.38  ? 148  ARG B CB  1 
ATOM   2768 C CG  . ARG B 1 167 ? 29.744  38.587 -43.965 1.00 63.62  ? 148  ARG B CG  1 
ATOM   2769 C CD  . ARG B 1 167 ? 30.206  39.399 -45.194 1.00 70.34  ? 148  ARG B CD  1 
ATOM   2770 N NE  . ARG B 1 167 ? 29.304  40.510 -45.515 1.00 77.69  ? 148  ARG B NE  1 
ATOM   2771 C CZ  . ARG B 1 167 ? 28.881  40.825 -46.741 1.00 81.06  ? 148  ARG B CZ  1 
ATOM   2772 N NH1 . ARG B 1 167 ? 29.274  40.111 -47.792 1.00 73.34  ? 148  ARG B NH1 1 
ATOM   2773 N NH2 . ARG B 1 167 ? 28.057  41.861 -46.917 1.00 83.09  ? 148  ARG B NH2 1 
ATOM   2774 N N   . GLU B 1 168 ? 26.154  39.325 -40.812 1.00 39.33  ? 149  GLU B N   1 
ATOM   2775 C CA  . GLU B 1 168 ? 25.246  40.132 -39.997 1.00 38.99  ? 149  GLU B CA  1 
ATOM   2776 C C   . GLU B 1 168 ? 24.962  39.485 -38.633 1.00 35.56  ? 149  GLU B C   1 
ATOM   2777 O O   . GLU B 1 168 ? 25.048  40.146 -37.588 1.00 34.49  ? 149  GLU B O   1 
ATOM   2778 C CB  . GLU B 1 168 ? 23.945  40.412 -40.767 1.00 35.27  ? 149  GLU B CB  1 
ATOM   2779 C CG  . GLU B 1 168 ? 24.132  41.293 -42.008 1.00 36.60  ? 149  GLU B CG  1 
ATOM   2780 C CD  . GLU B 1 168 ? 22.865  41.460 -42.855 1.00 43.87  ? 149  GLU B CD  1 
ATOM   2781 O OE1 . GLU B 1 168 ? 22.058  40.502 -42.935 1.00 45.21  ? 149  GLU B OE1 1 
ATOM   2782 O OE2 . GLU B 1 168 ? 22.678  42.554 -43.446 1.00 54.67  ? 149  GLU B OE2 1 
ATOM   2783 N N   . ILE B 1 169 ? 24.624  38.197 -38.657 1.00 28.12  ? 150  ILE B N   1 
ATOM   2784 C CA  . ILE B 1 169 ? 24.471  37.408 -37.437 1.00 30.76  ? 150  ILE B CA  1 
ATOM   2785 C C   . ILE B 1 169 ? 25.278  36.105 -37.513 1.00 34.89  ? 150  ILE B C   1 
ATOM   2786 O O   . ILE B 1 169 ? 25.149  35.335 -38.479 1.00 29.94  ? 150  ILE B O   1 
ATOM   2787 C CB  . ILE B 1 169 ? 22.985  37.054 -37.159 1.00 31.51  ? 150  ILE B CB  1 
ATOM   2788 C CG1 . ILE B 1 169 ? 22.202  38.295 -36.732 1.00 29.96  ? 150  ILE B CG1 1 
ATOM   2789 C CG2 . ILE B 1 169 ? 22.872  35.973 -36.087 1.00 26.42  ? 150  ILE B CG2 1 
ATOM   2790 C CD1 . ILE B 1 169 ? 20.738  38.030 -36.408 1.00 21.02  ? 150  ILE B CD1 1 
ATOM   2791 N N   . SER B 1 170 ? 26.110  35.869 -36.500 1.00 31.70  ? 151  SER B N   1 
ATOM   2792 C CA  . SER B 1 170 ? 26.729  34.563 -36.315 1.00 33.83  ? 151  SER B CA  1 
ATOM   2793 C C   . SER B 1 170 ? 26.168  33.858 -35.068 1.00 36.00  ? 151  SER B C   1 
ATOM   2794 O O   . SER B 1 170 ? 26.071  34.469 -33.991 1.00 33.26  ? 151  SER B O   1 
ATOM   2795 C CB  . SER B 1 170 ? 28.245  34.702 -36.212 1.00 35.10  ? 151  SER B CB  1 
ATOM   2796 O OG  . SER B 1 170 ? 28.611  35.367 -35.019 1.00 33.54  ? 151  SER B OG  1 
ATOM   2797 N N   . VAL B 1 171 ? 25.794  32.585 -35.214 1.00 33.33  ? 152  VAL B N   1 
ATOM   2798 C CA  . VAL B 1 171 ? 25.307  31.786 -34.084 1.00 33.86  ? 152  VAL B CA  1 
ATOM   2799 C C   . VAL B 1 171 ? 26.359  30.772 -33.660 1.00 34.79  ? 152  VAL B C   1 
ATOM   2800 O O   . VAL B 1 171 ? 26.978  30.129 -34.494 1.00 43.49  ? 152  VAL B O   1 
ATOM   2801 C CB  . VAL B 1 171 ? 23.995  31.031 -34.411 1.00 30.57  ? 152  VAL B CB  1 
ATOM   2802 C CG1 . VAL B 1 171 ? 22.794  31.945 -34.303 1.00 27.95  ? 152  VAL B CG1 1 
ATOM   2803 C CG2 . VAL B 1 171 ? 24.067  30.437 -35.785 1.00 31.37  ? 152  VAL B CG2 1 
ATOM   2804 N N   . ASP B 1 172 ? 26.553  30.629 -32.356 1.00 36.81  ? 153  ASP B N   1 
ATOM   2805 C CA  . ASP B 1 172 ? 27.584  29.752 -31.819 1.00 36.05  ? 153  ASP B CA  1 
ATOM   2806 C C   . ASP B 1 172 ? 27.052  29.047 -30.590 1.00 42.54  ? 153  ASP B C   1 
ATOM   2807 O O   . ASP B 1 172 ? 26.267  29.626 -29.832 1.00 38.54  ? 153  ASP B O   1 
ATOM   2808 C CB  . ASP B 1 172 ? 28.817  30.565 -31.427 1.00 40.72  ? 153  ASP B CB  1 
ATOM   2809 C CG  . ASP B 1 172 ? 29.142  31.690 -32.443 1.00 61.31  ? 153  ASP B CG  1 
ATOM   2810 O OD1 . ASP B 1 172 ? 29.738  31.389 -33.518 1.00 56.59  ? 153  ASP B OD1 1 
ATOM   2811 O OD2 . ASP B 1 172 ? 28.807  32.877 -32.159 1.00 50.13  ? 153  ASP B OD2 1 
ATOM   2812 N N   . PRO B 1 173 ? 27.453  27.782 -30.396 1.00 44.82  ? 154  PRO B N   1 
ATOM   2813 C CA  . PRO B 1 173 ? 27.049  27.040 -29.197 1.00 46.55  ? 154  PRO B CA  1 
ATOM   2814 C C   . PRO B 1 173 ? 27.792  27.595 -27.983 1.00 47.41  ? 154  PRO B C   1 
ATOM   2815 O O   . PRO B 1 173 ? 28.850  28.202 -28.134 1.00 46.74  ? 154  PRO B O   1 
ATOM   2816 C CB  . PRO B 1 173 ? 27.504  25.610 -29.499 1.00 40.10  ? 154  PRO B CB  1 
ATOM   2817 C CG  . PRO B 1 173 ? 27.680  25.572 -30.982 1.00 41.44  ? 154  PRO B CG  1 
ATOM   2818 C CD  . PRO B 1 173 ? 28.180  26.932 -31.346 1.00 39.65  ? 154  PRO B CD  1 
ATOM   2819 N N   . THR B 1 174 ? 27.245  27.385 -26.795 1.00 46.38  ? 155  THR B N   1 
ATOM   2820 C CA  . THR B 1 174 ? 27.841  27.927 -25.580 1.00 49.27  ? 155  THR B CA  1 
ATOM   2821 C C   . THR B 1 174 ? 29.035  27.103 -25.088 1.00 52.43  ? 155  THR B C   1 
ATOM   2822 O O   . THR B 1 174 ? 28.996  25.870 -25.071 1.00 58.95  ? 155  THR B O   1 
ATOM   2823 C CB  . THR B 1 174 ? 26.784  28.049 -24.465 1.00 51.92  ? 155  THR B CB  1 
ATOM   2824 O OG1 . THR B 1 174 ? 25.843  29.074 -24.818 1.00 49.88  ? 155  THR B OG1 1 
ATOM   2825 C CG2 . THR B 1 174 ? 27.435  28.394 -23.136 1.00 56.96  ? 155  THR B CG2 1 
ATOM   2826 N N   . ASP B 1 180 ? 23.122  18.237 -19.028 1.00 64.09  ? 161  ASP B N   1 
ATOM   2827 C CA  . ASP B 1 180 ? 22.145  17.647 -19.947 1.00 65.47  ? 161  ASP B CA  1 
ATOM   2828 C C   . ASP B 1 180 ? 20.767  17.522 -19.296 1.00 59.01  ? 161  ASP B C   1 
ATOM   2829 O O   . ASP B 1 180 ? 19.806  18.209 -19.665 1.00 55.24  ? 161  ASP B O   1 
ATOM   2830 C CB  . ASP B 1 180 ? 22.568  16.235 -20.382 1.00 67.70  ? 161  ASP B CB  1 
ATOM   2831 C CG  . ASP B 1 180 ? 23.977  16.166 -20.967 1.00 70.48  ? 161  ASP B CG  1 
ATOM   2832 O OD1 . ASP B 1 180 ? 24.423  17.139 -21.616 1.00 70.02  ? 161  ASP B OD1 1 
ATOM   2833 O OD2 . ASP B 1 180 ? 24.626  15.102 -20.781 1.00 70.78  ? 161  ASP B OD2 1 
ATOM   2834 N N   . SER B 1 181 ? 20.701  16.603 -18.337 1.00 56.92  ? 162  SER B N   1 
ATOM   2835 C CA  . SER B 1 181 ? 19.511  16.293 -17.550 1.00 60.88  ? 162  SER B CA  1 
ATOM   2836 C C   . SER B 1 181 ? 19.370  17.230 -16.354 1.00 51.98  ? 162  SER B C   1 
ATOM   2837 O O   . SER B 1 181 ? 18.573  16.965 -15.443 1.00 51.79  ? 162  SER B O   1 
ATOM   2838 C CB  . SER B 1 181 ? 19.594  14.844 -17.026 1.00 65.55  ? 162  SER B CB  1 
ATOM   2839 O OG  . SER B 1 181 ? 19.319  13.876 -18.036 1.00 61.06  ? 162  SER B OG  1 
ATOM   2840 N N   . GLU B 1 182 ? 20.149  18.309 -16.353 1.00 44.76  ? 163  GLU B N   1 
ATOM   2841 C CA  . GLU B 1 182 ? 20.243  19.166 -15.179 1.00 50.22  ? 163  GLU B CA  1 
ATOM   2842 C C   . GLU B 1 182 ? 18.876  19.693 -14.721 1.00 46.28  ? 163  GLU B C   1 
ATOM   2843 O O   . GLU B 1 182 ? 18.588  19.746 -13.527 1.00 50.18  ? 163  GLU B O   1 
ATOM   2844 C CB  . GLU B 1 182 ? 21.229  20.315 -15.416 1.00 53.24  ? 163  GLU B CB  1 
ATOM   2845 C CG  . GLU B 1 182 ? 21.569  21.071 -14.137 1.00 50.30  ? 163  GLU B CG  1 
ATOM   2846 C CD  . GLU B 1 182 ? 22.444  22.277 -14.384 1.00 69.17  ? 163  GLU B CD  1 
ATOM   2847 O OE1 . GLU B 1 182 ? 22.876  22.477 -15.546 1.00 85.84  ? 163  GLU B OE1 1 
ATOM   2848 O OE2 . GLU B 1 182 ? 22.696  23.027 -13.413 1.00 77.87  ? 163  GLU B OE2 1 
ATOM   2849 N N   . TYR B 1 183 ? 18.031  20.061 -15.676 1.00 40.11  ? 164  TYR B N   1 
ATOM   2850 C CA  . TYR B 1 183 ? 16.697  20.534 -15.358 1.00 28.98  ? 164  TYR B CA  1 
ATOM   2851 C C   . TYR B 1 183 ? 15.633  19.629 -15.972 1.00 32.93  ? 164  TYR B C   1 
ATOM   2852 O O   . TYR B 1 183 ? 14.456  19.995 -16.016 1.00 31.57  ? 164  TYR B O   1 
ATOM   2853 C CB  . TYR B 1 183 ? 16.502  21.940 -15.903 1.00 40.26  ? 164  TYR B CB  1 
ATOM   2854 C CG  . TYR B 1 183 ? 17.578  22.920 -15.512 1.00 51.59  ? 164  TYR B CG  1 
ATOM   2855 C CD1 . TYR B 1 183 ? 17.794  23.239 -14.175 1.00 50.98  ? 164  TYR B CD1 1 
ATOM   2856 C CD2 . TYR B 1 183 ? 18.367  23.545 -16.482 1.00 47.83  ? 164  TYR B CD2 1 
ATOM   2857 C CE1 . TYR B 1 183 ? 18.771  24.140 -13.808 1.00 55.10  ? 164  TYR B CE1 1 
ATOM   2858 C CE2 . TYR B 1 183 ? 19.351  24.445 -16.130 1.00 49.81  ? 164  TYR B CE2 1 
ATOM   2859 C CZ  . TYR B 1 183 ? 19.549  24.745 -14.788 1.00 64.78  ? 164  TYR B CZ  1 
ATOM   2860 O OH  . TYR B 1 183 ? 20.530  25.651 -14.425 1.00 73.97  ? 164  TYR B OH  1 
ATOM   2861 N N   . PHE B 1 184 ? 16.046  18.462 -16.463 1.00 31.44  ? 165  PHE B N   1 
ATOM   2862 C CA  . PHE B 1 184 ? 15.110  17.516 -17.062 1.00 31.02  ? 165  PHE B CA  1 
ATOM   2863 C C   . PHE B 1 184 ? 14.184  16.896 -16.025 1.00 36.31  ? 165  PHE B C   1 
ATOM   2864 O O   . PHE B 1 184 ? 14.610  16.554 -14.916 1.00 39.15  ? 165  PHE B O   1 
ATOM   2865 C CB  . PHE B 1 184 ? 15.826  16.405 -17.829 1.00 29.87  ? 165  PHE B CB  1 
ATOM   2866 C CG  . PHE B 1 184 ? 14.926  15.665 -18.768 1.00 22.70  ? 165  PHE B CG  1 
ATOM   2867 C CD1 . PHE B 1 184 ? 14.401  16.299 -19.891 1.00 24.03  ? 165  PHE B CD1 1 
ATOM   2868 C CD2 . PHE B 1 184 ? 14.597  14.346 -18.534 1.00 26.16  ? 165  PHE B CD2 1 
ATOM   2869 C CE1 . PHE B 1 184 ? 13.556  15.618 -20.776 1.00 26.14  ? 165  PHE B CE1 1 
ATOM   2870 C CE2 . PHE B 1 184 ? 13.751  13.643 -19.413 1.00 31.23  ? 165  PHE B CE2 1 
ATOM   2871 C CZ  . PHE B 1 184 ? 13.225  14.287 -20.535 1.00 29.81  ? 165  PHE B CZ  1 
ATOM   2872 N N   . SER B 1 185 ? 12.913  16.751 -16.391 1.00 31.96  ? 166  SER B N   1 
ATOM   2873 C CA  . SER B 1 185 ? 11.910  16.253 -15.467 1.00 27.00  ? 166  SER B CA  1 
ATOM   2874 C C   . SER B 1 185 ? 12.120  14.767 -15.153 1.00 34.80  ? 166  SER B C   1 
ATOM   2875 O O   . SER B 1 185 ? 12.259  13.935 -16.057 1.00 38.83  ? 166  SER B O   1 
ATOM   2876 C CB  . SER B 1 185 ? 10.516  16.479 -16.050 1.00 29.63  ? 166  SER B CB  1 
ATOM   2877 O OG  . SER B 1 185 ? 9.504   16.141 -15.111 1.00 30.79  ? 166  SER B OG  1 
ATOM   2878 N N   . GLN B 1 186 ? 12.138  14.437 -13.864 1.00 42.51  ? 167  GLN B N   1 
ATOM   2879 C CA  . GLN B 1 186 ? 12.192  13.040 -13.422 1.00 37.99  ? 167  GLN B CA  1 
ATOM   2880 C C   . GLN B 1 186 ? 10.895  12.312 -13.752 1.00 36.89  ? 167  GLN B C   1 
ATOM   2881 O O   . GLN B 1 186 ? 10.877  11.088 -13.807 1.00 44.91  ? 167  GLN B O   1 
ATOM   2882 C CB  . GLN B 1 186 ? 12.461  12.959 -11.919 1.00 35.05  ? 167  GLN B CB  1 
ATOM   2883 C CG  . GLN B 1 186 ? 11.725  14.041 -11.130 1.00 47.33  ? 167  GLN B CG  1 
ATOM   2884 C CD  . GLN B 1 186 ? 11.851  13.908 -9.612  1.00 54.15  ? 167  GLN B CD  1 
ATOM   2885 O OE1 . GLN B 1 186 ? 11.944  12.797 -9.073  1.00 41.75  ? 167  GLN B OE1 1 
ATOM   2886 N NE2 . GLN B 1 186 ? 11.838  15.055 -8.911  1.00 58.08  ? 167  GLN B NE2 1 
ATOM   2887 N N   . TYR B 1 187 ? 9.820   13.063 -13.988 1.00 31.54  ? 168  TYR B N   1 
ATOM   2888 C CA  . TYR B 1 187 ? 8.512   12.459 -14.228 1.00 32.72  ? 168  TYR B CA  1 
ATOM   2889 C C   . TYR B 1 187 ? 8.183   12.195 -15.706 1.00 35.87  ? 168  TYR B C   1 
ATOM   2890 O O   . TYR B 1 187 ? 7.166   11.569 -16.020 1.00 40.47  ? 168  TYR B O   1 
ATOM   2891 C CB  . TYR B 1 187 ? 7.398   13.246 -13.531 1.00 28.98  ? 168  TYR B CB  1 
ATOM   2892 C CG  . TYR B 1 187 ? 7.659   13.426 -12.051 1.00 37.32  ? 168  TYR B CG  1 
ATOM   2893 C CD1 . TYR B 1 187 ? 7.760   12.332 -11.200 1.00 42.14  ? 168  TYR B CD1 1 
ATOM   2894 C CD2 . TYR B 1 187 ? 7.814   14.683 -11.503 1.00 39.06  ? 168  TYR B CD2 1 
ATOM   2895 C CE1 . TYR B 1 187 ? 8.004   12.489 -9.841  1.00 39.40  ? 168  TYR B CE1 1 
ATOM   2896 C CE2 . TYR B 1 187 ? 8.070   14.848 -10.142 1.00 48.26  ? 168  TYR B CE2 1 
ATOM   2897 C CZ  . TYR B 1 187 ? 8.159   13.743 -9.319  1.00 39.71  ? 168  TYR B CZ  1 
ATOM   2898 O OH  . TYR B 1 187 ? 8.405   13.891 -7.974  1.00 42.61  ? 168  TYR B OH  1 
ATOM   2899 N N   . SER B 1 188 ? 9.047   12.635 -16.612 1.00 27.93  ? 169  SER B N   1 
ATOM   2900 C CA  . SER B 1 188 ? 8.909   12.249 -18.018 1.00 28.53  ? 169  SER B CA  1 
ATOM   2901 C C   . SER B 1 188 ? 8.945   10.720 -18.202 1.00 35.78  ? 169  SER B C   1 
ATOM   2902 O O   . SER B 1 188 ? 9.547   10.007 -17.384 1.00 38.89  ? 169  SER B O   1 
ATOM   2903 C CB  . SER B 1 188 ? 10.026  12.882 -18.849 1.00 27.66  ? 169  SER B CB  1 
ATOM   2904 O OG  . SER B 1 188 ? 9.826   12.642 -20.227 1.00 25.56  ? 169  SER B OG  1 
ATOM   2905 N N   . ARG B 1 189 ? 8.318   10.222 -19.275 1.00 32.89  ? 170  ARG B N   1 
ATOM   2906 C CA  . ARG B 1 189 ? 8.401   8.796  -19.629 1.00 30.56  ? 170  ARG B CA  1 
ATOM   2907 C C   . ARG B 1 189 ? 9.723   8.473  -20.307 1.00 30.28  ? 170  ARG B C   1 
ATOM   2908 O O   . ARG B 1 189 ? 9.965   7.324  -20.672 1.00 28.54  ? 170  ARG B O   1 
ATOM   2909 C CB  . ARG B 1 189 ? 7.267   8.365  -20.574 1.00 30.72  ? 170  ARG B CB  1 
ATOM   2910 C CG  . ARG B 1 189 ? 5.874   8.488  -20.004 1.00 26.64  ? 170  ARG B CG  1 
ATOM   2911 C CD  . ARG B 1 189 ? 5.027   7.312  -20.412 1.00 34.32  ? 170  ARG B CD  1 
ATOM   2912 N NE  . ARG B 1 189 ? 4.823   7.218  -21.857 1.00 49.24  ? 170  ARG B NE  1 
ATOM   2913 C CZ  . ARG B 1 189 ? 4.466   6.098  -22.496 1.00 62.14  ? 170  ARG B CZ  1 
ATOM   2914 N NH1 . ARG B 1 189 ? 4.292   4.960  -21.828 1.00 52.96  ? 170  ARG B NH1 1 
ATOM   2915 N NH2 . ARG B 1 189 ? 4.296   6.109  -23.812 1.00 66.35  ? 170  ARG B NH2 1 
ATOM   2916 N N   . PHE B 1 190 ? 10.561  9.493  -20.490 1.00 29.84  ? 171  PHE B N   1 
ATOM   2917 C CA  . PHE B 1 190 ? 11.815  9.333  -21.219 1.00 27.01  ? 171  PHE B CA  1 
ATOM   2918 C C   . PHE B 1 190 ? 12.984  9.845  -20.405 1.00 33.77  ? 171  PHE B C   1 
ATOM   2919 O O   . PHE B 1 190 ? 12.798  10.533 -19.391 1.00 37.60  ? 171  PHE B O   1 
ATOM   2920 C CB  . PHE B 1 190 ? 11.765  10.069 -22.564 1.00 29.02  ? 171  PHE B CB  1 
ATOM   2921 C CG  . PHE B 1 190 ? 10.577  9.702  -23.416 1.00 29.49  ? 171  PHE B CG  1 
ATOM   2922 C CD1 . PHE B 1 190 ? 9.346   10.314 -23.214 1.00 24.33  ? 171  PHE B CD1 1 
ATOM   2923 C CD2 . PHE B 1 190 ? 10.694  8.745  -24.427 1.00 32.23  ? 171  PHE B CD2 1 
ATOM   2924 C CE1 . PHE B 1 190 ? 8.244   9.975  -23.997 1.00 31.67  ? 171  PHE B CE1 1 
ATOM   2925 C CE2 . PHE B 1 190 ? 9.594   8.391  -25.220 1.00 31.77  ? 171  PHE B CE2 1 
ATOM   2926 C CZ  . PHE B 1 190 ? 8.367   9.008  -25.003 1.00 34.80  ? 171  PHE B CZ  1 
ATOM   2927 N N   . GLU B 1 191 ? 14.191  9.508  -20.856 1.00 35.94  ? 172  GLU B N   1 
ATOM   2928 C CA  . GLU B 1 191 ? 15.404  9.976  -20.196 1.00 31.04  ? 172  GLU B CA  1 
ATOM   2929 C C   . GLU B 1 191 ? 16.444  10.378 -21.231 1.00 33.52  ? 172  GLU B C   1 
ATOM   2930 O O   . GLU B 1 191 ? 16.450  9.860  -22.362 1.00 29.84  ? 172  GLU B O   1 
ATOM   2931 C CB  . GLU B 1 191 ? 15.944  8.923  -19.212 1.00 35.04  ? 172  GLU B CB  1 
ATOM   2932 C CG  . GLU B 1 191 ? 16.341  7.577  -19.828 1.00 42.10  ? 172  GLU B CG  1 
ATOM   2933 C CD  . GLU B 1 191 ? 16.706  6.538  -18.762 1.00 54.90  ? 172  GLU B CD  1 
ATOM   2934 O OE1 . GLU B 1 191 ? 16.850  6.937  -17.583 1.00 51.52  ? 172  GLU B OE1 1 
ATOM   2935 O OE2 . GLU B 1 191 ? 16.834  5.326  -19.096 1.00 61.27  ? 172  GLU B OE2 1 
ATOM   2936 N N   . ILE B 1 192 ? 17.313  11.312 -20.847 1.00 34.42  ? 173  ILE B N   1 
ATOM   2937 C CA  . ILE B 1 192 ? 18.331  11.822 -21.765 1.00 34.00  ? 173  ILE B CA  1 
ATOM   2938 C C   . ILE B 1 192 ? 19.627  11.051 -21.574 1.00 33.18  ? 173  ILE B C   1 
ATOM   2939 O O   . ILE B 1 192 ? 20.096  10.884 -20.452 1.00 32.80  ? 173  ILE B O   1 
ATOM   2940 C CB  . ILE B 1 192 ? 18.543  13.358 -21.604 1.00 31.15  ? 173  ILE B CB  1 
ATOM   2941 C CG1 . ILE B 1 192 ? 17.229  14.091 -21.879 1.00 29.05  ? 173  ILE B CG1 1 
ATOM   2942 C CG2 . ILE B 1 192 ? 19.653  13.875 -22.520 1.00 28.55  ? 173  ILE B CG2 1 
ATOM   2943 C CD1 . ILE B 1 192 ? 17.318  15.571 -21.701 1.00 36.75  ? 173  ILE B CD1 1 
ATOM   2944 N N   . LEU B 1 193 ? 20.183  10.562 -22.678 1.00 34.82  ? 174  LEU B N   1 
ATOM   2945 C CA  . LEU B 1 193 ? 21.451  9.838  -22.648 1.00 38.76  ? 174  LEU B CA  1 
ATOM   2946 C C   . LEU B 1 193 ? 22.622  10.771 -22.933 1.00 40.65  ? 174  LEU B C   1 
ATOM   2947 O O   . LEU B 1 193 ? 23.672  10.671 -22.296 1.00 43.93  ? 174  LEU B O   1 
ATOM   2948 C CB  . LEU B 1 193 ? 21.435  8.692  -23.656 1.00 41.12  ? 174  LEU B CB  1 
ATOM   2949 C CG  . LEU B 1 193 ? 20.247  7.746  -23.489 1.00 41.30  ? 174  LEU B CG  1 
ATOM   2950 C CD1 . LEU B 1 193 ? 20.236  6.655  -24.562 1.00 36.48  ? 174  LEU B CD1 1 
ATOM   2951 C CD2 . LEU B 1 193 ? 20.220  7.157  -22.080 1.00 34.19  ? 174  LEU B CD2 1 
ATOM   2952 N N   . ASP B 1 194 ? 22.432  11.685 -23.884 1.00 41.61  ? 175  ASP B N   1 
ATOM   2953 C CA  . ASP B 1 194 ? 23.462  12.673 -24.217 1.00 42.51  ? 175  ASP B CA  1 
ATOM   2954 C C   . ASP B 1 194 ? 22.943  13.844 -25.065 1.00 42.86  ? 175  ASP B C   1 
ATOM   2955 O O   . ASP B 1 194 ? 21.982  13.701 -25.839 1.00 39.42  ? 175  ASP B O   1 
ATOM   2956 C CB  . ASP B 1 194 ? 24.625  11.991 -24.949 1.00 44.92  ? 175  ASP B CB  1 
ATOM   2957 C CG  . ASP B 1 194 ? 25.908  12.793 -24.875 1.00 57.41  ? 175  ASP B CG  1 
ATOM   2958 O OD1 . ASP B 1 194 ? 26.145  13.424 -23.820 1.00 71.40  ? 175  ASP B OD1 1 
ATOM   2959 O OD2 . ASP B 1 194 ? 26.671  12.800 -25.871 1.00 56.43  ? 175  ASP B OD2 1 
ATOM   2960 N N   . VAL B 1 195 ? 23.587  15.000 -24.918 1.00 40.99  ? 176  VAL B N   1 
ATOM   2961 C CA  . VAL B 1 195 ? 23.285  16.154 -25.762 1.00 41.02  ? 176  VAL B CA  1 
ATOM   2962 C C   . VAL B 1 195 ? 24.564  16.726 -26.361 1.00 40.27  ? 176  VAL B C   1 
ATOM   2963 O O   . VAL B 1 195 ? 25.459  17.135 -25.627 1.00 45.93  ? 176  VAL B O   1 
ATOM   2964 C CB  . VAL B 1 195 ? 22.563  17.281 -24.976 1.00 40.76  ? 176  VAL B CB  1 
ATOM   2965 C CG1 . VAL B 1 195 ? 22.334  18.490 -25.871 1.00 38.29  ? 176  VAL B CG1 1 
ATOM   2966 C CG2 . VAL B 1 195 ? 21.248  16.790 -24.398 1.00 41.16  ? 176  VAL B CG2 1 
ATOM   2967 N N   . THR B 1 196 ? 24.651  16.756 -27.688 1.00 37.76  ? 177  THR B N   1 
ATOM   2968 C CA  . THR B 1 196 ? 25.793  17.375 -28.363 1.00 40.61  ? 177  THR B CA  1 
ATOM   2969 C C   . THR B 1 196 ? 25.377  18.553 -29.250 1.00 44.49  ? 177  THR B C   1 
ATOM   2970 O O   . THR B 1 196 ? 24.247  18.599 -29.739 1.00 47.24  ? 177  THR B O   1 
ATOM   2971 C CB  . THR B 1 196 ? 26.581  16.354 -29.202 1.00 45.17  ? 177  THR B CB  1 
ATOM   2972 O OG1 . THR B 1 196 ? 25.731  15.796 -30.216 1.00 50.98  ? 177  THR B OG1 1 
ATOM   2973 C CG2 . THR B 1 196 ? 27.108  15.247 -28.321 1.00 42.76  ? 177  THR B CG2 1 
ATOM   2974 N N   . GLN B 1 197 ? 26.299  19.495 -29.455 1.00 46.08  ? 178  GLN B N   1 
ATOM   2975 C CA  . GLN B 1 197 ? 26.029  20.701 -30.236 1.00 43.03  ? 178  GLN B CA  1 
ATOM   2976 C C   . GLN B 1 197 ? 27.085  20.844 -31.333 1.00 42.20  ? 178  GLN B C   1 
ATOM   2977 O O   . GLN B 1 197 ? 28.263  20.582 -31.099 1.00 49.45  ? 178  GLN B O   1 
ATOM   2978 C CB  . GLN B 1 197 ? 26.052  21.943 -29.321 1.00 47.01  ? 178  GLN B CB  1 
ATOM   2979 C CG  . GLN B 1 197 ? 25.135  21.863 -28.088 1.00 51.08  ? 178  GLN B CG  1 
ATOM   2980 C CD  . GLN B 1 197 ? 24.707  23.242 -27.557 1.00 72.34  ? 178  GLN B CD  1 
ATOM   2981 O OE1 . GLN B 1 197 ? 25.471  24.209 -27.634 1.00 70.32  ? 178  GLN B OE1 1 
ATOM   2982 N NE2 . GLN B 1 197 ? 23.472  23.333 -27.024 1.00 64.06  ? 178  GLN B NE2 1 
ATOM   2983 N N   . LYS B 1 198 ? 26.689  21.250 -32.531 1.00 36.99  ? 179  LYS B N   1 
ATOM   2984 C CA  . LYS B 1 198 ? 27.696  21.638 -33.514 1.00 38.78  ? 179  LYS B CA  1 
ATOM   2985 C C   . LYS B 1 198 ? 27.195  22.768 -34.412 1.00 45.29  ? 179  LYS B C   1 
ATOM   2986 O O   . LYS B 1 198 ? 25.990  22.945 -34.589 1.00 42.62  ? 179  LYS B O   1 
ATOM   2987 C CB  . LYS B 1 198 ? 28.160  20.442 -34.351 1.00 37.96  ? 179  LYS B CB  1 
ATOM   2988 C CG  . LYS B 1 198 ? 27.360  20.236 -35.616 1.00 43.20  ? 179  LYS B CG  1 
ATOM   2989 C CD  . LYS B 1 198 ? 27.984  19.174 -36.490 1.00 52.49  ? 179  LYS B CD  1 
ATOM   2990 C CE  . LYS B 1 198 ? 27.060  18.824 -37.663 1.00 78.90  ? 179  LYS B CE  1 
ATOM   2991 N NZ  . LYS B 1 198 ? 27.646  17.775 -38.560 1.00 94.09  ? 179  LYS B NZ  1 
ATOM   2992 N N   . LYS B 1 199 ? 28.126  23.524 -34.986 1.00 48.34  ? 180  LYS B N   1 
ATOM   2993 C CA  . LYS B 1 199 ? 27.774  24.674 -35.809 1.00 37.71  ? 180  LYS B CA  1 
ATOM   2994 C C   . LYS B 1 199 ? 27.890  24.395 -37.312 1.00 38.04  ? 180  LYS B C   1 
ATOM   2995 O O   . LYS B 1 199 ? 28.864  23.812 -37.767 1.00 42.30  ? 180  LYS B O   1 
ATOM   2996 C CB  . LYS B 1 199 ? 28.656  25.856 -35.423 1.00 42.58  ? 180  LYS B CB  1 
ATOM   2997 C CG  . LYS B 1 199 ? 28.632  26.988 -36.426 1.00 50.23  ? 180  LYS B CG  1 
ATOM   2998 C CD  . LYS B 1 199 ? 29.523  28.121 -35.965 1.00 49.04  ? 180  LYS B CD  1 
ATOM   2999 C CE  . LYS B 1 199 ? 29.601  29.189 -37.037 1.00 62.10  ? 180  LYS B CE  1 
ATOM   3000 N NZ  . LYS B 1 199 ? 30.303  30.425 -36.553 1.00 74.13  ? 180  LYS B NZ  1 
ATOM   3001 N N   . ASN B 1 200 ? 26.887  24.803 -38.082 1.00 41.31  ? 181  ASN B N   1 
ATOM   3002 C CA  . ASN B 1 200 ? 26.942  24.669 -39.537 1.00 37.68  ? 181  ASN B CA  1 
ATOM   3003 C C   . ASN B 1 200 ? 26.898  26.032 -40.247 1.00 40.40  ? 181  ASN B C   1 
ATOM   3004 O O   . ASN B 1 200 ? 26.373  27.022 -39.729 1.00 40.44  ? 181  ASN B O   1 
ATOM   3005 C CB  . ASN B 1 200 ? 25.799  23.787 -40.071 1.00 45.65  ? 181  ASN B CB  1 
ATOM   3006 C CG  . ASN B 1 200 ? 25.672  22.457 -39.333 1.00 58.13  ? 181  ASN B CG  1 
ATOM   3007 O OD1 . ASN B 1 200 ? 26.477  21.539 -39.534 1.00 59.13  ? 181  ASN B OD1 1 
ATOM   3008 N ND2 . ASN B 1 200 ? 24.636  22.337 -38.492 1.00 58.33  ? 181  ASN B ND2 1 
ATOM   3009 N N   . SER B 1 201 ? 27.456  26.073 -41.445 1.00 39.91  ? 182  SER B N   1 
ATOM   3010 C CA  . SER B 1 201 ? 27.365  27.248 -42.286 1.00 30.32  ? 182  SER B CA  1 
ATOM   3011 C C   . SER B 1 201 ? 26.873  26.791 -43.660 1.00 39.10  ? 182  SER B C   1 
ATOM   3012 O O   . SER B 1 201 ? 27.571  26.051 -44.361 1.00 46.93  ? 182  SER B O   1 
ATOM   3013 C CB  . SER B 1 201 ? 28.724  27.895 -42.394 1.00 29.52  ? 182  SER B CB  1 
ATOM   3014 O OG  . SER B 1 201 ? 28.606  29.168 -42.989 1.00 46.40  ? 182  SER B OG  1 
ATOM   3015 N N   . VAL B 1 202 ? 25.664  27.213 -44.031 1.00 33.62  ? 183  VAL B N   1 
ATOM   3016 C CA  . VAL B 1 202 ? 24.961  26.646 -45.186 1.00 33.68  ? 183  VAL B CA  1 
ATOM   3017 C C   . VAL B 1 202 ? 24.702  27.699 -46.265 1.00 31.13  ? 183  VAL B C   1 
ATOM   3018 O O   . VAL B 1 202 ? 24.346  28.831 -45.948 1.00 34.02  ? 183  VAL B O   1 
ATOM   3019 C CB  . VAL B 1 202 ? 23.612  26.050 -44.747 1.00 26.15  ? 183  VAL B CB  1 
ATOM   3020 C CG1 . VAL B 1 202 ? 22.834  25.532 -45.940 1.00 35.11  ? 183  VAL B CG1 1 
ATOM   3021 C CG2 . VAL B 1 202 ? 23.827  24.977 -43.743 1.00 23.16  ? 183  VAL B CG2 1 
ATOM   3022 N N   . THR B 1 203 ? 24.892  27.338 -47.534 1.00 31.61  ? 184  THR B N   1 
ATOM   3023 C CA  . THR B 1 203 ? 24.504  28.228 -48.620 1.00 34.62  ? 184  THR B CA  1 
ATOM   3024 C C   . THR B 1 203 ? 23.237  27.708 -49.289 1.00 39.83  ? 184  THR B C   1 
ATOM   3025 O O   . THR B 1 203 ? 23.208  26.578 -49.777 1.00 43.01  ? 184  THR B O   1 
ATOM   3026 C CB  . THR B 1 203 ? 25.632  28.427 -49.647 1.00 39.27  ? 184  THR B CB  1 
ATOM   3027 O OG1 . THR B 1 203 ? 26.692  29.183 -49.040 1.00 44.81  ? 184  THR B OG1 1 
ATOM   3028 C CG2 . THR B 1 203 ? 25.122  29.187 -50.877 1.00 35.63  ? 184  THR B CG2 1 
ATOM   3029 N N   . TYR B 1 204 ? 22.189  28.534 -49.301 1.00 46.00  ? 185  TYR B N   1 
ATOM   3030 C CA  . TYR B 1 204 ? 20.910  28.171 -49.933 1.00 44.82  ? 185  TYR B CA  1 
ATOM   3031 C C   . TYR B 1 204 ? 20.813  28.609 -51.402 1.00 48.94  ? 185  TYR B C   1 
ATOM   3032 O O   . TYR B 1 204 ? 21.548  29.494 -51.852 1.00 60.82  ? 185  TYR B O   1 
ATOM   3033 C CB  . TYR B 1 204 ? 19.729  28.733 -49.131 1.00 41.83  ? 185  TYR B CB  1 
ATOM   3034 C CG  . TYR B 1 204 ? 19.655  28.193 -47.726 1.00 39.54  ? 185  TYR B CG  1 
ATOM   3035 C CD1 . TYR B 1 204 ? 20.340  28.808 -46.685 1.00 37.97  ? 185  TYR B CD1 1 
ATOM   3036 C CD2 . TYR B 1 204 ? 18.915  27.053 -47.440 1.00 42.95  ? 185  TYR B CD2 1 
ATOM   3037 C CE1 . TYR B 1 204 ? 20.287  28.301 -45.389 1.00 38.61  ? 185  TYR B CE1 1 
ATOM   3038 C CE2 . TYR B 1 204 ? 18.854  26.533 -46.148 1.00 31.69  ? 185  TYR B CE2 1 
ATOM   3039 C CZ  . TYR B 1 204 ? 19.541  27.160 -45.124 1.00 35.88  ? 185  TYR B CZ  1 
ATOM   3040 O OH  . TYR B 1 204 ? 19.493  26.658 -43.827 1.00 39.07  ? 185  TYR B OH  1 
ATOM   3041 N N   . SER B 1 205 ? 19.884  27.995 -52.131 1.00 45.06  ? 186  SER B N   1 
ATOM   3042 C CA  . SER B 1 205 ? 19.731  28.215 -53.572 1.00 51.89  ? 186  SER B CA  1 
ATOM   3043 C C   . SER B 1 205 ? 19.333  29.638 -53.944 1.00 57.64  ? 186  SER B C   1 
ATOM   3044 O O   . SER B 1 205 ? 19.476  30.057 -55.095 1.00 60.88  ? 186  SER B O   1 
ATOM   3045 C CB  . SER B 1 205 ? 18.727  27.221 -54.160 1.00 51.73  ? 186  SER B CB  1 
ATOM   3046 O OG  . SER B 1 205 ? 19.192  25.891 -54.018 1.00 62.04  ? 186  SER B OG  1 
ATOM   3047 N N   . CYS B 1 206 ? 18.844  30.381 -52.964 1.00 59.60  ? 187  CYS B N   1 
ATOM   3048 C CA  . CYS B 1 206 ? 18.351  31.724 -53.207 1.00 58.88  ? 187  CYS B CA  1 
ATOM   3049 C C   . CYS B 1 206 ? 19.465  32.791 -53.283 1.00 64.85  ? 187  CYS B C   1 
ATOM   3050 O O   . CYS B 1 206 ? 19.413  33.674 -54.135 1.00 83.57  ? 187  CYS B O   1 
ATOM   3051 C CB  . CYS B 1 206 ? 17.311  32.098 -52.138 1.00 68.88  ? 187  CYS B CB  1 
ATOM   3052 S SG  . CYS B 1 206 ? 18.021  32.664 -50.530 1.00 79.64  ? 187  CYS B SG  1 
ATOM   3053 N N   . CYS B 1 207 ? 20.470  32.706 -52.408 1.00 65.37  ? 188  CYS B N   1 
ATOM   3054 C CA  . CYS B 1 207 ? 21.448  33.794 -52.215 1.00 57.35  ? 188  CYS B CA  1 
ATOM   3055 C C   . CYS B 1 207 ? 22.896  33.284 -52.150 1.00 56.75  ? 188  CYS B C   1 
ATOM   3056 O O   . CYS B 1 207 ? 23.133  32.137 -51.766 1.00 58.91  ? 188  CYS B O   1 
ATOM   3057 C CB  . CYS B 1 207 ? 21.104  34.566 -50.934 1.00 64.57  ? 188  CYS B CB  1 
ATOM   3058 S SG  . CYS B 1 207 ? 19.478  34.078 -50.205 1.00 112.64 ? 188  CYS B SG  1 
ATOM   3059 N N   . PRO B 1 208 ? 23.870  34.139 -52.521 1.00 63.19  ? 189  PRO B N   1 
ATOM   3060 C CA  . PRO B 1 208 ? 25.293  33.760 -52.552 1.00 59.87  ? 189  PRO B CA  1 
ATOM   3061 C C   . PRO B 1 208 ? 25.950  33.819 -51.174 1.00 59.22  ? 189  PRO B C   1 
ATOM   3062 O O   . PRO B 1 208 ? 27.119  33.474 -51.028 1.00 61.93  ? 189  PRO B O   1 
ATOM   3063 C CB  . PRO B 1 208 ? 25.913  34.837 -53.455 1.00 62.98  ? 189  PRO B CB  1 
ATOM   3064 C CG  . PRO B 1 208 ? 25.085  36.046 -53.183 1.00 63.57  ? 189  PRO B CG  1 
ATOM   3065 C CD  . PRO B 1 208 ? 23.666  35.522 -53.000 1.00 65.23  ? 189  PRO B CD  1 
ATOM   3066 N N   . GLU B 1 209 ? 25.198  34.266 -50.177 1.00 63.90  ? 190  GLU B N   1 
ATOM   3067 C CA  . GLU B 1 209 ? 25.711  34.434 -48.820 1.00 55.60  ? 190  GLU B CA  1 
ATOM   3068 C C   . GLU B 1 209 ? 25.496  33.164 -47.996 1.00 54.98  ? 190  GLU B C   1 
ATOM   3069 O O   . GLU B 1 209 ? 24.612  32.358 -48.306 1.00 59.64  ? 190  GLU B O   1 
ATOM   3070 C CB  . GLU B 1 209 ? 24.988  35.608 -48.157 1.00 56.17  ? 190  GLU B CB  1 
ATOM   3071 C CG  . GLU B 1 209 ? 24.831  36.842 -49.060 1.00 62.29  ? 190  GLU B CG  1 
ATOM   3072 C CD  . GLU B 1 209 ? 26.097  37.690 -49.124 1.00 70.27  ? 190  GLU B CD  1 
ATOM   3073 O OE1 . GLU B 1 209 ? 27.125  37.299 -48.517 1.00 68.82  ? 190  GLU B OE1 1 
ATOM   3074 O OE2 . GLU B 1 209 ? 26.063  38.756 -49.776 1.00 71.80  ? 190  GLU B OE2 1 
ATOM   3075 N N   . ALA B 1 210 ? 26.293  32.984 -46.946 1.00 46.25  ? 191  ALA B N   1 
ATOM   3076 C CA  . ALA B 1 210 ? 26.140  31.818 -46.078 1.00 30.81  ? 191  ALA B CA  1 
ATOM   3077 C C   . ALA B 1 210 ? 25.292  32.168 -44.866 1.00 32.02  ? 191  ALA B C   1 
ATOM   3078 O O   . ALA B 1 210 ? 25.393  33.269 -44.331 1.00 37.35  ? 191  ALA B O   1 
ATOM   3079 C CB  . ALA B 1 210 ? 27.487  31.329 -45.630 1.00 37.25  ? 191  ALA B CB  1 
ATOM   3080 N N   . TYR B 1 211 ? 24.474  31.226 -44.415 1.00 33.09  ? 192  TYR B N   1 
ATOM   3081 C CA  . TYR B 1 211 ? 23.674  31.414 -43.198 1.00 29.38  ? 192  TYR B CA  1 
ATOM   3082 C C   . TYR B 1 211 ? 24.100  30.424 -42.124 1.00 28.58  ? 192  TYR B C   1 
ATOM   3083 O O   . TYR B 1 211 ? 24.023  29.208 -42.326 1.00 31.54  ? 192  TYR B O   1 
ATOM   3084 C CB  . TYR B 1 211 ? 22.190  31.224 -43.508 1.00 31.45  ? 192  TYR B CB  1 
ATOM   3085 C CG  . TYR B 1 211 ? 21.624  32.321 -44.355 1.00 27.60  ? 192  TYR B CG  1 
ATOM   3086 C CD1 . TYR B 1 211 ? 21.891  32.387 -45.711 1.00 30.25  ? 192  TYR B CD1 1 
ATOM   3087 C CD2 . TYR B 1 211 ? 20.833  33.306 -43.795 1.00 33.66  ? 192  TYR B CD2 1 
ATOM   3088 C CE1 . TYR B 1 211 ? 21.378  33.417 -46.497 1.00 38.71  ? 192  TYR B CE1 1 
ATOM   3089 C CE2 . TYR B 1 211 ? 20.314  34.350 -44.566 1.00 34.42  ? 192  TYR B CE2 1 
ATOM   3090 C CZ  . TYR B 1 211 ? 20.588  34.397 -45.920 1.00 37.47  ? 192  TYR B CZ  1 
ATOM   3091 O OH  . TYR B 1 211 ? 20.077  35.425 -46.694 1.00 39.09  ? 192  TYR B OH  1 
ATOM   3092 N N   . GLU B 1 212 ? 24.548  30.933 -40.983 1.00 24.95  ? 193  GLU B N   1 
ATOM   3093 C CA  . GLU B 1 212 ? 24.910  30.050 -39.870 1.00 31.03  ? 193  GLU B CA  1 
ATOM   3094 C C   . GLU B 1 212 ? 23.710  29.468 -39.096 1.00 28.70  ? 193  GLU B C   1 
ATOM   3095 O O   . GLU B 1 212 ? 22.663  30.104 -38.941 1.00 27.49  ? 193  GLU B O   1 
ATOM   3096 C CB  . GLU B 1 212 ? 25.861  30.754 -38.906 1.00 27.04  ? 193  GLU B CB  1 
ATOM   3097 C CG  . GLU B 1 212 ? 27.092  31.291 -39.579 1.00 34.20  ? 193  GLU B CG  1 
ATOM   3098 C CD  . GLU B 1 212 ? 28.105  31.848 -38.589 1.00 45.39  ? 193  GLU B CD  1 
ATOM   3099 O OE1 . GLU B 1 212 ? 27.827  31.792 -37.370 1.00 44.73  ? 193  GLU B OE1 1 
ATOM   3100 O OE2 . GLU B 1 212 ? 29.178  32.338 -39.027 1.00 50.60  ? 193  GLU B OE2 1 
ATOM   3101 N N   . ASP B 1 213 ? 23.880  28.247 -38.611 1.00 28.03  ? 194  ASP B N   1 
ATOM   3102 C CA  . ASP B 1 213 ? 22.932  27.657 -37.673 1.00 32.77  ? 194  ASP B CA  1 
ATOM   3103 C C   . ASP B 1 213 ? 23.643  26.740 -36.671 1.00 36.06  ? 194  ASP B C   1 
ATOM   3104 O O   . ASP B 1 213 ? 24.795  26.352 -36.871 1.00 31.43  ? 194  ASP B O   1 
ATOM   3105 C CB  . ASP B 1 213 ? 21.853  26.869 -38.404 1.00 29.89  ? 194  ASP B CB  1 
ATOM   3106 C CG  . ASP B 1 213 ? 22.440  25.805 -39.326 1.00 51.73  ? 194  ASP B CG  1 
ATOM   3107 O OD1 . ASP B 1 213 ? 22.794  24.693 -38.834 1.00 51.06  ? 194  ASP B OD1 1 
ATOM   3108 O OD2 . ASP B 1 213 ? 22.551  26.096 -40.549 1.00 57.33  ? 194  ASP B OD2 1 
ATOM   3109 N N   . VAL B 1 214 ? 22.941  26.414 -35.590 1.00 34.57  ? 195  VAL B N   1 
ATOM   3110 C CA  . VAL B 1 214 ? 23.416  25.447 -34.620 1.00 24.53  ? 195  VAL B CA  1 
ATOM   3111 C C   . VAL B 1 214 ? 22.517  24.218 -34.691 1.00 32.73  ? 195  VAL B C   1 
ATOM   3112 O O   . VAL B 1 214 ? 21.286  24.325 -34.784 1.00 27.18  ? 195  VAL B O   1 
ATOM   3113 C CB  . VAL B 1 214 ? 23.452  26.047 -33.209 1.00 21.18  ? 195  VAL B CB  1 
ATOM   3114 C CG1 . VAL B 1 214 ? 23.683  24.978 -32.143 1.00 25.12  ? 195  VAL B CG1 1 
ATOM   3115 C CG2 . VAL B 1 214 ? 24.524  27.112 -33.147 1.00 24.94  ? 195  VAL B CG2 1 
ATOM   3116 N N   . GLU B 1 215 ? 23.154  23.049 -34.696 1.00 38.65  ? 196  GLU B N   1 
ATOM   3117 C CA  . GLU B 1 215 ? 22.460  21.771 -34.713 1.00 33.74  ? 196  GLU B CA  1 
ATOM   3118 C C   . GLU B 1 215 ? 22.635  21.133 -33.338 1.00 34.17  ? 196  GLU B C   1 
ATOM   3119 O O   . GLU B 1 215 ? 23.764  20.926 -32.875 1.00 37.07  ? 196  GLU B O   1 
ATOM   3120 C CB  . GLU B 1 215 ? 23.064  20.877 -35.791 1.00 43.99  ? 196  GLU B CB  1 
ATOM   3121 C CG  . GLU B 1 215 ? 22.062  20.263 -36.755 1.00 55.09  ? 196  GLU B CG  1 
ATOM   3122 C CD  . GLU B 1 215 ? 22.731  19.426 -37.863 1.00 73.56  ? 196  GLU B CD  1 
ATOM   3123 O OE1 . GLU B 1 215 ? 23.637  18.600 -37.553 1.00 70.08  ? 196  GLU B OE1 1 
ATOM   3124 O OE2 . GLU B 1 215 ? 22.343  19.611 -39.044 1.00 66.27  ? 196  GLU B OE2 1 
ATOM   3125 N N   . VAL B 1 216 ? 21.524  20.846 -32.669 1.00 29.97  ? 197  VAL B N   1 
ATOM   3126 C CA  . VAL B 1 216 ? 21.584  20.235 -31.344 1.00 31.60  ? 197  VAL B CA  1 
ATOM   3127 C C   . VAL B 1 216 ? 21.072  18.793 -31.400 1.00 31.48  ? 197  VAL B C   1 
ATOM   3128 O O   . VAL B 1 216 ? 19.910  18.542 -31.751 1.00 25.79  ? 197  VAL B O   1 
ATOM   3129 C CB  . VAL B 1 216 ? 20.787  21.048 -30.304 1.00 28.11  ? 197  VAL B CB  1 
ATOM   3130 C CG1 . VAL B 1 216 ? 20.820  20.355 -28.967 1.00 27.98  ? 197  VAL B CG1 1 
ATOM   3131 C CG2 . VAL B 1 216 ? 21.351  22.438 -30.174 1.00 33.29  ? 197  VAL B CG2 1 
ATOM   3132 N N   . SER B 1 217 ? 21.949  17.849 -31.063 1.00 31.51  ? 198  SER B N   1 
ATOM   3133 C CA  . SER B 1 217 ? 21.615  16.432 -31.142 1.00 30.40  ? 198  SER B CA  1 
ATOM   3134 C C   . SER B 1 217 ? 21.205  15.923 -29.782 1.00 31.74  ? 198  SER B C   1 
ATOM   3135 O O   . SER B 1 217 ? 21.966  15.984 -28.813 1.00 33.61  ? 198  SER B O   1 
ATOM   3136 C CB  . SER B 1 217 ? 22.788  15.617 -31.674 1.00 29.06  ? 198  SER B CB  1 
ATOM   3137 O OG  . SER B 1 217 ? 23.185  16.108 -32.931 1.00 34.50  ? 198  SER B OG  1 
ATOM   3138 N N   . LEU B 1 218 ? 19.987  15.417 -29.718 1.00 31.95  ? 199  LEU B N   1 
ATOM   3139 C CA  . LEU B 1 218 ? 19.434  14.954 -28.461 1.00 38.16  ? 199  LEU B CA  1 
ATOM   3140 C C   . LEU B 1 218 ? 19.282  13.430 -28.486 1.00 38.75  ? 199  LEU B C   1 
ATOM   3141 O O   . LEU B 1 218 ? 18.434  12.878 -29.203 1.00 33.90  ? 199  LEU B O   1 
ATOM   3142 C CB  . LEU B 1 218 ? 18.096  15.643 -28.188 1.00 34.79  ? 199  LEU B CB  1 
ATOM   3143 C CG  . LEU B 1 218 ? 17.285  15.020 -27.052 1.00 36.67  ? 199  LEU B CG  1 
ATOM   3144 C CD1 . LEU B 1 218 ? 18.028  15.185 -25.737 1.00 31.39  ? 199  LEU B CD1 1 
ATOM   3145 C CD2 . LEU B 1 218 ? 15.881  15.615 -26.980 1.00 36.35  ? 199  LEU B CD2 1 
ATOM   3146 N N   . ASN B 1 219 ? 20.116  12.752 -27.706 1.00 37.15  ? 200  ASN B N   1 
ATOM   3147 C CA  . ASN B 1 219 ? 20.027  11.302 -27.605 1.00 39.35  ? 200  ASN B CA  1 
ATOM   3148 C C   . ASN B 1 219 ? 19.202  10.885 -26.370 1.00 38.04  ? 200  ASN B C   1 
ATOM   3149 O O   . ASN B 1 219 ? 19.585  11.163 -25.225 1.00 37.26  ? 200  ASN B O   1 
ATOM   3150 C CB  . ASN B 1 219 ? 21.436  10.689 -27.590 1.00 44.52  ? 200  ASN B CB  1 
ATOM   3151 C CG  . ASN B 1 219 ? 21.423  9.163  -27.624 1.00 42.14  ? 200  ASN B CG  1 
ATOM   3152 O OD1 . ASN B 1 219 ? 22.177  8.515  -26.901 1.00 42.81  ? 200  ASN B OD1 1 
ATOM   3153 N ND2 . ASN B 1 219 ? 20.557  8.588  -28.457 1.00 41.07  ? 200  ASN B ND2 1 
ATOM   3154 N N   . PHE B 1 220 ? 18.065  10.231 -26.611 1.00 33.71  ? 201  PHE B N   1 
ATOM   3155 C CA  . PHE B 1 220 ? 17.118  9.888  -25.544 1.00 33.16  ? 201  PHE B CA  1 
ATOM   3156 C C   . PHE B 1 220 ? 16.415  8.552  -25.819 1.00 35.44  ? 201  PHE B C   1 
ATOM   3157 O O   . PHE B 1 220 ? 16.348  8.097  -26.970 1.00 33.64  ? 201  PHE B O   1 
ATOM   3158 C CB  . PHE B 1 220 ? 16.062  10.993 -25.410 1.00 33.43  ? 201  PHE B CB  1 
ATOM   3159 C CG  . PHE B 1 220 ? 15.055  11.018 -26.543 1.00 32.01  ? 201  PHE B CG  1 
ATOM   3160 C CD1 . PHE B 1 220 ? 15.433  11.400 -27.831 1.00 30.75  ? 201  PHE B CD1 1 
ATOM   3161 C CD2 . PHE B 1 220 ? 13.730  10.656 -26.321 1.00 32.76  ? 201  PHE B CD2 1 
ATOM   3162 C CE1 . PHE B 1 220 ? 14.511  11.413 -28.881 1.00 29.92  ? 201  PHE B CE1 1 
ATOM   3163 C CE2 . PHE B 1 220 ? 12.794  10.674 -27.369 1.00 35.83  ? 201  PHE B CE2 1 
ATOM   3164 C CZ  . PHE B 1 220 ? 13.191  11.048 -28.651 1.00 30.94  ? 201  PHE B CZ  1 
ATOM   3165 N N   . ARG B 1 221 ? 15.880  7.932  -24.768 1.00 34.28  ? 202  ARG B N   1 
ATOM   3166 C CA  . ARG B 1 221 ? 15.088  6.706  -24.927 1.00 34.18  ? 202  ARG B CA  1 
ATOM   3167 C C   . ARG B 1 221 ? 13.980  6.623  -23.901 1.00 32.97  ? 202  ARG B C   1 
ATOM   3168 O O   . ARG B 1 221 ? 13.968  7.384  -22.922 1.00 38.30  ? 202  ARG B O   1 
ATOM   3169 C CB  . ARG B 1 221 ? 15.961  5.456  -24.790 1.00 35.22  ? 202  ARG B CB  1 
ATOM   3170 C CG  . ARG B 1 221 ? 16.666  5.386  -23.466 1.00 29.12  ? 202  ARG B CG  1 
ATOM   3171 C CD  . ARG B 1 221 ? 16.832  3.978  -22.996 1.00 32.28  ? 202  ARG B CD  1 
ATOM   3172 N NE  . ARG B 1 221 ? 17.510  3.963  -21.704 1.00 45.13  ? 202  ARG B NE  1 
ATOM   3173 C CZ  . ARG B 1 221 ? 18.783  3.629  -21.525 1.00 46.54  ? 202  ARG B CZ  1 
ATOM   3174 N NH1 . ARG B 1 221 ? 19.519  3.243  -22.561 1.00 35.11  ? 202  ARG B NH1 1 
ATOM   3175 N NH2 . ARG B 1 221 ? 19.312  3.667  -20.304 1.00 48.85  ? 202  ARG B NH2 1 
ATOM   3176 N N   . LYS B 1 222 ? 13.070  5.674  -24.122 1.00 35.46  ? 203  LYS B N   1 
ATOM   3177 C CA  . LYS B 1 222 ? 12.000  5.354  -23.171 1.00 32.95  ? 203  LYS B CA  1 
ATOM   3178 C C   . LYS B 1 222 ? 12.539  4.633  -21.932 1.00 33.87  ? 203  LYS B C   1 
ATOM   3179 O O   . LYS B 1 222 ? 13.443  3.792  -22.024 1.00 35.41  ? 203  LYS B O   1 
ATOM   3180 C CB  . LYS B 1 222 ? 10.934  4.499  -23.854 1.00 33.98  ? 203  LYS B CB  1 
ATOM   3181 C CG  . LYS B 1 222 ? 9.715   4.235  -22.999 1.00 50.32  ? 203  LYS B CG  1 
ATOM   3182 C CD  . LYS B 1 222 ? 8.666   3.488  -23.807 1.00 59.02  ? 203  LYS B CD  1 
ATOM   3183 C CE  . LYS B 1 222 ? 7.394   3.242  -23.008 1.00 71.43  ? 203  LYS B CE  1 
ATOM   3184 N NZ  . LYS B 1 222 ? 6.414   2.442  -23.807 1.00 68.35  ? 203  LYS B NZ  1 
ATOM   3185 N N   . LYS B 1 223 ? 11.989  4.972  -20.772 1.00 37.00  ? 204  LYS B N   1 
ATOM   3186 C CA  . LYS B 1 223 ? 12.427  4.379  -19.510 1.00 46.86  ? 204  LYS B CA  1 
ATOM   3187 C C   . LYS B 1 223 ? 11.929  2.944  -19.355 1.00 48.35  ? 204  LYS B C   1 
ATOM   3188 O O   . LYS B 1 223 ? 10.888  2.576  -19.931 1.00 48.92  ? 204  LYS B O   1 
ATOM   3189 C CB  . LYS B 1 223 ? 11.907  5.208  -18.331 1.00 40.54  ? 204  LYS B CB  1 
ATOM   3190 C CG  . LYS B 1 223 ? 12.617  6.525  -18.056 1.00 33.92  ? 204  LYS B CG  1 
ATOM   3191 C CD  . LYS B 1 223 ? 11.830  7.280  -16.998 1.00 30.00  ? 204  LYS B CD  1 
ATOM   3192 C CE  . LYS B 1 223 ? 12.672  8.301  -16.259 1.00 49.03  ? 204  LYS B CE  1 
ATOM   3193 N NZ  . LYS B 1 223 ? 11.950  8.818  -15.059 1.00 51.29  ? 204  LYS B NZ  1 
ATOM   3194 N N   . GLY B 1 224 ? 12.654  2.159  -18.555 1.00 47.26  ? 205  GLY B N   1 
ATOM   3195 C CA  . GLY B 1 224 ? 12.263  0.796  -18.210 1.00 52.81  ? 205  GLY B CA  1 
ATOM   3196 C C   . GLY B 1 224 ? 11.987  -0.118 -19.390 1.00 53.89  ? 205  GLY B C   1 
ATOM   3197 O O   . GLY B 1 224 ? 10.857  -0.188 -19.877 1.00 57.78  ? 205  GLY B O   1 
ATOM   3198 N N   . LEU C 1 20  ? 24.396  57.125 -45.136 1.00 56.56  ? 1    LEU C N   1 
ATOM   3199 C CA  . LEU C 1 20  ? 23.275  56.387 -44.584 1.00 44.88  ? 1    LEU C CA  1 
ATOM   3200 C C   . LEU C 1 20  ? 23.749  55.126 -43.879 1.00 46.43  ? 1    LEU C C   1 
ATOM   3201 O O   . LEU C 1 20  ? 24.527  54.346 -44.445 1.00 48.32  ? 1    LEU C O   1 
ATOM   3202 C CB  . LEU C 1 20  ? 22.323  55.978 -45.703 1.00 47.22  ? 1    LEU C CB  1 
ATOM   3203 C CG  . LEU C 1 20  ? 21.400  57.044 -46.252 1.00 38.02  ? 1    LEU C CG  1 
ATOM   3204 C CD1 . LEU C 1 20  ? 20.394  56.375 -47.180 1.00 39.01  ? 1    LEU C CD1 1 
ATOM   3205 C CD2 . LEU C 1 20  ? 20.713  57.760 -45.106 1.00 32.58  ? 1    LEU C CD2 1 
ATOM   3206 N N   . ASP C 1 21  ? 23.271  54.918 -42.656 1.00 40.78  ? 2    ASP C N   1 
ATOM   3207 C CA  . ASP C 1 21  ? 23.443  53.624 -41.991 1.00 42.92  ? 2    ASP C CA  1 
ATOM   3208 C C   . ASP C 1 21  ? 22.110  52.883 -41.895 1.00 38.35  ? 2    ASP C C   1 
ATOM   3209 O O   . ASP C 1 21  ? 21.082  53.402 -42.325 1.00 36.88  ? 2    ASP C O   1 
ATOM   3210 C CB  . ASP C 1 21  ? 24.089  53.780 -40.610 1.00 41.49  ? 2    ASP C CB  1 
ATOM   3211 C CG  . ASP C 1 21  ? 23.502  54.927 -39.815 1.00 54.44  ? 2    ASP C CG  1 
ATOM   3212 O OD1 . ASP C 1 21  ? 22.264  55.096 -39.844 1.00 54.05  ? 2    ASP C OD1 1 
ATOM   3213 O OD2 . ASP C 1 21  ? 24.281  55.663 -39.162 1.00 71.11  ? 2    ASP C OD2 1 
ATOM   3214 N N   . ARG C 1 22  ? 22.127  51.671 -41.349 1.00 39.81  ? 3    ARG C N   1 
ATOM   3215 C CA  . ARG C 1 22  ? 20.902  50.893 -41.236 1.00 31.50  ? 3    ARG C CA  1 
ATOM   3216 C C   . ARG C 1 22  ? 19.862  51.633 -40.432 1.00 29.88  ? 3    ARG C C   1 
ATOM   3217 O O   . ARG C 1 22  ? 18.685  51.622 -40.795 1.00 31.89  ? 3    ARG C O   1 
ATOM   3218 C CB  . ARG C 1 22  ? 21.160  49.533 -40.598 1.00 31.06  ? 3    ARG C CB  1 
ATOM   3219 C CG  . ARG C 1 22  ? 21.736  48.527 -41.549 1.00 31.17  ? 3    ARG C CG  1 
ATOM   3220 C CD  . ARG C 1 22  ? 21.953  47.200 -40.867 1.00 42.73  ? 3    ARG C CD  1 
ATOM   3221 N NE  . ARG C 1 22  ? 22.447  46.210 -41.816 1.00 47.05  ? 3    ARG C NE  1 
ATOM   3222 C CZ  . ARG C 1 22  ? 23.728  46.079 -42.132 1.00 51.09  ? 3    ARG C CZ  1 
ATOM   3223 N NH1 . ARG C 1 22  ? 24.626  46.876 -41.558 1.00 59.49  ? 3    ARG C NH1 1 
ATOM   3224 N NH2 . ARG C 1 22  ? 24.108  45.157 -43.014 1.00 47.10  ? 3    ARG C NH2 1 
ATOM   3225 N N   . ALA C 1 23  ? 20.293  52.285 -39.355 1.00 27.26  ? 4    ALA C N   1 
ATOM   3226 C CA  . ALA C 1 23  ? 19.358  53.004 -38.499 1.00 24.84  ? 4    ALA C CA  1 
ATOM   3227 C C   . ALA C 1 23  ? 18.578  54.074 -39.272 1.00 31.51  ? 4    ALA C C   1 
ATOM   3228 O O   . ALA C 1 23  ? 17.352  54.196 -39.136 1.00 31.98  ? 4    ALA C O   1 
ATOM   3229 C CB  . ALA C 1 23  ? 20.065  53.599 -37.335 1.00 21.47  ? 4    ALA C CB  1 
ATOM   3230 N N   . ASP C 1 24  ? 19.294  54.833 -40.095 1.00 31.19  ? 5    ASP C N   1 
ATOM   3231 C CA  . ASP C 1 24  ? 18.684  55.853 -40.948 1.00 29.75  ? 5    ASP C CA  1 
ATOM   3232 C C   . ASP C 1 24  ? 17.675  55.300 -41.976 1.00 29.10  ? 5    ASP C C   1 
ATOM   3233 O O   . ASP C 1 24  ? 16.561  55.816 -42.095 1.00 22.34  ? 5    ASP C O   1 
ATOM   3234 C CB  . ASP C 1 24  ? 19.780  56.667 -41.631 1.00 32.74  ? 5    ASP C CB  1 
ATOM   3235 C CG  . ASP C 1 24  ? 20.547  57.553 -40.645 1.00 55.18  ? 5    ASP C CG  1 
ATOM   3236 O OD1 . ASP C 1 24  ? 19.906  58.023 -39.660 1.00 53.85  ? 5    ASP C OD1 1 
ATOM   3237 O OD2 . ASP C 1 24  ? 21.777  57.774 -40.858 1.00 61.69  ? 5    ASP C OD2 1 
ATOM   3238 N N   . ILE C 1 25  ? 18.062  54.234 -42.685 1.00 27.82  ? 6    ILE C N   1 
ATOM   3239 C CA  . ILE C 1 25  ? 17.211  53.597 -43.693 1.00 22.77  ? 6    ILE C CA  1 
ATOM   3240 C C   . ILE C 1 25  ? 15.906  53.076 -43.095 1.00 26.53  ? 6    ILE C C   1 
ATOM   3241 O O   . ILE C 1 25  ? 14.807  53.351 -43.611 1.00 24.50  ? 6    ILE C O   1 
ATOM   3242 C CB  . ILE C 1 25  ? 17.945  52.444 -44.423 1.00 23.05  ? 6    ILE C CB  1 
ATOM   3243 C CG1 . ILE C 1 25  ? 19.143  52.979 -45.190 1.00 27.10  ? 6    ILE C CG1 1 
ATOM   3244 C CG2 . ILE C 1 25  ? 17.017  51.713 -45.401 1.00 19.60  ? 6    ILE C CG2 1 
ATOM   3245 C CD1 . ILE C 1 25  ? 20.077  51.885 -45.652 1.00 33.26  ? 6    ILE C CD1 1 
ATOM   3246 N N   . LEU C 1 26  ? 16.029  52.328 -42.002 1.00 26.78  ? 7    LEU C N   1 
ATOM   3247 C CA  . LEU C 1 26  ? 14.860  51.763 -41.338 1.00 27.76  ? 7    LEU C CA  1 
ATOM   3248 C C   . LEU C 1 26  ? 13.950  52.869 -40.805 1.00 27.17  ? 7    LEU C C   1 
ATOM   3249 O O   . LEU C 1 26  ? 12.712  52.761 -40.839 1.00 28.27  ? 7    LEU C O   1 
ATOM   3250 C CB  . LEU C 1 26  ? 15.276  50.787 -40.235 1.00 27.47  ? 7    LEU C CB  1 
ATOM   3251 C CG  . LEU C 1 26  ? 15.906  49.513 -40.804 1.00 25.37  ? 7    LEU C CG  1 
ATOM   3252 C CD1 . LEU C 1 26  ? 16.731  48.779 -39.769 1.00 25.49  ? 7    LEU C CD1 1 
ATOM   3253 C CD2 . LEU C 1 26  ? 14.842  48.601 -41.360 1.00 21.82  ? 7    LEU C CD2 1 
ATOM   3254 N N   . TYR C 1 27  ? 14.565  53.953 -40.351 1.00 29.86  ? 8    TYR C N   1 
ATOM   3255 C CA  . TYR C 1 27  ? 13.802  55.127 -39.933 1.00 29.93  ? 8    TYR C CA  1 
ATOM   3256 C C   . TYR C 1 27  ? 12.966  55.692 -41.083 1.00 27.64  ? 8    TYR C C   1 
ATOM   3257 O O   . TYR C 1 27  ? 11.746  55.818 -40.970 1.00 24.43  ? 8    TYR C O   1 
ATOM   3258 C CB  . TYR C 1 27  ? 14.732  56.200 -39.379 1.00 31.74  ? 8    TYR C CB  1 
ATOM   3259 C CG  . TYR C 1 27  ? 14.000  57.425 -38.901 1.00 31.08  ? 8    TYR C CG  1 
ATOM   3260 C CD1 . TYR C 1 27  ? 13.298  57.417 -37.708 1.00 32.81  ? 8    TYR C CD1 1 
ATOM   3261 C CD2 . TYR C 1 27  ? 14.017  58.596 -39.645 1.00 38.62  ? 8    TYR C CD2 1 
ATOM   3262 C CE1 . TYR C 1 27  ? 12.628  58.550 -37.264 1.00 41.76  ? 8    TYR C CE1 1 
ATOM   3263 C CE2 . TYR C 1 27  ? 13.359  59.736 -39.215 1.00 45.22  ? 8    TYR C CE2 1 
ATOM   3264 C CZ  . TYR C 1 27  ? 12.662  59.711 -38.022 1.00 51.14  ? 8    TYR C CZ  1 
ATOM   3265 O OH  . TYR C 1 27  ? 12.002  60.850 -37.594 1.00 49.09  ? 8    TYR C OH  1 
ATOM   3266 N N   . ASN C 1 28  ? 13.625  56.019 -42.192 1.00 30.09  ? 9    ASN C N   1 
ATOM   3267 C CA  . ASN C 1 28  ? 12.917  56.525 -43.363 1.00 25.32  ? 9    ASN C CA  1 
ATOM   3268 C C   . ASN C 1 28  ? 11.825  55.588 -43.838 1.00 27.37  ? 9    ASN C C   1 
ATOM   3269 O O   . ASN C 1 28  ? 10.734  56.032 -44.188 1.00 28.33  ? 9    ASN C O   1 
ATOM   3270 C CB  . ASN C 1 28  ? 13.882  56.815 -44.501 1.00 24.26  ? 9    ASN C CB  1 
ATOM   3271 C CG  . ASN C 1 28  ? 14.897  57.863 -44.142 1.00 28.43  ? 9    ASN C CG  1 
ATOM   3272 O OD1 . ASN C 1 28  ? 14.646  58.732 -43.288 1.00 26.50  ? 9    ASN C OD1 1 
ATOM   3273 N ND2 . ASN C 1 28  ? 16.067  57.792 -44.787 1.00 29.71  ? 9    ASN C ND2 1 
ATOM   3274 N N   . ILE C 1 29  ? 12.109  54.289 -43.844 1.00 29.13  ? 10   ILE C N   1 
ATOM   3275 C CA  . ILE C 1 29  ? 11.084  53.321 -44.228 1.00 29.64  ? 10   ILE C CA  1 
ATOM   3276 C C   . ILE C 1 29  ? 9.874   53.338 -43.295 1.00 30.82  ? 10   ILE C C   1 
ATOM   3277 O O   . ILE C 1 29  ? 8.733   53.386 -43.753 1.00 33.22  ? 10   ILE C O   1 
ATOM   3278 C CB  . ILE C 1 29  ? 11.637  51.909 -44.357 1.00 26.44  ? 10   ILE C CB  1 
ATOM   3279 C CG1 . ILE C 1 29  ? 12.625  51.869 -45.531 1.00 27.59  ? 10   ILE C CG1 1 
ATOM   3280 C CG2 . ILE C 1 29  ? 10.491  50.914 -44.544 1.00 25.28  ? 10   ILE C CG2 1 
ATOM   3281 C CD1 . ILE C 1 29  ? 13.265  50.508 -45.796 1.00 23.26  ? 10   ILE C CD1 1 
ATOM   3282 N N   . ARG C 1 30  ? 10.117  53.343 -41.990 1.00 28.60  ? 11   ARG C N   1 
ATOM   3283 C CA  . ARG C 1 30  ? 9.011   53.433 -41.047 1.00 28.26  ? 11   ARG C CA  1 
ATOM   3284 C C   . ARG C 1 30  ? 8.126   54.686 -41.239 1.00 34.25  ? 11   ARG C C   1 
ATOM   3285 O O   . ARG C 1 30  ? 6.909   54.619 -41.061 1.00 39.30  ? 11   ARG C O   1 
ATOM   3286 C CB  . ARG C 1 30  ? 9.513   53.326 -39.615 1.00 26.46  ? 11   ARG C CB  1 
ATOM   3287 C CG  . ARG C 1 30  ? 8.619   52.468 -38.767 1.00 45.30  ? 11   ARG C CG  1 
ATOM   3288 C CD  . ARG C 1 30  ? 8.520   52.977 -37.342 1.00 72.04  ? 11   ARG C CD  1 
ATOM   3289 N NE  . ARG C 1 30  ? 7.329   52.436 -36.689 1.00 87.10  ? 11   ARG C NE  1 
ATOM   3290 C CZ  . ARG C 1 30  ? 6.948   52.726 -35.447 1.00 89.02  ? 11   ARG C CZ  1 
ATOM   3291 N NH1 . ARG C 1 30  ? 7.662   53.562 -34.698 1.00 84.78  ? 11   ARG C NH1 1 
ATOM   3292 N NH2 . ARG C 1 30  ? 5.848   52.177 -34.952 1.00 88.62  ? 11   ARG C NH2 1 
ATOM   3293 N N   . GLN C 1 31  ? 8.729   55.808 -41.637 1.00 32.41  ? 12   GLN C N   1 
ATOM   3294 C CA  . GLN C 1 31  ? 8.007   57.082 -41.768 1.00 30.44  ? 12   GLN C CA  1 
ATOM   3295 C C   . GLN C 1 31  ? 7.239   57.297 -43.076 1.00 32.45  ? 12   GLN C C   1 
ATOM   3296 O O   . GLN C 1 31  ? 6.315   58.101 -43.116 1.00 36.76  ? 12   GLN C O   1 
ATOM   3297 C CB  . GLN C 1 31  ? 8.967   58.266 -41.576 1.00 33.20  ? 12   GLN C CB  1 
ATOM   3298 C CG  . GLN C 1 31  ? 9.694   58.312 -40.237 1.00 38.57  ? 12   GLN C CG  1 
ATOM   3299 C CD  . GLN C 1 31  ? 8.748   58.518 -39.056 1.00 49.22  ? 12   GLN C CD  1 
ATOM   3300 O OE1 . GLN C 1 31  ? 7.597   58.940 -39.226 1.00 54.34  ? 12   GLN C OE1 1 
ATOM   3301 N NE2 . GLN C 1 31  ? 9.230   58.212 -37.852 1.00 44.09  ? 12   GLN C NE2 1 
ATOM   3302 N N   . THR C 1 32  ? 7.622   56.597 -44.141 1.00 27.43  ? 13   THR C N   1 
ATOM   3303 C CA  . THR C 1 32  ? 7.155   56.953 -45.477 1.00 27.41  ? 13   THR C CA  1 
ATOM   3304 C C   . THR C 1 32  ? 6.600   55.795 -46.299 1.00 37.00  ? 13   THR C C   1 
ATOM   3305 O O   . THR C 1 32  ? 6.282   55.951 -47.489 1.00 40.10  ? 13   THR C O   1 
ATOM   3306 C CB  . THR C 1 32  ? 8.302   57.586 -46.305 1.00 28.68  ? 13   THR C CB  1 
ATOM   3307 O OG1 . THR C 1 32  ? 9.359   56.629 -46.491 1.00 30.41  ? 13   THR C OG1 1 
ATOM   3308 C CG2 . THR C 1 32  ? 8.840   58.828 -45.624 1.00 28.66  ? 13   THR C CG2 1 
ATOM   3309 N N   . SER C 1 33  ? 6.536   54.636 -45.689 1.00 45.51  ? 14   SER C N   1 
ATOM   3310 C CA  . SER C 1 33  ? 6.292   53.386 -46.398 1.00 45.50  ? 14   SER C CA  1 
ATOM   3311 C C   . SER C 1 33  ? 4.944   53.180 -47.072 1.00 45.18  ? 14   SER C C   1 
ATOM   3312 O O   . SER C 1 33  ? 4.887   52.689 -48.181 1.00 33.87  ? 14   SER C O   1 
ATOM   3313 C CB  . SER C 1 33  ? 6.570   52.240 -45.461 1.00 37.94  ? 14   SER C CB  1 
ATOM   3314 O OG  . SER C 1 33  ? 6.322   51.058 -46.117 1.00 38.40  ? 14   SER C OG  1 
ATOM   3315 N N   . ARG C 1 34  ? 3.867   53.587 -46.409 1.00 43.81  ? 15   ARG C N   1 
ATOM   3316 C CA  . ARG C 1 34  ? 2.517   53.389 -46.905 1.00 34.04  ? 15   ARG C CA  1 
ATOM   3317 C C   . ARG C 1 34  ? 2.104   51.965 -47.162 1.00 33.83  ? 15   ARG C C   1 
ATOM   3318 O O   . ARG C 1 34  ? 1.970   51.539 -48.259 1.00 37.50  ? 15   ARG C O   1 
ATOM   3319 C CB  . ARG C 1 34  ? 2.233   54.262 -48.103 1.00 37.97  ? 15   ARG C CB  1 
ATOM   3320 C CG  . ARG C 1 34  ? 2.252   55.739 -47.813 1.00 35.57  ? 15   ARG C CG  1 
ATOM   3321 C CD  . ARG C 1 34  ? 1.226   56.134 -46.778 1.00 42.22  ? 15   ARG C CD  1 
ATOM   3322 N NE  . ARG C 1 34  ? -0.133  56.117 -47.306 1.00 47.11  ? 15   ARG C NE  1 
ATOM   3323 C CZ  . ARG C 1 34  ? -0.662  57.020 -48.112 1.00 39.84  ? 15   ARG C CZ  1 
ATOM   3324 N NH1 . ARG C 1 34  ? 0.031   58.050 -48.526 1.00 30.90  ? 15   ARG C NH1 1 
ATOM   3325 N NH2 . ARG C 1 34  ? -1.888  56.874 -48.520 1.00 30.62  ? 15   ARG C NH2 1 
ATOM   3326 N N   . PRO C 1 35  ? 1.908   51.216 -46.027 1.00 26.49  ? 16   PRO C N   1 
ATOM   3327 C CA  . PRO C 1 35  ? 1.641   49.804 -46.228 1.00 23.98  ? 16   PRO C CA  1 
ATOM   3328 C C   . PRO C 1 35  ? 0.327   49.484 -46.863 1.00 24.60  ? 16   PRO C C   1 
ATOM   3329 O O   . PRO C 1 35  ? 0.044   48.365 -47.150 1.00 23.26  ? 16   PRO C O   1 
ATOM   3330 C CB  . PRO C 1 35  ? 1.592   49.275 -44.821 1.00 26.17  ? 16   PRO C CB  1 
ATOM   3331 C CG  . PRO C 1 35  ? 2.374   50.185 -44.043 1.00 28.56  ? 16   PRO C CG  1 
ATOM   3332 C CD  . PRO C 1 35  ? 1.849   51.437 -44.527 1.00 31.01  ? 16   PRO C CD  1 
ATOM   3333 N N   . ASP C 1 36  ? -0.535  50.461 -46.927 1.00 28.96  ? 17   ASP C N   1 
ATOM   3334 C CA  . ASP C 1 36  ? -1.873  50.270 -47.408 1.00 25.94  ? 17   ASP C CA  1 
ATOM   3335 C C   . ASP C 1 36  ? -2.006  50.540 -48.876 1.00 26.25  ? 17   ASP C C   1 
ATOM   3336 O O   . ASP C 1 36  ? -3.010  50.286 -49.464 1.00 24.86  ? 17   ASP C O   1 
ATOM   3337 C CB  . ASP C 1 36  ? -2.842  51.106 -46.567 1.00 28.14  ? 17   ASP C CB  1 
ATOM   3338 C CG  . ASP C 1 36  ? -2.489  52.580 -46.513 1.00 42.90  ? 17   ASP C CG  1 
ATOM   3339 O OD1 . ASP C 1 36  ? -1.342  52.960 -46.270 1.00 40.36  ? 17   ASP C OD1 1 
ATOM   3340 O OD2 . ASP C 1 36  ? -3.405  53.386 -46.675 1.00 45.35  ? 17   ASP C OD2 1 
ATOM   3341 N N   . VAL C 1 37  ? -0.941  51.040 -49.462 1.00 24.93  ? 18   VAL C N   1 
ATOM   3342 C CA  . VAL C 1 37  ? -0.919  51.500 -50.865 1.00 27.98  ? 18   VAL C CA  1 
ATOM   3343 C C   . VAL C 1 37  ? -0.119  50.587 -51.790 1.00 24.06  ? 18   VAL C C   1 
ATOM   3344 O O   . VAL C 1 37  ? 1.109   50.505 -51.688 1.00 25.53  ? 18   VAL C O   1 
ATOM   3345 C CB  . VAL C 1 37  ? -0.303  52.911 -51.011 1.00 22.70  ? 18   VAL C CB  1 
ATOM   3346 C CG1 . VAL C 1 37  ? -0.218  53.288 -52.468 1.00 16.59  ? 18   VAL C CG1 1 
ATOM   3347 C CG2 . VAL C 1 37  ? -1.074  53.920 -50.211 1.00 25.60  ? 18   VAL C CG2 1 
ATOM   3348 N N   . ILE C 1 38  ? -0.818  49.925 -52.704 1.00 20.08  ? 19   ILE C N   1 
ATOM   3349 C CA  . ILE C 1 38  ? -0.177  49.082 -53.714 1.00 22.26  ? 19   ILE C CA  1 
ATOM   3350 C C   . ILE C 1 38  ? 0.785   49.878 -54.606 1.00 25.02  ? 19   ILE C C   1 
ATOM   3351 O O   . ILE C 1 38  ? 0.400   50.901 -55.171 1.00 32.15  ? 19   ILE C O   1 
ATOM   3352 C CB  . ILE C 1 38  ? -1.256  48.337 -54.549 1.00 25.91  ? 19   ILE C CB  1 
ATOM   3353 C CG1 . ILE C 1 38  ? -0.631  47.352 -55.541 1.00 25.46  ? 19   ILE C CG1 1 
ATOM   3354 C CG2 . ILE C 1 38  ? -2.210  49.310 -55.242 1.00 19.48  ? 19   ILE C CG2 1 
ATOM   3355 C CD1 . ILE C 1 38  ? -1.667  46.419 -56.181 1.00 23.98  ? 19   ILE C CD1 1 
ATOM   3356 N N   . PRO C 1 39  ? 2.053   49.418 -54.724 1.00 30.32  ? 20   PRO C N   1 
ATOM   3357 C CA  . PRO C 1 39  ? 3.106   50.152 -55.460 1.00 31.89  ? 20   PRO C CA  1 
ATOM   3358 C C   . PRO C 1 39  ? 3.049   49.962 -56.982 1.00 33.10  ? 20   PRO C C   1 
ATOM   3359 O O   . PRO C 1 39  ? 4.000   49.456 -57.588 1.00 33.36  ? 20   PRO C O   1 
ATOM   3360 C CB  . PRO C 1 39  ? 4.409   49.559 -54.889 1.00 30.59  ? 20   PRO C CB  1 
ATOM   3361 C CG  . PRO C 1 39  ? 4.055   48.142 -54.537 1.00 23.58  ? 20   PRO C CG  1 
ATOM   3362 C CD  . PRO C 1 39  ? 2.575   48.174 -54.117 1.00 27.37  ? 20   PRO C CD  1 
ATOM   3363 N N   . THR C 1 40  ? 1.928   50.347 -57.585 1.00 36.60  ? 21   THR C N   1 
ATOM   3364 C CA  . THR C 1 40  ? 1.785   50.285 -59.033 1.00 44.75  ? 21   THR C CA  1 
ATOM   3365 C C   . THR C 1 40  ? 2.672   51.343 -59.692 1.00 53.63  ? 21   THR C C   1 
ATOM   3366 O O   . THR C 1 40  ? 2.953   52.387 -59.108 1.00 48.15  ? 21   THR C O   1 
ATOM   3367 C CB  . THR C 1 40  ? 0.327   50.504 -59.463 1.00 47.26  ? 21   THR C CB  1 
ATOM   3368 O OG1 . THR C 1 40  ? -0.170  51.716 -58.872 1.00 55.62  ? 21   THR C OG1 1 
ATOM   3369 C CG2 . THR C 1 40  ? -0.542  49.355 -59.012 1.00 34.87  ? 21   THR C CG2 1 
ATOM   3370 N N   . GLN C 1 41  ? 3.158   51.023 -60.868 1.00 66.47  ? 22   GLN C N   1 
ATOM   3371 C CA  . GLN C 1 41  ? 3.924   51.957 -61.624 1.00 74.38  ? 22   GLN C CA  1 
ATOM   3372 C C   . GLN C 1 41  ? 3.156   52.243 -62.881 1.00 81.70  ? 22   GLN C C   1 
ATOM   3373 O O   . GLN C 1 41  ? 2.998   51.377 -63.720 1.00 80.99  ? 22   GLN C O   1 
ATOM   3374 C CB  . GLN C 1 41  ? 5.224   51.298 -62.010 1.00 70.73  ? 22   GLN C CB  1 
ATOM   3375 C CG  . GLN C 1 41  ? 6.278   51.292 -60.926 1.00 74.10  ? 22   GLN C CG  1 
ATOM   3376 C CD  . GLN C 1 41  ? 7.615   50.857 -61.467 1.00 82.04  ? 22   GLN C CD  1 
ATOM   3377 O OE1 . GLN C 1 41  ? 7.733   49.776 -62.005 1.00 70.60  ? 22   GLN C OE1 1 
ATOM   3378 N NE2 . GLN C 1 41  ? 8.627   51.708 -61.337 1.00 73.75  ? 22   GLN C NE2 1 
ATOM   3379 N N   . ARG C 1 42  ? 2.696   53.468 -63.032 1.00 76.25  ? 23   ARG C N   1 
ATOM   3380 C CA  . ARG C 1 42  ? 2.055   53.848 -64.264 1.00 84.13  ? 23   ARG C CA  1 
ATOM   3381 C C   . ARG C 1 42  ? 0.932   52.905 -64.570 1.00 80.44  ? 23   ARG C C   1 
ATOM   3382 O O   . ARG C 1 42  ? 0.709   52.538 -65.700 1.00 80.03  ? 23   ARG C O   1 
ATOM   3383 C CB  . ARG C 1 42  ? 3.074   53.890 -65.393 1.00 91.54  ? 23   ARG C CB  1 
ATOM   3384 C CG  . ARG C 1 42  ? 4.124   54.944 -65.131 1.00 93.06  ? 23   ARG C CG  1 
ATOM   3385 C CD  . ARG C 1 42  ? 5.195   55.026 -66.192 1.00 95.11  ? 23   ARG C CD  1 
ATOM   3386 N NE  . ARG C 1 42  ? 6.349   55.782 -65.713 1.00 104.22 ? 23   ARG C NE  1 
ATOM   3387 C CZ  . ARG C 1 42  ? 7.030   56.650 -66.445 1.00 103.15 ? 23   ARG C CZ  1 
ATOM   3388 N NH1 . ARG C 1 42  ? 6.674   56.908 -67.689 1.00 100.69 ? 23   ARG C NH1 1 
ATOM   3389 N NH2 . ARG C 1 42  ? 8.058   57.275 -65.923 1.00 103.07 ? 23   ARG C NH2 1 
ATOM   3390 N N   . ASP C 1 43  ? 0.217   52.512 -63.536 1.00 86.40  ? 24   ASP C N   1 
ATOM   3391 C CA  . ASP C 1 43  ? -0.967  51.665 -63.703 1.00 87.02  ? 24   ASP C CA  1 
ATOM   3392 C C   . ASP C 1 43  ? -0.686  50.433 -64.529 1.00 77.41  ? 24   ASP C C   1 
ATOM   3393 O O   . ASP C 1 43  ? -1.383  50.122 -65.458 1.00 80.61  ? 24   ASP C O   1 
ATOM   3394 C CB  . ASP C 1 43  ? -2.179  52.463 -64.177 1.00 99.04  ? 24   ASP C CB  1 
ATOM   3395 C CG  . ASP C 1 43  ? -2.557  53.546 -63.193 1.00 112.62 ? 24   ASP C CG  1 
ATOM   3396 O OD1 . ASP C 1 43  ? -1.656  53.968 -62.447 1.00 97.29  ? 24   ASP C OD1 1 
ATOM   3397 O OD2 . ASP C 1 43  ? -3.728  53.965 -63.147 1.00 119.37 ? 24   ASP C OD2 1 
ATOM   3398 N N   . ARG C 1 44  ? 0.383   49.761 -64.146 1.00 75.98  ? 25   ARG C N   1 
ATOM   3399 C CA  . ARG C 1 44  ? 0.798   48.506 -64.688 1.00 62.76  ? 25   ARG C CA  1 
ATOM   3400 C C   . ARG C 1 44  ? 0.788   47.668 -63.468 1.00 49.83  ? 25   ARG C C   1 
ATOM   3401 O O   . ARG C 1 44  ? 0.890   48.172 -62.374 1.00 50.28  ? 25   ARG C O   1 
ATOM   3402 C CB  . ARG C 1 44  ? 2.203   48.607 -65.256 1.00 68.38  ? 25   ARG C CB  1 
ATOM   3403 C CG  . ARG C 1 44  ? 2.425   49.946 -65.936 1.00 87.31  ? 25   ARG C CG  1 
ATOM   3404 C CD  . ARG C 1 44  ? 3.566   50.052 -66.924 1.00 104.01 ? 25   ARG C CD  1 
ATOM   3405 N NE  . ARG C 1 44  ? 3.615   51.421 -67.430 1.00 114.71 ? 25   ARG C NE  1 
ATOM   3406 C CZ  . ARG C 1 44  ? 4.182   51.794 -68.571 1.00 113.63 ? 25   ARG C CZ  1 
ATOM   3407 N NH1 . ARG C 1 44  ? 4.767   50.897 -69.344 1.00 113.14 ? 25   ARG C NH1 1 
ATOM   3408 N NH2 . ARG C 1 44  ? 4.160   53.069 -68.940 1.00 107.04 ? 25   ARG C NH2 1 
ATOM   3409 N N   . PRO C 1 45  ? 0.608   46.324 -63.694 1.00 44.26  ? 26   PRO C N   1 
ATOM   3410 C CA  . PRO C 1 45  ? 0.517   45.511 -62.493 1.00 40.11  ? 26   PRO C CA  1 
ATOM   3411 C C   . PRO C 1 45  ? 1.772   45.491 -61.695 1.00 38.97  ? 26   PRO C C   1 
ATOM   3412 O O   . PRO C 1 45  ? 2.823   45.761 -62.211 1.00 40.81  ? 26   PRO C O   1 
ATOM   3413 C CB  . PRO C 1 45  ? 0.343   44.120 -63.031 1.00 36.68  ? 26   PRO C CB  1 
ATOM   3414 C CG  . PRO C 1 45  ? -0.326  44.284 -64.275 1.00 38.46  ? 26   PRO C CG  1 
ATOM   3415 C CD  . PRO C 1 45  ? 0.363   45.401 -64.882 1.00 42.16  ? 26   PRO C CD  1 
ATOM   3416 N N   . VAL C 1 46  ? 1.657   45.179 -60.418 1.00 31.09  ? 27   VAL C N   1 
ATOM   3417 C CA  . VAL C 1 46  ? 2.840   44.816 -59.667 1.00 23.52  ? 27   VAL C CA  1 
ATOM   3418 C C   . VAL C 1 46  ? 3.094   43.362 -60.022 1.00 28.01  ? 27   VAL C C   1 
ATOM   3419 O O   . VAL C 1 46  ? 2.194   42.514 -59.908 1.00 26.50  ? 27   VAL C O   1 
ATOM   3420 C CB  . VAL C 1 46  ? 2.585   44.935 -58.164 1.00 23.24  ? 27   VAL C CB  1 
ATOM   3421 C CG1 . VAL C 1 46  ? 3.813   44.500 -57.357 1.00 22.90  ? 27   VAL C CG1 1 
ATOM   3422 C CG2 . VAL C 1 46  ? 2.166   46.347 -57.809 1.00 27.43  ? 27   VAL C CG2 1 
ATOM   3423 N N   . ALA C 1 47  ? 4.299   43.054 -60.473 1.00 26.84  ? 28   ALA C N   1 
ATOM   3424 C CA  . ALA C 1 47  ? 4.590   41.659 -60.802 1.00 32.06  ? 28   ALA C CA  1 
ATOM   3425 C C   . ALA C 1 47  ? 5.058   40.908 -59.562 1.00 29.46  ? 28   ALA C C   1 
ATOM   3426 O O   . ALA C 1 47  ? 6.155   41.150 -59.053 1.00 30.85  ? 28   ALA C O   1 
ATOM   3427 C CB  . ALA C 1 47  ? 5.622   41.556 -61.910 1.00 35.73  ? 28   ALA C CB  1 
ATOM   3428 N N   . VAL C 1 48  ? 4.225   39.994 -59.083 1.00 23.19  ? 29   VAL C N   1 
ATOM   3429 C CA  . VAL C 1 48  ? 4.581   39.182 -57.931 1.00 25.53  ? 29   VAL C CA  1 
ATOM   3430 C C   . VAL C 1 48  ? 5.026   37.781 -58.392 1.00 27.20  ? 29   VAL C C   1 
ATOM   3431 O O   . VAL C 1 48  ? 4.334   37.132 -59.162 1.00 33.43  ? 29   VAL C O   1 
ATOM   3432 C CB  . VAL C 1 48  ? 3.379   39.058 -56.953 1.00 25.50  ? 29   VAL C CB  1 
ATOM   3433 C CG1 . VAL C 1 48  ? 3.766   38.265 -55.714 1.00 22.51  ? 29   VAL C CG1 1 
ATOM   3434 C CG2 . VAL C 1 48  ? 2.851   40.411 -56.562 1.00 20.52  ? 29   VAL C CG2 1 
ATOM   3435 N N   . SER C 1 49  ? 6.172   37.308 -57.919 1.00 28.19  ? 30   SER C N   1 
ATOM   3436 C CA  . SER C 1 49  ? 6.594   35.940 -58.197 1.00 22.36  ? 30   SER C CA  1 
ATOM   3437 C C   . SER C 1 49  ? 6.342   35.100 -56.969 1.00 28.75  ? 30   SER C C   1 
ATOM   3438 O O   . SER C 1 49  ? 6.617   35.532 -55.837 1.00 31.60  ? 30   SER C O   1 
ATOM   3439 C CB  . SER C 1 49  ? 8.077   35.880 -58.512 1.00 20.07  ? 30   SER C CB  1 
ATOM   3440 O OG  . SER C 1 49  ? 8.450   36.959 -59.331 1.00 37.88  ? 30   SER C OG  1 
ATOM   3441 N N   . VAL C 1 50  ? 5.842   33.891 -57.191 1.00 26.38  ? 31   VAL C N   1 
ATOM   3442 C CA  . VAL C 1 50  ? 5.523   32.988 -56.105 1.00 26.47  ? 31   VAL C CA  1 
ATOM   3443 C C   . VAL C 1 50  ? 6.182   31.647 -56.332 1.00 31.16  ? 31   VAL C C   1 
ATOM   3444 O O   . VAL C 1 50  ? 6.086   31.088 -57.415 1.00 44.70  ? 31   VAL C O   1 
ATOM   3445 C CB  . VAL C 1 50  ? 4.012   32.767 -55.985 1.00 26.44  ? 31   VAL C CB  1 
ATOM   3446 C CG1 . VAL C 1 50  ? 3.721   31.827 -54.833 1.00 35.30  ? 31   VAL C CG1 1 
ATOM   3447 C CG2 . VAL C 1 50  ? 3.300   34.094 -55.774 1.00 23.36  ? 31   VAL C CG2 1 
ATOM   3448 N N   . SER C 1 51  ? 6.837   31.120 -55.305 1.00 31.40  ? 32   SER C N   1 
ATOM   3449 C CA  . SER C 1 51  ? 7.452   29.804 -55.393 1.00 30.02  ? 32   SER C CA  1 
ATOM   3450 C C   . SER C 1 51  ? 7.297   29.039 -54.075 1.00 28.74  ? 32   SER C C   1 
ATOM   3451 O O   . SER C 1 51  ? 7.677   29.555 -53.023 1.00 35.38  ? 32   SER C O   1 
ATOM   3452 C CB  . SER C 1 51  ? 8.931   29.967 -55.735 1.00 35.32  ? 32   SER C CB  1 
ATOM   3453 O OG  . SER C 1 51  ? 9.565   28.708 -55.869 1.00 50.36  ? 32   SER C OG  1 
ATOM   3454 N N   . LEU C 1 52  ? 6.744   27.825 -54.122 1.00 25.80  ? 33   LEU C N   1 
ATOM   3455 C CA  . LEU C 1 52  ? 6.653   26.981 -52.920 1.00 26.22  ? 33   LEU C CA  1 
ATOM   3456 C C   . LEU C 1 52  ? 7.826   25.999 -52.828 1.00 31.40  ? 33   LEU C C   1 
ATOM   3457 O O   . LEU C 1 52  ? 8.134   25.301 -53.796 1.00 41.64  ? 33   LEU C O   1 
ATOM   3458 C CB  . LEU C 1 52  ? 5.335   26.200 -52.874 1.00 20.63  ? 33   LEU C CB  1 
ATOM   3459 C CG  . LEU C 1 52  ? 4.082   27.035 -53.101 1.00 23.38  ? 33   LEU C CG  1 
ATOM   3460 C CD1 . LEU C 1 52  ? 2.812   26.256 -52.789 1.00 20.72  ? 33   LEU C CD1 1 
ATOM   3461 C CD2 . LEU C 1 52  ? 4.130   28.318 -52.294 1.00 23.89  ? 33   LEU C CD2 1 
ATOM   3462 N N   . LYS C 1 53  ? 8.483   25.950 -51.671 1.00 27.68  ? 34   LYS C N   1 
ATOM   3463 C CA  . LYS C 1 53  ? 9.492   24.925 -51.407 1.00 27.01  ? 34   LYS C CA  1 
ATOM   3464 C C   . LYS C 1 53  ? 8.939   23.996 -50.347 1.00 31.37  ? 34   LYS C C   1 
ATOM   3465 O O   . LYS C 1 53  ? 8.766   24.408 -49.186 1.00 29.21  ? 34   LYS C O   1 
ATOM   3466 C CB  . LYS C 1 53  ? 10.784  25.541 -50.883 1.00 33.62  ? 34   LYS C CB  1 
ATOM   3467 C CG  . LYS C 1 53  ? 11.207  26.821 -51.578 1.00 40.19  ? 34   LYS C CG  1 
ATOM   3468 C CD  . LYS C 1 53  ? 11.771  26.555 -52.958 1.00 46.52  ? 34   LYS C CD  1 
ATOM   3469 C CE  . LYS C 1 53  ? 12.148  27.873 -53.638 1.00 60.79  ? 34   LYS C CE  1 
ATOM   3470 N NZ  . LYS C 1 53  ? 12.671  27.659 -55.027 1.00 70.12  ? 34   LYS C NZ  1 
ATOM   3471 N N   . PHE C 1 54  ? 8.657   22.749 -50.730 1.00 30.07  ? 35   PHE C N   1 
ATOM   3472 C CA  . PHE C 1 54  ? 8.053   21.820 -49.784 1.00 24.15  ? 35   PHE C CA  1 
ATOM   3473 C C   . PHE C 1 54  ? 9.029   21.326 -48.735 1.00 24.18  ? 35   PHE C C   1 
ATOM   3474 O O   . PHE C 1 54  ? 10.156  20.968 -49.045 1.00 27.24  ? 35   PHE C O   1 
ATOM   3475 C CB  . PHE C 1 54  ? 7.356   20.693 -50.514 1.00 23.17  ? 35   PHE C CB  1 
ATOM   3476 C CG  . PHE C 1 54  ? 6.215   21.170 -51.329 1.00 26.84  ? 35   PHE C CG  1 
ATOM   3477 C CD1 . PHE C 1 54  ? 4.965   21.373 -50.745 1.00 26.48  ? 35   PHE C CD1 1 
ATOM   3478 C CD2 . PHE C 1 54  ? 6.400   21.493 -52.666 1.00 31.06  ? 35   PHE C CD2 1 
ATOM   3479 C CE1 . PHE C 1 54  ? 3.903   21.857 -51.502 1.00 28.82  ? 35   PHE C CE1 1 
ATOM   3480 C CE2 . PHE C 1 54  ? 5.348   21.978 -53.440 1.00 31.08  ? 35   PHE C CE2 1 
ATOM   3481 C CZ  . PHE C 1 54  ? 4.099   22.162 -52.862 1.00 32.97  ? 35   PHE C CZ  1 
ATOM   3482 N N   . ILE C 1 55  ? 8.593   21.356 -47.481 1.00 21.32  ? 36   ILE C N   1 
ATOM   3483 C CA  . ILE C 1 55  ? 9.447   20.945 -46.386 1.00 21.84  ? 36   ILE C CA  1 
ATOM   3484 C C   . ILE C 1 55  ? 8.973   19.632 -45.769 1.00 23.77  ? 36   ILE C C   1 
ATOM   3485 O O   . ILE C 1 55  ? 9.796   18.790 -45.403 1.00 27.67  ? 36   ILE C O   1 
ATOM   3486 C CB  . ILE C 1 55  ? 9.542   22.033 -45.299 1.00 22.60  ? 36   ILE C CB  1 
ATOM   3487 C CG1 . ILE C 1 55  ? 9.829   23.404 -45.925 1.00 26.48  ? 36   ILE C CG1 1 
ATOM   3488 C CG2 . ILE C 1 55  ? 10.606  21.662 -44.292 1.00 21.32  ? 36   ILE C CG2 1 
ATOM   3489 C CD1 . ILE C 1 55  ? 11.102  23.451 -46.799 1.00 26.48  ? 36   ILE C CD1 1 
ATOM   3490 N N   . ASN C 1 56  ? 7.654   19.458 -45.656 1.00 18.24  ? 37   ASN C N   1 
ATOM   3491 C CA  . ASN C 1 56  ? 7.101   18.252 -45.051 1.00 18.81  ? 37   ASN C CA  1 
ATOM   3492 C C   . ASN C 1 56  ? 5.682   17.938 -45.491 1.00 19.93  ? 37   ASN C C   1 
ATOM   3493 O O   . ASN C 1 56  ? 4.947   18.827 -45.891 1.00 22.26  ? 37   ASN C O   1 
ATOM   3494 C CB  . ASN C 1 56  ? 7.138   18.376 -43.525 1.00 26.52  ? 37   ASN C CB  1 
ATOM   3495 C CG  . ASN C 1 56  ? 7.572   17.072 -42.833 1.00 31.89  ? 37   ASN C CG  1 
ATOM   3496 O OD1 . ASN C 1 56  ? 7.083   15.978 -43.151 1.00 23.85  ? 37   ASN C OD1 1 
ATOM   3497 N ND2 . ASN C 1 56  ? 8.498   17.194 -41.878 1.00 34.87  ? 37   ASN C ND2 1 
ATOM   3498 N N   . ILE C 1 57  ? 5.300   16.665 -45.414 1.00 28.52  ? 38   ILE C N   1 
ATOM   3499 C CA  . ILE C 1 57  ? 3.909   16.245 -45.611 1.00 22.23  ? 38   ILE C CA  1 
ATOM   3500 C C   . ILE C 1 57  ? 3.489   15.443 -44.390 1.00 21.48  ? 38   ILE C C   1 
ATOM   3501 O O   . ILE C 1 57  ? 4.153   14.486 -44.024 1.00 28.39  ? 38   ILE C O   1 
ATOM   3502 C CB  . ILE C 1 57  ? 3.739   15.455 -46.898 1.00 16.48  ? 38   ILE C CB  1 
ATOM   3503 C CG1 . ILE C 1 57  ? 4.103   16.361 -48.079 1.00 16.01  ? 38   ILE C CG1 1 
ATOM   3504 C CG2 . ILE C 1 57  ? 2.313   14.968 -47.014 1.00 20.70  ? 38   ILE C CG2 1 
ATOM   3505 C CD1 . ILE C 1 57  ? 4.073   15.717 -49.419 1.00 18.42  ? 38   ILE C CD1 1 
ATOM   3506 N N   . LEU C 1 58  ? 2.414   15.855 -43.729 1.00 27.14  ? 39   LEU C N   1 
ATOM   3507 C CA  . LEU C 1 58  ? 2.236   15.458 -42.332 1.00 34.54  ? 39   LEU C CA  1 
ATOM   3508 C C   . LEU C 1 58  ? 1.072   14.545 -42.053 1.00 42.18  ? 39   LEU C C   1 
ATOM   3509 O O   . LEU C 1 58  ? 1.226   13.539 -41.365 1.00 56.51  ? 39   LEU C O   1 
ATOM   3510 C CB  . LEU C 1 58  ? 2.112   16.680 -41.424 1.00 33.04  ? 39   LEU C CB  1 
ATOM   3511 C CG  . LEU C 1 58  ? 3.393   17.458 -41.220 1.00 32.44  ? 39   LEU C CG  1 
ATOM   3512 C CD1 . LEU C 1 58  ? 3.117   18.625 -40.319 1.00 38.58  ? 39   LEU C CD1 1 
ATOM   3513 C CD2 . LEU C 1 58  ? 4.442   16.555 -40.621 1.00 34.50  ? 39   LEU C CD2 1 
ATOM   3514 N N   . GLU C 1 59  ? -0.107  14.908 -42.530 1.00 35.90  ? 40   GLU C N   1 
ATOM   3515 C CA  . GLU C 1 59  ? -1.269  14.108 -42.197 1.00 32.73  ? 40   GLU C CA  1 
ATOM   3516 C C   . GLU C 1 59  ? -2.133  13.943 -43.396 1.00 40.29  ? 40   GLU C C   1 
ATOM   3517 O O   . GLU C 1 59  ? -2.852  14.856 -43.792 1.00 53.30  ? 40   GLU C O   1 
ATOM   3518 C CB  . GLU C 1 59  ? -2.057  14.721 -41.056 1.00 35.94  ? 40   GLU C CB  1 
ATOM   3519 C CG  . GLU C 1 59  ? -1.926  13.931 -39.776 1.00 51.80  ? 40   GLU C CG  1 
ATOM   3520 C CD  . GLU C 1 59  ? -1.988  14.800 -38.537 1.00 72.13  ? 40   GLU C CD  1 
ATOM   3521 O OE1 . GLU C 1 59  ? -2.054  16.047 -38.682 1.00 72.87  ? 40   GLU C OE1 1 
ATOM   3522 O OE2 . GLU C 1 59  ? -1.970  14.229 -37.418 1.00 75.15  ? 40   GLU C OE2 1 
ATOM   3523 N N   . VAL C 1 60  ? -2.054  12.767 -43.991 1.00 36.96  ? 41   VAL C N   1 
ATOM   3524 C CA  . VAL C 1 60  ? -2.815  12.511 -45.189 1.00 29.16  ? 41   VAL C CA  1 
ATOM   3525 C C   . VAL C 1 60  ? -4.031  11.683 -44.834 1.00 26.65  ? 41   VAL C C   1 
ATOM   3526 O O   . VAL C 1 60  ? -3.960  10.785 -44.002 1.00 29.56  ? 41   VAL C O   1 
ATOM   3527 C CB  . VAL C 1 60  ? -1.931  11.826 -46.223 1.00 31.84  ? 41   VAL C CB  1 
ATOM   3528 C CG1 . VAL C 1 60  ? -2.736  11.405 -47.395 1.00 32.73  ? 41   VAL C CG1 1 
ATOM   3529 C CG2 . VAL C 1 60  ? -0.833  12.784 -46.664 1.00 36.69  ? 41   VAL C CG2 1 
ATOM   3530 N N   . ASN C 1 61  ? -5.164  12.030 -45.421 1.00 30.77  ? 42   ASN C N   1 
ATOM   3531 C CA  . ASN C 1 61  ? -6.376  11.238 -45.261 1.00 32.62  ? 42   ASN C CA  1 
ATOM   3532 C C   . ASN C 1 61  ? -7.008  10.997 -46.627 1.00 38.61  ? 42   ASN C C   1 
ATOM   3533 O O   . ASN C 1 61  ? -7.605  11.913 -47.211 1.00 38.78  ? 42   ASN C O   1 
ATOM   3534 C CB  . ASN C 1 61  ? -7.357  11.942 -44.315 1.00 33.88  ? 42   ASN C CB  1 
ATOM   3535 C CG  . ASN C 1 61  ? -8.573  11.071 -43.955 1.00 36.72  ? 42   ASN C CG  1 
ATOM   3536 O OD1 . ASN C 1 61  ? -9.097  10.324 -44.792 1.00 40.23  ? 42   ASN C OD1 1 
ATOM   3537 N ND2 . ASN C 1 61  ? -9.026  11.172 -42.704 1.00 28.63  ? 42   ASN C ND2 1 
ATOM   3538 N N   . GLU C 1 62  ? -6.869  9.769  -47.133 1.00 39.80  ? 43   GLU C N   1 
ATOM   3539 C CA  . GLU C 1 62  ? -7.368  9.424  -48.469 1.00 37.46  ? 43   GLU C CA  1 
ATOM   3540 C C   . GLU C 1 62  ? -8.902  9.389  -48.463 1.00 35.42  ? 43   GLU C C   1 
ATOM   3541 O O   . GLU C 1 62  ? -9.535  9.671  -49.482 1.00 37.04  ? 43   GLU C O   1 
ATOM   3542 C CB  . GLU C 1 62  ? -6.763  8.091  -48.961 1.00 44.74  ? 43   GLU C CB  1 
ATOM   3543 C CG  . GLU C 1 62  ? -6.806  7.867  -50.492 1.00 49.76  ? 43   GLU C CG  1 
ATOM   3544 C CD  . GLU C 1 62  ? -6.131  6.549  -50.955 1.00 57.45  ? 43   GLU C CD  1 
ATOM   3545 O OE1 . GLU C 1 62  ? -5.421  5.903  -50.138 1.00 53.44  ? 43   GLU C OE1 1 
ATOM   3546 O OE2 . GLU C 1 62  ? -6.314  6.169  -52.143 1.00 50.00  ? 43   GLU C OE2 1 
ATOM   3547 N N   . ILE C 1 63  ? -9.486  9.083  -47.304 1.00 31.69  ? 44   ILE C N   1 
ATOM   3548 C CA  . ILE C 1 63  ? -10.941 9.015  -47.174 1.00 36.36  ? 44   ILE C CA  1 
ATOM   3549 C C   . ILE C 1 63  ? -11.583 10.382 -47.366 1.00 36.19  ? 44   ILE C C   1 
ATOM   3550 O O   . ILE C 1 63  ? -12.574 10.505 -48.076 1.00 40.79  ? 44   ILE C O   1 
ATOM   3551 C CB  . ILE C 1 63  ? -11.422 8.477  -45.788 1.00 39.28  ? 44   ILE C CB  1 
ATOM   3552 C CG1 . ILE C 1 63  ? -10.828 7.097  -45.462 1.00 48.40  ? 44   ILE C CG1 1 
ATOM   3553 C CG2 . ILE C 1 63  ? -12.942 8.449  -45.733 1.00 36.47  ? 44   ILE C CG2 1 
ATOM   3554 C CD1 . ILE C 1 63  ? -11.262 5.974  -46.395 1.00 37.97  ? 44   ILE C CD1 1 
ATOM   3555 N N   . THR C 1 64  ? -11.031 11.405 -46.715 1.00 38.38  ? 45   THR C N   1 
ATOM   3556 C CA  . THR C 1 64  ? -11.647 12.740 -46.718 1.00 37.61  ? 45   THR C CA  1 
ATOM   3557 C C   . THR C 1 64  ? -10.973 13.680 -47.694 1.00 31.22  ? 45   THR C C   1 
ATOM   3558 O O   . THR C 1 64  ? -11.395 14.818 -47.843 1.00 30.55  ? 45   THR C O   1 
ATOM   3559 C CB  . THR C 1 64  ? -11.575 13.433 -45.349 1.00 31.55  ? 45   THR C CB  1 
ATOM   3560 O OG1 . THR C 1 64  ? -10.211 13.763 -45.063 1.00 37.74  ? 45   THR C OG1 1 
ATOM   3561 C CG2 . THR C 1 64  ? -12.127 12.556 -44.253 1.00 25.40  ? 45   THR C CG2 1 
ATOM   3562 N N   . ASN C 1 65  ? -9.914  13.208 -48.334 1.00 31.89  ? 46   ASN C N   1 
ATOM   3563 C CA  . ASN C 1 65  ? -9.183  14.015 -49.304 1.00 33.63  ? 46   ASN C CA  1 
ATOM   3564 C C   . ASN C 1 65  ? -8.636  15.314 -48.725 1.00 37.38  ? 46   ASN C C   1 
ATOM   3565 O O   . ASN C 1 65  ? -8.935  16.402 -49.231 1.00 36.58  ? 46   ASN C O   1 
ATOM   3566 C CB  . ASN C 1 65  ? -10.041 14.320 -50.542 1.00 38.94  ? 46   ASN C CB  1 
ATOM   3567 C CG  . ASN C 1 65  ? -9.887  13.286 -51.638 1.00 33.46  ? 46   ASN C CG  1 
ATOM   3568 O OD1 . ASN C 1 65  ? -8.920  12.511 -51.668 1.00 35.78  ? 46   ASN C OD1 1 
ATOM   3569 N ND2 . ASN C 1 65  ? -10.845 13.277 -52.556 1.00 30.18  ? 46   ASN C ND2 1 
ATOM   3570 N N   . GLU C 1 66  ? -7.830  15.181 -47.669 1.00 42.69  ? 47   GLU C N   1 
ATOM   3571 C CA  . GLU C 1 66  ? -7.200  16.315 -46.987 1.00 32.73  ? 47   GLU C CA  1 
ATOM   3572 C C   . GLU C 1 66  ? -5.735  16.038 -46.701 1.00 35.89  ? 47   GLU C C   1 
ATOM   3573 O O   . GLU C 1 66  ? -5.379  14.934 -46.287 1.00 40.02  ? 47   GLU C O   1 
ATOM   3574 C CB  . GLU C 1 66  ? -7.924  16.599 -45.677 1.00 30.18  ? 47   GLU C CB  1 
ATOM   3575 C CG  . GLU C 1 66  ? -9.360  16.991 -45.877 1.00 43.13  ? 47   GLU C CG  1 
ATOM   3576 C CD  . GLU C 1 66  ? -10.104 17.227 -44.571 1.00 60.36  ? 47   GLU C CD  1 
ATOM   3577 O OE1 . GLU C 1 66  ? -9.437  17.288 -43.507 1.00 56.79  ? 47   GLU C OE1 1 
ATOM   3578 O OE2 . GLU C 1 66  ? -11.359 17.350 -44.622 1.00 63.12  ? 47   GLU C OE2 1 
ATOM   3579 N N   . VAL C 1 67  ? -4.882  17.037 -46.911 1.00 38.57  ? 48   VAL C N   1 
ATOM   3580 C CA  . VAL C 1 67  ? -3.463  16.894 -46.573 1.00 38.53  ? 48   VAL C CA  1 
ATOM   3581 C C   . VAL C 1 67  ? -2.979  18.032 -45.690 1.00 38.49  ? 48   VAL C C   1 
ATOM   3582 O O   . VAL C 1 67  ? -3.555  19.125 -45.693 1.00 37.02  ? 48   VAL C O   1 
ATOM   3583 C CB  . VAL C 1 67  ? -2.579  16.829 -47.828 1.00 33.76  ? 48   VAL C CB  1 
ATOM   3584 C CG1 . VAL C 1 67  ? -3.001  15.689 -48.704 1.00 35.99  ? 48   VAL C CG1 1 
ATOM   3585 C CG2 . VAL C 1 67  ? -2.682  18.133 -48.601 1.00 38.01  ? 48   VAL C CG2 1 
ATOM   3586 N N   . ASP C 1 68  ? -1.905  17.766 -44.952 1.00 39.33  ? 49   ASP C N   1 
ATOM   3587 C CA  . ASP C 1 68  ? -1.249  18.774 -44.115 1.00 33.93  ? 49   ASP C CA  1 
ATOM   3588 C C   . ASP C 1 68  ? 0.149   19.057 -44.629 1.00 27.55  ? 49   ASP C C   1 
ATOM   3589 O O   . ASP C 1 68  ? 1.034   18.197 -44.567 1.00 29.25  ? 49   ASP C O   1 
ATOM   3590 C CB  . ASP C 1 68  ? -1.115  18.244 -42.702 1.00 39.05  ? 49   ASP C CB  1 
ATOM   3591 C CG  . ASP C 1 68  ? -1.651  19.188 -41.699 1.00 42.94  ? 49   ASP C CG  1 
ATOM   3592 O OD1 . ASP C 1 68  ? -2.511  20.004 -42.101 1.00 54.62  ? 49   ASP C OD1 1 
ATOM   3593 O OD2 . ASP C 1 68  ? -1.228  19.117 -40.522 1.00 50.09  ? 49   ASP C OD2 1 
ATOM   3594 N N   . VAL C 1 69  ? 0.370   20.257 -45.129 1.00 24.47  ? 50   VAL C N   1 
ATOM   3595 C CA  . VAL C 1 69  ? 1.659   20.550 -45.734 1.00 22.77  ? 50   VAL C CA  1 
ATOM   3596 C C   . VAL C 1 69  ? 2.437   21.614 -44.963 1.00 19.97  ? 50   VAL C C   1 
ATOM   3597 O O   . VAL C 1 69  ? 1.844   22.527 -44.401 1.00 23.08  ? 50   VAL C O   1 
ATOM   3598 C CB  . VAL C 1 69  ? 1.468   20.955 -47.201 1.00 22.64  ? 50   VAL C CB  1 
ATOM   3599 C CG1 . VAL C 1 69  ? 2.811   21.167 -47.889 1.00 24.25  ? 50   VAL C CG1 1 
ATOM   3600 C CG2 . VAL C 1 69  ? 0.696   19.866 -47.916 1.00 29.71  ? 50   VAL C CG2 1 
ATOM   3601 N N   . VAL C 1 70  ? 3.760   21.460 -44.904 1.00 20.44  ? 51   VAL C N   1 
ATOM   3602 C CA  . VAL C 1 70  ? 4.664   22.532 -44.477 1.00 17.76  ? 51   VAL C CA  1 
ATOM   3603 C C   . VAL C 1 70  ? 5.543   22.926 -45.654 1.00 18.41  ? 51   VAL C C   1 
ATOM   3604 O O   . VAL C 1 70  ? 6.237   22.089 -46.229 1.00 20.32  ? 51   VAL C O   1 
ATOM   3605 C CB  . VAL C 1 70  ? 5.574   22.122 -43.316 1.00 14.73  ? 51   VAL C CB  1 
ATOM   3606 C CG1 . VAL C 1 70  ? 6.604   23.197 -43.095 1.00 13.69  ? 51   VAL C CG1 1 
ATOM   3607 C CG2 . VAL C 1 70  ? 4.766   21.884 -42.045 1.00 16.01  ? 51   VAL C CG2 1 
ATOM   3608 N N   . PHE C 1 71  ? 5.515   24.205 -46.007 1.00 21.05  ? 52   PHE C N   1 
ATOM   3609 C CA  . PHE C 1 71  ? 6.258   24.709 -47.162 1.00 20.99  ? 52   PHE C CA  1 
ATOM   3610 C C   . PHE C 1 71  ? 6.739   26.140 -46.936 1.00 22.11  ? 52   PHE C C   1 
ATOM   3611 O O   . PHE C 1 71  ? 6.153   26.871 -46.135 1.00 25.58  ? 52   PHE C O   1 
ATOM   3612 C CB  . PHE C 1 71  ? 5.355   24.673 -48.393 1.00 24.28  ? 52   PHE C CB  1 
ATOM   3613 C CG  . PHE C 1 71  ? 4.068   25.454 -48.229 1.00 26.69  ? 52   PHE C CG  1 
ATOM   3614 C CD1 . PHE C 1 71  ? 2.969   24.886 -47.587 1.00 22.98  ? 52   PHE C CD1 1 
ATOM   3615 C CD2 . PHE C 1 71  ? 3.963   26.760 -48.713 1.00 24.49  ? 52   PHE C CD2 1 
ATOM   3616 C CE1 . PHE C 1 71  ? 1.788   25.601 -47.438 1.00 28.49  ? 52   PHE C CE1 1 
ATOM   3617 C CE2 . PHE C 1 71  ? 2.794   27.489 -48.561 1.00 22.84  ? 52   PHE C CE2 1 
ATOM   3618 C CZ  . PHE C 1 71  ? 1.702   26.911 -47.927 1.00 30.50  ? 52   PHE C CZ  1 
ATOM   3619 N N   . TRP C 1 72  ? 7.799   26.542 -47.635 1.00 21.87  ? 53   TRP C N   1 
ATOM   3620 C CA  . TRP C 1 72  ? 8.194   27.956 -47.659 1.00 21.69  ? 53   TRP C CA  1 
ATOM   3621 C C   . TRP C 1 72  ? 7.451   28.599 -48.801 1.00 22.54  ? 53   TRP C C   1 
ATOM   3622 O O   . TRP C 1 72  ? 7.412   28.047 -49.895 1.00 20.44  ? 53   TRP C O   1 
ATOM   3623 C CB  . TRP C 1 72  ? 9.692   28.137 -47.910 1.00 22.16  ? 53   TRP C CB  1 
ATOM   3624 C CG  . TRP C 1 72  ? 10.589  27.545 -46.862 1.00 21.21  ? 53   TRP C CG  1 
ATOM   3625 C CD1 . TRP C 1 72  ? 10.209  26.889 -45.726 1.00 19.18  ? 53   TRP C CD1 1 
ATOM   3626 C CD2 . TRP C 1 72  ? 12.025  27.546 -46.868 1.00 19.20  ? 53   TRP C CD2 1 
ATOM   3627 N NE1 . TRP C 1 72  ? 11.316  26.489 -45.021 1.00 15.59  ? 53   TRP C NE1 1 
ATOM   3628 C CE2 . TRP C 1 72  ? 12.442  26.880 -45.694 1.00 16.36  ? 53   TRP C CE2 1 
ATOM   3629 C CE3 . TRP C 1 72  ? 12.997  28.058 -47.745 1.00 19.62  ? 53   TRP C CE3 1 
ATOM   3630 C CZ2 . TRP C 1 72  ? 13.791  26.704 -45.377 1.00 16.99  ? 53   TRP C CZ2 1 
ATOM   3631 C CZ3 . TRP C 1 72  ? 14.337  27.893 -47.427 1.00 19.94  ? 53   TRP C CZ3 1 
ATOM   3632 C CH2 . TRP C 1 72  ? 14.721  27.212 -46.258 1.00 23.15  ? 53   TRP C CH2 1 
ATOM   3633 N N   . GLN C 1 73  ? 6.859   29.763 -48.554 1.00 25.72  ? 54   GLN C N   1 
ATOM   3634 C CA  . GLN C 1 73  ? 6.150   30.480 -49.609 1.00 24.04  ? 54   GLN C CA  1 
ATOM   3635 C C   . GLN C 1 73  ? 6.960   31.684 -50.057 1.00 25.71  ? 54   GLN C C   1 
ATOM   3636 O O   . GLN C 1 73  ? 6.757   32.806 -49.578 1.00 24.63  ? 54   GLN C O   1 
ATOM   3637 C CB  . GLN C 1 73  ? 4.776   30.917 -49.119 1.00 27.63  ? 54   GLN C CB  1 
ATOM   3638 C CG  . GLN C 1 73  ? 3.962   31.637 -50.164 1.00 26.36  ? 54   GLN C CG  1 
ATOM   3639 C CD  . GLN C 1 73  ? 2.551   31.906 -49.710 1.00 29.16  ? 54   GLN C CD  1 
ATOM   3640 O OE1 . GLN C 1 73  ? 1.814   30.989 -49.341 1.00 26.46  ? 54   GLN C OE1 1 
ATOM   3641 N NE2 . GLN C 1 73  ? 2.165   33.179 -49.729 1.00 46.34  ? 54   GLN C NE2 1 
ATOM   3642 N N   . GLN C 1 74  ? 7.891   31.452 -50.978 1.00 25.51  ? 55   GLN C N   1 
ATOM   3643 C CA  . GLN C 1 74  ? 8.804   32.509 -51.394 1.00 26.47  ? 55   GLN C CA  1 
ATOM   3644 C C   . GLN C 1 74  ? 8.118   33.516 -52.324 1.00 28.93  ? 55   GLN C C   1 
ATOM   3645 O O   . GLN C 1 74  ? 7.722   33.181 -53.439 1.00 29.28  ? 55   GLN C O   1 
ATOM   3646 C CB  . GLN C 1 74  ? 10.020  31.907 -52.071 1.00 28.90  ? 55   GLN C CB  1 
ATOM   3647 C CG  . GLN C 1 74  ? 10.969  32.956 -52.621 1.00 43.25  ? 55   GLN C CG  1 
ATOM   3648 C CD  . GLN C 1 74  ? 12.215  32.344 -53.248 1.00 48.93  ? 55   GLN C CD  1 
ATOM   3649 O OE1 . GLN C 1 74  ? 12.745  31.338 -52.764 1.00 58.52  ? 55   GLN C OE1 1 
ATOM   3650 N NE2 . GLN C 1 74  ? 12.686  32.950 -54.329 1.00 46.48  ? 55   GLN C NE2 1 
ATOM   3651 N N   . THR C 1 75  ? 7.981   34.753 -51.858 1.00 27.12  ? 56   THR C N   1 
ATOM   3652 C CA  . THR C 1 75  ? 7.202   35.771 -52.569 1.00 22.48  ? 56   THR C CA  1 
ATOM   3653 C C   . THR C 1 75  ? 8.093   36.975 -52.867 1.00 26.11  ? 56   THR C C   1 
ATOM   3654 O O   . THR C 1 75  ? 8.790   37.478 -51.970 1.00 24.20  ? 56   THR C O   1 
ATOM   3655 C CB  . THR C 1 75  ? 6.005   36.252 -51.719 1.00 20.21  ? 56   THR C CB  1 
ATOM   3656 O OG1 . THR C 1 75  ? 5.304   35.130 -51.161 1.00 26.85  ? 56   THR C OG1 1 
ATOM   3657 C CG2 . THR C 1 75  ? 5.049   37.048 -52.552 1.00 20.98  ? 56   THR C CG2 1 
ATOM   3658 N N   . THR C 1 76  ? 8.069   37.444 -54.115 1.00 22.23  ? 57   THR C N   1 
ATOM   3659 C CA  . THR C 1 76  ? 8.997   38.496 -54.543 1.00 22.37  ? 57   THR C CA  1 
ATOM   3660 C C   . THR C 1 76  ? 8.335   39.579 -55.410 1.00 24.75  ? 57   THR C C   1 
ATOM   3661 O O   . THR C 1 76  ? 7.588   39.273 -56.331 1.00 25.39  ? 57   THR C O   1 
ATOM   3662 C CB  . THR C 1 76  ? 10.229  37.875 -55.258 1.00 25.11  ? 57   THR C CB  1 
ATOM   3663 O OG1 . THR C 1 76  ? 11.015  37.150 -54.299 1.00 27.89  ? 57   THR C OG1 1 
ATOM   3664 C CG2 . THR C 1 76  ? 11.118  38.953 -55.907 1.00 37.11  ? 57   THR C CG2 1 
ATOM   3665 N N   . TRP C 1 77  ? 8.601   40.846 -55.109 1.00 20.98  ? 58   TRP C N   1 
ATOM   3666 C CA  . TRP C 1 77  ? 8.039   41.921 -55.910 1.00 22.70  ? 58   TRP C CA  1 
ATOM   3667 C C   . TRP C 1 77  ? 8.876   43.171 -55.794 1.00 22.74  ? 58   TRP C C   1 
ATOM   3668 O O   . TRP C 1 77  ? 9.847   43.216 -55.049 1.00 25.97  ? 58   TRP C O   1 
ATOM   3669 C CB  . TRP C 1 77  ? 6.602   42.228 -55.482 1.00 22.48  ? 58   TRP C CB  1 
ATOM   3670 C CG  . TRP C 1 77  ? 6.536   42.846 -54.125 1.00 22.36  ? 58   TRP C CG  1 
ATOM   3671 C CD1 . TRP C 1 77  ? 6.501   44.178 -53.831 1.00 24.37  ? 58   TRP C CD1 1 
ATOM   3672 C CD2 . TRP C 1 77  ? 6.524   42.158 -52.874 1.00 18.19  ? 58   TRP C CD2 1 
ATOM   3673 N NE1 . TRP C 1 77  ? 6.459   44.361 -52.475 1.00 22.04  ? 58   TRP C NE1 1 
ATOM   3674 C CE2 . TRP C 1 77  ? 6.468   43.135 -51.860 1.00 18.77  ? 58   TRP C CE2 1 
ATOM   3675 C CE3 . TRP C 1 77  ? 6.536   40.811 -52.514 1.00 19.85  ? 58   TRP C CE3 1 
ATOM   3676 C CZ2 . TRP C 1 77  ? 6.434   42.810 -50.498 1.00 16.90  ? 58   TRP C CZ2 1 
ATOM   3677 C CZ3 . TRP C 1 77  ? 6.499   40.486 -51.157 1.00 27.14  ? 58   TRP C CZ3 1 
ATOM   3678 C CH2 . TRP C 1 77  ? 6.454   41.490 -50.162 1.00 18.45  ? 58   TRP C CH2 1 
ATOM   3679 N N   . SER C 1 78  ? 8.478   44.207 -56.516 1.00 26.33  ? 59   SER C N   1 
ATOM   3680 C CA  . SER C 1 78  ? 9.240   45.456 -56.506 1.00 32.54  ? 59   SER C CA  1 
ATOM   3681 C C   . SER C 1 78  ? 8.452   46.659 -55.964 1.00 26.77  ? 59   SER C C   1 
ATOM   3682 O O   . SER C 1 78  ? 7.291   46.874 -56.321 1.00 33.04  ? 59   SER C O   1 
ATOM   3683 C CB  . SER C 1 78  ? 9.776   45.746 -57.904 1.00 37.84  ? 59   SER C CB  1 
ATOM   3684 O OG  . SER C 1 78  ? 10.503  46.953 -57.914 1.00 47.37  ? 59   SER C OG  1 
ATOM   3685 N N   . ASP C 1 79  ? 9.091   47.433 -55.093 1.00 25.26  ? 60   ASP C N   1 
ATOM   3686 C CA  . ASP C 1 79  ? 8.481   48.631 -54.515 1.00 29.07  ? 60   ASP C CA  1 
ATOM   3687 C C   . ASP C 1 79  ? 9.491   49.781 -54.461 1.00 31.17  ? 60   ASP C C   1 
ATOM   3688 O O   . ASP C 1 79  ? 10.247  49.892 -53.494 1.00 29.63  ? 60   ASP C O   1 
ATOM   3689 C CB  . ASP C 1 79  ? 7.956   48.336 -53.102 1.00 35.89  ? 60   ASP C CB  1 
ATOM   3690 C CG  . ASP C 1 79  ? 7.004   49.434 -52.565 1.00 40.08  ? 60   ASP C CG  1 
ATOM   3691 O OD1 . ASP C 1 79  ? 7.103   50.615 -52.997 1.00 27.56  ? 60   ASP C OD1 1 
ATOM   3692 O OD2 . ASP C 1 79  ? 6.147   49.105 -51.702 1.00 36.09  ? 60   ASP C OD2 1 
ATOM   3693 N N   . ARG C 1 80  ? 9.476   50.638 -55.488 1.00 32.09  ? 61   ARG C N   1 
ATOM   3694 C CA  . ARG C 1 80  ? 10.451  51.733 -55.639 1.00 38.39  ? 61   ARG C CA  1 
ATOM   3695 C C   . ARG C 1 80  ? 10.393  52.768 -54.501 1.00 36.01  ? 61   ARG C C   1 
ATOM   3696 O O   . ARG C 1 80  ? 11.369  53.470 -54.227 1.00 39.42  ? 61   ARG C O   1 
ATOM   3697 C CB  . ARG C 1 80  ? 10.296  52.441 -57.003 1.00 43.67  ? 61   ARG C CB  1 
ATOM   3698 C CG  . ARG C 1 80  ? 10.237  51.505 -58.215 1.00 66.00  ? 61   ARG C CG  1 
ATOM   3699 C CD  . ARG C 1 80  ? 11.601  50.943 -58.654 1.00 62.31  ? 61   ARG C CD  1 
ATOM   3700 N NE  . ARG C 1 80  ? 11.492  50.244 -59.943 1.00 73.61  ? 61   ARG C NE  1 
ATOM   3701 C CZ  . ARG C 1 80  ? 11.896  48.992 -60.177 1.00 83.93  ? 61   ARG C CZ  1 
ATOM   3702 N NH1 . ARG C 1 80  ? 12.465  48.273 -59.212 1.00 84.21  ? 61   ARG C NH1 1 
ATOM   3703 N NH2 . ARG C 1 80  ? 11.740  48.459 -61.387 1.00 75.64  ? 61   ARG C NH2 1 
ATOM   3704 N N   . THR C 1 81  ? 9.244   52.860 -53.848 1.00 31.05  ? 62   THR C N   1 
ATOM   3705 C CA  . THR C 1 81  ? 9.081   53.694 -52.659 1.00 29.76  ? 62   THR C CA  1 
ATOM   3706 C C   . THR C 1 81  ? 10.138  53.393 -51.582 1.00 29.88  ? 62   THR C C   1 
ATOM   3707 O O   . THR C 1 81  ? 10.498  54.261 -50.800 1.00 28.24  ? 62   THR C O   1 
ATOM   3708 C CB  . THR C 1 81  ? 7.658   53.503 -52.072 1.00 36.88  ? 62   THR C CB  1 
ATOM   3709 O OG1 . THR C 1 81  ? 6.684   53.816 -53.077 1.00 41.54  ? 62   THR C OG1 1 
ATOM   3710 C CG2 . THR C 1 81  ? 7.406   54.386 -50.853 1.00 38.58  ? 62   THR C CG2 1 
ATOM   3711 N N   . LEU C 1 82  ? 10.648  52.166 -51.552 1.00 28.87  ? 63   LEU C N   1 
ATOM   3712 C CA  . LEU C 1 82  ? 11.575  51.760 -50.504 1.00 23.85  ? 63   LEU C CA  1 
ATOM   3713 C C   . LEU C 1 82  ? 13.034  51.986 -50.874 1.00 29.20  ? 63   LEU C C   1 
ATOM   3714 O O   . LEU C 1 82  ? 13.928  51.780 -50.048 1.00 31.11  ? 63   LEU C O   1 
ATOM   3715 C CB  . LEU C 1 82  ? 11.373  50.283 -50.175 1.00 24.57  ? 63   LEU C CB  1 
ATOM   3716 C CG  . LEU C 1 82  ? 9.953   49.854 -49.825 1.00 20.70  ? 63   LEU C CG  1 
ATOM   3717 C CD1 . LEU C 1 82  ? 9.854   48.364 -49.884 1.00 17.59  ? 63   LEU C CD1 1 
ATOM   3718 C CD2 . LEU C 1 82  ? 9.606   50.346 -48.444 1.00 24.14  ? 63   LEU C CD2 1 
ATOM   3719 N N   . ALA C 1 83  ? 13.288  52.404 -52.108 1.00 28.09  ? 64   ALA C N   1 
ATOM   3720 C CA  . ALA C 1 83  ? 14.662  52.440 -52.609 1.00 28.58  ? 64   ALA C CA  1 
ATOM   3721 C C   . ALA C 1 83  ? 15.498  53.510 -51.914 1.00 30.28  ? 64   ALA C C   1 
ATOM   3722 O O   . ALA C 1 83  ? 14.950  54.503 -51.413 1.00 30.32  ? 64   ALA C O   1 
ATOM   3723 C CB  . ALA C 1 83  ? 14.678  52.634 -54.119 1.00 25.95  ? 64   ALA C CB  1 
ATOM   3724 N N   . TRP C 1 84  ? 16.817  53.295 -51.878 1.00 27.49  ? 65   TRP C N   1 
ATOM   3725 C CA  . TRP C 1 84  ? 17.763  54.308 -51.384 1.00 35.74  ? 65   TRP C CA  1 
ATOM   3726 C C   . TRP C 1 84  ? 19.093  54.271 -52.144 1.00 37.06  ? 65   TRP C C   1 
ATOM   3727 O O   . TRP C 1 84  ? 19.381  53.287 -52.837 1.00 40.94  ? 65   TRP C O   1 
ATOM   3728 C CB  . TRP C 1 84  ? 17.997  54.150 -49.875 1.00 28.02  ? 65   TRP C CB  1 
ATOM   3729 C CG  . TRP C 1 84  ? 18.751  52.919 -49.482 1.00 29.49  ? 65   TRP C CG  1 
ATOM   3730 C CD1 . TRP C 1 84  ? 20.106  52.796 -49.329 1.00 33.25  ? 65   TRP C CD1 1 
ATOM   3731 C CD2 . TRP C 1 84  ? 18.196  51.635 -49.170 1.00 32.55  ? 65   TRP C CD2 1 
ATOM   3732 N NE1 . TRP C 1 84  ? 20.429  51.514 -48.946 1.00 25.20  ? 65   TRP C NE1 1 
ATOM   3733 C CE2 . TRP C 1 84  ? 19.274  50.779 -48.837 1.00 29.12  ? 65   TRP C CE2 1 
ATOM   3734 C CE3 . TRP C 1 84  ? 16.890  51.119 -49.143 1.00 28.99  ? 65   TRP C CE3 1 
ATOM   3735 C CZ2 . TRP C 1 84  ? 19.089  49.432 -48.485 1.00 27.00  ? 65   TRP C CZ2 1 
ATOM   3736 C CZ3 . TRP C 1 84  ? 16.708  49.780 -48.799 1.00 22.35  ? 65   TRP C CZ3 1 
ATOM   3737 C CH2 . TRP C 1 84  ? 17.805  48.953 -48.476 1.00 22.09  ? 65   TRP C CH2 1 
ATOM   3738 N N   . ASN C 1 85  ? 19.940  55.245 -51.916 1.00 38.26  ? 66   ASN C N   1 
ATOM   3739 C CA  . ASN C 1 85  ? 21.269  55.222 -52.464 1.00 47.31  ? 66   ASN C CA  1 
ATOM   3740 C C   . ASN C 1 85  ? 22.193  54.339 -51.656 1.00 47.53  ? 66   ASN C C   1 
ATOM   3741 O O   . ASN C 1 85  ? 22.374  54.553 -50.492 1.00 50.66  ? 66   ASN C O   1 
ATOM   3742 C CB  . ASN C 1 85  ? 21.801  56.637 -52.448 1.00 44.31  ? 66   ASN C CB  1 
ATOM   3743 C CG  . ASN C 1 85  ? 22.923  56.839 -53.398 1.00 51.70  ? 66   ASN C CG  1 
ATOM   3744 O OD1 . ASN C 1 85  ? 23.602  55.913 -53.754 1.00 53.21  ? 66   ASN C OD1 1 
ATOM   3745 N ND2 . ASN C 1 85  ? 23.118  58.057 -53.818 1.00 60.96  ? 66   ASN C ND2 1 
ATOM   3746 N N   . SER C 1 86  ? 22.818  53.371 -52.292 1.00 44.25  ? 67   SER C N   1 
ATOM   3747 C CA  . SER C 1 86  ? 23.583  52.390 -51.576 1.00 46.91  ? 67   SER C CA  1 
ATOM   3748 C C   . SER C 1 86  ? 25.022  52.708 -51.603 1.00 54.95  ? 67   SER C C   1 
ATOM   3749 O O   . SER C 1 86  ? 25.834  51.880 -51.299 1.00 54.65  ? 67   SER C O   1 
ATOM   3750 C CB  . SER C 1 86  ? 23.365  51.001 -52.146 1.00 54.75  ? 67   SER C CB  1 
ATOM   3751 O OG  . SER C 1 86  ? 24.219  50.699 -53.219 1.00 53.37  ? 67   SER C OG  1 
ATOM   3752 N N   . SER C 1 87  ? 25.343  53.912 -52.015 1.00 59.29  ? 68   SER C N   1 
ATOM   3753 C CA  . SER C 1 87  ? 26.668  54.215 -52.447 1.00 58.11  ? 68   SER C CA  1 
ATOM   3754 C C   . SER C 1 87  ? 27.732  54.038 -51.415 1.00 61.66  ? 68   SER C C   1 
ATOM   3755 O O   . SER C 1 87  ? 28.747  53.463 -51.721 1.00 72.52  ? 68   SER C O   1 
ATOM   3756 C CB  . SER C 1 87  ? 26.715  55.617 -52.987 1.00 58.38  ? 68   SER C CB  1 
ATOM   3757 O OG  . SER C 1 87  ? 28.034  55.947 -53.306 1.00 67.33  ? 68   SER C OG  1 
ATOM   3758 N N   . HIS C 1 88  ? 27.521  54.492 -50.201 1.00 51.81  ? 69   HIS C N   1 
ATOM   3759 C CA  . HIS C 1 88  ? 28.478  54.235 -49.154 1.00 58.25  ? 69   HIS C CA  1 
ATOM   3760 C C   . HIS C 1 88  ? 27.700  53.622 -48.019 1.00 61.55  ? 69   HIS C C   1 
ATOM   3761 O O   . HIS C 1 88  ? 27.933  53.889 -46.869 1.00 64.52  ? 69   HIS C O   1 
ATOM   3762 C CB  . HIS C 1 88  ? 29.225  55.500 -48.747 1.00 60.91  ? 69   HIS C CB  1 
ATOM   3763 C CG  . HIS C 1 88  ? 30.134  56.039 -49.811 1.00 81.81  ? 69   HIS C CG  1 
ATOM   3764 N ND1 . HIS C 1 88  ? 31.200  55.327 -50.314 1.00 93.79  ? 69   HIS C ND1 1 
ATOM   3765 C CD2 . HIS C 1 88  ? 30.136  57.221 -50.469 1.00 80.54  ? 69   HIS C CD2 1 
ATOM   3766 C CE1 . HIS C 1 88  ? 31.806  56.036 -51.248 1.00 84.47  ? 69   HIS C CE1 1 
ATOM   3767 N NE2 . HIS C 1 88  ? 31.185  57.193 -51.354 1.00 81.40  ? 69   HIS C NE2 1 
ATOM   3768 N N   . SER C 1 89  ? 26.739  52.802 -48.380 1.00 53.93  ? 70   SER C N   1 
ATOM   3769 C CA  . SER C 1 89  ? 25.722  52.358 -47.489 1.00 46.57  ? 70   SER C CA  1 
ATOM   3770 C C   . SER C 1 89  ? 25.485  50.893 -47.538 1.00 49.73  ? 70   SER C C   1 
ATOM   3771 O O   . SER C 1 89  ? 26.027  50.201 -48.356 1.00 57.02  ? 70   SER C O   1 
ATOM   3772 C CB  . SER C 1 89  ? 24.438  53.044 -47.829 1.00 51.66  ? 70   SER C CB  1 
ATOM   3773 O OG  . SER C 1 89  ? 24.627  54.417 -47.757 1.00 59.64  ? 70   SER C OG  1 
ATOM   3774 N N   . PRO C 1 90  ? 24.651  50.421 -46.546 1.00 44.59  ? 71   PRO C N   1 
ATOM   3775 C CA  . PRO C 1 90  ? 24.248  49.028 -46.702 1.00 36.11  ? 71   PRO C CA  1 
ATOM   3776 C C   . PRO C 1 90  ? 23.375  48.882 -47.906 1.00 38.50  ? 71   PRO C C   1 
ATOM   3777 O O   . PRO C 1 90  ? 22.766  49.827 -48.263 1.00 44.60  ? 71   PRO C O   1 
ATOM   3778 C CB  . PRO C 1 90  ? 23.424  48.772 -45.467 1.00 38.91  ? 71   PRO C CB  1 
ATOM   3779 C CG  . PRO C 1 90  ? 23.910  49.717 -44.472 1.00 38.29  ? 71   PRO C CG  1 
ATOM   3780 C CD  . PRO C 1 90  ? 24.014  50.934 -45.257 1.00 35.57  ? 71   PRO C CD  1 
ATOM   3781 N N   . ASP C 1 91  ? 23.364  47.750 -48.569 1.00 39.39  ? 72   ASP C N   1 
ATOM   3782 C CA  . ASP C 1 91  ? 22.505  47.567 -49.714 1.00 39.20  ? 72   ASP C CA  1 
ATOM   3783 C C   . ASP C 1 91  ? 21.313  46.703 -49.454 1.00 40.00  ? 72   ASP C C   1 
ATOM   3784 O O   . ASP C 1 91  ? 20.582  46.402 -50.341 1.00 41.90  ? 72   ASP C O   1 
ATOM   3785 C CB  . ASP C 1 91  ? 23.286  46.971 -50.854 1.00 44.06  ? 72   ASP C CB  1 
ATOM   3786 C CG  . ASP C 1 91  ? 24.243  45.938 -50.409 1.00 58.47  ? 72   ASP C CG  1 
ATOM   3787 O OD1 . ASP C 1 91  ? 24.369  45.683 -49.197 1.00 60.97  ? 72   ASP C OD1 1 
ATOM   3788 O OD2 . ASP C 1 91  ? 24.897  45.377 -51.286 1.00 70.65  ? 72   ASP C OD2 1 
ATOM   3789 N N   . GLN C 1 92  ? 21.145  46.296 -48.220 1.00 39.04  ? 73   GLN C N   1 
ATOM   3790 C CA  . GLN C 1 92  ? 20.010  45.487 -47.778 1.00 30.79  ? 73   GLN C CA  1 
ATOM   3791 C C   . GLN C 1 92  ? 19.691  45.669 -46.299 1.00 30.76  ? 73   GLN C C   1 
ATOM   3792 O O   . GLN C 1 92  ? 20.579  45.951 -45.493 1.00 34.78  ? 73   GLN C O   1 
ATOM   3793 C CB  . GLN C 1 92  ? 20.322  44.029 -48.007 1.00 31.63  ? 73   GLN C CB  1 
ATOM   3794 C CG  . GLN C 1 92  ? 21.581  43.626 -47.305 1.00 42.55  ? 73   GLN C CG  1 
ATOM   3795 C CD  . GLN C 1 92  ? 21.756  42.125 -47.270 1.00 65.38  ? 73   GLN C CD  1 
ATOM   3796 O OE1 . GLN C 1 92  ? 21.477  41.427 -48.256 1.00 69.78  ? 73   GLN C OE1 1 
ATOM   3797 N NE2 . GLN C 1 92  ? 22.208  41.610 -46.123 1.00 54.07  ? 73   GLN C NE2 1 
ATOM   3798 N N   . VAL C 1 93  ? 18.418  45.495 -45.946 1.00 26.22  ? 74   VAL C N   1 
ATOM   3799 C CA  . VAL C 1 93  ? 17.979  45.535 -44.546 1.00 24.58  ? 74   VAL C CA  1 
ATOM   3800 C C   . VAL C 1 93  ? 16.832  44.550 -44.350 1.00 22.58  ? 74   VAL C C   1 
ATOM   3801 O O   . VAL C 1 93  ? 16.176  44.171 -45.324 1.00 24.46  ? 74   VAL C O   1 
ATOM   3802 C CB  . VAL C 1 93  ? 17.518  46.967 -44.110 1.00 25.26  ? 74   VAL C CB  1 
ATOM   3803 C CG1 . VAL C 1 93  ? 18.690  47.942 -44.055 1.00 21.96  ? 74   VAL C CG1 1 
ATOM   3804 C CG2 . VAL C 1 93  ? 16.431  47.492 -45.037 1.00 20.90  ? 74   VAL C CG2 1 
ATOM   3805 N N   . SER C 1 94  ? 16.574  44.147 -43.105 1.00 20.55  ? 75   SER C N   1 
ATOM   3806 C CA  . SER C 1 94  ? 15.379  43.345 -42.793 1.00 17.99  ? 75   SER C CA  1 
ATOM   3807 C C   . SER C 1 94  ? 14.291  44.226 -42.186 1.00 24.01  ? 75   SER C C   1 
ATOM   3808 O O   . SER C 1 94  ? 14.560  45.018 -41.280 1.00 25.81  ? 75   SER C O   1 
ATOM   3809 C CB  . SER C 1 94  ? 15.716  42.195 -41.845 1.00 19.80  ? 75   SER C CB  1 
ATOM   3810 O OG  . SER C 1 94  ? 16.391  41.155 -42.529 1.00 31.08  ? 75   SER C OG  1 
ATOM   3811 N N   . VAL C 1 95  ? 13.063  44.092 -42.677 1.00 23.17  ? 76   VAL C N   1 
ATOM   3812 C CA  . VAL C 1 95  ? 11.998  45.003 -42.285 1.00 18.89  ? 76   VAL C CA  1 
ATOM   3813 C C   . VAL C 1 95  ? 10.798  44.211 -41.814 1.00 20.35  ? 76   VAL C C   1 
ATOM   3814 O O   . VAL C 1 95  ? 10.392  43.267 -42.485 1.00 21.31  ? 76   VAL C O   1 
ATOM   3815 C CB  . VAL C 1 95  ? 11.571  45.873 -43.478 1.00 20.91  ? 76   VAL C CB  1 
ATOM   3816 C CG1 . VAL C 1 95  ? 10.448  46.825 -43.090 1.00 23.86  ? 76   VAL C CG1 1 
ATOM   3817 C CG2 . VAL C 1 95  ? 12.761  46.634 -44.041 1.00 17.78  ? 76   VAL C CG2 1 
ATOM   3818 N N   . PRO C 1 96  ? 10.213  44.595 -40.663 1.00 24.12  ? 77   PRO C N   1 
ATOM   3819 C CA  . PRO C 1 96  ? 8.984   43.911 -40.225 1.00 21.77  ? 77   PRO C CA  1 
ATOM   3820 C C   . PRO C 1 96  ? 7.872   44.119 -41.263 1.00 20.50  ? 77   PRO C C   1 
ATOM   3821 O O   . PRO C 1 96  ? 7.679   45.259 -41.699 1.00 21.49  ? 77   PRO C O   1 
ATOM   3822 C CB  . PRO C 1 96  ? 8.637   44.636 -38.918 1.00 22.94  ? 77   PRO C CB  1 
ATOM   3823 C CG  . PRO C 1 96  ? 9.920   45.286 -38.479 1.00 18.28  ? 77   PRO C CG  1 
ATOM   3824 C CD  . PRO C 1 96  ? 10.619  45.668 -39.734 1.00 17.24  ? 77   PRO C CD  1 
ATOM   3825 N N   . ILE C 1 97  ? 7.164   43.058 -41.660 1.00 19.77  ? 78   ILE C N   1 
ATOM   3826 C CA  . ILE C 1 97  ? 6.173   43.194 -42.735 1.00 22.44  ? 78   ILE C CA  1 
ATOM   3827 C C   . ILE C 1 97  ? 5.045   44.181 -42.391 1.00 24.99  ? 78   ILE C C   1 
ATOM   3828 O O   . ILE C 1 97  ? 4.350   44.687 -43.269 1.00 28.23  ? 78   ILE C O   1 
ATOM   3829 C CB  . ILE C 1 97  ? 5.560   41.852 -43.188 1.00 16.59  ? 78   ILE C CB  1 
ATOM   3830 C CG1 . ILE C 1 97  ? 4.835   41.170 -42.022 1.00 23.97  ? 78   ILE C CG1 1 
ATOM   3831 C CG2 . ILE C 1 97  ? 6.608   40.954 -43.789 1.00 16.29  ? 78   ILE C CG2 1 
ATOM   3832 C CD1 . ILE C 1 97  ? 4.003   39.963 -42.440 1.00 19.56  ? 78   ILE C CD1 1 
ATOM   3833 N N   . SER C 1 98  ? 4.854   44.460 -41.112 1.00 27.41  ? 79   SER C N   1 
ATOM   3834 C CA  . SER C 1 98  ? 3.824   45.417 -40.735 1.00 24.19  ? 79   SER C CA  1 
ATOM   3835 C C   . SER C 1 98  ? 4.139   46.809 -41.308 1.00 21.75  ? 79   SER C C   1 
ATOM   3836 O O   . SER C 1 98  ? 3.250   47.654 -41.405 1.00 20.91  ? 79   SER C O   1 
ATOM   3837 C CB  . SER C 1 98  ? 3.632   45.433 -39.208 1.00 22.22  ? 79   SER C CB  1 
ATOM   3838 O OG  . SER C 1 98  ? 4.799   45.883 -38.539 1.00 33.77  ? 79   SER C OG  1 
ATOM   3839 N N   . SER C 1 99  ? 5.394   47.036 -41.709 1.00 20.36  ? 80   SER C N   1 
ATOM   3840 C CA  . SER C 1 99  ? 5.807   48.355 -42.216 1.00 24.16  ? 80   SER C CA  1 
ATOM   3841 C C   . SER C 1 99  ? 5.944   48.412 -43.726 1.00 22.21  ? 80   SER C C   1 
ATOM   3842 O O   . SER C 1 99  ? 6.587   49.313 -44.231 1.00 24.56  ? 80   SER C O   1 
ATOM   3843 C CB  . SER C 1 99  ? 7.141   48.818 -41.597 1.00 23.63  ? 80   SER C CB  1 
ATOM   3844 O OG  . SER C 1 99  ? 7.166   48.657 -40.185 1.00 28.34  ? 80   SER C OG  1 
ATOM   3845 N N   . LEU C 1 100 ? 5.365   47.451 -44.440 1.00 21.88  ? 81   LEU C N   1 
ATOM   3846 C CA  . LEU C 1 100 ? 5.497   47.368 -45.895 1.00 17.24  ? 81   LEU C CA  1 
ATOM   3847 C C   . LEU C 1 100 ? 4.184   46.971 -46.494 1.00 21.67  ? 81   LEU C C   1 
ATOM   3848 O O   . LEU C 1 100 ? 3.412   46.231 -45.871 1.00 19.60  ? 81   LEU C O   1 
ATOM   3849 C CB  . LEU C 1 100 ? 6.432   46.237 -46.279 1.00 21.12  ? 81   LEU C CB  1 
ATOM   3850 C CG  . LEU C 1 100 ? 7.888   46.307 -45.896 1.00 24.62  ? 81   LEU C CG  1 
ATOM   3851 C CD1 . LEU C 1 100 ? 8.575   45.074 -46.396 1.00 21.19  ? 81   LEU C CD1 1 
ATOM   3852 C CD2 . LEU C 1 100 ? 8.448   47.535 -46.544 1.00 28.57  ? 81   LEU C CD2 1 
ATOM   3853 N N   . TRP C 1 101 ? 3.944   47.396 -47.731 1.00 22.57  ? 82   TRP C N   1 
ATOM   3854 C CA  . TRP C 1 101 ? 2.852   46.802 -48.489 1.00 19.20  ? 82   TRP C CA  1 
ATOM   3855 C C   . TRP C 1 101 ? 3.250   45.385 -48.828 1.00 19.14  ? 82   TRP C C   1 
ATOM   3856 O O   . TRP C 1 101 ? 4.406   45.126 -49.142 1.00 22.07  ? 82   TRP C O   1 
ATOM   3857 C CB  . TRP C 1 101 ? 2.580   47.544 -49.779 1.00 21.49  ? 82   TRP C CB  1 
ATOM   3858 C CG  . TRP C 1 101 ? 1.520   46.884 -50.592 1.00 18.41  ? 82   TRP C CG  1 
ATOM   3859 C CD1 . TRP C 1 101 ? 0.169   47.087 -50.510 1.00 18.66  ? 82   TRP C CD1 1 
ATOM   3860 C CD2 . TRP C 1 101 ? 1.718   45.909 -51.617 1.00 18.40  ? 82   TRP C CD2 1 
ATOM   3861 N NE1 . TRP C 1 101 ? -0.480  46.307 -51.436 1.00 16.46  ? 82   TRP C NE1 1 
ATOM   3862 C CE2 . TRP C 1 101 ? 0.446   45.572 -52.123 1.00 16.12  ? 82   TRP C CE2 1 
ATOM   3863 C CE3 . TRP C 1 101 ? 2.851   45.282 -52.154 1.00 21.70  ? 82   TRP C CE3 1 
ATOM   3864 C CZ2 . TRP C 1 101 ? 0.274   44.633 -53.135 1.00 19.29  ? 82   TRP C CZ2 1 
ATOM   3865 C CZ3 . TRP C 1 101 ? 2.685   44.342 -53.163 1.00 16.30  ? 82   TRP C CZ3 1 
ATOM   3866 C CH2 . TRP C 1 101 ? 1.405   44.028 -53.645 1.00 18.07  ? 82   TRP C CH2 1 
ATOM   3867 N N   . VAL C 1 102 ? 2.279   44.480 -48.778 1.00 19.97  ? 83   VAL C N   1 
ATOM   3868 C CA  . VAL C 1 102 ? 2.489   43.057 -49.036 1.00 18.10  ? 83   VAL C CA  1 
ATOM   3869 C C   . VAL C 1 102 ? 1.315   42.582 -49.883 1.00 16.34  ? 83   VAL C C   1 
ATOM   3870 O O   . VAL C 1 102 ? 0.178   43.023 -49.674 1.00 20.94  ? 83   VAL C O   1 
ATOM   3871 C CB  . VAL C 1 102 ? 2.562   42.277 -47.692 1.00 13.65  ? 83   VAL C CB  1 
ATOM   3872 C CG1 . VAL C 1 102 ? 2.110   40.844 -47.857 1.00 20.72  ? 83   VAL C CG1 1 
ATOM   3873 C CG2 . VAL C 1 102 ? 3.957   42.347 -47.121 1.00 12.31  ? 83   VAL C CG2 1 
ATOM   3874 N N   . PRO C 1 103 ? 1.571   41.692 -50.849 1.00 13.89  ? 84   PRO C N   1 
ATOM   3875 C CA  . PRO C 1 103 ? 0.464   41.184 -51.685 1.00 15.56  ? 84   PRO C CA  1 
ATOM   3876 C C   . PRO C 1 103 ? -0.527  40.321 -50.905 1.00 16.33  ? 84   PRO C C   1 
ATOM   3877 O O   . PRO C 1 103 ? -0.107  39.561 -50.035 1.00 18.70  ? 84   PRO C O   1 
ATOM   3878 C CB  . PRO C 1 103 ? 1.173   40.374 -52.774 1.00 11.44  ? 84   PRO C CB  1 
ATOM   3879 C CG  . PRO C 1 103 ? 2.501   40.048 -52.195 1.00 15.68  ? 84   PRO C CG  1 
ATOM   3880 C CD  . PRO C 1 103 ? 2.881   41.173 -51.259 1.00 15.62  ? 84   PRO C CD  1 
ATOM   3881 N N   . ASP C 1 104 ? -1.820  40.450 -51.210 1.00 19.89  ? 85   ASP C N   1 
ATOM   3882 C CA  . ASP C 1 104 ? -2.880  39.735 -50.479 1.00 19.93  ? 85   ASP C CA  1 
ATOM   3883 C C   . ASP C 1 104 ? -3.140  38.353 -51.059 1.00 20.12  ? 85   ASP C C   1 
ATOM   3884 O O   . ASP C 1 104 ? -4.261  38.045 -51.466 1.00 19.95  ? 85   ASP C O   1 
ATOM   3885 C CB  . ASP C 1 104 ? -4.199  40.539 -50.433 1.00 21.52  ? 85   ASP C CB  1 
ATOM   3886 C CG  . ASP C 1 104 ? -4.773  40.841 -51.837 1.00 27.71  ? 85   ASP C CG  1 
ATOM   3887 O OD1 . ASP C 1 104 ? -3.976  40.983 -52.795 1.00 29.69  ? 85   ASP C OD1 1 
ATOM   3888 O OD2 . ASP C 1 104 ? -6.022  40.927 -51.983 1.00 22.73  ? 85   ASP C OD2 1 
ATOM   3889 N N   . LEU C 1 105 ? -2.110  37.509 -51.070 1.00 17.18  ? 86   LEU C N   1 
ATOM   3890 C CA  . LEU C 1 105 ? -2.260  36.156 -51.604 1.00 16.50  ? 86   LEU C CA  1 
ATOM   3891 C C   . LEU C 1 105 ? -3.043  35.241 -50.640 1.00 18.88  ? 86   LEU C C   1 
ATOM   3892 O O   . LEU C 1 105 ? -2.964  35.387 -49.405 1.00 18.74  ? 86   LEU C O   1 
ATOM   3893 C CB  . LEU C 1 105 ? -0.890  35.564 -51.932 1.00 17.08  ? 86   LEU C CB  1 
ATOM   3894 C CG  . LEU C 1 105 ? -0.036  36.410 -52.873 1.00 17.56  ? 86   LEU C CG  1 
ATOM   3895 C CD1 . LEU C 1 105 ? 1.384   35.857 -52.962 1.00 17.99  ? 86   LEU C CD1 1 
ATOM   3896 C CD2 . LEU C 1 105 ? -0.666  36.506 -54.266 1.00 17.44  ? 86   LEU C CD2 1 
ATOM   3897 N N   . ALA C 1 106 ? -3.807  34.317 -51.216 1.00 14.71  ? 87   ALA C N   1 
ATOM   3898 C CA  . ALA C 1 106 ? -4.557  33.326 -50.459 1.00 14.69  ? 87   ALA C CA  1 
ATOM   3899 C C   . ALA C 1 106 ? -4.573  32.007 -51.220 1.00 23.14  ? 87   ALA C C   1 
ATOM   3900 O O   . ALA C 1 106 ? -4.513  31.990 -52.459 1.00 23.30  ? 87   ALA C O   1 
ATOM   3901 C CB  . ALA C 1 106 ? -5.965  33.800 -50.217 1.00 12.07  ? 87   ALA C CB  1 
ATOM   3902 N N   . ALA C 1 107 ? -4.644  30.901 -50.480 1.00 24.62  ? 88   ALA C N   1 
ATOM   3903 C CA  . ALA C 1 107 ? -4.787  29.576 -51.087 1.00 22.30  ? 88   ALA C CA  1 
ATOM   3904 C C   . ALA C 1 107 ? -6.271  29.249 -51.195 1.00 20.23  ? 88   ALA C C   1 
ATOM   3905 O O   . ALA C 1 107 ? -6.958  29.092 -50.185 1.00 22.93  ? 88   ALA C O   1 
ATOM   3906 C CB  . ALA C 1 107 ? -4.052  28.517 -50.264 1.00 21.24  ? 88   ALA C CB  1 
ATOM   3907 N N   . TYR C 1 108 ? -6.765  29.149 -52.424 1.00 21.49  ? 89   TYR C N   1 
ATOM   3908 C CA  . TYR C 1 108 ? -8.198  28.976 -52.663 1.00 19.42  ? 89   TYR C CA  1 
ATOM   3909 C C   . TYR C 1 108 ? -8.771  27.695 -52.071 1.00 23.93  ? 89   TYR C C   1 
ATOM   3910 O O   . TYR C 1 108 ? -9.950  27.656 -51.709 1.00 18.51  ? 89   TYR C O   1 
ATOM   3911 C CB  . TYR C 1 108 ? -8.498  29.051 -54.161 1.00 20.14  ? 89   TYR C CB  1 
ATOM   3912 C CG  . TYR C 1 108 ? -8.584  30.472 -54.699 1.00 24.82  ? 89   TYR C CG  1 
ATOM   3913 C CD1 . TYR C 1 108 ? -7.443  31.262 -54.827 1.00 23.20  ? 89   TYR C CD1 1 
ATOM   3914 C CD2 . TYR C 1 108 ? -9.799  31.014 -55.087 1.00 19.92  ? 89   TYR C CD2 1 
ATOM   3915 C CE1 . TYR C 1 108 ? -7.514  32.539 -55.300 1.00 22.94  ? 89   TYR C CE1 1 
ATOM   3916 C CE2 . TYR C 1 108 ? -9.884  32.293 -55.571 1.00 18.95  ? 89   TYR C CE2 1 
ATOM   3917 C CZ  . TYR C 1 108 ? -8.742  33.056 -55.672 1.00 26.12  ? 89   TYR C CZ  1 
ATOM   3918 O OH  . TYR C 1 108 ? -8.822  34.345 -56.159 1.00 32.28  ? 89   TYR C OH  1 
ATOM   3919 N N   . ASN C 1 109 ? -7.945  26.647 -51.988 1.00 25.83  ? 90   ASN C N   1 
ATOM   3920 C CA  . ASN C 1 109 ? -8.428  25.350 -51.519 1.00 23.61  ? 90   ASN C CA  1 
ATOM   3921 C C   . ASN C 1 109 ? -7.864  25.005 -50.148 1.00 24.14  ? 90   ASN C C   1 
ATOM   3922 O O   . ASN C 1 109 ? -7.789  23.836 -49.755 1.00 34.15  ? 90   ASN C O   1 
ATOM   3923 C CB  . ASN C 1 109 ? -8.176  24.231 -52.552 1.00 21.46  ? 90   ASN C CB  1 
ATOM   3924 C CG  . ASN C 1 109 ? -6.705  24.042 -52.871 1.00 19.02  ? 90   ASN C CG  1 
ATOM   3925 O OD1 . ASN C 1 109 ? -5.996  24.993 -53.159 1.00 22.25  ? 90   ASN C OD1 1 
ATOM   3926 N ND2 . ASN C 1 109 ? -6.240  22.804 -52.800 1.00 25.33  ? 90   ASN C ND2 1 
ATOM   3927 N N   . ALA C 1 110 ? -7.460  26.031 -49.414 1.00 18.25  ? 91   ALA C N   1 
ATOM   3928 C CA  . ALA C 1 110 ? -7.041  25.839 -48.028 1.00 19.16  ? 91   ALA C CA  1 
ATOM   3929 C C   . ALA C 1 110 ? -8.286  25.625 -47.163 1.00 18.98  ? 91   ALA C C   1 
ATOM   3930 O O   . ALA C 1 110 ? -9.341  26.195 -47.435 1.00 20.97  ? 91   ALA C O   1 
ATOM   3931 C CB  . ALA C 1 110 ? -6.240  27.037 -47.544 1.00 17.53  ? 91   ALA C CB  1 
ATOM   3932 N N   . ILE C 1 111 ? -8.186  24.783 -46.143 1.00 17.50  ? 92   ILE C N   1 
ATOM   3933 C CA  . ILE C 1 111 ? -9.325  24.591 -45.260 1.00 18.90  ? 92   ILE C CA  1 
ATOM   3934 C C   . ILE C 1 111 ? -8.979  24.937 -43.817 1.00 19.61  ? 92   ILE C C   1 
ATOM   3935 O O   . ILE C 1 111 ? -9.732  24.615 -42.896 1.00 17.36  ? 92   ILE C O   1 
ATOM   3936 C CB  . ILE C 1 111 ? -9.902  23.173 -45.351 1.00 21.05  ? 92   ILE C CB  1 
ATOM   3937 C CG1 . ILE C 1 111 ? -8.827  22.128 -45.089 1.00 23.46  ? 92   ILE C CG1 1 
ATOM   3938 C CG2 . ILE C 1 111 ? -10.528 22.942 -46.708 1.00 21.98  ? 92   ILE C CG2 1 
ATOM   3939 C CD1 . ILE C 1 111 ? -9.364  20.715 -45.057 1.00 24.40  ? 92   ILE C CD1 1 
ATOM   3940 N N   . SER C 1 112 ? -7.839  25.603 -43.645 1.00 17.46  ? 93   SER C N   1 
ATOM   3941 C CA  . SER C 1 112 ? -7.434  26.171 -42.358 1.00 26.21  ? 93   SER C CA  1 
ATOM   3942 C C   . SER C 1 112 ? -6.680  27.445 -42.674 1.00 22.68  ? 93   SER C C   1 
ATOM   3943 O O   . SER C 1 112 ? -6.199  27.593 -43.799 1.00 21.06  ? 93   SER C O   1 
ATOM   3944 C CB  . SER C 1 112 ? -6.532  25.191 -41.603 1.00 28.40  ? 93   SER C CB  1 
ATOM   3945 O OG  . SER C 1 112 ? -5.261  25.066 -42.231 1.00 29.66  ? 93   SER C OG  1 
ATOM   3946 N N   . LYS C 1 113 ? -6.556  28.361 -41.716 1.00 26.34  ? 94   LYS C N   1 
ATOM   3947 C CA  . LYS C 1 113 ? -5.756  29.572 -41.981 1.00 26.93  ? 94   LYS C CA  1 
ATOM   3948 C C   . LYS C 1 113 ? -4.254  29.262 -41.905 1.00 26.08  ? 94   LYS C C   1 
ATOM   3949 O O   . LYS C 1 113 ? -3.850  28.320 -41.225 1.00 29.17  ? 94   LYS C O   1 
ATOM   3950 C CB  . LYS C 1 113 ? -6.149  30.747 -41.071 1.00 26.82  ? 94   LYS C CB  1 
ATOM   3951 C CG  . LYS C 1 113 ? -5.877  30.550 -39.586 1.00 38.20  ? 94   LYS C CG  1 
ATOM   3952 C CD  . LYS C 1 113 ? -6.561  31.663 -38.777 1.00 49.27  ? 94   LYS C CD  1 
ATOM   3953 C CE  . LYS C 1 113 ? -6.214  33.052 -39.329 1.00 54.78  ? 94   LYS C CE  1 
ATOM   3954 N NZ  . LYS C 1 113 ? -6.649  34.182 -38.440 1.00 58.07  ? 94   LYS C NZ  1 
ATOM   3955 N N   . PRO C 1 114 ? -3.427  30.026 -42.638 1.00 25.17  ? 95   PRO C N   1 
ATOM   3956 C CA  . PRO C 1 114 ? -1.988  29.753 -42.606 1.00 19.47  ? 95   PRO C CA  1 
ATOM   3957 C C   . PRO C 1 114 ? -1.439  29.899 -41.198 1.00 21.57  ? 95   PRO C C   1 
ATOM   3958 O O   . PRO C 1 114 ? -1.736  30.884 -40.537 1.00 25.48  ? 95   PRO C O   1 
ATOM   3959 C CB  . PRO C 1 114 ? -1.406  30.868 -43.471 1.00 16.41  ? 95   PRO C CB  1 
ATOM   3960 C CG  . PRO C 1 114 ? -2.541  31.404 -44.249 1.00 16.21  ? 95   PRO C CG  1 
ATOM   3961 C CD  . PRO C 1 114 ? -3.752  31.210 -43.454 1.00 21.68  ? 95   PRO C CD  1 
ATOM   3962 N N   . GLU C 1 115 ? -0.659  28.928 -40.744 1.00 24.74  ? 96   GLU C N   1 
ATOM   3963 C CA  . GLU C 1 115 ? 0.037   29.030 -39.468 1.00 22.92  ? 96   GLU C CA  1 
ATOM   3964 C C   . GLU C 1 115 ? 1.481   29.412 -39.775 1.00 23.60  ? 96   GLU C C   1 
ATOM   3965 O O   . GLU C 1 115 ? 2.234   28.595 -40.324 1.00 21.30  ? 96   GLU C O   1 
ATOM   3966 C CB  . GLU C 1 115 ? 0.001   27.687 -38.750 1.00 21.16  ? 96   GLU C CB  1 
ATOM   3967 C CG  . GLU C 1 115 ? 0.556   27.696 -37.329 1.00 39.37  ? 96   GLU C CG  1 
ATOM   3968 C CD  . GLU C 1 115 ? 0.424   26.321 -36.652 1.00 58.45  ? 96   GLU C CD  1 
ATOM   3969 O OE1 . GLU C 1 115 ? -0.380  25.495 -37.164 1.00 61.40  ? 96   GLU C OE1 1 
ATOM   3970 O OE2 . GLU C 1 115 ? 1.124   26.064 -35.628 1.00 58.23  ? 96   GLU C OE2 1 
ATOM   3971 N N   . VAL C 1 116 ? 1.870   30.648 -39.448 1.00 24.45  ? 97   VAL C N   1 
ATOM   3972 C CA  . VAL C 1 116 ? 3.219   31.132 -39.796 1.00 20.84  ? 97   VAL C CA  1 
ATOM   3973 C C   . VAL C 1 116 ? 4.263   30.753 -38.767 1.00 18.23  ? 97   VAL C C   1 
ATOM   3974 O O   . VAL C 1 116 ? 4.204   31.177 -37.618 1.00 19.27  ? 97   VAL C O   1 
ATOM   3975 C CB  . VAL C 1 116 ? 3.272   32.643 -40.055 1.00 18.68  ? 97   VAL C CB  1 
ATOM   3976 C CG1 . VAL C 1 116 ? 4.637   33.022 -40.546 1.00 14.32  ? 97   VAL C CG1 1 
ATOM   3977 C CG2 . VAL C 1 116 ? 2.253   33.032 -41.087 1.00 20.89  ? 97   VAL C CG2 1 
ATOM   3978 N N   . LEU C 1 117 ? 5.233   29.955 -39.198 1.00 19.50  ? 98   LEU C N   1 
ATOM   3979 C CA  . LEU C 1 117 ? 6.171   29.334 -38.273 1.00 19.95  ? 98   LEU C CA  1 
ATOM   3980 C C   . LEU C 1 117 ? 7.380   30.201 -37.936 1.00 21.12  ? 98   LEU C C   1 
ATOM   3981 O O   . LEU C 1 117 ? 8.015   30.018 -36.891 1.00 19.22  ? 98   LEU C O   1 
ATOM   3982 C CB  . LEU C 1 117 ? 6.618   27.983 -38.828 1.00 19.34  ? 98   LEU C CB  1 
ATOM   3983 C CG  . LEU C 1 117 ? 5.518   26.927 -39.023 1.00 19.32  ? 98   LEU C CG  1 
ATOM   3984 C CD1 . LEU C 1 117 ? 6.131   25.630 -39.565 1.00 16.10  ? 98   LEU C CD1 1 
ATOM   3985 C CD2 . LEU C 1 117 ? 4.686   26.664 -37.756 1.00 13.20  ? 98   LEU C CD2 1 
ATOM   3986 N N   . THR C 1 118 ? 7.680   31.149 -38.817 1.00 17.75  ? 99   THR C N   1 
ATOM   3987 C CA  . THR C 1 118 ? 8.926   31.903 -38.725 1.00 17.86  ? 99   THR C CA  1 
ATOM   3988 C C   . THR C 1 118 ? 8.679   33.368 -38.378 1.00 20.03  ? 99   THR C C   1 
ATOM   3989 O O   . THR C 1 118 ? 7.539   33.838 -38.477 1.00 18.15  ? 99   THR C O   1 
ATOM   3990 C CB  . THR C 1 118 ? 9.673   31.814 -40.052 1.00 19.37  ? 99   THR C CB  1 
ATOM   3991 O OG1 . THR C 1 118 ? 8.759   32.126 -41.112 1.00 25.39  ? 99   THR C OG1 1 
ATOM   3992 C CG2 . THR C 1 118 ? 10.199  30.414 -40.248 1.00 19.58  ? 99   THR C CG2 1 
ATOM   3993 N N   . PRO C 1 119 ? 9.744   34.093 -37.973 1.00 20.69  ? 100  PRO C N   1 
ATOM   3994 C CA  . PRO C 1 119 ? 9.680   35.553 -37.778 1.00 23.19  ? 100  PRO C CA  1 
ATOM   3995 C C   . PRO C 1 119 ? 9.116   36.242 -39.015 1.00 21.26  ? 100  PRO C C   1 
ATOM   3996 O O   . PRO C 1 119 ? 9.450   35.841 -40.150 1.00 18.00  ? 100  PRO C O   1 
ATOM   3997 C CB  . PRO C 1 119 ? 11.153  35.949 -37.597 1.00 17.16  ? 100  PRO C CB  1 
ATOM   3998 C CG  . PRO C 1 119 ? 11.797  34.737 -37.012 1.00 16.28  ? 100  PRO C CG  1 
ATOM   3999 C CD  . PRO C 1 119 ? 11.050  33.539 -37.566 1.00 19.44  ? 100  PRO C CD  1 
ATOM   4000 N N   . GLN C 1 120 ? 8.282   37.260 -38.805 1.00 20.70  ? 101  GLN C N   1 
ATOM   4001 C CA  . GLN C 1 120 ? 7.653   37.946 -39.936 1.00 23.75  ? 101  GLN C CA  1 
ATOM   4002 C C   . GLN C 1 120 ? 8.438   39.177 -40.472 1.00 25.34  ? 101  GLN C C   1 
ATOM   4003 O O   . GLN C 1 120 ? 7.989   40.338 -40.392 1.00 23.20  ? 101  GLN C O   1 
ATOM   4004 C CB  . GLN C 1 120 ? 6.178   38.239 -39.635 1.00 22.59  ? 101  GLN C CB  1 
ATOM   4005 C CG  . GLN C 1 120 ? 5.323   36.975 -39.592 1.00 23.49  ? 101  GLN C CG  1 
ATOM   4006 C CD  . GLN C 1 120 ? 3.909   37.205 -39.082 1.00 31.30  ? 101  GLN C CD  1 
ATOM   4007 O OE1 . GLN C 1 120 ? 3.257   38.188 -39.437 1.00 51.25  ? 101  GLN C OE1 1 
ATOM   4008 N NE2 . GLN C 1 120 ? 3.430   36.295 -38.239 1.00 30.47  ? 101  GLN C NE2 1 
ATOM   4009 N N   . LEU C 1 121 ? 9.612   38.888 -41.033 1.00 22.19  ? 102  LEU C N   1 
ATOM   4010 C CA  . LEU C 1 121 ? 10.486  39.902 -41.606 1.00 17.91  ? 102  LEU C CA  1 
ATOM   4011 C C   . LEU C 1 121 ? 10.646  39.701 -43.098 1.00 25.63  ? 102  LEU C C   1 
ATOM   4012 O O   . LEU C 1 121 ? 10.731  38.561 -43.576 1.00 28.70  ? 102  LEU C O   1 
ATOM   4013 C CB  . LEU C 1 121 ? 11.866  39.813 -40.975 1.00 19.48  ? 102  LEU C CB  1 
ATOM   4014 C CG  . LEU C 1 121 ? 11.880  40.042 -39.467 1.00 22.71  ? 102  LEU C CG  1 
ATOM   4015 C CD1 . LEU C 1 121 ? 13.294  39.951 -38.899 1.00 19.84  ? 102  LEU C CD1 1 
ATOM   4016 C CD2 . LEU C 1 121 ? 11.251  41.389 -39.147 1.00 19.45  ? 102  LEU C CD2 1 
ATOM   4017 N N   . ALA C 1 122 ? 10.696  40.809 -43.835 1.00 28.04  ? 103  ALA C N   1 
ATOM   4018 C CA  . ALA C 1 122 ? 10.987  40.779 -45.274 1.00 20.86  ? 103  ALA C CA  1 
ATOM   4019 C C   . ALA C 1 122 ? 12.394  41.307 -45.544 1.00 22.77  ? 103  ALA C C   1 
ATOM   4020 O O   . ALA C 1 122 ? 12.930  42.144 -44.802 1.00 22.56  ? 103  ALA C O   1 
ATOM   4021 C CB  . ALA C 1 122 ? 9.959   41.585 -46.054 1.00 13.72  ? 103  ALA C CB  1 
ATOM   4022 N N   . HIS C 1 123 ? 12.986  40.820 -46.624 1.00 24.61  ? 104  HIS C N   1 
ATOM   4023 C CA  . HIS C 1 123 ? 14.310  41.256 -47.047 1.00 20.52  ? 104  HIS C CA  1 
ATOM   4024 C C   . HIS C 1 123 ? 14.134  42.365 -48.082 1.00 20.81  ? 104  HIS C C   1 
ATOM   4025 O O   . HIS C 1 123 ? 13.369  42.195 -49.030 1.00 27.16  ? 104  HIS C O   1 
ATOM   4026 C CB  . HIS C 1 123 ? 15.036  40.065 -47.654 1.00 23.73  ? 104  HIS C CB  1 
ATOM   4027 C CG  . HIS C 1 123 ? 16.496  40.282 -47.841 1.00 28.32  ? 104  HIS C CG  1 
ATOM   4028 N ND1 . HIS C 1 123 ? 17.060  40.498 -49.079 1.00 32.55  ? 104  HIS C ND1 1 
ATOM   4029 C CD2 . HIS C 1 123 ? 17.515  40.312 -46.946 1.00 33.72  ? 104  HIS C CD2 1 
ATOM   4030 C CE1 . HIS C 1 123 ? 18.368  40.659 -48.940 1.00 38.63  ? 104  HIS C CE1 1 
ATOM   4031 N NE2 . HIS C 1 123 ? 18.667  40.551 -47.657 1.00 39.31  ? 104  HIS C NE2 1 
ATOM   4032 N N   . VAL C 1 124 ? 14.812  43.498 -47.904 1.00 19.04  ? 105  VAL C N   1 
ATOM   4033 C CA  . VAL C 1 124 ? 14.676  44.629 -48.824 1.00 17.31  ? 105  VAL C CA  1 
ATOM   4034 C C   . VAL C 1 124 ? 16.048  45.025 -49.314 1.00 21.02  ? 105  VAL C C   1 
ATOM   4035 O O   . VAL C 1 124 ? 16.968  45.232 -48.523 1.00 24.46  ? 105  VAL C O   1 
ATOM   4036 C CB  . VAL C 1 124 ? 14.031  45.878 -48.155 1.00 18.11  ? 105  VAL C CB  1 
ATOM   4037 C CG1 . VAL C 1 124 ? 13.799  46.983 -49.174 1.00 17.46  ? 105  VAL C CG1 1 
ATOM   4038 C CG2 . VAL C 1 124 ? 12.739  45.530 -47.496 1.00 20.51  ? 105  VAL C CG2 1 
ATOM   4039 N N   . VAL C 1 125 ? 16.168  45.166 -50.624 1.00 22.96  ? 106  VAL C N   1 
ATOM   4040 C CA  . VAL C 1 125 ? 17.421  45.550 -51.265 1.00 29.20  ? 106  VAL C CA  1 
ATOM   4041 C C   . VAL C 1 125 ? 17.294  47.027 -51.668 1.00 26.14  ? 106  VAL C C   1 
ATOM   4042 O O   . VAL C 1 125 ? 16.188  47.473 -51.936 1.00 27.34  ? 106  VAL C O   1 
ATOM   4043 C CB  . VAL C 1 125 ? 17.696  44.619 -52.500 1.00 32.36  ? 106  VAL C CB  1 
ATOM   4044 C CG1 . VAL C 1 125 ? 18.902  45.072 -53.281 1.00 36.80  ? 106  VAL C CG1 1 
ATOM   4045 C CG2 . VAL C 1 125 ? 17.889  43.182 -52.051 1.00 25.37  ? 106  VAL C CG2 1 
ATOM   4046 N N   . SER C 1 126 ? 18.403  47.776 -51.705 1.00 24.96  ? 107  SER C N   1 
ATOM   4047 C CA  . SER C 1 126 ? 18.386  49.214 -52.022 1.00 24.23  ? 107  SER C CA  1 
ATOM   4048 C C   . SER C 1 126 ? 17.685  49.629 -53.320 1.00 29.89  ? 107  SER C C   1 
ATOM   4049 O O   . SER C 1 126 ? 17.280  50.787 -53.446 1.00 30.32  ? 107  SER C O   1 
ATOM   4050 C CB  . SER C 1 126 ? 19.789  49.788 -52.035 1.00 26.70  ? 107  SER C CB  1 
ATOM   4051 O OG  . SER C 1 126 ? 20.589  49.069 -52.952 1.00 40.47  ? 107  SER C OG  1 
ATOM   4052 N N   . ASP C 1 127 ? 17.548  48.717 -54.283 1.00 28.40  ? 108  ASP C N   1 
ATOM   4053 C CA  . ASP C 1 127 ? 16.823  49.052 -55.506 1.00 29.76  ? 108  ASP C CA  1 
ATOM   4054 C C   . ASP C 1 127 ? 15.293  49.061 -55.340 1.00 31.78  ? 108  ASP C C   1 
ATOM   4055 O O   . ASP C 1 127 ? 14.569  49.583 -56.188 1.00 40.53  ? 108  ASP C O   1 
ATOM   4056 C CB  . ASP C 1 127 ? 17.248  48.163 -56.695 1.00 37.15  ? 108  ASP C CB  1 
ATOM   4057 C CG  . ASP C 1 127 ? 17.024  46.666 -56.445 1.00 47.68  ? 108  ASP C CG  1 
ATOM   4058 O OD1 . ASP C 1 127 ? 16.342  46.307 -55.446 1.00 43.98  ? 108  ASP C OD1 1 
ATOM   4059 O OD2 . ASP C 1 127 ? 17.530  45.846 -57.261 1.00 47.43  ? 108  ASP C OD2 1 
ATOM   4060 N N   . GLY C 1 128 ? 14.801  48.481 -54.255 1.00 30.17  ? 109  GLY C N   1 
ATOM   4061 C CA  . GLY C 1 128 ? 13.366  48.382 -54.049 1.00 28.43  ? 109  GLY C CA  1 
ATOM   4062 C C   . GLY C 1 128 ? 12.814  46.968 -54.161 1.00 27.85  ? 109  GLY C C   1 
ATOM   4063 O O   . GLY C 1 128 ? 11.603  46.769 -54.141 1.00 22.28  ? 109  GLY C O   1 
ATOM   4064 N N   . GLU C 1 129 ? 13.701  45.984 -54.277 1.00 30.95  ? 110  GLU C N   1 
ATOM   4065 C CA  . GLU C 1 129 ? 13.279  44.590 -54.396 1.00 31.14  ? 110  GLU C CA  1 
ATOM   4066 C C   . GLU C 1 129 ? 12.997  43.976 -53.032 1.00 31.22  ? 110  GLU C C   1 
ATOM   4067 O O   . GLU C 1 129 ? 13.837  44.010 -52.125 1.00 30.13  ? 110  GLU C O   1 
ATOM   4068 C CB  . GLU C 1 129 ? 14.336  43.757 -55.124 1.00 34.63  ? 110  GLU C CB  1 
ATOM   4069 C CG  . GLU C 1 129 ? 14.227  43.788 -56.638 1.00 44.62  ? 110  GLU C CG  1 
ATOM   4070 C CD  . GLU C 1 129 ? 13.046  42.972 -57.155 1.00 60.37  ? 110  GLU C CD  1 
ATOM   4071 O OE1 . GLU C 1 129 ? 12.888  41.806 -56.703 1.00 65.49  ? 110  GLU C OE1 1 
ATOM   4072 O OE2 . GLU C 1 129 ? 12.280  43.501 -58.006 1.00 60.85  ? 110  GLU C OE2 1 
ATOM   4073 N N   . VAL C 1 130 ? 11.816  43.393 -52.893 1.00 27.91  ? 111  VAL C N   1 
ATOM   4074 C CA  . VAL C 1 130 ? 11.413  42.818 -51.624 1.00 19.36  ? 111  VAL C CA  1 
ATOM   4075 C C   . VAL C 1 130 ? 11.241  41.324 -51.765 1.00 22.79  ? 111  VAL C C   1 
ATOM   4076 O O   . VAL C 1 130 ? 10.699  40.847 -52.766 1.00 26.76  ? 111  VAL C O   1 
ATOM   4077 C CB  . VAL C 1 130 ? 10.110  43.435 -51.165 1.00 20.52  ? 111  VAL C CB  1 
ATOM   4078 C CG1 . VAL C 1 130 ? 9.722   42.897 -49.795 1.00 16.97  ? 111  VAL C CG1 1 
ATOM   4079 C CG2 . VAL C 1 130 ? 10.240  44.967 -51.166 1.00 19.74  ? 111  VAL C CG2 1 
ATOM   4080 N N   . GLN C 1 131 ? 11.712  40.576 -50.774 1.00 21.41  ? 112  GLN C N   1 
ATOM   4081 C CA  . GLN C 1 131 ? 11.426  39.144 -50.722 1.00 23.68  ? 112  GLN C CA  1 
ATOM   4082 C C   . GLN C 1 131 ? 10.896  38.756 -49.347 1.00 24.25  ? 112  GLN C C   1 
ATOM   4083 O O   . GLN C 1 131 ? 11.519  39.050 -48.329 1.00 28.73  ? 112  GLN C O   1 
ATOM   4084 C CB  . GLN C 1 131 ? 12.660  38.318 -51.052 1.00 24.17  ? 112  GLN C CB  1 
ATOM   4085 C CG  . GLN C 1 131 ? 12.396  36.833 -51.046 1.00 30.95  ? 112  GLN C CG  1 
ATOM   4086 C CD  . GLN C 1 131 ? 13.616  36.023 -51.447 1.00 41.44  ? 112  GLN C CD  1 
ATOM   4087 O OE1 . GLN C 1 131 ? 14.349  36.389 -52.375 1.00 40.33  ? 112  GLN C OE1 1 
ATOM   4088 N NE2 . GLN C 1 131 ? 13.840  34.909 -50.747 1.00 45.97  ? 112  GLN C NE2 1 
ATOM   4089 N N   . TYR C 1 132 ? 9.740   38.109 -49.315 1.00 16.22  ? 113  TYR C N   1 
ATOM   4090 C CA  . TYR C 1 132 ? 9.189   37.637 -48.062 1.00 18.95  ? 113  TYR C CA  1 
ATOM   4091 C C   . TYR C 1 132 ? 8.955   36.112 -48.140 1.00 26.98  ? 113  TYR C C   1 
ATOM   4092 O O   . TYR C 1 132 ? 8.162   35.630 -48.965 1.00 30.44  ? 113  TYR C O   1 
ATOM   4093 C CB  . TYR C 1 132 ? 7.909   38.415 -47.738 1.00 19.47  ? 113  TYR C CB  1 
ATOM   4094 C CG  . TYR C 1 132 ? 7.179   37.939 -46.501 1.00 18.60  ? 113  TYR C CG  1 
ATOM   4095 C CD1 . TYR C 1 132 ? 7.869   37.685 -45.318 1.00 18.32  ? 113  TYR C CD1 1 
ATOM   4096 C CD2 . TYR C 1 132 ? 5.801   37.761 -46.516 1.00 13.99  ? 113  TYR C CD2 1 
ATOM   4097 C CE1 . TYR C 1 132 ? 7.208   37.239 -44.179 1.00 19.82  ? 113  TYR C CE1 1 
ATOM   4098 C CE2 . TYR C 1 132 ? 5.124   37.314 -45.395 1.00 19.56  ? 113  TYR C CE2 1 
ATOM   4099 C CZ  . TYR C 1 132 ? 5.832   37.046 -44.224 1.00 22.86  ? 113  TYR C CZ  1 
ATOM   4100 O OH  . TYR C 1 132 ? 5.158   36.615 -43.097 1.00 21.10  ? 113  TYR C OH  1 
ATOM   4101 N N   . THR C 1 133 ? 9.659   35.353 -47.301 1.00 19.36  ? 114  THR C N   1 
ATOM   4102 C CA  . THR C 1 133 ? 9.620   33.896 -47.403 1.00 23.38  ? 114  THR C CA  1 
ATOM   4103 C C   . THR C 1 133 ? 9.285   33.251 -46.058 1.00 22.70  ? 114  THR C C   1 
ATOM   4104 O O   . THR C 1 133 ? 10.166  32.752 -45.346 1.00 22.32  ? 114  THR C O   1 
ATOM   4105 C CB  . THR C 1 133 ? 10.962  33.320 -47.935 1.00 27.30  ? 114  THR C CB  1 
ATOM   4106 O OG1 . THR C 1 133 ? 11.433  34.093 -49.053 1.00 27.08  ? 114  THR C OG1 1 
ATOM   4107 C CG2 . THR C 1 133 ? 10.829  31.836 -48.328 1.00 20.42  ? 114  THR C CG2 1 
ATOM   4108 N N   . PRO C 1 134 ? 7.999   33.265 -45.692 1.00 22.13  ? 115  PRO C N   1 
ATOM   4109 C CA  . PRO C 1 134 ? 7.637   32.613 -44.422 1.00 21.94  ? 115  PRO C CA  1 
ATOM   4110 C C   . PRO C 1 134 ? 7.519   31.104 -44.566 1.00 23.31  ? 115  PRO C C   1 
ATOM   4111 O O   . PRO C 1 134 ? 7.152   30.584 -45.643 1.00 24.06  ? 115  PRO C O   1 
ATOM   4112 C CB  . PRO C 1 134 ? 6.258   33.208 -44.103 1.00 19.47  ? 115  PRO C CB  1 
ATOM   4113 C CG  . PRO C 1 134 ? 5.682   33.564 -45.468 1.00 18.67  ? 115  PRO C CG  1 
ATOM   4114 C CD  . PRO C 1 134 ? 6.866   33.981 -46.314 1.00 20.62  ? 115  PRO C CD  1 
ATOM   4115 N N   . SER C 1 135 ? 7.821   30.388 -43.489 1.00 23.98  ? 116  SER C N   1 
ATOM   4116 C CA  . SER C 1 135 ? 7.488   28.964 -43.453 1.00 25.47  ? 116  SER C CA  1 
ATOM   4117 C C   . SER C 1 135 ? 6.058   28.799 -42.918 1.00 22.27  ? 116  SER C C   1 
ATOM   4118 O O   . SER C 1 135 ? 5.712   29.329 -41.863 1.00 21.60  ? 116  SER C O   1 
ATOM   4119 C CB  . SER C 1 135 ? 8.496   28.167 -42.621 1.00 23.30  ? 116  SER C CB  1 
ATOM   4120 O OG  . SER C 1 135 ? 8.220   26.771 -42.692 1.00 22.36  ? 116  SER C OG  1 
ATOM   4121 N N   . ILE C 1 136 ? 5.237   28.051 -43.647 1.00 24.70  ? 117  ILE C N   1 
ATOM   4122 C CA  . ILE C 1 136 ? 3.818   27.929 -43.341 1.00 20.32  ? 117  ILE C CA  1 
ATOM   4123 C C   . ILE C 1 136 ? 3.372   26.473 -43.224 1.00 20.60  ? 117  ILE C C   1 
ATOM   4124 O O   . ILE C 1 136 ? 3.675   25.652 -44.086 1.00 24.03  ? 117  ILE C O   1 
ATOM   4125 C CB  . ILE C 1 136 ? 2.980   28.635 -44.435 1.00 20.96  ? 117  ILE C CB  1 
ATOM   4126 C CG1 . ILE C 1 136 ? 3.252   30.139 -44.409 1.00 19.74  ? 117  ILE C CG1 1 
ATOM   4127 C CG2 . ILE C 1 136 ? 1.492   28.347 -44.273 1.00 21.42  ? 117  ILE C CG2 1 
ATOM   4128 C CD1 . ILE C 1 136 ? 2.619   30.901 -45.565 1.00 24.10  ? 117  ILE C CD1 1 
ATOM   4129 N N   . ARG C 1 137 ? 2.644   26.158 -42.157 1.00 23.63  ? 118  ARG C N   1 
ATOM   4130 C CA  . ARG C 1 137 ? 1.914   24.900 -42.081 1.00 18.96  ? 118  ARG C CA  1 
ATOM   4131 C C   . ARG C 1 137 ? 0.447   25.169 -42.411 1.00 21.03  ? 118  ARG C C   1 
ATOM   4132 O O   . ARG C 1 137 ? -0.164  26.054 -41.819 1.00 25.87  ? 118  ARG C O   1 
ATOM   4133 C CB  . ARG C 1 137 ? 2.040   24.290 -40.685 1.00 17.01  ? 118  ARG C CB  1 
ATOM   4134 C CG  . ARG C 1 137 ? 1.078   23.127 -40.451 1.00 28.41  ? 118  ARG C CG  1 
ATOM   4135 C CD  . ARG C 1 137 ? 1.516   22.222 -39.307 1.00 34.70  ? 118  ARG C CD  1 
ATOM   4136 N NE  . ARG C 1 137 ? 0.656   21.046 -39.166 1.00 36.18  ? 118  ARG C NE  1 
ATOM   4137 C CZ  . ARG C 1 137 ? 0.902   20.023 -38.349 1.00 38.01  ? 118  ARG C CZ  1 
ATOM   4138 N NH1 . ARG C 1 137 ? 1.995   20.007 -37.594 1.00 39.08  ? 118  ARG C NH1 1 
ATOM   4139 N NH2 . ARG C 1 137 ? 0.058   19.005 -38.297 1.00 35.99  ? 118  ARG C NH2 1 
ATOM   4140 N N   . GLN C 1 138 ? -0.118  24.426 -43.363 1.00 23.01  ? 119  GLN C N   1 
ATOM   4141 C CA  . GLN C 1 138 ? -1.525  24.618 -43.749 1.00 28.71  ? 119  GLN C CA  1 
ATOM   4142 C C   . GLN C 1 138 ? -2.207  23.317 -44.185 1.00 27.74  ? 119  GLN C C   1 
ATOM   4143 O O   . GLN C 1 138 ? -1.561  22.430 -44.737 1.00 29.94  ? 119  GLN C O   1 
ATOM   4144 C CB  . GLN C 1 138 ? -1.650  25.687 -44.850 1.00 29.39  ? 119  GLN C CB  1 
ATOM   4145 C CG  . GLN C 1 138 ? -3.050  26.288 -45.012 1.00 21.27  ? 119  GLN C CG  1 
ATOM   4146 C CD  . GLN C 1 138 ? -2.999  27.604 -45.764 1.00 23.24  ? 119  GLN C CD  1 
ATOM   4147 O OE1 . GLN C 1 138 ? -2.030  27.888 -46.480 1.00 22.13  ? 119  GLN C OE1 1 
ATOM   4148 N NE2 . GLN C 1 138 ? -4.024  28.432 -45.582 1.00 28.86  ? 119  GLN C NE2 1 
ATOM   4149 N N   . ARG C 1 139 ? -3.515  23.214 -43.938 1.00 29.38  ? 120  ARG C N   1 
ATOM   4150 C CA  . ARG C 1 139 ? -4.299  22.054 -44.364 1.00 26.39  ? 120  ARG C CA  1 
ATOM   4151 C C   . ARG C 1 139 ? -5.087  22.356 -45.666 1.00 29.78  ? 120  ARG C C   1 
ATOM   4152 O O   . ARG C 1 139 ? -5.713  23.417 -45.803 1.00 26.05  ? 120  ARG C O   1 
ATOM   4153 C CB  . ARG C 1 139 ? -5.220  21.605 -43.226 1.00 24.92  ? 120  ARG C CB  1 
ATOM   4154 C CG  . ARG C 1 139 ? -5.817  20.244 -43.427 1.00 29.81  ? 120  ARG C CG  1 
ATOM   4155 C CD  . ARG C 1 139 ? -6.268  19.560 -42.116 1.00 46.37  ? 120  ARG C CD  1 
ATOM   4156 N NE  . ARG C 1 139 ? -6.683  18.169 -42.386 1.00 53.21  ? 120  ARG C NE  1 
ATOM   4157 C CZ  . ARG C 1 139 ? -5.871  17.109 -42.328 1.00 49.64  ? 120  ARG C CZ  1 
ATOM   4158 N NH1 . ARG C 1 139 ? -4.595  17.257 -41.975 1.00 49.76  ? 120  ARG C NH1 1 
ATOM   4159 N NH2 . ARG C 1 139 ? -6.336  15.896 -42.619 1.00 52.08  ? 120  ARG C NH2 1 
ATOM   4160 N N   . PHE C 1 140 ? -5.040  21.436 -46.631 1.00 32.85  ? 121  PHE C N   1 
ATOM   4161 C CA  . PHE C 1 140 ? -5.716  21.644 -47.922 1.00 27.55  ? 121  PHE C CA  1 
ATOM   4162 C C   . PHE C 1 140 ? -6.695  20.547 -48.294 1.00 30.82  ? 121  PHE C C   1 
ATOM   4163 O O   . PHE C 1 140 ? -6.645  19.430 -47.778 1.00 34.12  ? 121  PHE C O   1 
ATOM   4164 C CB  . PHE C 1 140 ? -4.709  21.745 -49.066 1.00 27.72  ? 121  PHE C CB  1 
ATOM   4165 C CG  . PHE C 1 140 ? -3.753  22.876 -48.930 1.00 27.92  ? 121  PHE C CG  1 
ATOM   4166 C CD1 . PHE C 1 140 ? -2.580  22.725 -48.196 1.00 25.71  ? 121  PHE C CD1 1 
ATOM   4167 C CD2 . PHE C 1 140 ? -4.017  24.092 -49.536 1.00 24.34  ? 121  PHE C CD2 1 
ATOM   4168 C CE1 . PHE C 1 140 ? -1.679  23.779 -48.057 1.00 27.52  ? 121  PHE C CE1 1 
ATOM   4169 C CE2 . PHE C 1 140 ? -3.116  25.158 -49.407 1.00 29.14  ? 121  PHE C CE2 1 
ATOM   4170 C CZ  . PHE C 1 140 ? -1.942  25.000 -48.662 1.00 25.36  ? 121  PHE C CZ  1 
ATOM   4171 N N   . SER C 1 141 ? -7.567  20.872 -49.238 1.00 31.97  ? 122  SER C N   1 
ATOM   4172 C CA  . SER C 1 141 ? -8.499  19.906 -49.798 1.00 29.93  ? 122  SER C CA  1 
ATOM   4173 C C   . SER C 1 141 ? -8.078  19.634 -51.234 1.00 33.58  ? 122  SER C C   1 
ATOM   4174 O O   . SER C 1 141 ? -8.096  20.544 -52.078 1.00 30.21  ? 122  SER C O   1 
ATOM   4175 C CB  . SER C 1 141 ? -9.920  20.464 -49.761 1.00 30.73  ? 122  SER C CB  1 
ATOM   4176 O OG  . SER C 1 141 ? -10.748 19.816 -50.711 1.00 32.30  ? 122  SER C OG  1 
ATOM   4177 N N   . CYS C 1 142 ? -7.686  18.389 -51.509 1.00 40.77  ? 123  CYS C N   1 
ATOM   4178 C CA  . CYS C 1 142 ? -7.217  18.022 -52.846 1.00 42.22  ? 123  CYS C CA  1 
ATOM   4179 C C   . CYS C 1 142 ? -7.328  16.535 -53.120 1.00 36.50  ? 123  CYS C C   1 
ATOM   4180 O O   . CYS C 1 142 ? -7.784  15.782 -52.267 1.00 37.50  ? 123  CYS C O   1 
ATOM   4181 C CB  . CYS C 1 142 ? -5.777  18.491 -53.042 1.00 49.05  ? 123  CYS C CB  1 
ATOM   4182 S SG  . CYS C 1 142 ? -4.656  17.929 -51.738 1.00 67.46  ? 123  CYS C SG  1 
ATOM   4183 N N   . ASP C 1 143 ? -6.904  16.120 -54.314 1.00 40.25  ? 124  ASP C N   1 
ATOM   4184 C CA  . ASP C 1 143 ? -6.984  14.712 -54.712 1.00 41.21  ? 124  ASP C CA  1 
ATOM   4185 C C   . ASP C 1 143 ? -5.850  13.868 -54.108 1.00 41.95  ? 124  ASP C C   1 
ATOM   4186 O O   . ASP C 1 143 ? -4.670  14.043 -54.439 1.00 39.56  ? 124  ASP C O   1 
ATOM   4187 C CB  . ASP C 1 143 ? -6.994  14.580 -56.234 1.00 40.72  ? 124  ASP C CB  1 
ATOM   4188 C CG  . ASP C 1 143 ? -7.544  13.240 -56.705 1.00 48.29  ? 124  ASP C CG  1 
ATOM   4189 O OD1 . ASP C 1 143 ? -8.040  12.459 -55.853 1.00 49.80  ? 124  ASP C OD1 1 
ATOM   4190 O OD2 . ASP C 1 143 ? -7.500  12.982 -57.933 1.00 51.39  ? 124  ASP C OD2 1 
ATOM   4191 N N   . VAL C 1 144 ? -6.230  12.948 -53.225 1.00 37.25  ? 125  VAL C N   1 
ATOM   4192 C CA  . VAL C 1 144 ? -5.282  12.167 -52.448 1.00 32.34  ? 125  VAL C CA  1 
ATOM   4193 C C   . VAL C 1 144 ? -5.208  10.717 -52.944 1.00 35.96  ? 125  VAL C C   1 
ATOM   4194 O O   . VAL C 1 144 ? -4.282  9.973  -52.601 1.00 40.14  ? 125  VAL C O   1 
ATOM   4195 C CB  . VAL C 1 144 ? -5.672  12.223 -50.961 1.00 32.91  ? 125  VAL C CB  1 
ATOM   4196 C CG1 . VAL C 1 144 ? -4.682  11.475 -50.102 1.00 32.65  ? 125  VAL C CG1 1 
ATOM   4197 C CG2 . VAL C 1 144 ? -5.746  13.657 -50.518 1.00 34.05  ? 125  VAL C CG2 1 
ATOM   4198 N N   . SER C 1 145 ? -6.176  10.331 -53.774 1.00 39.01  ? 126  SER C N   1 
ATOM   4199 C CA  . SER C 1 145 ? -6.265  8.961  -54.300 1.00 47.77  ? 126  SER C CA  1 
ATOM   4200 C C   . SER C 1 145 ? -4.962  8.479  -54.953 1.00 36.89  ? 126  SER C C   1 
ATOM   4201 O O   . SER C 1 145 ? -4.363  9.184  -55.771 1.00 40.47  ? 126  SER C O   1 
ATOM   4202 C CB  . SER C 1 145 ? -7.410  8.856  -55.309 1.00 47.40  ? 126  SER C CB  1 
ATOM   4203 O OG  . SER C 1 145 ? -7.175  9.727  -56.402 1.00 46.77  ? 126  SER C OG  1 
ATOM   4204 N N   . GLY C 1 146 ? -4.526  7.283  -54.573 1.00 32.28  ? 127  GLY C N   1 
ATOM   4205 C CA  . GLY C 1 146 ? -3.328  6.698  -55.148 1.00 40.19  ? 127  GLY C CA  1 
ATOM   4206 C C   . GLY C 1 146 ? -2.067  7.084  -54.405 1.00 39.28  ? 127  GLY C C   1 
ATOM   4207 O O   . GLY C 1 146 ? -0.951  6.961  -54.924 1.00 37.74  ? 127  GLY C O   1 
ATOM   4208 N N   . VAL C 1 147 ? -2.247  7.553  -53.178 1.00 35.44  ? 128  VAL C N   1 
ATOM   4209 C CA  . VAL C 1 147 ? -1.116  7.975  -52.370 1.00 34.71  ? 128  VAL C CA  1 
ATOM   4210 C C   . VAL C 1 147 ? -0.267  6.762  -51.978 1.00 43.18  ? 128  VAL C C   1 
ATOM   4211 O O   . VAL C 1 147 ? 0.945   6.876  -51.770 1.00 38.97  ? 128  VAL C O   1 
ATOM   4212 C CB  . VAL C 1 147 ? -1.578  8.791  -51.131 1.00 29.65  ? 128  VAL C CB  1 
ATOM   4213 C CG1 . VAL C 1 147 ? -2.520  7.977  -50.259 1.00 30.18  ? 128  VAL C CG1 1 
ATOM   4214 C CG2 . VAL C 1 147 ? -0.393  9.279  -50.336 1.00 27.32  ? 128  VAL C CG2 1 
ATOM   4215 N N   . ASP C 1 148 ? -0.910  5.594  -51.909 1.00 52.65  ? 129  ASP C N   1 
ATOM   4216 C CA  . ASP C 1 148 ? -0.238  4.351  -51.511 1.00 50.76  ? 129  ASP C CA  1 
ATOM   4217 C C   . ASP C 1 148 ? 0.071   3.457  -52.732 1.00 50.67  ? 129  ASP C C   1 
ATOM   4218 O O   . ASP C 1 148 ? 0.025   2.234  -52.663 1.00 57.11  ? 129  ASP C O   1 
ATOM   4219 C CB  . ASP C 1 148 ? -1.088  3.611  -50.469 1.00 59.23  ? 129  ASP C CB  1 
ATOM   4220 C CG  . ASP C 1 148 ? -0.242  2.888  -49.423 1.00 76.73  ? 129  ASP C CG  1 
ATOM   4221 O OD1 . ASP C 1 148 ? 0.777   2.266  -49.801 1.00 80.15  ? 129  ASP C OD1 1 
ATOM   4222 O OD2 . ASP C 1 148 ? -0.600  2.939  -48.221 1.00 84.99  ? 129  ASP C OD2 1 
ATOM   4223 N N   . THR C 1 149 ? 0.420   4.108  -53.836 1.00 54.10  ? 130  THR C N   1 
ATOM   4224 C CA  . THR C 1 149 ? 0.602   3.495  -55.147 1.00 41.48  ? 130  THR C CA  1 
ATOM   4225 C C   . THR C 1 149 ? 1.964   3.923  -55.693 1.00 47.41  ? 130  THR C C   1 
ATOM   4226 O O   . THR C 1 149 ? 2.508   4.941  -55.273 1.00 53.62  ? 130  THR C O   1 
ATOM   4227 C CB  . THR C 1 149 ? -0.534  3.970  -56.082 1.00 43.91  ? 130  THR C CB  1 
ATOM   4228 O OG1 . THR C 1 149 ? -1.761  3.357  -55.668 1.00 36.35  ? 130  THR C OG1 1 
ATOM   4229 C CG2 . THR C 1 149 ? -0.271  3.651  -57.556 1.00 53.97  ? 130  THR C CG2 1 
ATOM   4230 N N   . GLU C 1 150 ? 2.531   3.155  -56.613 1.00 46.57  ? 131  GLU C N   1 
ATOM   4231 C CA  . GLU C 1 150 ? 3.834   3.493  -57.153 1.00 45.41  ? 131  GLU C CA  1 
ATOM   4232 C C   . GLU C 1 150 ? 3.823   4.807  -57.943 1.00 44.74  ? 131  GLU C C   1 
ATOM   4233 O O   . GLU C 1 150 ? 4.837   5.496  -58.006 1.00 43.64  ? 131  GLU C O   1 
ATOM   4234 C CB  . GLU C 1 150 ? 4.343   2.350  -58.020 1.00 54.10  ? 131  GLU C CB  1 
ATOM   4235 C CG  . GLU C 1 150 ? 5.821   2.413  -58.329 1.00 62.96  ? 131  GLU C CG  1 
ATOM   4236 C CD  . GLU C 1 150 ? 6.177   1.551  -59.521 1.00 72.17  ? 131  GLU C CD  1 
ATOM   4237 O OE1 . GLU C 1 150 ? 5.367   1.519  -60.477 1.00 64.06  ? 131  GLU C OE1 1 
ATOM   4238 O OE2 . GLU C 1 150 ? 7.248   0.900  -59.497 1.00 87.99  ? 131  GLU C OE2 1 
ATOM   4239 N N   . SER C 1 151 ? 2.681   5.157  -58.533 1.00 45.08  ? 132  SER C N   1 
ATOM   4240 C CA  . SER C 1 151 ? 2.560   6.401  -59.316 1.00 47.50  ? 132  SER C CA  1 
ATOM   4241 C C   . SER C 1 151 ? 2.138   7.652  -58.506 1.00 46.10  ? 132  SER C C   1 
ATOM   4242 O O   . SER C 1 151 ? 2.230   8.781  -58.995 1.00 39.79  ? 132  SER C O   1 
ATOM   4243 C CB  . SER C 1 151 ? 1.601   6.190  -60.488 1.00 49.49  ? 132  SER C CB  1 
ATOM   4244 O OG  . SER C 1 151 ? 0.376   5.647  -60.036 1.00 61.30  ? 132  SER C OG  1 
ATOM   4245 N N   . GLY C 1 152 ? 1.651   7.439  -57.285 1.00 49.14  ? 133  GLY C N   1 
ATOM   4246 C CA  . GLY C 1 152 ? 1.407   8.522  -56.348 1.00 40.37  ? 133  GLY C CA  1 
ATOM   4247 C C   . GLY C 1 152 ? 0.115   9.302  -56.535 1.00 38.77  ? 133  GLY C C   1 
ATOM   4248 O O   . GLY C 1 152 ? -0.619  9.095  -57.502 1.00 45.94  ? 133  GLY C O   1 
ATOM   4249 N N   . ALA C 1 153 ? -0.168  10.200 -55.591 1.00 38.76  ? 134  ALA C N   1 
ATOM   4250 C CA  . ALA C 1 153 ? -1.268  11.160 -55.731 1.00 39.27  ? 134  ALA C CA  1 
ATOM   4251 C C   . ALA C 1 153 ? -0.760  12.473 -56.322 1.00 38.87  ? 134  ALA C C   1 
ATOM   4252 O O   . ALA C 1 153 ? 0.423   12.819 -56.189 1.00 40.08  ? 134  ALA C O   1 
ATOM   4253 C CB  . ALA C 1 153 ? -1.913  11.424 -54.386 1.00 34.35  ? 134  ALA C CB  1 
ATOM   4254 N N   . THR C 1 154 ? -1.648  13.214 -56.972 1.00 36.48  ? 135  THR C N   1 
ATOM   4255 C CA  . THR C 1 154 ? -1.279  14.561 -57.406 1.00 41.44  ? 135  THR C CA  1 
ATOM   4256 C C   . THR C 1 154 ? -2.223  15.593 -56.820 1.00 36.34  ? 135  THR C C   1 
ATOM   4257 O O   . THR C 1 154 ? -3.381  15.693 -57.226 1.00 37.83  ? 135  THR C O   1 
ATOM   4258 C CB  . THR C 1 154 ? -1.217  14.716 -58.944 1.00 43.90  ? 135  THR C CB  1 
ATOM   4259 O OG1 . THR C 1 154 ? -0.448  13.644 -59.510 1.00 45.05  ? 135  THR C OG1 1 
ATOM   4260 C CG2 . THR C 1 154 ? -0.574  16.050 -59.311 1.00 32.54  ? 135  THR C CG2 1 
ATOM   4261 N N   . CYS C 1 155 ? -1.706  16.348 -55.858 1.00 38.30  ? 136  CYS C N   1 
ATOM   4262 C CA  . CYS C 1 155 ? -2.463  17.387 -55.179 1.00 44.40  ? 136  CYS C CA  1 
ATOM   4263 C C   . CYS C 1 155 ? -2.131  18.750 -55.788 1.00 39.35  ? 136  CYS C C   1 
ATOM   4264 O O   . CYS C 1 155 ? -0.953  19.064 -55.932 1.00 41.37  ? 136  CYS C O   1 
ATOM   4265 C CB  . CYS C 1 155 ? -2.097  17.377 -53.691 1.00 47.69  ? 136  CYS C CB  1 
ATOM   4266 S SG  . CYS C 1 155 ? -2.978  18.624 -52.687 1.00 86.00  ? 136  CYS C SG  1 
ATOM   4267 N N   . ARG C 1 156 ? -3.148  19.542 -56.157 1.00 41.51  ? 137  ARG C N   1 
ATOM   4268 C CA  . ARG C 1 156 ? -2.929  20.896 -56.703 1.00 34.53  ? 137  ARG C CA  1 
ATOM   4269 C C   . ARG C 1 156 ? -3.262  21.970 -55.679 1.00 33.18  ? 137  ARG C C   1 
ATOM   4270 O O   . ARG C 1 156 ? -4.289  21.890 -55.012 1.00 42.54  ? 137  ARG C O   1 
ATOM   4271 C CB  . ARG C 1 156 ? -3.762  21.150 -57.971 1.00 35.54  ? 137  ARG C CB  1 
ATOM   4272 C CG  . ARG C 1 156 ? -3.817  19.983 -58.976 1.00 52.48  ? 137  ARG C CG  1 
ATOM   4273 C CD  . ARG C 1 156 ? -4.609  20.347 -60.267 1.00 56.53  ? 137  ARG C CD  1 
ATOM   4274 N NE  . ARG C 1 156 ? -5.772  21.211 -60.021 1.00 67.85  ? 137  ARG C NE  1 
ATOM   4275 C CZ  . ARG C 1 156 ? -7.013  20.777 -59.769 1.00 69.98  ? 137  ARG C CZ  1 
ATOM   4276 N NH1 . ARG C 1 156 ? -7.273  19.475 -59.730 1.00 51.09  ? 137  ARG C NH1 1 
ATOM   4277 N NH2 . ARG C 1 156 ? -8.003  21.646 -59.552 1.00 60.73  ? 137  ARG C NH2 1 
ATOM   4278 N N   . ILE C 1 157 ? -2.402  22.981 -55.563 1.00 34.19  ? 138  ILE C N   1 
ATOM   4279 C CA  . ILE C 1 157 ? -2.663  24.130 -54.687 1.00 27.81  ? 138  ILE C CA  1 
ATOM   4280 C C   . ILE C 1 157 ? -2.764  25.411 -55.497 1.00 24.52  ? 138  ILE C C   1 
ATOM   4281 O O   . ILE C 1 157 ? -1.849  25.766 -56.238 1.00 25.21  ? 138  ILE C O   1 
ATOM   4282 C CB  . ILE C 1 157 ? -1.561  24.300 -53.638 1.00 23.53  ? 138  ILE C CB  1 
ATOM   4283 C CG1 . ILE C 1 157 ? -1.484  23.062 -52.754 1.00 26.01  ? 138  ILE C CG1 1 
ATOM   4284 C CG2 . ILE C 1 157 ? -1.806  25.533 -52.801 1.00 20.50  ? 138  ILE C CG2 1 
ATOM   4285 C CD1 . ILE C 1 157 ? -0.583  23.234 -51.568 1.00 23.43  ? 138  ILE C CD1 1 
ATOM   4286 N N   . LYS C 1 158 ? -3.880  26.107 -55.348 1.00 25.54  ? 139  LYS C N   1 
ATOM   4287 C CA  . LYS C 1 158 ? -4.148  27.300 -56.141 1.00 28.24  ? 139  LYS C CA  1 
ATOM   4288 C C   . LYS C 1 158 ? -3.948  28.567 -55.288 1.00 27.46  ? 139  LYS C C   1 
ATOM   4289 O O   . LYS C 1 158 ? -4.629  28.763 -54.280 1.00 27.68  ? 139  LYS C O   1 
ATOM   4290 C CB  . LYS C 1 158 ? -5.569  27.223 -56.716 1.00 22.87  ? 139  LYS C CB  1 
ATOM   4291 C CG  . LYS C 1 158 ? -6.015  28.455 -57.483 1.00 28.85  ? 139  LYS C CG  1 
ATOM   4292 C CD  . LYS C 1 158 ? -7.534  28.435 -57.712 1.00 24.73  ? 139  LYS C CD  1 
ATOM   4293 C CE  . LYS C 1 158 ? -8.069  29.816 -58.086 1.00 24.51  ? 139  LYS C CE  1 
ATOM   4294 N NZ  . LYS C 1 158 ? -9.496  29.757 -58.501 1.00 25.94  ? 139  LYS C NZ  1 
ATOM   4295 N N   . ILE C 1 159 ? -3.006  29.417 -55.690 1.00 28.12  ? 140  ILE C N   1 
ATOM   4296 C CA  . ILE C 1 159 ? -2.662  30.619 -54.932 1.00 22.94  ? 140  ILE C CA  1 
ATOM   4297 C C   . ILE C 1 159 ? -2.756  31.875 -55.785 1.00 25.61  ? 140  ILE C C   1 
ATOM   4298 O O   . ILE C 1 159 ? -2.185  31.940 -56.873 1.00 28.69  ? 140  ILE C O   1 
ATOM   4299 C CB  . ILE C 1 159 ? -1.231  30.519 -54.397 1.00 25.52  ? 140  ILE C CB  1 
ATOM   4300 C CG1 . ILE C 1 159 ? -1.118  29.336 -53.426 1.00 26.84  ? 140  ILE C CG1 1 
ATOM   4301 C CG2 . ILE C 1 159 ? -0.814  31.826 -53.734 1.00 24.51  ? 140  ILE C CG2 1 
ATOM   4302 C CD1 . ILE C 1 159 ? 0.231   29.217 -52.738 1.00 27.66  ? 140  ILE C CD1 1 
ATOM   4303 N N   . GLY C 1 160 ? -3.467  32.886 -55.297 1.00 28.98  ? 141  GLY C N   1 
ATOM   4304 C CA  . GLY C 1 160 ? -3.600  34.129 -56.050 1.00 31.90  ? 141  GLY C CA  1 
ATOM   4305 C C   . GLY C 1 160 ? -3.994  35.329 -55.215 1.00 23.08  ? 141  GLY C C   1 
ATOM   4306 O O   . GLY C 1 160 ? -4.260  35.199 -54.027 1.00 24.52  ? 141  GLY C O   1 
ATOM   4307 N N   . SER C 1 161 ? -4.021  36.507 -55.827 1.00 29.16  ? 142  SER C N   1 
ATOM   4308 C CA  . SER C 1 161 ? -4.524  37.694 -55.131 1.00 24.43  ? 142  SER C CA  1 
ATOM   4309 C C   . SER C 1 161 ? -6.024  37.608 -54.845 1.00 22.67  ? 142  SER C C   1 
ATOM   4310 O O   . SER C 1 161 ? -6.815  37.227 -55.708 1.00 28.02  ? 142  SER C O   1 
ATOM   4311 C CB  . SER C 1 161 ? -4.271  38.942 -55.944 1.00 20.94  ? 142  SER C CB  1 
ATOM   4312 O OG  . SER C 1 161 ? -4.889  40.023 -55.279 1.00 25.94  ? 142  SER C OG  1 
ATOM   4313 N N   . TRP C 1 162 ? -6.421  37.986 -53.638 1.00 22.05  ? 143  TRP C N   1 
ATOM   4314 C CA  . TRP C 1 162 ? -7.809  37.829 -53.233 1.00 20.44  ? 143  TRP C CA  1 
ATOM   4315 C C   . TRP C 1 162 ? -8.685  38.985 -53.712 1.00 23.60  ? 143  TRP C C   1 
ATOM   4316 O O   . TRP C 1 162 ? -9.846  38.778 -54.056 1.00 24.90  ? 143  TRP C O   1 
ATOM   4317 C CB  . TRP C 1 162 ? -7.919  37.670 -51.707 1.00 20.05  ? 143  TRP C CB  1 
ATOM   4318 C CG  . TRP C 1 162 ? -9.262  37.149 -51.270 1.00 19.78  ? 143  TRP C CG  1 
ATOM   4319 C CD1 . TRP C 1 162 ? -10.268 37.854 -50.654 1.00 21.50  ? 143  TRP C CD1 1 
ATOM   4320 C CD2 . TRP C 1 162 ? -9.756  35.822 -51.440 1.00 19.02  ? 143  TRP C CD2 1 
ATOM   4321 N NE1 . TRP C 1 162 ? -11.351 37.038 -50.435 1.00 18.70  ? 143  TRP C NE1 1 
ATOM   4322 C CE2 . TRP C 1 162 ? -11.059 35.777 -50.906 1.00 17.77  ? 143  TRP C CE2 1 
ATOM   4323 C CE3 . TRP C 1 162 ? -9.226  34.655 -52.005 1.00 21.68  ? 143  TRP C CE3 1 
ATOM   4324 C CZ2 . TRP C 1 162 ? -11.835 34.630 -50.912 1.00 20.86  ? 143  TRP C CZ2 1 
ATOM   4325 C CZ3 . TRP C 1 162 ? -9.992  33.510 -52.008 1.00 18.99  ? 143  TRP C CZ3 1 
ATOM   4326 C CH2 . TRP C 1 162 ? -11.283 33.504 -51.469 1.00 20.51  ? 143  TRP C CH2 1 
ATOM   4327 N N   . THR C 1 163 ? -8.136  40.199 -53.727 1.00 23.23  ? 144  THR C N   1 
ATOM   4328 C CA  . THR C 1 163 ? -8.931  41.378 -54.081 1.00 22.69  ? 144  THR C CA  1 
ATOM   4329 C C   . THR C 1 163 ? -8.415  42.186 -55.272 1.00 24.47  ? 144  THR C C   1 
ATOM   4330 O O   . THR C 1 163 ? -9.073  43.131 -55.701 1.00 36.75  ? 144  THR C O   1 
ATOM   4331 C CB  . THR C 1 163 ? -9.094  42.367 -52.902 1.00 22.35  ? 144  THR C CB  1 
ATOM   4332 O OG1 . THR C 1 163 ? -7.844  43.020 -52.639 1.00 21.32  ? 144  THR C OG1 1 
ATOM   4333 C CG2 . THR C 1 163 ? -9.617  41.661 -51.661 1.00 20.05  ? 144  THR C CG2 1 
ATOM   4334 N N   . HIS C 1 164 ? -7.246  41.859 -55.794 1.00 19.82  ? 145  HIS C N   1 
ATOM   4335 C CA  . HIS C 1 164 ? -6.699  42.654 -56.889 1.00 20.86  ? 145  HIS C CA  1 
ATOM   4336 C C   . HIS C 1 164 ? -6.754  41.898 -58.210 1.00 25.21  ? 145  HIS C C   1 
ATOM   4337 O O   . HIS C 1 164 ? -6.231  40.791 -58.315 1.00 27.93  ? 145  HIS C O   1 
ATOM   4338 C CB  . HIS C 1 164 ? -5.258  43.097 -56.586 1.00 21.45  ? 145  HIS C CB  1 
ATOM   4339 C CG  . HIS C 1 164 ? -5.145  44.077 -55.455 1.00 26.25  ? 145  HIS C CG  1 
ATOM   4340 N ND1 . HIS C 1 164 ? -5.574  45.381 -55.555 1.00 29.74  ? 145  HIS C ND1 1 
ATOM   4341 C CD2 . HIS C 1 164 ? -4.640  43.940 -54.199 1.00 23.52  ? 145  HIS C CD2 1 
ATOM   4342 C CE1 . HIS C 1 164 ? -5.341  46.013 -54.412 1.00 24.45  ? 145  HIS C CE1 1 
ATOM   4343 N NE2 . HIS C 1 164 ? -4.779  45.155 -53.577 1.00 24.82  ? 145  HIS C NE2 1 
ATOM   4344 N N   . HIS C 1 165 ? -7.377  42.491 -59.227 1.00 32.66  ? 146  HIS C N   1 
ATOM   4345 C CA  . HIS C 1 165 ? -7.444  41.847 -60.548 1.00 32.47  ? 146  HIS C CA  1 
ATOM   4346 C C   . HIS C 1 165 ? -6.140  41.957 -61.372 1.00 29.68  ? 146  HIS C C   1 
ATOM   4347 O O   . HIS C 1 165 ? -5.142  42.505 -60.915 1.00 28.24  ? 146  HIS C O   1 
ATOM   4348 C CB  . HIS C 1 165 ? -8.655  42.338 -61.343 1.00 35.48  ? 146  HIS C CB  1 
ATOM   4349 C CG  . HIS C 1 165 ? -8.629  43.808 -61.629 1.00 41.96  ? 146  HIS C CG  1 
ATOM   4350 N ND1 . HIS C 1 165 ? -7.661  44.396 -62.399 1.00 43.41  ? 146  HIS C ND1 1 
ATOM   4351 C CD2 . HIS C 1 165 ? -9.470  44.804 -61.234 1.00 39.30  ? 146  HIS C CD2 1 
ATOM   4352 C CE1 . HIS C 1 165 ? -7.891  45.705 -62.470 1.00 45.43  ? 146  HIS C CE1 1 
ATOM   4353 N NE2 . HIS C 1 165 ? -8.983  45.965 -61.779 1.00 41.66  ? 146  HIS C NE2 1 
ATOM   4354 N N   . SER C 1 166 ? -6.167  41.436 -62.593 1.00 31.63  ? 147  SER C N   1 
ATOM   4355 C CA  . SER C 1 166 ? -4.948  41.179 -63.364 1.00 35.96  ? 147  SER C CA  1 
ATOM   4356 C C   . SER C 1 166 ? -4.183  42.421 -63.806 1.00 36.38  ? 147  SER C C   1 
ATOM   4357 O O   . SER C 1 166 ? -3.016  42.312 -64.188 1.00 32.17  ? 147  SER C O   1 
ATOM   4358 C CB  . SER C 1 166 ? -5.279  40.361 -64.601 1.00 34.62  ? 147  SER C CB  1 
ATOM   4359 O OG  . SER C 1 166 ? -6.146  41.107 -65.432 1.00 38.52  ? 147  SER C OG  1 
ATOM   4360 N N   . ARG C 1 167 ? -4.842  43.580 -63.781 1.00 36.03  ? 148  ARG C N   1 
ATOM   4361 C CA  . ARG C 1 167 ? -4.187  44.837 -64.153 1.00 38.68  ? 148  ARG C CA  1 
ATOM   4362 C C   . ARG C 1 167 ? -3.524  45.533 -62.952 1.00 41.20  ? 148  ARG C C   1 
ATOM   4363 O O   . ARG C 1 167 ? -2.789  46.514 -63.117 1.00 39.66  ? 148  ARG C O   1 
ATOM   4364 C CB  . ARG C 1 167 ? -5.168  45.791 -64.842 1.00 43.33  ? 148  ARG C CB  1 
ATOM   4365 C CG  . ARG C 1 167 ? -5.683  45.328 -66.188 1.00 51.22  ? 148  ARG C CG  1 
ATOM   4366 C CD  . ARG C 1 167 ? -6.580  46.399 -66.836 1.00 76.04  ? 148  ARG C CD  1 
ATOM   4367 N NE  . ARG C 1 167 ? -7.030  47.421 -65.883 1.00 78.11  ? 148  ARG C NE  1 
ATOM   4368 C CZ  . ARG C 1 167 ? -8.274  47.897 -65.809 1.00 83.42  ? 148  ARG C CZ  1 
ATOM   4369 N NH1 . ARG C 1 167 ? -9.219  47.445 -66.631 1.00 83.32  ? 148  ARG C NH1 1 
ATOM   4370 N NH2 . ARG C 1 167 ? -8.577  48.825 -64.905 1.00 77.13  ? 148  ARG C NH2 1 
ATOM   4371 N N   . GLU C 1 168 ? -3.794  45.017 -61.752 1.00 34.44  ? 149  GLU C N   1 
ATOM   4372 C CA  . GLU C 1 168 ? -3.211  45.558 -60.529 1.00 33.62  ? 149  GLU C CA  1 
ATOM   4373 C C   . GLU C 1 168 ? -2.105  44.640 -59.984 1.00 33.97  ? 149  GLU C C   1 
ATOM   4374 O O   . GLU C 1 168 ? -1.024  45.112 -59.618 1.00 33.01  ? 149  GLU C O   1 
ATOM   4375 C CB  . GLU C 1 168 ? -4.300  45.840 -59.472 1.00 32.08  ? 149  GLU C CB  1 
ATOM   4376 C CG  . GLU C 1 168 ? -5.297  46.923 -59.870 1.00 35.77  ? 149  GLU C CG  1 
ATOM   4377 C CD  . GLU C 1 168 ? -6.488  47.036 -58.915 1.00 45.07  ? 149  GLU C CD  1 
ATOM   4378 O OE1 . GLU C 1 168 ? -6.928  45.996 -58.354 1.00 38.66  ? 149  GLU C OE1 1 
ATOM   4379 O OE2 . GLU C 1 168 ? -6.990  48.176 -58.739 1.00 55.94  ? 149  GLU C OE2 1 
ATOM   4380 N N   . ILE C 1 169 ? -2.386  43.336 -59.928 1.00 30.78  ? 150  ILE C N   1 
ATOM   4381 C CA  . ILE C 1 169 ? -1.401  42.331 -59.528 1.00 29.36  ? 150  ILE C CA  1 
ATOM   4382 C C   . ILE C 1 169 ? -1.390  41.190 -60.534 1.00 29.07  ? 150  ILE C C   1 
ATOM   4383 O O   . ILE C 1 169 ? -2.438  40.626 -60.865 1.00 26.14  ? 150  ILE C O   1 
ATOM   4384 C CB  . ILE C 1 169 ? -1.674  41.754 -58.109 1.00 23.43  ? 150  ILE C CB  1 
ATOM   4385 C CG1 . ILE C 1 169 ? -1.365  42.806 -57.043 1.00 28.65  ? 150  ILE C CG1 1 
ATOM   4386 C CG2 . ILE C 1 169 ? -0.837  40.494 -57.856 1.00 20.06  ? 150  ILE C CG2 1 
ATOM   4387 C CD1 . ILE C 1 169 ? -1.558  42.331 -55.600 1.00 28.45  ? 150  ILE C CD1 1 
ATOM   4388 N N   . SER C 1 170 ? -0.203  40.862 -61.027 1.00 31.07  ? 151  SER C N   1 
ATOM   4389 C CA  . SER C 1 170 ? -0.009  39.636 -61.791 1.00 32.01  ? 151  SER C CA  1 
ATOM   4390 C C   . SER C 1 170 ? 0.885   38.678 -60.994 1.00 37.13  ? 151  SER C C   1 
ATOM   4391 O O   . SER C 1 170 ? 1.926   39.091 -60.453 1.00 36.98  ? 151  SER C O   1 
ATOM   4392 C CB  . SER C 1 170 ? 0.614   39.943 -63.153 1.00 35.04  ? 151  SER C CB  1 
ATOM   4393 O OG  . SER C 1 170 ? 1.964   40.354 -63.016 1.00 31.11  ? 151  SER C OG  1 
ATOM   4394 N N   . VAL C 1 171 ? 0.474   37.411 -60.908 1.00 34.22  ? 152  VAL C N   1 
ATOM   4395 C CA  . VAL C 1 171 ? 1.295   36.378 -60.272 1.00 32.61  ? 152  VAL C CA  1 
ATOM   4396 C C   . VAL C 1 171 ? 1.877   35.463 -61.321 1.00 36.23  ? 152  VAL C C   1 
ATOM   4397 O O   . VAL C 1 171 ? 1.198   35.101 -62.272 1.00 39.29  ? 152  VAL C O   1 
ATOM   4398 C CB  . VAL C 1 171 ? 0.501   35.516 -59.291 1.00 35.70  ? 152  VAL C CB  1 
ATOM   4399 C CG1 . VAL C 1 171 ? 0.332   36.233 -57.965 1.00 39.02  ? 152  VAL C CG1 1 
ATOM   4400 C CG2 . VAL C 1 171 ? -0.844  35.172 -59.885 1.00 42.70  ? 152  VAL C CG2 1 
ATOM   4401 N N   . ASP C 1 172 ? 3.141   35.095 -61.139 1.00 42.43  ? 153  ASP C N   1 
ATOM   4402 C CA  . ASP C 1 172 ? 3.871   34.273 -62.097 1.00 38.07  ? 153  ASP C CA  1 
ATOM   4403 C C   . ASP C 1 172 ? 4.763   33.297 -61.336 1.00 42.89  ? 153  ASP C C   1 
ATOM   4404 O O   . ASP C 1 172 ? 5.297   33.629 -60.278 1.00 46.29  ? 153  ASP C O   1 
ATOM   4405 C CB  . ASP C 1 172 ? 4.733   35.154 -63.009 1.00 43.85  ? 153  ASP C CB  1 
ATOM   4406 C CG  . ASP C 1 172 ? 4.040   36.475 -63.390 1.00 65.31  ? 153  ASP C CG  1 
ATOM   4407 O OD1 . ASP C 1 172 ? 3.179   36.441 -64.310 1.00 57.50  ? 153  ASP C OD1 1 
ATOM   4408 O OD2 . ASP C 1 172 ? 4.353   37.539 -62.769 1.00 62.49  ? 153  ASP C OD2 1 
ATOM   4409 N N   . PRO C 1 173 ? 4.924   32.079 -61.865 1.00 41.74  ? 154  PRO C N   1 
ATOM   4410 C CA  . PRO C 1 173 ? 5.849   31.093 -61.296 1.00 34.82  ? 154  PRO C CA  1 
ATOM   4411 C C   . PRO C 1 173 ? 7.286   31.539 -61.502 1.00 42.81  ? 154  PRO C C   1 
ATOM   4412 O O   . PRO C 1 173 ? 7.546   32.332 -62.408 1.00 45.54  ? 154  PRO C O   1 
ATOM   4413 C CB  . PRO C 1 173 ? 5.593   29.856 -62.144 1.00 38.84  ? 154  PRO C CB  1 
ATOM   4414 C CG  . PRO C 1 173 ? 4.242   30.087 -62.764 1.00 39.30  ? 154  PRO C CG  1 
ATOM   4415 C CD  . PRO C 1 173 ? 4.175   31.541 -63.009 1.00 36.64  ? 154  PRO C CD  1 
ATOM   4416 N N   . THR C 1 174 ? 8.207   31.034 -60.687 1.00 51.57  ? 155  THR C N   1 
ATOM   4417 C CA  . THR C 1 174 ? 9.619   31.425 -60.779 1.00 50.72  ? 155  THR C CA  1 
ATOM   4418 C C   . THR C 1 174 ? 10.387  30.671 -61.861 1.00 48.78  ? 155  THR C C   1 
ATOM   4419 O O   . THR C 1 174 ? 10.204  29.470 -62.045 1.00 48.90  ? 155  THR C O   1 
ATOM   4420 C CB  . THR C 1 174 ? 10.329  31.230 -59.439 1.00 47.74  ? 155  THR C CB  1 
ATOM   4421 O OG1 . THR C 1 174 ? 9.814   32.179 -58.497 1.00 45.32  ? 155  THR C OG1 1 
ATOM   4422 C CG2 . THR C 1 174 ? 11.826  31.433 -59.600 1.00 57.46  ? 155  THR C CG2 1 
ATOM   4423 N N   . SER C 1 181 ? 12.601  18.309 -53.881 1.00 38.05  ? 162  SER C N   1 
ATOM   4424 C CA  . SER C 1 181 ? 12.978  17.642 -52.634 1.00 51.77  ? 162  SER C CA  1 
ATOM   4425 C C   . SER C 1 181 ? 14.167  18.332 -51.980 1.00 55.15  ? 162  SER C C   1 
ATOM   4426 O O   . SER C 1 181 ? 14.706  17.835 -50.981 1.00 62.96  ? 162  SER C O   1 
ATOM   4427 C CB  . SER C 1 181 ? 13.324  16.152 -52.866 1.00 58.00  ? 162  SER C CB  1 
ATOM   4428 O OG  . SER C 1 181 ? 12.166  15.329 -53.013 1.00 64.20  ? 162  SER C OG  1 
ATOM   4429 N N   . GLU C 1 182 ? 14.580  19.465 -52.545 1.00 38.68  ? 163  GLU C N   1 
ATOM   4430 C CA  . GLU C 1 182 ? 15.813  20.112 -52.115 1.00 40.98  ? 163  GLU C CA  1 
ATOM   4431 C C   . GLU C 1 182 ? 15.853  20.392 -50.605 1.00 45.38  ? 163  GLU C C   1 
ATOM   4432 O O   . GLU C 1 182 ? 16.887  20.233 -49.959 1.00 45.31  ? 163  GLU C O   1 
ATOM   4433 C CB  . GLU C 1 182 ? 16.052  21.398 -52.908 1.00 48.59  ? 163  GLU C CB  1 
ATOM   4434 C CG  . GLU C 1 182 ? 17.443  21.975 -52.692 1.00 52.52  ? 163  GLU C CG  1 
ATOM   4435 C CD  . GLU C 1 182 ? 17.644  23.320 -53.377 1.00 72.18  ? 163  GLU C CD  1 
ATOM   4436 O OE1 . GLU C 1 182 ? 16.716  23.797 -54.086 1.00 72.39  ? 163  GLU C OE1 1 
ATOM   4437 O OE2 . GLU C 1 182 ? 18.742  23.900 -53.196 1.00 70.38  ? 163  GLU C OE2 1 
ATOM   4438 N N   . TYR C 1 183 ? 14.720  20.795 -50.042 1.00 41.26  ? 164  TYR C N   1 
ATOM   4439 C CA  . TYR C 1 183 ? 14.653  21.023 -48.614 1.00 34.42  ? 164  TYR C CA  1 
ATOM   4440 C C   . TYR C 1 183 ? 13.657  20.092 -47.955 1.00 36.80  ? 164  TYR C C   1 
ATOM   4441 O O   . TYR C 1 183 ? 13.306  20.282 -46.788 1.00 35.79  ? 164  TYR C O   1 
ATOM   4442 C CB  . TYR C 1 183 ? 14.258  22.462 -48.316 1.00 41.75  ? 164  TYR C CB  1 
ATOM   4443 C CG  . TYR C 1 183 ? 15.106  23.490 -49.020 1.00 50.71  ? 164  TYR C CG  1 
ATOM   4444 C CD1 . TYR C 1 183 ? 16.469  23.588 -48.761 1.00 46.13  ? 164  TYR C CD1 1 
ATOM   4445 C CD2 . TYR C 1 183 ? 14.538  24.374 -49.942 1.00 53.32  ? 164  TYR C CD2 1 
ATOM   4446 C CE1 . TYR C 1 183 ? 17.250  24.534 -49.404 1.00 54.84  ? 164  TYR C CE1 1 
ATOM   4447 C CE2 . TYR C 1 183 ? 15.304  25.320 -50.598 1.00 54.40  ? 164  TYR C CE2 1 
ATOM   4448 C CZ  . TYR C 1 183 ? 16.664  25.403 -50.325 1.00 61.57  ? 164  TYR C CZ  1 
ATOM   4449 O OH  . TYR C 1 183 ? 17.442  26.350 -50.970 1.00 58.58  ? 164  TYR C OH  1 
ATOM   4450 N N   . PHE C 1 184 ? 13.193  19.094 -48.700 1.00 36.99  ? 165  PHE C N   1 
ATOM   4451 C CA  . PHE C 1 184 ? 12.196  18.168 -48.169 1.00 38.24  ? 165  PHE C CA  1 
ATOM   4452 C C   . PHE C 1 184 ? 12.789  17.248 -47.103 1.00 39.51  ? 165  PHE C C   1 
ATOM   4453 O O   . PHE C 1 184 ? 13.908  16.757 -47.244 1.00 42.84  ? 165  PHE C O   1 
ATOM   4454 C CB  . PHE C 1 184 ? 11.546  17.341 -49.272 1.00 34.40  ? 165  PHE C CB  1 
ATOM   4455 C CG  . PHE C 1 184 ? 10.280  16.658 -48.836 1.00 31.34  ? 165  PHE C CG  1 
ATOM   4456 C CD1 . PHE C 1 184 ? 9.137   17.400 -48.560 1.00 27.11  ? 165  PHE C CD1 1 
ATOM   4457 C CD2 . PHE C 1 184 ? 10.225  15.279 -48.703 1.00 35.40  ? 165  PHE C CD2 1 
ATOM   4458 C CE1 . PHE C 1 184 ? 7.954   16.772 -48.157 1.00 27.10  ? 165  PHE C CE1 1 
ATOM   4459 C CE2 . PHE C 1 184 ? 9.045   14.637 -48.308 1.00 33.59  ? 165  PHE C CE2 1 
ATOM   4460 C CZ  . PHE C 1 184 ? 7.907   15.387 -48.034 1.00 28.84  ? 165  PHE C CZ  1 
ATOM   4461 N N   . SER C 1 185 ? 12.029  17.029 -46.035 1.00 35.26  ? 166  SER C N   1 
ATOM   4462 C CA  . SER C 1 185 ? 12.492  16.242 -44.901 1.00 37.92  ? 166  SER C CA  1 
ATOM   4463 C C   . SER C 1 185 ? 12.669  14.758 -45.249 1.00 44.01  ? 166  SER C C   1 
ATOM   4464 O O   . SER C 1 185 ? 11.744  14.102 -45.766 1.00 40.80  ? 166  SER C O   1 
ATOM   4465 C CB  . SER C 1 185 ? 11.509  16.377 -43.736 1.00 30.83  ? 166  SER C CB  1 
ATOM   4466 O OG  . SER C 1 185 ? 11.951  15.630 -42.620 1.00 31.12  ? 166  SER C OG  1 
ATOM   4467 N N   . GLN C 1 186 ? 13.855  14.229 -44.950 1.00 40.14  ? 167  GLN C N   1 
ATOM   4468 C CA  . GLN C 1 186 ? 14.110  12.797 -45.107 1.00 40.04  ? 167  GLN C CA  1 
ATOM   4469 C C   . GLN C 1 186 ? 13.283  11.959 -44.128 1.00 40.87  ? 167  GLN C C   1 
ATOM   4470 O O   . GLN C 1 186 ? 13.082  10.768 -44.343 1.00 38.86  ? 167  GLN C O   1 
ATOM   4471 C CB  . GLN C 1 186 ? 15.591  12.494 -44.921 1.00 32.25  ? 167  GLN C CB  1 
ATOM   4472 C CG  . GLN C 1 186 ? 16.213  13.315 -43.814 1.00 43.74  ? 167  GLN C CG  1 
ATOM   4473 C CD  . GLN C 1 186 ? 17.656  12.920 -43.499 1.00 56.54  ? 167  GLN C CD  1 
ATOM   4474 O OE1 . GLN C 1 186 ? 18.048  11.749 -43.634 1.00 51.77  ? 167  GLN C OE1 1 
ATOM   4475 N NE2 . GLN C 1 186 ? 18.455  13.904 -43.065 1.00 57.54  ? 167  GLN C NE2 1 
ATOM   4476 N N   . TYR C 1 187 ? 12.787  12.583 -43.062 1.00 42.68  ? 168  TYR C N   1 
ATOM   4477 C CA  . TYR C 1 187 ? 12.078  11.832 -42.021 1.00 37.20  ? 168  TYR C CA  1 
ATOM   4478 C C   . TYR C 1 187 ? 10.557  11.773 -42.194 1.00 38.52  ? 168  TYR C C   1 
ATOM   4479 O O   . TYR C 1 187 ? 9.880   11.073 -41.442 1.00 36.67  ? 168  TYR C O   1 
ATOM   4480 C CB  . TYR C 1 187 ? 12.469  12.327 -40.624 1.00 35.53  ? 168  TYR C CB  1 
ATOM   4481 C CG  . TYR C 1 187 ? 13.965  12.310 -40.403 1.00 35.15  ? 168  TYR C CG  1 
ATOM   4482 C CD1 . TYR C 1 187 ? 14.667  11.120 -40.424 1.00 37.38  ? 168  TYR C CD1 1 
ATOM   4483 C CD2 . TYR C 1 187 ? 14.676  13.479 -40.192 1.00 35.19  ? 168  TYR C CD2 1 
ATOM   4484 C CE1 . TYR C 1 187 ? 16.037  11.084 -40.236 1.00 36.59  ? 168  TYR C CE1 1 
ATOM   4485 C CE2 . TYR C 1 187 ? 16.055  13.454 -40.000 1.00 45.53  ? 168  TYR C CE2 1 
ATOM   4486 C CZ  . TYR C 1 187 ? 16.728  12.247 -40.022 1.00 39.30  ? 168  TYR C CZ  1 
ATOM   4487 O OH  . TYR C 1 187 ? 18.096  12.199 -39.844 1.00 38.52  ? 168  TYR C OH  1 
ATOM   4488 N N   . SER C 1 188 ? 10.027  12.486 -43.188 1.00 38.59  ? 169  SER C N   1 
ATOM   4489 C CA  . SER C 1 188 ? 8.616   12.358 -43.562 1.00 28.73  ? 169  SER C CA  1 
ATOM   4490 C C   . SER C 1 188 ? 8.256   10.910 -43.943 1.00 36.81  ? 169  SER C C   1 
ATOM   4491 O O   . SER C 1 188 ? 9.111   10.143 -44.412 1.00 39.79  ? 169  SER C O   1 
ATOM   4492 C CB  . SER C 1 188 ? 8.308   13.286 -44.744 1.00 32.43  ? 169  SER C CB  1 
ATOM   4493 O OG  . SER C 1 188 ? 6.926   13.273 -45.049 1.00 33.89  ? 169  SER C OG  1 
ATOM   4494 N N   . ARG C 1 189 ? 6.993   10.534 -43.750 1.00 35.40  ? 170  ARG C N   1 
ATOM   4495 C CA  . ARG C 1 189 ? 6.524   9.221  -44.198 1.00 30.34  ? 170  ARG C CA  1 
ATOM   4496 C C   . ARG C 1 189 ? 6.299   9.200  -45.713 1.00 34.70  ? 170  ARG C C   1 
ATOM   4497 O O   . ARG C 1 189 ? 5.907   8.175  -46.277 1.00 37.10  ? 170  ARG C O   1 
ATOM   4498 C CB  . ARG C 1 189 ? 5.218   8.821  -43.500 1.00 24.54  ? 170  ARG C CB  1 
ATOM   4499 C CG  . ARG C 1 189 ? 5.323   8.666  -42.004 1.00 39.88  ? 170  ARG C CG  1 
ATOM   4500 C CD  . ARG C 1 189 ? 4.503   7.475  -41.517 1.00 49.91  ? 170  ARG C CD  1 
ATOM   4501 N NE  . ARG C 1 189 ? 3.073   7.612  -41.782 1.00 54.06  ? 170  ARG C NE  1 
ATOM   4502 C CZ  . ARG C 1 189 ? 2.224   6.588  -41.873 1.00 64.46  ? 170  ARG C CZ  1 
ATOM   4503 N NH1 . ARG C 1 189 ? 2.659   5.339  -41.732 1.00 74.60  ? 170  ARG C NH1 1 
ATOM   4504 N NH2 . ARG C 1 189 ? 0.939   6.810  -42.117 1.00 64.01  ? 170  ARG C NH2 1 
ATOM   4505 N N   . PHE C 1 190 ? 6.514   10.336 -46.366 1.00 28.95  ? 171  PHE C N   1 
ATOM   4506 C CA  . PHE C 1 190 ? 6.196   10.452 -47.782 1.00 29.84  ? 171  PHE C CA  1 
ATOM   4507 C C   . PHE C 1 190 ? 7.395   10.986 -48.538 1.00 33.59  ? 171  PHE C C   1 
ATOM   4508 O O   . PHE C 1 190 ? 8.345   11.486 -47.927 1.00 36.22  ? 171  PHE C O   1 
ATOM   4509 C CB  . PHE C 1 190 ? 5.007   11.389 -48.014 1.00 29.32  ? 171  PHE C CB  1 
ATOM   4510 C CG  . PHE C 1 190 ? 3.792   11.043 -47.221 1.00 25.81  ? 171  PHE C CG  1 
ATOM   4511 C CD1 . PHE C 1 190 ? 3.673   11.440 -45.881 1.00 27.69  ? 171  PHE C CD1 1 
ATOM   4512 C CD2 . PHE C 1 190 ? 2.750   10.343 -47.809 1.00 28.13  ? 171  PHE C CD2 1 
ATOM   4513 C CE1 . PHE C 1 190 ? 2.527   11.116 -45.129 1.00 26.95  ? 171  PHE C CE1 1 
ATOM   4514 C CE2 . PHE C 1 190 ? 1.598   10.014 -47.080 1.00 30.82  ? 171  PHE C CE2 1 
ATOM   4515 C CZ  . PHE C 1 190 ? 1.488   10.402 -45.733 1.00 30.06  ? 171  PHE C CZ  1 
ATOM   4516 N N   . GLU C 1 191 ? 7.337   10.882 -49.865 1.00 36.72  ? 172  GLU C N   1 
ATOM   4517 C CA  . GLU C 1 191 ? 8.397   11.383 -50.736 1.00 36.85  ? 172  GLU C CA  1 
ATOM   4518 C C   . GLU C 1 191 ? 7.823   12.122 -51.952 1.00 34.54  ? 172  GLU C C   1 
ATOM   4519 O O   . GLU C 1 191 ? 6.712   11.829 -52.410 1.00 34.75  ? 172  GLU C O   1 
ATOM   4520 C CB  . GLU C 1 191 ? 9.360   10.253 -51.150 1.00 34.58  ? 172  GLU C CB  1 
ATOM   4521 C CG  . GLU C 1 191 ? 8.748   9.110  -51.979 1.00 42.24  ? 172  GLU C CG  1 
ATOM   4522 C CD  . GLU C 1 191 ? 9.730   7.922  -52.157 1.00 56.09  ? 172  GLU C CD  1 
ATOM   4523 O OE1 . GLU C 1 191 ? 10.947  8.122  -51.890 1.00 53.68  ? 172  GLU C OE1 1 
ATOM   4524 O OE2 . GLU C 1 191 ? 9.287   6.796  -52.547 1.00 38.03  ? 172  GLU C OE2 1 
ATOM   4525 N N   . ILE C 1 192 ? 8.576   13.094 -52.462 1.00 34.79  ? 173  ILE C N   1 
ATOM   4526 C CA  . ILE C 1 192 ? 8.118   13.869 -53.617 1.00 34.10  ? 173  ILE C CA  1 
ATOM   4527 C C   . ILE C 1 192 ? 8.631   13.272 -54.918 1.00 36.05  ? 173  ILE C C   1 
ATOM   4528 O O   . ILE C 1 192 ? 9.825   13.011 -55.058 1.00 36.23  ? 173  ILE C O   1 
ATOM   4529 C CB  . ILE C 1 192 ? 8.528   15.352 -53.510 1.00 35.60  ? 173  ILE C CB  1 
ATOM   4530 C CG1 . ILE C 1 192 ? 7.903   15.963 -52.244 1.00 37.33  ? 173  ILE C CG1 1 
ATOM   4531 C CG2 . ILE C 1 192 ? 8.103   16.109 -54.761 1.00 25.98  ? 173  ILE C CG2 1 
ATOM   4532 C CD1 . ILE C 1 192 ? 8.221   17.399 -52.007 1.00 29.25  ? 173  ILE C CD1 1 
ATOM   4533 N N   . LEU C 1 193 ? 7.713   13.034 -55.855 1.00 39.27  ? 174  LEU C N   1 
ATOM   4534 C CA  . LEU C 1 193 ? 8.054   12.476 -57.164 1.00 36.37  ? 174  LEU C CA  1 
ATOM   4535 C C   . LEU C 1 193 ? 8.296   13.600 -58.163 1.00 35.67  ? 174  LEU C C   1 
ATOM   4536 O O   . LEU C 1 193 ? 9.235   13.546 -58.950 1.00 41.96  ? 174  LEU C O   1 
ATOM   4537 C CB  . LEU C 1 193 ? 6.953   11.537 -57.650 1.00 36.36  ? 174  LEU C CB  1 
ATOM   4538 C CG  . LEU C 1 193 ? 6.607   10.428 -56.643 1.00 35.39  ? 174  LEU C CG  1 
ATOM   4539 C CD1 . LEU C 1 193 ? 5.462   9.538  -57.131 1.00 32.76  ? 174  LEU C CD1 1 
ATOM   4540 C CD2 . LEU C 1 193 ? 7.838   9.597  -56.273 1.00 27.90  ? 174  LEU C CD2 1 
ATOM   4541 N N   . ASP C 1 194 ? 7.462   14.634 -58.102 1.00 41.27  ? 175  ASP C N   1 
ATOM   4542 C CA  . ASP C 1 194 ? 7.592   15.781 -58.999 1.00 42.55  ? 175  ASP C CA  1 
ATOM   4543 C C   . ASP C 1 194 ? 6.758   16.993 -58.560 1.00 42.65  ? 175  ASP C C   1 
ATOM   4544 O O   . ASP C 1 194 ? 5.701   16.849 -57.931 1.00 41.11  ? 175  ASP C O   1 
ATOM   4545 C CB  . ASP C 1 194 ? 7.197   15.387 -60.428 1.00 48.63  ? 175  ASP C CB  1 
ATOM   4546 C CG  . ASP C 1 194 ? 7.781   16.320 -61.476 1.00 61.03  ? 175  ASP C CG  1 
ATOM   4547 O OD1 . ASP C 1 194 ? 8.937   16.769 -61.285 1.00 64.85  ? 175  ASP C OD1 1 
ATOM   4548 O OD2 . ASP C 1 194 ? 7.087   16.602 -62.488 1.00 64.82  ? 175  ASP C OD2 1 
ATOM   4549 N N   . VAL C 1 195 ? 7.241   18.186 -58.903 1.00 39.36  ? 176  VAL C N   1 
ATOM   4550 C CA  . VAL C 1 195 ? 6.492   19.413 -58.667 1.00 35.76  ? 176  VAL C CA  1 
ATOM   4551 C C   . VAL C 1 195 ? 6.423   20.246 -59.940 1.00 40.57  ? 176  VAL C C   1 
ATOM   4552 O O   . VAL C 1 195 ? 7.456   20.652 -60.471 1.00 51.68  ? 176  VAL C O   1 
ATOM   4553 C CB  . VAL C 1 195 ? 7.142   20.285 -57.567 1.00 38.64  ? 176  VAL C CB  1 
ATOM   4554 C CG1 . VAL C 1 195 ? 6.385   21.596 -57.429 1.00 44.34  ? 176  VAL C CG1 1 
ATOM   4555 C CG2 . VAL C 1 195 ? 7.191   19.568 -56.232 1.00 29.92  ? 176  VAL C CG2 1 
ATOM   4556 N N   . THR C 1 196 ? 5.214   20.511 -60.423 1.00 34.68  ? 177  THR C N   1 
ATOM   4557 C CA  . THR C 1 196 ? 5.034   21.395 -61.584 1.00 39.60  ? 177  THR C CA  1 
ATOM   4558 C C   . THR C 1 196 ? 4.220   22.652 -61.249 1.00 39.22  ? 177  THR C C   1 
ATOM   4559 O O   . THR C 1 196 ? 3.397   22.644 -60.334 1.00 39.67  ? 177  THR C O   1 
ATOM   4560 C CB  . THR C 1 196 ? 4.380   20.660 -62.768 1.00 43.08  ? 177  THR C CB  1 
ATOM   4561 O OG1 . THR C 1 196 ? 3.077   20.187 -62.389 1.00 45.42  ? 177  THR C OG1 1 
ATOM   4562 C CG2 . THR C 1 196 ? 5.241   19.491 -63.197 1.00 48.99  ? 177  THR C CG2 1 
ATOM   4563 N N   . GLN C 1 197 ? 4.445   23.719 -62.007 1.00 38.82  ? 178  GLN C N   1 
ATOM   4564 C CA  . GLN C 1 197 ? 3.773   24.998 -61.780 1.00 37.36  ? 178  GLN C CA  1 
ATOM   4565 C C   . GLN C 1 197 ? 3.092   25.447 -63.079 1.00 41.62  ? 178  GLN C C   1 
ATOM   4566 O O   . GLN C 1 197 ? 3.664   25.290 -64.162 1.00 49.08  ? 178  GLN C O   1 
ATOM   4567 C CB  . GLN C 1 197 ? 4.797   26.063 -61.321 1.00 29.63  ? 178  GLN C CB  1 
ATOM   4568 C CG  . GLN C 1 197 ? 5.643   25.646 -60.104 1.00 37.79  ? 178  GLN C CG  1 
ATOM   4569 C CD  . GLN C 1 197 ? 6.189   26.833 -59.284 1.00 57.36  ? 178  GLN C CD  1 
ATOM   4570 O OE1 . GLN C 1 197 ? 6.494   27.894 -59.834 1.00 58.51  ? 178  GLN C OE1 1 
ATOM   4571 N NE2 . GLN C 1 197 ? 6.313   26.646 -57.956 1.00 51.69  ? 178  GLN C NE2 1 
ATOM   4572 N N   . LYS C 1 198 ? 1.881   25.992 -63.001 1.00 34.41  ? 179  LYS C N   1 
ATOM   4573 C CA  . LYS C 1 198 ? 1.336   26.687 -64.168 1.00 32.06  ? 179  LYS C CA  1 
ATOM   4574 C C   . LYS C 1 198 ? 0.484   27.886 -63.775 1.00 36.09  ? 179  LYS C C   1 
ATOM   4575 O O   . LYS C 1 198 ? -0.026  27.960 -62.656 1.00 39.17  ? 179  LYS C O   1 
ATOM   4576 C CB  . LYS C 1 198 ? 0.555   25.746 -65.070 1.00 33.37  ? 179  LYS C CB  1 
ATOM   4577 C CG  . LYS C 1 198 ? -0.914  25.672 -64.751 1.00 45.81  ? 179  LYS C CG  1 
ATOM   4578 C CD  . LYS C 1 198 ? -1.675  24.887 -65.826 1.00 49.73  ? 179  LYS C CD  1 
ATOM   4579 C CE  . LYS C 1 198 ? -3.105  24.596 -65.369 1.00 65.16  ? 179  LYS C CE  1 
ATOM   4580 N NZ  . LYS C 1 198 ? -3.869  23.786 -66.357 1.00 69.50  ? 179  LYS C NZ  1 
ATOM   4581 N N   . LYS C 1 199 ? 0.328   28.823 -64.702 1.00 33.60  ? 180  LYS C N   1 
ATOM   4582 C CA  . LYS C 1 199 ? -0.397  30.050 -64.407 1.00 35.77  ? 180  LYS C CA  1 
ATOM   4583 C C   . LYS C 1 199 ? -1.810  30.055 -65.004 1.00 35.86  ? 180  LYS C C   1 
ATOM   4584 O O   . LYS C 1 199 ? -1.994  29.683 -66.148 1.00 44.51  ? 180  LYS C O   1 
ATOM   4585 C CB  . LYS C 1 199 ? 0.404   31.253 -64.904 1.00 33.11  ? 180  LYS C CB  1 
ATOM   4586 C CG  . LYS C 1 199 ? -0.401  32.515 -65.002 1.00 39.71  ? 180  LYS C CG  1 
ATOM   4587 C CD  . LYS C 1 199 ? 0.454   33.663 -65.476 1.00 38.00  ? 180  LYS C CD  1 
ATOM   4588 C CE  . LYS C 1 199 ? -0.400  34.922 -65.621 1.00 45.14  ? 180  LYS C CE  1 
ATOM   4589 N NZ  . LYS C 1 199 ? 0.421   36.134 -65.933 1.00 54.23  ? 180  LYS C NZ  1 
ATOM   4590 N N   . ASN C 1 200 ? -2.808  30.465 -64.224 1.00 37.42  ? 181  ASN C N   1 
ATOM   4591 C CA  . ASN C 1 200 ? -4.168  30.587 -64.732 1.00 32.62  ? 181  ASN C CA  1 
ATOM   4592 C C   . ASN C 1 200 ? -4.681  32.019 -64.667 1.00 37.90  ? 181  ASN C C   1 
ATOM   4593 O O   . ASN C 1 200 ? -4.218  32.833 -63.865 1.00 42.45  ? 181  ASN C O   1 
ATOM   4594 C CB  . ASN C 1 200 ? -5.122  29.680 -63.962 1.00 38.46  ? 181  ASN C CB  1 
ATOM   4595 C CG  . ASN C 1 200 ? -4.629  28.246 -63.877 1.00 50.38  ? 181  ASN C CG  1 
ATOM   4596 O OD1 . ASN C 1 200 ? -4.666  27.503 -64.862 1.00 55.65  ? 181  ASN C OD1 1 
ATOM   4597 N ND2 . ASN C 1 200 ? -4.183  27.840 -62.686 1.00 53.55  ? 181  ASN C ND2 1 
ATOM   4598 N N   . SER C 1 201 ? -5.645  32.323 -65.523 1.00 37.71  ? 182  SER C N   1 
ATOM   4599 C CA  . SER C 1 201 ? -6.310  33.616 -65.498 1.00 34.24  ? 182  SER C CA  1 
ATOM   4600 C C   . SER C 1 201 ? -7.808  33.333 -65.539 1.00 33.33  ? 182  SER C C   1 
ATOM   4601 O O   . SER C 1 201 ? -8.311  32.810 -66.528 1.00 35.87  ? 182  SER C O   1 
ATOM   4602 C CB  . SER C 1 201 ? -5.872  34.471 -66.687 1.00 31.92  ? 182  SER C CB  1 
ATOM   4603 O OG  . SER C 1 201 ? -6.267  35.821 -66.525 1.00 34.42  ? 182  SER C OG  1 
ATOM   4604 N N   . VAL C 1 202 ? -8.506  33.661 -64.454 1.00 29.71  ? 183  VAL C N   1 
ATOM   4605 C CA  . VAL C 1 202 ? -9.886  33.245 -64.244 1.00 26.89  ? 183  VAL C CA  1 
ATOM   4606 C C   . VAL C 1 202 ? -10.830 34.439 -64.124 1.00 37.90  ? 183  VAL C C   1 
ATOM   4607 O O   . VAL C 1 202 ? -10.506 35.448 -63.479 1.00 34.68  ? 183  VAL C O   1 
ATOM   4608 C CB  . VAL C 1 202 ? -9.991  32.420 -62.943 1.00 34.25  ? 183  VAL C CB  1 
ATOM   4609 C CG1 . VAL C 1 202 ? -11.450 32.048 -62.628 1.00 32.28  ? 183  VAL C CG1 1 
ATOM   4610 C CG2 . VAL C 1 202 ? -9.108  31.194 -63.030 1.00 29.17  ? 183  VAL C CG2 1 
ATOM   4611 N N   . THR C 1 203 ? -12.005 34.326 -64.742 1.00 44.19  ? 184  THR C N   1 
ATOM   4612 C CA  . THR C 1 203 ? -13.053 35.323 -64.537 1.00 41.33  ? 184  THR C CA  1 
ATOM   4613 C C   . THR C 1 203 ? -14.171 34.779 -63.628 1.00 43.51  ? 184  THR C C   1 
ATOM   4614 O O   . THR C 1 203 ? -14.803 33.768 -63.926 1.00 50.11  ? 184  THR C O   1 
ATOM   4615 C CB  . THR C 1 203 ? -13.628 35.855 -65.868 1.00 34.83  ? 184  THR C CB  1 
ATOM   4616 O OG1 . THR C 1 203 ? -12.629 36.642 -66.540 1.00 44.62  ? 184  THR C OG1 1 
ATOM   4617 C CG2 . THR C 1 203 ? -14.843 36.734 -65.597 1.00 35.89  ? 184  THR C CG2 1 
ATOM   4618 N N   . TYR C 1 204 ? -14.410 35.451 -62.508 1.00 48.75  ? 185  TYR C N   1 
ATOM   4619 C CA  . TYR C 1 204 ? -15.452 35.025 -61.576 1.00 42.06  ? 185  TYR C CA  1 
ATOM   4620 C C   . TYR C 1 204 ? -16.789 35.700 -61.855 1.00 47.01  ? 185  TYR C C   1 
ATOM   4621 O O   . TYR C 1 204 ? -16.859 36.731 -62.535 1.00 52.43  ? 185  TYR C O   1 
ATOM   4622 C CB  . TYR C 1 204 ? -15.016 35.290 -60.136 1.00 34.81  ? 185  TYR C CB  1 
ATOM   4623 C CG  . TYR C 1 204 ? -13.794 34.503 -59.751 1.00 33.30  ? 185  TYR C CG  1 
ATOM   4624 C CD1 . TYR C 1 204 ? -12.518 35.000 -59.992 1.00 37.42  ? 185  TYR C CD1 1 
ATOM   4625 C CD2 . TYR C 1 204 ? -13.908 33.249 -59.168 1.00 32.97  ? 185  TYR C CD2 1 
ATOM   4626 C CE1 . TYR C 1 204 ? -11.380 34.263 -59.652 1.00 37.03  ? 185  TYR C CE1 1 
ATOM   4627 C CE2 . TYR C 1 204 ? -12.778 32.506 -58.815 1.00 31.82  ? 185  TYR C CE2 1 
ATOM   4628 C CZ  . TYR C 1 204 ? -11.516 33.017 -59.063 1.00 33.08  ? 185  TYR C CZ  1 
ATOM   4629 O OH  . TYR C 1 204 ? -10.382 32.295 -58.729 1.00 34.13  ? 185  TYR C OH  1 
ATOM   4630 N N   . SER C 1 205 ? -17.844 35.108 -61.306 1.00 43.88  ? 186  SER C N   1 
ATOM   4631 C CA  . SER C 1 205 ? -19.213 35.552 -61.550 1.00 52.87  ? 186  SER C CA  1 
ATOM   4632 C C   . SER C 1 205 ? -19.518 36.954 -61.030 1.00 50.55  ? 186  SER C C   1 
ATOM   4633 O O   . SER C 1 205 ? -20.504 37.572 -61.427 1.00 52.00  ? 186  SER C O   1 
ATOM   4634 C CB  . SER C 1 205 ? -20.199 34.550 -60.950 1.00 51.06  ? 186  SER C CB  1 
ATOM   4635 O OG  . SER C 1 205 ? -20.060 33.288 -61.573 1.00 64.70  ? 186  SER C OG  1 
ATOM   4636 N N   . CYS C 1 206 ? -18.668 37.454 -60.146 1.00 51.52  ? 187  CYS C N   1 
ATOM   4637 C CA  . CYS C 1 206 ? -18.906 38.744 -59.520 1.00 55.41  ? 187  CYS C CA  1 
ATOM   4638 C C   . CYS C 1 206 ? -18.489 39.939 -60.397 1.00 61.12  ? 187  CYS C C   1 
ATOM   4639 O O   . CYS C 1 206 ? -19.212 40.933 -60.453 1.00 71.01  ? 187  CYS C O   1 
ATOM   4640 C CB  . CYS C 1 206 ? -18.189 38.809 -58.168 1.00 61.20  ? 187  CYS C CB  1 
ATOM   4641 S SG  . CYS C 1 206 ? -16.400 39.152 -58.303 1.00 79.55  ? 187  CYS C SG  1 
ATOM   4642 N N   . CYS C 1 207 ? -17.343 39.837 -61.083 1.00 56.07  ? 188  CYS C N   1 
ATOM   4643 C CA  . CYS C 1 207 ? -16.714 40.990 -61.754 1.00 58.18  ? 188  CYS C CA  1 
ATOM   4644 C C   . CYS C 1 207 ? -16.285 40.671 -63.192 1.00 59.37  ? 188  CYS C C   1 
ATOM   4645 O O   . CYS C 1 207 ? -16.046 39.505 -63.526 1.00 58.00  ? 188  CYS C O   1 
ATOM   4646 C CB  . CYS C 1 207 ? -15.500 41.463 -60.931 1.00 57.57  ? 188  CYS C CB  1 
ATOM   4647 S SG  . CYS C 1 207 ? -15.375 40.629 -59.298 1.00 86.73  ? 188  CYS C SG  1 
ATOM   4648 N N   . PRO C 1 208 ? -16.176 41.706 -64.048 1.00 56.29  ? 189  PRO C N   1 
ATOM   4649 C CA  . PRO C 1 208 ? -15.775 41.534 -65.455 1.00 57.37  ? 189  PRO C CA  1 
ATOM   4650 C C   . PRO C 1 208 ? -14.263 41.432 -65.644 1.00 58.93  ? 189  PRO C C   1 
ATOM   4651 O O   . PRO C 1 208 ? -13.788 41.217 -66.764 1.00 62.57  ? 189  PRO C O   1 
ATOM   4652 C CB  . PRO C 1 208 ? -16.274 42.825 -66.113 1.00 61.58  ? 189  PRO C CB  1 
ATOM   4653 C CG  . PRO C 1 208 ? -16.162 43.842 -65.025 1.00 66.29  ? 189  PRO C CG  1 
ATOM   4654 C CD  . PRO C 1 208 ? -16.524 43.108 -63.746 1.00 60.55  ? 189  PRO C CD  1 
ATOM   4655 N N   . GLU C 1 209 ? -13.522 41.596 -64.553 1.00 57.15  ? 190  GLU C N   1 
ATOM   4656 C CA  . GLU C 1 209 ? -12.063 41.583 -64.591 1.00 52.43  ? 190  GLU C CA  1 
ATOM   4657 C C   . GLU C 1 209 ? -11.520 40.163 -64.388 1.00 44.38  ? 190  GLU C C   1 
ATOM   4658 O O   . GLU C 1 209 ? -12.192 39.306 -63.816 1.00 41.30  ? 190  GLU C O   1 
ATOM   4659 C CB  . GLU C 1 209 ? -11.526 42.515 -63.501 1.00 50.91  ? 190  GLU C CB  1 
ATOM   4660 C CG  . GLU C 1 209 ? -12.271 43.847 -63.388 1.00 57.44  ? 190  GLU C CG  1 
ATOM   4661 C CD  . GLU C 1 209 ? -11.841 44.843 -64.454 1.00 63.93  ? 190  GLU C CD  1 
ATOM   4662 O OE1 . GLU C 1 209 ? -11.007 44.460 -65.309 1.00 68.63  ? 190  GLU C OE1 1 
ATOM   4663 O OE2 . GLU C 1 209 ? -12.331 45.999 -64.432 1.00 56.46  ? 190  GLU C OE2 1 
ATOM   4664 N N   . ALA C 1 210 ? -10.303 39.911 -64.853 1.00 37.97  ? 191  ALA C N   1 
ATOM   4665 C CA  . ALA C 1 210 ? -9.681  38.609 -64.653 1.00 33.18  ? 191  ALA C CA  1 
ATOM   4666 C C   . ALA C 1 210 ? -8.778  38.624 -63.425 1.00 34.16  ? 191  ALA C C   1 
ATOM   4667 O O   . ALA C 1 210 ? -8.130  39.628 -63.143 1.00 38.81  ? 191  ALA C O   1 
ATOM   4668 C CB  . ALA C 1 210 ? -8.880  38.217 -65.870 1.00 38.93  ? 191  ALA C CB  1 
ATOM   4669 N N   . TYR C 1 211 ? -8.726  37.506 -62.704 1.00 35.84  ? 192  TYR C N   1 
ATOM   4670 C CA  . TYR C 1 211 ? -7.831  37.366 -61.549 1.00 31.81  ? 192  TYR C CA  1 
ATOM   4671 C C   . TYR C 1 211 ? -6.797  36.272 -61.793 1.00 31.65  ? 192  TYR C C   1 
ATOM   4672 O O   . TYR C 1 211 ? -7.149  35.111 -62.017 1.00 33.87  ? 192  TYR C O   1 
ATOM   4673 C CB  . TYR C 1 211 ? -8.640  37.054 -60.292 1.00 25.77  ? 192  TYR C CB  1 
ATOM   4674 C CG  . TYR C 1 211 ? -9.478  38.210 -59.829 1.00 28.11  ? 192  TYR C CG  1 
ATOM   4675 C CD1 . TYR C 1 211 ? -10.653 38.548 -60.475 1.00 27.32  ? 192  TYR C CD1 1 
ATOM   4676 C CD2 . TYR C 1 211 ? -9.086  38.975 -58.748 1.00 32.33  ? 192  TYR C CD2 1 
ATOM   4677 C CE1 . TYR C 1 211 ? -11.418 39.624 -60.053 1.00 34.61  ? 192  TYR C CE1 1 
ATOM   4678 C CE2 . TYR C 1 211 ? -9.841  40.053 -58.311 1.00 30.29  ? 192  TYR C CE2 1 
ATOM   4679 C CZ  . TYR C 1 211 ? -11.010 40.377 -58.965 1.00 34.83  ? 192  TYR C CZ  1 
ATOM   4680 O OH  . TYR C 1 211 ? -11.772 41.459 -58.537 1.00 35.60  ? 192  TYR C OH  1 
ATOM   4681 N N   . GLU C 1 212 ? -5.522  36.631 -61.756 1.00 29.55  ? 193  GLU C N   1 
ATOM   4682 C CA  . GLU C 1 212 ? -4.476  35.630 -61.953 1.00 34.12  ? 193  GLU C CA  1 
ATOM   4683 C C   . GLU C 1 212 ? -4.178  34.792 -60.706 1.00 33.53  ? 193  GLU C C   1 
ATOM   4684 O O   . GLU C 1 212 ? -4.276  35.268 -59.570 1.00 35.33  ? 193  GLU C O   1 
ATOM   4685 C CB  . GLU C 1 212 ? -3.188  36.284 -62.441 1.00 37.65  ? 193  GLU C CB  1 
ATOM   4686 C CG  . GLU C 1 212 ? -3.349  37.105 -63.704 1.00 39.20  ? 193  GLU C CG  1 
ATOM   4687 C CD  . GLU C 1 212 ? -2.018  37.609 -64.244 1.00 44.24  ? 193  GLU C CD  1 
ATOM   4688 O OE1 . GLU C 1 212 ? -0.970  37.316 -63.626 1.00 44.66  ? 193  GLU C OE1 1 
ATOM   4689 O OE2 . GLU C 1 212 ? -2.019  38.296 -65.291 1.00 53.83  ? 193  GLU C OE2 1 
ATOM   4690 N N   . ASP C 1 213 ? -3.800  33.542 -60.937 1.00 28.62  ? 194  ASP C N   1 
ATOM   4691 C CA  . ASP C 1 213 ? -3.311  32.672 -59.874 1.00 30.71  ? 194  ASP C CA  1 
ATOM   4692 C C   . ASP C 1 213 ? -2.257  31.703 -60.396 1.00 34.59  ? 194  ASP C C   1 
ATOM   4693 O O   . ASP C 1 213 ? -2.083  31.530 -61.599 1.00 34.92  ? 194  ASP C O   1 
ATOM   4694 C CB  . ASP C 1 213 ? -4.450  31.877 -59.233 1.00 39.57  ? 194  ASP C CB  1 
ATOM   4695 C CG  . ASP C 1 213 ? -5.273  31.086 -60.261 1.00 50.08  ? 194  ASP C CG  1 
ATOM   4696 O OD1 . ASP C 1 213 ? -4.863  29.946 -60.630 1.00 49.42  ? 194  ASP C OD1 1 
ATOM   4697 O OD2 . ASP C 1 213 ? -6.336  31.614 -60.690 1.00 50.69  ? 194  ASP C OD2 1 
ATOM   4698 N N   . VAL C 1 214 ? -1.553  31.070 -59.476 1.00 30.63  ? 195  VAL C N   1 
ATOM   4699 C CA  . VAL C 1 214 ? -0.617  30.039 -59.831 1.00 25.97  ? 195  VAL C CA  1 
ATOM   4700 C C   . VAL C 1 214 ? -1.135  28.743 -59.240 1.00 32.47  ? 195  VAL C C   1 
ATOM   4701 O O   . VAL C 1 214 ? -1.598  28.705 -58.095 1.00 27.01  ? 195  VAL C O   1 
ATOM   4702 C CB  . VAL C 1 214 ? 0.779   30.369 -59.298 1.00 25.14  ? 195  VAL C CB  1 
ATOM   4703 C CG1 . VAL C 1 214 ? 1.732   29.190 -59.457 1.00 27.24  ? 195  VAL C CG1 1 
ATOM   4704 C CG2 . VAL C 1 214 ? 1.320   31.584 -60.024 1.00 36.30  ? 195  VAL C CG2 1 
ATOM   4705 N N   . GLU C 1 215 ? -1.078  27.687 -60.047 1.00 36.36  ? 196  GLU C N   1 
ATOM   4706 C CA  . GLU C 1 215 ? -1.451  26.342 -59.616 1.00 34.59  ? 196  GLU C CA  1 
ATOM   4707 C C   . GLU C 1 215 ? -0.193  25.495 -59.467 1.00 32.84  ? 196  GLU C C   1 
ATOM   4708 O O   . GLU C 1 215 ? 0.578   25.344 -60.413 1.00 34.88  ? 196  GLU C O   1 
ATOM   4709 C CB  . GLU C 1 215 ? -2.377  25.710 -60.649 1.00 44.41  ? 196  GLU C CB  1 
ATOM   4710 C CG  . GLU C 1 215 ? -3.671  25.126 -60.093 1.00 51.62  ? 196  GLU C CG  1 
ATOM   4711 C CD  . GLU C 1 215 ? -4.616  24.608 -61.196 1.00 66.94  ? 196  GLU C CD  1 
ATOM   4712 O OE1 . GLU C 1 215 ? -4.152  23.853 -62.093 1.00 65.86  ? 196  GLU C OE1 1 
ATOM   4713 O OE2 . GLU C 1 215 ? -5.820  24.961 -61.161 1.00 61.98  ? 196  GLU C OE2 1 
ATOM   4714 N N   . VAL C 1 216 ? 0.025   24.952 -58.274 1.00 33.12  ? 197  VAL C N   1 
ATOM   4715 C CA  . VAL C 1 216 ? 1.214   24.149 -58.028 1.00 28.67  ? 197  VAL C CA  1 
ATOM   4716 C C   . VAL C 1 216 ? 0.813   22.697 -57.828 1.00 29.03  ? 197  VAL C C   1 
ATOM   4717 O O   . VAL C 1 216 ? 0.097   22.382 -56.879 1.00 24.64  ? 197  VAL C O   1 
ATOM   4718 C CB  . VAL C 1 216 ? 2.013   24.652 -56.806 1.00 26.67  ? 197  VAL C CB  1 
ATOM   4719 C CG1 . VAL C 1 216 ? 3.190   23.724 -56.517 1.00 29.49  ? 197  VAL C CG1 1 
ATOM   4720 C CG2 . VAL C 1 216 ? 2.496   26.064 -57.035 1.00 24.08  ? 197  VAL C CG2 1 
ATOM   4721 N N   . SER C 1 217 ? 1.280   21.822 -58.726 1.00 36.53  ? 198  SER C N   1 
ATOM   4722 C CA  . SER C 1 217 ? 0.950   20.394 -58.687 1.00 30.60  ? 198  SER C CA  1 
ATOM   4723 C C   . SER C 1 217 ? 2.027   19.596 -57.988 1.00 27.52  ? 198  SER C C   1 
ATOM   4724 O O   . SER C 1 217 ? 3.183   19.569 -58.410 1.00 32.75  ? 198  SER C O   1 
ATOM   4725 C CB  . SER C 1 217 ? 0.746   19.845 -60.093 1.00 31.42  ? 198  SER C CB  1 
ATOM   4726 O OG  . SER C 1 217 ? -0.260  20.572 -60.756 1.00 46.57  ? 198  SER C OG  1 
ATOM   4727 N N   . LEU C 1 218 ? 1.632   18.932 -56.917 1.00 24.90  ? 199  LEU C N   1 
ATOM   4728 C CA  . LEU C 1 218 ? 2.574   18.215 -56.088 1.00 26.95  ? 199  LEU C CA  1 
ATOM   4729 C C   . LEU C 1 218 ? 2.316   16.725 -56.224 1.00 33.98  ? 199  LEU C C   1 
ATOM   4730 O O   . LEU C 1 218 ? 1.292   16.210 -55.742 1.00 34.20  ? 199  LEU C O   1 
ATOM   4731 C CB  . LEU C 1 218 ? 2.435   18.658 -54.628 1.00 23.73  ? 199  LEU C CB  1 
ATOM   4732 C CG  . LEU C 1 218 ? 3.196   17.798 -53.623 1.00 29.50  ? 199  LEU C CG  1 
ATOM   4733 C CD1 . LEU C 1 218 ? 4.694   17.859 -53.889 1.00 31.73  ? 199  LEU C CD1 1 
ATOM   4734 C CD2 . LEU C 1 218 ? 2.872   18.195 -52.193 1.00 25.43  ? 199  LEU C CD2 1 
ATOM   4735 N N   . ASN C 1 219 ? 3.240   16.031 -56.883 1.00 32.68  ? 200  ASN C N   1 
ATOM   4736 C CA  . ASN C 1 219 ? 3.118   14.585 -57.054 1.00 37.78  ? 200  ASN C CA  1 
ATOM   4737 C C   . ASN C 1 219 ? 3.932   13.828 -55.994 1.00 35.43  ? 200  ASN C C   1 
ATOM   4738 O O   . ASN C 1 219 ? 5.161   13.912 -55.970 1.00 35.85  ? 200  ASN C O   1 
ATOM   4739 C CB  . ASN C 1 219 ? 3.522   14.183 -58.477 1.00 35.35  ? 200  ASN C CB  1 
ATOM   4740 C CG  . ASN C 1 219 ? 3.277   12.719 -58.757 1.00 40.32  ? 200  ASN C CG  1 
ATOM   4741 O OD1 . ASN C 1 219 ? 4.110   12.047 -59.372 1.00 51.24  ? 200  ASN C OD1 1 
ATOM   4742 N ND2 . ASN C 1 219 ? 2.134   12.208 -58.295 1.00 38.94  ? 200  ASN C ND2 1 
ATOM   4743 N N   . PHE C 1 220 ? 3.245   13.102 -55.114 1.00 31.03  ? 201  PHE C N   1 
ATOM   4744 C CA  . PHE C 1 220 ? 3.902   12.464 -53.963 1.00 36.35  ? 201  PHE C CA  1 
ATOM   4745 C C   . PHE C 1 220 ? 3.265   11.105 -53.605 1.00 35.28  ? 201  PHE C C   1 
ATOM   4746 O O   . PHE C 1 220 ? 2.104   10.830 -53.957 1.00 35.87  ? 201  PHE C O   1 
ATOM   4747 C CB  . PHE C 1 220 ? 3.844   13.395 -52.741 1.00 29.52  ? 201  PHE C CB  1 
ATOM   4748 C CG  . PHE C 1 220 ? 2.472   13.502 -52.132 1.00 28.73  ? 201  PHE C CG  1 
ATOM   4749 C CD1 . PHE C 1 220 ? 1.445   14.171 -52.801 1.00 26.44  ? 201  PHE C CD1 1 
ATOM   4750 C CD2 . PHE C 1 220 ? 2.195   12.919 -50.898 1.00 30.47  ? 201  PHE C CD2 1 
ATOM   4751 C CE1 . PHE C 1 220 ? 0.155   14.256 -52.239 1.00 28.49  ? 201  PHE C CE1 1 
ATOM   4752 C CE2 . PHE C 1 220 ? 0.907   13.008 -50.323 1.00 30.39  ? 201  PHE C CE2 1 
ATOM   4753 C CZ  . PHE C 1 220 ? -0.108  13.680 -50.992 1.00 22.26  ? 201  PHE C CZ  1 
ATOM   4754 N N   . ARG C 1 221 ? 4.012   10.262 -52.895 1.00 25.93  ? 202  ARG C N   1 
ATOM   4755 C CA  . ARG C 1 221 ? 3.463   8.990  -52.435 1.00 31.60  ? 202  ARG C CA  1 
ATOM   4756 C C   . ARG C 1 221 ? 4.050   8.570  -51.102 1.00 34.84  ? 202  ARG C C   1 
ATOM   4757 O O   . ARG C 1 221 ? 5.039   9.153  -50.644 1.00 34.60  ? 202  ARG C O   1 
ATOM   4758 C CB  . ARG C 1 221 ? 3.724   7.877  -53.453 1.00 40.44  ? 202  ARG C CB  1 
ATOM   4759 C CG  . ARG C 1 221 ? 5.201   7.635  -53.699 1.00 38.31  ? 202  ARG C CG  1 
ATOM   4760 C CD  . ARG C 1 221 ? 5.513   6.176  -53.960 1.00 36.29  ? 202  ARG C CD  1 
ATOM   4761 N NE  . ARG C 1 221 ? 6.942   6.013  -54.205 1.00 40.16  ? 202  ARG C NE  1 
ATOM   4762 C CZ  . ARG C 1 221 ? 7.483   5.829  -55.402 1.00 32.25  ? 202  ARG C CZ  1 
ATOM   4763 N NH1 . ARG C 1 221 ? 6.706   5.738  -56.469 1.00 33.06  ? 202  ARG C NH1 1 
ATOM   4764 N NH2 . ARG C 1 221 ? 8.801   5.710  -55.519 1.00 30.84  ? 202  ARG C NH2 1 
ATOM   4765 N N   . LYS C 1 222 ? 3.440   7.545  -50.499 1.00 34.68  ? 203  LYS C N   1 
ATOM   4766 C CA  . LYS C 1 222 ? 3.943   6.940  -49.268 1.00 31.74  ? 203  LYS C CA  1 
ATOM   4767 C C   . LYS C 1 222 ? 5.194   6.111  -49.564 1.00 32.62  ? 203  LYS C C   1 
ATOM   4768 O O   . LYS C 1 222 ? 5.287   5.466  -50.613 1.00 30.00  ? 203  LYS C O   1 
ATOM   4769 C CB  . LYS C 1 222 ? 2.867   6.069  -48.630 1.00 36.66  ? 203  LYS C CB  1 
ATOM   4770 C CG  . LYS C 1 222 ? 3.224   5.554  -47.244 1.00 48.82  ? 203  LYS C CG  1 
ATOM   4771 C CD  . LYS C 1 222 ? 2.038   4.806  -46.650 1.00 67.40  ? 203  LYS C CD  1 
ATOM   4772 C CE  . LYS C 1 222 ? 2.332   4.255  -45.262 1.00 86.76  ? 203  LYS C CE  1 
ATOM   4773 N NZ  . LYS C 1 222 ? 1.156   3.487  -44.732 1.00 80.94  ? 203  LYS C NZ  1 
ATOM   4774 N N   . LYS C 1 223 ? 6.165   6.161  -48.655 1.00 31.63  ? 204  LYS C N   1 
ATOM   4775 C CA  . LYS C 1 223 ? 7.417   5.423  -48.803 1.00 30.99  ? 204  LYS C CA  1 
ATOM   4776 C C   . LYS C 1 223 ? 7.234   3.921  -48.545 1.00 47.78  ? 204  LYS C C   1 
ATOM   4777 O O   . LYS C 1 223 ? 6.315   3.515  -47.807 1.00 50.80  ? 204  LYS C O   1 
ATOM   4778 C CB  . LYS C 1 223 ? 8.448   5.949  -47.812 1.00 34.36  ? 204  LYS C CB  1 
ATOM   4779 C CG  . LYS C 1 223 ? 9.088   7.278  -48.143 1.00 34.04  ? 204  LYS C CG  1 
ATOM   4780 C CD  . LYS C 1 223 ? 9.910   7.748  -46.936 1.00 34.95  ? 204  LYS C CD  1 
ATOM   4781 C CE  . LYS C 1 223 ? 11.024  8.707  -47.320 1.00 41.16  ? 204  LYS C CE  1 
ATOM   4782 N NZ  . LYS C 1 223 ? 11.943  8.936  -46.165 1.00 46.03  ? 204  LYS C NZ  1 
ATOM   4783 N N   . GLY C 1 224 ? 8.129   3.113  -49.129 1.00 43.18  ? 205  GLY C N   1 
ATOM   4784 C CA  . GLY C 1 224 ? 8.146   1.670  -48.919 1.00 44.34  ? 205  GLY C CA  1 
ATOM   4785 C C   . GLY C 1 224 ? 9.493   1.149  -48.436 1.00 56.65  ? 205  GLY C C   1 
ATOM   4786 O O   . GLY C 1 224 ? 9.594   0.072  -47.838 1.00 59.91  ? 205  GLY C O   1 
ATOM   4787 N N   . LEU D 1 20  ? -6.069  62.696 -58.543 1.00 44.00  ? 1    LEU D N   1 
ATOM   4788 C CA  . LEU D 1 20  ? -6.070  61.761 -57.428 1.00 37.09  ? 1    LEU D CA  1 
ATOM   4789 C C   . LEU D 1 20  ? -5.427  60.469 -57.845 1.00 39.56  ? 1    LEU D C   1 
ATOM   4790 O O   . LEU D 1 20  ? -5.772  59.922 -58.892 1.00 48.40  ? 1    LEU D O   1 
ATOM   4791 C CB  . LEU D 1 20  ? -7.499  61.450 -56.973 1.00 38.05  ? 1    LEU D CB  1 
ATOM   4792 C CG  . LEU D 1 20  ? -8.217  62.468 -56.095 1.00 27.10  ? 1    LEU D CG  1 
ATOM   4793 C CD1 . LEU D 1 20  ? -9.489  61.853 -55.594 1.00 32.15  ? 1    LEU D CD1 1 
ATOM   4794 C CD2 . LEU D 1 20  ? -7.340  62.888 -54.929 1.00 29.27  ? 1    LEU D CD2 1 
ATOM   4795 N N   . ASP D 1 21  ? -4.493  59.979 -57.032 1.00 39.67  ? 2    ASP D N   1 
ATOM   4796 C CA  . ASP D 1 21  ? -3.944  58.637 -57.236 1.00 46.32  ? 2    ASP D CA  1 
ATOM   4797 C C   . ASP D 1 21  ? -4.373  57.739 -56.084 1.00 38.48  ? 2    ASP D C   1 
ATOM   4798 O O   . ASP D 1 21  ? -5.028  58.213 -55.150 1.00 34.02  ? 2    ASP D O   1 
ATOM   4799 C CB  . ASP D 1 21  ? -2.417  58.668 -57.393 1.00 40.85  ? 2    ASP D CB  1 
ATOM   4800 C CG  . ASP D 1 21  ? -1.738  59.574 -56.377 1.00 48.27  ? 2    ASP D CG  1 
ATOM   4801 O OD1 . ASP D 1 21  ? -2.182  59.598 -55.208 1.00 49.96  ? 2    ASP D OD1 1 
ATOM   4802 O OD2 . ASP D 1 21  ? -0.755  60.265 -56.748 1.00 56.51  ? 2    ASP D OD2 1 
ATOM   4803 N N   . ARG D 1 22  ? -4.019  56.457 -56.154 1.00 31.35  ? 3    ARG D N   1 
ATOM   4804 C CA  . ARG D 1 22  ? -4.408  55.536 -55.099 1.00 36.85  ? 3    ARG D CA  1 
ATOM   4805 C C   . ARG D 1 22  ? -3.937  56.021 -53.740 1.00 33.14  ? 3    ARG D C   1 
ATOM   4806 O O   . ARG D 1 22  ? -4.683  55.926 -52.749 1.00 31.61  ? 3    ARG D O   1 
ATOM   4807 C CB  . ARG D 1 22  ? -3.901  54.114 -55.363 1.00 36.29  ? 3    ARG D CB  1 
ATOM   4808 C CG  . ARG D 1 22  ? -4.743  53.350 -56.336 1.00 33.69  ? 3    ARG D CG  1 
ATOM   4809 C CD  . ARG D 1 22  ? -4.201  51.964 -56.548 1.00 38.59  ? 3    ARG D CD  1 
ATOM   4810 N NE  . ARG D 1 22  ? -5.024  51.238 -57.508 1.00 44.47  ? 3    ARG D NE  1 
ATOM   4811 C CZ  . ARG D 1 22  ? -4.892  51.340 -58.826 1.00 47.77  ? 3    ARG D CZ  1 
ATOM   4812 N NH1 . ARG D 1 22  ? -3.958  52.136 -59.345 1.00 42.08  ? 3    ARG D NH1 1 
ATOM   4813 N NH2 . ARG D 1 22  ? -5.692  50.640 -59.619 1.00 51.26  ? 3    ARG D NH2 1 
ATOM   4814 N N   . ALA D 1 23  ? -2.718  56.553 -53.697 1.00 24.79  ? 4    ALA D N   1 
ATOM   4815 C CA  . ALA D 1 23  ? -2.139  56.950 -52.421 1.00 24.85  ? 4    ALA D CA  1 
ATOM   4816 C C   . ALA D 1 23  ? -3.011  58.015 -51.759 1.00 33.20  ? 4    ALA D C   1 
ATOM   4817 O O   . ALA D 1 23  ? -3.277  57.965 -50.547 1.00 33.50  ? 4    ALA D O   1 
ATOM   4818 C CB  . ALA D 1 23  ? -0.752  57.440 -52.601 1.00 19.79  ? 4    ALA D CB  1 
ATOM   4819 N N   . ASP D 1 24  ? -3.473  58.963 -52.567 1.00 33.52  ? 5    ASP D N   1 
ATOM   4820 C CA  . ASP D 1 24  ? -4.318  60.054 -52.083 1.00 33.94  ? 5    ASP D CA  1 
ATOM   4821 C C   . ASP D 1 24  ? -5.696  59.566 -51.567 1.00 32.64  ? 5    ASP D C   1 
ATOM   4822 O O   . ASP D 1 24  ? -6.162  59.985 -50.496 1.00 29.62  ? 5    ASP D O   1 
ATOM   4823 C CB  . ASP D 1 24  ? -4.475  61.119 -53.182 1.00 33.90  ? 5    ASP D CB  1 
ATOM   4824 C CG  . ASP D 1 24  ? -3.185  61.908 -53.430 1.00 51.26  ? 5    ASP D CG  1 
ATOM   4825 O OD1 . ASP D 1 24  ? -2.416  62.116 -52.457 1.00 52.26  ? 5    ASP D OD1 1 
ATOM   4826 O OD2 . ASP D 1 24  ? -2.948  62.323 -54.598 1.00 55.82  ? 5    ASP D OD2 1 
ATOM   4827 N N   . ILE D 1 25  ? -6.332  58.675 -52.325 1.00 28.94  ? 6    ILE D N   1 
ATOM   4828 C CA  . ILE D 1 25  ? -7.649  58.156 -51.963 1.00 25.06  ? 6    ILE D CA  1 
ATOM   4829 C C   . ILE D 1 25  ? -7.621  57.372 -50.653 1.00 29.57  ? 6    ILE D C   1 
ATOM   4830 O O   . ILE D 1 25  ? -8.447  57.606 -49.767 1.00 28.80  ? 6    ILE D O   1 
ATOM   4831 C CB  . ILE D 1 25  ? -8.219  57.245 -53.068 1.00 25.75  ? 6    ILE D CB  1 
ATOM   4832 C CG1 . ILE D 1 25  ? -8.453  58.040 -54.350 1.00 22.71  ? 6    ILE D CG1 1 
ATOM   4833 C CG2 . ILE D 1 25  ? -9.506  56.555 -52.604 1.00 20.95  ? 6    ILE D CG2 1 
ATOM   4834 C CD1 . ILE D 1 25  ? -8.690  57.157 -55.566 1.00 32.34  ? 6    ILE D CD1 1 
ATOM   4835 N N   . LEU D 1 26  ? -6.671  56.442 -50.537 1.00 29.27  ? 7    LEU D N   1 
ATOM   4836 C CA  . LEU D 1 26  ? -6.518  55.647 -49.315 1.00 23.82  ? 7    LEU D CA  1 
ATOM   4837 C C   . LEU D 1 26  ? -6.181  56.526 -48.112 1.00 28.12  ? 7    LEU D C   1 
ATOM   4838 O O   . LEU D 1 26  ? -6.601  56.235 -46.990 1.00 29.58  ? 7    LEU D O   1 
ATOM   4839 C CB  . LEU D 1 26  ? -5.475  54.550 -49.507 1.00 23.30  ? 7    LEU D CB  1 
ATOM   4840 C CG  . LEU D 1 26  ? -5.916  53.526 -50.555 1.00 23.77  ? 7    LEU D CG  1 
ATOM   4841 C CD1 . LEU D 1 26  ? -4.741  52.777 -51.166 1.00 23.08  ? 7    LEU D CD1 1 
ATOM   4842 C CD2 . LEU D 1 26  ? -6.906  52.556 -49.935 1.00 21.55  ? 7    LEU D CD2 1 
ATOM   4843 N N   . TYR D 1 27  ? -5.442  57.611 -48.359 1.00 27.36  ? 8    TYR D N   1 
ATOM   4844 C CA  . TYR D 1 27  ? -5.126  58.579 -47.320 1.00 22.35  ? 8    TYR D CA  1 
ATOM   4845 C C   . TYR D 1 27  ? -6.398  59.243 -46.815 1.00 25.29  ? 8    TYR D C   1 
ATOM   4846 O O   . TYR D 1 27  ? -6.680  59.218 -45.623 1.00 23.40  ? 8    TYR D O   1 
ATOM   4847 C CB  . TYR D 1 27  ? -4.159  59.636 -47.832 1.00 27.22  ? 8    TYR D CB  1 
ATOM   4848 C CG  . TYR D 1 27  ? -3.806  60.680 -46.797 1.00 30.68  ? 8    TYR D CG  1 
ATOM   4849 C CD1 . TYR D 1 27  ? -2.922  60.389 -45.766 1.00 30.95  ? 8    TYR D CD1 1 
ATOM   4850 C CD2 . TYR D 1 27  ? -4.359  61.961 -46.853 1.00 31.69  ? 8    TYR D CD2 1 
ATOM   4851 C CE1 . TYR D 1 27  ? -2.599  61.345 -44.810 1.00 40.90  ? 8    TYR D CE1 1 
ATOM   4852 C CE2 . TYR D 1 27  ? -4.045  62.922 -45.902 1.00 34.60  ? 8    TYR D CE2 1 
ATOM   4853 C CZ  . TYR D 1 27  ? -3.164  62.605 -44.884 1.00 41.43  ? 8    TYR D CZ  1 
ATOM   4854 O OH  . TYR D 1 27  ? -2.836  63.547 -43.947 1.00 50.40  ? 8    TYR D OH  1 
ATOM   4855 N N   . ASN D 1 28  ? -7.168  59.833 -47.722 1.00 23.69  ? 9    ASN D N   1 
ATOM   4856 C CA  . ASN D 1 28  ? -8.435  60.443 -47.340 1.00 21.41  ? 9    ASN D CA  1 
ATOM   4857 C C   . ASN D 1 28  ? -9.351  59.471 -46.609 1.00 23.70  ? 9    ASN D C   1 
ATOM   4858 O O   . ASN D 1 28  ? -9.988  59.832 -45.620 1.00 23.25  ? 9    ASN D O   1 
ATOM   4859 C CB  . ASN D 1 28  ? -9.146  61.028 -48.562 1.00 22.97  ? 9    ASN D CB  1 
ATOM   4860 C CG  . ASN D 1 28  ? -8.332  62.119 -49.245 1.00 28.81  ? 9    ASN D CG  1 
ATOM   4861 O OD1 . ASN D 1 28  ? -7.494  62.778 -48.604 1.00 32.20  ? 9    ASN D OD1 1 
ATOM   4862 N ND2 . ASN D 1 28  ? -8.560  62.310 -50.557 1.00 22.06  ? 9    ASN D ND2 1 
ATOM   4863 N N   . ILE D 1 29  ? -9.408  58.232 -47.086 1.00 23.80  ? 10   ILE D N   1 
ATOM   4864 C CA  . ILE D 1 29  ? -10.266 57.242 -46.452 1.00 25.78  ? 10   ILE D CA  1 
ATOM   4865 C C   . ILE D 1 29  ? -9.818  56.963 -45.024 1.00 24.74  ? 10   ILE D C   1 
ATOM   4866 O O   . ILE D 1 29  ? -10.633 56.914 -44.112 1.00 24.31  ? 10   ILE D O   1 
ATOM   4867 C CB  . ILE D 1 29  ? -10.363 55.937 -47.262 1.00 23.13  ? 10   ILE D CB  1 
ATOM   4868 C CG1 . ILE D 1 29  ? -11.135 56.193 -48.552 1.00 20.50  ? 10   ILE D CG1 1 
ATOM   4869 C CG2 . ILE D 1 29  ? -11.057 54.850 -46.450 1.00 22.70  ? 10   ILE D CG2 1 
ATOM   4870 C CD1 . ILE D 1 29  ? -11.312 54.967 -49.412 1.00 22.06  ? 10   ILE D CD1 1 
ATOM   4871 N N   . ARG D 1 30  ? -8.518  56.815 -44.827 1.00 22.01  ? 11   ARG D N   1 
ATOM   4872 C CA  . ARG D 1 30  ? -8.008  56.582 -43.487 1.00 24.82  ? 11   ARG D CA  1 
ATOM   4873 C C   . ARG D 1 30  ? -8.339  57.718 -42.507 1.00 30.86  ? 11   ARG D C   1 
ATOM   4874 O O   . ARG D 1 30  ? -8.582  57.468 -41.329 1.00 33.30  ? 11   ARG D O   1 
ATOM   4875 C CB  . ARG D 1 30  ? -6.504  56.313 -43.503 1.00 31.34  ? 11   ARG D CB  1 
ATOM   4876 C CG  . ARG D 1 30  ? -6.102  55.177 -42.580 1.00 46.87  ? 11   ARG D CG  1 
ATOM   4877 C CD  . ARG D 1 30  ? -4.746  55.407 -41.962 1.00 58.96  ? 11   ARG D CD  1 
ATOM   4878 N NE  . ARG D 1 30  ? -4.615  54.631 -40.731 1.00 81.76  ? 11   ARG D NE  1 
ATOM   4879 C CZ  . ARG D 1 30  ? -3.546  54.639 -39.940 1.00 84.31  ? 11   ARG D CZ  1 
ATOM   4880 N NH1 . ARG D 1 30  ? -2.485  55.383 -40.248 1.00 74.76  ? 11   ARG D NH1 1 
ATOM   4881 N NH2 . ARG D 1 30  ? -3.543  53.896 -38.840 1.00 80.51  ? 11   ARG D NH2 1 
ATOM   4882 N N   . GLN D 1 31  ? -8.387  58.953 -43.005 1.00 31.47  ? 12   GLN D N   1 
ATOM   4883 C CA  . GLN D 1 31  ? -8.571  60.133 -42.158 1.00 23.34  ? 12   GLN D CA  1 
ATOM   4884 C C   . GLN D 1 31  ? -10.019 60.506 -41.852 1.00 25.35  ? 12   GLN D C   1 
ATOM   4885 O O   . GLN D 1 31  ? -10.271 61.233 -40.902 1.00 33.43  ? 12   GLN D O   1 
ATOM   4886 C CB  . GLN D 1 31  ? -7.897  61.360 -42.781 1.00 29.34  ? 12   GLN D CB  1 
ATOM   4887 C CG  . GLN D 1 31  ? -6.398  61.244 -43.032 1.00 33.51  ? 12   GLN D CG  1 
ATOM   4888 C CD  . GLN D 1 31  ? -5.594  61.161 -41.750 1.00 40.35  ? 12   GLN D CD  1 
ATOM   4889 O OE1 . GLN D 1 31  ? -6.087  61.483 -40.673 1.00 46.86  ? 12   GLN D OE1 1 
ATOM   4890 N NE2 . GLN D 1 31  ? -4.345  60.729 -41.860 1.00 45.83  ? 12   GLN D NE2 1 
ATOM   4891 N N   . THR D 1 32  ? -10.967 60.037 -42.654 1.00 23.58  ? 13   THR D N   1 
ATOM   4892 C CA  . THR D 1 32  ? -12.331 60.561 -42.575 1.00 22.58  ? 13   THR D CA  1 
ATOM   4893 C C   . THR D 1 32  ? -13.426 59.495 -42.530 1.00 30.14  ? 13   THR D C   1 
ATOM   4894 O O   . THR D 1 32  ? -14.619 59.813 -42.615 1.00 31.88  ? 13   THR D O   1 
ATOM   4895 C CB  . THR D 1 32  ? -12.628 61.469 -43.796 1.00 29.56  ? 13   THR D CB  1 
ATOM   4896 O OG1 . THR D 1 32  ? -12.515 60.701 -45.003 1.00 33.05  ? 13   THR D OG1 1 
ATOM   4897 C CG2 . THR D 1 32  ? -11.674 62.646 -43.861 1.00 24.12  ? 13   THR D CG2 1 
ATOM   4898 N N   . SER D 1 33  ? -12.996 58.252 -42.475 1.00 41.49  ? 14   SER D N   1 
ATOM   4899 C CA  . SER D 1 33  ? -13.813 57.073 -42.733 1.00 36.06  ? 14   SER D CA  1 
ATOM   4900 C C   . SER D 1 33  ? -14.939 56.806 -41.767 1.00 34.83  ? 14   SER D C   1 
ATOM   4901 O O   . SER D 1 33  ? -16.012 56.473 -42.182 1.00 30.60  ? 14   SER D O   1 
ATOM   4902 C CB  . SER D 1 33  ? -12.906 55.862 -42.926 1.00 29.67  ? 14   SER D CB  1 
ATOM   4903 O OG  . SER D 1 33  ? -13.541 54.661 -42.627 1.00 38.04  ? 14   SER D OG  1 
ATOM   4904 N N   . ARG D 1 34  ? -14.711 57.004 -40.485 1.00 35.15  ? 15   ARG D N   1 
ATOM   4905 C CA  . ARG D 1 34  ? -15.713 56.687 -39.471 1.00 39.84  ? 15   ARG D CA  1 
ATOM   4906 C C   . ARG D 1 34  ? -16.222 55.251 -39.383 1.00 33.27  ? 15   ARG D C   1 
ATOM   4907 O O   . ARG D 1 34  ? -17.342 54.980 -39.645 1.00 31.23  ? 15   ARG D O   1 
ATOM   4908 C CB  . ARG D 1 34  ? -16.901 57.645 -39.517 1.00 34.74  ? 15   ARG D CB  1 
ATOM   4909 C CG  . ARG D 1 34  ? -16.610 59.123 -39.441 1.00 31.73  ? 15   ARG D CG  1 
ATOM   4910 C CD  . ARG D 1 34  ? -15.768 59.524 -38.259 1.00 43.91  ? 15   ARG D CD  1 
ATOM   4911 N NE  . ARG D 1 34  ? -16.393 59.215 -36.986 1.00 48.86  ? 15   ARG D NE  1 
ATOM   4912 C CZ  . ARG D 1 34  ? -17.185 60.020 -36.306 1.00 35.97  ? 15   ARG D CZ  1 
ATOM   4913 N NH1 . ARG D 1 34  ? -17.459 61.204 -36.743 1.00 33.93  ? 15   ARG D NH1 1 
ATOM   4914 N NH2 . ARG D 1 34  ? -17.694 59.629 -35.191 1.00 33.21  ? 15   ARG D NH2 1 
ATOM   4915 N N   . PRO D 1 35  ? -15.291 54.320 -38.976 1.00 29.13  ? 16   PRO D N   1 
ATOM   4916 C CA  . PRO D 1 35  ? -15.758 52.940 -38.872 1.00 25.17  ? 16   PRO D CA  1 
ATOM   4917 C C   . PRO D 1 35  ? -16.869 52.625 -37.909 1.00 24.73  ? 16   PRO D C   1 
ATOM   4918 O O   . PRO D 1 35  ? -17.408 51.567 -37.955 1.00 24.74  ? 16   PRO D O   1 
ATOM   4919 C CB  . PRO D 1 35  ? -14.548 52.222 -38.342 1.00 23.03  ? 16   PRO D CB  1 
ATOM   4920 C CG  . PRO D 1 35  ? -13.442 52.893 -38.959 1.00 24.06  ? 16   PRO D CG  1 
ATOM   4921 C CD  . PRO D 1 35  ? -13.775 54.292 -38.759 1.00 32.78  ? 16   PRO D CD  1 
ATOM   4922 N N   . ASP D 1 36  ? -17.107 53.475 -36.950 1.00 25.94  ? 17   ASP D N   1 
ATOM   4923 C CA  . ASP D 1 36  ? -18.081 53.236 -35.925 1.00 21.24  ? 17   ASP D CA  1 
ATOM   4924 C C   . ASP D 1 36  ? -19.412 53.813 -36.219 1.00 21.79  ? 17   ASP D C   1 
ATOM   4925 O O   . ASP D 1 36  ? -20.313 53.685 -35.461 1.00 29.12  ? 17   ASP D O   1 
ATOM   4926 C CB  . ASP D 1 36  ? -17.570 53.835 -34.644 1.00 26.68  ? 17   ASP D CB  1 
ATOM   4927 C CG  . ASP D 1 36  ? -17.137 55.274 -34.795 1.00 51.38  ? 17   ASP D CG  1 
ATOM   4928 O OD1 . ASP D 1 36  ? -16.484 55.645 -35.789 1.00 36.33  ? 17   ASP D OD1 1 
ATOM   4929 O OD2 . ASP D 1 36  ? -17.422 56.043 -33.855 1.00 50.72  ? 17   ASP D OD2 1 
ATOM   4930 N N   . VAL D 1 37  ? -19.531 54.467 -37.333 1.00 20.65  ? 18   VAL D N   1 
ATOM   4931 C CA  . VAL D 1 37  ? -20.762 55.159 -37.698 1.00 21.58  ? 18   VAL D CA  1 
ATOM   4932 C C   . VAL D 1 37  ? -21.444 54.519 -38.896 1.00 20.08  ? 18   VAL D C   1 
ATOM   4933 O O   . VAL D 1 37  ? -20.935 54.587 -40.021 1.00 22.37  ? 18   VAL D O   1 
ATOM   4934 C CB  . VAL D 1 37  ? -20.520 56.644 -38.083 1.00 24.92  ? 18   VAL D CB  1 
ATOM   4935 C CG1 . VAL D 1 37  ? -21.837 57.287 -38.534 1.00 18.66  ? 18   VAL D CG1 1 
ATOM   4936 C CG2 . VAL D 1 37  ? -19.878 57.418 -36.946 1.00 24.41  ? 18   VAL D CG2 1 
ATOM   4937 N N   . ILE D 1 38  ? -22.611 53.934 -38.654 1.00 18.55  ? 19   ILE D N   1 
ATOM   4938 C CA  . ILE D 1 38  ? -23.451 53.374 -39.714 1.00 23.35  ? 19   ILE D CA  1 
ATOM   4939 C C   . ILE D 1 38  ? -23.859 54.453 -40.760 1.00 26.97  ? 19   ILE D C   1 
ATOM   4940 O O   . ILE D 1 38  ? -24.323 55.552 -40.401 1.00 28.20  ? 19   ILE D O   1 
ATOM   4941 C CB  . ILE D 1 38  ? -24.669 52.636 -39.082 1.00 20.95  ? 19   ILE D CB  1 
ATOM   4942 C CG1 . ILE D 1 38  ? -25.525 51.946 -40.133 1.00 22.52  ? 19   ILE D CG1 1 
ATOM   4943 C CG2 . ILE D 1 38  ? -25.512 53.589 -38.230 1.00 28.81  ? 19   ILE D CG2 1 
ATOM   4944 C CD1 . ILE D 1 38  ? -26.573 51.025 -39.499 1.00 26.36  ? 19   ILE D CD1 1 
ATOM   4945 N N   . PRO D 1 39  ? -23.645 54.152 -42.056 1.00 23.71  ? 20   PRO D N   1 
ATOM   4946 C CA  . PRO D 1 39  ? -23.860 55.141 -43.131 1.00 22.14  ? 20   PRO D CA  1 
ATOM   4947 C C   . PRO D 1 39  ? -25.318 55.208 -43.596 1.00 28.17  ? 20   PRO D C   1 
ATOM   4948 O O   . PRO D 1 39  ? -25.624 54.925 -44.752 1.00 33.26  ? 20   PRO D O   1 
ATOM   4949 C CB  . PRO D 1 39  ? -22.946 54.633 -44.264 1.00 26.05  ? 20   PRO D CB  1 
ATOM   4950 C CG  . PRO D 1 39  ? -22.907 53.113 -44.066 1.00 29.48  ? 20   PRO D CG  1 
ATOM   4951 C CD  . PRO D 1 39  ? -23.084 52.876 -42.557 1.00 26.80  ? 20   PRO D CD  1 
ATOM   4952 N N   . THR D 1 40  ? -26.218 55.565 -42.688 1.00 33.46  ? 21   THR D N   1 
ATOM   4953 C CA  . THR D 1 40  ? -27.626 55.720 -43.044 1.00 31.63  ? 21   THR D CA  1 
ATOM   4954 C C   . THR D 1 40  ? -27.787 56.972 -43.888 1.00 46.15  ? 21   THR D C   1 
ATOM   4955 O O   . THR D 1 40  ? -26.979 57.906 -43.793 1.00 45.88  ? 21   THR D O   1 
ATOM   4956 C CB  . THR D 1 40  ? -28.525 55.832 -41.807 1.00 28.97  ? 21   THR D CB  1 
ATOM   4957 O OG1 . THR D 1 40  ? -28.049 56.890 -40.970 1.00 32.35  ? 21   THR D OG1 1 
ATOM   4958 C CG2 . THR D 1 40  ? -28.525 54.518 -41.016 1.00 31.14  ? 21   THR D CG2 1 
ATOM   4959 N N   . GLN D 1 41  ? -28.767 56.956 -44.775 1.00 54.37  ? 22   GLN D N   1 
ATOM   4960 C CA  . GLN D 1 41  ? -29.022 58.085 -45.634 1.00 56.60  ? 22   GLN D CA  1 
ATOM   4961 C C   . GLN D 1 41  ? -30.437 58.542 -45.532 1.00 60.75  ? 22   GLN D C   1 
ATOM   4962 O O   . GLN D 1 41  ? -31.321 57.881 -46.001 1.00 67.52  ? 22   GLN D O   1 
ATOM   4963 C CB  . GLN D 1 41  ? -28.801 57.680 -47.066 1.00 58.22  ? 22   GLN D CB  1 
ATOM   4964 C CG  . GLN D 1 41  ? -27.524 58.173 -47.702 1.00 65.47  ? 22   GLN D CG  1 
ATOM   4965 C CD  . GLN D 1 41  ? -27.496 57.844 -49.174 1.00 78.60  ? 22   GLN D CD  1 
ATOM   4966 O OE1 . GLN D 1 41  ? -27.814 56.737 -49.571 1.00 73.38  ? 22   GLN D OE1 1 
ATOM   4967 N NE2 . GLN D 1 41  ? -27.134 58.814 -49.990 1.00 78.68  ? 22   GLN D NE2 1 
ATOM   4968 N N   . ARG D 1 42  ? -30.640 59.723 -44.993 1.00 68.98  ? 23   ARG D N   1 
ATOM   4969 C CA  . ARG D 1 42  ? -31.965 60.294 -44.867 1.00 78.67  ? 23   ARG D CA  1 
ATOM   4970 C C   . ARG D 1 42  ? -32.963 59.377 -44.150 1.00 70.53  ? 23   ARG D C   1 
ATOM   4971 O O   . ARG D 1 42  ? -34.124 59.275 -44.520 1.00 62.39  ? 23   ARG D O   1 
ATOM   4972 C CB  . ARG D 1 42  ? -32.477 60.815 -46.196 1.00 71.87  ? 23   ARG D CB  1 
ATOM   4973 C CG  . ARG D 1 42  ? -31.790 62.090 -46.646 1.00 80.99  ? 23   ARG D CG  1 
ATOM   4974 C CD  . ARG D 1 42  ? -32.633 62.972 -47.559 1.00 93.71  ? 23   ARG D CD  1 
ATOM   4975 N NE  . ARG D 1 42  ? -32.556 62.617 -48.975 1.00 105.85 ? 23   ARG D NE  1 
ATOM   4976 C CZ  . ARG D 1 42  ? -33.607 62.473 -49.783 1.00 110.55 ? 23   ARG D CZ  1 
ATOM   4977 N NH1 . ARG D 1 42  ? -34.839 62.647 -49.334 1.00 101.79 ? 23   ARG D NH1 1 
ATOM   4978 N NH2 . ARG D 1 42  ? -33.420 62.158 -51.059 1.00 110.33 ? 23   ARG D NH2 1 
ATOM   4979 N N   . ASP D 1 43  ? -32.505 58.752 -43.078 1.00 64.65  ? 24   ASP D N   1 
ATOM   4980 C CA  . ASP D 1 43  ? -33.373 57.960 -42.244 1.00 80.97  ? 24   ASP D CA  1 
ATOM   4981 C C   . ASP D 1 43  ? -33.792 56.606 -42.799 1.00 73.21  ? 24   ASP D C   1 
ATOM   4982 O O   . ASP D 1 43  ? -34.832 56.069 -42.456 1.00 73.16  ? 24   ASP D O   1 
ATOM   4983 C CB  . ASP D 1 43  ? -34.609 58.767 -41.915 1.00 81.39  ? 24   ASP D CB  1 
ATOM   4984 C CG  . ASP D 1 43  ? -35.143 58.456 -40.573 1.00 92.38  ? 24   ASP D CG  1 
ATOM   4985 O OD1 . ASP D 1 43  ? -34.441 58.751 -39.594 1.00 88.80  ? 24   ASP D OD1 1 
ATOM   4986 O OD2 . ASP D 1 43  ? -36.256 57.914 -40.504 1.00 100.67 ? 24   ASP D OD2 1 
ATOM   4987 N N   . ARG D 1 44  ? -32.969 56.051 -43.656 1.00 66.89  ? 25   ARG D N   1 
ATOM   4988 C CA  . ARG D 1 44  ? -33.302 54.818 -44.300 1.00 55.20  ? 25   ARG D CA  1 
ATOM   4989 C C   . ARG D 1 44  ? -32.342 53.751 -43.933 1.00 50.90  ? 25   ARG D C   1 
ATOM   4990 O O   . ARG D 1 44  ? -31.241 53.998 -43.514 1.00 48.34  ? 25   ARG D O   1 
ATOM   4991 C CB  . ARG D 1 44  ? -33.277 54.992 -45.788 1.00 53.88  ? 25   ARG D CB  1 
ATOM   4992 C CG  . ARG D 1 44  ? -33.883 56.286 -46.217 1.00 64.61  ? 25   ARG D CG  1 
ATOM   4993 C CD  . ARG D 1 44  ? -34.741 56.121 -47.441 1.00 73.46  ? 25   ARG D CD  1 
ATOM   4994 N NE  . ARG D 1 44  ? -35.390 57.388 -47.721 1.00 90.80  ? 25   ARG D NE  1 
ATOM   4995 C CZ  . ARG D 1 44  ? -35.052 58.212 -48.702 1.00 87.54  ? 25   ARG D CZ  1 
ATOM   4996 N NH1 . ARG D 1 44  ? -34.085 57.898 -49.545 1.00 75.87  ? 25   ARG D NH1 1 
ATOM   4997 N NH2 . ARG D 1 44  ? -35.711 59.345 -48.845 1.00 92.29  ? 25   ARG D NH2 1 
ATOM   4998 N N   . PRO D 1 45  ? -32.858 52.487 -44.095 1.00 36.82  ? 26   PRO D N   1 
ATOM   4999 C CA  . PRO D 1 45  ? -31.931 51.405 -43.814 1.00 37.32  ? 26   PRO D CA  1 
ATOM   5000 C C   . PRO D 1 45  ? -30.715 51.376 -44.704 1.00 35.90  ? 26   PRO D C   1 
ATOM   5001 O O   . PRO D 1 45  ? -30.803 51.772 -45.814 1.00 37.15  ? 26   PRO D O   1 
ATOM   5002 C CB  . PRO D 1 45  ? -32.744 50.191 -44.165 1.00 37.86  ? 26   PRO D CB  1 
ATOM   5003 C CG  . PRO D 1 45  ? -34.073 50.540 -43.765 1.00 40.29  ? 26   PRO D CG  1 
ATOM   5004 C CD  . PRO D 1 45  ? -34.218 51.857 -44.357 1.00 34.72  ? 26   PRO D CD  1 
ATOM   5005 N N   . VAL D 1 46  ? -29.583 50.918 -44.214 1.00 30.53  ? 27   VAL D N   1 
ATOM   5006 C CA  . VAL D 1 46  ? -28.520 50.566 -45.124 1.00 24.42  ? 27   VAL D CA  1 
ATOM   5007 C C   . VAL D 1 46  ? -28.930 49.248 -45.748 1.00 29.14  ? 27   VAL D C   1 
ATOM   5008 O O   . VAL D 1 46  ? -29.221 48.285 -45.036 1.00 28.78  ? 27   VAL D O   1 
ATOM   5009 C CB  . VAL D 1 46  ? -27.210 50.363 -44.375 1.00 22.77  ? 27   VAL D CB  1 
ATOM   5010 C CG1 . VAL D 1 46  ? -26.104 49.948 -45.349 1.00 24.60  ? 27   VAL D CG1 1 
ATOM   5011 C CG2 . VAL D 1 46  ? -26.840 51.634 -43.624 1.00 27.49  ? 27   VAL D CG2 1 
ATOM   5012 N N   . ALA D 1 47  ? -28.985 49.185 -47.071 1.00 28.54  ? 28   ALA D N   1 
ATOM   5013 C CA  . ALA D 1 47  ? -29.367 47.932 -47.692 1.00 24.16  ? 28   ALA D CA  1 
ATOM   5014 C C   . ALA D 1 47  ? -28.128 47.064 -47.866 1.00 28.89  ? 28   ALA D C   1 
ATOM   5015 O O   . ALA D 1 47  ? -27.245 47.366 -48.679 1.00 25.50  ? 28   ALA D O   1 
ATOM   5016 C CB  . ALA D 1 47  ? -30.051 48.170 -49.001 1.00 21.99  ? 28   ALA D CB  1 
ATOM   5017 N N   . VAL D 1 48  ? -28.067 45.979 -47.099 1.00 28.66  ? 29   VAL D N   1 
ATOM   5018 C CA  . VAL D 1 48  ? -26.968 45.024 -47.210 1.00 23.83  ? 29   VAL D CA  1 
ATOM   5019 C C   . VAL D 1 48  ? -27.418 43.811 -48.007 1.00 23.57  ? 29   VAL D C   1 
ATOM   5020 O O   . VAL D 1 48  ? -28.475 43.253 -47.734 1.00 31.70  ? 29   VAL D O   1 
ATOM   5021 C CB  . VAL D 1 48  ? -26.502 44.575 -45.806 1.00 23.61  ? 29   VAL D CB  1 
ATOM   5022 C CG1 . VAL D 1 48  ? -25.307 43.633 -45.906 1.00 18.20  ? 29   VAL D CG1 1 
ATOM   5023 C CG2 . VAL D 1 48  ? -26.194 45.788 -44.921 1.00 17.19  ? 29   VAL D CG2 1 
ATOM   5024 N N   . SER D 1 49  ? -26.626 43.395 -48.985 1.00 23.08  ? 30   SER D N   1 
ATOM   5025 C CA  . SER D 1 49  ? -26.919 42.147 -49.693 1.00 25.80  ? 30   SER D CA  1 
ATOM   5026 C C   . SER D 1 49  ? -25.999 41.079 -49.188 1.00 26.67  ? 30   SER D C   1 
ATOM   5027 O O   . SER D 1 49  ? -24.818 41.331 -48.978 1.00 27.48  ? 30   SER D O   1 
ATOM   5028 C CB  . SER D 1 49  ? -26.680 42.299 -51.185 1.00 25.53  ? 30   SER D CB  1 
ATOM   5029 O OG  . SER D 1 49  ? -27.202 43.532 -51.624 1.00 46.92  ? 30   SER D OG  1 
ATOM   5030 N N   . VAL D 1 50  ? -26.533 39.879 -49.012 1.00 30.90  ? 31   VAL D N   1 
ATOM   5031 C CA  . VAL D 1 50  ? -25.733 38.751 -48.547 1.00 30.09  ? 31   VAL D CA  1 
ATOM   5032 C C   . VAL D 1 50  ? -25.891 37.544 -49.462 1.00 27.31  ? 31   VAL D C   1 
ATOM   5033 O O   . VAL D 1 50  ? -26.989 37.175 -49.825 1.00 35.59  ? 31   VAL D O   1 
ATOM   5034 C CB  . VAL D 1 50  ? -26.138 38.332 -47.129 1.00 31.05  ? 31   VAL D CB  1 
ATOM   5035 C CG1 . VAL D 1 50  ? -25.251 37.203 -46.652 1.00 28.86  ? 31   VAL D CG1 1 
ATOM   5036 C CG2 . VAL D 1 50  ? -26.055 39.523 -46.176 1.00 34.74  ? 31   VAL D CG2 1 
ATOM   5037 N N   . SER D 1 51  ? -24.784 36.921 -49.821 1.00 28.35  ? 32   SER D N   1 
ATOM   5038 C CA  . SER D 1 51  ? -24.825 35.726 -50.642 1.00 29.59  ? 32   SER D CA  1 
ATOM   5039 C C   . SER D 1 51  ? -23.737 34.732 -50.183 1.00 28.57  ? 32   SER D C   1 
ATOM   5040 O O   . SER D 1 51  ? -22.567 35.106 -50.053 1.00 27.45  ? 32   SER D O   1 
ATOM   5041 C CB  . SER D 1 51  ? -24.640 36.111 -52.117 1.00 33.28  ? 32   SER D CB  1 
ATOM   5042 O OG  . SER D 1 51  ? -24.691 34.969 -52.958 1.00 36.32  ? 32   SER D OG  1 
ATOM   5043 N N   . LEU D 1 52  ? -24.112 33.476 -49.935 1.00 26.63  ? 33   LEU D N   1 
ATOM   5044 C CA  . LEU D 1 52  ? -23.122 32.450 -49.597 1.00 22.87  ? 33   LEU D CA  1 
ATOM   5045 C C   . LEU D 1 52  ? -22.758 31.589 -50.803 1.00 21.23  ? 33   LEU D C   1 
ATOM   5046 O O   . LEU D 1 52  ? -23.637 31.065 -51.472 1.00 32.37  ? 33   LEU D O   1 
ATOM   5047 C CB  . LEU D 1 52  ? -23.624 31.537 -48.475 1.00 23.60  ? 33   LEU D CB  1 
ATOM   5048 C CG  . LEU D 1 52  ? -24.159 32.250 -47.238 1.00 23.27  ? 33   LEU D CG  1 
ATOM   5049 C CD1 . LEU D 1 52  ? -24.370 31.272 -46.082 1.00 23.03  ? 33   LEU D CD1 1 
ATOM   5050 C CD2 . LEU D 1 52  ? -23.237 33.390 -46.824 1.00 24.36  ? 33   LEU D CD2 1 
ATOM   5051 N N   . LYS D 1 53  ? -21.467 31.440 -51.073 1.00 18.53  ? 34   LYS D N   1 
ATOM   5052 C CA  . LYS D 1 53  ? -21.005 30.520 -52.094 1.00 18.62  ? 34   LYS D CA  1 
ATOM   5053 C C   . LYS D 1 53  ? -20.330 29.365 -51.384 1.00 22.86  ? 34   LYS D C   1 
ATOM   5054 O O   . LYS D 1 53  ? -19.280 29.551 -50.752 1.00 21.71  ? 34   LYS D O   1 
ATOM   5055 C CB  . LYS D 1 53  ? -20.007 31.194 -53.025 1.00 19.94  ? 34   LYS D CB  1 
ATOM   5056 C CG  . LYS D 1 53  ? -20.370 32.608 -53.412 1.00 31.20  ? 34   LYS D CG  1 
ATOM   5057 C CD  . LYS D 1 53  ? -21.499 32.663 -54.427 1.00 34.90  ? 34   LYS D CD  1 
ATOM   5058 C CE  . LYS D 1 53  ? -21.832 34.113 -54.801 1.00 42.48  ? 34   LYS D CE  1 
ATOM   5059 N NZ  . LYS D 1 53  ? -22.977 34.189 -55.765 1.00 54.13  ? 34   LYS D NZ  1 
ATOM   5060 N N   . PHE D 1 54  ? -20.912 28.170 -51.481 1.00 24.08  ? 35   PHE D N   1 
ATOM   5061 C CA  . PHE D 1 54  ? -20.345 27.035 -50.763 1.00 22.08  ? 35   PHE D CA  1 
ATOM   5062 C C   . PHE D 1 54  ? -19.111 26.478 -51.440 1.00 22.90  ? 35   PHE D C   1 
ATOM   5063 O O   . PHE D 1 54  ? -19.081 26.296 -52.653 1.00 24.91  ? 35   PHE D O   1 
ATOM   5064 C CB  . PHE D 1 54  ? -21.392 25.961 -50.527 1.00 21.78  ? 35   PHE D CB  1 
ATOM   5065 C CG  . PHE D 1 54  ? -22.490 26.420 -49.654 1.00 21.89  ? 35   PHE D CG  1 
ATOM   5066 C CD1 . PHE D 1 54  ? -22.343 26.406 -48.277 1.00 20.31  ? 35   PHE D CD1 1 
ATOM   5067 C CD2 . PHE D 1 54  ? -23.654 26.929 -50.204 1.00 27.88  ? 35   PHE D CD2 1 
ATOM   5068 C CE1 . PHE D 1 54  ? -23.367 26.863 -47.443 1.00 26.66  ? 35   PHE D CE1 1 
ATOM   5069 C CE2 . PHE D 1 54  ? -24.681 27.396 -49.384 1.00 36.69  ? 35   PHE D CE2 1 
ATOM   5070 C CZ  . PHE D 1 54  ? -24.540 27.359 -47.997 1.00 31.16  ? 35   PHE D CZ  1 
ATOM   5071 N N   . ILE D 1 55  ? -18.083 26.237 -50.637 1.00 20.05  ? 36   ILE D N   1 
ATOM   5072 C CA  . ILE D 1 55  ? -16.823 25.745 -51.166 1.00 26.16  ? 36   ILE D CA  1 
ATOM   5073 C C   . ILE D 1 55  ? -16.553 24.301 -50.729 1.00 29.58  ? 36   ILE D C   1 
ATOM   5074 O O   . ILE D 1 55  ? -15.979 23.516 -51.492 1.00 31.69  ? 36   ILE D O   1 
ATOM   5075 C CB  . ILE D 1 55  ? -15.626 26.658 -50.760 1.00 27.34  ? 36   ILE D CB  1 
ATOM   5076 C CG1 . ILE D 1 55  ? -15.959 28.143 -50.966 1.00 21.31  ? 36   ILE D CG1 1 
ATOM   5077 C CG2 . ILE D 1 55  ? -14.366 26.261 -51.528 1.00 22.65  ? 36   ILE D CG2 1 
ATOM   5078 C CD1 . ILE D 1 55  ? -16.353 28.500 -52.390 1.00 21.81  ? 36   ILE D CD1 1 
ATOM   5079 N N   . ASN D 1 56  ? -16.960 23.948 -49.508 1.00 22.92  ? 37   ASN D N   1 
ATOM   5080 C CA  . ASN D 1 56  ? -16.729 22.596 -49.009 1.00 19.36  ? 37   ASN D CA  1 
ATOM   5081 C C   . ASN D 1 56  ? -17.638 22.197 -47.859 1.00 23.90  ? 37   ASN D C   1 
ATOM   5082 O O   . ASN D 1 56  ? -18.146 23.044 -47.134 1.00 25.62  ? 37   ASN D O   1 
ATOM   5083 C CB  . ASN D 1 56  ? -15.279 22.456 -48.574 1.00 26.93  ? 37   ASN D CB  1 
ATOM   5084 C CG  . ASN D 1 56  ? -14.668 21.128 -48.986 1.00 24.77  ? 37   ASN D CG  1 
ATOM   5085 O OD1 . ASN D 1 56  ? -15.292 20.076 -48.847 1.00 22.10  ? 37   ASN D OD1 1 
ATOM   5086 N ND2 . ASN D 1 56  ? -13.436 21.177 -49.501 1.00 25.54  ? 37   ASN D ND2 1 
ATOM   5087 N N   . ILE D 1 57  ? -17.851 20.896 -47.695 1.00 24.33  ? 38   ILE D N   1 
ATOM   5088 C CA  . ILE D 1 57  ? -18.571 20.383 -46.532 1.00 19.60  ? 38   ILE D CA  1 
ATOM   5089 C C   . ILE D 1 57  ? -17.662 19.335 -45.924 1.00 23.61  ? 38   ILE D C   1 
ATOM   5090 O O   . ILE D 1 57  ? -17.188 18.450 -46.630 1.00 27.09  ? 38   ILE D O   1 
ATOM   5091 C CB  . ILE D 1 57  ? -19.939 19.809 -46.918 1.00 16.05  ? 38   ILE D CB  1 
ATOM   5092 C CG1 . ILE D 1 57  ? -20.822 20.927 -47.448 1.00 16.65  ? 38   ILE D CG1 1 
ATOM   5093 C CG2 . ILE D 1 57  ? -20.608 19.160 -45.733 1.00 14.86  ? 38   ILE D CG2 1 
ATOM   5094 C CD1 . ILE D 1 57  ? -22.149 20.489 -47.935 1.00 19.26  ? 38   ILE D CD1 1 
ATOM   5095 N N   . LEU D 1 58  ? -17.373 19.454 -44.630 1.00 28.52  ? 39   LEU D N   1 
ATOM   5096 C CA  . LEU D 1 58  ? -16.172 18.812 -44.087 1.00 26.73  ? 39   LEU D CA  1 
ATOM   5097 C C   . LEU D 1 58  ? -16.424 17.731 -43.079 1.00 34.43  ? 39   LEU D C   1 
ATOM   5098 O O   . LEU D 1 58  ? -15.841 16.654 -43.170 1.00 40.28  ? 39   LEU D O   1 
ATOM   5099 C CB  . LEU D 1 58  ? -15.221 19.844 -43.480 1.00 26.53  ? 39   LEU D CB  1 
ATOM   5100 C CG  . LEU D 1 58  ? -14.480 20.738 -44.464 1.00 30.48  ? 39   LEU D CG  1 
ATOM   5101 C CD1 . LEU D 1 58  ? -13.598 21.699 -43.709 1.00 25.44  ? 39   LEU D CD1 1 
ATOM   5102 C CD2 . LEU D 1 58  ? -13.650 19.898 -45.438 1.00 33.75  ? 39   LEU D CD2 1 
ATOM   5103 N N   . GLU D 1 59  ? -17.253 18.020 -42.088 1.00 33.31  ? 40   GLU D N   1 
ATOM   5104 C CA  . GLU D 1 59  ? -17.422 17.063 -41.008 1.00 41.02  ? 40   GLU D CA  1 
ATOM   5105 C C   . GLU D 1 59  ? -18.859 16.997 -40.599 1.00 47.18  ? 40   GLU D C   1 
ATOM   5106 O O   . GLU D 1 59  ? -19.368 17.863 -39.886 1.00 54.44  ? 40   GLU D O   1 
ATOM   5107 C CB  . GLU D 1 59  ? -16.534 17.398 -39.810 1.00 49.83  ? 40   GLU D CB  1 
ATOM   5108 C CG  . GLU D 1 59  ? -15.408 16.398 -39.610 1.00 69.63  ? 40   GLU D CG  1 
ATOM   5109 C CD  . GLU D 1 59  ? -14.165 17.034 -39.009 1.00 82.43  ? 40   GLU D CD  1 
ATOM   5110 O OE1 . GLU D 1 59  ? -14.186 18.265 -38.758 1.00 77.25  ? 40   GLU D OE1 1 
ATOM   5111 O OE2 . GLU D 1 59  ? -13.172 16.301 -38.793 1.00 97.63  ? 40   GLU D OE2 1 
ATOM   5112 N N   . VAL D 1 60  ? -19.523 15.953 -41.057 1.00 45.49  ? 41   VAL D N   1 
ATOM   5113 C CA  . VAL D 1 60  ? -20.935 15.838 -40.789 1.00 36.30  ? 41   VAL D CA  1 
ATOM   5114 C C   . VAL D 1 60  ? -21.119 14.805 -39.698 1.00 31.50  ? 41   VAL D C   1 
ATOM   5115 O O   . VAL D 1 60  ? -20.399 13.806 -39.651 1.00 34.88  ? 41   VAL D O   1 
ATOM   5116 C CB  . VAL D 1 60  ? -21.692 15.476 -42.067 1.00 37.44  ? 41   VAL D CB  1 
ATOM   5117 C CG1 . VAL D 1 60  ? -23.101 15.157 -41.760 1.00 34.85  ? 41   VAL D CG1 1 
ATOM   5118 C CG2 . VAL D 1 60  ? -21.633 16.635 -43.047 1.00 34.73  ? 41   VAL D CG2 1 
ATOM   5119 N N   . ASN D 1 61  ? -22.044 15.084 -38.790 1.00 27.08  ? 42   ASN D N   1 
ATOM   5120 C CA  . ASN D 1 61  ? -22.387 14.160 -37.724 1.00 29.53  ? 42   ASN D CA  1 
ATOM   5121 C C   . ASN D 1 61  ? -23.910 14.116 -37.632 1.00 34.45  ? 42   ASN D C   1 
ATOM   5122 O O   . ASN D 1 61  ? -24.554 15.060 -37.163 1.00 35.70  ? 42   ASN D O   1 
ATOM   5123 C CB  . ASN D 1 61  ? -21.733 14.574 -36.394 1.00 28.84  ? 42   ASN D CB  1 
ATOM   5124 C CG  . ASN D 1 61  ? -21.897 13.533 -35.299 1.00 31.74  ? 42   ASN D CG  1 
ATOM   5125 O OD1 . ASN D 1 61  ? -22.945 12.890 -35.173 1.00 32.42  ? 42   ASN D OD1 1 
ATOM   5126 N ND2 . ASN D 1 61  ? -20.857 13.372 -34.485 1.00 40.32  ? 42   ASN D ND2 1 
ATOM   5127 N N   . GLU D 1 62  ? -24.483 13.011 -38.105 1.00 42.31  ? 43   GLU D N   1 
ATOM   5128 C CA  . GLU D 1 62  ? -25.938 12.825 -38.105 1.00 35.73  ? 43   GLU D CA  1 
ATOM   5129 C C   . GLU D 1 62  ? -26.455 12.570 -36.694 1.00 35.32  ? 43   GLU D C   1 
ATOM   5130 O O   . GLU D 1 62  ? -27.598 12.899 -36.388 1.00 31.16  ? 43   GLU D O   1 
ATOM   5131 C CB  . GLU D 1 62  ? -26.340 11.681 -39.044 1.00 37.93  ? 43   GLU D CB  1 
ATOM   5132 C CG  . GLU D 1 62  ? -27.798 11.735 -39.534 1.00 45.96  ? 43   GLU D CG  1 
ATOM   5133 C CD  . GLU D 1 62  ? -28.150 10.626 -40.547 1.00 61.23  ? 43   GLU D CD  1 
ATOM   5134 O OE1 . GLU D 1 62  ? -27.222 9.943  -41.061 1.00 57.87  ? 43   GLU D OE1 1 
ATOM   5135 O OE2 . GLU D 1 62  ? -29.365 10.451 -40.828 1.00 57.99  ? 43   GLU D OE2 1 
ATOM   5136 N N   . ILE D 1 63  ? -25.605 11.996 -35.837 1.00 35.93  ? 44   ILE D N   1 
ATOM   5137 C CA  . ILE D 1 63  ? -25.970 11.762 -34.443 1.00 36.06  ? 44   ILE D CA  1 
ATOM   5138 C C   . ILE D 1 63  ? -26.193 13.066 -33.675 1.00 39.10  ? 44   ILE D C   1 
ATOM   5139 O O   . ILE D 1 63  ? -27.201 13.208 -32.979 1.00 48.23  ? 44   ILE D O   1 
ATOM   5140 C CB  . ILE D 1 63  ? -24.911 10.947 -33.656 1.00 42.07  ? 44   ILE D CB  1 
ATOM   5141 C CG1 . ILE D 1 63  ? -24.564 9.632  -34.363 1.00 41.89  ? 44   ILE D CG1 1 
ATOM   5142 C CG2 . ILE D 1 63  ? -25.394 10.711 -32.214 1.00 38.79  ? 44   ILE D CG2 1 
ATOM   5143 C CD1 . ILE D 1 63  ? -25.708 8.650  -34.449 1.00 44.30  ? 44   ILE D CD1 1 
ATOM   5144 N N   . THR D 1 64  ? -25.256 14.008 -33.793 1.00 35.83  ? 45   THR D N   1 
ATOM   5145 C CA  . THR D 1 64  ? -25.308 15.242 -33.004 1.00 34.61  ? 45   THR D CA  1 
ATOM   5146 C C   . THR D 1 64  ? -25.899 16.410 -33.769 1.00 33.85  ? 45   THR D C   1 
ATOM   5147 O O   . THR D 1 64  ? -26.031 17.501 -33.214 1.00 42.38  ? 45   THR D O   1 
ATOM   5148 C CB  . THR D 1 64  ? -23.928 15.682 -32.542 1.00 33.23  ? 45   THR D CB  1 
ATOM   5149 O OG1 . THR D 1 64  ? -23.154 16.049 -33.687 1.00 31.88  ? 45   THR D OG1 1 
ATOM   5150 C CG2 . THR D 1 64  ? -23.234 14.571 -31.785 1.00 31.81  ? 45   THR D CG2 1 
ATOM   5151 N N   . ASN D 1 65  ? -26.230 16.186 -35.036 1.00 30.11  ? 46   ASN D N   1 
ATOM   5152 C CA  . ASN D 1 65  ? -26.766 17.238 -35.890 1.00 32.41  ? 46   ASN D CA  1 
ATOM   5153 C C   . ASN D 1 65  ? -25.856 18.481 -36.045 1.00 34.93  ? 46   ASN D C   1 
ATOM   5154 O O   . ASN D 1 65  ? -26.277 19.615 -35.794 1.00 36.09  ? 46   ASN D O   1 
ATOM   5155 C CB  . ASN D 1 65  ? -28.172 17.635 -35.425 1.00 32.03  ? 46   ASN D CB  1 
ATOM   5156 C CG  . ASN D 1 65  ? -29.276 16.813 -36.093 1.00 37.06  ? 46   ASN D CG  1 
ATOM   5157 O OD1 . ASN D 1 65  ? -29.087 16.199 -37.151 1.00 44.20  ? 46   ASN D OD1 1 
ATOM   5158 N ND2 . ASN D 1 65  ? -30.447 16.828 -35.486 1.00 35.60  ? 46   ASN D ND2 1 
ATOM   5159 N N   . GLU D 1 66  ? -24.617 18.249 -36.471 1.00 31.49  ? 47   GLU D N   1 
ATOM   5160 C CA  . GLU D 1 66  ? -23.636 19.305 -36.627 1.00 30.23  ? 47   GLU D CA  1 
ATOM   5161 C C   . GLU D 1 66  ? -22.905 19.188 -37.952 1.00 26.04  ? 47   GLU D C   1 
ATOM   5162 O O   . GLU D 1 66  ? -22.507 18.107 -38.334 1.00 31.67  ? 47   GLU D O   1 
ATOM   5163 C CB  . GLU D 1 66  ? -22.634 19.245 -35.474 1.00 32.95  ? 47   GLU D CB  1 
ATOM   5164 C CG  . GLU D 1 66  ? -23.261 19.544 -34.124 1.00 43.68  ? 47   GLU D CG  1 
ATOM   5165 C CD  . GLU D 1 66  ? -22.267 19.491 -32.966 1.00 57.74  ? 47   GLU D CD  1 
ATOM   5166 O OE1 . GLU D 1 66  ? -21.031 19.529 -33.228 1.00 52.76  ? 47   GLU D OE1 1 
ATOM   5167 O OE2 . GLU D 1 66  ? -22.741 19.411 -31.798 1.00 52.75  ? 47   GLU D OE2 1 
ATOM   5168 N N   . VAL D 1 67  ? -22.712 20.303 -38.643 1.00 23.86  ? 48   VAL D N   1 
ATOM   5169 C CA  . VAL D 1 67  ? -21.919 20.290 -39.866 1.00 29.95  ? 48   VAL D CA  1 
ATOM   5170 C C   . VAL D 1 67  ? -20.773 21.309 -39.832 1.00 34.55  ? 48   VAL D C   1 
ATOM   5171 O O   . VAL D 1 67  ? -20.817 22.291 -39.083 1.00 34.06  ? 48   VAL D O   1 
ATOM   5172 C CB  . VAL D 1 67  ? -22.790 20.556 -41.104 1.00 28.95  ? 48   VAL D CB  1 
ATOM   5173 C CG1 . VAL D 1 67  ? -23.901 19.545 -41.185 1.00 31.31  ? 48   VAL D CG1 1 
ATOM   5174 C CG2 . VAL D 1 67  ? -23.371 21.956 -41.042 1.00 30.52  ? 48   VAL D CG2 1 
ATOM   5175 N N   . ASP D 1 68  ? -19.755 21.058 -40.654 1.00 33.84  ? 49   ASP D N   1 
ATOM   5176 C CA  . ASP D 1 68  ? -18.616 21.949 -40.812 1.00 28.11  ? 49   ASP D CA  1 
ATOM   5177 C C   . ASP D 1 68  ? -18.573 22.484 -42.229 1.00 28.40  ? 49   ASP D C   1 
ATOM   5178 O O   . ASP D 1 68  ? -18.307 21.736 -43.168 1.00 30.97  ? 49   ASP D O   1 
ATOM   5179 C CB  . ASP D 1 68  ? -17.333 21.185 -40.552 1.00 32.36  ? 49   ASP D CB  1 
ATOM   5180 C CG  . ASP D 1 68  ? -16.432 21.897 -39.578 1.00 47.27  ? 49   ASP D CG  1 
ATOM   5181 O OD1 . ASP D 1 68  ? -16.967 22.685 -38.765 1.00 58.09  ? 49   ASP D OD1 1 
ATOM   5182 O OD2 . ASP D 1 68  ? -15.198 21.679 -39.621 1.00 50.01  ? 49   ASP D OD2 1 
ATOM   5183 N N   . VAL D 1 69  ? -18.823 23.773 -42.402 1.00 23.59  ? 50   VAL D N   1 
ATOM   5184 C CA  . VAL D 1 69  ? -18.902 24.312 -43.746 1.00 20.56  ? 50   VAL D CA  1 
ATOM   5185 C C   . VAL D 1 69  ? -17.781 25.322 -44.047 1.00 24.26  ? 50   VAL D C   1 
ATOM   5186 O O   . VAL D 1 69  ? -17.325 26.041 -43.154 1.00 27.51  ? 50   VAL D O   1 
ATOM   5187 C CB  . VAL D 1 69  ? -20.282 24.908 -43.980 1.00 19.50  ? 50   VAL D CB  1 
ATOM   5188 C CG1 . VAL D 1 69  ? -20.419 25.389 -45.405 1.00 30.08  ? 50   VAL D CG1 1 
ATOM   5189 C CG2 . VAL D 1 69  ? -21.332 23.853 -43.686 1.00 20.49  ? 50   VAL D CG2 1 
ATOM   5190 N N   . VAL D 1 70  ? -17.307 25.328 -45.289 1.00 17.31  ? 51   VAL D N   1 
ATOM   5191 C CA  . VAL D 1 70  ? -16.475 26.408 -45.787 1.00 15.73  ? 51   VAL D CA  1 
ATOM   5192 C C   . VAL D 1 70  ? -17.240 27.106 -46.904 1.00 17.82  ? 51   VAL D C   1 
ATOM   5193 O O   . VAL D 1 70  ? -17.684 26.469 -47.860 1.00 21.16  ? 51   VAL D O   1 
ATOM   5194 C CB  . VAL D 1 70  ? -15.134 25.894 -46.331 1.00 22.91  ? 51   VAL D CB  1 
ATOM   5195 C CG1 . VAL D 1 70  ? -14.403 26.997 -47.075 1.00 15.86  ? 51   VAL D CG1 1 
ATOM   5196 C CG2 . VAL D 1 70  ? -14.279 25.339 -45.195 1.00 18.79  ? 51   VAL D CG2 1 
ATOM   5197 N N   . PHE D 1 71  ? -17.386 28.422 -46.788 1.00 21.22  ? 52   PHE D N   1 
ATOM   5198 C CA  . PHE D 1 71  ? -18.156 29.206 -47.751 1.00 19.50  ? 52   PHE D CA  1 
ATOM   5199 C C   . PHE D 1 71  ? -17.619 30.631 -47.889 1.00 18.89  ? 52   PHE D C   1 
ATOM   5200 O O   . PHE D 1 71  ? -16.994 31.152 -46.955 1.00 21.07  ? 52   PHE D O   1 
ATOM   5201 C CB  . PHE D 1 71  ? -19.616 29.249 -47.314 1.00 16.28  ? 52   PHE D CB  1 
ATOM   5202 C CG  . PHE D 1 71  ? -19.812 29.833 -45.956 1.00 16.18  ? 52   PHE D CG  1 
ATOM   5203 C CD1 . PHE D 1 71  ? -19.667 29.045 -44.826 1.00 17.05  ? 52   PHE D CD1 1 
ATOM   5204 C CD2 . PHE D 1 71  ? -20.139 31.177 -45.802 1.00 21.84  ? 52   PHE D CD2 1 
ATOM   5205 C CE1 . PHE D 1 71  ? -19.826 29.581 -43.548 1.00 19.80  ? 52   PHE D CE1 1 
ATOM   5206 C CE2 . PHE D 1 71  ? -20.311 31.739 -44.527 1.00 22.11  ? 52   PHE D CE2 1 
ATOM   5207 C CZ  . PHE D 1 71  ? -20.153 30.929 -43.393 1.00 22.27  ? 52   PHE D CZ  1 
ATOM   5208 N N   . TRP D 1 72  ? -17.861 31.255 -49.047 1.00 16.81  ? 53   TRP D N   1 
ATOM   5209 C CA  . TRP D 1 72  ? -17.594 32.685 -49.210 1.00 20.21  ? 53   TRP D CA  1 
ATOM   5210 C C   . TRP D 1 72  ? -18.826 33.416 -48.758 1.00 20.68  ? 53   TRP D C   1 
ATOM   5211 O O   . TRP D 1 72  ? -19.926 33.044 -49.137 1.00 21.17  ? 53   TRP D O   1 
ATOM   5212 C CB  . TRP D 1 72  ? -17.299 33.089 -50.670 1.00 19.46  ? 53   TRP D CB  1 
ATOM   5213 C CG  . TRP D 1 72  ? -16.061 32.469 -51.258 1.00 20.90  ? 53   TRP D CG  1 
ATOM   5214 C CD1 . TRP D 1 72  ? -15.193 31.595 -50.640 1.00 23.44  ? 53   TRP D CD1 1 
ATOM   5215 C CD2 . TRP D 1 72  ? -15.561 32.656 -52.580 1.00 19.12  ? 53   TRP D CD2 1 
ATOM   5216 N NE1 . TRP D 1 72  ? -14.191 31.230 -51.504 1.00 20.23  ? 53   TRP D NE1 1 
ATOM   5217 C CE2 . TRP D 1 72  ? -14.387 31.856 -52.708 1.00 18.28  ? 53   TRP D CE2 1 
ATOM   5218 C CE3 . TRP D 1 72  ? -15.991 33.415 -53.681 1.00 17.55  ? 53   TRP D CE3 1 
ATOM   5219 C CZ2 . TRP D 1 72  ? -13.630 31.791 -53.882 1.00 17.48  ? 53   TRP D CZ2 1 
ATOM   5220 C CZ3 . TRP D 1 72  ? -15.240 33.358 -54.862 1.00 26.44  ? 53   TRP D CZ3 1 
ATOM   5221 C CH2 . TRP D 1 72  ? -14.070 32.546 -54.953 1.00 26.87  ? 53   TRP D CH2 1 
ATOM   5222 N N   . GLN D 1 73  ? -18.648 34.456 -47.949 1.00 24.20  ? 54   GLN D N   1 
ATOM   5223 C CA  . GLN D 1 73  ? -19.774 35.248 -47.479 1.00 19.96  ? 54   GLN D CA  1 
ATOM   5224 C C   . GLN D 1 73  ? -19.752 36.594 -48.178 1.00 23.57  ? 54   GLN D C   1 
ATOM   5225 O O   . GLN D 1 73  ? -19.243 37.578 -47.644 1.00 24.61  ? 54   GLN D O   1 
ATOM   5226 C CB  . GLN D 1 73  ? -19.710 35.426 -45.970 1.00 18.80  ? 54   GLN D CB  1 
ATOM   5227 C CG  . GLN D 1 73  ? -20.879 36.187 -45.412 1.00 28.11  ? 54   GLN D CG  1 
ATOM   5228 C CD  . GLN D 1 73  ? -20.880 36.219 -43.890 1.00 38.96  ? 54   GLN D CD  1 
ATOM   5229 O OE1 . GLN D 1 73  ? -20.848 35.164 -43.223 1.00 31.18  ? 54   GLN D OE1 1 
ATOM   5230 N NE2 . GLN D 1 73  ? -20.908 37.440 -43.327 1.00 38.32  ? 54   GLN D NE2 1 
ATOM   5231 N N   . GLN D 1 74  ? -20.312 36.639 -49.382 1.00 23.71  ? 55   GLN D N   1 
ATOM   5232 C CA  . GLN D 1 74  ? -20.265 37.854 -50.177 1.00 23.49  ? 55   GLN D CA  1 
ATOM   5233 C C   . GLN D 1 74  ? -21.247 38.905 -49.645 1.00 23.11  ? 55   GLN D C   1 
ATOM   5234 O O   . GLN D 1 74  ? -22.460 38.701 -49.664 1.00 23.56  ? 55   GLN D O   1 
ATOM   5235 C CB  . GLN D 1 74  ? -20.534 37.539 -51.645 1.00 25.57  ? 55   GLN D CB  1 
ATOM   5236 C CG  . GLN D 1 74  ? -20.581 38.767 -52.519 1.00 31.53  ? 55   GLN D CG  1 
ATOM   5237 C CD  . GLN D 1 74  ? -20.826 38.442 -53.970 1.00 42.07  ? 55   GLN D CD  1 
ATOM   5238 O OE1 . GLN D 1 74  ? -20.338 37.431 -54.478 1.00 62.54  ? 55   GLN D OE1 1 
ATOM   5239 N NE2 . GLN D 1 74  ? -21.584 39.297 -54.653 1.00 45.61  ? 55   GLN D NE2 1 
ATOM   5240 N N   . THR D 1 75  ? -20.704 40.031 -49.174 1.00 24.20  ? 56   THR D N   1 
ATOM   5241 C CA  . THR D 1 75  ? -21.489 41.075 -48.509 1.00 20.50  ? 56   THR D CA  1 
ATOM   5242 C C   . THR D 1 75  ? -21.314 42.417 -49.221 1.00 19.99  ? 56   THR D C   1 
ATOM   5243 O O   . THR D 1 75  ? -20.188 42.836 -49.484 1.00 21.68  ? 56   THR D O   1 
ATOM   5244 C CB  . THR D 1 75  ? -21.064 41.233 -47.036 1.00 19.52  ? 56   THR D CB  1 
ATOM   5245 O OG1 . THR D 1 75  ? -20.880 39.942 -46.427 1.00 24.01  ? 56   THR D OG1 1 
ATOM   5246 C CG2 . THR D 1 75  ? -22.109 42.008 -46.269 1.00 18.15  ? 56   THR D CG2 1 
ATOM   5247 N N   . THR D 1 76  ? -22.417 43.101 -49.515 1.00 20.28  ? 57   THR D N   1 
ATOM   5248 C CA  . THR D 1 76  ? -22.370 44.305 -50.353 1.00 18.25  ? 57   THR D CA  1 
ATOM   5249 C C   . THR D 1 76  ? -23.303 45.385 -49.840 1.00 19.98  ? 57   THR D C   1 
ATOM   5250 O O   . THR D 1 76  ? -24.468 45.112 -49.518 1.00 22.89  ? 57   THR D O   1 
ATOM   5251 C CB  . THR D 1 76  ? -22.742 43.977 -51.820 1.00 27.24  ? 57   THR D CB  1 
ATOM   5252 O OG1 . THR D 1 76  ? -21.724 43.135 -52.409 1.00 30.56  ? 57   THR D OG1 1 
ATOM   5253 C CG2 . THR D 1 76  ? -22.887 45.267 -52.649 1.00 23.22  ? 57   THR D CG2 1 
ATOM   5254 N N   . TRP D 1 77  ? -22.789 46.609 -49.761 1.00 18.92  ? 58   TRP D N   1 
ATOM   5255 C CA  . TRP D 1 77  ? -23.585 47.742 -49.298 1.00 19.38  ? 58   TRP D CA  1 
ATOM   5256 C C   . TRP D 1 77  ? -23.027 49.054 -49.824 1.00 23.57  ? 58   TRP D C   1 
ATOM   5257 O O   . TRP D 1 77  ? -21.974 49.089 -50.459 1.00 20.84  ? 58   TRP D O   1 
ATOM   5258 C CB  . TRP D 1 77  ? -23.645 47.784 -47.768 1.00 18.88  ? 58   TRP D CB  1 
ATOM   5259 C CG  . TRP D 1 77  ? -22.339 48.140 -47.160 1.00 19.33  ? 58   TRP D CG  1 
ATOM   5260 C CD1 . TRP D 1 77  ? -21.916 49.385 -46.790 1.00 20.31  ? 58   TRP D CD1 1 
ATOM   5261 C CD2 . TRP D 1 77  ? -21.262 47.248 -46.872 1.00 20.35  ? 58   TRP D CD2 1 
ATOM   5262 N NE1 . TRP D 1 77  ? -20.640 49.320 -46.273 1.00 20.13  ? 58   TRP D NE1 1 
ATOM   5263 C CE2 . TRP D 1 77  ? -20.210 48.018 -46.313 1.00 18.87  ? 58   TRP D CE2 1 
ATOM   5264 C CE3 . TRP D 1 77  ? -21.080 45.866 -47.025 1.00 18.69  ? 58   TRP D CE3 1 
ATOM   5265 C CZ2 . TRP D 1 77  ? -18.992 47.465 -45.911 1.00 17.22  ? 58   TRP D CZ2 1 
ATOM   5266 C CZ3 . TRP D 1 77  ? -19.867 45.307 -46.630 1.00 19.94  ? 58   TRP D CZ3 1 
ATOM   5267 C CH2 . TRP D 1 77  ? -18.831 46.114 -46.076 1.00 19.82  ? 58   TRP D CH2 1 
ATOM   5268 N N   . SER D 1 78  ? -23.729 50.141 -49.531 1.00 28.94  ? 59   SER D N   1 
ATOM   5269 C CA  . SER D 1 78  ? -23.318 51.437 -50.031 1.00 24.34  ? 59   SER D CA  1 
ATOM   5270 C C   . SER D 1 78  ? -22.938 52.401 -48.909 1.00 22.43  ? 59   SER D C   1 
ATOM   5271 O O   . SER D 1 78  ? -23.672 52.524 -47.936 1.00 25.23  ? 59   SER D O   1 
ATOM   5272 C CB  . SER D 1 78  ? -24.420 52.022 -50.891 1.00 29.54  ? 59   SER D CB  1 
ATOM   5273 O OG  . SER D 1 78  ? -24.019 53.262 -51.427 1.00 46.28  ? 59   SER D OG  1 
ATOM   5274 N N   . ASP D 1 79  ? -21.789 53.076 -49.065 1.00 28.79  ? 60   ASP D N   1 
ATOM   5275 C CA  . ASP D 1 79  ? -21.301 54.099 -48.124 1.00 30.21  ? 60   ASP D CA  1 
ATOM   5276 C C   . ASP D 1 79  ? -20.783 55.358 -48.856 1.00 30.97  ? 60   ASP D C   1 
ATOM   5277 O O   . ASP D 1 79  ? -19.614 55.420 -49.236 1.00 28.80  ? 60   ASP D O   1 
ATOM   5278 C CB  . ASP D 1 79  ? -20.193 53.515 -47.237 1.00 26.71  ? 60   ASP D CB  1 
ATOM   5279 C CG  . ASP D 1 79  ? -19.904 54.370 -45.986 1.00 33.64  ? 60   ASP D CG  1 
ATOM   5280 O OD1 . ASP D 1 79  ? -20.200 55.594 -45.984 1.00 27.74  ? 60   ASP D OD1 1 
ATOM   5281 O OD2 . ASP D 1 79  ? -19.377 53.803 -44.992 1.00 31.09  ? 60   ASP D OD2 1 
ATOM   5282 N N   . ARG D 1 80  ? -21.653 56.355 -49.028 1.00 28.91  ? 61   ARG D N   1 
ATOM   5283 C CA  . ARG D 1 80  ? -21.320 57.563 -49.789 1.00 36.23  ? 61   ARG D CA  1 
ATOM   5284 C C   . ARG D 1 80  ? -20.158 58.362 -49.205 1.00 30.72  ? 61   ARG D C   1 
ATOM   5285 O O   . ARG D 1 80  ? -19.480 59.090 -49.928 1.00 33.57  ? 61   ARG D O   1 
ATOM   5286 C CB  . ARG D 1 80  ? -22.546 58.472 -49.954 1.00 46.81  ? 61   ARG D CB  1 
ATOM   5287 C CG  . ARG D 1 80  ? -23.808 57.754 -50.447 1.00 66.62  ? 61   ARG D CG  1 
ATOM   5288 C CD  . ARG D 1 80  ? -23.830 57.481 -51.967 1.00 71.05  ? 61   ARG D CD  1 
ATOM   5289 N NE  . ARG D 1 80  ? -25.151 56.999 -52.413 1.00 86.41  ? 61   ARG D NE  1 
ATOM   5290 C CZ  . ARG D 1 80  ? -25.381 55.860 -53.076 1.00 84.56  ? 61   ARG D CZ  1 
ATOM   5291 N NH1 . ARG D 1 80  ? -24.377 55.054 -53.412 1.00 82.45  ? 61   ARG D NH1 1 
ATOM   5292 N NH2 . ARG D 1 80  ? -26.624 55.525 -53.421 1.00 71.03  ? 61   ARG D NH2 1 
ATOM   5293 N N   . THR D 1 81  ? -19.936 58.228 -47.903 1.00 30.48  ? 62   THR D N   1 
ATOM   5294 C CA  . THR D 1 81  ? -18.776 58.822 -47.223 1.00 30.32  ? 62   THR D CA  1 
ATOM   5295 C C   . THR D 1 81  ? -17.436 58.455 -47.884 1.00 27.03  ? 62   THR D C   1 
ATOM   5296 O O   . THR D 1 81  ? -16.458 59.189 -47.778 1.00 27.35  ? 62   THR D O   1 
ATOM   5297 C CB  . THR D 1 81  ? -18.751 58.357 -45.745 1.00 38.95  ? 62   THR D CB  1 
ATOM   5298 O OG1 . THR D 1 81  ? -19.993 58.712 -45.114 1.00 43.81  ? 62   THR D OG1 1 
ATOM   5299 C CG2 . THR D 1 81  ? -17.552 58.930 -44.953 1.00 29.29  ? 62   THR D CG2 1 
ATOM   5300 N N   . LEU D 1 82  ? -17.390 57.315 -48.565 1.00 27.34  ? 63   LEU D N   1 
ATOM   5301 C CA  . LEU D 1 82  ? -16.144 56.857 -49.177 1.00 27.72  ? 63   LEU D CA  1 
ATOM   5302 C C   . LEU D 1 82  ? -15.965 57.323 -50.613 1.00 24.98  ? 63   LEU D C   1 
ATOM   5303 O O   . LEU D 1 82  ? -14.913 57.096 -51.198 1.00 31.26  ? 63   LEU D O   1 
ATOM   5304 C CB  . LEU D 1 82  ? -16.066 55.329 -49.153 1.00 27.95  ? 63   LEU D CB  1 
ATOM   5305 C CG  . LEU D 1 82  ? -16.270 54.689 -47.786 1.00 27.36  ? 63   LEU D CG  1 
ATOM   5306 C CD1 . LEU D 1 82  ? -16.579 53.215 -47.948 1.00 19.16  ? 63   LEU D CD1 1 
ATOM   5307 C CD2 . LEU D 1 82  ? -15.026 54.922 -46.921 1.00 23.19  ? 63   LEU D CD2 1 
ATOM   5308 N N   . ALA D 1 83  ? -16.983 57.961 -51.186 1.00 23.66  ? 64   ALA D N   1 
ATOM   5309 C CA  . ALA D 1 83  ? -16.965 58.268 -52.617 1.00 24.51  ? 64   ALA D CA  1 
ATOM   5310 C C   . ALA D 1 83  ? -15.924 59.336 -53.006 1.00 27.52  ? 64   ALA D C   1 
ATOM   5311 O O   . ALA D 1 83  ? -15.534 60.168 -52.191 1.00 29.82  ? 64   ALA D O   1 
ATOM   5312 C CB  . ALA D 1 83  ? -18.337 58.655 -53.090 1.00 25.36  ? 64   ALA D CB  1 
ATOM   5313 N N   . TRP D 1 84  ? -15.459 59.287 -54.254 1.00 33.40  ? 65   TRP D N   1 
ATOM   5314 C CA  . TRP D 1 84  ? -14.543 60.302 -54.791 1.00 26.64  ? 65   TRP D CA  1 
ATOM   5315 C C   . TRP D 1 84  ? -14.817 60.544 -56.280 1.00 30.81  ? 65   TRP D C   1 
ATOM   5316 O O   . TRP D 1 84  ? -15.518 59.753 -56.917 1.00 39.10  ? 65   TRP D O   1 
ATOM   5317 C CB  . TRP D 1 84  ? -13.081 59.894 -54.566 1.00 25.62  ? 65   TRP D CB  1 
ATOM   5318 C CG  . TRP D 1 84  ? -12.616 58.688 -55.363 1.00 31.95  ? 65   TRP D CG  1 
ATOM   5319 C CD1 . TRP D 1 84  ? -12.026 58.701 -56.597 1.00 32.58  ? 65   TRP D CD1 1 
ATOM   5320 C CD2 . TRP D 1 84  ? -12.688 57.302 -54.969 1.00 29.32  ? 65   TRP D CD2 1 
ATOM   5321 N NE1 . TRP D 1 84  ? -11.733 57.417 -56.996 1.00 29.26  ? 65   TRP D NE1 1 
ATOM   5322 C CE2 . TRP D 1 84  ? -12.122 56.539 -56.013 1.00 27.91  ? 65   TRP D CE2 1 
ATOM   5323 C CE3 . TRP D 1 84  ? -13.177 56.635 -53.835 1.00 19.94  ? 65   TRP D CE3 1 
ATOM   5324 C CZ2 . TRP D 1 84  ? -12.027 55.146 -55.962 1.00 29.84  ? 65   TRP D CZ2 1 
ATOM   5325 C CZ3 . TRP D 1 84  ? -13.087 55.258 -53.779 1.00 24.91  ? 65   TRP D CZ3 1 
ATOM   5326 C CH2 . TRP D 1 84  ? -12.516 54.522 -54.837 1.00 31.14  ? 65   TRP D CH2 1 
ATOM   5327 N N   . ASN D 1 85  ? -14.277 61.619 -56.827 1.00 38.92  ? 66   ASN D N   1 
ATOM   5328 C CA  . ASN D 1 85  ? -14.390 61.904 -58.243 1.00 40.02  ? 66   ASN D CA  1 
ATOM   5329 C C   . ASN D 1 85  ? -13.388 61.061 -58.942 1.00 42.56  ? 66   ASN D C   1 
ATOM   5330 O O   . ASN D 1 85  ? -12.251 61.105 -58.616 1.00 50.00  ? 66   ASN D O   1 
ATOM   5331 C CB  . ASN D 1 85  ? -14.085 63.365 -58.512 1.00 40.27  ? 66   ASN D CB  1 
ATOM   5332 C CG  . ASN D 1 85  ? -14.541 63.812 -59.871 1.00 50.15  ? 66   ASN D CG  1 
ATOM   5333 O OD1 . ASN D 1 85  ? -14.712 63.008 -60.750 1.00 52.33  ? 66   ASN D OD1 1 
ATOM   5334 N ND2 . ASN D 1 85  ? -14.725 65.096 -60.047 1.00 57.29  ? 66   ASN D ND2 1 
ATOM   5335 N N   . SER D 1 86  ? -13.809 60.290 -59.918 1.00 43.82  ? 67   SER D N   1 
ATOM   5336 C CA  . SER D 1 86  ? -12.934 59.340 -60.545 1.00 44.34  ? 67   SER D CA  1 
ATOM   5337 C C   . SER D 1 86  ? -12.710 59.767 -61.952 1.00 51.60  ? 67   SER D C   1 
ATOM   5338 O O   . SER D 1 86  ? -12.599 58.964 -62.833 1.00 55.25  ? 67   SER D O   1 
ATOM   5339 C CB  . SER D 1 86  ? -13.529 57.953 -60.498 1.00 46.63  ? 67   SER D CB  1 
ATOM   5340 O OG  . SER D 1 86  ? -14.451 57.746 -61.533 1.00 52.78  ? 67   SER D OG  1 
ATOM   5341 N N   . SER D 1 87  ? -12.724 61.059 -62.165 1.00 50.88  ? 68   SER D N   1 
ATOM   5342 C CA  . SER D 1 87  ? -12.628 61.608 -63.478 1.00 55.82  ? 68   SER D CA  1 
ATOM   5343 C C   . SER D 1 87  ? -11.348 61.292 -64.213 1.00 65.71  ? 68   SER D C   1 
ATOM   5344 O O   . SER D 1 87  ? -11.410 60.907 -65.351 1.00 76.52  ? 68   SER D O   1 
ATOM   5345 C CB  . SER D 1 87  ? -12.773 63.111 -63.368 1.00 66.27  ? 68   SER D CB  1 
ATOM   5346 O OG  . SER D 1 87  ? -13.055 63.702 -64.613 1.00 80.66  ? 68   SER D OG  1 
ATOM   5347 N N   . HIS D 1 88  ? -10.190 61.419 -63.596 1.00 64.83  ? 69   HIS D N   1 
ATOM   5348 C CA  . HIS D 1 88  ? -8.968  60.921 -64.211 1.00 60.35  ? 69   HIS D CA  1 
ATOM   5349 C C   . HIS D 1 88  ? -8.206  60.228 -63.128 1.00 57.96  ? 69   HIS D C   1 
ATOM   5350 O O   . HIS D 1 88  ? -7.159  60.654 -62.717 1.00 59.25  ? 69   HIS D O   1 
ATOM   5351 C CB  . HIS D 1 88  ? -8.138  62.056 -64.796 1.00 67.60  ? 69   HIS D CB  1 
ATOM   5352 C CG  . HIS D 1 88  ? -8.814  62.810 -65.900 1.00 91.48  ? 69   HIS D CG  1 
ATOM   5353 N ND1 . HIS D 1 88  ? -8.790  62.392 -67.211 1.00 97.15  ? 69   HIS D ND1 1 
ATOM   5354 C CD2 . HIS D 1 88  ? -9.507  63.971 -65.892 1.00 95.72  ? 69   HIS D CD2 1 
ATOM   5355 C CE1 . HIS D 1 88  ? -9.454  63.253 -67.959 1.00 95.52  ? 69   HIS D CE1 1 
ATOM   5356 N NE2 . HIS D 1 88  ? -9.900  64.221 -67.183 1.00 91.71  ? 69   HIS D NE2 1 
ATOM   5357 N N   . SER D 1 89  ? -8.760  59.146 -62.642 1.00 49.78  ? 70   SER D N   1 
ATOM   5358 C CA  . SER D 1 89  ? -8.298  58.559 -61.443 1.00 39.98  ? 70   SER D CA  1 
ATOM   5359 C C   . SER D 1 89  ? -8.717  57.151 -61.435 1.00 42.42  ? 70   SER D C   1 
ATOM   5360 O O   . SER D 1 89  ? -9.484  56.750 -62.243 1.00 41.54  ? 70   SER D O   1 
ATOM   5361 C CB  . SER D 1 89  ? -8.963  59.252 -60.303 1.00 49.41  ? 70   SER D CB  1 
ATOM   5362 O OG  . SER D 1 89  ? -9.045  60.608 -60.593 1.00 59.68  ? 70   SER D OG  1 
ATOM   5363 N N   . PRO D 1 90  ? -8.147  56.384 -60.442 1.00 43.72  ? 71   PRO D N   1 
ATOM   5364 C CA  . PRO D 1 90  ? -8.690  55.038 -60.312 1.00 36.79  ? 71   PRO D CA  1 
ATOM   5365 C C   . PRO D 1 90  ? -10.141 55.035 -59.910 1.00 35.10  ? 71   PRO D C   1 
ATOM   5366 O O   . PRO D 1 90  ? -10.576 55.952 -59.287 1.00 38.31  ? 71   PRO D O   1 
ATOM   5367 C CB  . PRO D 1 90  ? -7.882  54.461 -59.172 1.00 39.66  ? 71   PRO D CB  1 
ATOM   5368 C CG  . PRO D 1 90  ? -6.603  55.124 -59.252 1.00 42.92  ? 71   PRO D CG  1 
ATOM   5369 C CD  . PRO D 1 90  ? -7.003  56.511 -59.433 1.00 37.12  ? 71   PRO D CD  1 
ATOM   5370 N N   . ASP D 1 91  ? -10.885 54.017 -60.298 1.00 35.33  ? 72   ASP D N   1 
ATOM   5371 C CA  . ASP D 1 91  ? -12.295 53.894 -59.927 1.00 39.81  ? 72   ASP D CA  1 
ATOM   5372 C C   . ASP D 1 91  ? -12.525 52.848 -58.805 1.00 40.34  ? 72   ASP D C   1 
ATOM   5373 O O   . ASP D 1 91  ? -13.668 52.585 -58.404 1.00 36.96  ? 72   ASP D O   1 
ATOM   5374 C CB  . ASP D 1 91  ? -13.122 53.553 -61.170 1.00 41.47  ? 72   ASP D CB  1 
ATOM   5375 C CG  . ASP D 1 91  ? -12.465 52.474 -62.019 1.00 54.21  ? 72   ASP D CG  1 
ATOM   5376 O OD1 . ASP D 1 91  ? -11.313 52.096 -61.693 1.00 59.13  ? 72   ASP D OD1 1 
ATOM   5377 O OD2 . ASP D 1 91  ? -13.082 52.013 -63.012 1.00 66.28  ? 72   ASP D OD2 1 
ATOM   5378 N N   . GLN D 1 92  ? -11.436 52.268 -58.299 1.00 32.53  ? 73   GLN D N   1 
ATOM   5379 C CA  . GLN D 1 92  ? -11.505 51.262 -57.242 1.00 27.22  ? 73   GLN D CA  1 
ATOM   5380 C C   . GLN D 1 92  ? -10.195 51.150 -56.436 1.00 26.76  ? 73   GLN D C   1 
ATOM   5381 O O   . GLN D 1 92  ? -9.093  51.364 -56.957 1.00 30.68  ? 73   GLN D O   1 
ATOM   5382 C CB  . GLN D 1 92  ? -11.823 49.907 -57.850 1.00 26.11  ? 73   GLN D CB  1 
ATOM   5383 C CG  . GLN D 1 92  ? -10.781 49.522 -58.864 1.00 42.31  ? 73   GLN D CG  1 
ATOM   5384 C CD  . GLN D 1 92  ? -10.874 48.086 -59.288 1.00 54.57  ? 73   GLN D CD  1 
ATOM   5385 O OE1 . GLN D 1 92  ? -11.967 47.552 -59.494 1.00 61.18  ? 73   GLN D OE1 1 
ATOM   5386 N NE2 . GLN D 1 92  ? -9.720  47.440 -59.421 1.00 54.44  ? 73   GLN D NE2 1 
ATOM   5387 N N   . VAL D 1 93  ? -10.324 50.799 -55.162 1.00 20.70  ? 74   VAL D N   1 
ATOM   5388 C CA  . VAL D 1 93  ? -9.177  50.524 -54.306 1.00 21.04  ? 74   VAL D CA  1 
ATOM   5389 C C   . VAL D 1 93  ? -9.526  49.365 -53.342 1.00 20.32  ? 74   VAL D C   1 
ATOM   5390 O O   . VAL D 1 93  ? -10.703 49.056 -53.140 1.00 18.46  ? 74   VAL D O   1 
ATOM   5391 C CB  . VAL D 1 93  ? -8.746  51.773 -53.485 1.00 19.22  ? 74   VAL D CB  1 
ATOM   5392 C CG1 . VAL D 1 93  ? -8.168  52.861 -54.368 1.00 20.68  ? 74   VAL D CG1 1 
ATOM   5393 C CG2 . VAL D 1 93  ? -9.914  52.308 -52.697 1.00 23.51  ? 74   VAL D CG2 1 
ATOM   5394 N N   . SER D 1 94  ? -8.512  48.720 -52.765 1.00 16.16  ? 75   SER D N   1 
ATOM   5395 C CA  . SER D 1 94  ? -8.741  47.738 -51.711 1.00 15.60  ? 75   SER D CA  1 
ATOM   5396 C C   . SER D 1 94  ? -8.408  48.360 -50.356 1.00 20.48  ? 75   SER D C   1 
ATOM   5397 O O   . SER D 1 94  ? -7.361  48.993 -50.184 1.00 22.98  ? 75   SER D O   1 
ATOM   5398 C CB  . SER D 1 94  ? -7.899  46.483 -51.932 1.00 23.11  ? 75   SER D CB  1 
ATOM   5399 O OG  . SER D 1 94  ? -8.485  45.639 -52.906 1.00 28.63  ? 75   SER D OG  1 
ATOM   5400 N N   . VAL D 1 95  ? -9.299  48.182 -49.390 1.00 21.10  ? 76   VAL D N   1 
ATOM   5401 C CA  . VAL D 1 95  ? -9.169  48.879 -48.108 1.00 20.75  ? 76   VAL D CA  1 
ATOM   5402 C C   . VAL D 1 95  ? -9.242  47.881 -46.966 1.00 19.93  ? 76   VAL D C   1 
ATOM   5403 O O   . VAL D 1 95  ? -10.127 47.025 -46.945 1.00 20.93  ? 76   VAL D O   1 
ATOM   5404 C CB  . VAL D 1 95  ? -10.312 49.891 -47.936 1.00 17.98  ? 76   VAL D CB  1 
ATOM   5405 C CG1 . VAL D 1 95  ? -10.245 50.550 -46.566 1.00 16.60  ? 76   VAL D CG1 1 
ATOM   5406 C CG2 . VAL D 1 95  ? -10.330 50.905 -49.091 1.00 12.85  ? 76   VAL D CG2 1 
ATOM   5407 N N   . PRO D 1 96  ? -8.311  47.977 -46.006 1.00 21.98  ? 77   PRO D N   1 
ATOM   5408 C CA  . PRO D 1 96  ? -8.411  47.100 -44.825 1.00 21.99  ? 77   PRO D CA  1 
ATOM   5409 C C   . PRO D 1 96  ? -9.737  47.355 -44.097 1.00 19.04  ? 77   PRO D C   1 
ATOM   5410 O O   . PRO D 1 96  ? -10.062 48.529 -43.888 1.00 21.96  ? 77   PRO D O   1 
ATOM   5411 C CB  . PRO D 1 96  ? -7.226  47.549 -43.951 1.00 15.46  ? 77   PRO D CB  1 
ATOM   5412 C CG  . PRO D 1 96  ? -6.279  48.204 -44.902 1.00 17.47  ? 77   PRO D CG  1 
ATOM   5413 C CD  . PRO D 1 96  ? -7.148  48.878 -45.941 1.00 21.86  ? 77   PRO D CD  1 
ATOM   5414 N N   . ILE D 1 97  ? -10.478 46.306 -43.735 1.00 13.43  ? 78   ILE D N   1 
ATOM   5415 C CA  . ILE D 1 97  ? -11.795 46.493 -43.118 1.00 16.66  ? 78   ILE D CA  1 
ATOM   5416 C C   . ILE D 1 97  ? -11.748 47.268 -41.794 1.00 20.18  ? 78   ILE D C   1 
ATOM   5417 O O   . ILE D 1 97  ? -12.754 47.832 -41.337 1.00 20.15  ? 78   ILE D O   1 
ATOM   5418 C CB  . ILE D 1 97  ? -12.578 45.178 -42.906 1.00 16.10  ? 78   ILE D CB  1 
ATOM   5419 C CG1 . ILE D 1 97  ? -11.845 44.249 -41.958 1.00 13.18  ? 78   ILE D CG1 1 
ATOM   5420 C CG2 . ILE D 1 97  ? -12.880 44.496 -44.251 1.00 20.77  ? 78   ILE D CG2 1 
ATOM   5421 C CD1 . ILE D 1 97  ? -12.656 43.072 -41.552 1.00 9.71   ? 78   ILE D CD1 1 
ATOM   5422 N N   . SER D 1 98  ? -10.577 47.307 -41.178 1.00 17.70  ? 79   SER D N   1 
ATOM   5423 C CA  . SER D 1 98  ? -10.431 48.063 -39.949 1.00 20.40  ? 79   SER D CA  1 
ATOM   5424 C C   . SER D 1 98  ? -10.660 49.578 -40.171 1.00 23.82  ? 79   SER D C   1 
ATOM   5425 O O   . SER D 1 98  ? -10.926 50.318 -39.229 1.00 25.47  ? 79   SER D O   1 
ATOM   5426 C CB  . SER D 1 98  ? -9.069  47.769 -39.300 1.00 21.46  ? 79   SER D CB  1 
ATOM   5427 O OG  . SER D 1 98  ? -7.995  48.234 -40.108 1.00 28.86  ? 79   SER D OG  1 
ATOM   5428 N N   . SER D 1 99  ? -10.584 50.034 -41.415 1.00 24.57  ? 80   SER D N   1 
ATOM   5429 C CA  . SER D 1 99  ? -10.799 51.450 -41.721 1.00 22.29  ? 80   SER D CA  1 
ATOM   5430 C C   . SER D 1 99  ? -12.172 51.755 -42.313 1.00 24.76  ? 80   SER D C   1 
ATOM   5431 O O   . SER D 1 99  ? -12.357 52.831 -42.868 1.00 26.85  ? 80   SER D O   1 
ATOM   5432 C CB  . SER D 1 99  ? -9.752  51.955 -42.721 1.00 24.41  ? 80   SER D CB  1 
ATOM   5433 O OG  . SER D 1 99  ? -8.446  51.578 -42.341 1.00 38.37  ? 80   SER D OG  1 
ATOM   5434 N N   . LEU D 1 100 ? -13.117 50.820 -42.225 1.00 21.32  ? 81   LEU D N   1 
ATOM   5435 C CA  . LEU D 1 100 ? -14.451 51.005 -42.797 1.00 17.33  ? 81   LEU D CA  1 
ATOM   5436 C C   . LEU D 1 100 ? -15.523 50.611 -41.813 1.00 20.05  ? 81   LEU D C   1 
ATOM   5437 O O   . LEU D 1 100 ? -15.310 49.728 -40.964 1.00 20.34  ? 81   LEU D O   1 
ATOM   5438 C CB  . LEU D 1 100 ? -14.636 50.072 -43.972 1.00 21.46  ? 81   LEU D CB  1 
ATOM   5439 C CG  . LEU D 1 100 ? -13.776 50.282 -45.191 1.00 23.85  ? 81   LEU D CG  1 
ATOM   5440 C CD1 . LEU D 1 100 ? -14.166 49.237 -46.216 1.00 17.35  ? 81   LEU D CD1 1 
ATOM   5441 C CD2 . LEU D 1 100 ? -14.061 51.671 -45.688 1.00 25.77  ? 81   LEU D CD2 1 
ATOM   5442 N N   . TRP D 1 101 ? -16.698 51.216 -41.942 1.00 16.84  ? 82   TRP D N   1 
ATOM   5443 C CA  . TRP D 1 101 ? -17.849 50.633 -41.280 1.00 16.42  ? 82   TRP D CA  1 
ATOM   5444 C C   . TRP D 1 101 ? -18.188 49.325 -41.994 1.00 17.77  ? 82   TRP D C   1 
ATOM   5445 O O   . TRP D 1 101 ? -18.093 49.237 -43.203 1.00 19.16  ? 82   TRP D O   1 
ATOM   5446 C CB  . TRP D 1 101 ? -19.045 51.556 -41.299 1.00 14.16  ? 82   TRP D CB  1 
ATOM   5447 C CG  . TRP D 1 101 ? -20.236 50.927 -40.675 1.00 15.73  ? 82   TRP D CG  1 
ATOM   5448 C CD1 . TRP D 1 101 ? -20.585 50.949 -39.359 1.00 15.31  ? 82   TRP D CD1 1 
ATOM   5449 C CD2 . TRP D 1 101 ? -21.246 50.171 -41.350 1.00 18.72  ? 82   TRP D CD2 1 
ATOM   5450 N NE1 . TRP D 1 101 ? -21.756 50.264 -39.175 1.00 17.09  ? 82   TRP D NE1 1 
ATOM   5451 C CE2 . TRP D 1 101 ? -22.178 49.772 -40.376 1.00 17.83  ? 82   TRP D CE2 1 
ATOM   5452 C CE3 . TRP D 1 101 ? -21.447 49.797 -42.681 1.00 21.38  ? 82   TRP D CE3 1 
ATOM   5453 C CZ2 . TRP D 1 101 ? -23.306 49.005 -40.700 1.00 20.90  ? 82   TRP D CZ2 1 
ATOM   5454 C CZ3 . TRP D 1 101 ? -22.566 49.037 -42.999 1.00 20.49  ? 82   TRP D CZ3 1 
ATOM   5455 C CH2 . TRP D 1 101 ? -23.481 48.647 -42.010 1.00 21.66  ? 82   TRP D CH2 1 
ATOM   5456 N N   . VAL D 1 102 ? -18.590 48.319 -41.227 1.00 21.59  ? 83   VAL D N   1 
ATOM   5457 C CA  . VAL D 1 102 ? -18.931 46.991 -41.731 1.00 17.35  ? 83   VAL D CA  1 
ATOM   5458 C C   . VAL D 1 102 ? -20.190 46.537 -40.983 1.00 18.36  ? 83   VAL D C   1 
ATOM   5459 O O   . VAL D 1 102 ? -20.335 46.786 -39.784 1.00 19.89  ? 83   VAL D O   1 
ATOM   5460 C CB  . VAL D 1 102 ? -17.770 46.006 -41.478 1.00 13.45  ? 83   VAL D CB  1 
ATOM   5461 C CG1 . VAL D 1 102 ? -18.278 44.587 -41.378 1.00 18.92  ? 83   VAL D CG1 1 
ATOM   5462 C CG2 . VAL D 1 102 ? -16.720 46.131 -42.557 1.00 13.15  ? 83   VAL D CG2 1 
ATOM   5463 N N   . PRO D 1 103 ? -21.127 45.897 -41.689 1.00 19.41  ? 84   PRO D N   1 
ATOM   5464 C CA  . PRO D 1 103 ? -22.343 45.417 -41.005 1.00 18.65  ? 84   PRO D CA  1 
ATOM   5465 C C   . PRO D 1 103 ? -22.052 44.297 -39.997 1.00 20.16  ? 84   PRO D C   1 
ATOM   5466 O O   . PRO D 1 103 ? -21.216 43.412 -40.273 1.00 19.49  ? 84   PRO D O   1 
ATOM   5467 C CB  . PRO D 1 103 ? -23.217 44.901 -42.158 1.00 19.95  ? 84   PRO D CB  1 
ATOM   5468 C CG  . PRO D 1 103 ? -22.255 44.615 -43.283 1.00 18.47  ? 84   PRO D CG  1 
ATOM   5469 C CD  . PRO D 1 103 ? -21.126 45.611 -43.137 1.00 16.78  ? 84   PRO D CD  1 
ATOM   5470 N N   . ASP D 1 104 ? -22.743 44.338 -38.853 1.00 25.02  ? 85   ASP D N   1 
ATOM   5471 C CA  . ASP D 1 104 ? -22.530 43.375 -37.755 1.00 24.44  ? 85   ASP D CA  1 
ATOM   5472 C C   . ASP D 1 104 ? -23.317 42.070 -37.925 1.00 24.07  ? 85   ASP D C   1 
ATOM   5473 O O   . ASP D 1 104 ? -24.102 41.698 -37.056 1.00 26.78  ? 85   ASP D O   1 
ATOM   5474 C CB  . ASP D 1 104 ? -22.839 44.009 -36.384 1.00 22.60  ? 85   ASP D CB  1 
ATOM   5475 C CG  . ASP D 1 104 ? -24.288 44.507 -36.256 1.00 26.94  ? 85   ASP D CG  1 
ATOM   5476 O OD1 . ASP D 1 104 ? -24.873 44.909 -37.287 1.00 25.67  ? 85   ASP D OD1 1 
ATOM   5477 O OD2 . ASP D 1 104 ? -24.840 44.498 -35.116 1.00 27.99  ? 85   ASP D OD2 1 
ATOM   5478 N N   . LEU D 1 105 ? -23.096 41.369 -39.038 1.00 24.17  ? 86   LEU D N   1 
ATOM   5479 C CA  . LEU D 1 105 ? -23.804 40.118 -39.307 1.00 20.90  ? 86   LEU D CA  1 
ATOM   5480 C C   . LEU D 1 105 ? -23.300 38.959 -38.429 1.00 21.72  ? 86   LEU D C   1 
ATOM   5481 O O   . LEU D 1 105 ? -22.130 38.915 -38.037 1.00 21.87  ? 86   LEU D O   1 
ATOM   5482 C CB  . LEU D 1 105 ? -23.693 39.759 -40.789 1.00 21.97  ? 86   LEU D CB  1 
ATOM   5483 C CG  . LEU D 1 105 ? -24.172 40.853 -41.744 1.00 23.79  ? 86   LEU D CG  1 
ATOM   5484 C CD1 . LEU D 1 105 ? -23.904 40.470 -43.208 1.00 21.02  ? 86   LEU D CD1 1 
ATOM   5485 C CD2 . LEU D 1 105 ? -25.655 41.181 -41.527 1.00 28.43  ? 86   LEU D CD2 1 
ATOM   5486 N N   . ALA D 1 106 ? -24.203 38.039 -38.109 1.00 18.28  ? 87   ALA D N   1 
ATOM   5487 C CA  . ALA D 1 106 ? -23.863 36.870 -37.323 1.00 18.26  ? 87   ALA D CA  1 
ATOM   5488 C C   . ALA D 1 106 ? -24.742 35.724 -37.766 1.00 21.41  ? 87   ALA D C   1 
ATOM   5489 O O   . ALA D 1 106 ? -25.865 35.937 -38.225 1.00 22.33  ? 87   ALA D O   1 
ATOM   5490 C CB  . ALA D 1 106 ? -24.079 37.141 -35.853 1.00 21.38  ? 87   ALA D CB  1 
ATOM   5491 N N   . ALA D 1 107 ? -24.230 34.507 -37.621 1.00 20.71  ? 88   ALA D N   1 
ATOM   5492 C CA  . ALA D 1 107 ? -25.007 33.303 -37.912 1.00 20.40  ? 88   ALA D CA  1 
ATOM   5493 C C   . ALA D 1 107 ? -25.650 32.824 -36.621 1.00 22.46  ? 88   ALA D C   1 
ATOM   5494 O O   . ALA D 1 107 ? -24.954 32.412 -35.677 1.00 24.65  ? 88   ALA D O   1 
ATOM   5495 C CB  . ALA D 1 107 ? -24.112 32.208 -38.500 1.00 23.22  ? 88   ALA D CB  1 
ATOM   5496 N N   . TYR D 1 108 ? -26.976 32.869 -36.583 1.00 18.46  ? 89   TYR D N   1 
ATOM   5497 C CA  . TYR D 1 108 ? -27.709 32.569 -35.359 1.00 17.08  ? 89   TYR D CA  1 
ATOM   5498 C C   . TYR D 1 108 ? -27.547 31.135 -34.874 1.00 16.10  ? 89   TYR D C   1 
ATOM   5499 O O   . TYR D 1 108 ? -27.657 30.874 -33.688 1.00 17.10  ? 89   TYR D O   1 
ATOM   5500 C CB  . TYR D 1 108 ? -29.192 32.888 -35.545 1.00 22.91  ? 89   TYR D CB  1 
ATOM   5501 C CG  . TYR D 1 108 ? -29.526 34.348 -35.390 1.00 20.90  ? 89   TYR D CG  1 
ATOM   5502 C CD1 . TYR D 1 108 ? -29.153 35.273 -36.359 1.00 25.30  ? 89   TYR D CD1 1 
ATOM   5503 C CD2 . TYR D 1 108 ? -30.214 34.804 -34.276 1.00 20.28  ? 89   TYR D CD2 1 
ATOM   5504 C CE1 . TYR D 1 108 ? -29.456 36.623 -36.217 1.00 27.33  ? 89   TYR D CE1 1 
ATOM   5505 C CE2 . TYR D 1 108 ? -30.530 36.142 -34.119 1.00 20.24  ? 89   TYR D CE2 1 
ATOM   5506 C CZ  . TYR D 1 108 ? -30.156 37.053 -35.096 1.00 24.93  ? 89   TYR D CZ  1 
ATOM   5507 O OH  . TYR D 1 108 ? -30.474 38.393 -34.962 1.00 19.32  ? 89   TYR D OH  1 
ATOM   5508 N N   . ASN D 1 109 ? -27.309 30.197 -35.786 1.00 23.71  ? 90   ASN D N   1 
ATOM   5509 C CA  . ASN D 1 109 ? -27.160 28.784 -35.392 1.00 27.75  ? 90   ASN D CA  1 
ATOM   5510 C C   . ASN D 1 109 ? -25.720 28.267 -35.514 1.00 24.13  ? 90   ASN D C   1 
ATOM   5511 O O   . ASN D 1 109 ? -25.472 27.060 -35.621 1.00 23.33  ? 90   ASN D O   1 
ATOM   5512 C CB  . ASN D 1 109 ? -28.148 27.868 -36.147 1.00 21.46  ? 90   ASN D CB  1 
ATOM   5513 C CG  . ASN D 1 109 ? -28.002 27.956 -37.668 1.00 30.50  ? 90   ASN D CG  1 
ATOM   5514 O OD1 . ASN D 1 109 ? -27.985 29.049 -38.250 1.00 31.19  ? 90   ASN D OD1 1 
ATOM   5515 N ND2 . ASN D 1 109 ? -27.895 26.794 -38.319 1.00 34.73  ? 90   ASN D ND2 1 
ATOM   5516 N N   . ALA D 1 110 ? -24.771 29.197 -35.492 1.00 22.40  ? 91   ALA D N   1 
ATOM   5517 C CA  . ALA D 1 110 ? -23.358 28.841 -35.473 1.00 21.65  ? 91   ALA D CA  1 
ATOM   5518 C C   . ALA D 1 110 ? -22.995 28.349 -34.067 1.00 21.56  ? 91   ALA D C   1 
ATOM   5519 O O   . ALA D 1 110 ? -23.522 28.854 -33.072 1.00 20.52  ? 91   ALA D O   1 
ATOM   5520 C CB  . ALA D 1 110 ? -22.515 30.036 -35.869 1.00 19.81  ? 91   ALA D CB  1 
ATOM   5521 N N   . ILE D 1 111 ? -22.121 27.353 -33.979 1.00 19.13  ? 92   ILE D N   1 
ATOM   5522 C CA  . ILE D 1 111 ? -21.694 26.872 -32.671 1.00 21.80  ? 92   ILE D CA  1 
ATOM   5523 C C   . ILE D 1 111 ? -20.177 27.003 -32.489 1.00 23.86  ? 92   ILE D C   1 
ATOM   5524 O O   . ILE D 1 111 ? -19.590 26.445 -31.562 1.00 23.76  ? 92   ILE D O   1 
ATOM   5525 C CB  . ILE D 1 111 ? -22.160 25.443 -32.404 1.00 22.91  ? 92   ILE D CB  1 
ATOM   5526 C CG1 . ILE D 1 111 ? -21.685 24.520 -33.521 1.00 23.75  ? 92   ILE D CG1 1 
ATOM   5527 C CG2 . ILE D 1 111 ? -23.665 25.403 -32.264 1.00 20.40  ? 92   ILE D CG2 1 
ATOM   5528 C CD1 . ILE D 1 111 ? -22.032 23.061 -33.298 1.00 29.38  ? 92   ILE D CD1 1 
ATOM   5529 N N   . SER D 1 112 ? -19.557 27.757 -33.388 1.00 21.00  ? 93   SER D N   1 
ATOM   5530 C CA  . SER D 1 112 ? -18.162 28.141 -33.246 1.00 22.85  ? 93   SER D CA  1 
ATOM   5531 C C   . SER D 1 112 ? -18.022 29.519 -33.872 1.00 22.56  ? 93   SER D C   1 
ATOM   5532 O O   . SER D 1 112 ? -18.852 29.900 -34.707 1.00 19.47  ? 93   SER D O   1 
ATOM   5533 C CB  . SER D 1 112 ? -17.284 27.138 -33.979 1.00 23.55  ? 93   SER D CB  1 
ATOM   5534 O OG  . SER D 1 112 ? -17.458 27.266 -35.377 1.00 27.30  ? 93   SER D OG  1 
ATOM   5535 N N   . LYS D 1 113 ? -16.996 30.278 -33.488 1.00 23.42  ? 94   LYS D N   1 
ATOM   5536 C CA  . LYS D 1 113 ? -16.822 31.603 -34.113 1.00 27.71  ? 94   LYS D CA  1 
ATOM   5537 C C   . LYS D 1 113 ? -16.297 31.470 -35.537 1.00 21.93  ? 94   LYS D C   1 
ATOM   5538 O O   . LYS D 1 113 ? -15.648 30.475 -35.873 1.00 25.75  ? 94   LYS D O   1 
ATOM   5539 C CB  . LYS D 1 113 ? -15.958 32.556 -33.266 1.00 34.43  ? 94   LYS D CB  1 
ATOM   5540 C CG  . LYS D 1 113 ? -14.509 32.144 -33.069 1.00 40.17  ? 94   LYS D CG  1 
ATOM   5541 C CD  . LYS D 1 113 ? -13.863 33.013 -31.973 1.00 46.36  ? 94   LYS D CD  1 
ATOM   5542 C CE  . LYS D 1 113 ? -14.087 34.503 -32.239 1.00 45.18  ? 94   LYS D CE  1 
ATOM   5543 N NZ  . LYS D 1 113 ? -13.247 35.382 -31.356 1.00 53.53  ? 94   LYS D NZ  1 
ATOM   5544 N N   . PRO D 1 114 ? -16.601 32.457 -36.389 1.00 21.44  ? 95   PRO D N   1 
ATOM   5545 C CA  . PRO D 1 114 ? -16.134 32.325 -37.774 1.00 19.66  ? 95   PRO D CA  1 
ATOM   5546 C C   . PRO D 1 114 ? -14.602 32.279 -37.795 1.00 23.57  ? 95   PRO D C   1 
ATOM   5547 O O   . PRO D 1 114 ? -13.960 33.075 -37.108 1.00 31.44  ? 95   PRO D O   1 
ATOM   5548 C CB  . PRO D 1 114 ? -16.631 33.625 -38.439 1.00 15.38  ? 95   PRO D CB  1 
ATOM   5549 C CG  . PRO D 1 114 ? -17.663 34.201 -37.493 1.00 14.35  ? 95   PRO D CG  1 
ATOM   5550 C CD  . PRO D 1 114 ? -17.303 33.737 -36.139 1.00 17.85  ? 95   PRO D CD  1 
ATOM   5551 N N   . GLU D 1 115 ? -14.025 31.351 -38.546 1.00 21.63  ? 96   GLU D N   1 
ATOM   5552 C CA  . GLU D 1 115 ? -12.581 31.342 -38.792 1.00 23.96  ? 96   GLU D CA  1 
ATOM   5553 C C   . GLU D 1 115 ? -12.321 31.962 -40.173 1.00 25.67  ? 96   GLU D C   1 
ATOM   5554 O O   . GLU D 1 115 ? -12.646 31.360 -41.217 1.00 25.02  ? 96   GLU D O   1 
ATOM   5555 C CB  . GLU D 1 115 ? -12.060 29.909 -38.761 1.00 22.39  ? 96   GLU D CB  1 
ATOM   5556 C CG  . GLU D 1 115 ? -10.560 29.751 -38.826 1.00 22.94  ? 96   GLU D CG  1 
ATOM   5557 C CD  . GLU D 1 115 ? -10.169 28.275 -38.734 1.00 55.53  ? 96   GLU D CD  1 
ATOM   5558 O OE1 . GLU D 1 115 ? -11.038 27.461 -38.303 1.00 59.83  ? 96   GLU D OE1 1 
ATOM   5559 O OE2 . GLU D 1 115 ? -9.013  27.926 -39.106 1.00 58.88  ? 96   GLU D OE2 1 
ATOM   5560 N N   . VAL D 1 116 ? -11.757 33.168 -40.196 1.00 21.33  ? 97   VAL D N   1 
ATOM   5561 C CA  . VAL D 1 116 ? -11.524 33.847 -41.480 1.00 25.76  ? 97   VAL D CA  1 
ATOM   5562 C C   . VAL D 1 116 ? -10.244 33.404 -42.219 1.00 18.40  ? 97   VAL D C   1 
ATOM   5563 O O   . VAL D 1 116 ? -9.141  33.635 -41.762 1.00 24.21  ? 97   VAL D O   1 
ATOM   5564 C CB  . VAL D 1 116 ? -11.563 35.364 -41.320 1.00 21.93  ? 97   VAL D CB  1 
ATOM   5565 C CG1 . VAL D 1 116 ? -11.426 36.034 -42.676 1.00 25.33  ? 97   VAL D CG1 1 
ATOM   5566 C CG2 . VAL D 1 116 ? -12.861 35.743 -40.657 1.00 18.56  ? 97   VAL D CG2 1 
ATOM   5567 N N   . LEU D 1 117 ? -10.414 32.767 -43.368 1.00 18.27  ? 98   LEU D N   1 
ATOM   5568 C CA  . LEU D 1 117 ? -9.301  32.148 -44.070 1.00 18.73  ? 98   LEU D CA  1 
ATOM   5569 C C   . LEU D 1 117 ? -8.498  33.118 -44.962 1.00 23.70  ? 98   LEU D C   1 
ATOM   5570 O O   . LEU D 1 117 ? -7.346  32.870 -45.289 1.00 23.75  ? 98   LEU D O   1 
ATOM   5571 C CB  . LEU D 1 117 ? -9.828  30.983 -44.900 1.00 19.85  ? 98   LEU D CB  1 
ATOM   5572 C CG  . LEU D 1 117 ? -10.526 29.844 -44.130 1.00 22.94  ? 98   LEU D CG  1 
ATOM   5573 C CD1 . LEU D 1 117 ? -10.990 28.722 -45.068 1.00 14.36  ? 98   LEU D CD1 1 
ATOM   5574 C CD2 . LEU D 1 117 ? -9.659  29.281 -43.009 1.00 17.82  ? 98   LEU D CD2 1 
ATOM   5575 N N   . THR D 1 118 ? -9.101  34.236 -45.339 1.00 19.59  ? 99   THR D N   1 
ATOM   5576 C CA  . THR D 1 118 ? -8.510  35.099 -46.348 1.00 19.19  ? 99   THR D CA  1 
ATOM   5577 C C   . THR D 1 118 ? -8.079  36.434 -45.750 1.00 26.91  ? 99   THR D C   1 
ATOM   5578 O O   . THR D 1 118 ? -8.484  36.755 -44.624 1.00 25.24  ? 99   THR D O   1 
ATOM   5579 C CB  . THR D 1 118 ? -9.521  35.332 -47.474 1.00 26.10  ? 99   THR D CB  1 
ATOM   5580 O OG1 . THR D 1 118 ? -10.795 35.697 -46.897 1.00 29.52  ? 99   THR D OG1 1 
ATOM   5581 C CG2 . THR D 1 118 ? -9.651  34.067 -48.335 1.00 19.94  ? 99   THR D CG2 1 
ATOM   5582 N N   . PRO D 1 119 ? -7.247  37.211 -46.493 1.00 26.78  ? 100  PRO D N   1 
ATOM   5583 C CA  . PRO D 1 119 ? -6.893  38.596 -46.128 1.00 26.62  ? 100  PRO D CA  1 
ATOM   5584 C C   . PRO D 1 119 ? -8.146  39.437 -45.879 1.00 26.35  ? 100  PRO D C   1 
ATOM   5585 O O   . PRO D 1 119 ? -9.148  39.284 -46.609 1.00 27.04  ? 100  PRO D O   1 
ATOM   5586 C CB  . PRO D 1 119 ? -6.193  39.117 -47.385 1.00 20.27  ? 100  PRO D CB  1 
ATOM   5587 C CG  . PRO D 1 119 ? -5.595  37.915 -48.005 1.00 19.03  ? 100  PRO D CG  1 
ATOM   5588 C CD  . PRO D 1 119 ? -6.517  36.759 -47.693 1.00 20.60  ? 100  PRO D CD  1 
ATOM   5589 N N   . GLN D 1 120 ? -8.103  40.307 -44.877 1.00 19.36  ? 101  GLN D N   1 
ATOM   5590 C CA  . GLN D 1 120 ? -9.307  41.048 -44.517 1.00 23.65  ? 101  GLN D CA  1 
ATOM   5591 C C   . GLN D 1 120 ? -9.426  42.416 -45.212 1.00 21.04  ? 101  GLN D C   1 
ATOM   5592 O O   . GLN D 1 120 ? -9.407  43.469 -44.568 1.00 23.17  ? 101  GLN D O   1 
ATOM   5593 C CB  . GLN D 1 120 ? -9.467  41.115 -42.992 1.00 19.35  ? 101  GLN D CB  1 
ATOM   5594 C CG  . GLN D 1 120 ? -9.829  39.767 -42.394 1.00 23.90  ? 101  GLN D CG  1 
ATOM   5595 C CD  . GLN D 1 120 ? -9.879  39.740 -40.869 1.00 27.31  ? 101  GLN D CD  1 
ATOM   5596 O OE1 . GLN D 1 120 ? -10.340 40.684 -40.220 1.00 34.22  ? 101  GLN D OE1 1 
ATOM   5597 N NE2 . GLN D 1 120 ? -9.418  38.636 -40.291 1.00 27.67  ? 101  GLN D NE2 1 
ATOM   5598 N N   . LEU D 1 121 ? -9.554  42.373 -46.538 1.00 20.12  ? 102  LEU D N   1 
ATOM   5599 C CA  . LEU D 1 121 ? -9.695  43.577 -47.364 1.00 20.55  ? 102  LEU D CA  1 
ATOM   5600 C C   . LEU D 1 121 ? -11.074 43.665 -48.020 1.00 18.02  ? 102  LEU D C   1 
ATOM   5601 O O   . LEU D 1 121 ? -11.666 42.657 -48.408 1.00 14.23  ? 102  LEU D O   1 
ATOM   5602 C CB  . LEU D 1 121 ? -8.631  43.605 -48.460 1.00 21.10  ? 102  LEU D CB  1 
ATOM   5603 C CG  . LEU D 1 121 ? -7.191  43.542 -47.963 1.00 20.54  ? 102  LEU D CG  1 
ATOM   5604 C CD1 . LEU D 1 121 ? -6.200  43.514 -49.118 1.00 23.49  ? 102  LEU D CD1 1 
ATOM   5605 C CD2 . LEU D 1 121 ? -6.925  44.718 -47.060 1.00 19.61  ? 102  LEU D CD2 1 
ATOM   5606 N N   . ALA D 1 122 ? -11.579 44.886 -48.132 1.00 19.71  ? 103  ALA D N   1 
ATOM   5607 C CA  . ALA D 1 122 ? -12.828 45.152 -48.832 1.00 17.98  ? 103  ALA D CA  1 
ATOM   5608 C C   . ALA D 1 122 ? -12.551 45.903 -50.144 1.00 20.96  ? 103  ALA D C   1 
ATOM   5609 O O   . ALA D 1 122 ? -11.581 46.681 -50.259 1.00 21.61  ? 103  ALA D O   1 
ATOM   5610 C CB  . ALA D 1 122 ? -13.758 45.952 -47.945 1.00 13.73  ? 103  ALA D CB  1 
ATOM   5611 N N   . HIS D 1 123 ? -13.408 45.668 -51.129 1.00 21.57  ? 104  HIS D N   1 
ATOM   5612 C CA  . HIS D 1 123 ? -13.308 46.320 -52.429 1.00 19.99  ? 104  HIS D CA  1 
ATOM   5613 C C   . HIS D 1 123 ? -14.189 47.570 -52.391 1.00 17.10  ? 104  HIS D C   1 
ATOM   5614 O O   . HIS D 1 123 ? -15.350 47.486 -52.002 1.00 14.79  ? 104  HIS D O   1 
ATOM   5615 C CB  . HIS D 1 123 ? -13.777 45.348 -53.502 1.00 19.62  ? 104  HIS D CB  1 
ATOM   5616 C CG  . HIS D 1 123 ? -13.417 45.757 -54.887 1.00 26.85  ? 104  HIS D CG  1 
ATOM   5617 N ND1 . HIS D 1 123 ? -14.329 46.318 -55.754 1.00 30.05  ? 104  HIS D ND1 1 
ATOM   5618 C CD2 . HIS D 1 123 ? -12.244 45.674 -55.569 1.00 33.88  ? 104  HIS D CD2 1 
ATOM   5619 C CE1 . HIS D 1 123 ? -13.736 46.574 -56.910 1.00 37.99  ? 104  HIS D CE1 1 
ATOM   5620 N NE2 . HIS D 1 123 ? -12.470 46.194 -56.819 1.00 42.87  ? 104  HIS D NE2 1 
ATOM   5621 N N   . VAL D 1 124 ? -13.635 48.728 -52.755 1.00 19.08  ? 105  VAL D N   1 
ATOM   5622 C CA  . VAL D 1 124 ? -14.395 49.980 -52.746 1.00 17.01  ? 105  VAL D CA  1 
ATOM   5623 C C   . VAL D 1 124 ? -14.341 50.619 -54.109 1.00 20.76  ? 105  VAL D C   1 
ATOM   5624 O O   . VAL D 1 124 ? -13.268 50.809 -54.665 1.00 23.37  ? 105  VAL D O   1 
ATOM   5625 C CB  . VAL D 1 124 ? -13.841 51.009 -51.744 1.00 16.65  ? 105  VAL D CB  1 
ATOM   5626 C CG1 . VAL D 1 124 ? -14.771 52.191 -51.639 1.00 17.16  ? 105  VAL D CG1 1 
ATOM   5627 C CG2 . VAL D 1 124 ? -13.660 50.402 -50.382 1.00 22.93  ? 105  VAL D CG2 1 
ATOM   5628 N N   . VAL D 1 125 ? -15.510 50.960 -54.637 1.00 27.55  ? 106  VAL D N   1 
ATOM   5629 C CA  . VAL D 1 125 ? -15.636 51.619 -55.940 1.00 31.16  ? 106  VAL D CA  1 
ATOM   5630 C C   . VAL D 1 125 ? -15.879 53.123 -55.701 1.00 27.26  ? 106  VAL D C   1 
ATOM   5631 O O   . VAL D 1 125 ? -16.445 53.500 -54.673 1.00 22.44  ? 106  VAL D O   1 
ATOM   5632 C CB  . VAL D 1 125 ? -16.781 50.962 -56.761 1.00 26.87  ? 106  VAL D CB  1 
ATOM   5633 C CG1 . VAL D 1 125 ? -17.020 51.705 -58.049 1.00 39.13  ? 106  VAL D CG1 1 
ATOM   5634 C CG2 . VAL D 1 125 ? -16.445 49.527 -57.058 1.00 24.30  ? 106  VAL D CG2 1 
ATOM   5635 N N   . SER D 1 126 ? -15.452 53.975 -56.632 1.00 29.13  ? 107  SER D N   1 
ATOM   5636 C CA  . SER D 1 126 ? -15.558 55.430 -56.459 1.00 28.99  ? 107  SER D CA  1 
ATOM   5637 C C   . SER D 1 126 ? -16.950 55.960 -56.113 1.00 33.22  ? 107  SER D C   1 
ATOM   5638 O O   . SER D 1 126 ? -17.059 57.024 -55.501 1.00 30.53  ? 107  SER D O   1 
ATOM   5639 C CB  . SER D 1 126 ? -15.011 56.173 -57.674 1.00 29.86  ? 107  SER D CB  1 
ATOM   5640 O OG  . SER D 1 126 ? -15.675 55.750 -58.843 1.00 44.52  ? 107  SER D OG  1 
ATOM   5641 N N   . ASP D 1 127 ? -18.010 55.238 -56.486 1.00 34.15  ? 108  ASP D N   1 
ATOM   5642 C CA  . ASP D 1 127 ? -19.366 55.696 -56.141 1.00 30.66  ? 108  ASP D CA  1 
ATOM   5643 C C   . ASP D 1 127 ? -19.727 55.483 -54.672 1.00 34.88  ? 108  ASP D C   1 
ATOM   5644 O O   . ASP D 1 127 ? -20.706 56.050 -54.181 1.00 41.60  ? 108  ASP D O   1 
ATOM   5645 C CB  . ASP D 1 127 ? -20.446 55.090 -57.048 1.00 30.72  ? 108  ASP D CB  1 
ATOM   5646 C CG  . ASP D 1 127 ? -20.470 53.564 -57.015 1.00 44.34  ? 108  ASP D CG  1 
ATOM   5647 O OD1 . ASP D 1 127 ? -19.822 52.966 -56.123 1.00 52.25  ? 108  ASP D OD1 1 
ATOM   5648 O OD2 . ASP D 1 127 ? -21.148 52.955 -57.884 1.00 50.76  ? 108  ASP D OD2 1 
ATOM   5649 N N   . GLY D 1 128 ? -18.939 54.671 -53.971 1.00 32.29  ? 109  GLY D N   1 
ATOM   5650 C CA  . GLY D 1 128 ? -19.218 54.372 -52.575 1.00 34.03  ? 109  GLY D CA  1 
ATOM   5651 C C   . GLY D 1 128 ? -19.719 52.959 -52.330 1.00 31.93  ? 109  GLY D C   1 
ATOM   5652 O O   . GLY D 1 128 ? -20.129 52.646 -51.221 1.00 25.89  ? 109  GLY D O   1 
ATOM   5653 N N   . GLU D 1 129 ? -19.679 52.114 -53.362 1.00 34.45  ? 110  GLU D N   1 
ATOM   5654 C CA  . GLU D 1 129 ? -20.090 50.716 -53.248 1.00 27.27  ? 110  GLU D CA  1 
ATOM   5655 C C   . GLU D 1 129 ? -18.988 49.850 -52.669 1.00 25.61  ? 110  GLU D C   1 
ATOM   5656 O O   . GLU D 1 129 ? -17.853 49.848 -53.149 1.00 25.21  ? 110  GLU D O   1 
ATOM   5657 C CB  . GLU D 1 129 ? -20.482 50.159 -54.612 1.00 35.62  ? 110  GLU D CB  1 
ATOM   5658 C CG  . GLU D 1 129 ? -21.921 50.424 -54.996 1.00 46.68  ? 110  GLU D CG  1 
ATOM   5659 C CD  . GLU D 1 129 ? -22.908 49.563 -54.217 1.00 57.71  ? 110  GLU D CD  1 
ATOM   5660 O OE1 . GLU D 1 129 ? -22.700 48.318 -54.163 1.00 45.92  ? 110  GLU D OE1 1 
ATOM   5661 O OE2 . GLU D 1 129 ? -23.886 50.141 -53.666 1.00 64.13  ? 110  GLU D OE2 1 
ATOM   5662 N N   . VAL D 1 130 ? -19.338 49.089 -51.649 1.00 27.64  ? 111  VAL D N   1 
ATOM   5663 C CA  . VAL D 1 130 ? -18.359 48.274 -50.953 1.00 23.37  ? 111  VAL D CA  1 
ATOM   5664 C C   . VAL D 1 130 ? -18.739 46.828 -51.101 1.00 19.27  ? 111  VAL D C   1 
ATOM   5665 O O   . VAL D 1 130 ? -19.914 46.475 -51.025 1.00 22.02  ? 111  VAL D O   1 
ATOM   5666 C CB  . VAL D 1 130 ? -18.305 48.641 -49.460 1.00 21.15  ? 111  VAL D CB  1 
ATOM   5667 C CG1 . VAL D 1 130 ? -17.233 47.844 -48.749 1.00 14.33  ? 111  VAL D CG1 1 
ATOM   5668 C CG2 . VAL D 1 130 ? -18.071 50.144 -49.311 1.00 18.30  ? 111  VAL D CG2 1 
ATOM   5669 N N   . GLN D 1 131 ? -17.739 45.989 -51.326 1.00 21.95  ? 112  GLN D N   1 
ATOM   5670 C CA  . GLN D 1 131 ? -17.944 44.547 -51.289 1.00 22.69  ? 112  GLN D CA  1 
ATOM   5671 C C   . GLN D 1 131 ? -16.879 43.850 -50.430 1.00 19.45  ? 112  GLN D C   1 
ATOM   5672 O O   . GLN D 1 131 ? -15.676 44.019 -50.637 1.00 17.68  ? 112  GLN D O   1 
ATOM   5673 C CB  . GLN D 1 131 ? -17.983 43.950 -52.695 1.00 24.42  ? 112  GLN D CB  1 
ATOM   5674 C CG  . GLN D 1 131 ? -18.233 42.449 -52.696 1.00 28.50  ? 112  GLN D CG  1 
ATOM   5675 C CD  . GLN D 1 131 ? -18.294 41.872 -54.091 1.00 33.43  ? 112  GLN D CD  1 
ATOM   5676 O OE1 . GLN D 1 131 ? -18.845 42.486 -55.001 1.00 39.00  ? 112  GLN D OE1 1 
ATOM   5677 N NE2 . GLN D 1 131 ? -17.723 40.683 -54.268 1.00 36.91  ? 112  GLN D NE2 1 
ATOM   5678 N N   . TYR D 1 132 ? -17.337 43.070 -49.458 1.00 18.25  ? 113  TYR D N   1 
ATOM   5679 C CA  . TYR D 1 132 ? -16.431 42.326 -48.598 1.00 21.61  ? 113  TYR D CA  1 
ATOM   5680 C C   . TYR D 1 132 ? -16.803 40.828 -48.654 1.00 22.89  ? 113  TYR D C   1 
ATOM   5681 O O   . TYR D 1 132 ? -17.902 40.444 -48.250 1.00 22.30  ? 113  TYR D O   1 
ATOM   5682 C CB  . TYR D 1 132 ? -16.450 42.900 -47.168 1.00 13.33  ? 113  TYR D CB  1 
ATOM   5683 C CG  . TYR D 1 132 ? -15.608 42.130 -46.182 1.00 16.31  ? 113  TYR D CG  1 
ATOM   5684 C CD1 . TYR D 1 132 ? -14.308 41.752 -46.492 1.00 16.88  ? 113  TYR D CD1 1 
ATOM   5685 C CD2 . TYR D 1 132 ? -16.112 41.785 -44.933 1.00 17.21  ? 113  TYR D CD2 1 
ATOM   5686 C CE1 . TYR D 1 132 ? -13.527 41.032 -45.582 1.00 17.90  ? 113  TYR D CE1 1 
ATOM   5687 C CE2 . TYR D 1 132 ? -15.353 41.066 -44.015 1.00 17.96  ? 113  TYR D CE2 1 
ATOM   5688 C CZ  . TYR D 1 132 ? -14.060 40.684 -44.342 1.00 22.05  ? 113  TYR D CZ  1 
ATOM   5689 O OH  . TYR D 1 132 ? -13.305 39.966 -43.419 1.00 19.72  ? 113  TYR D OH  1 
ATOM   5690 N N   . THR D 1 133 ? -15.891 40.006 -49.186 1.00 19.20  ? 114  THR D N   1 
ATOM   5691 C CA  . THR D 1 133 ? -16.144 38.590 -49.435 1.00 18.58  ? 114  THR D CA  1 
ATOM   5692 C C   . THR D 1 133 ? -15.064 37.701 -48.805 1.00 20.71  ? 114  THR D C   1 
ATOM   5693 O O   . THR D 1 133 ? -14.173 37.205 -49.492 1.00 21.39  ? 114  THR D O   1 
ATOM   5694 C CB  . THR D 1 133 ? -16.215 38.301 -50.946 1.00 18.92  ? 114  THR D CB  1 
ATOM   5695 O OG1 . THR D 1 133 ? -17.024 39.292 -51.587 1.00 25.17  ? 114  THR D OG1 1 
ATOM   5696 C CG2 . THR D 1 133 ? -16.796 36.925 -51.210 1.00 18.58  ? 114  THR D CG2 1 
ATOM   5697 N N   . PRO D 1 134 ? -15.130 37.505 -47.479 1.00 21.73  ? 115  PRO D N   1 
ATOM   5698 C CA  . PRO D 1 134 ? -14.128 36.632 -46.855 1.00 15.35  ? 115  PRO D CA  1 
ATOM   5699 C C   . PRO D 1 134 ? -14.475 35.172 -47.057 1.00 22.29  ? 115  PRO D C   1 
ATOM   5700 O O   . PRO D 1 134 ? -15.663 34.825 -47.176 1.00 26.27  ? 115  PRO D O   1 
ATOM   5701 C CB  . PRO D 1 134 ? -14.259 36.977 -45.368 1.00 17.58  ? 115  PRO D CB  1 
ATOM   5702 C CG  . PRO D 1 134 ? -15.668 37.499 -45.203 1.00 13.64  ? 115  PRO D CG  1 
ATOM   5703 C CD  . PRO D 1 134 ? -16.002 38.183 -46.487 1.00 18.73  ? 115  PRO D CD  1 
ATOM   5704 N N   . SER D 1 135 ? -13.467 34.308 -47.093 1.00 20.59  ? 116  SER D N   1 
ATOM   5705 C CA  . SER D 1 135 ? -13.745 32.866 -47.030 1.00 23.21  ? 116  SER D CA  1 
ATOM   5706 C C   . SER D 1 135 ? -13.780 32.395 -45.565 1.00 22.96  ? 116  SER D C   1 
ATOM   5707 O O   . SER D 1 135 ? -12.833 32.628 -44.805 1.00 22.56  ? 116  SER D O   1 
ATOM   5708 C CB  . SER D 1 135 ? -12.712 32.073 -47.825 1.00 22.26  ? 116  SER D CB  1 
ATOM   5709 O OG  . SER D 1 135 ? -13.000 30.690 -47.782 1.00 23.28  ? 116  SER D OG  1 
ATOM   5710 N N   . ILE D 1 136 ? -14.862 31.724 -45.172 1.00 17.49  ? 117  ILE D N   1 
ATOM   5711 C CA  . ILE D 1 136 ? -15.058 31.375 -43.766 1.00 18.92  ? 117  ILE D CA  1 
ATOM   5712 C C   . ILE D 1 136 ? -15.272 29.884 -43.525 1.00 18.73  ? 117  ILE D C   1 
ATOM   5713 O O   . ILE D 1 136 ? -16.085 29.254 -44.196 1.00 22.92  ? 117  ILE D O   1 
ATOM   5714 C CB  . ILE D 1 136 ? -16.264 32.159 -43.197 1.00 23.88  ? 117  ILE D CB  1 
ATOM   5715 C CG1 . ILE D 1 136 ? -15.953 33.670 -43.189 1.00 23.16  ? 117  ILE D CG1 1 
ATOM   5716 C CG2 . ILE D 1 136 ? -16.641 31.649 -41.813 1.00 19.52  ? 117  ILE D CG2 1 
ATOM   5717 C CD1 . ILE D 1 136 ? -17.126 34.549 -42.806 1.00 21.65  ? 117  ILE D CD1 1 
ATOM   5718 N N   . ARG D 1 137 ? -14.545 29.314 -42.571 1.00 17.48  ? 118  ARG D N   1 
ATOM   5719 C CA  . ARG D 1 137 ? -14.868 27.974 -42.073 1.00 19.55  ? 118  ARG D CA  1 
ATOM   5720 C C   . ARG D 1 137 ? -15.624 28.063 -40.738 1.00 20.57  ? 118  ARG D C   1 
ATOM   5721 O O   . ARG D 1 137 ? -15.119 28.645 -39.777 1.00 23.24  ? 118  ARG D O   1 
ATOM   5722 C CB  . ARG D 1 137 ? -13.603 27.144 -41.894 1.00 18.41  ? 118  ARG D CB  1 
ATOM   5723 C CG  . ARG D 1 137 ? -13.855 25.868 -41.146 1.00 23.88  ? 118  ARG D CG  1 
ATOM   5724 C CD  . ARG D 1 137 ? -12.746 24.864 -41.314 1.00 28.68  ? 118  ARG D CD  1 
ATOM   5725 N NE  . ARG D 1 137 ? -13.095 23.569 -40.708 1.00 40.52  ? 118  ARG D NE  1 
ATOM   5726 C CZ  . ARG D 1 137 ? -12.371 22.456 -40.819 1.00 38.51  ? 118  ARG D CZ  1 
ATOM   5727 N NH1 . ARG D 1 137 ? -11.242 22.453 -41.530 1.00 34.08  ? 118  ARG D NH1 1 
ATOM   5728 N NH2 . ARG D 1 137 ? -12.791 21.338 -40.240 1.00 36.78  ? 118  ARG D NH2 1 
ATOM   5729 N N   . GLN D 1 138 ? -16.823 27.487 -40.673 1.00 16.38  ? 119  GLN D N   1 
ATOM   5730 C CA  . GLN D 1 138 ? -17.644 27.574 -39.455 1.00 23.54  ? 119  GLN D CA  1 
ATOM   5731 C C   . GLN D 1 138 ? -18.442 26.290 -39.174 1.00 24.87  ? 119  GLN D C   1 
ATOM   5732 O O   . GLN D 1 138 ? -18.855 25.590 -40.099 1.00 26.38  ? 119  GLN D O   1 
ATOM   5733 C CB  . GLN D 1 138 ? -18.592 28.795 -39.521 1.00 22.48  ? 119  GLN D CB  1 
ATOM   5734 C CG  . GLN D 1 138 ? -19.172 29.241 -38.169 1.00 20.56  ? 119  GLN D CG  1 
ATOM   5735 C CD  . GLN D 1 138 ? -19.670 30.674 -38.221 1.00 20.59  ? 119  GLN D CD  1 
ATOM   5736 O OE1 . GLN D 1 138 ? -19.995 31.170 -39.298 1.00 18.06  ? 119  GLN D OE1 1 
ATOM   5737 N NE2 . GLN D 1 138 ? -19.721 31.354 -37.062 1.00 21.36  ? 119  GLN D NE2 1 
ATOM   5738 N N   . ARG D 1 139 ? -18.663 25.991 -37.898 1.00 20.20  ? 120  ARG D N   1 
ATOM   5739 C CA  . ARG D 1 139 ? -19.486 24.848 -37.501 1.00 21.18  ? 120  ARG D CA  1 
ATOM   5740 C C   . ARG D 1 139 ? -20.942 25.280 -37.152 1.00 24.03  ? 120  ARG D C   1 
ATOM   5741 O O   . ARG D 1 139 ? -21.168 26.292 -36.471 1.00 21.53  ? 120  ARG D O   1 
ATOM   5742 C CB  . ARG D 1 139 ? -18.809 24.100 -36.349 1.00 22.83  ? 120  ARG D CB  1 
ATOM   5743 C CG  . ARG D 1 139 ? -19.366 22.716 -36.121 1.00 30.77  ? 120  ARG D CG  1 
ATOM   5744 C CD  . ARG D 1 139 ? -18.391 21.772 -35.370 1.00 49.12  ? 120  ARG D CD  1 
ATOM   5745 N NE  . ARG D 1 139 ? -18.946 20.412 -35.316 1.00 46.51  ? 120  ARG D NE  1 
ATOM   5746 C CZ  . ARG D 1 139 ? -18.752 19.479 -36.251 1.00 44.01  ? 120  ARG D CZ  1 
ATOM   5747 N NH1 . ARG D 1 139 ? -17.983 19.727 -37.302 1.00 43.00  ? 120  ARG D NH1 1 
ATOM   5748 N NH2 . ARG D 1 139 ? -19.327 18.288 -36.140 1.00 46.55  ? 120  ARG D NH2 1 
ATOM   5749 N N   . PHE D 1 140 ? -21.933 24.540 -37.648 1.00 26.30  ? 121  PHE D N   1 
ATOM   5750 C CA  . PHE D 1 140 ? -23.339 24.898 -37.408 1.00 21.23  ? 121  PHE D CA  1 
ATOM   5751 C C   . PHE D 1 140 ? -24.139 23.779 -36.788 1.00 26.28  ? 121  PHE D C   1 
ATOM   5752 O O   . PHE D 1 140 ? -23.743 22.615 -36.832 1.00 30.16  ? 121  PHE D O   1 
ATOM   5753 C CB  . PHE D 1 140 ? -24.041 25.283 -38.699 1.00 20.74  ? 121  PHE D CB  1 
ATOM   5754 C CG  . PHE D 1 140 ? -23.460 26.472 -39.359 1.00 23.55  ? 121  PHE D CG  1 
ATOM   5755 C CD1 . PHE D 1 140 ? -22.412 26.332 -40.254 1.00 19.43  ? 121  PHE D CD1 1 
ATOM   5756 C CD2 . PHE D 1 140 ? -23.956 27.745 -39.084 1.00 24.89  ? 121  PHE D CD2 1 
ATOM   5757 C CE1 . PHE D 1 140 ? -21.862 27.446 -40.871 1.00 21.29  ? 121  PHE D CE1 1 
ATOM   5758 C CE2 . PHE D 1 140 ? -23.408 28.871 -39.695 1.00 21.15  ? 121  PHE D CE2 1 
ATOM   5759 C CZ  . PHE D 1 140 ? -22.357 28.724 -40.590 1.00 18.47  ? 121  PHE D CZ  1 
ATOM   5760 N N   . SER D 1 141 ? -25.287 24.150 -36.232 1.00 27.89  ? 122  SER D N   1 
ATOM   5761 C CA  . SER D 1 141 ? -26.249 23.199 -35.692 1.00 28.18  ? 122  SER D CA  1 
ATOM   5762 C C   . SER D 1 141 ? -27.493 23.222 -36.580 1.00 30.60  ? 122  SER D C   1 
ATOM   5763 O O   . SER D 1 141 ? -28.171 24.245 -36.690 1.00 28.98  ? 122  SER D O   1 
ATOM   5764 C CB  . SER D 1 141 ? -26.609 23.582 -34.259 1.00 32.79  ? 122  SER D CB  1 
ATOM   5765 O OG  . SER D 1 141 ? -27.838 22.996 -33.865 1.00 44.14  ? 122  SER D OG  1 
ATOM   5766 N N   . CYS D 1 142 ? -27.784 22.097 -37.222 1.00 36.34  ? 123  CYS D N   1 
ATOM   5767 C CA  . CYS D 1 142 ? -28.894 22.037 -38.170 1.00 42.04  ? 123  CYS D CA  1 
ATOM   5768 C C   . CYS D 1 142 ? -29.357 20.612 -38.419 1.00 40.12  ? 123  CYS D C   1 
ATOM   5769 O O   . CYS D 1 142 ? -28.788 19.672 -37.869 1.00 41.10  ? 123  CYS D O   1 
ATOM   5770 C CB  . CYS D 1 142 ? -28.500 22.703 -39.492 1.00 44.99  ? 123  CYS D CB  1 
ATOM   5771 S SG  . CYS D 1 142 ? -26.950 22.080 -40.211 1.00 59.70  ? 123  CYS D SG  1 
ATOM   5772 N N   . ASP D 1 143 ? -30.379 20.458 -39.260 1.00 37.75  ? 124  ASP D N   1 
ATOM   5773 C CA  . ASP D 1 143 ? -30.949 19.139 -39.532 1.00 40.70  ? 124  ASP D CA  1 
ATOM   5774 C C   . ASP D 1 143 ? -30.110 18.356 -40.549 1.00 39.95  ? 124  ASP D C   1 
ATOM   5775 O O   . ASP D 1 143 ? -30.006 18.752 -41.716 1.00 36.66  ? 124  ASP D O   1 
ATOM   5776 C CB  . ASP D 1 143 ? -32.390 19.277 -40.022 1.00 46.94  ? 124  ASP D CB  1 
ATOM   5777 C CG  . ASP D 1 143 ? -33.195 17.989 -39.876 1.00 43.01  ? 124  ASP D CG  1 
ATOM   5778 O OD1 . ASP D 1 143 ? -32.691 17.024 -39.250 1.00 41.18  ? 124  ASP D OD1 1 
ATOM   5779 O OD2 . ASP D 1 143 ? -34.344 17.960 -40.378 1.00 36.81  ? 124  ASP D OD2 1 
ATOM   5780 N N   . VAL D 1 144 ? -29.529 17.244 -40.088 1.00 32.91  ? 125  VAL D N   1 
ATOM   5781 C CA  . VAL D 1 144 ? -28.575 16.459 -40.864 1.00 33.72  ? 125  VAL D CA  1 
ATOM   5782 C C   . VAL D 1 144 ? -29.173 15.117 -41.317 1.00 41.76  ? 125  VAL D C   1 
ATOM   5783 O O   . VAL D 1 144 ? -28.620 14.424 -42.178 1.00 42.94  ? 125  VAL D O   1 
ATOM   5784 C CB  . VAL D 1 144 ? -27.303 16.214 -40.035 1.00 37.19  ? 125  VAL D CB  1 
ATOM   5785 C CG1 . VAL D 1 144 ? -26.268 15.451 -40.825 1.00 31.59  ? 125  VAL D CG1 1 
ATOM   5786 C CG2 . VAL D 1 144 ? -26.729 17.531 -39.562 1.00 38.83  ? 125  VAL D CG2 1 
ATOM   5787 N N   . SER D 1 145 ? -30.312 14.758 -40.733 1.00 45.16  ? 126  SER D N   1 
ATOM   5788 C CA  . SER D 1 145 ? -31.002 13.508 -41.059 1.00 44.86  ? 126  SER D CA  1 
ATOM   5789 C C   . SER D 1 145 ? -31.225 13.331 -42.573 1.00 51.30  ? 126  SER D C   1 
ATOM   5790 O O   . SER D 1 145 ? -31.692 14.255 -43.273 1.00 47.26  ? 126  SER D O   1 
ATOM   5791 C CB  . SER D 1 145 ? -32.345 13.448 -40.332 1.00 39.44  ? 126  SER D CB  1 
ATOM   5792 O OG  . SER D 1 145 ? -33.192 14.508 -40.753 1.00 40.30  ? 126  SER D OG  1 
ATOM   5793 N N   . GLY D 1 146 ? -30.882 12.143 -43.072 1.00 48.56  ? 127  GLY D N   1 
ATOM   5794 C CA  . GLY D 1 146 ? -31.084 11.818 -44.473 1.00 45.99  ? 127  GLY D CA  1 
ATOM   5795 C C   . GLY D 1 146 ? -29.918 12.241 -45.337 1.00 39.38  ? 127  GLY D C   1 
ATOM   5796 O O   . GLY D 1 146 ? -30.027 12.371 -46.551 1.00 38.54  ? 127  GLY D O   1 
ATOM   5797 N N   . VAL D 1 147 ? -28.781 12.454 -44.700 1.00 42.12  ? 128  VAL D N   1 
ATOM   5798 C CA  . VAL D 1 147 ? -27.600 12.861 -45.431 1.00 39.22  ? 128  VAL D CA  1 
ATOM   5799 C C   . VAL D 1 147 ? -27.098 11.702 -46.291 1.00 40.31  ? 128  VAL D C   1 
ATOM   5800 O O   . VAL D 1 147 ? -26.476 11.923 -47.333 1.00 45.83  ? 128  VAL D O   1 
ATOM   5801 C CB  . VAL D 1 147 ? -26.502 13.394 -44.475 1.00 35.84  ? 128  VAL D CB  1 
ATOM   5802 C CG1 . VAL D 1 147 ? -26.098 12.331 -43.443 1.00 33.93  ? 128  VAL D CG1 1 
ATOM   5803 C CG2 . VAL D 1 147 ? -25.303 13.892 -45.266 1.00 37.80  ? 128  VAL D CG2 1 
ATOM   5804 N N   . ASP D 1 148 ? -27.389 10.473 -45.858 1.00 44.52  ? 129  ASP D N   1 
ATOM   5805 C CA  . ASP D 1 148 ? -26.937 9.276  -46.564 1.00 45.00  ? 129  ASP D CA  1 
ATOM   5806 C C   . ASP D 1 148 ? -28.060 8.649  -47.417 1.00 37.49  ? 129  ASP D C   1 
ATOM   5807 O O   . ASP D 1 148 ? -28.135 7.446  -47.573 1.00 38.32  ? 129  ASP D O   1 
ATOM   5808 C CB  . ASP D 1 148 ? -26.343 8.273  -45.565 1.00 49.72  ? 129  ASP D CB  1 
ATOM   5809 C CG  . ASP D 1 148 ? -25.161 7.481  -46.153 1.00 74.00  ? 129  ASP D CG  1 
ATOM   5810 O OD1 . ASP D 1 148 ? -25.240 7.056  -47.338 1.00 76.28  ? 129  ASP D OD1 1 
ATOM   5811 O OD2 . ASP D 1 148 ? -24.148 7.290  -45.431 1.00 67.55  ? 129  ASP D OD2 1 
ATOM   5812 N N   . THR D 1 149 ? -28.896 9.508  -47.988 1.00 36.85  ? 130  THR D N   1 
ATOM   5813 C CA  . THR D 1 149 ? -30.128 9.152  -48.678 1.00 31.79  ? 130  THR D CA  1 
ATOM   5814 C C   . THR D 1 149 ? -30.132 9.833  -50.045 1.00 46.23  ? 130  THR D C   1 
ATOM   5815 O O   . THR D 1 149 ? -29.453 10.837 -50.239 1.00 53.57  ? 130  THR D O   1 
ATOM   5816 C CB  . THR D 1 149 ? -31.330 9.639  -47.841 1.00 36.10  ? 130  THR D CB  1 
ATOM   5817 O OG1 . THR D 1 149 ? -31.444 8.823  -46.665 1.00 37.03  ? 130  THR D OG1 1 
ATOM   5818 C CG2 . THR D 1 149 ? -32.649 9.616  -48.622 1.00 44.70  ? 130  THR D CG2 1 
ATOM   5819 N N   . GLU D 1 150 ? -30.883 9.303  -51.000 1.00 49.98  ? 131  GLU D N   1 
ATOM   5820 C CA  . GLU D 1 150 ? -30.917 9.899  -52.328 1.00 53.48  ? 131  GLU D CA  1 
ATOM   5821 C C   . GLU D 1 150 ? -31.504 11.322 -52.349 1.00 49.86  ? 131  GLU D C   1 
ATOM   5822 O O   . GLU D 1 150 ? -31.158 12.126 -53.210 1.00 53.40  ? 131  GLU D O   1 
ATOM   5823 C CB  . GLU D 1 150 ? -31.682 8.982  -53.281 1.00 71.65  ? 131  GLU D CB  1 
ATOM   5824 C CG  . GLU D 1 150 ? -31.454 9.259  -54.752 1.00 73.14  ? 131  GLU D CG  1 
ATOM   5825 C CD  . GLU D 1 150 ? -32.543 8.657  -55.616 1.00 85.93  ? 131  GLU D CD  1 
ATOM   5826 O OE1 . GLU D 1 150 ? -33.727 8.716  -55.209 1.00 87.45  ? 131  GLU D OE1 1 
ATOM   5827 O OE2 . GLU D 1 150 ? -32.216 8.122  -56.698 1.00 93.00  ? 131  GLU D OE2 1 
ATOM   5828 N N   . SER D 1 151 ? -32.381 11.638 -51.402 1.00 47.16  ? 132  SER D N   1 
ATOM   5829 C CA  . SER D 1 151 ? -32.999 12.966 -51.358 1.00 43.22  ? 132  SER D CA  1 
ATOM   5830 C C   . SER D 1 151 ? -32.211 13.983 -50.506 1.00 43.11  ? 132  SER D C   1 
ATOM   5831 O O   . SER D 1 151 ? -32.474 15.188 -50.556 1.00 44.95  ? 132  SER D O   1 
ATOM   5832 C CB  . SER D 1 151 ? -34.444 12.856 -50.867 1.00 42.82  ? 132  SER D CB  1 
ATOM   5833 O OG  . SER D 1 151 ? -34.502 12.061 -49.694 1.00 62.42  ? 132  SER D OG  1 
ATOM   5834 N N   . GLY D 1 152 ? -31.263 13.493 -49.712 1.00 41.62  ? 133  GLY D N   1 
ATOM   5835 C CA  . GLY D 1 152 ? -30.355 14.354 -48.971 1.00 42.03  ? 133  GLY D CA  1 
ATOM   5836 C C   . GLY D 1 152 ? -30.899 15.031 -47.716 1.00 46.47  ? 133  GLY D C   1 
ATOM   5837 O O   . GLY D 1 152 ? -32.091 14.954 -47.413 1.00 40.63  ? 133  GLY D O   1 
ATOM   5838 N N   . ALA D 1 153 ? -30.004 15.696 -46.977 1.00 52.28  ? 134  ALA D N   1 
ATOM   5839 C CA  . ALA D 1 153 ? -30.382 16.524 -45.826 1.00 42.35  ? 134  ALA D CA  1 
ATOM   5840 C C   . ALA D 1 153 ? -30.579 17.970 -46.264 1.00 35.78  ? 134  ALA D C   1 
ATOM   5841 O O   . ALA D 1 153 ? -29.976 18.420 -47.243 1.00 36.29  ? 134  ALA D O   1 
ATOM   5842 C CB  . ALA D 1 153 ? -29.318 16.453 -44.755 1.00 36.19  ? 134  ALA D CB  1 
ATOM   5843 N N   . THR D 1 154 ? -31.425 18.696 -45.544 1.00 36.92  ? 135  THR D N   1 
ATOM   5844 C CA  . THR D 1 154 ? -31.544 20.142 -45.761 1.00 45.62  ? 135  THR D CA  1 
ATOM   5845 C C   . THR D 1 154 ? -31.193 20.942 -44.505 1.00 45.99  ? 135  THR D C   1 
ATOM   5846 O O   . THR D 1 154 ? -31.972 21.000 -43.545 1.00 43.31  ? 135  THR D O   1 
ATOM   5847 C CB  . THR D 1 154 ? -32.940 20.570 -46.263 1.00 48.95  ? 135  THR D CB  1 
ATOM   5848 O OG1 . THR D 1 154 ? -33.333 19.744 -47.364 1.00 52.25  ? 135  THR D OG1 1 
ATOM   5849 C CG2 . THR D 1 154 ? -32.916 22.035 -46.723 1.00 38.95  ? 135  THR D CG2 1 
ATOM   5850 N N   . CYS D 1 155 ? -30.008 21.548 -44.540 1.00 41.42  ? 136  CYS D N   1 
ATOM   5851 C CA  . CYS D 1 155 ? -29.499 22.370 -43.458 1.00 40.57  ? 136  CYS D CA  1 
ATOM   5852 C C   . CYS D 1 155 ? -29.787 23.871 -43.730 1.00 43.05  ? 136  CYS D C   1 
ATOM   5853 O O   . CYS D 1 155 ? -29.472 24.371 -44.815 1.00 41.36  ? 136  CYS D O   1 
ATOM   5854 C CB  . CYS D 1 155 ? -27.998 22.111 -43.304 1.00 31.54  ? 136  CYS D CB  1 
ATOM   5855 S SG  . CYS D 1 155 ? -27.206 23.072 -41.977 1.00 68.78  ? 136  CYS D SG  1 
ATOM   5856 N N   . ARG D 1 156 ? -30.407 24.572 -42.772 1.00 37.21  ? 137  ARG D N   1 
ATOM   5857 C CA  . ARG D 1 156 ? -30.668 26.011 -42.910 1.00 37.58  ? 137  ARG D CA  1 
ATOM   5858 C C   . ARG D 1 156 ? -29.694 26.865 -42.075 1.00 36.21  ? 137  ARG D C   1 
ATOM   5859 O O   . ARG D 1 156 ? -29.411 26.551 -40.915 1.00 42.60  ? 137  ARG D O   1 
ATOM   5860 C CB  . ARG D 1 156 ? -32.110 26.379 -42.525 1.00 39.04  ? 137  ARG D CB  1 
ATOM   5861 C CG  . ARG D 1 156 ? -33.184 25.412 -42.966 1.00 48.42  ? 137  ARG D CG  1 
ATOM   5862 C CD  . ARG D 1 156 ? -34.596 25.911 -42.580 1.00 62.20  ? 137  ARG D CD  1 
ATOM   5863 N NE  . ARG D 1 156 ? -34.661 26.575 -41.267 1.00 67.63  ? 137  ARG D NE  1 
ATOM   5864 C CZ  . ARG D 1 156 ? -34.929 25.964 -40.105 1.00 66.51  ? 137  ARG D CZ  1 
ATOM   5865 N NH1 . ARG D 1 156 ? -35.156 24.654 -40.065 1.00 64.84  ? 137  ARG D NH1 1 
ATOM   5866 N NH2 . ARG D 1 156 ? -34.965 26.663 -38.971 1.00 54.79  ? 137  ARG D NH2 1 
ATOM   5867 N N   . ILE D 1 157 ? -29.197 27.950 -42.664 1.00 26.11  ? 138  ILE D N   1 
ATOM   5868 C CA  . ILE D 1 157 ? -28.309 28.860 -41.958 1.00 30.04  ? 138  ILE D CA  1 
ATOM   5869 C C   . ILE D 1 157 ? -28.949 30.232 -41.906 1.00 33.58  ? 138  ILE D C   1 
ATOM   5870 O O   . ILE D 1 157 ? -29.318 30.791 -42.950 1.00 35.26  ? 138  ILE D O   1 
ATOM   5871 C CB  . ILE D 1 157 ? -26.944 28.978 -42.648 1.00 26.09  ? 138  ILE D CB  1 
ATOM   5872 C CG1 . ILE D 1 157 ? -26.229 27.624 -42.629 1.00 23.11  ? 138  ILE D CG1 1 
ATOM   5873 C CG2 . ILE D 1 157 ? -26.116 30.054 -41.971 1.00 19.00  ? 138  ILE D CG2 1 
ATOM   5874 C CD1 . ILE D 1 157 ? -24.787 27.687 -43.025 1.00 18.98  ? 138  ILE D CD1 1 
ATOM   5875 N N   . LYS D 1 158 ? -29.087 30.779 -40.699 1.00 29.05  ? 139  LYS D N   1 
ATOM   5876 C CA  . LYS D 1 158 ? -29.790 32.053 -40.514 1.00 23.34  ? 139  LYS D CA  1 
ATOM   5877 C C   . LYS D 1 158 ? -28.804 33.179 -40.200 1.00 22.14  ? 139  LYS D C   1 
ATOM   5878 O O   . LYS D 1 158 ? -28.113 33.159 -39.169 1.00 22.49  ? 139  LYS D O   1 
ATOM   5879 C CB  . LYS D 1 158 ? -30.841 31.904 -39.416 1.00 23.35  ? 139  LYS D CB  1 
ATOM   5880 C CG  . LYS D 1 158 ? -31.559 33.175 -39.044 1.00 29.28  ? 139  LYS D CG  1 
ATOM   5881 C CD  . LYS D 1 158 ? -32.284 33.006 -37.703 1.00 26.84  ? 139  LYS D CD  1 
ATOM   5882 C CE  . LYS D 1 158 ? -32.614 34.362 -37.059 1.00 32.05  ? 139  LYS D CE  1 
ATOM   5883 N NZ  . LYS D 1 158 ? -33.445 34.238 -35.820 1.00 32.40  ? 139  LYS D NZ  1 
ATOM   5884 N N   . ILE D 1 159 ? -28.733 34.155 -41.099 1.00 20.40  ? 140  ILE D N   1 
ATOM   5885 C CA  . ILE D 1 159 ? -27.762 35.238 -40.975 1.00 22.35  ? 140  ILE D CA  1 
ATOM   5886 C C   . ILE D 1 159 ? -28.433 36.603 -40.931 1.00 25.81  ? 140  ILE D C   1 
ATOM   5887 O O   . ILE D 1 159 ? -29.256 36.908 -41.790 1.00 29.72  ? 140  ILE D O   1 
ATOM   5888 C CB  . ILE D 1 159 ? -26.797 35.216 -42.144 1.00 17.70  ? 140  ILE D CB  1 
ATOM   5889 C CG1 . ILE D 1 159 ? -25.983 33.934 -42.100 1.00 21.92  ? 140  ILE D CG1 1 
ATOM   5890 C CG2 . ILE D 1 159 ? -25.878 36.418 -42.100 1.00 23.19  ? 140  ILE D CG2 1 
ATOM   5891 C CD1 . ILE D 1 159 ? -24.909 33.857 -43.172 1.00 32.64  ? 140  ILE D CD1 1 
ATOM   5892 N N   . GLY D 1 160 ? -28.090 37.425 -39.936 1.00 25.97  ? 141  GLY D N   1 
ATOM   5893 C CA  . GLY D 1 160 ? -28.677 38.756 -39.832 1.00 23.35  ? 141  GLY D CA  1 
ATOM   5894 C C   . GLY D 1 160 ? -27.875 39.719 -38.985 1.00 21.06  ? 141  GLY D C   1 
ATOM   5895 O O   . GLY D 1 160 ? -26.876 39.330 -38.373 1.00 21.31  ? 141  GLY D O   1 
ATOM   5896 N N   . SER D 1 161 ? -28.306 40.980 -38.949 1.00 24.53  ? 142  SER D N   1 
ATOM   5897 C CA  . SER D 1 161 ? -27.689 41.978 -38.061 1.00 24.03  ? 142  SER D CA  1 
ATOM   5898 C C   . SER D 1 161 ? -27.914 41.628 -36.588 1.00 23.66  ? 142  SER D C   1 
ATOM   5899 O O   . SER D 1 161 ? -29.029 41.248 -36.193 1.00 23.32  ? 142  SER D O   1 
ATOM   5900 C CB  . SER D 1 161 ? -28.245 43.375 -38.332 1.00 19.37  ? 142  SER D CB  1 
ATOM   5901 O OG  . SER D 1 161 ? -27.712 44.305 -37.415 1.00 20.68  ? 142  SER D OG  1 
ATOM   5902 N N   . TRP D 1 162 ? -26.869 41.770 -35.775 1.00 16.56  ? 143  TRP D N   1 
ATOM   5903 C CA  . TRP D 1 162 ? -26.966 41.396 -34.370 1.00 21.51  ? 143  TRP D CA  1 
ATOM   5904 C C   . TRP D 1 162 ? -27.575 42.493 -33.492 1.00 26.06  ? 143  TRP D C   1 
ATOM   5905 O O   . TRP D 1 162 ? -28.288 42.193 -32.516 1.00 23.55  ? 143  TRP D O   1 
ATOM   5906 C CB  . TRP D 1 162 ? -25.605 40.963 -33.807 1.00 20.80  ? 143  TRP D CB  1 
ATOM   5907 C CG  . TRP D 1 162 ? -25.729 40.196 -32.489 1.00 24.64  ? 143  TRP D CG  1 
ATOM   5908 C CD1 . TRP D 1 162 ? -25.408 40.651 -31.228 1.00 24.97  ? 143  TRP D CD1 1 
ATOM   5909 C CD2 . TRP D 1 162 ? -26.218 38.856 -32.311 1.00 18.51  ? 143  TRP D CD2 1 
ATOM   5910 N NE1 . TRP D 1 162 ? -25.656 39.669 -30.295 1.00 18.82  ? 143  TRP D NE1 1 
ATOM   5911 C CE2 . TRP D 1 162 ? -26.154 38.559 -30.935 1.00 16.96  ? 143  TRP D CE2 1 
ATOM   5912 C CE3 . TRP D 1 162 ? -26.693 37.872 -33.187 1.00 21.16  ? 143  TRP D CE3 1 
ATOM   5913 C CZ2 . TRP D 1 162 ? -26.559 37.337 -30.413 1.00 18.74  ? 143  TRP D CZ2 1 
ATOM   5914 C CZ3 . TRP D 1 162 ? -27.087 36.644 -32.670 1.00 16.96  ? 143  TRP D CZ3 1 
ATOM   5915 C CH2 . TRP D 1 162 ? -27.016 36.388 -31.297 1.00 16.34  ? 143  TRP D CH2 1 
ATOM   5916 N N   . THR D 1 163 ? -27.288 43.753 -33.833 1.00 21.60  ? 144  THR D N   1 
ATOM   5917 C CA  . THR D 1 163 ? -27.716 44.874 -33.001 1.00 20.35  ? 144  THR D CA  1 
ATOM   5918 C C   . THR D 1 163 ? -28.543 45.939 -33.712 1.00 22.03  ? 144  THR D C   1 
ATOM   5919 O O   . THR D 1 163 ? -29.055 46.850 -33.064 1.00 27.14  ? 144  THR D O   1 
ATOM   5920 C CB  . THR D 1 163 ? -26.530 45.592 -32.347 1.00 19.46  ? 144  THR D CB  1 
ATOM   5921 O OG1 . THR D 1 163 ? -25.739 46.195 -33.374 1.00 21.29  ? 144  THR D OG1 1 
ATOM   5922 C CG2 . THR D 1 163 ? -25.692 44.636 -31.534 1.00 16.11  ? 144  THR D CG2 1 
ATOM   5923 N N   . HIS D 1 164 ? -28.663 45.857 -35.030 1.00 22.00  ? 145  HIS D N   1 
ATOM   5924 C CA  . HIS D 1 164 ? -29.427 46.872 -35.767 1.00 22.57  ? 145  HIS D CA  1 
ATOM   5925 C C   . HIS D 1 164 ? -30.765 46.349 -36.283 1.00 25.67  ? 145  HIS D C   1 
ATOM   5926 O O   . HIS D 1 164 ? -30.805 45.342 -36.984 1.00 21.86  ? 145  HIS D O   1 
ATOM   5927 C CB  . HIS D 1 164 ? -28.611 47.420 -36.930 1.00 22.86  ? 145  HIS D CB  1 
ATOM   5928 C CG  . HIS D 1 164 ? -27.400 48.197 -36.511 1.00 25.01  ? 145  HIS D CG  1 
ATOM   5929 N ND1 . HIS D 1 164 ? -27.485 49.443 -35.925 1.00 28.63  ? 145  HIS D ND1 1 
ATOM   5930 C CD2 . HIS D 1 164 ? -26.079 47.916 -36.611 1.00 24.91  ? 145  HIS D CD2 1 
ATOM   5931 C CE1 . HIS D 1 164 ? -26.267 49.894 -35.677 1.00 27.13  ? 145  HIS D CE1 1 
ATOM   5932 N NE2 . HIS D 1 164 ? -25.396 48.989 -36.083 1.00 28.01  ? 145  HIS D NE2 1 
ATOM   5933 N N   . HIS D 1 165 ? -31.858 47.035 -35.941 1.00 30.44  ? 146  HIS D N   1 
ATOM   5934 C CA  . HIS D 1 165 ? -33.195 46.607 -36.365 1.00 26.95  ? 146  HIS D CA  1 
ATOM   5935 C C   . HIS D 1 165 ? -33.512 46.999 -37.819 1.00 30.12  ? 146  HIS D C   1 
ATOM   5936 O O   . HIS D 1 165 ? -32.678 47.573 -38.509 1.00 34.34  ? 146  HIS D O   1 
ATOM   5937 C CB  . HIS D 1 165 ? -34.273 47.088 -35.392 1.00 33.30  ? 146  HIS D CB  1 
ATOM   5938 C CG  . HIS D 1 165 ? -34.358 48.581 -35.262 1.00 37.21  ? 146  HIS D CG  1 
ATOM   5939 N ND1 . HIS D 1 165 ? -34.667 49.397 -36.328 1.00 40.34  ? 146  HIS D ND1 1 
ATOM   5940 C CD2 . HIS D 1 165 ? -34.180 49.379 -34.196 1.00 41.67  ? 146  HIS D CD2 1 
ATOM   5941 C CE1 . HIS D 1 165 ? -34.668 50.655 -35.914 1.00 45.84  ? 146  HIS D CE1 1 
ATOM   5942 N NE2 . HIS D 1 165 ? -34.378 50.679 -34.634 1.00 47.77  ? 146  HIS D NE2 1 
ATOM   5943 N N   . SER D 1 166 ? -34.720 46.693 -38.278 1.00 34.66  ? 147  SER D N   1 
ATOM   5944 C CA  . SER D 1 166 ? -35.057 46.753 -39.706 1.00 33.05  ? 147  SER D CA  1 
ATOM   5945 C C   . SER D 1 166 ? -35.035 48.144 -40.339 1.00 35.27  ? 147  SER D C   1 
ATOM   5946 O O   . SER D 1 166 ? -34.977 48.263 -41.561 1.00 38.95  ? 147  SER D O   1 
ATOM   5947 C CB  . SER D 1 166 ? -36.430 46.133 -39.942 1.00 32.49  ? 147  SER D CB  1 
ATOM   5948 O OG  . SER D 1 166 ? -37.407 46.870 -39.237 1.00 35.15  ? 147  SER D OG  1 
ATOM   5949 N N   . ARG D 1 167 ? -35.105 49.191 -39.525 1.00 36.33  ? 148  ARG D N   1 
ATOM   5950 C CA  . ARG D 1 167 ? -35.094 50.550 -40.061 1.00 40.21  ? 148  ARG D CA  1 
ATOM   5951 C C   . ARG D 1 167 ? -33.672 51.097 -40.175 1.00 40.08  ? 148  ARG D C   1 
ATOM   5952 O O   . ARG D 1 167 ? -33.455 52.166 -40.749 1.00 41.90  ? 148  ARG D O   1 
ATOM   5953 C CB  . ARG D 1 167 ? -35.956 51.492 -39.204 1.00 55.18  ? 148  ARG D CB  1 
ATOM   5954 C CG  . ARG D 1 167 ? -37.462 51.208 -39.208 1.00 53.31  ? 148  ARG D CG  1 
ATOM   5955 C CD  . ARG D 1 167 ? -38.237 52.256 -38.389 1.00 73.62  ? 148  ARG D CD  1 
ATOM   5956 N NE  . ARG D 1 167 ? -37.377 53.026 -37.481 1.00 80.34  ? 148  ARG D NE  1 
ATOM   5957 C CZ  . ARG D 1 167 ? -37.669 53.308 -36.210 1.00 87.40  ? 148  ARG D CZ  1 
ATOM   5958 N NH1 . ARG D 1 167 ? -38.809 52.882 -35.675 1.00 84.78  ? 148  ARG D NH1 1 
ATOM   5959 N NH2 . ARG D 1 167 ? -36.815 54.016 -35.470 1.00 88.10  ? 148  ARG D NH2 1 
ATOM   5960 N N   . GLU D 1 168 ? -32.716 50.357 -39.617 1.00 38.94  ? 149  GLU D N   1 
ATOM   5961 C CA  . GLU D 1 168 ? -31.307 50.737 -39.659 1.00 35.54  ? 149  GLU D CA  1 
ATOM   5962 C C   . GLU D 1 168 ? -30.514 49.879 -40.655 1.00 31.10  ? 149  GLU D C   1 
ATOM   5963 O O   . GLU D 1 168 ? -29.728 50.404 -41.439 1.00 33.45  ? 149  GLU D O   1 
ATOM   5964 C CB  . GLU D 1 168 ? -30.687 50.670 -38.253 1.00 38.35  ? 149  GLU D CB  1 
ATOM   5965 C CG  . GLU D 1 168 ? -31.254 51.676 -37.257 1.00 40.61  ? 149  GLU D CG  1 
ATOM   5966 C CD  . GLU D 1 168 ? -30.720 51.502 -35.822 1.00 50.78  ? 149  GLU D CD  1 
ATOM   5967 O OE1 . GLU D 1 168 ? -30.502 50.336 -35.382 1.00 39.25  ? 149  GLU D OE1 1 
ATOM   5968 O OE2 . GLU D 1 168 ? -30.533 52.546 -35.136 1.00 62.94  ? 149  GLU D OE2 1 
ATOM   5969 N N   . ILE D 1 169 ? -30.719 48.564 -40.610 1.00 28.89  ? 150  ILE D N   1 
ATOM   5970 C CA  . ILE D 1 169 ? -30.125 47.645 -41.582 1.00 27.82  ? 150  ILE D CA  1 
ATOM   5971 C C   . ILE D 1 169 ? -31.199 46.715 -42.127 1.00 28.10  ? 150  ILE D C   1 
ATOM   5972 O O   . ILE D 1 169 ? -31.943 46.103 -41.353 1.00 29.00  ? 150  ILE D O   1 
ATOM   5973 C CB  . ILE D 1 169 ? -28.959 46.794 -40.970 1.00 24.20  ? 150  ILE D CB  1 
ATOM   5974 C CG1 . ILE D 1 169 ? -27.735 47.680 -40.708 1.00 27.39  ? 150  ILE D CG1 1 
ATOM   5975 C CG2 . ILE D 1 169 ? -28.582 45.613 -41.877 1.00 16.36  ? 150  ILE D CG2 1 
ATOM   5976 C CD1 . ILE D 1 169 ? -26.534 46.941 -40.143 1.00 23.92  ? 150  ILE D CD1 1 
ATOM   5977 N N   . SER D 1 170 ? -31.297 46.624 -43.454 1.00 29.74  ? 151  SER D N   1 
ATOM   5978 C CA  . SER D 1 170 ? -32.094 45.568 -44.085 1.00 32.26  ? 151  SER D CA  1 
ATOM   5979 C C   . SER D 1 170 ? -31.184 44.592 -44.825 1.00 35.80  ? 151  SER D C   1 
ATOM   5980 O O   . SER D 1 170 ? -30.291 45.010 -45.566 1.00 43.15  ? 151  SER D O   1 
ATOM   5981 C CB  . SER D 1 170 ? -33.141 46.145 -45.038 1.00 34.53  ? 151  SER D CB  1 
ATOM   5982 O OG  . SER D 1 170 ? -32.536 46.733 -46.165 1.00 38.03  ? 151  SER D OG  1 
ATOM   5983 N N   . VAL D 1 171 ? -31.389 43.296 -44.610 1.00 40.25  ? 152  VAL D N   1 
ATOM   5984 C CA  . VAL D 1 171 ? -30.645 42.275 -45.355 1.00 41.67  ? 152  VAL D CA  1 
ATOM   5985 C C   . VAL D 1 171 ? -31.528 41.632 -46.413 1.00 40.65  ? 152  VAL D C   1 
ATOM   5986 O O   . VAL D 1 171 ? -32.698 41.350 -46.171 1.00 48.51  ? 152  VAL D O   1 
ATOM   5987 C CB  . VAL D 1 171 ? -30.107 41.175 -44.439 1.00 39.28  ? 152  VAL D CB  1 
ATOM   5988 C CG1 . VAL D 1 171 ? -28.843 41.646 -43.739 1.00 44.17  ? 152  VAL D CG1 1 
ATOM   5989 C CG2 . VAL D 1 171 ? -31.168 40.777 -43.430 1.00 34.89  ? 152  VAL D CG2 1 
ATOM   5990 N N   . ASP D 1 172 ? -30.962 41.405 -47.587 1.00 35.71  ? 153  ASP D N   1 
ATOM   5991 C CA  . ASP D 1 172 ? -31.709 40.844 -48.699 1.00 37.65  ? 153  ASP D CA  1 
ATOM   5992 C C   . ASP D 1 172 ? -30.822 39.874 -49.455 1.00 43.02  ? 153  ASP D C   1 
ATOM   5993 O O   . ASP D 1 172 ? -29.605 40.084 -49.555 1.00 37.43  ? 153  ASP D O   1 
ATOM   5994 C CB  . ASP D 1 172 ? -32.159 41.954 -49.635 1.00 37.76  ? 153  ASP D CB  1 
ATOM   5995 C CG  . ASP D 1 172 ? -32.582 43.214 -48.882 1.00 65.92  ? 153  ASP D CG  1 
ATOM   5996 O OD1 . ASP D 1 172 ? -33.745 43.234 -48.401 1.00 75.96  ? 153  ASP D OD1 1 
ATOM   5997 O OD2 . ASP D 1 172 ? -31.756 44.170 -48.761 1.00 59.99  ? 153  ASP D OD2 1 
ATOM   5998 N N   . PRO D 1 173 ? -31.417 38.787 -49.969 1.00 45.17  ? 154  PRO D N   1 
ATOM   5999 C CA  . PRO D 1 173 ? -30.681 37.827 -50.806 1.00 42.02  ? 154  PRO D CA  1 
ATOM   6000 C C   . PRO D 1 173 ? -30.337 38.475 -52.138 1.00 46.89  ? 154  PRO D C   1 
ATOM   6001 O O   . PRO D 1 173 ? -30.983 39.443 -52.545 1.00 48.01  ? 154  PRO D O   1 
ATOM   6002 C CB  . PRO D 1 173 ? -31.687 36.698 -51.025 1.00 36.25  ? 154  PRO D CB  1 
ATOM   6003 C CG  . PRO D 1 173 ? -32.726 36.880 -49.956 1.00 41.81  ? 154  PRO D CG  1 
ATOM   6004 C CD  . PRO D 1 173 ? -32.801 38.359 -49.717 1.00 39.53  ? 154  PRO D CD  1 
ATOM   6005 N N   . THR D 1 174 ? -29.352 37.964 -52.818 1.00 51.33  ? 155  THR D N   1 
ATOM   6006 C CA  . THR D 1 174 ? -28.948 38.545 -54.068 1.00 59.40  ? 155  THR D CA  1 
ATOM   6007 C C   . THR D 1 174 ? -29.911 38.207 -55.191 1.00 63.14  ? 155  THR D C   1 
ATOM   6008 O O   . THR D 1 174 ? -30.306 37.098 -55.360 1.00 69.07  ? 155  THR D O   1 
ATOM   6009 C CB  . THR D 1 174 ? -27.488 38.149 -54.341 1.00 64.34  ? 155  THR D CB  1 
ATOM   6010 O OG1 . THR D 1 174 ? -26.639 39.103 -53.711 1.00 58.33  ? 155  THR D OG1 1 
ATOM   6011 C CG2 . THR D 1 174 ? -27.143 38.105 -55.789 1.00 75.81  ? 155  THR D CG2 1 
ATOM   6012 N N   . THR D 1 175 ? -30.257 39.197 -55.981 1.00 74.57  ? 156  THR D N   1 
ATOM   6013 C CA  . THR D 1 175 ? -31.238 39.044 -57.033 1.00 80.66  ? 156  THR D CA  1 
ATOM   6014 C C   . THR D 1 175 ? -30.788 38.029 -58.064 1.00 82.51  ? 156  THR D C   1 
ATOM   6015 O O   . THR D 1 175 ? -31.575 37.276 -58.603 1.00 82.61  ? 156  THR D O   1 
ATOM   6016 C CB  . THR D 1 175 ? -31.501 40.383 -57.721 1.00 76.39  ? 156  THR D CB  1 
ATOM   6017 O OG1 . THR D 1 175 ? -30.295 40.872 -58.297 1.00 63.89  ? 156  THR D OG1 1 
ATOM   6018 C CG2 . THR D 1 175 ? -31.979 41.363 -56.724 1.00 64.59  ? 156  THR D CG2 1 
ATOM   6019 N N   . GLU D 1 176 ? -29.501 38.015 -58.312 1.00 81.75  ? 157  GLU D N   1 
ATOM   6020 C CA  . GLU D 1 176 ? -28.912 37.289 -59.393 1.00 80.33  ? 157  GLU D CA  1 
ATOM   6021 C C   . GLU D 1 176 ? -29.056 35.834 -59.117 1.00 83.47  ? 157  GLU D C   1 
ATOM   6022 O O   . GLU D 1 176 ? -29.500 35.439 -58.063 1.00 82.99  ? 157  GLU D O   1 
ATOM   6023 C CB  . GLU D 1 176 ? -27.441 37.613 -59.452 1.00 84.43  ? 157  GLU D CB  1 
ATOM   6024 C CG  . GLU D 1 176 ? -27.160 39.079 -59.223 1.00 86.51  ? 157  GLU D CG  1 
ATOM   6025 C CD  . GLU D 1 176 ? -25.905 39.302 -58.426 1.00 96.74  ? 157  GLU D CD  1 
ATOM   6026 O OE1 . GLU D 1 176 ? -25.401 38.331 -57.835 1.00 93.19  ? 157  GLU D OE1 1 
ATOM   6027 O OE2 . GLU D 1 176 ? -25.428 40.451 -58.396 1.00 96.84  ? 157  GLU D OE2 1 
ATOM   6028 N N   . ASN D 1 177 ? -28.760 35.036 -60.122 1.00 80.51  ? 158  ASN D N   1 
ATOM   6029 C CA  . ASN D 1 177 ? -29.013 33.624 -60.094 1.00 80.68  ? 158  ASN D CA  1 
ATOM   6030 C C   . ASN D 1 177 ? -27.750 32.796 -60.197 1.00 81.51  ? 158  ASN D C   1 
ATOM   6031 O O   . ASN D 1 177 ? -27.003 32.954 -61.155 1.00 82.05  ? 158  ASN D O   1 
ATOM   6032 C CB  . ASN D 1 177 ? -29.861 33.320 -61.306 1.00 79.63  ? 158  ASN D CB  1 
ATOM   6033 C CG  . ASN D 1 177 ? -29.335 33.995 -62.563 1.00 86.43  ? 158  ASN D CG  1 
ATOM   6034 O OD1 . ASN D 1 177 ? -30.066 34.200 -63.528 1.00 81.64  ? 158  ASN D OD1 1 
ATOM   6035 N ND2 . ASN D 1 177 ? -28.063 34.369 -62.535 1.00 71.24  ? 158  ASN D ND2 1 
ATOM   6036 N N   . SER D 1 178 ? -27.547 31.893 -59.236 1.00 62.97  ? 159  SER D N   1 
ATOM   6037 C CA  . SER D 1 178 ? -26.519 30.861 -59.273 1.00 67.55  ? 159  SER D CA  1 
ATOM   6038 C C   . SER D 1 178 ? -26.240 30.291 -57.891 1.00 66.42  ? 159  SER D C   1 
ATOM   6039 O O   . SER D 1 178 ? -25.271 29.564 -57.662 1.00 60.15  ? 159  SER D O   1 
ATOM   6040 C CB  . SER D 1 178 ? -25.225 31.349 -59.918 1.00 78.26  ? 159  SER D CB  1 
ATOM   6041 O OG  . SER D 1 178 ? -25.072 32.753 -59.857 1.00 71.93  ? 159  SER D OG  1 
ATOM   6042 N N   . ASP D 1 180 ? -24.025 28.007 -55.607 1.00 64.85  ? 161  ASP D N   1 
ATOM   6043 C CA  . ASP D 1 180 ? -24.294 26.576 -55.823 1.00 70.73  ? 161  ASP D CA  1 
ATOM   6044 C C   . ASP D 1 180 ? -22.991 25.843 -56.049 1.00 57.95  ? 161  ASP D C   1 
ATOM   6045 O O   . ASP D 1 180 ? -21.944 26.245 -55.532 1.00 56.73  ? 161  ASP D O   1 
ATOM   6046 C CB  . ASP D 1 180 ? -25.252 26.334 -57.010 1.00 70.12  ? 161  ASP D CB  1 
ATOM   6047 C CG  . ASP D 1 180 ? -26.744 26.357 -56.598 1.00 74.79  ? 161  ASP D CG  1 
ATOM   6048 O OD1 . ASP D 1 180 ? -27.315 27.470 -56.430 1.00 70.60  ? 161  ASP D OD1 1 
ATOM   6049 O OD2 . ASP D 1 180 ? -27.354 25.262 -56.470 1.00 65.11  ? 161  ASP D OD2 1 
ATOM   6050 N N   . SER D 1 181 ? -23.031 24.794 -56.861 1.00 53.31  ? 162  SER D N   1 
ATOM   6051 C CA  . SER D 1 181 ? -21.827 23.990 -57.028 1.00 63.31  ? 162  SER D CA  1 
ATOM   6052 C C   . SER D 1 181 ? -20.728 24.724 -57.802 1.00 66.83  ? 162  SER D C   1 
ATOM   6053 O O   . SER D 1 181 ? -19.677 24.135 -58.083 1.00 76.74  ? 162  SER D O   1 
ATOM   6054 C CB  . SER D 1 181 ? -22.133 22.635 -57.698 1.00 65.38  ? 162  SER D CB  1 
ATOM   6055 O OG  . SER D 1 181 ? -22.802 21.741 -56.816 1.00 64.40  ? 162  SER D OG  1 
ATOM   6056 N N   . GLU D 1 182 ? -20.961 25.994 -58.136 1.00 54.68  ? 163  GLU D N   1 
ATOM   6057 C CA  . GLU D 1 182 ? -20.082 26.707 -59.057 1.00 48.18  ? 163  GLU D CA  1 
ATOM   6058 C C   . GLU D 1 182 ? -18.640 26.736 -58.577 1.00 51.84  ? 163  GLU D C   1 
ATOM   6059 O O   . GLU D 1 182 ? -17.710 26.600 -59.374 1.00 55.47  ? 163  GLU D O   1 
ATOM   6060 C CB  . GLU D 1 182 ? -20.585 28.126 -59.304 1.00 50.16  ? 163  GLU D CB  1 
ATOM   6061 C CG  . GLU D 1 182 ? -19.843 28.824 -60.441 1.00 60.13  ? 163  GLU D CG  1 
ATOM   6062 C CD  . GLU D 1 182 ? -20.261 30.279 -60.635 1.00 67.50  ? 163  GLU D CD  1 
ATOM   6063 O OE1 . GLU D 1 182 ? -21.182 30.752 -59.924 1.00 68.49  ? 163  GLU D OE1 1 
ATOM   6064 O OE2 . GLU D 1 182 ? -19.659 30.947 -61.505 1.00 67.96  ? 163  GLU D OE2 1 
ATOM   6065 N N   . TYR D 1 183 ? -18.460 26.899 -57.270 1.00 47.66  ? 164  TYR D N   1 
ATOM   6066 C CA  . TYR D 1 183 ? -17.124 26.858 -56.694 1.00 46.11  ? 164  TYR D CA  1 
ATOM   6067 C C   . TYR D 1 183 ? -16.958 25.707 -55.704 1.00 46.80  ? 164  TYR D C   1 
ATOM   6068 O O   . TYR D 1 183 ? -15.970 25.662 -54.958 1.00 39.76  ? 164  TYR D O   1 
ATOM   6069 C CB  . TYR D 1 183 ? -16.807 28.169 -55.997 1.00 40.41  ? 164  TYR D CB  1 
ATOM   6070 C CG  . TYR D 1 183 ? -17.053 29.391 -56.840 1.00 51.06  ? 164  TYR D CG  1 
ATOM   6071 C CD1 . TYR D 1 183 ? -16.319 29.621 -58.002 1.00 52.05  ? 164  TYR D CD1 1 
ATOM   6072 C CD2 . TYR D 1 183 ? -18.002 30.333 -56.460 1.00 52.72  ? 164  TYR D CD2 1 
ATOM   6073 C CE1 . TYR D 1 183 ? -16.528 30.752 -58.770 1.00 42.34  ? 164  TYR D CE1 1 
ATOM   6074 C CE2 . TYR D 1 183 ? -18.230 31.464 -57.220 1.00 53.11  ? 164  TYR D CE2 1 
ATOM   6075 C CZ  . TYR D 1 183 ? -17.490 31.671 -58.375 1.00 51.06  ? 164  TYR D CZ  1 
ATOM   6076 O OH  . TYR D 1 183 ? -17.729 32.802 -59.131 1.00 56.25  ? 164  TYR D OH  1 
ATOM   6077 N N   . PHE D 1 184 ? -17.924 24.789 -55.696 1.00 42.51  ? 165  PHE D N   1 
ATOM   6078 C CA  . PHE D 1 184 ? -17.888 23.670 -54.760 1.00 39.03  ? 165  PHE D CA  1 
ATOM   6079 C C   . PHE D 1 184 ? -16.822 22.648 -55.131 1.00 35.08  ? 165  PHE D C   1 
ATOM   6080 O O   . PHE D 1 184 ? -16.630 22.340 -56.300 1.00 39.09  ? 165  PHE D O   1 
ATOM   6081 C CB  . PHE D 1 184 ? -19.239 22.980 -54.643 1.00 36.62  ? 165  PHE D CB  1 
ATOM   6082 C CG  . PHE D 1 184 ? -19.344 22.091 -53.444 1.00 30.55  ? 165  PHE D CG  1 
ATOM   6083 C CD1 . PHE D 1 184 ? -19.367 22.633 -52.171 1.00 29.31  ? 165  PHE D CD1 1 
ATOM   6084 C CD2 . PHE D 1 184 ? -19.419 20.715 -53.586 1.00 39.73  ? 165  PHE D CD2 1 
ATOM   6085 C CE1 . PHE D 1 184 ? -19.465 21.815 -51.052 1.00 30.62  ? 165  PHE D CE1 1 
ATOM   6086 C CE2 . PHE D 1 184 ? -19.522 19.880 -52.477 1.00 36.75  ? 165  PHE D CE2 1 
ATOM   6087 C CZ  . PHE D 1 184 ? -19.541 20.433 -51.204 1.00 33.17  ? 165  PHE D CZ  1 
ATOM   6088 N N   . SER D 1 185 ? -16.136 22.129 -54.118 1.00 31.52  ? 166  SER D N   1 
ATOM   6089 C CA  . SER D 1 185 ? -15.001 21.252 -54.327 1.00 29.60  ? 166  SER D CA  1 
ATOM   6090 C C   . SER D 1 185 ? -15.441 19.882 -54.846 1.00 37.73  ? 166  SER D C   1 
ATOM   6091 O O   . SER D 1 185 ? -16.310 19.225 -54.268 1.00 36.04  ? 166  SER D O   1 
ATOM   6092 C CB  . SER D 1 185 ? -14.200 21.106 -53.031 1.00 29.64  ? 166  SER D CB  1 
ATOM   6093 O OG  . SER D 1 185 ? -13.056 20.288 -53.218 1.00 33.48  ? 166  SER D OG  1 
ATOM   6094 N N   . GLN D 1 186 ? -14.827 19.454 -55.944 1.00 39.72  ? 167  GLN D N   1 
ATOM   6095 C CA  . GLN D 1 186 ? -15.071 18.125 -56.482 1.00 34.67  ? 167  GLN D CA  1 
ATOM   6096 C C   . GLN D 1 186 ? -14.535 17.047 -55.541 1.00 39.92  ? 167  GLN D C   1 
ATOM   6097 O O   . GLN D 1 186 ? -14.938 15.883 -55.633 1.00 39.66  ? 167  GLN D O   1 
ATOM   6098 C CB  . GLN D 1 186 ? -14.430 17.987 -57.864 1.00 37.85  ? 167  GLN D CB  1 
ATOM   6099 C CG  . GLN D 1 186 ? -13.078 18.684 -57.958 1.00 50.44  ? 167  GLN D CG  1 
ATOM   6100 C CD  . GLN D 1 186 ? -12.331 18.417 -59.264 1.00 52.64  ? 167  GLN D CD  1 
ATOM   6101 O OE1 . GLN D 1 186 ? -12.451 17.343 -59.857 1.00 47.76  ? 167  GLN D OE1 1 
ATOM   6102 N NE2 . GLN D 1 186 ? -11.538 19.400 -59.704 1.00 55.73  ? 167  GLN D NE2 1 
ATOM   6103 N N   . TYR D 1 187 ? -13.637 17.428 -54.630 1.00 37.59  ? 168  TYR D N   1 
ATOM   6104 C CA  . TYR D 1 187 ? -12.987 16.439 -53.766 1.00 32.55  ? 168  TYR D CA  1 
ATOM   6105 C C   . TYR D 1 187 ? -13.661 16.242 -52.414 1.00 30.78  ? 168  TYR D C   1 
ATOM   6106 O O   . TYR D 1 187 ? -13.264 15.369 -51.640 1.00 30.87  ? 168  TYR D O   1 
ATOM   6107 C CB  . TYR D 1 187 ? -11.492 16.728 -53.609 1.00 37.66  ? 168  TYR D CB  1 
ATOM   6108 C CG  . TYR D 1 187 ? -10.781 16.844 -54.937 1.00 38.74  ? 168  TYR D CG  1 
ATOM   6109 C CD1 . TYR D 1 187 ? -10.680 15.752 -55.784 1.00 39.72  ? 168  TYR D CD1 1 
ATOM   6110 C CD2 . TYR D 1 187 ? -10.226 18.046 -55.351 1.00 36.58  ? 168  TYR D CD2 1 
ATOM   6111 C CE1 . TYR D 1 187 ? -10.045 15.846 -57.014 1.00 40.79  ? 168  TYR D CE1 1 
ATOM   6112 C CE2 . TYR D 1 187 ? -9.583  18.147 -56.575 1.00 44.75  ? 168  TYR D CE2 1 
ATOM   6113 C CZ  . TYR D 1 187 ? -9.495  17.038 -57.402 1.00 41.58  ? 168  TYR D CZ  1 
ATOM   6114 O OH  . TYR D 1 187 ? -8.859  17.119 -58.619 1.00 50.15  ? 168  TYR D OH  1 
ATOM   6115 N N   . SER D 1 188 ? -14.688 17.037 -52.134 1.00 28.05  ? 169  SER D N   1 
ATOM   6116 C CA  . SER D 1 188 ? -15.518 16.792 -50.955 1.00 26.08  ? 169  SER D CA  1 
ATOM   6117 C C   . SER D 1 188 ? -16.147 15.391 -50.982 1.00 26.61  ? 169  SER D C   1 
ATOM   6118 O O   . SER D 1 188 ? -16.368 14.828 -52.059 1.00 31.60  ? 169  SER D O   1 
ATOM   6119 C CB  . SER D 1 188 ? -16.622 17.844 -50.875 1.00 27.30  ? 169  SER D CB  1 
ATOM   6120 O OG  . SER D 1 188 ? -17.357 17.713 -49.676 1.00 28.96  ? 169  SER D OG  1 
ATOM   6121 N N   . ARG D 1 189 ? -16.436 14.833 -49.805 1.00 28.22  ? 170  ARG D N   1 
ATOM   6122 C CA  . ARG D 1 189 ? -17.207 13.586 -49.708 1.00 25.64  ? 170  ARG D CA  1 
ATOM   6123 C C   . ARG D 1 189 ? -18.694 13.802 -50.001 1.00 29.84  ? 170  ARG D C   1 
ATOM   6124 O O   . ARG D 1 189 ? -19.470 12.841 -50.019 1.00 32.77  ? 170  ARG D O   1 
ATOM   6125 C CB  . ARG D 1 189 ? -17.066 12.941 -48.326 1.00 20.55  ? 170  ARG D CB  1 
ATOM   6126 C CG  . ARG D 1 189 ? -15.652 12.537 -47.973 1.00 35.00  ? 170  ARG D CG  1 
ATOM   6127 C CD  . ARG D 1 189 ? -15.620 11.180 -47.286 1.00 48.72  ? 170  ARG D CD  1 
ATOM   6128 N NE  . ARG D 1 189 ? -16.320 11.168 -45.998 1.00 55.07  ? 170  ARG D NE  1 
ATOM   6129 C CZ  . ARG D 1 189 ? -16.819 10.076 -45.414 1.00 55.49  ? 170  ARG D CZ  1 
ATOM   6130 N NH1 . ARG D 1 189 ? -16.715 8.885  -46.003 1.00 51.78  ? 170  ARG D NH1 1 
ATOM   6131 N NH2 . ARG D 1 189 ? -17.432 10.179 -44.239 1.00 58.62  ? 170  ARG D NH2 1 
ATOM   6132 N N   . PHE D 1 190 ? -19.089 15.058 -50.206 1.00 25.34  ? 171  PHE D N   1 
ATOM   6133 C CA  . PHE D 1 190 ? -20.500 15.398 -50.351 1.00 26.10  ? 171  PHE D CA  1 
ATOM   6134 C C   . PHE D 1 190 ? -20.753 16.171 -51.635 1.00 29.59  ? 171  PHE D C   1 
ATOM   6135 O O   . PHE D 1 190 ? -19.810 16.655 -52.277 1.00 34.23  ? 171  PHE D O   1 
ATOM   6136 C CB  . PHE D 1 190 ? -20.987 16.217 -49.154 1.00 24.54  ? 171  PHE D CB  1 
ATOM   6137 C CG  . PHE D 1 190 ? -20.719 15.567 -47.825 1.00 24.52  ? 171  PHE D CG  1 
ATOM   6138 C CD1 . PHE D 1 190 ? -19.464 15.642 -47.240 1.00 26.49  ? 171  PHE D CD1 1 
ATOM   6139 C CD2 . PHE D 1 190 ? -21.719 14.880 -47.154 1.00 29.58  ? 171  PHE D CD2 1 
ATOM   6140 C CE1 . PHE D 1 190 ? -19.207 15.031 -46.012 1.00 23.64  ? 171  PHE D CE1 1 
ATOM   6141 C CE2 . PHE D 1 190 ? -21.468 14.268 -45.927 1.00 27.70  ? 171  PHE D CE2 1 
ATOM   6142 C CZ  . PHE D 1 190 ? -20.209 14.350 -45.362 1.00 23.80  ? 171  PHE D CZ  1 
ATOM   6143 N N   . GLU D 1 191 ? -22.027 16.284 -52.005 1.00 27.62  ? 172  GLU D N   1 
ATOM   6144 C CA  . GLU D 1 191 ? -22.419 17.030 -53.197 1.00 35.13  ? 172  GLU D CA  1 
ATOM   6145 C C   . GLU D 1 191 ? -23.664 17.883 -52.934 1.00 36.38  ? 172  GLU D C   1 
ATOM   6146 O O   . GLU D 1 191 ? -24.504 17.534 -52.099 1.00 36.42  ? 172  GLU D O   1 
ATOM   6147 C CB  . GLU D 1 191 ? -22.605 16.109 -54.418 1.00 32.97  ? 172  GLU D CB  1 
ATOM   6148 C CG  . GLU D 1 191 ? -23.700 15.054 -54.304 1.00 41.48  ? 172  GLU D CG  1 
ATOM   6149 C CD  . GLU D 1 191 ? -23.668 14.055 -55.479 1.00 64.56  ? 172  GLU D CD  1 
ATOM   6150 O OE1 . GLU D 1 191 ? -22.979 14.351 -56.487 1.00 65.54  ? 172  GLU D OE1 1 
ATOM   6151 O OE2 . GLU D 1 191 ? -24.317 12.976 -55.392 1.00 61.11  ? 172  GLU D OE2 1 
ATOM   6152 N N   . ILE D 1 192 ? -23.769 19.010 -53.631 1.00 35.07  ? 173  ILE D N   1 
ATOM   6153 C CA  . ILE D 1 192 ? -24.887 19.914 -53.409 1.00 38.17  ? 173  ILE D CA  1 
ATOM   6154 C C   . ILE D 1 192 ? -25.994 19.629 -54.409 1.00 41.87  ? 173  ILE D C   1 
ATOM   6155 O O   . ILE D 1 192 ? -25.745 19.554 -55.612 1.00 45.34  ? 173  ILE D O   1 
ATOM   6156 C CB  . ILE D 1 192 ? -24.455 21.392 -53.476 1.00 42.01  ? 173  ILE D CB  1 
ATOM   6157 C CG1 . ILE D 1 192 ? -23.436 21.687 -52.370 1.00 33.45  ? 173  ILE D CG1 1 
ATOM   6158 C CG2 . ILE D 1 192 ? -25.666 22.323 -53.354 1.00 38.37  ? 173  ILE D CG2 1 
ATOM   6159 C CD1 . ILE D 1 192 ? -22.883 23.089 -52.434 1.00 43.29  ? 173  ILE D CD1 1 
ATOM   6160 N N   . LEU D 1 193 ? -27.211 19.460 -53.894 1.00 46.02  ? 174  LEU D N   1 
ATOM   6161 C CA  . LEU D 1 193 ? -28.390 19.171 -54.714 1.00 46.91  ? 174  LEU D CA  1 
ATOM   6162 C C   . LEU D 1 193 ? -29.113 20.463 -55.066 1.00 48.14  ? 174  LEU D C   1 
ATOM   6163 O O   . LEU D 1 193 ? -29.558 20.649 -56.199 1.00 59.16  ? 174  LEU D O   1 
ATOM   6164 C CB  . LEU D 1 193 ? -29.339 18.202 -53.989 1.00 37.42  ? 174  LEU D CB  1 
ATOM   6165 C CG  . LEU D 1 193 ? -28.644 16.911 -53.543 1.00 42.76  ? 174  LEU D CG  1 
ATOM   6166 C CD1 . LEU D 1 193 ? -29.583 15.976 -52.796 1.00 36.08  ? 174  LEU D CD1 1 
ATOM   6167 C CD2 . LEU D 1 193 ? -27.967 16.202 -54.734 1.00 42.00  ? 174  LEU D CD2 1 
ATOM   6168 N N   . ASP D 1 194 ? -29.214 21.359 -54.091 1.00 46.45  ? 175  ASP D N   1 
ATOM   6169 C CA  . ASP D 1 194 ? -29.857 22.650 -54.306 1.00 50.34  ? 175  ASP D CA  1 
ATOM   6170 C C   . ASP D 1 194 ? -29.566 23.680 -53.194 1.00 49.58  ? 175  ASP D C   1 
ATOM   6171 O O   . ASP D 1 194 ? -29.333 23.325 -52.029 1.00 42.20  ? 175  ASP D O   1 
ATOM   6172 C CB  . ASP D 1 194 ? -31.371 22.467 -54.474 1.00 50.56  ? 175  ASP D CB  1 
ATOM   6173 C CG  . ASP D 1 194 ? -32.023 23.648 -55.184 1.00 70.83  ? 175  ASP D CG  1 
ATOM   6174 O OD1 . ASP D 1 194 ? -31.382 24.207 -56.103 1.00 76.88  ? 175  ASP D OD1 1 
ATOM   6175 O OD2 . ASP D 1 194 ? -33.164 24.026 -54.822 1.00 67.13  ? 175  ASP D OD2 1 
ATOM   6176 N N   . VAL D 1 195 ? -29.574 24.960 -53.568 1.00 52.33  ? 176  VAL D N   1 
ATOM   6177 C CA  . VAL D 1 195 ? -29.462 26.045 -52.595 1.00 48.44  ? 176  VAL D CA  1 
ATOM   6178 C C   . VAL D 1 195 ? -30.576 27.073 -52.789 1.00 41.93  ? 176  VAL D C   1 
ATOM   6179 O O   . VAL D 1 195 ? -30.676 27.674 -53.849 1.00 50.82  ? 176  VAL D O   1 
ATOM   6180 C CB  . VAL D 1 195 ? -28.105 26.773 -52.686 1.00 40.94  ? 176  VAL D CB  1 
ATOM   6181 C CG1 . VAL D 1 195 ? -28.064 27.916 -51.697 1.00 34.83  ? 176  VAL D CG1 1 
ATOM   6182 C CG2 . VAL D 1 195 ? -26.949 25.814 -52.425 1.00 43.56  ? 176  VAL D CG2 1 
ATOM   6183 N N   . THR D 1 196 ? -31.405 27.268 -51.767 1.00 33.79  ? 177  THR D N   1 
ATOM   6184 C CA  . THR D 1 196 ? -32.443 28.298 -51.800 1.00 39.48  ? 177  THR D CA  1 
ATOM   6185 C C   . THR D 1 196 ? -32.259 29.358 -50.699 1.00 43.69  ? 177  THR D C   1 
ATOM   6186 O O   . THR D 1 196 ? -31.702 29.086 -49.637 1.00 44.61  ? 177  THR D O   1 
ATOM   6187 C CB  . THR D 1 196 ? -33.858 27.696 -51.698 1.00 43.99  ? 177  THR D CB  1 
ATOM   6188 O OG1 . THR D 1 196 ? -34.011 27.023 -50.440 1.00 48.53  ? 177  THR D OG1 1 
ATOM   6189 C CG2 . THR D 1 196 ? -34.097 26.713 -52.828 1.00 46.39  ? 177  THR D CG2 1 
ATOM   6190 N N   . GLN D 1 197 ? -32.744 30.564 -50.965 1.00 47.15  ? 178  GLN D N   1 
ATOM   6191 C CA  . GLN D 1 197 ? -32.596 31.683 -50.051 1.00 37.93  ? 178  GLN D CA  1 
ATOM   6192 C C   . GLN D 1 197 ? -33.979 32.269 -49.759 1.00 41.00  ? 178  GLN D C   1 
ATOM   6193 O O   . GLN D 1 197 ? -34.810 32.381 -50.662 1.00 47.56  ? 178  GLN D O   1 
ATOM   6194 C CB  . GLN D 1 197 ? -31.695 32.750 -50.694 1.00 38.14  ? 178  GLN D CB  1 
ATOM   6195 C CG  . GLN D 1 197 ? -30.305 32.246 -51.148 1.00 53.38  ? 178  GLN D CG  1 
ATOM   6196 C CD  . GLN D 1 197 ? -29.200 33.356 -51.178 1.00 77.19  ? 178  GLN D CD  1 
ATOM   6197 O OE1 . GLN D 1 197 ? -29.480 34.529 -51.471 1.00 72.82  ? 178  GLN D OE1 1 
ATOM   6198 N NE2 . GLN D 1 197 ? -27.941 32.970 -50.866 1.00 48.91  ? 178  GLN D NE2 1 
ATOM   6199 N N   . LYS D 1 198 ? -34.254 32.634 -48.514 1.00 38.71  ? 179  LYS D N   1 
ATOM   6200 C CA  . LYS D 1 198 ? -35.435 33.469 -48.267 1.00 48.80  ? 179  LYS D CA  1 
ATOM   6201 C C   . LYS D 1 198 ? -35.213 34.485 -47.148 1.00 43.68  ? 179  LYS D C   1 
ATOM   6202 O O   . LYS D 1 198 ? -34.345 34.309 -46.299 1.00 49.22  ? 179  LYS D O   1 
ATOM   6203 C CB  . LYS D 1 198 ? -36.677 32.627 -47.994 1.00 42.47  ? 179  LYS D CB  1 
ATOM   6204 C CG  . LYS D 1 198 ? -36.883 32.320 -46.541 1.00 49.72  ? 179  LYS D CG  1 
ATOM   6205 C CD  . LYS D 1 198 ? -38.210 31.598 -46.321 1.00 66.21  ? 179  LYS D CD  1 
ATOM   6206 C CE  . LYS D 1 198 ? -38.307 31.064 -44.890 1.00 79.23  ? 179  LYS D CE  1 
ATOM   6207 N NZ  . LYS D 1 198 ? -39.620 30.408 -44.625 1.00 83.53  ? 179  LYS D NZ  1 
ATOM   6208 N N   . LYS D 1 199 ? -35.999 35.550 -47.147 1.00 43.17  ? 180  LYS D N   1 
ATOM   6209 C CA  . LYS D 1 199 ? -35.829 36.608 -46.160 1.00 38.42  ? 180  LYS D CA  1 
ATOM   6210 C C   . LYS D 1 199 ? -36.889 36.545 -45.040 1.00 42.40  ? 180  LYS D C   1 
ATOM   6211 O O   . LYS D 1 199 ? -38.077 36.355 -45.306 1.00 36.54  ? 180  LYS D O   1 
ATOM   6212 C CB  . LYS D 1 199 ? -35.856 37.960 -46.859 1.00 28.06  ? 180  LYS D CB  1 
ATOM   6213 C CG  . LYS D 1 199 ? -36.045 39.104 -45.922 1.00 48.59  ? 180  LYS D CG  1 
ATOM   6214 C CD  . LYS D 1 199 ? -36.080 40.406 -46.675 1.00 55.78  ? 180  LYS D CD  1 
ATOM   6215 C CE  . LYS D 1 199 ? -36.381 41.553 -45.718 1.00 61.20  ? 180  LYS D CE  1 
ATOM   6216 N NZ  . LYS D 1 199 ? -36.246 42.888 -46.388 1.00 70.52  ? 180  LYS D NZ  1 
ATOM   6217 N N   . ASN D 1 200 ? -36.453 36.688 -43.787 1.00 45.15  ? 181  ASN D N   1 
ATOM   6218 C CA  . ASN D 1 200 ? -37.374 36.733 -42.648 1.00 37.65  ? 181  ASN D CA  1 
ATOM   6219 C C   . ASN D 1 200 ? -37.292 38.060 -41.895 1.00 39.99  ? 181  ASN D C   1 
ATOM   6220 O O   . ASN D 1 200 ? -36.266 38.750 -41.905 1.00 35.63  ? 181  ASN D O   1 
ATOM   6221 C CB  . ASN D 1 200 ? -37.117 35.593 -41.661 1.00 38.24  ? 181  ASN D CB  1 
ATOM   6222 C CG  . ASN D 1 200 ? -37.040 34.249 -42.332 1.00 52.93  ? 181  ASN D CG  1 
ATOM   6223 O OD1 . ASN D 1 200 ? -38.062 33.697 -42.733 1.00 58.44  ? 181  ASN D OD1 1 
ATOM   6224 N ND2 . ASN D 1 200 ? -35.821 33.700 -42.453 1.00 56.25  ? 181  ASN D ND2 1 
ATOM   6225 N N   . SER D 1 201 ? -38.392 38.401 -41.237 1.00 46.07  ? 182  SER D N   1 
ATOM   6226 C CA  . SER D 1 201 ? -38.462 39.580 -40.395 1.00 35.96  ? 182  SER D CA  1 
ATOM   6227 C C   . SER D 1 201 ? -39.039 39.142 -39.053 1.00 31.29  ? 182  SER D C   1 
ATOM   6228 O O   . SER D 1 201 ? -40.199 38.770 -38.979 1.00 34.89  ? 182  SER D O   1 
ATOM   6229 C CB  . SER D 1 201 ? -39.348 40.631 -41.056 1.00 35.54  ? 182  SER D CB  1 
ATOM   6230 O OG  . SER D 1 201 ? -39.193 41.890 -40.423 1.00 54.46  ? 182  SER D OG  1 
ATOM   6231 N N   . VAL D 1 202 ? -38.220 39.175 -38.005 1.00 36.02  ? 183  VAL D N   1 
ATOM   6232 C CA  . VAL D 1 202 ? -38.542 38.543 -36.718 1.00 30.79  ? 183  VAL D CA  1 
ATOM   6233 C C   . VAL D 1 202 ? -38.616 39.563 -35.594 1.00 32.91  ? 183  VAL D C   1 
ATOM   6234 O O   . VAL D 1 202 ? -37.798 40.497 -35.535 1.00 37.36  ? 183  VAL D O   1 
ATOM   6235 C CB  . VAL D 1 202 ? -37.443 37.524 -36.346 1.00 31.57  ? 183  VAL D CB  1 
ATOM   6236 C CG1 . VAL D 1 202 ? -37.703 36.919 -34.984 1.00 31.27  ? 183  VAL D CG1 1 
ATOM   6237 C CG2 . VAL D 1 202 ? -37.308 36.460 -37.429 1.00 29.12  ? 183  VAL D CG2 1 
ATOM   6238 N N   . THR D 1 203 ? -39.590 39.398 -34.701 1.00 32.58  ? 184  THR D N   1 
ATOM   6239 C CA  . THR D 1 203 ? -39.643 40.240 -33.506 1.00 34.64  ? 184  THR D CA  1 
ATOM   6240 C C   . THR D 1 203 ? -39.238 39.442 -32.278 1.00 33.43  ? 184  THR D C   1 
ATOM   6241 O O   . THR D 1 203 ? -39.848 38.438 -31.969 1.00 38.33  ? 184  THR D O   1 
ATOM   6242 C CB  . THR D 1 203 ? -41.025 40.900 -33.298 1.00 36.98  ? 184  THR D CB  1 
ATOM   6243 O OG1 . THR D 1 203 ? -41.240 41.888 -34.320 1.00 48.46  ? 184  THR D OG1 1 
ATOM   6244 C CG2 . THR D 1 203 ? -41.082 41.592 -31.947 1.00 46.62  ? 184  THR D CG2 1 
ATOM   6245 N N   . TYR D 1 204 ? -38.196 39.891 -31.583 1.00 45.54  ? 185  TYR D N   1 
ATOM   6246 C CA  . TYR D 1 204 ? -37.720 39.208 -30.379 1.00 42.76  ? 185  TYR D CA  1 
ATOM   6247 C C   . TYR D 1 204 ? -38.357 39.748 -29.097 1.00 42.29  ? 185  TYR D C   1 
ATOM   6248 O O   . TYR D 1 204 ? -38.900 40.858 -29.070 1.00 40.42  ? 185  TYR D O   1 
ATOM   6249 C CB  . TYR D 1 204 ? -36.190 39.273 -30.291 1.00 36.77  ? 185  TYR D CB  1 
ATOM   6250 C CG  . TYR D 1 204 ? -35.502 38.564 -31.441 1.00 37.14  ? 185  TYR D CG  1 
ATOM   6251 C CD1 . TYR D 1 204 ? -35.220 39.237 -32.624 1.00 35.21  ? 185  TYR D CD1 1 
ATOM   6252 C CD2 . TYR D 1 204 ? -35.146 37.219 -31.350 1.00 36.38  ? 185  TYR D CD2 1 
ATOM   6253 C CE1 . TYR D 1 204 ? -34.603 38.598 -33.688 1.00 29.58  ? 185  TYR D CE1 1 
ATOM   6254 C CE2 . TYR D 1 204 ? -34.517 36.566 -32.408 1.00 30.06  ? 185  TYR D CE2 1 
ATOM   6255 C CZ  . TYR D 1 204 ? -34.253 37.265 -33.581 1.00 30.51  ? 185  TYR D CZ  1 
ATOM   6256 O OH  . TYR D 1 204 ? -33.644 36.646 -34.658 1.00 33.03  ? 185  TYR D OH  1 
ATOM   6257 N N   . SER D 1 205 ? -38.271 38.949 -28.036 1.00 47.10  ? 186  SER D N   1 
ATOM   6258 C CA  . SER D 1 205 ? -38.937 39.249 -26.772 1.00 49.88  ? 186  SER D CA  1 
ATOM   6259 C C   . SER D 1 205 ? -38.383 40.481 -26.087 1.00 48.18  ? 186  SER D C   1 
ATOM   6260 O O   . SER D 1 205 ? -39.023 41.060 -25.215 1.00 57.99  ? 186  SER D O   1 
ATOM   6261 C CB  . SER D 1 205 ? -38.867 38.045 -25.832 1.00 55.77  ? 186  SER D CB  1 
ATOM   6262 O OG  . SER D 1 205 ? -39.599 36.956 -26.365 1.00 65.53  ? 186  SER D OG  1 
ATOM   6263 N N   . CYS D 1 206 ? -37.193 40.891 -26.492 1.00 54.98  ? 187  CYS D N   1 
ATOM   6264 C CA  . CYS D 1 206 ? -36.534 42.025 -25.863 1.00 55.93  ? 187  CYS D CA  1 
ATOM   6265 C C   . CYS D 1 206 ? -37.053 43.403 -26.327 1.00 61.47  ? 187  CYS D C   1 
ATOM   6266 O O   . CYS D 1 206 ? -37.217 44.299 -25.508 1.00 70.80  ? 187  CYS D O   1 
ATOM   6267 C CB  . CYS D 1 206 ? -35.026 41.932 -26.090 1.00 55.92  ? 187  CYS D CB  1 
ATOM   6268 S SG  . CYS D 1 206 ? -34.488 42.541 -27.724 1.00 59.13  ? 187  CYS D SG  1 
ATOM   6269 N N   . CYS D 1 207 ? -37.317 43.567 -27.627 1.00 64.68  ? 188  CYS D N   1 
ATOM   6270 C CA  . CYS D 1 207 ? -37.592 44.888 -28.227 1.00 61.36  ? 188  CYS D CA  1 
ATOM   6271 C C   . CYS D 1 207 ? -38.814 44.870 -29.158 1.00 67.63  ? 188  CYS D C   1 
ATOM   6272 O O   . CYS D 1 207 ? -39.185 43.810 -29.686 1.00 67.34  ? 188  CYS D O   1 
ATOM   6273 C CB  . CYS D 1 207 ? -36.355 45.360 -29.001 1.00 62.85  ? 188  CYS D CB  1 
ATOM   6274 S SG  . CYS D 1 207 ? -34.888 44.304 -28.691 1.00 90.74  ? 188  CYS D SG  1 
ATOM   6275 N N   . PRO D 1 208 ? -39.444 46.045 -29.367 1.00 67.17  ? 189  PRO D N   1 
ATOM   6276 C CA  . PRO D 1 208 ? -40.652 46.161 -30.206 1.00 66.56  ? 189  PRO D CA  1 
ATOM   6277 C C   . PRO D 1 208 ? -40.336 46.296 -31.687 1.00 68.84  ? 189  PRO D C   1 
ATOM   6278 O O   . PRO D 1 208 ? -41.251 46.367 -32.512 1.00 77.48  ? 189  PRO D O   1 
ATOM   6279 C CB  . PRO D 1 208 ? -41.282 47.467 -29.721 1.00 65.40  ? 189  PRO D CB  1 
ATOM   6280 C CG  . PRO D 1 208 ? -40.096 48.288 -29.314 1.00 63.02  ? 189  PRO D CG  1 
ATOM   6281 C CD  . PRO D 1 208 ? -39.109 47.321 -28.705 1.00 53.82  ? 189  PRO D CD  1 
ATOM   6282 N N   . GLU D 1 209 ? -39.048 46.350 -32.008 1.00 71.48  ? 190  GLU D N   1 
ATOM   6283 C CA  . GLU D 1 209 ? -38.579 46.519 -33.383 1.00 61.73  ? 190  GLU D CA  1 
ATOM   6284 C C   . GLU D 1 209 ? -38.351 45.158 -34.061 1.00 49.50  ? 190  GLU D C   1 
ATOM   6285 O O   . GLU D 1 209 ? -38.154 44.145 -33.382 1.00 45.82  ? 190  GLU D O   1 
ATOM   6286 C CB  . GLU D 1 209 ? -37.270 47.310 -33.361 1.00 62.82  ? 190  GLU D CB  1 
ATOM   6287 C CG  . GLU D 1 209 ? -37.273 48.506 -32.409 1.00 59.74  ? 190  GLU D CG  1 
ATOM   6288 C CD  . GLU D 1 209 ? -37.983 49.717 -33.008 1.00 77.57  ? 190  GLU D CD  1 
ATOM   6289 O OE1 . GLU D 1 209 ? -38.536 49.589 -34.127 1.00 83.95  ? 190  GLU D OE1 1 
ATOM   6290 O OE2 . GLU D 1 209 ? -37.984 50.799 -32.375 1.00 73.24  ? 190  GLU D OE2 1 
ATOM   6291 N N   . ALA D 1 210 ? -38.375 45.131 -35.394 1.00 46.87  ? 191  ALA D N   1 
ATOM   6292 C CA  . ALA D 1 210 ? -38.166 43.881 -36.126 1.00 40.28  ? 191  ALA D CA  1 
ATOM   6293 C C   . ALA D 1 210 ? -36.725 43.798 -36.570 1.00 37.94  ? 191  ALA D C   1 
ATOM   6294 O O   . ALA D 1 210 ? -36.112 44.816 -36.898 1.00 31.81  ? 191  ALA D O   1 
ATOM   6295 C CB  . ALA D 1 210 ? -39.069 43.784 -37.327 1.00 37.27  ? 191  ALA D CB  1 
ATOM   6296 N N   . TYR D 1 211 ? -36.190 42.579 -36.593 1.00 36.43  ? 192  TYR D N   1 
ATOM   6297 C CA  . TYR D 1 211 ? -34.827 42.348 -37.065 1.00 31.55  ? 192  TYR D CA  1 
ATOM   6298 C C   . TYR D 1 211 ? -34.851 41.463 -38.289 1.00 31.60  ? 192  TYR D C   1 
ATOM   6299 O O   . TYR D 1 211 ? -35.348 40.336 -38.224 1.00 37.11  ? 192  TYR D O   1 
ATOM   6300 C CB  . TYR D 1 211 ? -33.979 41.709 -35.958 1.00 30.46  ? 192  TYR D CB  1 
ATOM   6301 C CG  . TYR D 1 211 ? -33.667 42.666 -34.838 1.00 31.01  ? 192  TYR D CG  1 
ATOM   6302 C CD1 . TYR D 1 211 ? -34.614 42.963 -33.875 1.00 37.54  ? 192  TYR D CD1 1 
ATOM   6303 C CD2 . TYR D 1 211 ? -32.432 43.298 -34.761 1.00 31.43  ? 192  TYR D CD2 1 
ATOM   6304 C CE1 . TYR D 1 211 ? -34.342 43.864 -32.853 1.00 40.56  ? 192  TYR D CE1 1 
ATOM   6305 C CE2 . TYR D 1 211 ? -32.143 44.197 -33.743 1.00 32.69  ? 192  TYR D CE2 1 
ATOM   6306 C CZ  . TYR D 1 211 ? -33.102 44.480 -32.791 1.00 38.10  ? 192  TYR D CZ  1 
ATOM   6307 O OH  . TYR D 1 211 ? -32.815 45.377 -31.773 1.00 44.52  ? 192  TYR D OH  1 
ATOM   6308 N N   . GLU D 1 212 ? -34.321 41.961 -39.405 1.00 31.56  ? 193  GLU D N   1 
ATOM   6309 C CA  . GLU D 1 212 ? -34.250 41.149 -40.632 1.00 32.19  ? 193  GLU D CA  1 
ATOM   6310 C C   . GLU D 1 212 ? -33.108 40.136 -40.629 1.00 25.55  ? 193  GLU D C   1 
ATOM   6311 O O   . GLU D 1 212 ? -32.030 40.396 -40.087 1.00 26.36  ? 193  GLU D O   1 
ATOM   6312 C CB  . GLU D 1 212 ? -34.152 42.044 -41.868 1.00 30.36  ? 193  GLU D CB  1 
ATOM   6313 C CG  . GLU D 1 212 ? -35.279 43.053 -41.972 1.00 37.28  ? 193  GLU D CG  1 
ATOM   6314 C CD  . GLU D 1 212 ? -35.301 43.776 -43.303 1.00 48.26  ? 193  GLU D CD  1 
ATOM   6315 O OE1 . GLU D 1 212 ? -34.416 43.488 -44.147 1.00 48.38  ? 193  GLU D OE1 1 
ATOM   6316 O OE2 . GLU D 1 212 ? -36.210 44.626 -43.504 1.00 57.97  ? 193  GLU D OE2 1 
ATOM   6317 N N   . ASP D 1 213 ? -33.363 38.983 -41.236 1.00 27.80  ? 194  ASP D N   1 
ATOM   6318 C CA  . ASP D 1 213 ? -32.310 38.003 -41.530 1.00 30.98  ? 194  ASP D CA  1 
ATOM   6319 C C   . ASP D 1 213 ? -32.555 37.285 -42.846 1.00 28.61  ? 194  ASP D C   1 
ATOM   6320 O O   . ASP D 1 213 ? -33.646 37.337 -43.409 1.00 29.93  ? 194  ASP D O   1 
ATOM   6321 C CB  . ASP D 1 213 ? -32.177 36.962 -40.421 1.00 32.11  ? 194  ASP D CB  1 
ATOM   6322 C CG  . ASP D 1 213 ? -33.499 36.268 -40.113 1.00 48.15  ? 194  ASP D CG  1 
ATOM   6323 O OD1 . ASP D 1 213 ? -33.830 35.276 -40.811 1.00 47.33  ? 194  ASP D OD1 1 
ATOM   6324 O OD2 . ASP D 1 213 ? -34.207 36.722 -39.170 1.00 59.31  ? 194  ASP D OD2 1 
ATOM   6325 N N   . VAL D 1 214 ? -31.519 36.621 -43.331 1.00 24.83  ? 195  VAL D N   1 
ATOM   6326 C CA  . VAL D 1 214 ? -31.649 35.761 -44.488 1.00 23.49  ? 195  VAL D CA  1 
ATOM   6327 C C   . VAL D 1 214 ? -31.444 34.326 -44.034 1.00 27.41  ? 195  VAL D C   1 
ATOM   6328 O O   . VAL D 1 214 ? -30.572 34.031 -43.206 1.00 25.61  ? 195  VAL D O   1 
ATOM   6329 C CB  . VAL D 1 214 ? -30.662 36.146 -45.591 1.00 21.93  ? 195  VAL D CB  1 
ATOM   6330 C CG1 . VAL D 1 214 ? -30.677 35.127 -46.710 1.00 21.86  ? 195  VAL D CG1 1 
ATOM   6331 C CG2 . VAL D 1 214 ? -31.001 37.530 -46.121 1.00 36.13  ? 195  VAL D CG2 1 
ATOM   6332 N N   . GLU D 1 215 ? -32.298 33.445 -44.545 1.00 34.80  ? 196  GLU D N   1 
ATOM   6333 C CA  . GLU D 1 215 ? -32.219 32.015 -44.274 1.00 33.60  ? 196  GLU D CA  1 
ATOM   6334 C C   . GLU D 1 215 ? -31.777 31.290 -45.542 1.00 32.72  ? 196  GLU D C   1 
ATOM   6335 O O   . GLU D 1 215 ? -32.446 31.379 -46.580 1.00 34.81  ? 196  GLU D O   1 
ATOM   6336 C CB  . GLU D 1 215 ? -33.582 31.508 -43.837 1.00 31.70  ? 196  GLU D CB  1 
ATOM   6337 C CG  . GLU D 1 215 ? -33.560 30.688 -42.570 1.00 48.72  ? 196  GLU D CG  1 
ATOM   6338 C CD  . GLU D 1 215 ? -34.952 30.210 -42.141 1.00 77.66  ? 196  GLU D CD  1 
ATOM   6339 O OE1 . GLU D 1 215 ? -35.717 29.694 -43.003 1.00 78.86  ? 196  GLU D OE1 1 
ATOM   6340 O OE2 . GLU D 1 215 ? -35.275 30.362 -40.935 1.00 74.84  ? 196  GLU D OE2 1 
ATOM   6341 N N   . VAL D 1 216 ? -30.647 30.588 -45.472 1.00 31.19  ? 197  VAL D N   1 
ATOM   6342 C CA  . VAL D 1 216 ? -30.099 29.913 -46.652 1.00 30.21  ? 197  VAL D CA  1 
ATOM   6343 C C   . VAL D 1 216 ? -30.243 28.417 -46.485 1.00 30.90  ? 197  VAL D C   1 
ATOM   6344 O O   . VAL D 1 216 ? -29.656 27.844 -45.576 1.00 42.09  ? 197  VAL D O   1 
ATOM   6345 C CB  . VAL D 1 216 ? -28.606 30.268 -46.899 1.00 28.09  ? 197  VAL D CB  1 
ATOM   6346 C CG1 . VAL D 1 216 ? -28.061 29.458 -48.056 1.00 31.33  ? 197  VAL D CG1 1 
ATOM   6347 C CG2 . VAL D 1 216 ? -28.442 31.753 -47.185 1.00 29.77  ? 197  VAL D CG2 1 
ATOM   6348 N N   . SER D 1 217 ? -31.027 27.786 -47.353 1.00 31.66  ? 198  SER D N   1 
ATOM   6349 C CA  . SER D 1 217 ? -31.266 26.345 -47.256 1.00 36.46  ? 198  SER D CA  1 
ATOM   6350 C C   . SER D 1 217 ? -30.349 25.539 -48.166 1.00 36.32  ? 198  SER D C   1 
ATOM   6351 O O   . SER D 1 217 ? -30.375 25.689 -49.386 1.00 34.17  ? 198  SER D O   1 
ATOM   6352 C CB  . SER D 1 217 ? -32.717 26.025 -47.584 1.00 42.41  ? 198  SER D CB  1 
ATOM   6353 O OG  . SER D 1 217 ? -33.578 26.776 -46.754 1.00 46.84  ? 198  SER D OG  1 
ATOM   6354 N N   . LEU D 1 218 ? -29.547 24.674 -47.558 1.00 35.11  ? 199  LEU D N   1 
ATOM   6355 C CA  . LEU D 1 218 ? -28.549 23.920 -48.294 1.00 34.13  ? 199  LEU D CA  1 
ATOM   6356 C C   . LEU D 1 218 ? -28.932 22.453 -48.347 1.00 41.68  ? 199  LEU D C   1 
ATOM   6357 O O   . LEU D 1 218 ? -28.870 21.750 -47.337 1.00 38.88  ? 199  LEU D O   1 
ATOM   6358 C CB  . LEU D 1 218 ? -27.185 24.069 -47.633 1.00 38.50  ? 199  LEU D CB  1 
ATOM   6359 C CG  . LEU D 1 218 ? -26.110 23.118 -48.158 1.00 37.71  ? 199  LEU D CG  1 
ATOM   6360 C CD1 . LEU D 1 218 ? -25.838 23.401 -49.626 1.00 47.88  ? 199  LEU D CD1 1 
ATOM   6361 C CD2 . LEU D 1 218 ? -24.829 23.236 -47.344 1.00 37.36  ? 199  LEU D CD2 1 
ATOM   6362 N N   . ASN D 1 219 ? -29.331 21.993 -49.529 1.00 43.81  ? 200  ASN D N   1 
ATOM   6363 C CA  . ASN D 1 219 ? -29.705 20.599 -49.708 1.00 36.59  ? 200  ASN D CA  1 
ATOM   6364 C C   . ASN D 1 219 ? -28.511 19.815 -50.271 1.00 39.50  ? 200  ASN D C   1 
ATOM   6365 O O   . ASN D 1 219 ? -28.016 20.115 -51.365 1.00 38.89  ? 200  ASN D O   1 
ATOM   6366 C CB  . ASN D 1 219 ? -30.955 20.500 -50.599 1.00 43.43  ? 200  ASN D CB  1 
ATOM   6367 C CG  . ASN D 1 219 ? -31.470 19.071 -50.743 1.00 49.36  ? 200  ASN D CG  1 
ATOM   6368 O OD1 . ASN D 1 219 ? -31.842 18.636 -51.842 1.00 51.70  ? 200  ASN D OD1 1 
ATOM   6369 N ND2 . ASN D 1 219 ? -31.474 18.328 -49.639 1.00 44.81  ? 200  ASN D ND2 1 
ATOM   6370 N N   . PHE D 1 220 ? -28.035 18.828 -49.510 1.00 36.02  ? 201  PHE D N   1 
ATOM   6371 C CA  . PHE D 1 220 ? -26.814 18.101 -49.866 1.00 30.20  ? 201  PHE D CA  1 
ATOM   6372 C C   . PHE D 1 220 ? -26.883 16.666 -49.386 1.00 34.16  ? 201  PHE D C   1 
ATOM   6373 O O   . PHE D 1 220 ? -27.661 16.354 -48.476 1.00 32.69  ? 201  PHE D O   1 
ATOM   6374 C CB  . PHE D 1 220 ? -25.589 18.776 -49.233 1.00 31.69  ? 201  PHE D CB  1 
ATOM   6375 C CG  . PHE D 1 220 ? -25.483 18.576 -47.750 1.00 23.74  ? 201  PHE D CG  1 
ATOM   6376 C CD1 . PHE D 1 220 ? -26.370 19.205 -46.889 1.00 32.78  ? 201  PHE D CD1 1 
ATOM   6377 C CD2 . PHE D 1 220 ? -24.501 17.757 -47.215 1.00 26.00  ? 201  PHE D CD2 1 
ATOM   6378 C CE1 . PHE D 1 220 ? -26.292 19.020 -45.508 1.00 28.87  ? 201  PHE D CE1 1 
ATOM   6379 C CE2 . PHE D 1 220 ? -24.406 17.558 -45.830 1.00 30.36  ? 201  PHE D CE2 1 
ATOM   6380 C CZ  . PHE D 1 220 ? -25.305 18.191 -44.978 1.00 29.86  ? 201  PHE D CZ  1 
ATOM   6381 N N   . ARG D 1 221 ? -26.063 15.795 -49.985 1.00 39.69  ? 202  ARG D N   1 
ATOM   6382 C CA  . ARG D 1 221 ? -25.955 14.393 -49.545 1.00 34.77  ? 202  ARG D CA  1 
ATOM   6383 C C   . ARG D 1 221 ? -24.564 13.837 -49.730 1.00 27.99  ? 202  ARG D C   1 
ATOM   6384 O O   . ARG D 1 221 ? -23.731 14.438 -50.405 1.00 30.32  ? 202  ARG D O   1 
ATOM   6385 C CB  . ARG D 1 221 ? -26.936 13.497 -50.300 1.00 36.57  ? 202  ARG D CB  1 
ATOM   6386 C CG  . ARG D 1 221 ? -26.701 13.481 -51.794 1.00 38.84  ? 202  ARG D CG  1 
ATOM   6387 C CD  . ARG D 1 221 ? -27.009 12.120 -52.426 1.00 43.46  ? 202  ARG D CD  1 
ATOM   6388 N NE  . ARG D 1 221 ? -26.764 12.171 -53.865 1.00 49.74  ? 202  ARG D NE  1 
ATOM   6389 C CZ  . ARG D 1 221 ? -27.718 12.299 -54.787 1.00 64.49  ? 202  ARG D CZ  1 
ATOM   6390 N NH1 . ARG D 1 221 ? -28.991 12.338 -54.406 1.00 70.06  ? 202  ARG D NH1 1 
ATOM   6391 N NH2 . ARG D 1 221 ? -27.405 12.371 -56.088 1.00 52.53  ? 202  ARG D NH2 1 
ATOM   6392 N N   . LYS D 1 222 ? -24.326 12.672 -49.132 1.00 33.93  ? 203  LYS D N   1 
ATOM   6393 C CA  . LYS D 1 222 ? -23.072 11.937 -49.317 1.00 32.92  ? 203  LYS D CA  1 
ATOM   6394 C C   . LYS D 1 222 ? -23.004 11.284 -50.704 1.00 34.80  ? 203  LYS D C   1 
ATOM   6395 O O   . LYS D 1 222 ? -24.001 10.764 -51.210 1.00 41.18  ? 203  LYS D O   1 
ATOM   6396 C CB  . LYS D 1 222 ? -22.939 10.874 -48.242 1.00 29.30  ? 203  LYS D CB  1 
ATOM   6397 C CG  . LYS D 1 222 ? -21.595 10.172 -48.247 1.00 37.99  ? 203  LYS D CG  1 
ATOM   6398 C CD  . LYS D 1 222 ? -21.523 9.190  -47.083 1.00 56.40  ? 203  LYS D CD  1 
ATOM   6399 C CE  . LYS D 1 222 ? -20.210 8.432  -47.036 1.00 56.22  ? 203  LYS D CE  1 
ATOM   6400 N NZ  . LYS D 1 222 ? -20.231 7.445  -45.912 1.00 81.08  ? 203  LYS D NZ  1 
ATOM   6401 N N   . LYS D 1 223 ? -21.834 11.324 -51.325 1.00 31.46  ? 204  LYS D N   1 
ATOM   6402 C CA  . LYS D 1 223 ? -21.653 10.746 -52.657 1.00 37.79  ? 204  LYS D CA  1 
ATOM   6403 C C   . LYS D 1 223 ? -21.649 9.210  -52.601 1.00 42.62  ? 204  LYS D C   1 
ATOM   6404 O O   . LYS D 1 223 ? -21.301 8.620  -51.577 1.00 40.56  ? 204  LYS D O   1 
ATOM   6405 C CB  . LYS D 1 223 ? -20.325 11.216 -53.260 1.00 34.95  ? 204  LYS D CB  1 
ATOM   6406 C CG  . LYS D 1 223 ? -20.260 12.657 -53.712 1.00 30.21  ? 204  LYS D CG  1 
ATOM   6407 C CD  . LYS D 1 223 ? -18.805 13.005 -53.997 1.00 33.21  ? 204  LYS D CD  1 
ATOM   6408 C CE  . LYS D 1 223 ? -18.634 14.149 -54.980 1.00 37.94  ? 204  LYS D CE  1 
ATOM   6409 N NZ  . LYS D 1 223 ? -17.203 14.248 -55.441 1.00 32.23  ? 204  LYS D NZ  1 
ATOM   6410 N N   . GLY D 1 224 ? -22.009 8.560  -53.703 1.00 39.58  ? 205  GLY D N   1 
ATOM   6411 C CA  . GLY D 1 224 ? -22.005 7.107  -53.744 1.00 51.84  ? 205  GLY D CA  1 
ATOM   6412 C C   . GLY D 1 224 ? -20.669 6.536  -54.197 1.00 62.60  ? 205  GLY D C   1 
ATOM   6413 O O   . GLY D 1 224 ? -20.601 5.624  -55.028 1.00 63.23  ? 205  GLY D O   1 
ATOM   6414 N N   . LEU E 1 20  ? -28.087 66.936 -33.293 1.00 48.74  ? 1    LEU E N   1 
ATOM   6415 C CA  . LEU E 1 20  ? -27.180 65.806 -33.156 1.00 34.78  ? 1    LEU E CA  1 
ATOM   6416 C C   . LEU E 1 20  ? -27.549 64.705 -34.123 1.00 38.08  ? 1    LEU E C   1 
ATOM   6417 O O   . LEU E 1 20  ? -28.703 64.296 -34.190 1.00 45.36  ? 1    LEU E O   1 
ATOM   6418 C CB  . LEU E 1 20  ? -27.253 65.235 -31.747 1.00 39.01  ? 1    LEU E CB  1 
ATOM   6419 C CG  . LEU E 1 20  ? -26.531 65.992 -30.643 1.00 45.96  ? 1    LEU E CG  1 
ATOM   6420 C CD1 . LEU E 1 20  ? -26.534 65.148 -29.370 1.00 43.92  ? 1    LEU E CD1 1 
ATOM   6421 C CD2 . LEU E 1 20  ? -25.108 66.336 -31.075 1.00 42.97  ? 1    LEU E CD2 1 
ATOM   6422 N N   . ASP E 1 21  ? -26.568 64.216 -34.868 1.00 42.40  ? 2    ASP E N   1 
ATOM   6423 C CA  . ASP E 1 21  ? -26.753 62.994 -35.651 1.00 43.43  ? 2    ASP E CA  1 
ATOM   6424 C C   . ASP E 1 21  ? -25.934 61.855 -35.039 1.00 37.19  ? 2    ASP E C   1 
ATOM   6425 O O   . ASP E 1 21  ? -25.223 62.065 -34.045 1.00 36.61  ? 2    ASP E O   1 
ATOM   6426 C CB  . ASP E 1 21  ? -26.373 63.221 -37.120 1.00 50.42  ? 2    ASP E CB  1 
ATOM   6427 C CG  . ASP E 1 21  ? -25.072 64.022 -37.288 1.00 56.81  ? 2    ASP E CG  1 
ATOM   6428 O OD1 . ASP E 1 21  ? -24.113 63.788 -36.519 1.00 54.57  ? 2    ASP E OD1 1 
ATOM   6429 O OD2 . ASP E 1 21  ? -25.009 64.884 -38.202 1.00 65.24  ? 2    ASP E OD2 1 
ATOM   6430 N N   . ARG E 1 22  ? -26.025 60.663 -35.622 1.00 34.00  ? 3    ARG E N   1 
ATOM   6431 C CA  . ARG E 1 22  ? -25.274 59.522 -35.099 1.00 30.67  ? 3    ARG E CA  1 
ATOM   6432 C C   . ARG E 1 22  ? -23.776 59.765 -35.050 1.00 27.66  ? 3    ARG E C   1 
ATOM   6433 O O   . ARG E 1 22  ? -23.111 59.370 -34.083 1.00 24.09  ? 3    ARG E O   1 
ATOM   6434 C CB  . ARG E 1 22  ? -25.550 58.259 -35.903 1.00 28.74  ? 3    ARG E CB  1 
ATOM   6435 C CG  . ARG E 1 22  ? -26.856 57.609 -35.584 1.00 33.53  ? 3    ARG E CG  1 
ATOM   6436 C CD  . ARG E 1 22  ? -27.037 56.348 -36.386 1.00 42.10  ? 3    ARG E CD  1 
ATOM   6437 N NE  . ARG E 1 22  ? -28.287 55.689 -36.030 1.00 55.89  ? 3    ARG E NE  1 
ATOM   6438 C CZ  . ARG E 1 22  ? -29.464 56.018 -36.543 1.00 54.31  ? 3    ARG E CZ  1 
ATOM   6439 N NH1 . ARG E 1 22  ? -29.539 57.006 -37.440 1.00 43.66  ? 3    ARG E NH1 1 
ATOM   6440 N NH2 . ARG E 1 22  ? -30.552 55.357 -36.153 1.00 50.67  ? 3    ARG E NH2 1 
ATOM   6441 N N   . ALA E 1 23  ? -23.254 60.411 -36.091 1.00 26.40  ? 4    ALA E N   1 
ATOM   6442 C CA  . ALA E 1 23  ? -21.825 60.689 -36.168 1.00 25.04  ? 4    ALA E CA  1 
ATOM   6443 C C   . ALA E 1 23  ? -21.357 61.514 -34.966 1.00 29.03  ? 4    ALA E C   1 
ATOM   6444 O O   . ALA E 1 23  ? -20.328 61.218 -34.352 1.00 30.06  ? 4    ALA E O   1 
ATOM   6445 C CB  . ALA E 1 23  ? -21.506 61.400 -37.447 1.00 27.77  ? 4    ALA E CB  1 
ATOM   6446 N N   . ASP E 1 24  ? -22.135 62.538 -34.629 1.00 28.68  ? 5    ASP E N   1 
ATOM   6447 C CA  . ASP E 1 24  ? -21.845 63.408 -33.503 1.00 25.17  ? 5    ASP E CA  1 
ATOM   6448 C C   . ASP E 1 24  ? -21.866 62.683 -32.152 1.00 23.75  ? 5    ASP E C   1 
ATOM   6449 O O   . ASP E 1 24  ? -20.943 62.841 -31.348 1.00 24.83  ? 5    ASP E O   1 
ATOM   6450 C CB  . ASP E 1 24  ? -22.812 64.598 -33.513 1.00 31.64  ? 5    ASP E CB  1 
ATOM   6451 C CG  . ASP E 1 24  ? -22.490 65.618 -34.623 1.00 51.17  ? 5    ASP E CG  1 
ATOM   6452 O OD1 . ASP E 1 24  ? -21.291 65.770 -35.002 1.00 51.34  ? 5    ASP E OD1 1 
ATOM   6453 O OD2 . ASP E 1 24  ? -23.448 66.269 -35.111 1.00 54.31  ? 5    ASP E OD2 1 
ATOM   6454 N N   . ILE E 1 25  ? -22.905 61.881 -31.919 1.00 23.19  ? 6    ILE E N   1 
ATOM   6455 C CA  . ILE E 1 25  ? -23.049 61.114 -30.677 1.00 22.00  ? 6    ILE E CA  1 
ATOM   6456 C C   . ILE E 1 25  ? -21.907 60.119 -30.440 1.00 23.07  ? 6    ILE E C   1 
ATOM   6457 O O   . ILE E 1 25  ? -21.307 60.075 -29.360 1.00 21.77  ? 6    ILE E O   1 
ATOM   6458 C CB  . ILE E 1 25  ? -24.399 60.352 -30.640 1.00 25.81  ? 6    ILE E CB  1 
ATOM   6459 C CG1 . ILE E 1 25  ? -25.574 61.335 -30.661 1.00 30.26  ? 6    ILE E CG1 1 
ATOM   6460 C CG2 . ILE E 1 25  ? -24.494 59.427 -29.409 1.00 22.33  ? 6    ILE E CG2 1 
ATOM   6461 C CD1 . ILE E 1 25  ? -26.921 60.662 -30.913 1.00 34.98  ? 6    ILE E CD1 1 
ATOM   6462 N N   . LEU E 1 26  ? -21.616 59.314 -31.455 1.00 23.77  ? 7    LEU E N   1 
ATOM   6463 C CA  . LEU E 1 26  ? -20.540 58.343 -31.356 1.00 23.74  ? 7    LEU E CA  1 
ATOM   6464 C C   . LEU E 1 26  ? -19.196 59.037 -31.142 1.00 23.99  ? 7    LEU E C   1 
ATOM   6465 O O   . LEU E 1 26  ? -18.335 58.529 -30.415 1.00 28.26  ? 7    LEU E O   1 
ATOM   6466 C CB  . LEU E 1 26  ? -20.524 57.418 -32.581 1.00 25.43  ? 7    LEU E CB  1 
ATOM   6467 C CG  . LEU E 1 26  ? -21.767 56.520 -32.641 1.00 22.24  ? 7    LEU E CG  1 
ATOM   6468 C CD1 . LEU E 1 26  ? -22.019 55.993 -34.045 1.00 29.89  ? 7    LEU E CD1 1 
ATOM   6469 C CD2 . LEU E 1 26  ? -21.657 55.373 -31.673 1.00 13.01  ? 7    LEU E CD2 1 
ATOM   6470 N N   . TYR E 1 27  ? -19.030 60.207 -31.754 1.00 22.31  ? 8    TYR E N   1 
ATOM   6471 C CA  . TYR E 1 27  ? -17.835 61.011 -31.552 1.00 20.70  ? 8    TYR E CA  1 
ATOM   6472 C C   . TYR E 1 27  ? -17.692 61.411 -30.082 1.00 21.94  ? 8    TYR E C   1 
ATOM   6473 O O   . TYR E 1 27  ? -16.678 61.118 -29.448 1.00 22.21  ? 8    TYR E O   1 
ATOM   6474 C CB  . TYR E 1 27  ? -17.852 62.248 -32.448 1.00 25.70  ? 8    TYR E CB  1 
ATOM   6475 C CG  . TYR E 1 27  ? -16.632 63.128 -32.263 1.00 36.08  ? 8    TYR E CG  1 
ATOM   6476 C CD1 . TYR E 1 27  ? -15.416 62.783 -32.832 1.00 27.79  ? 8    TYR E CD1 1 
ATOM   6477 C CD2 . TYR E 1 27  ? -16.698 64.302 -31.506 1.00 35.89  ? 8    TYR E CD2 1 
ATOM   6478 C CE1 . TYR E 1 27  ? -14.296 63.573 -32.663 1.00 32.95  ? 8    TYR E CE1 1 
ATOM   6479 C CE2 . TYR E 1 27  ? -15.582 65.108 -31.332 1.00 38.78  ? 8    TYR E CE2 1 
ATOM   6480 C CZ  . TYR E 1 27  ? -14.379 64.738 -31.913 1.00 47.87  ? 8    TYR E CZ  1 
ATOM   6481 O OH  . TYR E 1 27  ? -13.260 65.540 -31.736 1.00 48.64  ? 8    TYR E OH  1 
ATOM   6482 N N   . ASN E 1 28  ? -18.711 62.071 -29.539 1.00 22.12  ? 9    ASN E N   1 
ATOM   6483 C CA  . ASN E 1 28  ? -18.714 62.418 -28.117 1.00 22.51  ? 9    ASN E CA  1 
ATOM   6484 C C   . ASN E 1 28  ? -18.435 61.235 -27.203 1.00 20.62  ? 9    ASN E C   1 
ATOM   6485 O O   . ASN E 1 28  ? -17.649 61.340 -26.261 1.00 17.55  ? 9    ASN E O   1 
ATOM   6486 C CB  . ASN E 1 28  ? -20.021 63.116 -27.712 1.00 17.41  ? 9    ASN E CB  1 
ATOM   6487 C CG  . ASN E 1 28  ? -20.230 64.421 -28.452 1.00 20.42  ? 9    ASN E CG  1 
ATOM   6488 O OD1 . ASN E 1 28  ? -19.271 65.047 -28.927 1.00 28.76  ? 9    ASN E OD1 1 
ATOM   6489 N ND2 . ASN E 1 28  ? -21.489 64.838 -28.570 1.00 18.72  ? 9    ASN E ND2 1 
ATOM   6490 N N   . ILE E 1 29  ? -19.074 60.104 -27.497 1.00 25.55  ? 10   ILE E N   1 
ATOM   6491 C CA  . ILE E 1 29  ? -18.872 58.896 -26.694 1.00 27.56  ? 10   ILE E CA  1 
ATOM   6492 C C   . ILE E 1 29  ? -17.430 58.404 -26.723 1.00 27.66  ? 10   ILE E C   1 
ATOM   6493 O O   . ILE E 1 29  ? -16.853 58.103 -25.680 1.00 26.66  ? 10   ILE E O   1 
ATOM   6494 C CB  . ILE E 1 29  ? -19.829 57.762 -27.087 1.00 22.29  ? 10   ILE E CB  1 
ATOM   6495 C CG1 . ILE E 1 29  ? -21.273 58.164 -26.741 1.00 25.17  ? 10   ILE E CG1 1 
ATOM   6496 C CG2 . ILE E 1 29  ? -19.418 56.473 -26.377 1.00 16.98  ? 10   ILE E CG2 1 
ATOM   6497 C CD1 . ILE E 1 29  ? -22.319 57.091 -26.985 1.00 22.12  ? 10   ILE E CD1 1 
ATOM   6498 N N   . ARG E 1 30  ? -16.842 58.367 -27.914 1.00 24.01  ? 11   ARG E N   1 
ATOM   6499 C CA  . ARG E 1 30  ? -15.445 57.986 -28.039 1.00 27.04  ? 11   ARG E CA  1 
ATOM   6500 C C   . ARG E 1 30  ? -14.487 58.879 -27.231 1.00 32.36  ? 11   ARG E C   1 
ATOM   6501 O O   . ARG E 1 30  ? -13.504 58.390 -26.659 1.00 33.35  ? 11   ARG E O   1 
ATOM   6502 C CB  . ARG E 1 30  ? -15.024 57.925 -29.513 1.00 29.40  ? 11   ARG E CB  1 
ATOM   6503 C CG  . ARG E 1 30  ? -14.172 56.711 -29.807 1.00 50.15  ? 11   ARG E CG  1 
ATOM   6504 C CD  . ARG E 1 30  ? -13.103 56.991 -30.831 1.00 64.90  ? 11   ARG E CD  1 
ATOM   6505 N NE  . ARG E 1 30  ? -12.018 56.016 -30.717 1.00 77.25  ? 11   ARG E NE  1 
ATOM   6506 C CZ  . ARG E 1 30  ? -10.922 56.013 -31.472 1.00 84.72  ? 11   ARG E CZ  1 
ATOM   6507 N NH1 . ARG E 1 30  ? -10.751 56.935 -32.418 1.00 76.14  ? 11   ARG E NH1 1 
ATOM   6508 N NH2 . ARG E 1 30  ? -9.998  55.079 -31.279 1.00 82.56  ? 11   ARG E NH2 1 
ATOM   6509 N N   . GLN E 1 31  ? -14.793 60.177 -27.167 1.00 31.22  ? 12   GLN E N   1 
ATOM   6510 C CA  . GLN E 1 31  ? -13.925 61.156 -26.496 1.00 29.70  ? 12   GLN E CA  1 
ATOM   6511 C C   . GLN E 1 31  ? -14.051 61.254 -24.967 1.00 29.85  ? 12   GLN E C   1 
ATOM   6512 O O   . GLN E 1 31  ? -13.123 61.717 -24.311 1.00 33.83  ? 12   GLN E O   1 
ATOM   6513 C CB  . GLN E 1 31  ? -14.125 62.560 -27.086 1.00 26.55  ? 12   GLN E CB  1 
ATOM   6514 C CG  . GLN E 1 31  ? -13.891 62.686 -28.583 1.00 34.50  ? 12   GLN E CG  1 
ATOM   6515 C CD  . GLN E 1 31  ? -12.435 62.466 -28.970 1.00 45.21  ? 12   GLN E CD  1 
ATOM   6516 O OE1 . GLN E 1 31  ? -11.543 62.491 -28.116 1.00 50.12  ? 12   GLN E OE1 1 
ATOM   6517 N NE2 . GLN E 1 31  ? -12.188 62.243 -30.261 1.00 41.28  ? 12   GLN E NE2 1 
ATOM   6518 N N   . THR E 1 32  ? -15.203 60.968 -24.412 1.00 24.90  ? 13   THR E N   1 
ATOM   6519 C CA  . THR E 1 32  ? -15.450 61.295 -23.044 1.00 28.64  ? 13   THR E CA  1 
ATOM   6520 C C   . THR E 1 32  ? -15.850 60.139 -22.197 1.00 38.54  ? 13   THR E C   1 
ATOM   6521 O O   . THR E 1 32  ? -16.259 60.311 -21.077 1.00 39.26  ? 13   THR E O   1 
ATOM   6522 C CB  . THR E 1 32  ? -16.576 62.326 -22.944 1.00 28.46  ? 13   THR E CB  1 
ATOM   6523 O OG1 . THR E 1 32  ? -17.753 61.776 -23.490 1.00 33.69  ? 13   THR E OG1 1 
ATOM   6524 C CG2 . THR E 1 32  ? -16.262 63.549 -23.697 1.00 22.28  ? 13   THR E CG2 1 
ATOM   6525 N N   . SER E 1 33  ? -15.849 58.963 -22.781 1.00 47.52  ? 14   SER E N   1 
ATOM   6526 C CA  . SER E 1 33  ? -16.471 57.781 -22.195 1.00 39.15  ? 14   SER E CA  1 
ATOM   6527 C C   . SER E 1 33  ? -15.925 57.204 -20.895 1.00 43.11  ? 14   SER E C   1 
ATOM   6528 O O   . SER E 1 33  ? -16.699 56.913 -20.020 1.00 41.31  ? 14   SER E O   1 
ATOM   6529 C CB  . SER E 1 33  ? -16.519 56.696 -23.238 1.00 25.96  ? 14   SER E CB  1 
ATOM   6530 O OG  . SER E 1 33  ? -17.049 55.541 -22.707 1.00 32.48  ? 14   SER E OG  1 
ATOM   6531 N N   . ARG E 1 34  ? -14.613 57.098 -20.742 1.00 35.08  ? 15   ARG E N   1 
ATOM   6532 C CA  . ARG E 1 34  ? -14.031 56.446 -19.583 1.00 34.21  ? 15   ARG E CA  1 
ATOM   6533 C C   . ARG E 1 34  ? -14.336 54.968 -19.369 1.00 30.38  ? 15   ARG E C   1 
ATOM   6534 O O   . ARG E 1 34  ? -15.041 54.615 -18.492 1.00 31.49  ? 15   ARG E O   1 
ATOM   6535 C CB  . ARG E 1 34  ? -14.383 57.223 -18.315 1.00 34.51  ? 15   ARG E CB  1 
ATOM   6536 C CG  . ARG E 1 34  ? -13.931 58.660 -18.260 1.00 37.42  ? 15   ARG E CG  1 
ATOM   6537 C CD  . ARG E 1 34  ? -12.480 58.897 -18.651 1.00 43.73  ? 15   ARG E CD  1 
ATOM   6538 N NE  . ARG E 1 34  ? -11.466 58.265 -17.808 1.00 51.22  ? 15   ARG E NE  1 
ATOM   6539 C CZ  . ARG E 1 34  ? -11.051 58.682 -16.622 1.00 38.35  ? 15   ARG E CZ  1 
ATOM   6540 N NH1 . ARG E 1 34  ? -11.563 59.734 -16.060 1.00 45.82  ? 15   ARG E NH1 1 
ATOM   6541 N NH2 . ARG E 1 34  ? -10.130 58.011 -16.003 1.00 27.29  ? 15   ARG E NH2 1 
ATOM   6542 N N   . PRO E 1 35  ? -13.748 54.098 -20.257 1.00 19.46  ? 16   PRO E N   1 
ATOM   6543 C CA  . PRO E 1 35  ? -14.116 52.688 -20.144 1.00 19.50  ? 16   PRO E CA  1 
ATOM   6544 C C   . PRO E 1 35  ? -13.746 51.831 -18.950 1.00 21.63  ? 16   PRO E C   1 
ATOM   6545 O O   . PRO E 1 35  ? -14.134 50.725 -18.776 1.00 20.12  ? 16   PRO E O   1 
ATOM   6546 C CB  . PRO E 1 35  ? -13.433 52.076 -21.335 1.00 19.95  ? 16   PRO E CB  1 
ATOM   6547 C CG  . PRO E 1 35  ? -13.343 53.145 -22.280 1.00 23.65  ? 16   PRO E CG  1 
ATOM   6548 C CD  . PRO E 1 35  ? -12.781 54.166 -21.419 1.00 22.74  ? 16   PRO E CD  1 
ATOM   6549 N N   . ASP E 1 36  ? -12.807 52.270 -18.125 1.00 23.29  ? 17   ASP E N   1 
ATOM   6550 C CA  A ASP E 1 36  ? -12.087 52.019 -16.894 0.42 22.26  ? 17   ASP E CA  1 
ATOM   6551 C CA  B ASP E 1 36  ? -12.106 52.184 -16.794 0.58 21.39  ? 17   ASP E CA  1 
ATOM   6552 C C   . ASP E 1 36  ? -12.804 52.507 -15.425 1.00 22.72  ? 17   ASP E C   1 
ATOM   6553 O O   . ASP E 1 36  ? -12.739 52.110 -14.241 1.00 31.06  ? 17   ASP E O   1 
ATOM   6554 C CB  A ASP E 1 36  ? -10.618 52.495 -16.872 0.42 23.80  ? 17   ASP E CB  1 
ATOM   6555 C CB  B ASP E 1 36  ? -10.656 52.594 -16.935 0.58 23.56  ? 17   ASP E CB  1 
ATOM   6556 C CG  A ASP E 1 36  ? -10.468 54.029 -17.067 0.42 26.78  ? 17   ASP E CG  1 
ATOM   6557 C CG  B ASP E 1 36  ? -9.921  51.740 -17.953 0.58 24.35  ? 17   ASP E CG  1 
ATOM   6558 O OD1 A ASP E 1 36  ? -11.184 54.641 -17.904 0.42 23.80  ? 17   ASP E OD1 1 
ATOM   6559 O OD1 B ASP E 1 36  ? -10.280 50.594 -18.158 0.58 23.07  ? 17   ASP E OD1 1 
ATOM   6560 O OD2 A ASP E 1 36  ? -9.603  54.624 -16.380 0.42 26.50  ? 17   ASP E OD2 1 
ATOM   6561 O OD2 B ASP E 1 36  ? -8.953  52.199 -18.570 0.58 23.44  ? 17   ASP E OD2 1 
ATOM   6562 N N   . VAL E 1 37  ? -13.724 53.410 -15.750 1.00 20.25  ? 18   VAL E N   1 
ATOM   6563 C CA  . VAL E 1 37  ? -14.398 53.995 -14.591 1.00 17.68  ? 18   VAL E CA  1 
ATOM   6564 C C   . VAL E 1 37  ? -15.824 53.497 -14.410 1.00 17.02  ? 18   VAL E C   1 
ATOM   6565 O O   . VAL E 1 37  ? -16.689 53.769 -15.228 1.00 20.96  ? 18   VAL E O   1 
ATOM   6566 C CB  . VAL E 1 37  ? -14.479 55.521 -14.681 1.00 19.79  ? 18   VAL E CB  1 
ATOM   6567 C CG1 . VAL E 1 37  ? -15.234 56.077 -13.468 1.00 12.47  ? 18   VAL E CG1 1 
ATOM   6568 C CG2 . VAL E 1 37  ? -13.101 56.129 -14.814 1.00 27.50  ? 18   VAL E CG2 1 
ATOM   6569 N N   . ILE E 1 38  ? -16.065 52.783 -13.320 1.00 19.47  ? 19   ILE E N   1 
ATOM   6570 C CA  . ILE E 1 38  ? -17.400 52.294 -12.976 1.00 18.40  ? 19   ILE E CA  1 
ATOM   6571 C C   . ILE E 1 38  ? -18.376 53.466 -12.739 1.00 22.13  ? 19   ILE E C   1 
ATOM   6572 O O   . ILE E 1 38  ? -18.068 54.414 -12.000 1.00 22.63  ? 19   ILE E O   1 
ATOM   6573 C CB  . ILE E 1 38  ? -17.319 51.320 -11.751 1.00 21.12  ? 19   ILE E CB  1 
ATOM   6574 C CG1 . ILE E 1 38  ? -18.672 50.713 -11.390 1.00 18.42  ? 19   ILE E CG1 1 
ATOM   6575 C CG2 . ILE E 1 38  ? -16.700 52.000 -10.530 1.00 18.77  ? 19   ILE E CG2 1 
ATOM   6576 C CD1 . ILE E 1 38  ? -18.538 49.586 -10.384 1.00 15.32  ? 19   ILE E CD1 1 
ATOM   6577 N N   . PRO E 1 39  ? -19.556 53.417 -13.390 1.00 22.37  ? 20   PRO E N   1 
ATOM   6578 C CA  . PRO E 1 39  ? -20.499 54.545 -13.343 1.00 25.68  ? 20   PRO E CA  1 
ATOM   6579 C C   . PRO E 1 39  ? -21.398 54.524 -12.094 1.00 24.61  ? 20   PRO E C   1 
ATOM   6580 O O   . PRO E 1 39  ? -22.620 54.423 -12.187 1.00 23.93  ? 20   PRO E O   1 
ATOM   6581 C CB  . PRO E 1 39  ? -21.317 54.364 -14.637 1.00 22.15  ? 20   PRO E CB  1 
ATOM   6582 C CG  . PRO E 1 39  ? -21.310 52.879 -14.889 1.00 15.92  ? 20   PRO E CG  1 
ATOM   6583 C CD  . PRO E 1 39  ? -20.015 52.345 -14.299 1.00 18.72  ? 20   PRO E CD  1 
ATOM   6584 N N   . THR E 1 40  ? -20.784 54.622 -10.924 1.00 27.63  ? 21   THR E N   1 
ATOM   6585 C CA  . THR E 1 40  ? -21.546 54.657 -9.680  1.00 32.70  ? 21   THR E CA  1 
ATOM   6586 C C   . THR E 1 40  ? -22.229 56.002 -9.562  1.00 44.28  ? 21   THR E C   1 
ATOM   6587 O O   . THR E 1 40  ? -21.746 57.000 -10.100 1.00 45.08  ? 21   THR E O   1 
ATOM   6588 C CB  . THR E 1 40  ? -20.659 54.421 -8.440  1.00 34.29  ? 21   THR E CB  1 
ATOM   6589 O OG1 . THR E 1 40  ? -19.567 55.353 -8.443  1.00 45.05  ? 21   THR E OG1 1 
ATOM   6590 C CG2 . THR E 1 40  ? -20.113 52.987 -8.432  1.00 27.30  ? 21   THR E CG2 1 
ATOM   6591 N N   . GLN E 1 41  ? -23.407 56.013 -8.975  1.00 59.69  ? 22   GLN E N   1 
ATOM   6592 C CA  . GLN E 1 41  ? -24.087 57.249 -8.722  1.00 55.40  ? 22   GLN E CA  1 
ATOM   6593 C C   . GLN E 1 41  ? -24.202 57.374 -7.246  1.00 55.45  ? 22   GLN E C   1 
ATOM   6594 O O   . GLN E 1 41  ? -24.999 56.725 -6.636  1.00 60.46  ? 22   GLN E O   1 
ATOM   6595 C CB  . GLN E 1 41  ? -25.482 57.212 -9.337  1.00 49.07  ? 22   GLN E CB  1 
ATOM   6596 C CG  . GLN E 1 41  ? -25.571 57.842 -10.699 1.00 53.66  ? 22   GLN E CG  1 
ATOM   6597 C CD  . GLN E 1 41  ? -26.938 57.724 -11.335 1.00 76.60  ? 22   GLN E CD  1 
ATOM   6598 O OE1 . GLN E 1 41  ? -27.422 56.633 -11.562 1.00 79.49  ? 22   GLN E OE1 1 
ATOM   6599 N NE2 . GLN E 1 41  ? -27.553 58.860 -11.665 1.00 81.50  ? 22   GLN E NE2 1 
ATOM   6600 N N   . ARG E 1 42  ? -23.453 58.277 -6.677  1.00 57.21  ? 23   ARG E N   1 
ATOM   6601 C CA  . ARG E 1 42  ? -23.635 58.622 -5.282  1.00 74.70  ? 23   ARG E CA  1 
ATOM   6602 C C   . ARG E 1 42  ? -23.529 57.484 -4.287  1.00 67.69  ? 23   ARG E C   1 
ATOM   6603 O O   . ARG E 1 42  ? -24.340 57.359 -3.388  1.00 66.79  ? 23   ARG E O   1 
ATOM   6604 C CB  . ARG E 1 42  ? -24.965 59.340 -5.106  1.00 76.19  ? 23   ARG E CB  1 
ATOM   6605 C CG  . ARG E 1 42  ? -25.327 60.216 -6.276  1.00 77.17  ? 23   ARG E CG  1 
ATOM   6606 C CD  . ARG E 1 42  ? -26.207 61.341 -5.819  1.00 83.54  ? 23   ARG E CD  1 
ATOM   6607 N NE  . ARG E 1 42  ? -27.199 61.671 -6.811  1.00 84.47  ? 23   ARG E NE  1 
ATOM   6608 C CZ  . ARG E 1 42  ? -28.307 62.323 -6.528  1.00 91.06  ? 23   ARG E CZ  1 
ATOM   6609 N NH1 . ARG E 1 42  ? -28.538 62.694 -5.285  1.00 87.48  ? 23   ARG E NH1 1 
ATOM   6610 N NH2 . ARG E 1 42  ? -29.188 62.581 -7.485  1.00 92.29  ? 23   ARG E NH2 1 
ATOM   6611 N N   . ASP E 1 43  ? -22.531 56.646 -4.452  1.00 66.51  ? 24   ASP E N   1 
ATOM   6612 C CA  . ASP E 1 43  ? -22.283 55.609 -3.477  1.00 75.37  ? 24   ASP E CA  1 
ATOM   6613 C C   . ASP E 1 43  ? -23.347 54.533 -3.498  1.00 67.82  ? 24   ASP E C   1 
ATOM   6614 O O   . ASP E 1 43  ? -23.525 53.802 -2.545  1.00 65.08  ? 24   ASP E O   1 
ATOM   6615 C CB  . ASP E 1 43  ? -22.173 56.220 -2.090  1.00 74.76  ? 24   ASP E CB  1 
ATOM   6616 C CG  . ASP E 1 43  ? -20.739 56.371 -1.630  1.00 82.87  ? 24   ASP E CG  1 
ATOM   6617 O OD1 . ASP E 1 43  ? -19.840 55.934 -2.365  1.00 84.43  ? 24   ASP E OD1 1 
ATOM   6618 O OD2 . ASP E 1 43  ? -20.511 56.914 -0.526  1.00 81.65  ? 24   ASP E OD2 1 
ATOM   6619 N N   . ARG E 1 44  ? -24.030 54.430 -4.617  1.00 57.16  ? 25   ARG E N   1 
ATOM   6620 C CA  . ARG E 1 44  ? -25.009 53.410 -4.819  1.00 48.63  ? 25   ARG E CA  1 
ATOM   6621 C C   . ARG E 1 44  ? -24.411 52.480 -5.794  1.00 44.87  ? 25   ARG E C   1 
ATOM   6622 O O   . ARG E 1 44  ? -23.573 52.869 -6.562  1.00 50.26  ? 25   ARG E O   1 
ATOM   6623 C CB  . ARG E 1 44  ? -26.261 54.007 -5.386  1.00 53.59  ? 25   ARG E CB  1 
ATOM   6624 C CG  . ARG E 1 44  ? -27.039 54.799 -4.366  1.00 69.68  ? 25   ARG E CG  1 
ATOM   6625 C CD  . ARG E 1 44  ? -28.373 55.245 -4.904  1.00 74.90  ? 25   ARG E CD  1 
ATOM   6626 N NE  . ARG E 1 44  ? -28.987 56.165 -3.961  1.00 109.05 ? 25   ARG E NE  1 
ATOM   6627 C CZ  . ARG E 1 44  ? -29.081 57.486 -4.117  1.00 117.90 ? 25   ARG E CZ  1 
ATOM   6628 N NH1 . ARG E 1 44  ? -28.615 58.068 -5.224  1.00 116.64 ? 25   ARG E NH1 1 
ATOM   6629 N NH2 . ARG E 1 44  ? -29.663 58.220 -3.161  1.00 106.46 ? 25   ARG E NH2 1 
ATOM   6630 N N   . PRO E 1 45  ? -24.827 51.170 -5.699  1.00 35.96  ? 26   PRO E N   1 
ATOM   6631 C CA  . PRO E 1 45  ? -24.181 50.250 -6.638  1.00 29.56  ? 26   PRO E CA  1 
ATOM   6632 C C   . PRO E 1 45  ? -24.626 50.467 -8.038  1.00 24.36  ? 26   PRO E C   1 
ATOM   6633 O O   . PRO E 1 45  ? -25.557 51.177 -8.203  1.00 28.92  ? 26   PRO E O   1 
ATOM   6634 C CB  . PRO E 1 45  ? -24.705 48.913 -6.215  1.00 30.33  ? 26   PRO E CB  1 
ATOM   6635 C CG  . PRO E 1 45  ? -25.000 49.061 -4.817  1.00 32.67  ? 26   PRO E CG  1 
ATOM   6636 C CD  . PRO E 1 45  ? -25.707 50.329 -4.785  1.00 24.03  ? 26   PRO E CD  1 
ATOM   6637 N N   . VAL E 1 46  ? -23.941 49.930 -9.031  1.00 23.45  ? 27   VAL E N   1 
ATOM   6638 C CA  . VAL E 1 46  ? -24.506 49.920 -10.363 1.00 18.96  ? 27   VAL E CA  1 
ATOM   6639 C C   . VAL E 1 46  ? -25.364 48.690 -10.383 1.00 18.73  ? 27   VAL E C   1 
ATOM   6640 O O   . VAL E 1 46  ? -24.884 47.601 -10.071 1.00 22.99  ? 27   VAL E O   1 
ATOM   6641 C CB  . VAL E 1 46  ? -23.411 49.787 -11.419 1.00 22.17  ? 27   VAL E CB  1 
ATOM   6642 C CG1 . VAL E 1 46  ? -24.012 49.689 -12.811 1.00 19.95  ? 27   VAL E CG1 1 
ATOM   6643 C CG2 . VAL E 1 46  ? -22.433 50.971 -11.321 1.00 25.53  ? 27   VAL E CG2 1 
ATOM   6644 N N   . ALA E 1 47  ? -26.638 48.841 -10.722 1.00 21.46  ? 28   ALA E N   1 
ATOM   6645 C CA  . ALA E 1 47  ? -27.504 47.662 -10.813 1.00 23.79  ? 28   ALA E CA  1 
ATOM   6646 C C   . ALA E 1 47  ? -27.373 46.982 -12.175 1.00 26.05  ? 28   ALA E C   1 
ATOM   6647 O O   . ALA E 1 47  ? -27.813 47.521 -13.193 1.00 28.00  ? 28   ALA E O   1 
ATOM   6648 C CB  . ALA E 1 47  ? -28.937 48.019 -10.534 1.00 17.14  ? 28   ALA E CB  1 
ATOM   6649 N N   . VAL E 1 48  ? -26.769 45.797 -12.186 1.00 21.39  ? 29   VAL E N   1 
ATOM   6650 C CA  . VAL E 1 48  ? -26.640 45.023 -13.412 1.00 21.71  ? 29   VAL E CA  1 
ATOM   6651 C C   . VAL E 1 48  ? -27.691 43.903 -13.432 1.00 25.58  ? 29   VAL E C   1 
ATOM   6652 O O   . VAL E 1 48  ? -27.819 43.149 -12.473 1.00 25.16  ? 29   VAL E O   1 
ATOM   6653 C CB  . VAL E 1 48  ? -25.242 44.394 -13.513 1.00 21.38  ? 29   VAL E CB  1 
ATOM   6654 C CG1 . VAL E 1 48  ? -25.079 43.640 -14.838 1.00 14.12  ? 29   VAL E CG1 1 
ATOM   6655 C CG2 . VAL E 1 48  ? -24.163 45.459 -13.320 1.00 16.33  ? 29   VAL E CG2 1 
ATOM   6656 N N   . SER E 1 49  ? -28.441 43.794 -14.521 1.00 22.60  ? 30   SER E N   1 
ATOM   6657 C CA  . SER E 1 49  ? -29.341 42.671 -14.697 1.00 20.26  ? 30   SER E CA  1 
ATOM   6658 C C   . SER E 1 49  ? -28.716 41.665 -15.635 1.00 28.37  ? 30   SER E C   1 
ATOM   6659 O O   . SER E 1 49  ? -28.145 42.043 -16.662 1.00 34.51  ? 30   SER E O   1 
ATOM   6660 C CB  . SER E 1 49  ? -30.632 43.134 -15.315 1.00 25.37  ? 30   SER E CB  1 
ATOM   6661 O OG  . SER E 1 49  ? -30.997 44.364 -14.748 1.00 44.60  ? 30   SER E OG  1 
ATOM   6662 N N   . VAL E 1 50  ? -28.840 40.384 -15.291 1.00 29.08  ? 31   VAL E N   1 
ATOM   6663 C CA  . VAL E 1 50  ? -28.281 39.303 -16.094 1.00 25.63  ? 31   VAL E CA  1 
ATOM   6664 C C   . VAL E 1 50  ? -29.353 38.287 -16.430 1.00 26.22  ? 31   VAL E C   1 
ATOM   6665 O O   . VAL E 1 50  ? -30.122 37.884 -15.564 1.00 34.06  ? 31   VAL E O   1 
ATOM   6666 C CB  . VAL E 1 50  ? -27.148 38.584 -15.358 1.00 24.50  ? 31   VAL E CB  1 
ATOM   6667 C CG1 . VAL E 1 50  ? -26.557 37.511 -16.242 1.00 25.07  ? 31   VAL E CG1 1 
ATOM   6668 C CG2 . VAL E 1 50  ? -26.067 39.572 -14.961 1.00 21.94  ? 31   VAL E CG2 1 
ATOM   6669 N N   . SER E 1 51  ? -29.403 37.870 -17.689 1.00 22.90  ? 32   SER E N   1 
ATOM   6670 C CA  . SER E 1 51  ? -30.366 36.862 -18.115 1.00 27.29  ? 32   SER E CA  1 
ATOM   6671 C C   . SER E 1 51  ? -29.741 35.920 -19.155 1.00 25.74  ? 32   SER E C   1 
ATOM   6672 O O   . SER E 1 51  ? -29.200 36.378 -20.166 1.00 31.73  ? 32   SER E O   1 
ATOM   6673 C CB  . SER E 1 51  ? -31.611 37.555 -18.680 1.00 28.67  ? 32   SER E CB  1 
ATOM   6674 O OG  . SER E 1 51  ? -32.597 36.612 -19.062 1.00 44.27  ? 32   SER E OG  1 
ATOM   6675 N N   . LEU E 1 52  ? -29.800 34.615 -18.917 1.00 18.87  ? 33   LEU E N   1 
ATOM   6676 C CA  . LEU E 1 52  ? -29.317 33.660 -19.930 1.00 26.32  ? 33   LEU E CA  1 
ATOM   6677 C C   . LEU E 1 52  ? -30.444 33.081 -20.819 1.00 28.17  ? 33   LEU E C   1 
ATOM   6678 O O   . LEU E 1 52  ? -31.451 32.569 -20.332 1.00 33.11  ? 33   LEU E O   1 
ATOM   6679 C CB  . LEU E 1 52  ? -28.521 32.511 -19.297 1.00 21.43  ? 33   LEU E CB  1 
ATOM   6680 C CG  . LEU E 1 52  ? -27.461 32.917 -18.275 1.00 22.42  ? 33   LEU E CG  1 
ATOM   6681 C CD1 . LEU E 1 52  ? -26.588 31.742 -17.896 1.00 25.25  ? 33   LEU E CD1 1 
ATOM   6682 C CD2 . LEU E 1 52  ? -26.606 34.032 -18.814 1.00 26.31  ? 33   LEU E CD2 1 
ATOM   6683 N N   . LYS E 1 53  ? -30.269 33.168 -22.128 1.00 24.85  ? 34   LYS E N   1 
ATOM   6684 C CA  . LYS E 1 53  ? -31.179 32.527 -23.045 1.00 21.35  ? 34   LYS E CA  1 
ATOM   6685 C C   . LYS E 1 53  ? -30.434 31.334 -23.657 1.00 24.70  ? 34   LYS E C   1 
ATOM   6686 O O   . LYS E 1 53  ? -29.460 31.512 -24.411 1.00 20.35  ? 34   LYS E O   1 
ATOM   6687 C CB  . LYS E 1 53  ? -31.603 33.501 -24.142 1.00 17.00  ? 34   LYS E CB  1 
ATOM   6688 C CG  . LYS E 1 53  ? -31.897 34.893 -23.651 1.00 24.85  ? 34   LYS E CG  1 
ATOM   6689 C CD  . LYS E 1 53  ? -33.223 34.989 -22.915 1.00 36.40  ? 34   LYS E CD  1 
ATOM   6690 C CE  . LYS E 1 53  ? -33.517 36.433 -22.487 1.00 42.62  ? 34   LYS E CE  1 
ATOM   6691 N NZ  . LYS E 1 53  ? -34.782 36.537 -21.669 1.00 51.15  ? 34   LYS E NZ  1 
ATOM   6692 N N   . PHE E 1 54  ? -30.880 30.119 -23.351 1.00 19.50  ? 35   PHE E N   1 
ATOM   6693 C CA  . PHE E 1 54  ? -30.172 28.966 -23.864 1.00 15.89  ? 35   PHE E CA  1 
ATOM   6694 C C   . PHE E 1 54  ? -30.483 28.722 -25.315 1.00 17.05  ? 35   PHE E C   1 
ATOM   6695 O O   . PHE E 1 54  ? -31.620 28.834 -25.737 1.00 20.20  ? 35   PHE E O   1 
ATOM   6696 C CB  . PHE E 1 54  ? -30.432 27.754 -23.000 1.00 19.29  ? 35   PHE E CB  1 
ATOM   6697 C CG  . PHE E 1 54  ? -29.903 27.915 -21.624 1.00 19.83  ? 35   PHE E CG  1 
ATOM   6698 C CD1 . PHE E 1 54  ? -28.582 27.629 -21.341 1.00 16.40  ? 35   PHE E CD1 1 
ATOM   6699 C CD2 . PHE E 1 54  ? -30.712 28.412 -20.614 1.00 25.16  ? 35   PHE E CD2 1 
ATOM   6700 C CE1 . PHE E 1 54  ? -28.083 27.808 -20.049 1.00 17.27  ? 35   PHE E CE1 1 
ATOM   6701 C CE2 . PHE E 1 54  ? -30.221 28.598 -19.327 1.00 18.32  ? 35   PHE E CE2 1 
ATOM   6702 C CZ  . PHE E 1 54  ? -28.908 28.306 -19.049 1.00 16.36  ? 35   PHE E CZ  1 
ATOM   6703 N N   . ILE E 1 55  ? -29.443 28.425 -26.079 1.00 19.71  ? 36   ILE E N   1 
ATOM   6704 C CA  . ILE E 1 55  ? -29.579 28.210 -27.512 1.00 24.68  ? 36   ILE E CA  1 
ATOM   6705 C C   . ILE E 1 55  ? -29.281 26.750 -27.881 1.00 25.93  ? 36   ILE E C   1 
ATOM   6706 O O   . ILE E 1 55  ? -29.940 26.174 -28.753 1.00 29.89  ? 36   ILE E O   1 
ATOM   6707 C CB  . ILE E 1 55  ? -28.666 29.175 -28.328 1.00 21.72  ? 36   ILE E CB  1 
ATOM   6708 C CG1 . ILE E 1 55  ? -28.790 30.615 -27.808 1.00 17.56  ? 36   ILE E CG1 1 
ATOM   6709 C CG2 . ILE E 1 55  ? -28.981 29.100 -29.813 1.00 14.42  ? 36   ILE E CG2 1 
ATOM   6710 C CD1 . ILE E 1 55  ? -30.193 31.154 -27.795 1.00 15.83  ? 36   ILE E CD1 1 
ATOM   6711 N N   . ASN E 1 56  ? -28.297 26.150 -27.215 1.00 21.98  ? 37   ASN E N   1 
ATOM   6712 C CA  . ASN E 1 56  ? -27.937 24.771 -27.518 1.00 22.74  ? 37   ASN E CA  1 
ATOM   6713 C C   . ASN E 1 56  ? -27.215 24.071 -26.379 1.00 25.85  ? 37   ASN E C   1 
ATOM   6714 O O   . ASN E 1 56  ? -26.561 24.718 -25.560 1.00 25.36  ? 37   ASN E O   1 
ATOM   6715 C CB  . ASN E 1 56  ? -27.061 24.733 -28.768 1.00 24.00  ? 37   ASN E CB  1 
ATOM   6716 C CG  . ASN E 1 56  ? -27.422 23.601 -29.700 1.00 24.19  ? 37   ASN E CG  1 
ATOM   6717 O OD1 . ASN E 1 56  ? -27.608 22.463 -29.277 1.00 26.18  ? 37   ASN E OD1 1 
ATOM   6718 N ND2 . ASN E 1 56  ? -27.527 23.911 -30.981 1.00 28.99  ? 37   ASN E ND2 1 
ATOM   6719 N N   . ILE E 1 57  ? -27.342 22.746 -26.333 1.00 27.17  ? 38   ILE E N   1 
ATOM   6720 C CA  . ILE E 1 57  ? -26.542 21.916 -25.437 1.00 22.22  ? 38   ILE E CA  1 
ATOM   6721 C C   . ILE E 1 57  ? -25.797 20.901 -26.294 1.00 21.10  ? 38   ILE E C   1 
ATOM   6722 O O   . ILE E 1 57  ? -26.402 20.228 -27.118 1.00 25.28  ? 38   ILE E O   1 
ATOM   6723 C CB  . ILE E 1 57  ? -27.400 21.266 -24.361 1.00 18.88  ? 38   ILE E CB  1 
ATOM   6724 C CG1 . ILE E 1 57  ? -28.053 22.365 -23.514 1.00 21.86  ? 38   ILE E CG1 1 
ATOM   6725 C CG2 . ILE E 1 57  ? -26.548 20.355 -23.491 1.00 17.61  ? 38   ILE E CG2 1 
ATOM   6726 C CD1 . ILE E 1 57  ? -29.086 21.887 -22.506 1.00 18.69  ? 38   ILE E CD1 1 
ATOM   6727 N N   . LEU E 1 58  ? -24.480 20.822 -26.140 1.00 23.56  ? 39   LEU E N   1 
ATOM   6728 C CA  . LEU E 1 58  ? -23.671 20.260 -27.214 1.00 25.90  ? 39   LEU E CA  1 
ATOM   6729 C C   . LEU E 1 58  ? -22.960 18.996 -26.860 1.00 29.05  ? 39   LEU E C   1 
ATOM   6730 O O   . LEU E 1 58  ? -23.039 18.027 -27.606 1.00 42.08  ? 39   LEU E O   1 
ATOM   6731 C CB  . LEU E 1 58  ? -22.648 21.278 -27.722 1.00 29.57  ? 39   LEU E CB  1 
ATOM   6732 C CG  . LEU E 1 58  ? -23.240 22.415 -28.542 1.00 30.02  ? 39   LEU E CG  1 
ATOM   6733 C CD1 . LEU E 1 58  ? -22.146 23.342 -28.979 1.00 34.24  ? 39   LEU E CD1 1 
ATOM   6734 C CD2 . LEU E 1 58  ? -23.984 21.852 -29.757 1.00 35.75  ? 39   LEU E CD2 1 
ATOM   6735 N N   . GLU E 1 59  ? -22.237 19.002 -25.749 1.00 31.38  ? 40   GLU E N   1 
ATOM   6736 C CA  . GLU E 1 59  ? -21.417 17.842 -25.423 1.00 40.10  ? 40   GLU E CA  1 
ATOM   6737 C C   . GLU E 1 59  ? -21.514 17.527 -23.966 1.00 39.66  ? 40   GLU E C   1 
ATOM   6738 O O   . GLU E 1 59  ? -20.885 18.176 -23.133 1.00 41.07  ? 40   GLU E O   1 
ATOM   6739 C CB  . GLU E 1 59  ? -19.958 18.046 -25.826 1.00 39.60  ? 40   GLU E CB  1 
ATOM   6740 C CG  . GLU E 1 59  ? -19.530 17.179 -26.995 1.00 49.17  ? 40   GLU E CG  1 
ATOM   6741 C CD  . GLU E 1 59  ? -18.483 17.852 -27.872 1.00 61.36  ? 40   GLU E CD  1 
ATOM   6742 O OE1 . GLU E 1 59  ? -18.102 19.013 -27.575 1.00 59.86  ? 40   GLU E OE1 1 
ATOM   6743 O OE2 . GLU E 1 59  ? -18.047 17.214 -28.859 1.00 71.46  ? 40   GLU E OE2 1 
ATOM   6744 N N   . VAL E 1 60  ? -22.310 16.517 -23.662 1.00 33.38  ? 41   VAL E N   1 
ATOM   6745 C CA  . VAL E 1 60  ? -22.517 16.157 -22.284 1.00 29.02  ? 41   VAL E CA  1 
ATOM   6746 C C   . VAL E 1 60  ? -21.670 14.946 -21.953 1.00 31.94  ? 41   VAL E C   1 
ATOM   6747 O O   . VAL E 1 60  ? -21.530 14.036 -22.776 1.00 33.72  ? 41   VAL E O   1 
ATOM   6748 C CB  . VAL E 1 60  ? -23.987 15.919 -22.039 1.00 29.93  ? 41   VAL E CB  1 
ATOM   6749 C CG1 . VAL E 1 60  ? -24.211 15.381 -20.677 1.00 30.29  ? 41   VAL E CG1 1 
ATOM   6750 C CG2 . VAL E 1 60  ? -24.713 17.231 -22.209 1.00 35.07  ? 41   VAL E CG2 1 
ATOM   6751 N N   . ASN E 1 61  ? -21.050 14.975 -20.777 1.00 28.15  ? 42   ASN E N   1 
ATOM   6752 C CA  . ASN E 1 61  ? -20.312 13.824 -20.278 1.00 33.70  ? 42   ASN E CA  1 
ATOM   6753 C C   . ASN E 1 61  ? -20.746 13.536 -18.840 1.00 38.00  ? 42   ASN E C   1 
ATOM   6754 O O   . ASN E 1 61  ? -20.395 14.275 -17.917 1.00 35.32  ? 42   ASN E O   1 
ATOM   6755 C CB  . ASN E 1 61  ? -18.796 14.057 -20.387 1.00 30.14  ? 42   ASN E CB  1 
ATOM   6756 C CG  . ASN E 1 61  ? -17.969 12.789 -20.105 1.00 35.91  ? 42   ASN E CG  1 
ATOM   6757 O OD1 . ASN E 1 61  ? -18.301 11.980 -19.222 1.00 31.98  ? 42   ASN E OD1 1 
ATOM   6758 N ND2 . ASN E 1 61  ? -16.882 12.620 -20.859 1.00 35.77  ? 42   ASN E ND2 1 
ATOM   6759 N N   . GLU E 1 62  ? -21.528 12.470 -18.658 1.00 35.97  ? 43   GLU E N   1 
ATOM   6760 C CA  . GLU E 1 62  ? -22.027 12.112 -17.331 1.00 34.08  ? 43   GLU E CA  1 
ATOM   6761 C C   . GLU E 1 62  ? -20.895 11.556 -16.446 1.00 37.09  ? 43   GLU E C   1 
ATOM   6762 O O   . GLU E 1 62  ? -20.925 11.692 -15.217 1.00 37.53  ? 43   GLU E O   1 
ATOM   6763 C CB  . GLU E 1 62  ? -23.207 11.126 -17.437 1.00 38.86  ? 43   GLU E CB  1 
ATOM   6764 C CG  . GLU E 1 62  ? -24.112 11.041 -16.181 1.00 45.97  ? 43   GLU E CG  1 
ATOM   6765 C CD  . GLU E 1 62  ? -25.326 10.092 -16.349 1.00 58.20  ? 43   GLU E CD  1 
ATOM   6766 O OE1 . GLU E 1 62  ? -25.622 9.681  -17.502 1.00 54.02  ? 43   GLU E OE1 1 
ATOM   6767 O OE2 . GLU E 1 62  ? -25.987 9.763  -15.323 1.00 53.04  ? 43   GLU E OE2 1 
ATOM   6768 N N   . ILE E 1 63  ? -19.888 10.952 -17.078 1.00 31.59  ? 44   ILE E N   1 
ATOM   6769 C CA  . ILE E 1 63  ? -18.744 10.404 -16.339 1.00 34.85  ? 44   ILE E CA  1 
ATOM   6770 C C   . ILE E 1 63  ? -17.914 11.490 -15.651 1.00 35.41  ? 44   ILE E C   1 
ATOM   6771 O O   . ILE E 1 63  ? -17.540 11.339 -14.482 1.00 29.27  ? 44   ILE E O   1 
ATOM   6772 C CB  . ILE E 1 63  ? -17.761 9.586  -17.235 1.00 40.94  ? 44   ILE E CB  1 
ATOM   6773 C CG1 . ILE E 1 63  ? -18.472 8.465  -18.016 1.00 30.77  ? 44   ILE E CG1 1 
ATOM   6774 C CG2 . ILE E 1 63  ? -16.593 9.065  -16.393 1.00 31.72  ? 44   ILE E CG2 1 
ATOM   6775 C CD1 . ILE E 1 63  ? -19.101 7.401  -17.163 1.00 25.82  ? 44   ILE E CD1 1 
ATOM   6776 N N   . THR E 1 64  ? -17.613 12.569 -16.388 1.00 39.53  ? 45   THR E N   1 
ATOM   6777 C CA  . THR E 1 64  ? -16.730 13.640 -15.892 1.00 30.27  ? 45   THR E CA  1 
ATOM   6778 C C   . THR E 1 64  ? -17.485 14.833 -15.373 1.00 26.21  ? 45   THR E C   1 
ATOM   6779 O O   . THR E 1 64  ? -16.875 15.780 -14.897 1.00 27.89  ? 45   THR E O   1 
ATOM   6780 C CB  . THR E 1 64  ? -15.780 14.166 -16.965 1.00 25.08  ? 45   THR E CB  1 
ATOM   6781 O OG1 . THR E 1 64  ? -16.541 14.849 -17.958 1.00 32.90  ? 45   THR E OG1 1 
ATOM   6782 C CG2 . THR E 1 64  ? -15.010 13.032 -17.629 1.00 33.62  ? 45   THR E CG2 1 
ATOM   6783 N N   . ASN E 1 65  ? -18.810 14.797 -15.480 1.00 29.03  ? 46   ASN E N   1 
ATOM   6784 C CA  . ASN E 1 65  ? -19.645 15.934 -15.067 1.00 34.04  ? 46   ASN E CA  1 
ATOM   6785 C C   . ASN E 1 65  ? -19.305 17.291 -15.739 1.00 28.23  ? 46   ASN E C   1 
ATOM   6786 O O   . ASN E 1 65  ? -19.028 18.284 -15.061 1.00 23.51  ? 46   ASN E O   1 
ATOM   6787 C CB  . ASN E 1 65  ? -19.643 16.077 -13.546 1.00 33.89  ? 46   ASN E CB  1 
ATOM   6788 C CG  . ASN E 1 65  ? -20.735 15.261 -12.874 1.00 34.61  ? 46   ASN E CG  1 
ATOM   6789 O OD1 . ASN E 1 65  ? -21.730 14.874 -13.496 1.00 33.76  ? 46   ASN E OD1 1 
ATOM   6790 N ND2 . ASN E 1 65  ? -20.559 15.010 -11.579 1.00 37.26  ? 46   ASN E ND2 1 
ATOM   6791 N N   . GLU E 1 66  ? -19.338 17.306 -17.072 1.00 26.43  ? 47   GLU E N   1 
ATOM   6792 C CA  . GLU E 1 66  ? -19.025 18.484 -17.853 1.00 25.88  ? 47   GLU E CA  1 
ATOM   6793 C C   . GLU E 1 66  ? -20.058 18.673 -18.959 1.00 31.29  ? 47   GLU E C   1 
ATOM   6794 O O   . GLU E 1 66  ? -20.478 17.698 -19.587 1.00 30.99  ? 47   GLU E O   1 
ATOM   6795 C CB  . GLU E 1 66  ? -17.631 18.349 -18.453 1.00 26.52  ? 47   GLU E CB  1 
ATOM   6796 C CG  . GLU E 1 66  ? -16.541 18.241 -17.417 1.00 30.07  ? 47   GLU E CG  1 
ATOM   6797 C CD  . GLU E 1 66  ? -15.141 18.113 -18.018 1.00 41.31  ? 47   GLU E CD  1 
ATOM   6798 O OE1 . GLU E 1 66  ? -14.989 18.307 -19.259 1.00 42.20  ? 47   GLU E OE1 1 
ATOM   6799 O OE2 . GLU E 1 66  ? -14.193 17.820 -17.230 1.00 37.78  ? 47   GLU E OE2 1 
ATOM   6800 N N   . VAL E 1 67  ? -20.466 19.923 -19.192 1.00 30.37  ? 48   VAL E N   1 
ATOM   6801 C CA  . VAL E 1 67  ? -21.381 20.238 -20.288 1.00 24.95  ? 48   VAL E CA  1 
ATOM   6802 C C   . VAL E 1 67  ? -20.843 21.360 -21.155 1.00 26.36  ? 48   VAL E C   1 
ATOM   6803 O O   . VAL E 1 67  ? -20.023 22.161 -20.717 1.00 24.57  ? 48   VAL E O   1 
ATOM   6804 C CB  . VAL E 1 67  ? -22.787 20.620 -19.788 1.00 25.48  ? 48   VAL E CB  1 
ATOM   6805 C CG1 . VAL E 1 67  ? -23.360 19.520 -18.933 1.00 31.88  ? 48   VAL E CG1 1 
ATOM   6806 C CG2 . VAL E 1 67  ? -22.727 21.868 -18.980 1.00 27.06  ? 48   VAL E CG2 1 
ATOM   6807 N N   . ASP E 1 68  ? -21.318 21.395 -22.397 1.00 35.62  ? 49   ASP E N   1 
ATOM   6808 C CA  . ASP E 1 68  ? -20.965 22.421 -23.370 1.00 24.53  ? 49   ASP E CA  1 
ATOM   6809 C C   . ASP E 1 68  ? -22.218 23.185 -23.743 1.00 24.37  ? 49   ASP E C   1 
ATOM   6810 O O   . ASP E 1 68  ? -23.109 22.644 -24.386 1.00 24.39  ? 49   ASP E O   1 
ATOM   6811 C CB  . ASP E 1 68  ? -20.423 21.763 -24.619 1.00 26.28  ? 49   ASP E CB  1 
ATOM   6812 C CG  . ASP E 1 68  ? -19.116 22.326 -25.024 1.00 34.11  ? 49   ASP E CG  1 
ATOM   6813 O OD1 . ASP E 1 68  ? -18.466 22.904 -24.134 1.00 48.87  ? 49   ASP E OD1 1 
ATOM   6814 O OD2 . ASP E 1 68  ? -18.736 22.195 -26.209 1.00 37.13  ? 49   ASP E OD2 1 
ATOM   6815 N N   . VAL E 1 69  ? -22.299 24.440 -23.342 1.00 26.20  ? 50   VAL E N   1 
ATOM   6816 C CA  . VAL E 1 69  ? -23.510 25.205 -23.572 1.00 21.86  ? 50   VAL E CA  1 
ATOM   6817 C C   . VAL E 1 69  ? -23.288 26.401 -24.511 1.00 21.75  ? 50   VAL E C   1 
ATOM   6818 O O   . VAL E 1 69  ? -22.227 27.038 -24.500 1.00 19.28  ? 50   VAL E O   1 
ATOM   6819 C CB  . VAL E 1 69  ? -24.084 25.656 -22.233 1.00 23.21  ? 50   VAL E CB  1 
ATOM   6820 C CG1 . VAL E 1 69  ? -25.409 26.368 -22.428 1.00 27.70  ? 50   VAL E CG1 1 
ATOM   6821 C CG2 . VAL E 1 69  ? -24.264 24.444 -21.340 1.00 22.20  ? 50   VAL E CG2 1 
ATOM   6822 N N   . VAL E 1 70  ? -24.288 26.671 -25.349 1.00 20.79  ? 51   VAL E N   1 
ATOM   6823 C CA  . VAL E 1 70  ? -24.350 27.915 -26.100 1.00 17.04  ? 51   VAL E CA  1 
ATOM   6824 C C   . VAL E 1 70  ? -25.539 28.702 -25.567 1.00 17.75  ? 51   VAL E C   1 
ATOM   6825 O O   . VAL E 1 70  ? -26.658 28.178 -25.508 1.00 20.32  ? 51   VAL E O   1 
ATOM   6826 C CB  . VAL E 1 70  ? -24.500 27.658 -27.616 1.00 13.92  ? 51   VAL E CB  1 
ATOM   6827 C CG1 . VAL E 1 70  ? -24.799 28.943 -28.335 1.00 14.24  ? 51   VAL E CG1 1 
ATOM   6828 C CG2 . VAL E 1 70  ? -23.242 27.012 -28.180 1.00 13.05  ? 51   VAL E CG2 1 
ATOM   6829 N N   . PHE E 1 71  ? -25.299 29.950 -25.173 1.00 15.90  ? 52   PHE E N   1 
ATOM   6830 C CA  . PHE E 1 71  ? -26.359 30.799 -24.628 1.00 16.83  ? 52   PHE E CA  1 
ATOM   6831 C C   . PHE E 1 71  ? -26.116 32.284 -24.914 1.00 16.03  ? 52   PHE E C   1 
ATOM   6832 O O   . PHE E 1 71  ? -24.980 32.686 -25.116 1.00 17.03  ? 52   PHE E O   1 
ATOM   6833 C CB  . PHE E 1 71  ? -26.435 30.587 -23.122 1.00 18.30  ? 52   PHE E CB  1 
ATOM   6834 C CG  . PHE E 1 71  ? -25.154 30.888 -22.419 1.00 19.93  ? 52   PHE E CG  1 
ATOM   6835 C CD1 . PHE E 1 71  ? -24.148 29.928 -22.355 1.00 22.93  ? 52   PHE E CD1 1 
ATOM   6836 C CD2 . PHE E 1 71  ? -24.937 32.136 -21.840 1.00 17.49  ? 52   PHE E CD2 1 
ATOM   6837 C CE1 . PHE E 1 71  ? -22.938 30.205 -21.718 1.00 22.90  ? 52   PHE E CE1 1 
ATOM   6838 C CE2 . PHE E 1 71  ? -23.740 32.425 -21.199 1.00 17.38  ? 52   PHE E CE2 1 
ATOM   6839 C CZ  . PHE E 1 71  ? -22.736 31.456 -21.136 1.00 19.11  ? 52   PHE E CZ  1 
ATOM   6840 N N   . TRP E 1 72  ? -27.180 33.088 -24.938 1.00 17.54  ? 53   TRP E N   1 
ATOM   6841 C CA  . TRP E 1 72  ? -27.047 34.551 -24.998 1.00 17.70  ? 53   TRP E CA  1 
ATOM   6842 C C   . TRP E 1 72  ? -26.961 35.065 -23.582 1.00 18.21  ? 53   TRP E C   1 
ATOM   6843 O O   . TRP E 1 72  ? -27.767 34.690 -22.730 1.00 15.53  ? 53   TRP E O   1 
ATOM   6844 C CB  . TRP E 1 72  ? -28.254 35.234 -25.654 1.00 16.62  ? 53   TRP E CB  1 
ATOM   6845 C CG  . TRP E 1 72  ? -28.504 34.874 -27.080 1.00 15.86  ? 53   TRP E CG  1 
ATOM   6846 C CD1 . TRP E 1 72  ? -27.765 34.032 -27.853 1.00 17.20  ? 53   TRP E CD1 1 
ATOM   6847 C CD2 . TRP E 1 72  ? -29.578 35.340 -27.904 1.00 16.18  ? 53   TRP E CD2 1 
ATOM   6848 N NE1 . TRP E 1 72  ? -28.317 33.938 -29.104 1.00 16.90  ? 53   TRP E NE1 1 
ATOM   6849 C CE2 . TRP E 1 72  ? -29.437 34.734 -29.164 1.00 11.19  ? 53   TRP E CE2 1 
ATOM   6850 C CE3 . TRP E 1 72  ? -30.658 36.219 -27.698 1.00 20.11  ? 53   TRP E CE3 1 
ATOM   6851 C CZ2 . TRP E 1 72  ? -30.312 34.964 -30.217 1.00 13.33  ? 53   TRP E CZ2 1 
ATOM   6852 C CZ3 . TRP E 1 72  ? -31.532 36.458 -28.744 1.00 22.11  ? 53   TRP E CZ3 1 
ATOM   6853 C CH2 . TRP E 1 72  ? -31.351 35.832 -29.992 1.00 22.16  ? 53   TRP E CH2 1 
ATOM   6854 N N   . GLN E 1 73  ? -25.995 35.941 -23.328 1.00 17.40  ? 54   GLN E N   1 
ATOM   6855 C CA  . GLN E 1 73  ? -25.828 36.481 -21.984 1.00 19.47  ? 54   GLN E CA  1 
ATOM   6856 C C   . GLN E 1 73  ? -26.312 37.920 -21.916 1.00 19.01  ? 54   GLN E C   1 
ATOM   6857 O O   . GLN E 1 73  ? -25.537 38.856 -22.000 1.00 21.38  ? 54   GLN E O   1 
ATOM   6858 C CB  . GLN E 1 73  ? -24.371 36.374 -21.532 1.00 19.13  ? 54   GLN E CB  1 
ATOM   6859 C CG  . GLN E 1 73  ? -24.144 36.859 -20.110 1.00 19.32  ? 54   GLN E CG  1 
ATOM   6860 C CD  . GLN E 1 73  ? -22.725 36.615 -19.635 1.00 27.72  ? 54   GLN E CD  1 
ATOM   6861 O OE1 . GLN E 1 73  ? -22.238 35.473 -19.609 1.00 18.60  ? 54   GLN E OE1 1 
ATOM   6862 N NE2 . GLN E 1 73  ? -22.039 37.698 -19.265 1.00 39.79  ? 54   GLN E NE2 1 
ATOM   6863 N N   . GLN E 1 74  ? -27.611 38.098 -21.764 1.00 21.68  ? 55   GLN E N   1 
ATOM   6864 C CA  . GLN E 1 74  ? -28.182 39.430 -21.859 1.00 22.28  ? 55   GLN E CA  1 
ATOM   6865 C C   . GLN E 1 74  ? -27.870 40.236 -20.603 1.00 27.83  ? 55   GLN E C   1 
ATOM   6866 O O   . GLN E 1 74  ? -28.335 39.906 -19.500 1.00 24.17  ? 55   GLN E O   1 
ATOM   6867 C CB  . GLN E 1 74  ? -29.686 39.337 -22.063 1.00 23.77  ? 55   GLN E CB  1 
ATOM   6868 C CG  . GLN E 1 74  ? -30.359 40.685 -22.086 1.00 33.94  ? 55   GLN E CG  1 
ATOM   6869 C CD  . GLN E 1 74  ? -31.852 40.593 -22.366 1.00 40.95  ? 55   GLN E CD  1 
ATOM   6870 O OE1 . GLN E 1 74  ? -32.297 39.733 -23.133 1.00 51.72  ? 55   GLN E OE1 1 
ATOM   6871 N NE2 . GLN E 1 74  ? -32.631 41.485 -21.751 1.00 36.90  ? 55   GLN E NE2 1 
ATOM   6872 N N   . THR E 1 75  ? -27.086 41.301 -20.780 1.00 27.74  ? 56   THR E N   1 
ATOM   6873 C CA  . THR E 1 75  ? -26.593 42.100 -19.658 1.00 21.86  ? 56   THR E CA  1 
ATOM   6874 C C   . THR E 1 75  ? -27.060 43.548 -19.796 1.00 22.49  ? 56   THR E C   1 
ATOM   6875 O O   . THR E 1 75  ? -26.906 44.150 -20.861 1.00 21.57  ? 56   THR E O   1 
ATOM   6876 C CB  . THR E 1 75  ? -25.047 42.058 -19.571 1.00 19.79  ? 56   THR E CB  1 
ATOM   6877 O OG1 . THR E 1 75  ? -24.562 40.724 -19.784 1.00 25.17  ? 56   THR E OG1 1 
ATOM   6878 C CG2 . THR E 1 75  ? -24.590 42.528 -18.211 1.00 19.95  ? 56   THR E CG2 1 
ATOM   6879 N N   . THR E 1 76  ? -27.617 44.111 -18.723 1.00 22.23  ? 57   THR E N   1 
ATOM   6880 C CA  . THR E 1 76  ? -28.213 45.451 -18.785 1.00 21.90  ? 57   THR E CA  1 
ATOM   6881 C C   . THR E 1 76  ? -27.889 46.342 -17.580 1.00 25.71  ? 57   THR E C   1 
ATOM   6882 O O   . THR E 1 76  ? -28.012 45.909 -16.434 1.00 30.42  ? 57   THR E O   1 
ATOM   6883 C CB  . THR E 1 76  ? -29.732 45.342 -18.934 1.00 27.44  ? 57   THR E CB  1 
ATOM   6884 O OG1 . THR E 1 76  ? -30.041 44.794 -20.231 1.00 31.37  ? 57   THR E OG1 1 
ATOM   6885 C CG2 . THR E 1 76  ? -30.391 46.718 -18.802 1.00 40.67  ? 57   THR E CG2 1 
ATOM   6886 N N   . TRP E 1 77  ? -27.477 47.583 -17.834 1.00 23.35  ? 58   TRP E N   1 
ATOM   6887 C CA  . TRP E 1 77  ? -27.151 48.507 -16.748 1.00 18.25  ? 58   TRP E CA  1 
ATOM   6888 C C   . TRP E 1 77  ? -27.294 49.951 -17.187 1.00 20.34  ? 58   TRP E C   1 
ATOM   6889 O O   . TRP E 1 77  ? -27.575 50.247 -18.348 1.00 20.02  ? 58   TRP E O   1 
ATOM   6890 C CB  . TRP E 1 77  ? -25.732 48.269 -16.230 1.00 17.25  ? 58   TRP E CB  1 
ATOM   6891 C CG  . TRP E 1 77  ? -24.696 48.662 -17.213 1.00 15.55  ? 58   TRP E CG  1 
ATOM   6892 C CD1 . TRP E 1 77  ? -24.059 49.863 -17.290 1.00 17.09  ? 58   TRP E CD1 1 
ATOM   6893 C CD2 . TRP E 1 77  ? -24.188 47.868 -18.286 1.00 15.37  ? 58   TRP E CD2 1 
ATOM   6894 N NE1 . TRP E 1 77  ? -23.179 49.865 -18.339 1.00 17.29  ? 58   TRP E NE1 1 
ATOM   6895 C CE2 . TRP E 1 77  ? -23.236 48.647 -18.971 1.00 14.23  ? 58   TRP E CE2 1 
ATOM   6896 C CE3 . TRP E 1 77  ? -24.447 46.568 -18.737 1.00 13.47  ? 58   TRP E CE3 1 
ATOM   6897 C CZ2 . TRP E 1 77  ? -22.526 48.178 -20.070 1.00 11.96  ? 58   TRP E CZ2 1 
ATOM   6898 C CZ3 . TRP E 1 77  ? -23.743 46.097 -19.832 1.00 14.25  ? 58   TRP E CZ3 1 
ATOM   6899 C CH2 . TRP E 1 77  ? -22.791 46.904 -20.490 1.00 13.62  ? 58   TRP E CH2 1 
ATOM   6900 N N   . SER E 1 78  ? -27.073 50.862 -16.253 1.00 21.62  ? 59   SER E N   1 
ATOM   6901 C CA  . SER E 1 78  ? -27.243 52.263 -16.568 1.00 17.53  ? 59   SER E CA  1 
ATOM   6902 C C   . SER E 1 78  ? -25.946 53.049 -16.433 1.00 19.37  ? 59   SER E C   1 
ATOM   6903 O O   . SER E 1 78  ? -25.208 52.876 -15.458 1.00 21.18  ? 59   SER E O   1 
ATOM   6904 C CB  . SER E 1 78  ? -28.319 52.855 -15.683 1.00 20.06  ? 59   SER E CB  1 
ATOM   6905 O OG  . SER E 1 78  ? -28.502 54.214 -16.005 1.00 37.59  ? 59   SER E OG  1 
ATOM   6906 N N   . ASP E 1 79  ? -25.674 53.915 -17.417 1.00 23.14  ? 60   ASP E N   1 
ATOM   6907 C CA  . ASP E 1 79  ? -24.478 54.771 -17.418 1.00 24.64  ? 60   ASP E CA  1 
ATOM   6908 C C   . ASP E 1 79  ? -24.800 56.183 -17.907 1.00 26.45  ? 60   ASP E C   1 
ATOM   6909 O O   . ASP E 1 79  ? -24.747 56.450 -19.112 1.00 27.02  ? 60   ASP E O   1 
ATOM   6910 C CB  . ASP E 1 79  ? -23.373 54.148 -18.281 1.00 21.13  ? 60   ASP E CB  1 
ATOM   6911 C CG  . ASP E 1 79  ? -22.007 54.802 -18.068 1.00 27.59  ? 60   ASP E CG  1 
ATOM   6912 O OD1 . ASP E 1 79  ? -21.949 55.974 -17.608 1.00 31.63  ? 60   ASP E OD1 1 
ATOM   6913 O OD2 . ASP E 1 79  ? -20.988 54.134 -18.363 1.00 24.94  ? 60   ASP E OD2 1 
ATOM   6914 N N   . ARG E 1 80  ? -25.104 57.083 -16.970 1.00 25.85  ? 61   ARG E N   1 
ATOM   6915 C CA  . ARG E 1 80  ? -25.557 58.440 -17.304 1.00 29.58  ? 61   ARG E CA  1 
ATOM   6916 C C   . ARG E 1 80  ? -24.519 59.262 -18.051 1.00 25.27  ? 61   ARG E C   1 
ATOM   6917 O O   . ARG E 1 80  ? -24.865 60.215 -18.735 1.00 36.84  ? 61   ARG E O   1 
ATOM   6918 C CB  . ARG E 1 80  ? -26.008 59.197 -16.050 1.00 32.39  ? 61   ARG E CB  1 
ATOM   6919 C CG  . ARG E 1 80  ? -26.952 58.408 -15.148 1.00 49.22  ? 61   ARG E CG  1 
ATOM   6920 C CD  . ARG E 1 80  ? -28.405 58.390 -15.637 1.00 55.40  ? 61   ARG E CD  1 
ATOM   6921 N NE  . ARG E 1 80  ? -29.304 57.851 -14.606 1.00 73.26  ? 61   ARG E NE  1 
ATOM   6922 C CZ  . ARG E 1 80  ? -30.159 56.842 -14.786 1.00 76.19  ? 61   ARG E CZ  1 
ATOM   6923 N NH1 . ARG E 1 80  ? -30.255 56.257 -15.975 1.00 71.80  ? 61   ARG E NH1 1 
ATOM   6924 N NH2 . ARG E 1 80  ? -30.927 56.420 -13.779 1.00 69.19  ? 61   ARG E NH2 1 
ATOM   6925 N N   . THR E 1 81  ? -23.250 58.907 -17.906 1.00 20.80  ? 62   THR E N   1 
ATOM   6926 C CA  . THR E 1 81  ? -22.170 59.525 -18.676 1.00 20.39  ? 62   THR E CA  1 
ATOM   6927 C C   . THR E 1 81  ? -22.419 59.479 -20.197 1.00 29.28  ? 62   THR E C   1 
ATOM   6928 O O   . THR E 1 81  ? -21.913 60.310 -20.944 1.00 33.76  ? 62   THR E O   1 
ATOM   6929 C CB  . THR E 1 81  ? -20.858 58.785 -18.368 1.00 25.50  ? 62   THR E CB  1 
ATOM   6930 O OG1 . THR E 1 81  ? -20.621 58.827 -16.958 1.00 29.06  ? 62   THR E OG1 1 
ATOM   6931 C CG2 . THR E 1 81  ? -19.656 59.354 -19.127 1.00 28.90  ? 62   THR E CG2 1 
ATOM   6932 N N   . LEU E 1 82  ? -23.196 58.500 -20.656 1.00 30.26  ? 63   LEU E N   1 
ATOM   6933 C CA  . LEU E 1 82  ? -23.406 58.302 -22.086 1.00 23.27  ? 63   LEU E CA  1 
ATOM   6934 C C   . LEU E 1 82  ? -24.610 59.070 -22.625 1.00 20.51  ? 63   LEU E C   1 
ATOM   6935 O O   . LEU E 1 82  ? -24.840 59.134 -23.840 1.00 19.52  ? 63   LEU E O   1 
ATOM   6936 C CB  . LEU E 1 82  ? -23.571 56.807 -22.374 1.00 21.73  ? 63   LEU E CB  1 
ATOM   6937 C CG  . LEU E 1 82  ? -22.425 55.900 -21.924 1.00 22.29  ? 63   LEU E CG  1 
ATOM   6938 C CD1 . LEU E 1 82  ? -22.848 54.444 -22.001 1.00 19.22  ? 63   LEU E CD1 1 
ATOM   6939 C CD2 . LEU E 1 82  ? -21.178 56.133 -22.782 1.00 18.93  ? 63   LEU E CD2 1 
ATOM   6940 N N   . ALA E 1 83  ? -25.389 59.652 -21.726 1.00 21.72  ? 64   ALA E N   1 
ATOM   6941 C CA  . ALA E 1 83  ? -26.694 60.188 -22.110 1.00 23.47  ? 64   ALA E CA  1 
ATOM   6942 C C   . ALA E 1 83  ? -26.581 61.410 -23.017 1.00 23.40  ? 64   ALA E C   1 
ATOM   6943 O O   . ALA E 1 83  ? -25.579 62.123 -22.991 1.00 28.70  ? 64   ALA E O   1 
ATOM   6944 C CB  . ALA E 1 83  ? -27.515 60.507 -20.888 1.00 22.35  ? 64   ALA E CB  1 
ATOM   6945 N N   . TRP E 1 84  ? -27.605 61.633 -23.829 1.00 20.87  ? 65   TRP E N   1 
ATOM   6946 C CA  . TRP E 1 84  ? -27.685 62.835 -24.660 1.00 28.08  ? 65   TRP E CA  1 
ATOM   6947 C C   . TRP E 1 84  ? -29.138 63.353 -24.776 1.00 31.74  ? 65   TRP E C   1 
ATOM   6948 O O   . TRP E 1 84  ? -30.087 62.653 -24.415 1.00 35.51  ? 65   TRP E O   1 
ATOM   6949 C CB  . TRP E 1 84  ? -27.046 62.594 -26.045 1.00 25.93  ? 65   TRP E CB  1 
ATOM   6950 C CG  . TRP E 1 84  ? -27.781 61.621 -26.954 1.00 27.85  ? 65   TRP E CG  1 
ATOM   6951 C CD1 . TRP E 1 84  ? -28.723 61.932 -27.890 1.00 31.59  ? 65   TRP E CD1 1 
ATOM   6952 C CD2 . TRP E 1 84  ? -27.616 60.187 -27.014 1.00 29.40  ? 65   TRP E CD2 1 
ATOM   6953 N NE1 . TRP E 1 84  ? -29.166 60.786 -28.522 1.00 30.54  ? 65   TRP E NE1 1 
ATOM   6954 C CE2 . TRP E 1 84  ? -28.495 59.704 -28.011 1.00 29.75  ? 65   TRP E CE2 1 
ATOM   6955 C CE3 . TRP E 1 84  ? -26.813 59.267 -26.319 1.00 23.79  ? 65   TRP E CE3 1 
ATOM   6956 C CZ2 . TRP E 1 84  ? -28.596 58.340 -28.333 1.00 31.15  ? 65   TRP E CZ2 1 
ATOM   6957 C CZ3 . TRP E 1 84  ? -26.909 57.920 -26.640 1.00 21.06  ? 65   TRP E CZ3 1 
ATOM   6958 C CH2 . TRP E 1 84  ? -27.796 57.465 -27.640 1.00 26.54  ? 65   TRP E CH2 1 
ATOM   6959 N N   . ASN E 1 85  ? -29.313 64.580 -25.256 1.00 35.39  ? 66   ASN E N   1 
ATOM   6960 C CA  . ASN E 1 85  ? -30.653 65.111 -25.526 1.00 45.51  ? 66   ASN E CA  1 
ATOM   6961 C C   . ASN E 1 85  ? -31.183 64.543 -26.857 1.00 45.81  ? 66   ASN E C   1 
ATOM   6962 O O   . ASN E 1 85  ? -30.661 64.881 -27.924 1.00 46.16  ? 66   ASN E O   1 
ATOM   6963 C CB  . ASN E 1 85  ? -30.610 66.653 -25.568 1.00 43.08  ? 66   ASN E CB  1 
ATOM   6964 C CG  . ASN E 1 85  ? -31.995 67.297 -25.547 1.00 52.14  ? 66   ASN E CG  1 
ATOM   6965 O OD1 . ASN E 1 85  ? -33.004 66.666 -25.890 1.00 63.47  ? 66   ASN E OD1 1 
ATOM   6966 N ND2 . ASN E 1 85  ? -32.046 68.573 -25.155 1.00 49.22  ? 66   ASN E ND2 1 
ATOM   6967 N N   . SER E 1 86  ? -32.211 63.689 -26.802 1.00 47.09  ? 67   SER E N   1 
ATOM   6968 C CA  . SER E 1 86  ? -32.713 63.034 -28.022 1.00 53.12  ? 67   SER E CA  1 
ATOM   6969 C C   . SER E 1 86  ? -33.879 63.778 -28.678 1.00 58.49  ? 67   SER E C   1 
ATOM   6970 O O   . SER E 1 86  ? -34.689 63.171 -29.375 1.00 67.14  ? 67   SER E O   1 
ATOM   6971 C CB  . SER E 1 86  ? -33.105 61.573 -27.752 1.00 47.65  ? 67   SER E CB  1 
ATOM   6972 O OG  . SER E 1 86  ? -34.351 61.484 -27.085 1.00 54.35  ? 67   SER E OG  1 
ATOM   6973 N N   . SER E 1 87  ? -33.942 65.090 -28.465 1.00 63.37  ? 68   SER E N   1 
ATOM   6974 C CA  . SER E 1 87  ? -35.032 65.923 -28.969 1.00 65.54  ? 68   SER E CA  1 
ATOM   6975 C C   . SER E 1 87  ? -35.281 65.778 -30.484 1.00 64.50  ? 68   SER E C   1 
ATOM   6976 O O   . SER E 1 87  ? -36.336 65.299 -30.906 1.00 65.93  ? 68   SER E O   1 
ATOM   6977 C CB  . SER E 1 87  ? -34.786 67.385 -28.589 1.00 64.22  ? 68   SER E CB  1 
ATOM   6978 O OG  . SER E 1 87  ? -35.930 68.174 -28.844 1.00 77.56  ? 68   SER E OG  1 
ATOM   6979 N N   . HIS E 1 88  ? -34.319 66.193 -31.299 1.00 60.14  ? 69   HIS E N   1 
ATOM   6980 C CA  . HIS E 1 88  ? -34.426 65.988 -32.742 1.00 70.24  ? 69   HIS E CA  1 
ATOM   6981 C C   . HIS E 1 88  ? -33.269 65.117 -33.213 1.00 68.68  ? 69   HIS E C   1 
ATOM   6982 O O   . HIS E 1 88  ? -32.584 65.425 -34.194 1.00 60.49  ? 69   HIS E O   1 
ATOM   6983 C CB  . HIS E 1 88  ? -34.448 67.322 -33.487 1.00 77.18  ? 69   HIS E CB  1 
ATOM   6984 C CG  . HIS E 1 88  ? -35.620 68.183 -33.135 1.00 85.40  ? 69   HIS E CG  1 
ATOM   6985 N ND1 . HIS E 1 88  ? -36.898 67.926 -33.590 1.00 88.95  ? 69   HIS E ND1 1 
ATOM   6986 C CD2 . HIS E 1 88  ? -35.709 69.288 -32.360 1.00 86.43  ? 69   HIS E CD2 1 
ATOM   6987 C CE1 . HIS E 1 88  ? -37.722 68.842 -33.113 1.00 87.31  ? 69   HIS E CE1 1 
ATOM   6988 N NE2 . HIS E 1 88  ? -37.027 69.683 -32.369 1.00 93.38  ? 69   HIS E NE2 1 
ATOM   6989 N N   . SER E 1 89  ? -33.078 64.013 -32.498 1.00 64.54  ? 70   SER E N   1 
ATOM   6990 C CA  . SER E 1 89  ? -31.884 63.205 -32.622 1.00 49.52  ? 70   SER E CA  1 
ATOM   6991 C C   . SER E 1 89  ? -32.248 61.745 -32.530 1.00 46.57  ? 70   SER E C   1 
ATOM   6992 O O   . SER E 1 89  ? -33.344 61.405 -32.065 1.00 43.58  ? 70   SER E O   1 
ATOM   6993 C CB  . SER E 1 89  ? -30.928 63.558 -31.487 1.00 47.35  ? 70   SER E CB  1 
ATOM   6994 O OG  . SER E 1 89  ? -30.677 64.953 -31.460 1.00 60.99  ? 70   SER E OG  1 
ATOM   6995 N N   . PRO E 1 90  ? -31.330 60.868 -32.971 1.00 41.61  ? 71   PRO E N   1 
ATOM   6996 C CA  . PRO E 1 90  ? -31.541 59.431 -32.747 1.00 38.42  ? 71   PRO E CA  1 
ATOM   6997 C C   . PRO E 1 90  ? -31.638 59.142 -31.250 1.00 35.17  ? 71   PRO E C   1 
ATOM   6998 O O   . PRO E 1 90  ? -30.987 59.809 -30.442 1.00 38.27  ? 71   PRO E O   1 
ATOM   6999 C CB  . PRO E 1 90  ? -30.271 58.788 -33.326 1.00 38.29  ? 71   PRO E CB  1 
ATOM   7000 C CG  . PRO E 1 90  ? -29.719 59.799 -34.296 1.00 38.64  ? 71   PRO E CG  1 
ATOM   7001 C CD  . PRO E 1 90  ? -30.095 61.150 -33.733 1.00 37.18  ? 71   PRO E CD  1 
ATOM   7002 N N   . ASP E 1 91  ? -32.438 58.156 -30.877 1.00 34.26  ? 72   ASP E N   1 
ATOM   7003 C CA  . ASP E 1 91  ? -32.586 57.818 -29.468 1.00 42.85  ? 72   ASP E CA  1 
ATOM   7004 C C   . ASP E 1 91  ? -31.759 56.582 -29.092 1.00 37.94  ? 72   ASP E C   1 
ATOM   7005 O O   . ASP E 1 91  ? -31.770 56.146 -27.937 1.00 33.21  ? 72   ASP E O   1 
ATOM   7006 C CB  . ASP E 1 91  ? -34.067 57.611 -29.138 1.00 49.85  ? 72   ASP E CB  1 
ATOM   7007 C CG  . ASP E 1 91  ? -34.774 56.782 -30.189 1.00 54.47  ? 72   ASP E CG  1 
ATOM   7008 O OD1 . ASP E 1 91  ? -34.124 56.477 -31.221 1.00 52.30  ? 72   ASP E OD1 1 
ATOM   7009 O OD2 . ASP E 1 91  ? -35.968 56.442 -29.992 1.00 72.00  ? 72   ASP E OD2 1 
ATOM   7010 N N   . GLN E 1 92  ? -31.033 56.041 -30.070 1.00 37.14  ? 73   GLN E N   1 
ATOM   7011 C CA  . GLN E 1 92  ? -30.175 54.880 -29.849 1.00 35.87  ? 73   GLN E CA  1 
ATOM   7012 C C   . GLN E 1 92  ? -28.993 54.805 -30.834 1.00 31.70  ? 73   GLN E C   1 
ATOM   7013 O O   . GLN E 1 92  ? -29.077 55.301 -31.959 1.00 35.08  ? 73   GLN E O   1 
ATOM   7014 C CB  . GLN E 1 92  ? -31.004 53.621 -29.983 1.00 32.01  ? 73   GLN E CB  1 
ATOM   7015 C CG  . GLN E 1 92  ? -31.674 53.579 -31.319 1.00 45.91  ? 73   GLN E CG  1 
ATOM   7016 C CD  . GLN E 1 92  ? -32.286 52.252 -31.605 1.00 54.70  ? 73   GLN E CD  1 
ATOM   7017 O OE1 . GLN E 1 92  ? -32.891 51.632 -30.724 1.00 59.18  ? 73   GLN E OE1 1 
ATOM   7018 N NE2 . GLN E 1 92  ? -32.137 51.791 -32.844 1.00 60.19  ? 73   GLN E NE2 1 
ATOM   7019 N N   . VAL E 1 93  ? -27.898 54.182 -30.397 1.00 23.03  ? 74   VAL E N   1 
ATOM   7020 C CA  . VAL E 1 93  ? -26.748 53.919 -31.250 1.00 18.74  ? 74   VAL E CA  1 
ATOM   7021 C C   . VAL E 1 93  ? -26.107 52.593 -30.833 1.00 17.40  ? 74   VAL E C   1 
ATOM   7022 O O   . VAL E 1 93  ? -26.344 52.117 -29.717 1.00 14.87  ? 74   VAL E O   1 
ATOM   7023 C CB  . VAL E 1 93  ? -25.681 55.053 -31.181 1.00 20.21  ? 74   VAL E CB  1 
ATOM   7024 C CG1 . VAL E 1 93  ? -26.179 56.321 -31.833 1.00 27.23  ? 74   VAL E CG1 1 
ATOM   7025 C CG2 . VAL E 1 93  ? -25.286 55.328 -29.745 1.00 15.75  ? 74   VAL E CG2 1 
ATOM   7026 N N   . SER E 1 94  ? -25.304 52.006 -31.727 1.00 15.08  ? 75   SER E N   1 
ATOM   7027 C CA  . SER E 1 94  ? -24.520 50.822 -31.405 1.00 13.83  ? 75   SER E CA  1 
ATOM   7028 C C   . SER E 1 94  ? -23.080 51.231 -31.194 1.00 16.11  ? 75   SER E C   1 
ATOM   7029 O O   . SER E 1 94  ? -22.521 51.998 -31.979 1.00 17.46  ? 75   SER E O   1 
ATOM   7030 C CB  . SER E 1 94  ? -24.623 49.776 -32.508 1.00 20.25  ? 75   SER E CB  1 
ATOM   7031 O OG  . SER E 1 94  ? -25.868 49.100 -32.426 1.00 35.67  ? 75   SER E OG  1 
ATOM   7032 N N   . VAL E 1 95  ? -22.476 50.727 -30.125 1.00 15.83  ? 76   VAL E N   1 
ATOM   7033 C CA  . VAL E 1 95  ? -21.154 51.185 -29.715 1.00 13.17  ? 76   VAL E CA  1 
ATOM   7034 C C   . VAL E 1 95  ? -20.242 49.990 -29.471 1.00 13.48  ? 76   VAL E C   1 
ATOM   7035 O O   . VAL E 1 95  ? -20.612 49.049 -28.763 1.00 13.98  ? 76   VAL E O   1 
ATOM   7036 C CB  . VAL E 1 95  ? -21.249 51.993 -28.415 1.00 11.11  ? 76   VAL E CB  1 
ATOM   7037 C CG1 . VAL E 1 95  ? -19.860 52.453 -27.972 1.00 11.36  ? 76   VAL E CG1 1 
ATOM   7038 C CG2 . VAL E 1 95  ? -22.221 53.144 -28.559 1.00 11.93  ? 76   VAL E CG2 1 
ATOM   7039 N N   . PRO E 1 96  ? -19.033 50.024 -30.036 1.00 13.65  ? 77   PRO E N   1 
ATOM   7040 C CA  . PRO E 1 96  ? -18.092 48.926 -29.748 1.00 15.26  ? 77   PRO E CA  1 
ATOM   7041 C C   . PRO E 1 96  ? -17.796 48.890 -28.253 1.00 15.47  ? 77   PRO E C   1 
ATOM   7042 O O   . PRO E 1 96  ? -17.536 49.960 -27.689 1.00 16.42  ? 77   PRO E O   1 
ATOM   7043 C CB  . PRO E 1 96  ? -16.828 49.328 -30.523 1.00 11.56  ? 77   PRO E CB  1 
ATOM   7044 C CG  . PRO E 1 96  ? -17.305 50.306 -31.550 1.00 12.03  ? 77   PRO E CG  1 
ATOM   7045 C CD  . PRO E 1 96  ? -18.447 51.055 -30.907 1.00 13.80  ? 77   PRO E CD  1 
ATOM   7046 N N   . ILE E 1 97  ? -17.834 47.709 -27.625 1.00 17.71  ? 78   ILE E N   1 
ATOM   7047 C CA  . ILE E 1 97  ? -17.675 47.618 -26.160 1.00 16.34  ? 78   ILE E CA  1 
ATOM   7048 C C   . ILE E 1 97  ? -16.314 48.110 -25.674 1.00 15.24  ? 78   ILE E C   1 
ATOM   7049 O O   . ILE E 1 97  ? -16.146 48.432 -24.504 1.00 18.68  ? 78   ILE E O   1 
ATOM   7050 C CB  . ILE E 1 97  ? -17.921 46.214 -25.599 1.00 13.26  ? 78   ILE E CB  1 
ATOM   7051 C CG1 . ILE E 1 97  ? -16.930 45.215 -26.200 1.00 16.62  ? 78   ILE E CG1 1 
ATOM   7052 C CG2 . ILE E 1 97  ? -19.381 45.792 -25.789 1.00 12.49  ? 78   ILE E CG2 1 
ATOM   7053 C CD1 . ILE E 1 97  ? -16.939 43.858 -25.480 1.00 18.64  ? 78   ILE E CD1 1 
ATOM   7054 N N   . SER E 1 98  ? -15.341 48.170 -26.568 1.00 13.15  ? 79   SER E N   1 
ATOM   7055 C CA  . SER E 1 98  ? -14.057 48.727 -26.194 1.00 14.97  ? 79   SER E CA  1 
ATOM   7056 C C   . SER E 1 98  ? -14.148 50.211 -25.770 1.00 20.95  ? 79   SER E C   1 
ATOM   7057 O O   . SER E 1 98  ? -13.271 50.703 -25.060 1.00 21.50  ? 79   SER E O   1 
ATOM   7058 C CB  . SER E 1 98  ? -13.046 48.530 -27.320 1.00 21.50  ? 79   SER E CB  1 
ATOM   7059 O OG  . SER E 1 98  ? -13.349 49.350 -28.439 1.00 31.87  ? 79   SER E OG  1 
ATOM   7060 N N   . SER E 1 99  ? -15.208 50.914 -26.179 1.00 18.40  ? 80   SER E N   1 
ATOM   7061 C CA  . SER E 1 99  ? -15.385 52.324 -25.800 1.00 14.30  ? 80   SER E CA  1 
ATOM   7062 C C   . SER E 1 99  ? -16.361 52.552 -24.654 1.00 14.88  ? 80   SER E C   1 
ATOM   7063 O O   . SER E 1 99  ? -16.867 53.640 -24.521 1.00 19.44  ? 80   SER E O   1 
ATOM   7064 C CB  . SER E 1 99  ? -15.881 53.147 -26.990 1.00 15.06  ? 80   SER E CB  1 
ATOM   7065 O OG  . SER E 1 99  ? -15.142 52.843 -28.154 1.00 26.95  ? 80   SER E OG  1 
ATOM   7066 N N   . LEU E 1 100 ? -16.650 51.537 -23.851 1.00 17.00  ? 81   LEU E N   1 
ATOM   7067 C CA  . LEU E 1 100 ? -17.634 51.652 -22.773 1.00 16.71  ? 81   LEU E CA  1 
ATOM   7068 C C   . LEU E 1 100 ? -17.151 50.938 -21.541 1.00 16.48  ? 81   LEU E C   1 
ATOM   7069 O O   . LEU E 1 100 ? -16.444 49.928 -21.642 1.00 17.66  ? 81   LEU E O   1 
ATOM   7070 C CB  . LEU E 1 100 ? -18.903 50.902 -23.148 1.00 21.99  ? 81   LEU E CB  1 
ATOM   7071 C CG  . LEU E 1 100 ? -19.756 51.435 -24.263 1.00 20.44  ? 81   LEU E CG  1 
ATOM   7072 C CD1 . LEU E 1 100 ? -20.955 50.550 -24.347 1.00 16.58  ? 81   LEU E CD1 1 
ATOM   7073 C CD2 . LEU E 1 100 ? -20.147 52.856 -23.904 1.00 26.68  ? 81   LEU E CD2 1 
ATOM   7074 N N   . TRP E 1 101 ? -17.577 51.396 -20.373 1.00 15.19  ? 82   TRP E N   1 
ATOM   7075 C CA  . TRP E 1 101 ? -17.387 50.563 -19.197 1.00 15.06  ? 82   TRP E CA  1 
ATOM   7076 C C   . TRP E 1 101 ? -18.323 49.376 -19.326 1.00 16.80  ? 82   TRP E C   1 
ATOM   7077 O O   . TRP E 1 101 ? -19.443 49.505 -19.810 1.00 15.52  ? 82   TRP E O   1 
ATOM   7078 C CB  . TRP E 1 101 ? -17.685 51.313 -17.908 1.00 15.12  ? 82   TRP E CB  1 
ATOM   7079 C CG  . TRP E 1 101 ? -17.570 50.420 -16.728 1.00 13.87  ? 82   TRP E CG  1 
ATOM   7080 C CD1 . TRP E 1 101 ? -16.441 50.142 -16.014 1.00 15.47  ? 82   TRP E CD1 1 
ATOM   7081 C CD2 . TRP E 1 101 ? -18.620 49.680 -16.120 1.00 13.73  ? 82   TRP E CD2 1 
ATOM   7082 N NE1 . TRP E 1 101 ? -16.729 49.282 -14.989 1.00 15.06  ? 82   TRP E NE1 1 
ATOM   7083 C CE2 . TRP E 1 101 ? -18.070 48.975 -15.032 1.00 16.32  ? 82   TRP E CE2 1 
ATOM   7084 C CE3 . TRP E 1 101 ? -19.992 49.544 -16.385 1.00 15.22  ? 82   TRP E CE3 1 
ATOM   7085 C CZ2 . TRP E 1 101 ? -18.830 48.131 -14.207 1.00 16.96  ? 82   TRP E CZ2 1 
ATOM   7086 C CZ3 . TRP E 1 101 ? -20.757 48.711 -15.566 1.00 14.49  ? 82   TRP E CZ3 1 
ATOM   7087 C CH2 . TRP E 1 101 ? -20.169 48.012 -14.490 1.00 15.86  ? 82   TRP E CH2 1 
ATOM   7088 N N   . VAL E 1 102 ? -17.850 48.216 -18.891 1.00 21.37  ? 83   VAL E N   1 
ATOM   7089 C CA  . VAL E 1 102 ? -18.610 46.968 -18.962 1.00 16.35  ? 83   VAL E CA  1 
ATOM   7090 C C   . VAL E 1 102 ? -18.376 46.225 -17.644 1.00 18.93  ? 83   VAL E C   1 
ATOM   7091 O O   . VAL E 1 102 ? -17.246 46.204 -17.134 1.00 17.48  ? 83   VAL E O   1 
ATOM   7092 C CB  . VAL E 1 102 ? -18.140 46.118 -20.159 1.00 12.16  ? 83   VAL E CB  1 
ATOM   7093 C CG1 . VAL E 1 102 ? -18.403 44.647 -19.912 1.00 25.92  ? 83   VAL E CG1 1 
ATOM   7094 C CG2 . VAL E 1 102 ? -18.810 46.577 -21.422 1.00 11.05  ? 83   VAL E CG2 1 
ATOM   7095 N N   . PRO E 1 103 ? -19.439 45.630 -17.072 1.00 17.40  ? 84   PRO E N   1 
ATOM   7096 C CA  . PRO E 1 103 ? -19.267 44.874 -15.819 1.00 16.16  ? 84   PRO E CA  1 
ATOM   7097 C C   . PRO E 1 103 ? -18.359 43.629 -15.990 1.00 18.06  ? 84   PRO E C   1 
ATOM   7098 O O   . PRO E 1 103 ? -18.420 42.957 -17.033 1.00 18.68  ? 84   PRO E O   1 
ATOM   7099 C CB  . PRO E 1 103 ? -20.701 44.474 -15.445 1.00 15.29  ? 84   PRO E CB  1 
ATOM   7100 C CG  . PRO E 1 103 ? -21.458 44.493 -16.744 1.00 16.73  ? 84   PRO E CG  1 
ATOM   7101 C CD  . PRO E 1 103 ? -20.819 45.576 -17.592 1.00 16.74  ? 84   PRO E CD  1 
ATOM   7102 N N   . ASP E 1 104 ? -17.526 43.350 -14.981 1.00 18.03  ? 85   ASP E N   1 
ATOM   7103 C CA  . ASP E 1 104 ? -16.553 42.243 -15.017 1.00 19.02  ? 85   ASP E CA  1 
ATOM   7104 C C   . ASP E 1 104 ? -17.148 40.915 -14.549 1.00 22.44  ? 85   ASP E C   1 
ATOM   7105 O O   . ASP E 1 104 ? -16.660 40.295 -13.595 1.00 22.40  ? 85   ASP E O   1 
ATOM   7106 C CB  . ASP E 1 104 ? -15.288 42.570 -14.192 1.00 18.30  ? 85   ASP E CB  1 
ATOM   7107 C CG  . ASP E 1 104 ? -15.587 42.832 -12.699 1.00 22.03  ? 85   ASP E CG  1 
ATOM   7108 O OD1 . ASP E 1 104 ? -16.701 43.281 -12.342 1.00 21.58  ? 85   ASP E OD1 1 
ATOM   7109 O OD2 . ASP E 1 104 ? -14.689 42.593 -11.869 1.00 23.72  ? 85   ASP E OD2 1 
ATOM   7110 N N   . LEU E 1 105 ? -18.200 40.470 -15.232 1.00 22.36  ? 86   LEU E N   1 
ATOM   7111 C CA  . LEU E 1 105 ? -18.868 39.230 -14.874 1.00 17.15  ? 86   LEU E CA  1 
ATOM   7112 C C   . LEU E 1 105 ? -18.031 38.021 -15.292 1.00 16.22  ? 86   LEU E C   1 
ATOM   7113 O O   . LEU E 1 105 ? -17.312 38.065 -16.293 1.00 15.30  ? 86   LEU E O   1 
ATOM   7114 C CB  . LEU E 1 105 ? -20.245 39.193 -15.521 1.00 18.07  ? 86   LEU E CB  1 
ATOM   7115 C CG  . LEU E 1 105 ? -21.129 40.387 -15.138 1.00 17.38  ? 86   LEU E CG  1 
ATOM   7116 C CD1 . LEU E 1 105 ? -22.463 40.374 -15.911 1.00 16.84  ? 86   LEU E CD1 1 
ATOM   7117 C CD2 . LEU E 1 105 ? -21.392 40.422 -13.624 1.00 16.14  ? 86   LEU E CD2 1 
ATOM   7118 N N   . ALA E 1 106 ? -18.102 36.958 -14.494 1.00 20.49  ? 87   ALA E N   1 
ATOM   7119 C CA  . ALA E 1 106 ? -17.439 35.680 -14.808 1.00 17.67  ? 87   ALA E CA  1 
ATOM   7120 C C   . ALA E 1 106 ? -18.300 34.526 -14.318 1.00 18.62  ? 87   ALA E C   1 
ATOM   7121 O O   . ALA E 1 106 ? -19.061 34.658 -13.355 1.00 21.41  ? 87   ALA E O   1 
ATOM   7122 C CB  . ALA E 1 106 ? -16.049 35.614 -14.178 1.00 13.22  ? 87   ALA E CB  1 
ATOM   7123 N N   . ALA E 1 107 ? -18.182 33.393 -14.992 1.00 16.65  ? 88   ALA E N   1 
ATOM   7124 C CA  . ALA E 1 107 ? -18.836 32.166 -14.553 1.00 16.24  ? 88   ALA E CA  1 
ATOM   7125 C C   . ALA E 1 107 ? -17.901 31.361 -13.608 1.00 17.05  ? 88   ALA E C   1 
ATOM   7126 O O   . ALA E 1 107 ? -16.844 30.849 -14.025 1.00 14.66  ? 88   ALA E O   1 
ATOM   7127 C CB  . ALA E 1 107 ? -19.245 31.347 -15.770 1.00 13.64  ? 88   ALA E CB  1 
ATOM   7128 N N   . TYR E 1 108 ? -18.289 31.254 -12.338 1.00 17.15  ? 89   TYR E N   1 
ATOM   7129 C CA  . TYR E 1 108 ? -17.427 30.643 -11.327 1.00 13.15  ? 89   TYR E CA  1 
ATOM   7130 C C   . TYR E 1 108 ? -17.111 29.166 -11.606 1.00 11.97  ? 89   TYR E C   1 
ATOM   7131 O O   . TYR E 1 108 ? -16.053 28.663 -11.248 1.00 13.03  ? 89   TYR E O   1 
ATOM   7132 C CB  . TYR E 1 108 ? -18.044 30.802 -9.945  1.00 14.87  ? 89   TYR E CB  1 
ATOM   7133 C CG  . TYR E 1 108 ? -17.828 32.155 -9.330  1.00 21.11  ? 89   TYR E CG  1 
ATOM   7134 C CD1 . TYR E 1 108 ? -18.520 33.270 -9.782  1.00 28.19  ? 89   TYR E CD1 1 
ATOM   7135 C CD2 . TYR E 1 108 ? -16.939 32.321 -8.285  1.00 26.71  ? 89   TYR E CD2 1 
ATOM   7136 C CE1 . TYR E 1 108 ? -18.322 34.520 -9.209  1.00 27.94  ? 89   TYR E CE1 1 
ATOM   7137 C CE2 . TYR E 1 108 ? -16.725 33.559 -7.706  1.00 26.30  ? 89   TYR E CE2 1 
ATOM   7138 C CZ  . TYR E 1 108 ? -17.420 34.655 -8.169  1.00 32.03  ? 89   TYR E CZ  1 
ATOM   7139 O OH  . TYR E 1 108 ? -17.217 35.890 -7.587  1.00 36.81  ? 89   TYR E OH  1 
ATOM   7140 N N   . ASN E 1 109 ? -18.020 28.460 -12.252 1.00 16.89  ? 90   ASN E N   1 
ATOM   7141 C CA  . ASN E 1 109 ? -17.785 27.040 -12.529 1.00 20.54  ? 90   ASN E CA  1 
ATOM   7142 C C   . ASN E 1 109 ? -17.517 26.763 -14.008 1.00 22.01  ? 90   ASN E C   1 
ATOM   7143 O O   . ASN E 1 109 ? -17.748 25.659 -14.507 1.00 22.77  ? 90   ASN E O   1 
ATOM   7144 C CB  . ASN E 1 109 ? -18.924 26.153 -11.985 1.00 16.53  ? 90   ASN E CB  1 
ATOM   7145 C CG  . ASN E 1 109 ? -20.290 26.516 -12.556 1.00 19.68  ? 90   ASN E CG  1 
ATOM   7146 O OD1 . ASN E 1 109 ? -20.703 27.693 -12.583 1.00 21.99  ? 90   ASN E OD1 1 
ATOM   7147 N ND2 . ASN E 1 109 ? -21.004 25.499 -13.015 1.00 22.38  ? 90   ASN E ND2 1 
ATOM   7148 N N   . ALA E 1 110 ? -17.041 27.784 -14.718 1.00 21.27  ? 91   ALA E N   1 
ATOM   7149 C CA  . ALA E 1 110 ? -16.599 27.589 -16.102 1.00 24.27  ? 91   ALA E CA  1 
ATOM   7150 C C   . ALA E 1 110 ? -15.233 26.893 -16.098 1.00 21.88  ? 91   ALA E C   1 
ATOM   7151 O O   . ALA E 1 110 ? -14.433 27.074 -15.170 1.00 29.37  ? 91   ALA E O   1 
ATOM   7152 C CB  . ALA E 1 110 ? -16.541 28.908 -16.838 1.00 18.58  ? 91   ALA E CB  1 
ATOM   7153 N N   . ILE E 1 111 ? -14.965 26.068 -17.100 1.00 22.26  ? 92   ILE E N   1 
ATOM   7154 C CA  . ILE E 1 111 ? -13.665 25.394 -17.148 1.00 26.42  ? 92   ILE E CA  1 
ATOM   7155 C C   . ILE E 1 111 ? -12.946 25.711 -18.451 1.00 20.92  ? 92   ILE E C   1 
ATOM   7156 O O   . ILE E 1 111 ? -11.955 25.084 -18.805 1.00 26.62  ? 92   ILE E O   1 
ATOM   7157 C CB  . ILE E 1 111 ? -13.760 23.855 -16.909 1.00 24.70  ? 92   ILE E CB  1 
ATOM   7158 C CG1 . ILE E 1 111 ? -14.783 23.216 -17.840 1.00 25.49  ? 92   ILE E CG1 1 
ATOM   7159 C CG2 . ILE E 1 111 ? -14.118 23.550 -15.462 1.00 23.51  ? 92   ILE E CG2 1 
ATOM   7160 C CD1 . ILE E 1 111 ? -14.836 21.713 -17.715 1.00 29.60  ? 92   ILE E CD1 1 
ATOM   7161 N N   . SER E 1 112 ? -13.472 26.691 -19.166 1.00 18.38  ? 93   SER E N   1 
ATOM   7162 C CA  . SER E 1 112 ? -12.866 27.173 -20.399 1.00 20.05  ? 93   SER E CA  1 
ATOM   7163 C C   . SER E 1 112 ? -13.219 28.646 -20.466 1.00 22.93  ? 93   SER E C   1 
ATOM   7164 O O   . SER E 1 112 ? -14.200 29.078 -19.851 1.00 21.51  ? 93   SER E O   1 
ATOM   7165 C CB  . SER E 1 112 ? -13.443 26.442 -21.611 1.00 21.05  ? 93   SER E CB  1 
ATOM   7166 O OG  . SER E 1 112 ? -14.810 26.770 -21.832 1.00 21.96  ? 93   SER E OG  1 
ATOM   7167 N N   . LYS E 1 113 ? -12.452 29.430 -21.212 1.00 22.82  ? 94   LYS E N   1 
ATOM   7168 C CA  . LYS E 1 113 ? -12.821 30.843 -21.339 1.00 22.95  ? 94   LYS E CA  1 
ATOM   7169 C C   . LYS E 1 113 ? -14.005 31.039 -22.290 1.00 20.00  ? 94   LYS E C   1 
ATOM   7170 O O   . LYS E 1 113 ? -14.240 30.211 -23.177 1.00 22.12  ? 94   LYS E O   1 
ATOM   7171 C CB  . LYS E 1 113 ? -11.618 31.710 -21.722 1.00 24.78  ? 94   LYS E CB  1 
ATOM   7172 C CG  . LYS E 1 113 ? -11.004 31.416 -23.073 1.00 29.50  ? 94   LYS E CG  1 
ATOM   7173 C CD  . LYS E 1 113 ? -9.676  32.180 -23.203 1.00 43.71  ? 94   LYS E CD  1 
ATOM   7174 C CE  . LYS E 1 113 ? -9.821  33.671 -22.781 1.00 45.47  ? 94   LYS E CE  1 
ATOM   7175 N NZ  . LYS E 1 113 ? -8.629  34.509 -23.135 1.00 39.55  ? 94   LYS E NZ  1 
ATOM   7176 N N   . PRO E 1 114 ? -14.773 32.122 -22.093 1.00 19.78  ? 95   PRO E N   1 
ATOM   7177 C CA  . PRO E 1 114 ? -15.927 32.321 -22.972 1.00 22.43  ? 95   PRO E CA  1 
ATOM   7178 C C   . PRO E 1 114 ? -15.469 32.487 -24.417 1.00 19.03  ? 95   PRO E C   1 
ATOM   7179 O O   . PRO E 1 114 ? -14.532 33.237 -24.669 1.00 16.83  ? 95   PRO E O   1 
ATOM   7180 C CB  . PRO E 1 114 ? -16.524 33.642 -22.471 1.00 19.95  ? 95   PRO E CB  1 
ATOM   7181 C CG  . PRO E 1 114 ? -15.964 33.850 -21.123 1.00 16.13  ? 95   PRO E CG  1 
ATOM   7182 C CD  . PRO E 1 114 ? -14.622 33.220 -21.125 1.00 18.47  ? 95   PRO E CD  1 
ATOM   7183 N N   . GLU E 1 115 ? -16.105 31.776 -25.340 1.00 21.46  ? 96   GLU E N   1 
ATOM   7184 C CA  . GLU E 1 115 ? -15.863 31.969 -26.768 1.00 23.34  ? 96   GLU E CA  1 
ATOM   7185 C C   . GLU E 1 115 ? -17.002 32.838 -27.305 1.00 23.02  ? 96   GLU E C   1 
ATOM   7186 O O   . GLU E 1 115 ? -18.159 32.376 -27.397 1.00 20.43  ? 96   GLU E O   1 
ATOM   7187 C CB  . GLU E 1 115 ? -15.850 30.616 -27.480 1.00 25.66  ? 96   GLU E CB  1 
ATOM   7188 C CG  . GLU E 1 115 ? -15.442 30.646 -28.950 1.00 39.53  ? 96   GLU E CG  1 
ATOM   7189 C CD  . GLU E 1 115 ? -15.414 29.230 -29.561 1.00 60.91  ? 96   GLU E CD  1 
ATOM   7190 O OE1 . GLU E 1 115 ? -15.390 28.258 -28.754 1.00 58.11  ? 96   GLU E OE1 1 
ATOM   7191 O OE2 . GLU E 1 115 ? -15.427 29.089 -30.828 1.00 48.97  ? 96   GLU E OE2 1 
ATOM   7192 N N   . VAL E 1 116 ? -16.694 34.095 -27.639 1.00 17.61  ? 97   VAL E N   1 
ATOM   7193 C CA  . VAL E 1 116 ? -17.740 35.025 -28.093 1.00 18.06  ? 97   VAL E CA  1 
ATOM   7194 C C   . VAL E 1 116 ? -18.041 34.874 -29.582 1.00 17.13  ? 97   VAL E C   1 
ATOM   7195 O O   . VAL E 1 116 ? -17.187 35.134 -30.422 1.00 24.70  ? 97   VAL E O   1 
ATOM   7196 C CB  . VAL E 1 116 ? -17.392 36.479 -27.738 1.00 15.47  ? 97   VAL E CB  1 
ATOM   7197 C CG1 . VAL E 1 116 ? -18.499 37.411 -28.157 1.00 19.36  ? 97   VAL E CG1 1 
ATOM   7198 C CG2 . VAL E 1 116 ? -17.184 36.585 -26.267 1.00 8.06   ? 97   VAL E CG2 1 
ATOM   7199 N N   . LEU E 1 117 ? -19.263 34.463 -29.897 1.00 14.46  ? 98   LEU E N   1 
ATOM   7200 C CA  . LEU E 1 117 ? -19.637 34.115 -31.265 1.00 16.91  ? 98   LEU E CA  1 
ATOM   7201 C C   . LEU E 1 117 ? -20.049 35.308 -32.133 1.00 19.52  ? 98   LEU E C   1 
ATOM   7202 O O   . LEU E 1 117 ? -19.944 35.254 -33.360 1.00 20.25  ? 98   LEU E O   1 
ATOM   7203 C CB  . LEU E 1 117 ? -20.761 33.074 -31.238 1.00 16.99  ? 98   LEU E CB  1 
ATOM   7204 C CG  . LEU E 1 117 ? -20.422 31.750 -30.534 1.00 19.83  ? 98   LEU E CG  1 
ATOM   7205 C CD1 . LEU E 1 117 ? -21.588 30.769 -30.558 1.00 17.90  ? 98   LEU E CD1 1 
ATOM   7206 C CD2 . LEU E 1 117 ? -19.154 31.100 -31.096 1.00 22.27  ? 98   LEU E CD2 1 
ATOM   7207 N N   . THR E 1 118 ? -20.503 36.383 -31.490 1.00 16.54  ? 99   THR E N   1 
ATOM   7208 C CA  . THR E 1 118 ? -21.142 37.498 -32.194 1.00 17.73  ? 99   THR E CA  1 
ATOM   7209 C C   . THR E 1 118 ? -20.297 38.753 -32.163 1.00 20.57  ? 99   THR E C   1 
ATOM   7210 O O   . THR E 1 118 ? -19.364 38.827 -31.368 1.00 28.36  ? 99   THR E O   1 
ATOM   7211 C CB  . THR E 1 118 ? -22.477 37.800 -31.554 1.00 22.21  ? 99   THR E CB  1 
ATOM   7212 O OG1 . THR E 1 118 ? -22.293 37.938 -30.132 1.00 29.34  ? 99   THR E OG1 1 
ATOM   7213 C CG2 . THR E 1 118 ? -23.454 36.661 -31.852 1.00 19.34  ? 99   THR E CG2 1 
ATOM   7214 N N   . PRO E 1 119 ? -20.606 39.736 -33.031 1.00 17.36  ? 100  PRO E N   1 
ATOM   7215 C CA  . PRO E 1 119 ? -19.956 41.060 -33.011 1.00 26.23  ? 100  PRO E CA  1 
ATOM   7216 C C   . PRO E 1 119 ? -19.985 41.680 -31.617 1.00 25.52  ? 100  PRO E C   1 
ATOM   7217 O O   . PRO E 1 119 ? -21.002 41.540 -30.931 1.00 28.71  ? 100  PRO E O   1 
ATOM   7218 C CB  . PRO E 1 119 ? -20.840 41.893 -33.938 1.00 22.61  ? 100  PRO E CB  1 
ATOM   7219 C CG  . PRO E 1 119 ? -21.334 40.888 -34.952 1.00 25.21  ? 100  PRO E CG  1 
ATOM   7220 C CD  . PRO E 1 119 ? -21.493 39.578 -34.197 1.00 22.25  ? 100  PRO E CD  1 
ATOM   7221 N N   . GLN E 1 120 ? -18.906 42.333 -31.194 1.00 18.52  ? 101  GLN E N   1 
ATOM   7222 C CA  . GLN E 1 120 ? -18.877 42.856 -29.834 1.00 22.14  ? 101  GLN E CA  1 
ATOM   7223 C C   . GLN E 1 120 ? -19.388 44.310 -29.685 1.00 19.04  ? 101  GLN E C   1 
ATOM   7224 O O   . GLN E 1 120 ? -18.653 45.211 -29.288 1.00 15.98  ? 101  GLN E O   1 
ATOM   7225 C CB  . GLN E 1 120 ? -17.507 42.626 -29.215 1.00 19.06  ? 101  GLN E CB  1 
ATOM   7226 C CG  . GLN E 1 120 ? -17.269 41.156 -28.910 1.00 24.91  ? 101  GLN E CG  1 
ATOM   7227 C CD  . GLN E 1 120 ? -15.856 40.846 -28.417 1.00 33.53  ? 101  GLN E CD  1 
ATOM   7228 O OE1 . GLN E 1 120 ? -15.288 41.595 -27.623 1.00 53.53  ? 101  GLN E OE1 1 
ATOM   7229 N NE2 . GLN E 1 120 ? -15.281 39.734 -28.895 1.00 29.74  ? 101  GLN E NE2 1 
ATOM   7230 N N   . LEU E 1 121 ? -20.670 44.501 -30.002 1.00 17.81  ? 102  LEU E N   1 
ATOM   7231 C CA  . LEU E 1 121 ? -21.331 45.799 -29.921 1.00 14.58  ? 102  LEU E CA  1 
ATOM   7232 C C   . LEU E 1 121 ? -22.382 45.848 -28.813 1.00 15.57  ? 102  LEU E C   1 
ATOM   7233 O O   . LEU E 1 121 ? -23.052 44.847 -28.543 1.00 19.56  ? 102  LEU E O   1 
ATOM   7234 C CB  . LEU E 1 121 ? -22.008 46.124 -31.247 1.00 13.39  ? 102  LEU E CB  1 
ATOM   7235 C CG  . LEU E 1 121 ? -21.058 46.143 -32.441 1.00 15.24  ? 102  LEU E CG  1 
ATOM   7236 C CD1 . LEU E 1 121 ? -21.799 46.440 -33.738 1.00 16.89  ? 102  LEU E CD1 1 
ATOM   7237 C CD2 . LEU E 1 121 ? -19.971 47.160 -32.199 1.00 13.65  ? 102  LEU E CD2 1 
ATOM   7238 N N   . ALA E 1 122 ? -22.521 47.012 -28.176 1.00 15.23  ? 103  ALA E N   1 
ATOM   7239 C CA  . ALA E 1 122 ? -23.549 47.229 -27.157 1.00 16.15  ? 103  ALA E CA  1 
ATOM   7240 C C   . ALA E 1 122 ? -24.583 48.207 -27.683 1.00 13.85  ? 103  ALA E C   1 
ATOM   7241 O O   . ALA E 1 122 ? -24.282 49.063 -28.508 1.00 16.77  ? 103  ALA E O   1 
ATOM   7242 C CB  . ALA E 1 122 ? -22.937 47.755 -25.861 1.00 14.84  ? 103  ALA E CB  1 
ATOM   7243 N N   . HIS E 1 123 ? -25.803 48.079 -27.190 1.00 12.57  ? 104  HIS E N   1 
ATOM   7244 C CA  . HIS E 1 123 ? -26.886 48.963 -27.571 1.00 15.95  ? 104  HIS E CA  1 
ATOM   7245 C C   . HIS E 1 123 ? -26.988 50.069 -26.523 1.00 23.58  ? 104  HIS E C   1 
ATOM   7246 O O   . HIS E 1 123 ? -27.039 49.782 -25.317 1.00 25.78  ? 104  HIS E O   1 
ATOM   7247 C CB  . HIS E 1 123 ? -28.171 48.157 -27.616 1.00 20.20  ? 104  HIS E CB  1 
ATOM   7248 C CG  . HIS E 1 123 ? -29.302 48.850 -28.303 1.00 22.82  ? 104  HIS E CG  1 
ATOM   7249 N ND1 . HIS E 1 123 ? -30.369 49.384 -27.613 1.00 26.04  ? 104  HIS E ND1 1 
ATOM   7250 C CD2 . HIS E 1 123 ? -29.557 49.054 -29.613 1.00 26.49  ? 104  HIS E CD2 1 
ATOM   7251 C CE1 . HIS E 1 123 ? -31.222 49.914 -28.471 1.00 30.01  ? 104  HIS E CE1 1 
ATOM   7252 N NE2 . HIS E 1 123 ? -30.755 49.728 -29.690 1.00 34.99  ? 104  HIS E NE2 1 
ATOM   7253 N N   . VAL E 1 124 ? -26.998 51.328 -26.965 1.00 19.27  ? 105  VAL E N   1 
ATOM   7254 C CA  . VAL E 1 124 ? -27.079 52.453 -26.038 1.00 16.99  ? 105  VAL E CA  1 
ATOM   7255 C C   . VAL E 1 124 ? -28.267 53.340 -26.386 1.00 22.00  ? 105  VAL E C   1 
ATOM   7256 O O   . VAL E 1 124 ? -28.417 53.782 -27.520 1.00 22.55  ? 105  VAL E O   1 
ATOM   7257 C CB  . VAL E 1 124 ? -25.797 53.338 -26.070 1.00 20.96  ? 105  VAL E CB  1 
ATOM   7258 C CG1 . VAL E 1 124 ? -25.818 54.405 -24.935 1.00 16.45  ? 105  VAL E CG1 1 
ATOM   7259 C CG2 . VAL E 1 124 ? -24.538 52.505 -25.996 1.00 18.32  ? 105  VAL E CG2 1 
ATOM   7260 N N   . VAL E 1 125 ? -29.095 53.617 -25.390 1.00 24.51  ? 106  VAL E N   1 
ATOM   7261 C CA  . VAL E 1 125 ? -30.274 54.462 -25.551 1.00 24.27  ? 106  VAL E CA  1 
ATOM   7262 C C   . VAL E 1 125 ? -29.952 55.834 -24.969 1.00 26.26  ? 106  VAL E C   1 
ATOM   7263 O O   . VAL E 1 125 ? -29.140 55.924 -24.048 1.00 31.12  ? 106  VAL E O   1 
ATOM   7264 C CB  . VAL E 1 125 ? -31.475 53.822 -24.817 1.00 24.05  ? 106  VAL E CB  1 
ATOM   7265 C CG1 . VAL E 1 125 ? -32.653 54.767 -24.763 1.00 28.24  ? 106  VAL E CG1 1 
ATOM   7266 C CG2 . VAL E 1 125 ? -31.861 52.511 -25.496 1.00 20.69  ? 106  VAL E CG2 1 
ATOM   7267 N N   . SER E 1 126 ? -30.569 56.893 -25.493 1.00 27.05  ? 107  SER E N   1 
ATOM   7268 C CA  . SER E 1 126 ? -30.223 58.265 -25.085 1.00 31.91  ? 107  SER E CA  1 
ATOM   7269 C C   . SER E 1 126 ? -30.276 58.550 -23.578 1.00 27.94  ? 107  SER E C   1 
ATOM   7270 O O   . SER E 1 126 ? -29.595 59.462 -23.103 1.00 25.70  ? 107  SER E O   1 
ATOM   7271 C CB  . SER E 1 126 ? -31.067 59.293 -25.836 1.00 31.19  ? 107  SER E CB  1 
ATOM   7272 O OG  . SER E 1 126 ? -32.436 59.013 -25.660 1.00 45.08  ? 107  SER E OG  1 
ATOM   7273 N N   . ASP E 1 127 ? -31.070 57.787 -22.830 1.00 23.20  ? 108  ASP E N   1 
ATOM   7274 C CA  . ASP E 1 127 ? -31.116 58.002 -21.384 1.00 25.99  ? 108  ASP E CA  1 
ATOM   7275 C C   . ASP E 1 127 ? -29.873 57.486 -20.633 1.00 27.95  ? 108  ASP E C   1 
ATOM   7276 O O   . ASP E 1 127 ? -29.646 57.833 -19.474 1.00 32.28  ? 108  ASP E O   1 
ATOM   7277 C CB  . ASP E 1 127 ? -32.414 57.447 -20.764 1.00 27.64  ? 108  ASP E CB  1 
ATOM   7278 C CG  . ASP E 1 127 ? -32.582 55.942 -20.963 1.00 39.88  ? 108  ASP E CG  1 
ATOM   7279 O OD1 . ASP E 1 127 ? -31.606 55.263 -21.365 1.00 45.91  ? 108  ASP E OD1 1 
ATOM   7280 O OD2 . ASP E 1 127 ? -33.700 55.428 -20.699 1.00 45.81  ? 108  ASP E OD2 1 
ATOM   7281 N N   . GLY E 1 128 ? -29.070 56.662 -21.299 1.00 28.18  ? 109  GLY E N   1 
ATOM   7282 C CA  . GLY E 1 128 ? -27.894 56.082 -20.681 1.00 26.15  ? 109  GLY E CA  1 
ATOM   7283 C C   . GLY E 1 128 ? -28.013 54.590 -20.414 1.00 25.95  ? 109  GLY E C   1 
ATOM   7284 O O   . GLY E 1 128 ? -27.145 53.997 -19.770 1.00 22.34  ? 109  GLY E O   1 
ATOM   7285 N N   . GLU E 1 129 ? -29.086 53.978 -20.908 1.00 28.01  ? 110  GLU E N   1 
ATOM   7286 C CA  . GLU E 1 129 ? -29.295 52.542 -20.720 1.00 27.84  ? 110  GLU E CA  1 
ATOM   7287 C C   . GLU E 1 129 ? -28.488 51.724 -21.711 1.00 23.37  ? 110  GLU E C   1 
ATOM   7288 O O   . GLU E 1 129 ? -28.539 51.947 -22.912 1.00 21.55  ? 110  GLU E O   1 
ATOM   7289 C CB  . GLU E 1 129 ? -30.774 52.178 -20.837 1.00 32.30  ? 110  GLU E CB  1 
ATOM   7290 C CG  . GLU E 1 129 ? -31.551 52.373 -19.541 1.00 47.54  ? 110  GLU E CG  1 
ATOM   7291 C CD  . GLU E 1 129 ? -31.272 51.266 -18.521 1.00 60.01  ? 110  GLU E CD  1 
ATOM   7292 O OE1 . GLU E 1 129 ? -31.263 50.072 -18.927 1.00 59.29  ? 110  GLU E OE1 1 
ATOM   7293 O OE2 . GLU E 1 129 ? -31.054 51.592 -17.324 1.00 55.00  ? 110  GLU E OE2 1 
ATOM   7294 N N   . VAL E 1 130 ? -27.738 50.767 -21.196 1.00 27.11  ? 111  VAL E N   1 
ATOM   7295 C CA  . VAL E 1 130 ? -26.873 49.959 -22.033 1.00 20.94  ? 111  VAL E CA  1 
ATOM   7296 C C   . VAL E 1 130 ? -27.334 48.524 -21.973 1.00 22.70  ? 111  VAL E C   1 
ATOM   7297 O O   . VAL E 1 130 ? -27.697 48.019 -20.897 1.00 21.88  ? 111  VAL E O   1 
ATOM   7298 C CB  . VAL E 1 130 ? -25.410 50.042 -21.562 1.00 20.26  ? 111  VAL E CB  1 
ATOM   7299 C CG1 . VAL E 1 130 ? -24.494 49.313 -22.538 1.00 18.78  ? 111  VAL E CG1 1 
ATOM   7300 C CG2 . VAL E 1 130 ? -24.985 51.503 -21.455 1.00 21.62  ? 111  VAL E CG2 1 
ATOM   7301 N N   . GLN E 1 131 ? -27.349 47.873 -23.135 1.00 21.51  ? 112  GLN E N   1 
ATOM   7302 C CA  . GLN E 1 131 ? -27.585 46.437 -23.183 1.00 22.38  ? 112  GLN E CA  1 
ATOM   7303 C C   . GLN E 1 131 ? -26.547 45.742 -24.057 1.00 23.84  ? 112  GLN E C   1 
ATOM   7304 O O   . GLN E 1 131 ? -26.337 46.117 -25.211 1.00 23.30  ? 112  GLN E O   1 
ATOM   7305 C CB  . GLN E 1 131 ? -28.995 46.116 -23.659 1.00 20.84  ? 112  GLN E CB  1 
ATOM   7306 C CG  . GLN E 1 131 ? -29.262 44.618 -23.717 1.00 31.03  ? 112  GLN E CG  1 
ATOM   7307 C CD  . GLN E 1 131 ? -30.662 44.280 -24.202 1.00 37.47  ? 112  GLN E CD  1 
ATOM   7308 O OE1 . GLN E 1 131 ? -31.634 44.961 -23.860 1.00 41.49  ? 112  GLN E OE1 1 
ATOM   7309 N NE2 . GLN E 1 131 ? -30.768 43.226 -25.017 1.00 34.00  ? 112  GLN E NE2 1 
ATOM   7310 N N   . TYR E 1 132 ? -25.886 44.738 -23.491 1.00 21.51  ? 113  TYR E N   1 
ATOM   7311 C CA  . TYR E 1 132 ? -24.891 43.966 -24.222 1.00 21.97  ? 113  TYR E CA  1 
ATOM   7312 C C   . TYR E 1 132 ? -25.259 42.481 -24.120 1.00 25.48  ? 113  TYR E C   1 
ATOM   7313 O O   . TYR E 1 132 ? -25.290 41.905 -23.014 1.00 25.03  ? 113  TYR E O   1 
ATOM   7314 C CB  . TYR E 1 132 ? -23.488 44.239 -23.660 1.00 22.95  ? 113  TYR E CB  1 
ATOM   7315 C CG  . TYR E 1 132 ? -22.378 43.404 -24.282 1.00 21.98  ? 113  TYR E CG  1 
ATOM   7316 C CD1 . TYR E 1 132 ? -22.276 43.270 -25.661 1.00 17.81  ? 113  TYR E CD1 1 
ATOM   7317 C CD2 . TYR E 1 132 ? -21.419 42.769 -23.480 1.00 17.34  ? 113  TYR E CD2 1 
ATOM   7318 C CE1 . TYR E 1 132 ? -21.261 42.516 -26.229 1.00 18.87  ? 113  TYR E CE1 1 
ATOM   7319 C CE2 . TYR E 1 132 ? -20.399 42.020 -24.034 1.00 15.38  ? 113  TYR E CE2 1 
ATOM   7320 C CZ  . TYR E 1 132 ? -20.324 41.892 -25.407 1.00 22.04  ? 113  TYR E CZ  1 
ATOM   7321 O OH  . TYR E 1 132 ? -19.307 41.140 -25.971 1.00 28.97  ? 113  TYR E OH  1 
ATOM   7322 N N   . THR E 1 133 ? -25.552 41.874 -25.273 1.00 23.05  ? 114  THR E N   1 
ATOM   7323 C CA  . THR E 1 133 ? -26.056 40.499 -25.332 1.00 18.66  ? 114  THR E CA  1 
ATOM   7324 C C   . THR E 1 133 ? -25.229 39.657 -26.307 1.00 20.44  ? 114  THR E C   1 
ATOM   7325 O O   . THR E 1 133 ? -25.654 39.403 -27.436 1.00 24.60  ? 114  THR E O   1 
ATOM   7326 C CB  . THR E 1 133 ? -27.541 40.468 -25.769 1.00 20.53  ? 114  THR E CB  1 
ATOM   7327 O OG1 . THR E 1 133 ? -28.297 41.428 -25.018 1.00 25.40  ? 114  THR E OG1 1 
ATOM   7328 C CG2 . THR E 1 133 ? -28.147 39.086 -25.581 1.00 20.64  ? 114  THR E CG2 1 
ATOM   7329 N N   . PRO E 1 134 ? -24.028 39.229 -25.883 1.00 20.36  ? 115  PRO E N   1 
ATOM   7330 C CA  . PRO E 1 134 ? -23.235 38.375 -26.781 1.00 18.73  ? 115  PRO E CA  1 
ATOM   7331 C C   . PRO E 1 134 ? -23.733 36.927 -26.755 1.00 21.89  ? 115  PRO E C   1 
ATOM   7332 O O   . PRO E 1 134 ? -24.265 36.446 -25.735 1.00 19.08  ? 115  PRO E O   1 
ATOM   7333 C CB  . PRO E 1 134 ? -21.832 38.458 -26.176 1.00 15.09  ? 115  PRO E CB  1 
ATOM   7334 C CG  . PRO E 1 134 ? -22.085 38.700 -24.709 1.00 15.23  ? 115  PRO E CG  1 
ATOM   7335 C CD  . PRO E 1 134 ? -23.310 39.554 -24.633 1.00 16.43  ? 115  PRO E CD  1 
ATOM   7336 N N   . SER E 1 135 ? -23.563 36.228 -27.870 1.00 19.91  ? 116  SER E N   1 
ATOM   7337 C CA  . SER E 1 135 ? -23.768 34.782 -27.854 1.00 21.98  ? 116  SER E CA  1 
ATOM   7338 C C   . SER E 1 135 ? -22.453 34.103 -27.472 1.00 19.31  ? 116  SER E C   1 
ATOM   7339 O O   . SER E 1 135 ? -21.404 34.389 -28.054 1.00 19.37  ? 116  SER E O   1 
ATOM   7340 C CB  . SER E 1 135 ? -24.261 34.257 -29.202 1.00 22.23  ? 116  SER E CB  1 
ATOM   7341 O OG  . SER E 1 135 ? -24.509 32.864 -29.103 1.00 23.63  ? 116  SER E OG  1 
ATOM   7342 N N   . ILE E 1 136 ? -22.521 33.202 -26.497 1.00 18.09  ? 117  ILE E N   1 
ATOM   7343 C CA  . ILE E 1 136 ? -21.329 32.571 -25.937 1.00 17.53  ? 117  ILE E CA  1 
ATOM   7344 C C   . ILE E 1 136 ? -21.400 31.032 -25.940 1.00 17.60  ? 117  ILE E C   1 
ATOM   7345 O O   . ILE E 1 136 ? -22.395 30.429 -25.517 1.00 17.94  ? 117  ILE E O   1 
ATOM   7346 C CB  . ILE E 1 136 ? -21.066 33.093 -24.498 1.00 15.11  ? 117  ILE E CB  1 
ATOM   7347 C CG1 . ILE E 1 136 ? -20.798 34.599 -24.524 1.00 16.07  ? 117  ILE E CG1 1 
ATOM   7348 C CG2 . ILE E 1 136 ? -19.908 32.347 -23.836 1.00 14.38  ? 117  ILE E CG2 1 
ATOM   7349 C CD1 . ILE E 1 136 ? -20.710 35.207 -23.143 1.00 20.96  ? 117  ILE E CD1 1 
ATOM   7350 N N   . ARG E 1 137 ? -20.341 30.397 -26.417 1.00 14.51  ? 118  ARG E N   1 
ATOM   7351 C CA  . ARG E 1 137 ? -20.157 28.972 -26.188 1.00 15.98  ? 118  ARG E CA  1 
ATOM   7352 C C   . ARG E 1 137 ? -19.125 28.761 -25.069 1.00 19.36  ? 118  ARG E C   1 
ATOM   7353 O O   . ARG E 1 137 ? -18.010 29.268 -25.160 1.00 19.18  ? 118  ARG E O   1 
ATOM   7354 C CB  . ARG E 1 137 ? -19.676 28.281 -27.459 1.00 17.91  ? 118  ARG E CB  1 
ATOM   7355 C CG  . ARG E 1 137 ? -19.207 26.864 -27.225 1.00 23.05  ? 118  ARG E CG  1 
ATOM   7356 C CD  . ARG E 1 137 ? -19.158 26.054 -28.498 1.00 24.25  ? 118  ARG E CD  1 
ATOM   7357 N NE  . ARG E 1 137 ? -18.853 24.648 -28.243 1.00 30.02  ? 118  ARG E NE  1 
ATOM   7358 C CZ  . ARG E 1 137 ? -18.870 23.684 -29.165 1.00 32.92  ? 118  ARG E CZ  1 
ATOM   7359 N NH1 . ARG E 1 137 ? -19.187 23.969 -30.422 1.00 36.82  ? 118  ARG E NH1 1 
ATOM   7360 N NH2 . ARG E 1 137 ? -18.585 22.430 -28.828 1.00 31.49  ? 118  ARG E NH2 1 
ATOM   7361 N N   . GLN E 1 138 ? -19.490 28.010 -24.026 1.00 19.28  ? 119  GLN E N   1 
ATOM   7362 C CA  . GLN E 1 138 ? -18.602 27.777 -22.870 1.00 17.29  ? 119  GLN E CA  1 
ATOM   7363 C C   . GLN E 1 138 ? -18.787 26.398 -22.234 1.00 20.34  ? 119  GLN E C   1 
ATOM   7364 O O   . GLN E 1 138 ? -19.887 25.849 -22.211 1.00 23.01  ? 119  GLN E O   1 
ATOM   7365 C CB  . GLN E 1 138 ? -18.802 28.857 -21.804 1.00 18.47  ? 119  GLN E CB  1 
ATOM   7366 C CG  . GLN E 1 138 ? -17.678 28.980 -20.799 1.00 15.42  ? 119  GLN E CG  1 
ATOM   7367 C CD  . GLN E 1 138 ? -17.703 30.327 -20.065 1.00 19.72  ? 119  GLN E CD  1 
ATOM   7368 O OE1 . GLN E 1 138 ? -18.732 31.013 -19.992 1.00 21.40  ? 119  GLN E OE1 1 
ATOM   7369 N NE2 . GLN E 1 138 ? -16.554 30.721 -19.543 1.00 23.67  ? 119  GLN E NE2 1 
ATOM   7370 N N   . ARG E 1 139 ? -17.702 25.847 -21.703 1.00 20.03  ? 120  ARG E N   1 
ATOM   7371 C CA  . ARG E 1 139 ? -17.749 24.545 -21.060 1.00 21.61  ? 120  ARG E CA  1 
ATOM   7372 C C   . ARG E 1 139 ? -17.828 24.683 -19.515 1.00 23.37  ? 120  ARG E C   1 
ATOM   7373 O O   . ARG E 1 139 ? -17.090 25.473 -18.916 1.00 21.96  ? 120  ARG E O   1 
ATOM   7374 C CB  . ARG E 1 139 ? -16.539 23.716 -21.512 1.00 21.43  ? 120  ARG E CB  1 
ATOM   7375 C CG  . ARG E 1 139 ? -16.665 22.236 -21.156 1.00 41.20  ? 120  ARG E CG  1 
ATOM   7376 C CD  . ARG E 1 139 ? -15.789 21.278 -21.998 1.00 42.47  ? 120  ARG E CD  1 
ATOM   7377 N NE  . ARG E 1 139 ? -16.121 19.877 -21.681 1.00 37.63  ? 120  ARG E NE  1 
ATOM   7378 C CZ  . ARG E 1 139 ? -17.067 19.171 -22.303 1.00 40.74  ? 120  ARG E CZ  1 
ATOM   7379 N NH1 . ARG E 1 139 ? -17.741 19.733 -23.297 1.00 43.84  ? 120  ARG E NH1 1 
ATOM   7380 N NH2 . ARG E 1 139 ? -17.338 17.911 -21.947 1.00 36.58  ? 120  ARG E NH2 1 
ATOM   7381 N N   . PHE E 1 140 ? -18.732 23.942 -18.874 1.00 23.44  ? 121  PHE E N   1 
ATOM   7382 C CA  . PHE E 1 140 ? -18.923 24.057 -17.410 1.00 26.06  ? 121  PHE E CA  1 
ATOM   7383 C C   . PHE E 1 140 ? -18.757 22.752 -16.662 1.00 29.31  ? 121  PHE E C   1 
ATOM   7384 O O   . PHE E 1 140 ? -18.817 21.665 -17.236 1.00 34.15  ? 121  PHE E O   1 
ATOM   7385 C CB  . PHE E 1 140 ? -20.309 24.597 -17.055 1.00 21.36  ? 121  PHE E CB  1 
ATOM   7386 C CG  . PHE E 1 140 ? -20.575 25.958 -17.590 1.00 26.36  ? 121  PHE E CG  1 
ATOM   7387 C CD1 . PHE E 1 140 ? -21.108 26.117 -18.867 1.00 22.02  ? 121  PHE E CD1 1 
ATOM   7388 C CD2 . PHE E 1 140 ? -20.280 27.089 -16.826 1.00 21.80  ? 121  PHE E CD2 1 
ATOM   7389 C CE1 . PHE E 1 140 ? -21.352 27.382 -19.374 1.00 24.12  ? 121  PHE E CE1 1 
ATOM   7390 C CE2 . PHE E 1 140 ? -20.519 28.356 -17.323 1.00 18.43  ? 121  PHE E CE2 1 
ATOM   7391 C CZ  . PHE E 1 140 ? -21.055 28.510 -18.601 1.00 19.70  ? 121  PHE E CZ  1 
ATOM   7392 N N   . SER E 1 141 ? -18.583 22.875 -15.356 1.00 30.21  ? 122  SER E N   1 
ATOM   7393 C CA  . SER E 1 141 ? -18.489 21.724 -14.472 1.00 26.55  ? 122  SER E CA  1 
ATOM   7394 C C   . SER E 1 141 ? -19.728 21.769 -13.581 1.00 30.05  ? 122  SER E C   1 
ATOM   7395 O O   . SER E 1 141 ? -19.923 22.718 -12.814 1.00 31.93  ? 122  SER E O   1 
ATOM   7396 C CB  . SER E 1 141 ? -17.204 21.802 -13.643 1.00 19.85  ? 122  SER E CB  1 
ATOM   7397 O OG  . SER E 1 141 ? -17.355 21.129 -12.410 1.00 27.38  ? 122  SER E OG  1 
ATOM   7398 N N   . CYS E 1 142 ? -20.579 20.757 -13.704 1.00 29.20  ? 123  CYS E N   1 
ATOM   7399 C CA  . CYS E 1 142 ? -21.826 20.717 -12.945 1.00 33.74  ? 123  CYS E CA  1 
ATOM   7400 C C   . CYS E 1 142 ? -22.399 19.300 -12.849 1.00 37.56  ? 123  CYS E C   1 
ATOM   7401 O O   . CYS E 1 142 ? -21.827 18.344 -13.393 1.00 30.37  ? 123  CYS E O   1 
ATOM   7402 C CB  . CYS E 1 142 ? -22.851 21.681 -13.557 1.00 36.10  ? 123  CYS E CB  1 
ATOM   7403 S SG  . CYS E 1 142 ? -23.120 21.431 -15.321 1.00 53.90  ? 123  CYS E SG  1 
ATOM   7404 N N   . ASP E 1 143 ? -23.533 19.176 -12.156 1.00 42.61  ? 124  ASP E N   1 
ATOM   7405 C CA  . ASP E 1 143 ? -24.170 17.876 -11.932 1.00 34.92  ? 124  ASP E CA  1 
ATOM   7406 C C   . ASP E 1 143 ? -24.938 17.423 -13.166 1.00 31.70  ? 124  ASP E C   1 
ATOM   7407 O O   . ASP E 1 143 ? -25.913 18.058 -13.570 1.00 34.08  ? 124  ASP E O   1 
ATOM   7408 C CB  . ASP E 1 143 ? -25.106 17.937 -10.723 1.00 33.69  ? 124  ASP E CB  1 
ATOM   7409 C CG  . ASP E 1 143 ? -25.455 16.566 -10.187 1.00 37.70  ? 124  ASP E CG  1 
ATOM   7410 O OD1 . ASP E 1 143 ? -24.872 15.564 -10.665 1.00 44.86  ? 124  ASP E OD1 1 
ATOM   7411 O OD2 . ASP E 1 143 ? -26.302 16.496 -9.273  1.00 38.83  ? 124  ASP E OD2 1 
ATOM   7412 N N   . VAL E 1 144 ? -24.488 16.319 -13.751 1.00 27.37  ? 125  VAL E N   1 
ATOM   7413 C CA  . VAL E 1 144 ? -25.013 15.825 -15.019 1.00 29.86  ? 125  VAL E CA  1 
ATOM   7414 C C   . VAL E 1 144 ? -25.820 14.519 -14.827 1.00 37.72  ? 125  VAL E C   1 
ATOM   7415 O O   . VAL E 1 144 ? -26.521 14.047 -15.733 1.00 32.09  ? 125  VAL E O   1 
ATOM   7416 C CB  . VAL E 1 144 ? -23.847 15.596 -16.005 1.00 27.97  ? 125  VAL E CB  1 
ATOM   7417 C CG1 . VAL E 1 144 ? -24.343 15.112 -17.349 1.00 27.52  ? 125  VAL E CG1 1 
ATOM   7418 C CG2 . VAL E 1 144 ? -23.041 16.863 -16.162 1.00 33.18  ? 125  VAL E CG2 1 
ATOM   7419 N N   . SER E 1 145 ? -25.716 13.943 -13.632 1.00 39.03  ? 126  SER E N   1 
ATOM   7420 C CA  . SER E 1 145 ? -26.389 12.687 -13.316 1.00 34.26  ? 126  SER E CA  1 
ATOM   7421 C C   . SER E 1 145 ? -27.894 12.759 -13.595 1.00 34.90  ? 126  SER E C   1 
ATOM   7422 O O   . SER E 1 145 ? -28.576 13.731 -13.229 1.00 32.93  ? 126  SER E O   1 
ATOM   7423 C CB  . SER E 1 145 ? -26.147 12.315 -11.853 1.00 32.52  ? 126  SER E CB  1 
ATOM   7424 O OG  . SER E 1 145 ? -26.644 13.332 -10.993 1.00 32.56  ? 126  SER E OG  1 
ATOM   7425 N N   . GLY E 1 146 ? -28.403 11.729 -14.263 1.00 38.81  ? 127  GLY E N   1 
ATOM   7426 C CA  . GLY E 1 146 ? -29.821 11.630 -14.547 1.00 37.24  ? 127  GLY E CA  1 
ATOM   7427 C C   . GLY E 1 146 ? -30.183 12.289 -15.857 1.00 38.04  ? 127  GLY E C   1 
ATOM   7428 O O   . GLY E 1 146 ? -31.351 12.564 -16.117 1.00 37.13  ? 127  GLY E O   1 
ATOM   7429 N N   . VAL E 1 147 ? -29.180 12.540 -16.691 1.00 36.36  ? 128  VAL E N   1 
ATOM   7430 C CA  . VAL E 1 147 ? -29.425 13.230 -17.949 1.00 38.93  ? 128  VAL E CA  1 
ATOM   7431 C C   . VAL E 1 147 ? -30.227 12.325 -18.886 1.00 38.52  ? 128  VAL E C   1 
ATOM   7432 O O   . VAL E 1 147 ? -30.984 12.798 -19.735 1.00 41.88  ? 128  VAL E O   1 
ATOM   7433 C CB  . VAL E 1 147 ? -28.096 13.716 -18.606 1.00 39.84  ? 128  VAL E CB  1 
ATOM   7434 C CG1 . VAL E 1 147 ? -27.153 12.546 -18.852 1.00 29.67  ? 128  VAL E CG1 1 
ATOM   7435 C CG2 . VAL E 1 147 ? -28.359 14.525 -19.896 1.00 30.86  ? 128  VAL E CG2 1 
ATOM   7436 N N   . ASP E 1 148 ? -30.075 11.018 -18.706 1.00 48.69  ? 129  ASP E N   1 
ATOM   7437 C CA  . ASP E 1 148 ? -30.770 10.043 -19.549 1.00 47.44  ? 129  ASP E CA  1 
ATOM   7438 C C   . ASP E 1 148 ? -32.014 9.451  -18.856 1.00 38.54  ? 129  ASP E C   1 
ATOM   7439 O O   . ASP E 1 148 ? -32.343 8.288  -19.024 1.00 37.51  ? 129  ASP E O   1 
ATOM   7440 C CB  . ASP E 1 148 ? -29.793 8.948  -19.980 1.00 48.20  ? 129  ASP E CB  1 
ATOM   7441 C CG  . ASP E 1 148 ? -30.054 8.456  -21.399 1.00 65.13  ? 129  ASP E CG  1 
ATOM   7442 O OD1 . ASP E 1 148 ? -31.242 8.245  -21.755 1.00 53.27  ? 129  ASP E OD1 1 
ATOM   7443 O OD2 . ASP E 1 148 ? -29.070 8.284  -22.159 1.00 78.11  ? 129  ASP E OD2 1 
ATOM   7444 N N   . THR E 1 149 ? -32.704 10.299 -18.102 1.00 37.15  ? 130  THR E N   1 
ATOM   7445 C CA  . THR E 1 149 ? -33.789 9.923  -17.204 1.00 35.49  ? 130  THR E CA  1 
ATOM   7446 C C   . THR E 1 149 ? -34.975 10.830 -17.502 1.00 45.92  ? 130  THR E C   1 
ATOM   7447 O O   . THR E 1 149 ? -34.806 11.911 -18.065 1.00 43.57  ? 130  THR E O   1 
ATOM   7448 C CB  . THR E 1 149 ? -33.332 10.104 -15.733 1.00 43.54  ? 130  THR E CB  1 
ATOM   7449 O OG1 . THR E 1 149 ? -32.362 9.094  -15.415 1.00 59.25  ? 130  THR E OG1 1 
ATOM   7450 C CG2 . THR E 1 149 ? -34.491 10.031 -14.728 1.00 42.59  ? 130  THR E CG2 1 
ATOM   7451 N N   . GLU E 1 150 ? -36.180 10.399 -17.154 1.00 53.73  ? 131  GLU E N   1 
ATOM   7452 C CA  . GLU E 1 150 ? -37.360 11.204 -17.435 1.00 55.60  ? 131  GLU E CA  1 
ATOM   7453 C C   . GLU E 1 150 ? -37.390 12.532 -16.647 1.00 52.21  ? 131  GLU E C   1 
ATOM   7454 O O   . GLU E 1 150 ? -37.986 13.517 -17.096 1.00 44.21  ? 131  GLU E O   1 
ATOM   7455 C CB  . GLU E 1 150 ? -38.616 10.382 -17.174 1.00 60.33  ? 131  GLU E CB  1 
ATOM   7456 C CG  . GLU E 1 150 ? -39.876 10.946 -17.793 1.00 61.84  ? 131  GLU E CG  1 
ATOM   7457 C CD  . GLU E 1 150 ? -41.129 10.401 -17.124 1.00 87.21  ? 131  GLU E CD  1 
ATOM   7458 O OE1 . GLU E 1 150 ? -41.122 10.234 -15.878 1.00 88.29  ? 131  GLU E OE1 1 
ATOM   7459 O OE2 . GLU E 1 150 ? -42.117 10.135 -17.846 1.00 88.07  ? 131  GLU E OE2 1 
ATOM   7460 N N   . SER E 1 151 ? -36.738 12.561 -15.484 1.00 47.90  ? 132  SER E N   1 
ATOM   7461 C CA  . SER E 1 151 ? -36.716 13.768 -14.642 1.00 39.70  ? 132  SER E CA  1 
ATOM   7462 C C   . SER E 1 151 ? -35.541 14.722 -14.934 1.00 41.00  ? 132  SER E C   1 
ATOM   7463 O O   . SER E 1 151 ? -35.547 15.888 -14.505 1.00 35.10  ? 132  SER E O   1 
ATOM   7464 C CB  . SER E 1 151 ? -36.745 13.384 -13.160 1.00 43.94  ? 132  SER E CB  1 
ATOM   7465 O OG  . SER E 1 151 ? -35.773 12.387 -12.888 1.00 65.81  ? 132  SER E OG  1 
ATOM   7466 N N   . GLY E 1 152 ? -34.538 14.222 -15.656 1.00 44.20  ? 133  GLY E N   1 
ATOM   7467 C CA  . GLY E 1 152 ? -33.456 15.051 -16.177 1.00 36.30  ? 133  GLY E CA  1 
ATOM   7468 C C   . GLY E 1 152 ? -32.350 15.378 -15.181 1.00 41.34  ? 133  GLY E C   1 
ATOM   7469 O O   . GLY E 1 152 ? -32.450 15.060 -13.988 1.00 40.54  ? 133  GLY E O   1 
ATOM   7470 N N   . ALA E 1 153 ? -31.286 16.010 -15.679 1.00 38.58  ? 134  ALA E N   1 
ATOM   7471 C CA  . ALA E 1 153 ? -30.228 16.548 -14.821 1.00 34.46  ? 134  ALA E CA  1 
ATOM   7472 C C   . ALA E 1 153 ? -30.500 18.021 -14.514 1.00 32.42  ? 134  ALA E C   1 
ATOM   7473 O O   . ALA E 1 153 ? -31.148 18.717 -15.296 1.00 34.19  ? 134  ALA E O   1 
ATOM   7474 C CB  . ALA E 1 153 ? -28.877 16.394 -15.491 1.00 36.07  ? 134  ALA E CB  1 
ATOM   7475 N N   . THR E 1 154 ? -30.011 18.498 -13.372 1.00 38.57  ? 135  THR E N   1 
ATOM   7476 C CA  . THR E 1 154 ? -30.068 19.929 -13.080 1.00 37.42  ? 135  THR E CA  1 
ATOM   7477 C C   . THR E 1 154 ? -28.676 20.518 -12.886 1.00 39.70  ? 135  THR E C   1 
ATOM   7478 O O   . THR E 1 154 ? -28.016 20.276 -11.869 1.00 37.59  ? 135  THR E O   1 
ATOM   7479 C CB  . THR E 1 154 ? -30.944 20.249 -11.864 1.00 45.63  ? 135  THR E CB  1 
ATOM   7480 O OG1 . THR E 1 154 ? -32.201 19.564 -11.981 1.00 44.35  ? 135  THR E OG1 1 
ATOM   7481 C CG2 . THR E 1 154 ? -31.190 21.762 -11.778 1.00 42.11  ? 135  THR E CG2 1 
ATOM   7482 N N   . CYS E 1 155 ? -28.245 21.281 -13.890 1.00 39.91  ? 136  CYS E N   1 
ATOM   7483 C CA  . CYS E 1 155 ? -26.950 21.946 -13.892 1.00 38.36  ? 136  CYS E CA  1 
ATOM   7484 C C   . CYS E 1 155 ? -27.093 23.416 -13.438 1.00 33.22  ? 136  CYS E C   1 
ATOM   7485 O O   . CYS E 1 155 ? -27.938 24.137 -13.962 1.00 33.71  ? 136  CYS E O   1 
ATOM   7486 C CB  . CYS E 1 155 ? -26.363 21.864 -15.299 1.00 28.52  ? 136  CYS E CB  1 
ATOM   7487 S SG  . CYS E 1 155 ? -24.746 22.663 -15.455 1.00 67.01  ? 136  CYS E SG  1 
ATOM   7488 N N   . ARG E 1 156 ? -26.291 23.852 -12.460 1.00 32.43  ? 137  ARG E N   1 
ATOM   7489 C CA  . ARG E 1 156 ? -26.323 25.255 -12.004 1.00 30.45  ? 137  ARG E CA  1 
ATOM   7490 C C   . ARG E 1 156 ? -25.114 26.064 -12.504 1.00 27.48  ? 137  ARG E C   1 
ATOM   7491 O O   . ARG E 1 156 ? -23.977 25.597 -12.475 1.00 30.13  ? 137  ARG E O   1 
ATOM   7492 C CB  . ARG E 1 156 ? -26.405 25.368 -10.473 1.00 31.09  ? 137  ARG E CB  1 
ATOM   7493 C CG  . ARG E 1 156 ? -27.340 24.392 -9.772  1.00 31.33  ? 137  ARG E CG  1 
ATOM   7494 C CD  . ARG E 1 156 ? -27.338 24.584 -8.234  1.00 46.46  ? 137  ARG E CD  1 
ATOM   7495 N NE  . ARG E 1 156 ? -26.046 25.011 -7.661  1.00 50.14  ? 137  ARG E NE  1 
ATOM   7496 C CZ  . ARG E 1 156 ? -25.109 24.193 -7.178  1.00 55.67  ? 137  ARG E CZ  1 
ATOM   7497 N NH1 . ARG E 1 156 ? -25.292 22.877 -7.196  1.00 55.88  ? 137  ARG E NH1 1 
ATOM   7498 N NH2 . ARG E 1 156 ? -23.981 24.691 -6.677  1.00 57.28  ? 137  ARG E NH2 1 
ATOM   7499 N N   . ILE E 1 157 ? -25.367 27.285 -12.953 1.00 28.66  ? 138  ILE E N   1 
ATOM   7500 C CA  . ILE E 1 157 ? -24.298 28.154 -13.414 1.00 25.20  ? 138  ILE E CA  1 
ATOM   7501 C C   . ILE E 1 157 ? -24.298 29.402 -12.556 1.00 23.24  ? 138  ILE E C   1 
ATOM   7502 O O   . ILE E 1 157 ? -25.319 30.073 -12.418 1.00 22.44  ? 138  ILE E O   1 
ATOM   7503 C CB  . ILE E 1 157 ? -24.484 28.549 -14.884 1.00 24.31  ? 138  ILE E CB  1 
ATOM   7504 C CG1 . ILE E 1 157 ? -24.423 27.309 -15.769 1.00 20.39  ? 138  ILE E CG1 1 
ATOM   7505 C CG2 . ILE E 1 157 ? -23.440 29.585 -15.308 1.00 24.60  ? 138  ILE E CG2 1 
ATOM   7506 C CD1 . ILE E 1 157 ? -24.356 27.633 -17.234 1.00 22.63  ? 138  ILE E CD1 1 
ATOM   7507 N N   . LYS E 1 158 ? -23.144 29.707 -11.977 1.00 27.89  ? 139  LYS E N   1 
ATOM   7508 C CA  . LYS E 1 158 ? -23.016 30.829 -11.056 1.00 25.38  ? 139  LYS E CA  1 
ATOM   7509 C C   . LYS E 1 158 ? -22.244 31.988 -11.725 1.00 26.98  ? 139  LYS E C   1 
ATOM   7510 O O   . LYS E 1 158 ? -21.076 31.856 -12.128 1.00 24.12  ? 139  LYS E O   1 
ATOM   7511 C CB  . LYS E 1 158 ? -22.340 30.348 -9.765  1.00 25.17  ? 139  LYS E CB  1 
ATOM   7512 C CG  . LYS E 1 158 ? -22.025 31.442 -8.764  1.00 31.77  ? 139  LYS E CG  1 
ATOM   7513 C CD  . LYS E 1 158 ? -21.034 30.929 -7.703  1.00 38.44  ? 139  LYS E CD  1 
ATOM   7514 C CE  . LYS E 1 158 ? -20.328 32.062 -6.956  1.00 37.62  ? 139  LYS E CE  1 
ATOM   7515 N NZ  . LYS E 1 158 ? -19.466 31.544 -5.841  1.00 33.04  ? 139  LYS E NZ  1 
ATOM   7516 N N   . ILE E 1 159 ? -22.908 33.126 -11.857 1.00 21.61  ? 140  ILE E N   1 
ATOM   7517 C CA  . ILE E 1 159 ? -22.317 34.268 -12.536 1.00 18.46  ? 140  ILE E CA  1 
ATOM   7518 C C   . ILE E 1 159 ? -22.339 35.506 -11.642 1.00 22.32  ? 140  ILE E C   1 
ATOM   7519 O O   . ILE E 1 159 ? -23.381 35.867 -11.104 1.00 25.18  ? 140  ILE E O   1 
ATOM   7520 C CB  . ILE E 1 159 ? -23.088 34.573 -13.822 1.00 21.49  ? 140  ILE E CB  1 
ATOM   7521 C CG1 . ILE E 1 159 ? -22.959 33.406 -14.793 1.00 22.20  ? 140  ILE E CG1 1 
ATOM   7522 C CG2 . ILE E 1 159 ? -22.594 35.842 -14.475 1.00 18.66  ? 140  ILE E CG2 1 
ATOM   7523 C CD1 . ILE E 1 159 ? -23.623 33.675 -16.114 1.00 19.48  ? 140  ILE E CD1 1 
ATOM   7524 N N   . GLY E 1 160 ? -21.191 36.165 -11.494 1.00 23.49  ? 141  GLY E N   1 
ATOM   7525 C CA  . GLY E 1 160 ? -21.118 37.382 -10.711 1.00 20.99  ? 141  GLY E CA  1 
ATOM   7526 C C   . GLY E 1 160 ? -19.941 38.270 -11.065 1.00 20.18  ? 141  GLY E C   1 
ATOM   7527 O O   . GLY E 1 160 ? -19.121 37.912 -11.913 1.00 19.27  ? 141  GLY E O   1 
ATOM   7528 N N   . SER E 1 161 ? -19.860 39.435 -10.418 1.00 24.03  ? 142  SER E N   1 
ATOM   7529 C CA  . SER E 1 161 ? -18.700 40.321 -10.555 1.00 19.72  ? 142  SER E CA  1 
ATOM   7530 C C   . SER E 1 161 ? -17.455 39.706 -9.941  1.00 21.61  ? 142  SER E C   1 
ATOM   7531 O O   . SER E 1 161 ? -17.500 39.186 -8.822  1.00 24.72  ? 142  SER E O   1 
ATOM   7532 C CB  . SER E 1 161 ? -18.954 41.654 -9.860  1.00 20.92  ? 142  SER E CB  1 
ATOM   7533 O OG  . SER E 1 161 ? -17.780 42.457 -9.918  1.00 27.00  ? 142  SER E OG  1 
ATOM   7534 N N   . TRP E 1 162 ? -16.336 39.798 -10.654 1.00 20.38  ? 143  TRP E N   1 
ATOM   7535 C CA  . TRP E 1 162 ? -15.086 39.176 -10.198 1.00 20.80  ? 143  TRP E CA  1 
ATOM   7536 C C   . TRP E 1 162 ? -14.304 39.992 -9.176  1.00 23.03  ? 143  TRP E C   1 
ATOM   7537 O O   . TRP E 1 162 ? -13.644 39.416 -8.293  1.00 21.32  ? 143  TRP E O   1 
ATOM   7538 C CB  . TRP E 1 162 ? -14.174 38.841 -11.379 1.00 17.38  ? 143  TRP E CB  1 
ATOM   7539 C CG  . TRP E 1 162 ? -13.086 37.850 -11.008 1.00 20.96  ? 143  TRP E CG  1 
ATOM   7540 C CD1 . TRP E 1 162 ? -11.749 38.107 -10.856 1.00 16.67  ? 143  TRP E CD1 1 
ATOM   7541 C CD2 . TRP E 1 162 ? -13.259 36.448 -10.743 1.00 19.40  ? 143  TRP E CD2 1 
ATOM   7542 N NE1 . TRP E 1 162 ? -11.086 36.956 -10.527 1.00 17.38  ? 143  TRP E NE1 1 
ATOM   7543 C CE2 . TRP E 1 162 ? -11.985 35.926 -10.437 1.00 21.32  ? 143  TRP E CE2 1 
ATOM   7544 C CE3 . TRP E 1 162 ? -14.370 35.595 -10.717 1.00 18.47  ? 143  TRP E CE3 1 
ATOM   7545 C CZ2 . TRP E 1 162 ? -11.791 34.579 -10.108 1.00 21.64  ? 143  TRP E CZ2 1 
ATOM   7546 C CZ3 . TRP E 1 162 ? -14.181 34.263 -10.399 1.00 21.58  ? 143  TRP E CZ3 1 
ATOM   7547 C CH2 . TRP E 1 162 ? -12.894 33.765 -10.101 1.00 24.79  ? 143  TRP E CH2 1 
ATOM   7548 N N   . THR E 1 163 ? -14.370 41.324 -9.311  1.00 21.64  ? 144  THR E N   1 
ATOM   7549 C CA  . THR E 1 163 ? -13.595 42.231 -8.458  1.00 18.67  ? 144  THR E CA  1 
ATOM   7550 C C   . THR E 1 163 ? -14.410 43.278 -7.707  1.00 16.69  ? 144  THR E C   1 
ATOM   7551 O O   . THR E 1 163 ? -13.870 43.984 -6.863  1.00 27.45  ? 144  THR E O   1 
ATOM   7552 C CB  . THR E 1 163 ? -12.461 42.962 -9.227  1.00 13.07  ? 144  THR E CB  1 
ATOM   7553 O OG1 . THR E 1 163 ? -13.033 43.878 -10.159 1.00 20.80  ? 144  THR E OG1 1 
ATOM   7554 C CG2 . THR E 1 163 ? -11.588 41.993 -9.966  1.00 14.64  ? 144  THR E CG2 1 
ATOM   7555 N N   . HIS E 1 164 ? -15.687 43.414 -8.009  1.00 14.84  ? 145  HIS E N   1 
ATOM   7556 C CA  . HIS E 1 164 ? -16.477 44.445 -7.336  1.00 20.17  ? 145  HIS E CA  1 
ATOM   7557 C C   . HIS E 1 164 ? -17.467 43.868 -6.308  1.00 26.67  ? 145  HIS E C   1 
ATOM   7558 O O   . HIS E 1 164 ? -18.277 43.000 -6.639  1.00 25.93  ? 145  HIS E O   1 
ATOM   7559 C CB  . HIS E 1 164 ? -17.227 45.309 -8.356  1.00 19.86  ? 145  HIS E CB  1 
ATOM   7560 C CG  . HIS E 1 164 ? -16.334 46.148 -9.208  1.00 22.29  ? 145  HIS E CG  1 
ATOM   7561 N ND1 . HIS E 1 164 ? -15.665 47.245 -8.746  1.00 22.16  ? 145  HIS E ND1 1 
ATOM   7562 C CD2 . HIS E 1 164 ? -15.999 46.042 -10.538 1.00 22.80  ? 145  HIS E CD2 1 
ATOM   7563 C CE1 . HIS E 1 164 ? -14.952 47.799 -9.724  1.00 20.87  ? 145  HIS E CE1 1 
ATOM   7564 N NE2 . HIS E 1 164 ? -15.156 47.072 -10.815 1.00 21.60  ? 145  HIS E NE2 1 
ATOM   7565 N N   . HIS E 1 165 ? -17.417 44.357 -5.069  1.00 25.06  ? 146  HIS E N   1 
ATOM   7566 C CA  . HIS E 1 165 ? -18.322 43.861 -4.037  1.00 26.38  ? 146  HIS E CA  1 
ATOM   7567 C C   . HIS E 1 165 ? -19.736 44.465 -4.126  1.00 28.13  ? 146  HIS E C   1 
ATOM   7568 O O   . HIS E 1 165 ? -20.036 45.230 -5.037  1.00 27.04  ? 146  HIS E O   1 
ATOM   7569 C CB  . HIS E 1 165 ? -17.718 44.024 -2.644  1.00 28.50  ? 146  HIS E CB  1 
ATOM   7570 C CG  . HIS E 1 165 ? -17.429 45.445 -2.274  1.00 37.18  ? 146  HIS E CG  1 
ATOM   7571 N ND1 . HIS E 1 165 ? -18.411 46.392 -2.138  1.00 34.62  ? 146  HIS E ND1 1 
ATOM   7572 C CD2 . HIS E 1 165 ? -16.250 46.066 -2.002  1.00 41.24  ? 146  HIS E CD2 1 
ATOM   7573 C CE1 . HIS E 1 165 ? -17.856 47.551 -1.799  1.00 39.95  ? 146  HIS E CE1 1 
ATOM   7574 N NE2 . HIS E 1 165 ? -16.553 47.372 -1.706  1.00 39.30  ? 146  HIS E NE2 1 
ATOM   7575 N N   . SER E 1 166 ? -20.600 44.107 -3.178  1.00 29.97  ? 147  SER E N   1 
ATOM   7576 C CA  . SER E 1 166 ? -22.042 44.371 -3.274  1.00 30.77  ? 147  SER E CA  1 
ATOM   7577 C C   . SER E 1 166 ? -22.449 45.843 -3.222  1.00 33.93  ? 147  SER E C   1 
ATOM   7578 O O   . SER E 1 166 ? -23.582 46.182 -3.579  1.00 32.78  ? 147  SER E O   1 
ATOM   7579 C CB  . SER E 1 166 ? -22.786 43.632 -2.165  1.00 32.15  ? 147  SER E CB  1 
ATOM   7580 O OG  . SER E 1 166 ? -22.396 44.152 -0.904  1.00 34.65  ? 147  SER E OG  1 
ATOM   7581 N N   . ARG E 1 167 ? -21.554 46.708 -2.746  1.00 38.47  ? 148  ARG E N   1 
ATOM   7582 C CA  . ARG E 1 167 ? -21.844 48.147 -2.688  1.00 40.09  ? 148  ARG E CA  1 
ATOM   7583 C C   . ARG E 1 167 ? -21.381 48.871 -3.951  1.00 34.02  ? 148  ARG E C   1 
ATOM   7584 O O   . ARG E 1 167 ? -21.656 50.057 -4.135  1.00 35.89  ? 148  ARG E O   1 
ATOM   7585 C CB  . ARG E 1 167 ? -21.214 48.810 -1.458  1.00 40.67  ? 148  ARG E CB  1 
ATOM   7586 C CG  . ARG E 1 167 ? -21.769 48.340 -0.115  1.00 52.29  ? 148  ARG E CG  1 
ATOM   7587 C CD  . ARG E 1 167 ? -21.108 49.096 1.050   1.00 69.69  ? 148  ARG E CD  1 
ATOM   7588 N NE  . ARG E 1 167 ? -19.880 49.798 0.651   1.00 73.87  ? 148  ARG E NE  1 
ATOM   7589 C CZ  . ARG E 1 167 ? -18.750 49.818 1.358   1.00 81.58  ? 148  ARG E CZ  1 
ATOM   7590 N NH1 . ARG E 1 167 ? -18.679 49.163 2.516   1.00 85.39  ? 148  ARG E NH1 1 
ATOM   7591 N NH2 . ARG E 1 167 ? -17.689 50.489 0.902   1.00 70.29  ? 148  ARG E NH2 1 
ATOM   7592 N N   . GLU E 1 168 ? -20.676 48.146 -4.812  1.00 29.43  ? 149  GLU E N   1 
ATOM   7593 C CA  . GLU E 1 168 ? -20.219 48.686 -6.084  1.00 28.72  ? 149  GLU E CA  1 
ATOM   7594 C C   . GLU E 1 168 ? -21.015 48.127 -7.278  1.00 25.14  ? 149  GLU E C   1 
ATOM   7595 O O   . GLU E 1 168 ? -21.447 48.872 -8.150  1.00 28.43  ? 149  GLU E O   1 
ATOM   7596 C CB  . GLU E 1 168 ? -18.708 48.445 -6.253  1.00 31.00  ? 149  GLU E CB  1 
ATOM   7597 C CG  . GLU E 1 168 ? -17.839 49.188 -5.239  1.00 38.60  ? 149  GLU E CG  1 
ATOM   7598 C CD  . GLU E 1 168 ? -16.354 48.830 -5.324  1.00 45.05  ? 149  GLU E CD  1 
ATOM   7599 O OE1 . GLU E 1 168 ? -16.050 47.647 -5.621  1.00 41.58  ? 149  GLU E OE1 1 
ATOM   7600 O OE2 . GLU E 1 168 ? -15.497 49.730 -5.088  1.00 51.81  ? 149  GLU E OE2 1 
ATOM   7601 N N   . ILE E 1 169 ? -21.198 46.813 -7.319  1.00 25.66  ? 150  ILE E N   1 
ATOM   7602 C CA  . ILE E 1 169 ? -22.054 46.190 -8.328  1.00 21.50  ? 150  ILE E CA  1 
ATOM   7603 C C   . ILE E 1 169 ? -23.018 45.252 -7.637  1.00 25.02  ? 150  ILE E C   1 
ATOM   7604 O O   . ILE E 1 169 ? -22.599 44.416 -6.818  1.00 26.39  ? 150  ILE E O   1 
ATOM   7605 C CB  . ILE E 1 169 ? -21.235 45.385 -9.357  1.00 18.29  ? 150  ILE E CB  1 
ATOM   7606 C CG1 . ILE E 1 169 ? -20.471 46.331 -10.287 1.00 18.47  ? 150  ILE E CG1 1 
ATOM   7607 C CG2 . ILE E 1 169 ? -22.129 44.478 -10.162 1.00 14.35  ? 150  ILE E CG2 1 
ATOM   7608 C CD1 . ILE E 1 169 ? -19.711 45.649 -11.427 1.00 10.41  ? 150  ILE E CD1 1 
ATOM   7609 N N   . SER E 1 170 ? -24.306 45.407 -7.936  1.00 21.45  ? 151  SER E N   1 
ATOM   7610 C CA  . SER E 1 170 ? -25.300 44.389 -7.576  1.00 29.25  ? 151  SER E CA  1 
ATOM   7611 C C   . SER E 1 170 ? -25.845 43.668 -8.832  1.00 33.39  ? 151  SER E C   1 
ATOM   7612 O O   . SER E 1 170 ? -26.228 44.313 -9.827  1.00 32.44  ? 151  SER E O   1 
ATOM   7613 C CB  . SER E 1 170 ? -26.437 45.009 -6.757  1.00 27.41  ? 151  SER E CB  1 
ATOM   7614 O OG  . SER E 1 170 ? -27.257 45.823 -7.567  1.00 30.82  ? 151  SER E OG  1 
ATOM   7615 N N   . VAL E 1 171 ? -25.876 42.337 -8.798  1.00 30.77  ? 152  VAL E N   1 
ATOM   7616 C CA  . VAL E 1 171 ? -26.465 41.575 -9.904  1.00 30.94  ? 152  VAL E CA  1 
ATOM   7617 C C   . VAL E 1 171 ? -27.808 41.038 -9.494  1.00 27.07  ? 152  VAL E C   1 
ATOM   7618 O O   . VAL E 1 171 ? -27.972 40.584 -8.378  1.00 32.50  ? 152  VAL E O   1 
ATOM   7619 C CB  . VAL E 1 171 ? -25.596 40.391 -10.346 1.00 27.40  ? 152  VAL E CB  1 
ATOM   7620 C CG1 . VAL E 1 171 ? -24.482 40.866 -11.242 1.00 22.86  ? 152  VAL E CG1 1 
ATOM   7621 C CG2 . VAL E 1 171 ? -25.037 39.676 -9.138  1.00 29.17  ? 152  VAL E CG2 1 
ATOM   7622 N N   . ASP E 1 172 ? -28.761 41.084 -10.415 1.00 37.42  ? 153  ASP E N   1 
ATOM   7623 C CA  . ASP E 1 172 ? -30.134 40.658 -10.159 1.00 38.14  ? 153  ASP E CA  1 
ATOM   7624 C C   . ASP E 1 172 ? -30.673 39.937 -11.386 1.00 38.24  ? 153  ASP E C   1 
ATOM   7625 O O   . ASP E 1 172 ? -30.320 40.292 -12.505 1.00 37.05  ? 153  ASP E O   1 
ATOM   7626 C CB  . ASP E 1 172 ? -31.013 41.872 -9.863  1.00 39.30  ? 153  ASP E CB  1 
ATOM   7627 C CG  . ASP E 1 172 ? -30.306 42.909 -8.989  1.00 52.80  ? 153  ASP E CG  1 
ATOM   7628 O OD1 . ASP E 1 172 ? -30.242 42.703 -7.748  1.00 58.71  ? 153  ASP E OD1 1 
ATOM   7629 O OD2 . ASP E 1 172 ? -29.811 43.923 -9.547  1.00 49.29  ? 153  ASP E OD2 1 
ATOM   7630 N N   . PRO E 1 173 ? -31.509 38.903 -11.177 1.00 40.38  ? 154  PRO E N   1 
ATOM   7631 C CA  . PRO E 1 173 ? -32.187 38.210 -12.279 1.00 34.61  ? 154  PRO E CA  1 
ATOM   7632 C C   . PRO E 1 173 ? -33.271 39.097 -12.874 1.00 47.83  ? 154  PRO E C   1 
ATOM   7633 O O   . PRO E 1 173 ? -33.770 39.988 -12.182 1.00 46.47  ? 154  PRO E O   1 
ATOM   7634 C CB  . PRO E 1 173 ? -32.843 37.031 -11.588 1.00 33.32  ? 154  PRO E CB  1 
ATOM   7635 C CG  . PRO E 1 173 ? -32.123 36.897 -10.288 1.00 30.31  ? 154  PRO E CG  1 
ATOM   7636 C CD  . PRO E 1 173 ? -31.764 38.253 -9.881  1.00 30.96  ? 154  PRO E CD  1 
ATOM   7637 N N   . THR E 1 174 ? -33.639 38.848 -14.129 1.00 54.89  ? 155  THR E N   1 
ATOM   7638 C CA  . THR E 1 174 ? -34.594 39.703 -14.835 1.00 52.37  ? 155  THR E CA  1 
ATOM   7639 C C   . THR E 1 174 ? -36.042 39.373 -14.488 1.00 49.74  ? 155  THR E C   1 
ATOM   7640 O O   . THR E 1 174 ? -36.412 38.208 -14.377 1.00 53.83  ? 155  THR E O   1 
ATOM   7641 C CB  . THR E 1 174 ? -34.391 39.616 -16.360 1.00 64.53  ? 155  THR E CB  1 
ATOM   7642 O OG1 . THR E 1 174 ? -33.139 40.232 -16.710 1.00 58.65  ? 155  THR E OG1 1 
ATOM   7643 C CG2 . THR E 1 174 ? -35.532 40.313 -17.097 1.00 75.58  ? 155  THR E CG2 1 
ATOM   7644 N N   . SER E 1 178 ? -40.763 34.218 -18.463 1.00 71.66  ? 159  SER E N   1 
ATOM   7645 C CA  . SER E 1 178 ? -40.084 33.873 -19.713 1.00 74.06  ? 159  SER E CA  1 
ATOM   7646 C C   . SER E 1 178 ? -40.530 32.520 -20.275 1.00 75.74  ? 159  SER E C   1 
ATOM   7647 O O   . SER E 1 178 ? -41.459 31.894 -19.755 1.00 70.65  ? 159  SER E O   1 
ATOM   7648 C CB  . SER E 1 178 ? -38.563 33.867 -19.518 1.00 70.05  ? 159  SER E CB  1 
ATOM   7649 O OG  . SER E 1 178 ? -38.070 35.153 -19.185 1.00 66.70  ? 159  SER E OG  1 
ATOM   7650 N N   . ASP E 1 179 ? -39.873 32.092 -21.353 1.00 78.45  ? 160  ASP E N   1 
ATOM   7651 C CA  . ASP E 1 179 ? -39.988 30.714 -21.853 1.00 72.55  ? 160  ASP E CA  1 
ATOM   7652 C C   . ASP E 1 179 ? -38.596 30.145 -22.162 1.00 74.95  ? 160  ASP E C   1 
ATOM   7653 O O   . ASP E 1 179 ? -37.895 30.659 -23.044 1.00 76.67  ? 160  ASP E O   1 
ATOM   7654 C CB  . ASP E 1 179 ? -40.885 30.630 -23.093 1.00 64.17  ? 160  ASP E CB  1 
ATOM   7655 C CG  . ASP E 1 179 ? -40.953 29.205 -23.683 1.00 81.47  ? 160  ASP E CG  1 
ATOM   7656 O OD1 . ASP E 1 179 ? -40.833 28.210 -22.920 1.00 84.32  ? 160  ASP E OD1 1 
ATOM   7657 O OD2 . ASP E 1 179 ? -41.129 29.077 -24.918 1.00 81.19  ? 160  ASP E OD2 1 
ATOM   7658 N N   . ASP E 1 180 ? -38.217 29.085 -21.434 1.00 65.91  ? 161  ASP E N   1 
ATOM   7659 C CA  . ASP E 1 180 ? -36.855 28.523 -21.454 1.00 57.85  ? 161  ASP E CA  1 
ATOM   7660 C C   . ASP E 1 180 ? -36.349 28.268 -22.861 1.00 57.63  ? 161  ASP E C   1 
ATOM   7661 O O   . ASP E 1 180 ? -35.258 28.708 -23.261 1.00 48.23  ? 161  ASP E O   1 
ATOM   7662 C CB  . ASP E 1 180 ? -36.799 27.179 -20.713 1.00 59.95  ? 161  ASP E CB  1 
ATOM   7663 C CG  . ASP E 1 180 ? -37.987 26.942 -19.770 1.00 70.88  ? 161  ASP E CG  1 
ATOM   7664 O OD1 . ASP E 1 180 ? -38.148 27.731 -18.804 1.00 67.38  ? 161  ASP E OD1 1 
ATOM   7665 O OD2 . ASP E 1 180 ? -38.717 25.925 -19.962 1.00 68.08  ? 161  ASP E OD2 1 
ATOM   7666 N N   . SER E 1 181 ? -37.196 27.546 -23.589 1.00 64.17  ? 162  SER E N   1 
ATOM   7667 C CA  . SER E 1 181 ? -36.912 26.964 -24.896 1.00 66.51  ? 162  SER E CA  1 
ATOM   7668 C C   . SER E 1 181 ? -37.200 27.932 -26.037 1.00 66.11  ? 162  SER E C   1 
ATOM   7669 O O   . SER E 1 181 ? -37.206 27.524 -27.209 1.00 66.94  ? 162  SER E O   1 
ATOM   7670 C CB  . SER E 1 181 ? -37.776 25.699 -25.098 1.00 62.23  ? 162  SER E CB  1 
ATOM   7671 O OG  . SER E 1 181 ? -37.305 24.583 -24.346 1.00 60.03  ? 162  SER E OG  1 
ATOM   7672 N N   . GLU E 1 182 ? -37.442 29.197 -25.702 1.00 55.07  ? 163  GLU E N   1 
ATOM   7673 C CA  . GLU E 1 182 ? -37.920 30.157 -26.686 1.00 51.46  ? 163  GLU E CA  1 
ATOM   7674 C C   . GLU E 1 182 ? -36.986 30.264 -27.889 1.00 52.60  ? 163  GLU E C   1 
ATOM   7675 O O   . GLU E 1 182 ? -37.445 30.361 -29.031 1.00 54.22  ? 163  GLU E O   1 
ATOM   7676 C CB  . GLU E 1 182 ? -38.130 31.526 -26.048 1.00 60.70  ? 163  GLU E CB  1 
ATOM   7677 C CG  . GLU E 1 182 ? -38.846 32.509 -26.957 1.00 63.64  ? 163  GLU E CG  1 
ATOM   7678 C CD  . GLU E 1 182 ? -38.954 33.908 -26.362 1.00 74.48  ? 163  GLU E CD  1 
ATOM   7679 O OE1 . GLU E 1 182 ? -38.526 34.118 -25.198 1.00 71.07  ? 163  GLU E OE1 1 
ATOM   7680 O OE2 . GLU E 1 182 ? -39.474 34.802 -27.072 1.00 89.65  ? 163  GLU E OE2 1 
ATOM   7681 N N   . TYR E 1 183 ? -35.679 30.234 -27.631 1.00 47.49  ? 164  TYR E N   1 
ATOM   7682 C CA  . TYR E 1 183 ? -34.692 30.260 -28.709 1.00 42.13  ? 164  TYR E CA  1 
ATOM   7683 C C   . TYR E 1 183 ? -33.866 28.983 -28.760 1.00 42.69  ? 164  TYR E C   1 
ATOM   7684 O O   . TYR E 1 183 ? -32.835 28.941 -29.435 1.00 34.22  ? 164  TYR E O   1 
ATOM   7685 C CB  . TYR E 1 183 ? -33.750 31.446 -28.557 1.00 37.02  ? 164  TYR E CB  1 
ATOM   7686 C CG  . TYR E 1 183 ? -34.451 32.761 -28.362 1.00 48.55  ? 164  TYR E CG  1 
ATOM   7687 C CD1 . TYR E 1 183 ? -35.281 33.274 -29.351 1.00 54.20  ? 164  TYR E CD1 1 
ATOM   7688 C CD2 . TYR E 1 183 ? -34.281 33.495 -27.189 1.00 42.05  ? 164  TYR E CD2 1 
ATOM   7689 C CE1 . TYR E 1 183 ? -35.932 34.487 -29.186 1.00 60.24  ? 164  TYR E CE1 1 
ATOM   7690 C CE2 . TYR E 1 183 ? -34.926 34.705 -27.004 1.00 43.08  ? 164  TYR E CE2 1 
ATOM   7691 C CZ  . TYR E 1 183 ? -35.753 35.203 -28.012 1.00 60.42  ? 164  TYR E CZ  1 
ATOM   7692 O OH  . TYR E 1 183 ? -36.411 36.415 -27.861 1.00 62.24  ? 164  TYR E OH  1 
ATOM   7693 N N   . PHE E 1 184 ? -34.312 27.952 -28.038 1.00 44.64  ? 165  PHE E N   1 
ATOM   7694 C CA  . PHE E 1 184 ? -33.560 26.706 -27.961 1.00 31.77  ? 165  PHE E CA  1 
ATOM   7695 C C   . PHE E 1 184 ? -33.690 25.928 -29.245 1.00 32.44  ? 165  PHE E C   1 
ATOM   7696 O O   . PHE E 1 184 ? -34.770 25.881 -29.834 1.00 40.01  ? 165  PHE E O   1 
ATOM   7697 C CB  . PHE E 1 184 ? -33.998 25.846 -26.784 1.00 30.15  ? 165  PHE E CB  1 
ATOM   7698 C CG  . PHE E 1 184 ? -33.029 24.747 -26.464 1.00 29.04  ? 165  PHE E CG  1 
ATOM   7699 C CD1 . PHE E 1 184 ? -31.781 25.041 -25.948 1.00 23.99  ? 165  PHE E CD1 1 
ATOM   7700 C CD2 . PHE E 1 184 ? -33.362 23.422 -26.680 1.00 32.33  ? 165  PHE E CD2 1 
ATOM   7701 C CE1 . PHE E 1 184 ? -30.886 24.029 -25.658 1.00 28.17  ? 165  PHE E CE1 1 
ATOM   7702 C CE2 . PHE E 1 184 ? -32.471 22.399 -26.389 1.00 26.72  ? 165  PHE E CE2 1 
ATOM   7703 C CZ  . PHE E 1 184 ? -31.238 22.697 -25.881 1.00 27.39  ? 165  PHE E CZ  1 
ATOM   7704 N N   . SER E 1 185 ? -32.584 25.326 -29.674 1.00 30.97  ? 166  SER E N   1 
ATOM   7705 C CA  . SER E 1 185 ? -32.522 24.626 -30.953 1.00 33.64  ? 166  SER E CA  1 
ATOM   7706 C C   . SER E 1 185 ? -33.348 23.349 -30.938 1.00 37.50  ? 166  SER E C   1 
ATOM   7707 O O   . SER E 1 185 ? -33.204 22.512 -30.040 1.00 42.08  ? 166  SER E O   1 
ATOM   7708 C CB  . SER E 1 185 ? -31.070 24.291 -31.305 1.00 31.87  ? 166  SER E CB  1 
ATOM   7709 O OG  . SER E 1 185 ? -31.001 23.695 -32.588 1.00 33.76  ? 166  SER E OG  1 
ATOM   7710 N N   . GLN E 1 186 ? -34.211 23.200 -31.937 1.00 38.72  ? 167  GLN E N   1 
ATOM   7711 C CA  . GLN E 1 186 ? -34.979 21.965 -32.103 1.00 41.98  ? 167  GLN E CA  1 
ATOM   7712 C C   . GLN E 1 186 ? -34.082 20.799 -32.519 1.00 40.82  ? 167  GLN E C   1 
ATOM   7713 O O   . GLN E 1 186 ? -34.468 19.645 -32.379 1.00 42.77  ? 167  GLN E O   1 
ATOM   7714 C CB  . GLN E 1 186 ? -36.083 22.157 -33.145 1.00 38.89  ? 167  GLN E CB  1 
ATOM   7715 C CG  . GLN E 1 186 ? -35.657 23.047 -34.303 1.00 44.95  ? 167  GLN E CG  1 
ATOM   7716 C CD  . GLN E 1 186 ? -36.670 23.115 -35.440 1.00 55.68  ? 167  GLN E CD  1 
ATOM   7717 O OE1 . GLN E 1 186 ? -37.425 22.165 -35.695 1.00 60.91  ? 167  GLN E OE1 1 
ATOM   7718 N NE2 . GLN E 1 186 ? -36.674 24.247 -36.144 1.00 61.74  ? 167  GLN E NE2 1 
ATOM   7719 N N   . TYR E 1 187 ? -32.885 21.098 -33.025 1.00 35.69  ? 168  TYR E N   1 
ATOM   7720 C CA  . TYR E 1 187 ? -32.004 20.047 -33.540 1.00 34.64  ? 168  TYR E CA  1 
ATOM   7721 C C   . TYR E 1 187 ? -31.014 19.495 -32.505 1.00 32.67  ? 168  TYR E C   1 
ATOM   7722 O O   . TYR E 1 187 ? -30.285 18.538 -32.774 1.00 31.69  ? 168  TYR E O   1 
ATOM   7723 C CB  . TYR E 1 187 ? -31.306 20.508 -34.837 1.00 33.90  ? 168  TYR E CB  1 
ATOM   7724 C CG  . TYR E 1 187 ? -32.300 20.957 -35.891 1.00 37.68  ? 168  TYR E CG  1 
ATOM   7725 C CD1 . TYR E 1 187 ? -33.224 20.063 -36.419 1.00 45.52  ? 168  TYR E CD1 1 
ATOM   7726 C CD2 . TYR E 1 187 ? -32.339 22.268 -36.335 1.00 38.01  ? 168  TYR E CD2 1 
ATOM   7727 C CE1 . TYR E 1 187 ? -34.153 20.454 -37.365 1.00 41.15  ? 168  TYR E CE1 1 
ATOM   7728 C CE2 . TYR E 1 187 ? -33.270 22.676 -37.290 1.00 44.84  ? 168  TYR E CE2 1 
ATOM   7729 C CZ  . TYR E 1 187 ? -34.172 21.754 -37.801 1.00 47.55  ? 168  TYR E CZ  1 
ATOM   7730 O OH  . TYR E 1 187 ? -35.109 22.120 -38.744 1.00 52.14  ? 168  TYR E OH  1 
ATOM   7731 N N   . SER E 1 188 ? -30.994 20.093 -31.318 1.00 32.54  ? 169  SER E N   1 
ATOM   7732 C CA  . SER E 1 188 ? -30.170 19.580 -30.222 1.00 33.16  ? 169  SER E CA  1 
ATOM   7733 C C   . SER E 1 188 ? -30.563 18.136 -29.885 1.00 30.90  ? 169  SER E C   1 
ATOM   7734 O O   . SER E 1 188 ? -31.703 17.729 -30.118 1.00 35.55  ? 169  SER E O   1 
ATOM   7735 C CB  . SER E 1 188 ? -30.318 20.477 -28.978 1.00 30.01  ? 169  SER E CB  1 
ATOM   7736 O OG  . SER E 1 188 ? -29.451 20.056 -27.938 1.00 31.30  ? 169  SER E OG  1 
ATOM   7737 N N   . ARG E 1 189 ? -29.626 17.359 -29.349 1.00 29.65  ? 170  ARG E N   1 
ATOM   7738 C CA  . ARG E 1 189 ? -29.958 16.023 -28.843 1.00 30.35  ? 170  ARG E CA  1 
ATOM   7739 C C   . ARG E 1 189 ? -30.667 16.100 -27.485 1.00 35.86  ? 170  ARG E C   1 
ATOM   7740 O O   . ARG E 1 189 ? -31.011 15.073 -26.895 1.00 32.31  ? 170  ARG E O   1 
ATOM   7741 C CB  . ARG E 1 189 ? -28.709 15.147 -28.689 1.00 27.84  ? 170  ARG E CB  1 
ATOM   7742 C CG  . ARG E 1 189 ? -27.964 14.875 -29.963 1.00 36.23  ? 170  ARG E CG  1 
ATOM   7743 C CD  . ARG E 1 189 ? -27.481 13.444 -29.996 1.00 49.29  ? 170  ARG E CD  1 
ATOM   7744 N NE  . ARG E 1 189 ? -26.515 13.123 -28.943 1.00 57.93  ? 170  ARG E NE  1 
ATOM   7745 C CZ  . ARG E 1 189 ? -26.270 11.884 -28.501 1.00 66.02  ? 170  ARG E CZ  1 
ATOM   7746 N NH1 . ARG E 1 189 ? -26.931 10.839 -29.001 1.00 55.83  ? 170  ARG E NH1 1 
ATOM   7747 N NH2 . ARG E 1 189 ? -25.369 11.685 -27.544 1.00 63.98  ? 170  ARG E NH2 1 
ATOM   7748 N N   . PHE E 1 190 ? -30.852 17.316 -26.974 1.00 31.64  ? 171  PHE E N   1 
ATOM   7749 C CA  . PHE E 1 190 ? -31.402 17.487 -25.635 1.00 29.32  ? 171  PHE E CA  1 
ATOM   7750 C C   . PHE E 1 190 ? -32.594 18.428 -25.645 1.00 27.79  ? 171  PHE E C   1 
ATOM   7751 O O   . PHE E 1 190 ? -32.830 19.143 -26.632 1.00 30.80  ? 171  PHE E O   1 
ATOM   7752 C CB  . PHE E 1 190 ? -30.331 18.013 -24.678 1.00 25.59  ? 171  PHE E CB  1 
ATOM   7753 C CG  . PHE E 1 190 ? -29.078 17.175 -24.640 1.00 22.89  ? 171  PHE E CG  1 
ATOM   7754 C CD1 . PHE E 1 190 ? -28.076 17.360 -25.588 1.00 20.22  ? 171  PHE E CD1 1 
ATOM   7755 C CD2 . PHE E 1 190 ? -28.889 16.221 -23.637 1.00 24.36  ? 171  PHE E CD2 1 
ATOM   7756 C CE1 . PHE E 1 190 ? -26.908 16.597 -25.552 1.00 24.64  ? 171  PHE E CE1 1 
ATOM   7757 C CE2 . PHE E 1 190 ? -27.722 15.447 -23.591 1.00 28.33  ? 171  PHE E CE2 1 
ATOM   7758 C CZ  . PHE E 1 190 ? -26.729 15.635 -24.556 1.00 24.53  ? 171  PHE E CZ  1 
ATOM   7759 N N   . GLU E 1 191 ? -33.346 18.422 -24.549 1.00 20.39  ? 172  GLU E N   1 
ATOM   7760 C CA  . GLU E 1 191 ? -34.457 19.353 -24.412 1.00 32.09  ? 172  GLU E CA  1 
ATOM   7761 C C   . GLU E 1 191 ? -34.493 19.973 -23.017 1.00 34.31  ? 172  GLU E C   1 
ATOM   7762 O O   . GLU E 1 191 ? -34.053 19.347 -22.040 1.00 34.21  ? 172  GLU E O   1 
ATOM   7763 C CB  . GLU E 1 191 ? -35.789 18.679 -24.762 1.00 39.32  ? 172  GLU E CB  1 
ATOM   7764 C CG  . GLU E 1 191 ? -36.161 17.486 -23.895 1.00 42.30  ? 172  GLU E CG  1 
ATOM   7765 C CD  . GLU E 1 191 ? -37.375 16.742 -24.444 1.00 50.88  ? 172  GLU E CD  1 
ATOM   7766 O OE1 . GLU E 1 191 ? -38.035 17.314 -25.342 1.00 53.72  ? 172  GLU E OE1 1 
ATOM   7767 O OE2 . GLU E 1 191 ? -37.661 15.599 -23.989 1.00 47.08  ? 172  GLU E OE2 1 
ATOM   7768 N N   . ILE E 1 192 ? -34.996 21.205 -22.934 1.00 32.60  ? 173  ILE E N   1 
ATOM   7769 C CA  . ILE E 1 192 ? -35.079 21.917 -21.653 1.00 37.37  ? 173  ILE E CA  1 
ATOM   7770 C C   . ILE E 1 192 ? -36.419 21.684 -20.950 1.00 29.50  ? 173  ILE E C   1 
ATOM   7771 O O   . ILE E 1 192 ? -37.476 21.901 -21.525 1.00 31.37  ? 173  ILE E O   1 
ATOM   7772 C CB  . ILE E 1 192 ? -34.829 23.440 -21.822 1.00 38.46  ? 173  ILE E CB  1 
ATOM   7773 C CG1 . ILE E 1 192 ? -33.451 23.676 -22.437 1.00 32.90  ? 173  ILE E CG1 1 
ATOM   7774 C CG2 . ILE E 1 192 ? -34.960 24.171 -20.482 1.00 30.93  ? 173  ILE E CG2 1 
ATOM   7775 C CD1 . ILE E 1 192 ? -33.139 25.129 -22.687 1.00 34.82  ? 173  ILE E CD1 1 
ATOM   7776 N N   . LEU E 1 193 ? -36.357 21.236 -19.703 1.00 28.29  ? 174  LEU E N   1 
ATOM   7777 C CA  . LEU E 1 193 ? -37.559 20.993 -18.911 1.00 33.60  ? 174  LEU E CA  1 
ATOM   7778 C C   . LEU E 1 193 ? -37.930 22.244 -18.132 1.00 33.09  ? 174  LEU E C   1 
ATOM   7779 O O   . LEU E 1 193 ? -39.097 22.595 -18.048 1.00 51.89  ? 174  LEU E O   1 
ATOM   7780 C CB  . LEU E 1 193 ? -37.365 19.798 -17.967 1.00 24.71  ? 174  LEU E CB  1 
ATOM   7781 C CG  . LEU E 1 193 ? -36.869 18.555 -18.695 1.00 22.82  ? 174  LEU E CG  1 
ATOM   7782 C CD1 . LEU E 1 193 ? -36.582 17.425 -17.738 1.00 27.24  ? 174  LEU E CD1 1 
ATOM   7783 C CD2 . LEU E 1 193 ? -37.847 18.131 -19.796 1.00 23.45  ? 174  LEU E CD2 1 
ATOM   7784 N N   . ASP E 1 194 ? -36.934 22.921 -17.575 1.00 35.01  ? 175  ASP E N   1 
ATOM   7785 C CA  . ASP E 1 194 ? -37.177 24.145 -16.820 1.00 42.90  ? 175  ASP E CA  1 
ATOM   7786 C C   . ASP E 1 194 ? -35.915 24.985 -16.582 1.00 38.28  ? 175  ASP E C   1 
ATOM   7787 O O   . ASP E 1 194 ? -34.802 24.455 -16.490 1.00 34.26  ? 175  ASP E O   1 
ATOM   7788 C CB  . ASP E 1 194 ? -37.828 23.815 -15.471 1.00 37.45  ? 175  ASP E CB  1 
ATOM   7789 C CG  . ASP E 1 194 ? -38.544 25.013 -14.873 1.00 53.81  ? 175  ASP E CG  1 
ATOM   7790 O OD1 . ASP E 1 194 ? -39.096 25.820 -15.663 1.00 55.55  ? 175  ASP E OD1 1 
ATOM   7791 O OD2 . ASP E 1 194 ? -38.545 25.159 -13.628 1.00 61.71  ? 175  ASP E OD2 1 
ATOM   7792 N N   . VAL E 1 195 ? -36.101 26.296 -16.463 1.00 38.28  ? 176  VAL E N   1 
ATOM   7793 C CA  . VAL E 1 195 ? -35.007 27.194 -16.077 1.00 44.70  ? 176  VAL E CA  1 
ATOM   7794 C C   . VAL E 1 195 ? -35.393 28.121 -14.917 1.00 41.95  ? 176  VAL E C   1 
ATOM   7795 O O   . VAL E 1 195 ? -36.308 28.930 -15.059 1.00 35.77  ? 176  VAL E O   1 
ATOM   7796 C CB  . VAL E 1 195 ? -34.544 28.090 -17.251 1.00 36.12  ? 176  VAL E CB  1 
ATOM   7797 C CG1 . VAL E 1 195 ? -33.462 29.023 -16.781 1.00 40.20  ? 176  VAL E CG1 1 
ATOM   7798 C CG2 . VAL E 1 195 ? -34.026 27.265 -18.403 1.00 30.36  ? 176  VAL E CG2 1 
ATOM   7799 N N   . THR E 1 196 ? -34.686 28.015 -13.788 1.00 37.34  ? 177  THR E N   1 
ATOM   7800 C CA  . THR E 1 196 ? -34.935 28.890 -12.639 1.00 37.62  ? 177  THR E CA  1 
ATOM   7801 C C   . THR E 1 196 ? -33.711 29.748 -12.318 1.00 39.11  ? 177  THR E C   1 
ATOM   7802 O O   . THR E 1 196 ? -32.578 29.359 -12.620 1.00 39.30  ? 177  THR E O   1 
ATOM   7803 C CB  . THR E 1 196 ? -35.375 28.103 -11.382 1.00 42.02  ? 177  THR E CB  1 
ATOM   7804 O OG1 . THR E 1 196 ? -34.330 27.201 -10.987 1.00 53.15  ? 177  THR E OG1 1 
ATOM   7805 C CG2 . THR E 1 196 ? -36.648 27.318 -11.659 1.00 46.58  ? 177  THR E CG2 1 
ATOM   7806 N N   . GLN E 1 197 ? -33.949 30.911 -11.707 1.00 34.69  ? 178  GLN E N   1 
ATOM   7807 C CA  . GLN E 1 197 ? -32.888 31.862 -11.360 1.00 30.33  ? 178  GLN E CA  1 
ATOM   7808 C C   . GLN E 1 197 ? -32.991 32.243 -9.892  1.00 34.82  ? 178  GLN E C   1 
ATOM   7809 O O   . GLN E 1 197 ? -34.090 32.449 -9.378  1.00 51.52  ? 178  GLN E O   1 
ATOM   7810 C CB  . GLN E 1 197 ? -33.019 33.132 -12.206 1.00 31.42  ? 178  GLN E CB  1 
ATOM   7811 C CG  . GLN E 1 197 ? -33.072 32.885 -13.726 1.00 45.32  ? 178  GLN E CG  1 
ATOM   7812 C CD  . GLN E 1 197 ? -32.613 34.097 -14.570 1.00 60.25  ? 178  GLN E CD  1 
ATOM   7813 O OE1 . GLN E 1 197 ? -32.817 35.251 -14.182 1.00 64.86  ? 178  GLN E OE1 1 
ATOM   7814 N NE2 . GLN E 1 197 ? -31.986 33.826 -15.731 1.00 47.30  ? 178  GLN E NE2 1 
ATOM   7815 N N   . LYS E 1 198 ? -31.871 32.334 -9.195  1.00 28.30  ? 179  LYS E N   1 
ATOM   7816 C CA  . LYS E 1 198 ? -31.926 32.912 -7.861  1.00 27.25  ? 179  LYS E CA  1 
ATOM   7817 C C   . LYS E 1 198 ? -30.663 33.729 -7.565  1.00 30.28  ? 179  LYS E C   1 
ATOM   7818 O O   . LYS E 1 198 ? -29.620 33.519 -8.187  1.00 31.76  ? 179  LYS E O   1 
ATOM   7819 C CB  . LYS E 1 198 ? -32.188 31.845 -6.798  1.00 26.03  ? 179  LYS E CB  1 
ATOM   7820 C CG  . LYS E 1 198 ? -30.913 31.246 -6.213  1.00 45.95  ? 179  LYS E CG  1 
ATOM   7821 C CD  . LYS E 1 198 ? -31.209 30.347 -5.016  1.00 60.16  ? 179  LYS E CD  1 
ATOM   7822 C CE  . LYS E 1 198 ? -29.950 29.583 -4.565  1.00 59.04  ? 179  LYS E CE  1 
ATOM   7823 N NZ  . LYS E 1 198 ? -30.202 28.706 -3.351  1.00 63.08  ? 179  LYS E NZ  1 
ATOM   7824 N N   . LYS E 1 199 ? -30.764 34.671 -6.630  1.00 27.09  ? 180  LYS E N   1 
ATOM   7825 C CA  . LYS E 1 199 ? -29.639 35.536 -6.288  1.00 22.19  ? 180  LYS E CA  1 
ATOM   7826 C C   . LYS E 1 199 ? -28.928 35.144 -4.982  1.00 25.10  ? 180  LYS E C   1 
ATOM   7827 O O   . LYS E 1 199 ? -29.573 34.903 -3.957  1.00 29.86  ? 180  LYS E O   1 
ATOM   7828 C CB  . LYS E 1 199 ? -30.128 36.972 -6.193  1.00 29.40  ? 180  LYS E CB  1 
ATOM   7829 C CG  . LYS E 1 199 ? -29.159 37.906 -5.523  1.00 30.40  ? 180  LYS E CG  1 
ATOM   7830 C CD  . LYS E 1 199 ? -29.713 39.300 -5.509  1.00 35.67  ? 180  LYS E CD  1 
ATOM   7831 C CE  . LYS E 1 199 ? -28.783 40.228 -4.762  1.00 49.85  ? 180  LYS E CE  1 
ATOM   7832 N NZ  . LYS E 1 199 ? -29.197 41.671 -4.893  1.00 44.57  ? 180  LYS E NZ  1 
ATOM   7833 N N   . ASN E 1 200 ? -27.598 35.072 -5.021  1.00 27.08  ? 181  ASN E N   1 
ATOM   7834 C CA  . ASN E 1 200 ? -26.811 34.811 -3.815  1.00 28.42  ? 181  ASN E CA  1 
ATOM   7835 C C   . ASN E 1 200 ? -25.895 35.959 -3.422  1.00 29.71  ? 181  ASN E C   1 
ATOM   7836 O O   . ASN E 1 200 ? -25.478 36.748 -4.255  1.00 30.64  ? 181  ASN E O   1 
ATOM   7837 C CB  . ASN E 1 200 ? -25.960 33.547 -3.956  1.00 31.56  ? 181  ASN E CB  1 
ATOM   7838 C CG  . ASN E 1 200 ? -26.749 32.354 -4.468  1.00 38.69  ? 181  ASN E CG  1 
ATOM   7839 O OD1 . ASN E 1 200 ? -27.511 31.712 -3.729  1.00 37.84  ? 181  ASN E OD1 1 
ATOM   7840 N ND2 . ASN E 1 200 ? -26.552 32.035 -5.744  1.00 39.44  ? 181  ASN E ND2 1 
ATOM   7841 N N   . SER E 1 201 ? -25.579 36.040 -2.137  1.00 38.89  ? 182  SER E N   1 
ATOM   7842 C CA  . SER E 1 201 ? -24.651 37.042 -1.628  1.00 33.89  ? 182  SER E CA  1 
ATOM   7843 C C   . SER E 1 201 ? -23.662 36.306 -0.753  1.00 34.99  ? 182  SER E C   1 
ATOM   7844 O O   . SER E 1 201 ? -24.005 35.811 0.312   1.00 48.19  ? 182  SER E O   1 
ATOM   7845 C CB  . SER E 1 201 ? -25.387 38.112 -0.824  1.00 38.87  ? 182  SER E CB  1 
ATOM   7846 O OG  . SER E 1 201 ? -24.531 39.189 -0.495  1.00 46.35  ? 182  SER E OG  1 
ATOM   7847 N N   . VAL E 1 202 ? -22.428 36.227 -1.217  1.00 31.30  ? 183  VAL E N   1 
ATOM   7848 C CA  . VAL E 1 202 ? -21.409 35.382 -0.597  1.00 36.45  ? 183  VAL E CA  1 
ATOM   7849 C C   . VAL E 1 202 ? -20.242 36.167 0.011   1.00 38.51  ? 183  VAL E C   1 
ATOM   7850 O O   . VAL E 1 202 ? -19.736 37.117 -0.597  1.00 35.15  ? 183  VAL E O   1 
ATOM   7851 C CB  . VAL E 1 202 ? -20.834 34.455 -1.659  1.00 31.50  ? 183  VAL E CB  1 
ATOM   7852 C CG1 . VAL E 1 202 ? -19.699 33.630 -1.103  1.00 23.74  ? 183  VAL E CG1 1 
ATOM   7853 C CG2 . VAL E 1 202 ? -21.947 33.597 -2.233  1.00 47.14  ? 183  VAL E CG2 1 
ATOM   7854 N N   . THR E 1 203 ? -19.812 35.779 1.208   1.00 40.78  ? 184  THR E N   1 
ATOM   7855 C CA  . THR E 1 203 ? -18.590 36.358 1.772   1.00 43.85  ? 184  THR E CA  1 
ATOM   7856 C C   . THR E 1 203 ? -17.399 35.389 1.678   1.00 53.01  ? 184  THR E C   1 
ATOM   7857 O O   . THR E 1 203 ? -17.431 34.289 2.252   1.00 48.18  ? 184  THR E O   1 
ATOM   7858 C CB  . THR E 1 203 ? -18.769 36.814 3.222   1.00 41.24  ? 184  THR E CB  1 
ATOM   7859 O OG1 . THR E 1 203 ? -19.657 37.943 3.274   1.00 25.39  ? 184  THR E OG1 1 
ATOM   7860 C CG2 . THR E 1 203 ? -17.417 37.201 3.799   1.00 50.34  ? 184  THR E CG2 1 
ATOM   7861 N N   . TYR E 1 204 ? -16.357 35.801 0.948   1.00 60.19  ? 185  TYR E N   1 
ATOM   7862 C CA  . TYR E 1 204 ? -15.179 34.957 0.734   1.00 56.06  ? 185  TYR E CA  1 
ATOM   7863 C C   . TYR E 1 204 ? -14.139 35.170 1.830   1.00 72.30  ? 185  TYR E C   1 
ATOM   7864 O O   . TYR E 1 204 ? -14.187 36.170 2.569   1.00 68.43  ? 185  TYR E O   1 
ATOM   7865 C CB  . TYR E 1 204 ? -14.575 35.176 -0.658  1.00 49.26  ? 185  TYR E CB  1 
ATOM   7866 C CG  . TYR E 1 204 ? -15.506 34.790 -1.782  1.00 47.14  ? 185  TYR E CG  1 
ATOM   7867 C CD1 . TYR E 1 204 ? -16.415 35.703 -2.295  1.00 47.09  ? 185  TYR E CD1 1 
ATOM   7868 C CD2 . TYR E 1 204 ? -15.487 33.512 -2.321  1.00 45.59  ? 185  TYR E CD2 1 
ATOM   7869 C CE1 . TYR E 1 204 ? -17.283 35.353 -3.322  1.00 55.64  ? 185  TYR E CE1 1 
ATOM   7870 C CE2 . TYR E 1 204 ? -16.348 33.147 -3.352  1.00 46.19  ? 185  TYR E CE2 1 
ATOM   7871 C CZ  . TYR E 1 204 ? -17.247 34.073 -3.849  1.00 53.17  ? 185  TYR E CZ  1 
ATOM   7872 O OH  . TYR E 1 204 ? -18.120 33.737 -4.871  1.00 58.79  ? 185  TYR E OH  1 
ATOM   7873 N N   . SER E 1 205 ? -13.208 34.217 1.930   1.00 80.18  ? 186  SER E N   1 
ATOM   7874 C CA  . SER E 1 205 ? -12.172 34.210 2.975   1.00 84.70  ? 186  SER E CA  1 
ATOM   7875 C C   . SER E 1 205 ? -11.162 35.362 2.859   1.00 81.26  ? 186  SER E C   1 
ATOM   7876 O O   . SER E 1 205 ? -10.460 35.685 3.819   1.00 78.63  ? 186  SER E O   1 
ATOM   7877 C CB  . SER E 1 205 ? -11.433 32.869 2.979   1.00 74.28  ? 186  SER E CB  1 
ATOM   7878 O OG  . SER E 1 205 ? -12.327 31.803 3.232   1.00 70.75  ? 186  SER E OG  1 
ATOM   7879 N N   . CYS E 1 206 ? -11.124 35.986 1.685   1.00 79.76  ? 187  CYS E N   1 
ATOM   7880 C CA  A CYS E 1 206 ? -10.196 37.087 1.393   0.38 78.81  ? 187  CYS E CA  1 
ATOM   7881 C CA  B CYS E 1 206 ? -10.190 37.058 1.400   0.62 78.46  ? 187  CYS E CA  1 
ATOM   7882 C C   . CYS E 1 206 ? -10.605 38.427 2.023   1.00 82.97  ? 187  CYS E C   1 
ATOM   7883 O O   . CYS E 1 206 ? -9.781  39.121 2.631   1.00 84.52  ? 187  CYS E O   1 
ATOM   7884 C CB  A CYS E 1 206 ? -9.984  37.250 -0.132  0.38 75.53  ? 187  CYS E CB  1 
ATOM   7885 C CB  B CYS E 1 206 ? -10.021 37.126 -0.127  0.62 75.87  ? 187  CYS E CB  1 
ATOM   7886 S SG  A CYS E 1 206 ? -11.268 38.166 -1.081  0.38 44.85  ? 187  CYS E SG  1 
ATOM   7887 S SG  B CYS E 1 206 ? -10.275 35.485 -0.944  0.62 52.07  ? 187  CYS E SG  1 
ATOM   7888 N N   . CYS E 1 207 ? -11.883 38.794 1.895   1.00 79.13  ? 188  CYS E N   1 
ATOM   7889 C CA  . CYS E 1 207 ? -12.364 40.144 2.235   1.00 77.49  ? 188  CYS E CA  1 
ATOM   7890 C C   . CYS E 1 207 ? -13.637 40.145 3.109   1.00 82.64  ? 188  CYS E C   1 
ATOM   7891 O O   . CYS E 1 207 ? -14.414 39.181 3.085   1.00 87.17  ? 188  CYS E O   1 
ATOM   7892 C CB  . CYS E 1 207 ? -12.630 40.901 0.921   1.00 78.07  ? 188  CYS E CB  1 
ATOM   7893 S SG  . CYS E 1 207 ? -12.020 39.999 -0.585  1.00 83.57  ? 188  CYS E SG  1 
ATOM   7894 N N   . PRO E 1 208 ? -13.863 41.228 3.879   1.00 78.67  ? 189  PRO E N   1 
ATOM   7895 C CA  . PRO E 1 208 ? -15.044 41.361 4.759   1.00 78.37  ? 189  PRO E CA  1 
ATOM   7896 C C   . PRO E 1 208 ? -16.329 41.802 4.032   1.00 76.09  ? 189  PRO E C   1 
ATOM   7897 O O   . PRO E 1 208 ? -17.398 41.907 4.650   1.00 67.39  ? 189  PRO E O   1 
ATOM   7898 C CB  . PRO E 1 208 ? -14.623 42.468 5.732   1.00 75.23  ? 189  PRO E CB  1 
ATOM   7899 C CG  . PRO E 1 208 ? -13.742 43.349 4.892   1.00 82.98  ? 189  PRO E CG  1 
ATOM   7900 C CD  . PRO E 1 208 ? -12.966 42.396 3.984   1.00 75.25  ? 189  PRO E CD  1 
ATOM   7901 N N   . GLU E 1 209 ? -16.208 42.079 2.735   1.00 73.35  ? 190  GLU E N   1 
ATOM   7902 C CA  . GLU E 1 209 ? -17.318 42.564 1.923   1.00 49.15  ? 190  GLU E CA  1 
ATOM   7903 C C   . GLU E 1 209 ? -18.060 41.396 1.276   1.00 46.34  ? 190  GLU E C   1 
ATOM   7904 O O   . GLU E 1 209 ? -17.486 40.309 1.086   1.00 49.47  ? 190  GLU E O   1 
ATOM   7905 C CB  . GLU E 1 209 ? -16.765 43.474 0.835   1.00 42.11  ? 190  GLU E CB  1 
ATOM   7906 C CG  . GLU E 1 209 ? -15.715 44.452 1.319   1.00 54.79  ? 190  GLU E CG  1 
ATOM   7907 C CD  . GLU E 1 209 ? -16.331 45.654 2.016   1.00 76.40  ? 190  GLU E CD  1 
ATOM   7908 O OE1 . GLU E 1 209 ? -17.576 45.675 2.175   1.00 80.21  ? 190  GLU E OE1 1 
ATOM   7909 O OE2 . GLU E 1 209 ? -15.575 46.579 2.398   1.00 82.54  1 190  GLU E OE2 1 
ATOM   7910 N N   . ALA E 1 210 ? -19.325 41.619 0.922   1.00 31.66  ? 191  ALA E N   1 
ATOM   7911 C CA  . ALA E 1 210 ? -20.111 40.589 0.238   1.00 30.59  ? 191  ALA E CA  1 
ATOM   7912 C C   . ALA E 1 210 ? -20.067 40.738 -1.287  1.00 30.57  ? 191  ALA E C   1 
ATOM   7913 O O   . ALA E 1 210 ? -20.071 41.849 -1.818  1.00 24.44  ? 191  ALA E O   1 
ATOM   7914 C CB  . ALA E 1 210 ? -21.533 40.622 0.714   1.00 26.82  ? 191  ALA E CB  1 
ATOM   7915 N N   . TYR E 1 211 ? -20.043 39.612 -1.988  1.00 30.62  ? 192  TYR E N   1 
ATOM   7916 C CA  . TYR E 1 211 ? -20.065 39.621 -3.447  1.00 27.78  ? 192  TYR E CA  1 
ATOM   7917 C C   . TYR E 1 211 ? -21.334 38.956 -3.991  1.00 26.41  ? 192  TYR E C   1 
ATOM   7918 O O   . TYR E 1 211 ? -21.558 37.771 -3.766  1.00 28.32  ? 192  TYR E O   1 
ATOM   7919 C CB  . TYR E 1 211 ? -18.829 38.904 -3.989  1.00 25.91  ? 192  TYR E CB  1 
ATOM   7920 C CG  . TYR E 1 211 ? -17.564 39.678 -3.771  1.00 28.07  ? 192  TYR E CG  1 
ATOM   7921 C CD1 . TYR E 1 211 ? -16.947 39.691 -2.535  1.00 33.57  ? 192  TYR E CD1 1 
ATOM   7922 C CD2 . TYR E 1 211 ? -16.989 40.415 -4.801  1.00 34.74  ? 192  TYR E CD2 1 
ATOM   7923 C CE1 . TYR E 1 211 ? -15.781 40.412 -2.319  1.00 37.42  ? 192  TYR E CE1 1 
ATOM   7924 C CE2 . TYR E 1 211 ? -15.816 41.138 -4.604  1.00 32.99  ? 192  TYR E CE2 1 
ATOM   7925 C CZ  . TYR E 1 211 ? -15.219 41.129 -3.354  1.00 36.14  ? 192  TYR E CZ  1 
ATOM   7926 O OH  . TYR E 1 211 ? -14.063 41.837 -3.124  1.00 42.25  ? 192  TYR E OH  1 
ATOM   7927 N N   . GLU E 1 212 ? -22.160 39.705 -4.711  1.00 20.28  ? 193  GLU E N   1 
ATOM   7928 C CA  . GLU E 1 212 ? -23.377 39.127 -5.250  1.00 20.47  ? 193  GLU E CA  1 
ATOM   7929 C C   . GLU E 1 212 ? -23.110 38.300 -6.511  1.00 25.39  ? 193  GLU E C   1 
ATOM   7930 O O   . GLU E 1 212 ? -22.204 38.613 -7.294  1.00 26.71  ? 193  GLU E O   1 
ATOM   7931 C CB  . GLU E 1 212 ? -24.411 40.211 -5.536  1.00 22.54  ? 193  GLU E CB  1 
ATOM   7932 C CG  . GLU E 1 212 ? -24.754 41.062 -4.333  1.00 30.66  ? 193  GLU E CG  1 
ATOM   7933 C CD  . GLU E 1 212 ? -25.890 42.049 -4.615  1.00 47.53  ? 193  GLU E CD  1 
ATOM   7934 O OE1 . GLU E 1 212 ? -26.413 42.073 -5.768  1.00 42.84  ? 193  GLU E OE1 1 
ATOM   7935 O OE2 . GLU E 1 212 ? -26.266 42.798 -3.677  1.00 48.36  ? 193  GLU E OE2 1 
ATOM   7936 N N   . ASP E 1 213 ? -23.906 37.243 -6.689  1.00 24.95  ? 194  ASP E N   1 
ATOM   7937 C CA  . ASP E 1 213 ? -23.964 36.489 -7.939  1.00 20.01  ? 194  ASP E CA  1 
ATOM   7938 C C   . ASP E 1 213 ? -25.373 35.973 -8.244  1.00 23.69  ? 194  ASP E C   1 
ATOM   7939 O O   . ASP E 1 213 ? -26.243 35.934 -7.377  1.00 26.21  ? 194  ASP E O   1 
ATOM   7940 C CB  . ASP E 1 213 ? -23.005 35.326 -7.903  1.00 24.61  ? 194  ASP E CB  1 
ATOM   7941 C CG  . ASP E 1 213 ? -23.248 34.415 -6.704  1.00 45.35  ? 194  ASP E CG  1 
ATOM   7942 O OD1 . ASP E 1 213 ? -24.165 33.548 -6.771  1.00 48.41  ? 194  ASP E OD1 1 
ATOM   7943 O OD2 . ASP E 1 213 ? -22.515 34.574 -5.693  1.00 46.44  ? 194  ASP E OD2 1 
ATOM   7944 N N   . VAL E 1 214 ? -25.594 35.592 -9.495  1.00 23.82  ? 195  VAL E N   1 
ATOM   7945 C CA  . VAL E 1 214 ? -26.835 34.951 -9.891  1.00 23.99  ? 195  VAL E CA  1 
ATOM   7946 C C   . VAL E 1 214 ? -26.580 33.480 -10.218 1.00 31.71  ? 195  VAL E C   1 
ATOM   7947 O O   . VAL E 1 214 ? -25.609 33.143 -10.910 1.00 28.84  ? 195  VAL E O   1 
ATOM   7948 C CB  . VAL E 1 214 ? -27.461 35.666 -11.089 1.00 24.55  ? 195  VAL E CB  1 
ATOM   7949 C CG1 . VAL E 1 214 ? -28.638 34.872 -11.643 1.00 28.28  ? 195  VAL E CG1 1 
ATOM   7950 C CG2 . VAL E 1 214 ? -27.904 37.059 -10.678 1.00 32.22  ? 195  VAL E CG2 1 
ATOM   7951 N N   . GLU E 1 215 ? -27.431 32.608 -9.676  1.00 31.50  ? 196  GLU E N   1 
ATOM   7952 C CA  . GLU E 1 215 ? -27.345 31.181 -9.938  1.00 32.44  ? 196  GLU E CA  1 
ATOM   7953 C C   . GLU E 1 215 ? -28.470 30.807 -10.893 1.00 29.89  ? 196  GLU E C   1 
ATOM   7954 O O   . GLU E 1 215 ? -29.645 31.048 -10.602 1.00 31.64  ? 196  GLU E O   1 
ATOM   7955 C CB  . GLU E 1 215 ? -27.470 30.390 -8.633  1.00 38.00  ? 196  GLU E CB  1 
ATOM   7956 C CG  . GLU E 1 215 ? -26.376 29.336 -8.403  1.00 47.67  ? 196  GLU E CG  1 
ATOM   7957 C CD  . GLU E 1 215 ? -26.469 28.654 -7.022  1.00 67.78  ? 196  GLU E CD  1 
ATOM   7958 O OE1 . GLU E 1 215 ? -27.596 28.232 -6.633  1.00 51.33  ? 196  GLU E OE1 1 
ATOM   7959 O OE2 . GLU E 1 215 ? -25.412 28.557 -6.332  1.00 71.32  ? 196  GLU E OE2 1 
ATOM   7960 N N   . VAL E 1 216 ? -28.121 30.226 -12.035 1.00 24.74  ? 197  VAL E N   1 
ATOM   7961 C CA  . VAL E 1 216 ? -29.139 29.824 -12.999 1.00 26.02  ? 197  VAL E CA  1 
ATOM   7962 C C   . VAL E 1 216 ? -29.200 28.313 -13.098 1.00 23.84  ? 197  VAL E C   1 
ATOM   7963 O O   . VAL E 1 216 ? -28.243 27.674 -13.532 1.00 21.24  ? 197  VAL E O   1 
ATOM   7964 C CB  . VAL E 1 216 ? -28.866 30.421 -14.392 1.00 31.28  ? 197  VAL E CB  1 
ATOM   7965 C CG1 . VAL E 1 216 ? -29.891 29.924 -15.397 1.00 25.98  ? 197  VAL E CG1 1 
ATOM   7966 C CG2 . VAL E 1 216 ? -28.863 31.929 -14.335 1.00 25.34  ? 197  VAL E CG2 1 
ATOM   7967 N N   . SER E 1 217 ? -30.335 27.750 -12.698 1.00 32.08  ? 198  SER E N   1 
ATOM   7968 C CA  . SER E 1 217 ? -30.523 26.296 -12.702 1.00 34.81  ? 198  SER E CA  1 
ATOM   7969 C C   . SER E 1 217 ? -31.174 25.828 -13.998 1.00 28.82  ? 198  SER E C   1 
ATOM   7970 O O   . SER E 1 217 ? -32.280 26.252 -14.356 1.00 34.90  ? 198  SER E O   1 
ATOM   7971 C CB  . SER E 1 217 ? -31.368 25.862 -11.502 1.00 36.61  ? 198  SER E CB  1 
ATOM   7972 O OG  . SER E 1 217 ? -30.789 26.330 -10.302 1.00 42.69  ? 198  SER E OG  1 
ATOM   7973 N N   . LEU E 1 218 ? -30.483 24.947 -14.697 1.00 23.89  ? 199  LEU E N   1 
ATOM   7974 C CA  . LEU E 1 218 ? -30.963 24.469 -15.980 1.00 27.04  ? 199  LEU E CA  1 
ATOM   7975 C C   . LEU E 1 218 ? -31.351 23.006 -15.864 1.00 28.41  ? 199  LEU E C   1 
ATOM   7976 O O   . LEU E 1 218 ? -30.490 22.149 -15.691 1.00 29.00  ? 199  LEU E O   1 
ATOM   7977 C CB  . LEU E 1 218 ? -29.876 24.644 -17.037 1.00 27.12  ? 199  LEU E CB  1 
ATOM   7978 C CG  . LEU E 1 218 ? -30.134 23.932 -18.363 1.00 29.25  ? 199  LEU E CG  1 
ATOM   7979 C CD1 . LEU E 1 218 ? -31.403 24.505 -19.010 1.00 33.31  ? 199  LEU E CD1 1 
ATOM   7980 C CD2 . LEU E 1 218 ? -28.914 24.031 -19.304 1.00 20.00  ? 199  LEU E CD2 1 
ATOM   7981 N N   . ASN E 1 219 ? -32.650 22.720 -15.941 1.00 32.25  ? 200  ASN E N   1 
ATOM   7982 C CA  . ASN E 1 219 ? -33.126 21.338 -15.903 1.00 30.29  ? 200  ASN E CA  1 
ATOM   7983 C C   . ASN E 1 219 ? -33.359 20.804 -17.315 1.00 23.87  ? 200  ASN E C   1 
ATOM   7984 O O   . ASN E 1 219 ? -34.210 21.310 -18.035 1.00 26.46  ? 200  ASN E O   1 
ATOM   7985 C CB  . ASN E 1 219 ? -34.397 21.245 -15.050 1.00 36.76  ? 200  ASN E CB  1 
ATOM   7986 C CG  . ASN E 1 219 ? -34.855 19.797 -14.814 1.00 40.03  ? 200  ASN E CG  1 
ATOM   7987 O OD1 . ASN E 1 219 ? -36.050 19.497 -14.865 1.00 41.17  ? 200  ASN E OD1 1 
ATOM   7988 N ND2 . ASN E 1 219 ? -33.903 18.897 -14.567 1.00 38.50  ? 200  ASN E ND2 1 
ATOM   7989 N N   . PHE E 1 220 ? -32.591 19.793 -17.715 1.00 20.51  ? 201  PHE E N   1 
ATOM   7990 C CA  . PHE E 1 220 ? -32.625 19.300 -19.098 1.00 25.47  ? 201  PHE E CA  1 
ATOM   7991 C C   . PHE E 1 220 ? -32.410 17.789 -19.155 1.00 29.62  ? 201  PHE E C   1 
ATOM   7992 O O   . PHE E 1 220 ? -31.879 17.195 -18.200 1.00 32.14  ? 201  PHE E O   1 
ATOM   7993 C CB  . PHE E 1 220 ? -31.548 20.004 -19.942 1.00 26.33  ? 201  PHE E CB  1 
ATOM   7994 C CG  . PHE E 1 220 ? -30.139 19.558 -19.627 1.00 23.69  ? 201  PHE E CG  1 
ATOM   7995 C CD1 . PHE E 1 220 ? -29.548 19.873 -18.406 1.00 25.31  ? 201  PHE E CD1 1 
ATOM   7996 C CD2 . PHE E 1 220 ? -29.404 18.813 -20.543 1.00 23.37  ? 201  PHE E CD2 1 
ATOM   7997 C CE1 . PHE E 1 220 ? -28.253 19.452 -18.099 1.00 19.19  ? 201  PHE E CE1 1 
ATOM   7998 C CE2 . PHE E 1 220 ? -28.105 18.390 -20.243 1.00 19.07  ? 201  PHE E CE2 1 
ATOM   7999 C CZ  . PHE E 1 220 ? -27.533 18.714 -19.025 1.00 16.70  ? 201  PHE E CZ  1 
ATOM   8000 N N   . ARG E 1 221 ? -32.816 17.161 -20.263 1.00 28.32  ? 202  ARG E N   1 
ATOM   8001 C CA  . ARG E 1 221 ? -32.554 15.715 -20.465 1.00 31.70  ? 202  ARG E CA  1 
ATOM   8002 C C   . ARG E 1 221 ? -32.348 15.368 -21.924 1.00 33.41  ? 202  ARG E C   1 
ATOM   8003 O O   . ARG E 1 221 ? -32.621 16.188 -22.817 1.00 38.56  ? 202  ARG E O   1 
ATOM   8004 C CB  . ARG E 1 221 ? -33.694 14.854 -19.924 1.00 29.10  ? 202  ARG E CB  1 
ATOM   8005 C CG  . ARG E 1 221 ? -35.013 15.169 -20.589 1.00 26.61  ? 202  ARG E CG  1 
ATOM   8006 C CD  . ARG E 1 221 ? -35.862 13.948 -20.743 1.00 41.56  ? 202  ARG E CD  1 
ATOM   8007 N NE  . ARG E 1 221 ? -37.131 14.284 -21.380 1.00 39.15  ? 202  ARG E NE  1 
ATOM   8008 C CZ  . ARG E 1 221 ? -38.286 14.407 -20.733 1.00 40.43  ? 202  ARG E CZ  1 
ATOM   8009 N NH1 . ARG E 1 221 ? -38.341 14.197 -19.421 1.00 34.87  ? 202  ARG E NH1 1 
ATOM   8010 N NH2 . ARG E 1 221 ? -39.387 14.735 -21.406 1.00 36.01  ? 202  ARG E NH2 1 
ATOM   8011 N N   . LYS E 1 222 ? -31.887 14.142 -22.157 1.00 32.75  ? 203  LYS E N   1 
ATOM   8012 C CA  . LYS E 1 222 ? -31.726 13.609 -23.507 1.00 33.23  ? 203  LYS E CA  1 
ATOM   8013 C C   . LYS E 1 222 ? -33.091 13.262 -24.092 1.00 37.07  ? 203  LYS E C   1 
ATOM   8014 O O   . LYS E 1 222 ? -33.972 12.761 -23.382 1.00 40.72  ? 203  LYS E O   1 
ATOM   8015 C CB  . LYS E 1 222 ? -30.829 12.368 -23.487 1.00 31.50  ? 203  LYS E CB  1 
ATOM   8016 C CG  . LYS E 1 222 ? -30.498 11.827 -24.859 1.00 34.58  ? 203  LYS E CG  1 
ATOM   8017 C CD  . LYS E 1 222 ? -29.491 10.698 -24.742 1.00 56.01  ? 203  LYS E CD  1 
ATOM   8018 C CE  . LYS E 1 222 ? -29.099 10.127 -26.104 1.00 67.79  ? 203  LYS E CE  1 
ATOM   8019 N NZ  . LYS E 1 222 ? -28.157 8.977  -25.939 1.00 74.39  ? 203  LYS E NZ  1 
ATOM   8020 N N   . LYS E 1 223 ? -33.268 13.541 -25.381 1.00 37.72  ? 204  LYS E N   1 
ATOM   8021 C CA  . LYS E 1 223 ? -34.517 13.246 -26.085 1.00 41.66  ? 204  LYS E CA  1 
ATOM   8022 C C   . LYS E 1 223 ? -34.751 11.739 -26.303 1.00 41.16  ? 204  LYS E C   1 
ATOM   8023 O O   . LYS E 1 223 ? -33.804 10.954 -26.391 1.00 44.65  ? 204  LYS E O   1 
ATOM   8024 C CB  . LYS E 1 223 ? -34.536 13.963 -27.433 1.00 40.11  ? 204  LYS E CB  1 
ATOM   8025 C CG  . LYS E 1 223 ? -34.805 15.462 -27.386 1.00 36.46  ? 204  LYS E CG  1 
ATOM   8026 C CD  . LYS E 1 223 ? -34.549 16.042 -28.778 1.00 28.28  ? 204  LYS E CD  1 
ATOM   8027 C CE  . LYS E 1 223 ? -35.289 17.334 -29.015 1.00 34.26  ? 204  LYS E CE  1 
ATOM   8028 N NZ  . LYS E 1 223 ? -35.275 17.711 -30.462 1.00 37.85  ? 204  LYS E NZ  1 
HETATM 8029 C C1  . 09P F 2 .   ? 14.282  30.539 -15.249 1.00 26.02  ? 211  09P A C1  1 
HETATM 8030 N N1  . 09P F 2 .   ? 14.188  31.374 -14.017 1.00 29.60  ? 211  09P A N1  1 
HETATM 8031 C C2  . 09P F 2 .   ? 15.301  31.340 -13.027 1.00 30.14  ? 211  09P A C2  1 
HETATM 8032 C C3  . 09P F 2 .   ? 16.536  32.127 -13.510 1.00 32.01  ? 211  09P A C3  1 
HETATM 8033 C C4  . 09P F 2 .   ? 17.091  31.607 -14.843 1.00 34.82  ? 211  09P A C4  1 
HETATM 8034 N N2  . 09P F 2 .   ? 16.218  32.090 -15.923 1.00 26.50  ? 211  09P A N2  1 
HETATM 8035 C C5  . 09P F 2 .   ? 15.261  31.036 -16.345 1.00 22.81  ? 211  09P A C5  1 
HETATM 8036 C C6  . 09P F 2 .   ? 16.900  35.630 -18.066 1.00 26.31  ? 211  09P A C6  1 
HETATM 8037 C C7  . 09P F 2 .   ? 17.836  35.244 -17.091 1.00 40.17  ? 211  09P A C7  1 
HETATM 8038 C C8  . 09P F 2 .   ? 17.602  34.039 -16.354 1.00 37.54  ? 211  09P A C8  1 
HETATM 8039 C C9  . 09P F 2 .   ? 16.455  33.247 -16.607 1.00 29.90  ? 211  09P A C9  1 
HETATM 8040 C C10 . 09P F 2 .   ? 15.603  33.756 -17.626 1.00 32.12  ? 211  09P A C10 1 
HETATM 8041 N N3  . 09P F 2 .   ? 15.812  34.899 -18.333 1.00 32.68  ? 211  09P A N3  1 
HETATM 8042 O O1  . 09P F 2 .   ? 18.909  36.088 -16.867 1.00 48.20  ? 211  09P A O1  1 
HETATM 8043 C C11 . 09P F 2 .   ? 18.868  36.750 -15.598 1.00 41.81  ? 211  09P A C11 1 
HETATM 8044 C C12 . 09P F 2 .   ? 20.272  36.748 -15.013 1.00 58.36  ? 211  09P A C12 1 
HETATM 8045 C C1  . 09P G 2 .   ? 15.241  30.417 -44.505 1.00 24.26  ? 211  09P B C1  1 
HETATM 8046 N N1  . 09P G 2 .   ? 16.495  30.942 -43.909 1.00 25.54  ? 211  09P B N1  1 
HETATM 8047 C C2  . 09P G 2 .   ? 17.753  30.815 -44.694 1.00 30.21  ? 211  09P B C2  1 
HETATM 8048 C C3  . 09P G 2 .   ? 17.820  31.837 -45.849 1.00 29.22  ? 211  09P B C3  1 
HETATM 8049 C C4  . 09P G 2 .   ? 16.603  31.809 -46.785 1.00 22.28  ? 211  09P B C4  1 
HETATM 8050 N N2  . 09P G 2 .   ? 15.434  32.392 -46.109 1.00 27.20  ? 211  09P B N2  1 
HETATM 8051 C C5  . 09P G 2 .   ? 14.546  31.356 -45.525 1.00 24.52  ? 211  09P B C5  1 
HETATM 8052 C C6  . 09P G 2 .   ? 13.980  36.145 -47.028 1.00 37.31  ? 211  09P B C6  1 
HETATM 8053 C C7  . 09P G 2 .   ? 15.270  35.827 -47.518 1.00 38.95  ? 211  09P B C7  1 
HETATM 8054 C C8  . 09P G 2 .   ? 15.772  34.533 -47.196 1.00 33.69  ? 211  09P B C8  1 
HETATM 8055 C C9  . 09P G 2 .   ? 14.986  33.638 -46.417 1.00 33.51  ? 211  09P B C9  1 
HETATM 8056 C C10 . 09P G 2 .   ? 13.714  34.109 -45.994 1.00 31.69  ? 211  09P B C10 1 
HETATM 8057 N N3  . 09P G 2 .   ? 13.210  35.329 -46.291 1.00 30.52  ? 211  09P B N3  1 
HETATM 8058 O O1  . 09P G 2 .   ? 15.935  36.801 -48.273 1.00 50.51  ? 211  09P B O1  1 
HETATM 8059 C C11 . 09P G 2 .   ? 17.175  36.523 -48.934 1.00 44.00  ? 211  09P B C11 1 
HETATM 8060 C C12 . 09P G 2 .   ? 16.926  36.570 -50.439 1.00 38.14  ? 211  09P B C12 1 
HETATM 8061 C C1  . 09P H 2 .   ? -11.634 35.516 -55.001 1.00 24.53  ? 211  09P C C1  1 
HETATM 8062 N N1  . 09P H 2 .   ? -10.759 36.181 -55.991 1.00 22.64  ? 211  09P C N1  1 
HETATM 8063 C C2  . 09P H 2 .   ? -11.332 36.605 -57.277 1.00 20.21  ? 211  09P C C2  1 
HETATM 8064 C C3  . 09P H 2 .   ? -12.359 37.720 -57.070 1.00 22.01  ? 211  09P C C3  1 
HETATM 8065 C C4  . 09P H 2 .   ? -13.483 37.247 -56.143 1.00 23.38  ? 211  09P C C4  1 
HETATM 8066 N N2  . 09P H 2 .   ? -13.117 37.554 -54.746 1.00 25.82  ? 211  09P C N2  1 
HETATM 8067 C C5  . 09P H 2 .   ? -12.345 36.501 -54.053 1.00 23.62  ? 211  09P C C5  1 
HETATM 8068 C C6  . 09P H 2 .   ? -13.854 41.147 -52.920 1.00 26.04  ? 211  09P C C6  1 
HETATM 8069 C C7  . 09P H 2 .   ? -13.969 41.115 -54.324 1.00 28.97  ? 211  09P C C7  1 
HETATM 8070 C C8  . 09P H 2 .   ? -13.715 39.880 -54.965 1.00 27.93  ? 211  09P C C8  1 
HETATM 8071 C C9  . 09P H 2 .   ? -13.361 38.745 -54.177 1.00 25.83  ? 211  09P C C9  1 
HETATM 8072 C C10 . 09P H 2 .   ? -13.272 38.902 -52.778 1.00 20.76  ? 211  09P C C10 1 
HETATM 8073 N N3  . 09P H 2 .   ? -13.522 40.079 -52.172 1.00 26.58  ? 211  09P C N3  1 
HETATM 8074 O O1  . 09P H 2 .   ? -14.320 42.281 -54.976 1.00 44.48  ? 211  09P C O1  1 
HETATM 8075 C C11 . 09P H 2 .   ? -14.315 42.331 -56.403 1.00 42.90  ? 211  09P C C11 1 
HETATM 8076 C C12 . 09P H 2 .   ? -15.391 43.324 -56.830 1.00 36.76  ? 211  09P C C12 1 
HETATM 8077 C C1  . 09P I 2 .   ? -29.805 38.965 -31.464 1.00 19.29  ? 211  09P D C1  1 
HETATM 8078 N N1  . 09P I 2 .   ? -30.316 39.838 -32.545 1.00 20.59  ? 211  09P D N1  1 
HETATM 8079 C C2  . 09P I 2 .   ? -31.747 40.212 -32.456 1.00 21.88  ? 211  09P D C2  1 
HETATM 8080 C C3  . 09P I 2 .   ? -32.021 41.142 -31.255 1.00 28.14  ? 211  09P D C3  1 
HETATM 8081 C C4  . 09P I 2 .   ? -31.519 40.651 -29.886 1.00 19.14  ? 211  09P D C4  1 
HETATM 8082 N N2  . 09P I 2 .   ? -30.065 40.884 -29.748 1.00 23.53  ? 211  09P D N2  1 
HETATM 8083 C C5  . 09P I 2 .   ? -29.257 39.733 -30.240 1.00 24.43  ? 211  09P D C5  1 
HETATM 8084 C C6  . 09P I 2 .   ? -28.306 44.237 -27.983 1.00 21.96  ? 211  09P D C6  1 
HETATM 8085 C C7  . 09P I 2 .   ? -29.695 44.262 -28.193 1.00 24.04  ? 211  09P D C7  1 
HETATM 8086 C C8  . 09P I 2 .   ? -30.293 43.122 -28.794 1.00 29.63  ? 211  09P D C8  1 
HETATM 8087 C C9  . 09P I 2 .   ? -29.508 41.997 -29.166 1.00 28.93  ? 211  09P D C9  1 
HETATM 8088 C C10 . 09P I 2 .   ? -28.117 42.127 -28.885 1.00 27.84  ? 211  09P D C10 1 
HETATM 8089 N N3  . 09P I 2 .   ? -27.527 43.209 -28.315 1.00 20.27  ? 211  09P D N3  1 
HETATM 8090 O O1  . 09P I 2 .   ? -30.377 45.398 -27.805 1.00 35.12  ? 211  09P D O1  1 
HETATM 8091 C C11 . 09P I 2 .   ? -31.727 45.634 -28.228 1.00 37.54  ? 211  09P D C11 1 
HETATM 8092 C C12 . 09P I 2 .   ? -32.518 46.118 -27.012 1.00 32.01  ? 211  09P D C12 1 
HETATM 8093 C C1  . NAG J 3 .   ? -14.380 65.862 -61.881 1.00 44.52  ? 1206 NAG D C1  1 
HETATM 8094 C C2  . NAG J 3 .   ? -15.314 67.029 -61.552 1.00 49.39  ? 1206 NAG D C2  1 
HETATM 8095 C C3  . NAG J 3 .   ? -15.589 67.650 -62.903 1.00 50.82  ? 1206 NAG D C3  1 
HETATM 8096 C C4  . NAG J 3 .   ? -14.319 68.168 -63.561 1.00 50.83  ? 1206 NAG D C4  1 
HETATM 8097 C C5  . NAG J 3 .   ? -13.215 67.111 -63.743 1.00 50.10  ? 1206 NAG D C5  1 
HETATM 8098 C C6  . NAG J 3 .   ? -11.853 67.811 -64.052 1.00 50.28  ? 1206 NAG D C6  1 
HETATM 8099 C C7  . NAG J 3 .   ? -17.219 66.889 -59.808 1.00 51.12  ? 1206 NAG D C7  1 
HETATM 8100 C C8  . NAG J 3 .   ? -16.481 67.584 -58.699 1.00 53.33  ? 1206 NAG D C8  1 
HETATM 8101 N N2  . NAG J 3 .   ? -16.625 66.678 -61.008 1.00 51.97  ? 1206 NAG D N2  1 
HETATM 8102 O O3  . NAG J 3 .   ? -16.401 68.744 -62.620 1.00 52.02  ? 1206 NAG D O3  1 
HETATM 8103 O O4  . NAG J 3 .   ? -14.603 68.937 -64.713 1.00 52.34  ? 1206 NAG D O4  1 
HETATM 8104 O O5  . NAG J 3 .   ? -13.190 66.227 -62.622 1.00 47.14  ? 1206 NAG D O5  1 
HETATM 8105 O O6  . NAG J 3 .   ? -10.599 67.211 -63.710 1.00 54.69  ? 1206 NAG D O6  1 
HETATM 8106 O O7  . NAG J 3 .   ? -18.364 66.519 -59.536 1.00 53.65  ? 1206 NAG D O7  1 
HETATM 8107 C C1  . 09P K 2 .   ? -13.788 35.871 -6.779  1.00 26.45  ? 211  09P E C1  1 
HETATM 8108 N N1  . 09P K 2 .   ? -14.673 37.051 -6.680  1.00 32.04  ? 211  09P E N1  1 
HETATM 8109 C C2  . 09P K 2 .   ? -15.067 37.512 -5.321  1.00 35.59  ? 211  09P E C2  1 
HETATM 8110 C C3  . 09P K 2 .   ? -13.891 38.158 -4.567  1.00 31.66  ? 211  09P E C3  1 
HETATM 8111 C C4  . 09P K 2 .   ? -12.662 37.240 -4.563  1.00 31.24  ? 211  09P E C4  1 
HETATM 8112 N N2  . 09P K 2 .   ? -11.973 37.365 -5.865  1.00 40.75  ? 211  09P E N2  1 
HETATM 8113 C C5  . 09P K 2 .   ? -12.304 36.272 -6.820  1.00 23.51  ? 211  09P E C5  1 
HETATM 8114 C C6  . 09P K 2 .   ? -9.365  40.423 -6.879  1.00 27.92  ? 211  09P E C6  1 
HETATM 8115 C C7  . 09P K 2 .   ? -9.878  40.446 -5.568  1.00 37.86  ? 211  09P E C7  1 
HETATM 8116 C C8  . 09P K 2 .   ? -10.774 39.394 -5.212  1.00 38.65  ? 211  09P E C8  1 
HETATM 8117 C C9  . 09P K 2 .   ? -11.118 38.388 -6.165  1.00 39.57  ? 211  09P E C9  1 
HETATM 8118 C C10 . 09P K 2 .   ? -10.512 38.504 -7.445  1.00 30.90  ? 211  09P E C10 1 
HETATM 8119 N N3  . 09P K 2 .   ? -9.666  39.490 -7.790  1.00 25.65  ? 211  09P E N3  1 
HETATM 8120 O O1  . 09P K 2 .   ? -9.484  41.486 -4.732  1.00 43.52  ? 211  09P E O1  1 
HETATM 8121 C C11 . 09P K 2 .   ? -10.111 41.671 -3.459  1.00 40.16  ? 211  09P E C11 1 
HETATM 8122 C C12 . 09P K 2 .   ? -9.041  42.086 -2.450  1.00 39.42  ? 211  09P E C12 1 
HETATM 8123 O O   . HOH L 4 .   ? -13.327 51.271 -9.338  1.00 16.79  ? 2001 HOH A O   1 
HETATM 8124 O O   . HOH L 4 .   ? -2.363  52.948 -22.898 1.00 43.21  ? 2002 HOH A O   1 
HETATM 8125 O O   . HOH L 4 .   ? 2.290   50.017 -11.219 1.00 18.15  ? 2003 HOH A O   1 
HETATM 8126 O O   . HOH L 4 .   ? 5.758   50.830 -10.538 1.00 22.07  ? 2004 HOH A O   1 
HETATM 8127 O O   . HOH L 4 .   ? 3.982   44.706 -15.231 1.00 16.76  ? 2005 HOH A O   1 
HETATM 8128 O O   . HOH L 4 .   ? 5.404   44.041 -0.965  1.00 21.53  ? 2006 HOH A O   1 
HETATM 8129 O O   . HOH L 4 .   ? 2.615   40.680 0.374   1.00 27.01  ? 2007 HOH A O   1 
HETATM 8130 O O   . HOH L 4 .   ? -11.690 13.520 -14.884 1.00 35.11  ? 2008 HOH A O   1 
HETATM 8131 O O   . HOH L 4 .   ? 5.388   14.227 -17.125 1.00 26.48  ? 2009 HOH A O   1 
HETATM 8132 O O   . HOH L 4 .   ? 2.008   47.114 -9.029  1.00 18.57  ? 2010 HOH A O   1 
HETATM 8133 O O   . HOH L 4 .   ? 1.720   45.079 -16.470 1.00 21.93  ? 2011 HOH A O   1 
HETATM 8134 O O   . HOH L 4 .   ? 7.295   42.254 -14.635 1.00 24.63  ? 2012 HOH A O   1 
HETATM 8135 O O   . HOH L 4 .   ? 9.463   43.837 -14.466 1.00 15.88  ? 2013 HOH A O   1 
HETATM 8136 O O   . HOH L 4 .   ? -2.611  26.769 -23.161 1.00 26.26  ? 2014 HOH A O   1 
HETATM 8137 O O   . HOH L 4 .   ? -5.710  33.619 -21.035 1.00 23.00  ? 2015 HOH A O   1 
HETATM 8138 O O   . HOH L 4 .   ? -10.326 41.179 -19.262 1.00 21.32  ? 2016 HOH A O   1 
HETATM 8139 O O   . HOH L 4 .   ? -8.166  39.671 -9.949  1.00 16.94  ? 2017 HOH A O   1 
HETATM 8140 O O   . HOH L 4 .   ? -6.084  45.342 -2.705  1.00 23.55  ? 2018 HOH A O   1 
HETATM 8141 O O   . HOH L 4 .   ? 11.684  18.544 -8.886  1.00 30.86  ? 2019 HOH A O   1 
HETATM 8142 O O   . HOH L 4 .   ? 13.423  35.531 -6.701  1.00 20.73  ? 2020 HOH A O   1 
HETATM 8143 O O   . HOH L 4 .   ? 25.749  40.200 -6.707  1.00 31.14  ? 2021 HOH A O   1 
HETATM 8144 O O   . HOH L 4 .   ? -7.133  25.371 -1.274  1.00 40.52  ? 2022 HOH A O   1 
HETATM 8145 O O   . HOH L 4 .   ? -19.124 23.011 -10.109 1.00 26.53  ? 2023 HOH A O   1 
HETATM 8146 O O   . HOH L 4 .   ? -24.276 18.531 -3.749  1.00 37.26  ? 2024 HOH A O   1 
HETATM 8147 O O   . HOH L 4 .   ? -21.392 18.964 -1.570  1.00 29.93  ? 2025 HOH A O   1 
HETATM 8148 O O   . HOH L 4 .   ? -16.714 18.327 -12.884 1.00 26.72  ? 2026 HOH A O   1 
HETATM 8149 O O   . HOH L 4 .   ? 13.929  29.000 -7.936  1.00 31.20  ? 2027 HOH A O   1 
HETATM 8150 O O   . HOH M 4 .   ? 31.800  40.981 -30.006 1.00 29.58  ? 2001 HOH B O   1 
HETATM 8151 O O   . HOH M 4 .   ? 17.527  47.458 -29.084 1.00 26.56  ? 2002 HOH B O   1 
HETATM 8152 O O   . HOH M 4 .   ? 13.408  42.661 -32.912 1.00 19.18  ? 2003 HOH B O   1 
HETATM 8153 O O   . HOH M 4 .   ? 29.133  40.539 -31.177 1.00 22.03  ? 2004 HOH B O   1 
HETATM 8154 O O   . HOH M 4 .   ? 27.691  39.737 -28.975 1.00 23.29  ? 2005 HOH B O   1 
HETATM 8155 O O   . HOH M 4 .   ? 10.575  32.863 -29.062 1.00 21.99  ? 2006 HOH B O   1 
HETATM 8156 O O   . HOH M 4 .   ? 1.677   16.705 -35.381 1.00 40.77  ? 2007 HOH B O   1 
HETATM 8157 O O   . HOH M 4 .   ? 21.940  45.935 -8.751  1.00 37.44  ? 2008 HOH B O   1 
HETATM 8158 O O   . HOH M 4 .   ? 28.162  44.846 -9.667  1.00 25.19  ? 2009 HOH B O   1 
HETATM 8159 O O   . HOH M 4 .   ? 11.886  42.742 -30.732 1.00 14.47  ? 2010 HOH B O   1 
HETATM 8160 O O   . HOH M 4 .   ? 16.361  42.443 -37.485 1.00 17.71  ? 2011 HOH B O   1 
HETATM 8161 O O   . HOH M 4 .   ? 14.323  40.685 -35.381 1.00 22.40  ? 2012 HOH B O   1 
HETATM 8162 O O   . HOH M 4 .   ? 11.138  28.009 -34.426 1.00 18.19  ? 2013 HOH B O   1 
HETATM 8163 O O   . HOH M 4 .   ? 11.630  25.308 -42.553 1.00 22.49  ? 2014 HOH B O   1 
HETATM 8164 O O   . HOH M 4 .   ? 19.808  29.661 -40.469 1.00 27.20  ? 2015 HOH B O   1 
HETATM 8165 O O   . HOH M 4 .   ? 0.400   32.155 -37.451 1.00 28.08  ? 2016 HOH B O   1 
HETATM 8166 O O   . HOH M 4 .   ? 4.542   38.507 -21.081 1.00 7.54   ? 2017 HOH B O   1 
HETATM 8167 O O   . HOH M 4 .   ? 27.359  37.641 -25.664 1.00 29.96  ? 2018 HOH B O   1 
HETATM 8168 O O   . HOH M 4 .   ? 9.402   35.080 -27.280 1.00 18.47  ? 2019 HOH B O   1 
HETATM 8169 O O   . HOH M 4 .   ? 17.100  7.970  -33.994 1.00 40.87  ? 2020 HOH B O   1 
HETATM 8170 O O   . HOH M 4 .   ? 23.534  33.483 -40.546 1.00 27.00  ? 2021 HOH B O   1 
HETATM 8171 O O   . HOH M 4 .   ? 24.853  18.210 -33.238 1.00 27.39  ? 2022 HOH B O   1 
HETATM 8172 O O   . HOH M 4 .   ? 26.001  24.787 -47.734 1.00 26.51  ? 2023 HOH B O   1 
HETATM 8173 O O   . HOH M 4 .   ? 11.206  36.149 -43.945 1.00 35.40  ? 2024 HOH B O   1 
HETATM 8174 O O   . HOH N 4 .   ? 26.311  57.595 -42.753 1.00 31.08  ? 2001 HOH C O   1 
HETATM 8175 O O   . HOH N 4 .   ? 5.734   49.597 -48.726 1.00 24.27  ? 2002 HOH C O   1 
HETATM 8176 O O   . HOH N 4 .   ? 0.139   45.401 -46.729 1.00 20.40  ? 2003 HOH C O   1 
HETATM 8177 O O   . HOH N 4 .   ? 8.663   39.530 -59.380 1.00 21.37  ? 2004 HOH C O   1 
HETATM 8178 O O   . HOH N 4 .   ? 8.012   43.554 -59.180 1.00 20.01  ? 2005 HOH C O   1 
HETATM 8179 O O   . HOH N 4 .   ? 25.864  45.260 -47.354 1.00 26.47  ? 2006 HOH C O   1 
HETATM 8180 O O   . HOH N 4 .   ? 18.427  44.890 -41.073 1.00 22.64  ? 2007 HOH C O   1 
HETATM 8181 O O   . HOH N 4 .   ? 5.644   42.273 -38.681 1.00 26.36  ? 2008 HOH C O   1 
HETATM 8182 O O   . HOH N 4 .   ? -3.949  46.302 -50.956 1.00 15.12  ? 2009 HOH C O   1 
HETATM 8183 O O   . HOH N 4 .   ? -2.305  43.908 -48.715 1.00 22.50  ? 2010 HOH C O   1 
HETATM 8184 O O   . HOH N 4 .   ? -12.081 29.548 -51.667 1.00 21.63  ? 2011 HOH C O   1 
HETATM 8185 O O   . HOH N 4 .   ? -8.497  21.540 -55.691 1.00 27.35  ? 2012 HOH C O   1 
HETATM 8186 O O   . HOH N 4 .   ? 8.546   38.334 -35.415 1.00 15.07  ? 2013 HOH C O   1 
HETATM 8187 O O   . HOH N 4 .   ? 2.324   36.607 -41.830 1.00 24.19  ? 2014 HOH C O   1 
HETATM 8188 O O   . HOH N 4 .   ? 8.222   23.151 -63.249 1.00 31.32  ? 2015 HOH C O   1 
HETATM 8189 O O   . HOH N 4 .   ? -13.679 38.114 -62.368 1.00 44.18  ? 2016 HOH C O   1 
HETATM 8190 O O   . HOH N 4 .   ? -13.110 40.839 -49.546 1.00 22.46  ? 2017 HOH C O   1 
HETATM 8191 O O   . HOH O 4 .   ? -7.468  51.974 -62.221 1.00 37.03  ? 2001 HOH D O   1 
HETATM 8192 O O   . HOH O 4 .   ? -11.903 24.111 -53.144 1.00 26.15  ? 2002 HOH D O   1 
HETATM 8193 O O   . HOH O 4 .   ? -16.913 53.860 -43.705 1.00 20.07  ? 2003 HOH D O   1 
HETATM 8194 O O   . HOH O 4 .   ? -16.907 48.481 -38.701 1.00 20.73  ? 2004 HOH D O   1 
HETATM 8195 O O   . HOH O 4 .   ? -27.380 51.678 -48.346 1.00 28.16  ? 2005 HOH D O   1 
HETATM 8196 O O   . HOH O 4 .   ? -27.102 46.501 -51.470 1.00 20.96  ? 2006 HOH D O   1 
HETATM 8197 O O   . HOH O 4 .   ? -26.259 49.585 -49.647 1.00 24.67  ? 2007 HOH D O   1 
HETATM 8198 O O   . HOH O 4 .   ? -12.135 23.179 -50.230 1.00 22.10  ? 2008 HOH D O   1 
HETATM 8199 O O   . HOH O 4 .   ? -18.376 51.226 -45.090 1.00 14.31  ? 2009 HOH D O   1 
HETATM 8200 O O   . HOH O 4 .   ? -6.051  49.466 -53.690 1.00 23.70  ? 2010 HOH D O   1 
HETATM 8201 O O   . HOH O 4 .   ? -19.975 47.442 -36.879 1.00 24.84  ? 2011 HOH D O   1 
HETATM 8202 O O   . HOH O 4 .   ? -19.570 40.734 -41.580 1.00 24.48  ? 2012 HOH D O   1 
HETATM 8203 O O   . HOH O 4 .   ? -19.597 40.614 -38.584 1.00 23.96  ? 2013 HOH D O   1 
HETATM 8204 O O   . HOH O 4 .   ? -20.299 36.672 -37.145 1.00 27.40  ? 2014 HOH D O   1 
HETATM 8205 O O   . HOH O 4 .   ? -21.247 34.015 -36.934 1.00 17.12  ? 2015 HOH D O   1 
HETATM 8206 O O   . HOH O 4 .   ? -31.239 39.886 -37.788 1.00 24.84  ? 2016 HOH D O   1 
HETATM 8207 O O   . HOH O 4 .   ? -13.699 34.646 -27.807 1.00 23.53  ? 2017 HOH D O   1 
HETATM 8208 O O   . HOH O 4 .   ? -5.603  40.466 -43.133 1.00 17.95  ? 2018 HOH D O   1 
HETATM 8209 O O   . HOH O 4 .   ? -22.546 58.242 -54.842 1.00 37.62  ? 2019 HOH D O   1 
HETATM 8210 O O   . HOH O 4 .   ? -31.768 22.755 -40.373 1.00 38.55  ? 2020 HOH D O   1 
HETATM 8211 O O   . HOH O 4 .   ? -22.860 40.764 -29.124 1.00 25.24  ? 2021 HOH D O   1 
HETATM 8212 O O   . HOH O 4 .   ? -32.557 43.840 -38.888 1.00 28.34  ? 2022 HOH D O   1 
HETATM 8213 O O   . HOH O 4 .   ? -8.355  15.607 -60.792 1.00 29.95  ? 2023 HOH D O   1 
HETATM 8214 O O   . HOH O 4 .   ? -41.653 37.800 -42.976 1.00 18.45  ? 2024 HOH D O   1 
HETATM 8215 O O   . HOH O 4 .   ? -34.682 29.325 -46.257 1.00 27.28  ? 2025 HOH D O   1 
HETATM 8216 O O   . HOH O 4 .   ? -24.713 42.867 -27.832 1.00 18.50  ? 2026 HOH D O   1 
HETATM 8217 O O   . HOH P 4 .   ? -28.311 60.458 -38.159 1.00 32.27  ? 2001 HOH E O   1 
HETATM 8218 O O   . HOH P 4 .   ? -18.111 64.800 -36.434 1.00 36.07  ? 2002 HOH E O   1 
HETATM 8219 O O   . HOH P 4 .   ? -18.703 54.248 -20.220 1.00 16.40  ? 2003 HOH E O   1 
HETATM 8220 O O   . HOH P 4 .   ? -30.949 46.929 -14.260 1.00 18.76  ? 2004 HOH E O   1 
HETATM 8221 O O   . HOH P 4 .   ? -27.746 26.548 -31.795 1.00 28.51  ? 2005 HOH E O   1 
HETATM 8222 O O   . HOH P 4 .   ? -26.687 18.229 -29.000 1.00 28.09  ? 2006 HOH E O   1 
HETATM 8223 O O   . HOH P 4 .   ? -21.762 39.953 -20.024 1.00 20.10  ? 2007 HOH E O   1 
HETATM 8224 O O   . HOH P 4 .   ? -21.079 51.776 -19.616 1.00 16.51  ? 2008 HOH E O   1 
HETATM 8225 O O   . HOH P 4 .   ? -25.193 53.066 -34.455 1.00 25.18  ? 2009 HOH E O   1 
HETATM 8226 O O   . HOH P 4 .   ? -14.313 48.620 -13.337 1.00 19.94  ? 2010 HOH E O   1 
HETATM 8227 O O   . HOH P 4 .   ? -14.233 46.915 -15.746 1.00 15.62  ? 2011 HOH E O   1 
HETATM 8228 O O   . HOH P 4 .   ? -17.814 39.811 -18.810 1.00 23.23  ? 2012 HOH E O   1 
HETATM 8229 O O   . HOH P 4 .   ? -15.295 36.277 -17.913 1.00 23.08  ? 2013 HOH E O   1 
HETATM 8230 O O   . HOH P 4 .   ? -16.518 33.623 -17.598 1.00 24.49  ? 2014 HOH E O   1 
HETATM 8231 O O   . HOH P 4 .   ? -19.604 37.545 -7.767  1.00 26.98  ? 2015 HOH E O   1 
HETATM 8232 O O   . HOH P 4 .   ? -18.903 37.073 -34.844 1.00 19.50  ? 2016 HOH E O   1 
HETATM 8233 O O   . HOH P 4 .   ? -16.133 42.167 -32.506 1.00 24.34  ? 2017 HOH E O   1 
HETATM 8234 O O   . HOH P 4 .   ? -13.706 43.652 -27.941 1.00 25.70  ? 2018 HOH E O   1 
HETATM 8235 O O   . HOH P 4 .   ? -17.720 40.237 -24.866 1.00 19.76  ? 2019 HOH E O   1 
HETATM 8236 O O   . HOH P 4 .   ? -20.901 42.029 -5.890  1.00 24.44  ? 2020 HOH E O   1 
HETATM 8237 O O   . HOH P 4 .   ? -29.478 11.040 -29.204 1.00 41.01  ? 2021 HOH E O   1 
HETATM 8238 O O   . HOH P 4 .   ? -22.047 37.049 2.572   1.00 28.92  ? 2022 HOH E 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   MET 1   -18 ?   ?   ?   A . n 
A 1 2   ARG 2   -17 ?   ?   ?   A . n 
A 1 3   ARG 3   -16 ?   ?   ?   A . n 
A 1 4   ASN 4   -15 ?   ?   ?   A . n 
A 1 5   ILE 5   -14 ?   ?   ?   A . n 
A 1 6   PHE 6   -13 ?   ?   ?   A . n 
A 1 7   CYS 7   -12 ?   ?   ?   A . n 
A 1 8   LEU 8   -11 ?   ?   ?   A . n 
A 1 9   ALA 9   -10 ?   ?   ?   A . n 
A 1 10  CYS 10  -9  ?   ?   ?   A . n 
A 1 11  LEU 11  -8  ?   ?   ?   A . n 
A 1 12  TRP 12  -7  ?   ?   ?   A . n 
A 1 13  ILE 13  -6  ?   ?   ?   A . n 
A 1 14  VAL 14  -5  ?   ?   ?   A . n 
A 1 15  GLN 15  -4  ?   ?   ?   A . n 
A 1 16  ALA 16  -3  ?   ?   ?   A . n 
A 1 17  CYS 17  -2  ?   ?   ?   A . n 
A 1 18  LEU 18  -1  ?   ?   ?   A . n 
A 1 19  SER 19  0   ?   ?   ?   A . n 
A 1 20  LEU 20  1   1   LEU LEU A . n 
A 1 21  ASP 21  2   2   ASP ASP A . n 
A 1 22  ARG 22  3   3   ARG ARG A . n 
A 1 23  ALA 23  4   4   ALA ALA A . n 
A 1 24  ASP 24  5   5   ASP ASP A . n 
A 1 25  ILE 25  6   6   ILE ILE A . n 
A 1 26  LEU 26  7   7   LEU LEU A . n 
A 1 27  TYR 27  8   8   TYR TYR A . n 
A 1 28  ASN 28  9   9   ASN ASN A . n 
A 1 29  ILE 29  10  10  ILE ILE A . n 
A 1 30  ARG 30  11  11  ARG ARG A . n 
A 1 31  GLN 31  12  12  GLN GLN A . n 
A 1 32  THR 32  13  13  THR THR A . n 
A 1 33  SER 33  14  14  SER SER A . n 
A 1 34  ARG 34  15  15  ARG ARG A . n 
A 1 35  PRO 35  16  16  PRO PRO A . n 
A 1 36  ASP 36  17  17  ASP ASP A . n 
A 1 37  VAL 37  18  18  VAL VAL A . n 
A 1 38  ILE 38  19  19  ILE ILE A . n 
A 1 39  PRO 39  20  20  PRO PRO A . n 
A 1 40  THR 40  21  21  THR THR A . n 
A 1 41  GLN 41  22  22  GLN GLN A . n 
A 1 42  ARG 42  23  23  ARG ARG A . n 
A 1 43  ASP 43  24  24  ASP ASP A . n 
A 1 44  ARG 44  25  25  ARG ARG A . n 
A 1 45  PRO 45  26  26  PRO PRO A . n 
A 1 46  VAL 46  27  27  VAL VAL A . n 
A 1 47  ALA 47  28  28  ALA ALA A . n 
A 1 48  VAL 48  29  29  VAL VAL A . n 
A 1 49  SER 49  30  30  SER SER A . n 
A 1 50  VAL 50  31  31  VAL VAL A . n 
A 1 51  SER 51  32  32  SER SER A . n 
A 1 52  LEU 52  33  33  LEU LEU A . n 
A 1 53  LYS 53  34  34  LYS LYS A . n 
A 1 54  PHE 54  35  35  PHE PHE A . n 
A 1 55  ILE 55  36  36  ILE ILE A . n 
A 1 56  ASN 56  37  37  ASN ASN A . n 
A 1 57  ILE 57  38  38  ILE ILE A . n 
A 1 58  LEU 58  39  39  LEU LEU A . n 
A 1 59  GLU 59  40  40  GLU GLU A . n 
A 1 60  VAL 60  41  41  VAL VAL A . n 
A 1 61  ASN 61  42  42  ASN ASN A . n 
A 1 62  GLU 62  43  43  GLU GLU A . n 
A 1 63  ILE 63  44  44  ILE ILE A . n 
A 1 64  THR 64  45  45  THR THR A . n 
A 1 65  ASN 65  46  46  ASN ASN A . n 
A 1 66  GLU 66  47  47  GLU GLU A . n 
A 1 67  VAL 67  48  48  VAL VAL A . n 
A 1 68  ASP 68  49  49  ASP ASP A . n 
A 1 69  VAL 69  50  50  VAL VAL A . n 
A 1 70  VAL 70  51  51  VAL VAL A . n 
A 1 71  PHE 71  52  52  PHE PHE A . n 
A 1 72  TRP 72  53  53  TRP TRP A . n 
A 1 73  GLN 73  54  54  GLN GLN A . n 
A 1 74  GLN 74  55  55  GLN GLN A . n 
A 1 75  THR 75  56  56  THR THR A . n 
A 1 76  THR 76  57  57  THR THR A . n 
A 1 77  TRP 77  58  58  TRP TRP A . n 
A 1 78  SER 78  59  59  SER SER A . n 
A 1 79  ASP 79  60  60  ASP ASP A . n 
A 1 80  ARG 80  61  61  ARG ARG A . n 
A 1 81  THR 81  62  62  THR THR A . n 
A 1 82  LEU 82  63  63  LEU LEU A . n 
A 1 83  ALA 83  64  64  ALA ALA A . n 
A 1 84  TRP 84  65  65  TRP TRP A . n 
A 1 85  ASN 85  66  66  ASN ASN A . n 
A 1 86  SER 86  67  67  SER SER A . n 
A 1 87  SER 87  68  68  SER SER A . n 
A 1 88  HIS 88  69  69  HIS HIS A . n 
A 1 89  SER 89  70  70  SER SER A . n 
A 1 90  PRO 90  71  71  PRO PRO A . n 
A 1 91  ASP 91  72  72  ASP ASP A . n 
A 1 92  GLN 92  73  73  GLN GLN A . n 
A 1 93  VAL 93  74  74  VAL VAL A . n 
A 1 94  SER 94  75  75  SER SER A . n 
A 1 95  VAL 95  76  76  VAL VAL A . n 
A 1 96  PRO 96  77  77  PRO PRO A . n 
A 1 97  ILE 97  78  78  ILE ILE A . n 
A 1 98  SER 98  79  79  SER SER A . n 
A 1 99  SER 99  80  80  SER SER A . n 
A 1 100 LEU 100 81  81  LEU LEU A . n 
A 1 101 TRP 101 82  82  TRP TRP A . n 
A 1 102 VAL 102 83  83  VAL VAL A . n 
A 1 103 PRO 103 84  84  PRO PRO A . n 
A 1 104 ASP 104 85  85  ASP ASP A . n 
A 1 105 LEU 105 86  86  LEU LEU A . n 
A 1 106 ALA 106 87  87  ALA ALA A . n 
A 1 107 ALA 107 88  88  ALA ALA A . n 
A 1 108 TYR 108 89  89  TYR TYR A . n 
A 1 109 ASN 109 90  90  ASN ASN A . n 
A 1 110 ALA 110 91  91  ALA ALA A . n 
A 1 111 ILE 111 92  92  ILE ILE A . n 
A 1 112 SER 112 93  93  SER SER A . n 
A 1 113 LYS 113 94  94  LYS LYS A . n 
A 1 114 PRO 114 95  95  PRO PRO A . n 
A 1 115 GLU 115 96  96  GLU GLU A . n 
A 1 116 VAL 116 97  97  VAL VAL A . n 
A 1 117 LEU 117 98  98  LEU LEU A . n 
A 1 118 THR 118 99  99  THR THR A . n 
A 1 119 PRO 119 100 100 PRO PRO A . n 
A 1 120 GLN 120 101 101 GLN GLN A . n 
A 1 121 LEU 121 102 102 LEU LEU A . n 
A 1 122 ALA 122 103 103 ALA ALA A . n 
A 1 123 HIS 123 104 104 HIS HIS A . n 
A 1 124 VAL 124 105 105 VAL VAL A . n 
A 1 125 VAL 125 106 106 VAL VAL A . n 
A 1 126 SER 126 107 107 SER SER A . n 
A 1 127 ASP 127 108 108 ASP ASP A . n 
A 1 128 GLY 128 109 109 GLY GLY A . n 
A 1 129 GLU 129 110 110 GLU GLU A . n 
A 1 130 VAL 130 111 111 VAL VAL A . n 
A 1 131 GLN 131 112 112 GLN GLN A . n 
A 1 132 TYR 132 113 113 TYR TYR A . n 
A 1 133 THR 133 114 114 THR THR A . n 
A 1 134 PRO 134 115 115 PRO PRO A . n 
A 1 135 SER 135 116 116 SER SER A . n 
A 1 136 ILE 136 117 117 ILE ILE A . n 
A 1 137 ARG 137 118 118 ARG ARG A . n 
A 1 138 GLN 138 119 119 GLN GLN A . n 
A 1 139 ARG 139 120 120 ARG ARG A . n 
A 1 140 PHE 140 121 121 PHE PHE A . n 
A 1 141 SER 141 122 122 SER SER A . n 
A 1 142 CYS 142 123 123 CYS CYS A . n 
A 1 143 ASP 143 124 124 ASP ASP A . n 
A 1 144 VAL 144 125 125 VAL VAL A . n 
A 1 145 SER 145 126 126 SER SER A . n 
A 1 146 GLY 146 127 127 GLY GLY A . n 
A 1 147 VAL 147 128 128 VAL VAL A . n 
A 1 148 ASP 148 129 129 ASP ASP A . n 
A 1 149 THR 149 130 130 THR THR A . n 
A 1 150 GLU 150 131 131 GLU GLU A . n 
A 1 151 SER 151 132 132 SER SER A . n 
A 1 152 GLY 152 133 133 GLY GLY A . n 
A 1 153 ALA 153 134 134 ALA ALA A . n 
A 1 154 THR 154 135 135 THR THR A . n 
A 1 155 CYS 155 136 136 CYS CYS A . n 
A 1 156 ARG 156 137 137 ARG ARG A . n 
A 1 157 ILE 157 138 138 ILE ILE A . n 
A 1 158 LYS 158 139 139 LYS LYS A . n 
A 1 159 ILE 159 140 140 ILE ILE A . n 
A 1 160 GLY 160 141 141 GLY GLY A . n 
A 1 161 SER 161 142 142 SER SER A . n 
A 1 162 TRP 162 143 143 TRP TRP A . n 
A 1 163 THR 163 144 144 THR THR A . n 
A 1 164 HIS 164 145 145 HIS HIS A . n 
A 1 165 HIS 165 146 146 HIS HIS A . n 
A 1 166 SER 166 147 147 SER SER A . n 
A 1 167 ARG 167 148 148 ARG ARG A . n 
A 1 168 GLU 168 149 149 GLU GLU A . n 
A 1 169 ILE 169 150 150 ILE ILE A . n 
A 1 170 SER 170 151 151 SER SER A . n 
A 1 171 VAL 171 152 152 VAL VAL A . n 
A 1 172 ASP 172 153 153 ASP ASP A . n 
A 1 173 PRO 173 154 154 PRO PRO A . n 
A 1 174 THR 174 155 155 THR THR A . n 
A 1 175 THR 175 156 156 THR THR A . n 
A 1 176 GLU 176 157 ?   ?   ?   A . n 
A 1 177 ASN 177 158 ?   ?   ?   A . n 
A 1 178 SER 178 159 ?   ?   ?   A . n 
A 1 179 ASP 179 160 ?   ?   ?   A . n 
A 1 180 ASP 180 161 161 ASP ASP A . n 
A 1 181 SER 181 162 162 SER SER A . n 
A 1 182 GLU 182 163 163 GLU GLU A . n 
A 1 183 TYR 183 164 164 TYR TYR A . n 
A 1 184 PHE 184 165 165 PHE PHE A . n 
A 1 185 SER 185 166 166 SER SER A . n 
A 1 186 GLN 186 167 167 GLN GLN A . n 
A 1 187 TYR 187 168 168 TYR TYR A . n 
A 1 188 SER 188 169 169 SER SER A . n 
A 1 189 ARG 189 170 170 ARG ARG A . n 
A 1 190 PHE 190 171 171 PHE PHE A . n 
A 1 191 GLU 191 172 172 GLU GLU A . n 
A 1 192 ILE 192 173 173 ILE ILE A . n 
A 1 193 LEU 193 174 174 LEU LEU A . n 
A 1 194 ASP 194 175 175 ASP ASP A . n 
A 1 195 VAL 195 176 176 VAL VAL A . n 
A 1 196 THR 196 177 177 THR THR A . n 
A 1 197 GLN 197 178 178 GLN GLN A . n 
A 1 198 LYS 198 179 179 LYS LYS A . n 
A 1 199 LYS 199 180 180 LYS LYS A . n 
A 1 200 ASN 200 181 181 ASN ASN A . n 
A 1 201 SER 201 182 182 SER SER A . n 
A 1 202 VAL 202 183 183 VAL VAL A . n 
A 1 203 THR 203 184 184 THR THR A . n 
A 1 204 TYR 204 185 185 TYR TYR A . n 
A 1 205 SER 205 186 186 SER SER A . n 
A 1 206 CYS 206 187 187 CYS CYS A . n 
A 1 207 CYS 207 188 188 CYS CYS A . n 
A 1 208 PRO 208 189 189 PRO PRO A . n 
A 1 209 GLU 209 190 190 GLU GLU A . n 
A 1 210 ALA 210 191 191 ALA ALA A . n 
A 1 211 TYR 211 192 192 TYR TYR A . n 
A 1 212 GLU 212 193 193 GLU GLU A . n 
A 1 213 ASP 213 194 194 ASP ASP A . n 
A 1 214 VAL 214 195 195 VAL VAL A . n 
A 1 215 GLU 215 196 196 GLU GLU A . n 
A 1 216 VAL 216 197 197 VAL VAL A . n 
A 1 217 SER 217 198 198 SER SER A . n 
A 1 218 LEU 218 199 199 LEU LEU A . n 
A 1 219 ASN 219 200 200 ASN ASN A . n 
A 1 220 PHE 220 201 201 PHE PHE A . n 
A 1 221 ARG 221 202 202 ARG ARG A . n 
A 1 222 LYS 222 203 203 LYS LYS A . n 
A 1 223 LYS 223 204 204 LYS LYS A . n 
A 1 224 GLY 224 205 ?   ?   ?   A . n 
A 1 225 ARG 225 206 ?   ?   ?   A . n 
A 1 226 SER 226 207 ?   ?   ?   A . n 
A 1 227 GLU 227 208 ?   ?   ?   A . n 
A 1 228 ILE 228 209 ?   ?   ?   A . n 
A 1 229 LEU 229 210 ?   ?   ?   A . n 
B 1 1   MET 1   -18 ?   ?   ?   B . n 
B 1 2   ARG 2   -17 ?   ?   ?   B . n 
B 1 3   ARG 3   -16 ?   ?   ?   B . n 
B 1 4   ASN 4   -15 ?   ?   ?   B . n 
B 1 5   ILE 5   -14 ?   ?   ?   B . n 
B 1 6   PHE 6   -13 ?   ?   ?   B . n 
B 1 7   CYS 7   -12 ?   ?   ?   B . n 
B 1 8   LEU 8   -11 ?   ?   ?   B . n 
B 1 9   ALA 9   -10 ?   ?   ?   B . n 
B 1 10  CYS 10  -9  ?   ?   ?   B . n 
B 1 11  LEU 11  -8  ?   ?   ?   B . n 
B 1 12  TRP 12  -7  ?   ?   ?   B . n 
B 1 13  ILE 13  -6  ?   ?   ?   B . n 
B 1 14  VAL 14  -5  ?   ?   ?   B . n 
B 1 15  GLN 15  -4  ?   ?   ?   B . n 
B 1 16  ALA 16  -3  ?   ?   ?   B . n 
B 1 17  CYS 17  -2  ?   ?   ?   B . n 
B 1 18  LEU 18  -1  ?   ?   ?   B . n 
B 1 19  SER 19  0   ?   ?   ?   B . n 
B 1 20  LEU 20  1   1   LEU LEU B . n 
B 1 21  ASP 21  2   2   ASP ASP B . n 
B 1 22  ARG 22  3   3   ARG ARG B . n 
B 1 23  ALA 23  4   4   ALA ALA B . n 
B 1 24  ASP 24  5   5   ASP ASP B . n 
B 1 25  ILE 25  6   6   ILE ILE B . n 
B 1 26  LEU 26  7   7   LEU LEU B . n 
B 1 27  TYR 27  8   8   TYR TYR B . n 
B 1 28  ASN 28  9   9   ASN ASN B . n 
B 1 29  ILE 29  10  10  ILE ILE B . n 
B 1 30  ARG 30  11  11  ARG ARG B . n 
B 1 31  GLN 31  12  12  GLN GLN B . n 
B 1 32  THR 32  13  13  THR THR B . n 
B 1 33  SER 33  14  14  SER SER B . n 
B 1 34  ARG 34  15  15  ARG ARG B . n 
B 1 35  PRO 35  16  16  PRO PRO B . n 
B 1 36  ASP 36  17  17  ASP ASP B . n 
B 1 37  VAL 37  18  18  VAL VAL B . n 
B 1 38  ILE 38  19  19  ILE ILE B . n 
B 1 39  PRO 39  20  20  PRO PRO B . n 
B 1 40  THR 40  21  21  THR THR B . n 
B 1 41  GLN 41  22  22  GLN GLN B . n 
B 1 42  ARG 42  23  23  ARG ARG B . n 
B 1 43  ASP 43  24  24  ASP ASP B . n 
B 1 44  ARG 44  25  25  ARG ARG B . n 
B 1 45  PRO 45  26  26  PRO PRO B . n 
B 1 46  VAL 46  27  27  VAL VAL B . n 
B 1 47  ALA 47  28  28  ALA ALA B . n 
B 1 48  VAL 48  29  29  VAL VAL B . n 
B 1 49  SER 49  30  30  SER SER B . n 
B 1 50  VAL 50  31  31  VAL VAL B . n 
B 1 51  SER 51  32  32  SER SER B . n 
B 1 52  LEU 52  33  33  LEU LEU B . n 
B 1 53  LYS 53  34  34  LYS LYS B . n 
B 1 54  PHE 54  35  35  PHE PHE B . n 
B 1 55  ILE 55  36  36  ILE ILE B . n 
B 1 56  ASN 56  37  37  ASN ASN B . n 
B 1 57  ILE 57  38  38  ILE ILE B . n 
B 1 58  LEU 58  39  39  LEU LEU B . n 
B 1 59  GLU 59  40  40  GLU GLU B . n 
B 1 60  VAL 60  41  41  VAL VAL B . n 
B 1 61  ASN 61  42  42  ASN ASN B . n 
B 1 62  GLU 62  43  43  GLU GLU B . n 
B 1 63  ILE 63  44  44  ILE ILE B . n 
B 1 64  THR 64  45  45  THR THR B . n 
B 1 65  ASN 65  46  46  ASN ASN B . n 
B 1 66  GLU 66  47  47  GLU GLU B . n 
B 1 67  VAL 67  48  48  VAL VAL B . n 
B 1 68  ASP 68  49  49  ASP ASP B . n 
B 1 69  VAL 69  50  50  VAL VAL B . n 
B 1 70  VAL 70  51  51  VAL VAL B . n 
B 1 71  PHE 71  52  52  PHE PHE B . n 
B 1 72  TRP 72  53  53  TRP TRP B . n 
B 1 73  GLN 73  54  54  GLN GLN B . n 
B 1 74  GLN 74  55  55  GLN GLN B . n 
B 1 75  THR 75  56  56  THR THR B . n 
B 1 76  THR 76  57  57  THR THR B . n 
B 1 77  TRP 77  58  58  TRP TRP B . n 
B 1 78  SER 78  59  59  SER SER B . n 
B 1 79  ASP 79  60  60  ASP ASP B . n 
B 1 80  ARG 80  61  61  ARG ARG B . n 
B 1 81  THR 81  62  62  THR THR B . n 
B 1 82  LEU 82  63  63  LEU LEU B . n 
B 1 83  ALA 83  64  64  ALA ALA B . n 
B 1 84  TRP 84  65  65  TRP TRP B . n 
B 1 85  ASN 85  66  66  ASN ASN B . n 
B 1 86  SER 86  67  67  SER SER B . n 
B 1 87  SER 87  68  68  SER SER B . n 
B 1 88  HIS 88  69  69  HIS HIS B . n 
B 1 89  SER 89  70  70  SER SER B . n 
B 1 90  PRO 90  71  71  PRO PRO B . n 
B 1 91  ASP 91  72  72  ASP ASP B . n 
B 1 92  GLN 92  73  73  GLN GLN B . n 
B 1 93  VAL 93  74  74  VAL VAL B . n 
B 1 94  SER 94  75  75  SER SER B . n 
B 1 95  VAL 95  76  76  VAL VAL B . n 
B 1 96  PRO 96  77  77  PRO PRO B . n 
B 1 97  ILE 97  78  78  ILE ILE B . n 
B 1 98  SER 98  79  79  SER SER B . n 
B 1 99  SER 99  80  80  SER SER B . n 
B 1 100 LEU 100 81  81  LEU LEU B . n 
B 1 101 TRP 101 82  82  TRP TRP B . n 
B 1 102 VAL 102 83  83  VAL VAL B . n 
B 1 103 PRO 103 84  84  PRO PRO B . n 
B 1 104 ASP 104 85  85  ASP ASP B . n 
B 1 105 LEU 105 86  86  LEU LEU B . n 
B 1 106 ALA 106 87  87  ALA ALA B . n 
B 1 107 ALA 107 88  88  ALA ALA B . n 
B 1 108 TYR 108 89  89  TYR TYR B . n 
B 1 109 ASN 109 90  90  ASN ASN B . n 
B 1 110 ALA 110 91  91  ALA ALA B . n 
B 1 111 ILE 111 92  92  ILE ILE B . n 
B 1 112 SER 112 93  93  SER SER B . n 
B 1 113 LYS 113 94  94  LYS LYS B . n 
B 1 114 PRO 114 95  95  PRO PRO B . n 
B 1 115 GLU 115 96  96  GLU GLU B . n 
B 1 116 VAL 116 97  97  VAL VAL B . n 
B 1 117 LEU 117 98  98  LEU LEU B . n 
B 1 118 THR 118 99  99  THR THR B . n 
B 1 119 PRO 119 100 100 PRO PRO B . n 
B 1 120 GLN 120 101 101 GLN GLN B . n 
B 1 121 LEU 121 102 102 LEU LEU B . n 
B 1 122 ALA 122 103 103 ALA ALA B . n 
B 1 123 HIS 123 104 104 HIS HIS B . n 
B 1 124 VAL 124 105 105 VAL VAL B . n 
B 1 125 VAL 125 106 106 VAL VAL B . n 
B 1 126 SER 126 107 107 SER SER B . n 
B 1 127 ASP 127 108 108 ASP ASP B . n 
B 1 128 GLY 128 109 109 GLY GLY B . n 
B 1 129 GLU 129 110 110 GLU GLU B . n 
B 1 130 VAL 130 111 111 VAL VAL B . n 
B 1 131 GLN 131 112 112 GLN GLN B . n 
B 1 132 TYR 132 113 113 TYR TYR B . n 
B 1 133 THR 133 114 114 THR THR B . n 
B 1 134 PRO 134 115 115 PRO PRO B . n 
B 1 135 SER 135 116 116 SER SER B . n 
B 1 136 ILE 136 117 117 ILE ILE B . n 
B 1 137 ARG 137 118 118 ARG ARG B . n 
B 1 138 GLN 138 119 119 GLN GLN B . n 
B 1 139 ARG 139 120 120 ARG ARG B . n 
B 1 140 PHE 140 121 121 PHE PHE B . n 
B 1 141 SER 141 122 122 SER SER B . n 
B 1 142 CYS 142 123 123 CYS CYS B . n 
B 1 143 ASP 143 124 124 ASP ASP B . n 
B 1 144 VAL 144 125 125 VAL VAL B . n 
B 1 145 SER 145 126 126 SER SER B . n 
B 1 146 GLY 146 127 127 GLY GLY B . n 
B 1 147 VAL 147 128 128 VAL VAL B . n 
B 1 148 ASP 148 129 129 ASP ASP B . n 
B 1 149 THR 149 130 130 THR THR B . n 
B 1 150 GLU 150 131 131 GLU GLU B . n 
B 1 151 SER 151 132 132 SER SER B . n 
B 1 152 GLY 152 133 133 GLY GLY B . n 
B 1 153 ALA 153 134 134 ALA ALA B . n 
B 1 154 THR 154 135 135 THR THR B . n 
B 1 155 CYS 155 136 136 CYS CYS B . n 
B 1 156 ARG 156 137 137 ARG ARG B . n 
B 1 157 ILE 157 138 138 ILE ILE B . n 
B 1 158 LYS 158 139 139 LYS LYS B . n 
B 1 159 ILE 159 140 140 ILE ILE B . n 
B 1 160 GLY 160 141 141 GLY GLY B . n 
B 1 161 SER 161 142 142 SER SER B . n 
B 1 162 TRP 162 143 143 TRP TRP B . n 
B 1 163 THR 163 144 144 THR THR B . n 
B 1 164 HIS 164 145 145 HIS HIS B . n 
B 1 165 HIS 165 146 146 HIS HIS B . n 
B 1 166 SER 166 147 147 SER SER B . n 
B 1 167 ARG 167 148 148 ARG ARG B . n 
B 1 168 GLU 168 149 149 GLU GLU B . n 
B 1 169 ILE 169 150 150 ILE ILE B . n 
B 1 170 SER 170 151 151 SER SER B . n 
B 1 171 VAL 171 152 152 VAL VAL B . n 
B 1 172 ASP 172 153 153 ASP ASP B . n 
B 1 173 PRO 173 154 154 PRO PRO B . n 
B 1 174 THR 174 155 155 THR THR B . n 
B 1 175 THR 175 156 ?   ?   ?   B . n 
B 1 176 GLU 176 157 ?   ?   ?   B . n 
B 1 177 ASN 177 158 ?   ?   ?   B . n 
B 1 178 SER 178 159 ?   ?   ?   B . n 
B 1 179 ASP 179 160 ?   ?   ?   B . n 
B 1 180 ASP 180 161 161 ASP ASP B . n 
B 1 181 SER 181 162 162 SER SER B . n 
B 1 182 GLU 182 163 163 GLU GLU B . n 
B 1 183 TYR 183 164 164 TYR TYR B . n 
B 1 184 PHE 184 165 165 PHE PHE B . n 
B 1 185 SER 185 166 166 SER SER B . n 
B 1 186 GLN 186 167 167 GLN GLN B . n 
B 1 187 TYR 187 168 168 TYR TYR B . n 
B 1 188 SER 188 169 169 SER SER B . n 
B 1 189 ARG 189 170 170 ARG ARG B . n 
B 1 190 PHE 190 171 171 PHE PHE B . n 
B 1 191 GLU 191 172 172 GLU GLU B . n 
B 1 192 ILE 192 173 173 ILE ILE B . n 
B 1 193 LEU 193 174 174 LEU LEU B . n 
B 1 194 ASP 194 175 175 ASP ASP B . n 
B 1 195 VAL 195 176 176 VAL VAL B . n 
B 1 196 THR 196 177 177 THR THR B . n 
B 1 197 GLN 197 178 178 GLN GLN B . n 
B 1 198 LYS 198 179 179 LYS LYS B . n 
B 1 199 LYS 199 180 180 LYS LYS B . n 
B 1 200 ASN 200 181 181 ASN ASN B . n 
B 1 201 SER 201 182 182 SER SER B . n 
B 1 202 VAL 202 183 183 VAL VAL B . n 
B 1 203 THR 203 184 184 THR THR B . n 
B 1 204 TYR 204 185 185 TYR TYR B . n 
B 1 205 SER 205 186 186 SER SER B . n 
B 1 206 CYS 206 187 187 CYS CYS B . n 
B 1 207 CYS 207 188 188 CYS CYS B . n 
B 1 208 PRO 208 189 189 PRO PRO B . n 
B 1 209 GLU 209 190 190 GLU GLU B . n 
B 1 210 ALA 210 191 191 ALA ALA B . n 
B 1 211 TYR 211 192 192 TYR TYR B . n 
B 1 212 GLU 212 193 193 GLU GLU B . n 
B 1 213 ASP 213 194 194 ASP ASP B . n 
B 1 214 VAL 214 195 195 VAL VAL B . n 
B 1 215 GLU 215 196 196 GLU GLU B . n 
B 1 216 VAL 216 197 197 VAL VAL B . n 
B 1 217 SER 217 198 198 SER SER B . n 
B 1 218 LEU 218 199 199 LEU LEU B . n 
B 1 219 ASN 219 200 200 ASN ASN B . n 
B 1 220 PHE 220 201 201 PHE PHE B . n 
B 1 221 ARG 221 202 202 ARG ARG B . n 
B 1 222 LYS 222 203 203 LYS LYS B . n 
B 1 223 LYS 223 204 204 LYS LYS B . n 
B 1 224 GLY 224 205 205 GLY GLY B . n 
B 1 225 ARG 225 206 ?   ?   ?   B . n 
B 1 226 SER 226 207 ?   ?   ?   B . n 
B 1 227 GLU 227 208 ?   ?   ?   B . n 
B 1 228 ILE 228 209 ?   ?   ?   B . n 
B 1 229 LEU 229 210 ?   ?   ?   B . n 
C 1 1   MET 1   -18 ?   ?   ?   C . n 
C 1 2   ARG 2   -17 ?   ?   ?   C . n 
C 1 3   ARG 3   -16 ?   ?   ?   C . n 
C 1 4   ASN 4   -15 ?   ?   ?   C . n 
C 1 5   ILE 5   -14 ?   ?   ?   C . n 
C 1 6   PHE 6   -13 ?   ?   ?   C . n 
C 1 7   CYS 7   -12 ?   ?   ?   C . n 
C 1 8   LEU 8   -11 ?   ?   ?   C . n 
C 1 9   ALA 9   -10 ?   ?   ?   C . n 
C 1 10  CYS 10  -9  ?   ?   ?   C . n 
C 1 11  LEU 11  -8  ?   ?   ?   C . n 
C 1 12  TRP 12  -7  ?   ?   ?   C . n 
C 1 13  ILE 13  -6  ?   ?   ?   C . n 
C 1 14  VAL 14  -5  ?   ?   ?   C . n 
C 1 15  GLN 15  -4  ?   ?   ?   C . n 
C 1 16  ALA 16  -3  ?   ?   ?   C . n 
C 1 17  CYS 17  -2  ?   ?   ?   C . n 
C 1 18  LEU 18  -1  ?   ?   ?   C . n 
C 1 19  SER 19  0   ?   ?   ?   C . n 
C 1 20  LEU 20  1   1   LEU LEU C . n 
C 1 21  ASP 21  2   2   ASP ASP C . n 
C 1 22  ARG 22  3   3   ARG ARG C . n 
C 1 23  ALA 23  4   4   ALA ALA C . n 
C 1 24  ASP 24  5   5   ASP ASP C . n 
C 1 25  ILE 25  6   6   ILE ILE C . n 
C 1 26  LEU 26  7   7   LEU LEU C . n 
C 1 27  TYR 27  8   8   TYR TYR C . n 
C 1 28  ASN 28  9   9   ASN ASN C . n 
C 1 29  ILE 29  10  10  ILE ILE C . n 
C 1 30  ARG 30  11  11  ARG ARG C . n 
C 1 31  GLN 31  12  12  GLN GLN C . n 
C 1 32  THR 32  13  13  THR THR C . n 
C 1 33  SER 33  14  14  SER SER C . n 
C 1 34  ARG 34  15  15  ARG ARG C . n 
C 1 35  PRO 35  16  16  PRO PRO C . n 
C 1 36  ASP 36  17  17  ASP ASP C . n 
C 1 37  VAL 37  18  18  VAL VAL C . n 
C 1 38  ILE 38  19  19  ILE ILE C . n 
C 1 39  PRO 39  20  20  PRO PRO C . n 
C 1 40  THR 40  21  21  THR THR C . n 
C 1 41  GLN 41  22  22  GLN GLN C . n 
C 1 42  ARG 42  23  23  ARG ARG C . n 
C 1 43  ASP 43  24  24  ASP ASP C . n 
C 1 44  ARG 44  25  25  ARG ARG C . n 
C 1 45  PRO 45  26  26  PRO PRO C . n 
C 1 46  VAL 46  27  27  VAL VAL C . n 
C 1 47  ALA 47  28  28  ALA ALA C . n 
C 1 48  VAL 48  29  29  VAL VAL C . n 
C 1 49  SER 49  30  30  SER SER C . n 
C 1 50  VAL 50  31  31  VAL VAL C . n 
C 1 51  SER 51  32  32  SER SER C . n 
C 1 52  LEU 52  33  33  LEU LEU C . n 
C 1 53  LYS 53  34  34  LYS LYS C . n 
C 1 54  PHE 54  35  35  PHE PHE C . n 
C 1 55  ILE 55  36  36  ILE ILE C . n 
C 1 56  ASN 56  37  37  ASN ASN C . n 
C 1 57  ILE 57  38  38  ILE ILE C . n 
C 1 58  LEU 58  39  39  LEU LEU C . n 
C 1 59  GLU 59  40  40  GLU GLU C . n 
C 1 60  VAL 60  41  41  VAL VAL C . n 
C 1 61  ASN 61  42  42  ASN ASN C . n 
C 1 62  GLU 62  43  43  GLU GLU C . n 
C 1 63  ILE 63  44  44  ILE ILE C . n 
C 1 64  THR 64  45  45  THR THR C . n 
C 1 65  ASN 65  46  46  ASN ASN C . n 
C 1 66  GLU 66  47  47  GLU GLU C . n 
C 1 67  VAL 67  48  48  VAL VAL C . n 
C 1 68  ASP 68  49  49  ASP ASP C . n 
C 1 69  VAL 69  50  50  VAL VAL C . n 
C 1 70  VAL 70  51  51  VAL VAL C . n 
C 1 71  PHE 71  52  52  PHE PHE C . n 
C 1 72  TRP 72  53  53  TRP TRP C . n 
C 1 73  GLN 73  54  54  GLN GLN C . n 
C 1 74  GLN 74  55  55  GLN GLN C . n 
C 1 75  THR 75  56  56  THR THR C . n 
C 1 76  THR 76  57  57  THR THR C . n 
C 1 77  TRP 77  58  58  TRP TRP C . n 
C 1 78  SER 78  59  59  SER SER C . n 
C 1 79  ASP 79  60  60  ASP ASP C . n 
C 1 80  ARG 80  61  61  ARG ARG C . n 
C 1 81  THR 81  62  62  THR THR C . n 
C 1 82  LEU 82  63  63  LEU LEU C . n 
C 1 83  ALA 83  64  64  ALA ALA C . n 
C 1 84  TRP 84  65  65  TRP TRP C . n 
C 1 85  ASN 85  66  66  ASN ASN C . n 
C 1 86  SER 86  67  67  SER SER C . n 
C 1 87  SER 87  68  68  SER SER C . n 
C 1 88  HIS 88  69  69  HIS HIS C . n 
C 1 89  SER 89  70  70  SER SER C . n 
C 1 90  PRO 90  71  71  PRO PRO C . n 
C 1 91  ASP 91  72  72  ASP ASP C . n 
C 1 92  GLN 92  73  73  GLN GLN C . n 
C 1 93  VAL 93  74  74  VAL VAL C . n 
C 1 94  SER 94  75  75  SER SER C . n 
C 1 95  VAL 95  76  76  VAL VAL C . n 
C 1 96  PRO 96  77  77  PRO PRO C . n 
C 1 97  ILE 97  78  78  ILE ILE C . n 
C 1 98  SER 98  79  79  SER SER C . n 
C 1 99  SER 99  80  80  SER SER C . n 
C 1 100 LEU 100 81  81  LEU LEU C . n 
C 1 101 TRP 101 82  82  TRP TRP C . n 
C 1 102 VAL 102 83  83  VAL VAL C . n 
C 1 103 PRO 103 84  84  PRO PRO C . n 
C 1 104 ASP 104 85  85  ASP ASP C . n 
C 1 105 LEU 105 86  86  LEU LEU C . n 
C 1 106 ALA 106 87  87  ALA ALA C . n 
C 1 107 ALA 107 88  88  ALA ALA C . n 
C 1 108 TYR 108 89  89  TYR TYR C . n 
C 1 109 ASN 109 90  90  ASN ASN C . n 
C 1 110 ALA 110 91  91  ALA ALA C . n 
C 1 111 ILE 111 92  92  ILE ILE C . n 
C 1 112 SER 112 93  93  SER SER C . n 
C 1 113 LYS 113 94  94  LYS LYS C . n 
C 1 114 PRO 114 95  95  PRO PRO C . n 
C 1 115 GLU 115 96  96  GLU GLU C . n 
C 1 116 VAL 116 97  97  VAL VAL C . n 
C 1 117 LEU 117 98  98  LEU LEU C . n 
C 1 118 THR 118 99  99  THR THR C . n 
C 1 119 PRO 119 100 100 PRO PRO C . n 
C 1 120 GLN 120 101 101 GLN GLN C . n 
C 1 121 LEU 121 102 102 LEU LEU C . n 
C 1 122 ALA 122 103 103 ALA ALA C . n 
C 1 123 HIS 123 104 104 HIS HIS C . n 
C 1 124 VAL 124 105 105 VAL VAL C . n 
C 1 125 VAL 125 106 106 VAL VAL C . n 
C 1 126 SER 126 107 107 SER SER C . n 
C 1 127 ASP 127 108 108 ASP ASP C . n 
C 1 128 GLY 128 109 109 GLY GLY C . n 
C 1 129 GLU 129 110 110 GLU GLU C . n 
C 1 130 VAL 130 111 111 VAL VAL C . n 
C 1 131 GLN 131 112 112 GLN GLN C . n 
C 1 132 TYR 132 113 113 TYR TYR C . n 
C 1 133 THR 133 114 114 THR THR C . n 
C 1 134 PRO 134 115 115 PRO PRO C . n 
C 1 135 SER 135 116 116 SER SER C . n 
C 1 136 ILE 136 117 117 ILE ILE C . n 
C 1 137 ARG 137 118 118 ARG ARG C . n 
C 1 138 GLN 138 119 119 GLN GLN C . n 
C 1 139 ARG 139 120 120 ARG ARG C . n 
C 1 140 PHE 140 121 121 PHE PHE C . n 
C 1 141 SER 141 122 122 SER SER C . n 
C 1 142 CYS 142 123 123 CYS CYS C . n 
C 1 143 ASP 143 124 124 ASP ASP C . n 
C 1 144 VAL 144 125 125 VAL VAL C . n 
C 1 145 SER 145 126 126 SER SER C . n 
C 1 146 GLY 146 127 127 GLY GLY C . n 
C 1 147 VAL 147 128 128 VAL VAL C . n 
C 1 148 ASP 148 129 129 ASP ASP C . n 
C 1 149 THR 149 130 130 THR THR C . n 
C 1 150 GLU 150 131 131 GLU GLU C . n 
C 1 151 SER 151 132 132 SER SER C . n 
C 1 152 GLY 152 133 133 GLY GLY C . n 
C 1 153 ALA 153 134 134 ALA ALA C . n 
C 1 154 THR 154 135 135 THR THR C . n 
C 1 155 CYS 155 136 136 CYS CYS C . n 
C 1 156 ARG 156 137 137 ARG ARG C . n 
C 1 157 ILE 157 138 138 ILE ILE C . n 
C 1 158 LYS 158 139 139 LYS LYS C . n 
C 1 159 ILE 159 140 140 ILE ILE C . n 
C 1 160 GLY 160 141 141 GLY GLY C . n 
C 1 161 SER 161 142 142 SER SER C . n 
C 1 162 TRP 162 143 143 TRP TRP C . n 
C 1 163 THR 163 144 144 THR THR C . n 
C 1 164 HIS 164 145 145 HIS HIS C . n 
C 1 165 HIS 165 146 146 HIS HIS C . n 
C 1 166 SER 166 147 147 SER SER C . n 
C 1 167 ARG 167 148 148 ARG ARG C . n 
C 1 168 GLU 168 149 149 GLU GLU C . n 
C 1 169 ILE 169 150 150 ILE ILE C . n 
C 1 170 SER 170 151 151 SER SER C . n 
C 1 171 VAL 171 152 152 VAL VAL C . n 
C 1 172 ASP 172 153 153 ASP ASP C . n 
C 1 173 PRO 173 154 154 PRO PRO C . n 
C 1 174 THR 174 155 155 THR THR C . n 
C 1 175 THR 175 156 ?   ?   ?   C . n 
C 1 176 GLU 176 157 ?   ?   ?   C . n 
C 1 177 ASN 177 158 ?   ?   ?   C . n 
C 1 178 SER 178 159 ?   ?   ?   C . n 
C 1 179 ASP 179 160 ?   ?   ?   C . n 
C 1 180 ASP 180 161 ?   ?   ?   C . n 
C 1 181 SER 181 162 162 SER SER C . n 
C 1 182 GLU 182 163 163 GLU GLU C . n 
C 1 183 TYR 183 164 164 TYR TYR C . n 
C 1 184 PHE 184 165 165 PHE PHE C . n 
C 1 185 SER 185 166 166 SER SER C . n 
C 1 186 GLN 186 167 167 GLN GLN C . n 
C 1 187 TYR 187 168 168 TYR TYR C . n 
C 1 188 SER 188 169 169 SER SER C . n 
C 1 189 ARG 189 170 170 ARG ARG C . n 
C 1 190 PHE 190 171 171 PHE PHE C . n 
C 1 191 GLU 191 172 172 GLU GLU C . n 
C 1 192 ILE 192 173 173 ILE ILE C . n 
C 1 193 LEU 193 174 174 LEU LEU C . n 
C 1 194 ASP 194 175 175 ASP ASP C . n 
C 1 195 VAL 195 176 176 VAL VAL C . n 
C 1 196 THR 196 177 177 THR THR C . n 
C 1 197 GLN 197 178 178 GLN GLN C . n 
C 1 198 LYS 198 179 179 LYS LYS C . n 
C 1 199 LYS 199 180 180 LYS LYS C . n 
C 1 200 ASN 200 181 181 ASN ASN C . n 
C 1 201 SER 201 182 182 SER SER C . n 
C 1 202 VAL 202 183 183 VAL VAL C . n 
C 1 203 THR 203 184 184 THR THR C . n 
C 1 204 TYR 204 185 185 TYR TYR C . n 
C 1 205 SER 205 186 186 SER SER C . n 
C 1 206 CYS 206 187 187 CYS CYS C . n 
C 1 207 CYS 207 188 188 CYS CYS C . n 
C 1 208 PRO 208 189 189 PRO PRO C . n 
C 1 209 GLU 209 190 190 GLU GLU C . n 
C 1 210 ALA 210 191 191 ALA ALA C . n 
C 1 211 TYR 211 192 192 TYR TYR C . n 
C 1 212 GLU 212 193 193 GLU GLU C . n 
C 1 213 ASP 213 194 194 ASP ASP C . n 
C 1 214 VAL 214 195 195 VAL VAL C . n 
C 1 215 GLU 215 196 196 GLU GLU C . n 
C 1 216 VAL 216 197 197 VAL VAL C . n 
C 1 217 SER 217 198 198 SER SER C . n 
C 1 218 LEU 218 199 199 LEU LEU C . n 
C 1 219 ASN 219 200 200 ASN ASN C . n 
C 1 220 PHE 220 201 201 PHE PHE C . n 
C 1 221 ARG 221 202 202 ARG ARG C . n 
C 1 222 LYS 222 203 203 LYS LYS C . n 
C 1 223 LYS 223 204 204 LYS LYS C . n 
C 1 224 GLY 224 205 205 GLY GLY C . n 
C 1 225 ARG 225 206 ?   ?   ?   C . n 
C 1 226 SER 226 207 ?   ?   ?   C . n 
C 1 227 GLU 227 208 ?   ?   ?   C . n 
C 1 228 ILE 228 209 ?   ?   ?   C . n 
C 1 229 LEU 229 210 ?   ?   ?   C . n 
D 1 1   MET 1   -18 ?   ?   ?   D . n 
D 1 2   ARG 2   -17 ?   ?   ?   D . n 
D 1 3   ARG 3   -16 ?   ?   ?   D . n 
D 1 4   ASN 4   -15 ?   ?   ?   D . n 
D 1 5   ILE 5   -14 ?   ?   ?   D . n 
D 1 6   PHE 6   -13 ?   ?   ?   D . n 
D 1 7   CYS 7   -12 ?   ?   ?   D . n 
D 1 8   LEU 8   -11 ?   ?   ?   D . n 
D 1 9   ALA 9   -10 ?   ?   ?   D . n 
D 1 10  CYS 10  -9  ?   ?   ?   D . n 
D 1 11  LEU 11  -8  ?   ?   ?   D . n 
D 1 12  TRP 12  -7  ?   ?   ?   D . n 
D 1 13  ILE 13  -6  ?   ?   ?   D . n 
D 1 14  VAL 14  -5  ?   ?   ?   D . n 
D 1 15  GLN 15  -4  ?   ?   ?   D . n 
D 1 16  ALA 16  -3  ?   ?   ?   D . n 
D 1 17  CYS 17  -2  ?   ?   ?   D . n 
D 1 18  LEU 18  -1  ?   ?   ?   D . n 
D 1 19  SER 19  0   ?   ?   ?   D . n 
D 1 20  LEU 20  1   1   LEU LEU D . n 
D 1 21  ASP 21  2   2   ASP ASP D . n 
D 1 22  ARG 22  3   3   ARG ARG D . n 
D 1 23  ALA 23  4   4   ALA ALA D . n 
D 1 24  ASP 24  5   5   ASP ASP D . n 
D 1 25  ILE 25  6   6   ILE ILE D . n 
D 1 26  LEU 26  7   7   LEU LEU D . n 
D 1 27  TYR 27  8   8   TYR TYR D . n 
D 1 28  ASN 28  9   9   ASN ASN D . n 
D 1 29  ILE 29  10  10  ILE ILE D . n 
D 1 30  ARG 30  11  11  ARG ARG D . n 
D 1 31  GLN 31  12  12  GLN GLN D . n 
D 1 32  THR 32  13  13  THR THR D . n 
D 1 33  SER 33  14  14  SER SER D . n 
D 1 34  ARG 34  15  15  ARG ARG D . n 
D 1 35  PRO 35  16  16  PRO PRO D . n 
D 1 36  ASP 36  17  17  ASP ASP D . n 
D 1 37  VAL 37  18  18  VAL VAL D . n 
D 1 38  ILE 38  19  19  ILE ILE D . n 
D 1 39  PRO 39  20  20  PRO PRO D . n 
D 1 40  THR 40  21  21  THR THR D . n 
D 1 41  GLN 41  22  22  GLN GLN D . n 
D 1 42  ARG 42  23  23  ARG ARG D . n 
D 1 43  ASP 43  24  24  ASP ASP D . n 
D 1 44  ARG 44  25  25  ARG ARG D . n 
D 1 45  PRO 45  26  26  PRO PRO D . n 
D 1 46  VAL 46  27  27  VAL VAL D . n 
D 1 47  ALA 47  28  28  ALA ALA D . n 
D 1 48  VAL 48  29  29  VAL VAL D . n 
D 1 49  SER 49  30  30  SER SER D . n 
D 1 50  VAL 50  31  31  VAL VAL D . n 
D 1 51  SER 51  32  32  SER SER D . n 
D 1 52  LEU 52  33  33  LEU LEU D . n 
D 1 53  LYS 53  34  34  LYS LYS D . n 
D 1 54  PHE 54  35  35  PHE PHE D . n 
D 1 55  ILE 55  36  36  ILE ILE D . n 
D 1 56  ASN 56  37  37  ASN ASN D . n 
D 1 57  ILE 57  38  38  ILE ILE D . n 
D 1 58  LEU 58  39  39  LEU LEU D . n 
D 1 59  GLU 59  40  40  GLU GLU D . n 
D 1 60  VAL 60  41  41  VAL VAL D . n 
D 1 61  ASN 61  42  42  ASN ASN D . n 
D 1 62  GLU 62  43  43  GLU GLU D . n 
D 1 63  ILE 63  44  44  ILE ILE D . n 
D 1 64  THR 64  45  45  THR THR D . n 
D 1 65  ASN 65  46  46  ASN ASN D . n 
D 1 66  GLU 66  47  47  GLU GLU D . n 
D 1 67  VAL 67  48  48  VAL VAL D . n 
D 1 68  ASP 68  49  49  ASP ASP D . n 
D 1 69  VAL 69  50  50  VAL VAL D . n 
D 1 70  VAL 70  51  51  VAL VAL D . n 
D 1 71  PHE 71  52  52  PHE PHE D . n 
D 1 72  TRP 72  53  53  TRP TRP D . n 
D 1 73  GLN 73  54  54  GLN GLN D . n 
D 1 74  GLN 74  55  55  GLN GLN D . n 
D 1 75  THR 75  56  56  THR THR D . n 
D 1 76  THR 76  57  57  THR THR D . n 
D 1 77  TRP 77  58  58  TRP TRP D . n 
D 1 78  SER 78  59  59  SER SER D . n 
D 1 79  ASP 79  60  60  ASP ASP D . n 
D 1 80  ARG 80  61  61  ARG ARG D . n 
D 1 81  THR 81  62  62  THR THR D . n 
D 1 82  LEU 82  63  63  LEU LEU D . n 
D 1 83  ALA 83  64  64  ALA ALA D . n 
D 1 84  TRP 84  65  65  TRP TRP D . n 
D 1 85  ASN 85  66  66  ASN ASN D . n 
D 1 86  SER 86  67  67  SER SER D . n 
D 1 87  SER 87  68  68  SER SER D . n 
D 1 88  HIS 88  69  69  HIS HIS D . n 
D 1 89  SER 89  70  70  SER SER D . n 
D 1 90  PRO 90  71  71  PRO PRO D . n 
D 1 91  ASP 91  72  72  ASP ASP D . n 
D 1 92  GLN 92  73  73  GLN GLN D . n 
D 1 93  VAL 93  74  74  VAL VAL D . n 
D 1 94  SER 94  75  75  SER SER D . n 
D 1 95  VAL 95  76  76  VAL VAL D . n 
D 1 96  PRO 96  77  77  PRO PRO D . n 
D 1 97  ILE 97  78  78  ILE ILE D . n 
D 1 98  SER 98  79  79  SER SER D . n 
D 1 99  SER 99  80  80  SER SER D . n 
D 1 100 LEU 100 81  81  LEU LEU D . n 
D 1 101 TRP 101 82  82  TRP TRP D . n 
D 1 102 VAL 102 83  83  VAL VAL D . n 
D 1 103 PRO 103 84  84  PRO PRO D . n 
D 1 104 ASP 104 85  85  ASP ASP D . n 
D 1 105 LEU 105 86  86  LEU LEU D . n 
D 1 106 ALA 106 87  87  ALA ALA D . n 
D 1 107 ALA 107 88  88  ALA ALA D . n 
D 1 108 TYR 108 89  89  TYR TYR D . n 
D 1 109 ASN 109 90  90  ASN ASN D . n 
D 1 110 ALA 110 91  91  ALA ALA D . n 
D 1 111 ILE 111 92  92  ILE ILE D . n 
D 1 112 SER 112 93  93  SER SER D . n 
D 1 113 LYS 113 94  94  LYS LYS D . n 
D 1 114 PRO 114 95  95  PRO PRO D . n 
D 1 115 GLU 115 96  96  GLU GLU D . n 
D 1 116 VAL 116 97  97  VAL VAL D . n 
D 1 117 LEU 117 98  98  LEU LEU D . n 
D 1 118 THR 118 99  99  THR THR D . n 
D 1 119 PRO 119 100 100 PRO PRO D . n 
D 1 120 GLN 120 101 101 GLN GLN D . n 
D 1 121 LEU 121 102 102 LEU LEU D . n 
D 1 122 ALA 122 103 103 ALA ALA D . n 
D 1 123 HIS 123 104 104 HIS HIS D . n 
D 1 124 VAL 124 105 105 VAL VAL D . n 
D 1 125 VAL 125 106 106 VAL VAL D . n 
D 1 126 SER 126 107 107 SER SER D . n 
D 1 127 ASP 127 108 108 ASP ASP D . n 
D 1 128 GLY 128 109 109 GLY GLY D . n 
D 1 129 GLU 129 110 110 GLU GLU D . n 
D 1 130 VAL 130 111 111 VAL VAL D . n 
D 1 131 GLN 131 112 112 GLN GLN D . n 
D 1 132 TYR 132 113 113 TYR TYR D . n 
D 1 133 THR 133 114 114 THR THR D . n 
D 1 134 PRO 134 115 115 PRO PRO D . n 
D 1 135 SER 135 116 116 SER SER D . n 
D 1 136 ILE 136 117 117 ILE ILE D . n 
D 1 137 ARG 137 118 118 ARG ARG D . n 
D 1 138 GLN 138 119 119 GLN GLN D . n 
D 1 139 ARG 139 120 120 ARG ARG D . n 
D 1 140 PHE 140 121 121 PHE PHE D . n 
D 1 141 SER 141 122 122 SER SER D . n 
D 1 142 CYS 142 123 123 CYS CYS D . n 
D 1 143 ASP 143 124 124 ASP ASP D . n 
D 1 144 VAL 144 125 125 VAL VAL D . n 
D 1 145 SER 145 126 126 SER SER D . n 
D 1 146 GLY 146 127 127 GLY GLY D . n 
D 1 147 VAL 147 128 128 VAL VAL D . n 
D 1 148 ASP 148 129 129 ASP ASP D . n 
D 1 149 THR 149 130 130 THR THR D . n 
D 1 150 GLU 150 131 131 GLU GLU D . n 
D 1 151 SER 151 132 132 SER SER D . n 
D 1 152 GLY 152 133 133 GLY GLY D . n 
D 1 153 ALA 153 134 134 ALA ALA D . n 
D 1 154 THR 154 135 135 THR THR D . n 
D 1 155 CYS 155 136 136 CYS CYS D . n 
D 1 156 ARG 156 137 137 ARG ARG D . n 
D 1 157 ILE 157 138 138 ILE ILE D . n 
D 1 158 LYS 158 139 139 LYS LYS D . n 
D 1 159 ILE 159 140 140 ILE ILE D . n 
D 1 160 GLY 160 141 141 GLY GLY D . n 
D 1 161 SER 161 142 142 SER SER D . n 
D 1 162 TRP 162 143 143 TRP TRP D . n 
D 1 163 THR 163 144 144 THR THR D . n 
D 1 164 HIS 164 145 145 HIS HIS D . n 
D 1 165 HIS 165 146 146 HIS HIS D . n 
D 1 166 SER 166 147 147 SER SER D . n 
D 1 167 ARG 167 148 148 ARG ARG D . n 
D 1 168 GLU 168 149 149 GLU GLU D . n 
D 1 169 ILE 169 150 150 ILE ILE D . n 
D 1 170 SER 170 151 151 SER SER D . n 
D 1 171 VAL 171 152 152 VAL VAL D . n 
D 1 172 ASP 172 153 153 ASP ASP D . n 
D 1 173 PRO 173 154 154 PRO PRO D . n 
D 1 174 THR 174 155 155 THR THR D . n 
D 1 175 THR 175 156 156 THR THR D . n 
D 1 176 GLU 176 157 157 GLU GLU D . n 
D 1 177 ASN 177 158 158 ASN ASN D . n 
D 1 178 SER 178 159 159 SER SER D . n 
D 1 179 ASP 179 160 ?   ?   ?   D . n 
D 1 180 ASP 180 161 161 ASP ASP D . n 
D 1 181 SER 181 162 162 SER SER D . n 
D 1 182 GLU 182 163 163 GLU GLU D . n 
D 1 183 TYR 183 164 164 TYR TYR D . n 
D 1 184 PHE 184 165 165 PHE PHE D . n 
D 1 185 SER 185 166 166 SER SER D . n 
D 1 186 GLN 186 167 167 GLN GLN D . n 
D 1 187 TYR 187 168 168 TYR TYR D . n 
D 1 188 SER 188 169 169 SER SER D . n 
D 1 189 ARG 189 170 170 ARG ARG D . n 
D 1 190 PHE 190 171 171 PHE PHE D . n 
D 1 191 GLU 191 172 172 GLU GLU D . n 
D 1 192 ILE 192 173 173 ILE ILE D . n 
D 1 193 LEU 193 174 174 LEU LEU D . n 
D 1 194 ASP 194 175 175 ASP ASP D . n 
D 1 195 VAL 195 176 176 VAL VAL D . n 
D 1 196 THR 196 177 177 THR THR D . n 
D 1 197 GLN 197 178 178 GLN GLN D . n 
D 1 198 LYS 198 179 179 LYS LYS D . n 
D 1 199 LYS 199 180 180 LYS LYS D . n 
D 1 200 ASN 200 181 181 ASN ASN D . n 
D 1 201 SER 201 182 182 SER SER D . n 
D 1 202 VAL 202 183 183 VAL VAL D . n 
D 1 203 THR 203 184 184 THR THR D . n 
D 1 204 TYR 204 185 185 TYR TYR D . n 
D 1 205 SER 205 186 186 SER SER D . n 
D 1 206 CYS 206 187 187 CYS CYS D . n 
D 1 207 CYS 207 188 188 CYS CYS D . n 
D 1 208 PRO 208 189 189 PRO PRO D . n 
D 1 209 GLU 209 190 190 GLU GLU D . n 
D 1 210 ALA 210 191 191 ALA ALA D . n 
D 1 211 TYR 211 192 192 TYR TYR D . n 
D 1 212 GLU 212 193 193 GLU GLU D . n 
D 1 213 ASP 213 194 194 ASP ASP D . n 
D 1 214 VAL 214 195 195 VAL VAL D . n 
D 1 215 GLU 215 196 196 GLU GLU D . n 
D 1 216 VAL 216 197 197 VAL VAL D . n 
D 1 217 SER 217 198 198 SER SER D . n 
D 1 218 LEU 218 199 199 LEU LEU D . n 
D 1 219 ASN 219 200 200 ASN ASN D . n 
D 1 220 PHE 220 201 201 PHE PHE D . n 
D 1 221 ARG 221 202 202 ARG ARG D . n 
D 1 222 LYS 222 203 203 LYS LYS D . n 
D 1 223 LYS 223 204 204 LYS LYS D . n 
D 1 224 GLY 224 205 205 GLY GLY D . n 
D 1 225 ARG 225 206 ?   ?   ?   D . n 
D 1 226 SER 226 207 ?   ?   ?   D . n 
D 1 227 GLU 227 208 ?   ?   ?   D . n 
D 1 228 ILE 228 209 ?   ?   ?   D . n 
D 1 229 LEU 229 210 ?   ?   ?   D . n 
E 1 1   MET 1   -18 ?   ?   ?   E . n 
E 1 2   ARG 2   -17 ?   ?   ?   E . n 
E 1 3   ARG 3   -16 ?   ?   ?   E . n 
E 1 4   ASN 4   -15 ?   ?   ?   E . n 
E 1 5   ILE 5   -14 ?   ?   ?   E . n 
E 1 6   PHE 6   -13 ?   ?   ?   E . n 
E 1 7   CYS 7   -12 ?   ?   ?   E . n 
E 1 8   LEU 8   -11 ?   ?   ?   E . n 
E 1 9   ALA 9   -10 ?   ?   ?   E . n 
E 1 10  CYS 10  -9  ?   ?   ?   E . n 
E 1 11  LEU 11  -8  ?   ?   ?   E . n 
E 1 12  TRP 12  -7  ?   ?   ?   E . n 
E 1 13  ILE 13  -6  ?   ?   ?   E . n 
E 1 14  VAL 14  -5  ?   ?   ?   E . n 
E 1 15  GLN 15  -4  ?   ?   ?   E . n 
E 1 16  ALA 16  -3  ?   ?   ?   E . n 
E 1 17  CYS 17  -2  ?   ?   ?   E . n 
E 1 18  LEU 18  -1  ?   ?   ?   E . n 
E 1 19  SER 19  0   ?   ?   ?   E . n 
E 1 20  LEU 20  1   1   LEU LEU E . n 
E 1 21  ASP 21  2   2   ASP ASP E . n 
E 1 22  ARG 22  3   3   ARG ARG E . n 
E 1 23  ALA 23  4   4   ALA ALA E . n 
E 1 24  ASP 24  5   5   ASP ASP E . n 
E 1 25  ILE 25  6   6   ILE ILE E . n 
E 1 26  LEU 26  7   7   LEU LEU E . n 
E 1 27  TYR 27  8   8   TYR TYR E . n 
E 1 28  ASN 28  9   9   ASN ASN E . n 
E 1 29  ILE 29  10  10  ILE ILE E . n 
E 1 30  ARG 30  11  11  ARG ARG E . n 
E 1 31  GLN 31  12  12  GLN GLN E . n 
E 1 32  THR 32  13  13  THR THR E . n 
E 1 33  SER 33  14  14  SER SER E . n 
E 1 34  ARG 34  15  15  ARG ARG E . n 
E 1 35  PRO 35  16  16  PRO PRO E . n 
E 1 36  ASP 36  17  17  ASP ASP E . n 
E 1 37  VAL 37  18  18  VAL VAL E . n 
E 1 38  ILE 38  19  19  ILE ILE E . n 
E 1 39  PRO 39  20  20  PRO PRO E . n 
E 1 40  THR 40  21  21  THR THR E . n 
E 1 41  GLN 41  22  22  GLN GLN E . n 
E 1 42  ARG 42  23  23  ARG ARG E . n 
E 1 43  ASP 43  24  24  ASP ASP E . n 
E 1 44  ARG 44  25  25  ARG ARG E . n 
E 1 45  PRO 45  26  26  PRO PRO E . n 
E 1 46  VAL 46  27  27  VAL VAL E . n 
E 1 47  ALA 47  28  28  ALA ALA E . n 
E 1 48  VAL 48  29  29  VAL VAL E . n 
E 1 49  SER 49  30  30  SER SER E . n 
E 1 50  VAL 50  31  31  VAL VAL E . n 
E 1 51  SER 51  32  32  SER SER E . n 
E 1 52  LEU 52  33  33  LEU LEU E . n 
E 1 53  LYS 53  34  34  LYS LYS E . n 
E 1 54  PHE 54  35  35  PHE PHE E . n 
E 1 55  ILE 55  36  36  ILE ILE E . n 
E 1 56  ASN 56  37  37  ASN ASN E . n 
E 1 57  ILE 57  38  38  ILE ILE E . n 
E 1 58  LEU 58  39  39  LEU LEU E . n 
E 1 59  GLU 59  40  40  GLU GLU E . n 
E 1 60  VAL 60  41  41  VAL VAL E . n 
E 1 61  ASN 61  42  42  ASN ASN E . n 
E 1 62  GLU 62  43  43  GLU GLU E . n 
E 1 63  ILE 63  44  44  ILE ILE E . n 
E 1 64  THR 64  45  45  THR THR E . n 
E 1 65  ASN 65  46  46  ASN ASN E . n 
E 1 66  GLU 66  47  47  GLU GLU E . n 
E 1 67  VAL 67  48  48  VAL VAL E . n 
E 1 68  ASP 68  49  49  ASP ASP E . n 
E 1 69  VAL 69  50  50  VAL VAL E . n 
E 1 70  VAL 70  51  51  VAL VAL E . n 
E 1 71  PHE 71  52  52  PHE PHE E . n 
E 1 72  TRP 72  53  53  TRP TRP E . n 
E 1 73  GLN 73  54  54  GLN GLN E . n 
E 1 74  GLN 74  55  55  GLN GLN E . n 
E 1 75  THR 75  56  56  THR THR E . n 
E 1 76  THR 76  57  57  THR THR E . n 
E 1 77  TRP 77  58  58  TRP TRP E . n 
E 1 78  SER 78  59  59  SER SER E . n 
E 1 79  ASP 79  60  60  ASP ASP E . n 
E 1 80  ARG 80  61  61  ARG ARG E . n 
E 1 81  THR 81  62  62  THR THR E . n 
E 1 82  LEU 82  63  63  LEU LEU E . n 
E 1 83  ALA 83  64  64  ALA ALA E . n 
E 1 84  TRP 84  65  65  TRP TRP E . n 
E 1 85  ASN 85  66  66  ASN ASN E . n 
E 1 86  SER 86  67  67  SER SER E . n 
E 1 87  SER 87  68  68  SER SER E . n 
E 1 88  HIS 88  69  69  HIS HIS E . n 
E 1 89  SER 89  70  70  SER SER E . n 
E 1 90  PRO 90  71  71  PRO PRO E . n 
E 1 91  ASP 91  72  72  ASP ASP E . n 
E 1 92  GLN 92  73  73  GLN GLN E . n 
E 1 93  VAL 93  74  74  VAL VAL E . n 
E 1 94  SER 94  75  75  SER SER E . n 
E 1 95  VAL 95  76  76  VAL VAL E . n 
E 1 96  PRO 96  77  77  PRO PRO E . n 
E 1 97  ILE 97  78  78  ILE ILE E . n 
E 1 98  SER 98  79  79  SER SER E . n 
E 1 99  SER 99  80  80  SER SER E . n 
E 1 100 LEU 100 81  81  LEU LEU E . n 
E 1 101 TRP 101 82  82  TRP TRP E . n 
E 1 102 VAL 102 83  83  VAL VAL E . n 
E 1 103 PRO 103 84  84  PRO PRO E . n 
E 1 104 ASP 104 85  85  ASP ASP E . n 
E 1 105 LEU 105 86  86  LEU LEU E . n 
E 1 106 ALA 106 87  87  ALA ALA E . n 
E 1 107 ALA 107 88  88  ALA ALA E . n 
E 1 108 TYR 108 89  89  TYR TYR E . n 
E 1 109 ASN 109 90  90  ASN ASN E . n 
E 1 110 ALA 110 91  91  ALA ALA E . n 
E 1 111 ILE 111 92  92  ILE ILE E . n 
E 1 112 SER 112 93  93  SER SER E . n 
E 1 113 LYS 113 94  94  LYS LYS E . n 
E 1 114 PRO 114 95  95  PRO PRO E . n 
E 1 115 GLU 115 96  96  GLU GLU E . n 
E 1 116 VAL 116 97  97  VAL VAL E . n 
E 1 117 LEU 117 98  98  LEU LEU E . n 
E 1 118 THR 118 99  99  THR THR E . n 
E 1 119 PRO 119 100 100 PRO PRO E . n 
E 1 120 GLN 120 101 101 GLN GLN E . n 
E 1 121 LEU 121 102 102 LEU LEU E . n 
E 1 122 ALA 122 103 103 ALA ALA E . n 
E 1 123 HIS 123 104 104 HIS HIS E . n 
E 1 124 VAL 124 105 105 VAL VAL E . n 
E 1 125 VAL 125 106 106 VAL VAL E . n 
E 1 126 SER 126 107 107 SER SER E . n 
E 1 127 ASP 127 108 108 ASP ASP E . n 
E 1 128 GLY 128 109 109 GLY GLY E . n 
E 1 129 GLU 129 110 110 GLU GLU E . n 
E 1 130 VAL 130 111 111 VAL VAL E . n 
E 1 131 GLN 131 112 112 GLN GLN E . n 
E 1 132 TYR 132 113 113 TYR TYR E . n 
E 1 133 THR 133 114 114 THR THR E . n 
E 1 134 PRO 134 115 115 PRO PRO E . n 
E 1 135 SER 135 116 116 SER SER E . n 
E 1 136 ILE 136 117 117 ILE ILE E . n 
E 1 137 ARG 137 118 118 ARG ARG E . n 
E 1 138 GLN 138 119 119 GLN GLN E . n 
E 1 139 ARG 139 120 120 ARG ARG E . n 
E 1 140 PHE 140 121 121 PHE PHE E . n 
E 1 141 SER 141 122 122 SER SER E . n 
E 1 142 CYS 142 123 123 CYS CYS E . n 
E 1 143 ASP 143 124 124 ASP ASP E . n 
E 1 144 VAL 144 125 125 VAL VAL E . n 
E 1 145 SER 145 126 126 SER SER E . n 
E 1 146 GLY 146 127 127 GLY GLY E . n 
E 1 147 VAL 147 128 128 VAL VAL E . n 
E 1 148 ASP 148 129 129 ASP ASP E . n 
E 1 149 THR 149 130 130 THR THR E . n 
E 1 150 GLU 150 131 131 GLU GLU E . n 
E 1 151 SER 151 132 132 SER SER E . n 
E 1 152 GLY 152 133 133 GLY GLY E . n 
E 1 153 ALA 153 134 134 ALA ALA E . n 
E 1 154 THR 154 135 135 THR THR E . n 
E 1 155 CYS 155 136 136 CYS CYS E . n 
E 1 156 ARG 156 137 137 ARG ARG E . n 
E 1 157 ILE 157 138 138 ILE ILE E . n 
E 1 158 LYS 158 139 139 LYS LYS E . n 
E 1 159 ILE 159 140 140 ILE ILE E . n 
E 1 160 GLY 160 141 141 GLY GLY E . n 
E 1 161 SER 161 142 142 SER SER E . n 
E 1 162 TRP 162 143 143 TRP TRP E . n 
E 1 163 THR 163 144 144 THR THR E . n 
E 1 164 HIS 164 145 145 HIS HIS E . n 
E 1 165 HIS 165 146 146 HIS HIS E . n 
E 1 166 SER 166 147 147 SER SER E . n 
E 1 167 ARG 167 148 148 ARG ARG E . n 
E 1 168 GLU 168 149 149 GLU GLU E . n 
E 1 169 ILE 169 150 150 ILE ILE E . n 
E 1 170 SER 170 151 151 SER SER E . n 
E 1 171 VAL 171 152 152 VAL VAL E . n 
E 1 172 ASP 172 153 153 ASP ASP E . n 
E 1 173 PRO 173 154 154 PRO PRO E . n 
E 1 174 THR 174 155 155 THR THR E . n 
E 1 175 THR 175 156 ?   ?   ?   E . n 
E 1 176 GLU 176 157 ?   ?   ?   E . n 
E 1 177 ASN 177 158 ?   ?   ?   E . n 
E 1 178 SER 178 159 159 SER SER E . n 
E 1 179 ASP 179 160 160 ASP ASP E . n 
E 1 180 ASP 180 161 161 ASP ASP E . n 
E 1 181 SER 181 162 162 SER SER E . n 
E 1 182 GLU 182 163 163 GLU GLU E . n 
E 1 183 TYR 183 164 164 TYR TYR E . n 
E 1 184 PHE 184 165 165 PHE PHE E . n 
E 1 185 SER 185 166 166 SER SER E . n 
E 1 186 GLN 186 167 167 GLN GLN E . n 
E 1 187 TYR 187 168 168 TYR TYR E . n 
E 1 188 SER 188 169 169 SER SER E . n 
E 1 189 ARG 189 170 170 ARG ARG E . n 
E 1 190 PHE 190 171 171 PHE PHE E . n 
E 1 191 GLU 191 172 172 GLU GLU E . n 
E 1 192 ILE 192 173 173 ILE ILE E . n 
E 1 193 LEU 193 174 174 LEU LEU E . n 
E 1 194 ASP 194 175 175 ASP ASP E . n 
E 1 195 VAL 195 176 176 VAL VAL E . n 
E 1 196 THR 196 177 177 THR THR E . n 
E 1 197 GLN 197 178 178 GLN GLN E . n 
E 1 198 LYS 198 179 179 LYS LYS E . n 
E 1 199 LYS 199 180 180 LYS LYS E . n 
E 1 200 ASN 200 181 181 ASN ASN E . n 
E 1 201 SER 201 182 182 SER SER E . n 
E 1 202 VAL 202 183 183 VAL VAL E . n 
E 1 203 THR 203 184 184 THR THR E . n 
E 1 204 TYR 204 185 185 TYR TYR E . n 
E 1 205 SER 205 186 186 SER SER E . n 
E 1 206 CYS 206 187 187 CYS CYS E . n 
E 1 207 CYS 207 188 188 CYS CYS E . n 
E 1 208 PRO 208 189 189 PRO PRO E . n 
E 1 209 GLU 209 190 190 GLU GLU E . n 
E 1 210 ALA 210 191 191 ALA ALA E . n 
E 1 211 TYR 211 192 192 TYR TYR E . n 
E 1 212 GLU 212 193 193 GLU GLU E . n 
E 1 213 ASP 213 194 194 ASP ASP E . n 
E 1 214 VAL 214 195 195 VAL VAL E . n 
E 1 215 GLU 215 196 196 GLU GLU E . n 
E 1 216 VAL 216 197 197 VAL VAL E . n 
E 1 217 SER 217 198 198 SER SER E . n 
E 1 218 LEU 218 199 199 LEU LEU E . n 
E 1 219 ASN 219 200 200 ASN ASN E . n 
E 1 220 PHE 220 201 201 PHE PHE E . n 
E 1 221 ARG 221 202 202 ARG ARG E . n 
E 1 222 LYS 222 203 203 LYS LYS E . n 
E 1 223 LYS 223 204 204 LYS LYS E . n 
E 1 224 GLY 224 205 ?   ?   ?   E . n 
E 1 225 ARG 225 206 ?   ?   ?   E . n 
E 1 226 SER 226 207 ?   ?   ?   E . n 
E 1 227 GLU 227 208 ?   ?   ?   E . n 
E 1 228 ILE 228 209 ?   ?   ?   E . n 
E 1 229 LEU 229 210 ?   ?   ?   E . 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 
F 2 09P 1  211  211  09P 09P A . 
G 2 09P 1  211  211  09P 09P B . 
H 2 09P 1  211  211  09P 09P C . 
I 2 09P 1  211  211  09P 09P D . 
J 3 NAG 1  1206 1206 NAG NAG D . 
K 2 09P 1  211  211  09P 09P E . 
L 4 HOH 1  2001 2001 HOH HOH A . 
L 4 HOH 2  2002 2002 HOH HOH A . 
L 4 HOH 3  2003 2003 HOH HOH A . 
L 4 HOH 4  2004 2004 HOH HOH A . 
L 4 HOH 5  2005 2005 HOH HOH A . 
L 4 HOH 6  2006 2006 HOH HOH A . 
L 4 HOH 7  2007 2007 HOH HOH A . 
L 4 HOH 8  2008 2008 HOH HOH A . 
L 4 HOH 9  2009 2009 HOH HOH A . 
L 4 HOH 10 2010 2010 HOH HOH A . 
L 4 HOH 11 2011 2011 HOH HOH A . 
L 4 HOH 12 2012 2012 HOH HOH A . 
L 4 HOH 13 2013 2013 HOH HOH A . 
L 4 HOH 14 2014 2014 HOH HOH A . 
L 4 HOH 15 2015 2015 HOH HOH A . 
L 4 HOH 16 2016 2016 HOH HOH A . 
L 4 HOH 17 2017 2017 HOH HOH A . 
L 4 HOH 18 2018 2018 HOH HOH A . 
L 4 HOH 19 2019 2019 HOH HOH A . 
L 4 HOH 20 2020 2020 HOH HOH A . 
L 4 HOH 21 2021 2021 HOH HOH A . 
L 4 HOH 22 2022 2022 HOH HOH A . 
L 4 HOH 23 2023 2023 HOH HOH A . 
L 4 HOH 24 2024 2024 HOH HOH A . 
L 4 HOH 25 2025 2025 HOH HOH A . 
L 4 HOH 26 2026 2026 HOH HOH A . 
L 4 HOH 27 2027 2027 HOH HOH A . 
M 4 HOH 1  2001 2001 HOH HOH B . 
M 4 HOH 2  2002 2002 HOH HOH B . 
M 4 HOH 3  2003 2003 HOH HOH B . 
M 4 HOH 4  2004 2004 HOH HOH B . 
M 4 HOH 5  2005 2005 HOH HOH B . 
M 4 HOH 6  2006 2006 HOH HOH B . 
M 4 HOH 7  2007 2007 HOH HOH B . 
M 4 HOH 8  2008 2008 HOH HOH B . 
M 4 HOH 9  2009 2009 HOH HOH B . 
M 4 HOH 10 2010 2010 HOH HOH B . 
M 4 HOH 11 2011 2011 HOH HOH B . 
M 4 HOH 12 2012 2012 HOH HOH B . 
M 4 HOH 13 2013 2013 HOH HOH B . 
M 4 HOH 14 2014 2014 HOH HOH B . 
M 4 HOH 15 2015 2015 HOH HOH B . 
M 4 HOH 16 2016 2016 HOH HOH B . 
M 4 HOH 17 2017 2017 HOH HOH B . 
M 4 HOH 18 2018 2018 HOH HOH B . 
M 4 HOH 19 2019 2019 HOH HOH B . 
M 4 HOH 20 2020 2020 HOH HOH B . 
M 4 HOH 21 2021 2021 HOH HOH B . 
M 4 HOH 22 2022 2022 HOH HOH B . 
M 4 HOH 23 2023 2023 HOH HOH B . 
M 4 HOH 24 2024 2024 HOH HOH B . 
N 4 HOH 1  2001 2001 HOH HOH C . 
N 4 HOH 2  2002 2002 HOH HOH C . 
N 4 HOH 3  2003 2003 HOH HOH C . 
N 4 HOH 4  2004 2004 HOH HOH C . 
N 4 HOH 5  2005 2005 HOH HOH C . 
N 4 HOH 6  2006 2006 HOH HOH C . 
N 4 HOH 7  2007 2007 HOH HOH C . 
N 4 HOH 8  2008 2008 HOH HOH C . 
N 4 HOH 9  2009 2009 HOH HOH C . 
N 4 HOH 10 2010 2010 HOH HOH C . 
N 4 HOH 11 2011 2011 HOH HOH C . 
N 4 HOH 12 2012 2012 HOH HOH C . 
N 4 HOH 13 2013 2013 HOH HOH C . 
N 4 HOH 14 2014 2014 HOH HOH C . 
N 4 HOH 15 2015 2015 HOH HOH C . 
N 4 HOH 16 2016 2016 HOH HOH C . 
N 4 HOH 17 2017 2017 HOH HOH C . 
O 4 HOH 1  2001 2001 HOH HOH D . 
O 4 HOH 2  2002 2002 HOH HOH D . 
O 4 HOH 3  2003 2003 HOH HOH D . 
O 4 HOH 4  2004 2004 HOH HOH D . 
O 4 HOH 5  2005 2005 HOH HOH D . 
O 4 HOH 6  2006 2006 HOH HOH D . 
O 4 HOH 7  2007 2007 HOH HOH D . 
O 4 HOH 8  2008 2008 HOH HOH D . 
O 4 HOH 9  2009 2009 HOH HOH D . 
O 4 HOH 10 2010 2010 HOH HOH D . 
O 4 HOH 11 2011 2011 HOH HOH D . 
O 4 HOH 12 2012 2012 HOH HOH D . 
O 4 HOH 13 2013 2013 HOH HOH D . 
O 4 HOH 14 2014 2014 HOH HOH D . 
O 4 HOH 15 2015 2015 HOH HOH D . 
O 4 HOH 16 2016 2016 HOH HOH D . 
O 4 HOH 17 2017 2017 HOH HOH D . 
O 4 HOH 18 2018 2018 HOH HOH D . 
O 4 HOH 19 2019 2019 HOH HOH D . 
O 4 HOH 20 2020 2020 HOH HOH D . 
O 4 HOH 21 2021 2021 HOH HOH D . 
O 4 HOH 22 2022 2022 HOH HOH D . 
O 4 HOH 23 2023 2023 HOH HOH D . 
O 4 HOH 24 2024 2024 HOH HOH D . 
O 4 HOH 25 2025 2025 HOH HOH D . 
O 4 HOH 26 2026 2026 HOH HOH D . 
P 4 HOH 1  2001 2001 HOH HOH E . 
P 4 HOH 2  2002 2002 HOH HOH E . 
P 4 HOH 3  2003 2003 HOH HOH E . 
P 4 HOH 4  2004 2004 HOH HOH E . 
P 4 HOH 5  2005 2005 HOH HOH E . 
P 4 HOH 6  2006 2006 HOH HOH E . 
P 4 HOH 7  2007 2007 HOH HOH E . 
P 4 HOH 8  2008 2008 HOH HOH E . 
P 4 HOH 9  2009 2009 HOH HOH E . 
P 4 HOH 10 2010 2010 HOH HOH E . 
P 4 HOH 11 2011 2011 HOH HOH E . 
P 4 HOH 12 2012 2012 HOH HOH E . 
P 4 HOH 13 2013 2013 HOH HOH E . 
P 4 HOH 14 2014 2014 HOH HOH E . 
P 4 HOH 15 2015 2015 HOH HOH E . 
P 4 HOH 16 2016 2016 HOH HOH E . 
P 4 HOH 17 2017 2017 HOH HOH E . 
P 4 HOH 18 2018 2018 HOH HOH E . 
P 4 HOH 19 2019 2019 HOH HOH E . 
P 4 HOH 20 2020 2020 HOH HOH E . 
P 4 HOH 21 2021 2021 HOH HOH E . 
P 4 HOH 22 2022 2022 HOH HOH E . 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    D 
_pdbx_struct_mod_residue.label_comp_id    ASN 
_pdbx_struct_mod_residue.label_seq_id     85 
_pdbx_struct_mod_residue.auth_asym_id     D 
_pdbx_struct_mod_residue.auth_comp_id     ASN 
_pdbx_struct_mod_residue.auth_seq_id      66 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   ASN 
_pdbx_struct_mod_residue.details          'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   pentameric 
_pdbx_struct_assembly.oligomeric_count     5 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P 
# 
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)' 13560 ? 
1 MORE         -37.9 ? 
1 'SSA (A^2)'  42870 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2015-07-22 
2 'Structure model' 1 1 2015-07-29 
3 'Structure model' 1 2 2015-09-02 
# 
_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 
PHENIX refinement       '(PHENIX.REFINE)' ? 1 
XDS    'data reduction' .                 ? 2 
SCALA  'data scaling'   .                 ? 3 
PHASER phasing          .                 ? 4 
# 
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 OH E TYR 113 ? ? O E HOH 2019 ? ? 2.13 
2 1 OG D SER 14  ? ? O D SER 80   ? ? 2.19 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CA 
_pdbx_validate_rmsd_bond.auth_asym_id_1            E 
_pdbx_validate_rmsd_bond.auth_comp_id_1            ASP 
_pdbx_validate_rmsd_bond.auth_seq_id_1             17 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            A 
_pdbx_validate_rmsd_bond.auth_atom_id_2            C 
_pdbx_validate_rmsd_bond.auth_asym_id_2            E 
_pdbx_validate_rmsd_bond.auth_comp_id_2            ASP 
_pdbx_validate_rmsd_bond.auth_seq_id_2             17 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.706 
_pdbx_validate_rmsd_bond.bond_target_value         1.525 
_pdbx_validate_rmsd_bond.bond_deviation            0.181 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.026 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 C  E PRO 16 ? ? N E ASP 17 ? ? CA E ASP 17 ? A 145.53 121.70 23.83  2.50 Y 
2 1 C  E PRO 16 ? ? N E ASP 17 ? ? CA E ASP 17 ? B 149.42 121.70 27.72  2.50 Y 
3 1 CA E ASP 17 ? A C E ASP 17 ? ? O  E ASP 17 ? ? 134.64 120.10 14.54  2.10 N 
4 1 CA E ASP 17 ? B C E ASP 17 ? ? O  E ASP 17 ? ? 137.48 120.10 17.38  2.10 N 
5 1 CA E ASP 17 ? B C E ASP 17 ? ? N  E VAL 18 ? ? 103.54 117.20 -13.66 2.20 Y 
# 
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 ARG B 15  ? ? 59.90  71.26 
2 1 ARG C 15  ? ? 58.64  71.54 
3 1 SER D 162 ? ? -69.95 4.38  
4 1 ARG E 15  ? ? 62.30  70.58 
# 
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 MET -18 ? A MET 1   
2   1 Y 1 A ARG -17 ? A ARG 2   
3   1 Y 1 A ARG -16 ? A ARG 3   
4   1 Y 1 A ASN -15 ? A ASN 4   
5   1 Y 1 A ILE -14 ? A ILE 5   
6   1 Y 1 A PHE -13 ? A PHE 6   
7   1 Y 1 A CYS -12 ? A CYS 7   
8   1 Y 1 A LEU -11 ? A LEU 8   
9   1 Y 1 A ALA -10 ? A ALA 9   
10  1 Y 1 A CYS -9  ? A CYS 10  
11  1 Y 1 A LEU -8  ? A LEU 11  
12  1 Y 1 A TRP -7  ? A TRP 12  
13  1 Y 1 A ILE -6  ? A ILE 13  
14  1 Y 1 A VAL -5  ? A VAL 14  
15  1 Y 1 A GLN -4  ? A GLN 15  
16  1 Y 1 A ALA -3  ? A ALA 16  
17  1 Y 1 A CYS -2  ? A CYS 17  
18  1 Y 1 A LEU -1  ? A LEU 18  
19  1 Y 1 A SER 0   ? A SER 19  
20  1 Y 1 A GLU 157 ? A GLU 176 
21  1 Y 1 A ASN 158 ? A ASN 177 
22  1 Y 1 A SER 159 ? A SER 178 
23  1 Y 1 A ASP 160 ? A ASP 179 
24  1 Y 1 A GLY 205 ? A GLY 224 
25  1 Y 1 A ARG 206 ? A ARG 225 
26  1 Y 1 A SER 207 ? A SER 226 
27  1 Y 1 A GLU 208 ? A GLU 227 
28  1 Y 1 A ILE 209 ? A ILE 228 
29  1 Y 1 A LEU 210 ? A LEU 229 
30  1 Y 1 B MET -18 ? B MET 1   
31  1 Y 1 B ARG -17 ? B ARG 2   
32  1 Y 1 B ARG -16 ? B ARG 3   
33  1 Y 1 B ASN -15 ? B ASN 4   
34  1 Y 1 B ILE -14 ? B ILE 5   
35  1 Y 1 B PHE -13 ? B PHE 6   
36  1 Y 1 B CYS -12 ? B CYS 7   
37  1 Y 1 B LEU -11 ? B LEU 8   
38  1 Y 1 B ALA -10 ? B ALA 9   
39  1 Y 1 B CYS -9  ? B CYS 10  
40  1 Y 1 B LEU -8  ? B LEU 11  
41  1 Y 1 B TRP -7  ? B TRP 12  
42  1 Y 1 B ILE -6  ? B ILE 13  
43  1 Y 1 B VAL -5  ? B VAL 14  
44  1 Y 1 B GLN -4  ? B GLN 15  
45  1 Y 1 B ALA -3  ? B ALA 16  
46  1 Y 1 B CYS -2  ? B CYS 17  
47  1 Y 1 B LEU -1  ? B LEU 18  
48  1 Y 1 B SER 0   ? B SER 19  
49  1 Y 1 B THR 156 ? B THR 175 
50  1 Y 1 B GLU 157 ? B GLU 176 
51  1 Y 1 B ASN 158 ? B ASN 177 
52  1 Y 1 B SER 159 ? B SER 178 
53  1 Y 1 B ASP 160 ? B ASP 179 
54  1 Y 1 B ARG 206 ? B ARG 225 
55  1 Y 1 B SER 207 ? B SER 226 
56  1 Y 1 B GLU 208 ? B GLU 227 
57  1 Y 1 B ILE 209 ? B ILE 228 
58  1 Y 1 B LEU 210 ? B LEU 229 
59  1 Y 1 C MET -18 ? C MET 1   
60  1 Y 1 C ARG -17 ? C ARG 2   
61  1 Y 1 C ARG -16 ? C ARG 3   
62  1 Y 1 C ASN -15 ? C ASN 4   
63  1 Y 1 C ILE -14 ? C ILE 5   
64  1 Y 1 C PHE -13 ? C PHE 6   
65  1 Y 1 C CYS -12 ? C CYS 7   
66  1 Y 1 C LEU -11 ? C LEU 8   
67  1 Y 1 C ALA -10 ? C ALA 9   
68  1 Y 1 C CYS -9  ? C CYS 10  
69  1 Y 1 C LEU -8  ? C LEU 11  
70  1 Y 1 C TRP -7  ? C TRP 12  
71  1 Y 1 C ILE -6  ? C ILE 13  
72  1 Y 1 C VAL -5  ? C VAL 14  
73  1 Y 1 C GLN -4  ? C GLN 15  
74  1 Y 1 C ALA -3  ? C ALA 16  
75  1 Y 1 C CYS -2  ? C CYS 17  
76  1 Y 1 C LEU -1  ? C LEU 18  
77  1 Y 1 C SER 0   ? C SER 19  
78  1 Y 1 C THR 156 ? C THR 175 
79  1 Y 1 C GLU 157 ? C GLU 176 
80  1 Y 1 C ASN 158 ? C ASN 177 
81  1 Y 1 C SER 159 ? C SER 178 
82  1 Y 1 C ASP 160 ? C ASP 179 
83  1 Y 1 C ASP 161 ? C ASP 180 
84  1 Y 1 C ARG 206 ? C ARG 225 
85  1 Y 1 C SER 207 ? C SER 226 
86  1 Y 1 C GLU 208 ? C GLU 227 
87  1 Y 1 C ILE 209 ? C ILE 228 
88  1 Y 1 C LEU 210 ? C LEU 229 
89  1 Y 1 D MET -18 ? D MET 1   
90  1 Y 1 D ARG -17 ? D ARG 2   
91  1 Y 1 D ARG -16 ? D ARG 3   
92  1 Y 1 D ASN -15 ? D ASN 4   
93  1 Y 1 D ILE -14 ? D ILE 5   
94  1 Y 1 D PHE -13 ? D PHE 6   
95  1 Y 1 D CYS -12 ? D CYS 7   
96  1 Y 1 D LEU -11 ? D LEU 8   
97  1 Y 1 D ALA -10 ? D ALA 9   
98  1 Y 1 D CYS -9  ? D CYS 10  
99  1 Y 1 D LEU -8  ? D LEU 11  
100 1 Y 1 D TRP -7  ? D TRP 12  
101 1 Y 1 D ILE -6  ? D ILE 13  
102 1 Y 1 D VAL -5  ? D VAL 14  
103 1 Y 1 D GLN -4  ? D GLN 15  
104 1 Y 1 D ALA -3  ? D ALA 16  
105 1 Y 1 D CYS -2  ? D CYS 17  
106 1 Y 1 D LEU -1  ? D LEU 18  
107 1 Y 1 D SER 0   ? D SER 19  
108 1 Y 1 D ASP 160 ? D ASP 179 
109 1 Y 1 D ARG 206 ? D ARG 225 
110 1 Y 1 D SER 207 ? D SER 226 
111 1 Y 1 D GLU 208 ? D GLU 227 
112 1 Y 1 D ILE 209 ? D ILE 228 
113 1 Y 1 D LEU 210 ? D LEU 229 
114 1 Y 1 E MET -18 ? E MET 1   
115 1 Y 1 E ARG -17 ? E ARG 2   
116 1 Y 1 E ARG -16 ? E ARG 3   
117 1 Y 1 E ASN -15 ? E ASN 4   
118 1 Y 1 E ILE -14 ? E ILE 5   
119 1 Y 1 E PHE -13 ? E PHE 6   
120 1 Y 1 E CYS -12 ? E CYS 7   
121 1 Y 1 E LEU -11 ? E LEU 8   
122 1 Y 1 E ALA -10 ? E ALA 9   
123 1 Y 1 E CYS -9  ? E CYS 10  
124 1 Y 1 E LEU -8  ? E LEU 11  
125 1 Y 1 E TRP -7  ? E TRP 12  
126 1 Y 1 E ILE -6  ? E ILE 13  
127 1 Y 1 E VAL -5  ? E VAL 14  
128 1 Y 1 E GLN -4  ? E GLN 15  
129 1 Y 1 E ALA -3  ? E ALA 16  
130 1 Y 1 E CYS -2  ? E CYS 17  
131 1 Y 1 E LEU -1  ? E LEU 18  
132 1 Y 1 E SER 0   ? E SER 19  
133 1 Y 1 E THR 156 ? E THR 175 
134 1 Y 1 E GLU 157 ? E GLU 176 
135 1 Y 1 E ASN 158 ? E ASN 177 
136 1 Y 1 E GLY 205 ? E GLY 224 
137 1 Y 1 E ARG 206 ? E ARG 225 
138 1 Y 1 E SER 207 ? E SER 226 
139 1 Y 1 E GLU 208 ? E GLU 227 
140 1 Y 1 E ILE 209 ? E ILE 228 
141 1 Y 1 E LEU 210 ? E LEU 229 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '1-(5-ethoxypyridin-3-yl)-1,4-diazepane' 09P 
3 N-ACETYL-D-GLUCOSAMINE                   NAG 
4 water                                    HOH 
# 
