data_9ORL
# 
_entry.id   9ORL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9ORL         pdb_00009orl 10.2210/pdb9orl/pdb 
WWPDB D_1000296176 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-18 
_pdbx_audit_revision_history.part_number         ? 
# 
_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         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9ORL 
_pdbx_database_status.recvd_initial_deposition_date   2025-05-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'XRD structure of the same protein-ligand complex' 
_pdbx_database_related.db_id          9OR7 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jrodriguez@mbi.ucla.edu 
_pdbx_contact_author.name_first         Jose 
_pdbx_contact_author.name_last          Rodriguez 
_pdbx_contact_author.name_mi            A 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0248-4964 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Vlahakis, N.W.'  1 ? 
'Rodriguez, J.A.' 2 ? 
'Jacobs, L.M.C.'  3 ? 
'Chen, Y.'        4 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Combining MicroED and native mass spectrometry for structural discovert of enzyme-small molecule complexes' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Vlahakis, N.W.'  1  ? 
primary 'Flowers, C.W.'   2  ? 
primary 'Liu, M.'         3  ? 
primary 'Agdanowski, M.'  4  ? 
primary 'Johnson, S.'     5  ? 
primary 'Summers, J.A.'   6  ? 
primary 'Jacobs, L.M.C.'  7  ? 
primary 'Keyser, C.'      8  ? 
primary 'Russell, P.'     9  ? 
primary 'Rose, S.'        10 ? 
primary 'Orlans, J.'      11 ? 
primary 'Adhami, N.'      12 ? 
primary 'Chen, Y.'        13 ? 
primary 'Sawaya, M.R.'    14 ? 
primary 'Basu, S.'        15 ? 
primary 'De Sanctis, D.'  16 ? 
primary 'Chen, Y.'        17 ? 
primary 'Wakatsuki, S.'   18 ? 
primary 'Nelson, H.M.'    19 ? 
primary 'Loo, J.'         20 ? 
primary 'Tang, Y.'        21 ? 
primary 'Rodriguez, J.A.' 22 ? 
# 
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 Beta-lactamase                                                 28000.547 2  3.5.2.6 ? 'UNP residues 23-284' ? 
2 non-polymer syn '(2S,5R)-1-formyl-5-[(sulfooxy)amino]piperidine-2-carboxamide' 267.260   2  ?       ? ?                     ? 
3 water       nat water                                                          18.015    27 ?       ? ?                     ? 
# 
_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       
;QTSAVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVMAAAAVLKQSETQKQLLNQPVEIKPADLVNY
NPIAEKHVNGTMTLAELSAAALQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPGDPRDTTTPRA
MAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLPTSWTVGDKTGSGDYGTTNDIAVIWPQGRAPLVLVTYFTQ
PQQNAESRRDVLASAARIIAEGL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;QTSAVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVMAAAAVLKQSETQKQLLNQPVEIKPADLVNY
NPIAEKHVNGTMTLAELSAAALQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPGDPRDTTTPRA
MAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLPTSWTVGDKTGSGDYGTTNDIAVIWPQGRAPLVLVTYFTQ
PQQNAESRRDVLASAARIIAEGL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(2S,5R)-1-formyl-5-[(sulfooxy)amino]piperidine-2-carboxamide' NXL 
3 water                                                          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLN n 
1 2   THR n 
1 3   SER n 
1 4   ALA n 
1 5   VAL n 
1 6   GLN n 
1 7   GLN n 
1 8   LYS n 
1 9   LEU n 
1 10  ALA n 
1 11  ALA n 
1 12  LEU n 
1 13  GLU n 
1 14  LYS n 
1 15  SER n 
1 16  SER n 
1 17  GLY n 
1 18  GLY n 
1 19  ARG n 
1 20  LEU n 
1 21  GLY n 
1 22  VAL n 
1 23  ALA n 
1 24  LEU n 
1 25  ILE n 
1 26  ASP n 
1 27  THR n 
1 28  ALA n 
1 29  ASP n 
1 30  ASN n 
1 31  THR n 
1 32  GLN n 
1 33  VAL n 
1 34  LEU n 
1 35  TYR n 
1 36  ARG n 
1 37  GLY n 
1 38  ASP n 
1 39  GLU n 
1 40  ARG n 
1 41  PHE n 
1 42  PRO n 
1 43  MET n 
1 44  CYS n 
1 45  SER n 
1 46  THR n 
1 47  SER n 
1 48  LYS n 
1 49  VAL n 
1 50  MET n 
1 51  ALA n 
1 52  ALA n 
1 53  ALA n 
1 54  ALA n 
1 55  VAL n 
1 56  LEU n 
1 57  LYS n 
1 58  GLN n 
1 59  SER n 
1 60  GLU n 
1 61  THR n 
1 62  GLN n 
1 63  LYS n 
1 64  GLN n 
1 65  LEU n 
1 66  LEU n 
1 67  ASN n 
1 68  GLN n 
1 69  PRO n 
1 70  VAL n 
1 71  GLU n 
1 72  ILE n 
1 73  LYS n 
1 74  PRO n 
1 75  ALA n 
1 76  ASP n 
1 77  LEU n 
1 78  VAL n 
1 79  ASN n 
1 80  TYR n 
1 81  ASN n 
1 82  PRO n 
1 83  ILE n 
1 84  ALA n 
1 85  GLU n 
1 86  LYS n 
1 87  HIS n 
1 88  VAL n 
1 89  ASN n 
1 90  GLY n 
1 91  THR n 
1 92  MET n 
1 93  THR n 
1 94  LEU n 
1 95  ALA n 
1 96  GLU n 
1 97  LEU n 
1 98  SER n 
1 99  ALA n 
1 100 ALA n 
1 101 ALA n 
1 102 LEU n 
1 103 GLN n 
1 104 TYR n 
1 105 SER n 
1 106 ASP n 
1 107 ASN n 
1 108 THR n 
1 109 ALA n 
1 110 MET n 
1 111 ASN n 
1 112 LYS n 
1 113 LEU n 
1 114 ILE n 
1 115 ALA n 
1 116 GLN n 
1 117 LEU n 
1 118 GLY n 
1 119 GLY n 
1 120 PRO n 
1 121 GLY n 
1 122 GLY n 
1 123 VAL n 
1 124 THR n 
1 125 ALA n 
1 126 PHE n 
1 127 ALA n 
1 128 ARG n 
1 129 ALA n 
1 130 ILE n 
1 131 GLY n 
1 132 ASP n 
1 133 GLU n 
1 134 THR n 
1 135 PHE n 
1 136 ARG n 
1 137 LEU n 
1 138 ASP n 
1 139 ARG n 
1 140 THR n 
1 141 GLU n 
1 142 PRO n 
1 143 THR n 
1 144 LEU n 
1 145 ASN n 
1 146 THR n 
1 147 ALA n 
1 148 ILE n 
1 149 PRO n 
1 150 GLY n 
1 151 ASP n 
1 152 PRO n 
1 153 ARG n 
1 154 ASP n 
1 155 THR n 
1 156 THR n 
1 157 THR n 
1 158 PRO n 
1 159 ARG n 
1 160 ALA n 
1 161 MET n 
1 162 ALA n 
1 163 GLN n 
1 164 THR n 
1 165 LEU n 
1 166 ARG n 
1 167 GLN n 
1 168 LEU n 
1 169 THR n 
1 170 LEU n 
1 171 GLY n 
1 172 HIS n 
1 173 ALA n 
1 174 LEU n 
1 175 GLY n 
1 176 GLU n 
1 177 THR n 
1 178 GLN n 
1 179 ARG n 
1 180 ALA n 
1 181 GLN n 
1 182 LEU n 
1 183 VAL n 
1 184 THR n 
1 185 TRP n 
1 186 LEU n 
1 187 LYS n 
1 188 GLY n 
1 189 ASN n 
1 190 THR n 
1 191 THR n 
1 192 GLY n 
1 193 ALA n 
1 194 ALA n 
1 195 SER n 
1 196 ILE n 
1 197 ARG n 
1 198 ALA n 
1 199 GLY n 
1 200 LEU n 
1 201 PRO n 
1 202 THR n 
1 203 SER n 
1 204 TRP n 
1 205 THR n 
1 206 VAL n 
1 207 GLY n 
1 208 ASP n 
1 209 LYS n 
1 210 THR n 
1 211 GLY n 
1 212 SER n 
1 213 GLY n 
1 214 ASP n 
1 215 TYR n 
1 216 GLY n 
1 217 THR n 
1 218 THR n 
1 219 ASN n 
1 220 ASP n 
1 221 ILE n 
1 222 ALA n 
1 223 VAL n 
1 224 ILE n 
1 225 TRP n 
1 226 PRO n 
1 227 GLN n 
1 228 GLY n 
1 229 ARG n 
1 230 ALA n 
1 231 PRO n 
1 232 LEU n 
1 233 VAL n 
1 234 LEU n 
1 235 VAL n 
1 236 THR n 
1 237 TYR n 
1 238 PHE n 
1 239 THR n 
1 240 GLN n 
1 241 PRO n 
1 242 GLN n 
1 243 GLN n 
1 244 ASN n 
1 245 ALA n 
1 246 GLU n 
1 247 SER n 
1 248 ARG n 
1 249 ARG n 
1 250 ASP n 
1 251 VAL n 
1 252 LEU n 
1 253 ALA n 
1 254 SER n 
1 255 ALA n 
1 256 ALA n 
1 257 ARG n 
1 258 ILE n 
1 259 ILE n 
1 260 ALA n 
1 261 GLU n 
1 262 GLY n 
1 263 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                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   263 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 
;blaCTX-M-14, beta-lactamase CTX-M-14, bla, bla CTX-M-14, bla-CTX-M-14a, blaCTX-M, blaCTX-M-14a, blaCTX-M-14b, blaCTX-M-14c, blaCTX-M-27b, blatoho-3, blaUOE-2, CTX-M-14, AM333_26030, AM340_28340, AM465_01285, AM465_06510, AM465_23360, APT94_14605, BEN53_26220, BJJ90_27545, BK334_27290, BOH76_00730, BON63_16015, BON65_15195, BON66_01305, BON69_22545, BON72_03470, BON75_10525, BON76_14325, BON83_15455, BON86_08515, BON91_02075, BON92_04750, BON94_23850, BON95_01680, BON96_03940, BON98_23175, BXT93_06855, C5N07_28500, CDL37_21060, CR538_26855, DW236_20870, E4K51_21070, EIA08_25160, EIA21_26975, ELT23_05930, ELV24_09995, ELX61_24095, EST51_15935, EST51_18575, EST51_22260, EST51_22365, ETN48_p0088, FNJ69_13810, FTV90_03295, GE096_24920, GE096_25355, GQE36_23945, HGR36_01450, HGR36_27140, HHH24_004455, HHH24_005319, HJI79_003882, HJI79_004995, HK427_004976, HK427_005087, HL152_24835, HL152_25835, HL563_21800, HL563_23665, HLT96_25270, HLT96_28700, HLU13_27785, HLY53_18605, HLY53_26190, HLZ85_26065, HMW26_20895, HMW26_29355, HNC73_28650, HNC75_27190, HNC75_29165, HNC80_26145, HNC80_27675, HNC88_26185, HNC88_27880, HND23_26750, HND23_28285, HNV91_23425, HNV91_24920, HNV94_24095, HNV94_27845, pCT_085, pHK01_011, RCS103_P0010, RCS30_P0082, RCS56_P0085, RCS60_P0031, RCS63_P0006, RCS65_P0008, RCS66_P0053, SAMEA4362930_00013, SAMEA4363083_00099, SAMEA4370290_00046, WP4S18E07_P40650, WP7S17E01_P10270, WP7S18E09_37980
;
_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      'Escherichia coli' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     562 
_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               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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               ? 
_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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                        ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                                       ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                     ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                                       ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                      ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                                        ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                                      ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                          ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                     ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                                        ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                         ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                                     ? 'C5 H11 N O2 S'  149.211 
NXL non-polymer         . '(2S,5R)-1-formyl-5-[(sulfooxy)amino]piperidine-2-carboxamide' 
'avibactam, bound form; NXL104, bound form' 'C7 H13 N3 O6 S' 267.260 
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 
# 
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   GLN 1   25  ?   ?   ?   A . n 
A 1 2   THR 2   26  ?   ?   ?   A . n 
A 1 3   SER 3   27  27  SER SER A . n 
A 1 4   ALA 4   28  28  ALA ALA A . n 
A 1 5   VAL 5   29  29  VAL VAL A . n 
A 1 6   GLN 6   30  30  GLN GLN A . n 
A 1 7   GLN 7   31  31  GLN GLN A . n 
A 1 8   LYS 8   32  32  LYS LYS A . n 
A 1 9   LEU 9   33  33  LEU LEU A . n 
A 1 10  ALA 10  34  34  ALA ALA A . n 
A 1 11  ALA 11  35  35  ALA ALA A . n 
A 1 12  LEU 12  36  36  LEU LEU A . n 
A 1 13  GLU 13  37  37  GLU GLU A . n 
A 1 14  LYS 14  38  38  LYS LYS A . n 
A 1 15  SER 15  39  39  SER SER A . n 
A 1 16  SER 16  40  40  SER SER A . n 
A 1 17  GLY 17  41  41  GLY GLY A . n 
A 1 18  GLY 18  42  42  GLY GLY A . n 
A 1 19  ARG 19  43  43  ARG ARG A . n 
A 1 20  LEU 20  44  44  LEU LEU A . n 
A 1 21  GLY 21  45  45  GLY GLY A . n 
A 1 22  VAL 22  46  46  VAL VAL A . n 
A 1 23  ALA 23  47  47  ALA ALA A . n 
A 1 24  LEU 24  48  48  LEU LEU A . n 
A 1 25  ILE 25  49  49  ILE ILE A . n 
A 1 26  ASP 26  50  50  ASP ASP A . n 
A 1 27  THR 27  51  51  THR THR A . n 
A 1 28  ALA 28  52  52  ALA ALA A . n 
A 1 29  ASP 29  53  53  ASP ASP A . n 
A 1 30  ASN 30  54  54  ASN ASN A . n 
A 1 31  THR 31  55  55  THR THR A . n 
A 1 32  GLN 32  56  56  GLN GLN A . n 
A 1 33  VAL 33  57  57  VAL VAL A . n 
A 1 34  LEU 34  59  59  LEU LEU A . n 
A 1 35  TYR 35  60  60  TYR TYR A . n 
A 1 36  ARG 36  61  61  ARG ARG A . n 
A 1 37  GLY 37  62  62  GLY GLY A . n 
A 1 38  ASP 38  63  63  ASP ASP A . n 
A 1 39  GLU 39  64  64  GLU GLU A . n 
A 1 40  ARG 40  65  65  ARG ARG A . n 
A 1 41  PHE 41  66  66  PHE PHE A . n 
A 1 42  PRO 42  67  67  PRO PRO A . n 
A 1 43  MET 43  68  68  MET MET A . n 
A 1 44  CYS 44  69  69  CYS CYS A . n 
A 1 45  SER 45  70  70  SER SER A . n 
A 1 46  THR 46  71  71  THR THR A . n 
A 1 47  SER 47  72  72  SER SER A . n 
A 1 48  LYS 48  73  73  LYS LYS A . n 
A 1 49  VAL 49  74  74  VAL VAL A . n 
A 1 50  MET 50  75  75  MET MET A . n 
A 1 51  ALA 51  76  76  ALA ALA A . n 
A 1 52  ALA 52  77  77  ALA ALA A . n 
A 1 53  ALA 53  78  78  ALA ALA A . n 
A 1 54  ALA 54  79  79  ALA ALA A . n 
A 1 55  VAL 55  80  80  VAL VAL A . n 
A 1 56  LEU 56  81  81  LEU LEU A . n 
A 1 57  LYS 57  82  82  LYS LYS A . n 
A 1 58  GLN 58  83  83  GLN GLN A . n 
A 1 59  SER 59  84  84  SER SER A . n 
A 1 60  GLU 60  85  85  GLU GLU A . n 
A 1 61  THR 61  86  86  THR THR A . n 
A 1 62  GLN 62  87  87  GLN GLN A . n 
A 1 63  LYS 63  88  88  LYS LYS A . n 
A 1 64  GLN 64  89  89  GLN GLN A . n 
A 1 65  LEU 65  90  90  LEU LEU A . n 
A 1 66  LEU 66  91  91  LEU LEU A . n 
A 1 67  ASN 67  92  92  ASN ASN A . n 
A 1 68  GLN 68  93  93  GLN GLN A . n 
A 1 69  PRO 69  94  94  PRO PRO A . n 
A 1 70  VAL 70  95  95  VAL VAL A . n 
A 1 71  GLU 71  96  96  GLU GLU A . n 
A 1 72  ILE 72  97  97  ILE ILE A . n 
A 1 73  LYS 73  98  98  LYS LYS A . n 
A 1 74  PRO 74  99  99  PRO PRO A . n 
A 1 75  ALA 75  100 100 ALA ALA A . n 
A 1 76  ASP 76  101 101 ASP ASP A . n 
A 1 77  LEU 77  102 102 LEU LEU A . n 
A 1 78  VAL 78  103 103 VAL VAL A . n 
A 1 79  ASN 79  104 104 ASN ASN A . n 
A 1 80  TYR 80  105 105 TYR TYR A . n 
A 1 81  ASN 81  106 106 ASN ASN A . n 
A 1 82  PRO 82  107 107 PRO PRO A . n 
A 1 83  ILE 83  108 108 ILE ILE A . n 
A 1 84  ALA 84  109 109 ALA ALA A . n 
A 1 85  GLU 85  110 110 GLU GLU A . n 
A 1 86  LYS 86  111 111 LYS LYS A . n 
A 1 87  HIS 87  112 112 HIS HIS A . n 
A 1 88  VAL 88  113 113 VAL VAL A . n 
A 1 89  ASN 89  114 114 ASN ASN A . n 
A 1 90  GLY 90  115 115 GLY GLY A . n 
A 1 91  THR 91  116 116 THR THR A . n 
A 1 92  MET 92  117 117 MET MET A . n 
A 1 93  THR 93  118 118 THR THR A . n 
A 1 94  LEU 94  119 119 LEU LEU A . n 
A 1 95  ALA 95  120 120 ALA ALA A . n 
A 1 96  GLU 96  121 121 GLU GLU A . n 
A 1 97  LEU 97  122 122 LEU LEU A . n 
A 1 98  SER 98  123 123 SER SER A . n 
A 1 99  ALA 99  124 124 ALA ALA A . n 
A 1 100 ALA 100 125 125 ALA ALA A . n 
A 1 101 ALA 101 126 126 ALA ALA A . n 
A 1 102 LEU 102 127 127 LEU LEU A . n 
A 1 103 GLN 103 128 128 GLN GLN A . n 
A 1 104 TYR 104 129 129 TYR TYR A . n 
A 1 105 SER 105 130 130 SER SER A . n 
A 1 106 ASP 106 131 131 ASP ASP A . n 
A 1 107 ASN 107 132 132 ASN ASN A . n 
A 1 108 THR 108 133 133 THR THR A . n 
A 1 109 ALA 109 134 134 ALA ALA A . n 
A 1 110 MET 110 135 135 MET MET A . n 
A 1 111 ASN 111 136 136 ASN ASN A . n 
A 1 112 LYS 112 137 137 LYS LYS A . n 
A 1 113 LEU 113 138 138 LEU LEU A . n 
A 1 114 ILE 114 139 139 ILE ILE A . n 
A 1 115 ALA 115 140 140 ALA ALA A . n 
A 1 116 GLN 116 141 141 GLN GLN A . n 
A 1 117 LEU 117 142 142 LEU LEU A . n 
A 1 118 GLY 118 143 143 GLY GLY A . n 
A 1 119 GLY 119 144 144 GLY GLY A . n 
A 1 120 PRO 120 145 145 PRO PRO A . n 
A 1 121 GLY 121 146 146 GLY GLY A . n 
A 1 122 GLY 122 147 147 GLY GLY A . n 
A 1 123 VAL 123 148 148 VAL VAL A . n 
A 1 124 THR 124 149 149 THR THR A . n 
A 1 125 ALA 125 150 150 ALA ALA A . n 
A 1 126 PHE 126 151 151 PHE PHE A . n 
A 1 127 ALA 127 152 152 ALA ALA A . n 
A 1 128 ARG 128 153 153 ARG ARG A . n 
A 1 129 ALA 129 154 154 ALA ALA A . n 
A 1 130 ILE 130 155 155 ILE ILE A . n 
A 1 131 GLY 131 156 156 GLY GLY A . n 
A 1 132 ASP 132 157 157 ASP ASP A . n 
A 1 133 GLU 133 158 158 GLU GLU A . n 
A 1 134 THR 134 159 159 THR THR A . n 
A 1 135 PHE 135 160 160 PHE PHE A . n 
A 1 136 ARG 136 161 161 ARG ARG A . n 
A 1 137 LEU 137 162 162 LEU LEU A . n 
A 1 138 ASP 138 163 163 ASP ASP A . n 
A 1 139 ARG 139 164 164 ARG ARG A . n 
A 1 140 THR 140 165 165 THR THR A . n 
A 1 141 GLU 141 166 166 GLU GLU A . n 
A 1 142 PRO 142 167 167 PRO PRO A . n 
A 1 143 THR 143 168 168 THR THR A . n 
A 1 144 LEU 144 169 169 LEU LEU A . n 
A 1 145 ASN 145 170 170 ASN ASN A . n 
A 1 146 THR 146 171 171 THR THR A . n 
A 1 147 ALA 147 172 172 ALA ALA A . n 
A 1 148 ILE 148 173 173 ILE ILE A . n 
A 1 149 PRO 149 174 174 PRO PRO A . n 
A 1 150 GLY 150 175 175 GLY GLY A . n 
A 1 151 ASP 151 176 176 ASP ASP A . n 
A 1 152 PRO 152 177 177 PRO PRO A . n 
A 1 153 ARG 153 178 178 ARG ARG A . n 
A 1 154 ASP 154 179 179 ASP ASP A . n 
A 1 155 THR 155 180 180 THR THR A . n 
A 1 156 THR 156 181 181 THR THR A . n 
A 1 157 THR 157 182 182 THR THR A . n 
A 1 158 PRO 158 183 183 PRO PRO A . n 
A 1 159 ARG 159 184 184 ARG ARG A . n 
A 1 160 ALA 160 185 185 ALA ALA A . n 
A 1 161 MET 161 186 186 MET MET A . n 
A 1 162 ALA 162 187 187 ALA ALA A . n 
A 1 163 GLN 163 188 188 GLN GLN A . n 
A 1 164 THR 164 189 189 THR THR A . n 
A 1 165 LEU 165 190 190 LEU LEU A . n 
A 1 166 ARG 166 191 191 ARG ARG A . n 
A 1 167 GLN 167 192 192 GLN GLN A . n 
A 1 168 LEU 168 193 193 LEU LEU A . n 
A 1 169 THR 169 194 194 THR THR A . n 
A 1 170 LEU 170 195 195 LEU LEU A . n 
A 1 171 GLY 171 196 196 GLY GLY A . n 
A 1 172 HIS 172 197 197 HIS HIS A . n 
A 1 173 ALA 173 198 198 ALA ALA A . n 
A 1 174 LEU 174 199 199 LEU LEU A . n 
A 1 175 GLY 175 200 200 GLY GLY A . n 
A 1 176 GLU 176 201 201 GLU GLU A . n 
A 1 177 THR 177 202 202 THR THR A . n 
A 1 178 GLN 178 203 203 GLN GLN A . n 
A 1 179 ARG 179 204 204 ARG ARG A . n 
A 1 180 ALA 180 205 205 ALA ALA A . n 
A 1 181 GLN 181 206 206 GLN GLN A . n 
A 1 182 LEU 182 207 207 LEU LEU A . n 
A 1 183 VAL 183 208 208 VAL VAL A . n 
A 1 184 THR 184 209 209 THR THR A . n 
A 1 185 TRP 185 210 210 TRP TRP A . n 
A 1 186 LEU 186 211 211 LEU LEU A . n 
A 1 187 LYS 187 212 212 LYS LYS A . n 
A 1 188 GLY 188 213 213 GLY GLY A . n 
A 1 189 ASN 189 214 214 ASN ASN A . n 
A 1 190 THR 190 215 215 THR THR A . n 
A 1 191 THR 191 216 216 THR THR A . n 
A 1 192 GLY 192 217 217 GLY GLY A . n 
A 1 193 ALA 193 218 218 ALA ALA A . n 
A 1 194 ALA 194 219 219 ALA ALA A . n 
A 1 195 SER 195 220 220 SER SER A . n 
A 1 196 ILE 196 221 221 ILE ILE A . n 
A 1 197 ARG 197 222 222 ARG ARG A . n 
A 1 198 ALA 198 223 223 ALA ALA A . n 
A 1 199 GLY 199 224 224 GLY GLY A . n 
A 1 200 LEU 200 225 225 LEU LEU A . n 
A 1 201 PRO 201 226 226 PRO PRO A . n 
A 1 202 THR 202 227 227 THR THR A . n 
A 1 203 SER 203 228 228 SER SER A . n 
A 1 204 TRP 204 229 229 TRP TRP A . n 
A 1 205 THR 205 230 230 THR THR A . n 
A 1 206 VAL 206 231 231 VAL VAL A . n 
A 1 207 GLY 207 232 232 GLY GLY A . n 
A 1 208 ASP 208 233 233 ASP ASP A . n 
A 1 209 LYS 209 234 234 LYS LYS A . n 
A 1 210 THR 210 235 235 THR THR A . n 
A 1 211 GLY 211 236 236 GLY GLY A . n 
A 1 212 SER 212 237 237 SER SER A . n 
A 1 213 GLY 213 238 238 GLY GLY A . n 
A 1 214 ASP 214 240 240 ASP ASP A . n 
A 1 215 TYR 215 241 241 TYR TYR A . n 
A 1 216 GLY 216 242 242 GLY GLY A . n 
A 1 217 THR 217 243 243 THR THR A . n 
A 1 218 THR 218 244 244 THR THR A . n 
A 1 219 ASN 219 245 245 ASN ASN A . n 
A 1 220 ASP 220 246 246 ASP ASP A . n 
A 1 221 ILE 221 247 247 ILE ILE A . n 
A 1 222 ALA 222 248 248 ALA ALA A . n 
A 1 223 VAL 223 249 249 VAL VAL A . n 
A 1 224 ILE 224 250 250 ILE ILE A . n 
A 1 225 TRP 225 251 251 TRP TRP A . n 
A 1 226 PRO 226 252 252 PRO PRO A . n 
A 1 227 GLN 227 254 254 GLN GLN A . n 
A 1 228 GLY 228 255 255 GLY GLY A . n 
A 1 229 ARG 229 256 256 ARG ARG A . n 
A 1 230 ALA 230 257 257 ALA ALA A . n 
A 1 231 PRO 231 258 258 PRO PRO A . n 
A 1 232 LEU 232 259 259 LEU LEU A . n 
A 1 233 VAL 233 260 260 VAL VAL A . n 
A 1 234 LEU 234 261 261 LEU LEU A . n 
A 1 235 VAL 235 262 262 VAL VAL A . n 
A 1 236 THR 236 263 263 THR THR A . n 
A 1 237 TYR 237 264 264 TYR TYR A . n 
A 1 238 PHE 238 265 265 PHE PHE A . n 
A 1 239 THR 239 266 266 THR THR A . n 
A 1 240 GLN 240 267 267 GLN GLN A . n 
A 1 241 PRO 241 268 268 PRO PRO A . n 
A 1 242 GLN 242 269 269 GLN GLN A . n 
A 1 243 GLN 243 270 270 GLN GLN A . n 
A 1 244 ASN 244 271 271 ASN ASN A . n 
A 1 245 ALA 245 272 272 ALA ALA A . n 
A 1 246 GLU 246 273 273 GLU GLU A . n 
A 1 247 SER 247 274 274 SER SER A . n 
A 1 248 ARG 248 275 275 ARG ARG A . n 
A 1 249 ARG 249 276 276 ARG ARG A . n 
A 1 250 ASP 250 277 277 ASP ASP A . n 
A 1 251 VAL 251 278 278 VAL VAL A . n 
A 1 252 LEU 252 279 279 LEU LEU A . n 
A 1 253 ALA 253 280 280 ALA ALA A . n 
A 1 254 SER 254 281 281 SER SER A . n 
A 1 255 ALA 255 282 282 ALA ALA A . n 
A 1 256 ALA 256 283 283 ALA ALA A . n 
A 1 257 ARG 257 284 284 ARG ARG A . n 
A 1 258 ILE 258 285 285 ILE ILE A . n 
A 1 259 ILE 259 286 286 ILE ILE A . n 
A 1 260 ALA 260 287 287 ALA ALA A . n 
A 1 261 GLU 261 288 288 GLU GLU A . n 
A 1 262 GLY 262 289 289 GLY GLY A . n 
A 1 263 LEU 263 290 290 LEU LEU A . n 
B 1 1   GLN 1   25  25  GLN GLN B . n 
B 1 2   THR 2   26  26  THR THR B . n 
B 1 3   SER 3   27  27  SER SER B . n 
B 1 4   ALA 4   28  28  ALA ALA B . n 
B 1 5   VAL 5   29  29  VAL VAL B . n 
B 1 6   GLN 6   30  30  GLN GLN B . n 
B 1 7   GLN 7   31  31  GLN GLN B . n 
B 1 8   LYS 8   32  32  LYS LYS B . n 
B 1 9   LEU 9   33  33  LEU LEU B . n 
B 1 10  ALA 10  34  34  ALA ALA B . n 
B 1 11  ALA 11  35  35  ALA ALA B . n 
B 1 12  LEU 12  36  36  LEU LEU B . n 
B 1 13  GLU 13  37  37  GLU GLU B . n 
B 1 14  LYS 14  38  38  LYS LYS B . n 
B 1 15  SER 15  39  39  SER SER B . n 
B 1 16  SER 16  40  40  SER SER B . n 
B 1 17  GLY 17  41  41  GLY GLY B . n 
B 1 18  GLY 18  42  42  GLY GLY B . n 
B 1 19  ARG 19  43  43  ARG ARG B . n 
B 1 20  LEU 20  44  44  LEU LEU B . n 
B 1 21  GLY 21  45  45  GLY GLY B . n 
B 1 22  VAL 22  46  46  VAL VAL B . n 
B 1 23  ALA 23  47  47  ALA ALA B . n 
B 1 24  LEU 24  48  48  LEU LEU B . n 
B 1 25  ILE 25  49  49  ILE ILE B . n 
B 1 26  ASP 26  50  50  ASP ASP B . n 
B 1 27  THR 27  51  51  THR THR B . n 
B 1 28  ALA 28  52  52  ALA ALA B . n 
B 1 29  ASP 29  53  53  ASP ASP B . n 
B 1 30  ASN 30  54  54  ASN ASN B . n 
B 1 31  THR 31  55  55  THR THR B . n 
B 1 32  GLN 32  56  56  GLN GLN B . n 
B 1 33  VAL 33  57  57  VAL VAL B . n 
B 1 34  LEU 34  59  59  LEU LEU B . n 
B 1 35  TYR 35  60  60  TYR TYR B . n 
B 1 36  ARG 36  61  61  ARG ARG B . n 
B 1 37  GLY 37  62  62  GLY GLY B . n 
B 1 38  ASP 38  63  63  ASP ASP B . n 
B 1 39  GLU 39  64  64  GLU GLU B . n 
B 1 40  ARG 40  65  65  ARG ARG B . n 
B 1 41  PHE 41  66  66  PHE PHE B . n 
B 1 42  PRO 42  67  67  PRO PRO B . n 
B 1 43  MET 43  68  68  MET MET B . n 
B 1 44  CYS 44  69  69  CYS CYS B . n 
B 1 45  SER 45  70  70  SER SER B . n 
B 1 46  THR 46  71  71  THR THR B . n 
B 1 47  SER 47  72  72  SER SER B . n 
B 1 48  LYS 48  73  73  LYS LYS B . n 
B 1 49  VAL 49  74  74  VAL VAL B . n 
B 1 50  MET 50  75  75  MET MET B . n 
B 1 51  ALA 51  76  76  ALA ALA B . n 
B 1 52  ALA 52  77  77  ALA ALA B . n 
B 1 53  ALA 53  78  78  ALA ALA B . n 
B 1 54  ALA 54  79  79  ALA ALA B . n 
B 1 55  VAL 55  80  80  VAL VAL B . n 
B 1 56  LEU 56  81  81  LEU LEU B . n 
B 1 57  LYS 57  82  82  LYS LYS B . n 
B 1 58  GLN 58  83  83  GLN GLN B . n 
B 1 59  SER 59  84  84  SER SER B . n 
B 1 60  GLU 60  85  85  GLU GLU B . n 
B 1 61  THR 61  86  86  THR THR B . n 
B 1 62  GLN 62  87  87  GLN GLN B . n 
B 1 63  LYS 63  88  88  LYS LYS B . n 
B 1 64  GLN 64  89  89  GLN GLN B . n 
B 1 65  LEU 65  90  90  LEU LEU B . n 
B 1 66  LEU 66  91  91  LEU LEU B . n 
B 1 67  ASN 67  92  92  ASN ASN B . n 
B 1 68  GLN 68  93  93  GLN GLN B . n 
B 1 69  PRO 69  94  94  PRO PRO B . n 
B 1 70  VAL 70  95  95  VAL VAL B . n 
B 1 71  GLU 71  96  96  GLU GLU B . n 
B 1 72  ILE 72  97  97  ILE ILE B . n 
B 1 73  LYS 73  98  98  LYS LYS B . n 
B 1 74  PRO 74  99  99  PRO PRO B . n 
B 1 75  ALA 75  100 100 ALA ALA B . n 
B 1 76  ASP 76  101 101 ASP ASP B . n 
B 1 77  LEU 77  102 102 LEU LEU B . n 
B 1 78  VAL 78  103 103 VAL VAL B . n 
B 1 79  ASN 79  104 104 ASN ASN B . n 
B 1 80  TYR 80  105 105 TYR TYR B . n 
B 1 81  ASN 81  106 106 ASN ASN B . n 
B 1 82  PRO 82  107 107 PRO PRO B . n 
B 1 83  ILE 83  108 108 ILE ILE B . n 
B 1 84  ALA 84  109 109 ALA ALA B . n 
B 1 85  GLU 85  110 110 GLU GLU B . n 
B 1 86  LYS 86  111 111 LYS LYS B . n 
B 1 87  HIS 87  112 112 HIS HIS B . n 
B 1 88  VAL 88  113 113 VAL VAL B . n 
B 1 89  ASN 89  114 114 ASN ASN B . n 
B 1 90  GLY 90  115 115 GLY GLY B . n 
B 1 91  THR 91  116 116 THR THR B . n 
B 1 92  MET 92  117 117 MET MET B . n 
B 1 93  THR 93  118 118 THR THR B . n 
B 1 94  LEU 94  119 119 LEU LEU B . n 
B 1 95  ALA 95  120 120 ALA ALA B . n 
B 1 96  GLU 96  121 121 GLU GLU B . n 
B 1 97  LEU 97  122 122 LEU LEU B . n 
B 1 98  SER 98  123 123 SER SER B . n 
B 1 99  ALA 99  124 124 ALA ALA B . n 
B 1 100 ALA 100 125 125 ALA ALA B . n 
B 1 101 ALA 101 126 126 ALA ALA B . n 
B 1 102 LEU 102 127 127 LEU LEU B . n 
B 1 103 GLN 103 128 128 GLN GLN B . n 
B 1 104 TYR 104 129 129 TYR TYR B . n 
B 1 105 SER 105 130 130 SER SER B . n 
B 1 106 ASP 106 131 131 ASP ASP B . n 
B 1 107 ASN 107 132 132 ASN ASN B . n 
B 1 108 THR 108 133 133 THR THR B . n 
B 1 109 ALA 109 134 134 ALA ALA B . n 
B 1 110 MET 110 135 135 MET MET B . n 
B 1 111 ASN 111 136 136 ASN ASN B . n 
B 1 112 LYS 112 137 137 LYS LYS B . n 
B 1 113 LEU 113 138 138 LEU LEU B . n 
B 1 114 ILE 114 139 139 ILE ILE B . n 
B 1 115 ALA 115 140 140 ALA ALA B . n 
B 1 116 GLN 116 141 141 GLN GLN B . n 
B 1 117 LEU 117 142 142 LEU LEU B . n 
B 1 118 GLY 118 143 143 GLY GLY B . n 
B 1 119 GLY 119 144 144 GLY GLY B . n 
B 1 120 PRO 120 145 145 PRO PRO B . n 
B 1 121 GLY 121 146 146 GLY GLY B . n 
B 1 122 GLY 122 147 147 GLY GLY B . n 
B 1 123 VAL 123 148 148 VAL VAL B . n 
B 1 124 THR 124 149 149 THR THR B . n 
B 1 125 ALA 125 150 150 ALA ALA B . n 
B 1 126 PHE 126 151 151 PHE PHE B . n 
B 1 127 ALA 127 152 152 ALA ALA B . n 
B 1 128 ARG 128 153 153 ARG ARG B . n 
B 1 129 ALA 129 154 154 ALA ALA B . n 
B 1 130 ILE 130 155 155 ILE ILE B . n 
B 1 131 GLY 131 156 156 GLY GLY B . n 
B 1 132 ASP 132 157 157 ASP ASP B . n 
B 1 133 GLU 133 158 158 GLU GLU B . n 
B 1 134 THR 134 159 159 THR THR B . n 
B 1 135 PHE 135 160 160 PHE PHE B . n 
B 1 136 ARG 136 161 161 ARG ARG B . n 
B 1 137 LEU 137 162 162 LEU LEU B . n 
B 1 138 ASP 138 163 163 ASP ASP B . n 
B 1 139 ARG 139 164 164 ARG ARG B . n 
B 1 140 THR 140 165 165 THR THR B . n 
B 1 141 GLU 141 166 166 GLU GLU B . n 
B 1 142 PRO 142 167 167 PRO PRO B . n 
B 1 143 THR 143 168 168 THR THR B . n 
B 1 144 LEU 144 169 169 LEU LEU B . n 
B 1 145 ASN 145 170 170 ASN ASN B . n 
B 1 146 THR 146 171 171 THR THR B . n 
B 1 147 ALA 147 172 172 ALA ALA B . n 
B 1 148 ILE 148 173 173 ILE ILE B . n 
B 1 149 PRO 149 174 174 PRO PRO B . n 
B 1 150 GLY 150 175 175 GLY GLY B . n 
B 1 151 ASP 151 176 176 ASP ASP B . n 
B 1 152 PRO 152 177 177 PRO PRO B . n 
B 1 153 ARG 153 178 178 ARG ARG B . n 
B 1 154 ASP 154 179 179 ASP ASP B . n 
B 1 155 THR 155 180 180 THR THR B . n 
B 1 156 THR 156 181 181 THR THR B . n 
B 1 157 THR 157 182 182 THR THR B . n 
B 1 158 PRO 158 183 183 PRO PRO B . n 
B 1 159 ARG 159 184 184 ARG ARG B . n 
B 1 160 ALA 160 185 185 ALA ALA B . n 
B 1 161 MET 161 186 186 MET MET B . n 
B 1 162 ALA 162 187 187 ALA ALA B . n 
B 1 163 GLN 163 188 188 GLN GLN B . n 
B 1 164 THR 164 189 189 THR THR B . n 
B 1 165 LEU 165 190 190 LEU LEU B . n 
B 1 166 ARG 166 191 191 ARG ARG B . n 
B 1 167 GLN 167 192 192 GLN GLN B . n 
B 1 168 LEU 168 193 193 LEU LEU B . n 
B 1 169 THR 169 194 194 THR THR B . n 
B 1 170 LEU 170 195 195 LEU LEU B . n 
B 1 171 GLY 171 196 196 GLY GLY B . n 
B 1 172 HIS 172 197 197 HIS HIS B . n 
B 1 173 ALA 173 198 198 ALA ALA B . n 
B 1 174 LEU 174 199 199 LEU LEU B . n 
B 1 175 GLY 175 200 200 GLY GLY B . n 
B 1 176 GLU 176 201 201 GLU GLU B . n 
B 1 177 THR 177 202 202 THR THR B . n 
B 1 178 GLN 178 203 203 GLN GLN B . n 
B 1 179 ARG 179 204 204 ARG ARG B . n 
B 1 180 ALA 180 205 205 ALA ALA B . n 
B 1 181 GLN 181 206 206 GLN GLN B . n 
B 1 182 LEU 182 207 207 LEU LEU B . n 
B 1 183 VAL 183 208 208 VAL VAL B . n 
B 1 184 THR 184 209 209 THR THR B . n 
B 1 185 TRP 185 210 210 TRP TRP B . n 
B 1 186 LEU 186 211 211 LEU LEU B . n 
B 1 187 LYS 187 212 212 LYS LYS B . n 
B 1 188 GLY 188 213 213 GLY GLY B . n 
B 1 189 ASN 189 214 214 ASN ASN B . n 
B 1 190 THR 190 215 215 THR THR B . n 
B 1 191 THR 191 216 216 THR THR B . n 
B 1 192 GLY 192 217 217 GLY GLY B . n 
B 1 193 ALA 193 218 218 ALA ALA B . n 
B 1 194 ALA 194 219 219 ALA ALA B . n 
B 1 195 SER 195 220 220 SER SER B . n 
B 1 196 ILE 196 221 221 ILE ILE B . n 
B 1 197 ARG 197 222 222 ARG ARG B . n 
B 1 198 ALA 198 223 223 ALA ALA B . n 
B 1 199 GLY 199 224 224 GLY GLY B . n 
B 1 200 LEU 200 225 225 LEU LEU B . n 
B 1 201 PRO 201 226 226 PRO PRO B . n 
B 1 202 THR 202 227 227 THR THR B . n 
B 1 203 SER 203 228 228 SER SER B . n 
B 1 204 TRP 204 229 229 TRP TRP B . n 
B 1 205 THR 205 230 230 THR THR B . n 
B 1 206 VAL 206 231 231 VAL VAL B . n 
B 1 207 GLY 207 232 232 GLY GLY B . n 
B 1 208 ASP 208 233 233 ASP ASP B . n 
B 1 209 LYS 209 234 234 LYS LYS B . n 
B 1 210 THR 210 235 235 THR THR B . n 
B 1 211 GLY 211 236 236 GLY GLY B . n 
B 1 212 SER 212 237 237 SER SER B . n 
B 1 213 GLY 213 238 238 GLY GLY B . n 
B 1 214 ASP 214 240 240 ASP ASP B . n 
B 1 215 TYR 215 241 241 TYR TYR B . n 
B 1 216 GLY 216 242 242 GLY GLY B . n 
B 1 217 THR 217 243 243 THR THR B . n 
B 1 218 THR 218 244 244 THR THR B . n 
B 1 219 ASN 219 245 245 ASN ASN B . n 
B 1 220 ASP 220 246 246 ASP ASP B . n 
B 1 221 ILE 221 247 247 ILE ILE B . n 
B 1 222 ALA 222 248 248 ALA ALA B . n 
B 1 223 VAL 223 249 249 VAL VAL B . n 
B 1 224 ILE 224 250 250 ILE ILE B . n 
B 1 225 TRP 225 251 251 TRP TRP B . n 
B 1 226 PRO 226 252 252 PRO PRO B . n 
B 1 227 GLN 227 254 254 GLN GLN B . n 
B 1 228 GLY 228 255 255 GLY GLY B . n 
B 1 229 ARG 229 256 256 ARG ARG B . n 
B 1 230 ALA 230 257 257 ALA ALA B . n 
B 1 231 PRO 231 258 258 PRO PRO B . n 
B 1 232 LEU 232 259 259 LEU LEU B . n 
B 1 233 VAL 233 260 260 VAL VAL B . n 
B 1 234 LEU 234 261 261 LEU LEU B . n 
B 1 235 VAL 235 262 262 VAL VAL B . n 
B 1 236 THR 236 263 263 THR THR B . n 
B 1 237 TYR 237 264 264 TYR TYR B . n 
B 1 238 PHE 238 265 265 PHE PHE B . n 
B 1 239 THR 239 266 266 THR THR B . n 
B 1 240 GLN 240 267 267 GLN GLN B . n 
B 1 241 PRO 241 268 268 PRO PRO B . n 
B 1 242 GLN 242 269 269 GLN GLN B . n 
B 1 243 GLN 243 270 270 GLN GLN B . n 
B 1 244 ASN 244 271 271 ASN ASN B . n 
B 1 245 ALA 245 272 272 ALA ALA B . n 
B 1 246 GLU 246 273 273 GLU GLU B . n 
B 1 247 SER 247 274 274 SER SER B . n 
B 1 248 ARG 248 275 275 ARG ARG B . n 
B 1 249 ARG 249 276 276 ARG ARG B . n 
B 1 250 ASP 250 277 277 ASP ASP B . n 
B 1 251 VAL 251 278 278 VAL VAL B . n 
B 1 252 LEU 252 279 279 LEU LEU B . n 
B 1 253 ALA 253 280 280 ALA ALA B . n 
B 1 254 SER 254 281 281 SER SER B . n 
B 1 255 ALA 255 282 282 ALA ALA B . n 
B 1 256 ALA 256 283 283 ALA ALA B . n 
B 1 257 ARG 257 284 284 ARG ARG B . n 
B 1 258 ILE 258 285 285 ILE ILE B . n 
B 1 259 ILE 259 286 286 ILE ILE B . n 
B 1 260 ALA 260 287 287 ALA ALA B . n 
B 1 261 GLU 261 288 288 GLU GLU B . n 
B 1 262 GLY 262 289 289 GLY GLY B . n 
B 1 263 LEU 263 290 290 LEU LEU B . 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 
C 2 NXL 1  301 301 NXL LIG A . 
D 2 NXL 1  301 301 NXL LIG B . 
E 3 HOH 1  401 19  HOH HOH A . 
E 3 HOH 2  402 4   HOH HOH A . 
E 3 HOH 3  403 15  HOH HOH A . 
E 3 HOH 4  404 1   HOH HOH A . 
E 3 HOH 5  405 7   HOH HOH A . 
E 3 HOH 6  406 18  HOH HOH A . 
E 3 HOH 7  407 10  HOH HOH A . 
E 3 HOH 8  408 17  HOH HOH A . 
E 3 HOH 9  409 11  HOH HOH A . 
E 3 HOH 10 410 5   HOH HOH A . 
E 3 HOH 11 411 20  HOH HOH A . 
E 3 HOH 12 412 25  HOH HOH A . 
E 3 HOH 13 413 27  HOH HOH A . 
E 3 HOH 14 414 24  HOH HOH A . 
E 3 HOH 15 415 21  HOH HOH A . 
F 3 HOH 1  401 12  HOH HOH B . 
F 3 HOH 2  402 26  HOH HOH B . 
F 3 HOH 3  403 14  HOH HOH B . 
F 3 HOH 4  404 13  HOH HOH B . 
F 3 HOH 5  405 23  HOH HOH B . 
F 3 HOH 6  406 3   HOH HOH B . 
F 3 HOH 7  407 28  HOH HOH B . 
F 3 HOH 8  408 8   HOH HOH B . 
F 3 HOH 9  409 16  HOH HOH B . 
F 3 HOH 10 410 2   HOH HOH B . 
F 3 HOH 11 411 22  HOH HOH B . 
F 3 HOH 12 412 29  HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.dependencies 
_software.description 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.pdbx_ordinal 
_software.pdbx_reference_DOI 
_software.type 
_software.version 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? 1 ? ? 1.20.1_4487 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? 2 ? ? .           
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? XSCALE      ? ? 3 ? ? .           
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? 4 ? ? .           
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? 5 ? ? .           
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   100.95 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9ORL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     44.990 
_cell.length_a_esd                 ? 
_cell.length_b                     105.700 
_cell.length_b_esd                 ? 
_cell.length_c                     47.490 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9ORL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9ORL 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON CRYSTALLOGRAPHY' 
_exptl.method_details             ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9ORL 
_refine.pdbx_refine_id                           'ELECTRON CRYSTALLOGRAPHY' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.30 
_refine.ls_d_res_low                             46.63 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     18786 
_refine.ls_number_reflns_R_free                  1876 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.82 
_refine.ls_percent_reflns_R_free                 9.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1767 
_refine.ls_R_factor_R_free                       0.2219 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1716 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.37 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 21.50 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.29 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON CRYSTALLOGRAPHY' ? 0.005 ? 4015 ? f_bond_d           ? ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 1.073 ? 5470 ? f_angle_d          ? ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 7.046 ? 588  ? f_dihedral_angle_d ? ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 0.056 ? 650  ? f_chiral_restr     ? ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 0.009 ? 720  ? f_plane_restr      ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'ELECTRON CRYSTALLOGRAPHY' 2.30 2.36  . . 143 1289 95.00 . . . . 0.2365 . . . . . . . . . . . . . . . 0.3385 
'ELECTRON CRYSTALLOGRAPHY' 2.36 2.43  . . 145 1300 99.00 . . . . 0.2274 . . . . . . . . . . . . . . . 0.2863 
'ELECTRON CRYSTALLOGRAPHY' 2.43 2.51  . . 146 1312 98.00 . . . . 0.2237 . . . . . . . . . . . . . . . 0.3082 
'ELECTRON CRYSTALLOGRAPHY' 2.51 2.60  . . 141 1286 97.00 . . . . 0.2208 . . . . . . . . . . . . . . . 0.2755 
'ELECTRON CRYSTALLOGRAPHY' 2.60 2.70  . . 145 1305 97.00 . . . . 0.2171 . . . . . . . . . . . . . . . 0.2696 
'ELECTRON CRYSTALLOGRAPHY' 2.70 2.83  . . 148 1326 97.00 . . . . 0.2142 . . . . . . . . . . . . . . . 0.2764 
'ELECTRON CRYSTALLOGRAPHY' 2.83 2.98  . . 145 1307 97.00 . . . . 0.2040 . . . . . . . . . . . . . . . 0.2778 
'ELECTRON CRYSTALLOGRAPHY' 2.98 3.16  . . 144 1299 98.00 . . . . 0.2014 . . . . . . . . . . . . . . . 0.2744 
'ELECTRON CRYSTALLOGRAPHY' 3.16 3.41  . . 145 1312 97.00 . . . . 0.1701 . . . . . . . . . . . . . . . 0.2061 
'ELECTRON CRYSTALLOGRAPHY' 3.41 3.75  . . 145 1307 97.00 . . . . 0.1422 . . . . . . . . . . . . . . . 0.1844 
'ELECTRON CRYSTALLOGRAPHY' 3.75 4.29  . . 143 1286 96.00 . . . . 0.1254 . . . . . . . . . . . . . . . 0.1690 
'ELECTRON CRYSTALLOGRAPHY' 4.29 5.40  . . 145 1301 96.00 . . . . 0.1147 . . . . . . . . . . . . . . . 0.1379 
'ELECTRON CRYSTALLOGRAPHY' 5.41 46.63 . . 141 1280 93.00 . . . . 0.1502 . . . . . . . . . . . . . . . 0.1909 
# 
_struct.entry_id                     9ORL 
_struct.title                        'MicroED structure of CTX-M-14 beta-lactamase soaked with avibactam' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9ORL 
_struct_keywords.text            'Enzyme, beta-lactamase, inhibitor, complex, MicroED, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q9L5C7_ECOLX 
_struct_ref.pdbx_db_accession          Q9L5C7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;QTSAVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVMAAAAVLKQSETQKQLLNQPVEIKPADLVNY
NPIAEKHVNGTMTLAELSAAALQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPGDPRDTTTPRA
MAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLPTSWTVGDKTGSGDYGTTNDIAVIWPQGRAPLVLVTYFTQ
PQQNAESRRDVLASAARIIAEGL
;
_struct_ref.pdbx_align_begin           29 
# 
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 9ORL A 1 ? 263 ? Q9L5C7 29 ? 291 ? 25 290 
2 1 9ORL B 1 ? 263 ? Q9L5C7 29 ? 291 ? 25 290 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E 
2 1 B,D,F 
# 
_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_
_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  AA1 SER A 3   ? GLY A 17  ? SER A 27  GLY A 41  1 ? 15 
HELX_P HELX_P2  AA2 THR A 46  ? GLU A 60  ? THR A 71  GLU A 85  1 ? 15 
HELX_P HELX_P3  AA3 GLN A 64  ? ASN A 67  ? GLN A 89  ASN A 92  5 ? 4  
HELX_P HELX_P4  AA4 LYS A 73  ? LEU A 77  ? LYS A 98  LEU A 102 5 ? 5  
HELX_P HELX_P5  AA5 ILE A 83  ? VAL A 88  ? ILE A 108 VAL A 113 5 ? 6  
HELX_P HELX_P6  AA6 LEU A 94  ? TYR A 104 ? LEU A 119 TYR A 129 1 ? 11 
HELX_P HELX_P7  AA7 ASP A 106 ? LEU A 117 ? ASP A 131 LEU A 142 1 ? 12 
HELX_P HELX_P8  AA8 GLY A 119 ? ILE A 130 ? GLY A 144 ILE A 155 1 ? 12 
HELX_P HELX_P9  AA9 PRO A 142 ? THR A 146 ? PRO A 167 THR A 171 5 ? 5  
HELX_P HELX_P10 AB1 THR A 157 ? LEU A 170 ? THR A 182 LEU A 195 1 ? 14 
HELX_P HELX_P11 AB2 GLY A 175 ? GLY A 188 ? GLY A 200 GLY A 213 1 ? 14 
HELX_P HELX_P12 AB3 SER A 195 ? LEU A 200 ? SER A 220 LEU A 225 1 ? 6  
HELX_P HELX_P13 AB4 ARG A 248 ? LEU A 263 ? ARG A 275 LEU A 290 1 ? 16 
HELX_P HELX_P14 AB5 ALA B 4   ? GLY B 17  ? ALA B 28  GLY B 41  1 ? 14 
HELX_P HELX_P15 AB6 THR B 46  ? GLU B 60  ? THR B 71  GLU B 85  1 ? 15 
HELX_P HELX_P16 AB7 GLN B 64  ? ASN B 67  ? GLN B 89  ASN B 92  5 ? 4  
HELX_P HELX_P17 AB8 LYS B 73  ? LEU B 77  ? LYS B 98  LEU B 102 5 ? 5  
HELX_P HELX_P18 AB9 ILE B 83  ? VAL B 88  ? ILE B 108 VAL B 113 5 ? 6  
HELX_P HELX_P19 AC1 LEU B 94  ? SER B 105 ? LEU B 119 SER B 130 1 ? 12 
HELX_P HELX_P20 AC2 ASP B 106 ? LEU B 117 ? ASP B 131 LEU B 142 1 ? 12 
HELX_P HELX_P21 AC3 GLY B 119 ? ILE B 130 ? GLY B 144 ILE B 155 1 ? 12 
HELX_P HELX_P22 AC4 PRO B 142 ? THR B 146 ? PRO B 167 THR B 171 5 ? 5  
HELX_P HELX_P23 AC5 THR B 157 ? LEU B 170 ? THR B 182 LEU B 195 1 ? 14 
HELX_P HELX_P24 AC6 GLY B 175 ? GLY B 188 ? GLY B 200 GLY B 213 1 ? 14 
HELX_P HELX_P25 AC7 ILE B 196 ? LEU B 200 ? ILE B 221 LEU B 225 5 ? 5  
HELX_P HELX_P26 AC8 ARG B 248 ? GLY B 262 ? ARG B 275 GLY B 289 1 ? 15 
# 
_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 
_struct_conn.pdbx_role 
covale1 covale none ? A SER 45 OG ? ? ? 1_555 C NXL . CAN ? ? A SER 70 A NXL 301 1_555 ? ? ? ? ? ? ? 1.381 ? ? 
covale2 covale none ? B SER 45 OG ? ? ? 1_555 D NXL . CAN ? ? B SER 70 B NXL 301 1_555 ? ? ? ? ? ? ? 1.378 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NXL C . ? SER A 45 ? NXL A 301 ? 1_555 SER A 70 ? 1_555 CAN OG SER 2 NXL None 'Covalent chemical modification' 
2 NXL D . ? SER B 45 ? NXL B 301 ? 1_555 SER B 70 ? 1_555 CAN OG SER 2 NXL None 'Covalent chemical modification' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 141 A . ? GLU 166 A PRO 142 A ? PRO 167 A 1 3.04 
2 GLU 141 B . ? GLU 166 B PRO 142 B ? PRO 167 B 1 5.53 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 5 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 31  ? TYR A 35  ? THR A 55  TYR A 60  
AA1 2 ARG A 19  ? ASP A 26  ? ARG A 43  ASP A 50  
AA1 3 LEU A 232 ? THR A 239 ? LEU A 259 THR A 266 
AA1 4 THR A 217 ? TRP A 225 ? THR A 243 TRP A 251 
AA1 5 THR A 205 ? GLY A 213 ? THR A 230 GLY A 238 
AA2 1 PHE A 41  ? PRO A 42  ? PHE A 66  PRO A 67  
AA2 2 THR A 155 ? THR A 156 ? THR A 180 THR A 181 
AA3 1 PRO A 69  ? ILE A 72  ? PRO A 94  ILE A 97  
AA3 2 GLY A 90  ? THR A 93  ? GLY A 115 THR A 118 
AA4 1 THR B 31  ? TYR B 35  ? THR B 55  TYR B 60  
AA4 2 ARG B 19  ? ASP B 26  ? ARG B 43  ASP B 50  
AA4 3 LEU B 232 ? THR B 239 ? LEU B 259 THR B 266 
AA4 4 THR B 217 ? TRP B 225 ? THR B 243 TRP B 251 
AA4 5 THR B 205 ? GLY B 213 ? THR B 230 GLY B 238 
AA5 1 PHE B 41  ? PRO B 42  ? PHE B 66  PRO B 67  
AA5 2 THR B 155 ? THR B 156 ? THR B 180 THR B 181 
AA6 1 PRO B 69  ? ILE B 72  ? PRO B 94  ILE B 97  
AA6 2 GLY B 90  ? THR B 93  ? GLY B 115 THR B 118 
# 
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 
AA1 1 2 O THR A 31  ? O THR A 55  N ASP A 26  ? N ASP A 50  
AA1 2 3 N ARG A 19  ? N ARG A 43  O THR A 239 ? O THR A 266 
AA1 3 4 O THR A 236 ? O THR A 263 N ASP A 220 ? N ASP A 246 
AA1 4 5 O TRP A 225 ? O TRP A 251 N THR A 205 ? N THR A 230 
AA2 1 2 N PHE A 41  ? N PHE A 66  O THR A 156 ? O THR A 181 
AA3 1 2 N ILE A 72  ? N ILE A 97  O GLY A 90  ? O GLY A 115 
AA4 1 2 O THR B 31  ? O THR B 55  N ASP B 26  ? N ASP B 50  
AA4 2 3 N GLY B 21  ? N GLY B 45  O TYR B 237 ? O TYR B 264 
AA4 3 4 O THR B 236 ? O THR B 263 N ASP B 220 ? N ASP B 246 
AA4 4 5 O TRP B 225 ? O TRP B 251 N THR B 205 ? N THR B 230 
AA5 1 2 N PHE B 41  ? N PHE B 66  O THR B 156 ? O THR B 181 
AA6 1 2 N ILE B 72  ? N ILE B 97  O GLY B 90  ? O GLY B 115 
# 
_pdbx_entry_details.entry_id                   9ORL 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OG 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   SER 
_pdbx_validate_close_contact.auth_seq_id_1    70 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OAC 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   NXL 
_pdbx_validate_close_contact.auth_seq_id_2    301 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.15 
# 
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 N  A GLN 87  ? ? CA A GLN 87  ? ? C  A GLN 87  ? ? 94.19  111.00 -16.81 2.70 N 
2 1 CA B LEU 290 ? ? CB B LEU 290 ? ? CG B LEU 290 ? ? 129.42 115.30 14.12  2.30 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 CYS A 69  ? ? 51.45   -134.82 
2 1 VAL A 103 ? ? -116.18 -132.70 
3 1 SER A 220 ? ? -109.74 -126.46 
4 1 SER B 27  ? ? -64.68  -151.61 
5 1 ASP B 53  ? ? -147.46 10.69   
6 1 CYS B 69  ? ? 47.90   -134.14 
7 1 VAL B 103 ? ? -114.65 -132.48 
8 1 SER B 220 ? ? -108.06 -124.09 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9ORL 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  1YLT 
_em_3d_fitting_list.pdb_chain_id                  ? 
_em_3d_fitting_list.pdb_chain_residue_range       ? 
_em_3d_fitting_list.details                       ? 
_em_3d_fitting_list.chain_id                      ? 
_em_3d_fitting_list.chain_residue_range           ? 
_em_3d_fitting_list.source_name                   PDB 
_em_3d_fitting_list.type                          'experimental model' 
_em_3d_fitting_list.accession_code                1YLT 
_em_3d_fitting_list.initial_refinement_model_id   1 
# 
_em_3d_reconstruction.entry_id                    9ORL 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.3 
_em_3d_reconstruction.resolution_method           'DIFFRACTION PATTERN/LAYERLINES' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               ? 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               '3D CRYSTAL' 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       '1.4 M potassium phosphate' 
_em_buffer.pH            7.9 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'CTX-M-14 beta-lactamase bound to avibactam' 
_em_entity_assembly.details              
;Crystals were grown by hanging-drop vapor diffusion from drops of 25.7 mg/mL CTX-M-14 mixed 1:1 with crystallization solution (1.4 M potassium phosphate pH 7.9)
;
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9ORL 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS TALOS F200C' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            200 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            DIFFRACTION 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             0 
_em_imaging.nominal_defocus_max             0 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            70 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
_em_imaging.objective_aperture              ? 
_em_imaging.microscope_serial_number        ? 
_em_imaging.microscope_version              ? 
# 
_em_vitrification.entry_id              9ORL 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9ORL 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   CRYSTALLOGRAPHY 
_em_experiment.aggregation_state       '3D ARRAY' 
_em_experiment.entity_assembly_id      1 
# 
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 GLN 25 ? A GLN 1 
2 1 Y 1 A THR 26 ? A THR 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
NXL OAC  O N N 250 
NXL CAN  C N N 251 
NXL N    N N N 252 
NXL CAJ  C N N 253 
NXL CA   C N S 254 
NXL C    C N N 255 
NXL O    O N N 256 
NXL NAA  N N N 257 
NXL CB   C N N 258 
NXL CAH  C N N 259 
NXL CAO  C N R 260 
NXL NAK  N N N 261 
NXL OAL  O N N 262 
NXL SAR  S N N 263 
NXL OAD  O N N 264 
NXL OAE  O N N 265 
NXL OAG  O N N 266 
NXL H1   H N N 267 
NXL H2   H N N 268 
NXL H3   H N N 269 
NXL H4   H N N 270 
NXL H5   H N N 271 
NXL H6   H N N 272 
NXL H7   H N N 273 
NXL H8   H N N 274 
NXL H9   H N N 275 
NXL H10  H N N 276 
NXL H11  H N N 277 
NXL H12  H N N 278 
NXL H13  H N N 279 
PHE N    N N N 280 
PHE CA   C N S 281 
PHE C    C N N 282 
PHE O    O N N 283 
PHE CB   C N N 284 
PHE CG   C Y N 285 
PHE CD1  C Y N 286 
PHE CD2  C Y N 287 
PHE CE1  C Y N 288 
PHE CE2  C Y N 289 
PHE CZ   C Y N 290 
PHE OXT  O N N 291 
PHE H    H N N 292 
PHE H2   H N N 293 
PHE HA   H N N 294 
PHE HB2  H N N 295 
PHE HB3  H N N 296 
PHE HD1  H N N 297 
PHE HD2  H N N 298 
PHE HE1  H N N 299 
PHE HE2  H N N 300 
PHE HZ   H N N 301 
PHE HXT  H N N 302 
PRO N    N N N 303 
PRO CA   C N S 304 
PRO C    C N N 305 
PRO O    O N N 306 
PRO CB   C N N 307 
PRO CG   C N N 308 
PRO CD   C N N 309 
PRO OXT  O N N 310 
PRO H    H N N 311 
PRO HA   H N N 312 
PRO HB2  H N N 313 
PRO HB3  H N N 314 
PRO HG2  H N N 315 
PRO HG3  H N N 316 
PRO HD2  H N N 317 
PRO HD3  H N N 318 
PRO HXT  H N N 319 
SER N    N N N 320 
SER CA   C N S 321 
SER C    C N N 322 
SER O    O N N 323 
SER CB   C N N 324 
SER OG   O N N 325 
SER OXT  O N N 326 
SER H    H N N 327 
SER H2   H N N 328 
SER HA   H N N 329 
SER HB2  H N N 330 
SER HB3  H N N 331 
SER HG   H N N 332 
SER HXT  H N N 333 
THR N    N N N 334 
THR CA   C N S 335 
THR C    C N N 336 
THR O    O N N 337 
THR CB   C N R 338 
THR OG1  O N N 339 
THR CG2  C N N 340 
THR OXT  O N N 341 
THR H    H N N 342 
THR H2   H N N 343 
THR HA   H N N 344 
THR HB   H N N 345 
THR HG1  H N N 346 
THR HG21 H N N 347 
THR HG22 H N N 348 
THR HG23 H N N 349 
THR HXT  H N N 350 
TRP N    N N N 351 
TRP CA   C N S 352 
TRP C    C N N 353 
TRP O    O N N 354 
TRP CB   C N N 355 
TRP CG   C Y N 356 
TRP CD1  C Y N 357 
TRP CD2  C Y N 358 
TRP NE1  N Y N 359 
TRP CE2  C Y N 360 
TRP CE3  C Y N 361 
TRP CZ2  C Y N 362 
TRP CZ3  C Y N 363 
TRP CH2  C Y N 364 
TRP OXT  O N N 365 
TRP H    H N N 366 
TRP H2   H N N 367 
TRP HA   H N N 368 
TRP HB2  H N N 369 
TRP HB3  H N N 370 
TRP HD1  H N N 371 
TRP HE1  H N N 372 
TRP HE3  H N N 373 
TRP HZ2  H N N 374 
TRP HZ3  H N N 375 
TRP HH2  H N N 376 
TRP HXT  H N N 377 
TYR N    N N N 378 
TYR CA   C N S 379 
TYR C    C N N 380 
TYR O    O N N 381 
TYR CB   C N N 382 
TYR CG   C Y N 383 
TYR CD1  C Y N 384 
TYR CD2  C Y N 385 
TYR CE1  C Y N 386 
TYR CE2  C Y N 387 
TYR CZ   C Y N 388 
TYR OH   O N N 389 
TYR OXT  O N N 390 
TYR H    H N N 391 
TYR H2   H N N 392 
TYR HA   H N N 393 
TYR HB2  H N N 394 
TYR HB3  H N N 395 
TYR HD1  H N N 396 
TYR HD2  H N N 397 
TYR HE1  H N N 398 
TYR HE2  H N N 399 
TYR HH   H N N 400 
TYR HXT  H N N 401 
VAL N    N N N 402 
VAL CA   C N S 403 
VAL C    C N N 404 
VAL O    O N N 405 
VAL CB   C N N 406 
VAL CG1  C N N 407 
VAL CG2  C N N 408 
VAL OXT  O N N 409 
VAL H    H N N 410 
VAL H2   H N N 411 
VAL HA   H N N 412 
VAL HB   H N N 413 
VAL HG11 H N N 414 
VAL HG12 H N N 415 
VAL HG13 H N N 416 
VAL HG21 H N N 417 
VAL HG22 H N N 418 
VAL HG23 H N N 419 
VAL HXT  H N N 420 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
NXL NAK CAO  sing N N 237 
NXL CAJ CAO  sing N N 238 
NXL CAJ N    sing N N 239 
NXL OAL SAR  sing N N 240 
NXL CAO CAH  sing N N 241 
NXL CAN N    sing N N 242 
NXL CAN OAC  doub N N 243 
NXL OAG SAR  doub N N 244 
NXL N   CA   sing N N 245 
NXL SAR OAE  doub N N 246 
NXL SAR OAD  sing N N 247 
NXL O   C    doub N N 248 
NXL CAH CB   sing N N 249 
NXL CA  C    sing N N 250 
NXL CA  CB   sing N N 251 
NXL C   NAA  sing N N 252 
NXL NAK OAL  sing N N 253 
NXL CAN H1   sing N N 254 
NXL CAJ H2   sing N N 255 
NXL CAJ H3   sing N N 256 
NXL CA  H4   sing N N 257 
NXL NAA H5   sing N N 258 
NXL NAA H6   sing N N 259 
NXL CB  H7   sing N N 260 
NXL CB  H8   sing N N 261 
NXL CAH H9   sing N N 262 
NXL CAH H10  sing N N 263 
NXL CAO H11  sing N N 264 
NXL NAK H12  sing N N 265 
NXL OAD H13  sing N N 266 
PHE N   CA   sing N N 267 
PHE N   H    sing N N 268 
PHE N   H2   sing N N 269 
PHE CA  C    sing N N 270 
PHE CA  CB   sing N N 271 
PHE CA  HA   sing N N 272 
PHE C   O    doub N N 273 
PHE C   OXT  sing N N 274 
PHE CB  CG   sing N N 275 
PHE CB  HB2  sing N N 276 
PHE CB  HB3  sing N N 277 
PHE CG  CD1  doub Y N 278 
PHE CG  CD2  sing Y N 279 
PHE CD1 CE1  sing Y N 280 
PHE CD1 HD1  sing N N 281 
PHE CD2 CE2  doub Y N 282 
PHE CD2 HD2  sing N N 283 
PHE CE1 CZ   doub Y N 284 
PHE CE1 HE1  sing N N 285 
PHE CE2 CZ   sing Y N 286 
PHE CE2 HE2  sing N N 287 
PHE CZ  HZ   sing N N 288 
PHE OXT HXT  sing N N 289 
PRO N   CA   sing N N 290 
PRO N   CD   sing N N 291 
PRO N   H    sing N N 292 
PRO CA  C    sing N N 293 
PRO CA  CB   sing N N 294 
PRO CA  HA   sing N N 295 
PRO C   O    doub N N 296 
PRO C   OXT  sing N N 297 
PRO CB  CG   sing N N 298 
PRO CB  HB2  sing N N 299 
PRO CB  HB3  sing N N 300 
PRO CG  CD   sing N N 301 
PRO CG  HG2  sing N N 302 
PRO CG  HG3  sing N N 303 
PRO CD  HD2  sing N N 304 
PRO CD  HD3  sing N N 305 
PRO OXT HXT  sing N N 306 
SER N   CA   sing N N 307 
SER N   H    sing N N 308 
SER N   H2   sing N N 309 
SER CA  C    sing N N 310 
SER CA  CB   sing N N 311 
SER CA  HA   sing N N 312 
SER C   O    doub N N 313 
SER C   OXT  sing N N 314 
SER CB  OG   sing N N 315 
SER CB  HB2  sing N N 316 
SER CB  HB3  sing N N 317 
SER OG  HG   sing N N 318 
SER OXT HXT  sing N N 319 
THR N   CA   sing N N 320 
THR N   H    sing N N 321 
THR N   H2   sing N N 322 
THR CA  C    sing N N 323 
THR CA  CB   sing N N 324 
THR CA  HA   sing N N 325 
THR C   O    doub N N 326 
THR C   OXT  sing N N 327 
THR CB  OG1  sing N N 328 
THR CB  CG2  sing N N 329 
THR CB  HB   sing N N 330 
THR OG1 HG1  sing N N 331 
THR CG2 HG21 sing N N 332 
THR CG2 HG22 sing N N 333 
THR CG2 HG23 sing N N 334 
THR OXT HXT  sing N N 335 
TRP N   CA   sing N N 336 
TRP N   H    sing N N 337 
TRP N   H2   sing N N 338 
TRP CA  C    sing N N 339 
TRP CA  CB   sing N N 340 
TRP CA  HA   sing N N 341 
TRP C   O    doub N N 342 
TRP C   OXT  sing N N 343 
TRP CB  CG   sing N N 344 
TRP CB  HB2  sing N N 345 
TRP CB  HB3  sing N N 346 
TRP CG  CD1  doub Y N 347 
TRP CG  CD2  sing Y N 348 
TRP CD1 NE1  sing Y N 349 
TRP CD1 HD1  sing N N 350 
TRP CD2 CE2  doub Y N 351 
TRP CD2 CE3  sing Y N 352 
TRP NE1 CE2  sing Y N 353 
TRP NE1 HE1  sing N N 354 
TRP CE2 CZ2  sing Y N 355 
TRP CE3 CZ3  doub Y N 356 
TRP CE3 HE3  sing N N 357 
TRP CZ2 CH2  doub Y N 358 
TRP CZ2 HZ2  sing N N 359 
TRP CZ3 CH2  sing Y N 360 
TRP CZ3 HZ3  sing N N 361 
TRP CH2 HH2  sing N N 362 
TRP OXT HXT  sing N N 363 
TYR N   CA   sing N N 364 
TYR N   H    sing N N 365 
TYR N   H2   sing N N 366 
TYR CA  C    sing N N 367 
TYR CA  CB   sing N N 368 
TYR CA  HA   sing N N 369 
TYR C   O    doub N N 370 
TYR C   OXT  sing N N 371 
TYR CB  CG   sing N N 372 
TYR CB  HB2  sing N N 373 
TYR CB  HB3  sing N N 374 
TYR CG  CD1  doub Y N 375 
TYR CG  CD2  sing Y N 376 
TYR CD1 CE1  sing Y N 377 
TYR CD1 HD1  sing N N 378 
TYR CD2 CE2  doub Y N 379 
TYR CD2 HD2  sing N N 380 
TYR CE1 CZ   doub Y N 381 
TYR CE1 HE1  sing N N 382 
TYR CE2 CZ   sing Y N 383 
TYR CE2 HE2  sing N N 384 
TYR CZ  OH   sing N N 385 
TYR OH  HH   sing N N 386 
TYR OXT HXT  sing N N 387 
VAL N   CA   sing N N 388 
VAL N   H    sing N N 389 
VAL N   H2   sing N N 390 
VAL CA  C    sing N N 391 
VAL CA  CB   sing N N 392 
VAL CA  HA   sing N N 393 
VAL C   O    doub N N 394 
VAL C   OXT  sing N N 395 
VAL CB  CG1  sing N N 396 
VAL CB  CG2  sing N N 397 
VAL CB  HB   sing N N 398 
VAL CG1 HG11 sing N N 399 
VAL CG1 HG12 sing N N 400 
VAL CG1 HG13 sing N N 401 
VAL CG2 HG21 sing N N 402 
VAL CG2 HG22 sing N N 403 
VAL CG2 HG23 sing N N 404 
VAL OXT HXT  sing N N 405 
# 
_em_3d_crystal_entity.angle_alpha           90 
_em_3d_crystal_entity.angle_beta            100.951 
_em_3d_crystal_entity.angle_gamma           90 
_em_3d_crystal_entity.image_processing_id   1 
_em_3d_crystal_entity.id                    1 
_em_3d_crystal_entity.length_a              44.99 
_em_3d_crystal_entity.length_b              105.70 
_em_3d_crystal_entity.length_c              47.49 
_em_3d_crystal_entity.space_group_name      P21 
_em_3d_crystal_entity.space_group_num       4 
# 
_em_crystal_formation.atmosphere            ? 
_em_crystal_formation.details               
;Crystals were grown by hanging-drop vapor diffusion from drops of 25.7 mg/mL CTX-M-14 mixed 1:1 with crystallization solution (1.4 M potassium phosphate pH 7.9)
;
_em_crystal_formation.id                    1 
_em_crystal_formation.instrument            ? 
_em_crystal_formation.lipid_mixture         ? 
_em_crystal_formation.lipid_protein_ratio   ? 
_em_crystal_formation.specimen_id           1 
_em_crystal_formation.temperature           293 
_em_crystal_formation.time                  ? 
_em_crystal_formation.time_unit             ? 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     NONE 
# 
_em_diffraction_shell.em_diffraction_stats_id   1 
_em_diffraction_shell.fourier_space_coverage    96.1 
_em_diffraction_shell.high_resolution           2.3 
_em_diffraction_shell.id                        1 
_em_diffraction_shell.low_resolution            2.4 
_em_diffraction_shell.multiplicity              4.69 
_em_diffraction_shell.num_structure_factors     2241 
_em_diffraction_shell.phase_residual            33.1 
# 
_em_diffraction_stats.details                          ? 
_em_diffraction_stats.fourier_space_coverage           96.8 
_em_diffraction_stats.high_resolution                  2.3 
_em_diffraction_stats.id                               1 
_em_diffraction_stats.image_processing_id              1 
_em_diffraction_stats.num_intensities_measured         86854 
_em_diffraction_stats.num_structure_factors            18817 
_em_diffraction_stats.overall_phase_error              ? 
_em_diffraction_stats.overall_phase_residual           ? 
_em_diffraction_stats.phase_error_rejection_criteria   NONE 
_em_diffraction_stats.r_merge                          0.268 
_em_diffraction_stats.r_sym                            ? 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          562 
_em_entity_assembly_naturalsource.organism             'Escherichia coli' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          469008 
_em_entity_assembly_recombinant.organism             'Escherichia coli BL21(DE3)' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         0.09 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'DIRECT ELECTRON APOLLO (4k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
_em_software.reference_DOI 
'IMAGE ACQUISITION'             ? 1  ? ? 1 ? ? ? 
MASKING                         ? 2  ? ? ? ? ? ? 
'CTF CORRECTION'                ? 3  1 ? ? ? ? ? 
'LAYERLINE INDEXING'            ? 4  ? ? ? ? ? ? 
'DIFFRACTION INDEXING'          ? 5  ? ? ? ? ? ? 
'MODEL FITTING'                 ? 6  ? 1 ? ? ? ? 
OTHER                           ? 7  ? ? ? ? ? ? 
'MOLECULAR REPLACEMENT'         ? 8  1 ? ? ? ? ? 
'LATTICE DISTORTION CORRECTION' ? 9  1 ? ? ? ? ? 
'SYMMETRY DETERMINATION'        ? 10 1 ? ? ? ? ? 
'CRYSTALLOGRAPHY MERGING'       ? 11 1 ? ? ? ? ? 
RECONSTRUCTION                  ? 12 1 ? ? ? ? ? 
'MODEL REFINEMENT'              ? 13 ? 1 ? ? ? ? 
'PARTICLE SELECTION'            ? 14 1 1 1 ? ? ? 
'VOLUME SELECTION'              ? 15 1 1 1 ? ? ? 
CLASSIFICATION                  ? 16 1 1 1 ? ? ? 
'INITIAL EULER ASSIGNMENT'      ? 17 1 1 1 ? ? ? 
'FINAL EULER ASSIGNMENT'        ? 18 1 1 1 ? ? ? 
'SERIES ALIGNMENT'              ? 19 1 1 1 ? ? ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 
;Crystals were grown by hanging-drop vapor diffusion from drops of 25.7 mg/mL CTX-M-14 mixed 1:1 with crystallization solution (1.4 M potassium phosphate pH 7.9)
;
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Howard Hughes Medical Institute (HHMI)'           'United States' HHMI-EPI          1 
'National Science Foundation (NSF, United States)' 'United States' DMR-1548924       2 
'Department of Energy (DOE, United States)'        'United States' DE-FC02-02ER63421 3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1YLT 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9ORL 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.022227 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004300 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009461 
_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]   0.021448 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
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   . SER A 1 3   ? -26.277 -9.340  -35.431 1.00 45.46 ? 27  SER A N   1 
ATOM   2    C CA  . SER A 1 3   ? -27.192 -8.393  -34.804 1.00 49.58 ? 27  SER A CA  1 
ATOM   3    C C   . SER A 1 3   ? -26.681 -6.961  -34.955 1.00 49.34 ? 27  SER A C   1 
ATOM   4    O O   . SER A 1 3   ? -25.543 -6.744  -35.376 1.00 45.50 ? 27  SER A O   1 
ATOM   5    C CB  . SER A 1 3   ? -27.379 -8.735  -33.322 1.00 46.88 ? 27  SER A CB  1 
ATOM   6    O OG  . SER A 1 3   ? -27.871 -7.622  -32.593 1.00 46.87 ? 27  SER A OG  1 
ATOM   7    N N   . ALA A 1 4   ? -27.529 -5.988  -34.608 1.00 46.17 ? 28  ALA A N   1 
ATOM   8    C CA  . ALA A 1 4   ? -27.119 -4.588  -34.684 1.00 36.19 ? 28  ALA A CA  1 
ATOM   9    C C   . ALA A 1 4   ? -25.978 -4.303  -33.717 1.00 37.06 ? 28  ALA A C   1 
ATOM   10   O O   . ALA A 1 4   ? -25.038 -3.568  -34.046 1.00 41.39 ? 28  ALA A O   1 
ATOM   11   C CB  . ALA A 1 4   ? -28.312 -3.675  -34.400 1.00 37.25 ? 28  ALA A CB  1 
ATOM   12   N N   . VAL A 1 5   ? -26.036 -4.890  -32.520 1.00 34.18 ? 29  VAL A N   1 
ATOM   13   C CA  . VAL A 1 5   ? -24.964 -4.723  -31.543 1.00 29.57 ? 29  VAL A CA  1 
ATOM   14   C C   . VAL A 1 5   ? -23.675 -5.345  -32.071 1.00 31.58 ? 29  VAL A C   1 
ATOM   15   O O   . VAL A 1 5   ? -22.582 -4.787  -31.904 1.00 30.43 ? 29  VAL A O   1 
ATOM   16   C CB  . VAL A 1 5   ? -25.384 -5.294  -30.171 1.00 33.11 ? 29  VAL A CB  1 
ATOM   17   C CG1 . VAL A 1 5   ? -25.727 -6.777  -30.259 1.00 43.94 ? 29  VAL A CG1 1 
ATOM   18   C CG2 . VAL A 1 5   ? -24.307 -5.041  -29.129 1.00 31.34 ? 29  VAL A CG2 1 
ATOM   19   N N   . GLN A 1 6   ? -23.780 -6.513  -32.711 1.00 37.07 ? 30  GLN A N   1 
ATOM   20   C CA  . GLN A 1 6   ? -22.602 -7.160  -33.278 1.00 37.70 ? 30  GLN A CA  1 
ATOM   21   C C   . GLN A 1 6   ? -21.987 -6.292  -34.367 1.00 30.15 ? 30  GLN A C   1 
ATOM   22   O O   . GLN A 1 6   ? -20.768 -6.078  -34.398 1.00 23.96 ? 30  GLN A O   1 
ATOM   23   C CB  . GLN A 1 6   ? -22.985 -8.525  -33.862 1.00 37.21 ? 30  GLN A CB  1 
ATOM   24   C CG  . GLN A 1 6   ? -23.343 -9.599  -32.858 1.00 35.71 ? 30  GLN A CG  1 
ATOM   25   C CD  . GLN A 1 6   ? -22.368 -9.650  -31.711 1.00 34.95 ? 30  GLN A CD  1 
ATOM   26   O OE1 . GLN A 1 6   ? -22.741 -9.468  -30.554 1.00 34.93 ? 30  GLN A OE1 1 
ATOM   27   N NE2 . GLN A 1 6   ? -21.099 -9.883  -32.029 1.00 39.65 ? 30  GLN A NE2 1 
ATOM   28   N N   . GLN A 1 7   ? -22.824 -5.778  -35.268 1.00 19.73 ? 31  GLN A N   1 
ATOM   29   C CA  . GLN A 1 7   ? -22.312 -4.954  -36.353 1.00 32.53 ? 31  GLN A CA  1 
ATOM   30   C C   . GLN A 1 7   ? -21.672 -3.676  -35.814 1.00 29.81 ? 31  GLN A C   1 
ATOM   31   O O   . GLN A 1 7   ? -20.620 -3.242  -36.306 1.00 26.05 ? 31  GLN A O   1 
ATOM   32   C CB  . GLN A 1 7   ? -23.435 -4.657  -37.354 1.00 28.83 ? 31  GLN A CB  1 
ATOM   33   C CG  . GLN A 1 7   ? -24.155 -3.322  -37.203 1.00 41.76 ? 31  GLN A CG  1 
ATOM   34   C CD  . GLN A 1 7   ? -23.488 -2.212  -38.009 1.00 49.60 ? 31  GLN A CD  1 
ATOM   35   O OE1 . GLN A 1 7   ? -22.869 -2.470  -39.044 1.00 32.10 ? 31  GLN A OE1 1 
ATOM   36   N NE2 . GLN A 1 7   ? -23.615 -0.973  -37.539 1.00 37.58 ? 31  GLN A NE2 1 
ATOM   37   N N   . LYS A 1 8   ? -22.255 -3.088  -34.764 1.00 26.70 ? 32  LYS A N   1 
ATOM   38   C CA  . LYS A 1 8   ? -21.679 -1.854  -34.244 1.00 24.25 ? 32  LYS A CA  1 
ATOM   39   C C   . LYS A 1 8   ? -20.377 -2.110  -33.494 1.00 24.66 ? 32  LYS A C   1 
ATOM   40   O O   . LYS A 1 8   ? -19.443 -1.306  -33.591 1.00 26.98 ? 32  LYS A O   1 
ATOM   41   C CB  . LYS A 1 8   ? -22.683 -1.062  -33.409 1.00 31.15 ? 32  LYS A CB  1 
ATOM   42   C CG  . LYS A 1 8   ? -23.766 -0.531  -34.323 1.00 35.52 ? 32  LYS A CG  1 
ATOM   43   C CD  . LYS A 1 8   ? -24.795 0.334   -33.663 1.00 40.63 ? 32  LYS A CD  1 
ATOM   44   C CE  . LYS A 1 8   ? -24.383 1.774   -34.068 1.00 69.26 ? 32  LYS A CE  1 
ATOM   45   N NZ  . LYS A 1 8   ? -25.205 2.905   -33.548 1.00 51.17 ? 32  LYS A NZ  1 
ATOM   46   N N   . LEU A 1 9   ? -20.296 -3.183  -32.701 1.00 30.10 ? 33  LEU A N   1 
ATOM   47   C CA  . LEU A 1 9   ? -19.017 -3.460  -32.054 1.00 19.81 ? 33  LEU A CA  1 
ATOM   48   C C   . LEU A 1 9   ? -17.951 -3.785  -33.090 1.00 17.81 ? 33  LEU A C   1 
ATOM   49   O O   . LEU A 1 9   ? -16.785 -3.400  -32.924 1.00 19.21 ? 33  LEU A O   1 
ATOM   50   C CB  . LEU A 1 9   ? -19.134 -4.604  -31.047 1.00 20.96 ? 33  LEU A CB  1 
ATOM   51   C CG  . LEU A 1 9   ? -20.023 -4.359  -29.830 1.00 33.09 ? 33  LEU A CG  1 
ATOM   52   C CD1 . LEU A 1 9   ? -20.307 -5.669  -29.100 1.00 21.01 ? 33  LEU A CD1 1 
ATOM   53   C CD2 . LEU A 1 9   ? -19.390 -3.330  -28.903 1.00 20.25 ? 33  LEU A CD2 1 
ATOM   54   N N   . ALA A 1 10  ? -18.332 -4.449  -34.186 1.00 12.56 ? 34  ALA A N   1 
ATOM   55   C CA  . ALA A 1 10  ? -17.360 -4.710  -35.238 1.00 20.16 ? 34  ALA A CA  1 
ATOM   56   C C   . ALA A 1 10  ? -16.894 -3.409  -35.881 1.00 23.54 ? 34  ALA A C   1 
ATOM   57   O O   . ALA A 1 10  ? -15.708 -3.251  -36.188 1.00 17.66 ? 34  ALA A O   1 
ATOM   58   C CB  . ALA A 1 10  ? -17.958 -5.646  -36.289 1.00 13.19 ? 34  ALA A CB  1 
ATOM   59   N N   . ALA A 1 11  ? -17.813 -2.454  -36.063 1.00 19.35 ? 35  ALA A N   1 
ATOM   60   C CA  . ALA A 1 11  ? -17.445 -1.164  -36.641 1.00 22.76 ? 35  ALA A CA  1 
ATOM   61   C C   . ALA A 1 11  ? -16.562 -0.353  -35.699 1.00 21.07 ? 35  ALA A C   1 
ATOM   62   O O   . ALA A 1 11  ? -15.602 0.293   -36.140 1.00 22.16 ? 35  ALA A O   1 
ATOM   63   C CB  . ALA A 1 11  ? -18.704 -0.376  -37.006 1.00 18.05 ? 35  ALA A CB  1 
ATOM   64   N N   . LEU A 1 12  ? -16.857 -0.390  -34.398 1.00 15.55 ? 36  LEU A N   1 
ATOM   65   C CA  . LEU A 1 12  ? -15.988 0.260   -33.423 1.00 19.26 ? 36  LEU A CA  1 
ATOM   66   C C   . LEU A 1 12  ? -14.582 -0.321  -33.490 1.00 21.95 ? 36  LEU A C   1 
ATOM   67   O O   . LEU A 1 12  ? -13.586 0.418   -33.542 1.00 15.97 ? 36  LEU A O   1 
ATOM   68   C CB  . LEU A 1 12  ? -16.583 0.108   -32.020 1.00 10.27 ? 36  LEU A CB  1 
ATOM   69   C CG  . LEU A 1 12  ? -15.691 0.458   -30.828 1.00 20.33 ? 36  LEU A CG  1 
ATOM   70   C CD1 . LEU A 1 12  ? -15.317 1.930   -30.897 1.00 10.83 ? 36  LEU A CD1 1 
ATOM   71   C CD2 . LEU A 1 12  ? -16.384 0.134   -29.504 1.00 12.27 ? 36  LEU A CD2 1 
ATOM   72   N N   . GLU A 1 13  ? -14.483 -1.654  -33.492 1.00 15.48 ? 37  GLU A N   1 
ATOM   73   C CA  . GLU A 1 13  ? -13.174 -2.289  -33.554 1.00 13.15 ? 37  GLU A CA  1 
ATOM   74   C C   . GLU A 1 13  ? -12.445 -1.910  -34.836 1.00 14.83 ? 37  GLU A C   1 
ATOM   75   O O   . GLU A 1 13  ? -11.239 -1.633  -34.819 1.00 19.71 ? 37  GLU A O   1 
ATOM   76   C CB  . GLU A 1 13  ? -13.340 -3.801  -33.471 1.00 19.51 ? 37  GLU A CB  1 
ATOM   77   C CG  . GLU A 1 13  ? -12.043 -4.564  -33.566 1.00 17.60 ? 37  GLU A CG  1 
ATOM   78   C CD  . GLU A 1 13  ? -12.275 -6.056  -33.578 1.00 19.66 ? 37  GLU A CD  1 
ATOM   79   O OE1 . GLU A 1 13  ? -12.940 -6.545  -34.514 1.00 18.76 ? 37  GLU A OE1 1 
ATOM   80   O OE2 . GLU A 1 13  ? -11.781 -6.740  -32.660 1.00 22.42 ? 37  GLU A OE2 1 
ATOM   81   N N   . LYS A 1 14  ? -13.161 -1.930  -35.963 1.00 14.35 ? 38  LYS A N   1 
ATOM   82   C CA  . LYS A 1 14  ? -12.556 -1.598  -37.247 1.00 22.48 ? 38  LYS A CA  1 
ATOM   83   C C   . LYS A 1 14  ? -12.015 -0.181  -37.237 1.00 21.22 ? 38  LYS A C   1 
ATOM   84   O O   . LYS A 1 14  ? -10.926 0.084   -37.760 1.00 29.41 ? 38  LYS A O   1 
ATOM   85   C CB  . LYS A 1 14  ? -13.560 -1.785  -38.382 1.00 23.55 ? 38  LYS A CB  1 
ATOM   86   C CG  . LYS A 1 14  ? -13.014 -1.372  -39.745 1.00 29.32 ? 38  LYS A CG  1 
ATOM   87   C CD  . LYS A 1 14  ? -13.897 -1.870  -40.878 1.00 42.43 ? 38  LYS A CD  1 
ATOM   88   C CE  . LYS A 1 14  ? -15.348 -2.033  -40.430 1.00 58.11 ? 38  LYS A CE  1 
ATOM   89   N NZ  . LYS A 1 14  ? -16.070 -0.727  -40.373 1.00 38.02 ? 38  LYS A NZ  1 
ATOM   90   N N   . SER A 1 15  ? -12.747 0.742   -36.610 1.00 20.47 ? 39  SER A N   1 
ATOM   91   C CA  . SER A 1 15  ? -12.279 2.115   -36.575 1.00 20.77 ? 39  SER A CA  1 
ATOM   92   C C   . SER A 1 15  ? -11.204 2.331   -35.533 1.00 22.94 ? 39  SER A C   1 
ATOM   93   O O   . SER A 1 15  ? -10.541 3.373   -35.551 1.00 35.12 ? 39  SER A O   1 
ATOM   94   C CB  . SER A 1 15  ? -13.451 3.046   -36.268 1.00 19.66 ? 39  SER A CB  1 
ATOM   95   O OG  . SER A 1 15  ? -13.835 2.933   -34.910 1.00 22.14 ? 39  SER A OG  1 
ATOM   96   N N   . SER A 1 16  ? -10.991 1.361   -34.660 1.00 28.30 ? 40  SER A N   1 
ATOM   97   C CA  . SER A 1 16  ? -10.055 1.521   -33.564 1.00 26.75 ? 40  SER A CA  1 
ATOM   98   C C   . SER A 1 16  ? -8.641  1.149   -33.984 1.00 23.45 ? 40  SER A C   1 
ATOM   99   O O   . SER A 1 16  ? -7.677  1.595   -33.351 1.00 14.84 ? 40  SER A O   1 
ATOM   100  C CB  . SER A 1 16  ? -10.512 0.690   -32.365 1.00 20.69 ? 40  SER A CB  1 
ATOM   101  O OG  . SER A 1 16  ? -10.183 -0.672  -32.555 1.00 24.77 ? 40  SER A OG  1 
ATOM   102  N N   . GLY A 1 17  ? -8.506  0.341   -35.038 1.00 24.65 ? 41  GLY A N   1 
ATOM   103  C CA  . GLY A 1 17  ? -7.214  -0.158  -35.450 1.00 21.22 ? 41  GLY A CA  1 
ATOM   104  C C   . GLY A 1 17  ? -6.653  -1.229  -34.553 1.00 27.03 ? 41  GLY A C   1 
ATOM   105  O O   . GLY A 1 17  ? -5.486  -1.598  -34.707 1.00 28.42 ? 41  GLY A O   1 
ATOM   106  N N   . GLY A 1 18  ? -7.468  -1.791  -33.667 1.00 20.67 ? 42  GLY A N   1 
ATOM   107  C CA  . GLY A 1 18  ? -7.018  -2.870  -32.818 1.00 14.44 ? 42  GLY A CA  1 
ATOM   108  C C   . GLY A 1 18  ? -8.006  -4.007  -32.716 1.00 14.13 ? 42  GLY A C   1 
ATOM   109  O O   . GLY A 1 18  ? -8.889  -4.145  -33.566 1.00 26.17 ? 42  GLY A O   1 
ATOM   110  N N   . ARG A 1 19  ? -7.861  -4.833  -31.689 1.00 12.71 ? 43  ARG A N   1 
ATOM   111  C CA  . ARG A 1 19  ? -8.713  -5.989  -31.479 1.00 18.19 ? 43  ARG A CA  1 
ATOM   112  C C   . ARG A 1 19  ? -9.502  -5.829  -30.187 1.00 14.34 ? 43  ARG A C   1 
ATOM   113  O O   . ARG A 1 19  ? -8.922  -5.611  -29.114 1.00 11.11 ? 43  ARG A O   1 
ATOM   114  C CB  . ARG A 1 19  ? -7.850  -7.252  -31.427 1.00 12.95 ? 43  ARG A CB  1 
ATOM   115  C CG  . ARG A 1 19  ? -8.614  -8.538  -31.241 1.00 9.51  ? 43  ARG A CG  1 
ATOM   116  C CD  . ARG A 1 19  ? -7.706  -9.761  -31.428 1.00 10.40 ? 43  ARG A CD  1 
ATOM   117  N NE  . ARG A 1 19  ? -6.671  -9.855  -30.407 1.00 6.77  ? 43  ARG A NE  1 
ATOM   118  C CZ  . ARG A 1 19  ? -6.753  -10.655 -29.352 1.00 14.43 ? 43  ARG A CZ  1 
ATOM   119  N NH1 . ARG A 1 19  ? -7.787  -11.467 -29.183 1.00 14.24 ? 43  ARG A NH1 1 
ATOM   120  N NH2 . ARG A 1 19  ? -5.766  -10.660 -28.459 1.00 5.08  ? 43  ARG A NH2 1 
ATOM   121  N N   . LEU A 1 20  ? -10.824 -5.919  -30.312 1.00 13.55 ? 44  LEU A N   1 
ATOM   122  C CA  . LEU A 1 20  ? -11.776 -5.670  -29.240 1.00 11.46 ? 44  LEU A CA  1 
ATOM   123  C C   . LEU A 1 20  ? -12.476 -6.968  -28.872 1.00 14.66 ? 44  LEU A C   1 
ATOM   124  O O   . LEU A 1 20  ? -12.900 -7.720  -29.756 1.00 11.61 ? 44  LEU A O   1 
ATOM   125  C CB  . LEU A 1 20  ? -12.813 -4.624  -29.657 1.00 14.22 ? 44  LEU A CB  1 
ATOM   126  C CG  . LEU A 1 20  ? -13.922 -4.303  -28.644 1.00 16.62 ? 44  LEU A CG  1 
ATOM   127  C CD1 . LEU A 1 20  ? -13.381 -3.610  -27.400 1.00 7.32  ? 44  LEU A CD1 1 
ATOM   128  C CD2 . LEU A 1 20  ? -15.037 -3.475  -29.293 1.00 23.17 ? 44  LEU A CD2 1 
ATOM   129  N N   . GLY A 1 21  ? -12.601 -7.222  -27.575 1.00 14.89 ? 45  GLY A N   1 
ATOM   130  C CA  . GLY A 1 21  ? -13.358 -8.349  -27.077 1.00 10.31 ? 45  GLY A CA  1 
ATOM   131  C C   . GLY A 1 21  ? -14.342 -7.845  -26.046 1.00 10.97 ? 45  GLY A C   1 
ATOM   132  O O   . GLY A 1 21  ? -13.972 -7.091  -25.148 1.00 13.86 ? 45  GLY A O   1 
ATOM   133  N N   . VAL A 1 22  ? -15.598 -8.244  -26.157 1.00 17.87 ? 46  VAL A N   1 
ATOM   134  C CA  . VAL A 1 22  ? -16.655 -7.767  -25.277 1.00 13.82 ? 46  VAL A CA  1 
ATOM   135  C C   . VAL A 1 22  ? -17.467 -8.975  -24.857 1.00 8.88  ? 46  VAL A C   1 
ATOM   136  O O   . VAL A 1 22  ? -17.796 -9.830  -25.685 1.00 11.80 ? 46  VAL A O   1 
ATOM   137  C CB  . VAL A 1 22  ? -17.555 -6.708  -25.953 1.00 19.38 ? 46  VAL A CB  1 
ATOM   138  C CG1 . VAL A 1 22  ? -18.616 -6.212  -24.974 1.00 23.14 ? 46  VAL A CG1 1 
ATOM   139  C CG2 . VAL A 1 22  ? -16.720 -5.538  -26.472 1.00 7.80  ? 46  VAL A CG2 1 
ATOM   140  N N   . ALA A 1 23  ? -17.800 -9.041  -23.573 1.00 13.44 ? 47  ALA A N   1 
ATOM   141  C CA  . ALA A 1 23  ? -18.797 -9.989  -23.100 1.00 6.40  ? 47  ALA A CA  1 
ATOM   142  C C   . ALA A 1 23  ? -19.726 -9.314  -22.111 1.00 9.92  ? 47  ALA A C   1 
ATOM   143  O O   . ALA A 1 23  ? -19.278 -8.779  -21.096 1.00 12.10 ? 47  ALA A O   1 
ATOM   144  C CB  . ALA A 1 23  ? -18.139 -11.202 -22.448 1.00 6.73  ? 47  ALA A CB  1 
ATOM   145  N N   . LEU A 1 24  ? -21.014 -9.349  -22.422 1.00 18.24 ? 48  LEU A N   1 
ATOM   146  C CA  . LEU A 1 24  ? -22.076 -8.891  -21.549 1.00 11.92 ? 48  LEU A CA  1 
ATOM   147  C C   . LEU A 1 24  ? -22.869 -10.103 -21.092 1.00 16.79 ? 48  LEU A C   1 
ATOM   148  O O   . LEU A 1 24  ? -23.260 -10.934 -21.921 1.00 19.57 ? 48  LEU A O   1 
ATOM   149  C CB  . LEU A 1 24  ? -23.007 -7.931  -22.289 1.00 23.63 ? 48  LEU A CB  1 
ATOM   150  C CG  . LEU A 1 24  ? -24.336 -7.646  -21.582 1.00 26.26 ? 48  LEU A CG  1 
ATOM   151  C CD1 . LEU A 1 24  ? -24.138 -6.657  -20.433 1.00 20.73 ? 48  LEU A CD1 1 
ATOM   152  C CD2 . LEU A 1 24  ? -25.395 -7.160  -22.557 1.00 22.82 ? 48  LEU A CD2 1 
ATOM   153  N N   . ILE A 1 25  ? -23.160 -10.156 -19.796 1.00 16.86 ? 49  ILE A N   1 
ATOM   154  C CA  . ILE A 1 25  ? -24.172 -11.035 -19.226 1.00 20.47 ? 49  ILE A CA  1 
ATOM   155  C C   . ILE A 1 25  ? -25.225 -10.154 -18.569 1.00 22.78 ? 49  ILE A C   1 
ATOM   156  O O   . ILE A 1 25  ? -24.904 -9.343  -17.693 1.00 22.22 ? 49  ILE A O   1 
ATOM   157  C CB  . ILE A 1 25  ? -23.581 -12.019 -18.200 1.00 20.48 ? 49  ILE A CB  1 
ATOM   158  C CG1 . ILE A 1 25  ? -22.515 -12.918 -18.835 1.00 18.33 ? 49  ILE A CG1 1 
ATOM   159  C CG2 . ILE A 1 25  ? -24.681 -12.843 -17.556 1.00 12.17 ? 49  ILE A CG2 1 
ATOM   160  C CD1 . ILE A 1 25  ? -21.684 -13.682 -17.810 1.00 15.75 ? 49  ILE A CD1 1 
ATOM   161  N N   . ASP A 1 26  ? -26.471 -10.298 -19.000 1.00 19.32 ? 50  ASP A N   1 
ATOM   162  C CA  . ASP A 1 26  ? -27.605 -9.638  -18.377 1.00 22.01 ? 50  ASP A CA  1 
ATOM   163  C C   . ASP A 1 26  ? -28.229 -10.669 -17.450 1.00 26.93 ? 50  ASP A C   1 
ATOM   164  O O   . ASP A 1 26  ? -28.841 -11.643 -17.922 1.00 24.25 ? 50  ASP A O   1 
ATOM   165  C CB  . ASP A 1 26  ? -28.604 -9.178  -19.436 1.00 27.96 ? 50  ASP A CB  1 
ATOM   166  C CG  . ASP A 1 26  ? -29.662 -8.250  -18.881 1.00 48.79 ? 50  ASP A CG  1 
ATOM   167  O OD1 . ASP A 1 26  ? -29.620 -7.042  -19.188 1.00 51.59 ? 50  ASP A OD1 1 
ATOM   168  O OD2 . ASP A 1 26  ? -30.539 -8.725  -18.133 1.00 40.38 ? 50  ASP A OD2 1 
ATOM   169  N N   . THR A 1 27  ? -28.022 -10.486 -16.137 1.00 22.71 ? 51  THR A N   1 
ATOM   170  C CA  . THR A 1 27  ? -28.545 -11.421 -15.147 1.00 33.62 ? 51  THR A CA  1 
ATOM   171  C C   . THR A 1 27  ? -30.039 -11.256 -14.876 1.00 21.94 ? 51  THR A C   1 
ATOM   172  O O   . THR A 1 27  ? -30.597 -12.052 -14.112 1.00 29.15 ? 51  THR A O   1 
ATOM   173  C CB  . THR A 1 27  ? -27.774 -11.277 -13.828 1.00 23.40 ? 51  THR A CB  1 
ATOM   174  O OG1 . THR A 1 27  ? -28.116 -10.035 -13.198 1.00 19.33 ? 51  THR A OG1 1 
ATOM   175  C CG2 . THR A 1 27  ? -26.274 -11.308 -14.081 1.00 21.10 ? 51  THR A CG2 1 
ATOM   176  N N   . ALA A 1 28  ? -30.706 -10.259 -15.464 1.00 24.01 ? 52  ALA A N   1 
ATOM   177  C CA  . ALA A 1 28  ? -32.165 -10.230 -15.398 1.00 33.81 ? 52  ALA A CA  1 
ATOM   178  C C   . ALA A 1 28  ? -32.758 -11.439 -16.097 1.00 35.99 ? 52  ALA A C   1 
ATOM   179  O O   . ALA A 1 28  ? -33.780 -11.983 -15.664 1.00 46.68 ? 52  ALA A O   1 
ATOM   180  C CB  . ALA A 1 28  ? -32.713 -8.942  -16.003 1.00 22.85 ? 52  ALA A CB  1 
ATOM   181  N N   . ASP A 1 29  ? -32.105 -11.876 -17.167 1.00 28.11 ? 53  ASP A N   1 
ATOM   182  C CA  . ASP A 1 29  ? -32.565 -12.975 -17.998 1.00 25.42 ? 53  ASP A CA  1 
ATOM   183  C C   . ASP A 1 29  ? -31.410 -13.846 -18.482 1.00 34.76 ? 53  ASP A C   1 
ATOM   184  O O   . ASP A 1 29  ? -31.634 -14.722 -19.327 1.00 31.70 ? 53  ASP A O   1 
ATOM   185  C CB  . ASP A 1 29  ? -33.400 -12.440 -19.176 1.00 27.32 ? 53  ASP A CB  1 
ATOM   186  C CG  . ASP A 1 29  ? -32.629 -11.470 -20.064 1.00 42.77 ? 53  ASP A CG  1 
ATOM   187  O OD1 . ASP A 1 29  ? -31.413 -11.280 -19.850 1.00 45.52 ? 53  ASP A OD1 1 
ATOM   188  O OD2 . ASP A 1 29  ? -33.248 -10.882 -20.978 1.00 39.93 ? 53  ASP A OD2 1 
ATOM   189  N N   . ASN A 1 30  ? -30.181 -13.612 -18.001 1.00 39.45 ? 54  ASN A N   1 
ATOM   190  C CA  . ASN A 1 30  ? -29.001 -14.363 -18.430 1.00 21.87 ? 54  ASN A CA  1 
ATOM   191  C C   . ASN A 1 30  ? -28.715 -14.227 -19.913 1.00 21.52 ? 54  ASN A C   1 
ATOM   192  O O   . ASN A 1 30  ? -28.058 -15.094 -20.496 1.00 27.84 ? 54  ASN A O   1 
ATOM   193  C CB  . ASN A 1 30  ? -29.092 -15.846 -18.055 1.00 28.14 ? 54  ASN A CB  1 
ATOM   194  C CG  . ASN A 1 30  ? -29.305 -16.056 -16.575 1.00 39.25 ? 54  ASN A CG  1 
ATOM   195  O OD1 . ASN A 1 30  ? -28.388 -15.862 -15.776 1.00 36.35 ? 54  ASN A OD1 1 
ATOM   196  N ND2 . ASN A 1 30  ? -30.510 -16.471 -16.199 1.00 55.94 ? 54  ASN A ND2 1 
ATOM   197  N N   . THR A 1 31  ? -29.187 -13.171 -20.564 1.00 24.02 ? 55  THR A N   1 
ATOM   198  C CA  . THR A 1 31  ? -28.795 -13.111 -21.966 1.00 25.97 ? 55  THR A CA  1 
ATOM   199  C C   . THR A 1 31  ? -27.355 -12.620 -22.096 1.00 23.88 ? 55  THR A C   1 
ATOM   200  O O   . THR A 1 31  ? -26.791 -12.014 -21.188 1.00 20.72 ? 55  THR A O   1 
ATOM   201  C CB  . THR A 1 31  ? -29.746 -12.212 -22.763 1.00 32.17 ? 55  THR A CB  1 
ATOM   202  O OG1 . THR A 1 31  ? -29.852 -10.932 -22.130 1.00 27.85 ? 55  THR A OG1 1 
ATOM   203  C CG2 . THR A 1 31  ? -31.127 -12.851 -22.859 1.00 29.77 ? 55  THR A CG2 1 
ATOM   204  N N   . GLN A 1 32  ? -26.748 -12.922 -23.239 1.00 18.82 ? 56  GLN A N   1 
ATOM   205  C CA  . GLN A 1 32  ? -25.339 -12.628 -23.464 1.00 20.69 ? 56  GLN A CA  1 
ATOM   206  C C   . GLN A 1 32  ? -25.136 -11.841 -24.750 1.00 19.08 ? 56  GLN A C   1 
ATOM   207  O O   . GLN A 1 32  ? -25.777 -12.128 -25.766 1.00 24.66 ? 56  GLN A O   1 
ATOM   208  C CB  . GLN A 1 32  ? -24.587 -13.956 -23.546 1.00 20.11 ? 56  GLN A CB  1 
ATOM   209  C CG  . GLN A 1 32  ? -24.390 -14.646 -22.207 1.00 25.76 ? 56  GLN A CG  1 
ATOM   210  C CD  . GLN A 1 32  ? -23.368 -15.771 -22.270 1.00 27.83 ? 56  GLN A CD  1 
ATOM   211  O OE1 . GLN A 1 32  ? -22.259 -15.602 -22.778 1.00 19.87 ? 56  GLN A OE1 1 
ATOM   212  N NE2 . GLN A 1 32  ? -23.753 -16.939 -21.768 1.00 28.03 ? 56  GLN A NE2 1 
ATOM   213  N N   . VAL A 1 33  ? -24.263 -10.842 -24.716 1.00 15.89 ? 57  VAL A N   1 
ATOM   214  C CA  . VAL A 1 33  ? -23.719 -10.272 -25.950 1.00 19.35 ? 57  VAL A CA  1 
ATOM   215  C C   . VAL A 1 33  ? -22.221 -10.534 -26.003 1.00 16.37 ? 57  VAL A C   1 
ATOM   216  O O   . VAL A 1 33  ? -21.492 -10.149 -25.084 1.00 13.27 ? 57  VAL A O   1 
ATOM   217  C CB  . VAL A 1 33  ? -24.008 -8.765  -26.068 1.00 26.56 ? 57  VAL A CB  1 
ATOM   218  C CG1 . VAL A 1 33  ? -23.308 -8.181  -27.295 1.00 22.00 ? 57  VAL A CG1 1 
ATOM   219  C CG2 . VAL A 1 33  ? -25.509 -8.516  -26.154 1.00 22.28 ? 57  VAL A CG2 1 
ATOM   220  N N   . LEU A 1 34  ? -21.756 -11.167 -27.078 1.00 19.03 ? 59  LEU A N   1 
ATOM   221  C CA  . LEU A 1 34  ? -20.344 -11.493 -27.227 1.00 10.61 ? 59  LEU A CA  1 
ATOM   222  C C   . LEU A 1 34  ? -19.779 -10.906 -28.509 1.00 14.90 ? 59  LEU A C   1 
ATOM   223  O O   . LEU A 1 34  ? -20.415 -10.957 -29.566 1.00 16.10 ? 59  LEU A O   1 
ATOM   224  C CB  . LEU A 1 34  ? -20.055 -13.003 -27.228 1.00 15.15 ? 59  LEU A CB  1 
ATOM   225  C CG  . LEU A 1 34  ? -20.391 -13.989 -26.104 1.00 21.18 ? 59  LEU A CG  1 
ATOM   226  C CD1 . LEU A 1 34  ? -19.828 -13.490 -24.773 1.00 16.88 ? 59  LEU A CD1 1 
ATOM   227  C CD2 . LEU A 1 34  ? -21.879 -14.266 -26.016 1.00 28.81 ? 59  LEU A CD2 1 
ATOM   228  N N   . TYR A 1 35  ? -18.587 -10.333 -28.408 1.00 17.25 ? 60  TYR A N   1 
ATOM   229  C CA  . TYR A 1 35  ? -17.817 -9.948  -29.578 1.00 16.24 ? 60  TYR A CA  1 
ATOM   230  C C   . TYR A 1 35  ? -16.398 -10.432 -29.329 1.00 14.92 ? 60  TYR A C   1 
ATOM   231  O O   . TYR A 1 35  ? -15.748 -9.963  -28.391 1.00 13.96 ? 60  TYR A O   1 
ATOM   232  C CB  . TYR A 1 35  ? -17.852 -8.441  -29.833 1.00 17.24 ? 60  TYR A CB  1 
ATOM   233  C CG  . TYR A 1 35  ? -17.218 -8.099  -31.154 1.00 13.98 ? 60  TYR A CG  1 
ATOM   234  C CD1 . TYR A 1 35  ? -17.933 -8.250  -32.332 1.00 12.79 ? 60  TYR A CD1 1 
ATOM   235  C CD2 . TYR A 1 35  ? -15.902 -7.667  -31.232 1.00 18.38 ? 60  TYR A CD2 1 
ATOM   236  C CE1 . TYR A 1 35  ? -17.364 -7.961  -33.550 1.00 26.36 ? 60  TYR A CE1 1 
ATOM   237  C CE2 . TYR A 1 35  ? -15.320 -7.373  -32.452 1.00 19.92 ? 60  TYR A CE2 1 
ATOM   238  C CZ  . TYR A 1 35  ? -16.058 -7.522  -33.609 1.00 19.77 ? 60  TYR A CZ  1 
ATOM   239  O OH  . TYR A 1 35  ? -15.493 -7.239  -34.831 1.00 23.37 ? 60  TYR A OH  1 
ATOM   240  N N   . ARG A 1 36  ? -15.920 -11.366 -30.149 1.00 10.10 ? 61  ARG A N   1 
ATOM   241  C CA  . ARG A 1 36  ? -14.655 -12.058 -29.876 1.00 16.14 ? 61  ARG A CA  1 
ATOM   242  C C   . ARG A 1 36  ? -14.629 -12.606 -28.451 1.00 11.71 ? 61  ARG A C   1 
ATOM   243  O O   . ARG A 1 36  ? -13.599 -12.594 -27.772 1.00 12.65 ? 61  ARG A O   1 
ATOM   244  C CB  . ARG A 1 36  ? -13.470 -11.119 -30.107 1.00 13.66 ? 61  ARG A CB  1 
ATOM   245  C CG  . ARG A 1 36  ? -13.382 -10.575 -31.511 1.00 12.72 ? 61  ARG A CG  1 
ATOM   246  C CD  . ARG A 1 36  ? -12.022 -9.982  -31.801 1.00 14.72 ? 61  ARG A CD  1 
ATOM   247  N NE  . ARG A 1 36  ? -12.073 -9.220  -33.042 1.00 20.96 ? 61  ARG A NE  1 
ATOM   248  C CZ  . ARG A 1 36  ? -12.073 -9.759  -34.254 1.00 25.91 ? 61  ARG A CZ  1 
ATOM   249  N NH1 . ARG A 1 36  ? -11.922 -11.063 -34.432 1.00 11.05 ? 61  ARG A NH1 1 
ATOM   250  N NH2 . ARG A 1 36  ? -12.204 -8.966  -35.315 1.00 11.37 ? 61  ARG A NH2 1 
ATOM   251  N N   . GLY A 1 37  ? -15.769 -13.131 -28.004 1.00 12.88 ? 62  GLY A N   1 
ATOM   252  C CA  . GLY A 1 37  ? -15.913 -13.530 -26.615 1.00 9.28  ? 62  GLY A CA  1 
ATOM   253  C C   . GLY A 1 37  ? -15.055 -14.707 -26.213 1.00 13.63 ? 62  GLY A C   1 
ATOM   254  O O   . GLY A 1 37  ? -14.806 -14.897 -25.018 1.00 16.79 ? 62  GLY A O   1 
ATOM   255  N N   . ASP A 1 38  ? -14.584 -15.496 -27.180 1.00 15.26 ? 63  ASP A N   1 
ATOM   256  C CA  . ASP A 1 38  ? -13.746 -16.660 -26.912 1.00 18.36 ? 63  ASP A CA  1 
ATOM   257  C C   . ASP A 1 38  ? -12.314 -16.492 -27.412 1.00 20.96 ? 63  ASP A C   1 
ATOM   258  O O   . ASP A 1 38  ? -11.563 -17.471 -27.492 1.00 14.65 ? 63  ASP A O   1 
ATOM   259  C CB  . ASP A 1 38  ? -14.388 -17.911 -27.512 1.00 16.05 ? 63  ASP A CB  1 
ATOM   260  C CG  . ASP A 1 38  ? -15.725 -18.239 -26.873 1.00 22.71 ? 63  ASP A CG  1 
ATOM   261  O OD1 . ASP A 1 38  ? -15.783 -18.342 -25.633 1.00 24.85 ? 63  ASP A OD1 1 
ATOM   262  O OD2 . ASP A 1 38  ? -16.722 -18.391 -27.617 1.00 29.67 ? 63  ASP A OD2 1 
ATOM   263  N N   . GLU A 1 39  ? -11.923 -15.268 -27.728 1.00 10.38 ? 64  GLU A N   1 
ATOM   264  C CA  . GLU A 1 39  ? -10.545 -14.959 -28.052 1.00 13.44 ? 64  GLU A CA  1 
ATOM   265  C C   . GLU A 1 39  ? -9.804  -14.535 -26.788 1.00 14.52 ? 64  GLU A C   1 
ATOM   266  O O   . GLU A 1 39  ? -10.381 -13.911 -25.890 1.00 17.84 ? 64  GLU A O   1 
ATOM   267  C CB  . GLU A 1 39  ? -10.485 -13.870 -29.132 1.00 13.93 ? 64  GLU A CB  1 
ATOM   268  C CG  . GLU A 1 39  ? -11.225 -14.291 -30.427 1.00 27.32 ? 64  GLU A CG  1 
ATOM   269  C CD  . GLU A 1 39  ? -10.973 -13.363 -31.598 1.00 37.22 ? 64  GLU A CD  1 
ATOM   270  O OE1 . GLU A 1 39  ? -9.989  -12.583 -31.563 1.00 22.03 ? 64  GLU A OE1 1 
ATOM   271  O OE2 . GLU A 1 39  ? -11.776 -13.413 -32.568 1.00 35.52 ? 64  GLU A OE2 1 
ATOM   272  N N   . ARG A 1 40  ? -8.535  -14.914 -26.703 1.00 14.41 ? 65  ARG A N   1 
ATOM   273  C CA  . ARG A 1 40  ? -7.734  -14.543 -25.555 1.00 9.48  ? 65  ARG A CA  1 
ATOM   274  C C   . ARG A 1 40  ? -7.221  -13.121 -25.683 1.00 7.57  ? 65  ARG A C   1 
ATOM   275  O O   . ARG A 1 40  ? -6.894  -12.632 -26.767 1.00 19.09 ? 65  ARG A O   1 
ATOM   276  C CB  . ARG A 1 40  ? -6.562  -15.509 -25.390 1.00 8.12  ? 65  ARG A CB  1 
ATOM   277  C CG  . ARG A 1 40  ? -6.968  -16.842 -24.776 1.00 17.04 ? 65  ARG A CG  1 
ATOM   278  C CD  . ARG A 1 40  ? -5.796  -17.781 -24.545 1.00 12.44 ? 65  ARG A CD  1 
ATOM   279  N NE  . ARG A 1 40  ? -6.254  -19.026 -23.936 1.00 17.22 ? 65  ARG A NE  1 
ATOM   280  C CZ  . ARG A 1 40  ? -6.513  -19.186 -22.643 1.00 12.24 ? 65  ARG A CZ  1 
ATOM   281  N NH1 . ARG A 1 40  ? -6.294  -18.220 -21.766 1.00 16.11 ? 65  ARG A NH1 1 
ATOM   282  N NH2 . ARG A 1 40  ? -6.994  -20.350 -22.217 1.00 17.26 ? 65  ARG A NH2 1 
ATOM   283  N N   . PHE A 1 41  ? -7.151  -12.465 -24.541 1.00 11.76 ? 66  PHE A N   1 
ATOM   284  C CA  . PHE A 1 41  ? -6.643  -11.122 -24.392 1.00 14.17 ? 66  PHE A CA  1 
ATOM   285  C C   . PHE A 1 41  ? -5.757  -11.097 -23.163 1.00 11.11 ? 66  PHE A C   1 
ATOM   286  O O   . PHE A 1 41  ? -6.026  -11.808 -22.186 1.00 16.37 ? 66  PHE A O   1 
ATOM   287  C CB  . PHE A 1 41  ? -7.766  -10.082 -24.230 1.00 14.53 ? 66  PHE A CB  1 
ATOM   288  C CG  . PHE A 1 41  ? -8.609  -9.875  -25.464 1.00 13.71 ? 66  PHE A CG  1 
ATOM   289  C CD1 . PHE A 1 41  ? -9.604  -10.779 -25.820 1.00 8.96  ? 66  PHE A CD1 1 
ATOM   290  C CD2 . PHE A 1 41  ? -8.394  -8.763  -26.271 1.00 11.80 ? 66  PHE A CD2 1 
ATOM   291  C CE1 . PHE A 1 41  ? -10.368 -10.572 -26.956 1.00 12.22 ? 66  PHE A CE1 1 
ATOM   292  C CE2 . PHE A 1 41  ? -9.157  -8.547  -27.412 1.00 12.56 ? 66  PHE A CE2 1 
ATOM   293  C CZ  . PHE A 1 41  ? -10.145 -9.447  -27.755 1.00 10.07 ? 66  PHE A CZ  1 
ATOM   294  N N   . PRO A 1 42  ? -4.734  -10.254 -23.162 1.00 18.81 ? 67  PRO A N   1 
ATOM   295  C CA  . PRO A 1 42  ? -3.926  -10.086 -21.953 1.00 23.25 ? 67  PRO A CA  1 
ATOM   296  C C   . PRO A 1 42  ? -4.776  -9.371  -20.917 1.00 20.08 ? 67  PRO A C   1 
ATOM   297  O O   . PRO A 1 42  ? -5.364  -8.324  -21.201 1.00 18.66 ? 67  PRO A O   1 
ATOM   298  C CB  . PRO A 1 42  ? -2.742  -9.224  -22.411 1.00 14.98 ? 67  PRO A CB  1 
ATOM   299  C CG  . PRO A 1 42  ? -2.975  -8.901  -23.871 1.00 21.99 ? 67  PRO A CG  1 
ATOM   300  C CD  . PRO A 1 42  ? -4.309  -9.401  -24.291 1.00 19.68 ? 67  PRO A CD  1 
ATOM   301  N N   . MET A 1 43  ? -4.846  -9.943  -19.715 1.00 15.05 ? 68  MET A N   1 
ATOM   302  C CA  . MET A 1 43  ? -5.691  -9.329  -18.699 1.00 18.20 ? 68  MET A CA  1 
ATOM   303  C C   . MET A 1 43  ? -5.066  -8.075  -18.115 1.00 18.20 ? 68  MET A C   1 
ATOM   304  O O   . MET A 1 43  ? -5.791  -7.126  -17.792 1.00 15.58 ? 68  MET A O   1 
ATOM   305  C CB  . MET A 1 43  ? -6.004  -10.330 -17.590 1.00 9.90  ? 68  MET A CB  1 
ATOM   306  C CG  . MET A 1 43  ? -6.698  -11.593 -18.073 1.00 15.38 ? 68  MET A CG  1 
ATOM   307  S SD  . MET A 1 43  ? -6.768  -12.874 -16.820 1.00 23.68 ? 68  MET A SD  1 
ATOM   308  C CE  . MET A 1 43  ? -5.072  -13.399 -16.778 1.00 17.55 ? 68  MET A CE  1 
ATOM   309  N N   . CYS A 1 44  ? -3.742  -8.046  -18.012 1.00 13.51 ? 69  CYS A N   1 
ATOM   310  C CA  . CYS A 1 44  ? -3.016  -6.967  -17.342 1.00 17.60 ? 69  CYS A CA  1 
ATOM   311  C C   . CYS A 1 44  ? -3.622  -6.763  -15.951 1.00 11.62 ? 69  CYS A C   1 
ATOM   312  O O   . CYS A 1 44  ? -3.941  -7.754  -15.272 1.00 15.56 ? 69  CYS A O   1 
ATOM   313  C CB  . CYS A 1 44  ? -3.011  -5.736  -18.241 1.00 15.26 ? 69  CYS A CB  1 
ATOM   314  S SG  . CYS A 1 44  ? -2.240  -5.981  -19.854 1.00 27.64 ? 69  CYS A SG  1 
ATOM   315  N N   . SER A 1 45  ? -3.874  -5.523  -15.520 1.00 9.96  ? 70  SER A N   1 
ATOM   316  C CA  . SER A 1 45  ? -4.274  -5.283  -14.140 1.00 14.96 ? 70  SER A CA  1 
ATOM   317  C C   . SER A 1 45  ? -5.638  -5.866  -13.787 1.00 12.63 ? 70  SER A C   1 
ATOM   318  O O   . SER A 1 45  ? -5.937  -6.011  -12.595 1.00 16.14 ? 70  SER A O   1 
ATOM   319  C CB  . SER A 1 45  ? -4.265  -3.781  -13.863 1.00 9.98  ? 70  SER A CB  1 
ATOM   320  O OG  . SER A 1 45  ? -2.939  -3.323  -13.660 1.00 19.41 ? 70  SER A OG  1 
ATOM   321  N N   . THR A 1 46  ? -6.461  -6.240  -14.768 1.00 7.64  ? 71  THR A N   1 
ATOM   322  C CA  . THR A 1 46  ? -7.749  -6.807  -14.394 1.00 14.84 ? 71  THR A CA  1 
ATOM   323  C C   . THR A 1 46  ? -7.575  -8.170  -13.737 1.00 16.19 ? 71  THR A C   1 
ATOM   324  O O   . THR A 1 46  ? -8.438  -8.586  -12.943 1.00 13.26 ? 71  THR A O   1 
ATOM   325  C CB  . THR A 1 46  ? -8.668  -6.929  -15.615 1.00 14.46 ? 71  THR A CB  1 
ATOM   326  O OG1 . THR A 1 46  ? -8.125  -7.883  -16.533 1.00 17.39 ? 71  THR A OG1 1 
ATOM   327  C CG2 . THR A 1 46  ? -8.838  -5.590  -16.316 1.00 14.85 ? 71  THR A CG2 1 
ATOM   328  N N   . SER A 1 47  ? -6.399  -8.787  -13.910 1.00 9.05  ? 72  SER A N   1 
ATOM   329  C CA  . SER A 1 47  ? -6.144  -10.047 -13.233 1.00 12.91 ? 72  SER A CA  1 
ATOM   330  C C   . SER A 1 47  ? -6.132  -9.861  -11.726 1.00 13.58 ? 72  SER A C   1 
ATOM   331  O O   . SER A 1 47  ? -6.403  -10.816 -10.985 1.00 14.46 ? 72  SER A O   1 
ATOM   332  C CB  . SER A 1 47  ? -4.815  -10.638 -13.722 1.00 11.04 ? 72  SER A CB  1 
ATOM   333  O OG  . SER A 1 47  ? -3.726  -9.792  -13.405 1.00 12.04 ? 72  SER A OG  1 
ATOM   334  N N   . LYS A 1 48  ? -5.910  -8.626  -11.267 1.00 11.78 ? 73  LYS A N   1 
ATOM   335  C CA  . LYS A 1 48  ? -5.892  -8.355  -9.838  1.00 9.15  ? 73  LYS A CA  1 
ATOM   336  C C   . LYS A 1 48  ? -7.189  -8.784  -9.170  1.00 11.99 ? 73  LYS A C   1 
ATOM   337  O O   . LYS A 1 48  ? -7.159  -9.311  -8.048  1.00 10.76 ? 73  LYS A O   1 
ATOM   338  C CB  . LYS A 1 48  ? -5.594  -6.877  -9.595  1.00 14.46 ? 73  LYS A CB  1 
ATOM   339  C CG  . LYS A 1 48  ? -4.155  -6.537  -9.945  1.00 14.82 ? 73  LYS A CG  1 
ATOM   340  C CD  . LYS A 1 48  ? -3.877  -5.042  -10.014 1.00 10.94 ? 73  LYS A CD  1 
ATOM   341  C CE  . LYS A 1 48  ? -2.421  -4.823  -10.418 1.00 8.59  ? 73  LYS A CE  1 
ATOM   342  N NZ  . LYS A 1 48  ? -1.958  -3.433  -10.225 1.00 15.74 ? 73  LYS A NZ  1 
ATOM   343  N N   . VAL A 1 49  ? -8.334  -8.633  -9.862  1.00 13.73 ? 74  VAL A N   1 
ATOM   344  C CA  . VAL A 1 49  ? -9.592  -9.083  -9.255  1.00 11.65 ? 74  VAL A CA  1 
ATOM   345  C C   . VAL A 1 49  ? -9.443  -10.517 -8.773  1.00 10.42 ? 74  VAL A C   1 
ATOM   346  O O   . VAL A 1 49  ? -9.630  -10.820 -7.586  1.00 11.74 ? 74  VAL A O   1 
ATOM   347  C CB  . VAL A 1 49  ? -10.775 -8.951  -10.233 1.00 9.05  ? 74  VAL A CB  1 
ATOM   348  C CG1 . VAL A 1 49  ? -12.033 -9.574  -9.616  1.00 8.77  ? 74  VAL A CG1 1 
ATOM   349  C CG2 . VAL A 1 49  ? -11.035 -7.502  -10.579 1.00 9.78  ? 74  VAL A CG2 1 
ATOM   350  N N   . MET A 1 50  ? -9.028  -11.405 -9.679  1.00 13.44 ? 75  MET A N   1 
ATOM   351  C CA  . MET A 1 50  ? -8.896  -12.811 -9.320  1.00 14.71 ? 75  MET A CA  1 
ATOM   352  C C   . MET A 1 50  ? -8.006  -12.974 -8.096  1.00 11.87 ? 75  MET A C   1 
ATOM   353  O O   . MET A 1 50  ? -8.405  -13.613 -7.112  1.00 11.85 ? 75  MET A O   1 
ATOM   354  C CB  . MET A 1 50  ? -8.356  -13.596 -10.516 1.00 12.94 ? 75  MET A CB  1 
ATOM   355  C CG  . MET A 1 50  ? -8.545  -15.100 -10.425 1.00 26.39 ? 75  MET A CG  1 
ATOM   356  S SD  . MET A 1 50  ? -10.264 -15.571 -10.719 1.00 22.32 ? 75  MET A SD  1 
ATOM   357  C CE  . MET A 1 50  ? -10.238 -15.929 -12.475 1.00 34.57 ? 75  MET A CE  1 
ATOM   358  N N   . ALA A 1 51  ? -6.845  -12.312 -8.094  1.00 6.92  ? 76  ALA A N   1 
ATOM   359  C CA  . ALA A 1 51  ? -5.927  -12.483 -6.976  1.00 13.31 ? 76  ALA A CA  1 
ATOM   360  C C   . ALA A 1 51  ? -6.569  -12.022 -5.678  1.00 11.44 ? 76  ALA A C   1 
ATOM   361  O O   . ALA A 1 51  ? -6.546  -12.746 -4.673  1.00 13.89 ? 76  ALA A O   1 
ATOM   362  C CB  . ALA A 1 51  ? -4.626  -11.719 -7.233  1.00 9.56  ? 76  ALA A CB  1 
ATOM   363  N N   . ALA A 1 52  ? -7.260  -10.880 -5.711  1.00 11.00 ? 77  ALA A N   1 
ATOM   364  C CA  . ALA A 1 52  ? -7.898  -10.433 -4.482  1.00 15.89 ? 77  ALA A CA  1 
ATOM   365  C C   . ALA A 1 52  ? -8.984  -11.410 -4.071  1.00 13.22 ? 77  ALA A C   1 
ATOM   366  O O   . ALA A 1 52  ? -9.039  -11.829 -2.905  1.00 14.05 ? 77  ALA A O   1 
ATOM   367  C CB  . ALA A 1 52  ? -8.462  -9.023  -4.656  1.00 9.79  ? 77  ALA A CB  1 
ATOM   368  N N   . ALA A 1 53  ? -9.751  -11.906 -5.044  1.00 11.43 ? 78  ALA A N   1 
ATOM   369  C CA  . ALA A 1 53  ? -10.774 -12.878 -4.703  1.00 12.06 ? 78  ALA A CA  1 
ATOM   370  C C   . ALA A 1 53  ? -10.137 -14.129 -4.129  1.00 11.15 ? 78  ALA A C   1 
ATOM   371  O O   . ALA A 1 53  ? -10.606 -14.659 -3.112  1.00 11.81 ? 78  ALA A O   1 
ATOM   372  C CB  . ALA A 1 53  ? -11.609 -13.216 -5.937  1.00 15.38 ? 78  ALA A CB  1 
ATOM   373  N N   . ALA A 1 54  ? -8.973  -14.513 -4.658  1.00 9.07  ? 79  ALA A N   1 
ATOM   374  C CA  . ALA A 1 54  ? -8.350  -15.727 -4.151  1.00 14.40 ? 79  ALA A CA  1 
ATOM   375  C C   . ALA A 1 54  ? -7.901  -15.531 -2.716  1.00 9.46  ? 79  ALA A C   1 
ATOM   376  O O   . ALA A 1 54  ? -8.178  -16.378 -1.856  1.00 7.47  ? 79  ALA A O   1 
ATOM   377  C CB  . ALA A 1 54  ? -7.172  -16.131 -5.042  1.00 5.93  ? 79  ALA A CB  1 
ATOM   378  N N   . VAL A 1 55  ? -7.405  -14.331 -2.399  1.00 11.33 ? 80  VAL A N   1 
ATOM   379  C CA  . VAL A 1 55  ? -7.019  -14.077 -1.019  1.00 11.48 ? 80  VAL A CA  1 
ATOM   380  C C   . VAL A 1 55  ? -8.253  -13.968 -0.145  1.00 11.90 ? 80  VAL A C   1 
ATOM   381  O O   . VAL A 1 55  ? -8.297  -14.542 0.953   1.00 12.88 ? 80  VAL A O   1 
ATOM   382  C CB  . VAL A 1 55  ? -6.134  -12.823 -0.934  1.00 14.15 ? 80  VAL A CB  1 
ATOM   383  C CG1 . VAL A 1 55  ? -5.866  -12.459 0.521   1.00 15.81 ? 80  VAL A CG1 1 
ATOM   384  C CG2 . VAL A 1 55  ? -4.821  -13.065 -1.681  1.00 15.45 ? 80  VAL A CG2 1 
ATOM   385  N N   . LEU A 1 56  ? -9.327  -13.379 -0.681  1.00 11.46 ? 81  LEU A N   1 
ATOM   386  C CA  . LEU A 1 56  ? -10.584 -13.374 0.051   1.00 10.49 ? 81  LEU A CA  1 
ATOM   387  C C   . LEU A 1 56  ? -11.049 -14.788 0.315   1.00 13.59 ? 81  LEU A C   1 
ATOM   388  O O   . LEU A 1 56  ? -11.487 -15.108 1.428   1.00 17.71 ? 81  LEU A O   1 
ATOM   389  C CB  . LEU A 1 56  ? -11.655 -12.615 -0.731  1.00 14.65 ? 81  LEU A CB  1 
ATOM   390  C CG  . LEU A 1 56  ? -11.576 -11.094 -0.771  1.00 18.61 ? 81  LEU A CG  1 
ATOM   391  C CD1 . LEU A 1 56  ? -12.643 -10.561 -1.710  1.00 10.61 ? 81  LEU A CD1 1 
ATOM   392  C CD2 . LEU A 1 56  ? -11.768 -10.553 0.638   1.00 10.85 ? 81  LEU A CD2 1 
ATOM   393  N N   . LYS A 1 57  ? -10.901 -15.670 -0.673  1.00 8.90  ? 82  LYS A N   1 
ATOM   394  C CA  . LYS A 1 57  ? -11.308 -17.045 -0.448  1.00 16.56 ? 82  LYS A CA  1 
ATOM   395  C C   . LYS A 1 57  ? -10.470 -17.671 0.662   1.00 14.38 ? 82  LYS A C   1 
ATOM   396  O O   . LYS A 1 57  ? -11.009 -18.333 1.559   1.00 11.66 ? 82  LYS A O   1 
ATOM   397  C CB  . LYS A 1 57  ? -11.228 -17.837 -1.755  1.00 16.31 ? 82  LYS A CB  1 
ATOM   398  C CG  . LYS A 1 57  ? -11.482 -19.313 -1.606  1.00 15.00 ? 82  LYS A CG  1 
ATOM   399  C CD  . LYS A 1 57  ? -12.865 -19.425 -0.972  1.00 24.92 ? 82  LYS A CD  1 
ATOM   400  C CE  . LYS A 1 57  ? -13.776 -20.441 -1.620  1.00 33.70 ? 82  LYS A CE  1 
ATOM   401  N NZ  . LYS A 1 57  ? -15.198 -19.997 -1.432  1.00 27.04 ? 82  LYS A NZ  1 
ATOM   402  N N   . GLN A 1 58  ? -9.150  -17.440 0.639   1.00 14.01 ? 83  GLN A N   1 
ATOM   403  C CA  . GLN A 1 58  ? -8.308  -17.896 1.744   1.00 12.48 ? 83  GLN A CA  1 
ATOM   404  C C   . GLN A 1 58  ? -8.802  -17.393 3.092   1.00 10.29 ? 83  GLN A C   1 
ATOM   405  O O   . GLN A 1 58  ? -8.723  -18.111 4.093   1.00 15.58 ? 83  GLN A O   1 
ATOM   406  C CB  . GLN A 1 58  ? -6.845  -17.507 1.541   1.00 10.17 ? 83  GLN A CB  1 
ATOM   407  C CG  . GLN A 1 58  ? -6.144  -18.307 0.470   1.00 7.45  ? 83  GLN A CG  1 
ATOM   408  C CD  . GLN A 1 58  ? -4.679  -17.944 0.349   1.00 22.87 ? 83  GLN A CD  1 
ATOM   409  O OE1 . GLN A 1 58  ? -4.290  -16.787 0.518   1.00 20.22 ? 83  GLN A OE1 1 
ATOM   410  N NE2 . GLN A 1 58  ? -3.853  -18.941 0.064   1.00 14.01 ? 83  GLN A NE2 1 
ATOM   411  N N   . SER A 1 59  ? -9.320  -16.167 3.145   1.00 17.91 ? 84  SER A N   1 
ATOM   412  C CA  . SER A 1 59  ? -9.714  -15.655 4.448   1.00 15.72 ? 84  SER A CA  1 
ATOM   413  C C   . SER A 1 59  ? -10.925 -16.384 5.006   1.00 16.43 ? 84  SER A C   1 
ATOM   414  O O   . SER A 1 59  ? -11.240 -16.216 6.189   1.00 25.38 ? 84  SER A O   1 
ATOM   415  C CB  . SER A 1 59  ? -9.979  -14.145 4.358   1.00 14.61 ? 84  SER A CB  1 
ATOM   416  O OG  . SER A 1 59  ? -11.270 -13.852 3.834   1.00 11.95 ? 84  SER A OG  1 
ATOM   417  N N   . GLU A 1 60  ? -11.631 -17.164 4.186   1.00 18.49 ? 85  GLU A N   1 
ATOM   418  C CA  . GLU A 1 60  ? -12.762 -17.910 4.723   1.00 26.43 ? 85  GLU A CA  1 
ATOM   419  C C   . GLU A 1 60  ? -12.321 -19.022 5.670   1.00 21.06 ? 85  GLU A C   1 
ATOM   420  O O   . GLU A 1 60  ? -13.105 -19.423 6.539   1.00 19.24 ? 85  GLU A O   1 
ATOM   421  C CB  . GLU A 1 60  ? -13.596 -18.417 3.551   1.00 11.08 ? 85  GLU A CB  1 
ATOM   422  C CG  . GLU A 1 60  ? -14.064 -17.224 2.722   1.00 21.13 ? 85  GLU A CG  1 
ATOM   423  C CD  . GLU A 1 60  ? -14.913 -17.580 1.523   1.00 33.42 ? 85  GLU A CD  1 
ATOM   424  O OE1 . GLU A 1 60  ? -14.505 -17.269 0.382   1.00 30.58 ? 85  GLU A OE1 1 
ATOM   425  O OE2 . GLU A 1 60  ? -15.968 -18.221 1.715   1.00 36.30 ? 85  GLU A OE2 1 
ATOM   426  N N   . THR A 1 61  ? -11.102 -19.559 5.520   1.00 21.79 ? 86  THR A N   1 
ATOM   427  C CA  . THR A 1 61  ? -10.665 -20.596 6.452   1.00 26.33 ? 86  THR A CA  1 
ATOM   428  C C   . THR A 1 61  ? -9.449  -20.148 7.250   1.00 26.16 ? 86  THR A C   1 
ATOM   429  O O   . THR A 1 61  ? -8.857  -20.952 7.979   1.00 32.29 ? 86  THR A O   1 
ATOM   430  C CB  . THR A 1 61  ? -10.311 -21.867 5.683   1.00 20.38 ? 86  THR A CB  1 
ATOM   431  O OG1 . THR A 1 61  ? -9.415  -21.528 4.615   1.00 13.56 ? 86  THR A OG1 1 
ATOM   432  C CG2 . THR A 1 61  ? -11.565 -22.506 5.100   1.00 13.18 ? 86  THR A CG2 1 
ATOM   433  N N   . GLN A 1 62  ? -9.108  -18.866 7.168   1.00 28.31 ? 87  GLN A N   1 
ATOM   434  C CA  . GLN A 1 62  ? -8.012  -18.208 7.882   1.00 25.80 ? 87  GLN A CA  1 
ATOM   435  C C   . GLN A 1 62  ? -8.841  -16.984 8.255   1.00 21.63 ? 87  GLN A C   1 
ATOM   436  O O   . GLN A 1 62  ? -8.774  -15.955 7.577   1.00 26.91 ? 87  GLN A O   1 
ATOM   437  C CB  . GLN A 1 62  ? -6.831  -17.947 6.958   1.00 26.06 ? 87  GLN A CB  1 
ATOM   438  C CG  . GLN A 1 62  ? -6.112  -19.275 6.584   1.00 34.82 ? 87  GLN A CG  1 
ATOM   439  C CD  . GLN A 1 62  ? -4.761  -19.109 5.893   1.00 33.15 ? 87  GLN A CD  1 
ATOM   440  O OE1 . GLN A 1 62  ? -4.566  -19.598 4.778   1.00 15.99 ? 87  GLN A OE1 1 
ATOM   441  N NE2 . GLN A 1 62  ? -3.807  -18.489 6.578   1.00 34.33 ? 87  GLN A NE2 1 
ATOM   442  N N   . LYS A 1 63  ? -9.564  -17.076 9.367   1.00 18.96 ? 88  LYS A N   1 
ATOM   443  C CA  . LYS A 1 63  ? -10.323 -15.932 9.866   1.00 30.84 ? 88  LYS A CA  1 
ATOM   444  C C   . LYS A 1 63  ? -9.506  -14.673 10.132  1.00 26.03 ? 88  LYS A C   1 
ATOM   445  O O   . LYS A 1 63  ? -10.057 -13.570 10.028  1.00 32.65 ? 88  LYS A O   1 
ATOM   446  C CB  . LYS A 1 63  ? -11.092 -16.365 11.111  1.00 34.08 ? 88  LYS A CB  1 
ATOM   447  C CG  . LYS A 1 63  ? -11.875 -17.653 10.874  1.00 31.87 ? 88  LYS A CG  1 
ATOM   448  C CD  . LYS A 1 63  ? -13.268 -17.610 11.492  1.00 39.58 ? 88  LYS A CD  1 
ATOM   449  C CE  . LYS A 1 63  ? -14.151 -18.709 10.904  1.00 41.42 ? 88  LYS A CE  1 
ATOM   450  N NZ  . LYS A 1 63  ? -15.313 -18.163 10.130  1.00 26.69 ? 88  LYS A NZ  1 
ATOM   451  N N   . GLN A 1 64  ? -8.218  -14.769 10.434  1.00 20.88 ? 89  GLN A N   1 
ATOM   452  C CA  . GLN A 1 64  ? -7.481  -13.539 10.710  1.00 21.35 ? 89  GLN A CA  1 
ATOM   453  C C   . GLN A 1 64  ? -6.538  -13.145 9.579   1.00 20.17 ? 89  GLN A C   1 
ATOM   454  O O   . GLN A 1 64  ? -5.663  -12.294 9.777   1.00 21.78 ? 89  GLN A O   1 
ATOM   455  C CB  . GLN A 1 64  ? -6.732  -13.661 12.034  1.00 21.45 ? 89  GLN A CB  1 
ATOM   456  C CG  . GLN A 1 64  ? -7.490  -12.996 13.164  1.00 28.87 ? 89  GLN A CG  1 
ATOM   457  C CD  . GLN A 1 64  ? -8.844  -13.628 13.387  1.00 22.20 ? 89  GLN A CD  1 
ATOM   458  O OE1 . GLN A 1 64  ? -8.970  -14.852 13.448  1.00 23.57 ? 89  GLN A OE1 1 
ATOM   459  N NE2 . GLN A 1 64  ? -9.874  -12.796 13.490  1.00 33.64 ? 89  GLN A NE2 1 
ATOM   460  N N   . LEU A 1 65  ? -6.730  -13.706 8.379   1.00 26.29 ? 90  LEU A N   1 
ATOM   461  C CA  . LEU A 1 65  ? -5.733  -13.531 7.329   1.00 17.79 ? 90  LEU A CA  1 
ATOM   462  C C   . LEU A 1 65  ? -5.714  -12.111 6.780   1.00 21.71 ? 90  LEU A C   1 
ATOM   463  O O   . LEU A 1 65  ? -4.639  -11.566 6.503   1.00 21.65 ? 90  LEU A O   1 
ATOM   464  C CB  . LEU A 1 65  ? -6.014  -14.493 6.181   1.00 20.42 ? 90  LEU A CB  1 
ATOM   465  C CG  . LEU A 1 65  ? -5.023  -14.387 5.020   1.00 21.29 ? 90  LEU A CG  1 
ATOM   466  C CD1 . LEU A 1 65  ? -3.589  -14.712 5.462   1.00 23.03 ? 90  LEU A CD1 1 
ATOM   467  C CD2 . LEU A 1 65  ? -5.470  -15.224 3.836   1.00 26.90 ? 90  LEU A CD2 1 
ATOM   468  N N   . LEU A 1 66  ? -6.882  -11.491 6.614   1.00 12.85 ? 91  LEU A N   1 
ATOM   469  C CA  . LEU A 1 66  ? -6.889  -10.195 5.947   1.00 20.04 ? 91  LEU A CA  1 
ATOM   470  C C   . LEU A 1 66  ? -6.316  -9.102  6.828   1.00 20.52 ? 91  LEU A C   1 
ATOM   471  O O   . LEU A 1 66  ? -5.993  -8.017  6.330   1.00 17.62 ? 91  LEU A O   1 
ATOM   472  C CB  . LEU A 1 66  ? -8.324  -9.815  5.560   1.00 13.55 ? 91  LEU A CB  1 
ATOM   473  C CG  . LEU A 1 66  ? -9.041  -10.641 4.495   1.00 12.56 ? 91  LEU A CG  1 
ATOM   474  C CD1 . LEU A 1 66  ? -10.370 -9.997  4.125   1.00 20.68 ? 91  LEU A CD1 1 
ATOM   475  C CD2 . LEU A 1 66  ? -8.161  -10.837 3.263   1.00 15.88 ? 91  LEU A CD2 1 
ATOM   476  N N   . ASN A 1 67  ? -6.131  -9.398  8.106   1.00 17.87 ? 92  ASN A N   1 
ATOM   477  C CA  . ASN A 1 67  ? -5.575  -8.484  9.083   1.00 20.73 ? 92  ASN A CA  1 
ATOM   478  C C   . ASN A 1 67  ? -4.089  -8.700  9.336   1.00 20.33 ? 92  ASN A C   1 
ATOM   479  O O   . ASN A 1 67  ? -3.519  -8.034  10.205  1.00 22.08 ? 92  ASN A O   1 
ATOM   480  C CB  . ASN A 1 67  ? -6.379  -8.651  10.370  1.00 27.97 ? 92  ASN A CB  1 
ATOM   481  C CG  . ASN A 1 67  ? -7.712  -7.936  10.295  1.00 44.66 ? 92  ASN A CG  1 
ATOM   482  O OD1 . ASN A 1 67  ? -7.925  -7.099  9.415   1.00 20.07 ? 92  ASN A OD1 1 
ATOM   483  N ND2 . ASN A 1 67  ? -8.645  -8.319  11.163  1.00 65.08 ? 92  ASN A ND2 1 
ATOM   484  N N   . GLN A 1 68  ? -3.455  -9.607  8.600   1.00 19.54 ? 93  GLN A N   1 
ATOM   485  C CA  . GLN A 1 68  ? -2.100  -10.081 8.855   1.00 21.83 ? 93  GLN A CA  1 
ATOM   486  C C   . GLN A 1 68  ? -1.078  -9.161  8.195   1.00 24.29 ? 93  GLN A C   1 
ATOM   487  O O   . GLN A 1 68  ? -1.208  -8.857  7.003   1.00 23.40 ? 93  GLN A O   1 
ATOM   488  C CB  . GLN A 1 68  ? -1.933  -11.498 8.333   1.00 28.94 ? 93  GLN A CB  1 
ATOM   489  C CG  . GLN A 1 68  ? -0.504  -11.998 8.281   1.00 46.07 ? 93  GLN A CG  1 
ATOM   490  C CD  . GLN A 1 68  ? -0.380  -13.288 7.489   1.00 54.07 ? 93  GLN A CD  1 
ATOM   491  O OE1 . GLN A 1 68  ? -0.905  -14.330 7.890   1.00 34.30 ? 93  GLN A OE1 1 
ATOM   492  N NE2 . GLN A 1 68  ? 0.313   -13.223 6.355   1.00 46.09 ? 93  GLN A NE2 1 
ATOM   493  N N   . PRO A 1 69  ? -0.055  -8.715  8.921   1.00 31.27 ? 94  PRO A N   1 
ATOM   494  C CA  . PRO A 1 69  ? 0.908   -7.775  8.337   1.00 29.44 ? 94  PRO A CA  1 
ATOM   495  C C   . PRO A 1 69  ? 1.818   -8.431  7.309   1.00 17.43 ? 94  PRO A C   1 
ATOM   496  O O   . PRO A 1 69  ? 2.170   -9.610  7.403   1.00 27.71 ? 94  PRO A O   1 
ATOM   497  C CB  . PRO A 1 69  ? 1.710   -7.290  9.553   1.00 33.76 ? 94  PRO A CB  1 
ATOM   498  C CG  . PRO A 1 69  ? 0.832   -7.618  10.741  1.00 34.33 ? 94  PRO A CG  1 
ATOM   499  C CD  . PRO A 1 69  ? 0.159   -8.892  10.366  1.00 15.95 ? 94  PRO A CD  1 
ATOM   500  N N   . VAL A 1 70  ? 2.174   -7.639  6.302   1.00 20.60 ? 95  VAL A N   1 
ATOM   501  C CA  . VAL A 1 70  ? 3.095   -8.003  5.236   1.00 18.56 ? 95  VAL A CA  1 
ATOM   502  C C   . VAL A 1 70  ? 4.161   -6.921  5.161   1.00 25.16 ? 95  VAL A C   1 
ATOM   503  O O   . VAL A 1 70  ? 3.831   -5.731  5.099   1.00 22.01 ? 95  VAL A O   1 
ATOM   504  C CB  . VAL A 1 70  ? 2.369   -8.132  3.881   1.00 19.64 ? 95  VAL A CB  1 
ATOM   505  C CG1 . VAL A 1 70  ? 3.354   -8.475  2.764   1.00 11.60 ? 95  VAL A CG1 1 
ATOM   506  C CG2 . VAL A 1 70  ? 1.256   -9.169  3.968   1.00 18.00 ? 95  VAL A CG2 1 
ATOM   507  N N   . GLU A 1 71  ? 5.426   -7.330  5.146   1.00 19.65 ? 96  GLU A N   1 
ATOM   508  C CA  . GLU A 1 71  ? 6.526   -6.381  5.036   1.00 17.09 ? 96  GLU A CA  1 
ATOM   509  C C   . GLU A 1 71  ? 6.612   -5.825  3.618   1.00 20.71 ? 96  GLU A C   1 
ATOM   510  O O   . GLU A 1 71  ? 6.685   -6.586  2.649   1.00 24.90 ? 96  GLU A O   1 
ATOM   511  C CB  . GLU A 1 71  ? 7.844   -7.061  5.413   1.00 26.67 ? 96  GLU A CB  1 
ATOM   512  C CG  . GLU A 1 71  ? 8.480   -6.565  6.713   1.00 59.77 ? 96  GLU A CG  1 
ATOM   513  C CD  . GLU A 1 71  ? 8.775   -5.066  6.704   1.00 73.03 ? 96  GLU A CD  1 
ATOM   514  O OE1 . GLU A 1 71  ? 9.517   -4.608  5.804   1.00 48.12 ? 96  GLU A OE1 1 
ATOM   515  O OE2 . GLU A 1 71  ? 8.277   -4.353  7.607   1.00 46.43 ? 96  GLU A OE2 1 
ATOM   516  N N   . ILE A 1 72  ? 6.594   -4.498  3.493   1.00 19.49 ? 97  ILE A N   1 
ATOM   517  C CA  . ILE A 1 72  ? 6.919   -3.818  2.243   1.00 14.78 ? 97  ILE A CA  1 
ATOM   518  C C   . ILE A 1 72  ? 8.380   -3.403  2.327   1.00 30.21 ? 97  ILE A C   1 
ATOM   519  O O   . ILE A 1 72  ? 8.751   -2.555  3.147   1.00 26.41 ? 97  ILE A O   1 
ATOM   520  C CB  . ILE A 1 72  ? 6.017   -2.606  1.979   1.00 32.27 ? 97  ILE A CB  1 
ATOM   521  C CG1 . ILE A 1 72  ? 4.537   -2.957  2.161   1.00 15.64 ? 97  ILE A CG1 1 
ATOM   522  C CG2 . ILE A 1 72  ? 6.289   -2.054  0.579   1.00 27.85 ? 97  ILE A CG2 1 
ATOM   523  C CD1 . ILE A 1 72  ? 4.034   -3.949  1.146   1.00 14.08 ? 97  ILE A CD1 1 
ATOM   524  N N   . LYS A 1 73  ? 9.206   -3.992  1.494   1.00 24.27 ? 98  LYS A N   1 
ATOM   525  C CA  . LYS A 1 73  ? 10.617  -3.662  1.482   1.00 22.17 ? 98  LYS A CA  1 
ATOM   526  C C   . LYS A 1 73  ? 10.950  -2.799  0.271   1.00 17.85 ? 98  LYS A C   1 
ATOM   527  O O   . LYS A 1 73  ? 10.214  -2.797  -0.720  1.00 27.90 ? 98  LYS A O   1 
ATOM   528  C CB  . LYS A 1 73  ? 11.379  -4.991  1.492   1.00 31.35 ? 98  LYS A CB  1 
ATOM   529  C CG  . LYS A 1 73  ? 12.118  -5.247  2.794   1.00 43.44 ? 98  LYS A CG  1 
ATOM   530  C CD  . LYS A 1 73  ? 12.173  -6.745  3.117   1.00 54.52 ? 98  LYS A CD  1 
ATOM   531  C CE  . LYS A 1 73  ? 12.341  -7.670  1.928   1.00 44.68 ? 98  LYS A CE  1 
ATOM   532  N NZ  . LYS A 1 73  ? 12.662  -9.046  2.426   1.00 43.78 ? 98  LYS A NZ  1 
ATOM   533  N N   . PRO A 1 74  ? 12.035  -2.016  0.326   1.00 30.63 ? 99  PRO A N   1 
ATOM   534  C CA  . PRO A 1 74  ? 12.420  -1.211  -0.852  1.00 23.13 ? 99  PRO A CA  1 
ATOM   535  C C   . PRO A 1 74  ? 12.531  -2.007  -2.141  1.00 24.14 ? 99  PRO A C   1 
ATOM   536  O O   . PRO A 1 74  ? 12.122  -1.526  -3.206  1.00 23.01 ? 99  PRO A O   1 
ATOM   537  C CB  . PRO A 1 74  ? 13.768  -0.618  -0.431  1.00 28.59 ? 99  PRO A CB  1 
ATOM   538  C CG  . PRO A 1 74  ? 13.676  -0.536  1.055   1.00 26.92 ? 99  PRO A CG  1 
ATOM   539  C CD  . PRO A 1 74  ? 12.928  -1.771  1.473   1.00 21.42 ? 99  PRO A CD  1 
ATOM   540  N N   . ALA A 1 75  ? 13.098  -3.212  -2.075  1.00 19.66 ? 100 ALA A N   1 
ATOM   541  C CA  . ALA A 1 75  ? 13.250  -4.042  -3.260  1.00 20.40 ? 100 ALA A CA  1 
ATOM   542  C C   . ALA A 1 75  ? 11.920  -4.536  -3.812  1.00 20.60 ? 100 ALA A C   1 
ATOM   543  O O   . ALA A 1 75  ? 11.878  -4.985  -4.963  1.00 21.95 ? 100 ALA A O   1 
ATOM   544  C CB  . ALA A 1 75  ? 14.152  -5.235  -2.950  1.00 27.73 ? 100 ALA A CB  1 
ATOM   545  N N   . ASP A 1 76  ? 10.834  -4.441  -3.041  1.00 20.26 ? 101 ASP A N   1 
ATOM   546  C CA  . ASP A 1 76  ? 9.555   -4.934  -3.530  1.00 23.08 ? 101 ASP A CA  1 
ATOM   547  C C   . ASP A 1 76  ? 8.897   -3.988  -4.516  1.00 25.27 ? 101 ASP A C   1 
ATOM   548  O O   . ASP A 1 76  ? 8.009   -4.421  -5.260  1.00 33.99 ? 101 ASP A O   1 
ATOM   549  C CB  . ASP A 1 76  ? 8.594   -5.174  -2.364  1.00 26.22 ? 101 ASP A CB  1 
ATOM   550  C CG  . ASP A 1 76  ? 9.039   -6.304  -1.463  1.00 34.26 ? 101 ASP A CG  1 
ATOM   551  O OD1 . ASP A 1 76  ? 9.791   -7.185  -1.935  1.00 37.84 ? 101 ASP A OD1 1 
ATOM   552  O OD2 . ASP A 1 76  ? 8.625   -6.317  -0.284  1.00 27.82 ? 101 ASP A OD2 1 
ATOM   553  N N   . LEU A 1 77  ? 9.291   -2.718  -4.541  1.00 16.36 ? 102 LEU A N   1 
ATOM   554  C CA  . LEU A 1 77  ? 8.594   -1.768  -5.393  1.00 21.26 ? 102 LEU A CA  1 
ATOM   555  C C   . LEU A 1 77  ? 8.880   -2.092  -6.852  1.00 16.96 ? 102 LEU A C   1 
ATOM   556  O O   . LEU A 1 77  ? 10.015  -2.392  -7.230  1.00 19.02 ? 102 LEU A O   1 
ATOM   557  C CB  . LEU A 1 77  ? 9.000   -0.328  -5.077  1.00 19.31 ? 102 LEU A CB  1 
ATOM   558  C CG  . LEU A 1 77  ? 8.651   0.188   -3.680  1.00 23.58 ? 102 LEU A CG  1 
ATOM   559  C CD1 . LEU A 1 77  ? 8.990   1.671   -3.568  1.00 17.02 ? 102 LEU A CD1 1 
ATOM   560  C CD2 . LEU A 1 77  ? 7.185   -0.077  -3.317  1.00 25.37 ? 102 LEU A CD2 1 
ATOM   561  N N   . VAL A 1 78  ? 7.840   -2.035  -7.672  1.00 23.69 ? 103 VAL A N   1 
ATOM   562  C CA  . VAL A 1 78  ? 7.995   -2.283  -9.097  1.00 23.02 ? 103 VAL A CA  1 
ATOM   563  C C   . VAL A 1 78  ? 7.642   -0.997  -9.836  1.00 24.64 ? 103 VAL A C   1 
ATOM   564  O O   . VAL A 1 78  ? 8.081   0.088   -9.441  1.00 18.70 ? 103 VAL A O   1 
ATOM   565  C CB  . VAL A 1 78  ? 7.157   -3.498  -9.546  1.00 19.10 ? 103 VAL A CB  1 
ATOM   566  C CG1 . VAL A 1 78  ? 7.799   -4.784  -9.047  1.00 15.02 ? 103 VAL A CG1 1 
ATOM   567  C CG2 . VAL A 1 78  ? 5.758   -3.423  -8.984  1.00 15.01 ? 103 VAL A CG2 1 
ATOM   568  N N   . ASN A 1 79  ? 6.823   -1.082  -10.878 1.00 25.22 ? 104 ASN A N   1 
ATOM   569  C CA  . ASN A 1 79  ? 6.698   0.058   -11.773 1.00 25.58 ? 104 ASN A CA  1 
ATOM   570  C C   . ASN A 1 79  ? 5.593   1.027   -11.371 1.00 33.68 ? 104 ASN A C   1 
ATOM   571  O O   . ASN A 1 79  ? 5.591   2.168   -11.848 1.00 40.36 ? 104 ASN A O   1 
ATOM   572  C CB  . ASN A 1 79  ? 6.463   -0.409  -13.210 1.00 27.26 ? 104 ASN A CB  1 
ATOM   573  C CG  . ASN A 1 79  ? 5.220   -1.255  -13.353 1.00 30.19 ? 104 ASN A CG  1 
ATOM   574  O OD1 . ASN A 1 79  ? 4.915   -2.082  -12.494 1.00 30.75 ? 104 ASN A OD1 1 
ATOM   575  N ND2 . ASN A 1 79  ? 4.489   -1.051  -14.441 1.00 30.11 ? 104 ASN A ND2 1 
ATOM   576  N N   . TYR A 1 80  ? 4.659   0.616   -10.516 1.00 22.29 ? 105 TYR A N   1 
ATOM   577  C CA  . TYR A 1 80  ? 3.524   1.475   -10.180 1.00 26.12 ? 105 TYR A CA  1 
ATOM   578  C C   . TYR A 1 80  ? 3.035   1.081   -8.788  1.00 20.38 ? 105 TYR A C   1 
ATOM   579  O O   . TYR A 1 80  ? 2.365   0.057   -8.621  1.00 25.16 ? 105 TYR A O   1 
ATOM   580  C CB  . TYR A 1 80  ? 2.422   1.358   -11.222 1.00 23.76 ? 105 TYR A CB  1 
ATOM   581  C CG  . TYR A 1 80  ? 1.288   2.326   -11.004 1.00 27.87 ? 105 TYR A CG  1 
ATOM   582  C CD1 . TYR A 1 80  ? 1.491   3.694   -11.102 1.00 30.32 ? 105 TYR A CD1 1 
ATOM   583  C CD2 . TYR A 1 80  ? 0.014   1.870   -10.694 1.00 21.30 ? 105 TYR A CD2 1 
ATOM   584  C CE1 . TYR A 1 80  ? 0.454   4.583   -10.899 1.00 35.66 ? 105 TYR A CE1 1 
ATOM   585  C CE2 . TYR A 1 80  ? -1.032  2.747   -10.492 1.00 15.90 ? 105 TYR A CE2 1 
ATOM   586  C CZ  . TYR A 1 80  ? -0.807  4.103   -10.594 1.00 27.51 ? 105 TYR A CZ  1 
ATOM   587  O OH  . TYR A 1 80  ? -1.843  4.988   -10.391 1.00 26.43 ? 105 TYR A OH  1 
ATOM   588  N N   . ASN A 1 81  ? 3.369   1.908   -7.803  1.00 22.98 ? 106 ASN A N   1 
ATOM   589  C CA  . ASN A 1 81  ? 3.237   1.552   -6.390  1.00 21.02 ? 106 ASN A CA  1 
ATOM   590  C C   . ASN A 1 81  ? 2.678   2.752   -5.640  1.00 24.64 ? 106 ASN A C   1 
ATOM   591  O O   . ASN A 1 81  ? 3.279   3.227   -4.675  1.00 27.88 ? 106 ASN A O   1 
ATOM   592  C CB  . ASN A 1 81  ? 4.589   1.155   -5.795  1.00 22.17 ? 106 ASN A CB  1 
ATOM   593  C CG  . ASN A 1 81  ? 5.538   0.571   -6.814  1.00 24.64 ? 106 ASN A CG  1 
ATOM   594  O OD1 . ASN A 1 81  ? 5.278   -0.481  -7.398  1.00 29.30 ? 106 ASN A OD1 1 
ATOM   595  N ND2 . ASN A 1 81  ? 6.647   1.264   -7.046  1.00 29.74 ? 106 ASN A ND2 1 
ATOM   596  N N   . PRO A 1 82  ? 1.518   3.271   -6.051  1.00 20.38 ? 107 PRO A N   1 
ATOM   597  C CA  . PRO A 1 82  ? 1.076   4.540   -5.457  1.00 22.68 ? 107 PRO A CA  1 
ATOM   598  C C   . PRO A 1 82  ? 0.783   4.408   -3.981  1.00 25.93 ? 107 PRO A C   1 
ATOM   599  O O   . PRO A 1 82  ? 0.903   5.392   -3.243  1.00 24.61 ? 107 PRO A O   1 
ATOM   600  C CB  . PRO A 1 82  ? -0.196  4.879   -6.249  1.00 37.86 ? 107 PRO A CB  1 
ATOM   601  C CG  . PRO A 1 82  ? -0.686  3.556   -6.745  1.00 28.84 ? 107 PRO A CG  1 
ATOM   602  C CD  . PRO A 1 82  ? 0.555   2.772   -7.050  1.00 31.88 ? 107 PRO A CD  1 
ATOM   603  N N   . ILE A 1 83  ? 0.409   3.217   -3.530  1.00 25.54 ? 108 ILE A N   1 
ATOM   604  C CA  . ILE A 1 83  ? 0.152   2.965   -2.123  1.00 22.06 ? 108 ILE A CA  1 
ATOM   605  C C   . ILE A 1 83  ? 1.343   2.305   -1.442  1.00 22.50 ? 108 ILE A C   1 
ATOM   606  O O   . ILE A 1 83  ? 1.776   2.740   -0.375  1.00 28.44 ? 108 ILE A O   1 
ATOM   607  C CB  . ILE A 1 83  ? -1.126  2.113   -1.962  1.00 24.79 ? 108 ILE A CB  1 
ATOM   608  C CG1 . ILE A 1 83  ? -2.273  2.736   -2.763  1.00 28.69 ? 108 ILE A CG1 1 
ATOM   609  C CG2 . ILE A 1 83  ? -1.500  1.993   -0.493  1.00 15.93 ? 108 ILE A CG2 1 
ATOM   610  C CD1 . ILE A 1 83  ? -2.545  4.174   -2.413  1.00 19.30 ? 108 ILE A CD1 1 
ATOM   611  N N   . ALA A 1 84  ? 1.909   1.268   -2.065  1.00 22.40 ? 109 ALA A N   1 
ATOM   612  C CA  . ALA A 1 84  ? 2.954   0.503   -1.397  1.00 23.75 ? 109 ALA A CA  1 
ATOM   613  C C   . ALA A 1 84  ? 4.184   1.348   -1.112  1.00 24.31 ? 109 ALA A C   1 
ATOM   614  O O   . ALA A 1 84  ? 4.876   1.118   -0.112  1.00 29.97 ? 109 ALA A O   1 
ATOM   615  C CB  . ALA A 1 84  ? 3.330   -0.714  -2.237  1.00 25.02 ? 109 ALA A CB  1 
ATOM   616  N N   . GLU A 1 85  ? 4.487   2.315   -1.980  1.00 29.20 ? 110 GLU A N   1 
ATOM   617  C CA  . GLU A 1 85  ? 5.681   3.123   -1.773  1.00 27.79 ? 110 GLU A CA  1 
ATOM   618  C C   . GLU A 1 85  ? 5.574   3.920   -0.482  1.00 27.04 ? 110 GLU A C   1 
ATOM   619  O O   . GLU A 1 85  ? 6.596   4.255   0.129   1.00 22.83 ? 110 GLU A O   1 
ATOM   620  C CB  . GLU A 1 85  ? 5.896   4.053   -2.966  1.00 32.93 ? 110 GLU A CB  1 
ATOM   621  C CG  . GLU A 1 85  ? 4.868   5.169   -3.058  1.00 30.74 ? 110 GLU A CG  1 
ATOM   622  C CD  . GLU A 1 85  ? 5.040   6.016   -4.301  1.00 37.90 ? 110 GLU A CD  1 
ATOM   623  O OE1 . GLU A 1 85  ? 4.050   6.649   -4.727  1.00 45.46 ? 110 GLU A OE1 1 
ATOM   624  O OE2 . GLU A 1 85  ? 6.153   6.020   -4.870  1.00 36.91 ? 110 GLU A OE2 1 
ATOM   625  N N   . LYS A 1 86  ? 4.343   4.213   -0.042  1.00 23.37 ? 111 LYS A N   1 
ATOM   626  C CA  . LYS A 1 86  ? 4.130   4.923   1.212   1.00 24.69 ? 111 LYS A CA  1 
ATOM   627  C C   . LYS A 1 86  ? 4.467   4.065   2.430   1.00 26.24 ? 111 LYS A C   1 
ATOM   628  O O   . LYS A 1 86  ? 4.648   4.606   3.526   1.00 23.92 ? 111 LYS A O   1 
ATOM   629  C CB  . LYS A 1 86  ? 2.683   5.413   1.286   1.00 32.63 ? 111 LYS A CB  1 
ATOM   630  C CG  . LYS A 1 86  ? 2.528   6.900   1.005   0.84 38.38 ? 111 LYS A CG  1 
ATOM   631  C CD  . LYS A 1 86  ? 1.354   7.171   0.075   0.72 36.68 ? 111 LYS A CD  1 
ATOM   632  C CE  . LYS A 1 86  ? 0.059   6.579   0.621   0.77 31.30 ? 111 LYS A CE  1 
ATOM   633  N NZ  . LYS A 1 86  ? -1.142  7.347   0.168   1.00 45.43 ? 111 LYS A NZ  1 
ATOM   634  N N   . HIS A 1 87  ? 4.539   2.743   2.268   1.00 21.76 ? 112 HIS A N   1 
ATOM   635  C CA  . HIS A 1 87  ? 4.669   1.820   3.391   1.00 21.83 ? 112 HIS A CA  1 
ATOM   636  C C   . HIS A 1 87  ? 5.954   1.007   3.305   1.00 18.36 ? 112 HIS A C   1 
ATOM   637  O O   . HIS A 1 87  ? 6.077   -0.027  3.968   1.00 18.40 ? 112 HIS A O   1 
ATOM   638  C CB  . HIS A 1 87  ? 3.446   0.910   3.502   1.00 19.61 ? 112 HIS A CB  1 
ATOM   639  C CG  . HIS A 1 87  ? 2.165   1.657   3.712   1.00 26.46 ? 112 HIS A CG  1 
ATOM   640  N ND1 . HIS A 1 87  ? 1.864   2.288   4.901   1.00 23.25 ? 112 HIS A ND1 1 
ATOM   641  C CD2 . HIS A 1 87  ? 1.115   1.886   2.889   1.00 19.16 ? 112 HIS A CD2 1 
ATOM   642  C CE1 . HIS A 1 87  ? 0.681   2.866   4.803   1.00 24.29 ? 112 HIS A CE1 1 
ATOM   643  N NE2 . HIS A 1 87  ? 0.205   2.639   3.592   1.00 20.58 ? 112 HIS A NE2 1 
ATOM   644  N N   . VAL A 1 88  ? 6.914   1.462   2.496   1.00 20.58 ? 113 VAL A N   1 
ATOM   645  C CA  . VAL A 1 88  ? 8.204   0.792   2.412   1.00 21.72 ? 113 VAL A CA  1 
ATOM   646  C C   . VAL A 1 88  ? 8.901   0.872   3.763   1.00 11.70 ? 113 VAL A C   1 
ATOM   647  O O   . VAL A 1 88  ? 8.773   1.863   4.494   1.00 21.00 ? 113 VAL A O   1 
ATOM   648  C CB  . VAL A 1 88  ? 9.048   1.417   1.288   1.00 16.95 ? 113 VAL A CB  1 
ATOM   649  C CG1 . VAL A 1 88  ? 10.488  0.955   1.365   1.00 23.86 ? 113 VAL A CG1 1 
ATOM   650  C CG2 . VAL A 1 88  ? 8.462   1.059   -0.056  1.00 17.79 ? 113 VAL A CG2 1 
ATOM   651  N N   . ASN A 1 89  ? 9.624   -0.193  4.109   1.00 14.74 ? 114 ASN A N   1 
ATOM   652  C CA  . ASN A 1 89  ? 10.230  -0.385  5.425   1.00 17.96 ? 114 ASN A CA  1 
ATOM   653  C C   . ASN A 1 89  ? 9.179   -0.448  6.523   1.00 19.17 ? 114 ASN A C   1 
ATOM   654  O O   . ASN A 1 89  ? 9.495   -0.287  7.707   1.00 23.72 ? 114 ASN A O   1 
ATOM   655  C CB  . ASN A 1 89  ? 11.272  0.695   5.733   1.00 17.52 ? 114 ASN A CB  1 
ATOM   656  C CG  . ASN A 1 89  ? 12.504  0.563   4.866   1.00 25.16 ? 114 ASN A CG  1 
ATOM   657  O OD1 . ASN A 1 89  ? 12.862  1.482   4.125   1.00 19.96 ? 114 ASN A OD1 1 
ATOM   658  N ND2 . ASN A 1 89  ? 13.151  -0.592  4.939   1.00 21.77 ? 114 ASN A ND2 1 
ATOM   659  N N   . GLY A 1 90  ? 7.922   -0.648  6.134   1.00 16.14 ? 115 GLY A N   1 
ATOM   660  C CA  . GLY A 1 90  ? 6.835   -0.825  7.068   1.00 13.42 ? 115 GLY A CA  1 
ATOM   661  C C   . GLY A 1 90  ? 6.022   -2.035  6.672   1.00 20.70 ? 115 GLY A C   1 
ATOM   662  O O   . GLY A 1 90  ? 6.520   -2.930  5.981   1.00 27.41 ? 115 GLY A O   1 
ATOM   663  N N   . THR A 1 91  ? 4.757   -2.075  7.071   1.00 15.68 ? 116 THR A N   1 
ATOM   664  C CA  . THR A 1 91  ? 3.899   -3.198  6.727   1.00 20.11 ? 116 THR A CA  1 
ATOM   665  C C   . THR A 1 91  ? 2.547   -2.707  6.229   1.00 18.27 ? 116 THR A C   1 
ATOM   666  O O   . THR A 1 91  ? 2.126   -1.577  6.498   1.00 23.57 ? 116 THR A O   1 
ATOM   667  C CB  . THR A 1 91  ? 3.694   -4.164  7.905   1.00 21.95 ? 116 THR A CB  1 
ATOM   668  O OG1 . THR A 1 91  ? 3.198   -3.449  9.040   1.00 29.37 ? 116 THR A OG1 1 
ATOM   669  C CG2 . THR A 1 91  ? 4.990   -4.858  8.265   1.00 22.23 ? 116 THR A CG2 1 
ATOM   670  N N   . MET A 1 92  ? 1.892   -3.579  5.471   1.00 20.96 ? 117 MET A N   1 
ATOM   671  C CA  . MET A 1 92  ? 0.512   -3.409  5.059   1.00 19.71 ? 117 MET A CA  1 
ATOM   672  C C   . MET A 1 92  ? -0.239  -4.700  5.353   1.00 22.98 ? 117 MET A C   1 
ATOM   673  O O   . MET A 1 92  ? 0.323   -5.791  5.217   1.00 18.31 ? 117 MET A O   1 
ATOM   674  C CB  . MET A 1 92  ? 0.413   -3.087  3.572   1.00 15.10 ? 117 MET A CB  1 
ATOM   675  C CG  . MET A 1 92  ? 0.645   -1.630  3.232   1.00 19.13 ? 117 MET A CG  1 
ATOM   676  S SD  . MET A 1 92  ? 0.762   -1.445  1.453   1.00 10.96 ? 117 MET A SD  1 
ATOM   677  C CE  . MET A 1 92  ? -0.985  -1.268  1.125   1.00 16.85 ? 117 MET A CE  1 
ATOM   678  N N   . THR A 1 93  ? -1.504  -4.598  5.758   1.00 20.62 ? 118 THR A N   1 
ATOM   679  C CA  . THR A 1 93  ? -2.226  -5.854  5.914   1.00 16.68 ? 118 THR A CA  1 
ATOM   680  C C   . THR A 1 93  ? -2.682  -6.361  4.544   1.00 15.85 ? 118 THR A C   1 
ATOM   681  O O   . THR A 1 93  ? -2.746  -5.607  3.571   1.00 14.30 ? 118 THR A O   1 
ATOM   682  C CB  . THR A 1 93  ? -3.409  -5.673  6.860   1.00 19.14 ? 118 THR A CB  1 
ATOM   683  O OG1 . THR A 1 93  ? -4.397  -4.842  6.237   1.00 15.58 ? 118 THR A OG1 1 
ATOM   684  C CG2 . THR A 1 93  ? -2.949  -5.042  8.165   1.00 16.98 ? 118 THR A CG2 1 
ATOM   685  N N   . LEU A 1 94  ? -3.010  -7.657  4.475   1.00 15.71 ? 119 LEU A N   1 
ATOM   686  C CA  . LEU A 1 94  ? -3.497  -8.226  3.220   1.00 11.57 ? 119 LEU A CA  1 
ATOM   687  C C   . LEU A 1 94  ? -4.803  -7.601  2.767   1.00 16.11 ? 119 LEU A C   1 
ATOM   688  O O   . LEU A 1 94  ? -5.068  -7.539  1.560   1.00 14.62 ? 119 LEU A O   1 
ATOM   689  C CB  . LEU A 1 94  ? -3.652  -9.738  3.328   1.00 9.78  ? 119 LEU A CB  1 
ATOM   690  C CG  . LEU A 1 94  ? -2.312  -10.458 3.215   1.00 16.81 ? 119 LEU A CG  1 
ATOM   691  C CD1 . LEU A 1 94  ? -2.426  -11.924 3.610   1.00 23.83 ? 119 LEU A CD1 1 
ATOM   692  C CD2 . LEU A 1 94  ? -1.765  -10.310 1.785   1.00 13.91 ? 119 LEU A CD2 1 
ATOM   693  N N   . ALA A 1 95  ? -5.632  -7.136  3.704   1.00 16.59 ? 120 ALA A N   1 
ATOM   694  C CA  . ALA A 1 95  ? -6.819  -6.393  3.305   1.00 15.76 ? 120 ALA A CA  1 
ATOM   695  C C   . ALA A 1 95  ? -6.419  -5.064  2.684   1.00 11.99 ? 120 ALA A C   1 
ATOM   696  O O   . ALA A 1 95  ? -6.969  -4.656  1.656   1.00 21.88 ? 120 ALA A O   1 
ATOM   697  C CB  . ALA A 1 95  ? -7.748  -6.182  4.502   1.00 17.10 ? 120 ALA A CB  1 
ATOM   698  N N   . GLU A 1 96  ? -5.480  -4.360  3.315   1.00 12.71 ? 121 GLU A N   1 
ATOM   699  C CA  . GLU A 1 96  ? -4.985  -3.112  2.739   1.00 17.84 ? 121 GLU A CA  1 
ATOM   700  C C   . GLU A 1 96  ? -4.352  -3.359  1.378   1.00 17.86 ? 121 GLU A C   1 
ATOM   701  O O   . GLU A 1 96  ? -4.525  -2.556  0.458   1.00 19.19 ? 121 GLU A O   1 
ATOM   702  C CB  . GLU A 1 96  ? -4.006  -2.432  3.695   1.00 18.04 ? 121 GLU A CB  1 
ATOM   703  C CG  . GLU A 1 96  ? -4.685  -1.821  4.910   1.00 23.43 ? 121 GLU A CG  1 
ATOM   704  C CD  . GLU A 1 96  ? -3.717  -1.107  5.828   1.00 46.59 ? 121 GLU A CD  1 
ATOM   705  O OE1 . GLU A 1 96  ? -3.447  0.106   5.655   1.00 52.72 ? 121 GLU A OE1 1 
ATOM   706  O OE2 . GLU A 1 96  ? -3.133  -1.839  6.658   1.00 33.98 ? 121 GLU A OE2 1 
ATOM   707  N N   . LEU A 1 97  ? -3.600  -4.456  1.233   1.00 11.21 ? 122 LEU A N   1 
ATOM   708  C CA  . LEU A 1 97  ? -2.964  -4.753  -0.049  1.00 18.46 ? 122 LEU A CA  1 
ATOM   709  C C   . LEU A 1 97  ? -4.012  -5.058  -1.109  1.00 17.52 ? 122 LEU A C   1 
ATOM   710  O O   . LEU A 1 97  ? -3.871  -4.644  -2.266  1.00 15.50 ? 122 LEU A O   1 
ATOM   711  C CB  . LEU A 1 97  ? -1.993  -5.920  0.104   1.00 10.20 ? 122 LEU A CB  1 
ATOM   712  C CG  . LEU A 1 97  ? -0.747  -5.592  0.922   1.00 17.79 ? 122 LEU A CG  1 
ATOM   713  C CD1 . LEU A 1 97  ? -0.132  -6.860  1.490   1.00 9.64  ? 122 LEU A CD1 1 
ATOM   714  C CD2 . LEU A 1 97  ? 0.256   -4.836  0.054   1.00 11.40 ? 122 LEU A CD2 1 
ATOM   715  N N   . SER A 1 98  ? -5.063  -5.787  -0.734  1.00 9.61  ? 123 SER A N   1 
ATOM   716  C CA  . SER A 1 98  ? -6.143  -6.078  -1.668  1.00 15.23 ? 123 SER A CA  1 
ATOM   717  C C   . SER A 1 98  ? -6.814  -4.785  -2.107  1.00 12.65 ? 123 SER A C   1 
ATOM   718  O O   . SER A 1 98  ? -7.107  -4.591  -3.292  1.00 15.80 ? 123 SER A O   1 
ATOM   719  C CB  . SER A 1 98  ? -7.147  -7.035  -1.031  1.00 10.17 ? 123 SER A CB  1 
ATOM   720  O OG  . SER A 1 98  ? -6.522  -8.266  -0.717  1.00 7.49  ? 123 SER A OG  1 
ATOM   721  N N   . ALA A 1 99  ? -7.103  -3.902  -1.148  1.00 15.34 ? 124 ALA A N   1 
ATOM   722  C CA  . ALA A 1 99  ? -7.726  -2.629  -1.488  1.00 11.38 ? 124 ALA A CA  1 
ATOM   723  C C   . ALA A 1 99  ? -6.812  -1.799  -2.380  1.00 9.83  ? 124 ALA A C   1 
ATOM   724  O O   . ALA A 1 99  ? -7.277  -1.164  -3.328  1.00 17.70 ? 124 ALA A O   1 
ATOM   725  C CB  . ALA A 1 99  ? -8.086  -1.854  -0.217  1.00 13.37 ? 124 ALA A CB  1 
ATOM   726  N N   . ALA A 1 100 ? -5.507  -1.790  -2.102  1.00 6.07  ? 125 ALA A N   1 
ATOM   727  C CA  . ALA A 1 100 ? -4.598  -1.011  -2.939  1.00 15.37 ? 125 ALA A CA  1 
ATOM   728  C C   . ALA A 1 100 ? -4.546  -1.576  -4.356  1.00 12.72 ? 125 ALA A C   1 
ATOM   729  O O   . ALA A 1 100 ? -4.630  -0.822  -5.334  1.00 14.24 ? 125 ALA A O   1 
ATOM   730  C CB  . ALA A 1 100 ? -3.201  -0.981  -2.316  1.00 10.19 ? 125 ALA A CB  1 
ATOM   731  N N   . ALA A 1 101 ? -4.518  -2.906  -4.475  1.00 10.93 ? 126 ALA A N   1 
ATOM   732  C CA  . ALA A 1 101 ? -4.482  -3.564  -5.778  1.00 15.30 ? 126 ALA A CA  1 
ATOM   733  C C   . ALA A 1 101 ? -5.760  -3.297  -6.569  1.00 12.88 ? 126 ALA A C   1 
ATOM   734  O O   . ALA A 1 101 ? -5.711  -3.008  -7.769  1.00 11.00 ? 126 ALA A O   1 
ATOM   735  C CB  . ALA A 1 101 ? -4.249  -5.067  -5.598  1.00 8.10  ? 126 ALA A CB  1 
ATOM   736  N N   . LEU A 1 102 ? -6.921  -3.405  -5.919  1.00 10.67 ? 127 LEU A N   1 
ATOM   737  C CA  . LEU A 1 102 ? -8.170  -3.276  -6.663  1.00 11.69 ? 127 LEU A CA  1 
ATOM   738  C C   . LEU A 1 102 ? -8.523  -1.820  -6.934  1.00 8.54  ? 127 LEU A C   1 
ATOM   739  O O   . LEU A 1 102 ? -8.961  -1.484  -8.040  1.00 11.00 ? 127 LEU A O   1 
ATOM   740  C CB  . LEU A 1 102 ? -9.319  -3.964  -5.928  1.00 12.76 ? 127 LEU A CB  1 
ATOM   741  C CG  . LEU A 1 102 ? -9.264  -5.484  -5.859  1.00 13.25 ? 127 LEU A CG  1 
ATOM   742  C CD1 . LEU A 1 102 ? -10.458 -6.012  -5.096  1.00 16.83 ? 127 LEU A CD1 1 
ATOM   743  C CD2 . LEU A 1 102 ? -9.244  -6.032  -7.266  1.00 11.01 ? 127 LEU A CD2 1 
ATOM   744  N N   . GLN A 1 103 ? -8.382  -0.947  -5.943  1.00 12.42 ? 128 GLN A N   1 
ATOM   745  C CA  . GLN A 1 103 ? -8.909  0.398   -6.064  1.00 11.85 ? 128 GLN A CA  1 
ATOM   746  C C   . GLN A 1 103 ? -7.884  1.364   -6.632  1.00 10.65 ? 128 GLN A C   1 
ATOM   747  O O   . GLN A 1 103 ? -8.268  2.356   -7.263  1.00 14.51 ? 128 GLN A O   1 
ATOM   748  C CB  . GLN A 1 103 ? -9.390  0.878   -4.693  1.00 13.55 ? 128 GLN A CB  1 
ATOM   749  C CG  . GLN A 1 103 ? -10.398 -0.073  -4.057  1.00 14.18 ? 128 GLN A CG  1 
ATOM   750  C CD  . GLN A 1 103 ? -11.017 0.483   -2.798  1.00 12.65 ? 128 GLN A CD  1 
ATOM   751  O OE1 . GLN A 1 103 ? -10.332 1.052   -1.954  1.00 23.70 ? 128 GLN A OE1 1 
ATOM   752  N NE2 . GLN A 1 103 ? -12.329 0.327   -2.668  1.00 21.05 ? 128 GLN A NE2 1 
ATOM   753  N N   . TYR A 1 104 ? -6.588  1.109   -6.429  1.00 11.36 ? 129 TYR A N   1 
ATOM   754  C CA  . TYR A 1 104 ? -5.555  1.974   -6.977  1.00 18.42 ? 129 TYR A CA  1 
ATOM   755  C C   . TYR A 1 104 ? -4.668  1.268   -7.987  1.00 14.12 ? 129 TYR A C   1 
ATOM   756  O O   . TYR A 1 104 ? -3.808  1.920   -8.592  1.00 16.57 ? 129 TYR A O   1 
ATOM   757  C CB  . TYR A 1 104 ? -4.672  2.555   -5.866  1.00 17.04 ? 129 TYR A CB  1 
ATOM   758  C CG  . TYR A 1 104 ? -5.415  3.415   -4.872  1.00 19.55 ? 129 TYR A CG  1 
ATOM   759  C CD1 . TYR A 1 104 ? -6.135  2.834   -3.830  1.00 14.11 ? 129 TYR A CD1 1 
ATOM   760  C CD2 . TYR A 1 104 ? -5.427  4.801   -4.989  1.00 11.41 ? 129 TYR A CD2 1 
ATOM   761  C CE1 . TYR A 1 104 ? -6.821  3.607   -2.912  1.00 20.42 ? 129 TYR A CE1 1 
ATOM   762  C CE2 . TYR A 1 104 ? -6.118  5.587   -4.068  1.00 23.99 ? 129 TYR A CE2 1 
ATOM   763  C CZ  . TYR A 1 104 ? -6.811  4.980   -3.034  1.00 12.85 ? 129 TYR A CZ  1 
ATOM   764  O OH  . TYR A 1 104 ? -7.502  5.738   -2.119  1.00 16.94 ? 129 TYR A OH  1 
ATOM   765  N N   . SER A 1 105 ? -4.859  -0.035  -8.192  1.00 8.07  ? 130 SER A N   1 
ATOM   766  C CA  . SER A 1 105 ? -4.072  -0.818  -9.140  1.00 16.91 ? 130 SER A CA  1 
ATOM   767  C C   . SER A 1 105 ? -2.581  -0.728  -8.804  1.00 14.19 ? 130 SER A C   1 
ATOM   768  O O   . SER A 1 105 ? -1.733  -0.505  -9.669  1.00 21.26 ? 130 SER A O   1 
ATOM   769  C CB  . SER A 1 105 ? -4.351  -0.385  -10.583 1.00 15.50 ? 130 SER A CB  1 
ATOM   770  O OG  . SER A 1 105 ? -4.113  -1.442  -11.489 1.00 12.42 ? 130 SER A OG  1 
ATOM   771  N N   . ASP A 1 106 ? -2.276  -0.880  -7.515  1.00 12.17 ? 131 ASP A N   1 
ATOM   772  C CA  . ASP A 1 106 ? -0.900  -0.911  -7.022  1.00 22.38 ? 131 ASP A CA  1 
ATOM   773  C C   . ASP A 1 106 ? -0.247  -2.250  -7.374  1.00 20.28 ? 131 ASP A C   1 
ATOM   774  O O   . ASP A 1 106 ? -0.745  -3.306  -6.971  1.00 21.12 ? 131 ASP A O   1 
ATOM   775  C CB  . ASP A 1 106 ? -0.883  -0.672  -5.512  1.00 21.64 ? 131 ASP A CB  1 
ATOM   776  C CG  . ASP A 1 106 ? 0.518   -0.420  -4.972  1.00 27.49 ? 131 ASP A CG  1 
ATOM   777  O OD1 . ASP A 1 106 ? 1.400   -1.285  -5.170  1.00 20.71 ? 131 ASP A OD1 1 
ATOM   778  O OD2 . ASP A 1 106 ? 0.736   0.650   -4.360  1.00 26.74 ? 131 ASP A OD2 1 
ATOM   779  N N   . ASN A 1 107 ? 0.867   -2.221  -8.119  1.00 15.20 ? 132 ASN A N   1 
ATOM   780  C CA  . ASN A 1 107 ? 1.467   -3.478  -8.570  1.00 10.69 ? 132 ASN A CA  1 
ATOM   781  C C   . ASN A 1 107 ? 2.278   -4.185  -7.485  1.00 14.52 ? 132 ASN A C   1 
ATOM   782  O O   . ASN A 1 107 ? 2.361   -5.419  -7.497  1.00 16.68 ? 132 ASN A O   1 
ATOM   783  C CB  . ASN A 1 107 ? 2.382   -3.242  -9.773  1.00 13.52 ? 132 ASN A CB  1 
ATOM   784  C CG  . ASN A 1 107 ? 1.640   -3.216  -11.083 1.00 12.05 ? 132 ASN A CG  1 
ATOM   785  O OD1 . ASN A 1 107 ? 0.486   -3.622  -11.161 1.00 18.15 ? 132 ASN A OD1 1 
ATOM   786  N ND2 . ASN A 1 107 ? 2.314   -2.768  -12.135 1.00 18.89 ? 132 ASN A ND2 1 
ATOM   787  N N   . THR A 1 108 ? 2.861   -3.450  -6.535  1.00 14.16 ? 133 THR A N   1 
ATOM   788  C CA  . THR A 1 108 ? 3.514   -4.121  -5.412  1.00 16.04 ? 133 THR A CA  1 
ATOM   789  C C   . THR A 1 108 ? 2.477   -4.845  -4.567  1.00 13.83 ? 133 THR A C   1 
ATOM   790  O O   . THR A 1 108 ? 2.714   -5.967  -4.100  1.00 19.82 ? 133 THR A O   1 
ATOM   791  C CB  . THR A 1 108 ? 4.316   -3.122  -4.578  1.00 20.94 ? 133 THR A CB  1 
ATOM   792  O OG1 . THR A 1 108 ? 5.344   -2.538  -5.386  1.00 20.18 ? 133 THR A OG1 1 
ATOM   793  C CG2 . THR A 1 108 ? 4.970   -3.815  -3.395  1.00 24.53 ? 133 THR A CG2 1 
ATOM   794  N N   . ALA A 1 109 ? 1.321   -4.214  -4.360  1.00 13.55 ? 134 ALA A N   1 
ATOM   795  C CA  . ALA A 1 109 ? 0.248   -4.877  -3.637  1.00 16.50 ? 134 ALA A CA  1 
ATOM   796  C C   . ALA A 1 109 ? -0.186  -6.134  -4.379  1.00 19.37 ? 134 ALA A C   1 
ATOM   797  O O   . ALA A 1 109 ? -0.465  -7.165  -3.753  1.00 17.40 ? 134 ALA A O   1 
ATOM   798  C CB  . ALA A 1 109 ? -0.930  -3.922  -3.456  1.00 12.72 ? 134 ALA A CB  1 
ATOM   799  N N   . MET A 1 110 ? -0.290  -6.058  -5.714  1.00 13.55 ? 135 MET A N   1 
ATOM   800  C CA  . MET A 1 110 ? -0.650  -7.248  -6.478  1.00 15.53 ? 135 MET A CA  1 
ATOM   801  C C   . MET A 1 110 ? 0.392   -8.349  -6.271  1.00 14.23 ? 135 MET A C   1 
ATOM   802  O O   . MET A 1 110 ? 0.050   -9.531  -6.129  1.00 11.80 ? 135 MET A O   1 
ATOM   803  C CB  . MET A 1 110 ? -0.751  -6.908  -7.970  1.00 16.18 ? 135 MET A CB  1 
ATOM   804  C CG  . MET A 1 110 ? -0.914  -8.137  -8.880  1.00 15.63 ? 135 MET A CG  1 
ATOM   805  S SD  . MET A 1 110 ? -2.190  -9.296  -8.377  1.00 22.69 ? 135 MET A SD  1 
ATOM   806  C CE  . MET A 1 110 ? -2.627  -9.986  -9.970  1.00 9.39  ? 135 MET A CE  1 
ATOM   807  N N   . ASN A 1 111 ? 1.679   -7.982  -6.268  1.00 14.64 ? 136 ASN A N   1 
ATOM   808  C CA  . ASN A 1 111 ? 2.714   -8.994  -6.064  1.00 11.04 ? 136 ASN A CA  1 
ATOM   809  C C   . ASN A 1 111 ? 2.633   -9.606  -4.677  1.00 9.30  ? 136 ASN A C   1 
ATOM   810  O O   . ASN A 1 111 ? 2.885   -10.802 -4.515  1.00 8.43  ? 136 ASN A O   1 
ATOM   811  C CB  . ASN A 1 111 ? 4.097   -8.408  -6.308  1.00 11.21 ? 136 ASN A CB  1 
ATOM   812  C CG  . ASN A 1 111 ? 4.469   -8.402  -7.774  1.00 14.56 ? 136 ASN A CG  1 
ATOM   813  O OD1 . ASN A 1 111 ? 3.786   -8.999  -8.611  1.00 12.60 ? 136 ASN A OD1 1 
ATOM   814  N ND2 . ASN A 1 111 ? 5.575   -7.742  -8.092  1.00 21.28 ? 136 ASN A ND2 1 
ATOM   815  N N   . LYS A 1 112 ? 2.217   -8.819  -3.683  1.00 19.47 ? 137 LYS A N   1 
ATOM   816  C CA  . LYS A 1 112 ? 2.028   -9.383  -2.352  1.00 17.58 ? 137 LYS A CA  1 
ATOM   817  C C   . LYS A 1 112 ? 0.851   -10.350 -2.336  1.00 13.15 ? 137 LYS A C   1 
ATOM   818  O O   . LYS A 1 112 ? 0.916   -11.406 -1.692  1.00 15.18 ? 137 LYS A O   1 
ATOM   819  C CB  . LYS A 1 112 ? 1.811   -8.266  -1.326  1.00 17.75 ? 137 LYS A CB  1 
ATOM   820  C CG  . LYS A 1 112 ? 3.037   -7.401  -1.006  1.00 20.42 ? 137 LYS A CG  1 
ATOM   821  C CD  . LYS A 1 112 ? 4.329   -8.193  -0.913  1.00 16.46 ? 137 LYS A CD  1 
ATOM   822  C CE  . LYS A 1 112 ? 5.519   -7.245  -0.774  1.00 21.73 ? 137 LYS A CE  1 
ATOM   823  N NZ  . LYS A 1 112 ? 6.720   -7.906  -0.178  1.00 21.76 ? 137 LYS A NZ  1 
ATOM   824  N N   . LEU A 1 113 ? -0.226  -10.016 -3.053  1.00 10.82 ? 138 LEU A N   1 
ATOM   825  C CA  . LEU A 1 113 ? -1.344  -10.951 -3.167  1.00 15.58 ? 138 LEU A CA  1 
ATOM   826  C C   . LEU A 1 113 ? -0.907  -12.242 -3.854  1.00 19.57 ? 138 LEU A C   1 
ATOM   827  O O   . LEU A 1 113 ? -1.224  -13.345 -3.396  1.00 20.75 ? 138 LEU A O   1 
ATOM   828  C CB  . LEU A 1 113 ? -2.508  -10.312 -3.927  1.00 18.29 ? 138 LEU A CB  1 
ATOM   829  C CG  . LEU A 1 113 ? -3.130  -9.024  -3.381  1.00 21.06 ? 138 LEU A CG  1 
ATOM   830  C CD1 . LEU A 1 113 ? -4.244  -8.557  -4.293  1.00 14.78 ? 138 LEU A CD1 1 
ATOM   831  C CD2 . LEU A 1 113 ? -3.641  -9.204  -1.956  1.00 19.60 ? 138 LEU A CD2 1 
ATOM   832  N N   . ILE A 1 114 ? -0.180  -12.115 -4.966  1.00 10.03 ? 139 ILE A N   1 
ATOM   833  C CA  . ILE A 1 114 ? 0.303   -13.281 -5.697  1.00 13.59 ? 139 ILE A CA  1 
ATOM   834  C C   . ILE A 1 114 ? 1.167   -14.149 -4.794  1.00 16.82 ? 139 ILE A C   1 
ATOM   835  O O   . ILE A 1 114 ? 1.012   -15.375 -4.757  1.00 18.87 ? 139 ILE A O   1 
ATOM   836  C CB  . ILE A 1 114 ? 1.052   -12.839 -6.970  1.00 23.01 ? 139 ILE A CB  1 
ATOM   837  C CG1 . ILE A 1 114 ? 0.083   -12.176 -7.958  1.00 17.00 ? 139 ILE A CG1 1 
ATOM   838  C CG2 . ILE A 1 114 ? 1.820   -13.999 -7.595  1.00 20.20 ? 139 ILE A CG2 1 
ATOM   839  C CD1 . ILE A 1 114 ? 0.767   -11.534 -9.158  1.00 15.70 ? 139 ILE A CD1 1 
ATOM   840  N N   . ALA A 1 115 ? 2.075   -13.527 -4.035  1.00 10.97 ? 140 ALA A N   1 
ATOM   841  C CA  . ALA A 1 115 ? 2.965   -14.294 -3.173  1.00 18.04 ? 140 ALA A CA  1 
ATOM   842  C C   . ALA A 1 115 ? 2.171   -14.983 -2.075  1.00 17.97 ? 140 ALA A C   1 
ATOM   843  O O   . ALA A 1 115 ? 2.494   -16.108 -1.673  1.00 14.18 ? 140 ALA A O   1 
ATOM   844  C CB  . ALA A 1 115 ? 4.040   -13.387 -2.571  1.00 14.62 ? 140 ALA A CB  1 
ATOM   845  N N   . GLN A 1 116 ? 1.122   -14.321 -1.582  1.00 11.13 ? 141 GLN A N   1 
ATOM   846  C CA  . GLN A 1 116 ? 0.275   -14.929 -0.567  1.00 16.17 ? 141 GLN A CA  1 
ATOM   847  C C   . GLN A 1 116 ? -0.425  -16.179 -1.094  1.00 12.79 ? 141 GLN A C   1 
ATOM   848  O O   . GLN A 1 116 ? -0.748  -17.081 -0.313  1.00 15.99 ? 141 GLN A O   1 
ATOM   849  C CB  . GLN A 1 116 ? -0.752  -13.898 -0.087  1.00 12.09 ? 141 GLN A CB  1 
ATOM   850  C CG  . GLN A 1 116 ? -1.871  -14.467 0.767   1.00 11.25 ? 141 GLN A CG  1 
ATOM   851  C CD  . GLN A 1 116 ? -1.353  -15.145 2.019   1.00 14.45 ? 141 GLN A CD  1 
ATOM   852  O OE1 . GLN A 1 116 ? -0.285  -14.796 2.536   1.00 13.90 ? 141 GLN A OE1 1 
ATOM   853  N NE2 . GLN A 1 116 ? -2.092  -16.134 2.502   1.00 14.54 ? 141 GLN A NE2 1 
ATOM   854  N N   . LEU A 1 117 ? -0.591  -16.288 -2.405  1.00 11.23 ? 142 LEU A N   1 
ATOM   855  C CA  . LEU A 1 117 ? -1.219  -17.449 -3.015  1.00 14.94 ? 142 LEU A CA  1 
ATOM   856  C C   . LEU A 1 117 ? -0.204  -18.461 -3.517  1.00 13.92 ? 142 LEU A C   1 
ATOM   857  O O   . LEU A 1 117 ? -0.596  -19.453 -4.137  1.00 24.30 ? 142 LEU A O   1 
ATOM   858  C CB  . LEU A 1 117 ? -2.116  -16.997 -4.170  1.00 10.90 ? 142 LEU A CB  1 
ATOM   859  C CG  . LEU A 1 117 ? -3.196  -16.022 -3.695  1.00 24.05 ? 142 LEU A CG  1 
ATOM   860  C CD1 . LEU A 1 117 ? -3.793  -15.268 -4.867  1.00 10.15 ? 142 LEU A CD1 1 
ATOM   861  C CD2 . LEU A 1 117 ? -4.274  -16.752 -2.897  1.00 6.29  ? 142 LEU A CD2 1 
ATOM   862  N N   . GLY A 1 118 ? 1.085   -18.236 -3.271  1.00 18.32 ? 143 GLY A N   1 
ATOM   863  C CA  . GLY A 1 118 ? 2.102   -19.175 -3.691  1.00 9.16  ? 143 GLY A CA  1 
ATOM   864  C C   . GLY A 1 118 ? 2.593   -18.955 -5.097  1.00 17.52 ? 143 GLY A C   1 
ATOM   865  O O   . GLY A 1 118 ? 3.168   -19.877 -5.687  1.00 16.94 ? 143 GLY A O   1 
ATOM   866  N N   . GLY A 1 119 ? 2.396   -17.762 -5.654  1.00 15.89 ? 144 GLY A N   1 
ATOM   867  C CA  . GLY A 1 119 ? 2.854   -17.481 -6.990  1.00 11.33 ? 144 GLY A CA  1 
ATOM   868  C C   . GLY A 1 119 ? 1.677   -17.422 -7.943  1.00 19.80 ? 144 GLY A C   1 
ATOM   869  O O   . GLY A 1 119 ? 0.532   -17.694 -7.570  1.00 16.82 ? 144 GLY A O   1 
ATOM   870  N N   . PRO A 1 120 ? 1.941   -17.050 -9.198  1.00 18.09 ? 145 PRO A N   1 
ATOM   871  C CA  . PRO A 1 120 ? 0.850   -16.924 -10.184 1.00 21.56 ? 145 PRO A CA  1 
ATOM   872  C C   . PRO A 1 120 ? 0.012   -18.185 -10.293 1.00 21.27 ? 145 PRO A C   1 
ATOM   873  O O   . PRO A 1 120 ? -1.216  -18.117 -10.477 1.00 27.03 ? 145 PRO A O   1 
ATOM   874  C CB  . PRO A 1 120 ? 1.601   -16.619 -11.488 1.00 18.15 ? 145 PRO A CB  1 
ATOM   875  C CG  . PRO A 1 120 ? 2.864   -15.936 -11.029 1.00 23.25 ? 145 PRO A CG  1 
ATOM   876  C CD  . PRO A 1 120 ? 3.249   -16.672 -9.765  1.00 11.47 ? 145 PRO A CD  1 
ATOM   877  N N   . GLY A 1 121 ? 0.656   -19.348 -10.188 1.00 21.38 ? 146 GLY A N   1 
ATOM   878  C CA  . GLY A 1 121 ? -0.084  -20.591 -10.240 1.00 17.85 ? 146 GLY A CA  1 
ATOM   879  C C   . GLY A 1 121 ? -1.122  -20.715 -9.142  1.00 16.25 ? 146 GLY A C   1 
ATOM   880  O O   . GLY A 1 121 ? -2.114  -21.417 -9.313  1.00 23.15 ? 146 GLY A O   1 
ATOM   881  N N   . GLY A 1 122 ? -0.927  -20.039 -8.009  1.00 21.31 ? 147 GLY A N   1 
ATOM   882  C CA  . GLY A 1 122 ? -1.965  -20.068 -6.988  1.00 12.85 ? 147 GLY A CA  1 
ATOM   883  C C   . GLY A 1 122 ? -3.205  -19.283 -7.378  1.00 17.09 ? 147 GLY A C   1 
ATOM   884  O O   . GLY A 1 122 ? -4.332  -19.705 -7.088  1.00 17.44 ? 147 GLY A O   1 
ATOM   885  N N   . VAL A 1 123 ? -3.028  -18.192 -8.129  1.00 15.70 ? 148 VAL A N   1 
ATOM   886  C CA  . VAL A 1 123 ? -4.177  -17.475 -8.674  1.00 14.90 ? 148 VAL A CA  1 
ATOM   887  C C   . VAL A 1 123 ? -4.881  -18.325 -9.721  1.00 16.25 ? 148 VAL A C   1 
ATOM   888  O O   . VAL A 1 123 ? -6.117  -18.422 -9.745  1.00 18.53 ? 148 VAL A O   1 
ATOM   889  C CB  . VAL A 1 123 ? -3.733  -16.125 -9.267  1.00 19.51 ? 148 VAL A CB  1 
ATOM   890  C CG1 . VAL A 1 123 ? -4.940  -15.315 -9.721  1.00 13.21 ? 148 VAL A CG1 1 
ATOM   891  C CG2 . VAL A 1 123 ? -2.895  -15.339 -8.263  1.00 18.52 ? 148 VAL A CG2 1 
ATOM   892  N N   . THR A 1 124 ? -4.107  -18.931 -10.624 1.00 18.65 ? 149 THR A N   1 
ATOM   893  C CA  . THR A 1 124 ? -4.711  -19.834 -11.600 1.00 23.91 ? 149 THR A CA  1 
ATOM   894  C C   . THR A 1 124 ? -5.445  -20.983 -10.915 1.00 10.33 ? 149 THR A C   1 
ATOM   895  O O   . THR A 1 124 ? -6.523  -21.394 -11.359 1.00 23.03 ? 149 THR A O   1 
ATOM   896  C CB  . THR A 1 124 ? -3.658  -20.351 -12.580 1.00 11.51 ? 149 THR A CB  1 
ATOM   897  O OG1 . THR A 1 124 ? -2.972  -19.238 -13.165 1.00 12.94 ? 149 THR A OG1 1 
ATOM   898  C CG2 . THR A 1 124 ? -4.310  -21.158 -13.682 1.00 11.04 ? 149 THR A CG2 1 
ATOM   899  N N   . ALA A 1 125 ? -4.861  -21.535 -9.850  1.00 12.25 ? 150 ALA A N   1 
ATOM   900  C CA  . ALA A 1 125 ? -5.504  -22.632 -9.142  1.00 16.77 ? 150 ALA A CA  1 
ATOM   901  C C   . ALA A 1 125 ? -6.825  -22.193 -8.534  1.00 17.15 ? 150 ALA A C   1 
ATOM   902  O O   . ALA A 1 125 ? -7.806  -22.944 -8.556  1.00 20.83 ? 150 ALA A O   1 
ATOM   903  C CB  . ALA A 1 125 ? -4.567  -23.177 -8.064  1.00 17.08 ? 150 ALA A CB  1 
ATOM   904  N N   . PHE A 1 126 ? -6.873  -20.981 -7.977  1.00 16.93 ? 151 PHE A N   1 
ATOM   905  C CA  . PHE A 1 126 ? -8.152  -20.477 -7.486  1.00 11.98 ? 151 PHE A CA  1 
ATOM   906  C C   . PHE A 1 126 ? -9.165  -20.345 -8.618  1.00 16.33 ? 151 PHE A C   1 
ATOM   907  O O   . PHE A 1 126 ? -10.341 -20.709 -8.459  1.00 23.66 ? 151 PHE A O   1 
ATOM   908  C CB  . PHE A 1 126 ? -7.982  -19.143 -6.770  1.00 12.92 ? 151 PHE A CB  1 
ATOM   909  C CG  . PHE A 1 126 ? -9.291  -18.490 -6.437  1.00 19.70 ? 151 PHE A CG  1 
ATOM   910  C CD1 . PHE A 1 126 ? -10.087 -18.991 -5.420  1.00 8.79  ? 151 PHE A CD1 1 
ATOM   911  C CD2 . PHE A 1 126 ? -9.732  -17.382 -7.145  1.00 15.26 ? 151 PHE A CD2 1 
ATOM   912  C CE1 . PHE A 1 126 ? -11.305 -18.403 -5.124  1.00 12.59 ? 151 PHE A CE1 1 
ATOM   913  C CE2 . PHE A 1 126 ? -10.939 -16.785 -6.838  1.00 12.63 ? 151 PHE A CE2 1 
ATOM   914  C CZ  . PHE A 1 126 ? -11.724 -17.295 -5.829  1.00 12.19 ? 151 PHE A CZ  1 
ATOM   915  N N   . ALA A 1 127 ? -8.731  -19.805 -9.762  1.00 15.45 ? 152 ALA A N   1 
ATOM   916  C CA  . ALA A 1 127 ? -9.621  -19.709 -10.915 1.00 18.24 ? 152 ALA A CA  1 
ATOM   917  C C   . ALA A 1 127 ? -10.209 -21.067 -11.260 1.00 18.24 ? 152 ALA A C   1 
ATOM   918  O O   . ALA A 1 127 ? -11.413 -21.193 -11.512 1.00 21.27 ? 152 ALA A O   1 
ATOM   919  C CB  . ALA A 1 127 ? -8.869  -19.138 -12.118 1.00 16.27 ? 152 ALA A CB  1 
ATOM   920  N N   . ARG A 1 128 ? -9.362  -22.096 -11.300 1.00 16.85 ? 153 ARG A N   1 
ATOM   921  C CA  . ARG A 1 128 ? -9.854  -23.438 -11.588 1.00 16.68 ? 153 ARG A CA  1 
ATOM   922  C C   . ARG A 1 128 ? -10.832 -23.889 -10.512 1.00 18.38 ? 153 ARG A C   1 
ATOM   923  O O   . ARG A 1 128 ? -11.851 -24.524 -10.808 1.00 23.69 ? 153 ARG A O   1 
ATOM   924  C CB  . ARG A 1 128 ? -8.685  -24.413 -11.694 1.00 22.38 ? 153 ARG A CB  1 
ATOM   925  C CG  . ARG A 1 128 ? -7.762  -24.087 -12.852 1.00 18.98 ? 153 ARG A CG  1 
ATOM   926  C CD  . ARG A 1 128 ? -8.426  -24.255 -14.207 1.00 15.62 ? 153 ARG A CD  1 
ATOM   927  N NE  . ARG A 1 128 ? -7.490  -23.899 -15.267 1.00 14.50 ? 153 ARG A NE  1 
ATOM   928  C CZ  . ARG A 1 128 ? -7.237  -22.652 -15.639 1.00 19.52 ? 153 ARG A CZ  1 
ATOM   929  N NH1 . ARG A 1 128 ? -7.935  -21.635 -15.158 1.00 18.76 ? 153 ARG A NH1 1 
ATOM   930  N NH2 . ARG A 1 128 ? -6.286  -22.421 -16.541 1.00 10.54 ? 153 ARG A NH2 1 
ATOM   931  N N   . ALA A 1 129 ? -10.530 -23.569 -9.250  1.00 19.64 ? 154 ALA A N   1 
ATOM   932  C CA  . ALA A 1 129 ? -11.366 -24.003 -8.140  1.00 16.70 ? 154 ALA A CA  1 
ATOM   933  C C   . ALA A 1 129 ? -12.749 -23.363 -8.148  1.00 26.13 ? 154 ALA A C   1 
ATOM   934  O O   . ALA A 1 129 ? -13.674 -23.927 -7.555  1.00 27.66 ? 154 ALA A O   1 
ATOM   935  C CB  . ALA A 1 129 ? -10.667 -23.702 -6.816  1.00 15.41 ? 154 ALA A CB  1 
ATOM   936  N N   . ILE A 1 130 ? -12.921 -22.205 -8.789  1.00 19.13 ? 155 ILE A N   1 
ATOM   937  C CA  . ILE A 1 130 ? -14.249 -21.599 -8.877  1.00 18.00 ? 155 ILE A CA  1 
ATOM   938  C C   . ILE A 1 130 ? -14.890 -21.818 -10.245 1.00 24.61 ? 155 ILE A C   1 
ATOM   939  O O   . ILE A 1 130 ? -15.889 -21.167 -10.567 1.00 32.06 ? 155 ILE A O   1 
ATOM   940  C CB  . ILE A 1 130 ? -14.226 -20.104 -8.522  1.00 23.54 ? 155 ILE A CB  1 
ATOM   941  C CG1 . ILE A 1 130 ? -13.372 -19.314 -9.509  1.00 20.07 ? 155 ILE A CG1 1 
ATOM   942  C CG2 . ILE A 1 130 ? -13.725 -19.910 -7.104  1.00 19.14 ? 155 ILE A CG2 1 
ATOM   943  C CD1 . ILE A 1 130 ? -13.615 -17.821 -9.436  1.00 20.11 ? 155 ILE A CD1 1 
ATOM   944  N N   . GLY A 1 131 ? -14.356 -22.735 -11.046 1.00 25.10 ? 156 GLY A N   1 
ATOM   945  C CA  . GLY A 1 131 ? -14.986 -23.127 -12.290 1.00 26.80 ? 156 GLY A CA  1 
ATOM   946  C C   . GLY A 1 131 ? -14.518 -22.392 -13.525 1.00 25.08 ? 156 GLY A C   1 
ATOM   947  O O   . GLY A 1 131 ? -15.133 -22.547 -14.585 1.00 34.35 ? 156 GLY A O   1 
ATOM   948  N N   . ASP A 1 132 ? -13.464 -21.587 -13.428 1.00 27.82 ? 157 ASP A N   1 
ATOM   949  C CA  . ASP A 1 132 ? -12.926 -20.870 -14.581 1.00 23.94 ? 157 ASP A CA  1 
ATOM   950  C C   . ASP A 1 132 ? -11.814 -21.719 -15.191 1.00 20.79 ? 157 ASP A C   1 
ATOM   951  O O   . ASP A 1 132 ? -10.742 -21.876 -14.596 1.00 21.06 ? 157 ASP A O   1 
ATOM   952  C CB  . ASP A 1 132 ? -12.406 -19.492 -14.180 1.00 17.97 ? 157 ASP A CB  1 
ATOM   953  C CG  . ASP A 1 132 ? -12.039 -18.622 -15.388 1.00 30.63 ? 157 ASP A CG  1 
ATOM   954  O OD1 . ASP A 1 132 ? -12.261 -17.395 -15.316 1.00 27.59 ? 157 ASP A OD1 1 
ATOM   955  O OD2 . ASP A 1 132 ? -11.531 -19.150 -16.404 1.00 21.09 ? 157 ASP A OD2 1 
ATOM   956  N N   . GLU A 1 133 ? -12.055 -22.236 -16.389 1.00 22.12 ? 158 GLU A N   1 
ATOM   957  C CA  . GLU A 1 133 ? -11.104 -23.117 -17.049 1.00 22.73 ? 158 GLU A CA  1 
ATOM   958  C C   . GLU A 1 133 ? -10.147 -22.388 -17.980 1.00 24.99 ? 158 GLU A C   1 
ATOM   959  O O   . GLU A 1 133 ? -9.140  -22.976 -18.391 1.00 26.72 ? 158 GLU A O   1 
ATOM   960  C CB  . GLU A 1 133 ? -11.855 -24.182 -17.847 1.00 32.53 ? 158 GLU A CB  1 
ATOM   961  C CG  . GLU A 1 133 ? -12.986 -24.879 -17.110 1.00 40.19 ? 158 GLU A CG  1 
ATOM   962  C CD  . GLU A 1 133 ? -12.503 -25.718 -15.945 1.00 53.08 ? 158 GLU A CD  1 
ATOM   963  O OE1 . GLU A 1 133 ? -11.300 -26.060 -15.917 1.00 50.26 ? 158 GLU A OE1 1 
ATOM   964  O OE2 . GLU A 1 133 ? -13.329 -26.044 -15.063 1.00 45.48 ? 158 GLU A OE2 1 
ATOM   965  N N   . THR A 1 134 ? -10.433 -21.131 -18.317 1.00 15.79 ? 159 THR A N   1 
ATOM   966  C CA  . THR A 1 134 ? -9.714  -20.371 -19.332 1.00 14.84 ? 159 THR A CA  1 
ATOM   967  C C   . THR A 1 134 ? -8.624  -19.472 -18.757 1.00 16.77 ? 159 THR A C   1 
ATOM   968  O O   . THR A 1 134 ? -7.527  -19.402 -19.320 1.00 16.73 ? 159 THR A O   1 
ATOM   969  C CB  . THR A 1 134 ? -10.701 -19.532 -20.143 1.00 17.10 ? 159 THR A CB  1 
ATOM   970  O OG1 . THR A 1 134 ? -11.736 -20.381 -20.659 1.00 22.91 ? 159 THR A OG1 1 
ATOM   971  C CG2 . THR A 1 134 ? -10.000 -18.861 -21.302 1.00 23.39 ? 159 THR A CG2 1 
ATOM   972  N N   . PHE A 1 135 ? -8.920  -18.768 -17.665 1.00 19.34 ? 160 PHE A N   1 
ATOM   973  C CA  . PHE A 1 135 ? -7.971  -17.873 -17.007 1.00 15.45 ? 160 PHE A CA  1 
ATOM   974  C C   . PHE A 1 135 ? -6.641  -18.563 -16.746 1.00 12.39 ? 160 PHE A C   1 
ATOM   975  O O   . PHE A 1 135 ? -6.601  -19.704 -16.279 1.00 23.12 ? 160 PHE A O   1 
ATOM   976  C CB  . PHE A 1 135 ? -8.588  -17.404 -15.685 1.00 13.30 ? 160 PHE A CB  1 
ATOM   977  C CG  . PHE A 1 135 ? -7.676  -16.578 -14.813 1.00 13.79 ? 160 PHE A CG  1 
ATOM   978  C CD1 . PHE A 1 135 ? -6.728  -17.183 -13.997 1.00 18.27 ? 160 PHE A CD1 1 
ATOM   979  C CD2 . PHE A 1 135 ? -7.820  -15.199 -14.751 1.00 13.61 ? 160 PHE A CD2 1 
ATOM   980  C CE1 . PHE A 1 135 ? -5.907  -16.423 -13.173 1.00 19.47 ? 160 PHE A CE1 1 
ATOM   981  C CE2 . PHE A 1 135 ? -7.009  -14.431 -13.921 1.00 14.23 ? 160 PHE A CE2 1 
ATOM   982  C CZ  . PHE A 1 135 ? -6.051  -15.040 -13.138 1.00 15.21 ? 160 PHE A CZ  1 
ATOM   983  N N   . ARG A 1 136 ? -5.549  -17.871 -17.068 1.00 10.08 ? 161 ARG A N   1 
ATOM   984  C CA  . ARG A 1 136 ? -4.225  -18.271 -16.608 1.00 13.03 ? 161 ARG A CA  1 
ATOM   985  C C   . ARG A 1 136 ? -3.405  -17.050 -16.225 1.00 19.37 ? 161 ARG A C   1 
ATOM   986  O O   . ARG A 1 136 ? -3.302  -16.094 -17.000 1.00 17.91 ? 161 ARG A O   1 
ATOM   987  C CB  . ARG A 1 136 ? -3.498  -19.082 -17.678 1.00 9.14  ? 161 ARG A CB  1 
ATOM   988  C CG  . ARG A 1 136 ? -3.444  -18.420 -19.037 1.00 12.88 ? 161 ARG A CG  1 
ATOM   989  C CD  . ARG A 1 136 ? -2.795  -19.359 -20.016 1.00 15.61 ? 161 ARG A CD  1 
ATOM   990  N NE  . ARG A 1 136 ? -1.372  -19.493 -19.730 1.00 20.83 ? 161 ARG A NE  1 
ATOM   991  C CZ  . ARG A 1 136 ? -0.551  -20.290 -20.395 1.00 12.79 ? 161 ARG A CZ  1 
ATOM   992  N NH1 . ARG A 1 136 ? -0.986  -21.068 -21.375 1.00 16.61 ? 161 ARG A NH1 1 
ATOM   993  N NH2 . ARG A 1 136 ? 0.734   -20.317 -20.060 1.00 15.45 ? 161 ARG A NH2 1 
ATOM   994  N N   . LEU A 1 137 ? -2.836  -17.084 -15.028 1.00 12.27 ? 162 LEU A N   1 
ATOM   995  C CA  . LEU A 1 137 ? -1.865  -16.098 -14.580 1.00 15.97 ? 162 LEU A CA  1 
ATOM   996  C C   . LEU A 1 137 ? -0.511  -16.783 -14.519 1.00 21.13 ? 162 LEU A C   1 
ATOM   997  O O   . LEU A 1 137 ? -0.373  -17.833 -13.882 1.00 21.19 ? 162 LEU A O   1 
ATOM   998  C CB  . LEU A 1 137 ? -2.243  -15.505 -13.223 1.00 17.55 ? 162 LEU A CB  1 
ATOM   999  C CG  . LEU A 1 137 ? -1.551  -14.181 -12.878 1.00 19.37 ? 162 LEU A CG  1 
ATOM   1000 C CD1 . LEU A 1 137 ? -2.026  -13.055 -13.782 1.00 16.85 ? 162 LEU A CD1 1 
ATOM   1001 C CD2 . LEU A 1 137 ? -1.797  -13.822 -11.421 1.00 23.19 ? 162 LEU A CD2 1 
ATOM   1002 N N   . ASP A 1 138 ? 0.473   -16.209 -15.191 1.00 15.79 ? 163 ASP A N   1 
ATOM   1003 C CA  . ASP A 1 138 ? 1.739   -16.893 -15.385 1.00 19.35 ? 163 ASP A CA  1 
ATOM   1004 C C   . ASP A 1 138 ? 2.915   -16.168 -14.762 1.00 21.36 ? 163 ASP A C   1 
ATOM   1005 O O   . ASP A 1 138 ? 3.890   -16.818 -14.376 1.00 24.96 ? 163 ASP A O   1 
ATOM   1006 C CB  . ASP A 1 138 ? 2.009   -17.078 -16.884 1.00 16.81 ? 163 ASP A CB  1 
ATOM   1007 C CG  . ASP A 1 138 ? 1.036   -18.037 -17.529 1.00 29.92 ? 163 ASP A CG  1 
ATOM   1008 O OD1 . ASP A 1 138 ? -0.165  -17.686 -17.614 1.00 25.02 ? 163 ASP A OD1 1 
ATOM   1009 O OD2 . ASP A 1 138 ? 1.459   -19.142 -17.934 1.00 29.33 ? 163 ASP A OD2 1 
ATOM   1010 N N   . ARG A 1 139 ? 2.851   -14.847 -14.655 1.00 15.49 ? 164 ARG A N   1 
ATOM   1011 C CA  . ARG A 1 139 ? 3.955   -14.031 -14.186 1.00 13.07 ? 164 ARG A CA  1 
ATOM   1012 C C   . ARG A 1 139 ? 3.447   -13.071 -13.120 1.00 18.90 ? 164 ARG A C   1 
ATOM   1013 O O   . ARG A 1 139 ? 2.242   -12.895 -12.927 1.00 21.39 ? 164 ARG A O   1 
ATOM   1014 C CB  . ARG A 1 139 ? 4.617   -13.288 -15.353 1.00 12.16 ? 164 ARG A CB  1 
ATOM   1015 C CG  . ARG A 1 139 ? 5.388   -14.220 -16.265 1.00 17.58 ? 164 ARG A CG  1 
ATOM   1016 C CD  . ARG A 1 139 ? 5.788   -13.528 -17.543 1.00 17.62 ? 164 ARG A CD  1 
ATOM   1017 N NE  . ARG A 1 139 ? 4.592   -13.212 -18.315 1.00 17.78 ? 164 ARG A NE  1 
ATOM   1018 C CZ  . ARG A 1 139 ? 4.576   -12.480 -19.420 1.00 21.07 ? 164 ARG A CZ  1 
ATOM   1019 N NH1 . ARG A 1 139 ? 5.690   -12.002 -19.948 1.00 18.72 ? 164 ARG A NH1 1 
ATOM   1020 N NH2 . ARG A 1 139 ? 3.412   -12.226 -20.010 1.00 19.27 ? 164 ARG A NH2 1 
ATOM   1021 N N   . THR A 1 140 ? 4.388   -12.447 -12.427 1.00 16.74 ? 165 THR A N   1 
ATOM   1022 C CA  . THR A 1 140 ? 4.087   -11.397 -11.474 1.00 20.74 ? 165 THR A CA  1 
ATOM   1023 C C   . THR A 1 140 ? 4.103   -10.037 -12.169 1.00 18.48 ? 165 THR A C   1 
ATOM   1024 O O   . THR A 1 140 ? 4.327   -9.927  -13.377 1.00 16.80 ? 165 THR A O   1 
ATOM   1025 C CB  . THR A 1 140 ? 5.095   -11.423 -10.324 1.00 16.73 ? 165 THR A CB  1 
ATOM   1026 O OG1 . THR A 1 140 ? 6.418   -11.256 -10.851 1.00 14.03 ? 165 THR A OG1 1 
ATOM   1027 C CG2 . THR A 1 140 ? 5.023   -12.748 -9.580  1.00 15.65 ? 165 THR A CG2 1 
ATOM   1028 N N   . GLU A 1 141 ? 3.850   -8.979  -11.383 1.00 15.96 ? 166 GLU A N   1 
ATOM   1029 C CA  . GLU A 1 141 ? 4.048   -7.622  -11.864 1.00 10.28 ? 166 GLU A CA  1 
ATOM   1030 C C   . GLU A 1 141 ? 5.538   -7.297  -11.877 1.00 12.37 ? 166 GLU A C   1 
ATOM   1031 O O   . GLU A 1 141 ? 6.266   -7.683  -10.960 1.00 12.30 ? 166 GLU A O   1 
ATOM   1032 C CB  . GLU A 1 141 ? 3.306   -6.614  -10.980 1.00 11.75 ? 166 GLU A CB  1 
ATOM   1033 C CG  . GLU A 1 141 ? 1.810   -6.832  -10.912 1.00 15.03 ? 166 GLU A CG  1 
ATOM   1034 C CD  . GLU A 1 141 ? 1.100   -6.393  -12.198 1.00 27.43 ? 166 GLU A CD  1 
ATOM   1035 O OE1 . GLU A 1 141 ? 1.778   -5.897  -13.125 1.00 23.27 ? 166 GLU A OE1 1 
ATOM   1036 O OE2 . GLU A 1 141 ? -0.139  -6.538  -12.283 1.00 24.45 ? 166 GLU A OE2 1 
ATOM   1037 N N   . PRO A 1 142 ? 6.011   -6.562  -12.889 1.00 20.28 ? 167 PRO A N   1 
ATOM   1038 C CA  . PRO A 1 142 ? 5.238   -5.966  -13.983 1.00 13.19 ? 167 PRO A CA  1 
ATOM   1039 C C   . PRO A 1 142 ? 5.227   -6.787  -15.266 1.00 13.87 ? 167 PRO A C   1 
ATOM   1040 O O   . PRO A 1 142 ? 4.583   -6.376  -16.225 1.00 15.91 ? 167 PRO A O   1 
ATOM   1041 C CB  . PRO A 1 142 ? 5.967   -4.639  -14.199 1.00 13.98 ? 167 PRO A CB  1 
ATOM   1042 C CG  . PRO A 1 142 ? 7.416   -5.046  -14.008 1.00 14.32 ? 167 PRO A CG  1 
ATOM   1043 C CD  . PRO A 1 142 ? 7.381   -6.011  -12.843 1.00 14.34 ? 167 PRO A CD  1 
ATOM   1044 N N   . THR A 1 143 ? 5.873   -7.951  -15.337 1.00 10.62 ? 168 THR A N   1 
ATOM   1045 C CA  . THR A 1 143 ? 5.997   -8.611  -16.633 1.00 13.71 ? 168 THR A CA  1 
ATOM   1046 C C   . THR A 1 143 ? 4.703   -9.260  -17.105 1.00 15.80 ? 168 THR A C   1 
ATOM   1047 O O   . THR A 1 143 ? 4.611   -9.606  -18.287 1.00 19.04 ? 168 THR A O   1 
ATOM   1048 C CB  . THR A 1 143 ? 7.087   -9.689  -16.587 1.00 11.28 ? 168 THR A CB  1 
ATOM   1049 O OG1 . THR A 1 143 ? 6.713   -10.704 -15.644 1.00 15.05 ? 168 THR A OG1 1 
ATOM   1050 C CG2 . THR A 1 143 ? 8.417   -9.092  -16.161 1.00 8.69  ? 168 THR A CG2 1 
ATOM   1051 N N   . LEU A 1 144 ? 3.709   -9.445  -16.233 1.00 18.81 ? 169 LEU A N   1 
ATOM   1052 C CA  . LEU A 1 144 ? 2.423   -9.948  -16.708 1.00 24.50 ? 169 LEU A CA  1 
ATOM   1053 C C   . LEU A 1 144 ? 1.724   -8.979  -17.658 1.00 19.20 ? 169 LEU A C   1 
ATOM   1054 O O   . LEU A 1 144 ? 0.675   -9.330  -18.208 1.00 21.51 ? 169 LEU A O   1 
ATOM   1055 C CB  . LEU A 1 144 ? 1.498   -10.301 -15.527 1.00 25.07 ? 169 LEU A CB  1 
ATOM   1056 C CG  . LEU A 1 144 ? 0.947   -9.292  -14.511 1.00 25.22 ? 169 LEU A CG  1 
ATOM   1057 C CD1 . LEU A 1 144 ? -0.328  -8.625  -15.034 1.00 28.13 ? 169 LEU A CD1 1 
ATOM   1058 C CD2 . LEU A 1 144 ? 0.652   -9.989  -13.190 1.00 19.48 ? 169 LEU A CD2 1 
ATOM   1059 N N   . ASN A 1 145 ? 2.270   -7.781  -17.871 1.00 21.27 ? 170 ASN A N   1 
ATOM   1060 C CA  . ASN A 1 145 ? 1.655   -6.787  -18.739 1.00 19.05 ? 170 ASN A CA  1 
ATOM   1061 C C   . ASN A 1 145 ? 2.291   -6.691  -20.126 1.00 20.28 ? 170 ASN A C   1 
ATOM   1062 O O   . ASN A 1 145 ? 1.998   -5.738  -20.857 1.00 18.77 ? 170 ASN A O   1 
ATOM   1063 C CB  . ASN A 1 145 ? 1.707   -5.417  -18.054 1.00 17.16 ? 170 ASN A CB  1 
ATOM   1064 C CG  . ASN A 1 145 ? 1.064   -5.429  -16.677 1.00 21.08 ? 170 ASN A CG  1 
ATOM   1065 O OD1 . ASN A 1 145 ? -0.156  -5.525  -16.548 1.00 27.20 ? 170 ASN A OD1 1 
ATOM   1066 N ND2 . ASN A 1 145 ? 1.886   -5.333  -15.638 1.00 26.54 ? 170 ASN A ND2 1 
ATOM   1067 N N   . THR A 1 146 ? 3.144   -7.645  -20.513 1.00 20.88 ? 171 THR A N   1 
ATOM   1068 C CA  . THR A 1 146 ? 3.801   -7.540  -21.815 1.00 20.24 ? 171 THR A CA  1 
ATOM   1069 C C   . THR A 1 146 ? 2.805   -7.608  -22.966 1.00 22.33 ? 171 THR A C   1 
ATOM   1070 O O   . THR A 1 146 ? 3.023   -6.984  -24.012 1.00 22.79 ? 171 THR A O   1 
ATOM   1071 C CB  . THR A 1 146 ? 4.858   -8.633  -21.975 1.00 17.45 ? 171 THR A CB  1 
ATOM   1072 O OG1 . THR A 1 146 ? 4.284   -9.907  -21.648 1.00 20.38 ? 171 THR A OG1 1 
ATOM   1073 C CG2 . THR A 1 146 ? 6.058   -8.352  -21.071 1.00 11.69 ? 171 THR A CG2 1 
ATOM   1074 N N   . ALA A 1 147 ? 1.719   -8.365  -22.799 1.00 12.97 ? 172 ALA A N   1 
ATOM   1075 C CA  . ALA A 1 147 ? 0.577   -8.320  -23.715 1.00 21.60 ? 172 ALA A CA  1 
ATOM   1076 C C   . ALA A 1 147 ? 0.988   -8.647  -25.154 1.00 23.19 ? 172 ALA A C   1 
ATOM   1077 O O   . ALA A 1 147 ? 0.488   -8.054  -26.114 1.00 15.29 ? 172 ALA A O   1 
ATOM   1078 C CB  . ALA A 1 147 ? -0.120  -6.960  -23.640 1.00 9.44  ? 172 ALA A CB  1 
ATOM   1079 N N   . ILE A 1 148 ? 1.911   -9.587  -25.309 1.00 20.58 ? 173 ILE A N   1 
ATOM   1080 C CA  . ILE A 1 148 ? 2.452   -9.878  -26.642 1.00 19.76 ? 173 ILE A CA  1 
ATOM   1081 C C   . ILE A 1 148 ? 1.397   -10.614 -27.464 1.00 21.52 ? 173 ILE A C   1 
ATOM   1082 O O   . ILE A 1 148 ? 0.785   -11.574 -26.962 1.00 19.69 ? 173 ILE A O   1 
ATOM   1083 C CB  . ILE A 1 148 ? 3.736   -10.694 -26.536 1.00 25.22 ? 173 ILE A CB  1 
ATOM   1084 C CG1 . ILE A 1 148 ? 4.803   -9.904  -25.773 1.00 17.64 ? 173 ILE A CG1 1 
ATOM   1085 C CG2 . ILE A 1 148 ? 4.259   -10.950 -27.926 1.00 22.37 ? 173 ILE A CG2 1 
ATOM   1086 C CD1 . ILE A 1 148 ? 5.983   -10.733 -25.329 1.00 20.20 ? 173 ILE A CD1 1 
ATOM   1087 N N   . PRO A 1 149 ? 1.132   -10.195 -28.703 1.00 24.83 ? 174 PRO A N   1 
ATOM   1088 C CA  . PRO A 1 149 ? 0.150   -10.907 -29.529 1.00 17.10 ? 174 PRO A CA  1 
ATOM   1089 C C   . PRO A 1 149 ? 0.508   -12.375 -29.676 1.00 17.69 ? 174 PRO A C   1 
ATOM   1090 O O   . PRO A 1 149 ? 1.667   -12.736 -29.896 1.00 19.52 ? 174 PRO A O   1 
ATOM   1091 C CB  . PRO A 1 149 ? 0.236   -10.179 -30.875 1.00 22.51 ? 174 PRO A CB  1 
ATOM   1092 C CG  . PRO A 1 149 ? 0.690   -8.803  -30.522 1.00 15.70 ? 174 PRO A CG  1 
ATOM   1093 C CD  . PRO A 1 149 ? 1.647   -8.989  -29.376 1.00 13.74 ? 174 PRO A CD  1 
ATOM   1094 N N   . GLY A 1 150 ? -0.502  -13.228 -29.531 1.00 15.85 ? 175 GLY A N   1 
ATOM   1095 C CA  . GLY A 1 150 ? -0.306  -14.651 -29.674 1.00 26.99 ? 175 GLY A CA  1 
ATOM   1096 C C   . GLY A 1 150 ? 0.228   -15.325 -28.435 1.00 20.17 ? 175 GLY A C   1 
ATOM   1097 O O   . GLY A 1 150 ? 0.298   -16.560 -28.402 1.00 22.55 ? 175 GLY A O   1 
ATOM   1098 N N   . ASP A 1 151 ? 0.603   -14.554 -27.419 1.00 9.91  ? 176 ASP A N   1 
ATOM   1099 C CA  . ASP A 1 151 ? 1.159   -15.102 -26.197 1.00 16.84 ? 176 ASP A CA  1 
ATOM   1100 C C   . ASP A 1 151 ? 0.016   -15.477 -25.270 1.00 11.37 ? 176 ASP A C   1 
ATOM   1101 O O   . ASP A 1 151 ? -0.764  -14.597 -24.883 1.00 12.22 ? 176 ASP A O   1 
ATOM   1102 C CB  . ASP A 1 151 ? 2.067   -14.079 -25.522 1.00 20.67 ? 176 ASP A CB  1 
ATOM   1103 C CG  . ASP A 1 151 ? 2.826   -14.647 -24.323 1.00 14.30 ? 176 ASP A CG  1 
ATOM   1104 O OD1 . ASP A 1 151 ? 2.558   -15.794 -23.914 1.00 18.50 ? 176 ASP A OD1 1 
ATOM   1105 O OD2 . ASP A 1 151 ? 3.699   -13.937 -23.783 1.00 18.85 ? 176 ASP A OD2 1 
ATOM   1106 N N   . PRO A 1 152 ? -0.129  -16.746 -24.891 1.00 16.49 ? 177 PRO A N   1 
ATOM   1107 C CA  . PRO A 1 152 ? -1.250  -17.117 -24.021 1.00 18.30 ? 177 PRO A CA  1 
ATOM   1108 C C   . PRO A 1 152 ? -1.034  -16.773 -22.560 1.00 16.33 ? 177 PRO A C   1 
ATOM   1109 O O   . PRO A 1 152 ? -1.997  -16.850 -21.784 1.00 15.86 ? 177 PRO A O   1 
ATOM   1110 C CB  . PRO A 1 152 ? -1.363  -18.633 -24.229 1.00 19.96 ? 177 PRO A CB  1 
ATOM   1111 C CG  . PRO A 1 152 ? 0.010   -19.072 -24.630 1.00 11.51 ? 177 PRO A CG  1 
ATOM   1112 C CD  . PRO A 1 152 ? 0.707   -17.901 -25.267 1.00 15.99 ? 177 PRO A CD  1 
ATOM   1113 N N   . ARG A 1 153 ? 0.176   -16.382 -22.162 1.00 17.49 ? 178 ARG A N   1 
ATOM   1114 C CA  . ARG A 1 153 ? 0.439   -16.125 -20.754 1.00 10.68 ? 178 ARG A CA  1 
ATOM   1115 C C   . ARG A 1 153 ? -0.359  -14.916 -20.291 1.00 18.56 ? 178 ARG A C   1 
ATOM   1116 O O   . ARG A 1 153 ? -0.451  -13.904 -20.996 1.00 15.49 ? 178 ARG A O   1 
ATOM   1117 C CB  . ARG A 1 153 ? 1.920   -15.878 -20.505 1.00 16.12 ? 178 ARG A CB  1 
ATOM   1118 C CG  . ARG A 1 153 ? 2.831   -17.060 -20.783 1.00 18.62 ? 178 ARG A CG  1 
ATOM   1119 C CD  . ARG A 1 153 ? 4.270   -16.666 -20.500 1.00 11.05 ? 178 ARG A CD  1 
ATOM   1120 N NE  . ARG A 1 153 ? 4.752   -15.711 -21.491 1.00 21.22 ? 178 ARG A NE  1 
ATOM   1121 C CZ  . ARG A 1 153 ? 5.949   -15.143 -21.467 1.00 18.02 ? 178 ARG A CZ  1 
ATOM   1122 N NH1 . ARG A 1 153 ? 6.838   -15.443 -20.536 1.00 15.51 ? 178 ARG A NH1 1 
ATOM   1123 N NH2 . ARG A 1 153 ? 6.263   -14.253 -22.406 1.00 28.40 ? 178 ARG A NH2 1 
ATOM   1124 N N   . ASP A 1 154 ? -0.924  -15.025 -19.089 1.00 18.07 ? 179 ASP A N   1 
ATOM   1125 C CA  . ASP A 1 154 ? -1.613  -13.916 -18.432 1.00 17.15 ? 179 ASP A CA  1 
ATOM   1126 C C   . ASP A 1 154 ? -2.768  -13.403 -19.293 1.00 15.19 ? 179 ASP A C   1 
ATOM   1127 O O   . ASP A 1 154 ? -2.970  -12.197 -19.445 1.00 16.30 ? 179 ASP A O   1 
ATOM   1128 C CB  . ASP A 1 154 ? -0.634  -12.794 -18.086 1.00 12.73 ? 179 ASP A CB  1 
ATOM   1129 C CG  . ASP A 1 154 ? 0.579   -13.301 -17.309 1.00 23.38 ? 179 ASP A CG  1 
ATOM   1130 O OD1 . ASP A 1 154 ? 0.406   -13.777 -16.165 1.00 25.17 ? 179 ASP A OD1 1 
ATOM   1131 O OD2 . ASP A 1 154 ? 1.708   -13.223 -17.842 1.00 26.27 ? 179 ASP A OD2 1 
ATOM   1132 N N   . THR A 1 155 ? -3.525  -14.332 -19.872 1.00 10.69 ? 180 THR A N   1 
ATOM   1133 C CA  . THR A 1 155 ? -4.658  -14.008 -20.725 1.00 15.53 ? 180 THR A CA  1 
ATOM   1134 C C   . THR A 1 155 ? -5.927  -14.666 -20.202 1.00 14.14 ? 180 THR A C   1 
ATOM   1135 O O   . THR A 1 155 ? -5.889  -15.616 -19.413 1.00 11.74 ? 180 THR A O   1 
ATOM   1136 C CB  . THR A 1 155 ? -4.438  -14.470 -22.182 1.00 16.42 ? 180 THR A CB  1 
ATOM   1137 O OG1 . THR A 1 155 ? -4.339  -15.902 -22.225 1.00 19.61 ? 180 THR A OG1 1 
ATOM   1138 C CG2 . THR A 1 155 ? -3.196  -13.844 -22.792 1.00 11.43 ? 180 THR A CG2 1 
ATOM   1139 N N   . THR A 1 156 ? -7.059  -14.154 -20.679 1.00 11.91 ? 181 THR A N   1 
ATOM   1140 C CA  . THR A 1 156 ? -8.321  -14.874 -20.565 1.00 12.41 ? 181 THR A CA  1 
ATOM   1141 C C   . THR A 1 156 ? -9.201  -14.478 -21.745 1.00 13.34 ? 181 THR A C   1 
ATOM   1142 O O   . THR A 1 156 ? -8.817  -13.659 -22.581 1.00 14.84 ? 181 THR A O   1 
ATOM   1143 C CB  . THR A 1 156 ? -9.020  -14.589 -19.235 1.00 11.40 ? 181 THR A CB  1 
ATOM   1144 O OG1 . THR A 1 156 ? -10.119 -15.495 -19.069 1.00 10.02 ? 181 THR A OG1 1 
ATOM   1145 C CG2 . THR A 1 156 ? -9.552  -13.173 -19.235 1.00 15.45 ? 181 THR A CG2 1 
ATOM   1146 N N   . THR A 1 157 ? -10.387 -15.031 -21.796 1.00 11.50 ? 182 THR A N   1 
ATOM   1147 C CA  . THR A 1 157 ? -11.334 -14.606 -22.810 1.00 11.79 ? 182 THR A CA  1 
ATOM   1148 C C   . THR A 1 157 ? -12.408 -13.730 -22.196 1.00 9.02  ? 182 THR A C   1 
ATOM   1149 O O   . THR A 1 157 ? -12.631 -13.764 -20.983 1.00 14.58 ? 182 THR A O   1 
ATOM   1150 C CB  . THR A 1 157 ? -11.990 -15.823 -23.483 1.00 12.63 ? 182 THR A CB  1 
ATOM   1151 O OG1 . THR A 1 157 ? -12.790 -16.528 -22.529 1.00 7.34  ? 182 THR A OG1 1 
ATOM   1152 C CG2 . THR A 1 157 ? -10.936 -16.755 -24.073 1.00 8.91  ? 182 THR A CG2 1 
ATOM   1153 N N   . PRO A 1 158 ? -13.081 -12.904 -23.000 1.00 11.35 ? 183 PRO A N   1 
ATOM   1154 C CA  . PRO A 1 158 ? -14.190 -12.113 -22.440 1.00 11.11 ? 183 PRO A CA  1 
ATOM   1155 C C   . PRO A 1 158 ? -15.282 -12.973 -21.828 1.00 16.30 ? 183 PRO A C   1 
ATOM   1156 O O   . PRO A 1 158 ? -15.792 -12.640 -20.752 1.00 15.94 ? 183 PRO A O   1 
ATOM   1157 C CB  . PRO A 1 158 ? -14.692 -11.315 -23.652 1.00 10.55 ? 183 PRO A CB  1 
ATOM   1158 C CG  . PRO A 1 158 ? -13.493 -11.221 -24.552 1.00 15.46 ? 183 PRO A CG  1 
ATOM   1159 C CD  . PRO A 1 158 ? -12.786 -12.533 -24.395 1.00 11.27 ? 183 PRO A CD  1 
ATOM   1160 N N   . ARG A 1 159 ? -15.657 -14.075 -22.480 1.00 9.58  ? 184 ARG A N   1 
ATOM   1161 C CA  . ARG A 1 159 ? -16.720 -14.923 -21.951 1.00 13.90 ? 184 ARG A CA  1 
ATOM   1162 C C   . ARG A 1 159 ? -16.333 -15.506 -20.595 1.00 16.63 ? 184 ARG A C   1 
ATOM   1163 O O   . ARG A 1 159 ? -17.112 -15.452 -19.629 1.00 15.03 ? 184 ARG A O   1 
ATOM   1164 C CB  . ARG A 1 159 ? -17.036 -16.041 -22.948 1.00 19.06 ? 184 ARG A CB  1 
ATOM   1165 C CG  . ARG A 1 159 ? -18.162 -16.974 -22.519 1.00 16.57 ? 184 ARG A CG  1 
ATOM   1166 C CD  . ARG A 1 159 ? -18.195 -18.238 -23.376 1.00 18.19 ? 184 ARG A CD  1 
ATOM   1167 N NE  . ARG A 1 159 ? -18.248 -17.945 -24.804 1.00 17.05 ? 184 ARG A NE  1 
ATOM   1168 C CZ  . ARG A 1 159 ? -19.369 -17.804 -25.499 1.00 21.78 ? 184 ARG A CZ  1 
ATOM   1169 N NH1 . ARG A 1 159 ? -20.559 -17.908 -24.925 1.00 15.83 ? 184 ARG A NH1 1 
ATOM   1170 N NH2 . ARG A 1 159 ? -19.295 -17.563 -26.805 1.00 23.57 ? 184 ARG A NH2 1 
ATOM   1171 N N   . ALA A 1 160 ? -15.138 -16.094 -20.513 1.00 13.51 ? 185 ALA A N   1 
ATOM   1172 C CA  . ALA A 1 160 ? -14.682 -16.684 -19.259 1.00 12.25 ? 185 ALA A CA  1 
ATOM   1173 C C   . ALA A 1 160 ? -14.620 -15.643 -18.150 1.00 16.43 ? 185 ALA A C   1 
ATOM   1174 O O   . ALA A 1 160 ? -15.035 -15.907 -17.014 1.00 17.38 ? 185 ALA A O   1 
ATOM   1175 C CB  . ALA A 1 160 ? -13.315 -17.332 -19.455 1.00 5.03  ? 185 ALA A CB  1 
ATOM   1176 N N   . MET A 1 161 ? -14.121 -14.447 -18.463 1.00 9.20  ? 186 MET A N   1 
ATOM   1177 C CA  . MET A 1 161 ? -13.976 -13.430 -17.431 1.00 14.94 ? 186 MET A CA  1 
ATOM   1178 C C   . MET A 1 161 ? -15.329 -12.883 -17.000 1.00 10.28 ? 186 MET A C   1 
ATOM   1179 O O   . MET A 1 161 ? -15.526 -12.585 -15.821 1.00 16.60 ? 186 MET A O   1 
ATOM   1180 C CB  . MET A 1 161 ? -13.070 -12.299 -17.913 1.00 17.98 ? 186 MET A CB  1 
ATOM   1181 C CG  . MET A 1 161 ? -12.694 -11.305 -16.808 1.00 23.70 ? 186 MET A CG  1 
ATOM   1182 S SD  . MET A 1 161 ? -11.882 -12.103 -15.403 1.00 26.87 ? 186 MET A SD  1 
ATOM   1183 C CE  . MET A 1 161 ? -10.217 -11.451 -15.543 1.00 28.29 ? 186 MET A CE  1 
ATOM   1184 N N   . ALA A 1 162 ? -16.272 -12.742 -17.933 1.00 11.12 ? 187 ALA A N   1 
ATOM   1185 C CA  . ALA A 1 162 ? -17.613 -12.304 -17.560 1.00 12.93 ? 187 ALA A CA  1 
ATOM   1186 C C   . ALA A 1 162 ? -18.268 -13.314 -16.627 1.00 13.08 ? 187 ALA A C   1 
ATOM   1187 O O   . ALA A 1 162 ? -18.798 -12.948 -15.569 1.00 12.09 ? 187 ALA A O   1 
ATOM   1188 C CB  . ALA A 1 162 ? -18.466 -12.082 -18.809 1.00 8.11  ? 187 ALA A CB  1 
ATOM   1189 N N   . GLN A 1 163 ? -18.218 -14.601 -16.994 1.00 13.07 ? 188 GLN A N   1 
ATOM   1190 C CA  . GLN A 1 163 ? -18.800 -15.632 -16.136 1.00 11.56 ? 188 GLN A CA  1 
ATOM   1191 C C   . GLN A 1 163 ? -18.133 -15.654 -14.763 1.00 15.16 ? 188 GLN A C   1 
ATOM   1192 O O   . GLN A 1 163 ? -18.815 -15.735 -13.734 1.00 14.61 ? 188 GLN A O   1 
ATOM   1193 C CB  . GLN A 1 163 ? -18.692 -16.998 -16.812 1.00 18.89 ? 188 GLN A CB  1 
ATOM   1194 C CG  . GLN A 1 163 ? -19.432 -18.123 -16.085 1.00 17.57 ? 188 GLN A CG  1 
ATOM   1195 C CD  . GLN A 1 163 ? -20.895 -17.792 -15.822 1.00 27.71 ? 188 GLN A CD  1 
ATOM   1196 O OE1 . GLN A 1 163 ? -21.344 -17.766 -14.674 1.00 29.04 ? 188 GLN A OE1 1 
ATOM   1197 N NE2 . GLN A 1 163 ? -21.644 -17.535 -16.889 1.00 27.20 ? 188 GLN A NE2 1 
ATOM   1198 N N   . THR A 1 164 ? -16.797 -15.563 -14.728 1.00 16.24 ? 189 THR A N   1 
ATOM   1199 C CA  . THR A 1 164 ? -16.079 -15.573 -13.458 1.00 12.47 ? 189 THR A CA  1 
ATOM   1200 C C   . THR A 1 164 ? -16.429 -14.356 -12.611 1.00 16.65 ? 189 THR A C   1 
ATOM   1201 O O   . THR A 1 164 ? -16.647 -14.480 -11.402 1.00 12.81 ? 189 THR A O   1 
ATOM   1202 C CB  . THR A 1 164 ? -14.570 -15.647 -13.703 1.00 18.92 ? 189 THR A CB  1 
ATOM   1203 O OG1 . THR A 1 164 ? -14.232 -16.951 -14.189 1.00 25.67 ? 189 THR A OG1 1 
ATOM   1204 C CG2 . THR A 1 164 ? -13.795 -15.371 -12.428 1.00 18.04 ? 189 THR A CG2 1 
ATOM   1205 N N   . LEU A 1 165 ? -16.436 -13.162 -13.211 1.00 13.89 ? 190 LEU A N   1 
ATOM   1206 C CA  . LEU A 1 165 ? -16.751 -11.965 -12.443 1.00 9.24  ? 190 LEU A CA  1 
ATOM   1207 C C   . LEU A 1 165 ? -18.163 -12.042 -11.892 1.00 11.80 ? 190 LEU A C   1 
ATOM   1208 O O   . LEU A 1 165 ? -18.428 -11.597 -10.767 1.00 15.56 ? 190 LEU A O   1 
ATOM   1209 C CB  . LEU A 1 165 ? -16.595 -10.714 -13.313 1.00 12.80 ? 190 LEU A CB  1 
ATOM   1210 C CG  . LEU A 1 165 ? -16.705 -9.368  -12.582 1.00 17.80 ? 190 LEU A CG  1 
ATOM   1211 C CD1 . LEU A 1 165 ? -15.640 -9.236  -11.498 1.00 19.57 ? 190 LEU A CD1 1 
ATOM   1212 C CD2 . LEU A 1 165 ? -16.674 -8.173  -13.543 1.00 13.30 ? 190 LEU A CD2 1 
ATOM   1213 N N   . ARG A 1 166 ? -19.082 -12.633 -12.663 1.00 13.39 ? 191 ARG A N   1 
ATOM   1214 C CA  . ARG A 1 166 ? -20.441 -12.813 -12.173 1.00 17.88 ? 191 ARG A CA  1 
ATOM   1215 C C   . ARG A 1 166 ? -20.449 -13.742 -10.966 1.00 12.95 ? 191 ARG A C   1 
ATOM   1216 O O   . ARG A 1 166 ? -21.080 -13.444 -9.944  1.00 22.29 ? 191 ARG A O   1 
ATOM   1217 C CB  . ARG A 1 166 ? -21.335 -13.329 -13.308 1.00 18.18 ? 191 ARG A CB  1 
ATOM   1218 C CG  . ARG A 1 166 ? -22.813 -13.390 -12.958 1.00 22.36 ? 191 ARG A CG  1 
ATOM   1219 C CD  . ARG A 1 166 ? -23.508 -14.657 -13.417 1.00 24.75 ? 191 ARG A CD  1 
ATOM   1220 N NE  . ARG A 1 166 ? -24.939 -14.543 -13.154 1.00 21.90 ? 191 ARG A NE  1 
ATOM   1221 C CZ  . ARG A 1 166 ? -25.899 -14.767 -14.041 1.00 29.03 ? 191 ARG A CZ  1 
ATOM   1222 N NH1 . ARG A 1 166 ? -25.624 -15.125 -15.286 1.00 22.36 ? 191 ARG A NH1 1 
ATOM   1223 N NH2 . ARG A 1 166 ? -27.169 -14.608 -13.674 1.00 19.31 ? 191 ARG A NH2 1 
ATOM   1224 N N   . GLN A 1 167 ? -19.758 -14.879 -11.067 1.00 11.61 ? 192 GLN A N   1 
ATOM   1225 C CA  . GLN A 1 167 ? -19.718 -15.817 -9.945  1.00 21.20 ? 192 GLN A CA  1 
ATOM   1226 C C   . GLN A 1 167 ? -19.060 -15.190 -8.717  1.00 14.82 ? 192 GLN A C   1 
ATOM   1227 O O   . GLN A 1 167 ? -19.451 -15.472 -7.579  1.00 16.19 ? 192 GLN A O   1 
ATOM   1228 C CB  . GLN A 1 167 ? -19.018 -17.119 -10.341 1.00 29.34 ? 192 GLN A CB  1 
ATOM   1229 C CG  . GLN A 1 167 ? -19.843 -17.978 -11.303 1.00 27.91 ? 192 GLN A CG  1 
ATOM   1230 C CD  . GLN A 1 167 ? -18.995 -18.892 -12.158 1.00 47.65 ? 192 GLN A CD  1 
ATOM   1231 O OE1 . GLN A 1 167 ? -18.247 -18.437 -13.024 1.00 54.00 ? 192 GLN A OE1 1 
ATOM   1232 N NE2 . GLN A 1 167 ? -19.089 -20.195 -11.904 1.00 55.43 ? 192 GLN A NE2 1 
ATOM   1233 N N   . LEU A 1 168 ? -18.047 -14.348 -8.925  1.00 12.30 ? 193 LEU A N   1 
ATOM   1234 C CA  . LEU A 1 168 ? -17.333 -13.774 -7.789  1.00 13.67 ? 193 LEU A CA  1 
ATOM   1235 C C   . LEU A 1 168 ? -18.157 -12.698 -7.102  1.00 12.14 ? 193 LEU A C   1 
ATOM   1236 O O   . LEU A 1 168 ? -18.184 -12.629 -5.868  1.00 14.37 ? 193 LEU A O   1 
ATOM   1237 C CB  . LEU A 1 168 ? -16.001 -13.184 -8.254  1.00 11.03 ? 193 LEU A CB  1 
ATOM   1238 C CG  . LEU A 1 168 ? -14.901 -14.164 -8.646  1.00 16.78 ? 193 LEU A CG  1 
ATOM   1239 C CD1 . LEU A 1 168 ? -13.690 -13.437 -9.257  1.00 15.52 ? 193 LEU A CD1 1 
ATOM   1240 C CD2 . LEU A 1 168 ? -14.488 -14.950 -7.414  1.00 23.61 ? 193 LEU A CD2 1 
ATOM   1241 N N   . THR A 1 169 ? -18.840 -11.855 -7.878  1.00 10.02 ? 194 THR A N   1 
ATOM   1242 C CA  . THR A 1 169 ? -19.505 -10.681 -7.328  1.00 14.24 ? 194 THR A CA  1 
ATOM   1243 C C   . THR A 1 169 ? -20.999 -10.876 -7.111  1.00 20.44 ? 194 THR A C   1 
ATOM   1244 O O   . THR A 1 169 ? -21.571 -10.260 -6.204  1.00 17.94 ? 194 THR A O   1 
ATOM   1245 C CB  . THR A 1 169 ? -19.290 -9.486  -8.253  1.00 11.39 ? 194 THR A CB  1 
ATOM   1246 O OG1 . THR A 1 169 ? -19.834 -9.792  -9.542  1.00 14.52 ? 194 THR A OG1 1 
ATOM   1247 C CG2 . THR A 1 169 ? -17.815 -9.199  -8.403  1.00 16.25 ? 194 THR A CG2 1 
ATOM   1248 N N   . LEU A 1 170 ? -21.639 -11.724 -7.919  1.00 13.54 ? 195 LEU A N   1 
ATOM   1249 C CA  . LEU A 1 170 ? -23.076 -11.938 -7.857  1.00 20.58 ? 195 LEU A CA  1 
ATOM   1250 C C   . LEU A 1 170 ? -23.443 -13.373 -7.528  1.00 24.79 ? 195 LEU A C   1 
ATOM   1251 O O   . LEU A 1 170 ? -24.546 -13.611 -7.027  1.00 20.57 ? 195 LEU A O   1 
ATOM   1252 C CB  . LEU A 1 170 ? -23.744 -11.543 -9.185  1.00 14.88 ? 195 LEU A CB  1 
ATOM   1253 C CG  . LEU A 1 170 ? -23.531 -10.100 -9.665  1.00 16.08 ? 195 LEU A CG  1 
ATOM   1254 C CD1 . LEU A 1 170 ? -24.064 -9.933  -11.077 1.00 17.61 ? 195 LEU A CD1 1 
ATOM   1255 C CD2 . LEU A 1 170 ? -24.165 -9.067  -8.718  1.00 20.21 ? 195 LEU A CD2 1 
ATOM   1256 N N   . GLY A 1 171 ? -22.557 -14.325 -7.791  1.00 22.16 ? 196 GLY A N   1 
ATOM   1257 C CA  . GLY A 1 171 ? -22.794 -15.723 -7.507  1.00 17.11 ? 196 GLY A CA  1 
ATOM   1258 C C   . GLY A 1 171 ? -22.221 -16.096 -6.161  1.00 15.54 ? 196 GLY A C   1 
ATOM   1259 O O   . GLY A 1 171 ? -22.084 -15.258 -5.265  1.00 23.55 ? 196 GLY A O   1 
ATOM   1260 N N   . HIS A 1 172 ? -21.886 -17.371 -6.002  1.00 17.67 ? 197 HIS A N   1 
ATOM   1261 C CA  . HIS A 1 172 ? -21.431 -17.870 -4.711  1.00 23.84 ? 197 HIS A CA  1 
ATOM   1262 C C   . HIS A 1 172 ? -20.040 -18.496 -4.754  1.00 19.99 ? 197 HIS A C   1 
ATOM   1263 O O   . HIS A 1 172 ? -19.748 -19.423 -3.995  1.00 17.71 ? 197 HIS A O   1 
ATOM   1264 C CB  . HIS A 1 172 ? -22.483 -18.806 -4.130  1.00 23.02 ? 197 HIS A CB  1 
ATOM   1265 C CG  . HIS A 1 172 ? -23.835 -18.171 -4.092  1.00 16.31 ? 197 HIS A CG  1 
ATOM   1266 N ND1 . HIS A 1 172 ? -24.347 -17.579 -2.958  1.00 18.63 ? 197 HIS A ND1 1 
ATOM   1267 C CD2 . HIS A 1 172 ? -24.763 -17.996 -5.062  1.00 17.74 ? 197 HIS A CD2 1 
ATOM   1268 C CE1 . HIS A 1 172 ? -25.538 -17.075 -3.227  1.00 32.75 ? 197 HIS A CE1 1 
ATOM   1269 N NE2 . HIS A 1 172 ? -25.815 -17.315 -4.497  1.00 30.20 ? 197 HIS A NE2 1 
ATOM   1270 N N   . ALA A 1 173 ? -19.163 -17.990 -5.624  1.00 17.01 ? 198 ALA A N   1 
ATOM   1271 C CA  . ALA A 1 173 ? -17.772 -18.429 -5.582  1.00 15.35 ? 198 ALA A CA  1 
ATOM   1272 C C   . ALA A 1 173 ? -17.110 -18.033 -4.270  1.00 18.93 ? 198 ALA A C   1 
ATOM   1273 O O   . ALA A 1 173 ? -16.207 -18.732 -3.794  1.00 28.82 ? 198 ALA A O   1 
ATOM   1274 C CB  . ALA A 1 173 ? -16.992 -17.849 -6.763  1.00 16.24 ? 198 ALA A CB  1 
ATOM   1275 N N   . LEU A 1 174 ? -17.543 -16.932 -3.670  1.00 20.41 ? 199 LEU A N   1 
ATOM   1276 C CA  . LEU A 1 174 ? -17.065 -16.497 -2.368  1.00 19.14 ? 199 LEU A CA  1 
ATOM   1277 C C   . LEU A 1 174 ? -18.175 -16.601 -1.330  1.00 16.56 ? 199 LEU A C   1 
ATOM   1278 O O   . LEU A 1 174 ? -19.366 -16.615 -1.654  1.00 14.46 ? 199 LEU A O   1 
ATOM   1279 C CB  . LEU A 1 174 ? -16.550 -15.054 -2.434  1.00 17.43 ? 199 LEU A CB  1 
ATOM   1280 C CG  . LEU A 1 174 ? -15.396 -14.802 -3.399  1.00 18.60 ? 199 LEU A CG  1 
ATOM   1281 C CD1 . LEU A 1 174 ? -15.077 -13.312 -3.469  1.00 17.27 ? 199 LEU A CD1 1 
ATOM   1282 C CD2 . LEU A 1 174 ? -14.178 -15.600 -2.943  1.00 18.62 ? 199 LEU A CD2 1 
ATOM   1283 N N   . GLY A 1 175 ? -17.766 -16.664 -0.065  1.00 18.16 ? 200 GLY A N   1 
ATOM   1284 C CA  . GLY A 1 175 ? -18.717 -16.500 1.014   1.00 10.74 ? 200 GLY A CA  1 
ATOM   1285 C C   . GLY A 1 175 ? -19.351 -15.126 0.991   1.00 15.91 ? 200 GLY A C   1 
ATOM   1286 O O   . GLY A 1 175 ? -18.836 -14.187 0.380   1.00 22.29 ? 200 GLY A O   1 
ATOM   1287 N N   . GLU A 1 176 ? -20.486 -15.007 1.689   1.00 21.20 ? 201 GLU A N   1 
ATOM   1288 C CA  . GLU A 1 176 ? -21.281 -13.784 1.606   1.00 22.80 ? 201 GLU A CA  1 
ATOM   1289 C C   . GLU A 1 176 ? -20.467 -12.559 2.006   1.00 21.46 ? 201 GLU A C   1 
ATOM   1290 O O   . GLU A 1 176 ? -20.478 -11.539 1.302   1.00 21.04 ? 201 GLU A O   1 
ATOM   1291 C CB  . GLU A 1 176 ? -22.538 -13.908 2.471   1.00 31.55 ? 201 GLU A CB  1 
ATOM   1292 C CG  . GLU A 1 176 ? -23.527 -12.750 2.309   1.00 29.31 ? 201 GLU A CG  1 
ATOM   1293 C CD  . GLU A 1 176 ? -23.809 -12.374 0.852   1.00 63.99 ? 201 GLU A CD  1 
ATOM   1294 O OE1 . GLU A 1 176 ? -23.720 -13.250 -0.039  1.00 50.66 ? 201 GLU A OE1 1 
ATOM   1295 O OE2 . GLU A 1 176 ? -24.104 -11.183 0.598   1.00 52.97 ? 201 GLU A OE2 1 
ATOM   1296 N N   . THR A 1 177 ? -19.761 -12.630 3.139   1.00 20.82 ? 202 THR A N   1 
ATOM   1297 C CA  . THR A 1 177 ? -18.980 -11.476 3.573   1.00 20.79 ? 202 THR A CA  1 
ATOM   1298 C C   . THR A 1 177 ? -17.879 -11.170 2.568   1.00 13.74 ? 202 THR A C   1 
ATOM   1299 O O   . THR A 1 177 ? -17.603 -10.004 2.269   1.00 16.38 ? 202 THR A O   1 
ATOM   1300 C CB  . THR A 1 177 ? -18.381 -11.719 4.960   1.00 19.79 ? 202 THR A CB  1 
ATOM   1301 O OG1 . THR A 1 177 ? -19.416 -12.098 5.873   1.00 18.51 ? 202 THR A OG1 1 
ATOM   1302 C CG2 . THR A 1 177 ? -17.670 -10.473 5.475   1.00 25.53 ? 202 THR A CG2 1 
ATOM   1303 N N   . GLN A 1 178 ? -17.247 -12.210 2.027   1.00 12.06 ? 203 GLN A N   1 
ATOM   1304 C CA  . GLN A 1 178 ? -16.152 -11.998 1.090   1.00 16.98 ? 203 GLN A CA  1 
ATOM   1305 C C   . GLN A 1 178 ? -16.668 -11.446 -0.233  1.00 17.45 ? 203 GLN A C   1 
ATOM   1306 O O   . GLN A 1 178 ? -16.023 -10.597 -0.855  1.00 13.00 ? 203 GLN A O   1 
ATOM   1307 C CB  . GLN A 1 178 ? -15.387 -13.303 0.880   1.00 16.00 ? 203 GLN A CB  1 
ATOM   1308 C CG  . GLN A 1 178 ? -14.590 -13.734 2.104   1.00 23.14 ? 203 GLN A CG  1 
ATOM   1309 C CD  . GLN A 1 178 ? -15.472 -14.297 3.207   1.00 24.42 ? 203 GLN A CD  1 
ATOM   1310 O OE1 . GLN A 1 178 ? -16.558 -14.817 2.942   1.00 22.51 ? 203 GLN A OE1 1 
ATOM   1311 N NE2 . GLN A 1 178 ? -15.015 -14.188 4.450   1.00 21.81 ? 203 GLN A NE2 1 
ATOM   1312 N N   . ARG A 1 179 ? -17.831 -11.923 -0.680  1.00 15.01 ? 204 ARG A N   1 
ATOM   1313 C CA  . ARG A 1 179 ? -18.443 -11.373 -1.883  1.00 20.04 ? 204 ARG A CA  1 
ATOM   1314 C C   . ARG A 1 179 ? -18.768 -9.897  -1.695  1.00 15.88 ? 204 ARG A C   1 
ATOM   1315 O O   . ARG A 1 179 ? -18.473 -9.065  -2.563  1.00 21.59 ? 204 ARG A O   1 
ATOM   1316 C CB  . ARG A 1 179 ? -19.704 -12.168 -2.231  1.00 22.63 ? 204 ARG A CB  1 
ATOM   1317 C CG  . ARG A 1 179 ? -20.517 -11.600 -3.382  1.00 15.86 ? 204 ARG A CG  1 
ATOM   1318 C CD  . ARG A 1 179 ? -21.739 -12.459 -3.685  1.00 16.48 ? 204 ARG A CD  1 
ATOM   1319 N NE  . ARG A 1 179 ? -22.851 -12.176 -2.784  1.00 26.74 ? 204 ARG A NE  1 
ATOM   1320 C CZ  . ARG A 1 179 ? -24.077 -12.663 -2.928  1.00 30.63 ? 204 ARG A CZ  1 
ATOM   1321 N NH1 . ARG A 1 179 ? -24.387 -13.470 -3.929  1.00 32.18 ? 204 ARG A NH1 1 
ATOM   1322 N NH2 . ARG A 1 179 ? -25.016 -12.331 -2.046  1.00 40.40 ? 204 ARG A NH2 1 
ATOM   1323 N N   . ALA A 1 180 ? -19.378 -9.555  -0.558  1.00 16.09 ? 205 ALA A N   1 
ATOM   1324 C CA  . ALA A 1 180 ? -19.691 -8.157  -0.283  1.00 14.57 ? 205 ALA A CA  1 
ATOM   1325 C C   . ALA A 1 180 ? -18.424 -7.316  -0.212  1.00 11.97 ? 205 ALA A C   1 
ATOM   1326 O O   . ALA A 1 180 ? -18.403 -6.178  -0.690  1.00 13.46 ? 205 ALA A O   1 
ATOM   1327 C CB  . ALA A 1 180 ? -20.498 -8.034  1.010   1.00 9.34  ? 205 ALA A CB  1 
ATOM   1328 N N   . GLN A 1 181 ? -17.358 -7.859  0.389   1.00 18.27 ? 206 GLN A N   1 
ATOM   1329 C CA  . GLN A 1 181 ? -16.089 -7.139  0.455   1.00 12.81 ? 206 GLN A CA  1 
ATOM   1330 C C   . GLN A 1 181 ? -15.499 -6.914  -0.930  1.00 9.62  ? 206 GLN A C   1 
ATOM   1331 O O   . GLN A 1 181 ? -14.992 -5.826  -1.227  1.00 12.77 ? 206 GLN A O   1 
ATOM   1332 C CB  . GLN A 1 181 ? -15.100 -7.914  1.324   1.00 15.80 ? 206 GLN A CB  1 
ATOM   1333 C CG  . GLN A 1 181 ? -13.746 -7.235  1.463   1.00 14.85 ? 206 GLN A CG  1 
ATOM   1334 C CD  . GLN A 1 181 ? -13.864 -5.880  2.114   1.00 21.61 ? 206 GLN A CD  1 
ATOM   1335 O OE1 . GLN A 1 181 ? -13.978 -4.858  1.432   1.00 15.12 ? 206 GLN A OE1 1 
ATOM   1336 N NE2 . GLN A 1 181 ? -13.848 -5.860  3.447   1.00 22.02 ? 206 GLN A NE2 1 
ATOM   1337 N N   . LEU A 1 182 ? -15.560 -7.929  -1.793  1.00 13.98 ? 207 LEU A N   1 
ATOM   1338 C CA  . LEU A 1 182 ? -15.042 -7.780  -3.148  1.00 13.52 ? 207 LEU A CA  1 
ATOM   1339 C C   . LEU A 1 182 ? -15.822 -6.708  -3.892  1.00 14.63 ? 207 LEU A C   1 
ATOM   1340 O O   . LEU A 1 182 ? -15.242 -5.880  -4.609  1.00 17.54 ? 207 LEU A O   1 
ATOM   1341 C CB  . LEU A 1 182 ? -15.106 -9.107  -3.894  1.00 10.63 ? 207 LEU A CB  1 
ATOM   1342 C CG  . LEU A 1 182 ? -14.589 -9.018  -5.325  1.00 15.52 ? 207 LEU A CG  1 
ATOM   1343 C CD1 . LEU A 1 182 ? -13.129 -8.583  -5.296  1.00 13.68 ? 207 LEU A CD1 1 
ATOM   1344 C CD2 . LEU A 1 182 ? -14.755 -10.340 -6.061  1.00 19.63 ? 207 LEU A CD2 1 
ATOM   1345 N N   . VAL A 1 183 ? -17.146 -6.709  -3.725  1.00 11.61 ? 208 VAL A N   1 
ATOM   1346 C CA  . VAL A 1 183 ? -17.990 -5.740  -4.413  1.00 17.46 ? 208 VAL A CA  1 
ATOM   1347 C C   . VAL A 1 183 ? -17.719 -4.338  -3.879  1.00 14.06 ? 208 VAL A C   1 
ATOM   1348 O O   . VAL A 1 183 ? -17.667 -3.369  -4.643  1.00 11.21 ? 208 VAL A O   1 
ATOM   1349 C CB  . VAL A 1 183 ? -19.475 -6.139  -4.269  1.00 14.94 ? 208 VAL A CB  1 
ATOM   1350 C CG1 . VAL A 1 183 ? -20.388 -4.982  -4.634  1.00 6.82  ? 208 VAL A CG1 1 
ATOM   1351 C CG2 . VAL A 1 183 ? -19.778 -7.352  -5.129  1.00 13.81 ? 208 VAL A CG2 1 
ATOM   1352 N N   . THR A 1 184 ? -17.555 -4.210  -2.559  1.00 10.80 ? 209 THR A N   1 
ATOM   1353 C CA  . THR A 1 184 ? -17.182 -2.930  -1.962  1.00 13.51 ? 209 THR A CA  1 
ATOM   1354 C C   . THR A 1 184 ? -15.880 -2.406  -2.549  1.00 8.74  ? 209 THR A C   1 
ATOM   1355 O O   . THR A 1 184 ? -15.772 -1.222  -2.892  1.00 8.59  ? 209 THR A O   1 
ATOM   1356 C CB  . THR A 1 184 ? -17.044 -3.079  -0.444  1.00 10.90 ? 209 THR A CB  1 
ATOM   1357 O OG1 . THR A 1 184 ? -18.317 -3.410  0.122   1.00 24.47 ? 209 THR A OG1 1 
ATOM   1358 C CG2 . THR A 1 184 ? -16.534 -1.793  0.189   1.00 13.03 ? 209 THR A CG2 1 
ATOM   1359 N N   . TRP A 1 185 ? -14.874 -3.274  -2.663  1.00 8.67  ? 210 TRP A N   1 
ATOM   1360 C CA  . TRP A 1 185 ? -13.602 -2.845  -3.233  1.00 12.46 ? 210 TRP A CA  1 
ATOM   1361 C C   . TRP A 1 185 ? -13.778 -2.389  -4.677  1.00 10.47 ? 210 TRP A C   1 
ATOM   1362 O O   . TRP A 1 185 ? -13.287 -1.324  -5.068  1.00 15.37 ? 210 TRP A O   1 
ATOM   1363 C CB  . TRP A 1 185 ? -12.581 -3.973  -3.145  1.00 12.50 ? 210 TRP A CB  1 
ATOM   1364 C CG  . TRP A 1 185 ? -11.981 -4.087  -1.783  1.00 17.88 ? 210 TRP A CG  1 
ATOM   1365 C CD1 . TRP A 1 185 ? -11.833 -3.089  -0.859  1.00 15.23 ? 210 TRP A CD1 1 
ATOM   1366 C CD2 . TRP A 1 185 ? -11.418 -5.262  -1.197  1.00 13.18 ? 210 TRP A CD2 1 
ATOM   1367 N NE1 . TRP A 1 185 ? -11.235 -3.579  0.275   1.00 12.31 ? 210 TRP A NE1 1 
ATOM   1368 C CE2 . TRP A 1 185 ? -10.965 -4.910  0.092   1.00 14.70 ? 210 TRP A CE2 1 
ATOM   1369 C CE3 . TRP A 1 185 ? -11.257 -6.580  -1.634  1.00 9.05  ? 210 TRP A CE3 1 
ATOM   1370 C CZ2 . TRP A 1 185 ? -10.365 -5.832  0.950   1.00 17.22 ? 210 TRP A CZ2 1 
ATOM   1371 C CZ3 . TRP A 1 185 ? -10.663 -7.495  -0.778  1.00 16.49 ? 210 TRP A CZ3 1 
ATOM   1372 C CH2 . TRP A 1 185 ? -10.228 -7.118  0.500   1.00 17.58 ? 210 TRP A CH2 1 
ATOM   1373 N N   . LEU A 1 186 ? -14.480 -3.187  -5.486  1.00 11.87 ? 211 LEU A N   1 
ATOM   1374 C CA  . LEU A 1 186 ? -14.659 -2.835  -6.893  1.00 11.80 ? 211 LEU A CA  1 
ATOM   1375 C C   . LEU A 1 186 ? -15.419 -1.524  -7.048  1.00 10.49 ? 211 LEU A C   1 
ATOM   1376 O O   . LEU A 1 186 ? -15.114 -0.719  -7.934  1.00 14.29 ? 211 LEU A O   1 
ATOM   1377 C CB  . LEU A 1 186 ? -15.388 -3.949  -7.636  1.00 7.84  ? 211 LEU A CB  1 
ATOM   1378 C CG  . LEU A 1 186 ? -14.611 -5.255  -7.769  1.00 16.47 ? 211 LEU A CG  1 
ATOM   1379 C CD1 . LEU A 1 186 ? -15.522 -6.361  -8.282  1.00 11.37 ? 211 LEU A CD1 1 
ATOM   1380 C CD2 . LEU A 1 186 ? -13.400 -5.066  -8.665  1.00 17.87 ? 211 LEU A CD2 1 
ATOM   1381 N N   . LYS A 1 187 ? -16.430 -1.304  -6.208  1.00 9.12  ? 212 LYS A N   1 
ATOM   1382 C CA  . LYS A 1 187 ? -17.221 -0.084  -6.287  1.00 10.75 ? 212 LYS A CA  1 
ATOM   1383 C C   . LYS A 1 187 ? -16.422 1.150   -5.907  1.00 9.40  ? 212 LYS A C   1 
ATOM   1384 O O   . LYS A 1 187 ? -16.774 2.253   -6.330  1.00 19.96 ? 212 LYS A O   1 
ATOM   1385 C CB  . LYS A 1 187 ? -18.413 -0.224  -5.338  1.00 15.69 ? 212 LYS A CB  1 
ATOM   1386 C CG  . LYS A 1 187 ? -19.569 -1.067  -5.842  1.00 9.48  ? 212 LYS A CG  1 
ATOM   1387 C CD  . LYS A 1 187 ? -20.735 -0.895  -4.897  1.00 17.30 ? 212 LYS A CD  1 
ATOM   1388 C CE  . LYS A 1 187 ? -21.970 -1.644  -5.335  1.00 27.44 ? 212 LYS A CE  1 
ATOM   1389 N NZ  . LYS A 1 187 ? -23.129 -1.173  -4.523  1.00 27.64 ? 212 LYS A NZ  1 
ATOM   1390 N N   . GLY A 1 188 ? -15.348 0.985   -5.143  1.00 7.87  ? 213 GLY A N   1 
ATOM   1391 C CA  . GLY A 1 188 ? -14.496 2.094   -4.784  1.00 11.79 ? 213 GLY A CA  1 
ATOM   1392 C C   . GLY A 1 188 ? -13.287 2.238   -5.684  1.00 12.24 ? 213 GLY A C   1 
ATOM   1393 O O   . GLY A 1 188 ? -12.331 2.931   -5.325  1.00 8.71  ? 213 GLY A O   1 
ATOM   1394 N N   . ASN A 1 189 ? -13.312 1.586   -6.845  1.00 9.18  ? 214 ASN A N   1 
ATOM   1395 C CA  . ASN A 1 189 ? -12.235 1.760   -7.811  1.00 15.03 ? 214 ASN A CA  1 
ATOM   1396 C C   . ASN A 1 189 ? -12.078 3.237   -8.162  1.00 11.87 ? 214 ASN A C   1 
ATOM   1397 O O   . ASN A 1 189 ? -13.060 3.947   -8.390  1.00 13.73 ? 214 ASN A O   1 
ATOM   1398 C CB  . ASN A 1 189 ? -12.531 0.954   -9.079  1.00 10.93 ? 214 ASN A CB  1 
ATOM   1399 C CG  . ASN A 1 189 ? -11.410 1.031   -10.101 1.00 13.02 ? 214 ASN A CG  1 
ATOM   1400 O OD1 . ASN A 1 189 ? -10.241 1.142   -9.746  1.00 16.28 ? 214 ASN A OD1 1 
ATOM   1401 N ND2 . ASN A 1 189 ? -11.769 1.019   -11.377 1.00 12.14 ? 214 ASN A ND2 1 
ATOM   1402 N N   . THR A 1 190 ? -10.828 3.691   -8.229  1.00 12.51 ? 215 THR A N   1 
ATOM   1403 C CA  . THR A 1 190 ? -10.520 5.074   -8.568  1.00 16.74 ? 215 THR A CA  1 
ATOM   1404 C C   . THR A 1 190 ? -10.168 5.271   -10.036 1.00 11.22 ? 215 THR A C   1 
ATOM   1405 O O   . THR A 1 190 ? -10.087 6.421   -10.479 1.00 13.66 ? 215 THR A O   1 
ATOM   1406 C CB  . THR A 1 190 ? -9.386  5.615   -7.686  1.00 16.70 ? 215 THR A CB  1 
ATOM   1407 O OG1 . THR A 1 190 ? -8.155  4.954   -8.012  1.00 16.96 ? 215 THR A OG1 1 
ATOM   1408 C CG2 . THR A 1 190 ? -9.714  5.410   -6.210  1.00 21.10 ? 215 THR A CG2 1 
ATOM   1409 N N   . THR A 1 191 ? -9.988  4.191   -10.803 1.00 11.98 ? 216 THR A N   1 
ATOM   1410 C CA  . THR A 1 191 ? -9.359  4.268   -12.117 1.00 16.34 ? 216 THR A CA  1 
ATOM   1411 C C   . THR A 1 191 ? -10.344 4.074   -13.260 1.00 21.20 ? 216 THR A C   1 
ATOM   1412 O O   . THR A 1 191 ? -9.927  4.036   -14.422 1.00 20.00 ? 216 THR A O   1 
ATOM   1413 C CB  . THR A 1 191 ? -8.274  3.197   -12.246 1.00 20.63 ? 216 THR A CB  1 
ATOM   1414 O OG1 . THR A 1 191 ? -8.897  1.901   -12.294 1.00 19.48 ? 216 THR A OG1 1 
ATOM   1415 C CG2 . THR A 1 191 ? -7.318  3.255   -11.045 1.00 19.93 ? 216 THR A CG2 1 
ATOM   1416 N N   . GLY A 1 192 ? -11.636 3.978   -12.970 1.00 12.83 ? 217 GLY A N   1 
ATOM   1417 C CA  . GLY A 1 192 ? -12.568 3.470   -13.948 1.00 14.03 ? 217 GLY A CA  1 
ATOM   1418 C C   . GLY A 1 192 ? -13.420 4.474   -14.686 1.00 17.30 ? 217 GLY A C   1 
ATOM   1419 O O   . GLY A 1 192 ? -14.169 4.074   -15.583 1.00 20.10 ? 217 GLY A O   1 
ATOM   1420 N N   . ALA A 1 193 ? -13.344 5.764   -14.348 1.00 9.17  ? 218 ALA A N   1 
ATOM   1421 C CA  . ALA A 1 193 ? -14.361 6.684   -14.846 1.00 19.47 ? 218 ALA A CA  1 
ATOM   1422 C C   . ALA A 1 193 ? -14.252 6.946   -16.342 1.00 17.01 ? 218 ALA A C   1 
ATOM   1423 O O   . ALA A 1 193 ? -15.228 7.412   -16.937 1.00 13.16 ? 218 ALA A O   1 
ATOM   1424 C CB  . ALA A 1 193 ? -14.293 8.013   -14.091 1.00 19.17 ? 218 ALA A CB  1 
ATOM   1425 N N   . ALA A 1 194 ? -13.112 6.640   -16.970 1.00 15.78 ? 219 ALA A N   1 
ATOM   1426 C CA  . ALA A 1 194 ? -12.943 6.878   -18.398 1.00 11.00 ? 219 ALA A CA  1 
ATOM   1427 C C   . ALA A 1 194 ? -13.243 5.657   -19.252 1.00 11.34 ? 219 ALA A C   1 
ATOM   1428 O O   . ALA A 1 194 ? -13.175 5.748   -20.483 1.00 14.84 ? 219 ALA A O   1 
ATOM   1429 C CB  . ALA A 1 194 ? -11.526 7.388   -18.702 1.00 11.56 ? 219 ALA A CB  1 
ATOM   1430 N N   . SER A 1 195 ? -13.588 4.531   -18.647 1.00 18.56 ? 220 SER A N   1 
ATOM   1431 C CA  . SER A 1 195 ? -13.659 3.250   -19.344 1.00 15.73 ? 220 SER A CA  1 
ATOM   1432 C C   . SER A 1 195 ? -15.131 2.852   -19.458 1.00 17.51 ? 220 SER A C   1 
ATOM   1433 O O   . SER A 1 195 ? -15.914 3.658   -19.972 1.00 24.44 ? 220 SER A O   1 
ATOM   1434 C CB  . SER A 1 195 ? -12.761 2.246   -18.635 1.00 16.59 ? 220 SER A CB  1 
ATOM   1435 O OG  . SER A 1 195 ? -11.418 2.694   -18.633 1.00 10.25 ? 220 SER A OG  1 
ATOM   1436 N N   . ILE A 1 196 ? -15.544 1.654   -19.023 1.00 15.90 ? 221 ILE A N   1 
ATOM   1437 C CA  . ILE A 1 196 ? -16.945 1.244   -19.158 1.00 16.26 ? 221 ILE A CA  1 
ATOM   1438 C C   . ILE A 1 196 ? -17.879 2.296   -18.567 1.00 24.72 ? 221 ILE A C   1 
ATOM   1439 O O   . ILE A 1 196 ? -18.896 2.657   -19.175 1.00 21.41 ? 221 ILE A O   1 
ATOM   1440 C CB  . ILE A 1 196 ? -17.175 -0.143  -18.524 1.00 12.18 ? 221 ILE A CB  1 
ATOM   1441 C CG1 . ILE A 1 196 ? -16.610 -1.247  -19.423 1.00 15.65 ? 221 ILE A CG1 1 
ATOM   1442 C CG2 . ILE A 1 196 ? -18.650 -0.379  -18.224 1.00 12.54 ? 221 ILE A CG2 1 
ATOM   1443 C CD1 . ILE A 1 196 ? -16.536 -2.603  -18.751 1.00 13.61 ? 221 ILE A CD1 1 
ATOM   1444 N N   . ARG A 1 197 ? -17.537 2.811   -17.378 1.00 17.68 ? 222 ARG A N   1 
ATOM   1445 C CA  . ARG A 1 197 ? -18.383 3.792   -16.699 1.00 18.25 ? 222 ARG A CA  1 
ATOM   1446 C C   . ARG A 1 197 ? -18.795 4.931   -17.622 1.00 16.16 ? 222 ARG A C   1 
ATOM   1447 O O   . ARG A 1 197 ? -19.936 5.403   -17.566 1.00 21.83 ? 222 ARG A O   1 
ATOM   1448 C CB  . ARG A 1 197 ? -17.655 4.358   -15.477 1.00 23.93 ? 222 ARG A CB  1 
ATOM   1449 C CG  . ARG A 1 197 ? -18.438 4.286   -14.172 1.00 40.41 ? 222 ARG A CG  1 
ATOM   1450 C CD  . ARG A 1 197 ? -17.536 4.598   -12.974 1.00 45.27 ? 222 ARG A CD  1 
ATOM   1451 N NE  . ARG A 1 197 ? -16.836 3.411   -12.498 1.00 39.43 ? 222 ARG A NE  1 
ATOM   1452 C CZ  . ARG A 1 197 ? -17.091 2.801   -11.348 1.00 49.61 ? 222 ARG A CZ  1 
ATOM   1453 N NH1 . ARG A 1 197 ? -18.010 3.259   -10.512 1.00 43.45 ? 222 ARG A NH1 1 
ATOM   1454 N NH2 . ARG A 1 197 ? -16.401 1.709   -11.024 1.00 26.25 ? 222 ARG A NH2 1 
ATOM   1455 N N   . ALA A 1 198 ? -17.880 5.380   -18.487 1.00 15.30 ? 223 ALA A N   1 
ATOM   1456 C CA  . ALA A 1 198 ? -18.144 6.543   -19.327 1.00 17.08 ? 223 ALA A CA  1 
ATOM   1457 C C   . ALA A 1 198 ? -19.187 6.269   -20.404 1.00 20.31 ? 223 ALA A C   1 
ATOM   1458 O O   . ALA A 1 198 ? -19.813 7.216   -20.893 1.00 25.59 ? 223 ALA A O   1 
ATOM   1459 C CB  . ALA A 1 198 ? -16.845 7.032   -19.967 1.00 23.33 ? 223 ALA A CB  1 
ATOM   1460 N N   . GLY A 1 199 ? -19.375 5.014   -20.798 1.00 16.01 ? 224 GLY A N   1 
ATOM   1461 C CA  . GLY A 1 199 ? -20.345 4.666   -21.813 1.00 12.65 ? 224 GLY A CA  1 
ATOM   1462 C C   . GLY A 1 199 ? -21.707 4.309   -21.272 1.00 19.56 ? 224 GLY A C   1 
ATOM   1463 O O   . GLY A 1 199 ? -22.628 4.021   -22.041 1.00 19.02 ? 224 GLY A O   1 
ATOM   1464 N N   . LEU A 1 200 ? -21.879 4.354   -19.964 1.00 16.97 ? 225 LEU A N   1 
ATOM   1465 C CA  . LEU A 1 200 ? -23.098 3.939   -19.303 1.00 17.22 ? 225 LEU A CA  1 
ATOM   1466 C C   . LEU A 1 200 ? -23.829 5.167   -18.779 1.00 22.80 ? 225 LEU A C   1 
ATOM   1467 O O   . LEU A 1 200 ? -23.209 6.215   -18.567 1.00 20.63 ? 225 LEU A O   1 
ATOM   1468 C CB  . LEU A 1 200 ? -22.775 2.999   -18.138 1.00 19.79 ? 225 LEU A CB  1 
ATOM   1469 C CG  . LEU A 1 200 ? -21.968 1.752   -18.506 1.00 22.00 ? 225 LEU A CG  1 
ATOM   1470 C CD1 . LEU A 1 200 ? -21.743 0.902   -17.269 1.00 15.44 ? 225 LEU A CD1 1 
ATOM   1471 C CD2 . LEU A 1 200 ? -22.606 0.954   -19.637 1.00 23.98 ? 225 LEU A CD2 1 
ATOM   1472 N N   . PRO A 1 201 ? -25.154 5.094   -18.593 1.00 27.75 ? 226 PRO A N   1 
ATOM   1473 C CA  . PRO A 1 201 ? -25.861 6.226   -17.973 1.00 18.85 ? 226 PRO A CA  1 
ATOM   1474 C C   . PRO A 1 201 ? -25.304 6.531   -16.589 1.00 21.78 ? 226 PRO A C   1 
ATOM   1475 O O   . PRO A 1 201 ? -24.917 5.636   -15.835 1.00 25.73 ? 226 PRO A O   1 
ATOM   1476 C CB  . PRO A 1 201 ? -27.313 5.750   -17.911 1.00 17.77 ? 226 PRO A CB  1 
ATOM   1477 C CG  . PRO A 1 201 ? -27.410 4.676   -18.932 1.00 24.98 ? 226 PRO A CG  1 
ATOM   1478 C CD  . PRO A 1 201 ? -26.071 4.015   -18.992 1.00 19.05 ? 226 PRO A CD  1 
ATOM   1479 N N   . THR A 1 202 ? -25.263 7.825   -16.266 1.00 22.19 ? 227 THR A N   1 
ATOM   1480 C CA  . THR A 1 202 ? -24.680 8.285   -15.001 1.00 22.38 ? 227 THR A CA  1 
ATOM   1481 C C   . THR A 1 202 ? -25.376 7.717   -13.763 1.00 26.28 ? 227 THR A C   1 
ATOM   1482 O O   . THR A 1 202 ? -24.731 7.515   -12.727 1.00 36.94 ? 227 THR A O   1 
ATOM   1483 C CB  . THR A 1 202 ? -24.659 9.804   -14.980 1.00 27.30 ? 227 THR A CB  1 
ATOM   1484 O OG1 . THR A 1 202 ? -23.909 10.287  -16.104 1.00 14.71 ? 227 THR A OG1 1 
ATOM   1485 C CG2 . THR A 1 202 ? -24.010 10.337  -13.706 1.00 39.62 ? 227 THR A CG2 1 
ATOM   1486 N N   . SER A 1 203 ? -26.671 7.412   -13.849 1.00 25.08 ? 228 SER A N   1 
ATOM   1487 C CA  . SER A 1 203 ? -27.392 6.922   -12.675 1.00 23.91 ? 228 SER A CA  1 
ATOM   1488 C C   . SER A 1 203 ? -27.028 5.485   -12.303 1.00 32.60 ? 228 SER A C   1 
ATOM   1489 O O   . SER A 1 203 ? -27.323 5.058   -11.181 1.00 34.61 ? 228 SER A O   1 
ATOM   1490 C CB  . SER A 1 203 ? -28.902 7.025   -12.904 1.00 32.00 ? 228 SER A CB  1 
ATOM   1491 O OG  . SER A 1 203 ? -29.316 6.054   -13.859 1.00 32.09 ? 228 SER A OG  1 
ATOM   1492 N N   . TRP A 1 204 ? -26.364 4.761   -13.192 1.00 31.50 ? 229 TRP A N   1 
ATOM   1493 C CA  . TRP A 1 204 ? -25.998 3.381   -12.942 1.00 25.21 ? 229 TRP A CA  1 
ATOM   1494 C C   . TRP A 1 204 ? -24.737 3.260   -12.107 1.00 24.71 ? 229 TRP A C   1 
ATOM   1495 O O   . TRP A 1 204 ? -23.746 3.961   -12.334 1.00 32.43 ? 229 TRP A O   1 
ATOM   1496 C CB  . TRP A 1 204 ? -25.792 2.614   -14.245 1.00 24.57 ? 229 TRP A CB  1 
ATOM   1497 C CG  . TRP A 1 204 ? -26.956 2.615   -15.194 1.00 35.31 ? 229 TRP A CG  1 
ATOM   1498 C CD1 . TRP A 1 204 ? -28.125 3.323   -15.084 1.00 34.26 ? 229 TRP A CD1 1 
ATOM   1499 C CD2 . TRP A 1 204 ? -27.099 1.788   -16.349 1.00 25.87 ? 229 TRP A CD2 1 
ATOM   1500 N NE1 . TRP A 1 204 ? -28.961 3.025   -16.135 1.00 28.67 ? 229 TRP A NE1 1 
ATOM   1501 C CE2 . TRP A 1 204 ? -28.356 2.080   -16.923 1.00 30.03 ? 229 TRP A CE2 1 
ATOM   1502 C CE3 . TRP A 1 204 ? -26.278 0.843   -16.967 1.00 17.93 ? 229 TRP A CE3 1 
ATOM   1503 C CZ2 . TRP A 1 204 ? -28.806 1.457   -18.087 1.00 37.83 ? 229 TRP A CZ2 1 
ATOM   1504 C CZ3 . TRP A 1 204 ? -26.724 0.228   -18.121 1.00 27.49 ? 229 TRP A CZ3 1 
ATOM   1505 C CH2 . TRP A 1 204 ? -27.977 0.533   -18.668 1.00 33.59 ? 229 TRP A CH2 1 
ATOM   1506 N N   . THR A 1 205 ? -24.796 2.370   -11.117 1.00 17.57 ? 230 THR A N   1 
ATOM   1507 C CA  . THR A 1 205 ? -23.670 2.119   -10.228 1.00 22.20 ? 230 THR A CA  1 
ATOM   1508 C C   . THR A 1 205 ? -22.755 1.090   -10.866 1.00 22.10 ? 230 THR A C   1 
ATOM   1509 O O   . THR A 1 205 ? -23.219 0.103   -11.433 1.00 24.23 ? 230 THR A O   1 
ATOM   1510 C CB  . THR A 1 205 ? -24.152 1.606   -8.869  1.00 20.93 ? 230 THR A CB  1 
ATOM   1511 O OG1 . THR A 1 205 ? -25.002 2.586   -8.260  1.00 26.07 ? 230 THR A OG1 1 
ATOM   1512 C CG2 . THR A 1 205 ? -22.982 1.310   -7.942  1.00 30.49 ? 230 THR A CG2 1 
ATOM   1513 N N   . VAL A 1 206 ? -21.458 1.333   -10.801 1.00 25.01 ? 231 VAL A N   1 
ATOM   1514 C CA  . VAL A 1 206 ? -20.486 0.457   -11.435 1.00 23.54 ? 231 VAL A CA  1 
ATOM   1515 C C   . VAL A 1 206 ? -19.441 0.090   -10.393 1.00 24.34 ? 231 VAL A C   1 
ATOM   1516 O O   . VAL A 1 206 ? -18.962 0.952   -9.648  1.00 28.62 ? 231 VAL A O   1 
ATOM   1517 C CB  . VAL A 1 206 ? -19.835 1.116   -12.670 1.00 28.24 ? 231 VAL A CB  1 
ATOM   1518 C CG1 . VAL A 1 206 ? -18.745 0.214   -13.262 1.00 21.54 ? 231 VAL A CG1 1 
ATOM   1519 C CG2 . VAL A 1 206 ? -20.893 1.459   -13.715 1.00 27.20 ? 231 VAL A CG2 1 
ATOM   1520 N N   . GLY A 1 207 ? -19.077 -1.183  -10.353 1.00 14.28 ? 232 GLY A N   1 
ATOM   1521 C CA  . GLY A 1 207 ? -17.828 -1.545  -9.726  1.00 17.25 ? 232 GLY A CA  1 
ATOM   1522 C C   . GLY A 1 207 ? -16.979 -2.189  -10.789 1.00 12.50 ? 232 GLY A C   1 
ATOM   1523 O O   . GLY A 1 207 ? -17.461 -3.036  -11.538 1.00 20.29 ? 232 GLY A O   1 
ATOM   1524 N N   . ASP A 1 208 ? -15.717 -1.802  -10.884 1.00 12.88 ? 233 ASP A N   1 
ATOM   1525 C CA  . ASP A 1 208 ? -14.933 -2.224  -12.028 1.00 16.65 ? 233 ASP A CA  1 
ATOM   1526 C C   . ASP A 1 208 ? -13.469 -2.315  -11.646 1.00 17.30 ? 233 ASP A C   1 
ATOM   1527 O O   . ASP A 1 208 ? -13.041 -1.860  -10.581 1.00 13.57 ? 233 ASP A O   1 
ATOM   1528 C CB  . ASP A 1 208 ? -15.108 -1.259  -13.205 1.00 14.85 ? 233 ASP A CB  1 
ATOM   1529 C CG  . ASP A 1 208 ? -14.259 -0.012  -13.055 1.00 22.67 ? 233 ASP A CG  1 
ATOM   1530 O OD1 . ASP A 1 208 ? -14.527 0.773   -12.121 1.00 23.78 ? 233 ASP A OD1 1 
ATOM   1531 O OD2 . ASP A 1 208 ? -13.308 0.175   -13.845 1.00 17.46 ? 233 ASP A OD2 1 
ATOM   1532 N N   . LYS A 1 209 ? -12.711 -2.927  -12.545 1.00 9.30  ? 234 LYS A N   1 
ATOM   1533 C CA  . LYS A 1 209 ? -11.261 -2.963  -12.464 1.00 14.43 ? 234 LYS A CA  1 
ATOM   1534 C C   . LYS A 1 209 ? -10.712 -2.717  -13.857 1.00 9.93  ? 234 LYS A C   1 
ATOM   1535 O O   . LYS A 1 209 ? -11.090 -3.412  -14.807 1.00 12.21 ? 234 LYS A O   1 
ATOM   1536 C CB  . LYS A 1 209 ? -10.763 -4.303  -11.912 1.00 11.64 ? 234 LYS A CB  1 
ATOM   1537 C CG  . LYS A 1 209 ? -9.247  -4.401  -11.799 1.00 13.27 ? 234 LYS A CG  1 
ATOM   1538 C CD  . LYS A 1 209 ? -8.747  -3.527  -10.656 1.00 6.86  ? 234 LYS A CD  1 
ATOM   1539 C CE  . LYS A 1 209 ? -7.249  -3.333  -10.720 1.00 14.45 ? 234 LYS A CE  1 
ATOM   1540 N NZ  . LYS A 1 209 ? -6.874  -2.246  -11.666 1.00 17.30 ? 234 LYS A NZ  1 
ATOM   1541 N N   . THR A 1 210 ? -9.890  -1.685  -13.985 1.00 12.25 ? 235 THR A N   1 
ATOM   1542 C CA  . THR A 1 210 ? -9.290  -1.367  -15.265 1.00 17.98 ? 235 THR A CA  1 
ATOM   1543 C C   . THR A 1 210 ? -7.969  -2.105  -15.379 1.00 18.90 ? 235 THR A C   1 
ATOM   1544 O O   . THR A 1 210 ? -7.439  -2.649  -14.407 1.00 18.95 ? 235 THR A O   1 
ATOM   1545 C CB  . THR A 1 210 ? -9.051  0.135   -15.436 1.00 20.73 ? 235 THR A CB  1 
ATOM   1546 O OG1 . THR A 1 210 ? -8.292  0.633   -14.327 1.00 20.32 ? 235 THR A OG1 1 
ATOM   1547 C CG2 . THR A 1 210 ? -10.365 0.889   -15.555 1.00 17.88 ? 235 THR A CG2 1 
ATOM   1548 N N   . GLY A 1 211 ? -7.427  -2.103  -16.583 1.00 15.02 ? 236 GLY A N   1 
ATOM   1549 C CA  . GLY A 1 211 ? -6.069  -2.565  -16.766 1.00 14.64 ? 236 GLY A CA  1 
ATOM   1550 C C   . GLY A 1 211 ? -5.492  -1.966  -18.022 1.00 15.24 ? 236 GLY A C   1 
ATOM   1551 O O   . GLY A 1 211 ? -6.217  -1.539  -18.924 1.00 13.42 ? 236 GLY A O   1 
ATOM   1552 N N   . SER A 1 212 ? -4.171  -1.961  -18.085 1.00 8.48  ? 237 SER A N   1 
ATOM   1553 C CA  . SER A 1 212 ? -3.529  -1.567  -19.319 1.00 19.93 ? 237 SER A CA  1 
ATOM   1554 C C   . SER A 1 212 ? -2.171  -2.231  -19.390 1.00 18.13 ? 237 SER A C   1 
ATOM   1555 O O   . SER A 1 212 ? -1.617  -2.681  -18.384 1.00 29.92 ? 237 SER A O   1 
ATOM   1556 C CB  . SER A 1 212 ? -3.396  -0.042  -19.416 1.00 20.83 ? 237 SER A CB  1 
ATOM   1557 O OG  . SER A 1 212 ? -4.510  0.512   -20.093 1.00 33.49 ? 237 SER A OG  1 
ATOM   1558 N N   . GLY A 1 213 ? -1.645  -2.291  -20.599 1.00 14.95 ? 238 GLY A N   1 
ATOM   1559 C CA  . GLY A 1 213 ? -0.355  -2.906  -20.783 1.00 21.25 ? 238 GLY A CA  1 
ATOM   1560 C C   . GLY A 1 213 ? 0.262   -2.489  -22.092 1.00 11.23 ? 238 GLY A C   1 
ATOM   1561 O O   . GLY A 1 213 ? -0.279  -1.645  -22.815 1.00 12.60 ? 238 GLY A O   1 
ATOM   1562 N N   . ASP A 1 214 ? 1.313   -3.220  -22.461 1.00 14.77 ? 240 ASP A N   1 
ATOM   1563 C CA  . ASP A 1 214 ? 1.955   -2.990  -23.737 1.00 14.15 ? 240 ASP A CA  1 
ATOM   1564 C C   . ASP A 1 214 ? 0.974   -3.277  -24.870 1.00 18.24 ? 240 ASP A C   1 
ATOM   1565 O O   . ASP A 1 214 ? -0.114  -3.830  -24.669 1.00 11.54 ? 240 ASP A O   1 
ATOM   1566 C CB  . ASP A 1 214 ? 3.178   -3.894  -23.862 1.00 19.55 ? 240 ASP A CB  1 
ATOM   1567 C CG  . ASP A 1 214 ? 4.345   -3.410  -23.034 1.00 20.78 ? 240 ASP A CG  1 
ATOM   1568 O OD1 . ASP A 1 214 ? 4.264   -2.286  -22.490 1.00 30.82 ? 240 ASP A OD1 1 
ATOM   1569 O OD2 . ASP A 1 214 ? 5.328   -4.171  -22.898 1.00 27.91 ? 240 ASP A OD2 1 
ATOM   1570 N N   . TYR A 1 215 ? 1.388   -2.918  -26.083 1.00 12.56 ? 241 TYR A N   1 
ATOM   1571 C CA  . TYR A 1 215 ? 0.529   -3.061  -27.249 1.00 16.32 ? 241 TYR A CA  1 
ATOM   1572 C C   . TYR A 1 215 ? -0.758  -2.268  -27.064 1.00 16.44 ? 241 TYR A C   1 
ATOM   1573 O O   . TYR A 1 215 ? -1.812  -2.631  -27.594 1.00 16.34 ? 241 TYR A O   1 
ATOM   1574 C CB  . TYR A 1 215 ? 0.275   -4.530  -27.597 1.00 9.56  ? 241 TYR A CB  1 
ATOM   1575 C CG  . TYR A 1 215 ? 1.545   -5.187  -28.111 1.00 22.67 ? 241 TYR A CG  1 
ATOM   1576 C CD1 . TYR A 1 215 ? 2.463   -5.771  -27.244 1.00 15.24 ? 241 TYR A CD1 1 
ATOM   1577 C CD2 . TYR A 1 215 ? 1.853   -5.159  -29.469 1.00 26.22 ? 241 TYR A CD2 1 
ATOM   1578 C CE1 . TYR A 1 215 ? 3.636   -6.353  -27.722 1.00 18.95 ? 241 TYR A CE1 1 
ATOM   1579 C CE2 . TYR A 1 215 ? 3.021   -5.727  -29.955 1.00 24.74 ? 241 TYR A CE2 1 
ATOM   1580 C CZ  . TYR A 1 215 ? 3.907   -6.322  -29.081 1.00 25.35 ? 241 TYR A CZ  1 
ATOM   1581 O OH  . TYR A 1 215 ? 5.057   -6.888  -29.579 1.00 19.45 ? 241 TYR A OH  1 
ATOM   1582 N N   . GLY A 1 216 ? -0.661  -1.162  -26.324 1.00 18.49 ? 242 GLY A N   1 
ATOM   1583 C CA  . GLY A 1 216 ? -1.811  -0.303  -26.118 1.00 13.66 ? 242 GLY A CA  1 
ATOM   1584 C C   . GLY A 1 216 ? -2.956  -1.038  -25.474 1.00 14.58 ? 242 GLY A C   1 
ATOM   1585 O O   . GLY A 1 216 ? -4.118  -0.667  -25.674 1.00 17.20 ? 242 GLY A O   1 
ATOM   1586 N N   . THR A 1 217 ? -2.656  -2.058  -24.671 1.00 15.82 ? 243 THR A N   1 
ATOM   1587 C CA  . THR A 1 217 ? -3.719  -2.877  -24.107 1.00 10.92 ? 243 THR A CA  1 
ATOM   1588 C C   . THR A 1 217 ? -4.509  -2.071  -23.089 1.00 16.82 ? 243 THR A C   1 
ATOM   1589 O O   . THR A 1 217 ? -3.937  -1.470  -22.176 1.00 17.39 ? 243 THR A O   1 
ATOM   1590 C CB  . THR A 1 217 ? -3.137  -4.132  -23.468 1.00 15.65 ? 243 THR A CB  1 
ATOM   1591 O OG1 . THR A 1 217 ? -2.503  -4.914  -24.486 1.00 14.06 ? 243 THR A OG1 1 
ATOM   1592 C CG2 . THR A 1 217 ? -4.247  -4.965  -22.839 1.00 10.44 ? 243 THR A CG2 1 
ATOM   1593 N N   . THR A 1 218 ? -5.830  -2.086  -23.248 1.00 7.26  ? 244 THR A N   1 
ATOM   1594 C CA  . THR A 1 218 ? -6.752  -1.240  -22.506 1.00 13.30 ? 244 THR A CA  1 
ATOM   1595 C C   . THR A 1 218 ? -7.950  -2.109  -22.154 1.00 11.92 ? 244 THR A C   1 
ATOM   1596 O O   . THR A 1 218 ? -8.695  -2.539  -23.041 1.00 11.17 ? 244 THR A O   1 
ATOM   1597 C CB  . THR A 1 218 ? -7.179  -0.043  -23.360 1.00 13.93 ? 244 THR A CB  1 
ATOM   1598 O OG1 . THR A 1 218 ? -6.022  0.548   -23.968 1.00 21.21 ? 244 THR A OG1 1 
ATOM   1599 C CG2 . THR A 1 218 ? -7.864  1.006   -22.512 1.00 16.85 ? 244 THR A CG2 1 
ATOM   1600 N N   . ASN A 1 219 ? -8.128  -2.381  -20.866 1.00 13.06 ? 245 ASN A N   1 
ATOM   1601 C CA  . ASN A 1 219 ? -9.086  -3.371  -20.410 1.00 10.63 ? 245 ASN A CA  1 
ATOM   1602 C C   . ASN A 1 219 ? -9.957  -2.765  -19.329 1.00 15.08 ? 245 ASN A C   1 
ATOM   1603 O O   . ASN A 1 219 ? -9.530  -1.881  -18.582 1.00 16.64 ? 245 ASN A O   1 
ATOM   1604 C CB  . ASN A 1 219 ? -8.411  -4.622  -19.825 1.00 10.79 ? 245 ASN A CB  1 
ATOM   1605 C CG  . ASN A 1 219 ? -7.573  -5.366  -20.831 1.00 13.72 ? 245 ASN A CG  1 
ATOM   1606 O OD1 . ASN A 1 219 ? -7.851  -5.335  -22.028 1.00 13.89 ? 245 ASN A OD1 1 
ATOM   1607 N ND2 . ASN A 1 219 ? -6.565  -6.086  -20.344 1.00 13.85 ? 245 ASN A ND2 1 
ATOM   1608 N N   . ASP A 1 220 ? -11.148 -3.335  -19.190 1.00 17.52 ? 246 ASP A N   1 
ATOM   1609 C CA  . ASP A 1 220 ? -12.015 -3.016  -18.071 1.00 15.89 ? 246 ASP A CA  1 
ATOM   1610 C C   . ASP A 1 220 ? -12.958 -4.184  -17.860 1.00 14.06 ? 246 ASP A C   1 
ATOM   1611 O O   . ASP A 1 220 ? -13.424 -4.796  -18.822 1.00 21.33 ? 246 ASP A O   1 
ATOM   1612 C CB  . ASP A 1 220 ? -12.803 -1.726  -18.332 1.00 14.35 ? 246 ASP A CB  1 
ATOM   1613 C CG  . ASP A 1 220 ? -13.335 -1.101  -17.059 1.00 24.61 ? 246 ASP A CG  1 
ATOM   1614 O OD1 . ASP A 1 220 ? -14.463 -0.567  -17.070 1.00 23.78 ? 246 ASP A OD1 1 
ATOM   1615 O OD2 . ASP A 1 220 ? -12.627 -1.163  -16.036 1.00 28.71 ? 246 ASP A OD2 1 
ATOM   1616 N N   . ILE A 1 221 ? -13.209 -4.514  -16.601 1.00 12.43 ? 247 ILE A N   1 
ATOM   1617 C CA  . ILE A 1 221 ? -14.215 -5.512  -16.266 1.00 14.15 ? 247 ILE A CA  1 
ATOM   1618 C C   . ILE A 1 221 ? -15.085 -4.916  -15.174 1.00 14.62 ? 247 ILE A C   1 
ATOM   1619 O O   . ILE A 1 221 ? -14.570 -4.333  -14.215 1.00 18.85 ? 247 ILE A O   1 
ATOM   1620 C CB  . ILE A 1 221 ? -13.600 -6.869  -15.850 1.00 14.09 ? 247 ILE A CB  1 
ATOM   1621 C CG1 . ILE A 1 221 ? -12.872 -6.784  -14.503 1.00 19.67 ? 247 ILE A CG1 1 
ATOM   1622 C CG2 . ILE A 1 221 ? -12.702 -7.418  -16.954 1.00 16.90 ? 247 ILE A CG2 1 
ATOM   1623 C CD1 . ILE A 1 221 ? -12.317 -8.123  -14.024 1.00 15.87 ? 247 ILE A CD1 1 
ATOM   1624 N N   . ALA A 1 222 ? -16.399 -5.024  -15.337 1.00 13.72 ? 248 ALA A N   1 
ATOM   1625 C CA  . ALA A 1 222 ? -17.317 -4.265  -14.508 1.00 10.50 ? 248 ALA A CA  1 
ATOM   1626 C C   . ALA A 1 222 ? -18.555 -5.080  -14.166 1.00 11.41 ? 248 ALA A C   1 
ATOM   1627 O O   . ALA A 1 222 ? -19.088 -5.808  -15.006 1.00 9.71  ? 248 ALA A O   1 
ATOM   1628 C CB  . ALA A 1 222 ? -17.728 -2.965  -15.214 1.00 9.23  ? 248 ALA A CB  1 
ATOM   1629 N N   . VAL A 1 223 ? -19.005 -4.946  -12.926 1.00 11.03 ? 249 VAL A N   1 
ATOM   1630 C CA  . VAL A 1 223 ? -20.368 -5.269  -12.533 1.00 16.44 ? 249 VAL A CA  1 
ATOM   1631 C C   . VAL A 1 223 ? -21.161 -3.972  -12.540 1.00 15.11 ? 249 VAL A C   1 
ATOM   1632 O O   . VAL A 1 223 ? -20.706 -2.952  -12.007 1.00 18.56 ? 249 VAL A O   1 
ATOM   1633 C CB  . VAL A 1 223 ? -20.409 -5.933  -11.150 1.00 15.01 ? 249 VAL A CB  1 
ATOM   1634 C CG1 . VAL A 1 223 ? -21.814 -6.409  -10.849 1.00 19.19 ? 249 VAL A CG1 1 
ATOM   1635 C CG2 . VAL A 1 223 ? -19.422 -7.076  -11.105 1.00 11.35 ? 249 VAL A CG2 1 
ATOM   1636 N N   . ILE A 1 224 ? -22.334 -3.997  -13.159 1.00 16.94 ? 250 ILE A N   1 
ATOM   1637 C CA  . ILE A 1 224 ? -23.132 -2.801  -13.367 1.00 17.14 ? 250 ILE A CA  1 
ATOM   1638 C C   . ILE A 1 224 ? -24.474 -3.018  -12.691 1.00 15.73 ? 250 ILE A C   1 
ATOM   1639 O O   . ILE A 1 224 ? -25.107 -4.058  -12.885 1.00 23.36 ? 250 ILE A O   1 
ATOM   1640 C CB  . ILE A 1 224 ? -23.318 -2.525  -14.871 1.00 14.32 ? 250 ILE A CB  1 
ATOM   1641 C CG1 . ILE A 1 224 ? -21.958 -2.327  -15.554 1.00 23.88 ? 250 ILE A CG1 1 
ATOM   1642 C CG2 . ILE A 1 224 ? -24.195 -1.307  -15.094 1.00 23.31 ? 250 ILE A CG2 1 
ATOM   1643 C CD1 . ILE A 1 224 ? -21.973 -2.621  -17.049 1.00 16.77 ? 250 ILE A CD1 1 
ATOM   1644 N N   . TRP A 1 225 ? -24.903 -2.053  -11.886 1.00 16.15 ? 251 TRP A N   1 
ATOM   1645 C CA  . TRP A 1 225 ? -26.243 -2.063  -11.317 1.00 18.57 ? 251 TRP A CA  1 
ATOM   1646 C C   . TRP A 1 225 ? -27.032 -0.941  -11.968 1.00 13.61 ? 251 TRP A C   1 
ATOM   1647 O O   . TRP A 1 225 ? -26.911 0.232   -11.563 1.00 22.88 ? 251 TRP A O   1 
ATOM   1648 C CB  . TRP A 1 225 ? -26.208 -1.905  -9.798  1.00 17.88 ? 251 TRP A CB  1 
ATOM   1649 C CG  . TRP A 1 225 ? -25.676 -3.105  -9.089  1.00 23.10 ? 251 TRP A CG  1 
ATOM   1650 C CD1 . TRP A 1 225 ? -26.410 -4.124  -8.550  1.00 28.10 ? 251 TRP A CD1 1 
ATOM   1651 C CD2 . TRP A 1 225 ? -24.301 -3.418  -8.823  1.00 20.69 ? 251 TRP A CD2 1 
ATOM   1652 N NE1 . TRP A 1 225 ? -25.580 -5.053  -7.970  1.00 24.24 ? 251 TRP A NE1 1 
ATOM   1653 C CE2 . TRP A 1 225 ? -24.281 -4.645  -8.122  1.00 19.21 ? 251 TRP A CE2 1 
ATOM   1654 C CE3 . TRP A 1 225 ? -23.086 -2.787  -9.114  1.00 21.22 ? 251 TRP A CE3 1 
ATOM   1655 C CZ2 . TRP A 1 225 ? -23.096 -5.252  -7.707  1.00 17.43 ? 251 TRP A CZ2 1 
ATOM   1656 C CZ3 . TRP A 1 225 ? -21.905 -3.395  -8.698  1.00 22.32 ? 251 TRP A CZ3 1 
ATOM   1657 C CH2 . TRP A 1 225 ? -21.923 -4.614  -8.001  1.00 21.55 ? 251 TRP A CH2 1 
ATOM   1658 N N   . PRO A 1 226 ? -27.741 -1.222  -13.057 1.00 21.48 ? 252 PRO A N   1 
ATOM   1659 C CA  . PRO A 1 226 ? -28.548 -0.185  -13.699 1.00 33.59 ? 252 PRO A CA  1 
ATOM   1660 C C   . PRO A 1 226 ? -29.713 0.196   -12.801 1.00 37.14 ? 252 PRO A C   1 
ATOM   1661 O O   . PRO A 1 226 ? -30.164 -0.587  -11.960 1.00 28.35 ? 252 PRO A O   1 
ATOM   1662 C CB  . PRO A 1 226 ? -29.008 -0.839  -15.006 1.00 23.95 ? 252 PRO A CB  1 
ATOM   1663 C CG  . PRO A 1 226 ? -28.130 -2.057  -15.168 1.00 27.26 ? 252 PRO A CG  1 
ATOM   1664 C CD  . PRO A 1 226 ? -27.847 -2.504  -13.767 1.00 23.28 ? 252 PRO A CD  1 
ATOM   1665 N N   . GLN A 1 227 ? -30.184 1.421   -12.974 1.00 33.37 ? 254 GLN A N   1 
ATOM   1666 C CA  . GLN A 1 227 ? -31.347 1.882   -12.231 1.00 47.58 ? 254 GLN A CA  1 
ATOM   1667 C C   . GLN A 1 227 ? -32.609 1.087   -12.606 1.00 38.52 ? 254 GLN A C   1 
ATOM   1668 O O   . GLN A 1 227 ? -33.005 1.023   -13.774 1.00 36.28 ? 254 GLN A O   1 
ATOM   1669 C CB  . GLN A 1 227 ? -31.464 3.393   -12.480 1.00 63.37 ? 254 GLN A CB  1 
ATOM   1670 C CG  . GLN A 1 227 ? -31.869 3.825   -13.892 1.00 59.90 ? 254 GLN A CG  1 
ATOM   1671 C CD  . GLN A 1 227 ? -32.675 5.114   -13.915 1.00 69.39 ? 254 GLN A CD  1 
ATOM   1672 O OE1 . GLN A 1 227 ? -32.176 6.164   -14.335 1.00 58.91 ? 254 GLN A OE1 1 
ATOM   1673 N NE2 . GLN A 1 227 ? -33.895 5.060   -13.395 1.00 56.45 ? 254 GLN A NE2 1 
ATOM   1674 N N   . GLY A 1 228 ? -33.212 0.457   -11.597 1.00 31.26 ? 255 GLY A N   1 
ATOM   1675 C CA  . GLY A 1 228 ? -34.461 -0.289  -11.660 1.00 43.50 ? 255 GLY A CA  1 
ATOM   1676 C C   . GLY A 1 228 ? -34.409 -1.639  -12.349 1.00 42.19 ? 255 GLY A C   1 
ATOM   1677 O O   . GLY A 1 228 ? -35.467 -2.188  -12.674 1.00 36.95 ? 255 GLY A O   1 
ATOM   1678 N N   . ARG A 1 229 ? -33.223 -2.203  -12.573 1.00 44.69 ? 256 ARG A N   1 
ATOM   1679 C CA  . ARG A 1 229 ? -33.069 -3.482  -13.263 1.00 42.08 ? 256 ARG A CA  1 
ATOM   1680 C C   . ARG A 1 229 ? -31.980 -4.292  -12.559 1.00 32.90 ? 256 ARG A C   1 
ATOM   1681 O O   . ARG A 1 229 ? -31.124 -3.745  -11.859 1.00 27.07 ? 256 ARG A O   1 
ATOM   1682 C CB  . ARG A 1 229 ? -32.874 -3.324  -14.781 1.00 29.80 ? 256 ARG A CB  1 
ATOM   1683 C CG  . ARG A 1 229 ? -31.561 -2.847  -15.249 1.00 41.33 ? 256 ARG A CG  1 
ATOM   1684 C CD  . ARG A 1 229 ? -31.565 -2.627  -16.769 1.00 37.03 ? 256 ARG A CD  1 
ATOM   1685 N NE  . ARG A 1 229 ? -31.839 -3.802  -17.599 1.00 41.69 ? 256 ARG A NE  1 
ATOM   1686 C CZ  . ARG A 1 229 ? -31.351 -5.029  -17.429 1.00 56.76 ? 256 ARG A CZ  1 
ATOM   1687 N NH1 . ARG A 1 229 ? -30.557 -5.339  -16.414 1.00 32.23 ? 256 ARG A NH1 1 
ATOM   1688 N NH2 . ARG A 1 229 ? -31.680 -5.979  -18.301 1.00 46.73 ? 256 ARG A NH2 1 
ATOM   1689 N N   . ALA A 1 230 ? -32.024 -5.612  -12.758 1.00 29.90 ? 257 ALA A N   1 
ATOM   1690 C CA  . ALA A 1 230 ? -30.976 -6.495  -12.263 1.00 24.39 ? 257 ALA A CA  1 
ATOM   1691 C C   . ALA A 1 230 ? -29.605 -6.199  -12.879 1.00 25.89 ? 257 ALA A C   1 
ATOM   1692 O O   . ALA A 1 230 ? -29.496 -5.615  -13.962 1.00 21.89 ? 257 ALA A O   1 
ATOM   1693 C CB  . ALA A 1 230 ? -31.367 -7.946  -12.548 1.00 16.94 ? 257 ALA A CB  1 
ATOM   1694 N N   . PRO A 1 231 ? -28.540 -6.585  -12.174 1.00 20.81 ? 258 PRO A N   1 
ATOM   1695 C CA  . PRO A 1 231 ? -27.183 -6.231  -12.603 1.00 16.57 ? 258 PRO A CA  1 
ATOM   1696 C C   . PRO A 1 231 ? -26.749 -6.903  -13.896 1.00 20.71 ? 258 PRO A C   1 
ATOM   1697 O O   . PRO A 1 231 ? -27.264 -7.941  -14.316 1.00 26.20 ? 258 PRO A O   1 
ATOM   1698 C CB  . PRO A 1 231 ? -26.298 -6.691  -11.434 1.00 17.67 ? 258 PRO A CB  1 
ATOM   1699 C CG  . PRO A 1 231 ? -27.147 -7.580  -10.602 1.00 10.88 ? 258 PRO A CG  1 
ATOM   1700 C CD  . PRO A 1 231 ? -28.560 -7.194  -10.831 1.00 11.45 ? 258 PRO A CD  1 
ATOM   1701 N N   . LEU A 1 232 ? -25.760 -6.269  -14.515 1.00 14.76 ? 259 LEU A N   1 
ATOM   1702 C CA  . LEU A 1 232 ? -25.066 -6.727  -15.700 1.00 16.75 ? 259 LEU A CA  1 
ATOM   1703 C C   . LEU A 1 232 ? -23.615 -7.009  -15.339 1.00 17.47 ? 259 LEU A C   1 
ATOM   1704 O O   . LEU A 1 232 ? -23.083 -6.464  -14.371 1.00 16.42 ? 259 LEU A O   1 
ATOM   1705 C CB  . LEU A 1 232 ? -25.093 -5.653  -16.795 1.00 16.71 ? 259 LEU A CB  1 
ATOM   1706 C CG  . LEU A 1 232 ? -26.401 -4.885  -16.954 1.00 26.98 ? 259 LEU A CG  1 
ATOM   1707 C CD1 . LEU A 1 232 ? -26.205 -3.660  -17.838 1.00 19.71 ? 259 LEU A CD1 1 
ATOM   1708 C CD2 . LEU A 1 232 ? -27.448 -5.799  -17.518 1.00 24.33 ? 259 LEU A CD2 1 
ATOM   1709 N N   . VAL A 1 233 ? -22.978 -7.878  -16.107 1.00 12.56 ? 260 VAL A N   1 
ATOM   1710 C CA  . VAL A 1 233 ? -21.534 -8.039  -16.055 1.00 13.50 ? 260 VAL A CA  1 
ATOM   1711 C C   . VAL A 1 233 ? -21.007 -7.722  -17.443 1.00 16.91 ? 260 VAL A C   1 
ATOM   1712 O O   . VAL A 1 233 ? -21.528 -8.237  -18.437 1.00 23.17 ? 260 VAL A O   1 
ATOM   1713 C CB  . VAL A 1 233 ? -21.112 -9.448  -15.603 1.00 15.88 ? 260 VAL A CB  1 
ATOM   1714 C CG1 . VAL A 1 233 ? -19.604 -9.565  -15.631 1.00 17.25 ? 260 VAL A CG1 1 
ATOM   1715 C CG2 . VAL A 1 233 ? -21.626 -9.718  -14.190 1.00 22.32 ? 260 VAL A CG2 1 
ATOM   1716 N N   . LEU A 1 234 ? -20.000 -6.860  -17.515 1.00 4.98  ? 261 LEU A N   1 
ATOM   1717 C CA  . LEU A 1 234 ? -19.504 -6.381  -18.795 1.00 10.96 ? 261 LEU A CA  1 
ATOM   1718 C C   . LEU A 1 234 ? -17.985 -6.382  -18.766 1.00 14.43 ? 261 LEU A C   1 
ATOM   1719 O O   . LEU A 1 234 ? -17.371 -5.692  -17.950 1.00 11.71 ? 261 LEU A O   1 
ATOM   1720 C CB  . LEU A 1 234 ? -20.047 -4.988  -19.118 1.00 11.04 ? 261 LEU A CB  1 
ATOM   1721 C CG  . LEU A 1 234 ? -19.500 -4.452  -20.440 1.00 19.44 ? 261 LEU A CG  1 
ATOM   1722 C CD1 . LEU A 1 234 ? -19.907 -5.375  -21.585 1.00 12.08 ? 261 LEU A CD1 1 
ATOM   1723 C CD2 . LEU A 1 234 ? -20.041 -3.049  -20.668 1.00 15.45 ? 261 LEU A CD2 1 
ATOM   1724 N N   . VAL A 1 235 ? -17.390 -7.175  -19.647 1.00 17.60 ? 262 VAL A N   1 
ATOM   1725 C CA  . VAL A 1 235 ? -15.948 -7.242  -19.831 1.00 12.10 ? 262 VAL A CA  1 
ATOM   1726 C C   . VAL A 1 235 ? -15.642 -6.643  -21.191 1.00 10.80 ? 262 VAL A C   1 
ATOM   1727 O O   . VAL A 1 235 ? -16.256 -7.036  -22.189 1.00 11.63 ? 262 VAL A O   1 
ATOM   1728 C CB  . VAL A 1 235 ? -15.451 -8.694  -19.748 1.00 9.56  ? 262 VAL A CB  1 
ATOM   1729 C CG1 . VAL A 1 235 ? -14.025 -8.793  -20.240 1.00 20.56 ? 262 VAL A CG1 1 
ATOM   1730 C CG2 . VAL A 1 235 ? -15.608 -9.230  -18.329 1.00 15.29 ? 262 VAL A CG2 1 
ATOM   1731 N N   . THR A 1 236 ? -14.724 -5.679  -21.234 1.00 10.74 ? 263 THR A N   1 
ATOM   1732 C CA  . THR A 1 236 ? -14.263 -5.091  -22.489 1.00 13.20 ? 263 THR A CA  1 
ATOM   1733 C C   . THR A 1 236 ? -12.741 -5.086  -22.487 1.00 13.88 ? 263 THR A C   1 
ATOM   1734 O O   . THR A 1 236 ? -12.114 -4.346  -21.722 1.00 19.34 ? 263 THR A O   1 
ATOM   1735 C CB  . THR A 1 236 ? -14.821 -3.678  -22.697 1.00 13.28 ? 263 THR A CB  1 
ATOM   1736 O OG1 . THR A 1 236 ? -14.421 -2.832  -21.609 1.00 17.81 ? 263 THR A OG1 1 
ATOM   1737 C CG2 . THR A 1 236 ? -16.341 -3.703  -22.803 1.00 15.79 ? 263 THR A CG2 1 
ATOM   1738 N N   . TYR A 1 237 ? -12.157 -5.924  -23.332 1.00 10.08 ? 264 TYR A N   1 
ATOM   1739 C CA  . TYR A 1 237 ? -10.722 -6.025  -23.519 1.00 8.34  ? 264 TYR A CA  1 
ATOM   1740 C C   . TYR A 1 237 ? -10.370 -5.401  -24.859 1.00 14.22 ? 264 TYR A C   1 
ATOM   1741 O O   . TYR A 1 237 ? -11.114 -5.544  -25.831 1.00 12.21 ? 264 TYR A O   1 
ATOM   1742 C CB  . TYR A 1 237 ? -10.273 -7.488  -23.488 1.00 10.14 ? 264 TYR A CB  1 
ATOM   1743 C CG  . TYR A 1 237 ? -10.307 -8.124  -22.108 1.00 23.56 ? 264 TYR A CG  1 
ATOM   1744 C CD1 . TYR A 1 237 ? -10.026 -7.380  -20.979 1.00 28.55 ? 264 TYR A CD1 1 
ATOM   1745 C CD2 . TYR A 1 237 ? -10.603 -9.470  -21.940 1.00 28.28 ? 264 TYR A CD2 1 
ATOM   1746 C CE1 . TYR A 1 237 ? -10.041 -7.944  -19.725 1.00 30.42 ? 264 TYR A CE1 1 
ATOM   1747 C CE2 . TYR A 1 237 ? -10.620 -10.044 -20.679 1.00 28.28 ? 264 TYR A CE2 1 
ATOM   1748 C CZ  . TYR A 1 237 ? -10.339 -9.273  -19.580 1.00 20.30 ? 264 TYR A CZ  1 
ATOM   1749 O OH  . TYR A 1 237 ? -10.351 -9.835  -18.328 1.00 28.40 ? 264 TYR A OH  1 
ATOM   1750 N N   . PHE A 1 238 ? -9.235  -4.718  -24.919 1.00 12.98 ? 265 PHE A N   1 
ATOM   1751 C CA  . PHE A 1 238 ? -8.827  -4.082  -26.159 1.00 10.95 ? 265 PHE A CA  1 
ATOM   1752 C C   . PHE A 1 238 ? -7.313  -4.115  -26.246 1.00 10.74 ? 265 PHE A C   1 
ATOM   1753 O O   . PHE A 1 238 ? -6.633  -3.851  -25.257 1.00 12.37 ? 265 PHE A O   1 
ATOM   1754 C CB  . PHE A 1 238 ? -9.343  -2.644  -26.233 1.00 13.78 ? 265 PHE A CB  1 
ATOM   1755 C CG  . PHE A 1 238 ? -9.013  -1.954  -27.523 1.00 19.75 ? 265 PHE A CG  1 
ATOM   1756 C CD1 . PHE A 1 238 ? -9.657  -2.315  -28.699 1.00 11.98 ? 265 PHE A CD1 1 
ATOM   1757 C CD2 . PHE A 1 238 ? -8.066  -0.938  -27.560 1.00 7.77  ? 265 PHE A CD2 1 
ATOM   1758 C CE1 . PHE A 1 238 ? -9.352  -1.685  -29.896 1.00 14.89 ? 265 PHE A CE1 1 
ATOM   1759 C CE2 . PHE A 1 238 ? -7.763  -0.301  -28.747 1.00 15.04 ? 265 PHE A CE2 1 
ATOM   1760 C CZ  . PHE A 1 238 ? -8.409  -0.674  -29.922 1.00 14.92 ? 265 PHE A CZ  1 
ATOM   1761 N N   . THR A 1 239 ? -6.784  -4.462  -27.410 1.00 6.49  ? 266 THR A N   1 
ATOM   1762 C CA  . THR A 1 239 ? -5.336  -4.493  -27.552 1.00 13.48 ? 266 THR A CA  1 
ATOM   1763 C C   . THR A 1 239 ? -5.021  -4.119  -28.988 1.00 9.83  ? 266 THR A C   1 
ATOM   1764 O O   . THR A 1 239 ? -5.867  -4.231  -29.868 1.00 10.90 ? 266 THR A O   1 
ATOM   1765 C CB  . THR A 1 239 ? -4.739  -5.856  -27.185 1.00 11.06 ? 266 THR A CB  1 
ATOM   1766 O OG1 . THR A 1 239 ? -3.317  -5.728  -27.056 1.00 8.24  ? 266 THR A OG1 1 
ATOM   1767 C CG2 . THR A 1 239 ? -5.037  -6.875  -28.259 1.00 13.14 ? 266 THR A CG2 1 
ATOM   1768 N N   . GLN A 1 240 ? -3.815  -3.639  -29.222 1.00 11.05 ? 267 GLN A N   1 
ATOM   1769 C CA  . GLN A 1 240 ? -3.491  -2.979  -30.476 1.00 14.77 ? 267 GLN A CA  1 
ATOM   1770 C C   . GLN A 1 240 ? -2.241  -3.566  -31.101 1.00 19.77 ? 267 GLN A C   1 
ATOM   1771 O O   . GLN A 1 240 ? -1.481  -4.285  -30.443 1.00 22.91 ? 267 GLN A O   1 
ATOM   1772 C CB  . GLN A 1 240 ? -3.316  -1.467  -30.247 1.00 11.27 ? 267 GLN A CB  1 
ATOM   1773 C CG  . GLN A 1 240 ? -4.521  -0.784  -29.646 1.00 16.74 ? 267 GLN A CG  1 
ATOM   1774 C CD  . GLN A 1 240 ? -4.264  0.675   -29.355 1.00 13.93 ? 267 GLN A CD  1 
ATOM   1775 O OE1 . GLN A 1 240 ? -4.099  1.480   -30.272 1.00 20.05 ? 267 GLN A OE1 1 
ATOM   1776 N NE2 . GLN A 1 240 ? -4.203  1.023   -28.080 1.00 16.73 ? 267 GLN A NE2 1 
ATOM   1777 N N   . PRO A 1 241 ? -1.987  -3.264  -32.385 1.00 24.15 ? 268 PRO A N   1 
ATOM   1778 C CA  . PRO A 1 241 ? -0.930  -3.980  -33.120 1.00 21.05 ? 268 PRO A CA  1 
ATOM   1779 C C   . PRO A 1 241 ? 0.485   -3.531  -32.778 1.00 23.73 ? 268 PRO A C   1 
ATOM   1780 O O   . PRO A 1 241 ? 1.415   -4.329  -32.961 1.00 17.29 ? 268 PRO A O   1 
ATOM   1781 C CB  . PRO A 1 241 ? -1.268  -3.729  -34.600 1.00 12.73 ? 268 PRO A CB  1 
ATOM   1782 C CG  . PRO A 1 241 ? -2.580  -3.051  -34.629 1.00 19.33 ? 268 PRO A CG  1 
ATOM   1783 C CD  . PRO A 1 241 ? -2.856  -2.486  -33.287 1.00 19.42 ? 268 PRO A CD  1 
ATOM   1784 N N   . GLN A 1 242 ? 0.699   -2.321  -32.266 1.00 22.66 ? 269 GLN A N   1 
ATOM   1785 C CA  . GLN A 1 242 ? 2.056   -1.872  -31.992 1.00 25.52 ? 269 GLN A CA  1 
ATOM   1786 C C   . GLN A 1 242 ? 2.351   -1.832  -30.507 1.00 22.26 ? 269 GLN A C   1 
ATOM   1787 O O   . GLN A 1 242 ? 1.499   -1.486  -29.687 1.00 21.99 ? 269 GLN A O   1 
ATOM   1788 C CB  . GLN A 1 242 ? 2.309   -0.444  -32.503 1.00 31.99 ? 269 GLN A CB  1 
ATOM   1789 C CG  . GLN A 1 242 ? 2.541   -0.224  -33.961 1.00 53.20 ? 269 GLN A CG  1 
ATOM   1790 C CD  . GLN A 1 242 ? 4.053   -0.099  -34.184 1.00 64.57 ? 269 GLN A CD  1 
ATOM   1791 O OE1 . GLN A 1 242 ? 4.844   -0.389  -33.276 1.00 52.99 ? 269 GLN A OE1 1 
ATOM   1792 N NE2 . GLN A 1 242 ? 4.455   0.358   -35.365 1.00 52.45 ? 269 GLN A NE2 1 
ATOM   1793 N N   . GLN A 1 243 ? 3.609   -2.156  -30.192 1.00 18.01 ? 270 GLN A N   1 
ATOM   1794 C CA  . GLN A 1 243 ? 3.976   -2.431  -28.810 1.00 22.52 ? 270 GLN A CA  1 
ATOM   1795 C C   . GLN A 1 243 ? 3.866   -1.172  -27.963 1.00 23.58 ? 270 GLN A C   1 
ATOM   1796 O O   . GLN A 1 243 ? 3.424   -1.225  -26.810 1.00 12.88 ? 270 GLN A O   1 
ATOM   1797 C CB  . GLN A 1 243 ? 5.373   -3.051  -28.732 1.00 24.20 ? 270 GLN A CB  1 
ATOM   1798 C CG  . GLN A 1 243 ? 5.972   -3.045  -27.324 1.00 22.83 ? 270 GLN A CG  1 
ATOM   1799 C CD  . GLN A 1 243 ? 7.282   -3.808  -27.231 1.00 28.91 ? 270 GLN A CD  1 
ATOM   1800 O OE1 . GLN A 1 243 ? 8.353   -3.218  -27.085 1.00 31.62 ? 270 GLN A OE1 1 
ATOM   1801 N NE2 . GLN A 1 243 ? 7.198   -5.136  -27.305 1.00 15.71 ? 270 GLN A NE2 1 
ATOM   1802 N N   . ASN A 1 244 ? 4.260   -0.030  -28.525 1.00 17.94 ? 271 ASN A N   1 
ATOM   1803 C CA  . ASN A 1 244 ? 4.276   1.240   -27.814 1.00 29.13 ? 271 ASN A CA  1 
ATOM   1804 C C   . ASN A 1 244 ? 2.986   2.036   -27.992 1.00 24.93 ? 271 ASN A C   1 
ATOM   1805 O O   . ASN A 1 244 ? 2.965   3.233   -27.682 1.00 30.07 ? 271 ASN A O   1 
ATOM   1806 C CB  . ASN A 1 244 ? 5.477   2.074   -28.271 1.00 23.44 ? 271 ASN A CB  1 
ATOM   1807 C CG  . ASN A 1 244 ? 5.256   2.713   -29.631 1.00 46.87 ? 271 ASN A CG  1 
ATOM   1808 O OD1 . ASN A 1 244 ? 4.812   2.054   -30.574 1.00 31.04 ? 271 ASN A OD1 1 
ATOM   1809 N ND2 . ASN A 1 244 ? 5.578   3.998   -29.743 1.00 71.99 ? 271 ASN A ND2 1 
ATOM   1810 N N   . ALA A 1 245 ? 1.912   1.397   -28.457 1.00 25.10 ? 272 ALA A N   1 
ATOM   1811 C CA  . ALA A 1 245 ? 0.682   2.113   -28.764 1.00 28.35 ? 272 ALA A CA  1 
ATOM   1812 C C   . ALA A 1 245 ? 0.077   2.740   -27.512 1.00 23.60 ? 272 ALA A C   1 
ATOM   1813 O O   . ALA A 1 245 ? 0.207   2.226   -26.397 1.00 27.50 ? 272 ALA A O   1 
ATOM   1814 C CB  . ALA A 1 245 ? -0.334  1.171   -29.417 1.00 22.59 ? 272 ALA A CB  1 
ATOM   1815 N N   . GLU A 1 246 ? -0.559  3.886   -27.714 1.00 18.80 ? 273 GLU A N   1 
ATOM   1816 C CA  . GLU A 1 246 ? -1.238  4.622   -26.657 1.00 29.07 ? 273 GLU A CA  1 
ATOM   1817 C C   . GLU A 1 246 ? -2.548  3.955   -26.235 1.00 27.26 ? 273 GLU A C   1 
ATOM   1818 O O   . GLU A 1 246 ? -3.244  3.323   -27.036 1.00 25.76 ? 273 GLU A O   1 
ATOM   1819 C CB  . GLU A 1 246 ? -1.451  6.068   -27.114 1.00 32.89 ? 273 GLU A CB  1 
ATOM   1820 C CG  . GLU A 1 246 ? -2.625  6.281   -28.069 1.00 51.89 ? 273 GLU A CG  1 
ATOM   1821 C CD  . GLU A 1 246 ? -2.408  5.563   -29.406 1.00 52.65 ? 273 GLU A CD  1 
ATOM   1822 O OE1 . GLU A 1 246 ? -1.301  5.691   -29.980 1.00 39.68 ? 273 GLU A OE1 1 
ATOM   1823 O OE2 . GLU A 1 246 ? -3.340  4.880   -29.886 1.00 50.71 ? 273 GLU A OE2 1 
ATOM   1824 N N   . SER A 1 247 ? -2.878  4.117   -24.954 1.00 25.30 ? 274 SER A N   1 
ATOM   1825 C CA  . SER A 1 247 ? -4.115  3.587   -24.390 1.00 22.23 ? 274 SER A CA  1 
ATOM   1826 C C   . SER A 1 247 ? -5.333  4.143   -25.127 1.00 19.15 ? 274 SER A C   1 
ATOM   1827 O O   . SER A 1 247 ? -5.277  5.200   -25.763 1.00 24.25 ? 274 SER A O   1 
ATOM   1828 C CB  . SER A 1 247 ? -4.212  3.943   -22.906 1.00 14.15 ? 274 SER A CB  1 
ATOM   1829 O OG  . SER A 1 247 ? -3.424  3.073   -22.111 1.00 37.65 ? 274 SER A OG  1 
ATOM   1830 N N   . ARG A 1 248 ? -6.454  3.422   -25.033 1.00 17.07 ? 275 ARG A N   1 
ATOM   1831 C CA  . ARG A 1 248 ? -7.688  3.795   -25.738 1.00 16.44 ? 275 ARG A CA  1 
ATOM   1832 C C   . ARG A 1 248 ? -8.916  3.471   -24.883 1.00 17.83 ? 275 ARG A C   1 
ATOM   1833 O O   . ARG A 1 248 ? -9.777  2.664   -25.236 1.00 15.65 ? 275 ARG A O   1 
ATOM   1834 C CB  . ARG A 1 248 ? -7.799  3.108   -27.100 1.00 13.62 ? 275 ARG A CB  1 
ATOM   1835 C CG  . ARG A 1 248 ? -6.767  3.531   -28.148 1.00 20.09 ? 275 ARG A CG  1 
ATOM   1836 C CD  . ARG A 1 248 ? -6.926  4.994   -28.555 1.00 22.95 ? 275 ARG A CD  1 
ATOM   1837 N NE  . ARG A 1 248 ? -8.287  5.300   -28.981 1.00 21.09 ? 275 ARG A NE  1 
ATOM   1838 C CZ  . ARG A 1 248 ? -8.733  5.202   -30.225 1.00 25.09 ? 275 ARG A CZ  1 
ATOM   1839 N NH1 . ARG A 1 248 ? -7.956  4.776   -31.208 1.00 23.45 ? 275 ARG A NH1 1 
ATOM   1840 N NH2 . ARG A 1 248 ? -9.997  5.521   -30.483 1.00 22.21 ? 275 ARG A NH2 1 
ATOM   1841 N N   . ARG A 1 249 ? -9.007  4.142   -23.736 1.00 19.45 ? 276 ARG A N   1 
ATOM   1842 C CA  . ARG A 1 249 ? -10.131 3.943   -22.841 1.00 18.67 ? 276 ARG A CA  1 
ATOM   1843 C C   . ARG A 1 249 ? -11.436 4.404   -23.470 1.00 22.67 ? 276 ARG A C   1 
ATOM   1844 O O   . ARG A 1 249 ? -12.515 3.900   -23.115 1.00 16.57 ? 276 ARG A O   1 
ATOM   1845 C CB  . ARG A 1 249 ? -9.831  4.662   -21.530 1.00 18.24 ? 276 ARG A CB  1 
ATOM   1846 C CG  . ARG A 1 249 ? -8.742  3.961   -20.709 1.00 22.73 ? 276 ARG A CG  1 
ATOM   1847 C CD  . ARG A 1 249 ? -8.365  4.812   -19.518 1.00 27.56 ? 276 ARG A CD  1 
ATOM   1848 N NE  . ARG A 1 249 ? -7.762  4.049   -18.433 1.00 47.06 ? 276 ARG A NE  1 
ATOM   1849 C CZ  . ARG A 1 249 ? -7.407  4.581   -17.273 1.00 59.65 ? 276 ARG A CZ  1 
ATOM   1850 N NH1 . ARG A 1 249 ? -7.649  5.855   -16.997 1.00 40.07 ? 276 ARG A NH1 1 
ATOM   1851 N NH2 . ARG A 1 249 ? -6.924  3.789   -16.320 1.00 40.75 ? 276 ARG A NH2 1 
ATOM   1852 N N   . ASP A 1 250 ? -11.357 5.356   -24.401 1.00 15.47 ? 277 ASP A N   1 
ATOM   1853 C CA  . ASP A 1 250 ? -12.550 5.785   -25.111 1.00 13.92 ? 277 ASP A CA  1 
ATOM   1854 C C   . ASP A 1 250 ? -13.167 4.624   -25.886 1.00 9.60  ? 277 ASP A C   1 
ATOM   1855 O O   . ASP A 1 250 ? -14.380 4.596   -26.094 1.00 7.76  ? 277 ASP A O   1 
ATOM   1856 C CB  . ASP A 1 250 ? -12.224 6.973   -26.016 1.00 12.10 ? 277 ASP A CB  1 
ATOM   1857 C CG  . ASP A 1 250 ? -11.261 6.609   -27.133 1.00 38.68 ? 277 ASP A CG  1 
ATOM   1858 O OD1 . ASP A 1 250 ? -10.104 6.249   -26.820 1.00 24.85 ? 277 ASP A OD1 1 
ATOM   1859 O OD2 . ASP A 1 250 ? -11.654 6.693   -28.317 1.00 34.29 ? 277 ASP A OD2 1 
ATOM   1860 N N   . VAL A 1 251 ? -12.355 3.654   -26.321 1.00 12.84 ? 278 VAL A N   1 
ATOM   1861 C CA  . VAL A 1 251 ? -12.916 2.504   -27.032 1.00 11.26 ? 278 VAL A CA  1 
ATOM   1862 C C   . VAL A 1 251 ? -13.719 1.632   -26.079 1.00 11.14 ? 278 VAL A C   1 
ATOM   1863 O O   . VAL A 1 251 ? -14.780 1.105   -26.441 1.00 13.86 ? 278 VAL A O   1 
ATOM   1864 C CB  . VAL A 1 251 ? -11.813 1.696   -27.738 1.00 16.71 ? 278 VAL A CB  1 
ATOM   1865 C CG1 . VAL A 1 251 ? -12.338 0.305   -28.153 1.00 14.59 ? 278 VAL A CG1 1 
ATOM   1866 C CG2 . VAL A 1 251 ? -11.313 2.463   -28.975 1.00 20.25 ? 278 VAL A CG2 1 
ATOM   1867 N N   . LEU A 1 252 ? -13.239 1.470   -24.848 1.00 11.57 ? 279 LEU A N   1 
ATOM   1868 C CA  . LEU A 1 252 ? -14.015 0.724   -23.872 1.00 12.02 ? 279 LEU A CA  1 
ATOM   1869 C C   . LEU A 1 252 ? -15.315 1.453   -23.577 1.00 14.00 ? 279 LEU A C   1 
ATOM   1870 O O   . LEU A 1 252 ? -16.377 0.827   -23.458 1.00 14.99 ? 279 LEU A O   1 
ATOM   1871 C CB  . LEU A 1 252 ? -13.187 0.495   -22.610 1.00 13.27 ? 279 LEU A CB  1 
ATOM   1872 C CG  . LEU A 1 252 ? -11.824 -0.143  -22.917 1.00 11.56 ? 279 LEU A CG  1 
ATOM   1873 C CD1 . LEU A 1 252 ? -11.089 -0.515  -21.638 1.00 13.01 ? 279 LEU A CD1 1 
ATOM   1874 C CD2 . LEU A 1 252 ? -11.995 -1.364  -23.798 1.00 12.00 ? 279 LEU A CD2 1 
ATOM   1875 N N   . ALA A 1 253 ? -15.246 2.781   -23.447 1.00 13.86 ? 280 ALA A N   1 
ATOM   1876 C CA  . ALA A 1 253 ? -16.462 3.557   -23.230 1.00 14.85 ? 280 ALA A CA  1 
ATOM   1877 C C   . ALA A 1 253 ? -17.424 3.397   -24.403 1.00 16.81 ? 280 ALA A C   1 
ATOM   1878 O O   . ALA A 1 253 ? -18.639 3.293   -24.207 1.00 18.07 ? 280 ALA A O   1 
ATOM   1879 C CB  . ALA A 1 253 ? -16.117 5.030   -23.010 1.00 12.90 ? 280 ALA A CB  1 
ATOM   1880 N N   . SER A 1 254 ? -16.901 3.393   -25.634 1.00 12.58 ? 281 SER A N   1 
ATOM   1881 C CA  . SER A 1 254 ? -17.763 3.244   -26.803 1.00 8.31  ? 281 SER A CA  1 
ATOM   1882 C C   . SER A 1 254 ? -18.425 1.874   -26.823 1.00 13.75 ? 281 SER A C   1 
ATOM   1883 O O   . SER A 1 254 ? -19.611 1.750   -27.160 1.00 18.39 ? 281 SER A O   1 
ATOM   1884 C CB  . SER A 1 254 ? -16.956 3.456   -28.085 1.00 14.32 ? 281 SER A CB  1 
ATOM   1885 O OG  . SER A 1 254 ? -16.519 4.798   -28.212 1.00 14.20 ? 281 SER A OG  1 
ATOM   1886 N N   . ALA A 1 255 ? -17.671 0.829   -26.472 1.00 8.98  ? 282 ALA A N   1 
ATOM   1887 C CA  . ALA A 1 255 ? -18.258 -0.505  -26.442 1.00 16.00 ? 282 ALA A CA  1 
ATOM   1888 C C   . ALA A 1 255 ? -19.339 -0.590  -25.374 1.00 17.19 ? 282 ALA A C   1 
ATOM   1889 O O   . ALA A 1 255 ? -20.422 -1.145  -25.609 1.00 18.40 ? 282 ALA A O   1 
ATOM   1890 C CB  . ALA A 1 255 ? -17.175 -1.558  -26.199 1.00 12.85 ? 282 ALA A CB  1 
ATOM   1891 N N   . ALA A 1 256 ? -19.074 -0.009  -24.201 1.00 15.57 ? 283 ALA A N   1 
ATOM   1892 C CA  . ALA A 1 256 ? -20.072 0.004   -23.138 1.00 16.85 ? 283 ALA A CA  1 
ATOM   1893 C C   . ALA A 1 256 ? -21.307 0.791   -23.547 1.00 20.69 ? 283 ALA A C   1 
ATOM   1894 O O   . ALA A 1 256 ? -22.434 0.420   -23.197 1.00 23.36 ? 283 ALA A O   1 
ATOM   1895 C CB  . ALA A 1 256 ? -19.467 0.587   -21.865 1.00 20.63 ? 283 ALA A CB  1 
ATOM   1896 N N   . ARG A 1 257 ? -21.117 1.880   -24.291 1.00 12.43 ? 284 ARG A N   1 
ATOM   1897 C CA  . ARG A 1 257 ? -22.257 2.677   -24.724 1.00 27.84 ? 284 ARG A CA  1 
ATOM   1898 C C   . ARG A 1 257 ? -23.100 1.907   -25.734 1.00 24.99 ? 284 ARG A C   1 
ATOM   1899 O O   . ARG A 1 257 ? -24.332 1.931   -25.662 1.00 22.07 ? 284 ARG A O   1 
ATOM   1900 C CB  . ARG A 1 257 ? -21.755 4.017   -25.272 1.00 24.97 ? 284 ARG A CB  1 
ATOM   1901 C CG  . ARG A 1 257 ? -22.756 4.851   -26.031 1.00 24.12 ? 284 ARG A CG  1 
ATOM   1902 C CD  . ARG A 1 257 ? -22.307 6.324   -26.128 1.00 23.79 ? 284 ARG A CD  1 
ATOM   1903 N NE  . ARG A 1 257 ? -21.457 6.782   -25.028 1.00 30.25 ? 284 ARG A NE  1 
ATOM   1904 C CZ  . ARG A 1 257 ? -20.144 6.984   -25.112 1.00 40.51 ? 284 ARG A CZ  1 
ATOM   1905 N NH1 . ARG A 1 257 ? -19.486 6.801   -26.247 1.00 31.23 ? 284 ARG A NH1 1 
ATOM   1906 N NH2 . ARG A 1 257 ? -19.478 7.403   -24.038 1.00 22.14 ? 284 ARG A NH2 1 
ATOM   1907 N N   . ILE A 1 258 ? -22.451 1.184   -26.651 1.00 22.67 ? 285 ILE A N   1 
ATOM   1908 C CA  . ILE A 1 258 ? -23.176 0.334   -27.600 1.00 22.44 ? 285 ILE A CA  1 
ATOM   1909 C C   . ILE A 1 258 ? -23.969 -0.742  -26.862 1.00 19.27 ? 285 ILE A C   1 
ATOM   1910 O O   . ILE A 1 258 ? -25.134 -1.012  -27.181 1.00 27.81 ? 285 ILE A O   1 
ATOM   1911 C CB  . ILE A 1 258 ? -22.199 -0.290  -28.615 1.00 24.93 ? 285 ILE A CB  1 
ATOM   1912 C CG1 . ILE A 1 258 ? -21.702 0.755   -29.622 1.00 17.77 ? 285 ILE A CG1 1 
ATOM   1913 C CG2 . ILE A 1 258 ? -22.822 -1.521  -29.290 1.00 22.35 ? 285 ILE A CG2 1 
ATOM   1914 C CD1 . ILE A 1 258 ? -20.395 0.379   -30.294 1.00 16.92 ? 285 ILE A CD1 1 
ATOM   1915 N N   . ILE A 1 259 ? -23.350 -1.350  -25.846 1.00 25.11 ? 286 ILE A N   1 
ATOM   1916 C CA  . ILE A 1 259 ? -23.986 -2.394  -25.040 1.00 28.75 ? 286 ILE A CA  1 
ATOM   1917 C C   . ILE A 1 259 ? -25.204 -1.844  -24.301 1.00 30.21 ? 286 ILE A C   1 
ATOM   1918 O O   . ILE A 1 259 ? -26.262 -2.485  -24.250 1.00 34.24 ? 286 ILE A O   1 
ATOM   1919 C CB  . ILE A 1 259 ? -22.957 -3.019  -24.082 1.00 34.16 ? 286 ILE A CB  1 
ATOM   1920 C CG1 . ILE A 1 259 ? -21.926 -3.820  -24.887 1.00 27.45 ? 286 ILE A CG1 1 
ATOM   1921 C CG2 . ILE A 1 259 ? -23.650 -3.893  -23.048 1.00 39.79 ? 286 ILE A CG2 1 
ATOM   1922 C CD1 . ILE A 1 259 ? -22.449 -5.139  -25.413 1.00 24.32 ? 286 ILE A CD1 1 
ATOM   1923 N N   . ALA A 1 260 ? -25.077 -0.647  -23.726 1.00 21.01 ? 287 ALA A N   1 
ATOM   1924 C CA  . ALA A 1 260 ? -26.171 -0.055  -22.965 1.00 30.73 ? 287 ALA A CA  1 
ATOM   1925 C C   . ALA A 1 260 ? -27.379 0.186   -23.863 1.00 35.64 ? 287 ALA A C   1 
ATOM   1926 O O   . ALA A 1 260 ? -28.524 0.037   -23.422 1.00 37.17 ? 287 ALA A O   1 
ATOM   1927 C CB  . ALA A 1 260 ? -25.718 1.250   -22.305 1.00 30.68 ? 287 ALA A CB  1 
ATOM   1928 N N   . GLU A 1 261 ? -27.148 0.561   -25.125 1.00 38.50 ? 288 GLU A N   1 
ATOM   1929 C CA  . GLU A 1 261 ? -28.254 0.861   -26.025 1.00 34.36 ? 288 GLU A CA  1 
ATOM   1930 C C   . GLU A 1 261 ? -28.982 -0.401  -26.465 1.00 38.58 ? 288 GLU A C   1 
ATOM   1931 O O   . GLU A 1 261 ? -30.127 -0.320  -26.922 1.00 38.02 ? 288 GLU A O   1 
ATOM   1932 C CB  . GLU A 1 261 ? -27.710 1.532   -27.284 1.00 36.79 ? 288 GLU A CB  1 
ATOM   1933 C CG  . GLU A 1 261 ? -26.840 2.734   -27.055 1.00 39.98 ? 288 GLU A CG  1 
ATOM   1934 C CD  . GLU A 1 261 ? -25.940 3.022   -28.258 1.00 61.81 ? 288 GLU A CD  1 
ATOM   1935 O OE1 . GLU A 1 261 ? -26.170 2.437   -29.342 1.00 43.17 ? 288 GLU A OE1 1 
ATOM   1936 O OE2 . GLU A 1 261 ? -24.996 3.832   -28.113 1.00 48.05 ? 288 GLU A OE2 1 
ATOM   1937 N N   . GLY A 1 262 ? -28.347 -1.563  -26.330 1.00 42.66 ? 289 GLY A N   1 
ATOM   1938 C CA  . GLY A 1 262 ? -28.904 -2.842  -26.718 1.00 49.59 ? 289 GLY A CA  1 
ATOM   1939 C C   . GLY A 1 262 ? -29.664 -3.519  -25.601 1.00 53.01 ? 289 GLY A C   1 
ATOM   1940 O O   . GLY A 1 262 ? -30.363 -4.514  -25.824 1.00 46.35 ? 289 GLY A O   1 
ATOM   1941 N N   . LEU A 1 263 ? -29.531 -2.985  -24.390 1.00 58.05 ? 290 LEU A N   1 
ATOM   1942 C CA  . LEU A 1 263 ? -30.183 -3.513  -23.202 1.00 65.99 ? 290 LEU A CA  1 
ATOM   1943 C C   . LEU A 1 263 ? -31.701 -3.380  -23.257 1.00 70.16 ? 290 LEU A C   1 
ATOM   1944 O O   . LEU A 1 263 ? -32.415 -4.292  -22.834 1.00 64.61 ? 290 LEU A O   1 
ATOM   1945 C CB  . LEU A 1 263 ? -29.647 -2.792  -21.964 1.00 58.41 ? 290 LEU A CB  1 
ATOM   1946 C CG  . LEU A 1 263 ? -29.436 -3.634  -20.710 1.00 57.31 ? 290 LEU A CG  1 
ATOM   1947 C CD1 . LEU A 1 263 ? -28.245 -4.560  -20.898 1.00 53.82 ? 290 LEU A CD1 1 
ATOM   1948 C CD2 . LEU A 1 263 ? -29.238 -2.723  -19.511 1.00 59.15 ? 290 LEU A CD2 1 
ATOM   1949 O OXT . LEU A 1 263 ? -32.240 -2.370  -23.715 1.00 57.98 ? 290 LEU A OXT 1 
ATOM   1950 N N   . GLN B 1 1   ? 0.281   39.006  -20.538 1.00 52.40 ? 25  GLN B N   1 
ATOM   1951 C CA  . GLN B 1 1   ? 1.411   38.176  -20.946 1.00 56.63 ? 25  GLN B CA  1 
ATOM   1952 C C   . GLN B 1 1   ? 0.979   36.748  -21.224 1.00 47.31 ? 25  GLN B C   1 
ATOM   1953 O O   . GLN B 1 1   ? 1.234   35.856  -20.414 1.00 45.09 ? 25  GLN B O   1 
ATOM   1954 C CB  . GLN B 1 1   ? 2.500   38.158  -19.871 1.00 46.66 ? 25  GLN B CB  1 
ATOM   1955 C CG  . GLN B 1 1   ? 2.615   39.434  -19.086 1.00 46.23 ? 25  GLN B CG  1 
ATOM   1956 C CD  . GLN B 1 1   ? 1.669   39.507  -17.902 1.00 56.02 ? 25  GLN B CD  1 
ATOM   1957 O OE1 . GLN B 1 1   ? 0.962   38.547  -17.594 1.00 53.51 ? 25  GLN B OE1 1 
ATOM   1958 N NE2 . GLN B 1 1   ? 1.646   40.658  -17.234 1.00 34.68 ? 25  GLN B NE2 1 
ATOM   1959 N N   . THR B 1 2   ? 0.326   36.520  -22.358 1.00 39.09 ? 26  THR B N   1 
ATOM   1960 C CA  . THR B 1 2   ? 0.003   35.152  -22.739 1.00 44.59 ? 26  THR B CA  1 
ATOM   1961 C C   . THR B 1 2   ? 1.303   34.410  -23.019 1.00 41.43 ? 26  THR B C   1 
ATOM   1962 O O   . THR B 1 2   ? 1.945   34.622  -24.054 1.00 39.24 ? 26  THR B O   1 
ATOM   1963 C CB  . THR B 1 2   ? -0.923  35.114  -23.952 1.00 33.68 ? 26  THR B CB  1 
ATOM   1964 O OG1 . THR B 1 2   ? -0.214  35.552  -25.119 1.00 45.02 ? 26  THR B OG1 1 
ATOM   1965 C CG2 . THR B 1 2   ? -2.141  36.006  -23.718 1.00 38.98 ? 26  THR B CG2 1 
ATOM   1966 N N   . SER B 1 3   ? 1.702   33.556  -22.079 1.00 38.68 ? 27  SER B N   1 
ATOM   1967 C CA  . SER B 1 3   ? 2.820   32.642  -22.266 1.00 28.15 ? 27  SER B CA  1 
ATOM   1968 C C   . SER B 1 3   ? 2.491   31.642  -23.368 1.00 31.77 ? 27  SER B C   1 
ATOM   1969 O O   . SER B 1 3   ? 1.683   31.924  -24.258 1.00 31.90 ? 27  SER B O   1 
ATOM   1970 C CB  . SER B 1 3   ? 3.116   31.922  -20.948 1.00 37.96 ? 27  SER B CB  1 
ATOM   1971 O OG  . SER B 1 3   ? 2.016   31.113  -20.547 1.00 32.22 ? 27  SER B OG  1 
ATOM   1972 N N   . ALA B 1 4   ? 3.064   30.447  -23.303 1.00 38.02 ? 28  ALA B N   1 
ATOM   1973 C CA  . ALA B 1 4   ? 2.822   29.485  -24.367 1.00 32.23 ? 28  ALA B CA  1 
ATOM   1974 C C   . ALA B 1 4   ? 1.722   28.546  -23.925 1.00 29.19 ? 28  ALA B C   1 
ATOM   1975 O O   . ALA B 1 4   ? 0.865   28.153  -24.727 1.00 24.34 ? 28  ALA B O   1 
ATOM   1976 C CB  . ALA B 1 4   ? 4.089   28.700  -24.709 1.00 22.74 ? 28  ALA B CB  1 
ATOM   1977 N N   . VAL B 1 5   ? 1.752   28.181  -22.646 1.00 29.94 ? 29  VAL B N   1 
ATOM   1978 C CA  . VAL B 1 5   ? 0.797   27.219  -22.138 1.00 19.24 ? 29  VAL B CA  1 
ATOM   1979 C C   . VAL B 1 5   ? -0.592  27.845  -22.226 1.00 23.49 ? 29  VAL B C   1 
ATOM   1980 O O   . VAL B 1 5   ? -1.569  27.189  -22.599 1.00 24.88 ? 29  VAL B O   1 
ATOM   1981 C CB  . VAL B 1 5   ? 1.204   26.789  -20.708 1.00 22.49 ? 29  VAL B CB  1 
ATOM   1982 C CG1 . VAL B 1 5   ? 0.984   27.898  -19.689 1.00 30.54 ? 29  VAL B CG1 1 
ATOM   1983 C CG2 . VAL B 1 5   ? 0.484   25.531  -20.280 1.00 31.66 ? 29  VAL B CG2 1 
ATOM   1984 N N   . GLN B 1 6   ? -0.686  29.142  -21.893 1.00 24.46 ? 30  GLN B N   1 
ATOM   1985 C CA  . GLN B 1 6   ? -1.939  29.887  -21.999 1.00 26.74 ? 30  GLN B CA  1 
ATOM   1986 C C   . GLN B 1 6   ? -2.443  29.952  -23.438 1.00 25.80 ? 30  GLN B C   1 
ATOM   1987 O O   . GLN B 1 6   ? -3.654  29.936  -23.675 1.00 21.37 ? 30  GLN B O   1 
ATOM   1988 C CB  . GLN B 1 6   ? -1.777  31.294  -21.420 1.00 32.69 ? 30  GLN B CB  1 
ATOM   1989 C CG  . GLN B 1 6   ? -1.672  31.301  -19.899 1.00 30.99 ? 30  GLN B CG  1 
ATOM   1990 C CD  . GLN B 1 6   ? -1.250  32.637  -19.330 1.00 42.68 ? 30  GLN B CD  1 
ATOM   1991 O OE1 . GLN B 1 6   ? -2.090  33.508  -19.087 1.00 30.72 ? 30  GLN B OE1 1 
ATOM   1992 N NE2 . GLN B 1 6   ? 0.049   32.806  -19.102 1.00 54.87 ? 30  GLN B NE2 1 
ATOM   1993 N N   . GLN B 1 7   ? -1.539  30.068  -24.415 1.00 20.89 ? 31  GLN B N   1 
ATOM   1994 C CA  . GLN B 1 7   ? -1.996  30.136  -25.801 1.00 23.55 ? 31  GLN B CA  1 
ATOM   1995 C C   . GLN B 1 7   ? -2.485  28.783  -26.288 1.00 15.47 ? 31  GLN B C   1 
ATOM   1996 O O   . GLN B 1 7   ? -3.480  28.705  -27.017 1.00 16.30 ? 31  GLN B O   1 
ATOM   1997 C CB  . GLN B 1 7   ? -0.896  30.675  -26.713 1.00 28.91 ? 31  GLN B CB  1 
ATOM   1998 C CG  . GLN B 1 7   ? -0.976  32.180  -26.920 1.00 50.83 ? 31  GLN B CG  1 
ATOM   1999 C CD  . GLN B 1 7   ? 0.016   32.676  -27.948 1.00 58.12 ? 31  GLN B CD  1 
ATOM   2000 O OE1 . GLN B 1 7   ? 0.499   31.906  -28.780 1.00 52.72 ? 31  GLN B OE1 1 
ATOM   2001 N NE2 . GLN B 1 7   ? 0.324   33.970  -27.901 1.00 54.05 ? 31  GLN B NE2 1 
ATOM   2002 N N   . LYS B 1 8   ? -1.801  27.706  -25.904 1.00 14.29 ? 32  LYS B N   1 
ATOM   2003 C CA  . LYS B 1 8   ? -2.370  26.380  -26.119 1.00 20.01 ? 32  LYS B CA  1 
ATOM   2004 C C   . LYS B 1 8   ? -3.725  26.241  -25.439 1.00 10.80 ? 32  LYS B C   1 
ATOM   2005 O O   . LYS B 1 8   ? -4.644  25.634  -25.995 1.00 14.23 ? 32  LYS B O   1 
ATOM   2006 C CB  . LYS B 1 8   ? -1.427  25.273  -25.650 1.00 17.65 ? 32  LYS B CB  1 
ATOM   2007 C CG  . LYS B 1 8   ? -0.197  25.043  -26.497 1.00 16.37 ? 32  LYS B CG  1 
ATOM   2008 C CD  . LYS B 1 8   ? 1.011   24.840  -25.624 1.00 23.86 ? 32  LYS B CD  1 
ATOM   2009 C CE  . LYS B 1 8   ? 2.238   24.560  -26.456 1.00 30.29 ? 32  LYS B CE  1 
ATOM   2010 N NZ  . LYS B 1 8   ? 2.890   23.286  -26.001 1.00 41.27 ? 32  LYS B NZ  1 
ATOM   2011 N N   . LEU B 1 9   ? -3.880  26.814  -24.246 1.00 14.56 ? 33  LEU B N   1 
ATOM   2012 C CA  . LEU B 1 9   ? -5.168  26.724  -23.572 1.00 16.34 ? 33  LEU B CA  1 
ATOM   2013 C C   . LEU B 1 9   ? -6.230  27.518  -24.324 1.00 13.89 ? 33  LEU B C   1 
ATOM   2014 O O   . LEU B 1 9   ? -7.382  27.082  -24.418 1.00 16.67 ? 33  LEU B O   1 
ATOM   2015 C CB  . LEU B 1 9   ? -5.040  27.220  -22.128 1.00 11.49 ? 33  LEU B CB  1 
ATOM   2016 C CG  . LEU B 1 9   ? -4.200  26.371  -21.159 1.00 13.83 ? 33  LEU B CG  1 
ATOM   2017 C CD1 . LEU B 1 9   ? -4.011  27.069  -19.794 1.00 13.70 ? 33  LEU B CD1 1 
ATOM   2018 C CD2 . LEU B 1 9   ? -4.758  24.962  -20.979 1.00 13.82 ? 33  LEU B CD2 1 
ATOM   2019 N N   . ALA B 1 10  ? -5.865  28.684  -24.862 1.00 12.91 ? 34  ALA B N   1 
ATOM   2020 C CA  . ALA B 1 10  ? -6.805  29.464  -25.667 1.00 15.40 ? 34  ALA B CA  1 
ATOM   2021 C C   . ALA B 1 10  ? -7.219  28.704  -26.919 1.00 11.65 ? 34  ALA B C   1 
ATOM   2022 O O   . ALA B 1 10  ? -8.390  28.728  -27.314 1.00 13.51 ? 34  ALA B O   1 
ATOM   2023 C CB  . ALA B 1 10  ? -6.191  30.816  -26.042 1.00 8.88  ? 34  ALA B CB  1 
ATOM   2024 N N   . ALA B 1 11  ? -6.262  28.037  -27.568 1.00 13.51 ? 35  ALA B N   1 
ATOM   2025 C CA  . ALA B 1 11  ? -6.567  27.248  -28.759 1.00 13.73 ? 35  ALA B CA  1 
ATOM   2026 C C   . ALA B 1 11  ? -7.487  26.086  -28.410 1.00 9.50  ? 35  ALA B C   1 
ATOM   2027 O O   . ALA B 1 11  ? -8.438  25.780  -29.147 1.00 16.13 ? 35  ALA B O   1 
ATOM   2028 C CB  . ALA B 1 11  ? -5.270  26.754  -29.407 1.00 7.40  ? 35  ALA B CB  1 
ATOM   2029 N N   . LEU B 1 12  ? -7.210  25.421  -27.289 1.00 12.86 ? 36  LEU B N   1 
ATOM   2030 C CA  . LEU B 1 12  ? -8.092  24.363  -26.810 1.00 17.85 ? 36  LEU B CA  1 
ATOM   2031 C C   . LEU B 1 12  ? -9.498  24.900  -26.593 1.00 17.64 ? 36  LEU B C   1 
ATOM   2032 O O   . LEU B 1 12  ? -10.486 24.283  -27.008 1.00 20.03 ? 36  LEU B O   1 
ATOM   2033 C CB  . LEU B 1 12  ? -7.535  23.785  -25.508 1.00 17.75 ? 36  LEU B CB  1 
ATOM   2034 C CG  . LEU B 1 12  ? -8.429  22.819  -24.730 1.00 16.61 ? 36  LEU B CG  1 
ATOM   2035 C CD1 . LEU B 1 12  ? -8.708  21.564  -25.537 1.00 19.93 ? 36  LEU B CD1 1 
ATOM   2036 C CD2 . LEU B 1 12  ? -7.793  22.487  -23.391 1.00 15.76 ? 36  LEU B CD2 1 
ATOM   2037 N N   . GLU B 1 13  ? -9.601  26.065  -25.952 1.00 11.41 ? 37  GLU B N   1 
ATOM   2038 C CA  . GLU B 1 13  ? -10.906 26.653  -25.689 1.00 13.66 ? 37  GLU B CA  1 
ATOM   2039 C C   . GLU B 1 13  ? -11.638 26.982  -26.987 1.00 15.16 ? 37  GLU B C   1 
ATOM   2040 O O   . GLU B 1 13  ? -12.837 26.715  -27.115 1.00 13.31 ? 37  GLU B O   1 
ATOM   2041 C CB  . GLU B 1 13  ? -10.740 27.907  -24.832 1.00 14.08 ? 37  GLU B CB  1 
ATOM   2042 C CG  . GLU B 1 13  ? -12.034 28.617  -24.499 1.00 14.30 ? 37  GLU B CG  1 
ATOM   2043 C CD  . GLU B 1 13  ? -11.812 29.898  -23.720 1.00 14.32 ? 37  GLU B CD  1 
ATOM   2044 O OE1 . GLU B 1 13  ? -11.160 30.819  -24.262 1.00 15.69 ? 37  GLU B OE1 1 
ATOM   2045 O OE2 . GLU B 1 13  ? -12.290 29.985  -22.568 1.00 13.53 ? 37  GLU B OE2 1 
ATOM   2046 N N   . LYS B 1 14  ? -10.934 27.574  -27.956 1.00 12.37 ? 38  LYS B N   1 
ATOM   2047 C CA  . LYS B 1 14  ? -11.568 27.908  -29.228 1.00 20.51 ? 38  LYS B CA  1 
ATOM   2048 C C   . LYS B 1 14  ? -12.094 26.667  -29.934 1.00 21.28 ? 38  LYS B C   1 
ATOM   2049 O O   . LYS B 1 14  ? -13.224 26.663  -30.435 1.00 21.71 ? 38  LYS B O   1 
ATOM   2050 C CB  . LYS B 1 14  ? -10.578 28.648  -30.129 1.00 32.35 ? 38  LYS B CB  1 
ATOM   2051 C CG  . LYS B 1 14  ? -11.204 29.542  -31.199 1.00 26.30 ? 38  LYS B CG  1 
ATOM   2052 C CD  . LYS B 1 14  ? -10.141 30.467  -31.804 1.00 48.57 ? 38  LYS B CD  1 
ATOM   2053 C CE  . LYS B 1 14  ? -10.567 31.083  -33.141 1.00 44.42 ? 38  LYS B CE  1 
ATOM   2054 N NZ  . LYS B 1 14  ? -11.987 31.567  -33.154 1.00 45.92 ? 38  LYS B NZ  1 
ATOM   2055 N N   . SER B 1 15  ? -11.294 25.598  -29.965 1.00 28.90 ? 39  SER B N   1 
ATOM   2056 C CA  . SER B 1 15  ? -11.745 24.352  -30.584 1.00 22.36 ? 39  SER B CA  1 
ATOM   2057 C C   . SER B 1 15  ? -12.941 23.777  -29.837 1.00 21.94 ? 39  SER B C   1 
ATOM   2058 O O   . SER B 1 15  ? -13.854 23.207  -30.447 1.00 20.65 ? 39  SER B O   1 
ATOM   2059 C CB  . SER B 1 15  ? -10.596 23.347  -30.669 1.00 23.26 ? 39  SER B CB  1 
ATOM   2060 O OG  . SER B 1 15  ? -9.719  23.471  -29.562 1.00 40.06 ? 39  SER B OG  1 
ATOM   2061 N N   . SER B 1 16  ? -12.941 23.902  -28.509 1.00 21.53 ? 40  SER B N   1 
ATOM   2062 C CA  . SER B 1 16  ? -13.958 23.274  -27.673 1.00 30.13 ? 40  SER B CA  1 
ATOM   2063 C C   . SER B 1 16  ? -15.331 23.911  -27.832 1.00 20.10 ? 40  SER B C   1 
ATOM   2064 O O   . SER B 1 16  ? -16.339 23.249  -27.563 1.00 24.45 ? 40  SER B O   1 
ATOM   2065 C CB  . SER B 1 16  ? -13.539 23.346  -26.204 1.00 26.36 ? 40  SER B CB  1 
ATOM   2066 O OG  . SER B 1 16  ? -13.848 24.624  -25.673 1.00 19.32 ? 40  SER B OG  1 
ATOM   2067 N N   . GLY B 1 17  ? -15.401 25.170  -28.256 1.00 22.52 ? 41  GLY B N   1 
ATOM   2068 C CA  . GLY B 1 17  ? -16.666 25.874  -28.331 1.00 16.77 ? 41  GLY B CA  1 
ATOM   2069 C C   . GLY B 1 17  ? -17.188 26.409  -27.011 1.00 21.66 ? 41  GLY B C   1 
ATOM   2070 O O   . GLY B 1 17  ? -18.268 27.011  -26.992 1.00 18.16 ? 41  GLY B O   1 
ATOM   2071 N N   . GLY B 1 18  ? -16.485 26.182  -25.902 1.00 16.17 ? 42  GLY B N   1 
ATOM   2072 C CA  . GLY B 1 18  ? -16.982 26.650  -24.626 1.00 14.22 ? 42  GLY B CA  1 
ATOM   2073 C C   . GLY B 1 18  ? -16.088 27.690  -23.975 1.00 11.95 ? 42  GLY B C   1 
ATOM   2074 O O   . GLY B 1 18  ? -15.337 28.400  -24.650 1.00 17.22 ? 42  GLY B O   1 
ATOM   2075 N N   . ARG B 1 19  ? -16.169 27.783  -22.652 1.00 12.31 ? 43  ARG B N   1 
ATOM   2076 C CA  . ARG B 1 19  ? -15.397 28.719  -21.846 1.00 15.95 ? 43  ARG B CA  1 
ATOM   2077 C C   . ARG B 1 19  ? -14.585 27.925  -20.832 1.00 13.05 ? 43  ARG B C   1 
ATOM   2078 O O   . ARG B 1 19  ? -15.159 27.178  -20.026 1.00 16.24 ? 43  ARG B O   1 
ATOM   2079 C CB  . ARG B 1 19  ? -16.322 29.719  -21.144 1.00 8.17  ? 43  ARG B CB  1 
ATOM   2080 C CG  . ARG B 1 19  ? -15.597 30.815  -20.384 1.00 16.63 ? 43  ARG B CG  1 
ATOM   2081 C CD  . ARG B 1 19  ? -16.561 31.895  -19.910 1.00 16.75 ? 43  ARG B CD  1 
ATOM   2082 N NE  . ARG B 1 19  ? -17.529 31.385  -18.945 1.00 16.86 ? 43  ARG B NE  1 
ATOM   2083 C CZ  . ARG B 1 19  ? -17.423 31.528  -17.630 1.00 21.90 ? 43  ARG B CZ  1 
ATOM   2084 N NH1 . ARG B 1 19  ? -16.403 32.176  -17.086 1.00 13.99 ? 43  ARG B NH1 1 
ATOM   2085 N NH2 . ARG B 1 19  ? -18.361 31.006  -16.843 1.00 11.80 ? 43  ARG B NH2 1 
ATOM   2086 N N   . LEU B 1 20  ? -13.261 28.076  -20.882 1.00 14.06 ? 44  LEU B N   1 
ATOM   2087 C CA  . LEU B 1 20  ? -12.333 27.275  -20.093 1.00 12.93 ? 44  LEU B CA  1 
ATOM   2088 C C   . LEU B 1 20  ? -11.651 28.166  -19.061 1.00 12.53 ? 44  LEU B C   1 
ATOM   2089 O O   . LEU B 1 20  ? -11.157 29.243  -19.406 1.00 20.81 ? 44  LEU B O   1 
ATOM   2090 C CB  . LEU B 1 20  ? -11.282 26.617  -20.997 1.00 13.53 ? 44  LEU B CB  1 
ATOM   2091 C CG  . LEU B 1 20  ? -10.159 25.781  -20.373 1.00 8.49  ? 44  LEU B CG  1 
ATOM   2092 C CD1 . LEU B 1 20  ? -10.722 24.574  -19.638 1.00 9.26  ? 44  LEU B CD1 1 
ATOM   2093 C CD2 . LEU B 1 20  ? -9.128  25.354  -21.412 1.00 13.11 ? 44  LEU B CD2 1 
ATOM   2094 N N   . GLY B 1 21  ? -11.609 27.717  -17.808 1.00 11.88 ? 45  GLY B N   1 
ATOM   2095 C CA  . GLY B 1 21  ? -10.835 28.381  -16.773 1.00 11.76 ? 45  GLY B CA  1 
ATOM   2096 C C   . GLY B 1 21  ? -9.859  27.418  -16.125 1.00 17.66 ? 45  GLY B C   1 
ATOM   2097 O O   . GLY B 1 21  ? -10.241 26.318  -15.729 1.00 20.69 ? 45  GLY B O   1 
ATOM   2098 N N   . VAL B 1 22  ? -8.594  27.800  -16.019 1.00 12.11 ? 46  VAL B N   1 
ATOM   2099 C CA  . VAL B 1 22  ? -7.544  26.933  -15.494 1.00 19.58 ? 46  VAL B CA  1 
ATOM   2100 C C   . VAL B 1 22  ? -6.722  27.738  -14.501 1.00 16.27 ? 46  VAL B C   1 
ATOM   2101 O O   . VAL B 1 22  ? -6.339  28.877  -14.790 1.00 17.18 ? 46  VAL B O   1 
ATOM   2102 C CB  . VAL B 1 22  ? -6.650  26.355  -16.611 1.00 20.18 ? 46  VAL B CB  1 
ATOM   2103 C CG1 . VAL B 1 22  ? -5.545  25.478  -16.018 1.00 10.58 ? 46  VAL B CG1 1 
ATOM   2104 C CG2 . VAL B 1 22  ? -7.492  25.552  -17.599 1.00 13.91 ? 46  VAL B CG2 1 
ATOM   2105 N N   . ALA B 1 23  ? -6.437  27.151  -13.345 1.00 8.51  ? 47  ALA B N   1 
ATOM   2106 C CA  . ALA B 1 23  ? -5.451  27.735  -12.440 1.00 10.99 ? 47  ALA B CA  1 
ATOM   2107 C C   . ALA B 1 23  ? -4.577  26.639  -11.864 1.00 9.03  ? 47  ALA B C   1 
ATOM   2108 O O   . ALA B 1 23  ? -5.075  25.712  -11.223 1.00 14.53 ? 47  ALA B O   1 
ATOM   2109 C CB  . ALA B 1 23  ? -6.122  28.518  -11.309 1.00 8.98  ? 47  ALA B CB  1 
ATOM   2110 N N   . LEU B 1 24  ? -3.272  26.774  -12.073 1.00 11.38 ? 48  LEU B N   1 
ATOM   2111 C CA  . LEU B 1 24  ? -2.270  25.885  -11.517 1.00 11.54 ? 48  LEU B CA  1 
ATOM   2112 C C   . LEU B 1 24  ? -1.430  26.667  -10.522 1.00 16.90 ? 48  LEU B C   1 
ATOM   2113 O O   . LEU B 1 24  ? -1.008  27.793  -10.804 1.00 20.11 ? 48  LEU B O   1 
ATOM   2114 C CB  . LEU B 1 24  ? -1.375  25.310  -12.618 1.00 17.18 ? 48  LEU B CB  1 
ATOM   2115 C CG  . LEU B 1 24  ? -0.094  24.620  -12.146 1.00 15.89 ? 48  LEU B CG  1 
ATOM   2116 C CD1 . LEU B 1 24  ? -0.408  23.223  -11.613 1.00 14.53 ? 48  LEU B CD1 1 
ATOM   2117 C CD2 . LEU B 1 24  ? 0.956   24.580  -13.255 1.00 14.60 ? 48  LEU B CD2 1 
ATOM   2118 N N   . ILE B 1 25  ? -1.166  26.048  -9.378  1.00 14.41 ? 49  ILE B N   1 
ATOM   2119 C CA  . ILE B 1 25  ? -0.143  26.488  -8.442  1.00 19.16 ? 49  ILE B CA  1 
ATOM   2120 C C   . ILE B 1 25  ? 0.907   25.398  -8.317  1.00 18.19 ? 49  ILE B C   1 
ATOM   2121 O O   . ILE B 1 25  ? 0.588   24.247  -7.996  1.00 19.58 ? 49  ILE B O   1 
ATOM   2122 C CB  . ILE B 1 25  ? -0.742  26.824  -7.067  1.00 21.09 ? 49  ILE B CB  1 
ATOM   2123 C CG1 . ILE B 1 25  ? -1.778  27.947  -7.195  1.00 21.33 ? 49  ILE B CG1 1 
ATOM   2124 C CG2 . ILE B 1 25  ? 0.357   27.120  -6.053  1.00 23.82 ? 49  ILE B CG2 1 
ATOM   2125 C CD1 . ILE B 1 25  ? -2.649  28.110  -5.971  1.00 27.89 ? 49  ILE B CD1 1 
ATOM   2126 N N   . ASP B 1 26  ? 2.152   25.764  -8.577  1.00 16.81 ? 50  ASP B N   1 
ATOM   2127 C CA  . ASP B 1 26  ? 3.299   24.895  -8.382  1.00 20.78 ? 50  ASP B CA  1 
ATOM   2128 C C   . ASP B 1 26  ? 3.921   25.291  -7.048  1.00 26.06 ? 50  ASP B C   1 
ATOM   2129 O O   . ASP B 1 26  ? 4.464   26.404  -6.913  1.00 28.73 ? 50  ASP B O   1 
ATOM   2130 C CB  . ASP B 1 26  ? 4.294   25.050  -9.531  1.00 24.84 ? 50  ASP B CB  1 
ATOM   2131 C CG  . ASP B 1 26  ? 5.473   24.093  -9.426  1.00 51.61 ? 50  ASP B CG  1 
ATOM   2132 O OD1 . ASP B 1 26  ? 6.388   24.178  -10.279 1.00 44.88 ? 50  ASP B OD1 1 
ATOM   2133 O OD2 . ASP B 1 26  ? 5.481   23.244  -8.506  1.00 48.89 ? 50  ASP B OD2 1 
ATOM   2134 N N   . THR B 1 27  ? 3.758   24.409  -6.048  1.00 19.28 ? 51  THR B N   1 
ATOM   2135 C CA  . THR B 1 27  ? 4.220   24.634  -4.685  1.00 26.19 ? 51  THR B CA  1 
ATOM   2136 C C   . THR B 1 27  ? 5.718   24.425  -4.553  1.00 32.71 ? 51  THR B C   1 
ATOM   2137 O O   . THR B 1 27  ? 6.264   24.620  -3.461  1.00 28.81 ? 51  THR B O   1 
ATOM   2138 C CB  . THR B 1 27  ? 3.503   23.707  -3.693  1.00 21.38 ? 51  THR B CB  1 
ATOM   2139 O OG1 . THR B 1 27  ? 4.009   22.372  -3.832  1.00 24.48 ? 51  THR B OG1 1 
ATOM   2140 C CG2 . THR B 1 27  ? 1.998   23.710  -3.919  1.00 25.71 ? 51  THR B CG2 1 
ATOM   2141 N N   . ALA B 1 28  ? 6.388   24.023  -5.636  1.00 31.15 ? 52  ALA B N   1 
ATOM   2142 C CA  . ALA B 1 28  ? 7.841   23.978  -5.618  1.00 35.08 ? 52  ALA B CA  1 
ATOM   2143 C C   . ALA B 1 28  ? 8.381   25.382  -5.433  1.00 37.44 ? 52  ALA B C   1 
ATOM   2144 O O   . ALA B 1 28  ? 9.405   25.585  -4.769  1.00 27.02 ? 52  ALA B O   1 
ATOM   2145 C CB  . ALA B 1 28  ? 8.370   23.351  -6.909  1.00 26.31 ? 52  ALA B CB  1 
ATOM   2146 N N   . ASP B 1 29  ? 7.674   26.360  -5.995  1.00 31.00 ? 53  ASP B N   1 
ATOM   2147 C CA  . ASP B 1 29  ? 8.124   27.743  -5.976  1.00 22.80 ? 53  ASP B CA  1 
ATOM   2148 C C   . ASP B 1 29  ? 6.953   28.720  -5.915  1.00 15.73 ? 53  ASP B C   1 
ATOM   2149 O O   . ASP B 1 29  ? 7.171   29.922  -6.110  1.00 21.79 ? 53  ASP B O   1 
ATOM   2150 C CB  . ASP B 1 29  ? 9.009   27.986  -7.205  1.00 32.81 ? 53  ASP B CB  1 
ATOM   2151 C CG  . ASP B 1 29  ? 8.385   27.459  -8.491  1.00 32.04 ? 53  ASP B CG  1 
ATOM   2152 O OD1 . ASP B 1 29  ? 7.191   27.094  -8.473  1.00 30.23 ? 53  ASP B OD1 1 
ATOM   2153 O OD2 . ASP B 1 29  ? 9.102   27.382  -9.513  1.00 24.98 ? 53  ASP B OD2 1 
ATOM   2154 N N   . ASN B 1 30  ? 5.727   28.246  -5.670  1.00 18.73 ? 54  ASN B N   1 
ATOM   2155 C CA  . ASN B 1 30  ? 4.523   29.073  -5.570  1.00 22.30 ? 54  ASN B CA  1 
ATOM   2156 C C   . ASN B 1 30  ? 4.224   29.810  -6.861  1.00 23.93 ? 54  ASN B C   1 
ATOM   2157 O O   . ASN B 1 30  ? 3.534   30.833  -6.846  1.00 25.00 ? 54  ASN B O   1 
ATOM   2158 C CB  . ASN B 1 30  ? 4.596   30.067  -4.405  1.00 26.45 ? 54  ASN B CB  1 
ATOM   2159 C CG  . ASN B 1 30  ? 4.720   29.380  -3.063  1.00 27.27 ? 54  ASN B CG  1 
ATOM   2160 O OD1 . ASN B 1 30  ? 4.965   28.176  -2.989  1.00 28.63 ? 54  ASN B OD1 1 
ATOM   2161 N ND2 . ASN B 1 30  ? 4.550   30.146  -1.989  1.00 36.84 ? 54  ASN B ND2 1 
ATOM   2162 N N   . THR B 1 31  ? 4.721   29.311  -7.984  1.00 19.90 ? 55  THR B N   1 
ATOM   2163 C CA  . THR B 1 31  ? 4.351   29.949  -9.240  1.00 24.95 ? 55  THR B CA  1 
ATOM   2164 C C   . THR B 1 31  ? 2.967   29.502  -9.683  1.00 19.35 ? 55  THR B C   1 
ATOM   2165 O O   . THR B 1 31  ? 2.456   28.471  -9.258  1.00 19.34 ? 55  THR B O   1 
ATOM   2166 C CB  . THR B 1 31  ? 5.374   29.670  -10.343 1.00 21.90 ? 55  THR B CB  1 
ATOM   2167 O OG1 . THR B 1 31  ? 5.404   28.267  -10.635 1.00 31.31 ? 55  THR B OG1 1 
ATOM   2168 C CG2 . THR B 1 31  ? 6.768   30.167  -9.932  1.00 22.91 ? 55  THR B CG2 1 
ATOM   2169 N N   . GLN B 1 32  ? 2.344   30.307  -10.534 1.00 21.86 ? 56  GLN B N   1 
ATOM   2170 C CA  . GLN B 1 32  ? 0.992   30.007  -10.963 1.00 19.96 ? 56  GLN B CA  1 
ATOM   2171 C C   . GLN B 1 32  ? 0.912   30.124  -12.474 1.00 18.77 ? 56  GLN B C   1 
ATOM   2172 O O   . GLN B 1 32  ? 1.675   30.860  -13.108 1.00 32.92 ? 56  GLN B O   1 
ATOM   2173 C CB  . GLN B 1 32  ? -0.039  30.936  -10.293 1.00 19.92 ? 56  GLN B CB  1 
ATOM   2174 C CG  . GLN B 1 32  ? 0.103   31.036  -8.775  1.00 30.51 ? 56  GLN B CG  1 
ATOM   2175 C CD  . GLN B 1 32  ? -0.582  32.260  -8.183  1.00 43.08 ? 56  GLN B CD  1 
ATOM   2176 O OE1 . GLN B 1 32  ? -1.727  32.569  -8.517  1.00 39.80 ? 56  GLN B OE1 1 
ATOM   2177 N NE2 . GLN B 1 32  ? 0.111   32.950  -7.283  1.00 30.92 ? 56  GLN B NE2 1 
ATOM   2178 N N   . VAL B 1 33  ? -0.050  29.398  -13.032 1.00 14.72 ? 57  VAL B N   1 
ATOM   2179 C CA  . VAL B 1 33  ? -0.491  29.542  -14.414 1.00 16.08 ? 57  VAL B CA  1 
ATOM   2180 C C   . VAL B 1 33  ? -1.995  29.742  -14.421 1.00 15.96 ? 57  VAL B C   1 
ATOM   2181 O O   . VAL B 1 33  ? -2.737  28.933  -13.859 1.00 15.27 ? 57  VAL B O   1 
ATOM   2182 C CB  . VAL B 1 33  ? -0.104  28.319  -15.263 1.00 25.31 ? 57  VAL B CB  1 
ATOM   2183 C CG1 . VAL B 1 33  ? -0.733  28.418  -16.644 1.00 11.47 ? 57  VAL B CG1 1 
ATOM   2184 C CG2 . VAL B 1 33  ? 1.420   28.209  -15.357 1.00 12.75 ? 57  VAL B CG2 1 
ATOM   2185 N N   . LEU B 1 34  ? -2.440  30.823  -15.043 1.00 20.99 ? 59  LEU B N   1 
ATOM   2186 C CA  . LEU B 1 34  ? -3.847  31.176  -15.061 1.00 19.14 ? 59  LEU B CA  1 
ATOM   2187 C C   . LEU B 1 34  ? -4.355  31.408  -16.473 1.00 17.08 ? 59  LEU B C   1 
ATOM   2188 O O   . LEU B 1 34  ? -3.688  32.052  -17.288 1.00 28.73 ? 59  LEU B O   1 
ATOM   2189 C CB  . LEU B 1 34  ? -4.112  32.421  -14.215 1.00 13.53 ? 59  LEU B CB  1 
ATOM   2190 C CG  . LEU B 1 34  ? -3.772  32.213  -12.746 1.00 23.12 ? 59  LEU B CG  1 
ATOM   2191 C CD1 . LEU B 1 34  ? -3.110  33.466  -12.184 1.00 27.43 ? 59  LEU B CD1 1 
ATOM   2192 C CD2 . LEU B 1 34  ? -5.007  31.822  -11.961 1.00 26.24 ? 59  LEU B CD2 1 
ATOM   2193 N N   . TYR B 1 35  ? -5.517  30.836  -16.754 1.00 11.34 ? 60  TYR B N   1 
ATOM   2194 C CA  . TYR B 1 35  ? -6.264  31.048  -17.985 1.00 16.67 ? 60  TYR B CA  1 
ATOM   2195 C C   . TYR B 1 35  ? -7.702  31.309  -17.573 1.00 15.19 ? 60  TYR B C   1 
ATOM   2196 O O   . TYR B 1 35  ? -8.365  30.424  -17.031 1.00 12.99 ? 60  TYR B O   1 
ATOM   2197 C CB  . TYR B 1 35  ? -6.165  29.882  -18.963 1.00 12.03 ? 60  TYR B CB  1 
ATOM   2198 C CG  . TYR B 1 35  ? -6.786  30.281  -20.278 1.00 15.62 ? 60  TYR B CG  1 
ATOM   2199 C CD1 . TYR B 1 35  ? -6.077  30.980  -21.248 1.00 19.06 ? 60  TYR B CD1 1 
ATOM   2200 C CD2 . TYR B 1 35  ? -8.113  29.954  -20.541 1.00 15.16 ? 60  TYR B CD2 1 
ATOM   2201 C CE1 . TYR B 1 35  ? -6.687  31.350  -22.450 1.00 14.53 ? 60  TYR B CE1 1 
ATOM   2202 C CE2 . TYR B 1 35  ? -8.721  30.306  -21.721 1.00 15.43 ? 60  TYR B CE2 1 
ATOM   2203 C CZ  . TYR B 1 35  ? -8.008  31.001  -22.673 1.00 15.48 ? 60  TYR B CZ  1 
ATOM   2204 O OH  . TYR B 1 35  ? -8.632  31.351  -23.845 1.00 18.93 ? 60  TYR B OH  1 
ATOM   2205 N N   . ARG B 1 36  ? -8.168  32.533  -17.824 1.00 10.91 ? 61  ARG B N   1 
ATOM   2206 C CA  . ARG B 1 36  ? -9.444  33.006  -17.300 1.00 9.92  ? 61  ARG B CA  1 
ATOM   2207 C C   . ARG B 1 36  ? -9.491  32.781  -15.795 1.00 14.52 ? 61  ARG B C   1 
ATOM   2208 O O   . ARG B 1 36  ? -10.520 32.411  -15.226 1.00 22.04 ? 61  ARG B O   1 
ATOM   2209 C CB  . ARG B 1 36  ? -10.619 32.319  -17.996 1.00 17.82 ? 61  ARG B CB  1 
ATOM   2210 C CG  . ARG B 1 36  ? -10.656 32.594  -19.474 1.00 17.23 ? 61  ARG B CG  1 
ATOM   2211 C CD  . ARG B 1 36  ? -11.965 32.199  -20.102 1.00 11.91 ? 61  ARG B CD  1 
ATOM   2212 N NE  . ARG B 1 36  ? -11.835 32.222  -21.551 1.00 13.75 ? 61  ARG B NE  1 
ATOM   2213 C CZ  . ARG B 1 36  ? -11.851 33.330  -22.280 1.00 20.80 ? 61  ARG B CZ  1 
ATOM   2214 N NH1 . ARG B 1 36  ? -12.063 34.515  -21.730 1.00 20.06 ? 61  ARG B NH1 1 
ATOM   2215 N NH2 . ARG B 1 36  ? -11.671 33.246  -23.596 1.00 14.91 ? 61  ARG B NH2 1 
ATOM   2216 N N   . GLY B 1 37  ? -8.349  33.000  -15.143 1.00 16.69 ? 62  GLY B N   1 
ATOM   2217 C CA  . GLY B 1 37  ? -8.214  32.656  -13.743 1.00 10.83 ? 62  GLY B CA  1 
ATOM   2218 C C   . GLY B 1 37  ? -9.100  33.461  -12.820 1.00 13.51 ? 62  GLY B C   1 
ATOM   2219 O O   . GLY B 1 37  ? -9.360  33.022  -11.695 1.00 17.05 ? 62  GLY B O   1 
ATOM   2220 N N   . ASP B 1 38  ? -9.556  34.634  -13.258 1.00 9.87  ? 63  ASP B N   1 
ATOM   2221 C CA  . ASP B 1 38  ? -10.407 35.486  -12.438 1.00 17.82 ? 63  ASP B CA  1 
ATOM   2222 C C   . ASP B 1 38  ? -11.842 35.564  -12.943 1.00 14.27 ? 63  ASP B C   1 
ATOM   2223 O O   . ASP B 1 38  ? -12.609 36.401  -12.460 1.00 10.95 ? 63  ASP B O   1 
ATOM   2224 C CB  . ASP B 1 38  ? -9.808  36.889  -12.326 1.00 12.62 ? 63  ASP B CB  1 
ATOM   2225 C CG  . ASP B 1 38  ? -8.461  36.885  -11.638 1.00 19.61 ? 63  ASP B CG  1 
ATOM   2226 O OD1 . ASP B 1 38  ? -8.382  36.351  -10.512 1.00 26.34 ? 63  ASP B OD1 1 
ATOM   2227 O OD2 . ASP B 1 38  ? -7.479  37.396  -12.218 1.00 34.66 ? 63  ASP B OD2 1 
ATOM   2228 N N   . GLU B 1 39  ? -12.221 34.733  -13.908 1.00 12.68 ? 64  GLU B N   1 
ATOM   2229 C CA  . GLU B 1 39  ? -13.613 34.649  -14.320 1.00 17.14 ? 64  GLU B CA  1 
ATOM   2230 C C   . GLU B 1 39  ? -14.358 33.665  -13.427 1.00 15.89 ? 64  GLU B C   1 
ATOM   2231 O O   . GLU B 1 39  ? -13.795 32.674  -12.959 1.00 23.08 ? 64  GLU B O   1 
ATOM   2232 C CB  . GLU B 1 39  ? -13.739 34.254  -15.789 1.00 15.02 ? 64  GLU B CB  1 
ATOM   2233 C CG  . GLU B 1 39  ? -13.042 35.223  -16.727 1.00 13.64 ? 64  GLU B CG  1 
ATOM   2234 C CD  . GLU B 1 39  ? -13.355 34.958  -18.188 1.00 27.38 ? 64  GLU B CD  1 
ATOM   2235 O OE1 . GLU B 1 39  ? -14.410 34.349  -18.476 1.00 23.70 ? 64  GLU B OE1 1 
ATOM   2236 O OE2 . GLU B 1 39  ? -12.551 35.372  -19.051 1.00 28.75 ? 64  GLU B OE2 1 
ATOM   2237 N N   . ARG B 1 40  ? -15.627 33.960  -13.165 1.00 17.12 ? 65  ARG B N   1 
ATOM   2238 C CA  . ARG B 1 40  ? -16.439 33.054  -12.365 1.00 17.70 ? 65  ARG B CA  1 
ATOM   2239 C C   . ARG B 1 40  ? -16.940 31.866  -13.171 1.00 9.90  ? 65  ARG B C   1 
ATOM   2240 O O   . ARG B 1 40  ? -17.308 31.993  -14.342 1.00 12.29 ? 65  ARG B O   1 
ATOM   2241 C CB  . ARG B 1 40  ? -17.614 33.808  -11.751 1.00 21.48 ? 65  ARG B CB  1 
ATOM   2242 C CG  . ARG B 1 40  ? -17.163 34.627  -10.571 1.00 14.45 ? 65  ARG B CG  1 
ATOM   2243 C CD  . ARG B 1 40  ? -18.288 35.311  -9.845  1.00 21.53 ? 65  ARG B CD  1 
ATOM   2244 N NE  . ARG B 1 40  ? -17.728 35.973  -8.677  1.00 25.27 ? 65  ARG B NE  1 
ATOM   2245 C CZ  . ARG B 1 40  ? -17.450 35.347  -7.545  1.00 19.54 ? 65  ARG B CZ  1 
ATOM   2246 N NH1 . ARG B 1 40  ? -17.778 34.074  -7.362  1.00 11.19 ? 65  ARG B NH1 1 
ATOM   2247 N NH2 . ARG B 1 40  ? -16.830 36.011  -6.574  1.00 18.91 ? 65  ARG B NH2 1 
ATOM   2248 N N   . PHE B 1 41  ? -16.970 30.710  -12.519 1.00 13.83 ? 66  PHE B N   1 
ATOM   2249 C CA  . PHE B 1 41  ? -17.495 29.487  -13.092 1.00 12.29 ? 66  PHE B CA  1 
ATOM   2250 C C   . PHE B 1 41  ? -18.389 28.815  -12.064 1.00 13.15 ? 66  PHE B C   1 
ATOM   2251 O O   . PHE B 1 41  ? -18.127 28.897  -10.852 1.00 17.95 ? 66  PHE B O   1 
ATOM   2252 C CB  . PHE B 1 41  ? -16.367 28.511  -13.467 1.00 7.63  ? 66  PHE B CB  1 
ATOM   2253 C CG  . PHE B 1 41  ? -15.517 28.972  -14.616 1.00 13.28 ? 66  PHE B CG  1 
ATOM   2254 C CD1 . PHE B 1 41  ? -14.534 29.936  -14.416 1.00 11.57 ? 66  PHE B CD1 1 
ATOM   2255 C CD2 . PHE B 1 41  ? -15.702 28.466  -15.891 1.00 17.25 ? 66  PHE B CD2 1 
ATOM   2256 C CE1 . PHE B 1 41  ? -13.735 30.375  -15.462 1.00 13.93 ? 66  PHE B CE1 1 
ATOM   2257 C CE2 . PHE B 1 41  ? -14.910 28.908  -16.948 1.00 23.89 ? 66  PHE B CE2 1 
ATOM   2258 C CZ  . PHE B 1 41  ? -13.926 29.867  -16.729 1.00 17.73 ? 66  PHE B CZ  1 
ATOM   2259 N N   . PRO B 1 42  ? -19.439 28.131  -12.518 1.00 17.08 ? 67  PRO B N   1 
ATOM   2260 C CA  . PRO B 1 42  ? -20.247 27.318  -11.597 1.00 13.49 ? 67  PRO B CA  1 
ATOM   2261 C C   . PRO B 1 42  ? -19.416 26.145  -11.099 1.00 16.91 ? 67  PRO B C   1 
ATOM   2262 O O   . PRO B 1 42  ? -18.870 25.378  -11.896 1.00 14.61 ? 67  PRO B O   1 
ATOM   2263 C CB  . PRO B 1 42  ? -21.424 26.846  -12.458 1.00 11.79 ? 67  PRO B CB  1 
ATOM   2264 C CG  . PRO B 1 42  ? -21.201 27.389  -13.837 1.00 13.98 ? 67  PRO B CG  1 
ATOM   2265 C CD  . PRO B 1 42  ? -19.872 28.037  -13.922 1.00 11.44 ? 67  PRO B CD  1 
ATOM   2266 N N   . MET B 1 43  ? -19.314 26.006  -9.778  1.00 12.16 ? 68  MET B N   1 
ATOM   2267 C CA  . MET B 1 43  ? -18.499 24.915  -9.262  1.00 15.64 ? 68  MET B CA  1 
ATOM   2268 C C   . MET B 1 43  ? -19.173 23.560  -9.366  1.00 10.75 ? 68  MET B C   1 
ATOM   2269 O O   . MET B 1 43  ? -18.482 22.550  -9.557  1.00 16.34 ? 68  MET B O   1 
ATOM   2270 C CB  . MET B 1 43  ? -18.132 25.169  -7.809  1.00 11.16 ? 68  MET B CB  1 
ATOM   2271 C CG  . MET B 1 43  ? -17.805 26.591  -7.529  1.00 25.20 ? 68  MET B CG  1 
ATOM   2272 S SD  . MET B 1 43  ? -17.498 26.682  -5.777  1.00 27.40 ? 68  MET B SD  1 
ATOM   2273 C CE  . MET B 1 43  ? -19.015 27.463  -5.204  1.00 20.53 ? 68  MET B CE  1 
ATOM   2274 N N   . CYS B 1 44  ? -20.498 23.519  -9.301  1.00 7.52  ? 69  CYS B N   1 
ATOM   2275 C CA  . CYS B 1 44  ? -21.234 22.257  -9.194  1.00 11.85 ? 69  CYS B CA  1 
ATOM   2276 C C   . CYS B 1 44  ? -20.595 21.399  -8.097  1.00 11.58 ? 69  CYS B C   1 
ATOM   2277 O O   . CYS B 1 44  ? -20.237 21.927  -7.031  1.00 16.39 ? 69  CYS B O   1 
ATOM   2278 C CB  . CYS B 1 44  ? -21.293 21.618  -10.578 1.00 7.18  ? 69  CYS B CB  1 
ATOM   2279 S SG  . CYS B 1 44  ? -22.038 22.667  -11.854 1.00 19.37 ? 69  CYS B SG  1 
ATOM   2280 N N   . SER B 1 45  ? -20.363 20.107  -8.337  1.00 12.35 ? 70  SER B N   1 
ATOM   2281 C CA  . SER B 1 45  ? -19.932 19.194  -7.287  1.00 13.84 ? 70  SER B CA  1 
ATOM   2282 C C   . SER B 1 45  ? -18.562 19.518  -6.703  1.00 12.64 ? 70  SER B C   1 
ATOM   2283 O O   . SER B 1 45  ? -18.245 19.013  -5.619  1.00 21.42 ? 70  SER B O   1 
ATOM   2284 C CB  . SER B 1 45  ? -19.918 17.761  -7.815  1.00 19.77 ? 70  SER B CB  1 
ATOM   2285 O OG  . SER B 1 45  ? -21.229 17.224  -7.861  1.00 21.49 ? 70  SER B OG  1 
ATOM   2286 N N   . THR B 1 46  ? -17.743 20.345  -7.356  1.00 10.71 ? 71  THR B N   1 
ATOM   2287 C CA  . THR B 1 46  ? -16.455 20.636  -6.735  1.00 12.41 ? 71  THR B CA  1 
ATOM   2288 C C   . THR B 1 46  ? -16.620 21.434  -5.448  1.00 14.94 ? 71  THR B C   1 
ATOM   2289 O O   . THR B 1 46  ? -15.765 21.330  -4.551  1.00 12.95 ? 71  THR B O   1 
ATOM   2290 C CB  . THR B 1 46  ? -15.540 21.385  -7.711  1.00 14.66 ? 71  THR B CB  1 
ATOM   2291 O OG1 . THR B 1 46  ? -16.050 22.704  -7.940  1.00 14.90 ? 71  THR B OG1 1 
ATOM   2292 C CG2 . THR B 1 46  ? -15.442 20.641  -9.041  1.00 15.59 ? 71  THR B CG2 1 
ATOM   2293 N N   . SER B 1 47  ? -17.784 22.068  -5.258  1.00 15.27 ? 72  SER B N   1 
ATOM   2294 C CA  . SER B 1 47  ? -18.014 22.763  -3.998  1.00 15.11 ? 72  SER B CA  1 
ATOM   2295 C C   . SER B 1 47  ? -18.051 21.794  -2.831  1.00 12.88 ? 72  SER B C   1 
ATOM   2296 O O   . SER B 1 47  ? -17.797 22.203  -1.691  1.00 17.59 ? 72  SER B O   1 
ATOM   2297 C CB  . SER B 1 47  ? -19.324 23.549  -4.057  1.00 17.74 ? 72  SER B CB  1 
ATOM   2298 O OG  . SER B 1 47  ? -20.431 22.674  -4.200  1.00 16.67 ? 72  SER B OG  1 
ATOM   2299 N N   . LYS B 1 48  ? -18.311 20.510  -3.104  1.00 8.52  ? 73  LYS B N   1 
ATOM   2300 C CA  . LYS B 1 48  ? -18.329 19.514  -2.041  1.00 10.39 ? 73  LYS B CA  1 
ATOM   2301 C C   . LYS B 1 48  ? -17.034 19.523  -1.243  1.00 13.44 ? 73  LYS B C   1 
ATOM   2302 O O   . LYS B 1 48  ? -17.068 19.374  -0.012  1.00 10.60 ? 73  LYS B O   1 
ATOM   2303 C CB  . LYS B 1 48  ? -18.606 18.138  -2.633  1.00 8.46  ? 73  LYS B CB  1 
ATOM   2304 C CG  . LYS B 1 48  ? -20.013 18.053  -3.182  1.00 12.68 ? 73  LYS B CG  1 
ATOM   2305 C CD  . LYS B 1 48  ? -20.331 16.706  -3.794  1.00 10.22 ? 73  LYS B CD  1 
ATOM   2306 C CE  . LYS B 1 48  ? -21.770 16.719  -4.267  1.00 15.04 ? 73  LYS B CE  1 
ATOM   2307 N NZ  . LYS B 1 48  ? -22.109 15.519  -5.044  1.00 14.56 ? 73  LYS B NZ  1 
ATOM   2308 N N   . VAL B 1 49  ? -15.894 19.757  -1.905  1.00 12.70 ? 74  VAL B N   1 
ATOM   2309 C CA  . VAL B 1 49  ? -14.643 19.826  -1.154  1.00 9.14  ? 74  VAL B CA  1 
ATOM   2310 C C   . VAL B 1 49  ? -14.776 20.835  -0.026  1.00 11.18 ? 74  VAL B C   1 
ATOM   2311 O O   . VAL B 1 49  ? -14.620 20.496  1.157   1.00 14.37 ? 74  VAL B O   1 
ATOM   2312 C CB  . VAL B 1 49  ? -13.463 20.164  -2.081  1.00 12.92 ? 74  VAL B CB  1 
ATOM   2313 C CG1 . VAL B 1 49  ? -12.198 20.341  -1.263  1.00 5.04  ? 74  VAL B CG1 1 
ATOM   2314 C CG2 . VAL B 1 49  ? -13.274 19.060  -3.100  1.00 12.78 ? 74  VAL B CG2 1 
ATOM   2315 N N   . MET B 1 50  ? -15.139 22.074  -0.375  1.00 14.22 ? 75  MET B N   1 
ATOM   2316 C CA  . MET B 1 50  ? -15.375 23.099  0.635   1.00 16.45 ? 75  MET B CA  1 
ATOM   2317 C C   . MET B 1 50  ? -16.210 22.541  1.778   1.00 16.54 ? 75  MET B C   1 
ATOM   2318 O O   . MET B 1 50  ? -15.784 22.556  2.940   1.00 15.61 ? 75  MET B O   1 
ATOM   2319 C CB  . MET B 1 50  ? -16.093 24.296  0.017   1.00 13.05 ? 75  MET B CB  1 
ATOM   2320 C CG  . MET B 1 50  ? -15.788 25.627  0.662   1.00 21.07 ? 75  MET B CG  1 
ATOM   2321 S SD  . MET B 1 50  ? -14.038 25.880  0.978   1.00 22.80 ? 75  MET B SD  1 
ATOM   2322 C CE  . MET B 1 50  ? -13.725 27.008  -0.374  1.00 16.99 ? 75  MET B CE  1 
ATOM   2323 N N   . ALA B 1 51  ? -17.382 21.983  1.451   1.00 12.45 ? 76  ALA B N   1 
ATOM   2324 C CA  . ALA B 1 51  ? -18.299 21.544  2.497   1.00 11.17 ? 76  ALA B CA  1 
ATOM   2325 C C   . ALA B 1 51  ? -17.650 20.482  3.371   1.00 17.72 ? 76  ALA B C   1 
ATOM   2326 O O   . ALA B 1 51  ? -17.650 20.592  4.605   1.00 16.43 ? 76  ALA B O   1 
ATOM   2327 C CB  . ALA B 1 51  ? -19.599 21.021  1.881   1.00 17.47 ? 76  ALA B CB  1 
ATOM   2328 N N   . ALA B 1 52  ? -16.989 19.504  2.750   1.00 14.58 ? 77  ALA B N   1 
ATOM   2329 C CA  . ALA B 1 52  ? -16.333 18.485  3.555   1.00 16.75 ? 77  ALA B CA  1 
ATOM   2330 C C   . ALA B 1 52  ? -15.228 19.098  4.402   1.00 16.35 ? 77  ALA B C   1 
ATOM   2331 O O   . ALA B 1 52  ? -15.150 18.842  5.613   1.00 17.09 ? 77  ALA B O   1 
ATOM   2332 C CB  . ALA B 1 52  ? -15.777 17.383  2.659   1.00 11.84 ? 77  ALA B CB  1 
ATOM   2333 N N   . ALA B 1 53  ? -14.472 20.033  3.826   1.00 13.47 ? 78  ALA B N   1 
ATOM   2334 C CA  . ALA B 1 53  ? -13.438 20.687  4.614   1.00 20.22 ? 78  ALA B CA  1 
ATOM   2335 C C   . ALA B 1 53  ? -14.046 21.430  5.792   1.00 14.52 ? 78  ALA B C   1 
ATOM   2336 O O   . ALA B 1 53  ? -13.552 21.320  6.923   1.00 14.39 ? 78  ALA B O   1 
ATOM   2337 C CB  . ALA B 1 53  ? -12.629 21.637  3.730   1.00 7.64  ? 78  ALA B CB  1 
ATOM   2338 N N   . ALA B 1 54  ? -15.209 22.045  5.586   1.00 11.13 ? 79  ALA B N   1 
ATOM   2339 C CA  . ALA B 1 54  ? -15.808 22.799  6.677   1.00 13.17 ? 79  ALA B CA  1 
ATOM   2340 C C   . ALA B 1 54  ? -16.225 21.873  7.807   1.00 15.40 ? 79  ALA B C   1 
ATOM   2341 O O   . ALA B 1 54  ? -15.929 22.150  8.979   1.00 13.70 ? 79  ALA B O   1 
ATOM   2342 C CB  . ALA B 1 54  ? -17.000 23.608  6.172   1.00 7.57  ? 79  ALA B CB  1 
ATOM   2343 N N   . VAL B 1 55  ? -16.725 20.683  7.467   1.00 13.17 ? 80  VAL B N   1 
ATOM   2344 C CA  . VAL B 1 55  ? -17.072 19.749  8.528   1.00 14.26 ? 80  VAL B CA  1 
ATOM   2345 C C   . VAL B 1 55  ? -15.816 19.260  9.219   1.00 12.38 ? 80  VAL B C   1 
ATOM   2346 O O   . VAL B 1 55  ? -15.756 19.212  10.456  1.00 15.61 ? 80  VAL B O   1 
ATOM   2347 C CB  . VAL B 1 55  ? -17.909 18.585  7.961   1.00 21.10 ? 80  VAL B CB  1 
ATOM   2348 C CG1 . VAL B 1 55  ? -18.150 17.525  9.030   1.00 12.42 ? 80  VAL B CG1 1 
ATOM   2349 C CG2 . VAL B 1 55  ? -19.238 19.109  7.403   1.00 15.34 ? 80  VAL B CG2 1 
ATOM   2350 N N   . LEU B 1 56  ? -14.757 19.011  8.449   1.00 13.38 ? 81  LEU B N   1 
ATOM   2351 C CA  . LEU B 1 56  ? -13.486 18.671  9.070   1.00 10.42 ? 81  LEU B CA  1 
ATOM   2352 C C   . LEU B 1 56  ? -13.044 19.761  10.038  1.00 12.42 ? 81  LEU B C   1 
ATOM   2353 O O   . LEU B 1 56  ? -12.628 19.462  11.166  1.00 14.01 ? 81  LEU B O   1 
ATOM   2354 C CB  . LEU B 1 56  ? -12.426 18.416  8.006   1.00 9.92  ? 81  LEU B CB  1 
ATOM   2355 C CG  . LEU B 1 56  ? -12.596 17.044  7.351   1.00 14.91 ? 81  LEU B CG  1 
ATOM   2356 C CD1 . LEU B 1 56  ? -11.701 16.905  6.114   1.00 13.77 ? 81  LEU B CD1 1 
ATOM   2357 C CD2 . LEU B 1 56  ? -12.382 15.902  8.355   1.00 10.91 ? 81  LEU B CD2 1 
ATOM   2358 N N   . LYS B 1 57  ? -13.172 21.034  9.641   1.00 7.29  ? 82  LYS B N   1 
ATOM   2359 C CA  . LYS B 1 57  ? -12.779 22.104  10.553  1.00 12.78 ? 82  LYS B CA  1 
ATOM   2360 C C   . LYS B 1 57  ? -13.606 22.053  11.834  1.00 15.53 ? 82  LYS B C   1 
ATOM   2361 O O   . LYS B 1 57  ? -13.051 22.133  12.939  1.00 9.78  ? 82  LYS B O   1 
ATOM   2362 C CB  . LYS B 1 57  ? -12.916 23.459  9.851   1.00 11.80 ? 82  LYS B CB  1 
ATOM   2363 C CG  . LYS B 1 57  ? -12.717 24.683  10.738  1.00 16.90 ? 82  LYS B CG  1 
ATOM   2364 C CD  . LYS B 1 57  ? -11.345 24.711  11.410  1.00 19.29 ? 82  LYS B CD  1 
ATOM   2365 C CE  . LYS B 1 57  ? -10.232 24.913  10.404  1.00 26.77 ? 82  LYS B CE  1 
ATOM   2366 N NZ  . LYS B 1 57  ? -8.890  25.025  11.064  1.00 18.12 ? 82  LYS B NZ  1 
ATOM   2367 N N   . GLN B 1 58  ? -14.920 21.811  11.710  1.00 14.01 ? 83  GLN B N   1 
ATOM   2368 C CA  . GLN B 1 58  ? -15.751 21.681  12.905  1.00 15.10 ? 83  GLN B CA  1 
ATOM   2369 C C   . GLN B 1 58  ? -15.247 20.547  13.783  1.00 17.68 ? 83  GLN B C   1 
ATOM   2370 O O   . GLN B 1 58  ? -15.284 20.640  15.016  1.00 17.30 ? 83  GLN B O   1 
ATOM   2371 C CB  . GLN B 1 58  ? -17.220 21.452  12.540  1.00 17.50 ? 83  GLN B CB  1 
ATOM   2372 C CG  . GLN B 1 58  ? -17.975 22.671  12.031  1.00 18.33 ? 83  GLN B CG  1 
ATOM   2373 C CD  . GLN B 1 58  ? -19.458 22.383  11.848  1.00 24.71 ? 83  GLN B CD  1 
ATOM   2374 O OE1 . GLN B 1 58  ? -19.842 21.272  11.482  1.00 23.92 ? 83  GLN B OE1 1 
ATOM   2375 N NE2 . GLN B 1 58  ? -20.297 23.382  12.104  1.00 18.54 ? 83  GLN B NE2 1 
ATOM   2376 N N   . SER B 1 59  ? -14.784 19.459  13.159  1.00 9.80  ? 84  SER B N   1 
ATOM   2377 C CA  . SER B 1 59  ? -14.323 18.284  13.888  1.00 17.02 ? 84  SER B CA  1 
ATOM   2378 C C   . SER B 1 59  ? -12.989 18.495  14.608  1.00 10.67 ? 84  SER B C   1 
ATOM   2379 O O   . SER B 1 59  ? -12.596 17.631  15.397  1.00 11.11 ? 84  SER B O   1 
ATOM   2380 C CB  . SER B 1 59  ? -14.237 17.089  12.933  1.00 16.69 ? 84  SER B CB  1 
ATOM   2381 O OG  . SER B 1 59  ? -13.115 17.182  12.072  1.00 8.91  ? 84  SER B OG  1 
ATOM   2382 N N   . GLU B 1 60  ? -12.287 19.609  14.371  1.00 13.44 ? 85  GLU B N   1 
ATOM   2383 C CA  . GLU B 1 60  ? -11.071 19.890  15.144  1.00 19.95 ? 85  GLU B CA  1 
ATOM   2384 C C   . GLU B 1 60  ? -11.336 20.149  16.624  1.00 18.33 ? 85  GLU B C   1 
ATOM   2385 O O   . GLU B 1 60  ? -10.426 19.975  17.438  1.00 15.34 ? 85  GLU B O   1 
ATOM   2386 C CB  . GLU B 1 60  ? -10.261 21.042  14.548  1.00 14.03 ? 85  GLU B CB  1 
ATOM   2387 C CG  . GLU B 1 60  ? -9.748  20.750  13.151  1.00 21.25 ? 85  GLU B CG  1 
ATOM   2388 C CD  . GLU B 1 60  ? -8.960  21.901  12.560  1.00 28.87 ? 85  GLU B CD  1 
ATOM   2389 O OE1 . GLU B 1 60  ? -8.495  22.759  13.339  1.00 37.12 ? 85  GLU B OE1 1 
ATOM   2390 O OE2 . GLU B 1 60  ? -8.759  21.917  11.325  1.00 29.19 ? 85  GLU B OE2 1 
ATOM   2391 N N   . THR B 1 61  ? -12.540 20.574  16.992  1.00 19.32 ? 86  THR B N   1 
ATOM   2392 C CA  . THR B 1 61  ? -12.878 20.835  18.386  1.00 23.38 ? 86  THR B CA  1 
ATOM   2393 C C   . THR B 1 61  ? -13.937 19.892  18.926  1.00 19.70 ? 86  THR B C   1 
ATOM   2394 O O   . THR B 1 61  ? -13.937 19.606  20.126  1.00 30.24 ? 86  THR B O   1 
ATOM   2395 C CB  . THR B 1 61  ? -13.365 22.284  18.585  1.00 20.92 ? 86  THR B CB  1 
ATOM   2396 O OG1 . THR B 1 61  ? -14.439 22.576  17.681  1.00 17.20 ? 86  THR B OG1 1 
ATOM   2397 C CG2 . THR B 1 61  ? -12.237 23.280  18.383  1.00 20.24 ? 86  THR B CG2 1 
ATOM   2398 N N   . GLN B 1 62  ? -14.868 19.449  18.092  1.00 22.73 ? 87  GLN B N   1 
ATOM   2399 C CA  . GLN B 1 62  ? -15.732 18.317  18.424  1.00 26.98 ? 87  GLN B CA  1 
ATOM   2400 C C   . GLN B 1 62  ? -15.145 16.980  17.968  1.00 17.87 ? 87  GLN B C   1 
ATOM   2401 O O   . GLN B 1 62  ? -15.390 16.520  16.852  1.00 23.90 ? 87  GLN B O   1 
ATOM   2402 C CB  . GLN B 1 62  ? -17.096 18.560  17.794  1.00 22.93 ? 87  GLN B CB  1 
ATOM   2403 C CG  . GLN B 1 62  ? -18.228 18.684  18.776  1.00 36.35 ? 87  GLN B CG  1 
ATOM   2404 C CD  . GLN B 1 62  ? -19.506 19.089  18.093  1.00 31.89 ? 87  GLN B CD  1 
ATOM   2405 O OE1 . GLN B 1 62  ? -19.505 19.970  17.231  1.00 26.77 ? 87  GLN B OE1 1 
ATOM   2406 N NE2 . GLN B 1 62  ? -20.607 18.440  18.457  1.00 39.28 ? 87  GLN B NE2 1 
ATOM   2407 N N   . LYS B 1 63  ? -14.365 16.336  18.845  1.00 14.80 ? 88  LYS B N   1 
ATOM   2408 C CA  . LYS B 1 63  ? -13.489 15.243  18.417  1.00 28.42 ? 88  LYS B CA  1 
ATOM   2409 C C   . LYS B 1 63  ? -14.289 14.031  17.936  1.00 32.48 ? 88  LYS B C   1 
ATOM   2410 O O   . LYS B 1 63  ? -13.777 13.231  17.145  1.00 22.02 ? 88  LYS B O   1 
ATOM   2411 C CB  . LYS B 1 63  ? -12.549 14.829  19.560  1.00 36.62 ? 88  LYS B CB  1 
ATOM   2412 C CG  . LYS B 1 63  ? -11.687 13.577  19.298  1.00 44.98 ? 88  LYS B CG  1 
ATOM   2413 C CD  . LYS B 1 63  ? -11.137 12.994  20.602  1.00 53.86 ? 88  LYS B CD  1 
ATOM   2414 C CE  . LYS B 1 63  ? -9.713  12.446  20.457  1.00 41.64 ? 88  LYS B CE  1 
ATOM   2415 N NZ  . LYS B 1 63  ? -9.691  10.989  20.124  1.00 35.76 ? 88  LYS B NZ  1 
ATOM   2416 N N   . GLN B 1 64  ? -15.536 13.891  18.395  1.00 27.97 ? 89  GLN B N   1 
ATOM   2417 C CA  . GLN B 1 64  ? -16.429 12.805  18.014  1.00 25.59 ? 89  GLN B CA  1 
ATOM   2418 C C   . GLN B 1 64  ? -17.413 13.209  16.918  1.00 20.10 ? 89  GLN B C   1 
ATOM   2419 O O   . GLN B 1 64  ? -18.419 12.520  16.718  1.00 22.61 ? 89  GLN B O   1 
ATOM   2420 C CB  . GLN B 1 64  ? -17.209 12.309  19.237  1.00 30.08 ? 89  GLN B CB  1 
ATOM   2421 C CG  . GLN B 1 64  ? -16.380 11.583  20.287  1.00 36.41 ? 89  GLN B CG  1 
ATOM   2422 C CD  . GLN B 1 64  ? -15.595 10.423  19.715  1.00 31.93 ? 89  GLN B CD  1 
ATOM   2423 O OE1 . GLN B 1 64  ? -14.364 10.421  19.736  1.00 39.62 ? 89  GLN B OE1 1 
ATOM   2424 N NE2 . GLN B 1 64  ? -16.306 9.428   19.192  1.00 40.79 ? 89  GLN B NE2 1 
ATOM   2425 N N   . LEU B 1 65  ? -17.155 14.313  16.211  1.00 20.12 ? 90  LEU B N   1 
ATOM   2426 C CA  . LEU B 1 65  ? -18.144 14.808  15.256  1.00 15.37 ? 90  LEU B CA  1 
ATOM   2427 C C   . LEU B 1 65  ? -18.297 13.870  14.064  1.00 14.36 ? 90  LEU B C   1 
ATOM   2428 O O   . LEU B 1 65  ? -19.412 13.668  13.569  1.00 19.44 ? 90  LEU B O   1 
ATOM   2429 C CB  . LEU B 1 65  ? -17.759 16.200  14.760  1.00 23.43 ? 90  LEU B CB  1 
ATOM   2430 C CG  . LEU B 1 65  ? -18.755 16.829  13.779  1.00 16.10 ? 90  LEU B CG  1 
ATOM   2431 C CD1 . LEU B 1 65  ? -20.117 17.072  14.444  1.00 12.46 ? 90  LEU B CD1 1 
ATOM   2432 C CD2 . LEU B 1 65  ? -18.209 18.091  13.134  1.00 23.24 ? 90  LEU B CD2 1 
ATOM   2433 N N   . LEU B 1 66  ? -17.194 13.295  13.578  1.00 20.21 ? 91  LEU B N   1 
ATOM   2434 C CA  . LEU B 1 66  ? -17.282 12.488  12.366  1.00 15.39 ? 91  LEU B CA  1 
ATOM   2435 C C   . LEU B 1 66  ? -18.050 11.188  12.575  1.00 17.96 ? 91  LEU B C   1 
ATOM   2436 O O   . LEU B 1 66  ? -18.471 10.572  11.590  1.00 19.81 ? 91  LEU B O   1 
ATOM   2437 C CB  . LEU B 1 66  ? -15.884 12.201  11.814  1.00 14.24 ? 91  LEU B CB  1 
ATOM   2438 C CG  . LEU B 1 66  ? -15.156 13.440  11.269  1.00 22.90 ? 91  LEU B CG  1 
ATOM   2439 C CD1 . LEU B 1 66  ? -13.837 13.069  10.585  1.00 14.92 ? 91  LEU B CD1 1 
ATOM   2440 C CD2 . LEU B 1 66  ? -16.043 14.291  10.352  1.00 24.10 ? 91  LEU B CD2 1 
ATOM   2441 N N   . ASN B 1 67  ? -18.254 10.761  13.819  1.00 16.30 ? 92  ASN B N   1 
ATOM   2442 C CA  . ASN B 1 67  ? -19.060 9.581   14.096  1.00 19.89 ? 92  ASN B CA  1 
ATOM   2443 C C   . ASN B 1 67  ? -20.517 9.928   14.353  1.00 17.43 ? 92  ASN B C   1 
ATOM   2444 O O   . ASN B 1 67  ? -21.318 9.024   14.611  1.00 23.90 ? 92  ASN B O   1 
ATOM   2445 C CB  . ASN B 1 67  ? -18.502 8.798   15.290  1.00 24.82 ? 92  ASN B CB  1 
ATOM   2446 C CG  . ASN B 1 67  ? -17.045 8.425   15.122  1.00 17.74 ? 92  ASN B CG  1 
ATOM   2447 O OD1 . ASN B 1 67  ? -16.616 8.027   14.041  1.00 21.52 ? 92  ASN B OD1 1 
ATOM   2448 N ND2 . ASN B 1 67  ? -16.280 8.529   16.204  1.00 27.75 ? 92  ASN B ND2 1 
ATOM   2449 N N   . GLN B 1 68  ? -20.873 11.206  14.288  1.00 19.29 ? 93  GLN B N   1 
ATOM   2450 C CA  . GLN B 1 68  ? -22.222 11.629  14.630  1.00 18.27 ? 93  GLN B CA  1 
ATOM   2451 C C   . GLN B 1 68  ? -23.192 11.205  13.533  1.00 21.11 ? 93  GLN B C   1 
ATOM   2452 O O   . GLN B 1 68  ? -22.961 11.506  12.357  1.00 16.00 ? 93  GLN B O   1 
ATOM   2453 C CB  . GLN B 1 68  ? -22.263 13.140  14.835  1.00 21.26 ? 93  GLN B CB  1 
ATOM   2454 C CG  . GLN B 1 68  ? -23.641 13.701  15.143  1.00 27.56 ? 93  GLN B CG  1 
ATOM   2455 C CD  . GLN B 1 68  ? -23.672 15.219  15.071  1.00 43.96 ? 93  GLN B CD  1 
ATOM   2456 O OE1 . GLN B 1 68  ? -22.952 15.897  15.807  1.00 33.94 ? 93  GLN B OE1 1 
ATOM   2457 N NE2 . GLN B 1 68  ? -24.512 15.759  14.191  1.00 24.54 ? 93  GLN B NE2 1 
ATOM   2458 N N   . PRO B 1 69  ? -24.273 10.505  13.870  1.00 25.03 ? 94  PRO B N   1 
ATOM   2459 C CA  . PRO B 1 69  ? -25.207 10.039  12.842  1.00 22.63 ? 94  PRO B CA  1 
ATOM   2460 C C   . PRO B 1 69  ? -26.202 11.108  12.423  1.00 17.12 ? 94  PRO B C   1 
ATOM   2461 O O   . PRO B 1 69  ? -26.624 11.958  13.210  1.00 24.96 ? 94  PRO B O   1 
ATOM   2462 C CB  . PRO B 1 69  ? -25.920 8.855   13.514  1.00 26.50 ? 94  PRO B CB  1 
ATOM   2463 C CG  . PRO B 1 69  ? -25.516 8.899   14.996  1.00 27.99 ? 94  PRO B CG  1 
ATOM   2464 C CD  . PRO B 1 69  ? -24.718 10.143  15.226  1.00 15.17 ? 94  PRO B CD  1 
ATOM   2465 N N   . VAL B 1 70  ? -26.551 11.054  11.142  1.00 22.04 ? 95  VAL B N   1 
ATOM   2466 C CA  . VAL B 1 70  ? -27.469 11.969  10.482  1.00 23.47 ? 95  VAL B CA  1 
ATOM   2467 C C   . VAL B 1 70  ? -28.497 11.093  9.792   1.00 17.82 ? 95  VAL B C   1 
ATOM   2468 O O   . VAL B 1 70  ? -28.128 10.232  8.983   1.00 20.17 ? 95  VAL B O   1 
ATOM   2469 C CB  . VAL B 1 70  ? -26.756 12.866  9.453   1.00 17.16 ? 95  VAL B CB  1 
ATOM   2470 C CG1 . VAL B 1 70  ? -27.749 13.780  8.754   1.00 16.71 ? 95  VAL B CG1 1 
ATOM   2471 C CG2 . VAL B 1 70  ? -25.646 13.673  10.110  1.00 22.59 ? 95  VAL B CG2 1 
ATOM   2472 N N   . GLU B 1 71  ? -29.772 11.289  10.112  1.00 17.57 ? 96  GLU B N   1 
ATOM   2473 C CA  . GLU B 1 71  ? -30.791 10.408  9.566   1.00 20.98 ? 96  GLU B CA  1 
ATOM   2474 C C   . GLU B 1 71  ? -31.166 10.816  8.149   1.00 16.51 ? 96  GLU B C   1 
ATOM   2475 O O   . GLU B 1 71  ? -31.236 12.001  7.811   1.00 18.30 ? 96  GLU B O   1 
ATOM   2476 C CB  . GLU B 1 71  ? -32.033 10.364  10.461  1.00 24.86 ? 96  GLU B CB  1 
ATOM   2477 C CG  . GLU B 1 71  ? -32.607 11.690  10.902  1.00 41.96 ? 96  GLU B CG  1 
ATOM   2478 C CD  . GLU B 1 71  ? -33.726 11.496  11.923  1.00 70.44 ? 96  GLU B CD  1 
ATOM   2479 O OE1 . GLU B 1 71  ? -34.880 11.889  11.638  1.00 57.19 ? 96  GLU B OE1 1 
ATOM   2480 O OE2 . GLU B 1 71  ? -33.450 10.934  13.005  1.00 42.80 ? 96  GLU B OE2 1 
ATOM   2481 N N   . ILE B 1 72  ? -31.388 9.806   7.318   1.00 15.78 ? 97  ILE B N   1 
ATOM   2482 C CA  . ILE B 1 72  ? -31.693 9.949   5.901   1.00 16.91 ? 97  ILE B CA  1 
ATOM   2483 C C   . ILE B 1 72  ? -33.127 9.489   5.704   1.00 14.55 ? 97  ILE B C   1 
ATOM   2484 O O   . ILE B 1 72  ? -33.435 8.301   5.861   1.00 19.66 ? 97  ILE B O   1 
ATOM   2485 C CB  . ILE B 1 72  ? -30.735 9.138   5.020   1.00 23.82 ? 97  ILE B CB  1 
ATOM   2486 C CG1 . ILE B 1 72  ? -29.280 9.351   5.447   1.00 21.74 ? 97  ILE B CG1 1 
ATOM   2487 C CG2 . ILE B 1 72  ? -30.925 9.520   3.560   1.00 24.63 ? 97  ILE B CG2 1 
ATOM   2488 C CD1 . ILE B 1 72  ? -28.793 10.774  5.296   1.00 14.33 ? 97  ILE B CD1 1 
ATOM   2489 N N   . LYS B 1 73  ? -33.952 10.373  5.406   1.00 14.45 ? 98  LYS B N   1 
ATOM   2490 C CA  . LYS B 1 73  ? -35.344 10.111  5.154   1.00 25.11 ? 98  LYS B CA  1 
ATOM   2491 C C   . LYS B 1 73  ? -35.612 10.094  3.648   1.00 21.80 ? 98  LYS B C   1 
ATOM   2492 O O   . LYS B 1 73  ? -34.860 10.699  2.870   1.00 15.44 ? 98  LYS B O   1 
ATOM   2493 C CB  . LYS B 1 73  ? -36.239 11.144  5.846   1.00 20.64 ? 98  LYS B CB  1 
ATOM   2494 C CG  . LYS B 1 73  ? -36.272 11.020  7.381   1.00 32.88 ? 98  LYS B CG  1 
ATOM   2495 C CD  . LYS B 1 73  ? -37.166 12.139  7.938   1.00 54.42 ? 98  LYS B CD  1 
ATOM   2496 C CE  . LYS B 1 73  ? -37.267 12.111  9.467   1.00 64.04 ? 98  LYS B CE  1 
ATOM   2497 N NZ  . LYS B 1 73  ? -38.687 11.738  9.869   1.00 59.64 ? 98  LYS B NZ  1 
ATOM   2498 N N   . PRO B 1 74  ? -36.664 9.383   3.205   1.00 21.31 ? 99  PRO B N   1 
ATOM   2499 C CA  . PRO B 1 74  ? -36.995 9.343   1.761   1.00 28.35 ? 99  PRO B CA  1 
ATOM   2500 C C   . PRO B 1 74  ? -37.070 10.704  1.096   1.00 22.13 ? 99  PRO B C   1 
ATOM   2501 O O   . PRO B 1 74  ? -36.676 10.845  -0.071  1.00 29.75 ? 99  PRO B O   1 
ATOM   2502 C CB  . PRO B 1 74  ? -38.365 8.651   1.753   1.00 14.75 ? 99  PRO B CB  1 
ATOM   2503 C CG  . PRO B 1 74  ? -38.327 7.759   2.955   1.00 25.72 ? 99  PRO B CG  1 
ATOM   2504 C CD  . PRO B 1 74  ? -37.575 8.543   4.002   1.00 21.57 ? 99  PRO B CD  1 
ATOM   2505 N N   . ALA B 1 75  ? -37.576 11.710  1.805   1.00 16.60 ? 100 ALA B N   1 
ATOM   2506 C CA  . ALA B 1 75  ? -37.691 13.037  1.224   1.00 30.55 ? 100 ALA B CA  1 
ATOM   2507 C C   . ALA B 1 75  ? -36.329 13.698  1.046   1.00 25.48 ? 100 ALA B C   1 
ATOM   2508 O O   . ALA B 1 75  ? -36.225 14.673  0.293   1.00 20.63 ? 100 ALA B O   1 
ATOM   2509 C CB  . ALA B 1 75  ? -38.592 13.917  2.101   1.00 17.92 ? 100 ALA B CB  1 
ATOM   2510 N N   . ASP B 1 76  ? -35.281 13.171  1.694   1.00 22.16 ? 101 ASP B N   1 
ATOM   2511 C CA  . ASP B 1 76  ? -33.939 13.726  1.537   1.00 20.74 ? 101 ASP B CA  1 
ATOM   2512 C C   . ASP B 1 76  ? -33.311 13.405  0.190   1.00 22.76 ? 101 ASP B C   1 
ATOM   2513 O O   . ASP B 1 76  ? -32.374 14.102  -0.216  1.00 21.77 ? 101 ASP B O   1 
ATOM   2514 C CB  . ASP B 1 76  ? -33.007 13.194  2.630   1.00 31.97 ? 101 ASP B CB  1 
ATOM   2515 C CG  . ASP B 1 76  ? -33.460 13.570  4.017   1.00 42.53 ? 101 ASP B CG  1 
ATOM   2516 O OD1 . ASP B 1 76  ? -34.261 14.521  4.140   1.00 47.20 ? 101 ASP B OD1 1 
ATOM   2517 O OD2 . ASP B 1 76  ? -33.079 12.859  4.977   1.00 35.66 ? 101 ASP B OD2 1 
ATOM   2518 N N   . LEU B 1 77  ? -33.787 12.383  -0.513  1.00 16.28 ? 102 LEU B N   1 
ATOM   2519 C CA  . LEU B 1 77  ? -33.126 11.977  -1.746  1.00 14.83 ? 102 LEU B CA  1 
ATOM   2520 C C   . LEU B 1 77  ? -33.302 13.045  -2.814  1.00 18.64 ? 102 LEU B C   1 
ATOM   2521 O O   . LEU B 1 77  ? -34.392 13.596  -2.992  1.00 22.51 ? 102 LEU B O   1 
ATOM   2522 C CB  . LEU B 1 77  ? -33.681 10.643  -2.240  1.00 16.10 ? 102 LEU B CB  1 
ATOM   2523 C CG  . LEU B 1 77  ? -33.430 9.472   -1.293  1.00 27.48 ? 102 LEU B CG  1 
ATOM   2524 C CD1 . LEU B 1 77  ? -33.803 8.148   -1.961  1.00 22.72 ? 102 LEU B CD1 1 
ATOM   2525 C CD2 . LEU B 1 77  ? -31.967 9.460   -0.844  1.00 23.98 ? 102 LEU B CD2 1 
ATOM   2526 N N   . VAL B 1 78  ? -32.223 13.347  -3.529  1.00 18.47 ? 103 VAL B N   1 
ATOM   2527 C CA  . VAL B 1 78  ? -32.337 14.311  -4.612  1.00 16.90 ? 103 VAL B CA  1 
ATOM   2528 C C   . VAL B 1 78  ? -32.068 13.580  -5.920  1.00 17.45 ? 103 VAL B C   1 
ATOM   2529 O O   . VAL B 1 78  ? -32.610 12.493  -6.147  1.00 23.73 ? 103 VAL B O   1 
ATOM   2530 C CB  . VAL B 1 78  ? -31.403 15.513  -4.383  1.00 16.71 ? 103 VAL B CB  1 
ATOM   2531 C CG1 . VAL B 1 78  ? -31.960 16.383  -3.265  1.00 11.61 ? 103 VAL B CG1 1 
ATOM   2532 C CG2 . VAL B 1 78  ? -30.026 15.044  -3.998  1.00 14.30 ? 103 VAL B CG2 1 
ATOM   2533 N N   . ASN B 1 79  ? -31.225 14.140  -6.780  1.00 21.59 ? 104 ASN B N   1 
ATOM   2534 C CA  . ASN B 1 79  ? -31.125 13.636  -8.143  1.00 25.84 ? 104 ASN B CA  1 
ATOM   2535 C C   . ASN B 1 79  ? -30.038 12.587  -8.327  1.00 18.42 ? 104 ASN B C   1 
ATOM   2536 O O   . ASN B 1 79  ? -30.011 11.928  -9.371  1.00 21.63 ? 104 ASN B O   1 
ATOM   2537 C CB  . ASN B 1 79  ? -30.869 14.796  -9.100  1.00 15.89 ? 104 ASN B CB  1 
ATOM   2538 C CG  . ASN B 1 79  ? -29.585 15.518  -8.783  1.00 13.45 ? 104 ASN B CG  1 
ATOM   2539 O OD1 . ASN B 1 79  ? -29.283 15.767  -7.617  1.00 17.84 ? 104 ASN B OD1 1 
ATOM   2540 N ND2 . ASN B 1 79  ? -28.813 15.851  -9.814  1.00 14.96 ? 104 ASN B ND2 1 
ATOM   2541 N N   . TYR B 1 80  ? -29.147 12.416  -7.348  1.00 18.09 ? 105 TYR B N   1 
ATOM   2542 C CA  . TYR B 1 80  ? -28.015 11.505  -7.508  1.00 19.21 ? 105 TYR B CA  1 
ATOM   2543 C C   . TYR B 1 80  ? -27.514 11.141  -6.109  1.00 10.93 ? 105 TYR B C   1 
ATOM   2544 O O   . TYR B 1 80  ? -26.813 11.934  -5.476  1.00 18.54 ? 105 TYR B O   1 
ATOM   2545 C CB  . TYR B 1 80  ? -26.907 12.120  -8.349  1.00 17.30 ? 105 TYR B CB  1 
ATOM   2546 C CG  . TYR B 1 80  ? -25.821 11.112  -8.637  1.00 29.83 ? 105 TYR B CG  1 
ATOM   2547 C CD1 . TYR B 1 80  ? -26.076 10.015  -9.455  1.00 18.01 ? 105 TYR B CD1 1 
ATOM   2548 C CD2 . TYR B 1 80  ? -24.566 11.213  -8.038  1.00 23.76 ? 105 TYR B CD2 1 
ATOM   2549 C CE1 . TYR B 1 80  ? -25.104 9.070   -9.706  1.00 26.26 ? 105 TYR B CE1 1 
ATOM   2550 C CE2 . TYR B 1 80  ? -23.578 10.265  -8.283  1.00 23.57 ? 105 TYR B CE2 1 
ATOM   2551 C CZ  . TYR B 1 80  ? -23.858 9.196   -9.118  1.00 30.46 ? 105 TYR B CZ  1 
ATOM   2552 O OH  . TYR B 1 80  ? -22.897 8.245   -9.368  1.00 30.59 ? 105 TYR B OH  1 
ATOM   2553 N N   . ASN B 1 81  ? -27.881 9.954   -5.650  1.00 15.84 ? 106 ASN B N   1 
ATOM   2554 C CA  . ASN B 1 81  ? -27.742 9.537   -4.261  1.00 14.43 ? 106 ASN B CA  1 
ATOM   2555 C C   . ASN B 1 81  ? -27.207 8.112   -4.186  1.00 19.63 ? 106 ASN B C   1 
ATOM   2556 O O   . ASN B 1 81  ? -27.827 7.267   -3.528  1.00 20.27 ? 106 ASN B O   1 
ATOM   2557 C CB  . ASN B 1 81  ? -29.093 9.622   -3.554  1.00 26.65 ? 106 ASN B CB  1 
ATOM   2558 C CG  . ASN B 1 81  ? -29.969 10.713  -4.116  1.00 17.27 ? 106 ASN B CG  1 
ATOM   2559 O OD1 . ASN B 1 81  ? -29.709 11.896  -3.908  1.00 18.70 ? 106 ASN B OD1 1 
ATOM   2560 N ND2 . ASN B 1 81  ? -30.997 10.324  -4.863  1.00 18.68 ? 106 ASN B ND2 1 
ATOM   2561 N N   . PRO B 1 82  ? -26.086 7.793   -4.845  1.00 16.14 ? 107 PRO B N   1 
ATOM   2562 C CA  . PRO B 1 82  ? -25.688 6.376   -4.949  1.00 18.23 ? 107 PRO B CA  1 
ATOM   2563 C C   . PRO B 1 82  ? -25.416 5.705   -3.610  1.00 20.45 ? 107 PRO B C   1 
ATOM   2564 O O   . PRO B 1 82  ? -25.636 4.494   -3.481  1.00 29.29 ? 107 PRO B O   1 
ATOM   2565 C CB  . PRO B 1 82  ? -24.411 6.434   -5.800  1.00 16.64 ? 107 PRO B CB  1 
ATOM   2566 C CG  . PRO B 1 82  ? -23.882 7.823   -5.586  1.00 20.13 ? 107 PRO B CG  1 
ATOM   2567 C CD  . PRO B 1 82  ? -25.100 8.688   -5.475  1.00 15.09 ? 107 PRO B CD  1 
ATOM   2568 N N   . ILE B 1 83  ? -24.989 6.453   -2.601  1.00 12.82 ? 108 ILE B N   1 
ATOM   2569 C CA  . ILE B 1 83  ? -24.741 5.904   -1.273  1.00 19.12 ? 108 ILE B CA  1 
ATOM   2570 C C   . ILE B 1 83  ? -25.944 6.105   -0.361  1.00 19.86 ? 108 ILE B C   1 
ATOM   2571 O O   . ILE B 1 83  ? -26.368 5.183   0.335   1.00 19.76 ? 108 ILE B O   1 
ATOM   2572 C CB  . ILE B 1 83  ? -23.465 6.524   -0.658  1.00 18.34 ? 108 ILE B CB  1 
ATOM   2573 C CG1 . ILE B 1 83  ? -22.274 6.420   -1.620  1.00 21.96 ? 108 ILE B CG1 1 
ATOM   2574 C CG2 . ILE B 1 83  ? -23.113 5.804   0.639   1.00 12.05 ? 108 ILE B CG2 1 
ATOM   2575 C CD1 . ILE B 1 83  ? -21.972 5.023   -2.107  1.00 18.00 ? 108 ILE B CD1 1 
ATOM   2576 N N   . ALA B 1 84  ? -26.509 7.316   -0.359  1.00 18.40 ? 109 ALA B N   1 
ATOM   2577 C CA  . ALA B 1 84  ? -27.542 7.665   0.611   1.00 17.38 ? 109 ALA B CA  1 
ATOM   2578 C C   . ALA B 1 84  ? -28.811 6.843   0.421   1.00 21.25 ? 109 ALA B C   1 
ATOM   2579 O O   . ALA B 1 84  ? -29.543 6.614   1.391   1.00 22.81 ? 109 ALA B O   1 
ATOM   2580 C CB  . ALA B 1 84  ? -27.863 9.157   0.520   1.00 27.85 ? 109 ALA B CB  1 
ATOM   2581 N N   . GLU B 1 85  ? -29.104 6.408   -0.810  1.00 15.69 ? 110 GLU B N   1 
ATOM   2582 C CA  . GLU B 1 85  ? -30.297 5.593   -1.038  1.00 21.65 ? 110 GLU B CA  1 
ATOM   2583 C C   . GLU B 1 85  ? -30.205 4.259   -0.311  1.00 26.70 ? 110 GLU B C   1 
ATOM   2584 O O   . GLU B 1 85  ? -31.238 3.637   -0.034  1.00 24.77 ? 110 GLU B O   1 
ATOM   2585 C CB  . GLU B 1 85  ? -30.532 5.357   -2.535  1.00 12.93 ? 110 GLU B CB  1 
ATOM   2586 C CG  . GLU B 1 85  ? -29.500 4.468   -3.211  1.00 27.56 ? 110 GLU B CG  1 
ATOM   2587 C CD  . GLU B 1 85  ? -29.704 4.381   -4.717  1.00 58.62 ? 110 GLU B CD  1 
ATOM   2588 O OE1 . GLU B 1 85  ? -30.494 5.188   -5.256  1.00 38.62 ? 110 GLU B OE1 1 
ATOM   2589 O OE2 . GLU B 1 85  ? -29.084 3.501   -5.358  1.00 50.03 ? 110 GLU B OE2 1 
ATOM   2590 N N   . LYS B 1 86  ? -28.986 3.808   -0.011  1.00 18.32 ? 111 LYS B N   1 
ATOM   2591 C CA  . LYS B 1 86  ? -28.767 2.603   0.774   1.00 14.73 ? 111 LYS B CA  1 
ATOM   2592 C C   . LYS B 1 86  ? -29.142 2.801   2.236   1.00 25.21 ? 111 LYS B C   1 
ATOM   2593 O O   . LYS B 1 86  ? -29.333 1.816   2.960   1.00 25.13 ? 111 LYS B O   1 
ATOM   2594 C CB  . LYS B 1 86  ? -27.284 2.236   0.693   1.00 23.37 ? 111 LYS B CB  1 
ATOM   2595 C CG  . LYS B 1 86  ? -26.774 1.852   -0.691  0.81 24.87 ? 111 LYS B CG  1 
ATOM   2596 C CD  . LYS B 1 86  ? -25.253 1.659   -0.655  1.00 31.97 ? 111 LYS B CD  1 
ATOM   2597 C CE  . LYS B 1 86  ? -24.820 0.205   -0.627  1.00 47.37 ? 111 LYS B CE  1 
ATOM   2598 N NZ  . LYS B 1 86  ? -23.412 0.083   -1.116  1.00 34.12 ? 111 LYS B NZ  1 
ATOM   2599 N N   . HIS B 1 87  ? -29.246 4.053   2.683   1.00 20.73 ? 112 HIS B N   1 
ATOM   2600 C CA  . HIS B 1 87  ? -29.427 4.383   4.092   1.00 18.48 ? 112 HIS B CA  1 
ATOM   2601 C C   . HIS B 1 87  ? -30.728 5.125   4.370   1.00 17.91 ? 112 HIS B C   1 
ATOM   2602 O O   . HIS B 1 87  ? -30.883 5.689   5.460   1.00 19.85 ? 112 HIS B O   1 
ATOM   2603 C CB  . HIS B 1 87  ? -28.232 5.205   4.587   1.00 16.34 ? 112 HIS B CB  1 
ATOM   2604 C CG  . HIS B 1 87  ? -26.915 4.502   4.443   1.00 19.25 ? 112 HIS B CG  1 
ATOM   2605 N ND1 . HIS B 1 87  ? -26.503 3.507   5.304   1.00 27.92 ? 112 HIS B ND1 1 
ATOM   2606 C CD2 . HIS B 1 87  ? -25.932 4.630   3.520   1.00 15.70 ? 112 HIS B CD2 1 
ATOM   2607 C CE1 . HIS B 1 87  ? -25.315 3.065   4.927   1.00 22.40 ? 112 HIS B CE1 1 
ATOM   2608 N NE2 . HIS B 1 87  ? -24.946 3.730   3.847   1.00 19.20 ? 112 HIS B NE2 1 
ATOM   2609 N N   . VAL B 1 88  ? -31.654 5.163   3.408   1.00 16.16 ? 113 VAL B N   1 
ATOM   2610 C CA  . VAL B 1 88  ? -32.947 5.796   3.639   1.00 12.22 ? 113 VAL B CA  1 
ATOM   2611 C C   . VAL B 1 88  ? -33.652 5.079   4.782   1.00 17.82 ? 113 VAL B C   1 
ATOM   2612 O O   . VAL B 1 88  ? -33.552 3.852   4.923   1.00 20.56 ? 113 VAL B O   1 
ATOM   2613 C CB  . VAL B 1 88  ? -33.783 5.771   2.348   1.00 18.94 ? 113 VAL B CB  1 
ATOM   2614 C CG1 . VAL B 1 88  ? -35.167 6.316   2.593   1.00 22.77 ? 113 VAL B CG1 1 
ATOM   2615 C CG2 . VAL B 1 88  ? -33.091 6.559   1.253   1.00 21.95 ? 113 VAL B CG2 1 
ATOM   2616 N N   . ASN B 1 89  ? -34.357 5.850   5.616   1.00 12.38 ? 114 ASN B N   1 
ATOM   2617 C CA  . ASN B 1 89  ? -34.945 5.359   6.867   1.00 15.92 ? 114 ASN B CA  1 
ATOM   2618 C C   . ASN B 1 89  ? -33.869 4.799   7.785   1.00 14.02 ? 114 ASN B C   1 
ATOM   2619 O O   . ASN B 1 89  ? -34.142 3.960   8.645   1.00 22.65 ? 114 ASN B O   1 
ATOM   2620 C CB  . ASN B 1 89  ? -36.018 4.291   6.625   1.00 19.48 ? 114 ASN B CB  1 
ATOM   2621 C CG  . ASN B 1 89  ? -37.194 4.807   5.829   1.00 14.74 ? 114 ASN B CG  1 
ATOM   2622 O OD1 . ASN B 1 89  ? -37.807 5.817   6.175   1.00 19.01 ? 114 ASN B OD1 1 
ATOM   2623 N ND2 . ASN B 1 89  ? -37.537 4.091   4.766   1.00 14.95 ? 114 ASN B ND2 1 
ATOM   2624 N N   . GLY B 1 90  ? -32.643 5.280   7.615   1.00 20.47 ? 115 GLY B N   1 
ATOM   2625 C CA  . GLY B 1 90  ? -31.544 4.963   8.501   1.00 8.80  ? 115 GLY B CA  1 
ATOM   2626 C C   . GLY B 1 90  ? -30.668 6.180   8.689   1.00 13.49 ? 115 GLY B C   1 
ATOM   2627 O O   . GLY B 1 90  ? -31.152 7.304   8.577   1.00 14.88 ? 115 GLY B O   1 
ATOM   2628 N N   . THR B 1 91  ? -29.405 5.981   9.047   1.00 13.07 ? 116 THR B N   1 
ATOM   2629 C CA  . THR B 1 91  ? -28.478 7.079   9.267   1.00 13.67 ? 116 THR B CA  1 
ATOM   2630 C C   . THR B 1 91  ? -27.170 6.837   8.529   1.00 14.30 ? 116 THR B C   1 
ATOM   2631 O O   . THR B 1 91  ? -26.827 5.706   8.174   1.00 13.18 ? 116 THR B O   1 
ATOM   2632 C CB  . THR B 1 91  ? -28.173 7.280   10.758  1.00 13.24 ? 116 THR B CB  1 
ATOM   2633 O OG1 . THR B 1 91  ? -27.693 6.052   11.316  1.00 14.16 ? 116 THR B OG1 1 
ATOM   2634 C CG2 . THR B 1 91  ? -29.425 7.715   11.509  1.00 13.33 ? 116 THR B CG2 1 
ATOM   2635 N N   . MET B 1 92  ? -26.453 7.925   8.277   1.00 15.03 ? 117 MET B N   1 
ATOM   2636 C CA  . MET B 1 92  ? -25.035 7.815   7.970   1.00 22.43 ? 117 MET B CA  1 
ATOM   2637 C C   . MET B 1 92  ? -24.282 8.789   8.860   1.00 19.47 ? 117 MET B C   1 
ATOM   2638 O O   . MET B 1 92  ? -24.817 9.819   9.268   1.00 21.81 ? 117 MET B O   1 
ATOM   2639 C CB  . MET B 1 92  ? -24.697 8.085   6.487   1.00 19.61 ? 117 MET B CB  1 
ATOM   2640 C CG  . MET B 1 92  ? -25.622 7.428   5.488   1.00 19.88 ? 117 MET B CG  1 
ATOM   2641 S SD  . MET B 1 92  ? -25.528 8.183   3.855   1.00 19.93 ? 117 MET B SD  1 
ATOM   2642 C CE  . MET B 1 92  ? -23.753 8.273   3.619   1.00 19.97 ? 117 MET B CE  1 
ATOM   2643 N N   . THR B 1 93  ? -23.027 8.466   9.147   1.00 18.30 ? 118 THR B N   1 
ATOM   2644 C CA  . THR B 1 93  ? -22.236 9.368   9.961   1.00 15.45 ? 118 THR B CA  1 
ATOM   2645 C C   . THR B 1 93  ? -21.689 10.492  9.096   1.00 15.19 ? 118 THR B C   1 
ATOM   2646 O O   . THR B 1 93  ? -21.666 10.404  7.866   1.00 13.62 ? 118 THR B O   1 
ATOM   2647 C CB  . THR B 1 93  ? -21.101 8.622   10.658  1.00 23.17 ? 118 THR B CB  1 
ATOM   2648 O OG1 . THR B 1 93  ? -20.147 8.182   9.684   1.00 18.89 ? 118 THR B OG1 1 
ATOM   2649 C CG2 . THR B 1 93  ? -21.661 7.405   11.411  1.00 16.02 ? 118 THR B CG2 1 
ATOM   2650 N N   . LEU B 1 94  ? -21.261 11.572  9.753   1.00 15.48 ? 119 LEU B N   1 
ATOM   2651 C CA  . LEU B 1 94  ? -20.675 12.673  9.000   1.00 12.41 ? 119 LEU B CA  1 
ATOM   2652 C C   . LEU B 1 94  ? -19.390 12.247  8.299   1.00 18.71 ? 119 LEU B C   1 
ATOM   2653 O O   . LEU B 1 94  ? -19.056 12.787  7.241   1.00 22.61 ? 119 LEU B O   1 
ATOM   2654 C CB  . LEU B 1 94  ? -20.431 13.883  9.902   1.00 16.48 ? 119 LEU B CB  1 
ATOM   2655 C CG  . LEU B 1 94  ? -21.683 14.703  10.229  1.00 19.22 ? 119 LEU B CG  1 
ATOM   2656 C CD1 . LEU B 1 94  ? -21.408 15.702  11.353  1.00 12.81 ? 119 LEU B CD1 1 
ATOM   2657 C CD2 . LEU B 1 94  ? -22.214 15.412  8.993   1.00 22.46 ? 119 LEU B CD2 1 
ATOM   2658 N N   . ALA B 1 95  ? -18.651 11.293  8.867   1.00 14.36 ? 120 ALA B N   1 
ATOM   2659 C CA  . ALA B 1 95  ? -17.527 10.714  8.135   1.00 23.89 ? 120 ALA B CA  1 
ATOM   2660 C C   . ALA B 1 95  ? -18.012 10.010  6.873   1.00 20.75 ? 120 ALA B C   1 
ATOM   2661 O O   . ALA B 1 95  ? -17.452 10.193  5.784   1.00 23.09 ? 120 ALA B O   1 
ATOM   2662 C CB  . ALA B 1 95  ? -16.751 9.745   9.029   1.00 12.64 ? 120 ALA B CB  1 
ATOM   2663 N N   . GLU B 1 96  ? -19.050 9.182   7.007   1.00 12.57 ? 121 GLU B N   1 
ATOM   2664 C CA  . GLU B 1 96  ? -19.605 8.489   5.848   1.00 25.32 ? 121 GLU B CA  1 
ATOM   2665 C C   . GLU B 1 96  ? -20.195 9.460   4.841   1.00 15.72 ? 121 GLU B C   1 
ATOM   2666 O O   . GLU B 1 96  ? -20.081 9.251   3.631   1.00 19.17 ? 121 GLU B O   1 
ATOM   2667 C CB  . GLU B 1 96  ? -20.670 7.500   6.303   1.00 25.01 ? 121 GLU B CB  1 
ATOM   2668 C CG  . GLU B 1 96  ? -20.109 6.425   7.173   1.00 36.00 ? 121 GLU B CG  1 
ATOM   2669 C CD  . GLU B 1 96  ? -21.174 5.680   7.925   1.00 32.05 ? 121 GLU B CD  1 
ATOM   2670 O OE1 . GLU B 1 96  ? -20.791 4.799   8.706   1.00 32.95 ? 121 GLU B OE1 1 
ATOM   2671 O OE2 . GLU B 1 96  ? -22.375 5.987   7.756   1.00 31.69 ? 121 GLU B OE2 1 
ATOM   2672 N N   . LEU B 1 97  ? -20.835 10.530  5.320   1.00 15.31 ? 122 LEU B N   1 
ATOM   2673 C CA  . LEU B 1 97  ? -21.400 11.517  4.404   1.00 14.76 ? 122 LEU B CA  1 
ATOM   2674 C C   . LEU B 1 97  ? -20.305 12.273  3.678   1.00 15.06 ? 122 LEU B C   1 
ATOM   2675 O O   . LEU B 1 97  ? -20.419 12.553  2.481   1.00 15.90 ? 122 LEU B O   1 
ATOM   2676 C CB  . LEU B 1 97  ? -22.300 12.487  5.164   1.00 16.01 ? 122 LEU B CB  1 
ATOM   2677 C CG  . LEU B 1 97  ? -23.590 11.834  5.652   1.00 18.32 ? 122 LEU B CG  1 
ATOM   2678 C CD1 . LEU B 1 97  ? -24.183 12.615  6.814   1.00 15.76 ? 122 LEU B CD1 1 
ATOM   2679 C CD2 . LEU B 1 97  ? -24.588 11.701  4.502   1.00 16.92 ? 122 LEU B CD2 1 
ATOM   2680 N N   . SER B 1 98  ? -19.228 12.596  4.387   1.00 14.46 ? 123 SER B N   1 
ATOM   2681 C CA  . SER B 1 98  ? -18.114 13.282  3.756   1.00 15.21 ? 123 SER B CA  1 
ATOM   2682 C C   . SER B 1 98  ? -17.468 12.398  2.701   1.00 13.18 ? 123 SER B C   1 
ATOM   2683 O O   . SER B 1 98  ? -17.167 12.860  1.593   1.00 17.99 ? 123 SER B O   1 
ATOM   2684 C CB  . SER B 1 98  ? -17.099 13.688  4.818   1.00 13.60 ? 123 SER B CB  1 
ATOM   2685 O OG  . SER B 1 98  ? -17.680 14.565  5.767   1.00 14.83 ? 123 SER B OG  1 
ATOM   2686 N N   . ALA B 1 99  ? -17.272 11.113  3.017   1.00 10.52 ? 124 ALA B N   1 
ATOM   2687 C CA  . ALA B 1 99  ? -16.682 10.212  2.034   1.00 13.25 ? 124 ALA B CA  1 
ATOM   2688 C C   . ALA B 1 99  ? -17.616 9.998   0.850   1.00 13.46 ? 124 ALA B C   1 
ATOM   2689 O O   . ALA B 1 99  ? -17.162 9.968   -0.296  1.00 10.89 ? 124 ALA B O   1 
ATOM   2690 C CB  . ALA B 1 99  ? -16.333 8.870   2.684   1.00 8.15  ? 124 ALA B CB  1 
ATOM   2691 N N   . ALA B 1 100 ? -18.925 9.870   1.096   1.00 12.82 ? 125 ALA B N   1 
ATOM   2692 C CA  . ALA B 1 100 ? -19.863 9.687   -0.010  1.00 15.78 ? 125 ALA B CA  1 
ATOM   2693 C C   . ALA B 1 100 ? -19.907 10.914  -0.913  1.00 11.60 ? 125 ALA B C   1 
ATOM   2694 O O   . ALA B 1 100 ? -19.813 10.788  -2.141  1.00 16.48 ? 125 ALA B O   1 
ATOM   2695 C CB  . ALA B 1 100 ? -21.256 9.374   0.531   1.00 11.43 ? 125 ALA B CB  1 
ATOM   2696 N N   . ALA B 1 101 ? -19.941 12.107  -0.312  1.00 8.86  ? 126 ALA B N   1 
ATOM   2697 C CA  . ALA B 1 101 ? -19.904 13.356  -1.068  1.00 11.97 ? 126 ALA B CA  1 
ATOM   2698 C C   . ALA B 1 101 ? -18.630 13.479  -1.891  1.00 16.28 ? 126 ALA B C   1 
ATOM   2699 O O   . ALA B 1 101 ? -18.679 13.850  -3.068  1.00 13.58 ? 126 ALA B O   1 
ATOM   2700 C CB  . ALA B 1 101 ? -20.049 14.550  -0.127  1.00 8.19  ? 126 ALA B CB  1 
ATOM   2701 N N   . LEU B 1 102 ? -17.470 13.204  -1.287  1.00 12.56 ? 127 LEU B N   1 
ATOM   2702 C CA  . LEU B 1 102 ? -16.231 13.460  -2.014  1.00 12.65 ? 127 LEU B CA  1 
ATOM   2703 C C   . LEU B 1 102 ? -15.947 12.370  -3.040  1.00 12.36 ? 127 LEU B C   1 
ATOM   2704 O O   . LEU B 1 102 ? -15.647 12.668  -4.200  1.00 13.46 ? 127 LEU B O   1 
ATOM   2705 C CB  . LEU B 1 102 ? -15.057 13.583  -1.040  1.00 12.45 ? 127 LEU B CB  1 
ATOM   2706 C CG  . LEU B 1 102 ? -15.090 14.836  -0.168  1.00 23.31 ? 127 LEU B CG  1 
ATOM   2707 C CD1 . LEU B 1 102 ? -13.918 14.852  0.802   1.00 18.03 ? 127 LEU B CD1 1 
ATOM   2708 C CD2 . LEU B 1 102 ? -15.093 16.075  -1.052  1.00 8.03  ? 127 LEU B CD2 1 
ATOM   2709 N N   . GLN B 1 103 ? -16.067 11.105  -2.651  1.00 15.26 ? 128 GLN B N   1 
ATOM   2710 C CA  . GLN B 1 103 ? -15.587 10.025  -3.493  1.00 13.33 ? 128 GLN B CA  1 
ATOM   2711 C C   . GLN B 1 103 ? -16.644 9.523   -4.462  1.00 16.28 ? 128 GLN B C   1 
ATOM   2712 O O   . GLN B 1 103 ? -16.293 8.990   -5.521  1.00 17.68 ? 128 GLN B O   1 
ATOM   2713 C CB  . GLN B 1 103 ? -15.098 8.883   -2.606  1.00 16.85 ? 128 GLN B CB  1 
ATOM   2714 C CG  . GLN B 1 103 ? -14.059 9.353   -1.612  1.00 9.71  ? 128 GLN B CG  1 
ATOM   2715 C CD  . GLN B 1 103 ? -13.459 8.233   -0.810  1.00 19.47 ? 128 GLN B CD  1 
ATOM   2716 O OE1 . GLN B 1 103 ? -12.249 8.211   -0.556  1.00 20.01 ? 128 GLN B OE1 1 
ATOM   2717 N NE2 . GLN B 1 103 ? -14.292 7.273   -0.426  1.00 19.89 ? 128 GLN B NE2 1 
ATOM   2718 N N   . TYR B 1 104 ? -17.930 9.686   -4.143  1.00 17.86 ? 129 TYR B N   1 
ATOM   2719 C CA  . TYR B 1 104 ? -18.988 9.259   -5.042  1.00 16.28 ? 129 TYR B CA  1 
ATOM   2720 C C   . TYR B 1 104 ? -19.844 10.415  -5.518  1.00 13.43 ? 129 TYR B C   1 
ATOM   2721 O O   . TYR B 1 104 ? -20.762 10.197  -6.317  1.00 18.96 ? 129 TYR B O   1 
ATOM   2722 C CB  . TYR B 1 104 ? -19.863 8.167   -4.407  1.00 12.84 ? 129 TYR B CB  1 
ATOM   2723 C CG  . TYR B 1 104 ? -19.088 6.916   -4.086  1.00 16.74 ? 129 TYR B CG  1 
ATOM   2724 C CD1 . TYR B 1 104 ? -18.321 6.812   -2.929  1.00 11.69 ? 129 TYR B CD1 1 
ATOM   2725 C CD2 . TYR B 1 104 ? -19.065 5.854   -4.989  1.00 18.81 ? 129 TYR B CD2 1 
ATOM   2726 C CE1 . TYR B 1 104 ? -17.597 5.658   -2.657  1.00 28.38 ? 129 TYR B CE1 1 
ATOM   2727 C CE2 . TYR B 1 104 ? -18.340 4.701   -4.732  1.00 15.19 ? 129 TYR B CE2 1 
ATOM   2728 C CZ  . TYR B 1 104 ? -17.609 4.608   -3.567  1.00 20.08 ? 129 TYR B CZ  1 
ATOM   2729 O OH  . TYR B 1 104 ? -16.888 3.465   -3.314  1.00 21.11 ? 129 TYR B OH  1 
ATOM   2730 N N   . SER B 1 105 ? -19.557 11.635  -5.067  1.00 10.97 ? 130 SER B N   1 
ATOM   2731 C CA  . SER B 1 105 ? -20.325 12.817  -5.443  1.00 12.91 ? 130 SER B CA  1 
ATOM   2732 C C   . SER B 1 105 ? -21.822 12.618  -5.190  1.00 12.55 ? 130 SER B C   1 
ATOM   2733 O O   . SER B 1 105 ? -22.673 12.960  -6.012  1.00 15.58 ? 130 SER B O   1 
ATOM   2734 C CB  . SER B 1 105 ? -20.047 13.190  -6.901  1.00 10.17 ? 130 SER B CB  1 
ATOM   2735 O OG  . SER B 1 105 ? -20.195 14.584  -7.101  1.00 19.09 ? 130 SER B OG  1 
ATOM   2736 N N   . ASP B 1 106 ? -22.136 12.071  -4.019  1.00 13.34 ? 131 ASP B N   1 
ATOM   2737 C CA  . ASP B 1 106 ? -23.522 11.857  -3.615  1.00 13.49 ? 131 ASP B CA  1 
ATOM   2738 C C   . ASP B 1 106 ? -24.129 13.199  -3.212  1.00 11.90 ? 131 ASP B C   1 
ATOM   2739 O O   . ASP B 1 106 ? -23.646 13.849  -2.280  1.00 12.26 ? 131 ASP B O   1 
ATOM   2740 C CB  . ASP B 1 106 ? -23.577 10.863  -2.457  1.00 16.66 ? 131 ASP B CB  1 
ATOM   2741 C CG  . ASP B 1 106 ? -24.996 10.440  -2.101  1.00 16.63 ? 131 ASP B CG  1 
ATOM   2742 O OD1 . ASP B 1 106 ? -25.848 11.312  -1.820  1.00 19.75 ? 131 ASP B OD1 1 
ATOM   2743 O OD2 . ASP B 1 106 ? -25.252 9.217   -2.082  1.00 22.48 ? 131 ASP B OD2 1 
ATOM   2744 N N   . ASN B 1 107 ? -25.205 13.604  -3.895  1.00 11.93 ? 132 ASN B N   1 
ATOM   2745 C CA  . ASN B 1 107 ? -25.776 14.925  -3.645  1.00 19.08 ? 132 ASN B CA  1 
ATOM   2746 C C   . ASN B 1 107 ? -26.579 14.989  -2.352  1.00 7.88  ? 132 ASN B C   1 
ATOM   2747 O O   . ASN B 1 107 ? -26.633 16.051  -1.720  1.00 11.80 ? 132 ASN B O   1 
ATOM   2748 C CB  . ASN B 1 107 ? -26.663 15.341  -4.821  1.00 12.72 ? 132 ASN B CB  1 
ATOM   2749 C CG  . ASN B 1 107 ? -25.880 15.966  -5.945  1.00 16.73 ? 132 ASN B CG  1 
ATOM   2750 O OD1 . ASN B 1 107 ? -24.697 16.273  -5.792  1.00 16.18 ? 132 ASN B OD1 1 
ATOM   2751 N ND2 . ASN B 1 107 ? -26.528 16.151  -7.090  1.00 16.34 ? 132 ASN B ND2 1 
ATOM   2752 N N   . THR B 1 108 ? -27.192 13.885  -1.922  1.00 16.04 ? 133 THR B N   1 
ATOM   2753 C CA  . THR B 1 108 ? -27.857 13.910  -0.622  1.00 14.24 ? 133 THR B CA  1 
ATOM   2754 C C   . THR B 1 108 ? -26.830 14.061  0.493   1.00 8.60  ? 133 THR B C   1 
ATOM   2755 O O   . THR B 1 108 ? -27.075 14.758  1.485   1.00 10.83 ? 133 THR B O   1 
ATOM   2756 C CB  . THR B 1 108 ? -28.708 12.654  -0.432  1.00 15.10 ? 133 THR B CB  1 
ATOM   2757 O OG1 . THR B 1 108 ? -29.758 12.645  -1.406  1.00 15.42 ? 133 THR B OG1 1 
ATOM   2758 C CG2 . THR B 1 108 ? -29.323 12.613  0.966   1.00 20.59 ? 133 THR B CG2 1 
ATOM   2759 N N   . ALA B 1 109 ? -25.677 13.403  0.352   1.00 8.73  ? 134 ALA B N   1 
ATOM   2760 C CA  . ALA B 1 109 ? -24.608 13.563  1.332   1.00 7.71  ? 134 ALA B CA  1 
ATOM   2761 C C   . ALA B 1 109 ? -24.124 15.010  1.373   1.00 10.31 ? 134 ALA B C   1 
ATOM   2762 O O   . ALA B 1 109 ? -23.885 15.565  2.453   1.00 9.54  ? 134 ALA B O   1 
ATOM   2763 C CB  . ALA B 1 109 ? -23.460 12.607  1.022   1.00 9.33  ? 134 ALA B CB  1 
ATOM   2764 N N   . MET B 1 110 ? -23.896 15.610  0.197   1.00 10.45 ? 135 MET B N   1 
ATOM   2765 C CA  . MET B 1 110 ? -23.669 17.054  0.125   1.00 10.67 ? 135 MET B CA  1 
ATOM   2766 C C   . MET B 1 110 ? -24.692 17.828  0.937   1.00 9.05  ? 135 MET B C   1 
ATOM   2767 O O   . MET B 1 110 ? -24.331 18.714  1.720   1.00 10.44 ? 135 MET B O   1 
ATOM   2768 C CB  . MET B 1 110 ? -23.708 17.527  -1.329  1.00 14.34 ? 135 MET B CB  1 
ATOM   2769 C CG  . MET B 1 110 ? -23.193 18.956  -1.590  1.00 22.60 ? 135 MET B CG  1 
ATOM   2770 S SD  . MET B 1 110 ? -21.950 19.692  -0.507  1.00 20.18 ? 135 MET B SD  1 
ATOM   2771 C CE  . MET B 1 110 ? -21.537 21.172  -1.443  1.00 11.67 ? 135 MET B CE  1 
ATOM   2772 N N   . ASN B 1 111 ? -25.982 17.533  0.737   1.00 8.11  ? 136 ASN B N   1 
ATOM   2773 C CA  . ASN B 1 111 ? -26.994 18.321  1.433   1.00 7.87  ? 136 ASN B CA  1 
ATOM   2774 C C   . ASN B 1 111 ? -26.937 18.102  2.938   1.00 10.75 ? 136 ASN B C   1 
ATOM   2775 O O   . ASN B 1 111 ? -27.185 19.037  3.710   1.00 20.03 ? 136 ASN B O   1 
ATOM   2776 C CB  . ASN B 1 111 ? -28.394 18.001  0.911   1.00 4.60  ? 136 ASN B CB  1 
ATOM   2777 C CG  . ASN B 1 111 ? -28.725 18.750  -0.357  1.00 12.18 ? 136 ASN B CG  1 
ATOM   2778 O OD1 . ASN B 1 111 ? -28.002 19.662  -0.752  1.00 22.68 ? 136 ASN B OD1 1 
ATOM   2779 N ND2 . ASN B 1 111 ? -29.838 18.391  -0.990  1.00 14.31 ? 136 ASN B ND2 1 
ATOM   2780 N N   . LYS B 1 112 ? -26.569 16.897  3.372   1.00 7.34  ? 137 LYS B N   1 
ATOM   2781 C CA  . LYS B 1 112 ? -26.403 16.667  4.803   1.00 12.41 ? 137 LYS B CA  1 
ATOM   2782 C C   . LYS B 1 112 ? -25.219 17.457  5.355   1.00 11.36 ? 137 LYS B C   1 
ATOM   2783 O O   . LYS B 1 112 ? -25.293 17.999  6.466   1.00 14.14 ? 137 LYS B O   1 
ATOM   2784 C CB  . LYS B 1 112 ? -26.249 15.171  5.066   1.00 10.70 ? 137 LYS B CB  1 
ATOM   2785 C CG  . LYS B 1 112 ? -27.527 14.412  4.731   1.00 13.11 ? 137 LYS B CG  1 
ATOM   2786 C CD  . LYS B 1 112 ? -28.740 15.049  5.387   1.00 12.68 ? 137 LYS B CD  1 
ATOM   2787 C CE  . LYS B 1 112 ? -29.965 14.152  5.270   1.00 33.10 ? 137 LYS B CE  1 
ATOM   2788 N NZ  . LYS B 1 112 ? -31.235 14.900  5.491   1.00 21.65 ? 137 LYS B NZ  1 
ATOM   2789 N N   . LEU B 1 113 ? -24.135 17.568  4.582   1.00 7.03  ? 138 LEU B N   1 
ATOM   2790 C CA  . LEU B 1 113 ? -22.999 18.372  5.036   1.00 16.30 ? 138 LEU B CA  1 
ATOM   2791 C C   . LEU B 1 113 ? -23.395 19.837  5.130   1.00 13.68 ? 138 LEU B C   1 
ATOM   2792 O O   . LEU B 1 113 ? -23.050 20.526  6.097   1.00 13.78 ? 138 LEU B O   1 
ATOM   2793 C CB  . LEU B 1 113 ? -21.783 18.205  4.122   1.00 9.76  ? 138 LEU B CB  1 
ATOM   2794 C CG  . LEU B 1 113 ? -21.218 16.805  3.899   1.00 18.11 ? 138 LEU B CG  1 
ATOM   2795 C CD1 . LEU B 1 113 ? -20.003 16.882  2.977   1.00 18.85 ? 138 LEU B CD1 1 
ATOM   2796 C CD2 . LEU B 1 113 ? -20.856 16.166  5.232   1.00 15.00 ? 138 LEU B CD2 1 
ATOM   2797 N N   . ILE B 1 114 ? -24.082 20.337  4.102   1.00 11.08 ? 139 ILE B N   1 
ATOM   2798 C CA  . ILE B 1 114 ? -24.547 21.719  4.105   1.00 18.33 ? 139 ILE B CA  1 
ATOM   2799 C C   . ILE B 1 114 ? -25.414 21.979  5.330   1.00 13.57 ? 139 ILE B C   1 
ATOM   2800 O O   . ILE B 1 114 ? -25.268 23.006  6.004   1.00 15.12 ? 139 ILE B O   1 
ATOM   2801 C CB  . ILE B 1 114 ? -25.284 22.030  2.792   1.00 17.70 ? 139 ILE B CB  1 
ATOM   2802 C CG1 . ILE B 1 114 ? -24.294 22.000  1.626   1.00 9.01  ? 139 ILE B CG1 1 
ATOM   2803 C CG2 . ILE B 1 114 ? -25.958 23.376  2.874   1.00 19.23 ? 139 ILE B CG2 1 
ATOM   2804 C CD1 . ILE B 1 114 ? -24.946 22.098  0.273   1.00 15.03 ? 139 ILE B CD1 1 
ATOM   2805 N N   . ALA B 1 115 ? -26.314 21.045  5.652   1.00 11.77 ? 140 ALA B N   1 
ATOM   2806 C CA  . ALA B 1 115 ? -27.202 21.244  6.794   1.00 19.84 ? 140 ALA B CA  1 
ATOM   2807 C C   . ALA B 1 115 ? -26.404 21.239  8.094   1.00 16.55 ? 140 ALA B C   1 
ATOM   2808 O O   . ALA B 1 115 ? -26.699 22.005  9.018   1.00 19.65 ? 140 ALA B O   1 
ATOM   2809 C CB  . ALA B 1 115 ? -28.289 20.170  6.818   1.00 15.72 ? 140 ALA B CB  1 
ATOM   2810 N N   . GLN B 1 116 ? -25.400 20.363  8.186   1.00 15.33 ? 141 GLN B N   1 
ATOM   2811 C CA  . GLN B 1 116 ? -24.527 20.355  9.354   1.00 9.69  ? 141 GLN B CA  1 
ATOM   2812 C C   . GLN B 1 116 ? -23.869 21.712  9.558   1.00 12.48 ? 141 GLN B C   1 
ATOM   2813 O O   . GLN B 1 116 ? -23.605 22.110  10.697  1.00 15.25 ? 141 GLN B O   1 
ATOM   2814 C CB  . GLN B 1 116 ? -23.473 19.255  9.192   1.00 13.08 ? 141 GLN B CB  1 
ATOM   2815 C CG  . GLN B 1 116 ? -22.326 19.274  10.201  1.00 19.39 ? 141 GLN B CG  1 
ATOM   2816 C CD  . GLN B 1 116 ? -22.787 19.187  11.644  1.00 20.59 ? 141 GLN B CD  1 
ATOM   2817 O OE1 . GLN B 1 116 ? -23.797 18.553  11.953  1.00 21.17 ? 141 GLN B OE1 1 
ATOM   2818 N NE2 . GLN B 1 116 ? -22.044 19.831  12.537  1.00 15.43 ? 141 GLN B NE2 1 
ATOM   2819 N N   . LEU B 1 117 ? -23.599 22.437  8.475   1.00 15.33 ? 142 LEU B N   1 
ATOM   2820 C CA  . LEU B 1 117 ? -22.964 23.744  8.564   1.00 15.59 ? 142 LEU B CA  1 
ATOM   2821 C C   . LEU B 1 117 ? -23.979 24.866  8.716   1.00 16.11 ? 142 LEU B C   1 
ATOM   2822 O O   . LEU B 1 117 ? -23.590 26.037  8.774   1.00 22.22 ? 142 LEU B O   1 
ATOM   2823 C CB  . LEU B 1 117 ? -22.099 23.978  7.322   1.00 13.19 ? 142 LEU B CB  1 
ATOM   2824 C CG  . LEU B 1 117 ? -20.994 22.924  7.230   1.00 15.75 ? 142 LEU B CG  1 
ATOM   2825 C CD1 . LEU B 1 117 ? -20.384 22.883  5.845   1.00 18.52 ? 142 LEU B CD1 1 
ATOM   2826 C CD2 . LEU B 1 117 ? -19.936 23.193  8.286   1.00 16.30 ? 142 LEU B CD2 1 
ATOM   2827 N N   . GLY B 1 118 ? -25.266 24.534  8.765   1.00 11.18 ? 143 GLY B N   1 
ATOM   2828 C CA  . GLY B 1 118 ? -26.303 25.521  8.944   1.00 13.75 ? 143 GLY B CA  1 
ATOM   2829 C C   . GLY B 1 118 ? -26.812 26.126  7.660   1.00 16.34 ? 143 GLY B C   1 
ATOM   2830 O O   . GLY B 1 118 ? -27.487 27.159  7.705   1.00 34.62 ? 143 GLY B O   1 
ATOM   2831 N N   . GLY B 1 119 ? -26.531 25.507  6.520   1.00 16.69 ? 144 GLY B N   1 
ATOM   2832 C CA  . GLY B 1 119 ? -26.977 26.006  5.243   1.00 19.21 ? 144 GLY B CA  1 
ATOM   2833 C C   . GLY B 1 119 ? -25.794 26.386  4.375   1.00 18.69 ? 144 GLY B C   1 
ATOM   2834 O O   . GLY B 1 119 ? -24.652 26.445  4.839   1.00 23.30 ? 144 GLY B O   1 
ATOM   2835 N N   . PRO B 1 120 ? -26.055 26.673  3.098   1.00 21.93 ? 145 PRO B N   1 
ATOM   2836 C CA  . PRO B 1 120 ? -24.966 27.049  2.177   1.00 14.39 ? 145 PRO B CA  1 
ATOM   2837 C C   . PRO B 1 120 ? -24.116 28.202  2.686   1.00 23.22 ? 145 PRO B C   1 
ATOM   2838 O O   . PRO B 1 120 ? -22.891 28.241  2.453   1.00 21.60 ? 145 PRO B O   1 
ATOM   2839 C CB  . PRO B 1 120 ? -25.721 27.424  0.896   1.00 22.06 ? 145 PRO B CB  1 
ATOM   2840 C CG  . PRO B 1 120 ? -26.968 26.605  0.952   1.00 20.43 ? 145 PRO B CG  1 
ATOM   2841 C CD  . PRO B 1 120 ? -27.356 26.580  2.413   1.00 16.66 ? 145 PRO B CD  1 
ATOM   2842 N N   . GLY B 1 121 ? -24.734 29.152  3.388   1.00 19.79 ? 146 GLY B N   1 
ATOM   2843 C CA  . GLY B 1 121 ? -23.968 30.264  3.901   1.00 20.85 ? 146 GLY B CA  1 
ATOM   2844 C C   . GLY B 1 121 ? -22.934 29.847  4.924   1.00 18.29 ? 146 GLY B C   1 
ATOM   2845 O O   . GLY B 1 121 ? -21.935 30.544  5.090   1.00 22.20 ? 146 GLY B O   1 
ATOM   2846 N N   . GLY B 1 122 ? -23.137 28.715  5.607   1.00 12.24 ? 147 GLY B N   1 
ATOM   2847 C CA  . GLY B 1 122 ? -22.099 28.223  6.499   1.00 13.07 ? 147 GLY B CA  1 
ATOM   2848 C C   . GLY B 1 122 ? -20.880 27.722  5.750   1.00 16.20 ? 147 GLY B C   1 
ATOM   2849 O O   . GLY B 1 122 ? -19.741 27.932  6.189   1.00 14.03 ? 147 GLY B O   1 
ATOM   2850 N N   . VAL B 1 123 ? -21.093 27.125  4.576   1.00 15.96 ? 148 VAL B N   1 
ATOM   2851 C CA  . VAL B 1 123 ? -19.969 26.747  3.727   1.00 20.68 ? 148 VAL B CA  1 
ATOM   2852 C C   . VAL B 1 123 ? -19.237 27.990  3.239   1.00 13.56 ? 148 VAL B C   1 
ATOM   2853 O O   . VAL B 1 123 ? -17.997 28.050  3.257   1.00 12.63 ? 148 VAL B O   1 
ATOM   2854 C CB  . VAL B 1 123 ? -20.455 25.884  2.548   1.00 20.95 ? 148 VAL B CB  1 
ATOM   2855 C CG1 . VAL B 1 123 ? -19.266 25.357  1.739   1.00 19.42 ? 148 VAL B CG1 1 
ATOM   2856 C CG2 . VAL B 1 123 ? -21.336 24.747  3.036   1.00 20.02 ? 148 VAL B CG2 1 
ATOM   2857 N N   . THR B 1 124 ? -19.992 29.006  2.801   1.00 16.84 ? 149 THR B N   1 
ATOM   2858 C CA  . THR B 1 124 ? -19.356 30.255  2.387   1.00 13.89 ? 149 THR B CA  1 
ATOM   2859 C C   . THR B 1 124 ? -18.587 30.886  3.546   1.00 18.59 ? 149 THR B C   1 
ATOM   2860 O O   . THR B 1 124 ? -17.502 31.449  3.352   1.00 16.78 ? 149 THR B O   1 
ATOM   2861 C CB  . THR B 1 124 ? -20.404 31.229  1.845   1.00 20.27 ? 149 THR B CB  1 
ATOM   2862 O OG1 . THR B 1 124 ? -21.166 30.599  0.803   1.00 14.95 ? 149 THR B OG1 1 
ATOM   2863 C CG2 . THR B 1 124 ? -19.739 32.494  1.300   1.00 9.80  ? 149 THR B CG2 1 
ATOM   2864 N N   . ALA B 1 125 ? -19.155 30.833  4.754   1.00 14.84 ? 150 ALA B N   1 
ATOM   2865 C CA  . ALA B 1 125 ? -18.484 31.399  5.916   1.00 19.31 ? 150 ALA B CA  1 
ATOM   2866 C C   . ALA B 1 125 ? -17.167 30.685  6.195   1.00 20.49 ? 150 ALA B C   1 
ATOM   2867 O O   . ALA B 1 125 ? -16.166 31.325  6.541   1.00 18.31 ? 150 ALA B O   1 
ATOM   2868 C CB  . ALA B 1 125 ? -19.408 31.320  7.130   1.00 13.86 ? 150 ALA B CB  1 
ATOM   2869 N N   . PHE B 1 126 ? -17.140 29.357  6.034   1.00 17.69 ? 151 PHE B N   1 
ATOM   2870 C CA  . PHE B 1 126 ? -15.879 28.641  6.210   1.00 19.86 ? 151 PHE B CA  1 
ATOM   2871 C C   . PHE B 1 126 ? -14.868 29.080  5.161   1.00 16.17 ? 151 PHE B C   1 
ATOM   2872 O O   . PHE B 1 126 ? -13.687 29.312  5.469   1.00 16.53 ? 151 PHE B O   1 
ATOM   2873 C CB  . PHE B 1 126 ? -16.077 27.127  6.131   1.00 15.77 ? 151 PHE B CB  1 
ATOM   2874 C CG  . PHE B 1 126 ? -14.779 26.356  6.078   1.00 16.24 ? 151 PHE B CG  1 
ATOM   2875 C CD1 . PHE B 1 126 ? -13.959 26.288  7.196   1.00 15.75 ? 151 PHE B CD1 1 
ATOM   2876 C CD2 . PHE B 1 126 ? -14.368 25.720  4.910   1.00 14.18 ? 151 PHE B CD2 1 
ATOM   2877 C CE1 . PHE B 1 126 ? -12.760 25.593  7.153   1.00 18.38 ? 151 PHE B CE1 1 
ATOM   2878 C CE2 . PHE B 1 126 ? -13.170 25.018  4.863   1.00 9.23  ? 151 PHE B CE2 1 
ATOM   2879 C CZ  . PHE B 1 126 ? -12.368 24.954  5.984   1.00 13.50 ? 151 PHE B CZ  1 
ATOM   2880 N N   . ALA B 1 127 ? -15.325 29.206  3.912   1.00 13.76 ? 152 ALA B N   1 
ATOM   2881 C CA  . ALA B 1 127 ? -14.463 29.718  2.853   1.00 22.01 ? 152 ALA B CA  1 
ATOM   2882 C C   . ALA B 1 127 ? -13.846 31.056  3.240   1.00 15.96 ? 152 ALA B C   1 
ATOM   2883 O O   . ALA B 1 127 ? -12.642 31.273  3.059   1.00 21.72 ? 152 ALA B O   1 
ATOM   2884 C CB  . ALA B 1 127 ? -15.252 29.846  1.548   1.00 13.30 ? 152 ALA B CB  1 
ATOM   2885 N N   . ARG B 1 128 ? -14.661 31.979  3.752   1.00 18.14 ? 153 ARG B N   1 
ATOM   2886 C CA  . ARG B 1 128 ? -14.114 33.271  4.160   1.00 16.01 ? 153 ARG B CA  1 
ATOM   2887 C C   . ARG B 1 128 ? -13.117 33.094  5.300   1.00 18.67 ? 153 ARG B C   1 
ATOM   2888 O O   . ARG B 1 128 ? -12.075 33.758  5.338   1.00 20.68 ? 153 ARG B O   1 
ATOM   2889 C CB  . ARG B 1 128 ? -15.240 34.220  4.568   1.00 17.12 ? 153 ARG B CB  1 
ATOM   2890 C CG  . ARG B 1 128 ? -16.195 34.517  3.425   1.00 22.78 ? 153 ARG B CG  1 
ATOM   2891 C CD  . ARG B 1 128 ? -15.552 35.296  2.290   1.00 13.52 ? 153 ARG B CD  1 
ATOM   2892 N NE  . ARG B 1 128 ? -16.528 35.516  1.231   1.00 13.30 ? 153 ARG B NE  1 
ATOM   2893 C CZ  . ARG B 1 128 ? -16.797 34.638  0.272   1.00 21.21 ? 153 ARG B CZ  1 
ATOM   2894 N NH1 . ARG B 1 128 ? -16.080 33.531  0.125   1.00 7.77  ? 153 ARG B NH1 1 
ATOM   2895 N NH2 . ARG B 1 128 ? -17.784 34.893  -0.585  1.00 11.86 ? 153 ARG B NH2 1 
ATOM   2896 N N   . ALA B 1 129 ? -13.410 32.167  6.220   1.00 20.52 ? 154 ALA B N   1 
ATOM   2897 C CA  . ALA B 1 129 ? -12.559 31.953  7.388   1.00 20.89 ? 154 ALA B CA  1 
ATOM   2898 C C   . ALA B 1 129 ? -11.181 31.437  6.995   1.00 26.22 ? 154 ALA B C   1 
ATOM   2899 O O   . ALA B 1 129 ? -10.201 31.668  7.713   1.00 20.94 ? 154 ALA B O   1 
ATOM   2900 C CB  . ALA B 1 129 ? -13.227 30.982  8.361   1.00 25.65 ? 154 ALA B CB  1 
ATOM   2901 N N   . ILE B 1 130 ? -11.083 30.726  5.873   1.00 23.89 ? 155 ILE B N   1 
ATOM   2902 C CA  . ILE B 1 130 ? -9.794  30.224  5.410   1.00 25.96 ? 155 ILE B CA  1 
ATOM   2903 C C   . ILE B 1 130 ? -9.191  31.119  4.331   1.00 22.18 ? 155 ILE B C   1 
ATOM   2904 O O   . ILE B 1 130 ? -8.232  30.721  3.664   1.00 35.56 ? 155 ILE B O   1 
ATOM   2905 C CB  . ILE B 1 130 ? -9.893  28.763  4.937   1.00 21.87 ? 155 ILE B CB  1 
ATOM   2906 C CG1 . ILE B 1 130 ? -10.784 28.646  3.698   1.00 27.78 ? 155 ILE B CG1 1 
ATOM   2907 C CG2 . ILE B 1 130 ? -10.369 27.861  6.078   1.00 11.78 ? 155 ILE B CG2 1 
ATOM   2908 C CD1 . ILE B 1 130 ? -10.637 27.327  2.980   1.00 20.00 ? 155 ILE B CD1 1 
ATOM   2909 N N   . GLY B 1 131 ? -9.736  32.316  4.140   1.00 17.58 ? 156 GLY B N   1 
ATOM   2910 C CA  . GLY B 1 131 ? -9.124  33.305  3.276   1.00 25.12 ? 156 GLY B CA  1 
ATOM   2911 C C   . GLY B 1 131 ? -9.597  33.339  1.839   1.00 27.22 ? 156 GLY B C   1 
ATOM   2912 O O   . GLY B 1 131 ? -9.005  34.067  1.032   1.00 16.68 ? 156 GLY B O   1 
ATOM   2913 N N   . ASP B 1 132 ? -10.630 32.579  1.484   1.00 21.83 ? 157 ASP B N   1 
ATOM   2914 C CA  . ASP B 1 132 ? -11.188 32.630  0.134   1.00 26.80 ? 157 ASP B CA  1 
ATOM   2915 C C   . ASP B 1 132 ? -12.291 33.684  0.116   1.00 23.21 ? 157 ASP B C   1 
ATOM   2916 O O   . ASP B 1 132 ? -13.396 33.455  0.614   1.00 21.48 ? 157 ASP B O   1 
ATOM   2917 C CB  . ASP B 1 132 ? -11.709 31.263  -0.289  1.00 19.52 ? 157 ASP B CB  1 
ATOM   2918 C CG  . ASP B 1 132 ? -12.077 31.208  -1.766  1.00 25.40 ? 157 ASP B CG  1 
ATOM   2919 O OD1 . ASP B 1 132 ? -12.468 32.250  -2.337  1.00 27.23 ? 157 ASP B OD1 1 
ATOM   2920 O OD2 . ASP B 1 132 ? -11.968 30.113  -2.361  1.00 22.49 ? 157 ASP B OD2 1 
ATOM   2921 N N   . GLU B 1 133 ? -11.998 34.839  -0.472  1.00 22.03 ? 158 GLU B N   1 
ATOM   2922 C CA  . GLU B 1 133 ? -12.973 35.917  -0.556  1.00 21.80 ? 158 GLU B CA  1 
ATOM   2923 C C   . GLU B 1 133 ? -13.949 35.747  -1.713  1.00 22.74 ? 158 GLU B C   1 
ATOM   2924 O O   . GLU B 1 133 ? -14.922 36.503  -1.797  1.00 20.66 ? 158 GLU B O   1 
ATOM   2925 C CB  . GLU B 1 133 ? -12.248 37.257  -0.698  1.00 31.95 ? 158 GLU B CB  1 
ATOM   2926 C CG  . GLU B 1 133 ? -11.834 37.876  0.626   1.00 47.22 ? 158 GLU B CG  1 
ATOM   2927 C CD  . GLU B 1 133 ? -13.016 38.443  1.390   1.00 56.06 ? 158 GLU B CD  1 
ATOM   2928 O OE1 . GLU B 1 133 ? -14.050 38.745  0.751   1.00 51.64 ? 158 GLU B OE1 1 
ATOM   2929 O OE2 . GLU B 1 133 ? -12.916 38.578  2.628   1.00 47.75 ? 158 GLU B OE2 1 
ATOM   2930 N N   . THR B 1 134 ? -13.720 34.766  -2.583  1.00 19.82 ? 159 THR B N   1 
ATOM   2931 C CA  . THR B 1 134 ? -14.384 34.647  -3.876  1.00 20.16 ? 159 THR B CA  1 
ATOM   2932 C C   . THR B 1 134 ? -15.454 33.560  -3.912  1.00 13.55 ? 159 THR B C   1 
ATOM   2933 O O   . THR B 1 134 ? -16.537 33.780  -4.462  1.00 15.29 ? 159 THR B O   1 
ATOM   2934 C CB  . THR B 1 134 ? -13.330 34.387  -4.957  1.00 18.46 ? 159 THR B CB  1 
ATOM   2935 O OG1 . THR B 1 134 ? -12.361 35.443  -4.941  1.00 21.88 ? 159 THR B OG1 1 
ATOM   2936 C CG2 . THR B 1 134 ? -13.964 34.295  -6.326  1.00 21.52 ? 159 THR B CG2 1 
ATOM   2937 N N   . PHE B 1 135 ? -15.146 32.374  -3.388  1.00 12.73 ? 160 PHE B N   1 
ATOM   2938 C CA  . PHE B 1 135 ? -16.110 31.282  -3.322  1.00 5.89  ? 160 PHE B CA  1 
ATOM   2939 C C   . PHE B 1 135 ? -17.426 31.763  -2.714  1.00 13.90 ? 160 PHE B C   1 
ATOM   2940 O O   . PHE B 1 135 ? -17.441 32.489  -1.715  1.00 11.74 ? 160 PHE B O   1 
ATOM   2941 C CB  . PHE B 1 135 ? -15.507 30.149  -2.480  1.00 11.36 ? 160 PHE B CB  1 
ATOM   2942 C CG  . PHE B 1 135 ? -16.451 28.997  -2.187  1.00 27.87 ? 160 PHE B CG  1 
ATOM   2943 C CD1 . PHE B 1 135 ? -17.412 29.085  -1.174  1.00 14.41 ? 160 PHE B CD1 1 
ATOM   2944 C CD2 . PHE B 1 135 ? -16.300 27.786  -2.849  1.00 11.17 ? 160 PHE B CD2 1 
ATOM   2945 C CE1 . PHE B 1 135 ? -18.254 28.024  -0.893  1.00 12.31 ? 160 PHE B CE1 1 
ATOM   2946 C CE2 . PHE B 1 135 ? -17.129 26.713  -2.554  1.00 13.14 ? 160 PHE B CE2 1 
ATOM   2947 C CZ  . PHE B 1 135 ? -18.111 26.833  -1.586  1.00 16.40 ? 160 PHE B CZ  1 
ATOM   2948 N N   . ARG B 1 136 ? -18.539 31.356  -3.319  1.00 12.82 ? 161 ARG B N   1 
ATOM   2949 C CA  . ARG B 1 136 ? -19.840 31.523  -2.686  1.00 12.91 ? 161 ARG B CA  1 
ATOM   2950 C C   . ARG B 1 136 ? -20.695 30.295  -2.954  1.00 15.91 ? 161 ARG B C   1 
ATOM   2951 O O   . ARG B 1 136 ? -20.797 29.842  -4.096  1.00 10.99 ? 161 ARG B O   1 
ATOM   2952 C CB  . ARG B 1 136 ? -20.585 32.782  -3.167  1.00 6.98  ? 161 ARG B CB  1 
ATOM   2953 C CG  . ARG B 1 136 ? -20.698 32.946  -4.674  1.00 11.30 ? 161 ARG B CG  1 
ATOM   2954 C CD  . ARG B 1 136 ? -21.366 34.265  -5.023  1.00 9.08  ? 161 ARG B CD  1 
ATOM   2955 N NE  . ARG B 1 136 ? -22.776 34.254  -4.641  1.00 13.81 ? 161 ARG B NE  1 
ATOM   2956 C CZ  . ARG B 1 136 ? -23.607 35.278  -4.786  1.00 21.01 ? 161 ARG B CZ  1 
ATOM   2957 N NH1 . ARG B 1 136 ? -23.213 36.416  -5.337  1.00 18.56 ? 161 ARG B NH1 1 
ATOM   2958 N NH2 . ARG B 1 136 ? -24.870 35.151  -4.386  1.00 9.95  ? 161 ARG B NH2 1 
ATOM   2959 N N   . LEU B 1 137 ? -21.287 29.750  -1.902  1.00 14.44 ? 162 LEU B N   1 
ATOM   2960 C CA  . LEU B 1 137 ? -22.329 28.744  -2.035  1.00 22.67 ? 162 LEU B CA  1 
ATOM   2961 C C   . LEU B 1 137 ? -23.651 29.375  -1.628  1.00 18.70 ? 162 LEU B C   1 
ATOM   2962 O O   . LEU B 1 137 ? -23.762 29.949  -0.540  1.00 30.32 ? 162 LEU B O   1 
ATOM   2963 C CB  . LEU B 1 137 ? -22.026 27.511  -1.179  1.00 17.32 ? 162 LEU B CB  1 
ATOM   2964 C CG  . LEU B 1 137 ? -22.738 26.222  -1.598  1.00 16.10 ? 162 LEU B CG  1 
ATOM   2965 C CD1 . LEU B 1 137 ? -22.205 25.700  -2.924  1.00 17.76 ? 162 LEU B CD1 1 
ATOM   2966 C CD2 . LEU B 1 137 ? -22.582 25.171  -0.506  1.00 14.29 ? 162 LEU B CD2 1 
ATOM   2967 N N   . ASP B 1 138 ? -24.648 29.263  -2.500  1.00 23.75 ? 163 ASP B N   1 
ATOM   2968 C CA  . ASP B 1 138 ? -25.928 29.935  -2.319  1.00 25.46 ? 163 ASP B CA  1 
ATOM   2969 C C   . ASP B 1 138 ? -27.103 28.983  -2.208  1.00 23.82 ? 163 ASP B C   1 
ATOM   2970 O O   . ASP B 1 138 ? -28.105 29.332  -1.578  1.00 20.73 ? 163 ASP B O   1 
ATOM   2971 C CB  . ASP B 1 138 ? -26.195 30.907  -3.480  1.00 14.70 ? 163 ASP B CB  1 
ATOM   2972 C CG  . ASP B 1 138 ? -25.188 32.037  -3.533  1.00 22.38 ? 163 ASP B CG  1 
ATOM   2973 O OD1 . ASP B 1 138 ? -25.423 33.074  -2.877  1.00 20.45 ? 163 ASP B OD1 1 
ATOM   2974 O OD2 . ASP B 1 138 ? -24.153 31.881  -4.215  1.00 22.68 ? 163 ASP B OD2 1 
ATOM   2975 N N   . ARG B 1 139 ? -27.009 27.795  -2.793  1.00 16.23 ? 164 ARG B N   1 
ATOM   2976 C CA  . ARG B 1 139 ? -28.140 26.892  -2.883  1.00 25.30 ? 164 ARG B CA  1 
ATOM   2977 C C   . ARG B 1 139 ? -27.685 25.499  -2.474  1.00 20.55 ? 164 ARG B C   1 
ATOM   2978 O O   . ARG B 1 139 ? -26.489 25.214  -2.379  1.00 17.98 ? 164 ARG B O   1 
ATOM   2979 C CB  . ARG B 1 139 ? -28.718 26.850  -4.312  1.00 22.00 ? 164 ARG B CB  1 
ATOM   2980 C CG  . ARG B 1 139 ? -29.446 28.116  -4.754  1.00 15.51 ? 164 ARG B CG  1 
ATOM   2981 C CD  . ARG B 1 139 ? -29.749 28.077  -6.253  1.00 17.11 ? 164 ARG B CD  1 
ATOM   2982 N NE  . ARG B 1 139 ? -28.543 28.114  -7.072  1.00 20.77 ? 164 ARG B NE  1 
ATOM   2983 C CZ  . ARG B 1 139 ? -28.526 27.947  -8.388  1.00 18.71 ? 164 ARG B CZ  1 
ATOM   2984 N NH1 . ARG B 1 139 ? -29.643 27.809  -9.082  1.00 17.61 ? 164 ARG B NH1 1 
ATOM   2985 N NH2 . ARG B 1 139 ? -27.358 27.923  -9.026  1.00 16.26 ? 164 ARG B NH2 1 
ATOM   2986 N N   . THR B 1 140 ? -28.654 24.640  -2.193  1.00 21.74 ? 165 THR B N   1 
ATOM   2987 C CA  . THR B 1 140 ? -28.386 23.240  -1.913  1.00 21.67 ? 165 THR B CA  1 
ATOM   2988 C C   . THR B 1 140 ? -28.413 22.421  -3.206  1.00 16.93 ? 165 THR B C   1 
ATOM   2989 O O   . THR B 1 140 ? -28.686 22.938  -4.292  1.00 18.33 ? 165 THR B O   1 
ATOM   2990 C CB  . THR B 1 140 ? -29.409 22.711  -0.913  1.00 19.18 ? 165 THR B CB  1 
ATOM   2991 O OG1 . THR B 1 140 ? -30.724 22.858  -1.461  1.00 18.55 ? 165 THR B OG1 1 
ATOM   2992 C CG2 . THR B 1 140 ? -29.337 23.515  0.374   1.00 17.32 ? 165 THR B CG2 1 
ATOM   2993 N N   . GLU B 1 141 ? -28.109 21.105  -3.089  1.00 11.57 ? 166 GLU B N   1 
ATOM   2994 C CA  . GLU B 1 141 ? -28.343 20.177  -4.195  1.00 16.13 ? 166 GLU B CA  1 
ATOM   2995 C C   . GLU B 1 141 ? -29.834 19.864  -4.316  1.00 16.80 ? 166 GLU B C   1 
ATOM   2996 O O   . GLU B 1 141 ? -30.516 19.679  -3.304  1.00 22.44 ? 166 GLU B O   1 
ATOM   2997 C CB  . GLU B 1 141 ? -27.539 18.880  -4.047  1.00 22.91 ? 166 GLU B CB  1 
ATOM   2998 C CG  . GLU B 1 141 ? -26.023 19.042  -4.037  1.00 23.63 ? 166 GLU B CG  1 
ATOM   2999 C CD  . GLU B 1 141 ? -25.492 19.340  -5.445  1.00 36.63 ? 166 GLU B CD  1 
ATOM   3000 O OE1 . GLU B 1 141 ? -26.313 19.411  -6.390  1.00 36.64 ? 166 GLU B OE1 1 
ATOM   3001 O OE2 . GLU B 1 141 ? -24.258 19.462  -5.624  1.00 34.92 ? 166 GLU B OE2 1 
ATOM   3002 N N   . PRO B 1 142 ? -30.354 19.774  -5.545  1.00 12.61 ? 167 PRO B N   1 
ATOM   3003 C CA  . PRO B 1 142 ? -29.602 19.836  -6.805  1.00 20.94 ? 167 PRO B CA  1 
ATOM   3004 C C   . PRO B 1 142 ? -29.567 21.180  -7.515  1.00 14.90 ? 167 PRO B C   1 
ATOM   3005 O O   . PRO B 1 142 ? -28.900 21.279  -8.544  1.00 20.31 ? 167 PRO B O   1 
ATOM   3006 C CB  . PRO B 1 142 ? -30.335 18.805  -7.670  1.00 21.78 ? 167 PRO B CB  1 
ATOM   3007 C CG  . PRO B 1 142 ? -31.774 18.929  -7.230  1.00 16.62 ? 167 PRO B CG  1 
ATOM   3008 C CD  . PRO B 1 142 ? -31.737 19.312  -5.758  1.00 21.01 ? 167 PRO B CD  1 
ATOM   3009 N N   . THR B 1 143 ? -30.226 22.230  -7.022  1.00 9.60  ? 168 THR B N   1 
ATOM   3010 C CA  . THR B 1 143 ? -30.299 23.451  -7.816  1.00 13.52 ? 168 THR B CA  1 
ATOM   3011 C C   . THR B 1 143 ? -28.973 24.201  -7.889  1.00 18.53 ? 168 THR B C   1 
ATOM   3012 O O   . THR B 1 143 ? -28.834 25.074  -8.748  1.00 19.93 ? 168 THR B O   1 
ATOM   3013 C CB  . THR B 1 143 ? -31.379 24.400  -7.283  1.00 9.27  ? 168 THR B CB  1 
ATOM   3014 O OG1 . THR B 1 143 ? -31.055 24.807  -5.947  1.00 14.95 ? 168 THR B OG1 1 
ATOM   3015 C CG2 . THR B 1 143 ? -32.760 23.732  -7.314  1.00 12.85 ? 168 THR B CG2 1 
ATOM   3016 N N   . LEU B 1 144 ? -27.985 23.874  -7.047  1.00 16.23 ? 169 LEU B N   1 
ATOM   3017 C CA  . LEU B 1 144 ? -26.704 24.561  -7.173  1.00 18.82 ? 169 LEU B CA  1 
ATOM   3018 C C   . LEU B 1 144 ? -25.968 24.211  -8.463  1.00 27.21 ? 169 LEU B C   1 
ATOM   3019 O O   . LEU B 1 144 ? -24.937 24.827  -8.756  1.00 20.07 ? 169 LEU B O   1 
ATOM   3020 C CB  . LEU B 1 144 ? -25.810 24.244  -5.971  1.00 19.26 ? 169 LEU B CB  1 
ATOM   3021 C CG  . LEU B 1 144 ? -25.336 22.810  -5.706  1.00 25.30 ? 169 LEU B CG  1 
ATOM   3022 C CD1 . LEU B 1 144 ? -24.068 22.495  -6.486  1.00 18.54 ? 169 LEU B CD1 1 
ATOM   3023 C CD2 . LEU B 1 144 ? -25.101 22.580  -4.221  1.00 27.52 ? 169 LEU B CD2 1 
ATOM   3024 N N   . ASN B 1 145 ? -26.471 23.253  -9.239  1.00 23.60 ? 170 ASN B N   1 
ATOM   3025 C CA  . ASN B 1 145 ? -25.854 22.831  -10.486 1.00 21.24 ? 170 ASN B CA  1 
ATOM   3026 C C   . ASN B 1 145 ? -26.507 23.449  -11.713 1.00 25.92 ? 170 ASN B C   1 
ATOM   3027 O O   . ASN B 1 145 ? -26.281 22.961  -12.826 1.00 20.77 ? 170 ASN B O   1 
ATOM   3028 C CB  . ASN B 1 145 ? -25.859 21.304  -10.600 1.00 16.79 ? 170 ASN B CB  1 
ATOM   3029 C CG  . ASN B 1 145 ? -25.240 20.633  -9.392  1.00 19.88 ? 170 ASN B CG  1 
ATOM   3030 O OD1 . ASN B 1 145 ? -24.026 20.679  -9.205  1.00 23.59 ? 170 ASN B OD1 1 
ATOM   3031 N ND2 . ASN B 1 145 ? -26.068 20.006  -8.567  1.00 22.31 ? 170 ASN B ND2 1 
ATOM   3032 N N   . THR B 1 146 ? -27.333 24.489  -11.545 1.00 18.81 ? 171 THR B N   1 
ATOM   3033 C CA  . THR B 1 146 ? -28.038 25.018  -12.707 1.00 19.72 ? 171 THR B CA  1 
ATOM   3034 C C   . THR B 1 146 ? -27.057 25.679  -13.664 1.00 13.62 ? 171 THR B C   1 
ATOM   3035 O O   . THR B 1 146 ? -27.301 25.712  -14.874 1.00 14.18 ? 171 THR B O   1 
ATOM   3036 C CB  . THR B 1 146 ? -29.124 26.010  -12.285 1.00 23.67 ? 171 THR B CB  1 
ATOM   3037 O OG1 . THR B 1 146 ? -28.571 26.979  -11.382 1.00 14.37 ? 171 THR B OG1 1 
ATOM   3038 C CG2 . THR B 1 146 ? -30.291 25.274  -11.612 1.00 16.42 ? 171 THR B CG2 1 
ATOM   3039 N N   . ALA B 1 147 ? -25.948 26.199  -13.132 1.00 14.97 ? 172 ALA B N   1 
ATOM   3040 C CA  . ALA B 1 147 ? -24.804 26.630  -13.931 1.00 13.85 ? 172 ALA B CA  1 
ATOM   3041 C C   . ALA B 1 147 ? -25.198 27.629  -15.016 1.00 21.38 ? 172 ALA B C   1 
ATOM   3042 O O   . ALA B 1 147 ? -24.703 27.580  -16.144 1.00 15.95 ? 172 ALA B O   1 
ATOM   3043 C CB  . ALA B 1 147 ? -24.102 25.415  -14.533 1.00 12.00 ? 172 ALA B CB  1 
ATOM   3044 N N   . ILE B 1 148 ? -26.078 28.557  -14.673 1.00 13.43 ? 173 ILE B N   1 
ATOM   3045 C CA  . ILE B 1 148 ? -26.569 29.495  -15.687 1.00 14.34 ? 173 ILE B CA  1 
ATOM   3046 C C   . ILE B 1 148 ? -25.490 30.530  -15.986 1.00 19.86 ? 173 ILE B C   1 
ATOM   3047 O O   . ILE B 1 148 ? -24.876 31.074  -15.049 1.00 17.71 ? 173 ILE B O   1 
ATOM   3048 C CB  . ILE B 1 148 ? -27.865 30.163  -15.217 1.00 18.71 ? 173 ILE B CB  1 
ATOM   3049 C CG1 . ILE B 1 148 ? -28.888 29.105  -14.778 1.00 20.03 ? 173 ILE B CG1 1 
ATOM   3050 C CG2 . ILE B 1 148 ? -28.418 31.106  -16.275 1.00 24.76 ? 173 ILE B CG2 1 
ATOM   3051 C CD1 . ILE B 1 148 ? -30.062 29.670  -13.988 1.00 25.68 ? 173 ILE B CD1 1 
ATOM   3052 N N   . PRO B 1 149 ? -25.191 30.788  -17.260 1.00 28.88 ? 174 PRO B N   1 
ATOM   3053 C CA  . PRO B 1 149 ? -24.197 31.813  -17.606 1.00 17.42 ? 174 PRO B CA  1 
ATOM   3054 C C   . PRO B 1 149 ? -24.588 33.158  -17.016 1.00 16.77 ? 174 PRO B C   1 
ATOM   3055 O O   . PRO B 1 149 ? -25.736 33.593  -17.131 1.00 13.92 ? 174 PRO B O   1 
ATOM   3056 C CB  . PRO B 1 149 ? -24.245 31.844  -19.136 1.00 13.72 ? 174 PRO B CB  1 
ATOM   3057 C CG  . PRO B 1 149 ? -24.687 30.466  -19.515 1.00 17.82 ? 174 PRO B CG  1 
ATOM   3058 C CD  . PRO B 1 149 ? -25.686 30.079  -18.453 1.00 26.85 ? 174 PRO B CD  1 
ATOM   3059 N N   . GLY B 1 150 ? -23.634 33.800  -16.353 1.00 12.78 ? 175 GLY B N   1 
ATOM   3060 C CA  . GLY B 1 150 ? -23.878 35.083  -15.747 1.00 21.99 ? 175 GLY B CA  1 
ATOM   3061 C C   . GLY B 1 150 ? -24.409 35.010  -14.336 1.00 20.93 ? 175 GLY B C   1 
ATOM   3062 O O   . GLY B 1 150 ? -24.448 36.040  -13.650 1.00 13.89 ? 175 GLY B O   1 
ATOM   3063 N N   . ASP B 1 151 ? -24.783 33.827  -13.873 1.00 15.82 ? 176 ASP B N   1 
ATOM   3064 C CA  . ASP B 1 151 ? -25.362 33.687  -12.552 1.00 21.02 ? 176 ASP B CA  1 
ATOM   3065 C C   . ASP B 1 151 ? -24.212 33.559  -11.567 1.00 14.58 ? 176 ASP B C   1 
ATOM   3066 O O   . ASP B 1 151 ? -23.441 32.598  -11.655 1.00 18.42 ? 176 ASP B O   1 
ATOM   3067 C CB  . ASP B 1 151 ? -26.270 32.457  -12.493 1.00 15.97 ? 176 ASP B CB  1 
ATOM   3068 C CG  . ASP B 1 151 ? -27.110 32.392  -11.224 1.00 22.88 ? 176 ASP B CG  1 
ATOM   3069 O OD1 . ASP B 1 151 ? -26.847 33.170  -10.280 1.00 26.43 ? 176 ASP B OD1 1 
ATOM   3070 O OD2 . ASP B 1 151 ? -28.030 31.545  -11.169 1.00 26.90 ? 176 ASP B OD2 1 
ATOM   3071 N N   . PRO B 1 152 ? -24.078 34.469  -10.600 1.00 17.98 ? 177 PRO B N   1 
ATOM   3072 C CA  . PRO B 1 152 ? -22.947 34.371  -9.673  1.00 19.96 ? 177 PRO B CA  1 
ATOM   3073 C C   . PRO B 1 152 ? -23.188 33.372  -8.566  1.00 15.44 ? 177 PRO B C   1 
ATOM   3074 O O   . PRO B 1 152 ? -22.245 33.061  -7.828  1.00 15.82 ? 177 PRO B O   1 
ATOM   3075 C CB  . PRO B 1 152 ? -22.832 35.794  -9.103  1.00 16.15 ? 177 PRO B CB  1 
ATOM   3076 C CG  . PRO B 1 152 ? -24.204 36.375  -9.238  1.00 19.39 ? 177 PRO B CG  1 
ATOM   3077 C CD  . PRO B 1 152 ? -24.907 35.665  -10.367 1.00 14.77 ? 177 PRO B CD  1 
ATOM   3078 N N   . ARG B 1 153 ? -24.409 32.860  -8.424  1.00 14.14 ? 178 ARG B N   1 
ATOM   3079 C CA  . ARG B 1 153 ? -24.678 31.930  -7.340  1.00 16.87 ? 178 ARG B CA  1 
ATOM   3080 C C   . ARG B 1 153 ? -23.846 30.668  -7.535  1.00 9.87  ? 178 ARG B C   1 
ATOM   3081 O O   . ARG B 1 153 ? -23.698 30.178  -8.657  1.00 14.79 ? 178 ARG B O   1 
ATOM   3082 C CB  . ARG B 1 153 ? -26.159 31.559  -7.292  1.00 15.69 ? 178 ARG B CB  1 
ATOM   3083 C CG  . ARG B 1 153 ? -27.079 32.636  -6.759  1.00 8.11  ? 178 ARG B CG  1 
ATOM   3084 C CD  . ARG B 1 153 ? -28.516 32.173  -6.912  1.00 9.44  ? 178 ARG B CD  1 
ATOM   3085 N NE  . ARG B 1 153 ? -28.853 31.883  -8.298  1.00 8.90  ? 178 ARG B NE  1 
ATOM   3086 C CZ  . ARG B 1 153 ? -30.013 31.380  -8.697  1.00 21.99 ? 178 ARG B CZ  1 
ATOM   3087 N NH1 . ARG B 1 153 ? -30.984 31.112  -7.837  1.00 22.20 ? 178 ARG B NH1 1 
ATOM   3088 N NH2 . ARG B 1 153 ? -30.196 31.118  -9.989  1.00 10.82 ? 178 ARG B NH2 1 
ATOM   3089 N N   . ASP B 1 154 ? -23.319 30.132  -6.434  1.00 13.47 ? 179 ASP B N   1 
ATOM   3090 C CA  . ASP B 1 154 ? -22.612 28.847  -6.432  1.00 21.33 ? 179 ASP B CA  1 
ATOM   3091 C C   . ASP B 1 154 ? -21.449 28.838  -7.424  1.00 16.38 ? 179 ASP B C   1 
ATOM   3092 O O   . ASP B 1 154 ? -21.247 27.869  -8.157  1.00 18.11 ? 179 ASP B O   1 
ATOM   3093 C CB  . ASP B 1 154 ? -23.596 27.721  -6.752  1.00 17.02 ? 179 ASP B CB  1 
ATOM   3094 C CG  . ASP B 1 154 ? -24.880 27.842  -5.963  1.00 26.44 ? 179 ASP B CG  1 
ATOM   3095 O OD1 . ASP B 1 154 ? -24.829 27.762  -4.720  1.00 26.91 ? 179 ASP B OD1 1 
ATOM   3096 O OD2 . ASP B 1 154 ? -25.937 28.099  -6.586  1.00 27.11 ? 179 ASP B OD2 1 
ATOM   3097 N N   . THR B 1 155 ? -20.661 29.911  -7.437  1.00 9.97  ? 180 THR B N   1 
ATOM   3098 C CA  . THR B 1 155 ? -19.528 30.031  -8.345  1.00 16.84 ? 180 THR B CA  1 
ATOM   3099 C C   . THR B 1 155 ? -18.253 30.341  -7.579  1.00 10.91 ? 180 THR B C   1 
ATOM   3100 O O   . THR B 1 155 ? -18.280 30.745  -6.414  1.00 11.32 ? 180 THR B O   1 
ATOM   3101 C CB  . THR B 1 155 ? -19.743 31.108  -9.427  1.00 11.65 ? 180 THR B CB  1 
ATOM   3102 O OG1 . THR B 1 155 ? -19.914 32.392  -8.814  1.00 12.67 ? 180 THR B OG1 1 
ATOM   3103 C CG2 . THR B 1 155 ? -20.935 30.767  -10.310 1.00 13.64 ? 180 THR B CG2 1 
ATOM   3104 N N   . THR B 1 156 ? -17.130 30.120  -8.254  1.00 10.50 ? 181 THR B N   1 
ATOM   3105 C CA  . THR B 1 156 ? -15.862 30.694  -7.815  1.00 13.12 ? 181 THR B CA  1 
ATOM   3106 C C   . THR B 1 156 ? -14.993 30.979  -9.033  1.00 12.05 ? 181 THR B C   1 
ATOM   3107 O O   . THR B 1 156 ? -15.380 30.712  -10.170 1.00 13.68 ? 181 THR B O   1 
ATOM   3108 C CB  . THR B 1 156 ? -15.140 29.744  -6.848  1.00 15.13 ? 181 THR B CB  1 
ATOM   3109 O OG1 . THR B 1 156 ? -14.069 30.434  -6.191  1.00 18.51 ? 181 THR B OG1 1 
ATOM   3110 C CG2 . THR B 1 156 ? -14.582 28.557  -7.604  1.00 8.45  ? 181 THR B CG2 1 
ATOM   3111 N N   . THR B 1 157 ? -13.802 31.505  -8.790  1.00 12.88 ? 182 THR B N   1 
ATOM   3112 C CA  . THR B 1 157 ? -12.862 31.672  -9.886  1.00 13.66 ? 182 THR B CA  1 
ATOM   3113 C C   . THR B 1 157 ? -11.831 30.561  -9.825  1.00 8.70  ? 182 THR B C   1 
ATOM   3114 O O   . THR B 1 157 ? -11.618 29.956  -8.771  1.00 11.46 ? 182 THR B O   1 
ATOM   3115 C CB  . THR B 1 157 ? -12.149 33.035  -9.819  1.00 17.66 ? 182 THR B CB  1 
ATOM   3116 O OG1 . THR B 1 157 ? -11.266 33.075  -8.691  1.00 12.94 ? 182 THR B OG1 1 
ATOM   3117 C CG2 . THR B 1 157 ? -13.154 34.192  -9.742  1.00 17.88 ? 182 THR B CG2 1 
ATOM   3118 N N   . PRO B 1 158 ? -11.192 30.232  -10.946 1.00 15.59 ? 183 PRO B N   1 
ATOM   3119 C CA  . PRO B 1 158 ? -10.129 29.217  -10.883 1.00 10.45 ? 183 PRO B CA  1 
ATOM   3120 C C   . PRO B 1 158 ? -9.017  29.566  -9.910  1.00 14.29 ? 183 PRO B C   1 
ATOM   3121 O O   . PRO B 1 158 ? -8.568  28.686  -9.164  1.00 12.87 ? 183 PRO B O   1 
ATOM   3122 C CB  . PRO B 1 158 ? -9.632  29.148  -12.335 1.00 13.88 ? 183 PRO B CB  1 
ATOM   3123 C CG  . PRO B 1 158 ? -10.804 29.588  -13.147 1.00 18.66 ? 183 PRO B CG  1 
ATOM   3124 C CD  . PRO B 1 158 ? -11.487 30.644  -12.330 1.00 17.71 ? 183 PRO B CD  1 
ATOM   3125 N N   . ARG B 1 159 ? -8.562  30.825  -9.888  1.00 16.07 ? 184 ARG B N   1 
ATOM   3126 C CA  . ARG B 1 159 ? -7.458  31.197  -9.004  1.00 11.89 ? 184 ARG B CA  1 
ATOM   3127 C C   . ARG B 1 159 ? -7.834  31.009  -7.542  1.00 15.70 ? 184 ARG B C   1 
ATOM   3128 O O   . ARG B 1 159 ? -7.041  30.487  -6.746  1.00 11.59 ? 184 ARG B O   1 
ATOM   3129 C CB  . ARG B 1 159 ? -7.043  32.647  -9.243  1.00 23.51 ? 184 ARG B CB  1 
ATOM   3130 C CG  . ARG B 1 159 ? -6.016  33.159  -8.229  1.00 31.74 ? 184 ARG B CG  1 
ATOM   3131 C CD  . ARG B 1 159 ? -6.130  34.665  -8.004  1.00 30.87 ? 184 ARG B CD  1 
ATOM   3132 N NE  . ARG B 1 159 ? -5.882  35.415  -9.228  1.00 26.75 ? 184 ARG B NE  1 
ATOM   3133 C CZ  . ARG B 1 159 ? -4.676  35.669  -9.717  1.00 32.25 ? 184 ARG B CZ  1 
ATOM   3134 N NH1 . ARG B 1 159 ? -3.580  35.245  -9.107  1.00 32.78 ? 184 ARG B NH1 1 
ATOM   3135 N NH2 . ARG B 1 159 ? -4.567  36.367  -10.843 1.00 26.16 ? 184 ARG B NH2 1 
ATOM   3136 N N   . ALA B 1 160 ? -9.036  31.451  -7.168  1.00 16.22 ? 185 ALA B N   1 
ATOM   3137 C CA  . ALA B 1 160 ? -9.470  31.323  -5.784  1.00 14.95 ? 185 ALA B CA  1 
ATOM   3138 C C   . ALA B 1 160 ? -9.588  29.862  -5.382  1.00 20.84 ? 185 ALA B C   1 
ATOM   3139 O O   . ALA B 1 160 ? -9.148  29.476  -4.294  1.00 20.14 ? 185 ALA B O   1 
ATOM   3140 C CB  . ALA B 1 160 ? -10.799 32.042  -5.585  1.00 12.79 ? 185 ALA B CB  1 
ATOM   3141 N N   . MET B 1 161 ? -10.179 29.033  -6.244  1.00 12.69 ? 186 MET B N   1 
ATOM   3142 C CA  . MET B 1 161 ? -10.329 27.627  -5.892  1.00 19.15 ? 186 MET B CA  1 
ATOM   3143 C C   . MET B 1 161 ? -8.980  26.930  -5.804  1.00 15.30 ? 186 MET B C   1 
ATOM   3144 O O   . MET B 1 161 ? -8.785  26.067  -4.944  1.00 15.79 ? 186 MET B O   1 
ATOM   3145 C CB  . MET B 1 161 ? -11.251 26.910  -6.877  1.00 18.08 ? 186 MET B CB  1 
ATOM   3146 C CG  . MET B 1 161 ? -11.492 25.460  -6.478  1.00 20.34 ? 186 MET B CG  1 
ATOM   3147 S SD  . MET B 1 161 ? -12.442 25.267  -4.952  1.00 26.70 ? 186 MET B SD  1 
ATOM   3148 C CE  . MET B 1 161 ? -14.063 25.829  -5.448  1.00 40.35 ? 186 MET B CE  1 
ATOM   3149 N N   . ALA B 1 162 ? -8.028  27.300  -6.663  1.00 15.53 ? 187 ALA B N   1 
ATOM   3150 C CA  . ALA B 1 162 ? -6.698  26.706  -6.571  1.00 16.31 ? 187 ALA B CA  1 
ATOM   3151 C C   . ALA B 1 162 ? -6.019  27.101  -5.267  1.00 10.74 ? 187 ALA B C   1 
ATOM   3152 O O   . ALA B 1 162 ? -5.491  26.244  -4.547  1.00 21.61 ? 187 ALA B O   1 
ATOM   3153 C CB  . ALA B 1 162 ? -5.849  27.112  -7.776  1.00 8.97  ? 187 ALA B CB  1 
ATOM   3154 N N   . GLN B 1 163 ? -6.029  28.398  -4.946  1.00 9.47  ? 188 GLN B N   1 
ATOM   3155 C CA  . GLN B 1 163 ? -5.467  28.851  -3.679  1.00 13.73 ? 188 GLN B CA  1 
ATOM   3156 C C   . GLN B 1 163 ? -6.105  28.130  -2.497  1.00 18.99 ? 188 GLN B C   1 
ATOM   3157 O O   . GLN B 1 163 ? -5.402  27.651  -1.594  1.00 17.21 ? 188 GLN B O   1 
ATOM   3158 C CB  . GLN B 1 163 ? -5.643  30.362  -3.539  1.00 17.99 ? 188 GLN B CB  1 
ATOM   3159 C CG  . GLN B 1 163 ? -4.845  30.963  -2.394  1.00 30.25 ? 188 GLN B CG  1 
ATOM   3160 C CD  . GLN B 1 163 ? -3.362  30.666  -2.513  1.00 49.02 ? 188 GLN B CD  1 
ATOM   3161 O OE1 . GLN B 1 163 ? -2.711  30.295  -1.534  1.00 38.88 ? 188 GLN B OE1 1 
ATOM   3162 N NE2 . GLN B 1 163 ? -2.820  30.822  -3.721  1.00 32.03 ? 188 GLN B NE2 1 
ATOM   3163 N N   . THR B 1 164 ? -7.436  28.011  -2.501  1.00 11.16 ? 189 THR B N   1 
ATOM   3164 C CA  . THR B 1 164 ? -8.117  27.400  -1.367  1.00 17.84 ? 189 THR B CA  1 
ATOM   3165 C C   . THR B 1 164 ? -7.822  25.907  -1.273  1.00 15.47 ? 189 THR B C   1 
ATOM   3166 O O   . THR B 1 164 ? -7.588  25.386  -0.175  1.00 16.65 ? 189 THR B O   1 
ATOM   3167 C CB  . THR B 1 164 ? -9.624  27.620  -1.490  1.00 18.03 ? 189 THR B CB  1 
ATOM   3168 O OG1 . THR B 1 164 ? -9.935  28.996  -1.254  1.00 14.26 ? 189 THR B OG1 1 
ATOM   3169 C CG2 . THR B 1 164 ? -10.352 26.758  -0.493  1.00 20.58 ? 189 THR B CG2 1 
ATOM   3170 N N   . LEU B 1 165 ? -7.808  25.205  -2.409  1.00 10.07 ? 190 LEU B N   1 
ATOM   3171 C CA  . LEU B 1 165 ? -7.548  23.774  -2.369  1.00 14.68 ? 190 LEU B CA  1 
ATOM   3172 C C   . LEU B 1 165 ? -6.137  23.510  -1.877  1.00 13.25 ? 190 LEU B C   1 
ATOM   3173 O O   . LEU B 1 165 ? -5.896  22.551  -1.132  1.00 14.47 ? 190 LEU B O   1 
ATOM   3174 C CB  . LEU B 1 165 ? -7.754  23.156  -3.750  1.00 23.26 ? 190 LEU B CB  1 
ATOM   3175 C CG  . LEU B 1 165 ? -7.696  21.623  -3.761  1.00 20.03 ? 190 LEU B CG  1 
ATOM   3176 C CD1 . LEU B 1 165 ? -8.796  21.034  -2.887  1.00 20.46 ? 190 LEU B CD1 1 
ATOM   3177 C CD2 . LEU B 1 165 ? -7.765  21.074  -5.177  1.00 27.15 ? 190 LEU B CD2 1 
ATOM   3178 N N   . ARG B 1 166 ? -5.194  24.372  -2.266  1.00 14.97 ? 191 ARG B N   1 
ATOM   3179 C CA  . ARG B 1 166 ? -3.838  24.255  -1.746  1.00 18.18 ? 191 ARG B CA  1 
ATOM   3180 C C   . ARG B 1 166 ? -3.825  24.446  -0.239  1.00 14.05 ? 191 ARG B C   1 
ATOM   3181 O O   . ARG B 1 166 ? -3.219  23.655  0.494   1.00 20.52 ? 191 ARG B O   1 
ATOM   3182 C CB  . ARG B 1 166 ? -2.903  25.277  -2.390  1.00 14.98 ? 191 ARG B CB  1 
ATOM   3183 C CG  . ARG B 1 166 ? -1.499  25.171  -1.790  1.00 17.24 ? 191 ARG B CG  1 
ATOM   3184 C CD  . ARG B 1 166 ? -0.657  26.401  -2.018  1.00 21.54 ? 191 ARG B CD  1 
ATOM   3185 N NE  . ARG B 1 166 ? 0.733   26.171  -1.647  1.00 21.04 ? 191 ARG B NE  1 
ATOM   3186 C CZ  . ARG B 1 166 ? 1.763   26.827  -2.160  1.00 20.31 ? 191 ARG B CZ  1 
ATOM   3187 N NH1 . ARG B 1 166 ? 1.592   27.807  -3.031  1.00 29.82 ? 191 ARG B NH1 1 
ATOM   3188 N NH2 . ARG B 1 166 ? 2.994   26.517  -1.762  1.00 27.30 ? 191 ARG B NH2 1 
ATOM   3189 N N   . GLN B 1 167 ? -4.511  25.488  0.242   1.00 17.27 ? 192 GLN B N   1 
ATOM   3190 C CA  . GLN B 1 167 ? -4.518  25.762  1.674   1.00 18.63 ? 192 GLN B CA  1 
ATOM   3191 C C   . GLN B 1 167 ? -5.108  24.582  2.442   1.00 13.59 ? 192 GLN B C   1 
ATOM   3192 O O   . GLN B 1 167 ? -4.611  24.216  3.513   1.00 19.64 ? 192 GLN B O   1 
ATOM   3193 C CB  . GLN B 1 167 ? -5.324  27.035  1.943   1.00 16.32 ? 192 GLN B CB  1 
ATOM   3194 C CG  . GLN B 1 167 ? -4.682  28.312  1.375   1.00 40.77 ? 192 GLN B CG  1 
ATOM   3195 C CD  . GLN B 1 167 ? -3.616  28.940  2.245   1.00 66.07 ? 192 GLN B CD  1 
ATOM   3196 O OE1 . GLN B 1 167 ? -2.440  28.574  2.163   1.00 37.02 ? 192 GLN B OE1 1 
ATOM   3197 N NE2 . GLN B 1 167 ? -4.009  29.916  3.059   1.00 51.77 ? 192 GLN B NE2 1 
ATOM   3198 N N   . LEU B 1 168 ? -6.131  23.941  1.875   1.00 12.46 ? 193 LEU B N   1 
ATOM   3199 C CA  . LEU B 1 168 ? -6.843  22.855  2.547   1.00 16.55 ? 193 LEU B CA  1 
ATOM   3200 C C   . LEU B 1 168 ? -6.030  21.563  2.547   1.00 17.86 ? 193 LEU B C   1 
ATOM   3201 O O   . LEU B 1 168 ? -6.000  20.844  3.552   1.00 12.25 ? 193 LEU B O   1 
ATOM   3202 C CB  . LEU B 1 168 ? -8.205  22.613  1.893   1.00 10.91 ? 193 LEU B CB  1 
ATOM   3203 C CG  . LEU B 1 168 ? -9.268  23.691  2.105   1.00 15.78 ? 193 LEU B CG  1 
ATOM   3204 C CD1 . LEU B 1 168 ? -10.510 23.385  1.279   1.00 14.75 ? 193 LEU B CD1 1 
ATOM   3205 C CD2 . LEU B 1 168 ? -9.619  23.810  3.579   1.00 16.09 ? 193 LEU B CD2 1 
ATOM   3206 N N   . THR B 1 169 ? -5.383  21.246  1.427   1.00 11.74 ? 194 THR B N   1 
ATOM   3207 C CA  . THR B 1 169 ? -4.742  19.949  1.243   1.00 17.24 ? 194 THR B CA  1 
ATOM   3208 C C   . THR B 1 169 ? -3.243  19.967  1.507   1.00 17.93 ? 194 THR B C   1 
ATOM   3209 O O   . THR B 1 169 ? -2.681  18.937  1.891   1.00 20.01 ? 194 THR B O   1 
ATOM   3210 C CB  . THR B 1 169 ? -4.984  19.449  -0.185  1.00 13.33 ? 194 THR B CB  1 
ATOM   3211 O OG1 . THR B 1 169 ? -4.441  20.395  -1.116  1.00 11.46 ? 194 THR B OG1 1 
ATOM   3212 C CG2 . THR B 1 169 ? -6.473  19.308  -0.451  1.00 11.77 ? 194 THR B CG2 1 
ATOM   3213 N N   . LEU B 1 170 ? -2.578  21.106  1.317   1.00 22.12 ? 195 LEU B N   1 
ATOM   3214 C CA  . LEU B 1 170 ? -1.136  21.190  1.484   1.00 21.53 ? 195 LEU B CA  1 
ATOM   3215 C C   . LEU B 1 170 ? -0.701  22.181  2.549   1.00 21.62 ? 195 LEU B C   1 
ATOM   3216 O O   . LEU B 1 170 ? 0.426   22.069  3.045   1.00 23.08 ? 195 LEU B O   1 
ATOM   3217 C CB  . LEU B 1 170 ? -0.465  21.574  0.157   1.00 3.84  ? 195 LEU B CB  1 
ATOM   3218 C CG  . LEU B 1 170 ? -0.793  20.660  -1.021  1.00 25.57 ? 195 LEU B CG  1 
ATOM   3219 C CD1 . LEU B 1 170 ? -0.277  21.260  -2.317  1.00 14.44 ? 195 LEU B CD1 1 
ATOM   3220 C CD2 . LEU B 1 170 ? -0.214  19.272  -0.799  1.00 13.53 ? 195 LEU B CD2 1 
ATOM   3221 N N   . GLY B 1 171 ? -1.548  23.129  2.916   1.00 11.47 ? 196 GLY B N   1 
ATOM   3222 C CA  . GLY B 1 171 ? -1.249  24.137  3.906   1.00 16.55 ? 196 GLY B CA  1 
ATOM   3223 C C   . GLY B 1 171 ? -1.861  23.797  5.246   1.00 17.87 ? 196 GLY B C   1 
ATOM   3224 O O   . GLY B 1 171 ? -1.950  22.627  5.639   1.00 17.49 ? 196 GLY B O   1 
ATOM   3225 N N   . HIS B 1 172 ? -2.286  24.832  5.964   1.00 21.20 ? 197 HIS B N   1 
ATOM   3226 C CA  . HIS B 1 172 ? -2.669  24.711  7.364   1.00 25.62 ? 197 HIS B CA  1 
ATOM   3227 C C   . HIS B 1 172 ? -4.041  25.320  7.602   1.00 20.19 ? 197 HIS B C   1 
ATOM   3228 O O   . HIS B 1 172 ? -4.314  25.868  8.675   1.00 23.29 ? 197 HIS B O   1 
ATOM   3229 C CB  . HIS B 1 172 ? -1.612  25.314  8.291   1.00 30.39 ? 197 HIS B CB  1 
ATOM   3230 C CG  . HIS B 1 172 ? -0.249  24.726  8.097   1.00 41.03 ? 197 HIS B CG  1 
ATOM   3231 N ND1 . HIS B 1 172 ? 0.738   25.344  7.359   1.00 36.87 ? 197 HIS B ND1 1 
ATOM   3232 C CD2 . HIS B 1 172 ? 0.283   23.558  8.533   1.00 30.70 ? 197 HIS B CD2 1 
ATOM   3233 C CE1 . HIS B 1 172 ? 1.820   24.585  7.354   1.00 42.91 ? 197 HIS B CE1 1 
ATOM   3234 N NE2 . HIS B 1 172 ? 1.571   23.497  8.061   1.00 42.35 ? 197 HIS B NE2 1 
ATOM   3235 N N   . ALA B 1 173 ? -4.906  25.253  6.586   1.00 18.09 ? 198 ALA B N   1 
ATOM   3236 C CA  . ALA B 1 173 ? -6.294  25.643  6.786   1.00 18.15 ? 198 ALA B CA  1 
ATOM   3237 C C   . ALA B 1 173 ? -6.984  24.665  7.723   1.00 14.23 ? 198 ALA B C   1 
ATOM   3238 O O   . ALA B 1 173 ? -7.909  25.044  8.447   1.00 27.28 ? 198 ALA B O   1 
ATOM   3239 C CB  . ALA B 1 173 ? -7.024  25.713  5.444   1.00 17.88 ? 198 ALA B CB  1 
ATOM   3240 N N   . LEU B 1 174 ? -6.551  23.409  7.711   1.00 15.42 ? 199 LEU B N   1 
ATOM   3241 C CA  . LEU B 1 174 ? -7.064  22.354  8.570   1.00 12.25 ? 199 LEU B CA  1 
ATOM   3242 C C   . LEU B 1 174 ? -5.956  21.876  9.498   1.00 15.08 ? 199 LEU B C   1 
ATOM   3243 O O   . LEU B 1 174 ? -4.765  22.014  9.198   1.00 22.56 ? 199 LEU B O   1 
ATOM   3244 C CB  . LEU B 1 174 ? -7.600  21.162  7.763   1.00 20.96 ? 199 LEU B CB  1 
ATOM   3245 C CG  . LEU B 1 174 ? -8.764  21.375  6.794   1.00 18.60 ? 199 LEU B CG  1 
ATOM   3246 C CD1 . LEU B 1 174 ? -9.051  20.094  6.018   1.00 14.64 ? 199 LEU B CD1 1 
ATOM   3247 C CD2 . LEU B 1 174 ? -10.004 21.844  7.551   1.00 20.24 ? 199 LEU B CD2 1 
ATOM   3248 N N   . GLY B 1 175 ? -6.352  21.314  10.637  1.00 13.54 ? 200 GLY B N   1 
ATOM   3249 C CA  . GLY B 1 175 ? -5.389  20.620  11.466  1.00 12.56 ? 200 GLY B CA  1 
ATOM   3250 C C   . GLY B 1 175 ? -4.802  19.427  10.736  1.00 16.38 ? 200 GLY B C   1 
ATOM   3251 O O   . GLY B 1 175 ? -5.382  18.905  9.782   1.00 19.51 ? 200 GLY B O   1 
ATOM   3252 N N   . GLU B 1 176 ? -3.615  19.006  11.180  1.00 22.87 ? 201 GLU B N   1 
ATOM   3253 C CA  . GLU B 1 176 ? -2.843  18.022  10.421  1.00 26.56 ? 201 GLU B CA  1 
ATOM   3254 C C   . GLU B 1 176 ? -3.664  16.757  10.151  1.00 25.21 ? 201 GLU B C   1 
ATOM   3255 O O   . GLU B 1 176 ? -3.681  16.242  9.025   1.00 17.89 ? 201 GLU B O   1 
ATOM   3256 C CB  . GLU B 1 176 ? -1.522  17.721  11.149  1.00 38.18 ? 201 GLU B CB  1 
ATOM   3257 C CG  . GLU B 1 176 ? -1.431  16.401  11.916  1.00 61.01 ? 201 GLU B CG  1 
ATOM   3258 C CD  . GLU B 1 176 ? -1.997  16.501  13.328  1.00 73.95 ? 201 GLU B CD  1 
ATOM   3259 O OE1 . GLU B 1 176 ? -2.279  17.635  13.777  1.00 52.01 ? 201 GLU B OE1 1 
ATOM   3260 O OE2 . GLU B 1 176 ? -2.158  15.448  13.987  1.00 60.85 ? 201 GLU B OE2 1 
ATOM   3261 N N   . THR B 1 177 ? -4.353  16.240  11.176  1.00 23.82 ? 202 THR B N   1 
ATOM   3262 C CA  . THR B 1 177 ? -5.140  15.026  10.993  1.00 20.62 ? 202 THR B CA  1 
ATOM   3263 C C   . THR B 1 177 ? -6.273  15.260  9.998   1.00 19.22 ? 202 THR B C   1 
ATOM   3264 O O   . THR B 1 177 ? -6.581  14.393  9.169   1.00 16.38 ? 202 THR B O   1 
ATOM   3265 C CB  . THR B 1 177 ? -5.689  14.552  12.339  1.00 29.91 ? 202 THR B CB  1 
ATOM   3266 O OG1 . THR B 1 177 ? -4.605  14.239  13.226  1.00 41.32 ? 202 THR B OG1 1 
ATOM   3267 C CG2 . THR B 1 177 ? -6.586  13.332  12.158  1.00 31.02 ? 202 THR B CG2 1 
ATOM   3268 N N   . GLN B 1 178 ? -6.889  16.443  10.049  1.00 13.50 ? 203 GLN B N   1 
ATOM   3269 C CA  . GLN B 1 178 ? -8.007  16.732  9.155   1.00 22.67 ? 203 GLN B CA  1 
ATOM   3270 C C   . GLN B 1 178 ? -7.516  16.957  7.730   1.00 18.89 ? 203 GLN B C   1 
ATOM   3271 O O   . GLN B 1 178 ? -8.167  16.532  6.768   1.00 15.60 ? 203 GLN B O   1 
ATOM   3272 C CB  . GLN B 1 178 ? -8.787  17.944  9.664   1.00 17.77 ? 203 GLN B CB  1 
ATOM   3273 C CG  . GLN B 1 178 ? -9.577  17.691  10.945  1.00 14.02 ? 203 GLN B CG  1 
ATOM   3274 C CD  . GLN B 1 178 ? -8.696  17.671  12.185  1.00 13.20 ? 203 GLN B CD  1 
ATOM   3275 O OE1 . GLN B 1 178 ? -7.654  18.322  12.237  1.00 15.71 ? 203 GLN B OE1 1 
ATOM   3276 N NE2 . GLN B 1 178 ? -9.113  16.913  13.188  1.00 19.91 ? 203 GLN B NE2 1 
ATOM   3277 N N   . ARG B 1 179 ? -6.358  17.606  7.578   1.00 13.93 ? 204 ARG B N   1 
ATOM   3278 C CA  . ARG B 1 179 ? -5.761  17.732  6.254   1.00 13.52 ? 204 ARG B CA  1 
ATOM   3279 C C   . ARG B 1 179 ? -5.469  16.360  5.665   1.00 12.10 ? 204 ARG B C   1 
ATOM   3280 O O   . ARG B 1 179 ? -5.739  16.112  4.483   1.00 12.38 ? 204 ARG B O   1 
ATOM   3281 C CB  . ARG B 1 179 ? -4.481  18.564  6.325   1.00 17.73 ? 204 ARG B CB  1 
ATOM   3282 C CG  . ARG B 1 179 ? -3.625  18.472  5.061   1.00 21.37 ? 204 ARG B CG  1 
ATOM   3283 C CD  . ARG B 1 179 ? -2.348  19.287  5.163   1.00 21.89 ? 204 ARG B CD  1 
ATOM   3284 N NE  . ARG B 1 179 ? -1.440  18.775  6.185   1.00 35.69 ? 204 ARG B NE  1 
ATOM   3285 C CZ  . ARG B 1 179 ? -0.315  19.374  6.554   1.00 44.97 ? 204 ARG B CZ  1 
ATOM   3286 N NH1 . ARG B 1 179 ? 0.070   20.517  6.007   1.00 44.71 ? 204 ARG B NH1 1 
ATOM   3287 N NH2 . ARG B 1 179 ? 0.447   18.811  7.488   1.00 33.34 ? 204 ARG B NH2 1 
ATOM   3288 N N   . ALA B 1 180 ? -4.938  15.446  6.485   1.00 14.51 ? 205 ALA B N   1 
ATOM   3289 C CA  . ALA B 1 180 ? -4.649  14.106  5.992   1.00 18.48 ? 205 ALA B CA  1 
ATOM   3290 C C   . ALA B 1 180 ? -5.929  13.365  5.620   1.00 12.75 ? 205 ALA B C   1 
ATOM   3291 O O   . ALA B 1 180 ? -5.961  12.652  4.613   1.00 11.73 ? 205 ALA B O   1 
ATOM   3292 C CB  . ALA B 1 180 ? -3.854  13.315  7.033   1.00 4.43  ? 205 ALA B CB  1 
ATOM   3293 N N   . GLN B 1 181 ? -6.991  13.515  6.419   1.00 11.65 ? 206 GLN B N   1 
ATOM   3294 C CA  . GLN B 1 181 ? -8.252  12.854  6.082   1.00 10.72 ? 206 GLN B CA  1 
ATOM   3295 C C   . GLN B 1 181 ? -8.821  13.396  4.777   1.00 11.66 ? 206 GLN B C   1 
ATOM   3296 O O   . GLN B 1 181 ? -9.339  12.633  3.952   1.00 13.70 ? 206 GLN B O   1 
ATOM   3297 C CB  . GLN B 1 181 ? -9.255  12.996  7.223   1.00 13.05 ? 206 GLN B CB  1 
ATOM   3298 C CG  . GLN B 1 181 ? -10.599 12.306  6.970   1.00 13.95 ? 206 GLN B CG  1 
ATOM   3299 C CD  . GLN B 1 181 ? -10.479 10.804  6.777   1.00 17.66 ? 206 GLN B CD  1 
ATOM   3300 O OE1 . GLN B 1 181 ? -10.609 10.031  7.729   1.00 22.45 ? 206 GLN B OE1 1 
ATOM   3301 N NE2 . GLN B 1 181 ? -10.261 10.380  5.532   1.00 16.13 ? 206 GLN B NE2 1 
ATOM   3302 N N   . LEU B 1 182 ? -8.745  14.716  4.578   1.00 13.33 ? 207 LEU B N   1 
ATOM   3303 C CA  . LEU B 1 182 ? -9.230  15.304  3.333   1.00 9.61  ? 207 LEU B CA  1 
ATOM   3304 C C   . LEU B 1 182 ? -8.430  14.782  2.149   1.00 12.23 ? 207 LEU B C   1 
ATOM   3305 O O   . LEU B 1 182 ? -8.997  14.475  1.094   1.00 17.79 ? 207 LEU B O   1 
ATOM   3306 C CB  . LEU B 1 182 ? -9.163  16.829  3.387   1.00 10.96 ? 207 LEU B CB  1 
ATOM   3307 C CG  . LEU B 1 182 ? -9.646  17.542  2.115   1.00 10.81 ? 207 LEU B CG  1 
ATOM   3308 C CD1 . LEU B 1 182 ? -11.102 17.223  1.786   1.00 6.72  ? 207 LEU B CD1 1 
ATOM   3309 C CD2 . LEU B 1 182 ? -9.422  19.042  2.216   1.00 5.06  ? 207 LEU B CD2 1 
ATOM   3310 N N   . VAL B 1 183 ? -7.107  14.687  2.299   1.00 10.36 ? 208 VAL B N   1 
ATOM   3311 C CA  . VAL B 1 183 ? -6.280  14.206  1.198   1.00 14.80 ? 208 VAL B CA  1 
ATOM   3312 C C   . VAL B 1 183 ? -6.591  12.739  0.912   1.00 9.59  ? 208 VAL B C   1 
ATOM   3313 O O   . VAL B 1 183 ? -6.678  12.324  -0.249  1.00 13.51 ? 208 VAL B O   1 
ATOM   3314 C CB  . VAL B 1 183 ? -4.787  14.429  1.511   1.00 12.27 ? 208 VAL B CB  1 
ATOM   3315 C CG1 . VAL B 1 183 ? -3.917  13.598  0.593   1.00 13.09 ? 208 VAL B CG1 1 
ATOM   3316 C CG2 . VAL B 1 183 ? -4.427  15.906  1.389   1.00 7.99  ? 208 VAL B CG2 1 
ATOM   3317 N N   . THR B 1 184 ? -6.761  11.935  1.965   1.00 11.38 ? 209 THR B N   1 
ATOM   3318 C CA  . THR B 1 184 ? -7.161  10.540  1.799   1.00 12.40 ? 209 THR B CA  1 
ATOM   3319 C C   . THR B 1 184 ? -8.475  10.427  1.037   1.00 17.94 ? 209 THR B C   1 
ATOM   3320 O O   . THR B 1 184 ? -8.603  9.607   0.119   1.00 14.87 ? 209 THR B O   1 
ATOM   3321 C CB  . THR B 1 184 ? -7.277  9.869   3.171   1.00 13.08 ? 209 THR B CB  1 
ATOM   3322 O OG1 . THR B 1 184 ? -5.982  9.802   3.781   1.00 8.72  ? 209 THR B OG1 1 
ATOM   3323 C CG2 . THR B 1 184 ? -7.861  8.462   3.047   1.00 15.05 ? 209 THR B CG2 1 
ATOM   3324 N N   . TRP B 1 185 ? -9.464  11.252  1.395   1.00 10.32 ? 210 TRP B N   1 
ATOM   3325 C CA  . TRP B 1 185 ? -10.743 11.211  0.690   1.00 17.11 ? 210 TRP B CA  1 
ATOM   3326 C C   . TRP B 1 185 ? -10.580 11.615  -0.772  1.00 14.96 ? 210 TRP B C   1 
ATOM   3327 O O   . TRP B 1 185 ? -11.076 10.926  -1.671  1.00 14.50 ? 210 TRP B O   1 
ATOM   3328 C CB  . TRP B 1 185 ? -11.766 12.110  1.385   1.00 12.13 ? 210 TRP B CB  1 
ATOM   3329 C CG  . TRP B 1 185 ? -12.424 11.519  2.595   1.00 11.33 ? 210 TRP B CG  1 
ATOM   3330 C CD1 . TRP B 1 185 ? -12.633 10.191  2.857   1.00 12.36 ? 210 TRP B CD1 1 
ATOM   3331 C CD2 . TRP B 1 185 ? -12.972 12.238  3.708   1.00 11.03 ? 210 TRP B CD2 1 
ATOM   3332 N NE1 . TRP B 1 185 ? -13.283 10.042  4.060   1.00 15.01 ? 210 TRP B NE1 1 
ATOM   3333 C CE2 . TRP B 1 185 ? -13.501 11.283  4.604   1.00 13.61 ? 210 TRP B CE2 1 
ATOM   3334 C CE3 . TRP B 1 185 ? -13.067 13.598  4.033   1.00 12.13 ? 210 TRP B CE3 1 
ATOM   3335 C CZ2 . TRP B 1 185 ? -14.106 11.642  5.810   1.00 10.96 ? 210 TRP B CZ2 1 
ATOM   3336 C CZ3 . TRP B 1 185 ? -13.673 13.956  5.230   1.00 14.09 ? 210 TRP B CZ3 1 
ATOM   3337 C CH2 . TRP B 1 185 ? -14.179 12.978  6.108   1.00 11.76 ? 210 TRP B CH2 1 
ATOM   3338 N N   . LEU B 1 186 ? -9.881  12.728  -1.031  1.00 17.04 ? 211 LEU B N   1 
ATOM   3339 C CA  . LEU B 1 186 ? -9.699  13.176  -2.411  1.00 21.33 ? 211 LEU B CA  1 
ATOM   3340 C C   . LEU B 1 186 ? -8.996  12.115  -3.240  1.00 13.09 ? 211 LEU B C   1 
ATOM   3341 O O   . LEU B 1 186 ? -9.378  11.857  -4.388  1.00 18.40 ? 211 LEU B O   1 
ATOM   3342 C CB  . LEU B 1 186 ? -8.931  14.499  -2.452  1.00 24.14 ? 211 LEU B CB  1 
ATOM   3343 C CG  . LEU B 1 186 ? -9.715  15.683  -1.892  1.00 21.53 ? 211 LEU B CG  1 
ATOM   3344 C CD1 . LEU B 1 186 ? -8.804  16.885  -1.698  1.00 9.63  ? 211 LEU B CD1 1 
ATOM   3345 C CD2 . LEU B 1 186 ? -10.898 16.017  -2.795  1.00 20.80 ? 211 LEU B CD2 1 
ATOM   3346 N N   . LYS B 1 187 ? -7.965  11.490  -2.675  1.00 16.30 ? 212 LYS B N   1 
ATOM   3347 C CA  . LYS B 1 187 ? -7.239  10.446  -3.387  1.00 14.33 ? 212 LYS B CA  1 
ATOM   3348 C C   . LYS B 1 187 ? -8.096  9.213   -3.637  1.00 15.55 ? 212 LYS B C   1 
ATOM   3349 O O   . LYS B 1 187 ? -7.818  8.452   -4.571  1.00 12.62 ? 212 LYS B O   1 
ATOM   3350 C CB  . LYS B 1 187 ? -6.004  10.038  -2.591  1.00 14.38 ? 212 LYS B CB  1 
ATOM   3351 C CG  . LYS B 1 187 ? -4.869  11.055  -2.580  1.00 20.81 ? 212 LYS B CG  1 
ATOM   3352 C CD  . LYS B 1 187 ? -3.619  10.347  -2.078  1.00 34.87 ? 212 LYS B CD  1 
ATOM   3353 C CE  . LYS B 1 187 ? -2.389  11.222  -2.118  1.00 34.42 ? 212 LYS B CE  1 
ATOM   3354 N NZ  . LYS B 1 187 ? -1.171  10.375  -1.973  1.00 30.58 ? 212 LYS B NZ  1 
ATOM   3355 N N   . GLY B 1 188 ? -9.138  9.004   -2.838  1.00 11.49 ? 213 GLY B N   1 
ATOM   3356 C CA  . GLY B 1 188 ? -10.016 7.880   -3.057  1.00 11.95 ? 213 GLY B CA  1 
ATOM   3357 C C   . GLY B 1 188 ? -11.192 8.189   -3.948  1.00 10.69 ? 213 GLY B C   1 
ATOM   3358 O O   . GLY B 1 188 ? -12.116 7.375   -4.032  1.00 9.10  ? 213 GLY B O   1 
ATOM   3359 N N   . ASN B 1 189 ? -11.192 9.358   -4.591  1.00 12.70 ? 214 ASN B N   1 
ATOM   3360 C CA  . ASN B 1 189 ? -12.262 9.723   -5.507  1.00 17.54 ? 214 ASN B CA  1 
ATOM   3361 C C   . ASN B 1 189 ? -12.428 8.652   -6.577  1.00 8.29  ? 214 ASN B C   1 
ATOM   3362 O O   . ASN B 1 189 ? -11.445 8.146   -7.123  1.00 12.01 ? 214 ASN B O   1 
ATOM   3363 C CB  . ASN B 1 189 ? -11.956 11.073  -6.152  1.00 16.41 ? 214 ASN B CB  1 
ATOM   3364 C CG  . ASN B 1 189 ? -13.079 11.560  -7.036  1.00 17.52 ? 214 ASN B CG  1 
ATOM   3365 O OD1 . ASN B 1 189 ? -14.248 11.256  -6.792  1.00 16.68 ? 214 ASN B OD1 1 
ATOM   3366 N ND2 . ASN B 1 189 ? -12.733 12.308  -8.078  1.00 14.94 ? 214 ASN B ND2 1 
ATOM   3367 N N   . THR B 1 190 ? -13.682 8.332   -6.903  1.00 14.12 ? 215 THR B N   1 
ATOM   3368 C CA  . THR B 1 190 ? -14.002 7.362   -7.945  1.00 11.95 ? 215 THR B CA  1 
ATOM   3369 C C   . THR B 1 190 ? -14.291 7.979   -9.307  1.00 11.51 ? 215 THR B C   1 
ATOM   3370 O O   . THR B 1 190 ? -14.374 7.238   -10.290 1.00 18.72 ? 215 THR B O   1 
ATOM   3371 C CB  . THR B 1 190 ? -15.209 6.500   -7.528  1.00 8.27  ? 215 THR B CB  1 
ATOM   3372 O OG1 . THR B 1 190 ? -16.397 7.298   -7.532  1.00 14.14 ? 215 THR B OG1 1 
ATOM   3373 C CG2 . THR B 1 190 ? -15.010 5.922   -6.143  1.00 11.91 ? 215 THR B CG2 1 
ATOM   3374 N N   . THR B 1 191 ? -14.437 9.302   -9.403  1.00 14.01 ? 216 THR B N   1 
ATOM   3375 C CA  . THR B 1 191 ? -15.057 9.921   -10.570 1.00 15.33 ? 216 THR B CA  1 
ATOM   3376 C C   . THR B 1 191 ? -14.080 10.639  -11.492 1.00 16.93 ? 216 THR B C   1 
ATOM   3377 O O   . THR B 1 191 ? -14.521 11.268  -12.461 1.00 21.29 ? 216 THR B O   1 
ATOM   3378 C CB  . THR B 1 191 ? -16.149 10.911  -10.130 1.00 25.88 ? 216 THR B CB  1 
ATOM   3379 O OG1 . THR B 1 191 ? -15.545 12.033  -9.469  1.00 22.65 ? 216 THR B OG1 1 
ATOM   3380 C CG2 . THR B 1 191 ? -17.170 10.244  -9.197  1.00 8.84  ? 216 THR B CG2 1 
ATOM   3381 N N   . GLY B 1 192 ? -12.778 10.577  -11.231 1.00 16.24 ? 217 GLY B N   1 
ATOM   3382 C CA  . GLY B 1 192 ? -11.856 11.509  -11.845 1.00 17.07 ? 217 GLY B CA  1 
ATOM   3383 C C   . GLY B 1 192 ? -11.010 11.035  -13.008 1.00 21.28 ? 217 GLY B C   1 
ATOM   3384 O O   . GLY B 1 192 ? -10.262 11.847  -13.563 1.00 22.18 ? 217 GLY B O   1 
ATOM   3385 N N   . ALA B 1 193 ? -11.100 9.764   -13.412 1.00 17.77 ? 218 ALA B N   1 
ATOM   3386 C CA  . ALA B 1 193 ? -10.106 9.236   -14.343 1.00 17.62 ? 218 ALA B CA  1 
ATOM   3387 C C   . ALA B 1 193 ? -10.227 9.818   -15.749 1.00 17.86 ? 218 ALA B C   1 
ATOM   3388 O O   . ALA B 1 193 ? -9.289  9.677   -16.538 1.00 19.51 ? 218 ALA B O   1 
ATOM   3389 C CB  . ALA B 1 193 ? -10.211 7.711   -14.421 1.00 22.90 ? 218 ALA B CB  1 
ATOM   3390 N N   . ALA B 1 194 ? -11.346 10.459  -16.087 1.00 20.35 ? 219 ALA B N   1 
ATOM   3391 C CA  . ALA B 1 194 ? -11.533 11.031  -17.417 1.00 16.09 ? 219 ALA B CA  1 
ATOM   3392 C C   . ALA B 1 194 ? -11.215 12.519  -17.468 1.00 11.97 ? 219 ALA B C   1 
ATOM   3393 O O   . ALA B 1 194 ? -11.291 13.120  -18.543 1.00 14.17 ? 219 ALA B O   1 
ATOM   3394 C CB  . ALA B 1 194 ? -12.961 10.792  -17.916 1.00 12.60 ? 219 ALA B CB  1 
ATOM   3395 N N   . SER B 1 195 ? -10.845 13.120  -16.340 1.00 11.39 ? 220 SER B N   1 
ATOM   3396 C CA  . SER B 1 195 ? -10.727 14.569  -16.260 1.00 23.71 ? 220 SER B CA  1 
ATOM   3397 C C   . SER B 1 195 ? -9.262  14.978  -16.188 1.00 15.66 ? 220 SER B C   1 
ATOM   3398 O O   . SER B 1 195 ? -8.479  14.620  -17.073 1.00 16.52 ? 220 SER B O   1 
ATOM   3399 C CB  . SER B 1 195 ? -11.501 15.093  -15.048 1.00 14.29 ? 220 SER B CB  1 
ATOM   3400 O OG  . SER B 1 195 ? -12.882 14.786  -15.167 1.00 17.03 ? 220 SER B OG  1 
ATOM   3401 N N   . ILE B 1 196 ? -8.883  15.731  -15.152 1.00 16.20 ? 221 ILE B N   1 
ATOM   3402 C CA  . ILE B 1 196 ? -7.492  16.166  -15.009 1.00 15.65 ? 221 ILE B CA  1 
ATOM   3403 C C   . ILE B 1 196 ? -6.535  14.980  -15.105 1.00 22.48 ? 221 ILE B C   1 
ATOM   3404 O O   . ILE B 1 196 ? -5.519  15.035  -15.809 1.00 21.91 ? 221 ILE B O   1 
ATOM   3405 C CB  . ILE B 1 196 ? -7.303  16.950  -13.699 1.00 15.91 ? 221 ILE B CB  1 
ATOM   3406 C CG1 . ILE B 1 196 ? -7.883  18.362  -13.847 1.00 14.84 ? 221 ILE B CG1 1 
ATOM   3407 C CG2 . ILE B 1 196 ? -5.827  16.999  -13.306 1.00 14.12 ? 221 ILE B CG2 1 
ATOM   3408 C CD1 . ILE B 1 196 ? -7.986  19.133  -12.540 1.00 12.78 ? 221 ILE B CD1 1 
ATOM   3409 N N   . ARG B 1 197 ? -6.860  13.881  -14.414 1.00 20.72 ? 222 ARG B N   1 
ATOM   3410 C CA  . ARG B 1 197 ? -5.944  12.745  -14.349 1.00 15.47 ? 222 ARG B CA  1 
ATOM   3411 C C   . ARG B 1 197 ? -5.658  12.166  -15.731 1.00 18.47 ? 222 ARG B C   1 
ATOM   3412 O O   . ARG B 1 197 ? -4.523  11.770  -16.024 1.00 17.54 ? 222 ARG B O   1 
ATOM   3413 C CB  . ARG B 1 197 ? -6.501  11.663  -13.422 1.00 22.68 ? 222 ARG B CB  1 
ATOM   3414 C CG  . ARG B 1 197 ? -5.641  10.402  -13.403 1.00 39.94 ? 222 ARG B CG  1 
ATOM   3415 C CD  . ARG B 1 197 ? -5.362  9.915   -11.993 1.00 54.49 ? 222 ARG B CD  1 
ATOM   3416 N NE  . ARG B 1 197 ? -4.055  9.273   -11.896 1.00 51.19 ? 222 ARG B NE  1 
ATOM   3417 C CZ  . ARG B 1 197 ? -3.865  7.960   -11.859 1.00 77.19 ? 222 ARG B CZ  1 
ATOM   3418 N NH1 . ARG B 1 197 ? -4.884  7.113   -11.880 1.00 43.64 ? 222 ARG B NH1 1 
ATOM   3419 N NH2 . ARG B 1 197 ? -2.623  7.484   -11.792 1.00 52.17 ? 222 ARG B NH2 1 
ATOM   3420 N N   . ALA B 1 198 ? -6.670  12.119  -16.599 1.00 16.62 ? 223 ALA B N   1 
ATOM   3421 C CA  . ALA B 1 198 ? -6.469  11.587  -17.942 1.00 15.91 ? 223 ALA B CA  1 
ATOM   3422 C C   . ALA B 1 198 ? -5.435  12.380  -18.734 1.00 21.27 ? 223 ALA B C   1 
ATOM   3423 O O   . ALA B 1 198 ? -4.885  11.855  -19.708 1.00 20.65 ? 223 ALA B O   1 
ATOM   3424 C CB  . ALA B 1 198 ? -7.797  11.559  -18.701 1.00 14.59 ? 223 ALA B CB  1 
ATOM   3425 N N   . GLY B 1 199 ? -5.159  13.625  -18.347 1.00 13.52 ? 224 GLY B N   1 
ATOM   3426 C CA  . GLY B 1 199 ? -4.179  14.438  -19.033 1.00 16.09 ? 224 GLY B CA  1 
ATOM   3427 C C   . GLY B 1 199 ? -2.791  14.434  -18.432 1.00 15.57 ? 224 GLY B C   1 
ATOM   3428 O O   . GLY B 1 199 ? -1.908  15.129  -18.946 1.00 13.18 ? 224 GLY B O   1 
ATOM   3429 N N   . LEU B 1 200 ? -2.562  13.651  -17.385 1.00 16.48 ? 225 LEU B N   1 
ATOM   3430 C CA  . LEU B 1 200 ? -1.327  13.629  -16.619 1.00 23.95 ? 225 LEU B CA  1 
ATOM   3431 C C   . LEU B 1 200 ? -0.608  12.297  -16.796 1.00 30.67 ? 225 LEU B C   1 
ATOM   3432 O O   . LEU B 1 200 ? -1.231  11.289  -17.147 1.00 27.78 ? 225 LEU B O   1 
ATOM   3433 C CB  . LEU B 1 200 ? -1.606  13.861  -15.128 1.00 16.12 ? 225 LEU B CB  1 
ATOM   3434 C CG  . LEU B 1 200 ? -2.337  15.152  -14.752 1.00 17.91 ? 225 LEU B CG  1 
ATOM   3435 C CD1 . LEU B 1 200 ? -2.591  15.202  -13.250 1.00 12.52 ? 225 LEU B CD1 1 
ATOM   3436 C CD2 . LEU B 1 200 ? -1.592  16.406  -15.238 1.00 19.03 ? 225 LEU B CD2 1 
ATOM   3437 N N   . PRO B 1 201 ? 0.714   12.258  -16.593 1.00 29.29 ? 226 PRO B N   1 
ATOM   3438 C CA  . PRO B 1 201 ? 1.418   10.970  -16.638 1.00 25.96 ? 226 PRO B CA  1 
ATOM   3439 C C   . PRO B 1 201 ? 0.823   9.992   -15.634 1.00 20.37 ? 226 PRO B C   1 
ATOM   3440 O O   . PRO B 1 201 ? 0.403   10.367  -14.538 1.00 21.52 ? 226 PRO B O   1 
ATOM   3441 C CB  . PRO B 1 201 ? 2.859   11.338  -16.270 1.00 34.80 ? 226 PRO B CB  1 
ATOM   3442 C CG  . PRO B 1 201 ? 3.007   12.765  -16.686 1.00 19.13 ? 226 PRO B CG  1 
ATOM   3443 C CD  . PRO B 1 201 ? 1.643   13.403  -16.550 1.00 17.87 ? 226 PRO B CD  1 
ATOM   3444 N N   . THR B 1 202 ? 0.824   8.714   -16.019 1.00 26.70 ? 227 THR B N   1 
ATOM   3445 C CA  . THR B 1 202 ? 0.271   7.662   -15.172 1.00 30.14 ? 227 THR B CA  1 
ATOM   3446 C C   . THR B 1 202 ? 0.944   7.589   -13.804 1.00 30.97 ? 227 THR B C   1 
ATOM   3447 O O   . THR B 1 202 ? 0.284   7.268   -12.808 1.00 33.05 ? 227 THR B O   1 
ATOM   3448 C CB  . THR B 1 202 ? 0.373   6.319   -15.898 1.00 33.76 ? 227 THR B CB  1 
ATOM   3449 O OG1 . THR B 1 202 ? 1.708   6.140   -16.387 1.00 33.26 ? 227 THR B OG1 1 
ATOM   3450 C CG2 . THR B 1 202 ? -0.599  6.271   -17.073 1.00 26.63 ? 227 THR B CG2 1 
ATOM   3451 N N   . SER B 1 203 ? 2.245   7.871   -13.730 1.00 22.29 ? 228 SER B N   1 
ATOM   3452 C CA  . SER B 1 203 ? 2.986   7.745   -12.479 1.00 22.97 ? 228 SER B CA  1 
ATOM   3453 C C   . SER B 1 203 ? 2.634   8.817   -11.449 1.00 27.68 ? 228 SER B C   1 
ATOM   3454 O O   . SER B 1 203 ? 3.001   8.661   -10.279 1.00 31.40 ? 228 SER B O   1 
ATOM   3455 C CB  . SER B 1 203 ? 4.493   7.769   -12.751 1.00 13.67 ? 228 SER B CB  1 
ATOM   3456 O OG  . SER B 1 203 ? 4.906   9.021   -13.274 1.00 25.41 ? 228 SER B OG  1 
ATOM   3457 N N   . TRP B 1 204 ? 1.914   9.870   -11.835 1.00 22.25 ? 229 TRP B N   1 
ATOM   3458 C CA  . TRP B 1 204 ? 1.581   10.953  -10.915 1.00 20.72 ? 229 TRP B CA  1 
ATOM   3459 C C   . TRP B 1 204 ? 0.340   10.646  -10.085 1.00 28.05 ? 229 TRP B C   1 
ATOM   3460 O O   . TRP B 1 204 ? -0.676  10.183  -10.614 1.00 29.54 ? 229 TRP B O   1 
ATOM   3461 C CB  . TRP B 1 204 ? 1.348   12.261  -11.669 1.00 16.98 ? 229 TRP B CB  1 
ATOM   3462 C CG  . TRP B 1 204 ? 2.516   12.784  -12.438 1.00 31.63 ? 229 TRP B CG  1 
ATOM   3463 C CD1 . TRP B 1 204 ? 3.696   12.142  -12.705 1.00 26.23 ? 229 TRP B CD1 1 
ATOM   3464 C CD2 . TRP B 1 204 ? 2.644   14.101  -12.985 1.00 25.10 ? 229 TRP B CD2 1 
ATOM   3465 N NE1 . TRP B 1 204 ? 4.530   12.967  -13.418 1.00 20.24 ? 229 TRP B NE1 1 
ATOM   3466 C CE2 . TRP B 1 204 ? 3.912   14.177  -13.598 1.00 25.36 ? 229 TRP B CE2 1 
ATOM   3467 C CE3 . TRP B 1 204 ? 1.803   15.219  -13.027 1.00 16.05 ? 229 TRP B CE3 1 
ATOM   3468 C CZ2 . TRP B 1 204 ? 4.360   15.329  -14.245 1.00 21.44 ? 229 TRP B CZ2 1 
ATOM   3469 C CZ3 . TRP B 1 204 ? 2.248   16.361  -13.670 1.00 23.33 ? 229 TRP B CZ3 1 
ATOM   3470 C CH2 . TRP B 1 204 ? 3.516   16.408  -14.270 1.00 24.38 ? 229 TRP B CH2 1 
ATOM   3471 N N   . THR B 1 205 ? 0.436   10.887  -8.776  1.00 20.75 ? 230 THR B N   1 
ATOM   3472 C CA  . THR B 1 205 ? -0.687  10.646  -7.877  1.00 23.06 ? 230 THR B CA  1 
ATOM   3473 C C   . THR B 1 205 ? -1.615  11.855  -7.868  1.00 18.05 ? 230 THR B C   1 
ATOM   3474 O O   . THR B 1 205 ? -1.166  12.998  -7.892  1.00 21.55 ? 230 THR B O   1 
ATOM   3475 C CB  . THR B 1 205 ? -0.193  10.372  -6.452  1.00 25.12 ? 230 THR B CB  1 
ATOM   3476 O OG1 . THR B 1 205 ? 0.750   9.295   -6.460  1.00 27.91 ? 230 THR B OG1 1 
ATOM   3477 C CG2 . THR B 1 205 ? -1.357  10.021  -5.526  1.00 16.31 ? 230 THR B CG2 1 
ATOM   3478 N N   . VAL B 1 206 ? -2.918  11.605  -7.874  1.00 24.54 ? 231 VAL B N   1 
ATOM   3479 C CA  . VAL B 1 206 ? -3.911  12.667  -7.957  1.00 12.85 ? 231 VAL B CA  1 
ATOM   3480 C C   . VAL B 1 206 ? -4.973  12.418  -6.896  1.00 19.88 ? 231 VAL B C   1 
ATOM   3481 O O   . VAL B 1 206 ? -5.450  11.290  -6.737  1.00 15.95 ? 231 VAL B O   1 
ATOM   3482 C CB  . VAL B 1 206 ? -4.556  12.770  -9.355  1.00 19.05 ? 231 VAL B CB  1 
ATOM   3483 C CG1 . VAL B 1 206 ? -5.638  13.858  -9.363  1.00 14.45 ? 231 VAL B CG1 1 
ATOM   3484 C CG2 . VAL B 1 206 ? -3.501  13.061  -10.418 1.00 23.52 ? 231 VAL B CG2 1 
ATOM   3485 N N   . GLY B 1 207 ? -5.349  13.469  -6.181  1.00 21.37 ? 232 GLY B N   1 
ATOM   3486 C CA  . GLY B 1 207 ? -6.622  13.509  -5.477  1.00 18.22 ? 232 GLY B CA  1 
ATOM   3487 C C   . GLY B 1 207 ? -7.418  14.645  -6.082  1.00 16.64 ? 232 GLY B C   1 
ATOM   3488 O O   . GLY B 1 207 ? -6.881  15.719  -6.332  1.00 22.48 ? 232 GLY B O   1 
ATOM   3489 N N   . ASP B 1 208 ? -8.696  14.397  -6.335  1.00 23.15 ? 233 ASP B N   1 
ATOM   3490 C CA  . ASP B 1 208 ? -9.466  15.357  -7.110  1.00 25.88 ? 233 ASP B CA  1 
ATOM   3491 C C   . ASP B 1 208 ? -10.935 15.276  -6.746  1.00 16.27 ? 233 ASP B C   1 
ATOM   3492 O O   . ASP B 1 208 ? -11.397 14.332  -6.103  1.00 15.19 ? 233 ASP B O   1 
ATOM   3493 C CB  . ASP B 1 208 ? -9.295  15.107  -8.611  1.00 17.46 ? 233 ASP B CB  1 
ATOM   3494 C CG  . ASP B 1 208 ? -9.642  13.680  -8.990  1.00 33.88 ? 233 ASP B CG  1 
ATOM   3495 O OD1 . ASP B 1 208 ? -8.887  12.761  -8.598  1.00 40.07 ? 233 ASP B OD1 1 
ATOM   3496 O OD2 . ASP B 1 208 ? -10.683 13.468  -9.644  1.00 30.33 ? 233 ASP B OD2 1 
ATOM   3497 N N   . LYS B 1 209 ? -11.665 16.291  -7.188  1.00 16.83 ? 234 LYS B N   1 
ATOM   3498 C CA  . LYS B 1 209 ? -13.115 16.290  -7.126  1.00 17.99 ? 234 LYS B CA  1 
ATOM   3499 C C   . LYS B 1 209 ? -13.639 16.848  -8.438  1.00 18.12 ? 234 LYS B C   1 
ATOM   3500 O O   . LYS B 1 209 ? -13.249 17.946  -8.856  1.00 16.03 ? 234 LYS B O   1 
ATOM   3501 C CB  . LYS B 1 209 ? -13.625 17.127  -5.951  1.00 14.44 ? 234 LYS B CB  1 
ATOM   3502 C CG  . LYS B 1 209 ? -15.136 17.183  -5.860  1.00 17.13 ? 234 LYS B CG  1 
ATOM   3503 C CD  . LYS B 1 209 ? -15.667 15.847  -5.366  1.00 17.74 ? 234 LYS B CD  1 
ATOM   3504 C CE  . LYS B 1 209 ? -17.166 15.728  -5.569  1.00 18.34 ? 234 LYS B CE  1 
ATOM   3505 N NZ  . LYS B 1 209 ? -17.486 15.294  -6.949  1.00 15.99 ? 234 LYS B NZ  1 
ATOM   3506 N N   . THR B 1 210 ? -14.471 16.061  -9.104  1.00 17.64 ? 235 THR B N   1 
ATOM   3507 C CA  . THR B 1 210 ? -15.076 16.445  -10.363 1.00 15.65 ? 235 THR B CA  1 
ATOM   3508 C C   . THR B 1 210 ? -16.393 17.168  -10.097 1.00 16.82 ? 235 THR B C   1 
ATOM   3509 O O   . THR B 1 210 ? -16.909 17.196  -8.977  1.00 17.79 ? 235 THR B O   1 
ATOM   3510 C CB  . THR B 1 210 ? -15.322 15.215  -11.231 1.00 17.00 ? 235 THR B CB  1 
ATOM   3511 O OG1 . THR B 1 210 ? -16.014 14.231  -10.452 1.00 21.06 ? 235 THR B OG1 1 
ATOM   3512 C CG2 . THR B 1 210 ? -14.001 14.629  -11.723 1.00 13.57 ? 235 THR B CG2 1 
ATOM   3513 N N   . GLY B 1 211 ? -16.932 17.767  -11.146 1.00 17.79 ? 236 GLY B N   1 
ATOM   3514 C CA  . GLY B 1 211 ? -18.276 18.302  -11.075 1.00 10.41 ? 236 GLY B CA  1 
ATOM   3515 C C   . GLY B 1 211 ? -18.853 18.411  -12.464 1.00 19.30 ? 236 GLY B C   1 
ATOM   3516 O O   . GLY B 1 211 ? -18.124 18.501  -13.455 1.00 21.01 ? 236 GLY B O   1 
ATOM   3517 N N   . SER B 1 212 ? -20.176 18.385  -12.536 1.00 16.31 ? 237 SER B N   1 
ATOM   3518 C CA  . SER B 1 212 ? -20.840 18.513  -13.822 1.00 15.88 ? 237 SER B CA  1 
ATOM   3519 C C   . SER B 1 212 ? -22.164 19.217  -13.591 1.00 16.90 ? 237 SER B C   1 
ATOM   3520 O O   . SER B 1 212 ? -22.753 19.119  -12.510 1.00 17.31 ? 237 SER B O   1 
ATOM   3521 C CB  . SER B 1 212 ? -21.051 17.164  -14.523 1.00 9.90  ? 237 SER B CB  1 
ATOM   3522 O OG  . SER B 1 212 ? -22.090 16.424  -13.913 1.00 15.38 ? 237 SER B OG  1 
ATOM   3523 N N   . GLY B 1 213 ? -22.626 19.929  -14.606 1.00 9.88  ? 238 GLY B N   1 
ATOM   3524 C CA  . GLY B 1 213 ? -23.934 20.527  -14.484 1.00 11.30 ? 238 GLY B CA  1 
ATOM   3525 C C   . GLY B 1 213 ? -24.543 20.831  -15.829 1.00 13.26 ? 238 GLY B C   1 
ATOM   3526 O O   . GLY B 1 213 ? -23.970 20.517  -16.880 1.00 13.78 ? 238 GLY B O   1 
ATOM   3527 N N   . ASP B 1 214 ? -25.619 21.612  -15.777 1.00 13.12 ? 240 ASP B N   1 
ATOM   3528 C CA  . ASP B 1 214 ? -26.232 22.106  -16.993 1.00 10.46 ? 240 ASP B CA  1 
ATOM   3529 C C   . ASP B 1 214 ? -25.277 23.040  -17.710 1.00 13.46 ? 240 ASP B C   1 
ATOM   3530 O O   . ASP B 1 214 ? -24.221 23.422  -17.195 1.00 8.78  ? 240 ASP B O   1 
ATOM   3531 C CB  . ASP B 1 214 ? -27.535 22.851  -16.692 1.00 23.55 ? 240 ASP B CB  1 
ATOM   3532 C CG  . ASP B 1 214 ? -28.656 21.933  -16.236 1.00 30.98 ? 240 ASP B CG  1 
ATOM   3533 O OD1 . ASP B 1 214 ? -28.462 20.696  -16.241 1.00 33.66 ? 240 ASP B OD1 1 
ATOM   3534 O OD2 . ASP B 1 214 ? -29.737 22.456  -15.880 1.00 24.49 ? 240 ASP B OD2 1 
ATOM   3535 N N   . TYR B 1 215 ? -25.678 23.417  -18.921 1.00 15.90 ? 241 TYR B N   1 
ATOM   3536 C CA  . TYR B 1 215 ? -24.828 24.193  -19.807 1.00 11.94 ? 241 TYR B CA  1 
ATOM   3537 C C   . TYR B 1 215 ? -23.502 23.474  -20.034 1.00 14.85 ? 241 TYR B C   1 
ATOM   3538 O O   . TYR B 1 215 ? -22.449 24.105  -20.175 1.00 11.06 ? 241 TYR B O   1 
ATOM   3539 C CB  . TYR B 1 215 ? -24.627 25.614  -19.270 1.00 12.23 ? 241 TYR B CB  1 
ATOM   3540 C CG  . TYR B 1 215 ? -25.895 26.429  -19.393 1.00 20.29 ? 241 TYR B CG  1 
ATOM   3541 C CD1 . TYR B 1 215 ? -26.877 26.367  -18.406 1.00 16.47 ? 241 TYR B CD1 1 
ATOM   3542 C CD2 . TYR B 1 215 ? -26.146 27.203  -20.526 1.00 16.09 ? 241 TYR B CD2 1 
ATOM   3543 C CE1 . TYR B 1 215 ? -28.050 27.092  -18.520 1.00 23.69 ? 241 TYR B CE1 1 
ATOM   3544 C CE2 . TYR B 1 215 ? -27.324 27.927  -20.652 1.00 21.04 ? 241 TYR B CE2 1 
ATOM   3545 C CZ  . TYR B 1 215 ? -28.269 27.869  -19.645 1.00 25.59 ? 241 TYR B CZ  1 
ATOM   3546 O OH  . TYR B 1 215 ? -29.441 28.583  -19.765 1.00 28.41 ? 241 TYR B OH  1 
ATOM   3547 N N   . GLY B 1 216 ? -23.563 22.141  -20.058 1.00 14.82 ? 242 GLY B N   1 
ATOM   3548 C CA  . GLY B 1 216 ? -22.390 21.328  -20.323 1.00 12.80 ? 242 GLY B CA  1 
ATOM   3549 C C   . GLY B 1 216 ? -21.252 21.589  -19.367 1.00 9.21  ? 242 GLY B C   1 
ATOM   3550 O O   . GLY B 1 216 ? -20.087 21.455  -19.750 1.00 7.71  ? 242 GLY B O   1 
ATOM   3551 N N   . THR B 1 217 ? -21.560 21.972  -18.130 1.00 12.67 ? 243 THR B N   1 
ATOM   3552 C CA  . THR B 1 217 ? -20.503 22.296  -17.180 1.00 5.68  ? 243 THR B CA  1 
ATOM   3553 C C   . THR B 1 217 ? -19.720 21.054  -16.774 1.00 15.62 ? 243 THR B C   1 
ATOM   3554 O O   . THR B 1 217 ? -20.300 20.056  -16.338 1.00 16.16 ? 243 THR B O   1 
ATOM   3555 C CB  . THR B 1 217 ? -21.082 22.995  -15.955 1.00 6.73  ? 243 THR B CB  1 
ATOM   3556 O OG1 . THR B 1 217 ? -21.750 24.198  -16.371 1.00 7.86  ? 243 THR B OG1 1 
ATOM   3557 C CG2 . THR B 1 217 ? -19.972 23.363  -14.983 1.00 5.00  ? 243 THR B CG2 1 
ATOM   3558 N N   . THR B 1 218 ? -18.396 21.145  -16.887 1.00 12.37 ? 244 THR B N   1 
ATOM   3559 C CA  . THR B 1 218 ? -17.478 20.037  -16.649 1.00 16.12 ? 244 THR B CA  1 
ATOM   3560 C C   . THR B 1 218 ? -16.314 20.611  -15.856 1.00 12.54 ? 244 THR B C   1 
ATOM   3561 O O   . THR B 1 218 ? -15.584 21.470  -16.355 1.00 19.66 ? 244 THR B O   1 
ATOM   3562 C CB  . THR B 1 218 ? -16.985 19.431  -17.959 1.00 16.85 ? 244 THR B CB  1 
ATOM   3563 O OG1 . THR B 1 218 ? -18.095 19.234  -18.846 1.00 19.81 ? 244 THR B OG1 1 
ATOM   3564 C CG2 . THR B 1 218 ? -16.295 18.107  -17.693 1.00 21.65 ? 244 THR B CG2 1 
ATOM   3565 N N   . ASN B 1 219 ? -16.151 20.156  -14.624 1.00 14.15 ? 245 ASN B N   1 
ATOM   3566 C CA  . ASN B 1 219 ? -15.223 20.771  -13.700 1.00 13.90 ? 245 ASN B CA  1 
ATOM   3567 C C   . ASN B 1 219 ? -14.357 19.686  -13.085 1.00 15.02 ? 245 ASN B C   1 
ATOM   3568 O O   . ASN B 1 219 ? -14.782 18.537  -12.936 1.00 20.11 ? 245 ASN B O   1 
ATOM   3569 C CB  . ASN B 1 219 ? -15.980 21.518  -12.591 1.00 12.77 ? 245 ASN B CB  1 
ATOM   3570 C CG  . ASN B 1 219 ? -16.848 22.650  -13.132 1.00 22.86 ? 245 ASN B CG  1 
ATOM   3571 O OD1 . ASN B 1 219 ? -16.568 23.205  -14.194 1.00 20.08 ? 245 ASN B OD1 1 
ATOM   3572 N ND2 . ASN B 1 219 ? -17.907 22.997  -12.397 1.00 15.11 ? 245 ASN B ND2 1 
ATOM   3573 N N   . ASP B 1 220 ? -13.183 20.095  -12.628 1.00 13.25 ? 246 ASP B N   1 
ATOM   3574 C CA  . ASP B 1 220 ? -12.303 19.230  -11.863 1.00 21.43 ? 246 ASP B CA  1 
ATOM   3575 C C   . ASP B 1 220 ? -11.340 20.098  -11.078 1.00 12.52 ? 246 ASP B C   1 
ATOM   3576 O O   . ASP B 1 220 ? -10.865 21.116  -11.580 1.00 25.70 ? 246 ASP B O   1 
ATOM   3577 C CB  . ASP B 1 220 ? -11.521 18.278  -12.771 1.00 14.69 ? 246 ASP B CB  1 
ATOM   3578 C CG  . ASP B 1 220 ? -10.982 17.074  -12.023 1.00 25.31 ? 246 ASP B CG  1 
ATOM   3579 O OD1 . ASP B 1 220 ? -11.397 16.847  -10.867 1.00 27.20 ? 246 ASP B OD1 1 
ATOM   3580 O OD2 . ASP B 1 220 ? -10.138 16.350  -12.586 1.00 23.33 ? 246 ASP B OD2 1 
ATOM   3581 N N   . ILE B 1 221 ? -11.092 19.715  -9.834  1.00 11.71 ? 247 ILE B N   1 
ATOM   3582 C CA  . ILE B 1 221 ? -10.085 20.359  -9.003  1.00 9.76  ? 247 ILE B CA  1 
ATOM   3583 C C   . ILE B 1 221 ? -9.231  19.261  -8.389  1.00 10.72 ? 247 ILE B C   1 
ATOM   3584 O O   . ILE B 1 221 ? -9.760  18.249  -7.924  1.00 17.25 ? 247 ILE B O   1 
ATOM   3585 C CB  . ILE B 1 221 ? -10.709 21.289  -7.939  1.00 19.67 ? 247 ILE B CB  1 
ATOM   3586 C CG1 . ILE B 1 221 ? -11.475 20.509  -6.868  1.00 22.55 ? 247 ILE B CG1 1 
ATOM   3587 C CG2 . ILE B 1 221 ? -11.594 22.342  -8.595  1.00 11.77 ? 247 ILE B CG2 1 
ATOM   3588 C CD1 . ILE B 1 221 ? -12.014 21.390  -5.750  1.00 22.41 ? 247 ILE B CD1 1 
ATOM   3589 N N   . ALA B 1 222 ? -7.914  19.428  -8.430  1.00 14.95 ? 248 ALA B N   1 
ATOM   3590 C CA  . ALA B 1 222 ? -7.013  18.340  -8.091  1.00 15.04 ? 248 ALA B CA  1 
ATOM   3591 C C   . ALA B 1 222 ? -5.800  18.869  -7.352  1.00 11.99 ? 248 ALA B C   1 
ATOM   3592 O O   . ALA B 1 222 ? -5.323  19.971  -7.623  1.00 17.00 ? 248 ALA B O   1 
ATOM   3593 C CB  . ALA B 1 222 ? -6.556  17.582  -9.346  1.00 7.17  ? 248 ALA B CB  1 
ATOM   3594 N N   . VAL B 1 223 ? -5.319  18.080  -6.405  1.00 19.15 ? 249 VAL B N   1 
ATOM   3595 C CA  . VAL B 1 223 ? -3.970  18.203  -5.881  1.00 19.52 ? 249 VAL B CA  1 
ATOM   3596 C C   . VAL B 1 223 ? -3.196  17.008  -6.410  1.00 19.15 ? 249 VAL B C   1 
ATOM   3597 O O   . VAL B 1 223 ? -3.713  15.882  -6.450  1.00 20.78 ? 249 VAL B O   1 
ATOM   3598 C CB  . VAL B 1 223 ? -3.944  18.283  -4.339  1.00 22.19 ? 249 VAL B CB  1 
ATOM   3599 C CG1 . VAL B 1 223 ? -4.913  17.277  -3.724  1.00 29.10 ? 249 VAL B CG1 1 
ATOM   3600 C CG2 . VAL B 1 223 ? -2.533  18.095  -3.811  1.00 16.40 ? 249 VAL B CG2 1 
ATOM   3601 N N   . ILE B 1 224 ? -1.969  17.263  -6.849  1.00 21.35 ? 250 ILE B N   1 
ATOM   3602 C CA  . ILE B 1 224 ? -1.221  16.371  -7.722  1.00 18.44 ? 250 ILE B CA  1 
ATOM   3603 C C   . ILE B 1 224 ? 0.174   16.194  -7.154  1.00 24.16 ? 250 ILE B C   1 
ATOM   3604 O O   . ILE B 1 224 ? 0.846   17.177  -6.832  1.00 19.57 ? 250 ILE B O   1 
ATOM   3605 C CB  . ILE B 1 224 ? -1.156  16.929  -9.156  1.00 17.28 ? 250 ILE B CB  1 
ATOM   3606 C CG1 . ILE B 1 224 ? -2.577  17.124  -9.705  1.00 13.59 ? 250 ILE B CG1 1 
ATOM   3607 C CG2 . ILE B 1 224 ? -0.266  16.061  -10.045 1.00 19.53 ? 250 ILE B CG2 1 
ATOM   3608 C CD1 . ILE B 1 224 ? -2.682  18.159  -10.794 1.00 21.72 ? 250 ILE B CD1 1 
ATOM   3609 N N   . TRP B 1 225 ? 0.602   14.945  -7.004  1.00 20.48 ? 251 TRP B N   1 
ATOM   3610 C CA  . TRP B 1 225 ? 1.959   14.648  -6.570  1.00 21.17 ? 251 TRP B CA  1 
ATOM   3611 C C   . TRP B 1 225 ? 2.667   14.071  -7.785  1.00 19.28 ? 251 TRP B C   1 
ATOM   3612 O O   . TRP B 1 225 ? 2.541   12.870  -8.080  1.00 17.74 ? 251 TRP B O   1 
ATOM   3613 C CB  . TRP B 1 225 ? 1.951   13.660  -5.404  1.00 22.13 ? 251 TRP B CB  1 
ATOM   3614 C CG  . TRP B 1 225 ? 1.383   14.282  -4.162  1.00 25.63 ? 251 TRP B CG  1 
ATOM   3615 C CD1 . TRP B 1 225 ? 2.074   14.874  -3.141  1.00 18.77 ? 251 TRP B CD1 1 
ATOM   3616 C CD2 . TRP B 1 225 ? -0.008  14.386  -3.819  1.00 19.59 ? 251 TRP B CD2 1 
ATOM   3617 N NE1 . TRP B 1 225 ? 1.198   15.334  -2.184  1.00 20.22 ? 251 TRP B NE1 1 
ATOM   3618 C CE2 . TRP B 1 225 ? -0.084  15.047  -2.575  1.00 15.03 ? 251 TRP B CE2 1 
ATOM   3619 C CE3 . TRP B 1 225 ? -1.194  13.981  -4.443  1.00 26.03 ? 251 TRP B CE3 1 
ATOM   3620 C CZ2 . TRP B 1 225 ? -1.301  15.314  -1.943  1.00 20.12 ? 251 TRP B CZ2 1 
ATOM   3621 C CZ3 . TRP B 1 225 ? -2.405  14.244  -3.813  1.00 20.71 ? 251 TRP B CZ3 1 
ATOM   3622 C CH2 . TRP B 1 225 ? -2.448  14.900  -2.573  1.00 23.63 ? 251 TRP B CH2 1 
ATOM   3623 N N   . PRO B 1 226 ? 3.355   14.903  -8.562  1.00 24.00 ? 252 PRO B N   1 
ATOM   3624 C CA  . PRO B 1 226 ? 4.095   14.406  -9.720  1.00 24.57 ? 252 PRO B CA  1 
ATOM   3625 C C   . PRO B 1 226 ? 5.312   13.619  -9.276  1.00 30.64 ? 252 PRO B C   1 
ATOM   3626 O O   . PRO B 1 226 ? 5.859   13.841  -8.192  1.00 27.42 ? 252 PRO B O   1 
ATOM   3627 C CB  . PRO B 1 226 ? 4.499   15.685  -10.464 1.00 20.31 ? 252 PRO B CB  1 
ATOM   3628 C CG  . PRO B 1 226 ? 3.734   16.793  -9.807  1.00 17.24 ? 252 PRO B CG  1 
ATOM   3629 C CD  . PRO B 1 226 ? 3.504   16.357  -8.410  1.00 22.18 ? 252 PRO B CD  1 
ATOM   3630 N N   . GLN B 1 227 ? 5.712   12.663  -10.106 1.00 39.98 ? 254 GLN B N   1 
ATOM   3631 C CA  . GLN B 1 227 ? 6.885   11.867  -9.782  1.00 40.78 ? 254 GLN B CA  1 
ATOM   3632 C C   . GLN B 1 227 ? 8.108   12.765  -9.652  1.00 32.71 ? 254 GLN B C   1 
ATOM   3633 O O   . GLN B 1 227 ? 8.451   13.497  -10.586 1.00 34.62 ? 254 GLN B O   1 
ATOM   3634 C CB  . GLN B 1 227 ? 7.122   10.794  -10.847 1.00 57.50 ? 254 GLN B CB  1 
ATOM   3635 C CG  . GLN B 1 227 ? 7.908   9.577   -10.341 1.00 48.81 ? 254 GLN B CG  1 
ATOM   3636 C CD  . GLN B 1 227 ? 7.242   8.886   -9.153  1.00 55.95 ? 254 GLN B CD  1 
ATOM   3637 O OE1 . GLN B 1 227 ? 7.226   9.409   -8.033  1.00 42.71 ? 254 GLN B OE1 1 
ATOM   3638 N NE2 . GLN B 1 227 ? 6.694   7.699   -9.395  1.00 44.29 ? 254 GLN B NE2 1 
ATOM   3639 N N   . GLY B 1 228 ? 8.741   12.739  -8.483  1.00 25.13 ? 255 GLY B N   1 
ATOM   3640 C CA  . GLY B 1 228 ? 9.996   13.434  -8.304  1.00 34.00 ? 255 GLY B CA  1 
ATOM   3641 C C   . GLY B 1 228 ? 9.928   14.910  -7.980  1.00 38.30 ? 255 GLY B C   1 
ATOM   3642 O O   . GLY B 1 228 ? 10.971  15.575  -8.026  1.00 25.14 ? 255 GLY B O   1 
ATOM   3643 N N   . ARG B 1 229 ? 8.753   15.467  -7.682  1.00 31.82 ? 256 ARG B N   1 
ATOM   3644 C CA  . ARG B 1 229 ? 8.714   16.902  -7.441  1.00 34.26 ? 256 ARG B CA  1 
ATOM   3645 C C   . ARG B 1 229 ? 7.577   17.273  -6.495  1.00 21.34 ? 256 ARG B C   1 
ATOM   3646 O O   . ARG B 1 229 ? 6.741   16.444  -6.125  1.00 33.02 ? 256 ARG B O   1 
ATOM   3647 C CB  . ARG B 1 229 ? 8.692   17.618  -8.800  1.00 26.65 ? 256 ARG B CB  1 
ATOM   3648 C CG  . ARG B 1 229 ? 7.516   17.337  -9.716  1.00 31.16 ? 256 ARG B CG  1 
ATOM   3649 C CD  . ARG B 1 229 ? 7.726   18.137  -10.994 1.00 36.90 ? 256 ARG B CD  1 
ATOM   3650 N NE  . ARG B 1 229 ? 7.684   19.585  -10.842 1.00 46.36 ? 256 ARG B NE  1 
ATOM   3651 C CZ  . ARG B 1 229 ? 7.975   20.429  -11.822 1.00 56.56 ? 256 ARG B CZ  1 
ATOM   3652 N NH1 . ARG B 1 229 ? 8.402   19.997  -13.000 1.00 45.50 ? 256 ARG B NH1 1 
ATOM   3653 N NH2 . ARG B 1 229 ? 7.811   21.735  -11.626 1.00 39.25 ? 256 ARG B NH2 1 
ATOM   3654 N N   . ALA B 1 230 ? 7.578   18.541  -6.094  1.00 12.60 ? 257 ALA B N   1 
ATOM   3655 C CA  . ALA B 1 230 ? 6.645   19.058  -5.105  1.00 31.32 ? 257 ALA B CA  1 
ATOM   3656 C C   . ALA B 1 230 ? 5.227   19.035  -5.668  1.00 22.07 ? 257 ALA B C   1 
ATOM   3657 O O   . ALA B 1 230 ? 5.037   19.058  -6.886  1.00 16.56 ? 257 ALA B O   1 
ATOM   3658 C CB  . ALA B 1 230 ? 7.035   20.479  -4.696  1.00 23.79 ? 257 ALA B CB  1 
ATOM   3659 N N   . PRO B 1 231 ? 4.211   18.985  -4.808  1.00 22.74 ? 258 PRO B N   1 
ATOM   3660 C CA  . PRO B 1 231 ? 2.845   18.864  -5.325  1.00 19.52 ? 258 PRO B CA  1 
ATOM   3661 C C   . PRO B 1 231 ? 2.415   20.128  -6.058  1.00 20.92 ? 258 PRO B C   1 
ATOM   3662 O O   . PRO B 1 231 ? 2.909   21.235  -5.823  1.00 19.29 ? 258 PRO B O   1 
ATOM   3663 C CB  . PRO B 1 231 ? 1.994   18.641  -4.070  1.00 19.75 ? 258 PRO B CB  1 
ATOM   3664 C CG  . PRO B 1 231 ? 2.856   19.036  -2.920  1.00 24.07 ? 258 PRO B CG  1 
ATOM   3665 C CD  . PRO B 1 231 ? 4.272   18.859  -3.343  1.00 20.10 ? 258 PRO B CD  1 
ATOM   3666 N N   . LEU B 1 232 ? 1.458   19.928  -6.953  1.00 11.07 ? 259 LEU B N   1 
ATOM   3667 C CA  . LEU B 1 232 ? 0.746   20.944  -7.702  1.00 12.30 ? 259 LEU B CA  1 
ATOM   3668 C C   . LEU B 1 232 ? -0.702  20.997  -7.244  1.00 20.52 ? 259 LEU B C   1 
ATOM   3669 O O   . LEU B 1 232 ? -1.247  20.029  -6.712  1.00 20.12 ? 259 LEU B O   1 
ATOM   3670 C CB  . LEU B 1 232 ? 0.773   20.636  -9.204  1.00 18.17 ? 259 LEU B CB  1 
ATOM   3671 C CG  . LEU B 1 232 ? 2.076   20.102  -9.802  1.00 16.93 ? 259 LEU B CG  1 
ATOM   3672 C CD1 . LEU B 1 232 ? 1.825   19.528  -11.188 1.00 11.55 ? 259 LEU B CD1 1 
ATOM   3673 C CD2 . LEU B 1 232 ? 3.146   21.182  -9.834  1.00 21.14 ? 259 LEU B CD2 1 
ATOM   3674 N N   . VAL B 1 233 ? -1.327  22.142  -7.461  1.00 14.41 ? 260 VAL B N   1 
ATOM   3675 C CA  . VAL B 1 233 ? -2.771  22.256  -7.368  1.00 13.70 ? 260 VAL B CA  1 
ATOM   3676 C C   . VAL B 1 233 ? -3.251  22.715  -8.734  1.00 10.54 ? 260 VAL B C   1 
ATOM   3677 O O   . VAL B 1 233 ? -2.706  23.669  -9.296  1.00 14.22 ? 260 VAL B O   1 
ATOM   3678 C CB  . VAL B 1 233 ? -3.199  23.232  -6.256  1.00 24.53 ? 260 VAL B CB  1 
ATOM   3679 C CG1 . VAL B 1 233 ? -4.707  23.458  -6.292  1.00 16.01 ? 260 VAL B CG1 1 
ATOM   3680 C CG2 . VAL B 1 233 ? -2.740  22.718  -4.895  1.00 21.09 ? 260 VAL B CG2 1 
ATOM   3681 N N   . LEU B 1 234 ? -4.260  22.042  -9.273  1.00 11.39 ? 261 LEU B N   1 
ATOM   3682 C CA  . LEU B 1 234 ? -4.737  22.349  -10.612 1.00 14.20 ? 261 LEU B CA  1 
ATOM   3683 C C   . LEU B 1 234 ? -6.253  22.369  -10.627 1.00 14.26 ? 261 LEU B C   1 
ATOM   3684 O O   . LEU B 1 234 ? -6.903  21.426  -10.171 1.00 13.91 ? 261 LEU B O   1 
ATOM   3685 C CB  . LEU B 1 234 ? -4.212  21.330  -11.630 1.00 18.88 ? 261 LEU B CB  1 
ATOM   3686 C CG  . LEU B 1 234 ? -4.668  21.511  -13.077 1.00 15.89 ? 261 LEU B CG  1 
ATOM   3687 C CD1 . LEU B 1 234 ? -4.191  22.844  -13.624 1.00 11.37 ? 261 LEU B CD1 1 
ATOM   3688 C CD2 . LEU B 1 234 ? -4.155  20.358  -13.933 1.00 6.98  ? 261 LEU B CD2 1 
ATOM   3689 N N   . VAL B 1 235 ? -6.807  23.440  -11.172 1.00 8.36  ? 262 VAL B N   1 
ATOM   3690 C CA  . VAL B 1 235 ? -8.243  23.642  -11.247 1.00 12.37 ? 262 VAL B CA  1 
ATOM   3691 C C   . VAL B 1 235 ? -8.599  23.848  -12.711 1.00 10.95 ? 262 VAL B C   1 
ATOM   3692 O O   . VAL B 1 235 ? -8.031  24.728  -13.368 1.00 16.94 ? 262 VAL B O   1 
ATOM   3693 C CB  . VAL B 1 235 ? -8.676  24.843  -10.393 1.00 17.25 ? 262 VAL B CB  1 
ATOM   3694 C CG1 . VAL B 1 235 ? -10.103 25.147  -10.642 1.00 20.47 ? 262 VAL B CG1 1 
ATOM   3695 C CG2 . VAL B 1 235 ? -8.442  24.557  -8.906  1.00 16.35 ? 262 VAL B CG2 1 
ATOM   3696 N N   . THR B 1 236 ? -9.517  23.030  -13.228 1.00 13.22 ? 263 THR B N   1 
ATOM   3697 C CA  . THR B 1 236 ? -10.017 23.146  -14.598 1.00 22.34 ? 263 THR B CA  1 
ATOM   3698 C C   . THR B 1 236 ? -11.538 23.222  -14.554 1.00 20.15 ? 263 THR B C   1 
ATOM   3699 O O   . THR B 1 236 ? -12.203 22.229  -14.249 1.00 17.54 ? 263 THR B O   1 
ATOM   3700 C CB  . THR B 1 236 ? -9.571  21.965  -15.465 1.00 15.75 ? 263 THR B CB  1 
ATOM   3701 O OG1 . THR B 1 236 ? -10.014 20.738  -14.867 1.00 15.02 ? 263 THR B OG1 1 
ATOM   3702 C CG2 . THR B 1 236 ? -8.057  21.944  -15.653 1.00 8.16  ? 263 THR B CG2 1 
ATOM   3703 N N   . TYR B 1 237 ? -12.086 24.393  -14.862 1.00 15.77 ? 264 TYR B N   1 
ATOM   3704 C CA  . TYR B 1 237 ? -13.518 24.591  -15.024 1.00 12.94 ? 264 TYR B CA  1 
ATOM   3705 C C   . TYR B 1 237 ? -13.842 24.750  -16.504 1.00 17.95 ? 264 TYR B C   1 
ATOM   3706 O O   . TYR B 1 237 ? -13.054 25.323  -17.260 1.00 18.29 ? 264 TYR B O   1 
ATOM   3707 C CB  . TYR B 1 237 ? -13.996 25.824  -14.255 1.00 18.85 ? 264 TYR B CB  1 
ATOM   3708 C CG  . TYR B 1 237 ? -13.938 25.682  -12.748 1.00 28.44 ? 264 TYR B CG  1 
ATOM   3709 C CD1 . TYR B 1 237 ? -14.793 24.813  -12.089 1.00 40.00 ? 264 TYR B CD1 1 
ATOM   3710 C CD2 . TYR B 1 237 ? -13.081 26.453  -11.982 1.00 24.79 ? 264 TYR B CD2 1 
ATOM   3711 C CE1 . TYR B 1 237 ? -14.772 24.674  -10.717 1.00 25.06 ? 264 TYR B CE1 1 
ATOM   3712 C CE2 . TYR B 1 237 ? -13.070 26.334  -10.599 1.00 36.60 ? 264 TYR B CE2 1 
ATOM   3713 C CZ  . TYR B 1 237 ? -13.911 25.429  -9.979  1.00 28.06 ? 264 TYR B CZ  1 
ATOM   3714 O OH  . TYR B 1 237 ? -13.906 25.288  -8.614  1.00 31.14 ? 264 TYR B OH  1 
ATOM   3715 N N   . PHE B 1 238 ? -15.001 24.251  -16.919 1.00 9.06  ? 265 PHE B N   1 
ATOM   3716 C CA  . PHE B 1 238 ? -15.403 24.376  -18.309 1.00 10.12 ? 265 PHE B CA  1 
ATOM   3717 C C   . PHE B 1 238 ? -16.916 24.486  -18.360 1.00 12.90 ? 265 PHE B C   1 
ATOM   3718 O O   . PHE B 1 238 ? -17.612 23.767  -17.644 1.00 14.13 ? 265 PHE B O   1 
ATOM   3719 C CB  . PHE B 1 238 ? -14.922 23.172  -19.127 1.00 13.67 ? 265 PHE B CB  1 
ATOM   3720 C CG  . PHE B 1 238 ? -15.267 23.250  -20.585 1.00 17.56 ? 265 PHE B CG  1 
ATOM   3721 C CD1 . PHE B 1 238 ? -14.645 24.178  -21.407 1.00 17.16 ? 265 PHE B CD1 1 
ATOM   3722 C CD2 . PHE B 1 238 ? -16.216 22.392  -21.137 1.00 21.61 ? 265 PHE B CD2 1 
ATOM   3723 C CE1 . PHE B 1 238 ? -14.959 24.253  -22.764 1.00 15.70 ? 265 PHE B CE1 1 
ATOM   3724 C CE2 . PHE B 1 238 ? -16.539 22.460  -22.492 1.00 19.22 ? 265 PHE B CE2 1 
ATOM   3725 C CZ  . PHE B 1 238 ? -15.905 23.398  -23.308 1.00 15.53 ? 265 PHE B CZ  1 
ATOM   3726 N N   . THR B 1 239 ? -17.422 25.401  -19.182 1.00 10.44 ? 266 THR B N   1 
ATOM   3727 C CA  . THR B 1 239 ? -18.871 25.525  -19.312 1.00 12.27 ? 266 THR B CA  1 
ATOM   3728 C C   . THR B 1 239 ? -19.205 25.985  -20.725 1.00 12.01 ? 266 THR B C   1 
ATOM   3729 O O   . THR B 1 239 ? -18.358 26.533  -21.427 1.00 13.78 ? 266 THR B O   1 
ATOM   3730 C CB  . THR B 1 239 ? -19.456 26.479  -18.256 1.00 13.69 ? 266 THR B CB  1 
ATOM   3731 O OG1 . THR B 1 239 ? -20.883 26.336  -18.208 1.00 15.46 ? 266 THR B OG1 1 
ATOM   3732 C CG2 . THR B 1 239 ? -19.086 27.924  -18.555 1.00 22.49 ? 266 THR B CG2 1 
ATOM   3733 N N   . GLN B 1 240 ? -20.443 25.758  -21.144 1.00 10.40 ? 267 GLN B N   1 
ATOM   3734 C CA  . GLN B 1 240 ? -20.806 25.868  -22.549 1.00 11.78 ? 267 GLN B CA  1 
ATOM   3735 C C   . GLN B 1 240 ? -22.051 26.729  -22.712 1.00 9.82  ? 267 GLN B C   1 
ATOM   3736 O O   . GLN B 1 240 ? -22.775 26.973  -21.742 1.00 13.90 ? 267 GLN B O   1 
ATOM   3737 C CB  . GLN B 1 240 ? -21.039 24.470  -23.149 1.00 6.25  ? 267 GLN B CB  1 
ATOM   3738 C CG  . GLN B 1 240 ? -19.863 23.531  -22.963 1.00 13.29 ? 267 GLN B CG  1 
ATOM   3739 C CD  . GLN B 1 240 ? -20.071 22.177  -23.604 1.00 16.44 ? 267 GLN B CD  1 
ATOM   3740 O OE1 . GLN B 1 240 ? -20.134 22.059  -24.831 1.00 17.86 ? 267 GLN B OE1 1 
ATOM   3741 N NE2 . GLN B 1 240 ? -20.170 21.141  -22.778 1.00 15.17 ? 267 GLN B NE2 1 
ATOM   3742 N N   . PRO B 1 241 ? -22.337 27.203  -23.949 1.00 19.94 ? 268 PRO B N   1 
ATOM   3743 C CA  . PRO B 1 241 ? -23.443 28.161  -24.142 1.00 17.78 ? 268 PRO B CA  1 
ATOM   3744 C C   . PRO B 1 241 ? -24.847 27.561  -24.110 1.00 24.48 ? 268 PRO B C   1 
ATOM   3745 O O   . PRO B 1 241 ? -25.800 28.273  -23.782 1.00 22.90 ? 268 PRO B O   1 
ATOM   3746 C CB  . PRO B 1 241 ? -23.145 28.788  -25.513 1.00 19.57 ? 268 PRO B CB  1 
ATOM   3747 C CG  . PRO B 1 241 ? -21.815 28.292  -25.938 1.00 18.35 ? 268 PRO B CG  1 
ATOM   3748 C CD  . PRO B 1 241 ? -21.490 27.077  -25.150 1.00 15.07 ? 268 PRO B CD  1 
ATOM   3749 N N   . GLN B 1 242 ? -25.006 26.279  -24.439 1.00 26.94 ? 269 GLN B N   1 
ATOM   3750 C CA  . GLN B 1 242 ? -26.322 25.657  -24.568 1.00 20.06 ? 269 GLN B CA  1 
ATOM   3751 C C   . GLN B 1 242 ? -26.632 24.902  -23.287 1.00 16.47 ? 269 GLN B C   1 
ATOM   3752 O O   . GLN B 1 242 ? -25.789 24.149  -22.792 1.00 15.89 ? 269 GLN B O   1 
ATOM   3753 C CB  . GLN B 1 242 ? -26.416 24.655  -25.728 1.00 35.25 ? 269 GLN B CB  1 
ATOM   3754 C CG  . GLN B 1 242 ? -26.940 25.146  -27.073 1.00 32.55 ? 269 GLN B CG  1 
ATOM   3755 C CD  . GLN B 1 242 ? -25.938 25.949  -27.849 1.00 52.54 ? 269 GLN B CD  1 
ATOM   3756 O OE1 . GLN B 1 242 ? -24.755 25.989  -27.502 1.00 44.34 ? 269 GLN B OE1 1 
ATOM   3757 N NE2 . GLN B 1 242 ? -26.391 26.561  -28.939 1.00 52.20 ? 269 GLN B NE2 1 
ATOM   3758 N N   . GLN B 1 243 ? -27.837 25.110  -22.750 1.00 21.44 ? 270 GLN B N   1 
ATOM   3759 C CA  . GLN B 1 243 ? -28.176 24.527  -21.457 1.00 17.55 ? 270 GLN B CA  1 
ATOM   3760 C C   . GLN B 1 243 ? -28.065 23.009  -21.478 1.00 19.73 ? 270 GLN B C   1 
ATOM   3761 O O   . GLN B 1 243 ? -27.787 22.393  -20.442 1.00 25.92 ? 270 GLN B O   1 
ATOM   3762 C CB  . GLN B 1 243 ? -29.594 24.930  -21.040 1.00 26.01 ? 270 GLN B CB  1 
ATOM   3763 C CG  . GLN B 1 243 ? -30.064 24.271  -19.733 1.00 22.12 ? 270 GLN B CG  1 
ATOM   3764 C CD  . GLN B 1 243 ? -31.528 24.512  -19.426 1.00 21.59 ? 270 GLN B CD  1 
ATOM   3765 O OE1 . GLN B 1 243 ? -32.401 23.825  -19.951 1.00 33.89 ? 270 GLN B OE1 1 
ATOM   3766 N NE2 . GLN B 1 243 ? -31.803 25.479  -18.557 1.00 29.05 ? 270 GLN B NE2 1 
ATOM   3767 N N   A ASN B 1 244 ? -28.272 22.386  -22.630 0.57 21.27 ? 271 ASN B N   1 
ATOM   3768 N N   B ASN B 1 244 ? -28.253 22.391  -22.647 0.43 21.25 ? 271 ASN B N   1 
ATOM   3769 C CA  A ASN B 1 244 ? -28.272 20.932  -22.726 0.57 24.76 ? 271 ASN B CA  1 
ATOM   3770 C CA  B ASN B 1 244 ? -28.309 20.941  -22.780 0.43 24.62 ? 271 ASN B CA  1 
ATOM   3771 C C   A ASN B 1 244 ? -27.074 20.421  -23.519 0.57 24.75 ? 271 ASN B C   1 
ATOM   3772 C C   B ASN B 1 244 ? -27.035 20.343  -23.371 0.43 24.69 ? 271 ASN B C   1 
ATOM   3773 O O   A ASN B 1 244 ? -27.167 19.432  -24.249 0.57 25.02 ? 271 ASN B O   1 
ATOM   3774 O O   B ASN B 1 244 ? -27.058 19.194  -23.828 0.43 24.11 ? 271 ASN B O   1 
ATOM   3775 C CB  A ASN B 1 244 ? -29.583 20.437  -23.326 0.57 25.05 ? 271 ASN B CB  1 
ATOM   3776 C CB  B ASN B 1 244 ? -29.517 20.533  -23.629 0.43 24.70 ? 271 ASN B CB  1 
ATOM   3777 C CG  A ASN B 1 244 ? -30.681 20.328  -22.287 0.57 23.02 ? 271 ASN B CG  1 
ATOM   3778 C CG  B ASN B 1 244 ? -29.514 21.173  -25.011 0.43 23.47 ? 271 ASN B CG  1 
ATOM   3779 O OD1 A ASN B 1 244 ? -31.211 21.337  -21.817 0.57 16.40 ? 271 ASN B OD1 1 
ATOM   3780 O OD1 B ASN B 1 244 ? -28.511 21.735  -25.454 0.43 23.95 ? 271 ASN B OD1 1 
ATOM   3781 N ND2 A ASN B 1 244 ? -31.016 19.099  -21.906 0.57 31.89 ? 271 ASN B ND2 1 
ATOM   3782 N ND2 B ASN B 1 244 ? -30.644 21.080  -25.704 0.43 25.02 ? 271 ASN B ND2 1 
ATOM   3783 N N   . ALA B 1 245 ? -25.931 21.088  -23.376 1.00 25.81 ? 272 ALA B N   1 
ATOM   3784 C CA  . ALA B 1 245 ? -24.712 20.580  -23.985 1.00 20.22 ? 272 ALA B CA  1 
ATOM   3785 C C   . ALA B 1 245 ? -24.210 19.366  -23.213 1.00 19.06 ? 272 ALA B C   1 
ATOM   3786 O O   . ALA B 1 245 ? -24.412 19.239  -22.003 1.00 18.92 ? 272 ALA B O   1 
ATOM   3787 C CB  . ALA B 1 245 ? -23.637 21.662  -24.018 1.00 24.26 ? 272 ALA B CB  1 
ATOM   3788 N N   . GLU B 1 246 ? -23.554 18.464  -23.931 1.00 31.10 ? 273 GLU B N   1 
ATOM   3789 C CA  . GLU B 1 246 ? -22.967 17.297  -23.299 1.00 31.32 ? 273 GLU B CA  1 
ATOM   3790 C C   . GLU B 1 246 ? -21.759 17.687  -22.452 1.00 24.38 ? 273 GLU B C   1 
ATOM   3791 O O   . GLU B 1 246 ? -21.112 18.711  -22.688 1.00 21.89 ? 273 GLU B O   1 
ATOM   3792 C CB  . GLU B 1 246 ? -22.591 16.271  -24.362 1.00 45.15 ? 273 GLU B CB  1 
ATOM   3793 C CG  . GLU B 1 246 ? -23.765 15.963  -25.299 1.00 59.00 ? 273 GLU B CG  1 
ATOM   3794 C CD  . GLU B 1 246 ? -23.317 15.454  -26.654 1.00 74.49 ? 273 GLU B CD  1 
ATOM   3795 O OE1 . GLU B 1 246 ? -22.266 14.779  -26.694 1.00 72.08 ? 273 GLU B OE1 1 
ATOM   3796 O OE2 . GLU B 1 246 ? -24.001 15.726  -27.667 1.00 58.71 ? 273 GLU B OE2 1 
ATOM   3797 N N   . SER B 1 247 ? -21.467 16.860  -21.448 1.00 23.13 ? 274 SER B N   1 
ATOM   3798 C CA  . SER B 1 247 ? -20.244 17.008  -20.671 1.00 19.83 ? 274 SER B CA  1 
ATOM   3799 C C   . SER B 1 247 ? -19.023 16.872  -21.580 1.00 17.48 ? 274 SER B C   1 
ATOM   3800 O O   . SER B 1 247 ? -19.093 16.303  -22.674 1.00 15.64 ? 274 SER B O   1 
ATOM   3801 C CB  . SER B 1 247 ? -20.198 15.956  -19.561 1.00 23.90 ? 274 SER B CB  1 
ATOM   3802 O OG  . SER B 1 247 ? -19.493 16.424  -18.423 1.00 23.08 ? 274 SER B OG  1 
ATOM   3803 N N   . ARG B 1 248 ? -17.885 17.399  -21.119 1.00 20.05 ? 275 ARG B N   1 
ATOM   3804 C CA  . ARG B 1 248 ? -16.655 17.399  -21.917 1.00 13.50 ? 275 ARG B CA  1 
ATOM   3805 C C   . ARG B 1 248 ? -15.439 17.216  -21.002 1.00 13.54 ? 275 ARG B C   1 
ATOM   3806 O O   . ARG B 1 248 ? -14.560 18.068  -20.914 1.00 19.01 ? 275 ARG B O   1 
ATOM   3807 C CB  . ARG B 1 248 ? -16.513 18.696  -22.718 1.00 16.89 ? 275 ARG B CB  1 
ATOM   3808 C CG  . ARG B 1 248 ? -17.551 18.913  -23.826 1.00 21.80 ? 275 ARG B CG  1 
ATOM   3809 C CD  . ARG B 1 248 ? -17.416 17.923  -24.976 1.00 19.59 ? 275 ARG B CD  1 
ATOM   3810 N NE  . ARG B 1 248 ? -16.086 17.884  -25.574 1.00 23.67 ? 275 ARG B NE  1 
ATOM   3811 C CZ  . ARG B 1 248 ? -15.683 18.662  -26.569 1.00 22.50 ? 275 ARG B CZ  1 
ATOM   3812 N NH1 . ARG B 1 248 ? -16.447 19.636  -27.042 1.00 23.89 ? 275 ARG B NH1 1 
ATOM   3813 N NH2 . ARG B 1 248 ? -14.481 18.462  -27.099 1.00 30.23 ? 275 ARG B NH2 1 
ATOM   3814 N N   . ARG B 1 249 ? -15.375 16.083  -20.294 1.00 14.93 ? 276 ARG B N   1 
ATOM   3815 C CA  . ARG B 1 249 ? -14.204 15.811  -19.464 1.00 12.96 ? 276 ARG B CA  1 
ATOM   3816 C C   . ARG B 1 249 ? -12.902 15.713  -20.257 1.00 14.33 ? 276 ARG B C   1 
ATOM   3817 O O   . ARG B 1 249 ? -11.824 15.984  -19.701 1.00 10.79 ? 276 ARG B O   1 
ATOM   3818 C CB  . ARG B 1 249 ? -14.443 14.537  -18.637 1.00 22.17 ? 276 ARG B CB  1 
ATOM   3819 C CG  . ARG B 1 249 ? -15.663 14.613  -17.705 1.00 12.12 ? 276 ARG B CG  1 
ATOM   3820 C CD  . ARG B 1 249 ? -16.046 13.273  -17.066 1.00 16.30 ? 276 ARG B CD  1 
ATOM   3821 N NE  . ARG B 1 249 ? -16.593 12.292  -17.993 1.00 28.24 ? 276 ARG B NE  1 
ATOM   3822 C CZ  . ARG B 1 249 ? -17.862 12.266  -18.382 1.00 64.82 ? 276 ARG B CZ  1 
ATOM   3823 N NH1 . ARG B 1 249 ? -18.727 13.190  -17.990 1.00 41.84 ? 276 ARG B NH1 1 
ATOM   3824 N NH2 . ARG B 1 249 ? -18.274 11.290  -19.189 1.00 59.05 ? 276 ARG B NH2 1 
ATOM   3825 N N   . ASP B 1 250 ? -12.973 15.372  -21.547 1.00 15.87 ? 277 ASP B N   1 
ATOM   3826 C CA  . ASP B 1 250 ? -11.764 15.329  -22.362 1.00 12.55 ? 277 ASP B CA  1 
ATOM   3827 C C   . ASP B 1 250 ? -11.126 16.704  -22.480 1.00 9.59  ? 277 ASP B C   1 
ATOM   3828 O O   . ASP B 1 250 ? -9.907  16.809  -22.630 1.00 17.11 ? 277 ASP B O   1 
ATOM   3829 C CB  . ASP B 1 250 ? -12.070 14.772  -23.752 1.00 18.11 ? 277 ASP B CB  1 
ATOM   3830 C CG  . ASP B 1 250 ? -13.016 15.659  -24.537 1.00 29.55 ? 277 ASP B CG  1 
ATOM   3831 O OD1 . ASP B 1 250 ? -14.197 15.764  -24.143 1.00 31.07 ? 277 ASP B OD1 1 
ATOM   3832 O OD2 . ASP B 1 250 ? -12.569 16.266  -25.537 1.00 28.40 ? 277 ASP B OD2 1 
ATOM   3833 N N   . VAL B 1 251 ? -11.930 17.768  -22.419 1.00 12.35 ? 278 VAL B N   1 
ATOM   3834 C CA  . VAL B 1 251 ? -11.381 19.119  -22.467 1.00 11.80 ? 278 VAL B CA  1 
ATOM   3835 C C   . VAL B 1 251 ? -10.552 19.387  -21.220 1.00 12.66 ? 278 VAL B C   1 
ATOM   3836 O O   . VAL B 1 251 ? -9.478  19.998  -21.288 1.00 12.46 ? 278 VAL B O   1 
ATOM   3837 C CB  . VAL B 1 251 ? -12.509 20.152  -22.645 1.00 27.78 ? 278 VAL B CB  1 
ATOM   3838 C CG1 . VAL B 1 251 ? -11.985 21.561  -22.400 1.00 18.31 ? 278 VAL B CG1 1 
ATOM   3839 C CG2 . VAL B 1 251 ? -13.121 20.032  -24.039 1.00 16.58 ? 278 VAL B CG2 1 
ATOM   3840 N N   . LEU B 1 252 ? -11.032 18.932  -20.064 1.00 10.33 ? 279 LEU B N   1 
ATOM   3841 C CA  . LEU B 1 252 ? -10.263 19.089  -18.837 1.00 14.51 ? 279 LEU B CA  1 
ATOM   3842 C C   . LEU B 1 252 ? -8.972  18.294  -18.929 1.00 13.50 ? 279 LEU B C   1 
ATOM   3843 O O   . LEU B 1 252 ? -7.911  18.766  -18.506 1.00 10.40 ? 279 LEU B O   1 
ATOM   3844 C CB  . LEU B 1 252 ? -11.082 18.643  -17.628 1.00 13.10 ? 279 LEU B CB  1 
ATOM   3845 C CG  . LEU B 1 252 ? -12.482 19.247  -17.502 1.00 19.11 ? 279 LEU B CG  1 
ATOM   3846 C CD1 . LEU B 1 252 ? -13.101 18.824  -16.176 1.00 17.16 ? 279 LEU B CD1 1 
ATOM   3847 C CD2 . LEU B 1 252 ? -12.438 20.768  -17.628 1.00 10.20 ? 279 LEU B CD2 1 
ATOM   3848 N N   . ALA B 1 253 ? -9.052  17.067  -19.456 1.00 21.05 ? 280 ALA B N   1 
ATOM   3849 C CA  . ALA B 1 253 ? -7.840  16.275  -19.647 1.00 13.00 ? 280 ALA B CA  1 
ATOM   3850 C C   . ALA B 1 253 ? -6.856  16.990  -20.564 1.00 20.80 ? 280 ALA B C   1 
ATOM   3851 O O   . ALA B 1 253 ? -5.646  16.983  -20.314 1.00 20.65 ? 280 ALA B O   1 
ATOM   3852 C CB  . ALA B 1 253 ? -8.195  14.900  -20.214 1.00 12.24 ? 280 ALA B CB  1 
ATOM   3853 N N   . SER B 1 254 ? -7.358  17.611  -21.634 1.00 11.71 ? 281 SER B N   1 
ATOM   3854 C CA  . SER B 1 254 ? -6.487  18.326  -22.561 1.00 14.52 ? 281 SER B CA  1 
ATOM   3855 C C   . SER B 1 254 ? -5.844  19.533  -21.887 1.00 13.80 ? 281 SER B C   1 
ATOM   3856 O O   . SER B 1 254 ? -4.664  19.831  -22.117 1.00 17.76 ? 281 SER B O   1 
ATOM   3857 C CB  . SER B 1 254 ? -7.286  18.768  -23.789 1.00 13.48 ? 281 SER B CB  1 
ATOM   3858 O OG  . SER B 1 254 ? -7.657  17.666  -24.596 1.00 13.15 ? 281 SER B OG  1 
ATOM   3859 N N   . ALA B 1 255 ? -6.618  20.253  -21.073 1.00 9.70  ? 282 ALA B N   1 
ATOM   3860 C CA  . ALA B 1 255 ? -6.063  21.368  -20.317 1.00 14.37 ? 282 ALA B CA  1 
ATOM   3861 C C   . ALA B 1 255 ? -4.967  20.887  -19.377 1.00 13.37 ? 282 ALA B C   1 
ATOM   3862 O O   . ALA B 1 255 ? -3.905  21.516  -19.268 1.00 18.09 ? 282 ALA B O   1 
ATOM   3863 C CB  . ALA B 1 255 ? -7.175  22.077  -19.538 1.00 9.73  ? 282 ALA B CB  1 
ATOM   3864 N N   . ALA B 1 256 ? -5.203  19.767  -18.694 1.00 10.67 ? 283 ALA B N   1 
ATOM   3865 C CA  . ALA B 1 256 ? -4.187  19.245  -17.792 1.00 7.71  ? 283 ALA B CA  1 
ATOM   3866 C C   . ALA B 1 256 ? -2.948  18.832  -18.567 1.00 14.44 ? 283 ALA B C   1 
ATOM   3867 O O   . ALA B 1 256 ? -1.825  18.995  -18.084 1.00 20.31 ? 283 ALA B O   1 
ATOM   3868 C CB  . ALA B 1 256 ? -4.744  18.066  -16.997 1.00 13.72 ? 283 ALA B CB  1 
ATOM   3869 N N   . ARG B 1 257 ? -3.132  18.254  -19.757 1.00 11.61 ? 284 ARG B N   1 
ATOM   3870 C CA  . ARG B 1 257 ? -1.983  17.869  -20.568 1.00 13.90 ? 284 ARG B CA  1 
ATOM   3871 C C   . ARG B 1 257 ? -1.165  19.073  -21.010 1.00 10.08 ? 284 ARG B C   1 
ATOM   3872 O O   . ARG B 1 257 ? 0.067   19.043  -20.953 1.00 12.48 ? 284 ARG B O   1 
ATOM   3873 C CB  . ARG B 1 257 ? -2.436  17.031  -21.766 1.00 14.00 ? 284 ARG B CB  1 
ATOM   3874 C CG  . ARG B 1 257 ? -1.287  16.286  -22.431 1.00 16.83 ? 284 ARG B CG  1 
ATOM   3875 C CD  . ARG B 1 257 ? -1.734  15.238  -23.421 1.00 22.33 ? 284 ARG B CD  1 
ATOM   3876 N NE  . ARG B 1 257 ? -2.403  14.136  -22.736 1.00 24.68 ? 284 ARG B NE  1 
ATOM   3877 C CZ  . ARG B 1 257 ? -3.667  13.770  -22.901 1.00 41.29 ? 284 ARG B CZ  1 
ATOM   3878 N NH1 . ARG B 1 257 ? -4.469  14.400  -23.746 1.00 34.15 ? 284 ARG B NH1 1 
ATOM   3879 N NH2 . ARG B 1 257 ? -4.139  12.742  -22.198 1.00 39.14 ? 284 ARG B NH2 1 
ATOM   3880 N N   . ILE B 1 258 ? -1.830  20.136  -21.464 1.00 13.59 ? 285 ILE B N   1 
ATOM   3881 C CA  . ILE B 1 258 ? -1.123  21.369  -21.812 1.00 14.01 ? 285 ILE B CA  1 
ATOM   3882 C C   . ILE B 1 258 ? -0.360  21.925  -20.612 1.00 16.26 ? 285 ILE B C   1 
ATOM   3883 O O   . ILE B 1 258 ? 0.818   22.289  -20.722 1.00 23.79 ? 285 ILE B O   1 
ATOM   3884 C CB  . ILE B 1 258 ? -2.108  22.401  -22.390 1.00 16.68 ? 285 ILE B CB  1 
ATOM   3885 C CG1 . ILE B 1 258 ? -2.564  21.991  -23.795 1.00 11.32 ? 285 ILE B CG1 1 
ATOM   3886 C CG2 . ILE B 1 258 ? -1.478  23.770  -22.432 1.00 18.15 ? 285 ILE B CG2 1 
ATOM   3887 C CD1 . ILE B 1 258 ? -3.875  22.645  -24.222 1.00 9.17  ? 285 ILE B CD1 1 
ATOM   3888 N N   . ILE B 1 259 ? -1.003  21.944  -19.438 1.00 17.39 ? 286 ILE B N   1 
ATOM   3889 C CA  . ILE B 1 259 ? -0.375  22.468  -18.220 1.00 21.55 ? 286 ILE B CA  1 
ATOM   3890 C C   . ILE B 1 259 ? 0.828   21.627  -17.822 1.00 22.07 ? 286 ILE B C   1 
ATOM   3891 O O   . ILE B 1 259 ? 1.875   22.151  -17.423 1.00 21.67 ? 286 ILE B O   1 
ATOM   3892 C CB  . ILE B 1 259 ? -1.417  22.550  -17.094 1.00 17.16 ? 286 ILE B CB  1 
ATOM   3893 C CG1 . ILE B 1 259 ? -2.419  23.655  -17.432 1.00 27.28 ? 286 ILE B CG1 1 
ATOM   3894 C CG2 . ILE B 1 259 ? -0.748  22.754  -15.753 1.00 15.90 ? 286 ILE B CG2 1 
ATOM   3895 C CD1 . ILE B 1 259 ? -1.841  25.044  -17.297 1.00 22.86 ? 286 ILE B CD1 1 
ATOM   3896 N N   . ALA B 1 260 ? 0.687   20.310  -17.913 1.00 21.39 ? 287 ALA B N   1 
ATOM   3897 C CA  . ALA B 1 260 ? 1.728   19.368  -17.527 1.00 25.27 ? 287 ALA B CA  1 
ATOM   3898 C C   . ALA B 1 260 ? 2.924   19.494  -18.456 1.00 28.95 ? 287 ALA B C   1 
ATOM   3899 O O   . ALA B 1 260 ? 4.060   19.246  -18.038 1.00 26.32 ? 287 ALA B O   1 
ATOM   3900 C CB  . ALA B 1 260 ? 1.199   17.932  -17.515 1.00 14.85 ? 287 ALA B CB  1 
ATOM   3901 N N   . GLU B 1 261 ? 2.685   19.865  -19.720 1.00 29.34 ? 288 GLU B N   1 
ATOM   3902 C CA  . GLU B 1 261 ? 3.785   20.029  -20.660 1.00 29.96 ? 288 GLU B CA  1 
ATOM   3903 C C   . GLU B 1 261 ? 4.668   21.179  -20.196 1.00 34.04 ? 288 GLU B C   1 
ATOM   3904 O O   . GLU B 1 261 ? 5.897   21.061  -20.153 1.00 34.75 ? 288 GLU B O   1 
ATOM   3905 C CB  . GLU B 1 261 ? 3.242   20.422  -22.040 1.00 48.07 ? 288 GLU B CB  1 
ATOM   3906 C CG  . GLU B 1 261 ? 2.312   19.485  -22.869 1.00 51.55 ? 288 GLU B CG  1 
ATOM   3907 C CD  . GLU B 1 261 ? 2.592   17.993  -22.925 1.00 52.77 ? 288 GLU B CD  1 
ATOM   3908 O OE1 . GLU B 1 261 ? 3.496   17.476  -22.238 1.00 52.94 ? 288 GLU B OE1 1 
ATOM   3909 O OE2 . GLU B 1 261 ? 1.810   17.322  -23.646 1.00 39.83 ? 288 GLU B OE2 1 
ATOM   3910 N N   . GLY B 1 262 ? 4.044   22.295  -19.803 1.00 34.53 ? 289 GLY B N   1 
ATOM   3911 C CA  . GLY B 1 262 ? 4.737   23.501  -19.365 1.00 34.05 ? 289 GLY B CA  1 
ATOM   3912 C C   . GLY B 1 262 ? 5.403   23.351  -18.015 1.00 43.78 ? 289 GLY B C   1 
ATOM   3913 O O   . GLY B 1 262 ? 6.140   24.244  -17.581 1.00 46.11 ? 289 GLY B O   1 
ATOM   3914 N N   . LEU B 1 263 ? 5.122   22.237  -17.355 1.00 43.54 ? 290 LEU B N   1 
ATOM   3915 C CA  . LEU B 1 263 ? 5.613   21.788  -16.058 1.00 51.03 ? 290 LEU B CA  1 
ATOM   3916 C C   . LEU B 1 263 ? 6.969   21.085  -16.125 1.00 74.57 ? 290 LEU B C   1 
ATOM   3917 O O   . LEU B 1 263 ? 7.902   21.538  -15.445 1.00 73.86 ? 290 LEU B O   1 
ATOM   3918 C CB  . LEU B 1 263 ? 4.523   20.880  -15.471 1.00 47.93 ? 290 LEU B CB  1 
ATOM   3919 C CG  . LEU B 1 263 ? 4.158   20.624  -14.014 1.00 46.14 ? 290 LEU B CG  1 
ATOM   3920 C CD1 . LEU B 1 263 ? 5.252   19.827  -13.419 1.00 49.70 ? 290 LEU B CD1 1 
ATOM   3921 C CD2 . LEU B 1 263 ? 4.164   21.923  -13.287 1.00 46.43 ? 290 LEU B CD2 1 
ATOM   3922 O OXT . LEU B 1 263 ? 7.163   20.083  -16.825 1.00 70.94 ? 290 LEU B OXT 1 
HETATM 3923 O OAC . NXL C 2 .   ? -3.118  -2.754  -15.910 0.81 16.16 ? 301 NXL A OAC 1 
HETATM 3924 C CAN . NXL C 2 .   ? -2.611  -2.633  -14.811 0.81 13.04 ? 301 NXL A CAN 1 
HETATM 3925 N N   . NXL C 2 .   ? -1.571  -1.829  -14.519 0.81 17.13 ? 301 NXL A N   1 
HETATM 3926 C CAJ . NXL C 2 .   ? -1.282  -1.399  -13.148 0.81 14.43 ? 301 NXL A CAJ 1 
HETATM 3927 C CA  . NXL C 2 .   ? -0.765  -1.219  -15.594 0.81 21.72 ? 301 NXL A CA  1 
HETATM 3928 C C   . NXL C 2 .   ? 0.682   -1.753  -15.611 0.81 21.01 ? 301 NXL A C   1 
HETATM 3929 O O   . NXL C 2 .   ? 1.214   -2.226  -14.609 0.81 25.12 ? 301 NXL A O   1 
HETATM 3930 N NAA . NXL C 2 .   ? 1.305   -1.687  -16.778 0.81 24.60 ? 301 NXL A NAA 1 
HETATM 3931 C CB  . NXL C 2 .   ? -0.723  0.303   -15.447 0.81 13.89 ? 301 NXL A CB  1 
HETATM 3932 C CAH . NXL C 2 .   ? -0.586  0.740   -13.988 0.81 20.21 ? 301 NXL A CAH 1 
HETATM 3933 C CAO . NXL C 2 .   ? -1.649  0.085   -13.110 0.81 16.92 ? 301 NXL A CAO 1 
HETATM 3934 N NAK . NXL C 2 .   ? -3.058  0.239   -13.552 0.81 22.31 ? 301 NXL A NAK 1 
HETATM 3935 O OAL . NXL C 2 .   ? -3.462  0.300   -14.937 0.81 33.17 ? 301 NXL A OAL 1 
HETATM 3936 S SAR . NXL C 2 .   ? -4.975  0.903   -15.019 0.81 27.07 ? 301 NXL A SAR 1 
HETATM 3937 O OAD . NXL C 2 .   ? -5.689  0.101   -14.053 0.81 30.74 ? 301 NXL A OAD 1 
HETATM 3938 O OAE . NXL C 2 .   ? -4.815  2.289   -14.646 0.81 29.57 ? 301 NXL A OAE 1 
HETATM 3939 O OAG . NXL C 2 .   ? -5.367  0.687   -16.392 0.81 18.47 ? 301 NXL A OAG 1 
HETATM 3940 O OAC . NXL D 2 .   ? -21.170 17.834  -9.926  0.85 16.03 ? 301 NXL B OAC 1 
HETATM 3941 C CAN . NXL D 2 .   ? -21.787 17.164  -9.120  0.85 15.62 ? 301 NXL B CAN 1 
HETATM 3942 N N   . NXL D 2 .   ? -22.850 16.392  -9.416  0.85 15.75 ? 301 NXL B N   1 
HETATM 3943 C CAJ . NXL D 2 .   ? -23.280 15.293  -8.546  0.85 17.34 ? 301 NXL B CAJ 1 
HETATM 3944 C CA  . NXL D 2 .   ? -23.542 16.573  -10.704 0.85 15.49 ? 301 NXL B CA  1 
HETATM 3945 C C   . NXL D 2 .   ? -24.978 17.121  -10.554 0.85 18.45 ? 301 NXL B C   1 
HETATM 3946 O O   . NXL D 2 .   ? -25.585 17.072  -9.488  0.85 18.94 ? 301 NXL B O   1 
HETATM 3947 N NAA . NXL D 2 .   ? -25.509 17.651  -11.646 0.85 22.51 ? 301 NXL B NAA 1 
HETATM 3948 C CB  . NXL D 2 .   ? -23.576 15.255  -11.476 0.85 11.38 ? 301 NXL B CB  1 
HETATM 3949 C CAH . NXL D 2 .   ? -23.858 14.059  -10.564 0.85 17.24 ? 301 NXL B CAH 1 
HETATM 3950 C CAO . NXL D 2 .   ? -22.931 14.037  -9.351  0.85 14.16 ? 301 NXL B CAO 1 
HETATM 3951 N NAK . NXL D 2 .   ? -21.471 14.103  -9.599  0.85 12.99 ? 301 NXL B NAK 1 
HETATM 3952 O OAL . NXL D 2 .   ? -21.020 14.351  -10.948 0.85 30.02 ? 301 NXL B OAL 1 
HETATM 3953 S SAR . NXL D 2 .   ? -19.437 14.039  -11.158 0.85 27.48 ? 301 NXL B SAR 1 
HETATM 3954 O OAD . NXL D 2 .   ? -18.765 14.764  -10.106 0.85 23.24 ? 301 NXL B OAD 1 
HETATM 3955 O OAE . NXL D 2 .   ? -19.367 12.601  -11.048 0.85 24.18 ? 301 NXL B OAE 1 
HETATM 3956 O OAG . NXL D 2 .   ? -19.214 14.559  -12.487 0.85 19.90 ? 301 NXL B OAG 1 
HETATM 3957 O O   . HOH E 3 .   ? -1.435  -7.626  -27.284 1.00 11.77 ? 401 HOH A O   1 
HETATM 3958 O O   . HOH E 3 .   ? -12.790 -12.516 5.031   1.00 12.45 ? 402 HOH A O   1 
HETATM 3959 O O   . HOH E 3 .   ? -11.252 -15.760 -16.863 1.00 14.00 ? 403 HOH A O   1 
HETATM 3960 O O   . HOH E 3 .   ? -12.007 7.277   -11.857 1.00 11.74 ? 404 HOH A O   1 
HETATM 3961 O O   . HOH E 3 .   ? -14.330 -18.567 -23.558 1.00 6.35  ? 405 HOH A O   1 
HETATM 3962 O O   . HOH E 3 .   ? -27.782 -16.275 -5.760  1.00 20.17 ? 406 HOH A O   1 
HETATM 3963 O O   . HOH E 3 .   ? -10.779 4.981   -16.716 1.00 12.28 ? 407 HOH A O   1 
HETATM 3964 O O   . HOH E 3 .   ? -13.731 4.491   -10.926 1.00 13.14 ? 408 HOH A O   1 
HETATM 3965 O O   . HOH E 3 .   ? -15.689 3.105   -8.848  1.00 9.16  ? 409 HOH A O   1 
HETATM 3966 O O   . HOH E 3 .   ? -9.434  0.777   -19.027 1.00 6.95  ? 410 HOH A O   1 
HETATM 3967 O O   . HOH E 3 .   ? -15.047 -15.599 -29.842 1.00 9.31  ? 411 HOH A O   1 
HETATM 3968 O O   . HOH E 3 .   ? 12.311  -1.209  -6.394  1.00 12.38 ? 412 HOH A O   1 
HETATM 3969 O O   . HOH E 3 .   ? -4.955  -0.053  1.571   1.00 12.26 ? 413 HOH A O   1 
HETATM 3970 O O   . HOH E 3 .   ? -9.659  -12.492 7.321   1.00 16.53 ? 414 HOH A O   1 
HETATM 3971 O O   . HOH E 3 .   ? -21.367 -18.675 -22.197 1.00 14.27 ? 415 HOH A O   1 
HETATM 3972 O O   . HOH F 3 .   ? -7.565  22.678  -30.003 1.00 14.22 ? 401 HOH B O   1 
HETATM 3973 O O   . HOH F 3 .   ? -15.252 16.694  -14.458 1.00 14.63 ? 402 HOH B O   1 
HETATM 3974 O O   . HOH F 3 .   ? -10.129 7.923   5.811   1.00 8.83  ? 403 HOH B O   1 
HETATM 3975 O O   . HOH F 3 .   ? -13.484 11.887  -14.656 1.00 16.17 ? 404 HOH B O   1 
HETATM 3976 O O   . HOH F 3 .   ? -31.959 16.492  0.435   1.00 12.36 ? 405 HOH B O   1 
HETATM 3977 O O   . HOH F 3 .   ? -27.864 3.023   7.368   1.00 15.01 ? 406 HOH B O   1 
HETATM 3978 O O   . HOH F 3 .   ? -11.062 9.191   -9.854  1.00 12.20 ? 407 HOH B O   1 
HETATM 3979 O O   . HOH F 3 .   ? -11.968 4.899   -3.245  1.00 9.20  ? 408 HOH B O   1 
HETATM 3980 O O   . HOH F 3 .   ? -6.130  34.063  -16.075 1.00 12.82 ? 409 HOH B O   1 
HETATM 3981 O O   . HOH F 3 .   ? -26.913 29.165  -11.883 1.00 15.27 ? 410 HOH B O   1 
HETATM 3982 O O   . HOH F 3 .   ? -4.857  22.041  5.887   1.00 15.32 ? 411 HOH B O   1 
HETATM 3983 O O   . HOH F 3 .   ? -6.827  34.042  -24.468 1.00 12.41 ? 412 HOH B O   1 
# 
